"gene_id","gene_start","gene_stop","gene_length","pI","net_charge","mol_wt","gene_nuc_seq","gene_prot_seq","definition","cellular_location","genbank_definition","gendb_definition","ornl_definition","case1","case2","comment","blast_summary","interpro_summary","cogs_summary","blocks_summary","ProDom","paralog","pdb_hit","pfam_summary","bgene_id","defline","gi","mol_id","island_id","gene_id_lmd","gene_start_lmd","gene_stop_lmd","gene_length_lmd","pI_lmd","net_charge_lmd","mol_wt_lmd","gene_nuc_seq_lmd","gene_prot_seq_lmd","definition_lmd","case1_lmd","case2_lmd","comment_lmd","blast_summary_lmd","cogs_summary_lmd","blocks_summary_lmd","ProDom_lmd","paralog_lmd","pdb_hit_lmd","pfam_summary_lmd","bgene_id_lmd","defline_lmd","gi_lmd","mol_id_lmd","revisit","revisit_lmd","genbank_locus_tag" "ANA_0001","365","796","432","9.27","4.38","14886","ATGGCCCCCAAGAAGAAGGTCGCCGGGCTGATCAAGCTCCAGATCCAGGCCGGCCAGGCCAACCCCGCTCCGCCGATCGGCCCCGCCCTGGGTGCCCACGGCGTCAACATCATGGAGTTCTGCAAGGCGTACAACGCGGCGACCGAGTCGCAGCGCGGCAACGTCATCCCCGTGGAGATCACCGTCTACGAGGACCGCTCCTTCACCTTCATCACCAAGACCCCGCCGGCCGCCGAGCTCATCAAGAAGGCCGCGGGCGTCCCCAAGGGCTCCGCCACCCCCCACACCGTGAAGGTGGCCTCCCTGACCCAGGCGCAGGTGCGTGAGATCGCCGAGTCCAAGATGCCCGACCTCAACGCCAACGACATCGAGGCCGCCGCCAAGATCATCGCCGGCACCGCCCGCTCCATGGGCATCACCGTCGAGGCCTGA","MAPKKKVAGLIKLQIQAGQANPAPPIGPALGAHGVNIMEFCKAYNAATESQRGNVIPVEITVYEDRSFTFITKTPPAAELIKKAAGVPKGSATPHTVKVASLTQAQVREIAESKMPDLNANDIEAAAKIIAGTARSMGITVEA$","Ribosomal protein L11","Cytoplasm, Periplasm","ribosomal protein L11","ribosomal protein L11","ribosomal protein L11","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Pucciarelli M.G., Remacha M., Vilella M.D., Ballesta J.P. The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae. Nucleic Acids Res. 1990. 18(15):4409-4416. PMID: 2167467Choli T. Structural properties of ribosomal protein L11 from Escherichia coli. Biochem. Int. 1989. 19(6):1323-1338. PMID: 2483975","","","

InterPro
IPR000911
Family

Ribosomal protein L11
PD001367	$\"[11-74]T$	RL11_STRCO_P48954;
G3DSA:1.10.10.250	$\"[73-142]T$	no description
PIRSF002179	$\"[9-143]T$	Ribosomal protein L11/L12
PTHR11661	$\"[4-142]T$	60S RIBOSOMAL PROTEIN L12
PF00298	$\"[73-141]T$	Ribosomal_L11
PF03946	$\"[10-68]T$	Ribosomal_L11_N
SM00649	$\"[11-142]T$	RL11
PS00359	$\"[128-142]T$	RIBOSOMAL_L11

InterPro
IPR006519
Family

Ribosomal protein L11, bacterial
PTHR11661:SF1	$\"[4-142]T$	50S ROBOSOMAL PROTEIN L11
TIGR01632	$\"[5-143]T$	L11_bact: ribosomal protein L11

noIPR
unintegrated

unintegrated
G3DSA:3.30.1550.10	$\"[4-73]T$	no description
PIRSF500072	$\"[3-143]T$	Ribosomal protein L11

","BeTs to 26 clades of COG0080COG name: Ribosomal protein L11Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0080 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000911 (Ribosomal protein L11) with a combined E-value of 9.9e-83. IPB000911A 17-45 IPB000911B 56-94 IPB000911C 100-142","Residues 11-74 are similar to a (RIBOSOMAL RRNA-BINDING 50S L11 METHYLATION RIBONUCLEOPROTEIN L11P CHLOROPLAST MITOCHONDRION PEPTIDE) protein domain (PD001367) which is seen in RL11_STRCO.Residues 76-142 are similar to a (RIBOSOMAL RRNA-BINDING 50S L11 METHYLATION RIBONUCLEOPROTEIN L11P CHLOROPLAST SEQUENCING DIRECT) protein domain (PD082503) which is seen in Q6AH26_BBBBB.","","-80% similar to PDB:1NKW Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans (E_value = 1.5E_48);-80% similar to PDB:1NWX COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH ABT-773 (E_value = 1.5E_48);-80% similar to PDB:1NWY COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN (E_value = 1.5E_48);-80% similar to PDB:1PNU Crystal Structure of a Streptomycin Dependent Ribosome from Escherichia Coli, 50S Subunit of 70S Ribosome. THIS FILE, 1PNU, CONTAINS ONLY MOLECULES OF THE 50S RIBOSOMAL SUBUNIT. THE 30S SUBUNIT, MRNA, P-SITE TRNA, AND A-SITE TRNA ARE IN THE PDB FILE 1PNS. (E_value = 1.5E_48);-80% similar to PDB:1PNY Crystal Structure of the Wild Type Ribosome from E. Coli, 50S Subunit of 70S Ribosome. THIS FILE, 1PNY, CONTAINS ONLY MOLECULES OF THE 50S RIBOSOMAL SUBUNIT. THE 30S SUBUNIT IS IN THE PDB FILE 1PNX. (E_value = 1.5E_48);","Residues 10 to 68 (E_value = 1.4e-35) place ANA_0001 in the Ribosomal_L11_N family which is described as Ribosomal protein L11, N-terminal domain.Residues 73 to 141 (E_value = 1.6e-35) place ANA_0001 in the Ribosomal_L11 family which is described as Ribosomal protein L11, RNA binding domain.","","protein L11 (rplK)","","1","","","","","","","","","","","","","Wed Jul 25 18:06:41 2007","","","Wed Jul 25 18:02:16 2007","Wed Jul 25 18:02:16 2007","Wed Jul 25 18:02:16 2007","","Wed Jul 25 18:02:16 2007","Wed Jul 25 18:02:16 2007","","","","","yes","","" "ANA_0002","895","1584","690","9.60","7.67","24479","ATGACCAAGCGCTCCAAGGCCTACCGCGCCGCGGCAGAGAAGATCCAGTCCGGAGTCCTCTACACCCCGGCCGAGGCCGTTCACCTCGCCAAGTCCACCTCGATCACCAAGTTCGACGCCACCGTGGACGTCGTCTTCCGCCTCGGGGTCGACCCCCGCAAGGCGGACCAGATGGTCCGCGGAACCGTGTCCCTGCCGCACGGTACCGGTAAGACCGCCCGCGTCGTCGTCTTCGCCCAGGGTGAGCGCGCCGAGCAGGCCCTCGCCGCCGGCGCGGACGAGGTCGGTGGCGACGAGCTCATCGAGAAGGTCGCCAAGGGCTACACGGACTTCGACGCCGCCGTGGCCACCCCGGACCTCATGGGCAAGGTCGGCCGCCTGGGCCGCGTCCTGGGTCCCCGTGGCCTCATGCCCAACCCCCGCACCGGCACCGTGACGATGGACGTGGCCAAGGCCGTCTCCGACATCAAGGGCGGCCGTATCGAGTTCCGCGTGGACCGCGCCTCCAACCTCCACTTCATCATCGGCAAGGCATCCTTCACCGAGGAGCAGCTGACGGAGAACTTCCAGGCCGCCCTGGAGGAGGTCCTGCGCCTCAAGCCTTCGACCTCGAAGGGCCGCTACATCCTCAAGGCCACCATGACCACCACCATGGGCCCCGGCATTCCGATGGATGTCACCAAGGCCTGA","MTKRSKAYRAAAEKIQSGVLYTPAEAVHLAKSTSITKFDATVDVVFRLGVDPRKADQMVRGTVSLPHGTGKTARVVVFAQGERAEQALAAGADEVGGDELIEKVAKGYTDFDAAVATPDLMGKVGRLGRVLGPRGLMPNPRTGTVTMDVAKAVSDIKGGRIEFRVDRASNLHFIIGKASFTEEQLTENFQAALEEVLRLKPSTSKGRYILKATMTTTMGPGIPMDVTKA$","Ribosomal protein L1","Cytoplasm","ribosomal protein L1","50S ribosomal protein L1","ribosomal protein L1","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Nikonov S., Nevskaya N., Eliseikina I., Fomenkova N., Nikulin A., Ossina N., Garber M., Jonsson B.H., Briand C., Al-Karadaghi S., Svensson A., Aevarsson A., Liljas A. Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus. EMBO J. 1996. 15(6):1350-1359. PMID: 8635468Olvera J., Wool I.G. The primary structure of rat ribosomal protein L10a. Biochem. Biophys. Res. Commun. 1996. 220(3):954-957. PMID: 8607874","","","

InterPro
IPR002143
Family

Ribosomal protein L1
PD001314	$\"[14-225]T$	Q73SG1_MYCPA_Q73SG1;
PF00687	$\"[15-221]T$	Ribosomal_L1
PS01199	$\"[121-139]T$	RIBOSOMAL_L1

InterPro
IPR005878
Family

Ribosomal protein L1, bacterial and chloroplast form
PTHR23105:SF5	$\"[21-225]T$	50S RIBOSOMAL PROTEIN L1P
TIGR01169	$\"[3-229]T$	rplA_bact: ribosomal protein L1

noIPR
unintegrated

unintegrated
G3DSA:3.30.190.20	$\"[2-228]T$	no description
PTHR23105	$\"[21-225]T$	RIBOSOMAL PROTEIN L7AE FAMILY MEMBER

","No hits to the COGs database.","***** IPB002143 (Ribosomal protein L1) with a combined E-value of 6.4e-56. IPB002143A 37-48 IPB002143B 56-93 IPB002143C 127-140 IPB002143D 175-188 IPB002143E 205-224","Residues 1-108 are 73% similar to a (RIBOSOMAL RRNA-BINDING 50S RNA-BINDING L1) protein domain (PD866694) which is seen in RL1_STRA3.Residues 14-225 are similar to a (RIBOSOMAL 50S L1 RRNA-BINDING RNA-BINDING 60S L10A L1P RIBONUCLEOPROTEIN CHLOROPLAST) protein domain (PD001314) which is seen in Q73SG1_MYCPA.Residues 21-228 are 63% similar to a (RIBOSOMAL RRNA-BINDING 50S L1 RNA-BINDING) protein domain (PD723047) which is seen in RL1_MYCPE.","","-59% similar to PDB:1EG0 FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME (E_value = 6.1E_48);-59% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 6.1E_48);-59% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 6.1E_48);-59% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 6.1E_48);-59% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 6.1E_48);","Residues 15 to 221 (E_value = 3.7e-124) place ANA_0002 in the Ribosomal_L1 family which is described as Ribosomal protein L1p/L10e family.","","protein L1 (rplA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0003","3569","1866","1704","5.30","-14.65","59571","ATGCGTCGTCGTGTGTTTCTGTCTGGTGTGTTTCTGGCCGGTGTGGGGTTGCCGGTACTGGCCGGGTGCAAGCTTCCCTGGCAGTCGAAGGGTCAGGCCGGTTCCGCCTCGGCATCGGCGTCGGCGGGCGGGTCAGCGGCCGTGCCTGCCGCGTCGAGTGCGCCGCAGGGCTGGCAGGAGCTCGACGCCCACGTCATGGGTCACCATCTGGGGTTTCAGGTCTCACCGCTGGTGCGCCGCGATGCGAAGACCACCGTGCTGGCCCTGAAGCTGACGCGAGCCAAGGACGACGCCTCAGTCAAAGACATCGCAGAGTCCTACATCGACGGGGACGGCGATGTCTTCAAAGCGACCCACCCTTTGTCGCGCCCCGGCAGTAACCCGGCCTTTGAGCCGGCTGCAGGTGGGGTGCGTCTGCTGGACCTGCCCACCAACCGGGTGTGGGTGGCCACCACCGGTGTGGAGAACAAGGTCAAGGACAACTACAACAACCTGTCGCTCAAGCCGGGTGAGTCCACCAGCTGCTTCGTGCTCTTCGGGCCGGTGGACGCCAAGCAGGTCACCGTCTTCGTCCCCCAGGCAGGATTCGTCACCGTCAACGTCCTCGACAGCGGTGCCGCAGCTGCCTCCGGCATCGACTTCAAGGCCATCGACAAGGCCTTCGACAGCGCCACCATCCCCCAGTACACCCGGGACGAGGCCGACCCCAAACAGGTGCTGGCCGCCCCGGTGCCCATTGAGCGTTACACCAAGGCCCTGGACGACTCCACCAGCACCCATGCCGGTGGTAAGGACATCACCGTCACCCTCGCATCAGATGTCACCTTCGCCTCGGACTCCGCCGACCTAGCCTCAGGGGCCGAGGCTCAGCTCCAGACCGTCGCCGCCCAGCTCAGCCAGTACCCCGACGGCGGGACCCTGTCCATTGTGGGGCACACCGACGACGTCCAGGACGACGCCTACAACCAGACCCTGTCCGAGAAGCGAGCCAACGCCGTCAAGACCCGCCTCGAACAGCTCACGAGCCTGGACAAGTGGCAAACCAGTGTCTCCGGCAAGGGCGAGTCCGAACCCAAGGTCAACGACACGACCGACCAGGCCCGCGCCGTCAACCGACGCGTCGAGATCACCCTGACCCCCACCGGCGGCACCAGCAAGAAGAACGCATCCCCCACCCCCAACAGCAGTGGTGGTGGCAAGCTGCCCGACCCGAAAGGCCCCGTCGCCGAGGGCTCAGACGGCGTCACCGTCAAAAGTGACAGTGGCGCCCAGCTCACCATCACCATCGACCACGTCACCCGCCAAGGCGGATACCTCCTCGGCCAGCTCCACACCACCCTCAGCAGCAAGAACAGCACCAACCCCACTTTCTACGCCTGGTTTGATGACAAAGAAACCTTCTTCACCAACTCCCGGGGCGAGGACGGCAGCGAGGAAGCCACAACATACGCCGCCGACGGGTTGACCCTCCTGGCCGGAGGCGAGCGTATCTACCCCGCCGACTACCGCGACGCCGGCTTGGAGACCCACGTCCCCCTCAGCGAGCTCGAGCTCACTCCCCCTATCAAGGCCGGCACCACCACCGTCTGCGTCGTCTGGCCCGATCCCGGCGGCGACACCGTCACCCTCGACCACCTCCCCAACGAGTATCTCGGCTCCAGTTTCGCCTACCGTCTCACCGACATCCCTATCAAGAACGGCTGA","MRRRVFLSGVFLAGVGLPVLAGCKLPWQSKGQAGSASASASAGGSAAVPAASSAPQGWQELDAHVMGHHLGFQVSPLVRRDAKTTVLALKLTRAKDDASVKDIAESYIDGDGDVFKATHPLSRPGSNPAFEPAAGGVRLLDLPTNRVWVATTGVENKVKDNYNNLSLKPGESTSCFVLFGPVDAKQVTVFVPQAGFVTVNVLDSGAAAASGIDFKAIDKAFDSATIPQYTRDEADPKQVLAAPVPIERYTKALDDSTSTHAGGKDITVTLASDVTFASDSADLASGAEAQLQTVAAQLSQYPDGGTLSIVGHTDDVQDDAYNQTLSEKRANAVKTRLEQLTSLDKWQTSVSGKGESEPKVNDTTDQARAVNRRVEITLTPTGGTSKKNASPTPNSSGGGKLPDPKGPVAEGSDGVTVKSDSGAQLTITIDHVTRQGGYLLGQLHTTLSSKNSTNPTFYAWFDDKETFFTNSRGEDGSEEATTYAADGLTLLAGGERIYPADYRDAGLETHVPLSELELTPPIKAGTTTVCVVWPDPGGDTVTLDHLPNEYLGSSFAYRLTDIPIKNG$","OmpA/MotB domain protein","Extracellular, Periplasm","OmpA family domain protein","OmpA family protein","OmpA/MotB domain protein","","Freudl R., Klose M., Henning U. Export and sorting of the Escherichia coli outer membrane protein OmpA. J. Bioenerg. Biomembr. 1990. 22(3):441-449. PMID: 2202726Bouveret E., Benedetti H., Rigal A., Loret E., Lazdunski C. In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J. Bacteriol. 1999. 181(20):6306-6311. PMID: 10515919De Mot R., Proost P., Van Damme J., Vanderleyden J. Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. aeruginosa and P. syringae. Mol. Gen. Genet. 1992. 231(3):489-493. PMID: 1538702","","","

InterPro
IPR006664
Domain

Outer membrane protein, bacterial
PR01021	$\"[276-298]T$ $\"[307-322]T$ $\"[322-338]T$	OMPADOMAIN

InterPro
IPR006665
Domain

Outer membrane protein, OmpA/MotB, C-terminal
PD000930	$\"[266-333]T$	Q7P6E3_BBBBB_Q7P6E3;
G3DSA:3.30.1330.60	$\"[258-382]T$	no description
PF00691	$\"[275-372]T$	OmpA
PS51123	$\"[263-382]T$	OMPA_2

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[5-23]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB006690 (OmpA-like domain) with a combined E-value of 5.8e-24. IPB006690A 274-299 IPB006690B 307-358 IPB006690C 369-378***** IPB000498 (OmpA-like transmembrane domain) with a combined E-value of 3.8e-17. IPB000498F 301-348 IPB000498G 349-380***** IPB001035 (Sodium-type flagellar protein MotY precursor signature) with a combined E-value of 6.3e-06. IPB001035K 322-339 IPB001035M 361-381","Residues 266-333 are 67% similar to a (MEMBRANE OUTER LIPOPROTEIN OMPA MOTB PRECURSOR SIGNAL CHEMOTAXIS PORIN PEPTIDOGLYCAN-ASSOCIATED) protein domain (PD000930) which is seen in Q7P6E3_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 275 to 372 (E_value = 2.3e-25) place ANA_0003 in the OmpA family which is described as OmpA family.","","family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0004","5221","3584","1638","5.39","-11.87","57358","ATGCGTCGTCGTGTGTTTCTGTCCGGTGCGATTCTGACCGGTGTGGGGTTGCCGCTGCTGGCCGGGTGCAAGCTTCCCTGGCAGTCGAAACGTCAGGCCAGCTCGACCTCGGCCTCGGCGGGCGGGGCAGCGGGGGCGCCTGCGGCGCCGCAGGGCTGGCAGCAGCTCGACGGCCACATCGCCGGTCATCACATCATCGTGAACGTCTCCCCAATTGTTCGCAAGGATGAGTCCACCTCGATTCTGGCCTTGGAACTATTTCGAGCATCCGATGACAAAAACCGCACAGAAAACAAGCCAACGTCTTCTACGCCGGACAACAAGTTCACCATTGTTGACTACTGGGGAAGCCGAGCAAACCTCCAACCAGGGAACGGCGTCTCGGCTGTCAGAATCATGGACTTGCAGACTGGACGCGTATGGAACTCCATCAATGGAAGTAAGGCCGACCCCGGGATCGCACCGGGCGAAAAGATCACCTACTACGTTGCCTTCGGCAAGATCGACTCCGAGCAAGTGACCGTCTTCGTTCCTATGGCCGGGTTCGTGACTGTCTCCGTCCTCGAGGCAGGATCCGCCCAACAGGCAAAAATCGACCTATCTGCAGCTCAAACCGAACTGGATACGTTGCCTAATACTACGCTCGCCGCCTCGGCACCCATTGAACGATACACGCGCTCTCTGGATGACTCCACCAGCACCCACACGGGCGGCAAGGACATCACCGTCACCCTCGCATCAGACGTCACCTTCGCCTCCGACTCCGCCGACCTGGCCCCCGGAGCCGAAACCCAACTCCAGACAGTGGTCGGTCAGCTGGCCCAGTACCCCGACGGTGGGACGCTGACGATCGTGGGGCACACTGACGACGTCCAAGACGACGCCTACAACCAGACCCTCTCCGAAAAACGAGCCAACGCCGTCAAGACCCGCCTCGCACAGCTCACCAAGCTCGACAAGTGGCAGACATCCGTCTCCGGCAAAGGCGAGAGCCAGCCCAAGATCAACGACACCACCGACCAGGCCCGCGCCGCCAACCGACGCGTCGAGATCACCCTGACCCCCACCAGCGGCACCACCAAGAAGGGCTCATCCCCTACCCCCAACAGCAACGATGCCAGCACCCTGCCAGCCTCGGAAGGCCCCAGCGCCAAAGGCTCCGACGGTGTCACTGTGACTGCTAAAAGTGCTAACAGCAACGGTGAGGTCACCATCACCCTCGACCATGTCACTCGCCAAGGTGGTTACCTTGTAGGCACCTTGACCTGCACCGTCAAGCCCAGTTCTCACAGCGCAAATCTCACCGTGTTACTCACCGACCTGGAGAACAGATCCGGAAACCAGCGAGACGAGGACACTGGAAGTACCGCAACCTTCATGGCCACAGACGGGCTGACTCTCATCTCAGGCAACGAACGAGTCTTCCCTGCCGACTACGAGCAGGCCGACATCAAAGCTCATATACCGCTGACCGAGCTTTATGTCGGCGACGAACTCCTAGGTGGAACTGTCACCGCCGTTGGCGTTGTCTGGCCCGACCCCGGCGGCGACACAGTCACGCTCGACCATCCCCAATCAGAGGACAGCTACTCGACCACTGCCTTCCGTCTCACTGACATCCCCGTCAAGAACAAATGA","MRRRVFLSGAILTGVGLPLLAGCKLPWQSKRQASSTSASAGGAAGAPAAPQGWQQLDGHIAGHHIIVNVSPIVRKDESTSILALELFRASDDKNRTENKPTSSTPDNKFTIVDYWGSRANLQPGNGVSAVRIMDLQTGRVWNSINGSKADPGIAPGEKITYYVAFGKIDSEQVTVFVPMAGFVTVSVLEAGSAQQAKIDLSAAQTELDTLPNTTLAASAPIERYTRSLDDSTSTHTGGKDITVTLASDVTFASDSADLAPGAETQLQTVVGQLAQYPDGGTLTIVGHTDDVQDDAYNQTLSEKRANAVKTRLAQLTKLDKWQTSVSGKGESQPKINDTTDQARAANRRVEITLTPTSGTTKKGSSPTPNSNDASTLPASEGPSAKGSDGVTVTAKSANSNGEVTITLDHVTRQGGYLVGTLTCTVKPSSHSANLTVLLTDLENRSGNQRDEDTGSTATFMATDGLTLISGNERVFPADYEQADIKAHIPLTELYVGDELLGGTVTAVGVVWPDPGGDTVTLDHPQSEDSYSTTAFRLTDIPVKNK$","OmpA/MotB domain protein","Extracellular, Periplasm","OmpA family domain protein","OmpA/MotB","OmpA/MotB domain protein","","Freudl R., Klose M., Henning U. Export and sorting of the Escherichia coli outer membrane protein OmpA. J. Bioenerg. Biomembr. 1990. 22(3):441-449. PMID: 2202726Bouveret E., Benedetti H., Rigal A., Loret E., Lazdunski C. In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J. Bacteriol. 1999. 181(20):6306-6311. PMID: 10515919De Mot R., Proost P., Van Damme J., Vanderleyden J. Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. aeruginosa and P. syringae. Mol. Gen. Genet. 1992. 231(3):489-493. PMID: 1538702","","","

InterPro
IPR006664
Domain

Outer membrane protein, bacterial
PR01021	$\"[251-273]T$ $\"[282-297]T$ $\"[297-313]T$	OMPADOMAIN

InterPro
IPR006665
Domain

Outer membrane protein, OmpA/MotB, C-terminal
PD000930	$\"[242-308]T$	Q9CMN1_PASMU_Q9CMN1;
G3DSA:3.30.1330.60	$\"[233-357]T$	no description
PF00691	$\"[250-347]T$	OmpA
PS51123	$\"[238-357]T$	OMPA_2

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-23]?$	transmembrane_regions

","BeTs to 12 clades of COG2885COG name: Outer membrane protein and related peptidoglycan-associated (lipo)proteinsFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG2885 is -------q--r---efghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB006690 (OmpA-like domain) with a combined E-value of 1.7e-23. IPB006690A 249-274 IPB006690B 282-333 IPB006690C 344-353***** IPB000498 (OmpA-like transmembrane domain) with a combined E-value of 1.8e-17. IPB000498F 276-323 IPB000498G 324-355","Residues 242-308 are 62% similar to a (MEMBRANE OUTER LIPOPROTEIN OMPA MOTB PRECURSOR SIGNAL CHEMOTAXIS PORIN PEPTIDOGLYCAN-ASSOCIATED) protein domain (PD000930) which is seen in Q9CMN1_PASMU.","","No significant hits to the PDB database (E-value < E-10).","Residues 250 to 347 (E_value = 2.1e-23) place ANA_0004 in the OmpA family which is described as OmpA family.","","family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0005","6930","5236","1695","5.99","-7.42","59237","ATGCGTCGTCGTGTGTTTCTGTCCGGTGCGATTCTGACCGGTGTTGGGTTGCCGCTGCTGGCTGGGTGCAAGCTTCCCTGGCAGTCAAGGCGTCAGACAGGCCCGGCCTCGGCGTCGGCATCGGCGGGTGGGTCAGCGGGAGCGTCTGCCGTGCCTGCGGCGTCGGCGGCGCCGCAGGGATGGCAGGAGCTCGACGCCCACGTCATGGGTCACCACCTGGGGATCCAGGTCTCACCACTGGTGCGCCGCGACGAGACGACCACCGTGCTGGCCCTGAAGCTGACGCGAGCCAAGGACGACCCCGCAGTCAAGGACATCGCAGACGCCGCCAGCGACGGCGGCAACACCTTCGAGGCGTCCTTGCCTTTGTCACGCCCCGGACGCCTGAGGACATCCGACTGGGGCGCCAACGGGGTACGTCTGCTGGACCTGCCCACCAACCGGGCGTGGCTAGCCACCGCCAGCGTGGAGAACAAGGTCAAGGACAACTACAACAACCTGCCGCTCAAGCCGGGTGAGTCCACCAGCTGCTTCGTGCTCTTCGGTCCGGTGGATGCCAAGGAGGTCACCGTCTTCGTCCCCCAGGCCGGATTCGTCACCGTCAACGTCCTCGACAGCAGCGCCGCAGCAGCCTCCGGCATCGACTTCAAAGCCATCGACAAGGCCTTCGACAGCGTGGCCAACCCCGACGAGGCCAAGCCCTACCAGGCGCTGGCCGCCCCGGTACCCATTGAGCGCTACACCAAGGCCCTGGACGACTCCACCAGCACCCACACCGGAAGCAAGGACATCACCGTCACCCTCGCATCAGACGTCACCTTCGCCTCAGACTCAGCCGACCTGGCCTCAGGTGCCGAGGCCCAGCTCCAGACGGTGGCCGGCCAGCTAGCCCAGTACCCCGACGGCGGGACCCTGTCCATTGTGGGGCACACCGACGACGTCCAGGACGACGCCTACAACCAGACCCTGTCCGAGAAACGCGCCAACGCCGTCAAAACCCGCCTCGAACAGCTCACCAGCCTCGACAAGTGGCAGACATCCGTGTCCGGCAAGGGCGAGTCCGAGCCCAAGGTCAACGACACCAGCGACGAGGCCCGCGCCGTCAACCGACGCGTCGAGATCACCCTGACCCCCACCGGCGGCACCACGACCAAGACCACTACCCCGCCCGCTGGAACCGGTTCCTTGCCCGAGAACAAGGGCCCCGTCGCCAAGGGCTCCGAGGGCGTCACCGTCAAGCATGTCAGTGGCAACAGCCAGCTCACCATCACCATCGACCACGTCACCCGCTCTGGCGGATACCTCTTCGGCCAGCTCCACACCACCCTCAGCGTGAAGAAGGGCTCCGCCCCCGACCGCCTAGAGGACTGGCTCAACGACAAAGAGGCTCCCTTCTCCAACTCCCGCAGCGAGAAAGGCAGCCGCGACGCCGTAGCATTCGCCGCCAACGGGTTGACCCTCCTGGCCGCAGGCGAGCGCATCTACCCCGCCGACTACCTCGACGCCGGCTTCAAGACCCACCTCCCCCTCACCGAGCTCCAGCTCACTCCCCATATCAAGGCCGGCACCACCACCATCTGCGTCATCTGGCCCGACCCCGGCAGCGACACCGTCACCCTCGACCACGCAGCAACCGGGAAGGAAGTCGCCGACTTCGGCTACCGCCTCACCGACATCCCCGTCAAGAACAGCTGA","MRRRVFLSGAILTGVGLPLLAGCKLPWQSRRQTGPASASASAGGSAGASAVPAASAAPQGWQELDAHVMGHHLGIQVSPLVRRDETTTVLALKLTRAKDDPAVKDIADAASDGGNTFEASLPLSRPGRLRTSDWGANGVRLLDLPTNRAWLATASVENKVKDNYNNLPLKPGESTSCFVLFGPVDAKEVTVFVPQAGFVTVNVLDSSAAAASGIDFKAIDKAFDSVANPDEAKPYQALAAPVPIERYTKALDDSTSTHTGSKDITVTLASDVTFASDSADLASGAEAQLQTVAGQLAQYPDGGTLSIVGHTDDVQDDAYNQTLSEKRANAVKTRLEQLTSLDKWQTSVSGKGESEPKVNDTSDEARAVNRRVEITLTPTGGTTTKTTTPPAGTGSLPENKGPVAKGSEGVTVKHVSGNSQLTITIDHVTRSGGYLFGQLHTTLSVKKGSAPDRLEDWLNDKEAPFSNSRSEKGSRDAVAFAANGLTLLAAGERIYPADYLDAGFKTHLPLTELQLTPHIKAGTTTICVIWPDPGSDTVTLDHAATGKEVADFGYRLTDIPVKNS$","OmpA/MotB domain protein","Extracellular, Periplasm","OmpA family domain protein","OmpA family protein","OmpA/MotB domain protein","","Freudl R., Klose M., Henning U. Export and sorting of the Escherichia coli outer membrane protein OmpA. J. Bioenerg. Biomembr. 1990. 22(3):441-449. PMID: 2202726Bouveret E., Benedetti H., Rigal A., Loret E., Lazdunski C. In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J. Bacteriol. 1999. 181(20):6306-6311. PMID: 10515919De Mot R., Proost P., Van Damme J., Vanderleyden J. Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. aeruginosa and P. syringae. Mol. Gen. Genet. 1992. 231(3):489-493. PMID: 1538702","","","

InterPro
IPR006664
Domain

Outer membrane protein, bacterial
PR01021	$\"[274-296]T$ $\"[305-320]T$ $\"[320-336]T$	OMPADOMAIN

InterPro
IPR006665
Domain

Outer membrane protein, OmpA/MotB, C-terminal
PD000930	$\"[264-331]T$	Q7P6E3_BBBBB_Q7P6E3;
G3DSA:3.30.1330.60	$\"[256-380]T$	no description
PF00691	$\"[273-370]T$	OmpA
PS51123	$\"[261-380]T$	OMPA_2

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-23]?$	transmembrane_regions

","BeTs to 12 clades of COG2885COG name: Outer membrane protein and related peptidoglycan-associated (lipo)proteinsFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG2885 is -------q--r---efghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB006690 (OmpA-like domain) with a combined E-value of 1.6e-23. IPB006690A 272-297 IPB006690B 305-356 IPB006690C 367-376***** IPB000498 (OmpA-like transmembrane domain) with a combined E-value of 2.1e-17. IPB000498F 299-346 IPB000498G 347-378","Residues 264-331 are 66% similar to a (MEMBRANE OUTER LIPOPROTEIN OMPA MOTB PRECURSOR SIGNAL CHEMOTAXIS PORIN PEPTIDOGLYCAN-ASSOCIATED) protein domain (PD000930) which is seen in Q7P6E3_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 273 to 370 (E_value = 3.7e-24) place ANA_0005 in the OmpA family which is described as OmpA family.","","family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0006","8765","6945","1821","5.95","-8.93","63240","ATGGGGAGTACCCGGGGAGTCCCGCTTGCTAGGAAGATTACGTTACGATTACGCTCTGTCTTTGAGAAATTCCGGTGGACCCATGAAGGAGTTGTTGTGTCATTAGTATTCTCCCGTTCACTTGGAGTCTCTGCTCGGGGGACGTCTCGTCGGTCTTTCGTGGCTCTCTCGGCCCTGACGGGGCTGGCGTTGCCGGTGCTGGCGGGCTGTGACCTGCCGGGAGTCTCCAAGGGCAAGGGAGGCTCGACATCATCATCGGGCGCCACCGCCGGGGGATCCGCCTCGCCCGGCGGGTCAGCCACGGCCTCGGCCAGCGCTCCGGCTAAGGCTGGTAGCACCGAGTGGCAGAAGCTCGACGGTCACGTCATGGGCCACAAGGTGAGCGTGGAGGTCTCCCCCGTCGTCCGCCAGGACGACAAGACCTCGTACATCGCCGTGAAGCTCACCCGCGCGTCCGACGACGCCTCCATCGACACGATCAACACCAGCCCCTACAGCGACGACAACAAGCTCAACATCTCCAACTACCTAGGCGTGCCGTCAATCTACCGTCCTGGTACCGGAGTCTCCCTGGTCAAGCTGCTCGACACTGCCTCGGGGCGCGTGTGGAGCGCCATCGACGGCAGCGGCCTGTTCCTCGAGCTCGCCCCCGGCGAGGACATGACCTCCTACCTGTCCTTCGGCAAGGTCGACACCGACACCGTTACCGTCATGGTCCCCATGGCCGGCTTCACCACTGTCTCCGTCCTGGACGCCGGCGACGCTAAGAAAGCCAAGATCGACCTGTCTATCGCCCAGGCCGCGCTCAAGCAGTCCTCTCACGACGTCCCCGAGCTCGCCGCCCCCGTCGCCATCGAGCGTTACACCCGGGCCCTGGACGACTCCACCAGCACCCACGCCGGTGGCAAGGACATCACCGTCACCCTGGCATCAGATGTCACCTTCGCCTCGGACTCCGCCGACCTGGCCTCAGGAGCTGAGGCCCAGCTGAAGACCGTCGCCTCCCAGCTCAAGCAGCATCCCGACGGCGGGACGCTGACGATCGTTGGGCACACTGACGACGTCCAGGACGACGCCTACAACCAGACCCTGTCCGAGAAACGAGCCAACGCCGTCAAGACCAGACTCGAACAGCTCACCAAGCTCGACAAGTGGCAGACATCCGTGTCCGGCAAGGGCGAGTCCGAGCCCCGCATCAACGACACCAGCGACGAGGCCCGCGCCGCCAACCGACGCGTCGAGATCACCCTGACCCCCACCGGCGGCACCACCCCCAAGAACACCCCCACCCCCAACAGCAGCAGTGGCAAGCTGCCCGACCCCCAGGGCCCCGTCGCCAAGGGCCCTGAAGGTGTCACCCTCACCGCCACGGGCGGCTCCAACACCAGTGGGGAGGTCACCATCACCCTGGACCACGTCACCCGCTCCGGAAGCTTCCTTCTGGGCACCGTCACCTGCACCGTCAAGGACGGCTCCAACGACGTACCACTGCACCCTCTGCTCGAGGATCCCGAGACCCCCTTGAGCAACCAGCGCTCCGAATCTGGCGCCCTGTCAACCTTCAACGCCAGCGACGGCCTGACCCTCCTCAGCAACGGCGAGCGCATCTTCCCCGCCGACTACCTCGACGCCGACGTCGACCACCACCTCCCCCTGACCGAGCTACGCCTCGTGGACCACCTCAAGGCCGGCACCACCACCGTCTGCGTCGTCTGGCCCGACCCCGGCGGCGACACCATCACCCTCGACCATGCCAAAGGCGAGTACTCCGTCCCAGGCAACTCCTACCGCCTCACCGACATCCCCGTCAAGAACAAATGA","MGSTRGVPLARKITLRLRSVFEKFRWTHEGVVVSLVFSRSLGVSARGTSRRSFVALSALTGLALPVLAGCDLPGVSKGKGGSTSSSGATAGGSASPGGSATASASAPAKAGSTEWQKLDGHVMGHKVSVEVSPVVRQDDKTSYIAVKLTRASDDASIDTINTSPYSDDNKLNISNYLGVPSIYRPGTGVSLVKLLDTASGRVWSAIDGSGLFLELAPGEDMTSYLSFGKVDTDTVTVMVPMAGFTTVSVLDAGDAKKAKIDLSIAQAALKQSSHDVPELAAPVAIERYTRALDDSTSTHAGGKDITVTLASDVTFASDSADLASGAEAQLKTVASQLKQHPDGGTLTIVGHTDDVQDDAYNQTLSEKRANAVKTRLEQLTKLDKWQTSVSGKGESEPRINDTSDEARAANRRVEITLTPTGGTTPKNTPTPNSSSGKLPDPQGPVAKGPEGVTLTATGGSNTSGEVTITLDHVTRSGSFLLGTVTCTVKDGSNDVPLHPLLEDPETPLSNQRSESGALSTFNASDGLTLLSNGERIFPADYLDADVDHHLPLTELRLVDHLKAGTTTVCVVWPDPGGDTITLDHAKGEYSVPGNSYRLTDIPVKNK$","OmpA/MotB domain protein","Periplasm, Membrane, Extracellular","OmpA family domain protein","OmpA family protein","OmpA/MotB domain protein","","Freudl R., Klose M., Henning U. Export and sorting of the Escherichia coli outer membrane protein OmpA. J. Bioenerg. Biomembr. 1990. 22(3):441-449. PMID: 2202726Bouveret E., Benedetti H., Rigal A., Loret E., Lazdunski C. In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J. Bacteriol. 1999. 181(20):6306-6311. PMID: 10515919De Mot R., Proost P., Van Damme J., Vanderleyden J. Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. aeruginosa and P. syringae. Mol. Gen. Genet. 1992. 231(3):489-493. PMID: 1538702","","","

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[48-78]T$	TAT_signal_seq: Tat (twin-arginine transloc

InterPro
IPR006664
Domain

Outer membrane protein, bacterial
PR01021	$\"[315-337]T$ $\"[346-361]T$ $\"[361-377]T$	OMPADOMAIN

InterPro
IPR006665
Domain

Outer membrane protein, OmpA/MotB, C-terminal
PD000930	$\"[312-372]T$	Q88NT3_PSEPK_Q88NT3;
G3DSA:3.30.1330.60	$\"[297-421]T$	no description
PF00691	$\"[314-411]T$	OmpA
PS51123	$\"[302-421]T$	OMPA_2

noIPR
unintegrated

unintegrated
PS51257	$\"[1-24]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[9-29]?$	transmembrane_regions

InterPro
IPR006664
Domain

Bacterial outer membrane protein
PR01021	$\"[121-143]T$ $\"[151-166]T$ $\"[166-182]T$	OMPADOMAIN

InterPro
IPR006665
Domain

OmpA/MotB
PD000930	$\"[118-177]T$	Q9ABM6_CAUCR_Q9ABM6;
PF00691	$\"[120-220]T$	OmpA
PS51123	$\"[108-227]T$	OMPA_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.60	$\"[103-225]T$	no description
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[22-42]?$	transmembrane_regions

","BeTs to 13 clades of COG2885COG name: Outer membrane protein and related peptidoglycan-associated (lipo)proteinsFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG2885 is -------q--r---efghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB000498 (OmpA-like transmembrane domain) with a combined E-value of 9e-17. IPB000498E 105-133 IPB000498F 145-192***** IPB006690 (OmpA-like domain) with a combined E-value of 2.1e-15. IPB006690A 119-144 IPB006690B 151-202***** IPB001035 (Sodium-type flagellar protein MotY precursor signature) with a combined E-value of 1.8e-07. IPB001035K 166-183 IPB001035L 183-202","Residues 118-177 are similar to a (MEMBRANE OUTER LIPOPROTEIN OMPA MOTB PRECURSOR SIGNAL CHEMOTAXIS PORIN PEPTIDOGLYCAN-ASSOCIATED) protein domain (PD000930) which is seen in Q9ABM6_CAUCR.","","No significant hits to the PDB database (E-value < E-10).","Residues 120 to 220 (E_value = 7.2e-20) place ANA_0008 in the OmpA family which is described as OmpA family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0009","10794","10276","519","8.12","1.15","18853","ATGACCATCCAACGACGACGCGCCCTCCTAGCATTCTCAACGGCCGGAGCCGCGACGCTTCTGAGCAGCTGTTCCTCAGCACAGCATCCGGGCCCAGAAGGTGACTGGGATCGCCTTGAAGAGGGCGATCTGCTTCTCGCGGTGCCCAAGAACTGGGACCGATCAGTGGCACAGTCCAGCATCTGGGGCACCAAGTGGACCGACCCATCCGACAAGTCGGCCGTCCTCATGACAGCCCAGTCCGTCAAAGCGAAGGACGGCTACGACGCCCTCGACCTGGCCATGAATGCCGCCCGGGCCGTCACTCGCGGGTACCAGCCCATTGGCTCCCGGACCGCCGTCACCAACGGATCCATCATCCTGGCGCAGCAGCAGTACCAGACCACCTGGCCCTACCAGAAGAAGGGCTCCCTCTGGGCCATCAGCCGGGATTCCACGATCTACCTCGTGGACTTCTCCGGAGAGAAGATCACCAGTGATCAGATCTCGACTGTGGGCCAGTGGATCGAGCTGCGCTGA","MTIQRRRALLAFSTAGAATLLSSCSSAQHPGPEGDWDRLEEGDLLLAVPKNWDRSVAQSSIWGTKWTDPSDKSAVLMTAQSVKAKDGYDALDLAMNAARAVTRGYQPIGSRTAVTNGSIILAQQQYQTTWPYQKKGSLWAISRDSTIYLVDFSGEKITSDQISTVGQWIELR$","Lipoprotein, putative","Periplasm, Extracellular","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-24]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-27]?$	signal-peptide

noIPR
unintegrated

unintegrated
PS51257	$\"[1-21]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-21]?$	signal-peptide

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

InterPro
IPR000833
Family

Alpha-amylase inhibitor
SM00783	$\"[172-226]T$	no description

InterPro
IPR007733
Family

Agouti
SM00792	$\"[26-104]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-44]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 36-368 are 40% similar to a (SURFACE ANCHOR WALL FAMILY CELL) protein domain (PD579361) which is seen in Q97P71_STRPN.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","wall surface anchor family protein , putative","","1","","","","","","","","","","","","","Tue Jul 31 14:59:55 2007","","","Tue Jul 31 14:59:55 2007","","Tue Jul 31 14:59:55 2007","","Tue Jul 31 14:59:55 2007","Tue Jul 31 14:59:55 2007","","","","","yes","","" "ANA_0012.1","16873","16190","684","9.48","8.05","23779","ATGCGACGCATGACTCTATGCGACACAATCGCATTTCTCAGACGAGCGCTGGCATCACAGCGTGGAAGCATTCTTCCGTATCTTAGCGTTGCCGTCGGCATTGTCGCCCTGATCGCGTTAACCCTGATGACAGGTTTAGGTGATGTCATTCTGCATCGTCGCGACGCGAGCAACGCTGCGGACGCTGCAGCTTTGGCGGCAGCAGAAGCATGGGGGCATTCGATTGAATCGACATATGGAAACGCTGCGAAGTCTCGCAATGAGCACGACTTCTGGGGAAGCGTCGGGAAAGGGCTCGGTTCATTTGCTGGTCCGACGACCAAGCGGGCCGCCGAGCACTATGCGAAGCTCAATGGCGCCACAGTGACATCCTATTCGGTGGACGAAACCCGAGGTACTGTGACAGTTTCAGTCCGTACGGATTCGACGATCACCTACACCGACGAAAAAATGACTGCCACGTCAACCGCTCAAGTTGTCTTCGATAGCGGCGCGTGCCTCACGGGAGGGAAGGTGGGGGTCGAAATGAACGGGAAGTGCATGACACAACCCGCCTCACACCAATCTACTCCACGTAAGTCCCCTTCTCCTTCGGCGACCCCTCAGGCAACTCCAACAGCAACACCGTTCAAGCCGCCCACAGAAATGCGTGGATCCGCAAGGATATCAGCCCGACTGGTTTAG","MRRMTLCDTIAFLRRALASQRGSILPYLSVAVGIVALIALTLMTGLGDVILHRRDASNAADAAALAAAEAWGHSIESTYGNAAKSRNEHDFWGSVGKGLGSFAGPTTKRAAEHYAKLNGATVTSYSVDETRGTVTVSVRTDSTITYTDEKMTATSTAQVVFDSGACLTGGKVGVEMNGKCMTQPASHQSTPRKSPSPSATPQATPTATPFKPPTEMRGSARISARLV$","Hypothetical protein","Extracellular","","","","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[24-44]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-47]?$	signal-peptide
tmhmm	$\"[15-49]?$ $\"[55-77]?$ $\"[89-107]?$ $\"[113-133]?$	transmembrane_regions

InterPro
IPR006664
Domain

Bacterial outer membrane protein
PR01021	$\"[274-296]T$ $\"[305-320]T$ $\"[320-336]T$	OMPADOMAIN

InterPro
IPR006665
Domain

OmpA/MotB
PD000930	$\"[271-331]T$	Q88NT3_PSEPK_Q88NT3;
PF00691	$\"[273-370]T$	OmpA
PS51123	$\"[261-380]T$	OMPA_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.60	$\"[256-380]T$	no description
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[5-23]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[46-68]?$	transmembrane_regions

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[310-406]T$	HATPase_c
SM00387	$\"[310-407]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[202-269]T$	HisKA_3

InterPro
IPR013991
Domain

PhnA protein N-terminal, proteobacterial
SM00782	$\"[141-181]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[56-76]?$ $\"[82-100]?$ $\"[110-130]?$ $\"[152-172]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 2.7e-13. IPB011712A 201-218 IPB011712B 315-335","No significant hits to the ProDom database.","","","Residues 202 to 269 (E_value = 7.6e-06) place ANA_0014.1 in the HisKA_3 family which is described as Histidine kinase.Residues 310 to 406 (E_value = 6.4e-09) place ANA_0014.1 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","","","1","4","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:57:36 2007","Thu Aug 9 17:57:36 2007","Thu Aug 9 17:57:36 2007","Thu Aug 9 17:41:13 2007","","","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","Thu Aug 9 17:41:13 2007","","Thu Aug 9 17:41:13 2007","","Thu Aug 9 17:41:13 2007","yes","","" "ANA_0014.2","19726","19058","669","4.85","-11.88","24034","ATGAAGGTTCTGGTTGTTGATGATAATCCTATTGTGCGTGCAGGTCTTTCGGCGGTATTGGGACGAATGGCAGATGTCAGCGAGATTTTTGAGGCAGAAGACGCCTTCACCGCACTTGAAATGGCTGCGCTTCATTCTCCGGAGGTCATCCTGCTTGATGTCCTTATGCCGCCAGGACGTTCTGGCGTCGATATTCTTCCGGAGCTTCCGCAATCTTCCTCAGTCATTATGCTGACATCTACTCAAGATTCGTCAACGATTCGTCTTGCCTTGGAGAGAGGAGCAAGGGGGTACTTAGTTCACGGTCAACTCGGTACTAACGAGATCTCTGGGGCTATTGAGACCTGTCGAAATGGTGGGTTAGTTCTGGGGCAGGAAGCTGCCGATGTATTTTTTTGCGACCCACAGAATGAAGAATACAATCCGCTGCTATCAGAACTTTCAGACCGAGAAGCTGAAATTTTGTCGTTGGCTGCGCAGGGTTTAACAAATCAGGAGATCGCCTCTCAGCTATTTCTTTCGGAACGAACGGTAAAAAACTACATCAATGCTACGTACCCCAAGATCGGGGTTCATGACAGGTCTGAGGCGGTCGCCGCCTGGCACAGGGCGGCAACAGGGCGCCGGCAGGGGCGATCGCCCCAAGACAGGGCTGACCAACACCCGTAG","MKVLVVDDNPIVRAGLSAVLGRMADVSEIFEAEDAFTALEMAALHSPEVILLDVLMPPGRSGVDILPELPQSSSVIMLTSTQDSSTIRLALERGARGYLVHGQLGTNEISGAIETCRNGGLVLGQEAADVFFCDPQNEEYNPLLSELSDREAEILSLAAQGLTNQEIASQLFLSERTVKNYINATYPKIGVHDRSEAVAAWHRAATGRRQGRSPQDRADQHP$","Two-component transcriptional regulator, LuxR family","Cytoplasm","","","","","Zhang RG, Pappas T, Brace JL, Miller PC, Oulmassov T, Molyneaux JM, Anderson JC, Bashkin JK, Winans SC, Joachimiak A.Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA.Nature. 2002 Jun;417(6892):971-4.PMID: 12087407","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[148-197]T$	Q9KB13_BACHD_Q9KB13;
PR00038	$\"[147-161]T$ $\"[161-177]T$ $\"[177-189]T$	HTHLUXR
PF00196	$\"[144-201]T$	GerE
SM00421	$\"[144-201]T$	HTH_LUXR
PS50043	$\"[140-205]T$	HTH_LUXR_2
PS00622	$\"[161-188]T$	HTH_LUXR_1

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[2-117]T$	Q82IA9_STRAW_Q82IA9;
PF00072	$\"[1-100]T$	Response_reg
SM00448	$\"[1-113]T$	REC
PS50110	$\"[2-100]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[120-206]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[1-103]T$	no description
PTHR23283	$\"[1-100]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF31	$\"[1-100]T$	SENSOR HISTIDINE KINASE

","BeTs to 10 clades of COG2197COG name: Response regulators consisting of a CheY-like receiver domain and a HTH DNA-binding domainFunctional Class: T,KThe phylogenetic pattern of COG2197 is -------CEBRh---------Number of proteins in this genome belonging to this COG is","***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 1e-21. IPB000792 147-193***** IPB005143 (Autoinducer binding domain) with a combined E-value of 2.5e-12. IPB005143B 147-190***** IPB000673 (CheB methylesterase) with a combined E-value of 1.8e-06. IPB000673A 4-13 IPB000673B 20-73","Residues 2-117 are 63% similar to a (SENSORY TRANSDUCTION PHOSPHORYLATION REGULATOR DNA-BINDING TRANSCRIPTION REGULATION RESPONSE TWO-COMPONENT KINASE) protein domain (PD000039) which is seen in Q82IA9_STRAW.Residues 148-197 are 80% similar to a (DNA-BINDING TRANSCRIPTION REGULATION REGULATOR SENSORY PHOSPHORYLATION TRANSDUCTION RESPONSE TRANSCRIPTIONAL TWO-COMPONENT) protein domain (PD000307) which is seen in Q9KB13_BACHD.","","","Residues 1 to 114 (E_value = 1.4e-20) place ANA_0014.2 in the Response_reg family which is described as Response regulator receiver domain. Residues 137 to 189 (E_value = 7.7e-05) place ANA_0014.2 in the Sigma70_r4_2 family which is described as Sigma-70, region 4. Residues 144 to 201 (E_value = 1.6e-19) place ANA_0014.2 in the GerE family which is described as Bacterial regulatory proteins, luxR family.","","","","1","4","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:57:25 2007","Thu Aug 9 17:57:25 2007","Thu Aug 9 17:57:25 2007","Thu Aug 9 17:50:05 2007","","Mon Aug 20 17:32:41 2007","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:50:05 2007","Mon Aug 20 17:32:41 2007","Thu Aug 9 17:50:05 2007","Mon Aug 20 17:32:41 2007","Thu Aug 9 17:50:05 2007","Thu Aug 9 17:50:05 2007","Mon Aug 20 17:32:41 2007","","Thu Aug 9 17:50:05 2007","","Thu Aug 9 17:50:05 2007","yes","","" "ANA_0014.3","21870","20971","900","9.42","7.15","33781","ATGCTGCCAGTCATCATTGCTTCTTTGTCCTCTTTTTTGGTTCTCATGTCTGCGTACGGCGTTCGCATCATTCGGAGAGAAGGCGCCGAAAAGTATGTTGAGGTCACTGCCGGAAGCGACGTCGACTCGCCTGAAGAAAGACGTCGTCCATTTTATGCTATCATCGACGGCCTTGGATTACGCGCGCAAAGAACCCTTCGAAGGGTATACGGCGAGAAGCGTCTAGACGCGCTGGGCAAGCGAATCAGGCGTGCAGGTAATCCCGAGAACCTTACTTTGGATCAGTATATTCAAAGAGAATCGGGTTTCATAGTCCTGTCCGCAATCATACTGGTTCTATTTACGGCAGTGGGGAACATTTACTTAGGAGTCGCGTTCGGACTGCTTTTTTCTACCTGGATGCAGATCTGGCTATTCTACGAACTGCGGCGCAGGCGAAGTAGGATAGATCGAGACCTACCAGACTTTCTGGACGTTCTGACCGTCACAGTTCGCTCCGGAACACCATTCCGAAACGCGCTCGAGCGAGTGTGTGGGCACTACGCTAGTCCTCTTTCCGATGAAATGATGACTACACTTCGTGAAATACGAATGGGAGTGCCCTTCAGGACGGCATTCCTCAATGTCAAGGACCGATGCGACTCTGACAACTTCGATTCGTTCGTGGTGGCGCTCCTGCAGTCCGAAGAACTCGGCACTCCTATTGCAGATGCACTCCAATCCATAGTAAAAGAGATCAGAAGCGAGCGTGCCGAACAAGTCCGTCAAGCCGCCGCGAAGACATCACCGAAGGTCGCTTTCATTGCAACAGTCACAATGATGCCTGGCACTATGATTCTCATGATGGGAGGAATGTATTACGCGTATGGAGATGTGTTTAGCAAGATTTTTAAAGGGTAG","MLPVIIASLSSFLVLMSAYGVRIIRREGAEKYVEVTAGSDVDSPEERRRPFYAIIDGLGLRAQRTLRRVYGEKRLDALGKRIRRAGNPENLTLDQYIQRESGFIVLSAIILVLFTAVGNIYLGVAFGLLFSTWMQIWLFYELRRRRSRIDRDLPDFLDVLTVTVRSGTPFRNALERVCGHYASPLSDEMMTTLREIRMGVPFRTAFLNVKDRCDSDNFDSFVVALLQSEELGTPIADALQSIVKEIRSERAEQVRQAAAKTSPKVAFIATVTMMPGTMILMMGGMYYAYGDVFSKIFKG$","Type II secretion system protein","Membrane, Cytoplasm","","","","","","","","

InterPro
IPR001992
Family

Bacterial type II secretion system protein
PF00482	$\"[156-283]T$	GSPII_F

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[92-114]?$ $\"[120-140]?$ $\"[265-287]?$	transmembrane_regions

","BeTs to 5 clades of COG2064COG name: Uncharacterized membrane proteinsFunctional Class: SThe phylogenetic pattern of COG2064 is AMTK-----------------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 80-205 are similar to a (MEMBRANE TRANSMEMBRANE PILUS TADB TADC ASSEMBLY FLP INTEGRAL ADHERENCE TIGHT) protein domain (PD340157) which is seen in Q9KY91_STRCO.Residues 209-285 are 59% similar to a (TADC MEMBRANE PILUS TRANSMEMBRANE FLP ASSEMBLY INTEGRAL ADHERENCE TIGHT PROBABLE) protein domain (PD696416) which is seen in Q9KY91_STRCO.","","","Residues 156 to 283 (E_value = 2.7e-18) place ANA_0014.3 in the GSPII_F family which is described as Bacterial type II secretion system protein F domain.","","","","1","4","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:11 2007","Thu Aug 9 18:01:11 2007","Thu Aug 9 18:01:11 2007","Thu Aug 9 18:01:02 2007","","","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","Thu Aug 9 18:01:02 2007","","Thu Aug 9 18:01:02 2007","","Thu Aug 9 18:01:02 2007","yes","","" "ANA_0014.4","22796","21873","924","10.59","13.83","33913","ATGATCGATACGCCATTGATTTTCGTTTGCACGTTAGTCACTTTGATGACTGGCTGTTTTGCGGTCATCACTTTAAGCAGCAATACCTCACGGACCAGCGTGATTGAATATGGTCTAGGAGCAACATCCAACAGCAAACGACAGCCACTGAGAGGGTTGGCATTCAAGTACAACAATCTGTTCTTCAACCTACCATTACGTAGACGCCTGTCTCGGGCTGGACTACGATGGAGTGCACTATCGACTGAGCTAGTTCTTGGAAGTACGATGTTGCTCGTATACCTGGCATGCCGCCAGTTTATTGGGAATATTGCCGGCATGATTATGGCGCTTTCTACTCCGTTATTTTTCTTTCGTTGGCTTCAACGAAAGATACTACAACGTACCGAGCGGTTCGTAGACCAACTTCCCGAGGTGTCTAGAACTCTCTCTAACGGGACGTCCGCTGGCTTGTCAATAGAGAGGGCGCTTGCACTTGCTTCGCAAGAATCGTCGGATCCAGCTCGAACCGAGCTCCAGCAAGTGGTCGCTCAACTATCCTTGGGGCGATCGTTGGAGTACGCCATGAACAGCATGTCTGATCGAATGCCGTCCCGTGAGCTCAACATACTCGTGCGCACCATTGTCATCCAGTCTCGGTCGGGTGGTGCTCTTGTCTCAGCGCTACAGGACATAGCGAGAGCCTTAGAGGATCGAAAGCAACTCCGTCGAGAAGTGCGTACCGCGATATTGAGTGCCTCCGTGAGCGGATACATCGTTCCTTTCATCGGGATAGCGGCTGTTCTACTGATCAATGCAATGAAGCCTGGGGTTCTTGACGAGATGGCAAGGACAACTTTGGGACAGATTATCCTGCTGTCCTCACTGTTGTGTATTTTCTCGGGAATCATCCTGATGCGTATATTCTCGCGAGTTGAGGTGTGA","MIDTPLIFVCTLVTLMTGCFAVITLSSNTSRTSVIEYGLGATSNSKRQPLRGLAFKYNNLFFNLPLRRRLSRAGLRWSALSTELVLGSTMLLVYLACRQFIGNIAGMIMALSTPLFFFRWLQRKILQRTERFVDQLPEVSRTLSNGTSAGLSIERALALASQESSDPARTELQQVVAQLSLGRSLEYAMNSMSDRMPSRELNILVRTIVIQSRSGGALVSALQDIARALEDRKQLRREVRTAILSASVSGYIVPFIGIAAVLLINAMKPGVLDEMARTTLGQIILLSSLLCIFSGIILMRIFSRVEV$","Integral membrane protein","Membrane, Cytoplasm","","","","","","","","

InterPro
IPR001992
Family

Bacterial type II secretion system protein
PF00482	$\"[139-266]T$	GSPII_F

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[77-97]?$ $\"[101-121]?$ $\"[242-264]?$ $\"[283-303]?$	transmembrane_regions

","BeTs to 9 clades of COG2064COG name: Uncharacterized membrane proteinsFunctional Class: SThe phylogenetic pattern of COG2064 is AMTK-----------------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 91-188 are 62% similar to a (MEMBRANE TRANSMEMBRANE PILUS TADB TADC ASSEMBLY FLP INTEGRAL ADHERENCE TIGHT) protein domain (PD340157) which is seen in Q9KY92_STRCO.Residues 189-265 are similar to a (TADB PILUS MEMBRANE ASSEMBLY FLP TRANSMEMBRANE SECRETION PROBABLE INTEGRAL ADHERENCE) protein domain (PD603644) which is seen in Q82IA6_STRAW.","","","Residues 139 to 266 (E_value = 5.1e-17) place ANA_0014.4 in the GSPII_F family which is described as Bacterial type II secretion system protein F domain.","","","","1","4","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:30 2007","Thu Aug 9 18:05:30 2007","Thu Aug 9 18:05:30 2007","Thu Aug 9 18:06:10 2007","","","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","Thu Aug 9 18:05:15 2007","","Thu Aug 9 18:05:15 2007","","Thu Aug 9 18:05:15 2007","yes","","" "ANA_0015","24100","22811","1290","5.60","-9.02","47611","ATGGCACTCCGAGATCGTATTTCCGTCCCGATTTCTAAATCAACTCGAGCCTCCAAAGACAAGGAGGACCTCGTCACGCTCTACAAAGCTCGCCTTCTTGACGAAATCAATTTGGAGGAGGTTGCCGAGCTTGAGCTGGCTCAGCAACGTGCACGCCTAGAAAGAGTGCTTTCAAGGCTGCTCTCGCTTGAAGGCCCCGTCATGACGCCTCGCGAGCGCGCTTGGCTCATCAAAAGAGTCATCGATGACGCCGTTGGCTTAGGAGTGCTCGAACCCCTGATCGCAGATGAAACGGTCACTGAAATCATGGTCAACGGAGTCGACGATGTGTTCATTGAACGTTCCGGCCGAATAGAACGGGTGCCAACAAAATTCACGTCGGAAGCCGAGATATACCGGCTTATTGACCGCATCGTCTCATCGGTGAATCGCCGCGTCGACGAATCAAGTCCTATGGTGGACGCCCGTCTGGCAGGAGGCGAACGTGTCAACGTCATTATCCCTCCATTGGCTCTCGACGGACCCAGCATCACCATTCGTCGATTTCCTCAACCGTTCCAACTCTCTGACCTCGTCAACCGGAACAGCATTCCTTCAGAAGCTGCCGAATTTCTTGAGGCACTGGTCACCGCACGTTTCAGCATTCTGGTCTCCGGAGGAACTGGCACAGGAAAAACAACCTTCCTCAATGCCCTTTCCGGGGTGATTTCAGACCATGAACGTATCATCACAATCGAAGACGCCGCGGAGCTCTCGTTGCAACAGCCTCACGTCGTGCGTCTTGAAGCAAGACCGCCCAATATTGAGGGCAAGGGGCAGGTAACTATCCGTGACTTGGTGAAAAATTCACTGCGCATGCGCCCCGATAGAATCATTGTTGGTGAAGTTCGTGGGGGCGAGGCGCTGGACATGCTGCAGGCCATGAATACCGGCCATGAAGGCTCACTTACAACAGTCCACGCCAATTCGCCGATCGACGCCTTAAGCCGGCTTGAAACACTAGCCACGATGTCTGACGTGACACTTCCAGTGGATACCATCAGGGATCAAATCAACGGAGCTATTGACATCATAGTACAACTTGAAAGAGATTCTCAAGGCATGCGTCGCGTCAATACGATCGAAGCGGTGGTTTCAGAACATCGTGAACACTATTCAACAACTGTTCTTTTACGCCACGTCAAGAACGACGGAGAACTGGGGGACCATTTCGAGTTCCGCGGACTGCCCGACAACGTAAAACAACGTCTTCAAAGAAGCGGCATCCGTGTCGAAACTTCTGCGAGTTGA","MALRDRISVPISKSTRASKDKEDLVTLYKARLLDEINLEEVAELELAQQRARLERVLSRLLSLEGPVMTPRERAWLIKRVIDDAVGLGVLEPLIADETVTEIMVNGVDDVFIERSGRIERVPTKFTSEAEIYRLIDRIVSSVNRRVDESSPMVDARLAGGERVNVIIPPLALDGPSITIRRFPQPFQLSDLVNRNSIPSEAAEFLEALVTARFSILVSGGTGTGKTTFLNALSGVISDHERIITIEDAAELSLQQPHVVRLEARPPNIEGKGQVTIRDLVKNSLRMRPDRIIVGEVRGGEALDMLQAMNTGHEGSLTTVHANSPIDALSRLETLATMSDVTLPVDTIRDQINGAIDIIVQLERDSQGMRRVNTIEAVVSEHREHYSTTVLLRHVKNDGELGDHFEFRGLPDNVKQRLQRSGIRVETSAS$","Type II secretion system protein","Cytoplasm","type II secretion system protein","K02283 pilus assembly protein CpaF","type II secretion system protein E","","Salmond G.P., Reeves P.J. Membrane traffic wardens and protein secretion in gram-negative bacteria. Trends Biochem. Sci. 1993. 18(1):7-12. PMID: 8438237Hobbs M., Mattick J.S. Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes. Mol. Microbiol. 1993. 10(2):233-243. PMID: 7934814","","","

InterPro
IPR001482
Domain

Bacterial type II secretion system protein E
PD000739	$\"[190-289]T$	Q82IA5_STRAW_Q82IA5;
PF00437	$\"[76-365]T$	GSPII_E

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[178-375]T$	no description

","BeTs to 13 clades of COG0630COG name: Type IV secretory pathway, VirB11 components, and related ATPases involved in archaeal flagella biosynthesisFunctional Class: 1, ,NThe phylogenetic pattern of COG0630 is aompkz----r----f-hs-ujx---Number of proteins in this genome belonging to this COG is 3","***** IPB001482 (Bacterial type II secretion system protein E) with a combined E-value of 2.2e-42. IPB001482B 211-231 IPB001482C 241-251 IPB001482D 274-319","Residues 85-188 are similar to a (PLASMID TYPE SECRETION VIRB11 SYSTEM ATP-BINDING TRBB IV II TRANSFER) protein domain (PD003019) which is seen in Q9KY93_STRCO.Residues 86-365 are 44% similar to a (TYPE RELATED III B11 TVG1067415 VIR EXPORT NUCLEOTIDE BINDING) protein domain (PD252959) which is seen in Q979W9_THEVO.Residues 190-289 are similar to a (ATP-BINDING SECRETION TYPE PLASMID TWITCHING II PATHWAY SYSTEM E GENERAL) protein domain (PD000739) which is seen in Q82IA5_STRAW.Residues 295-394 are 71% similar to a (ATP-BINDING SECRETION TYPE PLASMID TWITCHING II PATHWAY SYSTEM E GENERAL) protein domain (PD002760) which is seen in Q7UR21_RHOBA.","","-54% similar to PDB:2OAP Crystal structure of the archaeal secretion ATPase GspE in complex with AMP-PNP (E_value = 5.4E_31);-54% similar to PDB:2OAQ Crystal structure of the archaeal secretion ATPase GspE in complex with phosphate (E_value = 5.4E_31);-52% similar to PDB:1G6O CRYSTAL STRUCTURE OF THE HELICOBACTER PYLORI ATPASE, HP0525, IN COMPLEX WITH ADP (E_value = 7.3E_28);-52% similar to PDB:1NLY Crystal structure of the traffic ATPase of the Helicobacter pylori type IV secretion system in complex with ATPgammaS (E_value = 7.3E_28);-52% similar to PDB:1NLZ Crystal structure of unliganded traffic ATPase of the type IV secretion system of helicobacter pylori (E_value = 7.3E_28);","Residues 76 to 365 (E_value = 3e-127) place ANA_0015 in the GSPII_E family which is described as Type II/IV secretion system protein.","","II secretion system protein (AF229646)","","1","4","","","","","","","","","","","","Thu Jul 26 17:14:57 2007","","","Thu Jul 26 17:13:44 2007","Thu Jul 26 17:13:44 2007","Thu Jul 26 17:13:44 2007","","Thu Jul 26 17:13:44 2007","Thu Jul 26 17:13:44 2007","","","","","yes","","" "ANA_0016","26041","24512","1530","5.94","-5.45","54348","ATGCTGTATCTAGTGACGAACCACGAAGAGACGCGTCAGCAGGTACTGGCGGCCATTGCCGAGGCAGAAGGAATCGGCGAGGTCCGCACGGTGGCCTCACCCGAGAAGCTGAGAGAATACATAGATCCCGACGTCACATCATGCGTCTTGGTCGACGAGGCATTGGCGCCGCACGCGGCTATGCCCACCGTTCAAGAGTTTTCTCATGCCTACCCACTCATCCCAGTCGTCCTGTTGAGCCGGACTCACACGTCCGAGAGTGTTGTCGCAGCAATGGACTCCGGCGCAAGGACCGTCCTGGCTCTTCCGTTGTCACTCGAGGAGATAACAAACCGTCTTCTTCCTGTTCTGGCATGGTCACGTGCAGTTCGTAGCGAAGCGTCAAGCAGAGAAGAGCTCACCACACGTCGCCAGGGCACGATTACCGCCATCGTGGGCGCCAAGGGAGGTGTGGGAACATCGACGATGGCACTCATGGCTGCAGCGCAACTCGCTCAGGGCACCCGCACCTGTTTGGTGGATCTCGATGTCCGCAGCGGCGATCTCGCTGCAATGACAGGTATCTCGGTACGTCGATCTATCGCCGATCTGGCCGACATAGCAGCCGAGGCCAGTACACGAGAAATTACCGAAGTCATGTATCCCCTCCCCGGCGGCATCTCCCTTCTCCCCGCCCCAGAACAGGGTGAAACAGGCGAGGCCCTTACTGAGTCCGCCACACGCCAGATTCTTGCCATGCTGCGCTACCAGTTCGACCATGTGATTCTGGACTGCGGTTGCCGGCTCGACGACGTTCTGGCCATGGGCCTTGACTCTGCCGACCAAGTGCTCATCGTGGCAACGCCCGACGCGCCGGCTCTGCGCTCCGTACGCAGGCTGACTGATGCTCTCGATCGGCTCGACATATCACTTGGGCGCTCTTTCGGGCTGGTGGTCAACATGACCACCCGGCGACGCGAGATCCAGCCCACCACAGCTGCGAAAATGACCGGAATAGCGTTGGCCACCAGCGTTCCCGACCTCACGGCGCACATCGAGATGGCAGTGAACTCGAACACTCTACTGACCTCGAAAGTCCCCTCGATGGCTAAAGCTGCCCGCTCTCTGTCCGACAGCATCTCAAGATACACTGCAGCGCCTCCAGATGCCGCTGCCCATCAAACGACCAGTCCGACCAAGTCGACACGACGACGCTGGCTTCGTCGCACAGAGCGAGGGCAAATCACCGTAGAGTTCCCCATTGTGTTCGCTCTGGCAACAGCCGCAATCTTGATGTGCGTCCAGGCGCTCAGCATCGGGGTGACATACATGTATGCCACGAACGCAGCCAACGAAGCGGCACGTGCTTACGGGACTGGTAAGACTCCAACCCAAGTACAACAGGTCGTCGCACAAAAACTACCTGACACGTACGTTCAAGGATTGAAGATCACCCGTTCTGGCTCCGACAACGTAACCGTCACTCTTCCCATCCCGTCGGTCGTTGACATCACCACTTCCGCCGACGCCGGAATCGTTTGGGAGAAATAA","MLYLVTNHEETRQQVLAAIAEAEGIGEVRTVASPEKLREYIDPDVTSCVLVDEALAPHAAMPTVQEFSHAYPLIPVVLLSRTHTSESVVAAMDSGARTVLALPLSLEEITNRLLPVLAWSRAVRSEASSREELTTRRQGTITAIVGAKGGVGTSTMALMAAAQLAQGTRTCLVDLDVRSGDLAAMTGISVRRSIADLADIAAEASTREITEVMYPLPGGISLLPAPEQGETGEALTESATRQILAMLRYQFDHVILDCGCRLDDVLAMGLDSADQVLIVATPDAPALRSVRRLTDALDRLDISLGRSFGLVVNMTTRRREIQPTTAAKMTGIALATSVPDLTAHIEMAVNSNTLLTSKVPSMAKAARSLSDSISRYTAAPPDAAAHQTTSPTKSTRRRWLRRTERGQITVEFPIVFALATAAILMCVQALSIGVTYMYATNAANEAARAYGTGKTPTQVQQVVAQKLPDTYVQGLKITRSGSDNVTVTLPIPSVVDITTSADAGIVWEK$","Septum site-determining protein","Cytoplasm, Membrane","putative septum site-determining protein","septum site-determining protein","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[28-109]T$	Q8F3K2_LEPIN_Q8F3K2;
PF00072	$\"[71-114]T$	Response_reg
SM00448	$\"[1-113]T$	REC
PS50110	$\"[2-117]T$	RESPONSE_REGULATORY

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[1-137]T$	no description
G3DSA:3.40.50.300	$\"[140-377]T$	no description

","BeTs to 9 clades of COG2894COG name: Septum formation inhibitor-activating ATPaseFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG2894 is -------qvd--bcefg-snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002586 (Cobyrinic acid a,c-diamide synthase) with a combined E-value of 1.4e-06. IPB002586A 142-175 IPB002586B 247-269","Residues 144-225 are 65% similar to a (PLASMID ATPASE ARSENICAL PARA ATP-BINDING RESISTANCE PUMP-DRIVING PARTITIONING PHOSPHORYLATION TRANSDUCTION) protein domain (PD023530) which is seen in Q9ZF15_STRGR.Residues 226-351 are 59% similar to a (SITE-DETERMINING PHOSPHORYLATION TRANSDUCTION SENSORY SEPTUM MIND) protein domain (PD092592) which is seen in Q9KY96_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 114 (E_value = 0.00037) place ANA_0016 in the Response_reg family which is described as Response regulator receiver domain.","","septum site-determining protein","","1","4","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0017","26760","26041","720","5.11","-5.79","25867","ATGAATCCACGTCAACGACGAGGCGTCCTCCTCATTCTCGTCACGATCCTCGGTGCAGTGGTGACCTTCGTAGCTGTCTTCAGTTACGTTCAGTCGGTCTCATCCCAGGTAGGCCCCATGACAACTGTTCTCAAGCTGTCGCAGCAGGTGACTGAGCTCAAGGAAATCAAAGCGGAGGACGTGGTCGCCGAGCAGGTTCCCAAGCGCTGGGTTCCCGACGACGCAGTGCACGACATCAAGGACGTCCAGGGAAAGGTCACGGCGGCCACATACAGCAAAGGTGCGGTGCTGCAGTCCAGCATGCTTCAGGACCCTCCACAGCTAACAGAAGGATATCGCGAGATATCGATCATGATCGACGCAGAGACAGGCGTTGCCGGAAAGGTGACTCCAGGATCGCGCGTCGACATCGTCTCCACACTGGAGGATCCGAACTCTAAAGCCCAAAAGGCTGAAATCATTATTGAGAATGCTCTCATTACTGAAGTCGGCGTTGTGACGAAAGTACAAGAAAAGGACAGTGACGGTAACTTCTCAGAAGAAAAAGACAGCCTTCCCGTGACCTTCTCGCTGACGCCTGAGCAGTCACTCAAGCTTGCCTACGCCGAGAGCTATTCAACAAAGGTTCGTCTCCTGCTGCGCCGCGACGGAGACCAGGGAAGCGCCAAGACCCAAGAATACTCCGCCAACAACGGAACTCCTGCTCAAGGAACAAACTGA","MNPRQRRGVLLILVTILGAVVTFVAVFSYVQSVSSQVGPMTTVLKLSQQVTELKEIKAEDVVAEQVPKRWVPDDAVHDIKDVQGKVTAATYSKGAVLQSSMLQDPPQLTEGYREISIMIDAETGVAGKVTPGSRVDIVSTLEDPNSKAQKAEIIIENALITEVGVVTKVQEKDSDGNFSEEKDSLPVTFSLTPEQSLKLAYAESYSTKVRLLLRRDGDQGSAKTQEYSANNGTPAQGTN$","Flp pilus assembly protein CpaB","Periplasm, Membrane, Extracellular","conserved hypothetical protein","hypothetical protein","SAF domain","","","","","

InterPro
IPR013974
Domain

SAF domain
PF08666	$\"[41-103]T$	SAF

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[10-30]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 45-164 are 65% similar to a (PILUS ASSEMBLY CPAB FLP PROBABLE SIGNAL MEMBRANE PLASMID PEPTIDE EXPORTED) protein domain (PD317430) which is seen in Q82IA2_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 41 to 103 (E_value = 0.0015) place ANA_0017 in the SAF family which is described as SAF domain.","","hypothetical protein","","1","4","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0018","28586","27777","810","6.52","-1.28","27629","ATGTCTCCCCAACCTTGGCTGCTCGGCGCCGTCGCGCTCGGCTCCGTTGCGCTCATCGCCGGACCGGTCTCCGCGTGGACGAGGCGCTACGTGCGAGAACCGTTCAAGGACGAGGGCGAGTCTGACGCCGGCTCGCGCTCCGAGACGGCCACCTCAGAAGACGCTGCGGATGGCACCACAGCCCGTGCAGGGAGTACCACCGAGCCACTCTCAGACGCCTCAGAGCCTCCCGCATCGTTTGAGCATCCGACACTCAAGCATCCCGGCCTCCTGGGCACGGCACCACAAGGACTGCTGGCCCTGACTCTGTGCTTCCTGTGCGTCTGGTGGGGCAGTCGGATAGGTACCACCGCCGCGACTCTCACTGCCATCCCCGTGTATGCACTTCTCGGATGCGCCGGAAGTGTCGACGCCGTGGCGCACCTACTGCCCAACCGCCTGCTGGGCGCCACGGCCGCTTGGCTGGCCGCCTGCGGGGTGGTCGCCGTTGCTATGGAACCCGGCAGAGCCCACACCGCGCTCACCGCGGCTCTGTGCGCACTGGCGGTGGGCAGCGTCAGCCTGGCCTTGGCGTACGTCCGCACCGGCCTGGGACTGGGAGATGTCAAGCTCGCCGCGGTGATCGGTCTCTGGCTGGGGTGGTTCGATCCCTGGATGCTCGCCTTCGGACTGTGCGTCGGAGTATTCCTGGGCGGAATCGCGGCATTGTTGCTGCTCATCACACGCCGAGCCTCTCGCAAGGACCCTATGGCCTACGGCCCGTACCTCATCGCCGGCGCCCTGCTCACCTGGCCATTGGCGATTGTCTGA","MSPQPWLLGAVALGSVALIAGPVSAWTRRYVREPFKDEGESDAGSRSETATSEDAADGTTARAGSTTEPLSDASEPPASFEHPTLKHPGLLGTAPQGLLALTLCFLCVWWGSRIGTTAATLTAIPVYALLGCAGSVDAVAHLLPNRLLGATAAWLAACGVVAVAMEPGRAHTALTAALCALAVGSVSLALAYVRTGLGLGDVKLAAVIGLWLGWFDPWMLAFGLCVGVFLGGIAALLLLITRRASRKDPMAYGPYLIAGALLTWPLAIV$","Type IV peptidase","Membrane, Cytoplasm, Extracellular","probable type IV peptidase","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Szecsi P.B. The aspartic proteases. Scand. J. Clin. Lab. Invest. Suppl. 1992. 210:5-22. PMID: 1455179Rawlings N.D., Barrett A.J. Families of cysteine peptidases. Meth. Enzymol. 1994. 244:461-486. PMID: 7845226","","","

InterPro
IPR000045
Domain

Peptidase A24A, prepilin type IV
PF01478	$\"[124-240]T$	Peptidase_A24

noIPR
unintegrated

unintegrated
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[4-26]?$ $\"[91-113]?$ $\"[119-139]?$ $\"[173-193]?$ $\"[220-240]?$ $\"[250-268]?$	transmembrane_regions

","BeTs to 7 clades of COG1989COG name: Signal peptidase, cleaves prepilin-like proteinsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1989 is aom-kz-qvd-lbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 124 to 240 (E_value = 0.0024) place ANA_0018 in the Peptidase_A24 family which is described as Type IV leader peptidase family.","","type IV peptidase","","1","4","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0018.1","29043","28597","447","11.35","8.83","16057","ATGAGTACGACGACTCCCACCTGGTCCACCGATCCGGTAGGCACGCTTCCCCGCCTCACCGTGGACGGGCAGGATACCGGGCTGGCGCTGTGGACCGCACGTACCCGGCGCGAGCGCAACATCGGCTTGCTGGGTACCGACTCGATCGACGGGGCCCTGTGGATCACTCGTTGCAACTGGGTGCACTGCTTCCGCATGCGTCACACGATCGACGTCGTCTATGTGGGGCGCCATGGGAGGGTCATCGCGGTGACGACGATGCCGCCAAACCGGATGGGAATGCCCCGGCTGCTCGCGACGGCCGTCGTCGAGATGCGGCAGGGAGACGCCTCTCGCCTGGGAATCCGCAGGGGCAGCATCCTGACACCGTCCCCTGCCGAGCCGCCCCCACGACCCGCCCCCGGTTCAGCAGGAGCCCAGAGCAAGGCGCTCGGATTGATTCACTGA","MSTTTPTWSTDPVGTLPRLTVDGQDTGLALWTARTRRERNIGLLGTDSIDGALWITRCNWVHCFRMRHTIDVVYVGRHGRVIAVTTMPPNRMGMPRLLATAVVEMRQGDASRLGIRRGSILTPSPAEPPPRPAPGSAGAQSKALGLIH$","Secreted protein","Periplasm, Membrane","","","","","","","","

InterPro
IPR003795
Family

Protein of unknown function DUF192
PF02643	$\"[16-125]T$	DUF192

","BeTs to 4 clades of COG1430COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG1430 is -mtk--vc--------ol---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 33-119 are similar to a (UPF0127 SIGNAL PLASMID EXPORTED DUF192 PRECURSOR PEPTIDE UNCHARACTERIZED SECRETED PF1050) protein domain (PD188026) which is seen in Q9KY83_STRCO.","","","Residues 16 to 125 (E_value = 6.9e-14) place ANA_0018.1 in the DUF192 family which is described as Uncharacterized ACR, COG1430.","","","","1","","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:18 2007","Tue Aug 14 18:01:18 2007","Tue Aug 14 18:01:18 2007","Tue Aug 14 18:01:05 2007","","","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","Tue Aug 14 18:01:05 2007","","Tue Aug 14 18:01:05 2007","","Tue Aug 14 18:01:05 2007","yes","","" "ANA_0019","29499","29873","375","11.49","23.60","13649","GTGCCTACCATTCAGCAGCTGGTCCGCAAGGGCCGCTCGACGAAGCGCTCCGCGTCCAAGACGCCGGCGCTCAAGGCCAGTCCGCAGCGCCGTGGCGTGTGCACCCGTGTGTACACCACGACCCCTAAGAAGCCGAACTCCGCCCTCCGTAAGGTCGCCCGTGTGCGCCTGTCCACCGGTATCGAGGTCACGGCCTACATCCCCGGTGAGGGCCACAACCTCCAGGAGCACTCCATCGTGCTCGTGCGCGGTGGTCGTGTGAAGGACCTTCCCGGTGTCCGCTACCACATCGTGCGCGGTGCCCTCGACACCCAGGGTGTCAAGGGCCGCCAGCAGGCACGTTCCAAGTACGGCGCCAAGAAGGAGAAGAAGTAA","VPTIQQLVRKGRSTKRSASKTPALKASPQRRGVCTRVYTTTPKKPNSALRKVARVRLSTGIEVTAYIPGEGHNLQEHSIVLVRGGRVKDLPGVRYHIVRGALDTQGVKGRQQARSKYGAKKEKK$","Ribosomal protein S12","Cytoplasm, Extracellular","ribosomal protein S12","30S ribosomal protein S12","ribosomal protein S12","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR005679
Family

Ribosomal protein S12, bacterial and chloroplast form
PR01034	$\"[27-42]T$ $\"[42-57]T$ $\"[58-77]T$ $\"[77-94]T$ $\"[94-110]T$ $\"[110-122]T$	RIBOSOMALS12
PTHR11652:SF1	$\"[2-123]T$	30S RIBOSOMAL PROTEIN S12
TIGR00981	$\"[1-124]T$	rpsL_bact: ribosomal protein S12

InterPro
IPR006032
Family

Ribosomal protein S12/S23
PTHR11652	$\"[2-123]T$	30S RIBOSOMAL PROTEIN S12 FAMILY MEMBER
PF00164	$\"[2-123]T$	Ribosomal_S12
PS00055	$\"[43-50]T$	RIBOSOMAL_S12

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[1-123]T$	no description

","BeTs to 26 clades of COG0048COG name: Ribosomal protein S12Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0048 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005679 (Ribosomal protein S12 signature) with a combined E-value of 1e-85. IPB005679A 27-42 IPB005679B 42-57 IPB005679C 58-77 IPB005679D 77-94 IPB005679E 94-110 IPB005679F 110-122","Residues 1-68 are similar to a (RIBOSOMAL S12 RRNA-BINDING RNA-BINDING 30S TRNA-BINDING RIBONUCLEOPROTEIN CHLOROPLAST MITOCHONDRION 40S) protein domain (PD605007) which is seen in RS12_LEPIN.Residues 69-94 are identical to a (RIBOSOMAL S12 RRNA-BINDING RNA-BINDING 30S TRNA-BINDING RIBONUCLEOPROTEIN CHLOROPLAST MITOCHONDRION MITOCHONDRIAL) protein domain (PD885016) which is seen in RS12_BIFLO.","","-84% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 1.3E_49);-84% similar to PDB:1GIX Crystal structure of the ribosome at 5.5 A resolution. This file, 1GIX, contains the 30S ribosome subunit, three tRNA, and mRNA molecules. 50S ribosome subunit is in the file 1GIY (E_value = 1.3E_49);-84% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 1.3E_49);-84% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 1.3E_49);-84% similar to PDB:1HNZ STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH HYGROMYCIN B (E_value = 1.3E_49);","Residues 2 to 123 (E_value = 4.5e-76) place ANA_0019 in the Ribosomal_S12 family which is described as Ribosomal protein S12.","","protein S12 (rpsL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0020","29873","30343","471","10.70","12.42","17588","ATGCCTCGTAAGGGTCCCGCACCCAAGCGCCCGCTCGTCGTCGACCCCGTCTACGGCTCGCCGGTCGTCACCCAGCTCGTCAACCGCGTTCTGCTGGACGGCAAGAAGTCCACCGCTGAGCGGATCGTCTACGGCGCCCTGGAGGGCGTGCGCTCCAAGACGGACCAGGACCCGGTCTCGGTCCTCAAGCGCGCTCTGGACAACATCCGCCCCGCCCTGGAGGTCCGCTCCCGTCGCGTCGGTGGCGCCACCTACCAGGTGCCCGTCGAGGTCCGCCCCGGCCGCGCCACCACCCTGGCTCTGCGCTGGCTCGTGGACTTCTCCCGCCAGCGCCGCGAGAACACCATGACCGAGCGTCTCATGAACGAGATTCTCGACGCCTCCAACGGCCTGGGCGCCGCGGTCAAGCGCCGTGAGGACATGCACCGCATGGCCGAGTCCAACAAGGCCTTCGCCCACTACCGCTGGTAG","MPRKGPAPKRPLVVDPVYGSPVVTQLVNRVLLDGKKSTAERIVYGALEGVRSKTDQDPVSVLKRALDNIRPALEVRSRRVGGATYQVPVEVRPGRATTLALRWLVDFSRQRRENTMTERLMNEILDASNGLGAAVKRREDMHRMAESNKAFAHYRW$","Ribosomal protein S7","Cytoplasm, Periplasm","ribosomal protein S7","ribosomal protein S7","ribosomal protein S7","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Klussmann S., Franke P., Bergmann U., Kostka S., Wittmann-Liebold B. N-terminal modification and amino-acid sequence of the ribosomal protein HmaS7 from Haloarcula marismortui and homology studies to other ribosomal proteins. Biol. Chem. Hoppe-Seyler 1993. 374(5):305-312. PMID: 8338632","","","

InterPro
IPR000235
Family

Ribosomal protein S7
PD000817	$\"[26-142]T$	RS7_STRRP_P95847;
G3DSA:1.10.455.10	$\"[6-156]T$	no description
PIRSF002122	$\"[15-156]T$	Ribosomal protein S7/S5
PTHR11205	$\"[1-156]T$	RIBOSOMAL PROTEIN S7
PF00177	$\"[1-149]T$	Ribosomal_S7
PS00052	$\"[20-46]T$	RIBOSOMAL_S7

InterPro
IPR005717
Family

Ribosomal protein S7, bacterial and organelle form
TIGR01029	$\"[3-156]T$	rpsG_bact: ribosomal protein S7

","No hits to the COGs database.","***** IPB000235 (Ribosomal protein S7) with a combined E-value of 4.8e-73. IPB000235A 15-48 IPB000235B 53-101 IPB000235C 123-155","Residues 2-25 are identical to a (RIBOSOMAL S7 30S RRNA-BINDING RNA-BINDING TRNA-BINDING RIBONUCLEOPROTEIN) protein domain (PD089561) which is seen in RS7_MICLU.Residues 18-155 are 50% similar to a (Y57G11C.34) protein domain (PD529058) which is seen in Q95Q11_CAEEL.Residues 26-142 are similar to a (RIBOSOMAL S7 RRNA-BINDING RNA-BINDING 30S CHLOROPLAST RIBONUCLEOPROTEIN TRNA-BINDING 40S S7P) protein domain (PD000817) which is seen in RS7_STRRP.Residues 28-156 are 48% similar to a (RIBOSOMAL S7 MITOCHONDRION RIBONUCLEOPROTEIN) protein domain (PDA0W810) which is seen in Q9G8T7_EEEEE.","","-80% similar to PDB:1HUS RIBOSOMAL PROTEIN S7 (E_value = 6.4E_54);-75% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 4.1E_45);-75% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 4.1E_45);-75% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 1.6E_44);-75% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 1.6E_44);","Residues 1 to 149 (E_value = 1.9e-85) place ANA_0020 in the Ribosomal_S7 family which is described as Ribosomal protein S7p/S5e.","","protein S7 (rpsG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0021","30389","32530","2142","5.03","-31.61","77970","GTGGCACTTGACGTGCTGACAGACCTCACCAAGGTCCGCAACATCGGCATCATGGCCCACATCGATGCCGGTAAGACCACCGTGACAGAGCGCATCCTGTTCTACACGGGCATCAACTACAAGATCGGCGAGACGCACGACGGCGCCTCGACGATGGACTGGATGGAGCAGGAGCAGGAGCGCGGTATCACCATTACCTCCGCGGCCACCACCTGCTTCTGGAAGAACAACCAGATCAACATCATCGACACCCCCGGACACGTGGACTTCACGGTCGAGGTCGAGCGCTCCCTGCGCGTGCTCGACGGCGCCGTGGCGGTCTTCGACGGCAAGGAGGGTGTGGAGCCGCAGTCGGAGACGGTGTGGCGCCAGGCGGACAAGTACAACGTCCCGCGCATCTGCTACATCAACAAGATGGACAAGCTGGGCGCGGACTTCGACTTCTCCGTCCAGACCATTCGTGACCGCCTCCACGCCACCCCGATCGTCCTCAACTTCCCGATCGGCGCCGAGAACGACTTCTCCGGCCTCGTCGACGTCCTGGAGATGCGGGCCATCCGCTTCCCCGAGAAGGACGCCGACGGCAAGGAGACCCGCGGCTCCGTCGTCGAGTACGAGGAGATCCCCTCCGAGCTGGTCGCCAAGGCCGAGGAGCTGCGCGCCCAGCTGGTCGAGACGGTCGCCGAGGCCGACGACGCCCTCATGGAGAAGTACCTCGAGGGCGAGGAGCTCAGCATCGCCGAGCTCAAGTCCGGCATCCGCAAGCTCACCGTGGCCGGTGAGGCCTTCCCGGTCCTGGCCGGGTCCGCCTTCAAGAACAAGGGCATCCAGCCCGTGCTCGACGCCGTCCTGGACTACCTGCCCTCCCCGCTCGACGTCCCCGACGTCGAGGGCCACGCCGTCGGTAACGAGGAGGAGGTGCTCACCCGTCCGGCCGACGAGAAGGCTCCCTTCTCCGCCCTGGCCTTCAAGGTGGCCACCCACCCCTTCTACGGCAAGCTCGTCTACGTGCGCGTCTACTCCGGCAAGGTCTCCCAGGGCGAGATGGTCCTCAACGCCACCAAGGGCAAGAAGGAGCGCATCGGCAAGCTCTTCCAGATGCACTCCAACAAGGAGAACCCGGTGGAGGAGGCCCACGCCGGCCACATCTACGCCTTCATCGGCCTCAAGGACGTCACCACCGGTGACACCCTGTGCGCCCAGGGCTCCCCGATCGTCCTGGAGTCCATGACCTTCCCGGCCCCGGTCATCCACGTGGCCATCGAGCCCAAGACCAAGGGCGACCAGGAGAAGCTGGGTGTGGCCATCCAGAAGCTCTCCGAGGAGGACCCCACCTTCACCGTCTCCCTCGACGAGGAGACCGGCCAGACCGTCATCGGCGGTATGGGCGAGCTCCACCTGGACGTGTTCGTGGACCGTATGCGCCGCGAGTTCAAGGTCGAGGCCAACGTGGGTGCTCCGCAGGTCGCCTACCGCGAGACCATCCGCAAGAAGGTGGACAAGGTCGAGTACACCCACAAGAAGCAGACGGGTGGCTCCGGCCAGTTCGCCAAGGTGCAGATGAGCTTCGAGCCCCTCGTGGCCGACGAGGCCGCCGAGACCGCCGACGGCGAGAAGGCGCACTACGAGTTCGCCAACGCCGTCACCGGTGGCCGCGTGCCCCGCGAGTACATCCCCAGCGTGGACGCCGGAGTCCAGGACGCCATGCTCACCGGTGTCCTGGCCGGCTACCCGATGGTGGACATCAAGGCCACCCTCATCGACGGCGCCTACCACGAGGTCGACTCCTCCGAGATGGCCTTCAAGATCGCCGGTTCCATGGCGTTCAAGGAGGGTGCCAAGAAGGCCTCGCCGGTCCTCCTCGAGCCCGTCATGGCCGTCGAGGTCCGTACTCCCGAGGAGTACATGGGCGACGTCATCGGTGACCTCAACTCCCGTCGCGGCATGATCGCCTCGATGGAGGACGCCGTCGGCGTCAAGGTCATCCGCGCCAACGTGCCCCTGTCGGAGATGTTCGGCTACGTCGGTGACCTGCGCTCCAAGACGCAGGGACGTGCCGTGTACTCCATGACCTTCGACTCGTACGCCGAGGTTCCCAAGAACGTCGCCGACGAGATCATCGCCAAGGTCAAGGGCGCCTGA","VALDVLTDLTKVRNIGIMAHIDAGKTTVTERILFYTGINYKIGETHDGASTMDWMEQEQERGITITSAATTCFWKNNQINIIDTPGHVDFTVEVERSLRVLDGAVAVFDGKEGVEPQSETVWRQADKYNVPRICYINKMDKLGADFDFSVQTIRDRLHATPIVLNFPIGAENDFSGLVDVLEMRAIRFPEKDADGKETRGSVVEYEEIPSELVAKAEELRAQLVETVAEADDALMEKYLEGEELSIAELKSGIRKLTVAGEAFPVLAGSAFKNKGIQPVLDAVLDYLPSPLDVPDVEGHAVGNEEEVLTRPADEKAPFSALAFKVATHPFYGKLVYVRVYSGKVSQGEMVLNATKGKKERIGKLFQMHSNKENPVEEAHAGHIYAFIGLKDVTTGDTLCAQGSPIVLESMTFPAPVIHVAIEPKTKGDQEKLGVAIQKLSEEDPTFTVSLDEETGQTVIGGMGELHLDVFVDRMRREFKVEANVGAPQVAYRETIRKKVDKVEYTHKKQTGGSGQFAKVQMSFEPLVADEAAETADGEKAHYEFANAVTGGRVPREYIPSVDAGVQDAMLTGVLAGYPMVDIKATLIDGAYHEVDSSEMAFKIAGSMAFKEGAKKASPVLLEPVMAVEVRTPEEYMGDVIGDLNSRRGMIASMEDAVGVKVIRANVPLSEMFGYVGDLRSKTQGRAVYSMTFDSYAEVPKNVADEIIAKVKGA$","Translation elongation factor G","Cytoplasm","translation elongation factor G","translation elongation factor G ","translation elongation factor G","","Paduch M., JeleD F., Otlewski J. Structure of small G proteins and their regulators. Acta Biochim. Pol. 2001. 48(4):829-850. PMID: 11995995","","","

InterPro
IPR000640
Domain

Translation elongation factor EFG/EF2, C-terminal
G3DSA:3.30.70.240	$\"[622-710]T$	no description
PF00679	$\"[619-706]T$	EFG_C

InterPro
IPR000795
Domain

Protein synthesis factor, GTP-binding
PR00315	$\"[14-27]T$ $\"[60-68]T$ $\"[80-90]T$ $\"[96-107]T$ $\"[132-141]T$	ELONGATNFCT
PF00009	$\"[10-291]T$	GTP_EFTU
PS00301	$\"[53-68]T$	EFACTOR_GTP

InterPro
IPR004161
Domain

Translation elongation factor EFTu/EF1A, domain 2
PF03144	$\"[332-399]T$	GTP_EFTU_D2

InterPro
IPR004540
Family

Translation elongation factor EFG/EF2
TIGR00484	$\"[3-712]T$	EF-G: translation elongation factor G

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[10-183]T$	small_GTP: small GTP-binding protein domain

InterPro
IPR005517
Domain

Translation elongation factor EFG/EF2, domain IV
PF03764	$\"[487-617]T$	EFG_IV

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[492-621]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.10	$\"[312-409]T$	no description
G3DSA:3.30.70.870	$\"[411-476]T$	no description
G3DSA:3.40.50.300	$\"[11-173]T$	no description
PTHR23115	$\"[7-159]T$ $\"[249-290]T$ $\"[311-432]T$	TRANSLATION FACTOR
PTHR23115:SF13	$\"[7-159]T$ $\"[249-290]T$ $\"[311-432]T$	TRANSLATION ELONGATION FACTOR G

","BeTs to 26 clades of COG0480COG name: Translation elongation and release factors (GTPases)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0480 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005517 (Elongation factor G, domain IV) with a combined E-value of 9.5e-101. IPB005517A 13-37 IPB005517B 52-74 IPB005517C 79-118 IPB005517D 279-290 IPB005517E 616-650***** IPB000640 (Elongation factor G, C-terminal) with a combined E-value of 3.4e-75. IPB000640A 13-33 IPB000640B 52-74 IPB000640C 79-118 IPB000640D 130-140 IPB000640E 672-686***** IPB013842 (GTP-binding protein LepA, C-terminal) with a combined E-value of 4.7e-30. IPB013842A 12-46 IPB013842B 73-113 IPB013842C 293-347 IPB013842F 611-655 IPB013842E 440-489***** IPB002127 (Tetracycline resistance protein TetO/TetQ/TetM family signature) with a combined E-value of 1.6e-19. IPB002127A 118-141 IPB002127B 262-284 IPB002127C 336-362 IPB002127E 554-576***** IPB000178 (Initiation factor 2) with a combined E-value of 5.7e-09. IPB000178C 79-114 IPB000178D 115-141***** IPB004160 (Elongation factor Tu, C-terminal) with a combined E-value of 1.7e-07. IPB004160A 12-32 IPB004160B 71-121","Residues 11-44 are 94% similar to a (GTP-BINDING FACTOR ELONGATION BIOSYNTHESIS G EF-G LEPA RESISTANCE PEPTIDE RELEASE) protein domain (PD000122) which is seen in Q6NJD6_CORDI.Residues 14-121 are 49% similar to a (INITIATION FACTOR GTPASE 2 BIOSYNTHESIS TRANSLATION GTP-BINDING) protein domain (PD971532) which is seen in Q8TV36_METKA.Residues 41-113 are 53% similar to a (GTP-BINDING) protein domain (PD792016) which is seen in Q825K7_STRAW.Residues 42-92 are 62% similar to a (ELONGATION FACTOR BIOSYNTHESIS GTP-BINDING G EF-G) protein domain (PD954552) which is seen in EFG_GLOVI.Residues 42-92 are 80% similar to a (ELONGATION FACTOR BIOSYNTHESIS GTP-BINDING G EF-G) protein domain (PD954549) which is seen in EFG_DEIRA.Residues 43-92 are 58% similar to a (ELONGATION FACTOR BIOSYNTHESIS GTP-BINDING PEPTIDE G MITOCHONDRION 1 PRECURSOR MITOCHONDRIAL) protein domain (PD954555) which is seen in EFG1_SCHPO.Residues 52-91 are 97% similar to a (FACTOR GTP-BINDING ELONGATION BIOSYNTHESIS TU G EF-TU EF-G LEPA TRANSLATION) protein domain (PD012708) which is seen in Q73SD2_MYCPA.Residues 63-157 are 50% similar to a (ELONGATION FACTOR GTP-BINDING EF-G TRANSLATION G G LIKE RESISTANCE BIOSYNTHESIS) protein domain (PD601213) which is seen in Q98I62_RHILO.Residues 93-161 are 94% similar to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS G EF-G PEPTIDE RELEASE CHAIN RF-3) protein domain (PD336744) which is seen in EFG_TROWT.Residues 164-224 are 75% similar to a (ELONGATION FACTOR GTP-BINDING G BIOSYNTHESIS EF-G TRANSLATION MITOCHONDRIAL PRECURSOR PEPTIDE) protein domain (PD798393) which is seen in Q6ACY9_BBBBB.Residues 225-292 are 60% similar to a (GTP-BINDING FACTOR BIOSYNTHESIS RESISTANCE RELEASE PEPTIDE CHAIN ANTIBIOTIC RF-3 TETRACYCLINE) protein domain (PD402543) which is seen in Q72IJ8_THET2.Residues 229-506 are 43% similar to a (ELONGATION FACTOR RESISTANCE BIOSYNTHESIS GTP-BINDING ANTIBIOTIC G TRANSLATION RELEASE) protein domain (PD324184) which is seen in Q9XD39_LEPIN.Residues 241-287 are 91% similar to a (ELONGATION FACTOR GTP-BINDING G BIOSYNTHESIS EF-G TRANSLATION MITOCHONDRIAL PRECURSOR PEPTIDE) protein domain (PD000509) which is seen in EFG_MYCLE.Residues 309-506 are 46% similar to a (RESISTANCE BIOSYNTHESIS GTP-BINDING ANTIBIOTIC ELONGATION CYCLIN TETRACYCLINE FACTOR DOMAIN RESISTANT) protein domain (PD842391) which is seen in Q8XLR6_CLOPE.Residues 320-500 are 39% similar to a (ELONGATION FACTOR G PLASMID) protein domain (PD566969) which is seen in Q92XB0_RHIME.Residues 328-390 are 92% similar to a (GTP-BINDING FACTOR ELONGATION BIOSYNTHESIS G EF-G LEPA PEPTIDE RELEASE CHAIN) protein domain (PD004660) which is seen in EFG_COREF.Residues 385-450 are 81% similar to a (ELONGATION FACTOR GTP-BINDING BIOSYNTHESIS G EF-G TRANSLATION EF-2 MITOCHONDRIAL PHOSPHORYLATION) protein domain (PD000980) which is seen in EFG_MICLU.Residues 454-497 are 95% similar to a (ELONGATION FACTOR GTP-BINDING BIOSYNTHESIS G EF-G TRANSLATION EF-2 TYPA/BIPA PHOSPHORYLATION) protein domain (PD117013) which is seen in EFG_STRAW.Residues 503-624 are 86% similar to a (ELONGATION FACTOR GTP-BINDING BIOSYNTHESIS G EF-G RESISTANCE ANTIBIOTIC TRANSLATION EF-2) protein domain (PD000296) which is seen in Q9AF78_ARTSP.Residues 625-699 are 92% similar to a (GTP-BINDING ELONGATION FACTOR BIOSYNTHESIS G EF-G LEPA TRANSLATION EF-2 TYPA) protein domain (PD011419) which is seen in Q6ACY9_BBBBB.","","-73% similar to PDB:1DAR ELONGATION FACTOR G IN COMPLEX WITH GDP (E_value = );-73% similar to PDB:1ELO ELONGATION FACTOR G WITHOUT NUCLEOTIDE (E_value = );-73% similar to PDB:1KTV Crystal Structure of Elongation Factor G Dimer Without Nucleotide (E_value = );-73% similar to PDB:1EFG THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION (E_value = );-73% similar to PDB:1JQM Fitting of L11 protein and elongation factor G (EF-G) in the cryo-em map of e. coli 70S ribosome bound with EF-G, GDP and fusidic acid (E_value = );","Residues 10 to 291 (E_value = 4.6e-109) place ANA_0021 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain.Residues 332 to 399 (E_value = 3.1e-17) place ANA_0021 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2.Residues 487 to 617 (E_value = 7.7e-64) place ANA_0021 in the EFG_IV family which is described as Elongation factor G, domain IV.Residues 619 to 706 (E_value = 1.7e-48) place ANA_0021 in the EFG_C family which is described as Elongation factor G C-terminus.","","elongation factor G (fusA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0022","32731","33921","1191","5.12","-19.89","43845","GTGGCCAAGGCCAAGTTCGAGCGGACCAAGCCGCACGTCAACATCGGAACGATCGGTCACGTCGACCACGGTAAGACGACGCTGACCGCTGCGATCTCCAAGGTTCTGCACGACGAGTACCCCGAGCTGAACCCCTTCACCCCCTTCGACGAGATCGACAAGGCTCCTGAGGAGCGTCAGCGCGGTATCACCATCAACATCGCGCACGTCGAGTACGAGACCGACAAGCGCCACTACGCGCACGTCGACGCCCCCGGGCACGCCGACTACATCAAGAACATGATTACCGGTGCCGCCCAGATGGATGGCGCGATCCTCGTGGTCGCCGCCACCGATGGCCCGATGGCCCAGACCCGCGAGCACGTCCTGCTCGCCCGCCAGGTGGGCGTCCCCGCCCTCCTCGTGGCCCTCAACAAGTCCGACATGGTGGACGACGAGGAGCTCCTCGACCTGGTTGAGATGGAGGTCCGTGAGCTGCTGTCCTCCCAGGACTACGACGGCGACGAGGCTCCCGTCATCCGCGTCTCCGCTCTCAAGGCCCTCGAGGGCGACGCCGAGTGGGCCGGCAAGATCAAGGAGCTCATGGACGCGGTGGATGACTTCATCCCCACCCCCGAGCGTGACATGGACAAGCCCTTCCTCATGCCCATCGAGGACGTCTTCACCATCACCGGTCGCGGCACCGTCGTCACCGGTCGTGTGGAGCGCGGCAAGCTCCCGATCAACTCCGAGGTCGAGATCCTCGGTATCCGCGAGGCCCAGAAGACCACGGTCACCGGTATCGAGATGTTCCACAAGCAGATGGACGAGGCCTGGGCCGGCGAGAACTGCGGTCTGCTCCTGCGCGGCACCCGTCGCGAGGACGTCGAGCGCGGTCAGGTCGTCTGCAAGCCCGGCTCCATCACCCCGCACACCGAGTTCGAGGGCCACGTCTACATCCTCACCAAGGACGAGGGCGGCCGCCACAACCCCTTCTACTCGAACTACCGTCCGCAGTTCTACTTCCGTACCACGGACGTCACCGGTGTCATCACCCTCCCCGAGGGCACCGAGATGGTCATGCCCGGCGACACCACCGAGATGACCGTCCAGCTCATCCAGCCCATCGCCATGGAGGAGGGCCTCGGCTTCGCCATCCGTGAGGGTGGCCGCACCGTCGGCTCCGGCCGCGTCACCAAGGTCATCAAGTGA","VAKAKFERTKPHVNIGTIGHVDHGKTTLTAAISKVLHDEYPELNPFTPFDEIDKAPEERQRGITINIAHVEYETDKRHYAHVDAPGHADYIKNMITGAAQMDGAILVVAATDGPMAQTREHVLLARQVGVPALLVALNKSDMVDDEELLDLVEMEVRELLSSQDYDGDEAPVIRVSALKALEGDAEWAGKIKELMDAVDDFIPTPERDMDKPFLMPIEDVFTITGRGTVVTGRVERGKLPINSEVEILGIREAQKTTVTGIEMFHKQMDEAWAGENCGLLLRGTRREDVERGQVVCKPGSITPHTEFEGHVYILTKDEGGRHNPFYSNYRPQFYFRTTDVTGVITLPEGTEMVMPGDTTEMTVQLIQPIAMEEGLGFAIREGGRTVGSGRVTKVIK$","Translation elongation factor Tu","Cytoplasm","translation elongation factor Tu","elongation factor EF-Tu ","translation elongation factor Tu","Hoflack L, Yeung MK.Actinomyces naeslundii fimbrial protein Orf977 shows similarity to a streptococcal adhesin.Oral Microbiol Immunol. 2001 Oct;16(5):319-20.PMID: 11555311","Paduch M., JeleD F., Otlewski J. Structure of small G proteins and their regulators. Acta Biochim. Pol. 2001. 48(4):829-850. PMID: 11995995","","","

InterPro
IPR000795
Domain

Protein synthesis factor, GTP-binding
PR00315	$\"[14-27]T$ $\"[60-68]T$ $\"[80-90]T$ $\"[96-107]T$ $\"[133-142]T$	ELONGATNFCT
PF00009	$\"[10-206]T$	GTP_EFTU
PS00301	$\"[53-68]T$	EFACTOR_GTP

InterPro
IPR004160
Domain

Translation elongation factor EFTu/EF1A, C-terminal
PF03143	$\"[301-395]T$	GTP_EFTU_D3

InterPro
IPR004161
Domain

Translation elongation factor EFTu/EF1A, domain 2
PF03144	$\"[227-296]T$	GTP_EFTU_D2

InterPro
IPR004541
Family

Translation elongation factor EFTu/EF1A, bacterial and organelle
PTHR23115:SF31	$\"[2-330]T$	ELONGATION FACTOR TU (EF-TU)
TIGR00485	$\"[1-396]T$	EF-Tu: translation elongation factor Tu

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[10-187]T$	small_GTP: small GTP-binding protein domain

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.10	$\"[208-337]T$ $\"[341-396]T$	no description
G3DSA:3.40.50.300	$\"[3-207]T$	no description
PTHR23115	$\"[2-330]T$	TRANSLATION FACTOR

","BeTs to 26 clades of COG0050COG name: GTPases - translation elongation factorsFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis] Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0050 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB004160 (Elongation factor Tu, C-terminal) with a combined E-value of 1.5e-116. IPB004160A 12-32 IPB004160B 71-121 IPB004160C 205-242 IPB004160D 256-294 IPB004160E 376-391***** IPB000640 (Elongation factor G, C-terminal) with a combined E-value of 5.7e-18. IPB000640A 13-33 IPB000640B 52-74 IPB000640C 79-118***** IPB005517 (Elongation factor G, domain IV) with a combined E-value of 5.1e-17. IPB005517A 13-37 IPB005517B 52-74 IPB005517C 79-118***** IPB013842 (GTP-binding protein LepA, C-terminal) with a combined E-value of 5e-10. IPB013842A 12-46 IPB013842B 73-113 IPB013842C 188-242***** IPB000178 (Initiation factor 2) with a combined E-value of 2.2e-07. IPB000178B 11-49 IPB000178C 79-114","Residues 1-57 are 98% similar to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS TU EF-TU TRANSLATION 1-ALPHA INITIATION EF-1-ALPHA) protein domain (PD053224) which is seen in EFT2_STRRA.Residues 10-118 are 47% similar to a (INITIATION FACTOR GTPASE 2 BIOSYNTHESIS TRANSLATION GTP-BINDING) protein domain (PD971532) which is seen in Q8TV36_METKA.Residues 12-95 are 46% similar to a (ELONGATION GTP-BINDING FACTOR BIOSYNTHESIS SELENOCYSTEINE-SPECIFIC SEC NUCLEAR HOMOLOGUE RE67487P TRANSLATION) protein domain (PD480916) which is seen in Q7Q5R3_EEEEE.Residues 46-75 are identical to a (ELONGATION FACTOR GTP-BINDING TU BIOSYNTHESIS EF-TU TRANSLATION CHLOROPLAST HYDROLASE TU) protein domain (PD187884) which is seen in EFTU_STRCJ.Residues 57-95 are 69% similar to a (ELONGATION FACTOR CHLOROPLAST TU BIOSYNTHESIS GTP-BINDING TRANSLATIONAL) protein domain (PDA0K2D1) which is seen in Q8M9W7_CHAGL.Residues 58-95 are identical to a (FACTOR GTP-BINDING ELONGATION BIOSYNTHESIS TU G EF-TU EF-G LEPA TRANSLATION) protein domain (PD012708) which is seen in EFTU_MICLU.Residues 96-139 are identical to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS TU EF-TU TRANSLATION INITIATION SUBUNIT 1-ALPHA) protein domain (PD173400) which is seen in EFTU_MICLU.Residues 161-223 are 85% similar to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS TU EF-TU 1-ALPHA TRANSLATION SUBUNIT EF-1-ALPHA) protein domain (PD007358) which is seen in EFTU_BRELN.Residues 239-293 are 94% similar to a (ELONGATION FACTOR GTP-BINDING TU BIOSYNTHESIS EF-TU TRANSLATION CHLOROPLAST TU HYDROLASE) protein domain (PD000168) which is seen in Q6ACZ0_BBBBB.Residues 294-322 are 93% similar to a (ELONGATION FACTOR GTP-BINDING TU BIOSYNTHESIS EF-TU TRANSLATION CHLOROPLAST TU PEPTIDE) protein domain (PDA0E3F2) which is seen in Q7VJ74_HELHP.Residues 299-393 are 55% similar to a (ELONGATION FACTOR BIOSYNTHESIS GTP-BINDING TU HOMOLOGUE PEPTIDE C43E11.4 ELEGANS CG12736-PA) protein domain (PD337982) which is seen in Q9V4M7_DROME.Residues 310-396 are similar to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS TU EF-TU 1-ALPHA EF-1-ALPHA TRANSLATION ALPHA) protein domain (PD000486) which is seen in EFTU_MICLU.","","-74% similar to PDB:1OB2 E. COLI ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC KIRROMYCIN, A GTP ANALOG, AND PHE-TRNA (E_value = 1.2E_143);-74% similar to PDB:1DG1 WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU). (E_value = 2.1E_143);-74% similar to PDB:1D8T CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (EF-TU-MGGDP) COMPLEXED WITH GE2270A, A THIAZOLYL PEPTIDE ANTIBIOTIC (E_value = 2.8E_143);-74% similar to PDB:1EFC INTACT ELONGATION FACTOR FROM E.COLI (E_value = 2.8E_143);-74% similar to PDB:1LS2 Fitting of EF-Tu and tRNA in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome (E_value = 2.8E_143);","Residues 10 to 206 (E_value = 4.3e-97) place ANA_0022 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain.Residues 227 to 296 (E_value = 8.4e-26) place ANA_0022 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2.Residues 301 to 395 (E_value = 1.1e-54) place ANA_0022 in the GTP_EFTU_D3 family which is described as Elongation factor Tu C-terminal domain.","","elongation factor Tu (tuf)","","1","","","","","","","","","","","","Thu Jul 26 14:57:58 2007","","","","Thu Jul 26 14:57:58 2007","Thu Jul 26 14:57:58 2007","Thu Jul 26 14:57:58 2007","","Thu Jul 26 14:57:58 2007","Thu Jul 26 14:57:58 2007","","","","","yes","","" "ANA_0023","34248","37118","2871","7.55","3.04","100791","GTGTTCCCTTTGTTGTCTCGTCGTGCCATCAAACCTCGCCTGCGTAAGCTCGTCGCCGGCGCTGCGGCACTCGCCTGCGTTGCTGCGGCGCTCGTGGGCACTGAGCAGCCTTCTGCCGGGGCGGCCCCGAGCGGGCTCCCCGCCGACGCGCTTCCGGCGGTCTTCGCTCAGGGCGGCACCAGCTGGTACCGGGACACCATCCAGTGGCTCCAGTGGGCGGACTACGACCAGAACTTCGCCGGCCAGACCAAGCCGAATGTTCCCGTGCTCGACTACGGGCAGCGCAGGACCTTCACCAACTACCGCGACCTGGGGGAGGCCGGATATCTGGTCACCACCTGCAATCTGTCCAATCTCAAGCACCTTGGTCACCAGAAGGGCTTTCCCGACGATCTTTCCCGCGGCCCGCTGGTCGCCACGATTCCGGGCACCTGGGCCGGTGACATCCTCGACAACCTCTACAACACCGGTGGCGCCGGGGGCTGGAGCGATGGCAGCTCGGAGTGGCACAACGGCCTGAAGTACCCGGACAACTACACCAACCACAACCGGATGGTTATCGGACTGGCCAACGGCTACGCCTACAACGGGGACAAGACCTGGGACGGCAGGGACAAGAACGACCGCCGGGCCAACCGCACGCCCACGGGCGGATACTCACGCATTAGCTTTGACGTCTCCTGCTCGGCAGCTGTCCAGGCCCCCGACGGCAGCTCCACACCGGTGGCCCTCAACGGCCTGGTCTTCGCCGACGCGGAGGCCTCCAACCCCGGCAGCACCAATGAGCCCTTCGACGGCGAGTGGATCCAGGCTGAGGTCCCCAGCAACCAGCGAGTCACCTGGCGCCTCCTGGACGGTGGGCGCTCCAGTAACTGCCCCAACACGCGTGGAAACCGGTGGGAGCCGGTCACGACCCGCGCGACCTTCTCCAACGCGAACCACACCCTGCGGCTGGATAACACGGCGCAGGAGTGCGTCTACCAGAACGGCGGAGGCTACTCCAAGCCCAACGGCATCGGTGGGCCCGCGGTCTCCATGTTCATGGAAGGGGCCACCAGCGCCACCATCACCATGCAGGGGTCGGGTTACTCCGCCGTCGCCCTGGGACTGGTCCTGGTCACCGACTTCGGTGACGCGCCGGTCTCCTACGGCAGCGCCTCCGCCCTCCTGCAGCCCAGGTGGGATGGTGGTGAGGTCACGAACCGCAACGGCTATGACCTGTTCGGTGGCCGCCTCATCAATACCACCCGCATGCAGCCCACCGGACCCTACCTGGGCTCGGGTACTGACGCCGAGTCCCAGCAGCGCTTCAGCGACGGGGCCGACGGCGACGACAACGACGGCTGGTACGGCAACGACGAGGACGGTGTCTCCATCCCCGACGCAGGCATCGCAACGGCCCCGGGACAGCAGTACACCACCAACGTCCGCTGTGGCGGCCGGGGAGCGGTGGCCGGTTGGATCGACTGGAACCACAACGGCGTCTTTGACGCCACCGAGAAGAGCGGTCAGACCACCTGTGACGGCTGGGGCAATGCCACACTGCGTTGGACCGTCCCCGAGGACGTCGTGCGCAGCATTGACGGGGAGGCTGGATCCCAGCCCCACACCTACCTACGGGTGAGGACAGCTGAGGCAGGAGTGAATCTCAAACCCACCGGCAGCACGATGGGTGGCGAGGTCGAGGACTACCGGATCGCGGTACGCGTCCCCACGATCCGGCTCGTGAAGAACGTCCAGGCCCCCTACACCGGGCAGGTCAGGGCCCTCGGGGCCGACCAGTGGACCCTCAAGGCCCAGCAGGGCAACGGTGGCGCGGCGTCCCAGCAGGTGACCGGCAACGTTGACACCGGGATCAAGGCGGTGCGTCCAGGACAGTACGCGCTCAGCGAGTCCTCCACGAACCCCCAGGCACCGGGCTACGAGGCGAGCGCATGGCAGTGCGCCCAGACCCCTGGGACGCGCGGCAGCTGGAGCGGATCGAGACTGACAGGATCCAAGATCCAAGTGCAGGGTGCCGATCGCATCACCTGCTCGGTGACCAACACGACCAAGCCCGGAGCGCTGTCCTGGACCAAGGTCGACCAGGACGGTCAGACACCCCTGGGCGGTACCAGCTGGACCCTGACCGGTCCCGGCGTCCCCGCCGGCACCGTCGTCGAGGACTGCCAGGCGGCGGGCTGCCGCGGCGGCGCCTACCGGGACACTAACCCGGCTCCGGGTGTCTTCGAGGTCAGTGGACTGGCGTGGGGGAGCTACTCCGTCACCGAGAAAACCGCCCCCAGTGGATACCAGCGCCTGGACAAGACCCTGGCCTTCAACGACGTCTCCGGCGCCAACCTCAAGGCTGGGCTCAAGGACACCACCGGTGTCACCAGGGGAGCCGTGACCAACCAACGTCTGACCGGAGCCGTGTCCTGGAAGAAGCAGGACACGAGCGGACATGCCCTGGGCGGCTCGGAGTGGACGCTCAGCGGCCCCGGAGTCCCGGCCAGGACCACCGTCACCGACTGCGTCATCGCCGGTGGCAGGGGACGGTGCCCGGGCGGCCCCTACGCCGATACGGACCCCGCGGCCGGTTCCTTCACCGTGACCGGCCTGCCCTGGGACACGCGCTCCTACTCCCTGGTGGAGAAGCGGGCTCCCGCGGGATACCGGCTTGACACGACGAGCCGCAGCTTCGCCATCAAGCCCAACGCCCTCCAGTACTCCTTCTCGAAGGCCTTCACCAACGAGAAGGCGGCCACCCCCCGCTTGCCCCTGACAGGCGGACGCGGTGCGCACATCTTCCTGATCGCAGGAGCGGTCGTCTCCGCTCTGGCGATCTCCACCGGACTCCTCAGGAGGCGCCGTCACTGCAACCTCGACTGA","VFPLLSRRAIKPRLRKLVAGAAALACVAAALVGTEQPSAGAAPSGLPADALPAVFAQGGTSWYRDTIQWLQWADYDQNFAGQTKPNVPVLDYGQRRTFTNYRDLGEAGYLVTTCNLSNLKHLGHQKGFPDDLSRGPLVATIPGTWAGDILDNLYNTGGAGGWSDGSSEWHNGLKYPDNYTNHNRMVIGLANGYAYNGDKTWDGRDKNDRRANRTPTGGYSRISFDVSCSAAVQAPDGSSTPVALNGLVFADAEASNPGSTNEPFDGEWIQAEVPSNQRVTWRLLDGGRSSNCPNTRGNRWEPVTTRATFSNANHTLRLDNTAQECVYQNGGGYSKPNGIGGPAVSMFMEGATSATITMQGSGYSAVALGLVLVTDFGDAPVSYGSASALLQPRWDGGEVTNRNGYDLFGGRLINTTRMQPTGPYLGSGTDAESQQRFSDGADGDDNDGWYGNDEDGVSIPDAGIATAPGQQYTTNVRCGGRGAVAGWIDWNHNGVFDATEKSGQTTCDGWGNATLRWTVPEDVVRSIDGEAGSQPHTYLRVRTAEAGVNLKPTGSTMGGEVEDYRIAVRVPTIRLVKNVQAPYTGQVRALGADQWTLKAQQGNGGAASQQVTGNVDTGIKAVRPGQYALSESSTNPQAPGYEASAWQCAQTPGTRGSWSGSRLTGSKIQVQGADRITCSVTNTTKPGALSWTKVDQDGQTPLGGTSWTLTGPGVPAGTVVEDCQAAGCRGGAYRDTNPAPGVFEVSGLAWGSYSVTEKTAPSGYQRLDKTLAFNDVSGANLKAGLKDTTGVTRGAVTNQRLTGAVSWKKQDTSGHALGGSEWTLSGPGVPARTTVTDCVIAGGRGRCPGGPYADTDPAAGSFTVTGLPWDTRSYSLVEKRAPAGYRLDTTSRSFAIKPNALQYSFSKAFTNEKAATPRLPLTGGRGAHIFLIAGAVVSALAISTGLLRRRRHCNLD$","LPXTG-motif cell wall anchor domain","Extracellular, Cellwall","Gram positive anchor domain protein","probable surface-anchored fimbrial subunit","LPXTG-motif cell wall anchor domain","Hoflack L, Yeung MK.Actinomyces naeslundii fimbrial protein Orf977 shows similarity to a streptococcal adhesin.Oral Microbiol Immunol. 2001 Oct;16(5):319-20.PMID: 11555311","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
PF00746	$\"[911-950]T$	Gram_pos_anchor
TIGR01167	$\"[918-952]T$	LPXTG_anchor: LPXTG-motif cell wall anchor
PS50847	$\"[919-956]T$	GRAM_POS_ANCHORING

InterPro
IPR008454
Domain

Cna B-type
PF05738	$\"[741-786]T$ $\"[860-906]T$	Cna_B

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[927-947]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues are similar to a () protein domain () which is seen in .Residues 341-563 are 37% similar to a (WALL PEPTIDOGLYCAN-ANCHOR CELL RELATED ADHESIN CSHA SDR-FAMILY) protein domain (PD913121) which is seen in Q54194_STRGN.Residues 613-891 are 41% similar to a () protein domain (PD856489) which is seen in Q8FMP5_COREF.Residues 774-854 are 53% similar to a () protein domain (PDA0W0T2) which is seen in Q9EV17_ACTNA.Residues 855-955 are similar to a (CELL WALL PEPTIDOGLYCAN-ANCHOR COLLAGEN ADHESION ANCHOR SURFACE DOMAIN SIALOPROTEIN-BINDING BONE) protein domain (PD407337) which is seen in Q9EV17_ACTNA.Residues 774-854 are 53% similar to a () protein domain (PDA0W0T2) which is seen in Q9EV17_ACTNA.Residues 855-955 are similar to a (CELL WALL PEPTIDOGLYCAN-ANCHOR COLLAGEN ADHESION ANCHOR SURFACE DOMAIN SIALOPROTEIN-BINDING BONE) protein domain (PD407337) which is seen in Q9EV17_ACTNA.","","No significant hits to the PDB database (E-value < E-10).","Residues 741 to 786 (E_value = 0.0044) place ANA_0023 in the Cna_B family which is described as Cna protein B-type domain.Residues 860 to 906 (E_value = 0.001) place ANA_0023 in the Cna_B family which is described as Cna protein B-type domain.Residues 911 to 950 (E_value = 0.00051) place ANA_0023 in the Gram_pos_anchor family which is described as Gram positive anchor.","","positive anchor domain protein","","1","","","","","","","","","","","","Thu Jul 26 14:58:36 2007","","","","Thu Jul 26 14:58:36 2007","","Thu Jul 26 14:58:36 2007","","Thu Jul 26 14:58:36 2007","Thu Jul 26 14:58:36 2007","","","","","yes","","" "ANA_0024","37158","38876","1719","6.33","-3.96","60058","GTGACGCCGTCGGACAAGACGGAGCCGTCCACCGGAGAAGAACTCCCTATCCATACCTCTGCCACGCGTTCGCATCTCCCCGCGGCGCACAGTGAAAGGAAATCCCAACCCATGAAGCACAACGCCAGCACGCTGGGGCGTCGGGCTGCTGCCGCAGCCGGTGTCCTCACCCTGGCCTTCCTCGGCCTGGCCCCTTCGGCCGTGGCCACGGAAACGCCTAACTACGGCAACATCAAGACGGATGCGACGGGCTCCCTGGTCATCCACAAGCACCTCACCGGCGGCGGTAAGGACATCGGTACCCCCACCGGTACCGCGCAGAACGCCGATGACAAGGGCCCGGCCGTTGAGGGCGTCGTCTTCACCGCCTACCCGATCACCGACATCAATCTGAAGGACCCTGCCGGGTGGGACACGATCAGCAACCTGTCCAGGACCGGTGTGCCGGACAGCGCCTGCGCCAACCCCGCCGCCCCCACGCTCGGAGCGCACCAGTTCGGCACTCCCAAGGTCTCCCCGGCCACCACCAAGGAGGGCCTCGCCACGATCACGGAGATGCCGGTTCAGGCCTACCTCGTGTGCGAGACCACGACCCCTGGTGACATCGTCCAGAAGGCCAAGCCCTTCGTGGTGACGATTCCTCACCCGAATACCGCTGCGGGTGCTGACGGCCAGTGGATCTACGACGTCAACGTCTACCCCAAGAACGAGGCCATTGACGTCGACAAGACCATCCAGGCGCAGAAGCTCAACGGCTACGGTGTCGGCTCCCTCATCAAGTTCCCGGTGGAGTCTACGGCGCCGACGCTCGACGCCAAGTCCTTCTACAAGTACTTCCAGCTCAAGGACACCCTGGACGAGCGCCTGTCGGAGGTGACCGCCACTGACGTCTCCCTCGAGGGTACGCCCCTGCAGCCCACCGACTACAAGGTGGAGACCAAGCAGCAGACCGTGACCGTCACCTTCACCGCCGAGGGTCTGAAGAAGATCAAGGCCGCCCCCGGCAAGAAGGTGTCCGCCGTCTTCCAGGGCAAGGTGACCAAGGCCGGCAACGGCGCCATCACGAACCGGGCTCAGGTCATCAGTGACACCCTCTACGCCGAGCAGCCCCCGACTCCTGAGACGCCCCCGACGGACCCTGAGAACCCGCCGACGTCCGACGAGGTGATCTCTCGCTGGGGCGACCTGAGCATCAAGAAGGTGGACACCCACCAGCAGGGCCAGACCAAGGCCGGCCTCCAGGGCGCGCAGTTCCAGCTGTACAAGGCCAAGAACGCCTACGCCAACACCTGCTCCAACGAGAAGGAGGGCGCCCCCATCGCCATCAACGGCCAGACCACGCTGACCACGGACGCCCAGGGCGCTATCGACATCAAGGGCCTGTTCATCTCCGACTCCATCGATGGTGCAGACCGTGACAACCAGGTGAATGCCATGGAGCGCTGCTACGTCCTGGTTGAGACCAAGGCACCCGCCGGCTACGTCCTGCCCGCCGGTAACGGCGCCGCGACCCCCGTCAAGGTCAAGGCCGGTGAGGAGACCACGGACAACGTCACCGTTGAGAACACCAAGCAGTCGGTTCCGGGCCTGCCCCTGACCGGTGCCAACGGCATGCTCATCCTGACCGCCTCCGGCGCGTCCCTGCTGATGATCGCCGTCGGCTCCGTCCTCGTGGCCCGCTACCGCGAGCGCAAGCAGAACGCGAACCTCGCGCTCTGA","VTPSDKTEPSTGEELPIHTSATRSHLPAAHSERKSQPMKHNASTLGRRAAAAAGVLTLAFLGLAPSAVATETPNYGNIKTDATGSLVIHKHLTGGGKDIGTPTGTAQNADDKGPAVEGVVFTAYPITDINLKDPAGWDTISNLSRTGVPDSACANPAAPTLGAHQFGTPKVSPATTKEGLATITEMPVQAYLVCETTTPGDIVQKAKPFVVTIPHPNTAAGADGQWIYDVNVYPKNEAIDVDKTIQAQKLNGYGVGSLIKFPVESTAPTLDAKSFYKYFQLKDTLDERLSEVTATDVSLEGTPLQPTDYKVETKQQTVTVTFTAEGLKKIKAAPGKKVSAVFQGKVTKAGNGAITNRAQVISDTLYAEQPPTPETPPTDPENPPTSDEVISRWGDLSIKKVDTHQQGQTKAGLQGAQFQLYKAKNAYANTCSNEKEGAPIAINGQTTLTTDAQGAIDIKGLFISDSIDGADRDNQVNAMERCYVLVETKAPAGYVLPAGNGAATPVKVKAGEETTDNVTVENTKQSVPGLPLTGANGMLILTASGASLLMIAVGSVLVARYRERKQNANLAL$","Type-2 fimbrial major subunit precursor","Extracellular, Periplasm, Cellwall","fimbrial structural subunit","hypothetical protein","LPXTG-motif cell wall anchor domain","Drobni M, Hallberg K, Ohman U, Birve A, Persson K, Johansson I, Strmberg N.Sequence analyses of fimbriae subunit FimA proteins on Actinomyces naeslundii genospecies 1 and 2 and Actinomyces odontolyticus with variant carbohydrate binding specificities.BMC Microbiol. 2006;6:43.PMID: 16686953Yeung MK, Cisar JO.Cloning and nucleotide sequence of a gene for Actinomyces naeslundii WVU45 type 2 fimbriae.J Bacteriol. 1988 Sep;170(9):3803-9.PMID: 2900829Hoflack L, Yeung MK.Actinomyces naeslundii fimbrial protein Orf977 shows similarity to a streptococcal adhesin.Oral Microbiol Immunol. 2001 Oct;16(5):319-20.PMID: 11555311Yeung MK, Donkersloot JA, Cisar JO, Ragsdale PA.Identification of a gene involved in assembly of Actinomyces naeslundii T14V type 2 fimbriae.Infect Immun. 1998 Apr;66(4):1482-91.PMID: 9529071","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
PF00746	$\"[522-562]T$	Gram_pos_anchor
TIGR01167	$\"[529-564]T$	LPXTG_anchor: LPXTG-motif cell wall anchor
PS50847	$\"[530-569]T$	GRAM_POS_ANCHORING

InterPro
IPR008454
Domain

Cna B-type
PF05738	$\"[413-461]T$ $\"[483-519]T$	Cna_B

noIPR
unintegrated

unintegrated
tmhmm	$\"[49-69]?$ $\"[539-559]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 77-235 are similar to a (FIMBRIAL SUBUNIT WALL PEPTIDOGLYCAN-ANCHOR CELL PRECURSOR SIGNAL TYPE MAJOR TYPE-1) protein domain (PD776919) which is seen in O68212_ACTNA.Residues 80-236 are 45% similar to a (WALL CELL SURFACE ANCHOR FAMILY ORF2 PEPTIDOGLYCAN-ANCHOR) protein domain (PD859080) which is seen in Q48707_LACLE.Residues 236-369 are 94% similar to a (CELL WALL FIMBRIAL SUBUNIT PEPTIDOGLYCAN-ANCHOR PRECURSOR SIGNAL SURFACE MAJOR TYPE-1) protein domain (PD014454) which is seen in O68212_ACTNA.Residues 394-564 are similar to a (CELL WALL PEPTIDOGLYCAN-ANCHOR COLLAGEN ADHESION ANCHOR SURFACE DOMAIN SIALOPROTEIN-BINDING BONE) protein domain (PD407337) which is seen in O68212_ACTNA.","","No significant hits to the PDB database (E-value < E-10).","Residues 413 to 519 (E_value = 0.0015) place ANA_0024 in the Cna_B family which is described as Cna protein B-type domain.Residues 522 to 562 (E_value = 1.7e-06) place ANA_0024 in the Gram_pos_anchor family which is described as Gram positive anchor.","","structural subunit","","1","","","","","","","","","","","","Thu Jul 26 15:08:13 2007","","","","Thu Jul 26 15:00:04 2007","","Thu Jul 26 15:00:04 2007","","Thu Jul 26 15:00:04 2007","Thu Jul 26 15:00:04 2007","","","","","yes","","" "ANA_0025","39113","40351","1239","7.03","0.13","44737","ATGATCTCTCGCAAAGCACGCATACCCCGCACCGCCCGGACTCCGCGCACTCGCGCCTCGAGCCTCCAGAAGCACCGCCGCCCCCGCGCCTGGCGCCTGTCGGTCTCCGCCCTGGTCACCTCCATCATGGCGCTGGTGGGCATGGGGCTGCTGACCTATCCGACGGCGGCCTCCTGGGTCTCCCAGTACAACCAGTCGAAGGTGACTGCCGACTACTCCGCCCAGGTCGATGGGGCTCGTCCCGATGCCAAGACCCAGGTCGAGCAGGCGCACGCCTACAATGACGCGCTCTCGGCCGGGGCGGTCCTGGAGGCCAACAACCACGTCCCCACCGGTGCCGGCTCGAGCAAGGACAGCTCCCTGCAGTACGCCAACATCCTCAAGGCCAATAACGAGGGCCTCATGGCCCGTCTCAAGATCCCCTCCATCTCCCTGGACCTGCCCGTCTACCACGGCACGGCCGACGACACCCTGCTCAAGGGCCTGGGGCACCTGGAGGGCACCTCGTTGCCGGTCGGGGGAGAGGGGACCCGCTCGGTCATCACGGGGCACCGCGGCCTGGCCGAGGCCACTATGTTCACCAACTTGGACAAGGTCAAGACCGGTGACAGCCTCATCGTCGAGGTCTTCGGAGAGGTCCTCACCTACCGGGTCACCAGCACCAAGGTCGTCGAGCCCGAGGAGACCGAGGCCTTGCGCGTCGAGGAGGGCAAGGACCTGCTCACCCTGGTGACCTGCACGCCCCTGGGCATCAACACCCACCGTATCCTGCTGACCGGCGAGCGCATCTACCCGACCCCGGCCAAGGACCTCGCGGCGGCGGGCAAGCGCCCCGACGTTCCCCACTTCCCCTGGTGGGCTGTGGGTCTGGCGGCGGGACTCATCGTCGTCGGGCTGTACCTGTGGCGCTCGGGCTACGCGGCGGCGAGGGCCAAGGAGCGGGCCCTGGCCAGGGCCCGGGCCGCGCAGGAGGAACCGCAGCCACAGACCTGGGCCGAGCAGATGCGTATCTGGATGGACGACGACGCCGGTGTTGAGCCCCAACGGTGGTTCACCGACCTGCCGGTCCCGCCTCAGCCCTCCGAGATGGAGAACCTGGCGCTTCTGGAGGAGATCGCCTCGCTGTCCGCGCCGTCCGGCCGCTGGGATGATCAGGAGCTCATCGACACCGCTGAGATCCCGGTACTGGACGCGACACGCCCGAGCGCGGGGACCAGTGGGCGGACTCACAGGCTCTAG","MISRKARIPRTARTPRTRASSLQKHRRPRAWRLSVSALVTSIMALVGMGLLTYPTAASWVSQYNQSKVTADYSAQVDGARPDAKTQVEQAHAYNDALSAGAVLEANNHVPTGAGSSKDSSLQYANILKANNEGLMARLKIPSISLDLPVYHGTADDTLLKGLGHLEGTSLPVGGEGTRSVITGHRGLAEATMFTNLDKVKTGDSLIVEVFGEVLTYRVTSTKVVEPEETEALRVEEGKDLLTLVTCTPLGINTHRILLTGERIYPTPAKDLAAAGKRPDVPHFPWWAVGLAAGLIVVGLYLWRSGYAAARAKERALARARAAQEEPQPQTWAEQMRIWMDDDAGVEPQRWFTDLPVPPQPSEMENLALLEEIASLSAPSGRWDDQELIDTAEIPVLDATRPSAGTSGRTHRL$","Fimbrial associated sortase-like protein","Periplasm, Cytoplasm","sortase-like protein","K07284 sortase A","sortase family protein","Yeung MK, Donkersloot JA, Cisar JO, Ragsdale PA.Identification of a gene involved in assembly of Actinomyces naeslundii T14V type 2 fimbriae.Infect Immun. 1998 Apr;66(4):1482-91.PMID: 9529071","Barrett A.J., Rawlings N.D. Evolutionary lines of cysteine peptidases. Biol. Chem. 2001. 382(5):727-733. PMID: 11517925Mazmanian S.K., Liu G., Ton-That H., Schneewind O. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 1999. 285(5428):760-763. PMID: 10427003Mazmanian S.K., Ton-that H., Schneewind O. Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus. Mol. Microbiol. 2001. 40(5):1049-1057. PMID: 11401711Pallen M.J., Chaudhuri R.R., Henderson I.R. Genomic analysis of secretion systems. Curr Opin Microbiol 2003. 6(5):519-527. PMID: 14572546","","","

InterPro
IPR005754
Family

Peptidase C60, sortase A and B
PF04203	$\"[138-263]T$	Sortase
TIGR01076	$\"[136-271]T$	sortase_fam: sortase family protein

noIPR
unintegrated

unintegrated
G3DSA:2.40.260.10	$\"[124-268]T$	no description
signalp	$\"[1-44]?$	signal-peptide
tmhmm	$\"[33-53]?$ $\"[282-302]?$	transmembrane_regions

","BeTs to 3 clades of COG3764COG name: Sortase (surface protein transpeptidase)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG3764 is --m--------lb-------------Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 53-130 are similar to a (FIMBRIA-ASSOCIATED SORTASE-LIKE FIMBRIAL ASSOCIATED) protein domain (PD769697) which is seen in O68213_ACTNA.Residues 135-173 are similar to a (SORTASE-LIKE SORTASE FAMILY FIMBRIA-ASSOCIATED FIMBRIAL ASSOCIATED SORTASE SIMILAR ACTINOMYCES NAESLUNDII) protein domain (PD107165) which is seen in O68213_ACTNA.Residues 174-261 are similar to a (SORTASE FAMILY SORTASE-LIKE FIMBRIA-ASSOCIATED TRANSPEPTIDASE LPXTG-SITE MEMBRANE ASSOCIATED FIMBRIAL SORTASE) protein domain (PD068544) which is seen in O68213_ACTNA.Residues 262-412 are similar to a (FIMBRIA-ASSOCIATED) protein domain (PD107167) which is seen in O68213_ACTNA.","","No significant hits to the PDB database (E-value < E-10).","Residues 138 to 263 (E_value = 1.2e-68) place ANA_0025 in the Sortase family which is described as Sortase family.","","protein ","","1","","","","","","","","","","","","Fri Jul 27 11:42:56 2007","Fri Jul 27 11:42:56 2007","","","Thu Jul 26 15:09:03 2007","","Thu Jul 26 15:09:03 2007","","Thu Jul 26 15:09:03 2007","Thu Jul 26 15:09:03 2007","","","","","yes","","" "ANA_0026","40610","40918","309","9.38","4.86","11570","ATGGCGGGACAGAAGATCCGCATCCGGCTCAAGTCCTACGACCACGAGGTCATTGACTCCTCGGCGCGCAAGATCGTCGACGTCGTGACCCGCGCTGGCGCGACGGTCGTGGGCCCGGTGCCGCTGCCGACCGAGAAGAACGTGTTCTGCGTGATCCGGTCGCCGCACAAGTACAAGGACAGCCGCGAGCACTTCGAGATGCGCACGCACAAGCGGCTGATCGACATCGTCGACCCGACGCCCAAGGCCGTCGACTCGCTCATGCGTCTCGACCTGCCCGCTGACGTCAACATCGAGATCAAGCTCTGA","MAGQKIRIRLKSYDHEVIDSSARKIVDVVTRAGATVVGPVPLPTEKNVFCVIRSPHKYKDSREHFEMRTHKRLIDIVDPTPKAVDSLMRLDLPADVNIEIKL$","Ribosomal protein S10","Cytoplasm","ribosomal protein S10","K02946 small subunit ribosomal protein S10","ribosomal protein S10","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Mueller F., Brimacombe R. A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data. J. Mol. Biol. 1997. 271(4):545-565. PMID: 9281425Hermann-Le Denmat S., Sipiczki M., Thuriaux P. Suppression of yeast RNA polymerase III mutations by the URP2 gene encoding a protein homologous to the mammalian ribosomal protein S20. J. Mol. Biol. 1994. 240(1):1-7. PMID: 8021936Agafonov D.E., Kolb V.A., Spirin A.S. Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(24):12892-12897. PMID: 9371771Otaka E., Suzuki K., Hashimoto T. Examination of protein sequence homologies. VII. The complementary molecular coevolution of ribosomal proteins equivalent to Escherichia coli L7/L12 and L10. Protein Seq. Data Anal. 1990. 3(1):11-19. PMID: 2179947","","","

InterPro
IPR001848
Family

Ribosomal protein S10
PD001272	$\"[13-101]T$	RS10_BIFLO_Q8G418;
PR00971	$\"[5-18]T$ $\"[40-55]T$ $\"[61-75]T$	RIBOSOMALS10
G3DSA:3.30.70.600	$\"[3-101]T$	no description
PTHR11700	$\"[1-102]T$	30S RIBOSOMAL PROTEIN S10 FAMILY MEMBER
PF00338	$\"[5-100]T$	Ribosomal_S10
PS00361	$\"[29-44]T$	RIBOSOMAL_S10

InterPro
IPR005731
Family

Ribosomal protein S10, bacterial form
PTHR11700:SF2	$\"[1-102]T$	30S RIBOSOMAL PROTEIN S10
TIGR01049	$\"[4-102]T$	rpsJ_bact: ribosomal protein S10

","BeTs to 26 clades of COG0051COG name: Ribosomal protein S10Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0051 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001848 (Ribosomal protein S10) with a combined E-value of 2.3e-30. IPB001848 14-68","Residues 6-100 are 53% similar to a (RIBOSOMAL S10) protein domain (PD766144) which is seen in Q8KTP3_CANTP.Residues 13-101 are similar to a (RIBOSOMAL 30S S10 S10P S20 40S CHLOROPLAST SEQUENCING DIRECT 3D-STRUCTURE) protein domain (PD001272) which is seen in RS10_BIFLO.","","-76% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 6.7E_30);-76% similar to PDB:1GIX Crystal structure of the ribosome at 5.5 A resolution. This file, 1GIX, contains the 30S ribosome subunit, three tRNA, and mRNA molecules. 50S ribosome subunit is in the file 1GIY (E_value = 6.7E_30);-76% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 6.7E_30);-76% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 6.7E_30);-76% similar to PDB:1HNZ STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH HYGROMYCIN B (E_value = 6.7E_30);","Residues 5 to 100 (E_value = 1.3e-61) place ANA_0026 in the Ribosomal_S10 family which is described as Ribosomal protein S10p/S20e.","","protein S10 (rpsJ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0027","40927","41595","669","10.51","15.59","23242","ATGACAACGCTTAACACGCCGGCTGCCGCCGCGCCTGCCAAGGCGCTGCTCGGCACCAAGCTCGGCATGACGCAGATCTGGGACGAGAACGGGGTCCTGCGCCCCGTGACCGTCGTCCGGGTCGACACCAACGTCGTGACCCAGGTCCGCACCATCGAGACCGATGGCTACGAGGCCGTTCAGCTCGCCTTCGGCGACATCGACGCCCGCAAGGTCACCAAGCCGCTCGCCGGCCACTTCGCCAAGGCCGGGGTCGAGCCCCGCCGCCACGTGGCGGAGATTCGCACCTCCCTGGCGTCGGAGTTCACCCCCGGCCAGGAGCTGGCCGCTGACACCTTCGAGGTCGGCCAGCTGGTCGACGTTACCGGAACCTCCAAGGGTAAGGGGTTCGCCGGTGTCATGAAGCGCCACGGCTTCGCCGGTGTGGGCGCCTCCCACGGTGCTCACCGCAACCACCGCAAGCCGGGCTCCATCGGCGCCTGCGCCACCCCCGGGCGCATCTTCAAGGGCCTGCGCATGGCCGGTCGTATGGGCCACGCGCGCCGCACCGTCCAGAACCTCAAGATCCGCGGCATCGACGTTGACAAGGGCGTTCTGCTCGTCAACGGCGCGATCCCCGGCCCCAAGGGCTCGGTCGTCGTCGTCCGCACCGCCGTGAAGGGAGCCTGA","MTTLNTPAAAAPAKALLGTKLGMTQIWDENGVLRPVTVVRVDTNVVTQVRTIETDGYEAVQLAFGDIDARKVTKPLAGHFAKAGVEPRRHVAEIRTSLASEFTPGQELAADTFEVGQLVDVTGTSKGKGFAGVMKRHGFAGVGASHGAHRNHRKPGSIGACATPGRIFKGLRMAGRMGHARRTVQNLKIRGIDVDKGVLLVNGAIPGPKGSVVVVRTAVKGA$","Ribosomal protein L3","Cytoplasm","ribosomal protein L3","50S ribosomal protein L3","ribosomal protein L3","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Graack H.R., Grohmann L., Kitakawa M., Schafer K.L., Kruft V. YmL9, a nucleus-encoded mitochondrial ribosomal protein of yeast, is homologous to L3 ribosomal proteins from all natural kingdoms and photosynthetic organelles. Eur. J. Biochem. 1992. 206(2):373-380. PMID: 1597181Herwig S., Kruft V., Wittmann-Liebold B. Primary structures of ribosomal proteins L3 and L4 from Bacillus stearothermophilus. Eur. J. Biochem. 1992. 207(3):877-885. PMID: 1499563Arndt E., Kromer W., Hatakeyama T. Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui. J. Biol. Chem. 1990. 265(6):3034-3039. PMID: 2406244","","","

InterPro
IPR000597
Family

Ribosomal protein L3
PD001374	$\"[125-178]T$	Q6ACZ5_BBBBB_Q6ACZ5;
PF00297	$\"[20-216]T$	Ribosomal_L3
PS00474	$\"[113-136]T$	RIBOSOMAL_L3

noIPR
unintegrated

unintegrated
PTHR11229	$\"[13-220]T$	50S RIBOSOMAL PROTEIN L3

","BeTs to 26 clades of COG0087COG name: Ribosomal protein L3Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0087 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000597 (Ribosomal protein L3) with a combined E-value of 1.3e-43. IPB000597A 15-26 IPB000597B 113-138 IPB000597C 164-193","Residues 23-79 are 80% similar to a (RIBOSOMAL L3 RRNA-BINDING RNA-BINDING 50S RIBONUCLEOPROTEIN CHLOROPLAST MITOCHONDRIAL 60S SEQUENCING) protein domain (PD105246) which is seen in RL3_BIFLO.Residues 105-220 are 57% similar to a (RIBOSOMAL RIBONUCLEOPROTEIN L3 RRNA-BINDING RNA-BINDING 60S L3P 50S SEQUENCING DIRECT) protein domain (PD859232) which is seen in RL3_NANEQ.Residues 125-178 are similar to a (RIBOSOMAL L3 RRNA-BINDING RNA-BINDING 50S RIBONUCLEOPROTEIN CHLOROPLAST MITOCHONDRIAL L3 SEQUENCING) protein domain (PD001374) which is seen in Q6ACZ5_BBBBB.","","-63% similar to PDB:1P85 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 1.7E_44);-63% similar to PDB:1P86 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 1.7E_44);-63% similar to PDB:1VS6 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 50s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.7E_44);-63% similar to PDB:1VS8 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.7E_44);-63% similar to PDB:2AW4 Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 50S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 1.7E_44);","Residues 20 to 216 (E_value = 7.6e-88) place ANA_0027 in the Ribosomal_L3 family which is described as Ribosomal protein L3.","","protein L3 (rplC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0028","41600","42244","645","9.98","10.15","23092","ATGACTGAGGCACTCACCGTCGACGTCGTCGACTCCGCGGGCAAGAAGACCGGCAGCGTCGAGCTGCCCGCCGAGGTCTTCGACGCCCCCCTCAACATTCCGCTCATGCACCAGGTGGTCGTCGGCCAGCTGGCCGCGGCCCGCCAGGGCACTCACGCCACCAAGACCCGCGGCGACGTCCGCGGCGGTGGTCGCAAGCCCTACCGCCAGAAGGGCACCGGCCGCGCCCGCCAGGGCTCGACCCGCGCCCCGCAGTTCGTCGGCGGTGGCACCGTCCACGGCCCGCAGCCGCGCGACTACACCCAGCGGACCCCCAAGAAGATGAAGGCCGCCGCCCTGCGCAGCGCCCTGTCCGACCGCGCCCGCAACGGCCGCGTCCACGTCATCACCGAGTTCGTCACCACCACGGTGCCCTCCACCAAGAACGCCCTGGTCGCGCTGCGCAACCTCACCGACCGCAAGGCCCTGGTGATCGTGGACCGTCAGGACGACCTGTCCAGGCTCAGCCTGCGCAACGCCCCCGAGGCGCACGTCCTGTGGGCCGACCAGCTCAACACCTACGACGTCCTGAAGTCCGACGACGTCGTCTTCACGGCCTCTGGCCTGGACGCGTTCCTGGGCAAGGGTGAGGAGGAGTCCAAGTGA","MTEALTVDVVDSAGKKTGSVELPAEVFDAPLNIPLMHQVVVGQLAAARQGTHATKTRGDVRGGGRKPYRQKGTGRARQGSTRAPQFVGGGTVHGPQPRDYTQRTPKKMKAAALRSALSDRARNGRVHVITEFVTTTVPSTKNALVALRNLTDRKALVIVDRQDDLSRLSLRNAPEAHVLWADQLNTYDVLKSDDVVFTASGLDAFLGKGEEESK$","Ribosomal protein L4","Periplasm, Cytoplasm","ribosomal protein L4/L1 family","50S ribosomal protein L4","ribosomal protein L4/L1e","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Yeh L.C., Lee J.C. Yeast ribosomal proteins L4, L17, L20, and L25 exhibit different binding characteristics for the yeast 35S precursor rRNA. Biochim. Biophys. Acta 1998. 1443(1):139-148. PMID: 9838082","","","

InterPro
IPR002136
Family

Ribosomal protein L4/L1e
PF00573	$\"[19-205]T$	Ribosomal_L4

InterPro
IPR013005
Family

Ribosomal protein L4/L1e, bacterial like
PTHR10746	$\"[21-203]T$	50S RIBOSOMAL PROTEIN L4

InterPro
IPR015498
Family

Ribosomal protein L4
PTHR10746:SF2	$\"[21-203]T$	50S RIBOSOMAL PROTEIN L4

noIPR
unintegrated

unintegrated
G3DSA:3.40.1370.10	$\"[5-207]T$	no description

","BeTs to 21 clades of COG0088COG name: Ribosomal protein L4Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0088 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 5-202 are 61% similar to a (RIBOSOMAL RRNA-BINDING L4 50S RNA-BINDING) protein domain (PD612579) which is seen in RL4_CHLTE.Residues 6-129 are 69% similar to a (RIBOSOMAL RRNA-BINDING L4 50S RNA-BINDING) protein domain (PDA1A9H3) which is seen in RL4_BDEBA.Residues 7-132 are 56% similar to a (RIBOSOMAL RRNA-BINDING 3D-STRUCTURE SEQUENCING L4 50S RNA-BINDING DIRECT) protein domain (PD735701) which is seen in RL4_DEIRA.Residues 14-198 are 68% similar to a (RIBOSOMAL L4 50S RNA-BINDING RRNA-BINDING 60S L4P TRANSCRIPTION REGULATION CHLOROPLAST) protein domain (PD001346) which is seen in RL4_THETN.Residues 22-148 are 52% similar to a (SPBC2D10.08C) protein domain (PD457818) which is seen in O74801_SCHPO.Residues 33-203 are 58% similar to a (RIBOSOMAL L4 50S CHLOROPLAST) protein domain (PDA189D7) which is seen in Q6B8V4_EEEEE.Residues 34-154 are 63% similar to a (RIBOSOMAL RRNA-BINDING L4 50S RNA-BINDING) protein domain (PDA1A502) which is seen in RL4_MYCGE.Residues 34-131 are 70% similar to a (RIBOSOMAL RESISTANCE RRNA-BINDING L4 50S RNA-BINDING ANTIBIOTIC) protein domain (PDA1A501) which is seen in RL4_MYCPN.Residues 35-203 are 55% similar to a (RIBOSOMAL CHLOROPLAST RRNA-BINDING L4 50S RNA-BINDING) protein domain (PD107424) which is seen in RK4_GUITH.Residues 156-205 are 78% similar to a (RIBOSOMAL L4 50S RRNA-BINDING RNA-BINDING TRANSCRIPTION REGULATION TERMINATION CHLOROPLAST REPRESSOR) protein domain (PD468876) which is seen in Q6A6M7_PROAC.","","-57% similar to PDB:1DMG CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4 (E_value = 1.3E_28);-52% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 4.9E_25);-52% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 4.9E_25);-52% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 4.9E_25);-52% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 4.9E_25);","Residues 19 to 205 (E_value = 7.2e-64) place ANA_0028 in the Ribosomal_L4 family which is described as Ribosomal protein L4/L1 family.","","protein L4-L1 family (rplD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0029","42241","42543","303","9.85","7.13","10964","GTGAGCCTCGAGAAGTCCAAGAACCCCCGCGACGTCATCATCGCGCCGGTGGTCTCCGAGAAGTCCTACGCCTGCATGGACCGTGGCCAGTACACGTTCATTGTGGCGCCGGGATCCAACAAGACCGAGATCAAGCAGGCCGTTGAGGCCATCTTCGATGTCAAGGTCTCCTCGGTGAACACCATCAACCGCAAGGGCAAGACGCACCGCACCCGTACCGGGATCGGCAAGTCCAAGGACACCCGCCGTGCGATCGTCACCCTGCGCGAGGGGACCATCGACATCTTCGGTGATGTGGCCTAG","VSLEKSKNPRDVIIAPVVSEKSYACMDRGQYTFIVAPGSNKTEIKQAVEAIFDVKVSSVNTINRKGKTHRTRTGIGKSKDTRRAIVTLREGTIDIFGDVA$","Ribosomal protein L23","Cytoplasm","ribosomal protein L23","50S ribosomal protein L23","Ribosomal protein L25/L23","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR012677
Domain

Nucleotide-binding, alpha-beta plait
G3DSA:3.30.70.330	$\"[6-100]T$	no description

InterPro
IPR013025
Domain

Ribosomal protein L25/L23
PD001141	$\"[15-91]T$	Q6ACZ7_BBBBB_Q6ACZ7;
PF00276	$\"[10-99]T$	Ribosomal_L23

noIPR
unintegrated

unintegrated
PTHR11620	$\"[33-64]T$	60S RIBOSOMAL PROTEIN L23A

","BeTs to 25 clades of COG0089COG name: Ribosomal protein L23Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0089 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001014 (Ribosomal L23 protein) with a combined E-value of 2.4e-24. IPB001014 29-70***** IPB005633 (Ribosomal protein L23, N-terminal domain) with a combined E-value of 4.5e-10. IPB005633B 33-62","Residues 15-91 are similar to a (RIBOSOMAL L23 RRNA-BINDING RIBONUCLEOPROTEIN 50S CHLOROPLAST L23P LSU SEQUENCING DIRECT) protein domain (PD001141) which is seen in Q6ACZ7_BBBBB.","","-65% similar to PDB:1N88 NMR structure of the ribosomal protein L23 from Thermus thermophilus. (E_value = 1.9E_16);-65% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 1.9E_16);-65% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 1.9E_16);-65% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 1.9E_16);-65% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 1.9E_16);","Residues 10 to 99 (E_value = 1.5e-30) place ANA_0029 in the Ribosomal_L23 family which is described as Ribosomal protein L23.","","protein L23 (rplW)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0030","42570","43406","837","11.32","36.31","30461","ATGGGAATCCGTAAGTACAAGCCCACGACCCCGGGTCGTCGCGGCTCCTCCGTGGCCGACTTCGTGGAGATCACGCGCAGCACGCCCGAGAAGTCGCTGGTACGCCCGCTGAGCAAGTCCGGTGGACGCAACTCCTCCGGCCGTATCACCACCCGCCACAAGGGTGGTGGCCACAAGCGCGCCTACCGTCTCATCGACTTCCGTCGTCACGACAAGGACGGCGTGCCCGCCAAGGTCGCTCACATCGAGTACGACCCCAACCGCACCGCGCGCATCGCCCTGCTGCACTACATGGACGGCGAGAAGCGCTACATCATCGCCCCGAACAAGCTCCGTCAGGGCGACGTCGTCGAGGCCGGCCCCAGCGCCGACATCAAGCCCGGCAACAACCTGCAGCTGCGTCACATCCCCACCGGTACGGTCGTCCACGCGGTCGAGCTGCGTCCCGGTGGCGGGGCCAAGATCGCTCGCAGCGCCGGCACCTCCGTCCAGCTGGTCGCCAAGGAGGGCAAGTACGCGCAGCTGCGCATGCCCTCCGGGGAGATCCGCAACGTGGAGGCCGCCTGCCGCGCCACCATCGGCGAGGTCGGCAACGCCGAGCAGTCCAACATCAACTGGGGCAAGGCCGGCCGTATGCGCTGGAAGGGCGTGCGCCCGACCGTCCGCGGTGTCGTCATGAACCCGGTGGACCACCCGCACGGTGGTGGTGAGGGCAAGACCTCCGGTGGTCGTCACCCCGTCTCGCCGTGGGGCAAGCCCGAGGGCCGCACCCGCCGTCCCAACAAGTCCAGCGACCGCCTCATCGTGCGTCGTCGTCGGACCGGCAAGAAGCGCTGA","MGIRKYKPTTPGRRGSSVADFVEITRSTPEKSLVRPLSKSGGRNSSGRITTRHKGGGHKRAYRLIDFRRHDKDGVPAKVAHIEYDPNRTARIALLHYMDGEKRYIIAPNKLRQGDVVEAGPSADIKPGNNLQLRHIPTGTVVHAVELRPGGGAKIARSAGTSVQLVAKEGKYAQLRMPSGEIRNVEAACRATIGEVGNAEQSNINWGKAGRMRWKGVRPTVRGVVMNPVDHPHGGGEGKTSGGRHPVSPWGKPEGRTRRPNKSSDRLIVRRRRTGKKR$","Ribosomal protein L2","Cytoplasm, Extracellular","ribosomal protein L2","ribosomal protein L2","ribosomal protein L2","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Willumeit R., Forthmann S., Beckmann J., Diedrich G., Ratering R., Stuhrmann H.B., Nierhaus K.H. Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome. J. Mol. Biol. 2001. 305(1):167-177. PMID: 11114255","","","

InterPro
IPR002171
Family

Ribosomal protein L2
PTHR13691	$\"[94-278]T$	RIBOSOMAL PROTEIN L2
PF00181	$\"[42-119]T$	Ribosomal_L2
PF03947	$\"[125-253]T$	Ribosomal_L2_C
PS00467	$\"[219-230]T$	RIBOSOMAL_L2

InterPro
IPR005880
Family

Ribosomal protein L2, bacterial and organelle form
PTHR13691:SF5	$\"[94-278]T$	50S RIBOSOMAL PROTEIN L2
TIGR01171	$\"[3-274]T$	rplB_bact: ribosomal protein L2

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[38-115]T$	no description

InterPro
IPR014722
Domain

Translation protein SH3-like, subgroup
G3DSA:2.30.30.30	$\"[119-198]T$	no description

","BeTs to 26 clades of COG0090COG name: Ribosomal protein L2Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0090 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002171 (Ribosomal protein L2) with a combined E-value of 6.5e-129. IPB002171A 42-69 IPB002171B 75-115 IPB002171C 128-169 IPB002171D 175-213 IPB002171E 214-239 IPB002171F 246-260 IPB002171A 41-68","Residues 1-30 are identical to a (RIBOSOMAL L2 50S RRNA-BINDING RNA-BINDING CHLOROPLAST SEQUENCING DIRECT 3D-STRUCTURE CYANELLE) protein domain (PDA0P1Z1) which is seen in RL2_STRCO.Residues 39-77 are 87% similar to a (RIBOSOMAL L2 50S CHLOROPLAST RRNA-BINDING RNA-BINDING MITOCHONDRION) protein domain (PD296079) which is seen in RL2_RALSO.Residues 47-123 are similar to a (RIBOSOMAL L2 50S RRNA-BINDING RNA-BINDING CHLOROPLAST 60S L2P L8 MITOCHONDRION) protein domain (PD445342) which is seen in RL2_COREF.Residues 128-198 are 92% similar to a (RIBOSOMAL L2 50S RRNA-BINDING RNA-BINDING CHLOROPLAST 60S L2P L8 MITOCHONDRION) protein domain (PD000953) which is seen in RL2_BIFLO.Residues 208-277 are similar to a (RIBOSOMAL L2 50S RNA-BINDING RRNA-BINDING CHLOROPLAST 60S MITOCHONDRION L8 L2P) protein domain (PD606103) which is seen in Q73SB1_MYCPA.Residues 237-278 are 90% similar to a (RIBOSOMAL L2 50S RNA-BINDING RRNA-BINDING) protein domain (PDA0R3H7) which is seen in Q6A6M9_PROAC.","","-76% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 1.7E_98);-76% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 1.7E_98);-76% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 1.7E_98);-76% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 1.7E_98);-76% similar to PDB:2J01 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 2 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE I. (E_value = 1.7E_98);","Residues 42 to 119 (E_value = 3.1e-46) place ANA_0030 in the Ribosomal_L2 family which is described as Ribosomal Proteins L2, RNA binding domain.Residues 125 to 253 (E_value = 1.6e-85) place ANA_0030 in the Ribosomal_L2_C family which is described as Ribosomal Proteins L2, C-terminal domain.","","protein L2 (rplB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0031","43421","43699","279","10.57","11.36","10545","ATGCCGCGTAGTCTGAAGAAGGGTCCCTTCGTCGACGACCACCTCCTCAAGAAGGTGGACGCTCAGAACGAGAAGGGCACCAAGAACGTCATTAAGACCTGGTCCCGCCGTTCGGTCATCACGCCGGACTTCCTGGGGCACACCTTCGCCGTCCACGACGGTCGTAAGCACGTGCCGGTCTTCGTTACCGAGTCCATGGTGGGCCACAAGCTCGGTGAGTTCGCTCCGACCCGCACCTTCCGCGGGCACGTCAAGGACGACCGCAAGTCGCGTCGCTGA","MPRSLKKGPFVDDHLLKKVDAQNEKGTKNVIKTWSRRSVITPDFLGHTFAVHDGRKHVPVFVTESMVGHKLGEFAPTRTFRGHVKDDRKSRR$","Ribosomal protein S19","Periplasm, Cytoplasm","ribosomal protein S19","30S ribosomal protein S19","ribosomal protein S19","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Agafonov D.E., Kolb V.A., Spirin A.S. Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(24):12892-12897. PMID: 9371771Kitagawa M., Takasawa S., Kikuchi N., Itoh T., Teraoka H., Yamamoto H., Okamoto H. rig encodes ribosomal protein S15. The primary structure of mammalian ribosomal protein S15. FEBS Lett. 1991. 283(2):210-214. PMID: 2044758","","","

InterPro
IPR002222
Family

Ribosomal protein S19/S15
PD001012	$\"[10-85]T$	Q8G413_BIFLO_Q8G413;
PR00975	$\"[33-52]T$ $\"[53-65]T$ $\"[65-80]T$	RIBOSOMALS19
G3DSA:3.30.860.10	$\"[1-92]T$	no description
PTHR11880	$\"[1-92]T$	RIBOSOMAL PROTEIN S19P FAMILY MEMBER
PF00203	$\"[3-83]T$	Ribosomal_S19
PS00323	$\"[53-77]T$	RIBOSOMAL_S19

InterPro
IPR005732
Family

Ribosomal protein S19, bacterial and organelle form
TIGR01050	$\"[1-92]T$	rpsS_bact: ribosomal protein S19

","BeTs to 26 clades of COG0185COG name: Ribosomal protein S19Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0185 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002222 (Ribosomal protein S19/S15) with a combined E-value of 1.4e-38. IPB002222 33-83","Residues 3-92 are 59% similar to a (RIBOSOMAL S19 MITOCHONDRION RIBONUCLEOPROTEIN) protein domain (PD932995) which is seen in Q8HDL0_MAGSO.Residues 10-85 are similar to a (RIBOSOMAL S19 30S RIBONUCLEOPROTEIN CHLOROPLAST RRNA-BINDING MITOCHONDRION S15 40S SEQUENCING) protein domain (PD001012) which is seen in Q8G413_BIFLO.","","-85% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 2.9E_33);-85% similar to PDB:1FKA STRUCTURE OF FUNCTIONALLY ACTIVATED SMALL RIBOSOMAL SUBUNIT AT 3.3 A RESOLUTION (E_value = 2.9E_33);-85% similar to PDB:1GIX Crystal structure of the ribosome at 5.5 A resolution. This file, 1GIX, contains the 30S ribosome subunit, three tRNA, and mRNA molecules. 50S ribosome subunit is in the file 1GIY (E_value = 2.9E_33);-85% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 2.9E_33);-85% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 2.9E_33);","Residues 3 to 83 (E_value = 5.1e-49) place ANA_0031 in the Ribosomal_S19 family which is described as Ribosomal protein S19.","","protein S19 (rpsS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0032","43731","44108","378","10.52","11.15","13890","ATGGAAGCCAAGGCGCAGGCCAAGTACGTGCGCTGCACGCCGATGAAGGCGCGCCGGGTCGTGGACGTCGTCCGCGGCAAGCGCGCCGTCGAGGCCGTCAACGTGCTCCGATTCGCCCCGCAGGCCGCTGCGGTGCCGGTGCGCAAGGTCCTCGAGTCCGCAATCGCCAACGCCCGGTTCAAGGCTGAGCGTGACGGTGAGCGTTTCGACGAGAACGACCTGTTCATCATCGAGGCGTTCGCCGACGAGGGTCCCACCCTGAAGCGGTTCCGTCCCCGTGCGCAGGGCCGGGCCAGCAGGATCCTCAAGCGGACCAGCCACATCACCGTCATCGTCGGGGACAAGTCCGACGCCGCAACGAAGGAAGGAGCCCGGTAA","MEAKAQAKYVRCTPMKARRVVDVVRGKRAVEAVNVLRFAPQAAAVPVRKVLESAIANARFKAERDGERFDENDLFIIEAFADEGPTLKRFRPRAQGRASRILKRTSHITVIVGDKSDAATKEGAR$","Ribosomal protein L22","Cytoplasm","ribosomal protein L22","50S ribosomal protein L22","ribosomal protein L22","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001063
Family

Ribosomal protein L22/L17
PD001032	$\"[31-115]T$	RL22_BIFLO_Q8G412;
G3DSA:3.90.470.10	$\"[1-118]T$	no description
PF00237	$\"[5-114]T$	Ribosomal_L22
PS00464	$\"[88-112]T$	RIBOSOMAL_L22

InterPro
IPR005727
Family

Ribosomal protein L22, bacterial and organelle form
PTHR13501	$\"[8-112]T$	CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED
TIGR01044	$\"[5-112]T$	rplV_bact: ribosomal protein L22

","BeTs to 25 clades of COG0091COG name: Ribosomal protein L22Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0091 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001063 (Ribosomal protein L22/L17) with a combined E-value of 8.1e-52. IPB001063A 5-34 IPB001063B 36-58 IPB001063C 68-112","Residues 31-115 are similar to a (RIBOSOMAL L22 50S RRNA-BINDING RNA-BINDING CHLOROPLAST L22P 60S L17 SEQUENCING) protein domain (PD001032) which is seen in RL22_BIFLO.","","-68% similar to PDB:1J5A STRUCTURAL BASIS FOR THE INTERACTION OF ANTIBIOTICS WITH THE PEPTIDYL TRANSFERASE CENTER IN EUBACTERIA (E_value = 6.4E_25);-68% similar to PDB:1JZX Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria (E_value = 6.4E_25);-68% similar to PDB:1JZY Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria (E_value = 6.4E_25);-68% similar to PDB:1JZZ Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria (E_value = 6.4E_25);-68% similar to PDB:1K01 Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria (E_value = 6.4E_25);","Residues 5 to 114 (E_value = 8.4e-42) place ANA_0032 in the Ribosomal_L22 family which is described as Ribosomal protein L22p/L17e.","","protein L22 (rplV)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0033","44108","44929","822","10.48","16.67","30593","ATGGGGCAGAAGGTCAACCCGACCGGGTTCCGCCTGGGCATCACCACGGACCACCGTTCGCGCTGGTTCGCCGACTCCACCAAGCCCGGTCAGCGTTACCGCGACTTCGTGGAGGAGGATGTCAAGATCCGCCGCCTCATGGAGGACGGCATGGAGCGGGCCGGTATCTCCAAGGTCGACATCGAGCGCACCCGTGACCGCGTGCGTGTCGACCTGCACACCGCCCGTCCCGGTATCGTCATCGGTCGCCGTGGGGCCGAGGCCGAGCGCCTGCGTGGTCAGCTCGAGAAGCTGACCGGCAAGCAGGTCCAGCTCAACATCCTCGAGGTCAAGAGCCCCGACCTGGACGCCCAGCTGGTCGCCCAGGGCATCGCTGAGCAGCTCGCCTCCCGCGTGTCCTTCCGTCGCGCCATGCGCAAGGGCATGCAGTCCGCGATGCGTGCCGGCGCCAAGGGCATCCGGGTGCAGTGCTCCGGTCGCCTGGGCGGCGCCGAGATGAGCCGCAGCGAGTTCTACCGCGAGGGGCGCGTGCCGCTGCACACCCTGCGCGCGAACATCGACTACGGCTTCTACGAGGCCAAGACCACCTTCGGCCGCCTCGGCGTCAAGGTGTGGATCTACAAGGGCGACATCACCGAGCGCGAGTTCGCCCGCCAGCAGGCCGAGTCCGGCTCCCGTGGCCGGGGCCGGGGCGAGCGCCGCGGCGGCCGTCGTGGCGACCGCGGTGAGCGCGGTTCGCGTCAGAACACCGAGCAGCAGCAGGCAGCCGAGCAGACGCCGGCCGCCGAGACCGCTGCCGCAGACCAGGGAACGGAGGCCTGA","MGQKVNPTGFRLGITTDHRSRWFADSTKPGQRYRDFVEEDVKIRRLMEDGMERAGISKVDIERTRDRVRVDLHTARPGIVIGRRGAEAERLRGQLEKLTGKQVQLNILEVKSPDLDAQLVAQGIAEQLASRVSFRRAMRKGMQSAMRAGAKGIRVQCSGRLGGAEMSRSEFYREGRVPLHTLRANIDYGFYEAKTTFGRLGVKVWIYKGDITEREFARQQAESGSRGRGRGERRGGRRGDRGERGSRQNTEQQQAAEQTPAAETAAADQGTEA$","Ribosomal protein S3","Cytoplasm, Extracellular","30S ribosomal protein","30S ribosomal protein S3","ribosomal protein S3","","Wimberly B.T., Brodersen D.E., Clemons W.M., Morgan-warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V. Structure of the 30S ribosomal subunit. Nature 2000. 407(6802):327-339. PMID: 11014182Chen X., Court D.L., Ji X. Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(15):8396-8401. PMID: 10411886Worbs M., Bourenkov G.P., Bartunik H.D., Huber R., Wahl M.C. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol. Cell 2001. 7(6):1177-1189. PMID: 11430821","","","

InterPro
IPR001351
Domain

Ribosomal protein S3, C-terminal
G3DSA:3.30.1140.32	$\"[112-211]T$	no description
PF00189	$\"[123-206]T$	Ribosomal_S3_C
PS00548	$\"[167-201]T$	RIBOSOMAL_S3

InterPro
IPR004044
Domain

KH, type 2
PF07650	$\"[67-121]T$	KH_2
PS50823	$\"[43-111]T$	KH_TYPE_2

InterPro
IPR004087
Domain

KH
SM00322	$\"[64-129]T$	KH

InterPro
IPR005704
Family

Bacterial ribosomal protein S3
TIGR01009	$\"[1-215]T$	rpsC_bact: ribosomal protein S3

InterPro
IPR008282
Domain

Ribosomal protein S3, N-terminal
PF00417	$\"[1-66]T$	Ribosomal_S3_N

InterPro
IPR009019
Domain

KH, prokaryotic type
G3DSA:3.30.300.20	$\"[17-111]T$	no description

noIPR
unintegrated

unintegrated
PTHR11760	$\"[94-271]T$	30S/40S RIBOSOMAL PROTEIN S3
PTHR11760:SF10	$\"[94-271]T$	CHLOROPLAST 30S RIBOSOMAL PROTEIN S3

","BeTs to 26 clades of COG0092COG name: Ribosomal protein S3Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0092 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001351 (Ribosomal protein S3) with a combined E-value of 5.4e-72. IPB001351A 1-23 IPB001351B 119-154 IPB001351C 158-207 IPB001351B 123-158","Residues 44-135 are similar to a (RIBOSOMAL RRNA-BINDING RNA-BINDING S3 30S RIBONUCLEOPROTEIN CHLOROPLAST S3P SEQUENCING DIRECT) protein domain (PD001959) which is seen in RS3_STRCO.Residues 119-209 are 72% similar to a (RIBOSOMAL S3 MITOCHONDRION RIBONUCLEOPROTEIN CHLOROPLAST MITOCHONDRIAL 30S RRNA-BINDING ORF SEQUENCING) protein domain (PD000851) which is seen in RR3_CHLEU.Residues 120-206 are 56% similar to a (RIBOSOMAL MITOCHONDRION S3 MITOCHONDRIAL RIBONUCLEOPROTEIN RNA EDITING) protein domain (PD720729) which is seen in RT03_MAIZE.","","-69% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 2.7E_56);-69% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 2.7E_56);-69% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 1.0E_55);-69% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 1.0E_55);-69% similar to PDB:2AVY Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 30S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 1.0E_55);","Residues 1 to 66 (E_value = 1.6e-24) place ANA_0033 in the Ribosomal_S3_N family which is described as Ribosomal protein S3, N-terminal domain.Residues 67 to 121 (E_value = 7.4e-23) place ANA_0033 in the KH_2 family which is described as KH domain.Residues 123 to 206 (E_value = 5.7e-46) place ANA_0033 in the Ribosomal_S3_C family which is described as Ribosomal protein S3, C-terminal domain.","","ribosomal protein (BS3)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0034","44933","45352","420","11.27","16.89","15747","GTGCTCATCCCCCGCCGGACCAAGTTCCGCAAGCAGCACCGCCCGCACCGCACGGGCCTTTCCAAGGGCGGCAACCAGATCGCCTTCGGTGAGTACGGCATCCAGGCTCTCGAGCCCGCCTACATCACCAACCGCCAGATCGAGGCGGCCCGTATCGCCATGACCCGCCACATCAAGCGTGGCGGCAAGGTGTGGATCAACATCTTCCCGGACCGCCCCCTGACCAAGAAGCCCGCCGAGACTCGTATGGGTTCCGGTAAGGGTGCACCTGAGTGGTGGATCGCCAACGTCAAGCCCGGACGCATCCTGTTCGAGCTCGGCGGTGTCGACGAGGCCCTCGCCCGCGAGGCCATGCGCCGCGCACAGCACAAGCTTCCGATGAAGACCCGTTTCGTGACTCGTGAGGGTGGTGACGTCTGA","VLIPRRTKFRKQHRPHRTGLSKGGNQIAFGEYGIQALEPAYITNRQIEAARIAMTRHIKRGGKVWINIFPDRPLTKKPAETRMGSGKGAPEWWIANVKPGRILFELGGVDEALAREAMRRAQHKLPMKTRFVTREGGDV$","Ribosomal protein L16","Cytoplasm","ribosomal protein L16","50S ribosomal protein L16","ribosomal protein L16","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000114
Family

Ribosomal protein L16
PR00060	$\"[24-36]T$ $\"[42-53]T$ $\"[58-87]T$ $\"[88-117]T$	RIBOSOMALL16
PF00252	$\"[1-132]T$	Ribosomal_L16
TIGR01164	$\"[2-127]T$	rplP_bact: ribosomal protein L16
PS00586	$\"[59-70]T$	RIBOSOMAL_L16_1
PS00701	$\"[82-93]T$	RIBOSOMAL_L16_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.1170.10	$\"[31-139]T$	no description
PTHR12220	$\"[1-135]T$	50S/60S RIBOSOMAL PROTEIN L16

","BeTs to 25 clades of COG0197COG name: Ribosomal protein L16/L10EFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0197 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000114 (Ribosomal protein L16) with a combined E-value of 3.1e-79. IPB000114A 6-58 IPB000114B 59-109","Residues 3-137 are 46% similar to a (RIBOSOMAL L16 MITOCHONDRION) protein domain (PD535476) which is seen in O21032_DICDI.Residues 3-128 are 47% similar to a (RIBOSOMAL L16 MITOCHONDRION 50S) protein domain (PD587820) which is seen in Q9ZZN8_CYAME.Residues 4-43 are similar to a (RIBOSOMAL L16 50S CHLOROPLAST RRNA-BINDING MITOCHONDRION L16/L10E 60S MITOCHONDRIAL SUBUNIT) protein domain (PD527590) which is seen in Q6NJC8_CORDI.Residues 48-121 are similar to a (RIBOSOMAL L10 60S L10E 50S QM HOMOLOG TUMOR SUPPRESSOR L10) protein domain (PDA16174) which is seen in Q7MTM0_PORGI.Residues 68-106 are similar to a (RIBOSOMAL L16 50S CHLOROPLAST MITOCHONDRION RRNA-BINDING MITOCHONDRIAL L16/L10E 60S SUBUNIT) protein domain (PD001146) which is seen in RL16_MYCTU.","","-81% similar to PDB:1NJM The crystal structure of the 50S Large ribosomal subunit from Deinococcus radiodurans complexed with a tRNA acceptor stem mimic (ASM) and the antibiotic sparsomycin (E_value = 4.5E_47);-81% similar to PDB:1NJP The crystal structure of the 50S Large ribosomal subunit from Deinococcus radiodurans complexed with a tRNA acceptor stem mimic (ASM) (E_value = 4.5E_47);-81% similar to PDB:1NKW Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans (E_value = 4.5E_47);-81% similar to PDB:1NWX COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH ABT-773 (E_value = 4.5E_47);-81% similar to PDB:1NWY COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN (E_value = 4.5E_47);","Residues 1 to 132 (E_value = 1.6e-83) place ANA_0034 in the Ribosomal_L16 family which is described as Ribosomal protein L16.","","protein L16 (rplP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0035","45352","45597","246","7.27","0.18","8985","ATGGCAATCGGTTCCAAGGGCCTGACCCCCGCCGACCTCGACGGCATGGACAACGAGCGCCTCTCCGAGGAGCTCTCCAAGGCCAAGGCCGAGCTGTTCAACCTCCGGTTCGCCTCGGCGACCGGCCAGCTCGAGGACCACGGACGTCTCAAGGCTGTGCGTCGCGACATCGCCCGCATCTACACGATCGTGCGCGAGCGTGAGCTCGGCATTCGCACCGCCCCGAGCACGGAGGAGTCCAAGTGA","MAIGSKGLTPADLDGMDNERLSEELSKAKAELFNLRFASATGQLEDHGRLKAVRRDIARIYTIVRERELGIRTAPSTEESK$","Ribosomal protein L29","Cytoplasm","50S ribosomal protein L29","50S ribosomal protein L29","ribosomal protein L29","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001854
Family

Ribosomal protein L29
PF00831	$\"[10-67]T$	Ribosomal_L29
TIGR00012	$\"[12-67]T$	L29: ribosomal protein L29

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.310	$\"[8-74]T$	no description

","BeTs to 24 clades of COG0255COG name: Ribosomal protein L29Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0255 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001854 (Ribosomal protein L29) with a combined E-value of 3e-15. IPB001854 35-67","Residues 29-71 are similar to a (RIBOSOMAL L29 50S L35 60S CHLOROPLAST L29P SEQUENCING DIRECT SUBUNIT) protein domain (PD187745) which is seen in RL29_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 10 to 67 (E_value = 4e-22) place ANA_0035 in the Ribosomal_L29 family which is described as Ribosomal L29 protein.","","ribosomal protein L29","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0036","45594","45887","294","9.65","5.65","11221","GTGAGCGAGCAGACCAGCACTGAGAACGTCGAGCAGTCCACCGAGCGCCCCCAGCGCAAGGTGCGTCGCGGCTACGTCGTCTCCGACAAGATGGACAAGACGGTCGTCGTCCTCGTCGAGGAGCGCTACAAGCACTCCCTGTACGGCAAGGTCCTCCGTCGCTCCAAGAAGGTCAAGGTCCACGACGAGAACAACGAGGCCGGTGTCGGCGATCTCGTCTCCATCATGGAGACCCGCCCGCTGAGCGCCACCAAGCACTTCCGCCTCCTGGAGATCCTCGAGCGCGCCAAGTGA","VSEQTSTENVEQSTERPQRKVRRGYVVSDKMDKTVVVLVEERYKHSLYGKVLRRSKKVKVHDENNEAGVGDLVSIMETRPLSATKHFRLLEILERAK$","Ribosomal protein S17","Cytoplasm","30S ribosomal protein S17","ribosomal protein S17","ribosomal protein S17","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Mueller F., Brimacombe R. A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data. J. Mol. Biol. 1997. 271(4):545-565. PMID: 9281425Agafonov D.E., Kolb V.A., Spirin A.S. Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(24):12892-12897. PMID: 9371771","","","

InterPro
IPR000266
Family

Ribosomal protein S17
PD001295	$\"[19-90]T$	Q6AD04_BBBBB_Q6AD04;
PR00973	$\"[38-61]T$ $\"[70-80]T$ $\"[80-87]T$	RIBOSOMALS17
PTHR10744	$\"[16-96]T$	40S RIBOSOMAL PROTEIN S11 FAMILY MEMBER
PF00366	$\"[24-92]T$	Ribosomal_S17
PS00056	$\"[70-82]T$	RIBOSOMAL_S17

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[17-94]T$	no description

","BeTs to 26 clades of COG0186COG name: Ribosomal protein S17Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0186 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000266 (Ribosomal protein S17) with a combined E-value of 7.3e-38. IPB000266A 24-63 IPB000266B 70-92","Residues 19-90 are similar to a (RIBOSOMAL S17 RIBONUCLEOPROTEIN 30S RRNA-BINDING 40S S11 S17P CHLOROPLAST SEQUENCING) protein domain (PD001295) which is seen in Q6AD04_BBBBB.","","-81% similar to PDB:1EG0 FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME (E_value = 3.4E_26);-81% similar to PDB:1QD7 PARTIAL MODEL FOR 30S RIBOSOMAL SUBUNIT (E_value = 3.8E_25);-81% similar to PDB:1RIP RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR (E_value = 3.8E_25);-77% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 3.1E_19);-77% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 3.1E_19);","Residues 24 to 92 (E_value = 1.6e-35) place ANA_0036 in the Ribosomal_S17 family which is described as Ribosomal protein S17.","","ribosomal protein S17 (BS16)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0037","47572","48456","885","11.20","29.16","31599","ATGTCAGCGCGATGGACACCGACGGTCCGCCCGGCGGCCTCCATCGGCCCACGGCCGAGGTTCAGGCGGATCGGGGACTGCGGTGTGCGACGGGGACGTCCTGTTCCTCCACAGGGCGACGGTCGCGCCCCAGTCGTCTGGAGGACAACGCAGTCCTCGGCGGGCAGGTACGTCGTCGGCCAGGGGTCGATGGGCCGACCGGGTGCTTCGAGCGTCGGCGTCGGAGACCCGGGAAAAGCCGGTGAGCAAAGGCACAGGGCGGGCTGGTCATCTCAGGTTCCGCGTGATGCGGCGGCTGGACTAGGCTTATGGAGTTGCGCGCGCCCTCGGTGCGCCCGGCAGAGACCTCGTGCAGTCTGCGCCTGTGTCTGTCGGGGCAGCGTATCGCGGGAATCCCCTATCCCTGGGTCAGCCTCGTGCGGCCTGTGGCCGGGGGAGACGTGTGCAAGACCAGAAGAACGTTCGGCCAGGCTCAGGAGCTTCCTGAGAACCGGCTCGACGACAGGAGAACACTCAATGATCCAGCAGGAGTCGCGACTGAAGGTCGCCGACAACACCGGTGCCAAGGAGATCCTTTGCATCCGTGTTCTCGGTGGATCGGGTCGGCGCTATGCGGGTATCGGCGACACGATCGTCGCCACCGTCAAGGACGCCATTCCCGGCGGCAACGTGAAGAAGGGCGAGGTCGTCAAGGCCGTCGTCGTGCGTGCCCGCAAGGAGCGTCGTCGTCCCGACGGCTCATACATCCGCTTCGACGAGAACGCCGCCGTCATCCTCAAGAACGATGGGGAGCCGCGCGGTACGCGCATCTTCGGCCCCGTCGGCCGTGAGCTTCGCGAGAAGAAGTTCATGCGCATCGTCTCGCTCGCCCCGGAGGTGATCTGA","MSARWTPTVRPAASIGPRPRFRRIGDCGVRRGRPVPPQGDGRAPVVWRTTQSSAGRYVVGQGSMGRPGASSVGVGDPGKAGEQRHRAGWSSQVPRDAAAGLGLWSCARPRCARQRPRAVCACVCRGSVSRESPIPGSASCGLWPGETCARPEERSARLRSFLRTGSTTGEHSMIQQESRLKVADNTGAKEILCIRVLGGSGRRYAGIGDTIVATVKDAIPGGNVKKGEVVKAVVVRARKERRRPDGSYIRFDENAAVILKNDGEPRGTRIFGPVGRELREKKFMRIVSLAPEVI$","Ribosomal protein L14","Cytoplasm, Extracellular","50S ribosomal protein L14","50S ribosomal protein L14","ribosomal protein L14","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000218
Family

Ribosomal protein L14b/L23e
PD001093	$\"[173-293]T$	Q82DN5_STRAW_Q82DN5;
G3DSA:2.40.150.20	$\"[173-294]T$	no description
PTHR11761	$\"[173-294]T$	50S/60S RIBOSOMAL PROTEIN L14/L23
PF00238	$\"[173-294]T$	Ribosomal_L14
PS00049	$\"[232-258]T$	RIBOSOMAL_L14

InterPro
IPR005745
Family

Ribosomal protein L14, bacterial and organelle form
PTHR11761:SF3	$\"[173-294]T$	50S RIBOSOMAL PROTEIN L14
TIGR01067	$\"[173-294]T$	rplN_bact: ribosomal protein L14

","BeTs to 26 clades of COG0093COG name: Ribosomal protein L14Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0093 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000218 (Ribosomal protein L14b/L23e) with a combined E-value of 1.2e-77. IPB000218A 173-198 IPB000218B 204-239 IPB000218C 245-280 IPB000218D 285-294","Residues 173-293 are similar to a (RIBOSOMAL L14 RIBONUCLEOPROTEIN RRNA-BINDING 50S CHLOROPLAST 60S L23 L14P MITOCHONDRION) protein domain (PD001093) which is seen in Q82DN5_STRAW.","","-75% similar to PDB:1C04 IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI (E_value = 8.7E_40);-75% similar to PDB:1GIY CRYSTAL STRUCTURE OF THE RIBOSOME AT 5.5 A RESOLUTION. THIS FILE, 1GIY, CONTAINS THE 50S RIBOSOME SUBUNIT. THE 30S RIBOSOME SUBUNIT, THREE TRNA, AND MRNA MOLECULES ARE IN THE FILE 1GIX (E_value = 8.7E_40);-75% similar to PDB:1ML5 Structure of the E. coli ribosomal termination complex with release factor 2 (E_value = 8.7E_40);-75% similar to PDB:1WHI RIBOSOMAL PROTEIN L14 (E_value = 8.7E_40);-75% similar to PDB:1YL3 Crystal structure of 70S ribosome with thrS operator and tRNAs. Large subunit. The coordinates for the small subunit are in the pdb entry 1YL4. (E_value = 8.7E_40);","Residues 173 to 294 (E_value = 1.5e-79) place ANA_0037 in the Ribosomal_L14 family which is described as Ribosomal protein L14p/L23e.","","ribosomal protein L14","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0038","48459","48803","345","10.68","14.41","12527","ATGGCACGCATCAAGAAGGGCGACCAGGTCATCGTCATCGCCGGTAAGGACAAGGGCAAGACCGGCCGCGTTCTGGAGGTCCTCAAGGGCACTGACCGTGTCATCGTCGAGGGCGTCCAGCGCGTGACCAAGCACACCAAGGTGGGGCAGTCCCAGCAGGGCGCCCGCACCGGCGGCATCGAGACCGTTGAGGCGCCCATCCACGCCTCCAACGTCATGCTCGTCGACCCCAAGACAAAGAAGCGCACCCGCGTGGGCTTCCGCGTCGAGGAGGGCGTGCGTCCCGACGGCCGCAAGCGCACCGTCCGCGTGCGTTACGCCAAGAAGAGCGGGGAGGACCTGTGA","MARIKKGDQVIVIAGKDKGKTGRVLEVLKGTDRVIVEGVQRVTKHTKVGQSQQGARTGGIETVEAPIHASNVMLVDPKTKKRTRVGFRVEEGVRPDGRKRTVRVRYAKKSGEDL$","Ribosomal protein L24","Cytoplasm, Extracellular","ribosomal protein L24","50S ribosomal protein L24","ribosomal protein L24","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Kyrpides N.C., Woese C.R., Ouzounis C.A. KOW: a novel motif linking a bacterial transcription factor with ribosomal proteins. Trends Biochem. Sci. 1996. 21(11):425-426. PMID: 8987397","","","

InterPro
IPR003256
Family

Ribosomal protein L24
PD001677	$\"[6-39]T$	RL24_CAUCR_Q9A8U2;
PTHR12903	$\"[2-114]T$	MITOCHONDRIAL RIBOSOMAL PROTEIN L24
TIGR01079	$\"[1-114]T$	rplX_bact: ribosomal protein L24

InterPro
IPR005824
Domain

KOW
PF00467	$\"[4-37]T$	KOW

InterPro
IPR005825
Family

Ribosomal protein L24/L26
PS01108	$\"[7-24]T$	RIBOSOMAL_L24

InterPro
IPR006646
Domain

KOW (Kyrpides, Ouzounis, Woese) motif
SM00739	$\"[3-30]T$	KOW

InterPro
IPR014723
Domain

Ribosomal protein L24, SH3-like
G3DSA:2.30.30.200	$\"[3-95]T$	no description

","BeTs to 25 clades of COG0198COG name: Ribosomal protein L24Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0198 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003256 (Ribosomal protein L24) with a combined E-value of 3.6e-32. IPB003256A 4-24 IPB003256B 33-48 IPB003256C 58-72***** IPB006646 (KOW (Kyprides, Ouzounis, Woese) motif) with a combined E-value of 4.2e-11. IPB006646 4-24","No significant hits to the ProDom database.","","-58% similar to PDB:1NKW Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans (E_value = 3.6E_15);-58% similar to PDB:1NWX COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH ABT-773 (E_value = 3.6E_15);-58% similar to PDB:1NWY COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN (E_value = 3.6E_15);-58% similar to PDB:1PNU Crystal Structure of a Streptomycin Dependent Ribosome from Escherichia Coli, 50S Subunit of 70S Ribosome. THIS FILE, 1PNU, CONTAINS ONLY MOLECULES OF THE 50S RIBOSOMAL SUBUNIT. THE 30S SUBUNIT, MRNA, P-SITE TRNA, AND A-SITE TRNA ARE IN THE PDB FILE 1PNS. (E_value = 3.6E_15);-58% similar to PDB:1PNY Crystal Structure of the Wild Type Ribosome from E. Coli, 50S Subunit of 70S Ribosome. THIS FILE, 1PNY, CONTAINS ONLY MOLECULES OF THE 50S RIBOSOMAL SUBUNIT. THE 30S SUBUNIT IS IN THE PDB FILE 1PNX. (E_value = 3.6E_15);","Residues 4 to 37 (E_value = 6.5e-11) place ANA_0038 in the KOW family which is described as KOW motif.","","protein L24 (rplX)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0039","48806","49363","558","9.52","5.92","20856","ATGGCTGAGAAGACCACCCCCCGTCTCAAGACGAAGTACACCGAGGAGGTGCGCCCCGCCCTGCTCAAGGAGTTCCAGCACGGCAACGTGATGGAGGTCGGGCGCGTCGTCAAGGTCGTCGTCAACATGGGTGTGGGCGAGGCCGCCCACGACTCCAAAATGATCGAGGGCGCCGTGCGCGACCTCGCCGCCATCACCGGCCAGAAGCCCCAGGTCACCCGGGCCCGCAAGTCCATCGCGCAGTTCAAGCTGCGTGAGGGCATGCCGATCGGTGCGCACTCCACGCTGCGCGGCGACCGCATGTGGGAGTTCCTGGACCGCCTGGTCTCGATCTCCCTTCCCCGTATCCGCGACTTCCGGGGTCTGAGCCCCAAGCAGTTCGACGGGAACGGCAACTACACCTTCGGTCTGACCGAGCAGGCTGTCTTCCACGAGATCGACCAGGACCAGATCGACCGCGTCCGCGGCATGGACATCACCGTGGTGACCACGGCCAAGACCGACGAGGAGGCCCGCTCGCTGCTCAAGCAGCTCGGCTTCCCCTTCAAGGAGAAGTGA","MAEKTTPRLKTKYTEEVRPALLKEFQHGNVMEVGRVVKVVVNMGVGEAAHDSKMIEGAVRDLAAITGQKPQVTRARKSIAQFKLREGMPIGAHSTLRGDRMWEFLDRLVSISLPRIRDFRGLSPKQFDGNGNYTFGLTEQAVFHEIDQDQIDRVRGMDITVVTTAKTDEEARSLLKQLGFPFKEK$","Ribosomal protein L5","Cytoplasm","50S ribosomal protein","50S ribosomal protein L5","ribosomal protein L5","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Hatakeyama T. Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui. Biochim. Biophys. Acta 1990. 1039(3):343-347. PMID: 2198942Rosendahl G., Andreasen P.H., Kristiansen K. Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21. Gene 1991. 98(2):161-167. PMID: 2016059Yang D., Gunther I., Matheson A.T., Auer J., Spicker G., Bock A. The structure of the gene for ribosomal protein L5 in the archaebacterium Sulfolobus acidocaldarius. Biochimie 1991. 73(6):679-682. PMID: 1840500","","","

InterPro
IPR002132
Family

Ribosomal protein L5
PTHR11994	$\"[3-185]T$	60S RIBOSOMAL PROTEIN L11-RELATED
PF00281	$\"[29-85]T$	Ribosomal_L5
PF00673	$\"[89-183]T$	Ribosomal_L5_C

InterPro
IPR003236
Family

Mitochondrial ribosomal protein L5
PD013434	$\"[13-183]T$	Q6AD07_BBBBB_Q6AD07;

noIPR
unintegrated

unintegrated
G3DSA:3.30.1440.10	$\"[6-184]T$	no description
PTHR11994:SF4	$\"[3-185]T$	50S RIBOSOMAL PROTEIN L5

","BeTs to 26 clades of COG0094COG name: Ribosomal protein L5Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0094 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003236 (Mitochondrial ribosomal protein L5) with a combined E-value of 1.1e-87. IPB003236A 29-48 IPB003236B 65-118 IPB003236C 127-144 IPB003236D 149-183","Residues 13-183 are similar to a (RIBOSOMAL RRNA-BINDING 50S RNA-BINDING L5 TRNA-BINDING 60S L11 RIBONUCLEOPROTEIN CHLOROPLAST) protein domain (PD013434) which is seen in Q6AD07_BBBBB.","","-71% similar to PDB:1MJI DETAILED ANALYSIS OF RNA-PROTEIN INTERACTIONS WITHIN THE BACTERIAL RIBOSOMAL PROTEIN L5/5S RRNA COMPLEX (E_value = 1.4E_51);-71% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 1.4E_51);-71% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 1.4E_51);-71% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 1.4E_51);-71% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 1.4E_51);","Residues 29 to 85 (E_value = 1.1e-28) place ANA_0039 in the Ribosomal_L5 family which is described as Ribosomal protein L5.Residues 89 to 183 (E_value = 3.2e-54) place ANA_0039 in the Ribosomal_L5_C family which is described as ribosomal L5P family C-terminus.","","ribosomal protein (BL6)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0040","49365","49550","186","10.68","12.03","6996","ATGGCGAAGACCGCACTGATTGAGAAGGCGAACCGCAAGCCCAAGTTCGGTGTCCGTGCCTACACGCGCTGCCAGCGCTGCGGCCGCCCGCACTCGGTCTACCGCAAGTTCGGCCTGTGCCGTATCTGCCTGCGTGAGATGGCCCTTCGCGGCGAGCTCCCGGGCGTGAGCAAGTCCAGCTGGTAA","MAKTALIEKANRKPKFGVRAYTRCQRCGRPHSVYRKFGLCRICLREMALRGELPGVSKSSW$","Ribosomal protein S14","Extracellular, Cytoplasm","ribosomal protein S14p/S29e","K02954 small subunit ribosomal protein S14","ribosomal protein S14","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Chan Y.L., Suzuki K., Olvera J., Wool I.G. Zinc finger-like motifs in rat ribosomal proteins S27 and S29. Nucleic Acids Res. 1993. 21(3):649-655. PMID: 8441676","","","

InterPro
IPR001209
Family

Ribosomal protein S14
PTHR19836	$\"[10-61]T$	30S RIBOSOMAL PROTEIN S14
PF00253	$\"[6-60]T$	Ribosomal_S14
PS00527	$\"[23-45]T$	RIBOSOMAL_S14

noIPR
unintegrated

unintegrated
G3DSA:4.10.830.10	$\"[1-61]T$	no description
PTHR19836:SF6	$\"[10-61]T$	30S RIBOSOMAL PROTEIN S14

","BeTs to 25 clades of COG0199COG name: Ribosomal protein S14Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0199 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001209 (Ribosomal protein S14) with a combined E-value of 1e-28. IPB001209 22-61","Residues 10-51 are similar to a (RIBOSOMAL S14 30S CHLOROPLAST S14-1 S14-2 S14P SEQUENCING DIRECT IRON) protein domain (PD833763) which is seen in R14A_STRCO.Residues 19-61 are 76% similar to a (RIBOSOMAL S14 CHLOROPLAST 30S MITOCHONDRION MITOCHONDRIAL S14MT 28S MRP-S14 S14-2) protein domain (PD001990) which is seen in Q7VKE6_HAEDU.","","-84% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 5.2E_22);-84% similar to PDB:1GIX Crystal structure of the ribosome at 5.5 A resolution. This file, 1GIX, contains the 30S ribosome subunit, three tRNA, and mRNA molecules. 50S ribosome subunit is in the file 1GIY (E_value = 5.2E_22);-84% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 5.2E_22);-84% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 5.2E_22);-84% similar to PDB:1HNZ STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH HYGROMYCIN B (E_value = 5.2E_22);","Residues 6 to 60 (E_value = 5.3e-22) place ANA_0040 in the Ribosomal_S14 family which is described as Ribosomal protein S14p/S29e.","","protein S14p-S29e (rpsN)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0041","49609","50007","399","9.70","6.16","14172","ATGACAATGACAGACCCCATCGCAGACATGCTGACCCGTCTGCGCAACGCAAACAGCGCCTACCACGACACCGTGTCGATGCCGTCGAGCAAGCTCAAGGTGAACATCGCTGAGATGCTCAAGGCCGAGGGCTACATCGCCGGCTACGAGGTCACGGACGCCGAGGTCGGCAAGACGCTCACGCTGAGCCTCAAGTACGGAGCCAACCGCCAGCGGGCCATCCAGGGCCTGCGCCGGATCTCCAAGCCCGGCCTGCGCGTCTACGCCAAGTCCACCAACCTGCCCAAGGTCCTCGGCGGCCTGGGAGTGGCAATCCTGTCCACCTCCTCCGGCCTCCTGACCGACAAGCAGGCCGAGTCGCGTGGCGTGGGCGGCGAAGTCCTCGCCTACGTCTGGTAA","MTMTDPIADMLTRLRNANSAYHDTVSMPSSKLKVNIAEMLKAEGYIAGYEVTDAEVGKTLTLSLKYGANRQRAIQGLRRISKPGLRVYAKSTNLPKVLGGLGVAILSTSSGLLTDKQAESRGVGGEVLAYVW$","Ribosomal protein S8","Extracellular","ribosomal protein S8","30S ribosomal protein S8","ribosomal protein S8","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000630
Family

Ribosomal protein S8
PD001098	$\"[10-132]T$	Q6AD08_BBBBB_Q6AD08;
PTHR11758	$\"[2-132]T$	30S RIBOSOMAL PROTEIN S8
PF00410	$\"[5-132]T$	Ribosomal_S8

noIPR
unintegrated

unintegrated
G3DSA:3.30.1370.30	$\"[2-73]T$	no description
G3DSA:3.30.1490.10	$\"[75-132]T$	no description

","BeTs to 26 clades of COG0096COG name: Ribosomal protein S8Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0096 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000630 (Ribosomal protein S8) with a combined E-value of 1e-45. IPB000630A 5-17 IPB000630B 28-49 IPB000630C 84-132","Residues 10-132 are similar to a (RIBOSOMAL S8 30S RRNA-BINDING RNA-BINDING RIBONUCLEOPROTEIN CHLOROPLAST S15A 40S S8P) protein domain (PD001098) which is seen in Q6AD08_BBBBB.","","-74% similar to PDB:1SEI STRUCTURE OF 30S RIBOSOMAL PROTEIN S8 (E_value = 2.2E_37);-72% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.4E_31);-72% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.4E_31);-64% similar to PDB:1EG0 FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME (E_value = 3.1E_31);-64% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 3.1E_31);","Residues 5 to 132 (E_value = 7.6e-71) place ANA_0041 in the Ribosomal_S8 family which is described as Ribosomal protein S8.","","protein S8 (rpsH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0042","50029","50568","540","9.88","8.42","19170","ATGTCTCGTATTGGACGGCTCCCCGTTCCGGTCCCTGCCGGAGTGGACGTCACCATCGACGGCCAGGACGTGACGGTCAAGGGCCCCAAGGGCACCCTGTCCCGCACGATCAGCGAGCCCCTGAGCGTCACCCGCCAGGAGGACGGCTCCATCCTGGTTACGCGCCCCGACGACGAGCGCCGCTCGCGCTCGCTGCACGGACTGTCGCGCACCCTCATCAACAACATGGTGATCGGCGTCACCGAGGGCTACACCAAGCAGCTCGAGATCGTCGGCACCGGTTACCGCGTCGCCGCCAAGGGCCAGGGCATCGAGCTCTCCCTCGGCTTCTCCCACACCGTGACCGTTGAGCCCCCCGAGGGCATCACCTTCACGGTCGACGGCAACCTGAAGATCACCGTCTCCGGTATCTCCAAGGAGCAGGTCGGCGAGGTCGCGGCGAACATCCGCAAGATCCGTCCGCCGGAGCCCTACAAGGGCAAGGGCGTGCGCTACGCCGGCGAGAACGTGCGCCGCAAGGTCGGAAAGGCTGGTAAGTGA","MSRIGRLPVPVPAGVDVTIDGQDVTVKGPKGTLSRTISEPLSVTRQEDGSILVTRPDDERRSRSLHGLSRTLINNMVIGVTEGYTKQLEIVGTGYRVAAKGQGIELSLGFSHTVTVEPPEGITFTVDGNLKITVSGISKEQVGEVAANIRKIRPPEPYKGKGVRYAGENVRRKVGKAGK$","Ribosomal protein L6","Cytoplasm, Extracellular","50S ribosomal protein","50S ribosomal protein L6","ribosomal protein L6","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Suzuki K., Olvera J., Wool I.G. The primary structure of rat ribosomal protein L9. Gene 1990. 93(2):297-300. PMID: 2227441Harrer R., Schwank S., Schuller H.J., Schweizer E. Molecular cloning and analysis of the nuclear gene MRP-L6 coding for a putative mitochondrial ribosomal protein from Saccharomyces cerevisiae. Curr. Genet. 1993. 24(1):136-140. PMID: 8358820Golden B.L., Ramakrishnan V., White S.W. Ribosomal protein L6: structural evidence of gene duplication from a primitive RNA binding protein. EMBO J. 1993. 12(13):4901-4908. PMID: 8262035","","","

InterPro
IPR000702
Family

Ribosomal protein L6
PD002236	$\"[88-176]T$	Q6AD09_BBBBB_Q6AD09;
PR00059	$\"[72-97]T$ $\"[100-116]T$ $\"[142-163]T$	RIBOSOMALL6
G3DSA:3.90.930.12	$\"[2-83]T$ $\"[84-179]T$	no description
PTHR11655	$\"[2-179]T$	60S/50S RIBOSOMAL PROTEIN L6/L9
PF00347	$\"[11-83]T$ $\"[91-166]T$	Ribosomal_L6

InterPro
IPR002358
Family

Ribosomal protein L6, signature 1
PS00525	$\"[155-163]T$	RIBOSOMAL_L6_1

noIPR
unintegrated

unintegrated
PTHR11655:SF6	$\"[2-179]T$	50S RIBOSOMAL PROTEIN L6

","BeTs to 26 clades of COG0097COG name: Ribosomal protein L6Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0097 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002358 (Ribosomal protein L6, signature 1) with a combined E-value of 4e-84. IPB002358A 1-31 IPB002358B 67-114 IPB002358C 136-176***** IPB002359 (Ribosomal protein L6, signature 2) with a combined E-value of 7.4e-19. IPB002359A 7-35 IPB002359B 60-97 IPB002359C 129-172","Residues 1-56 are 87% similar to a (RIBOSOMAL L6 RIBONUCLEOPROTEIN 50S RRNA-BINDING L6P 60S CHLOROPLAST LSU L9) protein domain (PD003414) which is seen in RL6_MYCTU.Residues 22-84 are 67% similar to a (RIBOSOMAL RIBONUCLEOPROTEIN 60S L9 L6P 50S STRAIN L6 NRRL LACTIS) protein domain (PDA1D631) which is seen in RM06_YEAST.Residues 57-87 are 93% similar to a (RIBOSOMAL L6 RIBONUCLEOPROTEIN 50S RRNA-BINDING CHLOROPLAST LSU L6P SEQUENCING DIRECT) protein domain (PD767578) which is seen in Q6A6P1_PROAC.Residues 88-176 are similar to a (RIBOSOMAL L6 RIBONUCLEOPROTEIN 50S RRNA-BINDING MITOCHONDRION CHLOROPLAST 60S MITOCHONDRIAL LSU) protein domain (PD002236) which is seen in Q6AD09_BBBBB.","","-72% similar to PDB:1C04 IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI (E_value = 7.0E_53);-72% similar to PDB:1GIY CRYSTAL STRUCTURE OF THE RIBOSOME AT 5.5 A RESOLUTION. THIS FILE, 1GIY, CONTAINS THE 50S RIBOSOME SUBUNIT. THE 30S RIBOSOME SUBUNIT, THREE TRNA, AND MRNA MOLECULES ARE IN THE FILE 1GIX (E_value = 7.0E_53);-72% similar to PDB:1ML5 Structure of the E. coli ribosomal termination complex with release factor 2 (E_value = 7.0E_53);-72% similar to PDB:1RL6 RIBOSOMAL PROTEIN L6 (E_value = 7.0E_53);-72% similar to PDB:1YL3 Crystal structure of 70S ribosome with thrS operator and tRNAs. Large subunit. The coordinates for the small subunit are in the pdb entry 1YL4. (E_value = 7.0E_53);","Residues 11 to 83 (E_value = 3e-27) place ANA_0042 in the Ribosomal_L6 family which is described as Ribosomal protein L6.Residues 91 to 166 (E_value = 5.8e-30) place ANA_0042 in the Ribosomal_L6 family which is described as Ribosomal protein L6.","","ribosomal protein (BL8)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0043","50571","50951","381","10.58","13.58","13528","ATGGCTTACTCGATCAAGAGGGGCAAGGGCAACCCCCGCGCCATCGCCCGCAAGATCCGTCACCAGCGCGTGCGCAAGCACATCTCCGGCACGCCCGAGCGTCCCCGCCTGGTGGTCACCCGATCCAACCGCCACATGGTGGCTCAAGTCGTGGACGACACCATCGGTCACACCCTGTGCGCCGCCTCCACCCTGGAGGAGGCCGCCAAGGGCGTCGAGGGCCACAAGGTGGGCGCCGCCCACAAGGTCGGCGAGCTCATCGCCGAGCGTGCCAAGGCGCTGGGCATTGAGGCAGTCGTGTTCGACCGCGGCGGCAACAAGTACCACGGCCGTGTCGCGGCCGTCGCCGAGGGCGCCCGTGAGGGCGGCCTGAAGCTGTGA","MAYSIKRGKGNPRAIARKIRHQRVRKHISGTPERPRLVVTRSNRHMVAQVVDDTIGHTLCAASTLEEAAKGVEGHKVGAAHKVGELIAERAKALGIEAVVFDRGGNKYHGRVAAVAEGAREGGLKL$","Ribosomal protein L18","Cytoplasm","ribosomal protein L18","ribosomal protein L18","ribosomal protein L18","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR004389
Family

Ribosomal protein L18
TIGR00060	$\"[13-126]T$	L18_bact: ribosomal protein L18

InterPro
IPR005484
Family

Ribosomal protein L18P/L5E
PD001394	$\"[39-108]T$	Q8G402_BIFLO_Q8G402;
PF00861	$\"[12-126]T$	Ribosomal_L18p

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.100	$\"[34-126]T$	no description

","BeTs to 24 clades of COG0256COG name: Ribosomal protein L18Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0256 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005484 (Ribosomal protein L18P/L5E) with a combined E-value of 6.6e-41. IPB005484A 12-30 IPB005484B 34-64 IPB005484C 76-90 IPB005484D 109-126","Residues 39-108 are similar to a (RIBOSOMAL L18 50S RRNA-BINDING 60S L5 L18P CHLOROPLAST LSU SUBUNIT) protein domain (PD001394) which is seen in Q8G402_BIFLO.","","-68% similar to PDB:1OVY Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus (E_value = 6.8E_22);-62% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 8.9E_14);-62% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 8.9E_14);-62% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 8.9E_14);-62% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 8.9E_14);","Residues 12 to 126 (E_value = 1.3e-55) place ANA_0043 in the Ribosomal_L18p family which is described as Ribosomal L18p/L5e family.","","protein L18 (rplR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0044","50986","51693","708","9.69","7.90","24999","ATGGCTGCACCGCAGCGAGACAGGTCCGCGTCGTCCGACGGCTCGGCCCAGCGCGAGAACGACGAGCGCCGGGGCGAGGGCCGCGGCCGCCGCGACCGCAACAACGACCGCCGCGACCGTGGTCGCGGCAACGACGACAAGTACATCGAGCGCGTCGTCACCATCAACCGCGTGTCCAAGGTCGTCAAGGGCGGCCGCCGCTTCACCTTCACGGCCCTCGTGGTCGTCGGTGACGGCGAGGGCACCGTCGGCGTGGGCTACGGCAAGGCGAAGGAAGTTCCCGCCGCCATCGCCAAGGCCGTCGAGATCGCGAAGAAGAACTTCTTCCACGTCCCGATGATCCGCCGCACCATCCCGCACCTGGTCCAGGGTGAGGACTCCGCCGGAGTCGTCCTCCTGCGCCCGGCGTCCCCCGGTACCGGTGTTATCGCCGGTGGCCCGGTGCGCGCCGTGCTGGACTGCGCCGGTGTCCACGACATCCTGTCCAAGTCGCTGGGCTCCTCCAACGCGATCAACATCGTGCACGCCACGGTGGACGCCCTCAAGCAGCTCGAGCAGCCGGAGGCCGTTGCGGCCCGCCGTGGCCTGCCGCTGGAGGACGTCGCCCCGCAGTCCATGCTGCGGGCCCGCGCCGAGGGTGAGGCTGACAAGCGCGCTCAGGCTGAGAAGCAGGAGGCCGAGAAGGCCGCTGAAGGAGTGGGTGCGTGA","MAAPQRDRSASSDGSAQRENDERRGEGRGRRDRNNDRRDRGRGNDDKYIERVVTINRVSKVVKGGRRFTFTALVVVGDGEGTVGVGYGKAKEVPAAIAKAVEIAKKNFFHVPMIRRTIPHLVQGEDSAGVVLLRPASPGTGVIAGGPVRAVLDCAGVHDILSKSLGSSNAINIVHATVDALKQLEQPEAVAARRGLPLEDVAPQSMLRARAEGEADKRAQAEKQEAEKAAEGVGA$","Ribosomal protein S5","Cytoplasm","30S ribosomal protein","30S ribosomal protein S5","ribosomal protein S5","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000851
Family

Ribosomal protein S5
PTHR13718	$\"[32-226]T$	RIBOSOMAL S SUBUNIT

InterPro
IPR005324
Domain

Ribosomal protein S5, C-terminal
PF03719	$\"[122-195]T$	Ribosomal_S5_C

InterPro
IPR005712
Family

Ribosomal protein S5, bacterial and chloroplast
TIGR01021	$\"[45-200]T$	rpsE_bact: ribosomal protein S5

InterPro
IPR013222
Domain

Glycosyl hydrolase family 98, putative carbohydrate-binding module
SM00776	$\"[8-154]T$	no description

InterPro
IPR013810
Domain

Ribosomal protein S5, N-terminal
PF00333	$\"[47-113]T$	Ribosomal_S5
PS50881	$\"[48-111]T$	S5_DSRBD
PS00585	$\"[65-97]T$	RIBOSOMAL_S5

InterPro
IPR014720
Domain

Double-stranded RNA-binding-like
G3DSA:3.30.160.20	$\"[38-110]T$	no description

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[111-187]T$	no description

noIPR
unintegrated

unintegrated
PTHR13718:SF2	$\"[32-226]T$	30S RIBOSOMAL PROTEIN S5

","BeTs to 26 clades of COG0098COG name: Ribosomal protein S5Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0098 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000851 (Ribosomal protein S5) with a combined E-value of 1.6e-61. IPB000851A 51-102 IPB000851B 131-172","Residues 117-186 are similar to a (RIBOSOMAL S5 30S RIBONUCLEOPROTEIN RNA-BINDING RRNA-BINDING S2 40S S5P CHLOROPLAST) protein domain (PD001364) which is seen in Q6AD11_BBBBB.","","-59% similar to PDB:1PKP THE STRUCTURE OF RIBOSOMAL PROTEIN S5 REVEALS SITES OF INTERACTION WITH 16S RRNA (E_value = 7.2E_28);-59% similar to PDB:1DV4 PARTIAL STRUCTURE OF 16S RNA OF THE SMALL RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS (E_value = 9.4E_28);-59% similar to PDB:1EG0 FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME (E_value = 9.4E_28);-59% similar to PDB:1QD7 PARTIAL MODEL FOR 30S RIBOSOMAL SUBUNIT (E_value = 9.4E_28);-59% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 2.7E_27);","Residues 47 to 113 (E_value = 4.1e-36) place ANA_0044 in the Ribosomal_S5 family which is described as Ribosomal protein S5, N-terminal domain.Residues 122 to 195 (E_value = 1.1e-38) place ANA_0044 in the Ribosomal_S5_C family which is described as Ribosomal protein S5, C-terminal domain.","","ribosomal protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0045","51693","51899","207","10.92","6.64","7532","ATGGCTGAGTCCGCATCGAAGCAGATGACCAAGCAGCTCAAGGTCACTCAGGTCCGCTCTGGCATCGGGGGCACCCACCGCCAGCGCGAGTCCCTCAAGACCCTGGGTCTGCGCAAGATCCGCCAGTCCGTCGTGCGCGAGGACAGCCCCAGCGTGCGCGGCCTGATTGCCACGGTGCACCACCTGGTCACCGTTGAGGAGGTCTGA","MAESASKQMTKQLKVTQVRSGIGGTHRQRESLKTLGLRKIRQSVVREDSPSVRGLIATVHHLVTVEEV$","Ribosomal protein L30","Cytoplasm","50S ribosomal protein-related protein","ribosomal protein L30","ribosomal protein L30","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Mizuta K., Hashimoto T., Otaka E. Yeast ribosomal proteins: XIII. Saccharomyces cerevisiae YL8A gene, interrupted with two introns, encodes a homolog of mammalian L7. Nucleic Acids Res. 1992. 20(5):1011-1016. PMID: 1549461","","","

InterPro
IPR000517
Domain

Ribosomal protein L30
PF00327	$\"[11-63]T$	Ribosomal_L30
PS00634	$\"[31-63]T$	RIBOSOMAL_L30

InterPro
IPR005996
Family

Ribosomal protein L30, bacterial
TIGR01308	$\"[13-67]T$	rpmD_bact: ribosomal protein L30

noIPR
unintegrated

unintegrated
G3DSA:3.30.1390.20	$\"[10-68]T$	no description

","BeTs to 15 clades of COG1841COG name: Ribosomal protein L30/L7EFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1841 is aompkzyqvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB000517 (Ribosomal protein L30) with a combined E-value of 4.2e-23. IPB000517 15-66","Residues 18-65 are similar to a (RIBOSOMAL L30 50S RIBONUCLEOPROTEIN L30P LSU L30/L7E SEQUENCING DIRECT STRAIN) protein domain (PD005137) which is seen in Q73S91_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 63 (E_value = 1.5e-12) place ANA_0045 in the Ribosomal_L30 family which is described as Ribosomal protein L30p/L7e.","","ribosomal protein-related protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0046","51901","52377","477","10.56","14.65","16890","ATGGCTGACACCGAGAACACGCAGGAGGAGAAGGTGCGCGTCGTCAAGCTGCACCACCTGCGTCCCGCCCCCGGCGCCAAGAAGGCCAAGACCCGCGTGGGTCGTGGTGAGGCGTCCAAGGGTAAGACCGCCGGTCGCGGTACCAAGGGCACCAAGGCTCGTTACCAGGTCCGTCCTGGTTTCGAGGGTGGCCAGATGCCGCTGCACATGCGTCTTCCCAAGCTGCGCGGCTTCCGCAACCCCAACCGGGTCGAGTTCCAGCCTGTGAACGTCGGCCGCATCGCCGAGCTGTTCCCCGAGGGCGGCACGGTGACCGTGGAGGATCTCGTCGCCAAGGGTGCGGTTCGCAAGAACCAGCTCGTCAAGGTCCTCGGCGGCGGCGACGTCACCGTGGCCCTGACGCTCACGGTCGACGCCTGGTCCGGCTCCGCCAAGGAGAAGATCGAGGCTGCTGGCGGCTCCATCGCCACGCGCTAA","MADTENTQEEKVRVVKLHHLRPAPGAKKAKTRVGRGEASKGKTAGRGTKGTKARYQVRPGFEGGQMPLHMRLPKLRGFRNPNRVEFQPVNVGRIAELFPEGGTVTVEDLVAKGAVRKNQLVKVLGGGDVTVALTLTVDAWSGSAKEKIEAAGGSIATR$","Ribosomal protein L15","Cytoplasm, Periplasm","ribosomal protein L15","50S ribosomal protein L15","ribosomal protein L15","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001196
Family

Ribosomal protein L15
PF00256	$\"[122-153]T$	L15
PF01305	$\"[15-115]T$	Ribosomal_L15

InterPro
IPR005749
Family

Ribosomal protein L15, bacterial form
PTHR12934	$\"[51-155]T$	50S RIBOSOMAL PROTEIN L15
TIGR01071	$\"[16-156]T$	rplO_bact: ribosomal protein L15

noIPR
unintegrated

unintegrated
G3DSA:3.100.10.10	$\"[78-156]T$	no description

","BeTs to 25 clades of COG0200COG name: Ribosomal protein L15Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0200 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001196 (Ribosomal protein L15) with a combined E-value of 3.7e-19. IPB001196A 29-55 IPB001196B 113-129 IPB001196C 132-153","Residues 68-152 are 59% similar to a (CHLOROPLAST RIBOSOMAL PEPTIDE CL15 L15 TRANSIT 50S PRECURSOR) protein domain (PD961413) which is seen in RK15_ARATH.Residues 85-155 are similar to a (RIBOSOMAL 50S L15 RIBONUCLEOPROTEIN L18E L15P RRNA-BINDING LSU SEQUENCING DIRECT) protein domain (PD002840) which is seen in RL15_MYCLE.","","-53% similar to PDB:1NKW Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans (E_value = 8.7E_14);-53% similar to PDB:1NWX COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH ABT-773 (E_value = 8.7E_14);-53% similar to PDB:1NWY COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH AZITHROMYCIN (E_value = 8.7E_14);-53% similar to PDB:1SM1 COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH QUINUPRISTIN AND DALFOPRISTIN (E_value = 8.7E_14);-53% similar to PDB:1XBP Inhibition of peptide bond formation by pleuromutilins: The structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with Tiamulin (E_value = 8.7E_14);","Residues 15 to 115 (E_value = 1.2e-53) place ANA_0046 in the Ribosomal_L15 family which is described as Ribosomal protein L15 amino terminal region.Residues 122 to 153 (E_value = 1.7e-09) place ANA_0046 in the L15 family which is described as Ribosomal protein L15.","","protein L15 (rplO)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0047","52724","54025","1302","9.47","9.59","46823","GTGCTCAGCGCGTTCACTCAGGCGTTCAGAACGCCAGACCTCAGGGCGAAGCTGCTCTTCACCCTCGGCATCATGGCCCTGTTCCGGCTCGGGTCGATCCTGCCGGCGCCCGGCGTCAACCTGGCCAACGCCAAGTACTGCATCGGAGAGGCCGGCAAGGAGCAGAACCTCCTCAGCCTGGTCAACGTCTTCTCCGGTGGTGCGCTGCTCCAGCTGAGCGTCTTCGCGCTGGGCATCATGCCCTACATCACCGCCTCCATCATCATCCAGCTCCTGCGGGTCGTCATCCCCCGCTTCGAGGAGCTCCACAAGGAGGGGCAGGCGGGCACCGCCAAACTCACCGAGTACACCCGCTACCTCACCATCGGCCTGGGGCTGCTCCAGTCCAGCACCATCGTGGCCACGGCCAAGAGCGGCCAGCTCTTCCAGGGATGCGCGCGCGCCCAGGACATCGTCCCCGGCGACTCGATCGTCACCCCGCTGCTCATCATCATCACCATGACCGCCGGCACCGGCCTCATCATGTGGCTGGGTGAGCTCATCACCGAGCGCGGCATCGGTAACGGCATGTCACTGCTCATCTTCACCTCCATCGTGGCCCAGTTCCCCTCCAACATGTTCTCCATCGCCGGAGGCAACAACGGGGCGGCCAACTTCGCCATCATCGTGGCCGTCGTCCTCCTGGCCACCCTCGCGGTCGTCTACATCGAGCAGGCCCAGCGGCGCATCCCCGTGCAGTACGCCAAGCGGATGATCGGGCGGCGCCAGTACGGCGGATCGACCACCTACATCCCGGTCAAGATCAACACCGCCGGCGTCATCCCCGTCATCTTCGCCTCCTCGATCCTGGCCATGCCCCAGCTCATCGCCGGCTTCGGCAATCAGGCGAGCAAGTGGGTGCAGTGGATCCTGACGAACCTGCAGCAGACGAGCCCGATCTACCTGACTGCCTACGGCGTCCTCATCCTGTTCTTCGCCTTCTTCTACACGGCCATCACCTTCGACGCCGAGGAGATCGCGGACAACATGAAGCGCTACGGCGGCTTCATCCCCGGCATCCGCGCCGGTGAGCCCACCGTGCGCTACCTGTCCTACGTCATCAACCGCATCACGACGGCGGGCTCCATCTACCTGGTGGTCCTCGCCCTCATCCCGACGCTCGCCGTCATCTGGCTGGACCTGGCTCAGCACCTGCCCTTCGGTGGAACCACTATCCTCATCATGGTGGGCGTGGGACTCCAGACCGTCAAGGAAGTCAACTCCCAGCTGCAGCAGCGTCACTACGAAGGGTTCTTGTCATGA","VLSAFTQAFRTPDLRAKLLFTLGIMALFRLGSILPAPGVNLANAKYCIGEAGKEQNLLSLVNVFSGGALLQLSVFALGIMPYITASIIIQLLRVVIPRFEELHKEGQAGTAKLTEYTRYLTIGLGLLQSSTIVATAKSGQLFQGCARAQDIVPGDSIVTPLLIIITMTAGTGLIMWLGELITERGIGNGMSLLIFTSIVAQFPSNMFSIAGGNNGAANFAIIVAVVLLATLAVVYIEQAQRRIPVQYAKRMIGRRQYGGSTTYIPVKINTAGVIPVIFASSILAMPQLIAGFGNQASKWVQWILTNLQQTSPIYLTAYGVLILFFAFFYTAITFDAEEIADNMKRYGGFIPGIRAGEPTVRYLSYVINRITTAGSIYLVVLALIPTLAVIWLDLAQHLPFGGTTILIMVGVGLQTVKEVNSQLQQRHYEGFLS$","Preprotein translocase, SecY subunit","Membrane, Cytoplasm","preprotein translocase, SecY subunit","K03076 preprotein translocase SecY subunit","preprotein translocase, SecY subunit","","Bieker K.L., Phillips G.J., Silhavy T.J. The sec and prl genes of Escherichia coli. J. Bioenerg. Biomembr. 1990. 22(3):291-310. PMID: 2202721Driessen A.J. SecB, a molecular chaperone with two faces. Trends Microbiol. 2001. 9(5):193-196. PMID: 11336818Muller J.P. Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. FEMS Microbiol. Lett. 1999. 176(1):219-227. PMID: 10418149Breyton C., Haase W., Rapoport T.A., Kuhlbrandt W., Collinson I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 2002. 418(6898):662-665. PMID: 12167867Ito K. SecY and integral membrane components of the Escherichia coli protein translocation system. Mol. Microbiol. 1992. 6(17):2423-2428. PMID: 1406280Suh J.W., Boylan S.A., Thomas S.M., Dolan K.M., Oliver D.B., Price C.W. Isolation of a secY homologue from Bacillus subtilis: evidence for a common protein export pathway in eubacteria. Mol. Microbiol. 1990. 4(2):305-314. PMID: 2110998Auer J., Spicker G., Bock A. Presence of a gene in the archaebacterium Methanococcus vannielii homologous to secY of eubacteria. Biochimie 1991. 73(6):683-688. PMID: 1764515Douglas S.E. A secY homologue is found in the plastid genome of Cryptomonas phi. FEBS Lett. 1992. 298(1):93-96. PMID: 1544427","","","

InterPro
IPR002208
Family

SecY protein
PR00303	$\"[18-36]T$ $\"[72-92]T$ $\"[113-136]T$ $\"[157-182]T$ $\"[183-206]T$ $\"[271-290]T$ $\"[312-334]T$ $\"[367-385]T$ $\"[401-419]T$	SECYTRNLCASE
PTHR10906	$\"[1-433]T$	SECY/SEC61-ALPHA FAMILY MEMBER
PF00344	$\"[73-418]T$	SecY
TIGR00967	$\"[15-428]T$	3a0501s007: preprotein translocase, SecY su
PS00755	$\"[73-92]T$	SECY_1
PS00756	$\"[176-193]T$	SECY_2

noIPR
unintegrated

unintegrated
PTHR10906:SF2	$\"[1-433]T$	PROTEIN TRANSLOCASE SECY SUBUNIT
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[19-39]?$ $\"[60-82]?$ $\"[157-177]?$ $\"[192-210]?$ $\"[216-236]?$ $\"[272-292]?$ $\"[314-334]?$ $\"[370-392]?$ $\"[398-416]?$	transmembrane_regions

","BeTs to 26 clades of COG0201COG name: Preprotein translocase subunit SecYFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0201 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002208 (SecY protein) with a combined E-value of 1.1e-119. IPB002208A 29-40 IPB002208B 64-87 IPB002208C 103-129 IPB002208D 167-203 IPB002208E 263-286 IPB002208F 314-330 IPB002208G 335-381 IPB002208H 401-428 IPB002208E 69-92","Residues 1-76 are 78% similar to a (TRANSMEMBRANE TRANSLOCATION SECY PREPROTEIN SUBUNIT TRANSLOCASE TRANSLOCASE CHLOROPLAST MEMBRANE SECRETION) protein domain (PD859015) which is seen in SECY_STRCO.Residues 77-183 are 83% similar to a (TRANSMEMBRANE TRANSLOCATION SECY PREPROTEIN SUBUNIT TRANSLOCASE TRANSLOCASE CHLOROPLAST MEMBRANE SECRETION) protein domain (PD331160) which is seen in SECY_STRSC.Residues 237-303 are 80% similar to a (TRANSMEMBRANE TRANSLOCATION SECY PREPROTEIN SUBUNIT TRANSLOCASE TRANSLOCASE CHLOROPLAST MEMBRANE SECRETION) protein domain (PD001699) which is seen in SECY_STRSC.Residues 283-428 are 74% similar to a (TRANSMEMBRANE TRANSLOCATION SUBUNIT SECY PREPROTEIN TRANSLOCASE SEC61 ALPHA TRANSLOCASE ENDOPLASMIC) protein domain (PD001749) which is seen in SECY_STRLI.","","-57% similar to PDB:2AKH Normal mode-based flexible fitted coordinates of a non-translocating SecYEG protein-conducting channel into the cryo-EM map of a SecYEG-nascent chain-70S ribosome complex from E. coli (E_value = 5.4E_71);-57% similar to PDB:2AKI Normal mode-based flexible fitted coordinates of a translocating SecYEG protein-conducting channel into the cryo-EM map of a SecYEG-nascent chain-70S ribosome complex from E. coli (E_value = 5.4E_71);","Residues 73 to 418 (E_value = 7.3e-171) place ANA_0047 in the SecY family which is described as eubacterial secY protein.","","translocase, SecY subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0048","54034","54609","576","4.64","-11.06","20079","ATGGTTCTTCTCGGTCCCCCCGGAGCGGGCAAGGGCACCCAGGCCGCCCGGATCGCCGAGCGCCTGGGCATCCCGGCCATCTCCACCGGAGACATCTTCCGTGCCAACGTCGCCGGCGCCACCGAGCTCGGCACCCAGGCCAAGGCCTACATGGACAAGGGCGAGTACGTCCCCGACTCCATCACCAACGCCATGGTCGCTGACCGCATCGCCCAGGCCGACTGCGAGAACGGATTCCTCCTGGACGGCTACCCGCGCACCACCGCGCAGGTCGGCGAGCTCGACTCCATGCTCAAGGACTCGGGTCTGGCCCTCGACGTCGTCGTCGAGATCACCGCCGACGCCGAGGCCGTCGTCGCCCGCCTGCTCAAGCGGGCCGGCGAGCAGGGGCGGGCCGACGACACCGAGCCCGTCATCCGCCGCCGCCTCGAGGTCTACGGCGAGTCCACCGCGCCGCTGGCCGATCTCTACGCCGAGCGCGACCTGCTCGTCCAGGTCGACGGTATGGGCGAGATCGACGTCGTCACCGGCCGCATCATGGAGGCCCTCGCCTCCCGCGGCATCACCGGCTCCTGA","MVLLGPPGAGKGTQAARIAERLGIPAISTGDIFRANVAGATELGTQAKAYMDKGEYVPDSITNAMVADRIAQADCENGFLLDGYPRTTAQVGELDSMLKDSGLALDVVVEITADAEAVVARLLKRAGEQGRADDTEPVIRRRLEVYGESTAPLADLYAERDLLVQVDGMGEIDVVTGRIMEALASRGITGS$","Adenylate kinase","Cytoplasm","Adenylate kinase (ATP-AMP transphosphorylase)","adenylate kinase ","adenylate kinase","","Wieland B., Tomasselli A.G., Noda L.H., Frank R., Schulz G.E. The amino acid sequence of GTP:AMP phosphotransferase from beef-heart mitochondria. Extensive homology with cytosolic adenylate kinase. Eur. J. Biochem. 1984. 143(2):331-339. PMID: 6088234Tomasselli A.G., Noda L.H. Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies. Eur. J. Biochem. 1979. 93(2):263-270. PMID: 218813Cooper A.J., Friedberg E.C. A putative second adenylate kinase-encoding gene from the yeast Saccharomyces cerevisiae. Gene 1992. 114(1):145-148. PMID: 1587477Briozzo P., Golinelli-Pimpaneau B., Gilles A.M., Gaucher J.F., Burlacu-Miron S., Sakamoto H., Janin J., Barzu O. Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity. Structure 1998. 6(12):1517-1527. PMID: 9862805","","","

InterPro
IPR000850
Family

Adenylate kinase
PR00094	$\"[2-15]T$ $\"[30-44]T$ $\"[79-95]T$ $\"[131-146]T$ $\"[148-162]T$	ADENYLTKNASE
PTHR23359	$\"[1-181]T$	NUCLEOTIDE KINASE
PF00406	$\"[3-162]T$	ADK
PS00113	$\"[79-90]T$	ADENYLATE_KINASE

InterPro
IPR006259
Family

Adenylate kinase, subfamily
TIGR01351	$\"[1-184]T$	adk: adenylate kinases

InterPro
IPR011769
Domain

Adenylate/cytidine kinase, N-terminal
PD000657	$\"[1-44]T$	KAD_CLOAB_Q97EJ9;

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-188]T$	no description
PTHR23359:SF13	$\"[1-181]T$	ADENYLATE KINASE

","BeTs to 22 clades of COG0563COG name: Adenylate kinase and related kinasesFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0563 is ao--k-yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000850 (Adenylate kinase) with a combined E-value of 1.4e-35. IPB000850A 1-30 IPB000850B 78-91 IPB000850C 131-157 IPB000850A 33-62***** IPB003136 (Cytidylate kinase) with a combined E-value of 9.5e-09. IPB003136A 1-34","Residues 1-44 are 81% similar to a (KINASE TRANSFERASE ATP-BINDING ADENYLATE TRANSPHOSPHORYLASE ATP-AMP CYTIDYLATE MONOPHOSPHATE CYTIDINE CMP) protein domain (PD000657) which is seen in KAD_CLOAB.Residues 3-168 are 41% similar to a (KINASE TRANSFERASE F13E6.2 CG9541-PA ENSANGP00000010647) protein domain (PD179439) which is seen in Q9VLG2_DROME.Residues 52-116 are similar to a (KINASE TRANSFERASE ADENYLATE ATP-BINDING TRANSPHOSPHORYLASE ATP-AMP ISOENZYME SEQUENCING DIRECT PROBABLE) protein domain (PD581534) which is seen in KAD_MICLU.Residues 122-175 are 74% similar to a (KINASE TRANSFERASE ADENYLATE ATP-BINDING TRANSPHOSPHORYLASE ATP-AMP CHLOROPLAST SEQUENCING DIRECT ISOENZYME) protein domain (PD022012) which is seen in Q6AD15_BBBBB.","","-66% similar to PDB:1P4S Solution structure of Mycobacterium tuberculosis adenylate kinase (E_value = 3.0E_44);-66% similar to PDB:2CDN CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ADENYLATE KINASE COMPLEXED WITH TWO MOLECULES OF ADP AND MG (E_value = 3.0E_44);-57% similar to PDB:1P3J Adenylate Kinase from Bacillus subtilis (E_value = 5.0E_39);-57% similar to PDB:2EU8 Crystal structure of a thermostable mutant of Bacillus subtilis Adenylate Kinase (Q199R) (E_value = 5.0E_39);-58% similar to PDB:1S3G Crystal structure of adenylate kinase from Bacillus globisporus (E_value = 5.5E_38);","Residues 3 to 162 (E_value = 6.4e-75) place ANA_0048 in the ADK family which is described as Adenylate kinase.","","kinase (ATP-AMP transphosphorylase) (adk)","","1","","","","","","","","","","","","","Tue Jul 31 15:05:18 2007","","","Tue Jul 31 15:05:18 2007","Tue Jul 31 15:05:18 2007","Tue Jul 31 15:05:18 2007","","Tue Jul 31 15:05:18 2007","Tue Jul 31 15:05:18 2007","","","","","yes","","" "ANA_0049","54744","55625","882","5.18","-11.94","30952","GTGCTCTCACGCGAACAGATCCAGATCAAGACGCCGGAGCAGGTCCGCCTCATGCGCCGGGCCGGGCTCGTCGTCGCCGACATCCACGCCGCCCTGCGCAAGGCGGTGCGCGCCGGCATCACCACCGCCGAGCTCGACGCCGTCTCAGCCGGAGTCATCAAGGCCGCCGGTGCCCACTCCAACTTCCTGGGCTACTACGACTACCCGGCCACCGTGTGCATCTCCGTCAACGACGAGGTCGTCCACGGCATCCCCGGTGAACGGGTCCTGGCCGACGGTGACCTGGTCACCTTCGACTGCGGCGCCTACATCCTCGACGAGGACGGTACCCAGTGGCACGGCGATGCCGCCTTCACCACCGTCGTCGGCGGCAGCTACCTGAACGAGACGGACCGGCTCGTGGACACCACCACCCGGCAGGCCCTGTGGGAGGCCATCGCCGCCGTCGCCCGTGCCGCAGCGGGGGAGGGGCGCGGACGCCAGCTGTGCCTCAACGCGGTCGGCGACGCCGTCGAGACCGTTGTCGCGGACGTGGCCGAACGGGAGGGCCACGAGCTGGGGATCCTCCAGGAGTACGTCGGCCACGGCATCGGCACGAGCATGCACATGGCCCCCGACGTCCTCAACTACTCCGTCAAACGGCGCGGCCCCCGCCTGCGCCCCGGCATGGTGCTGGCCATCGAGCCCATGCTCACCGCCGGCAGCCCGGCCACGCGCGAGCTCGACGACGGCTGGACCGTCGTCACCCGGGACGGCTCCCACGCCGCCCAGTGGGAGCACACCGTGGCCATCGTCCCCGGAGGCGTGTGGGTCCTCACCGCGCCCGACGGCGGAGCCGAGGGCCTGGCCCCCTACGGCATCGAGCCCAAGGCGCTGGGCTGA","VLSREQIQIKTPEQVRLMRRAGLVVADIHAALRKAVRAGITTAELDAVSAGVIKAAGAHSNFLGYYDYPATVCISVNDEVVHGIPGERVLADGDLVTFDCGAYILDEDGTQWHGDAAFTTVVGGSYLNETDRLVDTTTRQALWEAIAAVARAAAGEGRGRQLCLNAVGDAVETVVADVAEREGHELGILQEYVGHGIGTSMHMAPDVLNYSVKRRGPRLRPGMVLAIEPMLTAGSPATRELDDGWTVVTRDGSHAAQWEHTVAIVPGGVWVLTAPDGGAEGLAPYGIEPKALG$","Methionine aminopeptidase, type I","Cytoplasm, Extracellular","methionine aminopeptidase, type I","methionine aminopeptidase ","methionine aminopeptidase, type I","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., Bradshaw R.A. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(17):7714-7718. PMID: 7644482Keeling P.J., Doolittle W.F. Methionine aminopeptidase-1: the MAP of the mitochondrion?. Trends Biochem. Sci. 1996. 21(8):285-286. PMID: 8772380Roderick S.L., Matthews B.W. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 1993. 32(15):3907-3912. PMID: 8471602","","","

InterPro
IPR000994
Domain

Peptidase M24, catalytic core
G3DSA:3.90.230.10	$\"[6-273]T$	no description
PTHR10804	$\"[59-265]T$	PROTEASE FAMILY M24 (METHIONYL AMINOPEPTIDASE, AMINOPEPTIDASE P)
PF00557	$\"[16-274]T$	Peptidase_M24

InterPro
IPR001714
Family

Peptidase M24, methionine aminopeptidase
PR00599	$\"[72-85]T$ $\"[217-229]T$	MAPEPTIDASE

InterPro
IPR002467
Family

Peptidase M24A, methionine aminopeptidase, subfamily 1
PTHR10804:SF13	$\"[59-265]T$	METHIONINE AMINOPEPTIDASE 1
TIGR00500	$\"[7-275]T$	met_pdase_I: methionine aminopeptidase, typ
PS00680	$\"[192-210]T$	MAP_1

","BeTs to 21 clades of COG0024COG name: Methionine aminopeptidaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0024 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB002467 (Methionine aminopeptidase, subfamily 1) with a combined E-value of 2.8e-67. IPB002467A 7-48 IPB002467B 64-85 IPB002467D 185-210 IPB002467E 243-273***** IPB001714 (Methionine aminopeptidase-1 signature) with a combined E-value of 2e-16. IPB001714A 72-85 IPB001714C 186-198 IPB001714D 217-229***** IPB007865 (Aminopeptidase P, N-terminal) with a combined E-value of 8.6e-06. IPB007865A 3-33 IPB007865E 219-233","Residues 58-126 are 70% similar to a (AMINOPEPTIDASE HYDROLASE COBALT METHIONINE PROTEASE DIPEPTIDASE XAA-PRO PEPTIDASE P PROLINE) protein domain (PD556587) which is seen in O54208_STRCO.Residues 205-273 are similar to a (AMINOPEPTIDASE HYDROLASE COBALT METHIONINE PROTEASE MAP M PEPTIDASE AMINOPEPTIDASE I) protein domain (PD551357) which is seen in Q6AD16_BBBBB.","","-50% similar to PDB:1C21 E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE COMPLEX (E_value = 6.4E_35);-50% similar to PDB:1C22 E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX (E_value = 6.4E_35);-50% similar to PDB:1C23 E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE PHOSPHONATE COMPLEX (E_value = 6.4E_35);-50% similar to PDB:1C24 E. COLI METHIONINE AMINOPEPTIDASE: METHIONINE PHOSPHINATE COMPLEX (E_value = 6.4E_35);-50% similar to PDB:1C27 E. COLI METHIONINE AMINOPEPTIDASE:NORLEUCINE PHOSPHONATE COMPLEX (E_value = 6.4E_35);","Residues 16 to 274 (E_value = 3.1e-40) place ANA_0049 in the Peptidase_M24 family which is described as metallopeptidase family M24.","","aminopeptidase, type I (map)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0050","55897","56118","222","9.18","2.64","8320","ATGGCTAAGAAGGACGGAGTCATCGAGGTCGAGGGATCGGTCGTCGAGGCCCTTCCGAACGCGATGTTCCGGGTGGAGCTGAGCAACGGGCACGTCGTGCTCGCGCACATCTCCGGAAAGATGCGGCAGCACTACATCCGCATCCTCCCCGAGGACCGGGTGGTCGTGGAGCTGAGCCCCTACGACCTGTCCCGCGGCCGAATCGTCTACCGGTACAAGTGA","MAKKDGVIEVEGSVVEALPNAMFRVELSNGHVVLAHISGKMRQHYIRILPEDRVVVELSPYDLSRGRIVYRYK$","Translation initiation factor IF-1","Cytoplasm","translation initiation factor IF-1","translation initiation factor IF-1","translation initiation factor IF-1","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Bycroft M., Hubbard T.J., Proctor M., Freund S.M., Murzin A.G. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 1997. 88(2):235-242. PMID: 9008164","","","

InterPro
IPR003029
Domain

RNA binding S1
SM00316	$\"[5-73]T$	S1

InterPro
IPR004368
Family

Translation initiation factor IF-1
TIGR00008	$\"[4-72]T$	infA: translation initiation factor IF-1

InterPro
IPR006196
Family

S1, IF1 type
PF01176	$\"[6-71]T$	eIF-1a
PS50832	$\"[1-73]T$	S1_IF1_TYPE

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[2-72]T$	no description

","BeTs to 19 clades of COG0361COG name: Translation initiation factor IF-1Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0361 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 4-72 are similar to a (INITIATION FACTOR TRANSLATION BIOSYNTHESIS IF-1 CHLOROPLAST IF-1 IF1 RNA RIBOSOMAL) protein domain (PD003406) which is seen in Q6AD17_BBBBB.","","-87% similar to PDB:1AH9 THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES (E_value = 6.0E_23);-80% similar to PDB:1HR0 CRYSTAL STRUCTURE OF INITIATION FACTOR IF1 BOUND TO THE 30S RIBOSOMAL SUBUNIT (E_value = 1.5E_21);-80% similar to PDB:1ZO1 IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex (E_value = 1.5E_21);","Residues 3 to 73 (E_value = 2.3e-09) place ANA_0050 in the S1 family which is described as S1 RNA binding domain.Residues 6 to 71 (E_value = 2.6e-35) place ANA_0050 in the eIF-1a family which is described as Translation initiation factor 1A / IF-1.","","initiation factor IF-1 (infA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0051","56152","56265","114","10.62","9.30","4329","ATGAAGGTCAAGCCGAGCGTCAAGAAGATCTGTGACAGCTGCAAGGTGATTCGTCGCCACGGCCGCGTCATGGTCATCTGCGAGAACCCGCGGCACAAGCAGCGTCAGGGCTGA","MKVKPSVKKICDSCKVIRRHGRVMVICENPRHKQRQG$","Ribosomal protein L36","Extracellular, Cytoplasm","ribosomal protein L36","50S ribosomal protein L36","ribosomal protein L36","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000473
Family

Ribosomal protein L36
PD002101	$\"[1-36]T$	RL36_STRCO_O86772;
PTHR18804	$\"[1-37]T$	FAMILY NOT NAMED
PF00444	$\"[1-37]T$	Ribosomal_L36
TIGR01022	$\"[1-37]T$	rpmJ_bact: ribosomal protein L36
PS00828	$\"[11-36]T$	RIBOSOMAL_L36

","BeTs to 18 clades of COG0257COG name: Ribosomal protein L36Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0257 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB000473 (Ribosomal protein L36) with a combined E-value of 9.6e-21. IPB000473 1-27","Residues 1-36 are similar to a (RIBOSOMAL L36 50S CHLOROPLAST RIBONUCLEOPROTEIN SEQUENCING B DIRECT MITOCHONDRION MITOCHONDRIAL) protein domain (PD002101) which is seen in RL36_STRCO.","","-92% similar to PDB:1DFE NMR STRUCTURE OF RIBOSOMAL PROTEIN L36 FROM THERMUS THERMOPHILUS (E_value = 8.8E_14);-92% similar to PDB:1DGZ RIBOSMAL PROTEIN L36 FROM THERMUS THERMOPHILUS: NMR STRUCTURE ENSEMBLE (E_value = 8.8E_14);-92% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 8.8E_14);-92% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 8.8E_14);-92% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 8.8E_14);","Residues 1 to 37 (E_value = 1.5e-18) place ANA_0051 in the Ribosomal_L36 family which is described as Ribosomal protein L36.","","protein L36 (rpmJ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0052","56431","56805","375","10.51","14.86","14161","GTGGCACGCATTTCCGGTGTCGACCTGCCTCGCGAGAAGCGAGTCGAGATCGCACTCACCTACATCTTCGGGATCGGACGCACCCGCGCGGACGAGACCCTGAAGGCGACGGGCGTCAACCCCGACACCCGCGTCAAGGACCTCACCGAGGAGGAGCTGGTCAAGCTCCGCACCCACATCGACGGCAACTACCAGGTTGAGGGTGACCTGCGTCGTGAGGTTCAGGCGGACATCCGCCGCAAGATCGAGATCGGCTGCTACCAGGGCCTGCGCCACCGCCGCCACCTGCCGGTGCACGGTCAGCGCACCAAGACCAACGCGCGTACCCGCAAGGGCCCCAAGCGCACCGTGGCCGGTAAGAAGAAGGCCAAGTAA","VARISGVDLPREKRVEIALTYIFGIGRTRADETLKATGVNPDTRVKDLTEEELVKLRTHIDGNYQVEGDLRREVQADIRRKIEIGCYQGLRHRRHLPVHGQRTKTNARTRKGPKRTVAGKKKAK$","Ribosomal protein S13","Cytoplasm","ribosomal protein S13p/S18e","30S ribosomal protein S13","ribosomal protein S13","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Chan Y.L., Paz V., Wool I.G. The primary structure of rat ribosomal protein S18. Biochem. Biophys. Res. Commun. 1991. 178(3):1212-1218. PMID: 1872840","","","

InterPro
IPR001892
Family

Ribosomal protein S13
PD001363	$\"[44-122]T$	Q73S46_MYCPA_Q73S46;
PTHR10871:SF1	$\"[1-122]T$	30S RIBOSOMAL PROTEIN S13
PF00416	$\"[3-109]T$	Ribosomal_S13
PS50159	$\"[4-112]T$	RIBOSOMAL_S13_2
PS00646	$\"[88-101]?$	RIBOSOMAL_S13_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.50	$\"[1-72]T$	no description
G3DSA:4.10.910.10	$\"[73-124]T$	no description
PTHR10871	$\"[1-122]T$	30S/40S RIBOSOMAL PROTEIN
signalp	$\"[1-30]?$	signal-peptide

","BeTs to 26 clades of COG0099COG name: Ribosomal protein S13Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0099 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001892 (Ribosomal protein S13) with a combined E-value of 1.1e-51. IPB001892A 3-50 IPB001892B 77-109","Residues 1-42 are 92% similar to a (RIBOSOMAL S13 RNA-BINDING RRNA-BINDING 30S TRNA-BINDING RIBONUCLEOPROTEIN MITOCHONDRION S18 40S) protein domain (PD899588) which is seen in RS13_BIFLO.Residues 44-122 are similar to a (RIBOSOMAL S13 RNA-BINDING RRNA-BINDING 30S RIBONUCLEOPROTEIN TRNA-BINDING MITOCHONDRION S18 S13P) protein domain (PD001363) which is seen in Q73S46_MYCPA.","","-88% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 1.5E_45);-88% similar to PDB:1GIX Crystal structure of the ribosome at 5.5 A resolution. This file, 1GIX, contains the 30S ribosome subunit, three tRNA, and mRNA molecules. 50S ribosome subunit is in the file 1GIY (E_value = 1.5E_45);-88% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 1.5E_45);-88% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 1.5E_45);-88% similar to PDB:1HNZ STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH HYGROMYCIN B (E_value = 1.5E_45);","Residues 3 to 109 (E_value = 4.1e-53) place ANA_0052 in the Ribosomal_S13 family which is described as Ribosomal protein S13/S18.","","protein S13p-S18e (rpsM)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0053","56868","57269","402","11.17","17.58","14327","ATGCCTCCCAAGACCCGCGCCGCCGCGCGCAAGACGCGCCGCAAGGACCGCAAGAACGTTACCCACGGTCACGCCTACATCAAGTCCACCTTCAACAACACCATCGTCTCGCTGACGGACCCGCAGGGCGCCGTCATCGCCTGGTGCTCCTCCGGCCAGGTCGGCTTCAAGGGCTCGCGCAAGTCGACCCCCTACGCCGCCCAGCTCGCCGCCGAGGCCGCCGCCCGGCGCGCCCAGGAGCACGGCATGAAGAAGGTTGACGTCTTCGTCAAGGGTCCCGGCTCCGGCCGCGAGACCGCGATCCGCTCCCTCCAGGCCGCTGGCCTCGAGGTCGGCTCGATCACCGACGTCACCCCCCAGGCCTTCAACGGCTGCCGCCCGCCCAAGCGCCGTCGCGTCTGA","MPPKTRAAARKTRRKDRKNVTHGHAYIKSTFNNTIVSLTDPQGAVIAWCSSGQVGFKGSRKSTPYAAQLAAEAAARRAQEHGMKKVDVFVKGPGSGRETAIRSLQAAGLEVGSITDVTPQAFNGCRPPKRRRV$","Ribosomal protein S11","Extracellular","ribosomal protein S11","ribosomal protein S11","ribosomal protein S11","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Kimura M., Kimura J., Hatakeyama T. Amino acid sequences of ribosomal proteins S11 from Bacillus stearothermophilus and S19 from Halobacterium marismortui. Comparison of the ribosomal protein S11 family. FEBS Lett. 1988. 240(1):15-20. PMID: 3191988","","","

InterPro
IPR001971
Family

Ribosomal protein S11
PD001010	$\"[26-97]T$	Q6NJ65_CORDI_Q6NJ65;
G3DSA:3.30.420.80	$\"[7-132]T$	no description
PTHR11759	$\"[12-133]T$	40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
PF00411	$\"[23-132]T$	Ribosomal_S11
PS00054	$\"[101-123]T$	RIBOSOMAL_S11

noIPR
unintegrated

unintegrated
PTHR11759:SF3	$\"[12-133]T$	30S RIBOSOMAL PROTEIN S11

","BeTs to 26 clades of COG0100COG name: Ribosomal protein S11Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0100 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001971 (Ribosomal protein S11) with a combined E-value of 1e-62. IPB001971A 25-71 IPB001971B 91-132","Residues 26-132 are 50% similar to a (RIBOSOMAL S11 MITOCHONDRION MITOCHONDRIAL RIBONUCLEOPROTEIN) protein domain (PD888067) which is seen in Q6E793_SAPFE.Residues 26-97 are similar to a (RIBOSOMAL S11 30S RNA-BINDING RRNA-BINDING RIBONUCLEOPROTEIN CHLOROPLAST S14 40S S11P) protein domain (PD001010) which is seen in Q6NJ65_CORDI.Residues 100-132 are 93% similar to a (RIBOSOMAL S11 30S RRNA-BINDING RNA-BINDING RIBONUCLEOPROTEIN CHLOROPLAST S14 40S S11P) protein domain (PD889150) which is seen in Q6AD20_BBBBB.","","-68% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 3.9E_29);-68% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 3.9E_29);-68% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.9E_29);-68% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.9E_29);-68% similar to PDB:2AVY Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 30S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 3.9E_29);","Residues 23 to 132 (E_value = 1.7e-65) place ANA_0053 in the Ribosomal_S11 family which is described as Ribosomal protein S11.","","protein S11 (rpsK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0054","57428","58429","1002","4.73","-20.25","36334","GTGCTCATTGCACAGCGACCCACGCTCACCGAGGAGGTCGTGGTCGAGGACCGCCGCTCGCGCTTCGTGCTCGAGCCCCTCGAGCCCGGCTTCGGCTACACGCTCGGCAACTCCCTGCGCCGCACGCTGCTGTCCTCCATCCCGGGGGCGGCCGTGACCAGCGTCCGCATCGACGGGGTGCCCCACGAGTTCCGCACGATCCCCGGGGTCAAGGAGGATGTCGCCCAGATCATCCTCAACATCAAGGAGATCGTCCTGTCCTCGGAGAACGACGAGCCGGTCGTCATGTACCTGCGCAAGTCCGGTCCGAGCGAGGTCACCGCCGGTGACATCACCCCGCCGGCCGGCGTCGAGATCCACAACCCCGATCTGGTCATCGCCACTCTCAACGAGAAGGGCAAGTTGGAGATCGAGCTGACGGTCGAGCGCGGCCGCGGCTACGTCTCCGCCAACCAGAACAAGGACCCCAACGCGGAGATCTCCCGCATCCCGGTGGACTCGATCTACTCGCCGGTCAAGAAGGTCTCCTACTCCGTCGAGGCCACCCGTGTGGAGCAGCGCACCGACTTCGACCGTCTCATCGTCGACGTCGAGACTAAGTCCTCCATCACCCCGCGTGACGCTCTGGCCTCCGCCGGTAAGACGCTCGTGGAGCTCTTCGGCCTGGCCCGTGAGCTCAACGTCGAGGCCGAGGGCATCGAGGTCGGTCCCTCGCCGATCGACGAGGCCTTCCAGCAGGACCTGGCCCTCATGATCGACGAGCTCGACCTGCAGGCCCGGTCCTCCAACGCCCTCAAGCGCGAGGGCATCCACACCGTCGGTGAGCTCGTCTCGCGCAGCGAGGCCGACCTGCTCGACATCCGTAACTTCGGCGCCAAGTCCATCTCCGAGATCAAGGACAAGCTGGCCGAGCTGGGGCTCTCCCTCAAGGGCTCCCCGGTCGACTATGTCTCGGACGACGACTACGCCAACCCCACGTTCAGCGACGAGACCCAGGCCTGA","VLIAQRPTLTEEVVVEDRRSRFVLEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSVRIDGVPHEFRTIPGVKEDVAQIILNIKEIVLSSENDEPVVMYLRKSGPSEVTAGDITPPAGVEIHNPDLVIATLNEKGKLEIELTVERGRGYVSANQNKDPNAEISRIPVDSIYSPVKKVSYSVEATRVEQRTDFDRLIVDVETKSSITPRDALASAGKTLVELFGLARELNVEAEGIEVGPSPIDEAFQQDLALMIDELDLQARSSNALKREGIHTVGELVSRSEADLLDIRNFGAKSISEIKDKLAELGLSLKGSPVDYVSDDDYANPTFSDETQA$","DNA-directed RNA polymerase, alpha subunit","Cytoplasm","DNA-directed RNA polymerase, alpha subunit","DNA-directed RNA polymerase; alpha subunit ","DNA-directed RNA polymerase, alpha subunit","","Zhang G., Darst S.A. Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain. Science 1998. 281(5374):262-266. PMID: 9657722Ebright R.H., Busby S. The Escherichia coli RNA polymerase alpha subunit: structure and function. Curr. Opin. Genet. Dev. 1995. 5(2):197-203. PMID: 7613089","","","

InterPro
IPR011260
Domain

RNA polymerase, alpha subunit, C-terminal
PD001179	$\"[252-316]T$	Q73S43_MYCPA_Q73S43;
PF03118	$\"[237-304]T$	RNA_pol_A_CTD

InterPro
IPR011261
Domain

RNA polymerase, dimerisation
PF01193	$\"[17-225]T$	RNA_pol_L

InterPro
IPR011262
Domain

RNA polymerase, insert
G3DSA:2.170.120.12	$\"[49-169]T$	no description
PF01000	$\"[55-170]T$	RNA_pol_A_bac

InterPro
IPR011263
Domain

RNA polymerase, RpoA/D/Rpb3-type
SM00662	$\"[19-226]T$	RPOLD

InterPro
IPR011773
Family

DNA-directed RNA polymerase, alpha subunit
TIGR02027	$\"[19-312]T$	rpoA: DNA-directed RNA polymerase, alpha su

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.20	$\"[241-324]T$	no description

","BeTs to 21 clades of COG0202COG name: DNA-directed RNA polymerase alpha subunit/40 kD subunitFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0202 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB011263 (RNA polymerase, RpoA/D/Rpb3-type) with a combined E-value of 4.1e-90. IPB011263A 19-53 IPB011263B 62-82 IPB011263C 102-111 IPB011263D 165-179 IPB011263E 191-223 IPB011263F 252-294***** IPB001514 (DNA-directed RNA polymerase, 30-40 kDa subunit) with a combined E-value of 1.3e-49. IPB001514A 26-74 IPB001514B 123-164 IPB001514C 191-219","Residues 35-150 are similar to a (ALPHA RNA POLYMERASE SUBUNIT DNA-DIRECTED CHAIN TRANSFERASE TRANSCRIPTION TRANSCRIPTASE RNAP) protein domain (PD002883) which is seen in RPOA_STRGT.Residues 163-239 are similar to a (ALPHA RNA POLYMERASE SUBUNIT DNA-DIRECTED CHAIN TRANSFERASE TRANSCRIPTION TRANSCRIPTASE RNAP) protein domain (PD579875) which is seen in RPOA_CORGL.Residues 252-316 are 83% similar to a (ALPHA RNA POLYMERASE SUBUNIT DNA-DIRECTED CHAIN TRANSFERASE TRANSCRIPTION TRANSCRIPTASE RNAP) protein domain (PD001179) which is seen in Q73S43_MYCPA.","","-64% similar to PDB:1L9U THERMUS AQUATICUS RNA POLYMERASE HOLOENZYME AT 4 A RESOLUTION (E_value = 5.4E_65);-64% similar to PDB:1L9Z Thermus aquaticus RNA Polymerase Holoenzyme/Fork-Junction Promoter DNA Complex at 6.5 A Resolution (E_value = 5.4E_65);-64% similar to PDB:1YNJ Taq RNA polymerase-Sorangicin complex (E_value = 5.4E_65);-64% similar to PDB:1YNN Taq RNA polymerase-rifampicin complex (E_value = 5.4E_65);-64% similar to PDB:2GHO Recombinant Thermus aquaticus RNA polymerase for Structural Studies (E_value = 5.4E_65);","Residues 17 to 225 (E_value = 2e-24) place ANA_0054 in the RNA_pol_L family which is described as RNA polymerase Rpb3/Rpb11 dimerisation domain.Residues 55 to 170 (E_value = 8.7e-59) place ANA_0054 in the RNA_pol_A_bac family which is described as RNA polymerase Rpb3/RpoA insert domain.Residues 237 to 304 (E_value = 1.3e-26) place ANA_0054 in the RNA_pol_A_CTD family which is described as Bacterial RNA polymerase, alpha chain C terminal domain.","","RNA polymerase, alpha subunit (rpoA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0055","58460","59185","726","9.00","5.42","26357","ATGCCTCGCCCCACTAAGGGTCCCCGTCTGGGCGGCAGCGCCCAGCACGAGCGTCACCTGCTCGCCAACCTGGCCACGCAGCTCATCGTTCACGAGTCGATCAAGACCACGGAGGCTCGCGCTCGTCGCCTGCGTCCCTACGTCGAGAAGCTCATCACCAAGGGCAAGCGCGGCGACCTGCACGCCCGCCGCACCGTGCTGAAGAAGGTGACGGACAAGTACGCCGTCTACCGCCTCTTCGAGGAGCTCGCCCCCAAGTTCGAGGGCCGCGAGGGCGGTTACACCCGCATCATCAAGACGACCCCCCGTAAGGGCGACAACGCCCCCATGGCGGTCATCTCCCTGGTGCTGGAGCCGGTTGCCCGCAAGGAGATCGTGGAGGACGCGGTCGCCACCGCCAAGAAGGCCGCCCAGAAGGCCGTCGCCGACGAGGACAAGGCCGAGAAGAAGACCACGGCCGAGAAGGCTGAGGAGAAGGCCGACAAGGCTGAGAAGGCTGACAAGGCCGAGTACGCCGGCGCGGTCCGTCTCGAGGAGGGCGCCACTGACGCTCCCGACGACGACCACCTGGTCAAGGGCAACGAGGACTCCATGAAGTACCACGTTCCCGGCTCGCGCTGGTACGACGCCACGGTCGCCGAGGTCTGGTTCGCCAGCGCCGAGGATGCCGAGGCCGCGGGCTTCGCCCCCGCCGGCGGCGCCGCCGCCCAGAAGGTCGAGAAGTGA","MPRPTKGPRLGGSAQHERHLLANLATQLIVHESIKTTEARARRLRPYVEKLITKGKRGDLHARRTVLKKVTDKYAVYRLFEELAPKFEGREGGYTRIIKTTPRKGDNAPMAVISLVLEPVARKEIVEDAVATAKKAAQKAVADEDKAEKKTTAEKAEEKADKAEKADKAEYAGAVRLEEGATDAPDDDHLVKGNEDSMKYHVPGSRWYDATVAEVWFASAEDAEAAGFAPAGGAAAQKVEK$","Ribosomal protein L17","Cytoplasm, Periplasm","50S ribosomal protein","50S ribosomal protein L17","ribosomal protein L17","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000456
Family

Ribosomal protein L17
PD004277	$\"[23-111]T$	Q6NJ62_CORDI_Q6NJ62;
PTHR14413	$\"[1-160]T$	RIBOSOMAL PROTEIN L17
PF01196	$\"[20-116]T$	Ribosomal_L17
TIGR00059	$\"[6-117]T$	L17: ribosomal protein L17
PS01167	$\"[34-56]T$	RIBOSOMAL_L17

noIPR
unintegrated

unintegrated
G3DSA:3.90.1030.10	$\"[1-116]T$	no description

","BeTs to 19 clades of COG0203COG name: Ribosomal protein L17Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0203 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000456 (Ribosomal protein L17) with a combined E-value of 1.9e-58. IPB000456A 9-62 IPB000456B 63-113","Residues 23-111 are similar to a (RIBOSOMAL L17 RIBONUCLEOPROTEIN 50S SUBUNIT LSU L17P SEQUENCING L17 PROBABLE) protein domain (PD004277) which is seen in Q6NJ62_CORDI.Residues 183-217 are 80% similar to a (RIBOSOMAL PROTEIN L4 REGULATORY 50S) protein domain (PD901045) which is seen in Q6A9U2_PROAC.","","-64% similar to PDB:1GD8 THE CRYSTAL STRUCTURE OF BACTERIA-SPECIFIC L17 RIBOSOMAL PROTEIN. (E_value = 2.3E_21);-64% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 2.3E_21);-64% similar to PDB:1YL3 Crystal structure of 70S ribosome with thrS operator and tRNAs. Large subunit. The coordinates for the small subunit are in the pdb entry 1YL4. (E_value = 2.3E_21);-64% similar to PDB:2B66 50S ribosomal subunit from a crystal structure of release factor RF1, tRNAs and mRNA bound to the ribosome. This file contains the 50S subunit from a crystal structure of release factor RF1, tRNAs and mRNA bound to the ribosome and is described in remark 400 (E_value = 2.3E_21);-64% similar to PDB:2B9N 50S ribosomal subunit from a crystal structure of release factor RF2, tRNAs and mRNA bound to the ribosome. This file contains the 50S subunit from a crystal structure of release factor RF1, tRNAs and mRNA bound to the ribosome and is described in remark 400. (E_value = 2.3E_21);","Residues 20 to 116 (E_value = 5.9e-46) place ANA_0055 in the Ribosomal_L17 family which is described as Ribosomal protein L17.","","ribosomal protein (rplQ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0056","62399","59295","3105","8.23","12.29","115482","GTGACAGAGTTCCCCTCATCCATACCGACAACGTCCTCAGGTCAGTCGTGGATCGATGGGATACCCCCATTGATCAAGTGGATCTACAATTGGATCTTTAGCATCTTGGATAACCTTGGAGCCCAACACCCTTCCTTGACATGGGCACCTAGCCTAATATTCGCAATCGTGACAATCATCATCGTCTTCTGGGAAAAACTTTCGAGAAAACTGAAACAAGTGCATCGAAAACTGGACACATACAGGCGGCGCCAAAAACTTCAGCCAACCATAGTTCCATTCTCAATGAAAACCAAGACAGAACCGCTGACCTTTAACCCCATCCAACCACGGCACGAAAATACAACGAAACCCCTGAGCGACGCCCGAAAGCTTAAGGCAATTGCCACACCAACCCCATTCCTTGACCGCGCAAAGGTACTCAGCCACTTAGAAAAATGGGCTCGGGACAAGAAACCATTTGCAATCTACGTTATAGGTGGGGATGGAGGCTCCGGGAAGACCCGTCTCGGCGTGGAGCTCTGTAGGCGCCTCAACACCCCCAGCCTTCTCCGTCAAGGCAATAAGGTATGGAAAACAGGCTTCCTCCAAGATAACAGTGCTCCCGCAAACACAAATCCCATCGACAACATAAGCTCCCTTTTGCTTGTAGTAGACTATGCCGAATCTCGACCGAACATGGTAAAGAACGTCATCAACGCCGCCTATCGCGCAGCTGAGGATCCACAGAGACGAAGAGTGCGGATCGTTTTCTTGGTTCGACGCCCATCACCGCTCTCCGCTTTCCATCGAAGTTCCAATATGTGGATTGACGCTCTTCGCCCACAAGACTCCAACGACAACGAGGGCCTGAACCGCCTTCTTGACGAGGCCTCAACAACCACACTCAACGAGGAAGAGTTATCGGACACAGATCGAAGAGAGCTGTACATTCGGGCATACAAGTCATTCGCCAACACCCCTGACCCTACACCATCACCCAACTTTACTGAGCGACTCAGCGACCCTATGTATTCGCAGCCCCTGCTCGTCATAGTCGACGCTTTCCTGAACGCACAAACCCACCCGAGCTCACAAATTAGCTGCAGTCCGAGCGAGTTATTTGAGGAAGTTATTTGTCACGAGGAAAAATATTGGAAAAAACACTGGCCACCAAGTCTCACCATCAGTACCAGCCAAGACCAACCGAGTGACGGCGCCGCAAAACCCAGCACCCCTCAGACCAGAATAACGAAATCCTTCGATCCAGAGTTGGCGCGCCAGGCAGTAGCCGCCGCCACACTCACCAACATTCAGGACGAAGCGGACGCTATCAGCCTCCTCAATCTCCTTCCAGCCAATCCCGGCACGAACACCAAGACCCTAGCCAAGTGGCTGCGAGAATGCTACCCACCACACCTGAACGATAACGGACACTCGACCTTGTGGTGTGATCATCTTGAGCCGGACCGCATCGGAGAGCACCTCATTGCATCCGAAACCAACCACCTAGTACCTCTCCTCCAAGAACTTTTATCCCCAAGTAGAGTGGGAACGTCGTCCCTACGAACCTGGACGGTCCTTGAACGCGCATCGACAGATCCTCACCTCAATGAGCGCGTAGGACAAATTCTTAACGACGTGCTAGTGGAAGTCACTCGGGAACTTCACACACAAACCGTCAGCTCCCAGAGCCCAGACCTCGCTACAGCCTTCGCCAAGCTTTTTAGCGCAGTGTGTTGCCACATCGACCCTAACAAGGCTCACGAGGCAGAGAAGACCCTGTCCGAGGGCGGATACTTCACAGCATTCTTGAGATACGAACTTGCTCAACGTGCAGCCAATATCGACCGTCCGGCAGATGACGCTCCTGAAGCCGACCGAGCGACCTATGCTTCCCGGAAATCGTCACTTAGTAGCCGCTTAGCCGATACCGGAAGACACGAAGAAGCCCTCAATGCCGCGCGAGAAGCTACCGACCTCTACCGGACCCTGGTCGAGCACAACCCAGCCACCTACACCCCTGGCCTCGCCATGTCCCTCGACAACCTCGCCAACCAGCAGGCCAGCAACGGGCAACTGCACGACGCCCTCAAGAACGCCCAAGAAGCCACCAACCTCTACCGGACCCTGGTCGAGCACAACCCAGCCACCTACACCCCTGGCCTCGCCATGTCCCTCGACAACCTCGCCAACCAGCAGGCCAGCAACGGGCAACTGCACGACGCCCTCAAGAACGCCCAAGAAGCCACCAACCTCTACCGGACCCTGGTCGAGCACAACCCAGCCACCTACACCCCTGGCCTCGCCATGTCCCTCGACAACCTCGCCAGATGTCTGAGTGAAAACGCTAGGCTGCTCGACGGCCTCAAGAACGCCCAAGAAGCCACCAACCTCTACCGGACCCTGGCCGAGCACAACCCAGCCACCTACACCCCTGGCCTCGCCGGCTCCCTCAACGACCTCGCCAACCACTTGGCCGACAACAGGCGGCATAGCGAGGCCCTCAAGACCGCCCAAGAAGCAGTCACCATTCGCAGAAAATTAGCCGAGCACAACCCAGCCGCCTACACCCCTGGCCTCGCCATGTCCCTCAGCAACCTCGCCAACCGCTTCGCCGACAACAGGCGGCATCGTGAGGCCCTCAAGACCGCCCAAGAAGCCACCAACCTCTACCGGACCCTGGCCGAGCACAACCCAGCCACCTACACCCCCAACCTCGCCATATCCCTCAGCAACCTCGCCAACCGCTTCGCCAACAACAGGCGGCATCGTGAGGCCCTCAAGACCGCCCAAGAAGCCACCAACCTCTACCGGACCCTGGCCGAGCACAACCCAGCAGCCCACACCCCCAACCTCGCCATATCCCTAAACAACCTCGCCAACCGCTTCGCCAACAACAGGCGGCATCGCAAGGCCCTCAAGACCGCCCAAGAAGCCACCAACCTCTACCGGACCCTGGCCGAGCACAACCCAGCAGCCCACACCCCCAATCTCACCAGCTCCCTCAAAACCTACGCAAACATCCTGGAATGGAGTGGCAGCACTAAGGAGGCCGCCCGCATCCGGCAGGAGCGAGATGAGGTCCTCAAGCGGATGAAGGAGTTAGAGGAAGGCGATGCCTGA","VTEFPSSIPTTSSGQSWIDGIPPLIKWIYNWIFSILDNLGAQHPSLTWAPSLIFAIVTIIIVFWEKLSRKLKQVHRKLDTYRRRQKLQPTIVPFSMKTKTEPLTFNPIQPRHENTTKPLSDARKLKAIATPTPFLDRAKVLSHLEKWARDKKPFAIYVIGGDGGSGKTRLGVELCRRLNTPSLLRQGNKVWKTGFLQDNSAPANTNPIDNISSLLLVVDYAESRPNMVKNVINAAYRAAEDPQRRRVRIVFLVRRPSPLSAFHRSSNMWIDALRPQDSNDNEGLNRLLDEASTTTLNEEELSDTDRRELYIRAYKSFANTPDPTPSPNFTERLSDPMYSQPLLVIVDAFLNAQTHPSSQISCSPSELFEEVICHEEKYWKKHWPPSLTISTSQDQPSDGAAKPSTPQTRITKSFDPELARQAVAAATLTNIQDEADAISLLNLLPANPGTNTKTLAKWLRECYPPHLNDNGHSTLWCDHLEPDRIGEHLIASETNHLVPLLQELLSPSRVGTSSLRTWTVLERASTDPHLNERVGQILNDVLVEVTRELHTQTVSSQSPDLATAFAKLFSAVCCHIDPNKAHEAEKTLSEGGYFTAFLRYELAQRAANIDRPADDAPEADRATYASRKSSLSSRLADTGRHEEALNAAREATDLYRTLVEHNPATYTPGLAMSLDNLANQQASNGQLHDALKNAQEATNLYRTLVEHNPATYTPGLAMSLDNLANQQASNGQLHDALKNAQEATNLYRTLVEHNPATYTPGLAMSLDNLARCLSENARLLDGLKNAQEATNLYRTLAEHNPATYTPGLAGSLNDLANHLADNRRHSEALKTAQEAVTIRRKLAEHNPAAYTPGLAMSLSNLANRFADNRRHREALKTAQEATNLYRTLAEHNPATYTPNLAISLSNLANRFANNRRHREALKTAQEATNLYRTLAEHNPAAHTPNLAISLNNLANRFANNRRHRKALKTAQEATNLYRTLAEHNPAAHTPNLTSSLKTYANILEWSGSTKEAARIRQERDEVLKRMKELEEGDA$","TPR repeat-containing protein","Periplasm, Membrane, Extracellular","TPR Domain domain protein","TPR repeat","TPR repeat-containing protein","","Lamb J.R., Tugendreich S., Hieter P. Tetratrico peptide repeat interactions: to TPR or not to TPR?. Trends Biochem. Sci. 1995. 20(7):257-259. PMID: 7667876Das A.K., Cohen P.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 1998. 17(5):1192-1199. PMID: 9482716Goebl M., Yanagida M. The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Trends Biochem. Sci. 1991. 16(5):173-177. PMID: 1882418D'andrea L.D., Regan L. TPR proteins: the versatile helix. Trends Biochem. Sci. 2003. 28(12):655-662. PMID: 14659697","","","

InterPro
IPR001440
Repeat

Tetratricopeptide TPR_1
PF00515	$\"[809-842]T$ $\"[901-934]T$ $\"[947-980]T$	TPR_1

InterPro
IPR011990
Domain

Tetratricopeptide-like helical
G3DSA:1.25.40.10	$\"[633-801]T$ $\"[806-1018]T$	no description

InterPro
IPR013026
Domain

Tetratricopeptide region
SM00028	$\"[671-704]T$ $\"[717-750]T$ $\"[809-842]T$ $\"[855-888]T$ $\"[901-934]T$ $\"[947-980]T$	TPR

noIPR
unintegrated

unintegrated
tmhmm	$\"[46-64]?$	transmembrane_regions

","BeTs to 5 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","Residues 806-896 are 59% similar to a (REPEAT TPR DOMAIN TRANSFERASE TETRATRICOPEPTIDE MEMBRANE RECEPTOR SIGNAL CONTAINING RIKEN) protein domain (PD000069) which is seen in Q7MVD8_PORGI.","","No significant hits to the PDB database (E-value < E-10).","Residues 809 to 842 (E_value = 842) place ANA_0056 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 947 to 980 (E_value = 980) place ANA_0056 in the TPR_1 family which is described as Tetratricopeptide repeat.","","Domain domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0057","64698","62788","1911","7.10","0.85","68776","ATGTCTCCCCATCGCGGCAGCGCTCAGGCACCGTTTAGCGTGAGCACACCACCATTCCCCCACTCCCTGAGGCTTTCAGACGTGTTGCCCTCCCCCTGCGCCGCCCCCGAAGGGGCTGCTCGCGCCGGTCGGCTGCTGGAGCTCAGTGAGCGCCTGGCAGAGTCGGGCCGTCGGGGGGAGGCGCTGGATGCCGCACGGGAGGCCTGCCAGGTTCTCCGGGGACTGGCCCGGCTCAACCCGGACGTCTACCTGCCCGATCTGGCAGAGGGGCTGTCCGTCATGGCGGACCGTCTGCGCGAGGCCCGTCGCATGCGTGAGGGCGTTGCGGTCTCGCAGGAGATTGTCCGGCTCCGACGGCACCTGACCCGGTATGACTACGACGCCCACGCCTCCGGGCTGGCGCAGGCCCTGTGCCGCCTCGCCGTCGACCTGAGCGCTTCCGGCGATCTGCGTGACGCCCTAGCGAGTGCTCAGGAGTCCGTGGACCTCTACCGGAGCCTGCGCCGGGATGATCCCGCCAACGACGAGTCCGGGTTGGTTCAGGCTCTGGTCACACTCGCCTGCTGCCTGAGTGAGTCCCGTCGGCCGAGCGACGCCTTCGTCACCGCCCAGCAGGCCCTCACCGTCCGACGGCGTCTGGTCCGGGCTGATCCGGATGTACACACGCGCCGACTCGCGGCGGACCTGGCCCATCTGGCTCCCAGACTGCGCACGGTGGGCTATGTCGATGAGGCCCTCGAGCTGGCCCGGGAGGCCGTGGGTCTCTACCGCCGCCTCGACGAGGAGGAGATCGGTTCCTGCACCGGCGATCTTGCCGGAGCCCTGGAGGTGCTGGCCGCCTGCGGGGCCGCCGTCGGGCGTCGAACCACGGCCCTGGAGGCGGCCGAGGAAGCCGCTGCGCTCTACCGGGGACTGGCCCGCCGCACGCCGGCGCTCTACTCACCGAAGGCCACCCACGCCCTGGCGACACTGGCTCGGCGCCTGAGCGACGTGGGGCGGCATCGTGAGGCACTCGCCGCAGTCGAGGAGGCAGTCAGCCTCTCTCGCGCTCTGGCCCACAGCGCCCCCGACAACCACCTGCCCGACCTCGCCGATGCCCTCACGGTCCAGGCCGCCTGCCTGCGTGAGGCCGACAGGCTGGACCGAACACTGGCTTCAGCCCGGGAGGCGGTCAGCATTCGACGCACTCTGGAGCACAGCCGCCCCAGCACTGAGACCCCGGCCCTGGCTGAGTCCCTGTACGTCCTGGCCGTCTACCTGTACACGGCCGGGCAGCTGCAGGAGTCCTTCGCGATGGCCTGGGAGGCCATCGACATCTACCGGCAGCTGGTCCGTACCAACCCGGCTCCACATACCGCCGACCTCGCTCGGGCGCTCAACATCCTCACCTTGAACCTCAGCCGGGCCGGGCGTGCGCACGAGGCCCTGGCTGCGGTGCAGGAGGCGGTCACCTTCTACCGGAGCCTAACCCAGGTCGATCCGGTCGCCTACAAGCCGGACCTGGCGGCATGCCTGCACAACCTGGCCACGTGCCTGGGAGATGTCGGGGACCGCTCCGCCGCGCTGGCCGCGATCCGGGAGACGGCGGCTATCCGCCGGGAGCTGGCAGCGCGCGACCCGGCGACGCACGCCCCGGCGCTGGCCCCGTGCCTGCATCGGCTCGCCAAGCGCCTGGCCGAGGCGGGTCACCGAGGCGAGGCCCTGGAGACCGCACGGGAGGCGGTCGCCGCCTACCGGAGCCTGGTCCGCAGGCGCCCGGAGGACTTCGGCCGGGGGCTCGCCGGCGCGCTGCGAACCTATGCGTCAGTCCTCGAGTGGGTGGGCAGGGAGGCCGACGCCGCCCGCATCCGCCAGGTGAGCGAAGCCATGACGGAGGAAACGGCCTTGGAGGACTCCATCCGGGGATTCTGA","MSPHRGSAQAPFSVSTPPFPHSLRLSDVLPSPCAAPEGAARAGRLLELSERLAESGRRGEALDAAREACQVLRGLARLNPDVYLPDLAEGLSVMADRLREARRMREGVAVSQEIVRLRRHLTRYDYDAHASGLAQALCRLAVDLSASGDLRDALASAQESVDLYRSLRRDDPANDESGLVQALVTLACCLSESRRPSDAFVTAQQALTVRRRLVRADPDVHTRRLAADLAHLAPRLRTVGYVDEALELAREAVGLYRRLDEEEIGSCTGDLAGALEVLAACGAAVGRRTTALEAAEEAAALYRGLARRTPALYSPKATHALATLARRLSDVGRHREALAAVEEAVSLSRALAHSAPDNHLPDLADALTVQAACLREADRLDRTLASAREAVSIRRTLEHSRPSTETPALAESLYVLAVYLYTAGQLQESFAMAWEAIDIYRQLVRTNPAPHTADLARALNILTLNLSRAGRAHEALAAVQEAVTFYRSLTQVDPVAYKPDLAACLHNLATCLGDVGDRSAALAAIRETAAIRRELAARDPATHAPALAPCLHRLAKRLAEAGHRGEALETAREAVAAYRSLVRRRPEDFGRGLAGALRTYASVLEWVGREADAARIRQVSEAMTEETALEDSIRGF$","TPR repeat-containing protein","Cytoplasm, Extracellular","TPR Domain domain protein","TPR repeat","Tetratricopeptide TPR_4","","Lamb J.R., Tugendreich S., Hieter P. Tetratrico peptide repeat interactions: to TPR or not to TPR?. Trends Biochem. Sci. 1995. 20(7):257-259. PMID: 7667876Das A.K., Cohen P.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 1998. 17(5):1192-1199. PMID: 9482716Goebl M., Yanagida M. The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Trends Biochem. Sci. 1991. 16(5):173-177. PMID: 1882418D'andrea L.D., Regan L. TPR proteins: the versatile helix. Trends Biochem. Sci. 2003. 28(12):655-662. PMID: 14659697","","","

InterPro
IPR001440
Repeat

Tetratricopeptide TPR_1
PF00515	$\"[134-167]T$ $\"[364-397]T$ $\"[410-443]T$	TPR_1

InterPro
IPR011717
Repeat

Tetratricopeptide TPR_4
PF07721	$\"[318-343]T$ $\"[502-527]T$	TPR_4

InterPro
IPR011990
Domain

Tetratricopeptide-like helical
G3DSA:1.25.40.10	$\"[45-349]T$ $\"[361-580]T$	no description

InterPro
IPR013026
Domain

Tetratricopeptide region
SM00028	$\"[134-167]T$ $\"[180-213]T$ $\"[364-397]T$ $\"[410-443]T$ $\"[502-535]T$	TPR

","BeTs to 4 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 134 to 167 (E_value = 167) place ANA_0057 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 318 to 343 (E_value = 343) place ANA_0057 in the TPR_4 family which is described as Tetratricopeptide repeat.Residues 364 to 397 (E_value = 397) place ANA_0057 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 410 to 443 (E_value = 443) place ANA_0057 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 502 to 527 (E_value = 527) place ANA_0057 in the TPR_4 family which is described as Tetratricopeptide repeat.Residues 502 to 535 (E_value = 535) place ANA_0057 in the TPR_1 family which is described as Tetratricopeptide repeat.","","Domain domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0060","64847","65524","678","6.08","-2.97","23438","GTGGGGGTTCAGGTCGTCGCGATGCTCGCCACCTTCGTCCTGTGCATGACGCTGGGCGCCGAGCGCCACCTGCGCCACAAGGACGCCGGCGTCAAGACGCACGTCCTGGTGGGACTGGGCTCATGCCTGTTCACCCTGGTGTCCGCCTACGGCTTCGCCCCGATCACCGGCTCGGATGTCGCGGTGGACCCCAGCCGTGTGGCCGCGCAGATCGTCTCCGGTATCGGCTTCCTGGGAGCCGGGGTCATCTTCGTCAACAACGACACCGTCCGGGGCCTGACCACCGCCGCGACCGTCTGGCTCAGCGCCGCCATCGGCATGGCCTGCGGGGCGGGCATGATCCCCCTGGCGGCCACGGCGGTCGCGCTGGACTACATCGTCGTCCTGTTCCTGGGGCCCCTCACCTCGCGCCTGCAGCGCCGCCGCGGCGAGGTGACCGTGCGCATCGACTATGAGATCGGCAGCGCCGTCATGCCCGAGATCCTCCAGGTCGCCACCGCATCGGGCTTCACCGCCACCCTGGAGGAGACCGAGGTGACCCGCGGCGAGCACGGGCGCACCATGAACGCCGTCATGCGCTTCCACGGGCAGCGCCCCGCCGTCAACCTCATTGAGGCCCTCTCCGGGCTCGACGGCGTGGACGGCGTTGAGTGCCTCGAGGGAGGCCGGCTCGACTGA","VGVQVVAMLATFVLCMTLGAERHLRHKDAGVKTHVLVGLGSCLFTLVSAYGFAPITGSDVAVDPSRVAAQIVSGIGFLGAGVIFVNNDTVRGLTTAATVWLSAAIGMACGAGMIPLAATAVALDYIVVLFLGPLTSRLQRRRGEVTVRIDYEIGSAVMPEILQVATASGFTATLEETEVTRGEHGRTMNAVMRFHGQRPAVNLIEALSGLDGVDGVECLEGGRLD$","MgtC/SapB transporter","Membrane, Cytoplasm","cation transport ATPase yqgG","K07507 putative Mg2+ transporter-C (MgtC) family protein","MgtC/SapB transporter","","","","","

InterPro
IPR003416
Family

MgtC/SapB transporter
PR01837	$\"[11-30]T$ $\"[30-48]T$ $\"[63-85]T$ $\"[90-114]T$	MGTCSAPBPROT
PF02308	$\"[8-144]T$	MgtC

noIPR
unintegrated

unintegrated
signalp	$\"[1-15]?$	signal-peptide
tmhmm	$\"[35-53]?$ $\"[67-85]?$ $\"[90-110]?$ $\"[116-136]?$	transmembrane_regions

","BeTs to 9 clades of COG1285COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG1285 is -------q-drlbcef-h------t-Number of proteins in this genome belonging to this COG is 1","***** IPB003416 (MgtC/SapB transporter) with a combined E-value of 2.4e-51. IPB003416A 7-45 IPB003416B 64-84 IPB003416C 90-112","Residues 35-102 are 76% similar to a (MG2 FAMILY ATPASE MGTC TRANSMEMBRANE MEMBRANE C PROTEIN MGTC/SAPB TRANSPORTER) protein domain (PD007346) which is seen in YHID_ECOLI.","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 144 (E_value = 1.6e-46) place ANA_0060 in the MgtC family which is described as MgtC family.","","transport ATPase yqgG (mgtC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0060.1","65936","65652","285","8.92","2.38","10635","GTGGAGGTCTCCCAGGGGCCGGTGCGCTGGGGACTGACATACGACGACTACATCGGCGAGCACGAGCGCCTGCGCCTGGGCGACGCGCACTGGTCGCGCCGGGTGCGCCGCGTCGTCGACGCCCTGCGCCCCATGTACCTGTGGGACCGCCTCTACCTGGGCGGCGGCAACTCGCGGCGGATCACGGCGGCCCAGCTCGCCAAGATCGGCGACGACGTCGTCGTGGTCCCCAACGAGGCCGGCATGACCGGGGGCGCCCGCTGCTGGGACATGGCCCGCCCCTGA","VEVSQGPVRWGLTYDDYIGEHERLRLGDAHWSRRVRRVVDALRPMYLWDRLYLGGGNSRRITAAQLAKIGDDVVVVPNEAGMTGGARCWDMARP$","Hypothetical protein","Cytoplasm","","","","","","","","No hits reported.","BeTs to 3 clades of COG1940COG name: Transcriptional regulators of NagC/XylR familyFunctional Class: KThe phylogenetic pattern of COG1940 is a-t--qVcEBRH----O----Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 1-89 are 58% similar to a (MLR4209 ATU4836 AGR_L_95P KINASE POLYPHOSPHATE GLUCOKINASE) protein domain (PD589246) which is seen in Q8YX46_ANASP.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:26 2007","Wed Aug 15 09:38:26 2007","Wed Aug 15 09:38:26 2007","Wed Aug 15 09:38:11 2007","","","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","Wed Aug 15 09:38:11 2007","","Wed Aug 15 09:38:11 2007","","Wed Aug 15 09:38:11 2007","yes","","" "ANA_0061","65937","67355","1419","7.72","4.45","49756","GTGCGGAGCCAGGACTCCGTTGTCGAAAACGGCGTTGCCCAGGCCCGTGCCCAGGGTCACGATCATCTCCAGGCCGTGGCCCGTGACGACACCGGCCCCGGCGACCTCGGCGTCGTTGAGGACCAGGGAGGGGATTCCCAGGGCCCTGGAGACGGCGGCACCCATGTCGAAGCGGCCCCAGGCCTCCACCAGGTCGGGCAGCACCCTGGAGCGCGGGCCGTCCTTGGTGATGTAGTGCGGCGTGGCGACGACGACCCCGTGGCGGATCATGCCCGGCATCCCCACCGTCACCCGGTCCGCGCCCGGCAGCTGGGAGGCCAGCGAGGCGATGGTCTCCACCAGCTTCTCCGGCGGCAGCGGGTAGGGGGTCGGGGTGCGCACGGCGCGGGAGATGATGTTGCCCTCGCAGTCCAGCACCGAGGCCTTGATGCCGCCGCCTCCGCAGTCCACGGACAGAGTCGTTGTGCTCACGGCTGCGAGCCTAGTGGAAGCGCGAAGCCGGTGCGGTTCAATGGGGGCATGCCACGCATCCGCCTCGACCTGGCCTACGACGGCACCTTCTTCTCCGGGTGGGCCGCCCAGCCCGGGCTGCGCACCGTCGAGGGGGTCCTCACCTCCGCCCTGGCCACCGTGCTGCGTGAGCCCGTCCGCCTCACCGTGGCCGGACGCACCGACGCCGGCGTCCACGCCGCCGCCCAGGTGGCTCACCTCGATGTGAGTCCTGAGGCCTGGGCCGCGCTGCCCGGACGCTCCGAGCGCCTCCCCGAGACCGCCCTGCTCGCCCGGGTGGCGGGCGTCCTGGCCCGCGAGGCCCAGGAGAGCCTGGCGCGCACGCCGCGTGGGGCCGGCGACGTCGTCGTCACCGGGGCGCGCACCGTGCCGGAGGCCTTCGACGCCCGCTTCAGCGCCCTGAGCCGCCGCTACACCTACCGGATCGCCGACGCCGCCGCCCCGCGCGACCCCGCCCGGCGCGCCACCGTCCTGTGGCTGCCCGATGTGCTCGACGTCGAGGCCATGGACGCCTCCGCCCGCGCCCTGCTCGGCGAGCACGACTTCCTGTCCTACTGCAAGCCCCGCGAGGGTGCCACGACCATCCGCACCCTGCGCACCCTGCAGTGGCGACGGGCCGAGGCCGGGCCGGACGCAGGGCCGGACGCGGGGCTCGTGACCCTGAGCGTCGTCGCCGACGCCTTCTGCCACTCCATGGTCCGTTCCCTGGTGGGGGCGGGCCTGGCCGTCGGGCAGGGACGCAAGCCGGTCACCTGGCCGCGCGAGCTCCTGGACGCCCGCACTCGCCAGAGCGCCGCCCCCGTCGCCCCGCCGCACGGACTGACCCTGGAGGAGGTCACCTACCCGGCCGACGACGAGCTCGCCGCCCAGGCCGAGCGGGCCCGCACCACCCGGCGTCTGAGCTGCTGA","VRSQDSVVENGVAQARAQGHDHLQAVARDDTGPGDLGVVEDQGGDSQGPGDGGTHVEAAPGLHQVGQHPGARAVLGDVVRRGDDDPVADHARHPHRHPVRARQLGGQRGDGLHQLLRRQRVGGRGAHGAGDDVALAVQHRGLDAAASAVHGQSRCAHGCEPSGSAKPVRFNGGMPRIRLDLAYDGTFFSGWAAQPGLRTVEGVLTSALATVLREPVRLTVAGRTDAGVHAAAQVAHLDVSPEAWAALPGRSERLPETALLARVAGVLAREAQESLARTPRGAGDVVVTGARTVPEAFDARFSALSRRYTYRIADAAAPRDPARRATVLWLPDVLDVEAMDASARALLGEHDFLSYCKPREGATTIRTLRTLQWRRAEAGPDAGPDAGLVTLSVVADAFCHSMVRSLVGAGLAVGQGRKPVTWPRELLDARTRQSAAPVAPPHGLTLEEVTYPADDELAAQAERARTTRRLSC$","tRNA pseudouridine synthase A","Cytoplasm","tRNA pseudouridine synthase A (PseudouridylatesynthaseI) (Pseudouridine synthase I) (Uracil hydrolyase)","tRNA pseudouridine synthase A ","tRNA pseudouridine synthase A","","Arluison V., Hountondji C., Robert B., Grosjean H. Transfer RNA-pseudouridine synthetase Pus1 of Saccharomyces cerevisiae contains one atom of zinc essential for its native conformation and tRNA recognition. Biochemistry 1998. 37(20):7268-7276. PMID: 9585540","","","

InterPro
IPR001406
Family

tRNA pseudouridine synthase
G3DSA:3.30.70.580	$\"[172-303]T$	no description
G3DSA:3.30.70.660	$\"[305-450]T$	no description
PTHR11142	$\"[177-457]T$	PSEUDOURIDYLATE SYNTHASE
PF01416	$\"[179-302]T$ $\"[342-452]T$	PseudoU_synth_1
TIGR00071	$\"[176-446]T$	hisT_truA: tRNA pseudouridine synthase A

","BeTs to 25 clades of COG0101COG name: Pseudouridylate synthase (tRNA psi55)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0101 is aompk-yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001406 (tRNA pseudouridine synthase) with a combined E-value of 7e-52. IPB001406A 176-208 IPB001406B 221-237 IPB001406C 297-310 IPB001406D 346-357 IPB001406E 395-410 IPB001406F 437-451","Residues 202-255 are 62% similar to a (SYNTHASE TRNA PSEUDOURIDINE I LYASE PROCESSING A PSEUDOURIDYLATE HYDROLYASE URACIL) protein domain (PD003202) which is seen in TRUA_MYCPA.Residues 350-451 are 64% similar to a (SYNTHASE TRNA PSEUDOURIDINE I LYASE PROCESSING A PSEUDOURIDYLATE HYDROLYASE URACIL) protein domain (PD118232) which is seen in TRUA_MYCTU.","","-46% similar to PDB:1DJ0 THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION (E_value = 3.0E_30);-46% similar to PDB:2NQP Crystal structure of pseudoudirinde synthase TruA in complex with leucyl tRNA (E_value = 3.0E_30);-46% similar to PDB:2NR0 Crystal structure of pseudoudirinde synthase TruA in complex with leucyl tRNA (E_value = 3.0E_30);-46% similar to PDB:2NRE Crystal structure of pseudoudirinde synthase TruA in complex with leucyl tRNA (E_value = 3.0E_30);-44% similar to PDB:1VS3 Crystal Structure of the tRNA Pseudouridine Synthase TruA From Thermus thermophilus HB8 (E_value = 5.9E_26);","Residues 179 to 302 (E_value = 5e-17) place ANA_0061 in the PseudoU_synth_1 family which is described as tRNA pseudouridine synthase.Residues 342 to 452 (E_value = 2.6e-20) place ANA_0061 in the PseudoU_synth_1 family which is described as tRNA pseudouridine synthase.","","pseudouridine synthase A (Pseudouridylate synthaseI) (Pseudouridine synthase I) (Uracil hydrolyase) (AF213822)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0062","67476","68057","582","10.00","16.03","21102","GTGTCCGCGGTGCCGTCCCACTCGCCCCGGATCGCCTGTGCTCCGACCACTCACCTGACCATGGTGGTCTCGCCGAACCGCGAACGCTTCACCGCGCTTCGGCGTGCCCACTCGCCAAGAGAAACGAAGGCAACGCCCGTGCGCACGTACACACCGAAGCCCGGCGACGTCGAGAAGAACTGGTACGTCATCGACGCCACCGACGTCGTCCTGGGTCGACTCGCGGCCCAGGCCGCCACCCTGCTCCGTGGGAAGCACAAGCCCCAGTTCGCCCCCAACGAGGACTGCGGCGACTACGTCGTCATCATCAATGCCGACAAGGTGGCTCTCACCAACGGCAAGGCTGACAAGAAGTTCGCCTACCGCCACTCCGGCCACCCGGGTGGCCTGACCGCCGTCTCCTACCGCGAGCTGCTGGCCACCCGCCCGGAGCGCGCCGTTGAGAAGGCCATCAAGGGCATGGTTCCCCACACCAAGCTCGGTCGCGCCCAGCTCAAGAAGCTCAAGGTCTACGCGGGTGCCGAGCACCCGCACGCCTCCCAGAGCCCGAAGACGTTCGAGATCACCCAGGTCGCCCAGTAA","VSAVPSHSPRIACAPTTHLTMVVSPNRERFTALRRAHSPRETKATPVRTYTPKPGDVEKNWYVIDATDVVLGRLAAQAATLLRGKHKPQFAPNEDCGDYVVIINADKVALTNGKADKKFAYRHSGHPGGLTAVSYRELLATRPERAVEKAIKGMVPHTKLGRAQLKKLKVYAGAEHPHASQSPKTFEITQVAQ$","Ribosomal protein L13","Periplasm, Cytoplasm, Extracellular","50S ribosomal protein","ribosomal protein L13","ribosomal protein L13","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Chan Y.L., Olvera J., Gluck A., Wool I.G. A leucine zipper-like motif and a basic region-leucine zipper-like element in rat ribosomal protein L13a. Identification of the tum- transplantation antigen P198. J. Biol. Chem. 1994. 269(8):5589-5594. PMID: 8119894","","","

InterPro
IPR005822
Family

Ribosomal protein L13
PD001791	$\"[97-168]T$	Q82DL9_STRAW_Q82DL9;
PTHR11545	$\"[45-193]T$	RIBOSOMAL PROTEIN L13
PF00572	$\"[61-188]T$	Ribosomal_L13
PS00783	$\"[151-173]?$	RIBOSOMAL_L13

InterPro
IPR005823
Family

Ribosomal protein L13, bacterial and organelle form
PTHR11545:SF2	$\"[45-193]T$	50S RIBOSOMAL PROTEIN L13
TIGR01066	$\"[49-188]T$	rplM_bact: ribosomal protein L13

noIPR
unintegrated

unintegrated
G3DSA:3.90.1180.10	$\"[61-191]T$	no description

","BeTs to 26 clades of COG0102COG name: Ribosomal protein L13Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0102 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005822 (Ribosomal protein L13) with a combined E-value of 3.3e-28. IPB005822A 82-121 IPB005822B 141-157","Residues 47-99 are 69% similar to a (RIBOSOMAL L13 50S RIBONUCLEOPROTEIN RRNA-BINDING 3D-STRUCTURE SEQUENCING DIRECT RNA-BINDING) protein domain (PD866156) which is seen in RL13_HAESO.Residues 49-183 are 54% similar to a (CHLOROPLAST RIBOSOMAL L13 50S) protein domain (PD795418) which is seen in RK13_ODOSI.Residues 63-95 are 90% similar to a (RIBOSOMAL L13 RIBONUCLEOPROTEIN 50S CHLOROPLAST RPLM SUBUNIT PROBABLE I SEQUENCING) protein domain (PD335764) which is seen in RL13_MYCLE.Residues 64-171 are similar to a (RIBOSOMAL RIBONUCLEOPROTEIN 50S 60S L13 L13A L13P MULTIGENE FAMILY LSU) protein domain (PDA0W219) which is seen in Q7V521_PROMM.Residues 97-168 are 76% similar to a (RIBOSOMAL L13 RIBONUCLEOPROTEIN 50S CHLOROPLAST MITOCHONDRION L13 MITOCHONDRIAL SEQUENCING 60S) protein domain (PD001791) which is seen in Q82DL9_STRAW.","","-72% similar to PDB:1P85 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 1.4E_41);-72% similar to PDB:1P86 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 1.4E_41);-72% similar to PDB:1VS6 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 50s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.4E_41);-72% similar to PDB:1VS8 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.4E_41);-72% similar to PDB:2AW4 Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 50S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 1.4E_41);","Residues 61 to 188 (E_value = 4.1e-65) place ANA_0062 in the Ribosomal_L13 family which is described as Ribosomal protein L13.","","ribosomal protein (rpL13)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0063","68101","68595","495","10.05","7.43","17834","GTGGCTGAGACCACTGTCGACATTGACGCGCTGGACGAGGAGAACGCCCCCTCCAGCTACACCACCGAGACCGAGGAGTCCGCTCCGGGTCGCGGCCAGTCCATCACCGCCCCCGGCTCCGGCCTGGGTCGCCGCAAGGAGGCCGTCGCTCGCGTGCGCCTCGTTCCCGGCACCGGCCAGTGGACGCTCAACGGCCGCTCCCTGGAGGACTACTTCCCCAACAAGCTGCACCAGCAGCTCGTGCGCGCCCCCTTCACCATCCTGGACCTCGAGGGCCGCTTCGACGTCGTCGCCCGCATCAACGGCGGTGGCGTCTCCGGCCAGGCCGGCGCCCTGCGCCTGGGCATCGCCCGCGCGCTCAACGAGATCGACCGTGAGGCCAACCGCGCCACCCTGAAGAAGGCCGGTTTCCTCACTCGCGACTCGCGCATCGTGGAGCGCAAGAAGGCCGGTCTGCACAAGGCCCGCCGCGCCCCCCAGTACTCCAAGCGCTGA","VAETTVDIDALDEENAPSSYTTETEESAPGRGQSITAPGSGLGRRKEAVARVRLVPGTGQWTLNGRSLEDYFPNKLHQQLVRAPFTILDLEGRFDVVARINGGGVSGQAGALRLGIARALNEIDREANRATLKKAGFLTRDSRIVERKKAGLHKARRAPQYSKR$","Ribosomal protein S9","Cytoplasm, Extracellular","30S ribosomal protein S9","30S ribosomal protein S9","ribosomal protein S9","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000754
Domain

Ribosomal protein S9
PD001627	$\"[41-108]T$	RS9_STRAW_Q82DL8;
PF00380	$\"[43-164]T$	Ribosomal_S9
PS00360	$\"[102-120]T$	RIBOSOMAL_S9

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[36-164]T$	no description

noIPR
unintegrated

unintegrated
PTHR21569	$\"[35-164]T$	RIBOSOMAL PROTEIN S9

","BeTs to 26 clades of COG0103COG name: Ribosomal protein S9Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0103 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000754 (Ribosomal protein S9) with a combined E-value of 3.9e-48. IPB000754A 43-65 IPB000754B 94-120 IPB000754C 136-164","Residues 41-108 are similar to a (RIBOSOMAL 30S S9 RIBONUCLEOPROTEIN 40S S16 CHLOROPLAST S9P S9 SEQUENCING) protein domain (PD001627) which is seen in RS9_STRAW.Residues 135-164 are identical to a (RIBOSOMAL S9 30S RIBONUCLEOPROTEIN CHLOROPLAST S9 MITOCHONDRIAL 40S PEPTIDE TRANSIT) protein domain (PD556634) which is seen in RS9_BIFLO.","","-63% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 3.1E_25);-63% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 3.1E_25);-63% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.1E_25);-63% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.1E_25);-63% similar to PDB:2AVY Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 30S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 3.1E_25);","Residues 43 to 164 (E_value = 3.1e-58) place ANA_0063 in the Ribosomal_S9 family which is described as Ribosomal protein S9/S16.","","ribosomal protein S9 (BS10)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0064","68910","70271","1362","5.43","-10.87","46891","ATGGCTCGTCTCTTCGGAACCGACGGCGTACGCGGCCTGGCCAACGACCTGCTCACGCCCACCCTGGCCGTACAGCTCGGTGAGGCCGCGGCCCGCGTCCTGACCAAGGACACGTCCGCCGCACGGAGCTCACGCAGCGGCCGCCCCCGCGCGATCGTGGGCCGTGACACCCGCGCCTCCGGAGAGTTCCTCGACCACGCCATCAGCGCGGGCCTGGCCTCCTCCGGCATCGACGTCACCCGCGTGGGCGTCCTGCCCACCCCGGCGATCGCCCACCTGACGGCCACCCAGGACATCGAGCTGGGCGTCATGATCTCCGCCTCCCACAACCCCTTCCCGGACAACGGCATCAAGTTCATCGCCCGCGGCGGCTACAAGCTCGCCGACGCCGTCGAGGACGAGATCGAGGCCCTCCTGGGCAAGGTCAACGACCGCCCCACCGGCGCCGACGTCGGCCGCGTCATCAAGGGGGAGACCGTCGCGGATCAGAACTACATCAACCACCTCGTCGACTCCGTCGCCACTGACCTGTCCGGCCTGCGCATCGTCGTCGACGCCTCCAACGGCGCCGCCTCCGTCGTCGGTCCGGCCGCGCTGCGGGCCGCCGGCGCCGAGGTCATCGTCATCAACGCCTCCCCGGACGGCCTCAACATCAACGACAACTGCGGCTCCACCCACCCCGAGCAGCTGCAGAACTATGTCACGGCGGTCGGGGCGGACATGGGCGTGGCCTACGACGGCGACGCCGACCGCTGCCTGGCCGTGGACGCCGACGGCAAGCTCGTCGACGGTGACCAGATCATGGGCATGCTCGCTATCGGCATGAAGGCCGATGGCACTCTCGGCTCCGACACGCTCGTCGTGACCGTCATGAGCAACCTCGGCCTCATCCTGGCCATGCGTGAGCACGGCATCCGCACCGTCCAGACCGGCGTGGGCGACCGCTACGTGCTCGAGCGGATGCTCCAGGGCGGCTACACCCTGGGCGGCGAGCAGTCCGGGCACGTCATCGACACCGTCCACGCCACCACCGGTGACGGCGTGCTCACCTCCCTGCACGTGGCTGCGCGCGTCAAGCGCACCGGCAAGACGCTGGCCGAGCTCGCCAGCGTCGTCACCCGCCTGCCCCAGACCCTCATCAACGTCAAGAATGTCGACAAGGGCGCCGCCAGCACCAACAAGGCCGTGCAGGACGCCGTGGCCTCCGCGGAGAAGGACCTGGGCGAGACCGGCCGGGTCCTGCTGCGCCCCTCGGGCACCGAGCCGCTCGTGCGCGTCATGGTCGAGGCCGCCACCCAGGAGGAGGCCGACCGCGTCGCCCGCTCCCTGGCCGACACCGTCAAGAACAACCTCAGCCTGTGA","MARLFGTDGVRGLANDLLTPTLAVQLGEAAARVLTKDTSAARSSRSGRPRAIVGRDTRASGEFLDHAISAGLASSGIDVTRVGVLPTPAIAHLTATQDIELGVMISASHNPFPDNGIKFIARGGYKLADAVEDEIEALLGKVNDRPTGADVGRVIKGETVADQNYINHLVDSVATDLSGLRIVVDASNGAASVVGPAALRAAGAEVIVINASPDGLNINDNCGSTHPEQLQNYVTAVGADMGVAYDGDADRCLAVDADGKLVDGDQIMGMLAIGMKADGTLGSDTLVVTVMSNLGLILAMREHGIRTVQTGVGDRYVLERMLQGGYTLGGEQSGHVIDTVHATTGDGVLTSLHVAARVKRTGKTLAELASVVTRLPQTLINVKNVDKGAASTNKAVQDAVASAEKDLGETGRVLLRPSGTEPLVRVMVEAATQEEADRVARSLADTVKNNLSL$","Phosphoglucosamine mutase","Cytoplasm","phosphoglucosamine mutase","phosphoglucosamine mutase ","phosphoglucosamine mutase","","Mengin-Lecreulx D., van Heijenoort J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J. Biol. Chem. 1996. 271(1):32-39. PMID: 8550580De Reuse H., Labigne A., Mengin-Lecreulx D. The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase. J. Bacteriol. 1997. 179(11):3488-3493. PMID: 9171391Jolly L., Wu S., van Heijenoort J., de Lencastre H., Mengin-Lecreulx D., Tomasz A. The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase. J. Bacteriol. 1997. 179(17):5321-5325. PMID: 9286983","","","

InterPro
IPR005841
Family

Phosphoglucomutase/phosphomannomutase
PR00509	$\"[101-115]T$ $\"[179-198]T$ $\"[239-254]T$	PGMPMM
PS00710	$\"[102-111]T$	PGM_PMM

InterPro
IPR005843
Domain

Phosphoglucomutase/phosphomannomutase C-terminal
PF00408	$\"[411-449]T$	PGM_PMM_IV

InterPro
IPR005844
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I
PF02878	$\"[2-146]T$	PGM_PMM_I

InterPro
IPR005845
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II
PF02879	$\"[163-261]T$	PGM_PMM_II

InterPro
IPR005846
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III
PF02880	$\"[263-375]T$	PGM_PMM_III

InterPro
IPR006352
Family

Phosphoglucosamine mutase
TIGR01455	$\"[5-449]T$	glmM: phosphoglucosamine mutase

noIPR
unintegrated

unintegrated
G3DSA:3.40.120.10	$\"[4-154]T$ $\"[181-255]T$ $\"[256-370]T$	no description
PTHR22573	$\"[68-451]T$	PHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF2	$\"[68-451]T$	PHOSPHOGLUCOMUTASE

","BeTs to 25 clades of COG1109COG name: PhosphomannomutaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1109 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB005841 (Phosphoglucomutase/phosphomannomutase) with a combined E-value of 1.4e-17. IPB005841C 80-95 IPB005841D 101-111 IPB005841E 114-136 IPB005841I 240-251 IPB005841M 410-422","Residues 3-87 are 69% similar to a (PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOGLUCOMUTASE MUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE MAGNESIUM METAL-BINDING PHOSPHORYLATION PHOSPHOGLUCOSAMINE PHOSPHOMUTASE) protein domain (PD475365) which is seen in Q6NJ50_CORDI.Residues 90-138 are 79% similar to a (PHOSPHOMANNOMUTASE ISOMERASE MUTASE PHOSPHOGLUCOMUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE MAGNESIUM METAL-BINDING PHOSPHOGLUCOSAMINE PHOSPHORYLATION FAMILY) protein domain (PD000667) which is seen in Q82DL7_STRAW.Residues 165-272 are similar to a (PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOGLUCOMUTASE MUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE MAGNESIUM METAL-BINDING PHOSPHORYLATION PHOSPHOGLUCOSAMINE FAMILY) protein domain (PD000778) which is seen in Q8FS18_COREF.Residues 281-387 are similar to a (PHOSPHOMANNOMUTASE ISOMERASE MUTASE PHOSPHOGLUCOSAMINE PHOSPHOGLUCOMUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE MAGNESIUM METAL-BINDING PHOSPHORYLATION FAMILY) protein domain (PD001709) which is seen in Q6A6T5_PROAC.Residues 396-451 are 76% similar to a (PHOSPHOMANNOMUTASE ISOMERASE MUTASE PHOSPHOGLUCOMUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE PHOSPHOGLUCOSAMINE MAGNESIUM METAL-BINDING PHOSPHORYLATION FAMILY) protein domain (PD347884) which is seen in Q6GER6_STAAR.","","-52% similar to PDB:1WQA Crystal Structure of Pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with Mg2+ (E_value = 4.5E_60);-46% similar to PDB:2F7L Crystal structure of Sulfolobus tokodaii phosphomannomutase/phosphoglucomutase (E_value = 9.4E_42);-44% similar to PDB:1K35 Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa (E_value = 4.0E_32);-44% similar to PDB:1P5D Enzyme-ligand complex of P. aeruginosa PMM/PGM (E_value = 4.0E_32);-44% similar to PDB:1P5G Enzyme-ligand complex of P. aeruginosa PMM/PGM (E_value = 4.0E_32);","Residues 2 to 146 (E_value = 1.5e-49) place ANA_0064 in the PGM_PMM_I family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I.Residues 163 to 261 (E_value = 1.4e-30) place ANA_0064 in the PGM_PMM_II family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II.Residues 263 to 375 (E_value = 1.2e-18) place ANA_0064 in the PGM_PMM_III family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III.Residues 379 to 449 (E_value = 2.7e-05) place ANA_0064 in the PGM_PMM_IV family which is described as Phosphoglucomutase/phosphomannomutase, C-terminal domain.","","mutase (glmM)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0065","70380","73577","3198","5.48","-29.58","114890","ATGGGTGAGAATGGCCTCGTGACCTCCTCGTACCGCCTGGCTCTCCTGACGGAGCCGCCGACCTGGCAAGGCCGTACCCTGAGCGGGAGGAGCCTTGACCTGCTCGCCGTGCTCGCCGGCAGCCAGGACGCCAGGGTGAGCGACGGCGCCCTCATCGAGGCCCTGTGGCCCGACGACGCCCCGGCCCGGCCGCTGCGGGCGCTTCACGTCGTCGTCTCCCGGTTGCGTGCCGTCGTGGGGGAGGGCGTCGTCGAGCGCAACGGCGATGGCTACCGACTGGAGCTGGCGGAGGCGGAGGCTGATGTCCGGGACCTGTCGTATCGGGCGGAGCGCGCCCGAGCCTGCGCCGCCGCCGGCCAGTGGGAGCAGGTCCTCGATCTCACCGACCGACTGCCCCAGGTGCCCGTTCCCGACGAGGTCGATGACAACGGTGGAGCAGGAGCCGCCCCTATGGCCCTCTTGCGAGAGCGGGCTGCAGCCCTGACCGAGGAGGCCCGCCGCGACCAGGGGCTCGCCCTGGAGGCCACCGGTGAGCACGAGCGGGCCGTGGACCTGCTGCGTGAGGCCTCCCAGCGCGACGGCGGCGATGAGACCGTCCTGGCCGCCCTCATGCGCGCCGAGTCCTGGGTGCGCTCACCGGCTGCGGCCCTGGAGATCTACGAGCAGTACCGCCGTCGGCTGCGCGAGCTGGGAGCCGTGCCCGGCCCGGCCATGCGCGCCGCCCACGAGGCCGTCCTGGCCGCCGAGAGCCCTGTGCGCCACGGCCTGCAGCCCGAGCCCGAGCACTTCCTGGGGCGCGAGGCGGACGTGACCGGTGTTCTCAAGGCCCTGAGTACCCACCGTCTGGTGACGCTCACCGGCCCCGGTGGGGTCGGCAAGACCACCCTGGCCCAGGTGGTGGCGGCCCGCAGCCGCCGCCCCGCCGTCTACGTCGTCGCCCTCGCCGAGGTGTCACCCGGAGCCGATTTGGCCAGGGTCGTGCTCGACGCAGTCGGAGGCTCCGCAGTCATCAACGGTGACCCGCACCGCGATCTGGCCGCCGCCCTCTCCCAGCCCGGAACCGTCCTGGTGCTGGACAACTGCGAGCACCTGGCCGGCGAGGCGGCCGACCTCATCGGGCCGCTCCTGGTCGCCTGCCCCGATCTGCGCGTGCTGGCGACCTCGCGCCGCCCCGTCGACCTGGCCGCGGAGCACGTCCACCGCCTTGAGGCCCTCAATGCTGCCTCCTCCGCCGAGCTCTTCCGTGCCCGTGCTCTGGCCGCTCGCCCCGGCCAGGTCATCGACGATGACGACTTAGGCGAGCTCCTGAGCCGGTTGGAGGGCATCCCCTTGGCCATCGAGCTGGCCGCCGCGCGCACCCGCAGCCTGTCGGTCGGCCAGATCGCCGAGCGACTGCCCGGCAGACCCGATCTGCTCACCGCCGCCCGTGACGCCCCGGCCCGTCAACGCACCCTGACAGCGGTCATCGAGTGGTCCTGGAACCTGCTCGACGCCGCCGAACGCCGCGCCCTGGCTCGGCTGGCCCCGCTCCCCGACGGCTTCACCCTCCTGCCCGCGGAGGCGCTCATCGGCGCGCAGGCCGCCGACCTCCTCGACGCCCTGGTCTCCCACTCCCTGCTCGTGGTGCGCGACCACGGCCTGCCCCGCTTCCACATGCTCGTCACCGTCCGAGACTTCGCCCTGGAGCAGCTGTCCGCCTCCGGTGACGAGGCCGAGGCCCGCGCGACCCTGCGCCAGTGGGCGGTGGACCTGTGCTCCCAGATCCGTTTTCCCGTGGACGCCGGCGACTTCGGCGACGCCCGTCACCCCGAGGCGCGCCGCCACGACCGCCTCTTCCGGCAGGTCGCCCACGATGAGGCCGTCATCCTTCAACAGCTCGACCGGCTCCTGGCACAGGCCGACGGCCACGGCACGGATCACCTGCCGGCGGAGCTGCGCGACGCCATCTGTCTCATCGGTGCCGCCCTCATGCGCCTGTGGAGCGTCACCTGGAGCTATGAGCGCATCGCCGACTATGGTGCGCGCCTCATCGCTGCCGCTGTCCAACCCGCCCAGGACTCACGCGGCAACGAGGCAGGCCTGAGCGCGCTGGCCCTGTGCGTCACCCTCTTCGGGCTCCTGAGCCACGTGCCCGAACAGGTCCGCTCCCTGCTGCCGGCCTCCTTCGACGGAGAGGGACCGTTCATCCGGGTCAGGCGCTTCCTGCGTGCGAGCGACGAGCAGTGGCCCGAGCTGACCGGCGACGCCGACCCCTGGGTCGCCTGGGCGGCGACCCGCTGCCTGGCCGCCCAGCAGGAGGACGACGGCGATCCTCAGGCCTCCCTGGAGACCATCGAGGCCCTCCTGGGGCGGCTCCATGGCCACGACCTGGCCGGCATTCACCTGCTCGAGCTGCACCTCCACCGGCTACAGGTGCTCATGTCCCTGGGGCGTTACAGCCAGGTCGTCGACGCCTGCTCGCGCGCCCAGGTGCTCCTGGAACGGGTCCTGCCCAGCTGGGGCGAGTTCTTCCGCACGACACTGCACATGGAGGGGGCCTACTGCGCGGTCTACCTCGATCCGCGCCCCGAGACGGCGGGCAGGCTGCTGGAGAGCCTGGAACCGATCGACCTGCCGGGAACCCTGCGCTTCATCGCCCGCTCCGTGCGCGGTGAGCTGGAGCTCACCCGCGGGAACGTGCGCACCGCCGCCCTCATCCAGCGCGTGAGCCTGCGCTACGCCGGGAACTGGCGCTCCATCCTGGGATCGGGCTCCCAGTGGGAGCTCTACATCCTGAGCATGTGCCTGGTCACCGACGTCGAGCTCAGCCCCGACGACGCCGTCGAGCTCGATGCCCGAGCCGTCCGTGCCCGAGCCACCTCCCTGCTGCGCGAGATCCTCTCCGATCCGGCTCCACGGCAGCGTGACATTCCCACGCTCATGGCTTTCGCGGCCGCCGTCGGCCTGTCCGCCGTGGCTGCTGAGGACGTGGGCTCCGACCGGCGGGCAGTAGGGGGCGAGCTGGTCGCCACCGCCCTGGCGGTGGGCACCAACCAGACCTGCCGCCTGCTCTCCCACGACTACCTGCGCAGCCGCACTGAGCGGCTGGACGCCCGGGCGCTGGCGCAGGCCGAGGAGAGGATTCGGTCCCTGGACCGCGGTGGGCTCGTGGCTCACGCCGCCGACCTCGCCGGCCGTCTGGCGGGCGAGGTCGGCTGA","MGENGLVTSSYRLALLTEPPTWQGRTLSGRSLDLLAVLAGSQDARVSDGALIEALWPDDAPARPLRALHVVVSRLRAVVGEGVVERNGDGYRLELAEAEADVRDLSYRAERARACAAAGQWEQVLDLTDRLPQVPVPDEVDDNGGAGAAPMALLRERAAALTEEARRDQGLALEATGEHERAVDLLREASQRDGGDETVLAALMRAESWVRSPAAALEIYEQYRRRLRELGAVPGPAMRAAHEAVLAAESPVRHGLQPEPEHFLGREADVTGVLKALSTHRLVTLTGPGGVGKTTLAQVVAARSRRPAVYVVALAEVSPGADLARVVLDAVGGSAVINGDPHRDLAAALSQPGTVLVLDNCEHLAGEAADLIGPLLVACPDLRVLATSRRPVDLAAEHVHRLEALNAASSAELFRARALAARPGQVIDDDDLGELLSRLEGIPLAIELAAARTRSLSVGQIAERLPGRPDLLTAARDAPARQRTLTAVIEWSWNLLDAAERRALARLAPLPDGFTLLPAEALIGAQAADLLDALVSHSLLVVRDHGLPRFHMLVTVRDFALEQLSASGDEAEARATLRQWAVDLCSQIRFPVDAGDFGDARHPEARRHDRLFRQVAHDEAVILQQLDRLLAQADGHGTDHLPAELRDAICLIGAALMRLWSVTWSYERIADYGARLIAAAVQPAQDSRGNEAGLSALALCVTLFGLLSHVPEQVRSLLPASFDGEGPFIRVRRFLRASDEQWPELTGDADPWVAWAATRCLAAQQEDDGDPQASLETIEALLGRLHGHDLAGIHLLELHLHRLQVLMSLGRYSQVVDACSRAQVLLERVLPSWGEFFRTTLHMEGAYCAVYLDPRPETAGRLLESLEPIDLPGTLRFIARSVRGELELTRGNVRTAALIQRVSLRYAGNWRSILGSGSQWELYILSMCLVTDVELSPDDAVELDARAVRARATSLLREILSDPAPRQRDIPTLMAFAAAVGLSAVAAEDVGSDRRAVGGELVATALAVGTNQTCRLLSHDYLRSRTERLDARALAQAEERIRSLDRGGLVAHAADLAGRLAGEVG$","Transcriptional regulator possibly involved in actinorhodin production","Cytoplasm","transcriptional regulator, LuxR family","putative transcriptional regulator","transcriptional regulator domain protein","","Staskawicz B.J., Ausubel F.M., Baker B.J., Ellis J.G., Jones J.D. Molecular genetics of plant disease resistance. Science 1995. 268(5211):661-667. PMID: 7732374","","","

InterPro
IPR000767
Family

Disease resistance protein
PR00364	$\"[282-297]T$ $\"[348-362]T$ $\"[439-453]T$ $\"[861-877]T$	DISEASERSIST

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PF00486	$\"[24-93]T$	Trans_reg_C

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[279-433]T$	AAA

InterPro
IPR005158
Domain

Bacterial transcriptional activator domain
PF03704	$\"[152-246]T$	BTAD

","BeTs to 4 clades of COG2256COG name: Uncharacterized ATPase related to the helicase subunit of the Holliday junction resolvaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2256 is ------y-vdrlb-efghsnuj---wNumber of proteins in this genome belonging to this COG is 3","***** IPB005158 (Bacterial transcriptional activator domain) with a combined E-value of 1.1e-19. IPB005158A 30-73 IPB005158C 160-210 IPB005158D 210-250","Residues 169-248 are 56% similar to a (REGULATORY TRANSCRIPTIONAL REGULATOR ACTIVATOR PATHWAY SPECIFIC FAMILY SARP DNA-BINDING SYSTEM) protein domain (PD653716) which is seen in Q82AU6_STRAW.Residues 264-389 are 58% similar to a (TRANSCRIPTIONAL DNA-BINDING TRANSCRIPTION REGULATION ATP-BINDING REPEAT REGULATORY REGULATOR KINASE LYASE) protein domain (PD005851) which is seen in Q82AU6_STRAW.Residues 430-559 are 63% similar to a (TRANSCRIPTIONAL REGULATORY REGULATOR REPEAT ATP-BINDING DNA-BINDING TRANSCRIPTION REGULATION FAMILY LUXR) protein domain (PD010067) which is seen in Q82AU6_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 93 (E_value = 4.1e-07) place ANA_0065 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.Residues 152 to 246 (E_value = 7.3e-07) place ANA_0065 in the BTAD family which is described as Bacterial transcriptional activator domain.","","regulator, LuxR family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0066","74427","73594","834","8.48","2.60","29797","ATGACCGTCCCCACCACCGCGACCGCACCGACCAGTAGCTCCCTCTCCCCCGGCGTCTGGCGTTTCAGCGAGGCCCGGATCGTCCCGGACACCCTGACCATGGCCTGGCGCTCACTCATCACCATGATGCGCAACCCCGGGGAGTTCTACGACATCCTCATCCAGCCGGTCATGTTCACTGTCCTGTTCGGCGAGCTCTTCGGCGGCGCCATCGCCGGCGACGTCAAGGCCTACCTGCCCACGATCGTTCCGGGTCTCATCATCATGAATGCCTTGACCACGAGCCAGAGCGTGGGCGTGGACCTGCGCGAGGACATGGACAAGGGCGTCTTCGACCGCTTCCGCACCATGCCGATGTCCCGTATCGCGCCGGTCCTGGGGCCCATGGTCTCCGACGTGCTGCGTTACCTCATCTGCACCTCACTGACCGTACTCACCGGCTACATCCTGGGCTACCGGCCTGCCAACGGCTGGTCGGGAACGATTGGCGCCATCGCCCTGGCGGCGGGCTGCGCCTGGGCCATCGCCTGGATCTTCCTCTTCCTGGGGACGGTGTTCTCCTCGGCCCAAGCGGTCACTTCCTTCACGGTGATCGTCCTGTTCCCGCTGACCTTCCTGTCCAACGCCATGGTGCCCACCTCGACGCTACCGGGCTGGCTCAAGGCCTTCGTGCACCACAACCCGGTCTCGCACATCGTCGACGGCGACCGGTACCTGCTGGACGGAACAGCGGGCTCGGCCGGGGACGTACGGGCCGCGATCATCGGTTCACTCCTGATCCTGGCCGTCATGGCTCCCCTGACGGTCGTGCGCTACCAGCGGCGCAACGCCTGA","MTVPTTATAPTSSSLSPGVWRFSEARIVPDTLTMAWRSLITMMRNPGEFYDILIQPVMFTVLFGELFGGAIAGDVKAYLPTIVPGLIIMNALTTSQSVGVDLREDMDKGVFDRFRTMPMSRIAPVLGPMVSDVLRYLICTSLTVLTGYILGYRPANGWSGTIGAIALAAGCAWAIAWIFLFLGTVFSSAQAVTSFTVIVLFPLTFLSNAMVPTSTLPGWLKAFVHHNPVSHIVDGDRYLLDGTAGSAGDVRAAIIGSLLILAVMAPLTVVRYQRRNA$","Daunorubicin resistance ABC transporter, permease component","Membrane, Cytoplasm","ABC transporter, permease protein","K01992 ABC-2 type transport system permease protein","ABC-2 type transporter","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR000412
Family

ABC-2
PS51012	$\"[47-275]T$	ABC_TM2

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[29-235]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
tmhmm	$\"[52-72]?$ $\"[78-100]?$ $\"[133-151]?$ $\"[161-181]?$ $\"[191-211]?$ $\"[250-270]?$	transmembrane_regions

","BeTs to 15 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","***** IPB000412 (ABC transporter, family 2) with a combined E-value of 9.6e-17. IPB000412A 42-65 IPB000412C 202-242","Residues 37-85 are similar to a (TRANSMEMBRANE ABC TRANSPORTER PERMEASE MEMBRANE COMPONENT EFFLUX ABC-TRANSPORTER MULTIDRUG RESISTANCE) protein domain (PD207291) which is seen in Q88VX2_LACPL.Residues 37-275 are 41% similar to a (DRRB RESISTANCE MEMBRANE PROBABLE ABC INTEGRAL DAUNORUBICIN-DIM-TRANSPORT ANTIBIOTIC TRANSPORTER DAUNORUBICIN) protein domain (PD601649) which is seen in Q9XCF8_MYCAV.Residues 86-160 are similar to a (ABC PERMEASE TRANSPORTER MEMBRANE ATP-BINDING TRANSPORTER TRANSMEMBRANE PROTEIN COMPONENT INTEGRAL) protein domain (PD115342) which is seen in O86917_STRRO.Residues 179-275 are 53% similar to a (TRANSMEMBRANE ABC-TRANSPORTER COMPONENT) protein domain (PD986170) which is seen in Q6R7P4_STRRM.Residues 198-274 are similar to a (ABC PERMEASE TRANSPORTER MEMBRANE TRANSMEMBRANE ATP-BINDING TRANSPORTER INTEGRAL COMPONENT MULTIDRUG) protein domain (PD000633) which is seen in Q82EG1_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 29 to 241 (E_value = 1.8e-26) place ANA_0066 in the ABC2_membrane family which is described as ABC-2 type transporter.","","transporter, permease protein (permease)","","1","","","","","","","","","","","Mon Aug 13 09:26:20 2007","","Mon Aug 13 09:17:55 2007","","","Mon Aug 13 09:17:55 2007","Mon Aug 13 09:17:55 2007","Mon Aug 13 09:17:55 2007","","Mon Aug 13 09:17:55 2007","Mon Aug 13 09:17:55 2007","","","","","yes","","" "ANA_0067","75524","74424","1101","6.13","-3.55","38499","GTGAAACCGCCGGGGTCCAGCCTTGGCGGCATGGCAACACGAACAGCAAACGAATCGCTCTCACCGGGCGAGGCACCGGCCATCAGGACCGATGGCCTGACCCGCACCTTCGGCTCCTTCACCGCCGTCGACCGCCTGGACCTGGAGATCCCCACCGGCATCGTCTACGGCCTGCTCGGCCCCAACGGTGCCGGCAAGTCGACGGCGCTGCGCATGATCACCACCCTGTTGGCCCCCACCCGGGGCCGGGCGATGGTCCTGGGGCACGACGTCGTCCGCGAGCGCCACGCGGTGCGCAGCCTCATCGGGGTGACGGGACAGTACGCCAGCGTCGATGAGACGCTCACCGGCTCGGAGAACCTGCGCCTCTTCGGGCGTCTTCTGGGCCTTGGCCGGCGTCGGGCGCGGGAGCGGGCCGAGGAGCTGCTGGCCGCCTTCAGCCTGACCGAGGCAGGCGGCAAGCGGGTGAGCGGTTACTCCGGTGGGATGCGGCGGCGACTGGACCTGGCGGTCTCGCTCATCTCCCGTCCCCCGCTCATCTTCCTCGACGAGCCCACCACTGGTCTGGACCCGCGTACGCGTGAGCAGATGTGGGACGTCATCCGTTCCCTGGTGGAGGGCGGCTCGACGATCCTGCTGACCACTCAGTACCTGGAGGAGGCCGACCGTCTGGCTCACCGGGTCGGCATCATCGATGCCGGACGGCTCATCGCCGAGGGCACCCCCGATGAGCTCAAGGACCGGGTGGGCAGCAGCTCTCTGGTGCTAACCCCGGCGACCCCCGAGGACCAGGGGGCCACCGCGGCGATCATCGAGCGGGTGACCGGTCACGCCCCGGCGACTGTCGACCAGGGCACCCACCTGCAGGCGCCGCTGAGCGAGGCCTCGGTGGCCACCGAGGTGCTCGTGGCCCTACGCGACGCCGGATTGTCGCCCAGAACCGTCTCGGTGGACCGCCCCAGCATGGACTCGGTCTTCATGGCCCTGACCGGGCAACCCACGAAGCACGATGACGCGGCCTCACCCGATGCCGCCGCGCCGTCGGCGCCATCACCCGCTTCCTCGTCCTCCCGTCCCGCAGACTCTCAGGAGCAGTCATGA","VKPPGSSLGGMATRTANESLSPGEAPAIRTDGLTRTFGSFTAVDRLDLEIPTGIVYGLLGPNGAGKSTALRMITTLLAPTRGRAMVLGHDVVRERHAVRSLIGVTGQYASVDETLTGSENLRLFGRLLGLGRRRARERAEELLAAFSLTEAGGKRVSGYSGGMRRRLDLAVSLISRPPLIFLDEPTTGLDPRTREQMWDVIRSLVEGGSTILLTTQYLEEADRLAHRVGIIDAGRLIAEGTPDELKDRVGSSSLVLTPATPEDQGATAAIIERVTGHAPATVDQGTHLQAPLSEASVATEVLVALRDAGLSPRTVSVDRPSMDSVFMALTGQPTKHDDAASPDAAAPSAPSPASSSSRPADSQEQS$","Daunorubicin resistance ABC transporter, ATPase subunit","Membrane, Periplasm","AcrV","K01990 ABC-2 type transport system ATP-binding protein","daunorubicin resistance ABC transporter ATPase subunit","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[159-201]T$	Q88VX1_LACPL_Q88VX1;
PF00005	$\"[53-234]T$	ABC_tran
PS50893	$\"[28-258]T$	ABC_TRANSPORTER_2
PS00211	$\"[159-173]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[52-234]T$	AAA

InterPro
IPR005894
Family

Daunorubicin resistance ABC transporter ATP-binding subunit
TIGR01188	$\"[35-331]T$	drrA: daunorubicin resistance ABC transport

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[22-259]T$	no description
PTHR19222	$\"[28-255]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[28-255]T$	ABC TRANSPORTER

","BeTs to 17 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1e-20. IPB005074C 42-89 IPB005074D 147-190***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 6.4e-20. IPB013563A 42-76 IPB013563C 156-183 IPB013563D 210-262***** IPB005116 (TOBE domain) with a combined E-value of 2.1e-09. IPB005116A 60-76 IPB005116D 179-198***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.3e-08. IPB010509B 53-78 IPB010509D 154-198***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.2e-06. IPB010929K 40-84 IPB010929M 156-202***** IPB013283 (ABC transporter family E signature) with a combined E-value of 4.1e-06. IPB013283D 57-82","Residues 17-245 are 40% similar to a (GLP_38_64512_71054 ATP-BINDING) protein domain (PDA0H565) which is seen in Q7R1F8_EEEEE.Residues 26-115 are 55% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 26-96 are 56% similar to a (SYSTEM COMPONENT ABC-TYPE ATPASE ATP-BINDING MULTIDRUG) protein domain (PDA185O4) which is seen in Q82VH1_NITEU.Residues 36-89 are 66% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 38-262 are 45% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 42-231 are 50% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 43-91 are 77% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in DRRA_STRPE.Residues 57-246 are 48% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 147-245 are 52% similar to a (GLP_170_16420_13880 ATP-BINDING) protein domain (PDA0Z2E6) which is seen in Q7R6S2_EEEEE.Residues 147-231 are 61% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18641) which is seen in Q8EG59_SHEON.Residues 147-255 are 55% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 148-214 are 51% similar to a (TRANSPORT-LIKE ABC-TYPE ATP-BINDING) protein domain (PD272299) which is seen in Q9STU0_ARATH.Residues 154-249 are 63% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 156-236 are 56% similar to a (ATP-BINDING SUGAR ABC TRANSPORTER) protein domain (PDA0I778) which is seen in Q98JJ1_RHILO.Residues 156-237 are 58% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 157-247 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 159-201 are similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q88VX1_LACPL.Residues 160-239 are 61% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 164-225 are 69% similar to a (AMV130) protein domain (PD706071) which is seen in Q9EMR9_AMEPV.Residues 217-250 are 82% similar to a (ATP-BINDING ABC TRANSPORTER CASSETTE TRANSPORTER MEMBER SUB-FAMILY A COMPONENT ABC-TYPE) protein domain (PD000174) which is seen in Q7NIL6_GLOVI.","","-50% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 2.7E_28);-47% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 1.3E_19);-47% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 1.3E_19);-49% similar to PDB:1JI0 Crystal Structure Analysis of the ABC transporter from Thermotoga maritima (E_value = 3.0E_19);-43% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 2.5E_18);","Residues 53 to 234 (E_value = 1.9e-50) place ANA_0067 in the ABC_tran family which is described as ABC transporter.","","(drrA) ","","1","","","","","","","","","","","Mon Aug 13 09:25:45 2007","","Mon Aug 13 09:17:14 2007","","","Mon Aug 13 09:17:14 2007","Mon Aug 13 09:17:14 2007","Mon Aug 13 09:17:14 2007","","Mon Aug 13 09:17:14 2007","Mon Aug 13 09:17:14 2007","","","","","yes","","" "ANA_0068","76590","75553","1038","8.34","5.47","38285","ATGACAACCCAGGCAACACCTACAGATCCCATGAACGTCCTCGTCGTCGGTCTGGGGGTGATCGGGACGACGTACGGATACCTCTTTCAGAAGGCCGGTCACCACGTCGAGCACCTGGTGCGACAAAGCAGCACGAGGGCCTCAGTCAGCTCGCTCGAGGTCGAGATCCTCGATGGCAGGCGTGACCCGAAAAGTTCGCTGTCCCAGGACCAGTACACCGTTCACCACCGGGGACACACGAGCTACGACCTCATCGTGGTCTCAGTGCCGCAGGGCAGGATCGCCGAGGCAATGGCCGACCTCCGTACGGGTGGGATCGAGGGACCTGTGCTTCTATTCTGCGGGTTCTGGGGAGAACGCGAGGAGCTCGACCGTTTGATGGCCGGCCGCGATGTCCTCCTGGGGTACCCGGTGGCGGGCGGGAACATCACGGGAGAACGGCTCGCTTGCTGCGTCTTCGACTACGTCATGCTGGAGCGGCGCGACAAAGCCCGTTTCCCGGGCTACGAGAGGGTGGAGGCGCTGTTCGGCTCCTGCGGTGTCGGCTTCGAGAGCCCCCATGACATGCTCGAGTGGATCTGGCTGCATATGGCGATCAACGCCGGCGTCGGTGCCGTGGCAGCAATGTACGGCGACGTCGAGGACACGGCGCGCGCCGCCGAGCAGCTCATGGGCTCTACCAGGATGCTCGCCCGGGTGGTCAAAGCGATCCGGGAAACATCGAGGATCGTGGCCTCGCGCGGCGTTGATCTGAGGCGCTACCGCAGCGAGATGCTCGCCTACCGGCTGCCGACCGCCGTGTCCGCGCCCCTCATGAAGCGGATGTTCGCCAGGAATCTTCTCACCCGACGGATCATGACGCTGCATGGCAACACCGCTGACCTGTTGTTCGTGTGCCGGACCGTCTACGAGCAGGGCCGGGCCAACGGCGTCTCTGCTCCCATCTTCTACAGAAGCTACGAGGCGGCCCAAGACAAGGCCACCCGCCACGATCTGCACCTACCTGGCATGGTCCGTGGACGGAACGAAACGGCGTGA","MTTQATPTDPMNVLVVGLGVIGTTYGYLFQKAGHHVEHLVRQSSTRASVSSLEVEILDGRRDPKSSLSQDQYTVHHRGHTSYDLIVVSVPQGRIAEAMADLRTGGIEGPVLLFCGFWGEREELDRLMAGRDVLLGYPVAGGNITGERLACCVFDYVMLERRDKARFPGYERVEALFGSCGVGFESPHDMLEWIWLHMAINAGVGAVAAMYGDVEDTARAAEQLMGSTRMLARVVKAIRETSRIVASRGVDLRRYRSEMLAYRLPTAVSAPLMKRMFARNLLTRRIMTLHGNTADLLFVCRTVYEQGRANGVSAPIFYRSYEAAQDKATRHDLHLPGMVRGRNETA$","Ketopantoate reductase ApbA/PanE, N-terminal domain protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","Ketopantoate reductase ApbA/PanE, N-terminal domain protein","","Frodyma M.E., Downs D. ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway. J. Biol. Chem. 1998. 273(10):5572-5576. PMID: 9488683Frodyma M.E., Downs D. The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium. J. Bacteriol. 1998. 180(17):4757-4759. PMID: 9721324","","","

InterPro
IPR013332
Domain

Ketopantoate reductase ApbA/PanE, N-terminal
PF02558	$\"[13-163]T$	ApbA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[11-102]T$	no description
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[10-29]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 29-314 are similar to a (KETOPANTOATE SMU.296 HYDROLASE REDUCTASE GDSL POSSIBLE FAMILY PANE/APBA LIPASE/ACYLHYDROLASE) protein domain (PD568093) which is seen in Q8DVZ6_STRMU.","","-63% similar to PDB:2H12 Structure of Acetobacter aceti citrate synthase complexed with oxaloacetate and carboxymethyldethia coenzyme A (CMX) (E_value = );","Residues 13 to 163 (E_value = 0.00048) place ANA_0068 in the ApbA family which is described as Ketopantoate reductase PanE/ApbA.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0069","76638","76772","135","9.32","2.37","4635","GTGCTCAAGGTCCGCTCAGGACTTGCGCCGCAGGACCCGGCTCATGCGGTGCTCGGCGTCCTTGGCCGGGACCAGGGCTGCCCGCCCCGGGAAGGTCATCAGATCAGGATCGGTGAAGGGCGGGTTCTGGTGTGA","VLKVRSGLAPQDPAHAVLGVLGRDQGCPPREGHQIRIGEGRVLV$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0069.1","77328","78404","1077","7.51","3.21","40100","GTGCTGATAATCATTTGCGCCGTGCTTGGCCTGCTTGGGGGAGGTGTGACTTATTATGCTCATCGAAATATGACCTATGATCGGGCAGCGGAGGCGGTTGTTCGTCGTGCTGGTTTTGTTGAAAGGCGTGTAACGTTGCCGAGCGGCGCAATCATTCACTATGGTGAGGGACCGAACAATGGTTCACCGCTTATGTTGGTTCACGGTCAGCAAACAACGTGGAGGGACTATAGTGCGGTGCTTGGAGAGCTATCTCAACGCTATCACGTGTTTGCGGTCGACTGTTATGGCCATGGTGGATCGAGTAAAAATCCGGCAGATTATACGGCGATCAAGAATGCGATTGATTTCGTGTGGTTTATCCAGCACGTTGTCAAGTCTCCAGTCTTGATCTCCGGTCACTCTTCGGGAGGTCTGTTGGCGACCATCGTTGCCGCCAAGGCTCCACAGCTTGTCACTGGCTTATTGATTGAGGATGCACCATTCTTTGCGACTGAACCTGGAAGGGCCGAGAAGACATTTGCCTGGCTCGGGTTTCGTGACATGCATCATTTCTTGCACGGTGGTGAACGAAATTTCACCCGCTACTCGCTTGAGCACACCTATCTTGCGCAGGTTCTTGGGAAAAAGAACTTTGATGTGTTTGTTAAGCGGCCTGCCCTCGATTACATGAGGCGTCATCCTGGCGAAATACCGCGTCTTTGGTACTACCCTCCTGAGCTGCATGTCAATGAGTTCTTCGACTTGACGGCGAACTTGCAGGATGGTACGGGCGCTTATGATTTACGATTTGGTGAGACCTTCTATGATTTCTCGTGGTTTGCTGGTTTTAATCAGGCGGAAACACTGAAGGCTGTTCGCTGTCCGTCAATTCTTTTGCATGCTGCTCATCCGTCGAATATGCGGGGCTACTATGATGATCGTGGGGTACTGCTCGGTGCTATGGATGATCGTGACGCGTCGCGTGTCCACTCGCTTCTCTCTCGTAACACTCTAGTCGACAACGTTAAAAGTGGTCATAATATTCATTCTGAACGGCCTGAGGTTTTTATCAAGGCCGTCGATGATCTTCGTTAA","VLIIICAVLGLLGGGVTYYAHRNMTYDRAAEAVVRRAGFVERRVTLPSGAIIHYGEGPNNGSPLMLVHGQQTTWRDYSAVLGELSQRYHVFAVDCYGHGGSSKNPADYTAIKNAIDFVWFIQHVVKSPVLISGHSSGGLLATIVAAKAPQLVTGLLIEDAPFFATEPGRAEKTFAWLGFRDMHHFLHGGERNFTRYSLEHTYLAQVLGKKNFDVFVKRPALDYMRRHPGEIPRLWYYPPELHVNEFFDLTANLQDGTGAYDLRFGETFYDFSWFAGFNQAETLKAVRCPSILLHAAHPSNMRGYYDDRGVLLGAMDDRDASRVHSLLSRNTLVDNVKSGHNIHSERPEVFIKAVDDLR$","Hydrolase, alpha/beta fold family","Cytoplasm","","","","","","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[88-356]T$	Abhydrolase_1

InterPro
IPR008262
Active_site

Lipase, active site
PS00120	$\"[129-138]?$	LIPASE_SER

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[48-356]T$	no description
PTHR10992	$\"[64-166]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF14	$\"[64-166]T$	HYDROLASE
signalp	$\"[1-17]?$	signal-peptide

","BeTs to 15 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: RThe phylogenetic pattern of COG0596 is A---Yq-CEBR-ujgp----XNumber of proteins in this genome belonging to this COG is","***** IPB000639 (Epoxide hydrolase signature) with a combined E-value of 1.9e-07. IPB000639B 87-102 IPB000639F 335-357","Residues 22-159 are 46% similar to a (HYDROLASE ALPHA/BETA FOLD HYDROLASE FAMILY) protein domain (PD461356) which is seen in Q9ABK4_CAUCR.Residues 37-161 are 46% similar to a (MLR4436) protein domain (PD785445) which is seen in Q98E28_RHILO.Residues 39-166 are 45% similar to a (HYDROLASE) protein domain (PD757072) which is seen in Q988D4_RHILO.Residues 41-160 are 47% similar to a (MGC53864) protein domain (PD776028) which is seen in Q7ZX97_XENLA.Residues 43-177 are 45% similar to a (HALOALKANE DEHALOGENASE) protein domain (PD543118) which is seen in Q8Z0A5_ANASP.Residues 50-159 are 50% similar to a (HYDROLASE BLR7809 BLR7810 PROBABLE) protein domain (PD701794) which is seen in Q89CI7_BRAJA.Residues 50-157 are 50% similar to a (ACETYLTRANSFERASE-RELATED TRANSFERASE DIHYDROLIPOAMIDE) protein domain (PD634669) which is seen in Q9RUN2_DEIRA.Residues 52-105 are 59% similar to a (HYDROLASE ACYLTRANSFERASE OR TRANSFERASE) protein domain (PD494800) which is seen in Q8DUB4_STRMU.Residues 57-149 are 50% similar to a (BACTERIOCHLOROPHYLL PHOTOSYNTHESIS IX MG-PROTOPORPHYRIN SUBUNIT BIOSYNTHESIS CHELATASE LIGASE MAGNESIUM-CHELATASE) protein domain (PD775195) which is seen in BCHO_RHOCA.Residues 61-167 are 50% similar to a (ALL2761) protein domain (PDA1A256) which is seen in Q8YTF6_ANASP.Residues 63-161 are 60% similar to a (HYDROLASE ALPHA/BETA ENOL-LACTONE FOLD PEROXIDASE HYDROLASE FAMILY AMINOPEPTIDASE 3-OXOADIPATE BETA-KETOADIPATE) protein domain (PD036710) which is seen in Q8YNE1_ANASP.Residues 158-354 are 60% similar to a (HYDROLASE ACYLTRANSFERASE OR ALPHA/BETA FOLD TRANSFERASE HYDROLASE FAMILY) protein domain (PD824331) which is seen in Q73QV0_TREDE.","","","Residues 88 to 356 (E_value = 1.7e-06) place ANA_0069.1 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold. Residues 6 to 60 (E_value = 1.2e-15) place ANA_0069.2 in the HTH_3 family which is described as Helix-turn-helix.","","","","1","","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:31:12 2007","Fri Aug 10 09:31:12 2007","Fri Aug 10 09:31:12 2007","Fri Aug 10 09:30:27 2007","","","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","Fri Aug 10 09:30:27 2007","","Fri Aug 10 09:30:27 2007","","Fri Aug 10 09:30:27 2007","yes","","" "ANA_0069.2","76871","77311","441","8.18","1.64","16045","ATGATTAGTAGTAACATCGCCGCCTTGCGTAAAAAGCGTCGCTGGACTCAGGAAGCATTGGCAAACAAGGTTGGTGTCTCTCGGCAGACCATTGCCAAGTGGGAGGCTCCGGGTGGTAATCCCGACATTTCCTCATGTATCCGGTTAGCGCAGGCGTTCGATGTTGCGATCGACGATCTTGTCAACGGCGACACTTCATTTGTTTCCATGCTTGATCGCCCCGGCAAATACATATTTGGCACCGTTGTGATCGATCAGGATGGGAGGCTCACGCTTCCAGTGCGAGCCAGAAAGGTATTCAATATCAAGTCTGGCGACGAGCTCCTACTTATTGGCGACATCGATCAGGGGCTCGCTTTGATGGATGCGCAGTTCTTTGTGCAGGCTGCTCGTCACGTGGAGGGAGATCATCGTGCGGCACATGATAATACTAAAAACTAA","MISSNIAALRKKRRWTQEALANKVGVSRQTIAKWEAPGGNPDISSCIRLAQAFDVAIDDLVNGDTSFVSMLDRPGKYIFGTVVIDQDGRLTLPVRARKVFNIKSGDELLLIGDIDQGLALMDAQFFVQAARHVEGDHRAAHDNTKN$","Transcriptional regulator","Cytoplasm","","","","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[6-60]T$	HTH_3
SM00530	$\"[5-60]T$	HTH_XRE
PS50943	$\"[6-60]T$	HTH_CROC1

InterPro
IPR006339
Domain

Transcriptional regulator AbrB
TIGR01439	$\"[81-124]T$	lp_hng_hel_AbrB: transcriptional regulator,

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[1-64]T$	no description

","BeTs to 9 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1396 is --T--qV-EBR---------xNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","Residues 6 to 60 (E_value = 1.2e-15) place ANA_0069.2 in the HTH_3 family which is described as Helix-turn-helix.","","","","1","","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:58 2007","Fri Aug 10 09:35:58 2007","Fri Aug 10 09:35:58 2007","Fri Aug 10 09:35:16 2007","","","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","Fri Aug 10 09:35:16 2007","","Fri Aug 10 09:35:16 2007","","Fri Aug 10 09:35:16 2007","yes","","" "ANA_0070","79774","78797","978","5.59","-6.59","35664","GTGACATCCGAGCTGAGCGACCCAAGCGACCTGGGTATTCCGGGCGCCTCGCCCTACATCGAGCTGGACCGGGACCAGTGGTCCGCCCTGGCGTCCTCGGCGCCACTGCCGCTGACCCAGGCCGATGTCGAGAAGCTGCGGGGACTGGGCGACCCCATCGACCTGGCCGAGGTCGACGCCGTCTACCGGCCCCTGACCGCTCTGCTGGAGGACTACATCGCCACCTCGCGGGAGCGGGCGCACCGCACCGCCGCCTTCCTGGGGGTGAGCGAGCCGCCCACGCCCTTCATTGTCGCGGTGGCCGGGTCGGTCGCCGTGGGCAAGTCGACGACGGCGCGCCTCATCGCCCACTTGCTCGGCCGTTTCCCGGATACGCCCAGGGTGGACCTGGTGACCACCGACGGCTTCCTGCTGCCCAACCGGGTCCTTGAGGAGCGCGGACTCATGGCCCGCAAGGGATTCCCCGAGTCCTACGACCGTCGCGCCCTGCTGGAGTTCGTCGCGGCGGTGAAGTCCGGCAGCGAGTGCGTCCAGGCGCCCGTCTACTCCCACACGGTCTACGACATCGTCCCGGACCGGCACGTGACGGTGGAGCGCCCCGACATTCTCGTGCTGGAGGGACTCAACGTGCTCCAGCCCGCCCCGCGGGGGTCGCGGCCGGGGGCCTCGGCGCTGGCGGTGAGCGACTTCATCGACTTCTCGATCTACGTCGACGCCGACCCCGGCGACATCCGCCGCTGGTACCTGGACCGGTTCCTCACCCTCAAGCACACGGCCTTCACCCAGCCGGGCTCCTACTTCCGCCGCTTCGCCGAGATCCCCGACGACGTGGCCCTGGCTGGAGCAAACGAGATCTGGGAAAGCGTCAACCTGGTCAACCTGCGCGAGAACATCGCCCCCACCCGAGGGCGGGCCACCCTGGTCCTGACCAAGGACGCCGAGCACCGCATGAGCCGGGTCCTGCTGCGCAAGCCCTGA","VTSELSDPSDLGIPGASPYIELDRDQWSALASSAPLPLTQADVEKLRGLGDPIDLAEVDAVYRPLTALLEDYIATSRERAHRTAAFLGVSEPPTPFIVAVAGSVAVGKSTTARLIAHLLGRFPDTPRVDLVTTDGFLLPNRVLEERGLMARKGFPESYDRRALLEFVAAVKSGSECVQAPVYSHTVYDIVPDRHVTVERPDILVLEGLNVLQPAPRGSRPGASALAVSDFIDFSIYVDADPGDIRRWYLDRFLTLKHTAFTQPGSYFRRFAEIPDDVALAGANEIWESVNLVNLRENIAPTRGRATLVLTKDAEHRMSRVLLRKP$","Pantothenate kinase","Cytoplasm","Pantothenate kinase (Pantothenic acid kinase)","pantothenate kinase ","pantothenate kinase","","","","","

InterPro
IPR004566
Family

Bacterial pantothenate kinase
PIRSF000545	$\"[12-325]T$	Pantothenate kinase, bacterial type
TIGR00554	$\"[17-324]T$	panK_bact: pantothenate kinase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[16-324]T$	no description
PTHR10285	$\"[103-315]T$	URIDINE KINASE RELATED
PTHR10285:SF7	$\"[103-315]T$	PANTOTHENATE KINASE

","BeTs to 5 clades of COG1072COG name: Panthothenate kinaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1072 is ----------rlb-e-gh---j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 24-311 are 71% similar to a (KINASE TRANSFERASE ATP-BINDING PANTOTHENATE A COENZYME BIOSYNTHESIS PANTOTHENIC ACID PHOSPHORIBULOKINASE) protein domain (PD015803) which is seen in COAA_STRCO.Residues 134-205 are 58% similar to a (KINASE TRANSFERASE ATP-BINDING IPF477 CANDIDA YGGC PANTOTHENATE ALBICANS MLL4957 FRCK) protein domain (PD918076) which is seen in Q8UJ72_AGRT5.","","-62% similar to PDB:2GES Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-I (RT) (E_value = 4.3E_83);-62% similar to PDB:2GET Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-I (LT) (E_value = 4.3E_83);-62% similar to PDB:2GEU Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-II (RT) (E_value = 4.3E_83);-62% similar to PDB:2GEV Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-II (LT) (E_value = 4.3E_83);-67% similar to PDB:1ESM STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A (E_value = 4.1E_78);","No significant hits to the Pfam 21.0 database.","","kinase (Pantothenic acid kinase) (AE006212)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0071","79953","81857","1905","5.46","-21.75","67980","ATGTGTGGAATTGTCGGCCACGTCGGCCCTCCGAGTGAAACTGGTTCCTCCCGTTCCCTGACTGTTCTCATGGATGGCCTCGGCCGTCTGGAGTACCGCGGCTACGACTCTGCGGGCGTCGCGCTGGTGGGCCCCTCCGGCCTGGATGTCATCAAGGAGGCGGGCAAGCTCTCGGGGCTGCGCGCCATCCTTGAGGCCACCCCGCCGGCCCCCGCCACCGCGGGCATCGGCCACACCCGCTGGGCCACCCACGGCGGCCCGACGACGGCCAACGCCCACCCCCACCGCGCCGGCCACCTCGCCGTGGTCCACAACGGCATCATCGAGAACTTCCGCCCGCTGCGCGAGGAGGTCGAGGCCGCCGGGCGTGAGCTCGTCTCCGACACCGACACCGAGGTCGTCGCCCACGTCCTGGACATCGACTTCACCTCCCGTCTGCGCCAGGACCCGTCCGCCGCCTCCGACCCGACCCGGGTCGCCGACCTCCTGGTCGCCTCGATGCAGGCCGTCACCGCCCGCCTCGAGGGCGCCTTCGCGCTGCTGGCCGTCACCGACCTGGCCCCCGCGGCGATCGTCGCCGCCCGCCGCTCCAGCCCCCTGGTCATCGGCCTGGGCGAGGGCGAGAACTTCCTGGGCAGCGACGTCGCCGCCTTCGTCGCCTTCACCAAGAAGGCCGCCGAGGTCGACGACGACCAGGTCCTCCTGCTGACCGCCGACGCCGTCCACGTCTGGGACCAGGACGGCAAGACCGTCGAGCCCAAGACGTGGGAGGTCTCCTGGGACGCCTCCGCAGCCGTCAAGGGTGGCTACGACACCTTCATGGCCAAGGAGATCCACGAGCAGCCCACCGCCGTGGCCGACACCCTGCGCGGCCGCGTCGACGAGCGCGGTGAGCTCCAGCTCGACGAGATGCGCATCGACCCCGCCGTTCTGCGCAGCGTCGACAAGATCGTCGTCATCGCCTGCGGCACCGCCGCCTACGCCGGGCACGTCGCCAAGTACGCCATCGAGCACTGGTGCCGTATCCCCGTGGAGGTCGAGCTCGCCCACGAGTTCCGCTACCGCGACCCGGTCGTCAGCGAGAAGACCCTGACCGTGGCCATCTCCCAGTCCGGCGAGACCATGGACACGATCCAGGCCGTGCGTCACGCCCGCGAGCAGGGCAGCAAGGTCCTGGCCATTGTCAACACCTACGGCTCGACCATCGCCCGCGAGGCCGATGCCGTCCTCTACACCCATGCCGGCCCGGAGGTCGCCGTGGCCTCCACCAAGGCCTTCCTCGCCCAGATCACCGCCTGCTACCTGCTGGGGCTCTACCTGGCCCAGCTGCGTGGCAACAAGTGGCCCGACGAGGTCGCCGAGTACCTGGACAACCTCGCCGCCATGCCGGACCGCATCCAGCACGTCCTGGACCATGAGGAGACTCGCGTGCGTGAGCTGGGCACCGAGCTGGCGGACAAGTCCTCCTTCCTGTTCCTGGGCCGCCACGTCGGCTTCCCGGTGGCGCTGGAAGGGGCGCTCAAGCTCAAGGAGCTCGCCTACGTCCACGCGGAGGGCTTCGCCGCCGGTGAGCTCAAGCACGGCCCGATCGCGCTCATCGAGGAGGGCCTTCCGGTCTTCGTCATCGTGCCCACCCCGCGCCGCCCCGTCCTGCACGACAAGGTCATCTCCAACATCCAGGAGATCCGGGCCCGTGGCGCGCGCACCATCGTCATCGCGGAGGAGGGGGATACCGACGTCGAGCCCTTCGCCGACCACATCATCCGGGTGCCCGCCACCCCCACGATCCTGTGGCCGCTGCTGACCGTGGTCCCGCTGCAGATCTTCGCCGCGGCCCTGGCCGGGGCCAAGGGGCTGGACATCGACCAGCCGCGCAACCTGGCCAAGTCCGTCACCGTCGAGTAG","MCGIVGHVGPPSETGSSRSLTVLMDGLGRLEYRGYDSAGVALVGPSGLDVIKEAGKLSGLRAILEATPPAPATAGIGHTRWATHGGPTTANAHPHRAGHLAVVHNGIIENFRPLREEVEAAGRELVSDTDTEVVAHVLDIDFTSRLRQDPSAASDPTRVADLLVASMQAVTARLEGAFALLAVTDLAPAAIVAARRSSPLVIGLGEGENFLGSDVAAFVAFTKKAAEVDDDQVLLLTADAVHVWDQDGKTVEPKTWEVSWDASAAVKGGYDTFMAKEIHEQPTAVADTLRGRVDERGELQLDEMRIDPAVLRSVDKIVVIACGTAAYAGHVAKYAIEHWCRIPVEVELAHEFRYRDPVVSEKTLTVAISQSGETMDTIQAVRHAREQGSKVLAIVNTYGSTIAREADAVLYTHAGPEVAVASTKAFLAQITACYLLGLYLAQLRGNKWPDEVAEYLDNLAAMPDRIQHVLDHEETRVRELGTELADKSSFLFLGRHVGFPVALEGALKLKELAYVHAEGFAAGELKHGPIALIEEGLPVFVIVPTPRRPVLHDKVISNIQEIRARGARTIVIAEEGDTDVEPFADHIIRVPATPTILWPLLTVVPLQIFAAALAGAKGLDIDQPRNLAKSVTVE$","Glucosamine--fructose-6-phosphate aminotransferase, isomerizing","Cytoplasm","glucosamine--fructose-6-phosphateaminotransferase, isomerizing","D-fructose-6-phosphate amidotransferase ","glucosamine--fructose-6-phosphate aminotransferase, isomerizing","","Buchanan J.M. The amidotransferases. Adv. Enzymol. Relat. Areas Mol. Biol. 1973. 39:91-183. PMID: 4355768Weng M.L., Zalkin H. Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. J. Bacteriol. 1987. 169(7):3023-3028. PMID: 3298209Nyunoya H., Lusty C.J. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. J. Biol. Chem. 1984. 259(15):9790-9798. PMID: 6086650","","","

InterPro
IPR000583
Domain

Glutamine amidotransferase, class-II
PF00310	$\"[2-215]T$	GATase_2
PS00443	$\"[1-6]?$	GATASE_TYPE_II

InterPro
IPR001347
Domain

Sugar isomerase (SIS)
PF01380	$\"[310-442]T$ $\"[483-620]T$	SIS

InterPro
IPR005855
Family

Glucosamine-fructose-6-phosphate aminotransferase, isomerising
TIGR01135	$\"[2-634]T$	glmS: glucosamine--fructose-6-phosphate ami

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.10490	$\"[263-482]T$	no description
G3DSA:3.60.20.10	$\"[2-262]T$	no description
PTHR10937	$\"[2-634]T$	GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE

","BeTs to 23 clades of COG0449COG name: Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domainsFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0449 is -ompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB000583 (Glutamine amidotransferase, class-II) with a combined E-value of 1.9e-118. IPB000583A 2-9 IPB000583B 27-40 IPB000583C 75-94 IPB000583D 100-134 IPB000583E 273-282 IPB000583F 368-378 IPB000583G 400-429 IPB000583H 510-528 IPB000583I 607-634***** IPB001347 (Sugar isomerase (SIS)) with a combined E-value of 2.1e-16. IPB001347A 75-85 IPB001347B 363-388***** IPB000281 (Helix-turn-helix protein RpiR) with a combined E-value of 1e-08. IPB000281B 348-395","Residues 1-60 are 71% similar to a (AMINOTRANSFERASE AMIDOTRANSFERASE TRANSFERASE GLYCOSYLTRANSFERASE GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMIDOPHOSPHORIBOSYLTRANSFERASE ISOMERIZING GFAT HEXOSEPHOSPHATE PHOSPHATE) protein domain (PD001242) which is seen in Q72HF4_THET2.Residues 102-195 are 60% similar to a (AMINOTRANSFERASE AMIDOTRANSFERASE ASPARAGINE TRANSFERASE SYNTHETASE GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE ISOMERIZING GLUTAMINE GLYCOSYLTRANSFERASE GFAT) protein domain (PD000635) which is seen in GLMS_STRCO.Residues 199-273 are 81% similar to a (AMINOTRANSFERASE AMIDOTRANSFERASE GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE ISOMERIZING GFAT HEXOSEPHOSPHATE PHOSPHATE D-FRUCTOSE-6- L-GLUTAMINE-D-FRUCTOSE-6-PHOSPHATE GLUCOSAMINE-6) protein domain (PD859000) which is seen in Q8G545_BIFLO.Residues 274-634 are 84% similar to a (AMINOTRANSFERASE AMIDOTRANSFERASE GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE ISOMERASE TRANSFERASE ISOMERIZING L-GLUTAMINE-D-FRUCTOSE-6-PHOSPHATE HEXOSEPHOSPHATE PHOSPHATE D-FRUCTOSE-6-) protein domain (PD002268) which is seen in Q6NG33_CORDI.","","-58% similar to PDB:1JXA GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE (E_value = 6.3E_119);-58% similar to PDB:2BPL E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P (E_value = 6.3E_119);-58% similar to PDB:2J6H E. COLI GLUCOSAMINE-6-P SYNTHASE IN COMPLEX WITH GLUCOSE-6P AND 5-OXO-L-NORLEUCINE (E_value = 6.3E_119);-60% similar to PDB:1MOQ ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE (E_value = 1.7E_71);-60% similar to PDB:1MOR ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSE 6-PHOSPHATE (E_value = 1.7E_71);","Residues 2 to 215 (E_value = 4.8e-27) place ANA_0071 in the GATase_2 family which is described as Glutamine amidotransferases class-II.Residues 310 to 442 (E_value = 5.3e-39) place ANA_0071 in the SIS family which is described as SIS domain.Residues 483 to 620 (E_value = 1.9e-25) place ANA_0071 in the SIS family which is described as SIS domain.","","aminotransferase, isomerizing (glmS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0072","82602","81934","669","9.58","7.54","24009","TTGTCCTCCGCTCCGCTCTCCTCGCCCCTCCAACACGGCTTTGAGACGGGCAGTTTCACAGAGCAAGACCTCGCGGGTGGCCGCCGGCCCGCATTGCCCGTCCGCGGCCAAGCGCCAAGAAGTTGTCTCTTCCAGAATTGGTGGCGCGTTCACCCCTCGCGCTGCCCGCTCACCCGGCACAATGGCCGAGTGATCCGCGCTGTAGGGACCGACCTGGTTGATATCCCCCGCCTCGAAGGCTACATGGACCGGGTACCCGGCCTGCGCGAGCGGCTCTTCACCCCCGCCGAGCTGGCCGCCTGCCAGAAGCGGGCCGCCTCACTCGGGGCGCGCCTGGCGGCCAAGGAGGCGGTTCTCAAGGCCCTGGGGTCGGCCTACGCCGAGCTCGGGCTGGACGCGCCCCAGGGGTGGGAGTACCAGGACATCGAGGTGACCTCCACGCCCGGCACCCCACCGCGCCTGCGCCTGACCGGGGCGGCCGCGATGGCCGCCCGCCAGGCCGGCATCGGCCACTGGCACATCTCCCTGGCGCACGACGGCGGTATGGCCCAGGCCTTCGTCGTCGCCCAGGCCGACCACGTCGACAACGACGACGACCTGACCCTGTCCTCCCAGCGTTCACAGGCCCGCACGAAGCGGCAGATCAAGGCCTTGCGTCCCGCCCTGTAG","LSSAPLSSPLQHGFETGSFTEQDLAGGRRPALPVRGQAPRSCLFQNWWRVHPSRCPLTRHNGRVIRAVGTDLVDIPRLEGYMDRVPGLRERLFTPAELAACQKRAASLGARLAAKEAVLKALGSAYAELGLDAPQGWEYQDIEVTSTPGTPPRLRLTGAAAMAARQAGIGHWHISLAHDGGMAQAFVVAQADHVDNDDDLTLSSQRSQARTKRQIKALRPAL$","Holo-acyl-carrier-protein synthase","Cytoplasm, Periplasm","Holo-[acyl-carrier protein] synthase (Holo-ACPsynthase)(4'-phosphopantetheinyl transferase acpS)","holo-(acyl-carrier-protein) synthase ","holo-acyl-carrier-protein synthase","","Lambalot R.H., Walsh C.T. Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J. Biol. Chem. 1995. 270(42):24658-24661. PMID: 7559576Reuter K., Mofid M.R., Marahiel M.A., Ficner R. Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily. EMBO J. 1999. 18(23):6823-6831. PMID: 10581256","","","

InterPro
IPR002582
Family

Holo-acyl carrier protein synthase
TIGR00516	$\"[63-194]T$	acpS: holo-(acyl-carrier-protein) synthase

InterPro
IPR004568
Domain

Phosphopantethiene-protein transferase
PD004282	$\"[71-190]T$	Q74C71_GEOSL_Q74C71;
TIGR00556	$\"[64-192]T$	pantethn_trn: phosphopantethiene--protein t

InterPro
IPR008278
Domain

4'-phosphopantetheinyl transferase
PF01648	$\"[68-131]T$	ACPS

","No hits to the COGs database.","***** IPB008278 (4'-phosphopantetheinyl transferase) with a combined E-value of 6.9e-06. IPB008278A 68-77 IPB008278B 112-123","Residues 64-123 are 58% similar to a (SYNTHASE ACYL CARRIER) protein domain (PD981514) which is seen in Q6T711_SACER.Residues 71-190 are 50% similar to a (SYNTHASE TRANSFERASE HOLO-ACYL-CARRIER-PROTEIN HOLO-ACP FATTY ACID 4_apos;-PHOSPHOPANTETHEINYL SYNTHESIS MAGNESIUM BIOSYNTHESIS) protein domain (PD004282) which is seen in Q74C71_GEOSL.Residues 133-190 are 62% similar to a (SYNTHASE TRANSFERASE ACPS ACYL BIOSYNTHESIS HOLO-ACYL-CARRIER-PROTEIN ACID 4_apos;-PHOSPHOPANTETHEINYL LIPID FATTY) protein domain (PD698614) which is seen in ACPS_STRCO.","","-52% similar to PDB:2JBZ CRYSTAL STRUCTURE OF THE STREPTOMYCES COELICOLOR HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE (ACPS) IN COMPLEX WITH COENZYME A AT 1.6 A (E_value = 4.8E_18);-52% similar to PDB:2JCA CRYSTAL STRUCTURE OF THE STREPTOMYCES COELICOLOR HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE (ACPS) AT 2 A. (E_value = 4.8E_18);","Residues 68 to 131 (E_value = 8.3e-08) place ANA_0072 in the ACPS family which is described as 4'-phosphopantetheinyl transferase superfamily.","","protein] synthase (Holo-ACP synthase)(4-phosphopantetheinyl transferase acpS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0073","82731","84521","1791","6.80","-1.65","59189","ATGAGAGCCGCCGCCCACGCGGTGGCCCGGGCGGCGCTGCGCGAGCTGCGCCAAGGAACCGGCAATGCGGGCGCCGCGGTGGCCCCCGCCCGGCCGGTTCCGGCGCCGTTGACCTCGATGAGCCCCATGGGGGTGGCCGCCACCCCAGCCTCACCGCTGTCCCCGGCGACGCCGCTGGGAGGAGCAGGTGAGACGGCGGGGACGCAGACCGGCCCCGGATGGATCTCCGGGGCCCCGGTACTCCTCTTAGTCGGCGGCGGCCACAACGGGGCCGACACCCTCCTGGCTGGAGGTCTGCTCGCCCACAGCGGCTGCGCGGTCAGCGCCGTGCTCGCCACCGAGCACCCCCATCCCGTCGCCCTGGAGGAGGCCCGCGGCCACGGCGTCACCATTCACGGCGGCGGCTACCGCAGCGACGACGGAACCGGCCAGGACTCCGCCGAGGCCATGGCCGCTATCGAGGCCTTCCTCGTCCACGGCGGACTCGTCCTGGACGGACTGACCGGCATCGGCGCCACCGGGGCGCTGCGGCCCGACGCCGCCGCCCTCATCGCCCCGCTCATCGCCGCCGGGCAGCCGGGGCGTCGCCCGCTGCGCGTCATTGCCGTCGACCTGCCCAGCGGAACCGGCGTCGACGACGGCACGGTGGACGGTCCGGTCTTGGCCGCCGACCGTACCGTCACCTTCACCTGCCTCAAGGGGTGCCAGTGCCTGCCCCCGGCCCGGCACCTGTGTGGCGTCGTCGAGGTCGTCCCCCTCGGGCTGCCCGCGCCCACGAGCCGGCCCCTGGCCCGCCGCCCCGTCGACGGCGCCCTGGGCGACTACCTGACCCGCGCCGTTGGCGAGCCCGGCCCCGGCGACCACAAGTACACCCGCGGCGTGGTCGGCCTGTGGGCCAGCAGCGAGTCCTACCCCGGCGCCGCCGTCCTGGCCGCCAGCGGCGCGGTGCGCGCCGGCGCCGGCATGGTGCGCCTGTCCGCCCCCAGACGCGTGGAGGACCTCGTCCTGGCCGCCCGCCCCGAGGTGGTCCCCGCCGCCGGACGCGTTCAGGCGCTCGTCCTGGGGCCGGGCATCGACCCCGCTGACACCACCAGGGCCGATGAGGTGCGGACCGTACTCGCCTCCACCCTGGGTCCCTGCGGCAAAGACCGGCAGTGCCCCACCCGGATCCCCACCGTCGTCGACGCCGGCGCCCTGAGCATCCTGGCCCAGTTCCTCACCGAGGATCTGAGCTGCACGCCGCTGCACGTGCTGACCCCGCATGCCGGAGAGGCCGCCGCGCTGCTGAGCGCGCTGGAGGATCAGGGGACGCCGGCACAGAAGACTCGTCGCTGGAGCCGCGAGCGCGTCGAGGCCCACCCGGGGCTCGCCGCCCGCGAGATCTGCCGCCTCACCGGCGCCACCGTCCTGCTCAAAGGAGCCACCACCCTCATCGCCGCGCCGCAGCGCCCCCTGGTCAGTGTGGACGGAGGACCCGGTTGGATGGCGAGCGCCGGAAGCGGGGACGTGCTGGCCGGGATCCTCGGAGCCGTCCTGGCCGGCGCGACCGCCCGCTGGGAGCAGGGCGCGCCGGACGCCTCGGGGCCGGCCTCGGTCCTGGACGCGCTGGTCGACTCGGTGGCCGCCGGCGTCAGGCTGCACGCGCTCGCGGGGGCCTATGCCGCAGCAAGCCCGCAGAGCGCCGGGGGAGCGCGGACCGGCGGGTACCCGATCGCCGCCCTGGATATCGCCGCTGCCCTCGGTCCGGCCCGCCTCGAGCTCAACTGGCTCCAGGCGGTGCCCCACGCCTGA","MRAAAHAVARAALRELRQGTGNAGAAVAPARPVPAPLTSMSPMGVAATPASPLSPATPLGGAGETAGTQTGPGWISGAPVLLLVGGGHNGADTLLAGGLLAHSGCAVSAVLATEHPHPVALEEARGHGVTIHGGGYRSDDGTGQDSAEAMAAIEAFLVHGGLVLDGLTGIGATGALRPDAAALIAPLIAAGQPGRRPLRVIAVDLPSGTGVDDGTVDGPVLAADRTVTFTCLKGCQCLPPARHLCGVVEVVPLGLPAPTSRPLARRPVDGALGDYLTRAVGEPGPGDHKYTRGVVGLWASSESYPGAAVLAASGAVRAGAGMVRLSAPRRVEDLVLAARPEVVPAAGRVQALVLGPGIDPADTTRADEVRTVLASTLGPCGKDRQCPTRIPTVVDAGALSILAQFLTEDLSCTPLHVLTPHAGEAAALLSALEDQGTPAQKTRRWSRERVEAHPGLAAREICRLTGATVLLKGATTLIAAPQRPLVSVDGGPGWMASAGSGDVLAGILGAVLAGATARWEQGAPDASGPASVLDALVDSVAAGVRLHALAGAYAAASPQSAGGARTGGYPIAALDIAAALGPARLELNWLQAVPHA$","Predicted sugar kinase","Cytoplasm, Membrane","Predicted sugar kinase","hypothetical protein","protein of unknown function UPF0031","","","","","

InterPro
IPR000631
Domain

Carbohydrate kinase
PF01256	$\"[295-582]T$	Carb_kinase
PS01050	$\"[498-508]T$	UPF0031_2

InterPro
IPR004443
Domain

YjeF-related protein, N-terminal
PF03853	$\"[57-235]T$	YjeF_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[266-588]T$	no description
G3DSA:3.40.50.10260	$\"[75-249]T$	no description
PTHR12592	$\"[80-513]T$	UNCHARACTERIZED

","BeTs to 14 clades of COG0063COG name: Predicted sugar kinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0063 is aompkzyqvdrlbcefg-snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000631 (Protein of unknown function UPF0031) with a combined E-value of 1.3e-15. IPB000631A 288-307 IPB000631B 417-428 IPB000631C 498-508","Residues 75-269 are 43% similar to a (KINASE SUGAR YJEF UPF0031 PREDICTED FAMILY 5-PHOSPHATE OXIDASE CEREVISIAE YNL200C) protein domain (PD005835) which is seen in Q73S20_MYCPA.Residues 80-262 are 45% similar to a () protein domain (PD839765) which is seen in Q8G665_BIFLO.Residues 283-434 are 50% similar to a () protein domain (PDA1D1E9) which is seen in Q6ADB1_BBBBB.Residues 324-440 are 51% similar to a () protein domain (PD788587) which is seen in Q8G665_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 57 to 235 (E_value = 6.9e-09) place ANA_0073 in the YjeF_N family which is described as YjeF-related protein N-terminus.Residues 295 to 582 (E_value = 5.5e-17) place ANA_0073 in the Carb_kinase family which is described as Carbohydrate kinase.","","sugar kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0074","84616","85959","1344","5.58","-8.19","46050","GTGACCACCTCCTTGGACTCAGCCGCAATGCCCCCGTCCGCCGCTCCGCGCCCGGCAGTCGCCCAGTGCGCGCCACCGCCGGCGGCCACTACCTCGCGGGCCGTCGTCGACCTGGCGGCCGTGGCTCACAACGGGCGGCGCCTGGCACAGGTGGCGGGCGTGCCGTGGATGGCCGTGGTCAAGGCCGACGCCTACGGTCACGGGCTGGGGCCGGTCGCTCTGACCGCCCTGTCAGCAGGAGCCACCTGGCTGGGGGTGGCCCAGCTCGCCGAGGCCCTGAGTCTGCGTGCCCTTCTGGACGAGGCCGGTGTGAGACGCCCGGTGGGGGAGCCCACCTCGCAGGCCCCCCGGCTCCTCACCTGGCTCCTGCCCGTCATGGAGCCTGATCGGGCGGCCGCCGAGGACTCGCCACTGCGCGCCGCCCTGGCGGCCGACCTGGACCTGTCGGTCTCCACCCTGTACCAGCTCGAGGCCCTGTCGGCGGCGGCCCGGGCTCAGGGGAGGGCGGCGCGTCTCCACCTCAAGGTCGACACCGGCATGTCGCGCGGCGGCGCCACCGTCGAGGAGCTGCCCGCCCTGGCCGCCGCTCTGAAGCGGGCCGCGGATGAGGGAACGGTCGACGTCGTCGGCCTGTGGTCGCACCTCTCGCGCGCCGATGAGCCGGCCAGCGGCTCCACCGAGGAGCACCTGGAGCGCTACCGGCAGGCCGAGCAGGTCGTACGAGACGCCGGCCTCAATCCGCCCACTCACCACCTCGCTGCCACCGGAGGACTCCTGTGGCACCCGCAGGCCCGCATGGACCTGGTGCGTGTGGGGATCGGCCTGTACGGGCTGAGTCCCGACCCCGCCGTGGCCACCGGCGCCGAGCTCGGGCTGCGGCCCGCCATGCGCCTGGAGTCCCCGCTGGCGCAGGTCAAGCGCATCGAGGCCGGGCAGGCCGTCTCCTACGGGGGGACCTGGAGCGCCCCCACTGATCGCTGGGTGGGGCTCGTGCCCCTGGGCTACTCCGACGGCATCCCGCGCGCCGCCAGCTCCGCCGGTCCCGTGGGAGTCGGCAGCCTCATGACCTCCGTCGTGGGGCGCGTGTGCATGGACCAGGTGGTTATCGACCTCGGCCCGGCTGTGGACGAGACCGGCGCGCCCCTGCCGGCAGCGGCCCGGGTCGGGGACACCGCCGTGCTCTGGGGAGCCCCCGCGGTATCAGACCAGGAGGCCGTCCCCACCGCGGATGAGTGGGCGCAGGCCTGCGGCACCATCAACTACGAGATCGTGACCCGGTTGGGAGCTCGTGTCCCGCGCTGCTACGTCGGGGAATCCGGCACCGGCGACTACTCTCGACCCTAG","VTTSLDSAAMPPSAAPRPAVAQCAPPPAATTSRAVVDLAAVAHNGRRLAQVAGVPWMAVVKADAYGHGLGPVALTALSAGATWLGVAQLAEALSLRALLDEAGVRRPVGEPTSQAPRLLTWLLPVMEPDRAAAEDSPLRAALAADLDLSVSTLYQLEALSAAARAQGRAARLHLKVDTGMSRGGATVEELPALAAALKRAADEGTVDVVGLWSHLSRADEPASGSTEEHLERYRQAEQVVRDAGLNPPTHHLAATGGLLWHPQARMDLVRVGIGLYGLSPDPAVATGAELGLRPAMRLESPLAQVKRIEAGQAVSYGGTWSAPTDRWVGLVPLGYSDGIPRAASSAGPVGVGSLMTSVVGRVCMDQVVIDLGPAVDETGAPLPAAARVGDTAVLWGAPAVSDQEAVPTADEWAQACGTINYEIVTRLGARVPRCYVGESGTGDYSRP$","Alanine racemase","Cytoplasm, Membrane","alanine racemase","alanine racemase ","alanine racemase","","Whitchurch C.B., Hobbs M., Livingston S.P., Krishnapillai V., Mattick J.S. Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria. Gene 1991. 101(1):33-44. PMID: 1676385De Wergifosse P., Jacques B., Jonniaux J.L., Purnelle B., Skala J., Goffeau A. The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein. Yeast 1994. 10(11):1489-1496. PMID: 7871888Shaw J.P., Petsko G.A., Ringe D. Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Biochemistry 1997. 36(6):1329-1342. PMID: 9063881","","","

InterPro
IPR000821
Domain

Alanine racemase region
PR00992	$\"[53-69]T$ $\"[253-280]T$ $\"[311-326]T$ $\"[328-343]T$ $\"[349-366]T$	ALARACEMASE
TIGR00492	$\"[33-437]T$	alr: alanine racemase
PS00395	$\"[58-68]T$	ALANINE_RACEMASE

InterPro
IPR001608
Domain

Alanine racemase, N-terminal
PF01168	$\"[31-281]T$	Ala_racemase_N

InterPro
IPR011079
Domain

Alanine racemase, C-terminal
PF00842	$\"[295-436]T$	Ala_racemase_C

noIPR
unintegrated

unintegrated
G3DSA:2.40.37.10	$\"[282-435]T$	no description
G3DSA:3.20.20.10	$\"[25-275]T$	no description

","BeTs to 15 clades of COG0787COG name: Alanine racemaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0787 is -------q-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB011079 (Alanine racemase, C-terminal) with a combined E-value of 1.2e-70. IPB011079A 58-68 IPB011079B 80-107 IPB011079C 174-184 IPB011079D 210-222 IPB011079E 270-280 IPB011079F 311-341 IPB011079G 349-371 IPB011079H 409-435***** IPB000821 (Alanine racemase) with a combined E-value of 3.8e-61. IPB000821A 36-46 IPB000821B 58-68 IPB000821C 84-107 IPB000821D 174-184 IPB000821E 211-229 IPB000821F 254-280 IPB000821G 314-349 IPB000821H 357-371***** IPB001608 (Protein of unknown function UPF0001) with a combined E-value of 4e-21. IPB001608A 61-95 IPB001608C 172-185 IPB001608E 250-277","Residues 32-98 are 63% similar to a (RACEMASE PHOSPHATE ALANINE PYRIDOXAL ISOMERASE) protein domain (PD712392) which is seen in Q84IE4_BBBBB.Residues 32-97 are 70% similar to a (ALANINE ISOMERASE PHOSPHATE PYRIDOXAL RACEMASE WALL PEPTIDOGLYCAN SYNTHESIS CELL RACEMASE) protein domain (PD430024) which is seen in ALR_STRCO.Residues 174-262 are 49% similar to a (ISOMERASE ALANINE PHOSPHATE PYRIDOXAL RACEMASE WALL PEPTIDOGLYCAN SYNTHESIS CELL RACEMASE) protein domain (PD580546) which is seen in Q82DK9_STRAW.Residues 298-435 are 62% similar to a (ISOMERASE ALANINE PHOSPHATE PYRIDOXAL RACEMASE WALL SYNTHESIS CELL PEPTIDOGLYCAN RACEMASE) protein domain (PD003767) which is seen in ALR_STRCO.","","-50% similar to PDB:1VFH Crystal structure of alanine racemase from D-cycloserine producing Streptomyces lavendulae (E_value = 6.0E_65);-50% similar to PDB:1VFS Crystal structure of D-cycloserine-bound form of alanine racemase from D-cycloserine-producing Streptomyces lavendulae (E_value = 6.0E_65);-50% similar to PDB:1VFT Crystal structure of L-cycloserine-bound form of alanine racemase from D-cycloserine-producing Streptomyces lavendulae (E_value = 6.0E_65);-50% similar to PDB:1XFC The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site (E_value = 2.5E_55);-44% similar to PDB:1BD0 ALANINE RACEMASE COMPLEXED WITH ALANINE PHOSPHONATE (E_value = 7.6E_36);","Residues 31 to 281 (E_value = 5.1e-60) place ANA_0074 in the Ala_racemase_N family which is described as Alanine racemase, N-terminal domain.Residues 295 to 436 (E_value = 2.1e-50) place ANA_0074 in the Ala_racemase_C family which is described as Alanine racemase, C-terminal domain.","","racemase (alr)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0075","86040","86678","639","4.83","-11.85","21928","ATGAGCCCAGCGCCGCACACACCGCAGACCGCACCCGGGATCACCGTCGCCACCGGCGACGCCGACGAGACCCGGGCGCTGGGGGCCCGCCTGGCCCGCCTGCTGCGTGCCGGTGACCTCGTGATGCTCTCCGGGGGGCTGGGGGCCGGCAAGACCACGCTCGCCCAGGGCATCGGCGCAGCCCTCCAGGTGCGTGGCCGGGTCTCCTCACCCACCTTCATCATCGCCCGCGTGCATCCCGCCCTGTCCGACGGCCCCGACCTCATCCACGTGGACGCCTACCGGATCACCTCCCTGGAGGAGATCGACGCCCTCGACCTGGACTCCTCCCTGGAACGGGCCGTCACCCTGGTCGAGTGGGGCGAGGAGAAGGTGGAGGCCCTGAGCCCCGACCGCCTGGAGATCCAGGTGATGCGCCCCCACGGAGCCGTGCGCGCCGAGCACCCGCAGCCCGACGACGCCCCCGCCGGGGCGGAGTCTCCCGCCGCCTCGGCGACGGGGCAGCCGGTCGTGGACCTCGGCGAGGTCGACGACGGCAACCGGACGATCATCGTGCGCGCCGTCGGTCCGCGCTGGGCCGACGTCGACCTGAGCCCACTGGGAGCAGACGCCTCCTGCCAGCCGGGAGTGCCGCTGTGA","MSPAPHTPQTAPGITVATGDADETRALGARLARLLRAGDLVMLSGGLGAGKTTLAQGIGAALQVRGRVSSPTFIIARVHPALSDGPDLIHVDAYRITSLEEIDALDLDSSLERAVTLVEWGEEKVEALSPDRLEIQVMRPHGAVRAEHPQPDDAPAGAESPAASATGQPVVDLGEVDDGNRTIIVRAVGPRWADVDLSPLGADASCQPGVPL$","Predicted ATPase or kinase","Cytoplasm","Predicted ATPase or kinase","protein of unknown function UPF0079","protein of unknown function UPF0079","","Teplyakov A., Obmolova G., Tordova M., Thanki N., Bonander N., Eisenstein E., Howard A.J., Gilliland G.L. Crystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesis. Proteins 2002. 48(2):220-226. PMID: 12112691","","","

InterPro
IPR003442
Domain

Protein of unknown function UPF0079, ATPase bacteria
PF02367	$\"[24-147]T$	UPF0079
TIGR00150	$\"[22-145]T$	TIGR00150: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[11-164]T$	no description

","BeTs to 17 clades of COG0802COG name: Predicted ATPase or kinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0802 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003442 (Protein of unknown function UPF0079) with a combined E-value of 1.4e-23. IPB003442A 35-63 IPB003442B 68-80 IPB003442C 87-96 IPB003442D 113-122","Residues 39-142 are 79% similar to a (HYDROLASE KINASE UPF0079 ATP-BINDING PREDICTED YJEE NUCLEOTIDE-BINDING OR ATPASE ATP/GTP) protein domain (PD006723) which is seen in YBE7_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 147 (E_value = 5.2e-43) place ANA_0075 in the UPF0079 family which is described as Uncharacterised P-loop hydrolase UPF0079.","","ATPase or kinase (Q50706)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0076","86675","87724","1050","5.60","-6.64","36527","GTGAACACTCCCGCCACCGTGGCACCGGTCCGCAACGCCATCCCCATCCGGGCTGCTCAGCGCTCCCGGCGTCCCCGGCGTCTGCTCCTGCCGGCTGCGGCGGCGACGCTCCTGGGTGTCTGTCTCCTGGTCCCGGGGCCGGCCCGCGCCGTTGCCGACACCGGCCCCCACCCCGTGCCGATCACGTCGGCCGGCGGCGTGGCGGGTGTCGCGGCCGATGCCGACTCGCGCGATCAGGCCAAGGCGCTCATGGAGAGCGAGTGCGTGGCGCAGGTGCGTCAGAGCACCGGCGAGCAGGGCGAGATCACGGTGGGTGACCCGCGCAGCGTCTACACCTGGGCCTCCGGCTTCCTCGACGGCTCCCAGCCCTCCGCGCAACCCGTCGACACCGGCGACTGGGCCGCGACCGTCTCCTCGGGCGGCAAGCCCGTCGGTCTTCTCGAGGTGGTCCATGACAAGGGGCACGCCACCTGCACCCCCGTCTTTGACGACGACCTGGCCACCGATGTCGACCAGATGGGCGAGGCCCACCTCGTCCACGACCGCAACGCCAACGCCTGGTACTCGCTGAGTGGCACCACGGTGACGGCGATGGGGGAGGCCGCTACGCGGCGCCTGGCCGGCCCCATCGAGCTGCGCGACTACGGAGAGATCCTGCGTGAGCGCGCCGGGTCCAAGCCCAAGACCTCCACCGCTCAGGGCGAGGAGCGCTCCACCACGGGGGGTTGGGCGATCTGGGGGCCGGTCCTGGCGGTCGTCGTCGTCGGGATCGTCACCGTCATCATCACGGTGCGTCACGAGCGCAAAGTGACCGCCCCACTGCGCCAGGCCCGCAACCGCGCCGACATGGCCGAGCGCGCCGACCAGCTCAGCCGGGACGAGTCCGACACTCAGGGCGCCGCAGTACGCCGGGGCATCCCCCGCGCCGCCATCGACCTGTCCCTCCTGGGGGATGGGGCCGAGGACGACGCCGATGCGACCGCCGGTGAGACCCTGGGGGACACGATCCCTGAGAGCCGCGTCAACCTGCCACGAGACCCGAGGGCATAG","VNTPATVAPVRNAIPIRAAQRSRRPRRLLLPAAAATLLGVCLLVPGPARAVADTGPHPVPITSAGGVAGVAADADSRDQAKALMESECVAQVRQSTGEQGEITVGDPRSVYTWASGFLDGSQPSAQPVDTGDWAATVSSGGKPVGLLEVVHDKGHATCTPVFDDDLATDVDQMGEAHLVHDRNANAWYSLSGTTVTAMGEAATRRLAGPIELRDYGEILRERAGSKPKTSTAQGEERSTTGGWAIWGPVLAVVVVGIVTVIITVRHERKVTAPLRQARNRADMAERADQLSRDESDTQGAAVRRGIPRAAIDLSLLGDGAEDDADATAGETLGDTIPESRVNLPRDPRA$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-50]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[244-264]?$	transmembrane_regions

InterPro
IPR000905
Domain

Peptidase M22, glycoprotease
PF00814	$\"[29-245]T$	Peptidase_M22

","BeTs to 5 clades of COG1214COG name: Inactive homologs of metal-dependent proteases, putative molecular chaperonesFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1214 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 29 to 245 (E_value = 1.9e-17) place ANA_0077 in the Peptidase_M22 family which is described as Glycoprotease family.","","family subfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0078","88514","89119","606","5.43","-5.86","21200","GTGCCCGAGGCGACGGGAGCGGGCCGGGCCCCCGGTCTGCGGGAGATGGCGGCGGGGGACCTGGAGGCCGTCGCCCGACTCGAGGGTGAGCTCTTCGGAGCCGAGGCCTGGAGCCGTGACCTGCTGGCCGCCGAGCTGGCGGCCTCCCACGGGCCGATGGCGGACCGTCGCTACGTCGTCGTCGAGTCCGAAGAGCCCGACGACGATGCAGGCGCCCATGAAGCCGCGGATCGCGCTGCCGGGGCCGGGCCGCACGGGCCACGGCTCCTGGGCTACGCCGGGCTCTACCACGCCGGTGGGCTGACCAGTGCGGACCTGCTGACCATCGCCACCATCCCGGCCGCGCGCGGACGAGGGATCGCCTCCCTCATGCTCACCGAGCTTGTTGTCACCGCCCGAGAGATGAGCTGCCCCGATGTCCTGCTGGAGGTGCGCCAGTCCAACGAGACCGCCCAGCGGCTCTACACCAGGCACGGCTTCGTCCCCATCGGCCGGCGCCGCCGCTACTACCAGGCGCCTCCGGAGGACGCCGTGGTCATGCGTCTGACCCTGCGCCCGCGCCCGGGGCCGGTGGGGGCCGAGGCCGGTGAGTCGAGCCCGGTCTGA","VPEATGAGRAPGLREMAAGDLEAVARLEGELFGAEAWSRDLLAAELAASHGPMADRRYVVVESEEPDDDAGAHEAADRAAGAGPHGPRLLGYAGLYHAGGLTSADLLTIATIPAARGRGIASLMLTELVVTAREMSCPDVLLEVRQSNETAQRLYTRHGFVPIGRRRRYYQAPPEDAVVMRLTLRPRPGPVGAEAGESSPV$","Ribosomal-protein-alanine acetyltransferase","Cytoplasm","ribosomal-protein-alanine acetyltransferase","ribosomal-protein-alanine acetyltransferase ","ribosomal-protein-alanine acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Yoshikawa A., Isono S., Sheback A., Isono K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 1987. 209(3):481-488. PMID: 2828880","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[81-161]T$	Acetyltransf_1
PS51186	$\"[11-185]T$	GNAT

InterPro
IPR006464
Family

Ribosomal-protein-alanine acetyltransferase
TIGR01575	$\"[20-180]T$	rimI: ribosomal-protein-alanine acetyltrans

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[13-193]T$	no description
PTHR23091	$\"[16-62]T$ $\"[85-186]T$	N-TERMINAL ACETYLTRANSFERASE
PTHR23091:SF1	$\"[16-62]T$ $\"[85-186]T$	RIBOSOMAL-PROTEIN-ALANINE ACETYLTRANSFERASE

","BeTs to 18 clades of COG0456COG name: AcetyltransferasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0456 is aompkzyqvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 81 to 161 (E_value = 2.7e-15) place ANA_0078 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","acetyltransferase (rimI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0079","89447","90259","813","9.55","13.67","30385","GTGGCCAAAACATCTGCTCCTTCCCTGAAGAGGCGGACCGCCTTCTCCACGACCGTCTTCATGAAGCGCATGATGGCGATCTCGGGACTGGTGTTCCTGTTCTTCGTCCTCTTCCACGCCTACGGCAACCTGCACTACTTCGAGGGTGAGGTCGCCTACGATCACTACGCCGTGTTCCTGCGGGCACTGCTGGTGCCGATCATGCCCTACGGCGGTGTCCTGTGGATCCTCCGCCTGGCTCTCATGGCCTGCCTCCTGGCTCACGCCGGCAGCGCCTTCCACCTGTGGGCGCGAAACAAGCGGGCCCGCGGCAACGACAAGTACGCCGTCAAGAAGCCCGGCGCCGAGTACTTCGCCTCCCGCTACGCCATGCGCACCATGCGTTGGGGCGGCGTCATCCTCCTGCTGTTCATCATCTGGCACATCCTGCAGTACACCACCCTGTCGCTGACGCCAGGGGGACACTACGTGCACGGACGGGCCTACCTCAACATGTACTACGGCTTCCAGCTGTGGTGGGTGTGGCTCATCTACGCGGTTGCGCTGGCAGCCCTGTGCCTGCACGTGTGGCACGGCGTGTGGTCCGCCCTGCAGACACTGGGTGCGGTGCGAGGAAACACCATCCCCTTCATCCGGCTGATCGCCTTCGTGCTGGCCTTCGCGCTGTTCGCCGCCTTCATGGCTGTTCCGACGGCGATCCTTTTCGGCTATGTCGATGCCCCCATGGCCGTTGGCGACTACTACCCGCAGTTCTGTGACGCGATCGGCTCCTCCGCCGAGCACTTCGCCGAGTGTGTTGCGGCGACCCACTGA","VAKTSAPSLKRRTAFSTTVFMKRMMAISGLVFLFFVLFHAYGNLHYFEGEVAYDHYAVFLRALLVPIMPYGGVLWILRLALMACLLAHAGSAFHLWARNKRARGNDKYAVKKPGAEYFASRYAMRTMRWGGVILLLFIIWHILQYTTLSLTPGGHYVHGRAYLNMYYGFQLWWVWLIYAVALAALCLHVWHGVWSALQTLGAVRGNTIPFIRLIAFVLAFALFAAFMAVPTAILFGYVDAPMAVGDYYPQFCDAIGSSAEHFAECVAATH$","Succinate dehydrogenase or fumarate reductase, cytochrome b558 subunit","Membrane, Cytoplasm","putative cytochrome b subunit","succinate dehydrogenase; cytochrome b558 subunit ","succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family","","Magnusson K., Philips M.K., Guest J.R., Rutberg L. Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex. J. Bacteriol. 1986. 166(3):1067-1071. PMID: 3086287","","","

InterPro
IPR011138
Family

Succinate dehydrogenase, cytochrome b558 subunit
TIGR02046	$\"[17-238]T$	sdhC_b558_fam: succinate dehydrogenase (or

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[75-97]?$ $\"[129-149]?$ $\"[172-192]?$ $\"[213-233]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 35-202 are 63% similar to a (SUBUNIT CYTOCHROME B SUCCINATE DEHYDROGENASE SUBUNIT MEMBRANE FUMARATE C B-558) protein domain (PD690703) which is seen in Q825Y6_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","cytochrome b subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0080","90272","92272","2001","6.18","-7.82","74818","ATGACTGAACTCATCGACGGCCTGTACTACGAGGGCGAGAAGATCGCCGACACCAAGGCCCCCCACTCCGTCCCGATCGACCGGCGCTGGGAGCAGCGCAAGTTCGAGGCCAAGCTGGTCAACCCCGCCAACCGCCGCAAGCTGGACATCATCGTCGTCGGCTCCGGCCTGGCCGGCGGCGCCGCGGCCGCCTCCCTGGGCGAGCAGGGCTACAACGTCAAGGTCTTCTTCTACCAGGACTCGGCCCGCCGGGCGCACTCCATCGCCGCCCAGGGCGGCATCAACGCCGCGAAGAACTACCGCAATGACGGCGACTCCGTCTACCGGCTCTTCTACGACACGGTCAAGGGGGGTGACTACCGCGCCCGCGAGGACAACGTCTACCGCCTGGCGGAGGTCAGCGCCAACATCATCGACCAGTGCGTGGCCCAGGGTGTCCCCTTCGCCCGCGAGTACGGCGGTCTGCTGGACAACCGTTCCTTCGGTGGCGTGCAGGTCTCCCGTACCTTCTACGCCCGCGGCCAGACCGGCCAGCAGCTCCTCATCGGTGCCTACCAGGCCCTCGAGCGCCAGGTGCACGCCGGCACGGTCAAGGAGTTCCGTCGCCACGAGATGGTCGAGCTCATCATCGTCGACGGTCGCGCCCGTGGCATCGTCACCCGCGACATGGTCTCCGGGAAGATCGAGACCCACCTGGCCGACGCCGTCGTGCTGGCCAGTGGCGGCTACGGCAACGTGTTCTTCCTGTCGACCAACGCGATGGGTTGCAACGCCACCGCCGTGTGGCGCGCGCACCGCAAGGGCGCCTACTTCGCCAACCCCTGCTACACGCAGATCCACCCCACCTGCATCCCGCAGTCCGGGGACTTCCAGTCCAAGCTCACCCTCATGAGTGAGTCCCTGCGCAACGACGGACGCATCTGGGTGCCCAAGAAGGCCGAGGACTGCGACAAGGACCCGCGCGACATCCCCGAGGAGGCGCGCGACTACTACCTCGAGCGCATCTACCCGGCCTTCGGCAACCTCGTGCCGCGCGACATCGCCTCCCGCCAGGCCAAGAACATGTGCGACGAGGGTCGCGGCGTGGGGCCGGCCATCAAGGAGCGCGACGCCAACGGCAACGAGCGGATGATGCGTCGCGGCGTCTACCTGGACTTCTCCGAGGCCATCAACCGCCTGGGCAAGGACGCCGTCTCTGCCCGCTACGGCAACCTGTTCGAGATGTACCAGCGCATCACCGGGGACGACCCCTACGAGGTCCCCATGCGCATCTACCCAGCCGTGCACTACACGATGGGTGGCCTGTGGGTGGACTACGACCTGGAGTCCAACGTCCCGGGCCTCTACATCGCCGGAGAGGCCAACTTCTCCGACCACGGCGCCAACCGCCTGGGTGCCTCCGCCCTCATGCAGGGGCTGGCCGACGGTTACTTCGTCCTGCCCGACACCATGAACGACTACCTGGCGGACATGCTGCGCCTGGGCAAGGTCGACCCCAACGCCCCGGAGATCGCCGAGGCCAAGCGCTCCGTCGAGGAGCGCGTCGCCCGCCTCATGGCTCTTCGCGGCACCCGCAGCGTGGACGATTTCCACATGGCCCTGGGCCGCATCATGTGGGAGTACTGCGGCATGGAACGGCGCGACGCCGGGCTGCGCGACGCCATCGGGCAGATCCGGGCCCTCAAGGAGGAGTTCTGGCGCGACGCCCGCATCACGGGCCAGGCCGATGAGCTCAACCAGGCCCTGGAGAAGGCCGGCCGACTGCTGGACTTCTTCGAGCTGGCCGAGCTCATGTGCATCGACGCCCTGCACCGGAGGGAGTCCTGCGGTGGCCACTTCCGGGCGGAGTCCCAGACTCCCGAGGGTGAGGCCCTGCGGCACGACGACGAGTTCCTCTACGTCGCCGCCTGGGAGTGGGGCGGAGAGAACCAGCCGCCGATCCTCCACAAGGAGGACCTCGTCTACAAGGACATCGAGCTCAAGCAGCGGAGTTACAAGTGA","MTELIDGLYYEGEKIADTKAPHSVPIDRRWEQRKFEAKLVNPANRRKLDIIVVGSGLAGGAAAASLGEQGYNVKVFFYQDSARRAHSIAAQGGINAAKNYRNDGDSVYRLFYDTVKGGDYRAREDNVYRLAEVSANIIDQCVAQGVPFAREYGGLLDNRSFGGVQVSRTFYARGQTGQQLLIGAYQALERQVHAGTVKEFRRHEMVELIIVDGRARGIVTRDMVSGKIETHLADAVVLASGGYGNVFFLSTNAMGCNATAVWRAHRKGAYFANPCYTQIHPTCIPQSGDFQSKLTLMSESLRNDGRIWVPKKAEDCDKDPRDIPEEARDYYLERIYPAFGNLVPRDIASRQAKNMCDEGRGVGPAIKERDANGNERMMRRGVYLDFSEAINRLGKDAVSARYGNLFEMYQRITGDDPYEVPMRIYPAVHYTMGGLWVDYDLESNVPGLYIAGEANFSDHGANRLGASALMQGLADGYFVLPDTMNDYLADMLRLGKVDPNAPEIAEAKRSVEERVARLMALRGTRSVDDFHMALGRIMWEYCGMERRDAGLRDAIGQIRALKEEFWRDARITGQADELNQALEKAGRLLDFFELAELMCIDALHRRESCGGHFRAESQTPEGEALRHDDEFLYVAAWEWGGENQPPILHKEDLVYKDIELKQRSYK$","Succinate dehydrogenase or fumarate reductase, flavoprotein subunit","Cytoplasm","succinate dehydrogenase subunit A","succinate dehydrogenase flavoprotein subunit ","succinate dehydrogenase or fumarate reductase, flavoprotein subunit","","Blaut M., Whittaker K., Valdovinos A., Ackrell B.A., Gunsalus R.P., Cecchini G. Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin. J. Biol. Chem. 1989. 264(23):13599-13604. PMID: 2668268Birch-Machin M.A., Farnsworth L., Ackrell B.A., Cochran B., Jackson S., Bindoff L.A., Aitken A., Diamond A.G., Turnbull D.M. The sequence of the flavoprotein subunit of bovine heart succinate dehydrogenase. J. Biol. Chem. 1992. 267(16):11553-11558. PMID: 1375942","","","

InterPro
IPR003953
Domain

Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00890	$\"[49-469]T$	FAD_binding_2

InterPro
IPR004112
Domain

Fumarate reductase/succinate dehydrogenase flavoprotein, C-terminal
PF02910	$\"[531-665]T$	Succ_DH_flav_C

InterPro
IPR011280
Family

Succinate dehydrogenase or fumarate reductase, flavoprotein subunit, low-GC Gram-positive bacteria
PTHR11632:SF4	$\"[30-315]T$ $\"[331-665]T$	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
TIGR01811	$\"[50-665]T$	sdhA_Bsu: succinate dehydrogenase or fumara

noIPR
unintegrated

unintegrated
G3DSA:1.20.58.100	$\"[501-616]T$	no description
G3DSA:3.50.50.60	$\"[43-495]T$	no description
PTHR11632	$\"[30-315]T$ $\"[331-665]T$	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT

","BeTs to 23 clades of COG1053COG name: Succinate dehydrogenase/fumarate reductase, flavoprotein subunitsFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1053 is aomp-zyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB003952 (Fumarate reductase/succinate dehydrogenase, FAD-binding site) with a combined E-value of 7.6e-96. IPB003952A 49-63 IPB003952B 83-118 IPB003952C 135-158 IPB003952D 168-185 IPB003952E 202-247 IPB003952F 251-304 IPB003952G 412-438 IPB003952H 444-477 IPB003952I 582-622***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 7.7e-07. IPB001100A 48-73 IPB001100E 433-454***** IPB008471 (Protein of unknown function DUF752) with a combined E-value of 3.3e-06. IPB008471F 52-99***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 9.7e-06. IPB013027A 49-71 IPB013027C 49-74","Residues 4-81 are 78% similar to a (SUCCINATE SUBUNIT OXIDOREDUCTASE FLAVOPROTEIN DEHYDROGENASE) protein domain (PDA191Z3) which is seen in Q6A7S9_PROAC.Residues 15-81 are 79% similar to a (FUMARATE REDUCTASE SUBUNIT OXIDOREDUCTASE FLAVOPROTEIN) protein domain (PDA193W1) which is seen in Q74DY8_GEOSL.Residues 46-256 are similar to a (FLAVOPROTEIN SUBUNIT OXIDOREDUCTASE SUCCINATE DEHYDROGENASE OXIDASE L-ASPARTATE FUMARATE FAD REDUCTASE) protein domain (PD001219) which is seen in Q8F4Z1_LEPIN.Residues 276-413 are similar to a (FLAVOPROTEIN SUBUNIT OXIDOREDUCTASE SUCCINATE DEHYDROGENASE OXIDASE L-ASPARTATE FUMARATE FAD REDUCTASE) protein domain (PD520810) which is seen in Q6A7S9_PROAC.Residues 418-476 are 66% similar to a (OXIDOREDUCTASE FLAVOPROTEIN OXIDASE LASPO BIOSYNTHESIS L-ASPARTATE FAD QUINOLINATE SYNTHETASE NUCLEOTIDE) protein domain (PD706613) which is seen in NADB_SULTO.Residues 426-454 are 93% similar to a (FLAVOPROTEIN SUBUNIT OXIDOREDUCTASE SUCCINATE DEHYDROGENASE OXIDASE L-ASPARTATE FAD SYNTHETASE B) protein domain (PD309670) which is seen in Q6A7S9_PROAC.Residues 459-531 are 57% similar to a (OXIDOREDUCTASE SUCCINATE A FLAVOPROTEIN DEHYDROGENASE SUBUNITS DEHYDROGENASE/FUMARATE REDUCTASE) protein domain (PD895311) which is seen in Q8NTD6_CORGL.Residues 459-534 are 75% similar to a (SUBUNIT SUCCINATE FLAVOPROTEIN DEHYDROGENASE OXIDOREDUCTASE DEHYDROGENASE A FUMARATE REDUCTASE REDUCTASE) protein domain (PD806346) which is seen in Q6A7S9_PROAC.Residues 537-591 are 78% similar to a (SUBUNIT SUCCINATE FLAVOPROTEIN DEHYDROGENASE OXIDOREDUCTASE DEHYDROGENASE A REDUCTASE FUMARATE REDUCTASE) protein domain (PD597884) which is seen in Q6A7S9_PROAC.Residues 593-638 are 78% similar to a (FLAVOPROTEIN SUBUNIT SUCCINATE OXIDOREDUCTASE DEHYDROGENASE OXIDASE L-ASPARTATE FAD FUMARATE DEHYDROGENASE) protein domain (PD292374) which is seen in Q6MRQ0_BDEBA.Residues 593-626 are 94% similar to a (SUBUNIT FLAVOPROTEIN SUCCINATE DEHYDROGENASE OXIDOREDUCTASE FUMARATE REDUCTASE DEHYDROGENASE REDUCTASE A) protein domain (PD983375) which is seen in Q6A7S9_PROAC.Residues 628-666 are 79% similar to a (SUBUNIT FLAVOPROTEIN SUCCINATE DEHYDROGENASE OXIDOREDUCTASE FUMARATE REDUCTASE DEHYDROGENASE REDUCTASE PROBABLE) protein domain (PD983365) which is seen in Q6A7S9_PROAC.","","-45% similar to PDB:2B76 E. coli Quinol fumarate reductase FrdA E49Q mutation (E_value = 6.2E_48);-45% similar to PDB:1KF6 E. coli Quinol-Fumarate Reductase with Bound Inhibitor HQNO (E_value = 1.4E_47);-45% similar to PDB:1KFY QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL (E_value = 1.4E_47);-45% similar to PDB:1L0V Quinol-Fumarate Reductase with Menaquinol Molecules (E_value = 1.4E_47);-44% similar to PDB:1E7P QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES (E_value = 4.6E_43);","Residues 49 to 350 (E_value = 0.00085) place ANA_0080 in the DAO family which is described as FAD dependent oxidoreductase.Residues 49 to 469 (E_value = 1.3e-50) place ANA_0080 in the FAD_binding_2 family which is described as FAD binding domain.Residues 49 to 76 (E_value = 0.00033) place ANA_0080 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 531 to 665 (E_value = 1.4e-07) place ANA_0080 in the Succ_DH_flav_C family which is described as Fumarate reductase/succinate dehydrogenase flavoprotein C-terminal domain.","","dehydrogenase subunit A (NADH2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0082","92269","93039","771","6.30","-4.72","27538","GTGAACATCAAGCTCAAGATCTGGCGCCAGAAGAACCAGGACTCGAAGGGCCACTTCGAGGAGTACGCCATGAGCGGGATCGAGGAGCACATGAGCTTCCTCGAGGTCCTCGACCTGCTCAACGAGCAGCTCTTCGCCGAGGGCAAGGAGCCGGTGGCCTTCGACTCCGACTGCCGCGAGGGCATCTGCGGTCAGTGCGGTGTGGTCATCAACGGGCAGGCCCACGGGCCCATCCGCTCGACCACCTGCCAGCTGCACATGCGCCACCTGGCGGAGGACCCCTCCTTCAAGGACGGCTCCACCATCACGATCGAACCGTGGCGCTCCACCGGCTTCCCGGTGCTGCGTGACCTCATCGTGGACCGCTCCGCCCTGGACCGCATCGTTCAGGCCGGTGGCTACATCTCGGTCAACACCGGTGGGGCCCCGGAGGCCCACTCGGTGCCCGTGCAGAAGGAGAAGGCCGACGCCGCCTTCGAGGCGGCTGCTTGCATCGGCTGCGGTGCCTGCGTGGCGGCGTGCCCCAACGCCTCGGCCATGCTGTTCACCGGTGCGAAGATCTCGCACCTGGGTCTGCTGCCGCAGGGCCAGCCCGAGCGCCTGGCTCGCGTGGTGAGCATGCTCAACCAGCACGACGCCGAGGGCTTCGGCGGCTGCACCAACATCGGTGAGTGCGCGGCCGTGTGCCCCAAGTCGGTTCCGCTCGAGGTCATCTCGCGCCTCAACCGGGATCTCGGCCACGCCCTGTGGAAGGGCCAGCACGCCCACTGA","VNIKLKIWRQKNQDSKGHFEEYAMSGIEEHMSFLEVLDLLNEQLFAEGKEPVAFDSDCREGICGQCGVVINGQAHGPIRSTTCQLHMRHLAEDPSFKDGSTITIEPWRSTGFPVLRDLIVDRSALDRIVQAGGYISVNTGGAPEAHSVPVQKEKADAAFEAAACIGCGACVAACPNASAMLFTGAKISHLGLLPQGQPERLARVVSMLNQHDAEGFGGCTNIGECAAVCPKSVPLEVISRLNRDLGHALWKGQHAH$","Succinate dehydrogenase and fumarate reductase iron-sulfur protein","Cytoplasm","succinate dehydrogenase subunit B","putative succinate dehydrogenase iron-sulfur protein ","succinate dehydrogenase and fumarate reductase iron-sulfur protein","","Mason J.R., Cammack R. The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol. 1992. 46:277-305. PMID: 1444257Otaka E., Ooi T. Examination of protein sequence homologies: V. New perspectives on evolution between bacterial and chloroplast-type ferredoxins inferred from sequence evidence. J. Mol. Evol. 1989. 29(3):246-254. PMID: 2506358Rypniewski W.R., Breiter D.R., Benning M.M., Wesenberg G., Oh B.H., Markley J.L., Rayment I., Holden H.M. Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry 1991. 30(17):4126-4131. PMID: 1902376","","","

InterPro
IPR001450
Domain

4Fe-4S ferredoxin, iron-sulfur binding
PR00353	$\"[157-168]T$ $\"[169-180]T$	4FE4SFRDOXIN
PF00037	$\"[157-180]T$	Fer4
PS00198	$\"[164-175]T$	4FE4S_FERREDOXIN

InterPro
IPR004489
Family

Succinate dehydrogenase/fumarate reductase iron-sulfur protein
PIRSF000176	$\"[3-253]T$	Fumarate reductase/succinate dehydrogenase (ubiquinone), iron-sulphur protein
TIGR00384	$\"[7-242]T$	dhsB: succinate dehydrogenase and fumarate

InterPro
IPR006058
Binding_site

2Fe-2S ferredoxin, iron-sulfur binding site
PS00197	$\"[58-66]T$	2FE2S_FER_1

InterPro
IPR012285
Domain

Fumarate reductase, C-terminal
G3DSA:1.10.1060.10	$\"[131-249]T$	no description

InterPro
IPR012675
Domain

Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30	$\"[1-121]T$	no description

noIPR
unintegrated

unintegrated
PTHR11921	$\"[15-245]T$	SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN

","BeTs to 21 clades of COG0479COG name: Succinate dehydrogenase/fumarate reductase Fe-S proteinFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0479 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB001041 (Ferredoxin) with a combined E-value of 1.8e-06. IPB001041 58-73","Residues 1-121 are 74% similar to a (IRON-SULFUR IRON DEHYDROGENASE 2FE-2S OXIDOREDUCTASE SUCCINATE SUBUNIT METAL-BINDING 4FE-4S XANTHINE) protein domain (PD001472) which is seen in Q6A7T0_PROAC.Residues 175-231 are 77% similar to a (IRON-SULFUR 4FE-4S OXIDOREDUCTASE IRON METAL-BINDING PYRUVATE SUBUNIT DEHYDROGENASE PYRUVATE-FLAVODOXIN FERREDOXIN) protein domain (PD015404) which is seen in Q9RCY8_STRCO.Residues 175-251 are 85% similar to a (IRON-SULFUR METAL-BINDING IRON SUCCINATE 4FE-4S FUMARATE OXIDOREDUCTASE DEHYDROGENASE DEHYDROGENASE REDUCTASE) protein domain (PD315160) which is seen in Q6A7T0_PROAC.Residues 176-244 are 72% similar to a (IRON-SULFUR IRON SUCCINATE 2FE-2S OXIDOREDUCTASE DEHYDROGENASE METAL-BINDING 4FE-4S SUBUNIT REDUCTASE) protein domain (PDA0J7A3) which is seen in Q8F4Z2_LEPIN.","","No significant hits to the PDB database (E-value < E-10).","Residues 157 to 180 (E_value = 0.00026) place ANA_0082 in the Fer4 family which is described as 4Fe-4S binding domain.","","dehydrogenase subunit B","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0083","95430","94591","840","5.85","-4.64","28895","GTGTCCCTACCTTCCGTCGCCCCTAATTCTGAACGGCTTTCAGAACTCAGTAAGGTCCACCTTACTCTCGCCGCTGAACCACAGGCAACAGCCCCCAGGGACCATTACGGTGCTGCCATGACACGACCTGCGCGACTGGGCCGACCGACCGGACCGAGACCGGGCTTCTCGCGCGACGACGTCGTCGATGCCGCCCTCGAGATCGGCATCGCGGACTTCACGCTCACGGCGGTGGCCAAGCATCTGGGGGTGGCGGTCTCCGGGCTGTACCGAACAATCTCCTCACGCGAGGATCTGCTGGCTGCCTGCCTGGAGAGGATCGCTGCCGAGGTGGACGTCCCGGGCACCGGGAGGCGCTGGCCCGATGCGGTGCGGGCCCACGCCGAGGCCATCTGGGCGATGCTGGAGCGCTACCCCGGCCTGGCCGGGGTCATCATGGGGGTGCCGTGGGCCCACCAGCTCTTCGCCGCCCCCGTGGCTCAAGCGTGCCAGGCCCTGGTCGACGGCGGCTTGGGGGCCGAGGAGGCCGGGGTGGTCCTGGACTTCGTCGGCGACACCGTCATCTCCACGCACGCGCAAATCGAGGTCATGCGCTCCCCCGTGGCCTCCTCGGGGCAGGGCGGCCCCACGGGACTGGAGGAGACCAGCCGGTTCGCGGCCGCCGCCGGGAACCCTCCCCTGCCCGAGGCGCTGAGGCCCAACGAGAGCTGGCTGGAGCGCGGCGGCCTGGACCGAAAGATCGAGATCATCATCCGGGGAGTGGCCGCGGGCCTGCCCCCGGGCGCAACGGATACGGGAGGGAAGTCGGCGTCAGGGGGCGACGTCAGTGGGCGACGCTGA","VSLPSVAPNSERLSELSKVHLTLAAEPQATAPRDHYGAAMTRPARLGRPTGPRPGFSRDDVVDAALEIGIADFTLTAVAKHLGVAVSGLYRTISSREDLLAACLERIAAEVDVPGTGRRWPDAVRAHAEAIWAMLERYPGLAGVIMGVPWAHQLFAAPVAQACQALVDGGLGAEEAGVVLDFVGDTVISTHAQIEVMRSPVASSGQGGPTGLEETSRFAAAAGNPPLPEALRPNESWLERGGLDRKIEIIIRGVAAGLPPGATDTGGKSASGGDVSGRR$","Transcriptional regulator, TetR family","Cytoplasm","VarR","putative transcriptional regulator (TetR family)","Tetracyclin repressor domain protein","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PF00440	$\"[69-103]T$	TetR_N

InterPro
IPR004111
Domain

Tetracyclin repressor, C-terminal
PF02909	$\"[113-258]T$	TetR_C

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[54-114]T$	no description

","BeTs to 9 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB003012 (Tetracycline repressor protein signature) with a combined E-value of 7.2e-07. IPB003012A 69-92 IPB003012B 120-139***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 9.7e-06. IPB001647 57-99","Residues 51-263 are 51% similar to a (TRANSCRIPTIONAL TETR-FAMILY REGULATOR) protein domain (PDA0Z4B7) which is seen in Q6A626_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 69 to 103 (E_value = 0.0002) place ANA_0083 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.Residues 113 to 258 (E_value = 0.0013) place ANA_0083 in the TetR_C family which is described as Tetracyclin repressor, C-terminal all-alpha domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0084","93561","94607","1047","4.89","-16.52","36021","GTGAGCGACCCCCTCATTCTCGGCATCGAGTCCACCTGCGACGAGACCGGCGTGGCCCTCGTGCGCGGCCGCGAGCTCCTCGCCGATGTCACCGCCACCTCCATGGACCAGTACGCGCGCTTCGGCGGCATCATCCCCGAGATCGCCTCACGCGCCCACCTGGAGTCCTTCCTGCCGACCTTCGACGCCGCGCTGGAGAAGGCCGGTGTCGACCTCAGTGAGGTCGACGCCGTCGCCGTGTGCGCCGGCCCCGGACTCATCGGCTCCCTGACCGTCGGCATCTCCGCCGCCAAGGCCCTGGCCGCGAGCCTGAACCGGCCGATCTACGGCGTCAACCACGTCATCGGCCACCTGGCGGTCGATGAGCTGGTCGATGGCCCCCTGCCGGAGCGTTTCGTCGGACTCATCGTCTCCGGCGGCCACTCGAACCTCCTGAGCATCCGTAACATCGCCACCGACGTCGTCGAGCTCGGCGGCACTCTCGACGACGCCGCCGGTGAGGCCTTCGACAAGGTCGGCCGCCTCCTGGGCCTGCCCTACCCCGGTGGCCCGCACGTGGACCGGCTCTCCCAGGAGGGTGACCGCAGTGCCATCCGTTTCCCTCGGGGGCTGGCCGCGGGCAAGGACAAGGAGCGTCACCGCTACGACTTCTCCTTCTCCGGCCTCAAGACCGCCGTGGCCCGCTATGTGGAGTCCCTGGAGGACTCCGACCAGGAGGTGCCCAGTGCTGATGTCTGCGCCGCCTTCTCCGAGGCCGTCAACGACTCCCTGACGGCCAAGGCGGTCCAGGCCTGCCTGGACACCGGCTGCGGCACGCTCGTCGTCGGGGGAGGGTACTCGGCCAACTCCCGCCTGCGCTCCCTGGCCGCCGAGCGCTGCGAGGAGGCCGGCATCACCCTGCGCCTGCCACCACTGCGCTTCTGCACCGACAACGGCGCCCAGATCGCAGCCCTGGGGTCAGCGGCCGTGCGGGCCGGCGTCGTCCCCAGCCCCATGGACTTCGCCCCGGACTCGGGGATGCCGCTGGACGTCAGCGTCGCCCACTGA","VSDPLILGIESTCDETGVALVRGRELLADVTATSMDQYARFGGIIPEIASRAHLESFLPTFDAALEKAGVDLSEVDAVAVCAGPGLIGSLTVGISAAKALAASLNRPIYGVNHVIGHLAVDELVDGPLPERFVGLIVSGGHSNLLSIRNIATDVVELGGTLDDAAGEAFDKVGRLLGLPYPGGPHVDRLSQEGDRSAIRFPRGLAAGKDKERHRYDFSFSGLKTAVARYVESLEDSDQEVPSADVCAAFSEAVNDSLTAKAVQACLDTGCGTLVVGGGYSANSRLRSLAAERCEEAGITLRLPPLRFCTDNGAQIAALGSAAVRAGVVPSPMDFAPDSGMPLDVSVAH$","O-sialoglycoprotein endopeptidase","Cytoplasm, Extracellular","metalloendopeptidase Gcp","putative glycoprotease ","putative metalloendopeptidase, glycoprotease family","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Mellors A., Lo R.Y. O-sialoglycoprotease from Pasteurella haemolytica. Meth. Enzymol. 1995. 248:728-740. PMID: 7674959Abdullah K.M., Lo R.Y., Mellors A. Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene. J. Bacteriol. 1991. 173(18):5597-5603. PMID: 1885539","","","

InterPro
IPR000905
Domain

Peptidase M22, glycoprotease
PD002367	$\"[244-286]T$	Q6NJ39_CORDI_Q6NJ39;
PR00789	$\"[7-20]T$ $\"[78-98]T$ $\"[99-118]T$ $\"[133-145]T$ $\"[157-178]T$ $\"[273-282]T$	OSIALOPTASE
PF00814	$\"[25-317]T$	Peptidase_M22
TIGR00329	$\"[7-316]T$	gcp: metalloendopeptidase, putative, glycop
PS01016	$\"[98-118]T$	GLYCOPROTEASE

InterPro
IPR009180
Family

Peptidase M22, O-sialoglycoprotein endopeptidase
PIRSF004537	$\"[4-347]T$	O-sialoglycoprotein endopeptidase
PTHR11735	$\"[99-342]T$	O-SIALOGLYCOPROTEIN ENDOPEPTIDASE

","BeTs to 26 clades of COG0533COG name: Metal-dependent proteases with possible chaperone activityFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0533 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000905 (Glycoprotease (M22) metalloprotease) with a combined E-value of 1.5e-78. IPB000905A 6-17 IPB000905B 42-53 IPB000905C 74-118 IPB000905D 154-193 IPB000905E 214-226 IPB000905F 277-286 IPB000905G 307-319","Residues 6-53 are 93% similar to a (ENDOPEPTIDASE O-SIALOGLYCOPROTEIN HYDROLASE PROTEASE GLYCOPROTEASE PROBABLE ZINC METALLOPROTEASE GLYCOPROTEIN SIALOGLYCOPROTEASE) protein domain (PD577523) which is seen in Q8G4D1_BIFLO.Residues 55-121 are 80% similar to a (ENDOPEPTIDASE O-SIALOGLYCOPROTEIN PROTEASE HYDROLASE GLYCOPROTEASE PROBABLE METALLOPROTEASE ZINC GLYCOPROTEIN FAMILY) protein domain (PD163880) which is seen in Q6A6V2_PROAC.Residues 133-241 are similar to a (ENDOPEPTIDASE O-SIALOGLYCOPROTEIN HYDROLASE PROTEASE GLYCOPROTEASE PROBABLE ZINC METALLOPROTEASE GLYCOPROTEIN SIALOGLYCOPROTEASE) protein domain (PD605274) which is seen in Q6AD38_BBBBB.Residues 244-286 are 79% similar to a (ENDOPEPTIDASE O-SIALOGLYCOPROTEIN HYDROLASE PROTEASE GLYCOPROTEASE PROBABLE ZINC METALLOPROTEASE GLYCOPROTEIN SIALOGLYCOPROTEASE) protein domain (PD002367) which is seen in Q6NJ39_CORDI.Residues 291-342 are 67% similar to a (ENDOPEPTIDASE O-SIALOGLYCOPROTEIN PROBABLE HYDROLASE ZINC GLYCOPROTEASE METALLOPROTEASE GCP ACTIVITY PROTEASE) protein domain (PDA0P8L5) which is seen in GCP_MYCTU.","","No significant hits to the PDB database (E-value < E-10).","Residues 25 to 317 (E_value = 6.9e-64) place ANA_0084 in the Peptidase_M22 family which is described as Glycoprotease family.","","Gcp (660)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0085","95434","98910","3477","8.27","12.00","123083","ATGGACACGCGGACACAGTCGTCAGCTCCGGGAGCCTCGCCGCATCCATCGCCCGCGCCGTCGTCGCCGCCCTCAGCCGGTGCAGCAGTGCCTGGCGACGCAGCTGAGCCGACCCCTCAGGGCAACGCCGAGCGCTCGCGCGAGGGGCAGGCAGCCATCGCCCGCCTCGGCGCCCCCGTGCGTACCCGCCTGCGGATCGGTCAGGCCCTCGTCCTGCTCTCGGCGATCCTGGCCGTGGCCCCCTACATCGCACTGGTCCAGCTCGGCGATATCCTGCTGCGCGCCTACCGGGCGGGCCTGAGCCCGGATCCCCAGCAGGTGTCAGGCGCGGTCATGGTGCTTGTGAGTGCCTACTCCACCCGCCTGCTGCTGTACTTCCTGGCGCTGCTCATCACCCACCTGGCCGACCTGTCCCTGCGCGACCGCCTGCGCCGCGACATCGTTGCGCGTATCTCCCATGCCCCGCTGTCCTGGTTCACTGCCTCCACCTCCGGGCGCCTGCGCAAGGCCGTCCAGGACGACACGACCCTCGTCCACACCGTCATCGCTCACGGTCCCGTCGAGCGCCTCAACGCCATCGTCACCCCGCTGGCCCTGCTGGGCTGCGCCTTCTGGATCGACTGGCGCCTGGCCCTGCTGGCCGTCTCCACACTCGTCCTCTACGTGCTCACCTACTCGGTGTCCATGCGCGGCATGAACGAGAAGACCGTGGAGATGGACCGCAAGCTGGCAGCCATCTCCTCAGCCATGGTCGAGTTCGTCTCCGGGATCGGCGTGGTCAAGGCCTTCGGACGCGTGGGACGAGCGCACTCGGCCTACCTCACCGCCGCGGACGAGTTCTCCGCCTTCTACCGCGCCTGGGCGATGCCCCTGGTGACCGTCACCTGCCTGTCCTTCACCTGGGTCTCCATCCCCGTACTGCTCCTGGTCAACCTCGGCGGTGGGGCGCTGCTCATCCACGCCGGGGCCGTCACCCTGCCCCAGGTCCTGGCCACGACCCTCATTGCTCTGGTCCTGCCCGCCGCCCTCATCACCATCGCCTCGATCTCCTGGTCCTACCAGCTTGCCGGCGCGGCGGCCCTGCGGCTGTGCGAGGTCCTCGACACCCCCGTCCTTCCCGCCGCCGACCGGCCCGAACAGCCCCGCGCGGCGCGAGTCGAGATCGACCACGTCTCCTTCTCCTACGGGGAGGTCCTTGCCGTCGATGACGCCTGCCTGACCCTGGAGCCGGGAACCGTGACCGCGCTGCTGGGCCCCTCCGGCTCGGGCAAGTCGACACTGGCCACCCTCATCGCCCGCTTCGCCGACCCCGACGCCGGAGCCATTCGCATCGGCGGGGTGGACTTGCGGGACATGGACGAGTCCACCCTGTACTCCACCGTCTCCTTCGTCCTCCAGGACGCCCAGCTGCTCGCCACCACCGTGCGCGAGAACATCGCCCTCGGGCGCCCCGAGGCCGACCTGGCGCAGGTGCGCGCCGCCGCCCGCGTGGCCCGCATCCACGACGAGATCATGGCGCTGCCGCAGGGCTACGACACCGTCCTAGGGCAGGACACGGCACTGTCCGGTGGACAGGAGCAGCGCATCGCCATCGCCCGCGCCATCCTGCTGAACACCCCCGTCATCGTGCTTGACGAGGCCACCGCCATGGCCGACCCCGAGTCCGAGGCCGAGATCCAGGAGGCACTGAGCGCCCTGGTCAAGGACCGCACCGTCCTGGTCATCGCCCACCGGCCGGCTGCCGTGCGCGGCGCCGACCGCATCGCCGTCATGGACGGCGGACGCATCGTCGCCGCCGGCTCCCACGATGACCTGGCAGATGAGCCCCACTACCGGGCTCTGCTGCGCCAGGCCGGCGAGATCGAAGGTGCCACGGAGGTGGACGGTGACGAGACCGCCACCAGGACGGAGGGCCCCGCACTCGCCGACGGCGCGGCCGACAGTGCGGCTGACGGCGGTGCCCCGGCAGCAGTGGCCTCCCACATCGATGACCGGGCCGCGCGTCCGGAGCCCTCGTCTCCCGGTGGGTCCTCCCAGCCGGCGGACTCCCTGCTGTCCCGCTTCCGCCGACTCATGACCGACTCCTCTTGGAGGCAGACCCGAGGGTGCATCGCCCTGGCGGGAGTCAACGGGGTCCTGGTGGGACTCGCGCTGCTGGTGCTGCTGCCCGCCTCAGTGGCTCTGGCGACCGGTGCGCCCCGATGGGGGCTGTCCTTCGGCGGCTGGCTCGTCGTACTGGTCGTTCTCGGTCTCGGCGCGGCCGTCTGCGACTTCCAGGGACGGCGCATGGGCATGTCGGGGGCGCTGGGCTTCATGCACGACGTCCATCACGCGGTGGGTGACCGGATCGCGCGCCTGCCCCTGCGCTGGTTCACTGCCGACTCCGCCGGCACCCTGTCTCGGGCCGTGAGCCAGGAGATGGTGGCCCTGGGGGAGTCCGCCGCCCACTTCATGTACCTGCTCACCTCCACTGCTGCTGCATGCATGGTCGTCGGGGTCGGCTCCTGGGCCTGGGATTGGCGCCTGGGGCTCCTGCTGACGCTGGCTGCGCCCCTGTTCGCCGGACTCGTGCGCCTCTCGCGCCGTCTGCTGGACCGCGGTAAGTCCATCTCCGAGCCTGCCGAGCGTGAGCTCGCCACCCGCATCGTCGAGATCGCCCGCTGCCAGGGCGCCCTGCGATCCTGTCGGGCAGCCTCCGGCTACAGCCGCCTGACCGCCGCCTTCGACGACGGGGCCCGCGCCTCCAGGCGAGCCCTGTGGTGGGAGTCCGCCGGCAACCTCGTCAACGGCGCGCTGAGCCAGATCGTCGTCGTCGCCATGATCGTCCTGACCTCCTCACTGGCCGCCTCCGGCACCATGGAGCCGCTGGTGGCCATCGCCGTCATCGGCATGTGCCTGCGTTTCACCACCATGCTCGACGAGATCGGGGCAGCCGTCATGGGCGTGGAGGAGCGGCGCCAGATGATGAACCACCTCGATGCCGTCATGGACGCCGAGCTCATGGCCGAGCCGCAGGAGCCCAGTGCGCTGCCCGAGCCGGGGGCCGTCGAGCTCGACGACGTTGCCTTCGGCTACCGCCCCGACGAGCCCGTCCTGACCGGGGTCTCGGGTCTCGATGAGGGTGCCCGCGCGCACCATGTGCGCGATCGTGGGCCCCTCCGGCAGCGGCAAGACGACCATCGCCCGCCTCGTCGCCCGCTTCTGGGATGTGGACTCGGGAACCGTGCGTGTCGGCGGCACCGACGTGCGCGACATGCCGACATCCCAGCTCATGGAACAACTCTCCATGGTCTTCCAGGACGTCTACCTCTTCGACGACACCCTGGCCGCCAACATCTGTATCGGCAACCCCGCGGCCGACGACGCCCAGGTGCGCTGGGCCGCAGGGCTCGCCGGCGTCACGGAGATCATCCACCGCCTGCCCCATGGATGGGACACGCGCGTGGGAGAGGGCGGACGGGCCCTGTCCGGTGGTGA","MDTRTQSSAPGASPHPSPAPSSPPSAGAAVPGDAAEPTPQGNAERSREGQAAIARLGAPVRTRLRIGQALVLLSAILAVAPYIALVQLGDILLRAYRAGLSPDPQQVSGAVMVLVSAYSTRLLLYFLALLITHLADLSLRDRLRRDIVARISHAPLSWFTASTSGRLRKAVQDDTTLVHTVIAHGPVERLNAIVTPLALLGCAFWIDWRLALLAVSTLVLYVLTYSVSMRGMNEKTVEMDRKLAAISSAMVEFVSGIGVVKAFGRVGRAHSAYLTAADEFSAFYRAWAMPLVTVTCLSFTWVSIPVLLLVNLGGGALLIHAGAVTLPQVLATTLIALVLPAALITIASISWSYQLAGAAALRLCEVLDTPVLPAADRPEQPRAARVEIDHVSFSYGEVLAVDDACLTLEPGTVTALLGPSGSGKSTLATLIARFADPDAGAIRIGGVDLRDMDESTLYSTVSFVLQDAQLLATTVRENIALGRPEADLAQVRAAARVARIHDEIMALPQGYDTVLGQDTALSGGQEQRIAIARAILLNTPVIVLDEATAMADPESEAEIQEALSALVKDRTVLVIAHRPAAVRGADRIAVMDGGRIVAAGSHDDLADEPHYRALLRQAGEIEGATEVDGDETATRTEGPALADGAADSAADGGAPAAVASHIDDRAARPEPSSPGGSSQPADSLLSRFRRLMTDSSWRQTRGCIALAGVNGVLVGLALLVLLPASVALATGAPRWGLSFGGWLVVLVVLGLGAAVCDFQGRRMGMSGALGFMHDVHHAVGDRIARLPLRWFTADSAGTLSRAVSQEMVALGESAAHFMYLLTSTAAACMVVGVGSWAWDWRLGLLLTLAAPLFAGLVRLSRRLLDRGKSISEPAERELATRIVEIARCQGALRSCRAASGYSRLTAAFDDGARASRRALWWESAGNLVNGALSQIVVVAMIVLTSSLAASGTMEPLVAIAVIGMCLRFTTMLDEIGAAVMGVEERRQMMNHLDAVMDAELMAEPQEPSALPEPGAVELDDVAFGYRPDEPVLTGVSGLDEGARAHHVRDRGPLRQRQDDHRPPRRPLLGCGLGNRACRRHRRARHADIPAHGTTLHGLPGRLPLRRHPGRQHLYRQPRGRRRPGALGRRARRRHGDHPPPAPWMGHARGRGRTGPVRW$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","ABC transporter, permease/ATP-binding protein","K06147 ATP-binding cassette; subfamily B; bacterial","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[139-265]T$	ABC_membrane

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[521-563]T$	Q7NNT7_GLOVI_Q7NNT7;
PF00005	$\"[411-594]T$	ABC_tran
PS50893	$\"[386-618]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[410-595]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[69-348]T$ $\"[704-984]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[386-650]T$	no description
PTHR19242	$\"[36-616]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF92	$\"[36-616]T$	HLYB/MSBA FAMILY ABC TRANSPORTER
tmhmm	$\"[66-86]?$ $\"[117-137]?$ $\"[210-229]?$ $\"[243-263]?$ $\"[286-320]?$ $\"[326-346]?$ $\"[702-722]?$ $\"[736-756]?$ $\"[816-836]?$ $\"[842-860]?$ $\"[927-949]?$	transmembrane_regions

","BeTs to 19 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 13","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.2e-39. IPB005074C 400-447 IPB005074D 509-552 IPB005074E 571-591***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 7.3e-24. IPB013563A 400-434 IPB013563C 518-545 IPB013563D 570-622***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 7.6e-12. IPB010509B 411-436 IPB010509D 516-560***** IPB005116 (TOBE domain) with a combined E-value of 1.2e-11. IPB005116A 418-434 IPB005116C 521-534","Residues 45-268 are 48% similar to a (ATP-BINDING MEMBRANE ABC SUPERFAMILY) protein domain (PDA19606) which is seen in Q7P0D7_CHRVO.Residues 52-165 are 68% similar to a (ATP-BINDING ABC TRANSPORTER TRANSMEMBRANE TRANSPORTER ABC-TRANSPORTER ATP-BINDING/PERMEASE COMPOSITE CASSETTE A) protein domain (PD190163) which is seen in Q6A623_PROAC.Residues 55-381 are 40% similar to a (ATP-BINDING ABC TRANSPORTER PROBABLE COMPONENT PLASMID) protein domain (PD357109) which is seen in Q9HWG6_PSEAE.Residues 111-487 are 44% similar to a (LANTIBIOTIC MEMBRANE SYSTEM ABC-TRANSPORT ATP-BINDING) protein domain (PDA0J3N6) which is seen in Q6NIL4_CORDI.Residues 147-269 are 52% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER MULTIDRUG ATP-BINDING/PERMEASE TRANSMEMBRANE RESISTANCE PERMEASE MEMBRANE) protein domain (PD087348) which is seen in Q9ZB57_PROMI.Residues 168-217 are 72% similar to a (ATP-BINDING ABC TRANSPORTER CYDD TRANSPORTER COMPONENT ATP-BINDING/PERMEASE INNER MEMBRANE CYTOCHROME-RELATED) protein domain (PD600395) which is seen in Q6A623_PROAC.Residues 174-291 are 52% similar to a (ATP-BINDING RV1348/MT1390/MB1383 ABC TRANSMEMBRANE TRANSPORTER) protein domain (PD905579) which is seen in Q73X95_MYCPA.Residues 235-287 are 66% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD890637) which is seen in Q6A623_PROAC.Residues 243-374 are 51% similar to a (ABC PROTEIN PERMEASE/ATP-BINDING TRANSPORTER ATP-BINDING) protein domain (PD460771) which is seen in Q88JQ3_PSEPK.Residues 324-482 are 49% similar to a (ATP-BINDING/PERMEASE FUSION ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I2L4) which is seen in Q7NX92_CHRVO.Residues 324-487 are 45% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I309) which is seen in Q9AM85_RIEAN.Residues 362-554 are 43% similar to a () protein domain (PDA073I6) which is seen in Q6LGG1_PHOPR.Residues 366-487 are 45% similar to a (ATP-BINDING OXIDASE ABC IV TRANSPORTER SUBUNIT CYTOCHROME) protein domain (PD918529) which is seen in Q7X3M9_LEIXX.Residues 370-486 are 54% similar to a (ATP-BINDING PROTEIN CYDCD) protein domain (PDA1B3E1) which is seen in Q6ABD5_PROAC.Residues 378-590 are 48% similar to a (ATP-BINDING/PERMEASE ABC TRANSPORTER ATP-BINDING) protein domain (PD976112) which is seen in Q73QS1_TREDE.Residues 379-579 are 42% similar to a (ATP-BINDING SECRETION ABC TOXIN TRANSPORTER) protein domain (PD608939) which is seen in Q8PMA4_XANAC.Residues 381-477 are 60% similar to a (TRANSPORTER ABC EXPORT) protein domain (PDA18411) which is seen in Q7P4Z0_BBBBB.Residues 386-554 are 49% similar to a (ATP-BINDING/PERMEASE ABC TOXIN TRANSPORTER ATP-BINDING PLASMID) protein domain (PD416779) which is seen in Q82YJ4_ENTFA.Residues 402-608 are 42% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 403-605 are 44% similar to a (LANTIBIOTIC SYSTEM MERSACIDIN TRANSPORTER) protein domain (PDA0G5T2) which is seen in Q7UG09_RHOBA.Residues 406-577 are 48% similar to a (HLYB SECRETION ABC PROTEIN TOXIN FAMILY ATP-BINDING TRANSPORTER) protein domain (PD727846) which is seen in Q8E9W6_SHEON.Residues 406-452 are 91% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q6A623_PROAC.Residues 411-486 are 60% similar to a (ATP-BINDING PLASMID TRANSPORTER ABC) protein domain (PD741687) which is seen in Q83XI2_VIBAN.Residues 413-588 are 47% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 416-596 are 42% similar to a (ATP-BINDING ABC PROTEIN TRANSPORTER) protein domain (PD995669) which is seen in Q73R06_TREDE.Residues 452-518 are 71% similar to a (ATP-BINDING) protein domain (PDA1B3I1) which is seen in Q73TI3_MYCPA.Residues 453-597 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I0J1) which is seen in Q83A70_COXBU.Residues 502-578 are 71% similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PDA0I0J5) which is seen in Q7P0D6_CHRVO.Residues 505-605 are 53% similar to a (APRD ATP-BINDING) protein domain (PDA0I303) which is seen in Q89EV0_BRAJA.Residues 507-578 are 60% similar to a (ATP-BINDING LIN1097 LMO1131) protein domain (PD932075) which is seen in Q8Y7Y8_LISMO.Residues 507-578 are 72% similar to a (ATP-BINDING TRANSPORTER ABC RESISTANCE TRANSMEMBRANE SIMILAR MULTIGENE POLYMORPHISM FAMILY GLYCOPROTEIN) protein domain (PD250423) which is seen in Y742_STRCO.Residues 521-563 are 88% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q7NNT7_GLOVI.Residues 860-1001 are 45% similar to a (ATP-BINDING ABC TRANSPORTER PROBABLE COMPONENT PROTEIN PERMEASE/ATP-BINDING RV1349/MT1392/MB1384 TRANSMEMBRANE TRANSPORTER) protein domain (PD307473) which is seen in Q73X96_MYCPA.Residues 860-951 are 57% similar to a (ABC PERMEASE TRANSPORTER) protein domain (PD994011) which is seen in Q6A624_PROAC.","","-50% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 5.7E_52);-50% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 5.7E_52);-60% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 9.5E_39);-60% similar to PDB:2FF7 The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state (E_value = 9.5E_39);-60% similar to PDB:2FFB The crystal structure of the HlyB-NBD E631Q mutant in complex with ADP (E_value = 2.1E_38);","Residues 68 to 343 (E_value = 0.00012) place ANA_0085 in the ABC_membrane family which is described as ABC transporter transmembrane region.Residues 411 to 594 (E_value = 3.1e-55) place ANA_0085 in the ABC_tran family which is described as ABC transporter.","","transporter, permease-ATP-binding protein (ABC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0086","98549","99226","678","6.41","-1.89","24405","ATGAGGGTGCCCGCGCGCACCATGTGCGCGATCGTGGGCCCCTCCGGCAGCGGCAAGACGACCATCGCCCGCCTCGTCGCCCGCTTCTGGGATGTGGACTCGGGAACCGTGCGTGTCGGCGGCACCGACGTGCGCGACATGCCGACATCCCAGCTCATGGAACAACTCTCCATGGTCTTCCAGGACGTCTACCTCTTCGACGACACCCTGGCCGCCAACATCTGTATCGGCAACCCCGCGGCCGACGACGCCCAGGTGCGCTGGGCCGCAGGGCTCGCCGGCGTCACGGAGATCATCCACCGCCTGCCCCATGGATGGGACACGCGCGTGGGAGAGGGCGGACGGGCCCTGTCCGGTGGTGAGCGCCAGCGCGTCTCCATCGCCCGCGCCCTGCTCAAACGAGCCCCGATCGTCCTGCTCGATGAGGCCACCAGCGCGCTGGACGCCGAGAACGAGGCGAATATCGTCGCCGCGATGCAGGAGCTGCGCCGCACCTCGACCCTCATCGTCATTGCCCACAAGCTGGAGACGATTGCCGCCGCCGACCAGGTCGTCGTCCTCGACGACGCCGGGCGCATCGCCCAGCGGGGACACCACGATGAGCTCGTGGCCGTCGAGGGGCCCTACCGCAGCTTCTGGGAGCAGCGCACCCGGGCGCGCGGTTGGGCACTCGTCTAG","MRVPARTMCAIVGPSGSGKTTIARLVARFWDVDSGTVRVGGTDVRDMPTSQLMEQLSMVFQDVYLFDDTLAANICIGNPAADDAQVRWAAGLAGVTEIIHRLPHGWDTRVGEGGRALSGGERQRVSIARALLKRAPIVLLDEATSALDAENEANIVAAMQELRRTSTLIVIAHKLETIAAADQVVVLDDAGRIAQRGHHDELVAVEGPYRSFWEQRTRARGWALV$","ABC-type multidrug/protein/lipid transport system, ATPase component","Cytoplasm, Membrane","ABC transporter, permease/ATP-binding protein","K06147 ATP-binding cassette; subfamily B; bacterial","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[117-159]T$	Q6A625_PROAC_Q6A625;
PF00005	$\"[6-191]T$	ABC_tran
PS50893	$\"[1-215]T$	ABC_TRANSPORTER_2
PS00211	$\"[117-131]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[5-191]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-213]T$	no description
PTHR19242	$\"[1-225]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91	$\"[1-225]T$	LIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA

","BeTs to 20 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 13","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.6e-44. IPB005074D 105-148 IPB005074E 167-187***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 6.9e-25. IPB010509B 6-31 IPB010509D 112-156 IPB010509E 165-195***** IPB005116 (TOBE domain) with a combined E-value of 2.4e-20. IPB005116A 13-29 IPB005116C 117-130 IPB005116D 137-156***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2e-16. IPB013563C 114-141 IPB013563D 167-219","Residues 1-99 are 53% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I309) which is seen in Q9AM85_RIEAN.Residues 1-176 are 47% similar to a (HLYB SECRETION ABC PROTEIN TOXIN FAMILY ATP-BINDING TRANSPORTER) protein domain (PD727846) which is seen in Q8E9W6_SHEON.Residues 1-172 are 44% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 1-178 are 53% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 2-176 are 47% similar to a (ATP-BINDING SECRETION PROBABLE ABC TOXIN TRANSPORTER) protein domain (PDA0C7R3) which is seen in Q7UXT8_RHOBA.Residues 3-70 are 75% similar to a (TRANSPORTER ABC EXPORT) protein domain (PDA18411) which is seen in Q7P4Z0_BBBBB.Residues 5-178 are 49% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 6-210 are 47% similar to a (LANTIBIOTIC SYSTEM MERSACIDIN TRANSPORTER) protein domain (PDA0G5T2) which is seen in Q7UG09_RHOBA.Residues 8-46 are 89% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q6A625_PROAC.Residues 10-150 are 50% similar to a (ATP-BINDING/PERMEASE ABC TOXIN TRANSPORTER ATP-BINDING PLASMID) protein domain (PD416779) which is seen in Q82YJ4_ENTFA.Residues 11-174 are 42% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 11-178 are 46% similar to a (ATP-BINDING ABC PROTEIN TRANSPORTER) protein domain (PD995669) which is seen in Q73R06_TREDE.Residues 46-114 are 62% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA1B4P3) which is seen in Q9EWN7_STRCO.Residues 52-178 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I0J1) which is seen in Q83A70_COXBU.Residues 99-174 are similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PDA0I0J5) which is seen in Q7P0D6_CHRVO.Residues 101-174 are 66% similar to a (ATP-BINDING LIN1097 LMO1131) protein domain (PD932075) which is seen in Q8Y7Y8_LISMO.Residues 102-174 are similar to a (ATP-BINDING TRANSPORTER ABC RESISTANCE TRANSMEMBRANE SIMILAR MULTIGENE POLYMORPHISM FAMILY GLYCOPROTEIN) protein domain (PD250423) which is seen in Y742_STRCO.Residues 117-159 are 93% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6A625_PROAC.Residues 118-173 are 70% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.","","-60% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 6.3E_42);-60% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 6.3E_42);-61% similar to PDB:2GHI Crystal Structure of Plasmodium yoelii Multidrug Resistance Protein 2 (E_value = 7.0E_41);-61% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 1.1E_33);-61% similar to PDB:2FF7 The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state (E_value = 1.1E_33);","Residues 6 to 191 (E_value = 1.7e-58) place ANA_0086 in the ABC_tran family which is described as ABC transporter.","","transporter, permease-ATP-binding protein (atm1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0087","100484","99252","1233","5.02","-17.22","44883","ATGCAGAACACGACTGACACGACGAGCCCGAACGCCGCGTCCGCCGACGCTCAACTGCCGCCGGCCCGCCGCCCCCAGTCCCTCCCCTTCGCCGGATCGGCCCGCTCCACGCTGGGGGTGGAGTGGGAGCTGGCCCTCATCGACCGCGACAGCCTCGACCTGCGCCAGTGCGCCGAGGAGATCCTCCAGAAGGTGGGCCCGGACCCGCACGTGCACGGCGAGATGATGCTCAACACCATCGAGCTGGTCTCCGGGGCGCGCAGGACCGTGGCCGAGTGCATGGAGGACATCGCCTTCGCCTTCGACCGAGTCCTTCCCGTCACCGACCCCCTGCGCGTGGACCTGGCCTCGGCCGGGACCCACCCCTTCGCCGACCCGCTGGTGCAGAAGGTGACCAATGCCGAGCGCTACGCGCGCCTGGTGGACCGCACCCGGCTGTGGGGTCACCAGATGCTCATCTTCGGCACCCACGTCCACGTCGGCGTCGAGGACCGGAGCAAGGTCCTTCCGATCCTCAAGGCCCTGCTCACGCGCACCGCCCACCTGCAGTGCCTGAGCGCCTCCTCACCCTTCTGGGCGGGGGCGGACACGGGCTACGCGGACAACCGCGCCATGATGTTCCAGCAGCTGCCCACCGCCGGCGCCCCTGAGCAGTTCAGCACCTGGGAGCAGCTGGAGAGCTACACCGGGGACCTGGTCCACACCGGCGTCATCGAGGACTTCACCGAGATCCGCTGGGACGTGCGCCCCTCGCCGCGCCTGGGAACCATCGAGGTGCGGGCCTGCGACGCCGCCACGAACCTGACCGAGCTGGCCGGGATGGCGGCACTGACCCAGTGCCTCGTGGAGTCCTTCTCCCGCACCCTGGACCGGGGTGAGGAGCTCGATGCGTTGCCAGACTGGTACGTCGCCGAGAACAAGTGGCGCTCCGCCCGCTACGGCATGGACGCGATCCTCATCGTCAACTCCGCCGGTGAGGAGGAGCTGGTGGGAGACACGGTTGAGCGGATGCTCACCGAGCTCGCTCCCGTCGCCGAGGATCTCGGTTGCGCCGCCGAACTGGACTCCGTGCGCACCACGTTGGAGACGGGGGCCTCCTACCAGCGTCAGATCGCCGCCGTCAGGGCCTACGGCGGACAGCGGGAGGCGGCCGTCAGGCTGCTGCTGGCCGAGGCCCGCGCGGGCAGACCCCTGCGTCCCACCGAGGTGCTCTCGCTGGCGGCCAAGTCCTGA","MQNTTDTTSPNAASADAQLPPARRPQSLPFAGSARSTLGVEWELALIDRDSLDLRQCAEEILQKVGPDPHVHGEMMLNTIELVSGARRTVAECMEDIAFAFDRVLPVTDPLRVDLASAGTHPFADPLVQKVTNAERYARLVDRTRLWGHQMLIFGTHVHVGVEDRSKVLPILKALLTRTAHLQCLSASSPFWAGADTGYADNRAMMFQQLPTAGAPEQFSTWEQLESYTGDLVHTGVIEDFTEIRWDVRPSPRLGTIEVRACDAATNLTELAGMAALTQCLVESFSRTLDRGEELDALPDWYVAENKWRSARYGMDAILIVNSAGEEELVGDTVERMLTELAPVAEDLGCAAELDSVRTTLETGASYQRQIAAVRAYGGQREAAVRLLLAEARAGRPLRPTEVLSLAAKS$","Glutamate--cysteine ligase, GCS2","Cytoplasm","Uncharacterized BCR","hypothetical protein","glutamate--cysteine ligase, GCS2","","May M.J., Leaver C.J. Arabidopsis thaliana gamma-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast, and Escherichia coli homologs. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(21):10059-10063. PMID: 7937837","","","

InterPro
IPR006336
Family

Glutamate--cysteine ligase, GCS2
PF04107	$\"[37-315]T$	GCS2

InterPro
IPR011793
Family

Enzymatic protein of unknown function
TIGR02050	$\"[37-320]T$	gshA_cyan_rel: uncharacterized enzyme

","BeTs to 5 clades of COG2170COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2170 is -o--------r--cef----------Number of proteins in this genome belonging to this COG is 1","***** IPB006336 (Glutamate--cysteine ligase, plant) with a combined E-value of 1.5e-35. IPB006336A 33-45 IPB006336B 160-205 IPB006336C 234-281","Residues 30-162 are 63% similar to a (YBDK BLL3764 UNCHARACTERIZED ECS0619 BCR STY0626 GLL2294 VNG1397C SCO7331 RV0433/MT0448/MB0441) protein domain (PD887204) which is seen in Y433_MYCTU.Residues 169-204 are 80% similar to a (UNCHARACTERIZED BCR RV0433/MT0448/MB0441) protein domain (PDA0V306) which is seen in Q6AE97_BBBBB.Residues 205-379 are similar to a (YBDK UNCHARACTERIZED TLL0322 BLL3764 ECS0619 GLR2275 BCR STY0626 GLL2294 VNG1397C) protein domain (PD024872) which is seen in Y433_MYCTU.","","-46% similar to PDB:1TT4 Structure of NP459575, a predicted glutathione synthase from Salmonella typhimurium (E_value = 4.8E_37);-46% similar to PDB:1R8G Structure and function of YbdK (E_value = 2.0E_35);-50% similar to PDB:1CI1 CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI IN HEXANE (E_value = 2.0E_35);-50% similar to PDB:1SUX CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE FROM TRYPANOSOMA CRUZI AND 3-(2-benzothiazolylthio)-1-propanesulfonic acid (E_value = 2.0E_35);-50% similar to PDB:1TCD TRYPANOSOMA CRUZI TRIOSEPHOSPHATE ISOMERASE (E_value = 2.0E_35);","Residues 37 to 315 (E_value = 3.7e-53) place ANA_0087 in the GCS2 family which is described as Glutamate-cysteine ligase family 2(GCS2).","","BCR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0088","101832","100564","1269","5.33","-12.72","44181","ATGGCTGAGAACCACGTTGCGCTCCTCCTGACCCCCGAGGGCTGGGAGCTTCTGTCCTCCCTGCCCCCCTACGACCCCTCCGAGGCCCTGTCCCTGGGGCGCTCCCTGCGCGAGGAGGGCCACTCCCCTGCCCTGGTGGCGGCTGCGCTGACGCAGCAGCGCCTGCGCGAGCGGGCCGCAGCGAAGTTCGGGCCCTTCGCCCAGCAGATGCTCTTCACCGCCGACGGCCTGGAGCAGGCCACCCGGCTGACGGTCTCGGCCCACCATGCGGCCCGTTACGCGGCCGCGGGCGTGACGAAGGTCGCGGACCTGGGTTGTGGGATCGGGGGTGACGCCGTTGCCCTGGCAGGGCTCGATTTGCCGGTGCTCGCGGTGGACCGAGATGAGGCCGCGGCCGCCCTGGCCACCATCAATCTCATGCCCTTCCCCCACGCGAGCGTCGAGTGCGCCGACGCCTTGGAGATCGACCTGGTCGAGCGGGGGGTGGACGCCGTCTTCGCCGACCCCGCCCGCCGCGCCGACGGGCGGCGCATCACCGACCCGGAGCAGTGGTCTCCGGCTCTGTCGCAGGTGCTCGCGCTGCGCGAGACCGTGCCCGCCCTGGGAGTCAAGGTCGCTCCCGGCATCGACCACGCCGCTCTGCCGGCCGACGCCCACACCCAGTGGGTGAGCGTGGACGGCGACGTCGTCGAGGCGGCCATCTGGTGCGGTCCGCTGGCACCGGAGGGGCCCGGGCGCTCCGCACTGATCCTGCGCTCGGGGGCGCAGGGCCCAGCCGCCTGCACACTGGTCGATCCCAGCACCACCGACCCCTCACAGCCGCCGGTCCAGGTCGACCCGATCGGCTCGCCCGACGACCTGGGCAGCATCATCCACGTTCCCGACGGCGCCGCCGTGCGCGCCGGACTCATCGCCCACCTGTGCGAGACCCTGGACGCCAGGCCAGTGGGACCCCGGATCGGCTACCTCACGGGCGAGCGCCTGCCCGATGAGGCGACTGCCCCCTTCGTGCGCTCCTTCCGACTCACCGAGGTCCTGCCGCTACGGCTCAAGACCCTGCGCTCCCGTGGCCGCGAGCTCGGTATCGGGCGTCTGGAGATCCTCAAGCGCGGAGTCGACGTCTCCCCCGACGCCCTGCGCGCCTCGCTGAGGCTCAGCGGTCAGGAGTCGGAGACCTGGATCCTGACCCGGGTGGGAGACAAGGCGAAGGGCGCCGTCCTCGTCGTCGAACCAATCACCGGCACCTCATCAGCTCACTCACCGACGTAA","MAENHVALLLTPEGWELLSSLPPYDPSEALSLGRSLREEGHSPALVAAALTQQRLRERAAAKFGPFAQQMLFTADGLEQATRLTVSAHHAARYAAAGVTKVADLGCGIGGDAVALAGLDLPVLAVDRDEAAAALATINLMPFPHASVECADALEIDLVERGVDAVFADPARRADGRRITDPEQWSPALSQVLALRETVPALGVKVAPGIDHAALPADAHTQWVSVDGDVVEAAIWCGPLAPEGPGRSALILRSGAQGPAACTLVDPSTTDPSQPPVQVDPIGSPDDLGSIIHVPDGAAVRAGLIAHLCETLDARPVGPRIGYLTGERLPDEATAPFVRSFRLTEVLPLRLKTLRSRGRELGIGRLEILKRGVDVSPDALRASLRLSGQESETWILTRVGDKAKGAVLVVEPITGTSSAHSPT$","SAM-dependent methyltransferase","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[99-167]T$	no description
PTHR14741	$\"[4-250]T$	S-ADENOSYLMETHIONINE-DEPENDENT METHYLTRANSFERASE RELATED
PTHR14741:SF2	$\"[4-250]T$	gb def: Hypothetical protein SCO4758

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 35-139 are 78% similar to a (METHYLTRANSFERASE MB3063C SAM-DEPENDENT TRANSFERASE SCO4758 CGL1229) protein domain (PD560290) which is seen in Q6AD40_BBBBB.Residues 145-406 are 40% similar to a () protein domain (PDA09813) which is seen in Q7UQE5_RHOBA.Residues 164-401 are 51% similar to a (METHYLTRANSFERASE TRANSFERASE 2.1.1.- MB3063C SAM-DEPENDENT MA0195 TVG0562373 CT0100 PF1059 SCO4758) protein domain (PD135646) which is seen in Q6AD40_BBBBB.","","-57% similar to PDB:2I44 Crystal structure of serine-threonine phosphatase 2C from Toxoplasma gondii (E_value = );-39% similar to PDB:2GRV Crystal Structure of LpqW (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0090","102046","102855","810","6.55","-1.66","28497","ATGGCTGAGGAGGAGTCCCGGCTCGGTGCCGGTCAGGGGACTGGCGCCGCTTTAGGGCGCGAGGACGACGGCGTGAGCACAGCCCCAGTCCAGGGGCCTGACGCTGTGGGACACCTCCGGTCGCTTCTGCGTCCACTGGTACGGATCTGTGTGGCAGTCATGGGGGTCGCGGCCCTTTTGGCGGCCGGGGCCAGTGTCTGGGCGTGGACCGTCAGTGCCGGGCACATCGAGATCGCCGGTGAAGGATCCGGCGACGGTGCGGCGGCCAGGGCGCCGGTGGCGATCGTCCTGGGGGCGGCCGTTCACGCTGACGGACAGCCCTCACCTTGGCTGGCCCACCGCCTCGACGCCGCCGCCGAGCTCTACACCAGCGGTCGCGTCGAGGCGATCCTGGTCTCCGGGGACAACCGGCGAGCCGGCTACGACGAGCCCACTGTCATGCGCAGCTACCTCCTCTCCCGGGGGATCCCCGATCAGGCGATCGCCCTGGACTACGCGGGCTTCGACACCTACGACACCTGTGTGCGGGCGCGCAGGATCTTCGGGATCGAGCGGGCTCTGCTCGTGACCCAGGACTTCCACGAGCCGCGCGCGGTCGCCATCTGCCGCTCAGTCGGCCTCGACGTTGACGGTGTCGGAGACTCGCGGGCCCGCAGCGACCGCATCGGGTGGACGGTCAGCTGGGTGCGCGAGCGAGCGGCGGCGATCAAGGCCGTCGTCGATGTGGTCTCCCGACGTGACCCGACCCTGGGGCGCCAGGAGACGAGCGTCAAGGACGCTGTCGCCTGGACCCGGGAGCACCGGCGCTGA","MAEEESRLGAGQGTGAALGREDDGVSTAPVQGPDAVGHLRSLLRPLVRICVAVMGVAALLAAGASVWAWTVSAGHIEIAGEGSGDGAAARAPVAIVLGAAVHADGQPSPWLAHRLDAAAELYTSGRVEAILVSGDNRRAGYDEPTVMRSYLLSRGIPDQAIALDYAGFDTYDTCVRARRIFGIERALLVTQDFHEPRAVAICRSVGLDVDGVGDSRARSDRIGWTVSWVRERAAAIKAVVDVVSRRDPTLGRQETSVKDAVAWTREHRR$","Uncharacterized membrane protein","Cytoplasm, Membrane","sanA protein","hypothetical protein","protein of unknown function DUF218","","","","","

InterPro
IPR003848
Domain

Protein of unknown function DUF218
PF02698	$\"[90-235]T$	DUF218

noIPR
unintegrated

unintegrated
tmhmm	$\"[49-69]?$	transmembrane_regions

","BeTs to 4 clades of COG2949COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2949 is ---------d----e-gh--------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 96-240 are 70% similar to a (MEMBRANE TRANSMEMBRANE SANA UNCHARACTERIZED EXPORTED YGJQ YCBC INTEGRAL PROBABLE VANCOMYCIN) protein domain (PD006234) which is seen in Q9L2E7_STRCO.","","-43% similar to PDB:2HGS HUMAN GLUTATHIONE SYNTHETASE (E_value = );-43% similar to PDB:1KNQ Crystal structure of gluconate kinase (E_value = );-43% similar to PDB:1KO1 Crystal structure of gluconate kinase (E_value = );-43% similar to PDB:1KO4 Crystal structure of gluconate kinase (E_value = );-43% similar to PDB:1KO5 Crystal structure of gluconate kinase (E_value = );","Residues 90 to 235 (E_value = 3.8e-39) place ANA_0090 in the DUF218 family which is described as DUF218 domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0091","102953","103402","450","9.10","3.88","15996","GTGCTCGCCCCGTCCTGGGACGCGGGGCGGGCACCTTCTGCGACTCGCACTCCTGCATCGTGCCGGACCGACCCCCGCGACGGCGGTCGGGTACGTCTGGGGAGGGCGAACAAGCCGTTCTACTGCACGTTGAAGAGAAGGAGGAGGTCTCCAATGTCGATCTCCATCAAGCCGCTCGAGGACCGTATCGTCGTCCAGACCGCTGAGGCCGAGCAGACCACCGCATCCGGCCTGGTCATCCCCGACACCGCCAAGGAGAAGCCCCAGGAGGGCAAGGTCGTGGCCGTGGGCCCGGGTCGCATTGACGACTCCGGCAACCGCGTGCCCGTCGATGTCGCCGAGGGTGACGTCGTCATCTACTCCAAGTACGGGGGCACCGAGGTCAGCTACGCCGGTGAGGACTACCTCATCCTGTCGGCGCGCGACGTCCTGGCGGTCGTCACCAAGTGA","VLAPSWDAGRAPSATRTPASCRTDPRDGGRVRLGRANKPFYCTLKRRRRSPMSISIKPLEDRIVVQTAEAEQTTASGLVIPDTAKEKPQEGKVVAVGPGRIDDSGNRVPVDVAEGDVVIYSKYGGTEVSYAGEDYLILSARDVLAVVTK$","Co-chaperonin GroES","Cytoplasm, Extracellular","chaperonin","K04078 chaperonin GroES (Hsp10)","chaperonin Cpn10","","Prasad T.K., Stewart C.R. cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock. Plant Mol. Biol. 1992. 18(5):873-885. PMID: 1349837Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., Georgopoulos C.P., Hendrix R.W., Ellis R.J. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 1988. 333(6171):330-334. PMID: 2897629Levy-rimler G., Bell R.E., Ben-tal N., Azem A. Type I chaperonins: not all are created equal. FEBS Lett. 2002. 529(1):1-5. PMID: 12354603Schmidt A., Schiesswohl M., Volker U., Hecker M., Schumann W. Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis. J. Bacteriol. 1992. 174(12):3993-3999. PMID: 1350777Martin J., Geromanos S., Tempst P., Hartl F.U. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES. Nature 1993. 366(6452):279-282. PMID: 7901771","","","

InterPro
IPR001476
Family

Chaperonin Cpn10
PD000566	$\"[60-144]T$	Q6AD41_BBBBB_Q6AD41;
PR00297	$\"[56-71]T$ $\"[78-99]T$ $\"[113-125]T$ $\"[134-147]T$	CHAPERONIN10
G3DSA:2.30.33.40	$\"[52-149]T$	no description
PTHR10772	$\"[46-149]T$	GROES CHAPERONIN
PF00166	$\"[55-147]T$	Cpn10
PS00681	$\"[56-80]T$	CHAPERONINS_CPN10

","BeTs to 19 clades of COG0234COG name: Co-chaperonin GroES (HSP10)Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0234 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001476 (Chaperonin Cpn10) with a combined E-value of 4e-33. IPB001476 76-125","Residues 47-146 are 55% similar to a (CHAPERONE TVAGHSP10) protein domain (PD773806) which is seen in Q94830_TRIVA.Residues 54-145 are 56% similar to a (CHAPERONIN CHAPERONE) protein domain (PD775098) which is seen in Q8IDZ8_PLAF7.Residues 55-147 are 58% similar to a (GROES CHAPERONE CHAPERONIN) protein domain (PD962282) which is seen in Q6YR95_ONYPE.Residues 60-144 are similar to a (CHAPERONE CHAPERONIN GROES CPN10 SHOCK HEAT CHLOROPLAST CHAPERONIN HSP10 SEQUENCING) protein domain (PD000566) which is seen in Q6AD41_BBBBB.","","-89% similar to PDB:1HX5 Crystal structure of M. tuberculosis chaperonin-10 (E_value = 1.3E_37);-89% similar to PDB:1P3H Crystal Structure of the Mycobacterium tuberculosis chaperonin 10 tetradecamer (E_value = 1.3E_37);-86% similar to PDB:1LEP THREE-DIMENSIONAL STRUCTURE OF THE IMMUNODOMINANT HEAT-SHOCK PROTEIN CHAPERONIN-10 OF MYCOBACTERIUM LEPRAE (E_value = 9.3E_36);-83% similar to PDB:1WE3 Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus (E_value = 3.8E_29);-83% similar to PDB:1WF4 Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus (E_value = 3.8E_29);","Residues 55 to 147 (E_value = 3.4e-48) place ANA_0091 in the Cpn10 family which is described as Chaperonin 10 Kd subunit.","","(HSP10) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0091.1","103882","103580","303","6.77","-0.46","11635","ATGCACGACTCATCGCGTCTGCCCGGTCCGATCTCCACCCTCTGGGAGTGGCAGTACCGGGGGTCCTGCCTCGGCATGGACTCCTCGGTTTTCTTCCATCCCGAAGGAGAGAGAGGCGGTTCCCGTCGACGGCGGAACGAACGAGCAAAGGCCATTTGTCAGGACTGCCCCGTCCTGGAAGAGTGCCGGGACCACGCCCTGAGCACTCGCGAGCCCTATGGCGTCTGGGGAGGCATGAGCGAGGAGGAGCGGCGCGCTTACTACGAGCGGCAGGCACGCCGTTTCGCCGACGAACCGGCCTAA","MHDSSRLPGPISTLWEWQYRGSCLGMDSSVFFHPEGERGGSRRRRNERAKAICQDCPVLEECRDHALSTREPYGVWGGMSEEERRAYYERQARRFADEPA$","Transcriptional regulator, WhiB family","Cytoplasm, Extracellular","","","","","Kormanec J, Homerova D.Streptomyces aureofaciens whiB gene encoding putative transcription factor essential for differentiation.Nucleic Acids Res. 1993 May;21(10):2512.PMID: 8506145","","","

InterPro
IPR003482
Family

Transcription factor WhiB
PF02467	$\"[17-87]T$	Whib

","No hits to the COGs database.","***** IPB003482 (Transcription factor WhiB) with a combined E-value of 1.1e-09. IPB003482B 62-78","Residues 17-80 are similar to a (REGULATORY TRANSCRIPTIONAL REGULATOR WHIB-LIKE TRANSCRIPTION PROBABLE WHIB-FAMILY FACTOR WHIB WHIB3) protein domain (PD008027) which is seen in Q7TWJ2_MYCBO.","","","Residues 17 to 87 (E_value = 1.1e-34) place ANA_0091.1 in the Whib family which is described as Transcription factor WhiB.","","","","1","","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:08:11 2007","Fri Aug 10 11:08:11 2007","Fri Aug 10 11:08:11 2007","Fri Aug 10 11:07:27 2007","","Mon Aug 20 17:56:14 2007","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:07:27 2007","Mon Aug 20 17:56:14 2007","Fri Aug 10 11:07:27 2007","Mon Aug 20 17:56:14 2007","Fri Aug 10 11:07:27 2007","Fri Aug 10 11:07:27 2007","Mon Aug 20 17:56:14 2007","","Fri Aug 10 11:07:27 2007","","Fri Aug 10 11:07:27 2007","yes","","" "ANA_0092","104261","105823","1563","5.69","-8.20","55067","ATGCACAGGGTGGTCAGGTCGTCCTACGATGGCCCCGTGAGCGACTCGATCACCAGCCCTGACGTCTTTGCCCCCACCGGACTCACTTACGACGACGTGCTCCTGCTGCCCAGGCTGACCGACGTCATCCCCTCCGAGGTCGATACGACCTCCAGACTGACCCCGAGGATCAGCCTGGCCACCCCGCTGCTCTCGGCCGCGATGGACACGGTCACCGAGTCGGACATGGCCATTGCCATGGCTCGCCAAGGTGGTATCGGCATCCTCCACCGCAACCTGTCCATCGAGGACCAGGCCCAGCAGGTGCGACGCGTCAAGCGCTCGGAGTCCGGGATGGTCACCGACCCGGTGACCGTCGGACCGGATGCCACCATCGCCCAGCTCGACGAGCTCTGCGGCCACTACAAGGTTTCCGGCCTGCCCGTCGTCGATGCGGGAGGCAACCTTCAGGGGATCATCACCAACCGCGACCTGCGCTTCGTCCCCCCGGAGCGCTGGGCGAGCCTGACCGTGCGCGAGTGCATGACGCCGCGTGATCGCCTCATCACCGGCGAGACCGGCATCTCTCGGGAGGACGCCAAGGCGCTCCTGGCTGAGCACCGCATCGAGAAGCTGCCCCTGGTCGATGCCGAGGGGCGCCTCACCGGTCTCATCACCGTCAAGGACTTCGTCAAGACCGAGCAGTACCCCCACGCCACCAAGGACGCCGAGGGGCGCCTCGTGGTGGGCGCCGCCGTCGGCTACTGGGGAGACACGTGGGAGCGTGCCAGTGCCCTGGCTGAGGCCGGCGTGGATGTCCTCATCGTCGACACCGCTAACGGCGGTGCCAAGCTGGCCCTGGAGATGATCTCCCGCCTCAAGTCCGATTCCGCCTTCGGCGGCATCGAGGTCATCGGCGGAAACGTCGCTACCCGTGAGGGGGCTCAGGCGCTCATCGACGCCGGGGCCGACGCCGTCAAGGTCGGGGTGGGGCCGGGCTCGATCTGCACCACGCGCGTCGTCGCCGGCGTGGGTGTGCCCCAGGTGACGGCCATCTACGAGGCGGCTCGCGCCTGCAAGCCCGCCGGGGTCCCCCTCATCGCCGACGGCGGCCTGCAGTACTCCGGTGACATCGCCAAGGCCCTCGTGGCCGGCGCGGAGACGGTCATGCTCGGCTCCCTGCTGGCGGGCTGCACGGAGTCTCCCGGCGACCTCGTCTTCGTCAACGGCAAGCAGTGGAAGCGCTACCGCGGCATGGGGTCGCTGGGGGCCATGAGCTCGCGCGGGCGCACCTCCTACTCCAAGGACCGCTACTTCCAGGCCGACGTCTCCTCGGACTCCAAGATCGTCCCCGAGGGCATCGAGGGGCAGGTCCCCTACTCCGGAGCGCTGGGCGACGTCGTCTACCAGCTCATGGGCGGGCTGCACCAGTCCATGTTCTACGTGGGCGCGCGCACGATCCCCGAGCTCAAGGAGCGCGGGCAGTTCGTGCGGATCACGAGCGCCGGTCTCAAGGAGTCCCACCCCCACGACGTCAAGATGACCGTCGAGGCCCCCAACTACACCGGCCGCGACGGGGTCTGA","MHRVVRSSYDGPVSDSITSPDVFAPTGLTYDDVLLLPRLTDVIPSEVDTTSRLTPRISLATPLLSAAMDTVTESDMAIAMARQGGIGILHRNLSIEDQAQQVRRVKRSESGMVTDPVTVGPDATIAQLDELCGHYKVSGLPVVDAGGNLQGIITNRDLRFVPPERWASLTVRECMTPRDRLITGETGISREDAKALLAEHRIEKLPLVDAEGRLTGLITVKDFVKTEQYPHATKDAEGRLVVGAAVGYWGDTWERASALAEAGVDVLIVDTANGGAKLALEMISRLKSDSAFGGIEVIGGNVATREGAQALIDAGADAVKVGVGPGSICTTRVVAGVGVPQVTAIYEAARACKPAGVPLIADGGLQYSGDIAKALVAGAETVMLGSLLAGCTESPGDLVFVNGKQWKRYRGMGSLGAMSSRGRTSYSKDRYFQADVSSDSKIVPEGIEGQVPYSGALGDVVYQLMGGLHQSMFYVGARTIPELKERGQFVRITSAGLKESHPHDVKMTVEAPNYTGRDGV$","Inosine-5'-monophosphate dehydrogenase","Cytoplasm","inosine-5'-monophosphate dehydrogenase","inosine-5'-monophosphate dehydrogenase ","inosine-5'-monophosphate dehydrogenase","","Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 2004. 113(2):274-284. PMID: 14722619Carr G., Simmons N., Sayer J. A role for CBS domain 2 in trafficking of chloride channel CLC-5. Biochem. Biophys. Res. Commun. 2003. 310(2):600-605. PMID: 14521953Hebeisen S., Biela A., Giese B., Muller-Newen G., Hidalgo P., Fahlke C. The role of the carboxyl terminus in ClC chloride channel function. J. Biol. Chem. 2004. 279(13):13140-13147. PMID: 14718533","","","

InterPro
IPR000644
Domain

Cystathionine-beta-synthase
PF00571	$\"[110-228]T$	CBS
SM00116	$\"[115-163]T$ $\"[180-228]T$	CBS

InterPro
IPR001093
Family

IMP dehydrogenase/GMP reductase
PTHR11911:SF6	$\"[20-504]T$	INOSINE-5-MONOPHOSPHATE DEHYDROGENASE
PF00478	$\"[26-503]T$	IMPDH
PS00487	$\"[319-331]T$	IMP_DH_GMP_RED

InterPro
IPR005990
Family

IMP dehydrogenase
TIGR01302	$\"[27-485]T$	IMP_dehydrog: inosine-5'-monophosphate dehy

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[17-516]T$	no description

noIPR
unintegrated

unintegrated
PIRSF000130	$\"[22-517]T$	Inosine-5'-monophosphate dehydrogenase
PTHR11911	$\"[20-504]T$	INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED

","BeTs to 23 clades of COG0516COG name: IMP dehydrogenase/GMP reductaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0516 is -ompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 2","***** IPB001093 (IMP dehydrogenase/GMP reductase) with a combined E-value of 2.4e-99. IPB001093A 28-37 IPB001093B 61-94 IPB001093C 311-345 IPB001093D 358-397 IPB001093E 450-479***** IPB004136 (2-nitropropane dioxygenase, NPD) with a combined E-value of 8.2e-08. IPB004136A 63-86 IPB004136D 358-388 IPB004136A 242-265 IPB004136D 295-325","Residues 200-482 are 83% similar to a (OXIDOREDUCTASE DEHYDROGENASE BIOSYNTHESIS GMP NAD INOSINE-5_apos;-MONOPHOSPHATE IMP REDUCTASE GUANOSINE IMPD) protein domain (PD000662) which is seen in IMDH_STAEP.Residues 121-157 are 83% similar to a (DEHYDROGENASE BIOSYNTHESIS OXIDOREDUCTASE CBS GMP NAD INOSINE-5_apos;-MONOPHOSPHATE DOMAIN REPEAT IMP) protein domain (PD000251) which is seen in Q6AD43_BBBBB.Residues 143-510 are 58% similar to a (INOSINE-5_apos;-MONOPHOSPHATE DEHYDROGENASE) protein domain (PD793953) which is seen in Q8EW89_MYCPE.Residues 159-514 are 68% similar to a (BIOSYNTHESIS DEHYDROGENASE IMP OXIDOREDUCTASE NAD GMP) protein domain (PD951621) which is seen in Q6M0Y5_METMP.Residues 171-217 are 70% similar to a (DEHYDROGENASE BIOSYNTHESIS OXIDOREDUCTASE GMP NAD INOSINE-5_apos;-MONOPHOSPHATE IMP CBS DOMAIN IMPD) protein domain (PD616152) which is seen in Q9L0I7_STRCO.Residues 200-482 are 83% similar to a (OXIDOREDUCTASE DEHYDROGENASE BIOSYNTHESIS GMP NAD INOSINE-5_apos;-MONOPHOSPHATE IMP REDUCTASE GUANOSINE IMPD) protein domain (PD000662) which is seen in IMDH_STAEP.Residues 227-305 are 77% similar to a (DEHYDROGENASE BIOSYNTHESIS IMPDH CBS REPEAT NAD PURINE GMP OXIDOREDUCTASE DOMAIN) protein domain (PDA1B920) which is seen in IMDH_MYCTU.Residues 234-514 are 71% similar to a (BIOSYNTHESIS DEHYDROGENASE IMPD IMP OXIDOREDUCTASE IMPDH REPEAT PURINE NAD CBS) protein domain (PD951619) which is seen in IMDH_METJA.Residues 235-505 are 51% similar to a (DEHYDROGENASE BIOSYNTHESIS IMPDH CBS 3D-STRUCTURE REPEAT NAD PURINE GMP OXIDOREDUCTASE) protein domain (PDA185T9) which is seen in IMDH_TRIFO.Residues 235-505 are 50% similar to a (OXIDOREDUCTASE INOSINE-5_apos;-MONOPHOSPHATE DEHYDROGENASE) protein domain (PDA183D3) which is seen in Q73JB0_TREDE.Residues 240-505 are 51% similar to a (OXIDOREDUCTASE INOSINE-5_apos;-MONOPHOSPHATE DEHYDROGENASE) protein domain (PDA182V2) which is seen in Q7MWR9_PORGI.","","-73% similar to PDB:1VRD Crystal structure of Inosine-5'-monophosphate dehydrogenase (TM1347) from THERMOTOGA MARITIMA at 2.18 A resolution (E_value = 2.1E_149);-71% similar to PDB:1ZFJ INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH; EC 1.1.1.205) FROM STREPTOCOCCUS PYOGENES (E_value = 4.5E_144);-68% similar to PDB:2CU0 Crystal structure of inosine-5'-monophosphate dehydrogenase from Pyrococcus horikoshii OT3 (E_value = 5.2E_124);-61% similar to PDB:1JCN BINARY COMPLEX OF HUMAN TYPE-I INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP (E_value = 7.1E_97);-61% similar to PDB:1B3O TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE (E_value = 2.7E_96);","Residues 26 to 503 (E_value = 7.4e-221) place ANA_0092 in the IMPDH family which is described as IMP dehydrogenase / GMP reductase domain.Residues 110 to 228 (E_value = 1.2e-24) place ANA_0092 in the CBS family which is described as CBS domain pair.","","dehydrogenase (guaB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0093","106737","105955","783","5.48","-8.12","27874","ATGAGCACCTCGCACTCCTCCTCCATGTCCGACGCCGCCGCCCCCGTTCCCTCCGCCTGGCCCTTCGGCCCCCTGCTCGGCTTCGACACTGAGACCACCGGAGTGGACCCTTCCGGCGACCGTCTGGTCACGGCGGCGCTCGTCTGGCGGGCGGCTCCTCGGGCCGACGGCGTCCGGCCGCAGTCGGTGACCACGTGGCTCGCAGACCCCGGCGTGGAGATCCCCGAGGCCGCCGCCGCGGTCCACGGCGTGACCACCGAGCGGGCCCGCGCCGAGGGTCGGCCGGTGACCGAGGTGCTGGCAGAGGTCAGTGAGCACCTGGTGGCTGCGATGGCGGCCGGCACCCCGGTCGTCGCCTTCAACGCCTCCTACGACCTAACACTCATGGAGGCCGAGCTCGCTCGCCACGGGCTGCCCACGATGCGCTCTCGCCTTGGCCGAGAGCTGGGGCCCATCGCCGACCCGCTGGTCCTGGACCGGGCCGTGGACCGCTACCGCCGCGGCAAGCGCCGCCTGGGCGACCTCTGCGAGGTCTACGGCGTGCGCGTCGATGAGGCCCTGCACACCGCGGAGGTGGATGTGGCCGCCACACTCGATGTGCTCGAGGCCCTGGCCGCGGCCCATCCGAAGCTCTCAGAGCTCAGCCCCGATGAGCTCGTGGCCTTCCAGGCCCGAGCCCACCGCACCTGGGCGGAGTCCTTCAACGAGTGGCTGGCGCGCAAGAACCCCTCGCGGACCCCGGCCCAGACCGCCTGGCCGCTGCCCGACTCCCCCACGCACTGA","MSTSHSSSMSDAAAPVPSAWPFGPLLGFDTETTGVDPSGDRLVTAALVWRAAPRADGVRPQSVTTWLADPGVEIPEAAAAVHGVTTERARAEGRPVTEVLAEVSEHLVAAMAAGTPVVAFNASYDLTLMEAELARHGLPTMRSRLGRELGPIADPLVLDRAVDRYRRGKRRLGDLCEVYGVRVDEALHTAEVDVAATLDVLEALAAAHPKLSELSPDELVAFQARAHRTWAESFNEWLARKNPSRTPAQTAWPLPDSPTH$","DNA polymerase III, epsilon subunit","Cytoplasm","putative DNA polymerase III epsilon subunit","DNA polymerase III subunit epsilon","Exonuclease, RNase T and DNA polymerase III","","Koonin E.V., Deutscher M.P. RNase T shares conserved sequence motifs with DNA proofreading exonucleases. Nucleic Acids Res. 1993. 21(10):2521-2522. PMID: 8506149","","","

InterPro
IPR006055
Domain

Exonuclease
SM00479	$\"[24-210]T$	EXOIII

InterPro
IPR013520
Domain

Exonuclease, RNase T and DNA polymerase III
PF00929	$\"[25-201]T$	Exonuc_X-T

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[24-212]T$	no description

","BeTs to 12 clades of COG0847COG name: DNA polymerase III epsilon subunit and related 3'-5' exonucleasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0847 is a--p--yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 24-85 are 75% similar to a (DNA POLYMERASE EPSILON III SUBUNIT III EXONUCLEASE SUBUNIT PROBABLE TRANSFERASE) protein domain (PD290303) which is seen in Q9L275_STRCO.Residues 28-87 are 58% similar to a (DNA POLYMERASE EXONUCLEASE EPSILON III TRANSFERASE III SUBUNIT CHAIN HYDROLASE) protein domain (PD002851) which is seen in Q82L65_STRAW.Residues 93-258 are 52% similar to a (DNA POLYMERASE III CGL1243 TYPE SUBUNIT ALPHA GRAM-POSITIVE THE EPSILON) protein domain (PD304463) which is seen in Q9L275_STRCO.Residues 98-183 are 70% similar to a (DNA POLYMERASE EXONUCLEASE EPSILON III III SUBUNIT TRANSFERASE T HYDROLASE) protein domain (PD369841) which is seen in Q9ADH9_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 25 to 201 (E_value = 9.5e-06) place ANA_0093 in the Exonuc_X-T family which is described as Exonuclease.","","DNA polymerase III epsilon subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0094","106876","108000","1125","6.82","-0.87","39923","ATGAGCACAGAGGTCGAGATCGGACGCTCCAAGCGTGCCCTGCGCGCCTACTCCTTCGACGACATCGCCCTGGTGCCGGCGCGCCGTACCCGGGACACCTCCGAGGTGCGCGTGGGCTGGCAGATCGACGCCTACCACGTGGATCTGCCGGTCATGGCCTCCCCCATGGACTCGGTGATGAGTCCCGAGACCGCCATTATGGTGGGGCGCCTGGGCGGCATCGGTGTGCTGGACCTGGAGGGCCTGTGGACCCGCTACGAGGACCCCACCGAGGCGCTCGAGCGCATCCGCCGGGCCGATCCGTCCCGGGCCACCAGCGTCCTGCAGGAGGTCTACCGCGCCCCGGTCAGACCCGAGCTCATCACCGAGCGGCTCACCCAGATCCGTGCCTCCGGCGTCGTCGTGGCAGGGCGACTCAGCCCCGCCCAGACACAGCGTCACTGGCGCACCGTGGTCGAGGCGGGTGTGGACCTCATGGTCATCCGCGGCTCCTTCGTGTCGGCCGAGCACGTCTCCGGATCCGTCGAGCCCCTCAACCTCAAACGCTTCATCTACGAGCTCGACGTGCCCGTGGTGGTCGGCGGGGTGACCACCTACACCGCTGCCCTCCACCTCATGCGCACCGGCGCGGCCGGAGTCCTCGTGGGGCAGGGTGGCGGGGCCTCCTCCTCCGTGCGCCAGGTCCTGGGACTGCACATGCCCATGGCCACCGCCGTGGCCGACGTTGCCGGGGCCCGGCGCGACTACCTCGACGAGTCCGGGGGCCGCTACGTCCATGTCATCGCCGACGGCTCGGTGGGCAACTCCGGCGACGTCGTCAAGGCCATCGCCTGCGGCGCGGACGCCGTCATGCTCGGGGCCGCCCTGGCCCGTGCCGAAGAGGCTCCCGGCGGCGGTTACCACTGGGGCGCCGAGGCCCGCCATGAGCGCCTGCCGCGGGGCTTCCGCAGCCACGTGGGCACAGTGGGCACCATGGCCGAGATCCTCAACGGCCCCTCCGACCGCGCCGACGGCACACTCAACCTCATGGGAGCGCTGCGCCGCACCCTGGCCACCACCGGCTACGCGGACGTCAAGGAGCTCCAGCGGGTCGAGGTCGTCCTGGCTCCCTACACCGGTTCTTGA","MSTEVEIGRSKRALRAYSFDDIALVPARRTRDTSEVRVGWQIDAYHVDLPVMASPMDSVMSPETAIMVGRLGGIGVLDLEGLWTRYEDPTEALERIRRADPSRATSVLQEVYRAPVRPELITERLTQIRASGVVVAGRLSPAQTQRHWRTVVEAGVDLMVIRGSFVSAEHVSGSVEPLNLKRFIYELDVPVVVGGVTTYTAALHLMRTGAAGVLVGQGGGASSSVRQVLGLHMPMATAVADVAGARRDYLDESGGRYVHVIADGSVGNSGDVVKAIACGADAVMLGAALARAEEAPGGGYHWGAEARHERLPRGFRSHVGTVGTMAEILNGPSDRADGTLNLMGALRRTLATTGYADVKELQRVEVVLAPYTGS$","Inositol-5-monophosphate dehydrogenase","Cytoplasm","IMP dehydrogenase family protein","putative inosine-5'-monophosphate dehydrogenase ","IMP dehydrogenase family protein","","Collart F.R., Huberman E. Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs. J. Biol. Chem. 1988. 263(30):15769-15772. PMID: 2902093Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K. Two distinct cDNAs for human IMP dehydrogenase. J. Biol. Chem. 1990. 265(9):5292-5295. PMID: 1969416Andrews S.C., Guest J.R. Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12. Biochem. J. 1988. 255(1):35-43. PMID: 2904262","","","

InterPro
IPR001093
Family

IMP dehydrogenase/GMP reductase
PTHR11911:SF6	$\"[3-369]T$	INOSINE-5-MONOPHOSPHATE DEHYDROGENASE
PF00478	$\"[236-297]T$	IMPDH

InterPro
IPR005992
Family

IMP dehydrogenase related 2
TIGR01304	$\"[5-368]T$	IMP_DH_rel_2: IMP dehydrogenase family prot

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[6-369]T$	no description

noIPR
unintegrated

unintegrated
PTHR11911	$\"[3-369]T$	INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED

","BeTs to 23 clades of COG0516COG name: IMP dehydrogenase/GMP reductaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0516 is -ompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 2","***** IPB001093 (IMP dehydrogenase/GMP reductase) with a combined E-value of 1.2e-60. IPB001093A 17-26 IPB001093B 49-82 IPB001093C 205-239 IPB001093D 259-298 IPB001093E 328-357***** IPB004136 (2-nitropropane dioxygenase, NPD) with a combined E-value of 2.1e-08. IPB004136A 51-74 IPB004136D 259-289 IPB004136D 189-219***** IPB000262 (FMN-dependent alpha-hydroxy acid dehydrogenase) with a combined E-value of 5.9e-07. IPB000262E 255-308","Residues 5-141 are 77% similar to a (DEHYDROGENASE IMP INOSINE-5_apos;-MONOPHOSPHATE OXIDOREDUCTASE REDUCTASE GMP NAD / GUAB3 FOR) protein domain (PD021741) which is seen in Q6AD45_BBBBB.Residues 15-362 are 60% similar to a (OXIDOREDUCTASE DEHYDROGENASE BIOSYNTHESIS GMP NAD INOSINE-5_apos;-MONOPHOSPHATE IMP REDUCTASE GUANOSINE IMPD) protein domain (PD000662) which is seen in Q7VBF7_PROMA.Residues 133-297 are 53% similar to a (BIOSYNTHESIS DEHYDROGENASE IMP OXIDOREDUCTASE NAD GMP) protein domain (PD951621) which is seen in Q6M0Y5_METMP.Residues 133-362 are 49% similar to a (BIOSYNTHESIS DEHYDROGENASE IMPD IMP OXIDOREDUCTASE IMPDH REPEAT PURINE NAD CBS) protein domain (PD951619) which is seen in IMDH_METJA.Residues 226-362 are 43% similar to a (OXIDOREDUCTASE INOSINE-5_apos;-MONOPHOSPHATE DEHYDROGENASE) protein domain (PDA182V2) which is seen in Q7MWR9_PORGI.Residues 226-335 are 56% similar to a (INOSINE-5_apos;-MONOPHOSPHATE DEHYDROGENASE) protein domain (PD793953) which is seen in Q8EW89_MYCPE.Residues 299-368 are 78% similar to a (DEHYDROGENASE INOSINE-5_apos;-MONOPHOSPHATE REDUCTASE GMP OXIDOREDUCTASE IMP NAD / GUAB3 FOR) protein domain (PD021372) which is seen in Q6A6W7_PROAC.","","-41% similar to PDB:1EEP 2.4 A RESOLUTION CRYSTAL STRUCTURE OF BORRELIA BURGDORFERI INOSINE 5'-MONPHOSPHATE DEHYDROGENASE IN COMPLEX WITH A SULFATE ION (E_value = 1.5E_13);-46% similar to PDB:2CU0 Crystal structure of inosine-5'-monophosphate dehydrogenase from Pyrococcus horikoshii OT3 (E_value = 2.8E_12);-41% similar to PDB:1VRD Crystal structure of Inosine-5'-monophosphate dehydrogenase (TM1347) from THERMOTOGA MARITIMA at 2.18 A resolution (E_value = 2.4E_11);-46% similar to PDB:1ZFJ INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH; EC 1.1.1.205) FROM STREPTOCOCCUS PYOGENES (E_value = 1.5E_10);","Residues 15 to 374 (E_value = 1e-15) place ANA_0094 in the IMPDH family which is described as IMP dehydrogenase / GMP reductase domain.","","dehydrogenase family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0095","108167","108433","267","4.55","-5.83","8606","ATGGCCCAGGTCACCGCCACCATCGCTTCCAAGGTCGGTCTGCACGCCCGTCCCGCTGCCACCTTCGTCAAGGCCGTCGCCGAGAAGGGCGTCCCGGTCACCATCGCCAAGGAGGGCGGCGCTGCGGTTGACGCCTCCTCCATCCTCGGTGTGATGACCCTGGGCGCCGGCTTCGGCGACGTCGTCACCCTGGCCTCCGACGCCGACGGCGCCGAGGCGGCCCTCGAGGACCTCAAGGCCCTCCTGGAGACCGACCTGGACGCCTGA","MAQVTATIASKVGLHARPAATFVKAVAEKGVPVTIAKEGGAAVDASSILGVMTLGAGFGDVVTLASDADGAEAALEDLKALLETDLDA$","Phosphocarrier, HPr family","Cytoplasm","phosphocarrier protein hpr","phosphocarrier; HPr family","phosphocarrier, HPr family","","Postma P.W., Lengeler J.W., Jacobson G.R. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 1993. 57(3):543-594. PMID: 8246840Meadow N.D., Fox D.K., Roseman S. The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Annu. Rev. Biochem. 1990. 59:497-542. PMID: 2197982van Nuland N.A., Boelens R., Scheek R.M., Robillard G.T. High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data. J. Mol. Biol. 1995. 246(1):180-193. PMID: 7853396Liao D.I., Herzberg O. Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins. Structure 1994. 2(12):1203-1216. PMID: 7704530","","","

InterPro
IPR000032
Family

Phosphotransferase system, phosphocarrier HPr protein
PD002238	$\"[12-63]T$	Q6ABG7_PROAC_Q6ABG7;
PR00107	$\"[13-29]T$ $\"[39-54]T$ $\"[54-71]T$	PHOSPHOCPHPR
G3DSA:3.30.1340.10	$\"[1-86]T$	no description
PF00381	$\"[1-85]T$	PTS-HPr

InterPro
IPR001020
PTM

Phosphotransferase system, HPr histidine phosphorylation site
PS00369	$\"[13-20]T$	PTS_HPR_HIS

InterPro
IPR005698
Family

Phosphotransferase system, HPr
TIGR01003	$\"[1-83]T$	PTS_HPr_family: phosphocarrier, HPr family

","BeTs to 11 clades of COG1925COG name: Phosphotransferase system, HPr-related proteinsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1925 is ---------d-lb-efghsn-j-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB000032 (Phosphocarrier protein signature) with a combined E-value of 2.9e-14. IPB000032A 13-29 IPB000032B 39-54 IPB000032C 54-71","Residues 12-63 are similar to a (PHOSPHOCARRIER HPR SYSTEM PHOSPHOTRANSFERASE HISTIDINE-CONTAINING PHOSPHORYLATION SUGAR TRANSCRIPTION REGULATION PTS) protein domain (PD002238) which is seen in Q6ABG7_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 85 (E_value = 9.4e-12) place ANA_0095 in the PTS-HPr family which is described as PTS HPr component phosphorylation site.","","protein hpr (PTS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0096","108535","109428","894","11.16","9.04","29892","ATGAGCATTGCCATCGCCCTCGTGCCCTCCCTGCTGTTCGGGGCACTGTCCCTTCTTCTCGGAGCCTTCCCCACCGACATCCGCCGCCAGAACACCGCGGTCATGGTGGGAGCGGGAGCCGTCTCGCTCGGATGCACCGCCATGCTCGGCTCGTCCTGGTCTCTGAGCGCCACCGTGTGGGGCGTGGTCTGCGGACTCATGTGGACCGGCGGGCAGGTCTTCGTCCTGTGGGCCTTCCGCGCCTGGGGCGTCAGTCGCACCATGCCTCTGACCACCGCCCTCCAGCTCCTGCTCAACGCCACCCTGGGTGTGAGCCTCTTCGGTGAGTGGCGCGCTCCCGGGGCCCTGATCCTGGGGGTGGTGGCGCTCGCGCTCATCATGCTCGGCGCCGCCGCTTGCTCCTGGCAGGAGCGCACCGGCCCCGGTCCCACGGCCGCGCAGCGACGTGCCGGTCTGCTGGCCACCGCGGCCTCAGCCGTCCTCTACGGCTCCTACCCCTCGCTGCTGCGCGCCGTTGAGGTGCCCCCGGCCCACGCCGTCGGCCCCATGGGGCTGGGACTGCTGGCTGGTGCCGGACTGTGCGCTCTCATCCTGCCGCGGCGCGCGCCCCTACGAGGCCCGAGGATCGTTCCGGCCGCGCTCGCCGGGGGCCTGTGGGCGGTCGGTAACGCCCTCATGCTGCGCTCGACGGCGGCTGTTGGGGTGGCCTCCGGCTTCACCCTCTCCCAGCTTGGCTTCGTCCTGGCCACCATCGGTGGTCTGACCATCCTGGGGGAGGAGCGCACCGGTCGGGAACGCGCCGTGGTGGCTGCCGGCGTCGCGGCAGCCGTCGTCGGTCTGGTCCTCATGGGCCTGGCGACCAGCATGGACACCGGTGTGTCCCCGTCACAGTAG","MSIAIALVPSLLFGALSLLLGAFPTDIRRQNTAVMVGAGAVSLGCTAMLGSSWSLSATVWGVVCGLMWTGGQVFVLWAFRAWGVSRTMPLTTALQLLLNATLGVSLFGEWRAPGALILGVVALALIMLGAAACSWQERTGPGPTAAQRRAGLLATAASAVLYGSYPSLLRAVEVPPAHAVGPMGLGLLAGAGLCALILPRRAPLRGPRIVPAALAGGLWAVGNALMLRSTAAVGVASGFTLSQLGFVLATIGGLTILGEERTGRERAVVAAGVAAAVVGLVLMGLATSMDTGVSPSQ$","Glucose uptake protein","Membrane, Extracellular","glucose uptake protein homolog lin0215","K05340 glucose uptake protein","sugar transport family protein","","Fiegler H., Bassias J., Jankovic I., Bruckner R. Identification of a gene in Staphylococcus xylosus encoding a novel glucose uptake protein. J. Bacteriol. 1999. 181(16):4929-4936. PMID: 10438764","","","

InterPro
IPR010651
Family

Sugar transport
PF06800	$\"[13-283]T$	Sugar_transport

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[32-52]?$ $\"[58-78]?$ $\"[87-107]?$ $\"[113-135]?$ $\"[150-169]?$ $\"[179-199]?$ $\"[209-229]?$ $\"[235-257]?$ $\"[267-287]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB010651 (Sugar transport) with a combined E-value of 5.6e-41. IPB010651A 3-51 IPB010651B 82-125 IPB010651E 219-272","Residues 1-265 are 54% similar to a (SUGAR UPTAKE TRANSMEMBRANE GLUCOSE GLCU PROBABLE RBSU RIBOSE SPORULATION LIN0215) protein domain (PD017526) which is seen in Y215_LISIN.","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 283 (E_value = 3.7e-19) place ANA_0096 in the Sugar_transport family which is described as Sugar transport protein.","","uptake protein homolog lin0215","","1","","","","","","","","","","","Mon Aug 13 10:37:18 2007","","Mon Aug 13 10:37:18 2007","","","Mon Aug 13 10:37:18 2007","Mon Aug 13 10:37:18 2007","Mon Aug 13 10:37:18 2007","","Mon Aug 13 10:37:18 2007","Mon Aug 13 10:37:18 2007","","","","","yes","","" "ANA_0097","109807","109583","225","6.44","-0.11","7774","ATGAACAATCGTTCACTCACGGACATCCGGGCGGTCATCACCGGGGCTCTGGGGCTCATCGGCCTCTACCTGGTGGTGTGCTCGGTCCTGTTCAACAGCGCCGAGGAGATGAGCAAGACCGGCGGCATCAACGCCAACCTGTGGTCAGGTCTGGGTCTGTTGGCCATCGCCGCGGGCATGGGCCTGTGGTGGTGGATCAAGCCGAATCCCTCCGGGGGCGAGTAA","MNNRSLTDIRAVITGALGLIGLYLVVCSVLFNSAEEMSKTGGINANLWSGLGLLAIAAGMGLWWWIKPNPSGGE$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[12-32]?$ $\"[46-66]?$	transmembrane_regions

InterPro
IPR001734
Family

Na+/solute symporter
PTHR11819	$\"[39-246]T$ $\"[267-464]T$	SODIUM/SOLUTE SYMPORTER
PF00474	$\"[69-496]T$	SSF
TIGR00813	$\"[69-496]T$	sss: transporter, solute:sodium symporter (
PS50283	$\"[38-510]T$	NA_SOLUT_SYMP_3

noIPR
unintegrated

unintegrated
PTHR11819:SF7	$\"[39-246]T$ $\"[267-464]T$	SODIUM/GLUCOSE COTRANSPORTER
tmhmm	$\"[40-60]?$ $\"[75-93]?$ $\"[112-134]?$ $\"[155-175]?$ $\"[185-205]?$ $\"[215-233]?$ $\"[282-302]?$ $\"[334-354]?$ $\"[383-412]?$ $\"[433-453]?$ $\"[459-479]?$ $\"[488-508]?$ $\"[518-538]?$ $\"[577-595]?$	transmembrane_regions

","BeTs to 20 clades of COG0591COG name: Na+/proline, Na+/panthothenate symporters and related permeasesFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism],RThe phylogenetic pattern of COG0591 is aompkzyq-d--bcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001734 (Na+/solute symporter) with a combined E-value of 2.3e-40. IPB001734A 70-98 IPB001734B 184-237 IPB001734C 287-328 IPB001734D 467-496","Residues 37-83 are 74% similar to a (TRANSMEMBRANE SYMPORTER COTRANSPORTER PERMEASE SODIUM/PROLINE TRANSPORTER SODIUM FAMILY PROLINE SODIUM:SOLUTE) protein domain (PD001069) which is seen in Q6NHW8_CORDI.Residues 45-239 are 44% similar to a (SYMPORTER SODIUM:SOLUTE PROBABLE SODIUM/PROLINE) protein domain (PD673154) which is seen in Q6D0N4_BBBBB.Residues 97-149 are 94% similar to a (TRANSMEMBRANE COTRANSPORTER SODIUM/GLUCOSE NA/GLUCOSE SODIUM SYMPORT SUGAR AFFINITY GLYCOPROTEIN SODIUM-GLUCOSE) protein domain (PD002423) which is seen in Q6A5R4_PROAC.Residues 186-247 are 91% similar to a (TRANSMEMBRANE SYMPORTER COTRANSPORTER PERMEASE SODIUM/PROLINE FAMILY SODIUM PROLINE TRANSPORTER SYMPORT) protein domain (PD186798) which is seen in Q6A5R4_PROAC.Residues 302-396 are 85% similar to a (TRANSMEMBRANE SYMPORTER COTRANSPORTER SODIUM/PROLINE SODIUM PERMEASE PROLINE FAMILY TRANSPORTER SYMPORT) protein domain (PD000991) which is seen in Q6NHW8_CORDI.Residues 404-483 are 85% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/PROLINE PERMEASE COTRANSPORTER TRANSPORTER FAMILY PROLINE SODIUM SODIUM:SOLUTE) protein domain (PD477036) which is seen in Q6A5R4_PROAC.Residues 485-595 are 68% similar to a (SODIUM:SOLUTE TRANSMEMBRANE SYMPORTER NA/GALACTOSE COTRANSPORTER) protein domain (PD283278) which is seen in Q6NHW8_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 69 to 496 (E_value = 9.8e-15) place ANA_0098 in the SSF family which is described as Sodium:solute symporter family.","","Na+-galactose cotransporter (SGLT1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0099","111811","112377","567","7.39","0.61","19898","ATGACGCTGACTGCTGCTGCCGACGGCTCCTCCCTGGGCAATCCGGGACCGGCCGGCTGGGCCTGGTACGTGGACGATGACTGCTGGGCCGCTGGAGGCTGGGAGAGCTCGACCAACAACCGCGGCGAGCTCACCGCCGTCCTGGAGCTCCTGCGGGCCACCGAGGCCGCCGGGCTCGCCGGCGAGGAGCTTCTCATCCAGTGCGACTCCCAGTACGTCATCAACTCCCTGACCAAGTGGCGCCACGGCTGGAAGAAGCGCGGCTGGCGCAAGGCCGACGGCAAGCCCGTCCTCAACGCCGACCTCGTCAAGGACCTCGACGCCGCGCTCGCGGGCCGCACCGTGCGCTTCGAGTGGGTGCGCGGGCACGTCGGCCACCCCATGAACGAGGCCGCCGACTCCCGGGCCCGCGGCGCTGCCACCGCCTTCCAGCAGGGCCGCCCGGTGCCCGTGGGACCGGGCTGGACCCGGGGCGGTCGGGCACCGGGGAATCGGGAGGCGCAGCAGGCACCTGGTGCCACGCCGTCGAGCGCCCCCGCTGCGCCGCAGACCGACGCCCTGTTCTGA","MTLTAAADGSSLGNPGPAGWAWYVDDDCWAAGGWESSTNNRGELTAVLELLRATEAAGLAGEELLIQCDSQYVINSLTKWRHGWKKRGWRKADGKPVLNADLVKDLDAALAGRTVRFEWVRGHVGHPMNEAADSRARGAATAFQQGRPVPVGPGWTRGGRAPGNREAQQAPGATPSSAPAAPQTDALF$","Ribonuclease HI","Periplasm, Extracellular","ribonuclease HI","ribonuclease HI ","Ribonuclease H","","Goedken E.R., Marqusee S. Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension. Proteins 1998. 33(1):135-143. PMID: 9741851Ey P.L., Freeman N.L., Bela B., Haese P.M., Li P., McInnes J.L. Sequence and comparative structural analysis of the murine leukaemia virus amphotropic strain 4070A RNase H domain. Arch. Virol. 1999. 144(11):2185-2199. PMID: 10603172Yang W., Hendrickson W.A., Crouch R.J., Satow Y. Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. Science 1990. 249(4975):1398-1405. PMID: 2169648Katayanagi K., Okumura M., Morikawa K. Crystal structure of Escherichia coli RNase HI in complex with Mg2+ at 2.8 A resolution: proof for a single Mg(2+)-binding site. Proteins 1993. 17(4):337-346. PMID: 8108376Davies I.I. J.F., Hostomska Z., Hostomsky Z., Jordan S.R., Matthews D.A. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science 1991. 252(5002):88-95. PMID: 1707186","","","

InterPro
IPR002156
Domain

Ribonuclease H
PF00075	$\"[8-141]T$	RnaseH
PS50879	$\"[1-141]T$	RNASE_H

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[3-140]T$	no description
PTHR10642	$\"[1-145]T$	RIBONUCLEASE H1

","BeTs to 15 clades of COG0328COG name: Ribonuclease HIFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0328 is -o----y--dr-bcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB002156 (RNase H) with a combined E-value of 2.3e-14. IPB002156A 3-24 IPB002156B 63-73 IPB002156C 119-133","Residues 3-47 are similar to a (RIBONUCLEASE HYDROLASE H HI) protein domain (PD873976) which is seen in Q6A706_PROAC.Residues 8-47 are 64% similar to a (RIBONUCLEASE HI HYDROLASE H RNASE ENDONUCLEASE NUCLEASE MAGNESIUM TRANSFERASE DNA) protein domain (PD774933) which is seen in Q54388_STRLN.","","-49% similar to PDB:1RBT STRUCTURAL STUDY OF MUTANTS OF ESCHERICHIA COLI RIBONUCLEASE HI WITH ENHANCED THERMOSTABILITY (E_value = 1.5E_19);-49% similar to PDB:1F21 DIVALENT METAL COFACTOR BINDING IN THE KINETIC FOLDING TRAJECTORY OF E. COLI RIBONUCLEASE HI (E_value = 7.3E_19);-49% similar to PDB:1JXB I53A, a point mutant of the cysteine-free variant of E. coli Rnase HI (E_value = 7.3E_19);-48% similar to PDB:1RBU STRUCTURAL STUDY OF MUTANTS OF ESCHERICHIA COLI RIBONUCLEASE HI WITH ENHANCED THERMOSTABILITY (E_value = 7.3E_19);-48% similar to PDB:1RBV STRUCTURAL STUDY OF MUTANTS OF ESCHERICHIA COLI RIBONUCLEASE HI WITH ENHANCED THERMOSTABILITY (E_value = 7.3E_19);","Residues 4 to 141 (E_value = 1.4e-30) place ANA_0099 in the RnaseH family which is described as RNase H.","","HI ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0100","113703","112978","726","6.96","-0.09","26402","GTGAGTCCATCCGCCCCCTCCGGGTCAGGCACCGAGAGCTCGTCGAGCCACCTCAGGCCGATCACGGTGATGATCGTCGACGACCAGCGAGCCACCCGCATGGGCCTGTCCCTCATCATCAACCGGGCCGACGACCTGCAGGTCACGGCCGAGGCCGTCCACGGTCAGGACACCCTCGACCAGCTCGCCGCCCTGCTTGAGGAGCGCCGGCCGCTTCCCGACGTCGTCCTCATGGACGTGCGCATGCCGGTGCTCAACGGGATCGATGCCACGGCCCGCATCTGCCAGCTCTACCCCTCAATCCGGGTCCTGGTGCTGACCACCTACGACCAGGACGAGTTCGCCTTCGGGGCGCTGTCGGCCGGCGCCTCAGGGTTCCTGCTCAAAGACACCCGCACGGCCGACCTCCACCAGGCGCTGCGGGCGGTCAGCTCCGGGGACGCGATCCTCACTCCGCGCATCACCCGCGAGCTGCTCAACCGGCACATGCTCAGCCCCGTGGCCTCACCCCGTCAGCGCGCGGCACGCCAGCGCCTCGACGATCTCAGCCCCCGCGAGCGCGAGGTGGCCGACCTGGTGTCCCAGGGGCTGACGAACGCGGAGATCGCTCAGCGCCTCGTCCTGGCCCCGGACTCGGTCAAGAAGAACGTCACCCGGATCCTGACCAAGCTGGACCTGCGCGACCGGGTCCAGCTCGTCATCCTCATGCGCGACGCCCAGTCCTGA","VSPSAPSGSGTESSSSHLRPITVMIVDDQRATRMGLSLIINRADDLQVTAEAVHGQDTLDQLAALLEERRPLPDVVLMDVRMPVLNGIDATARICQLYPSIRVLVLTTYDQDEFAFGALSAGASGFLLKDTRTADLHQALRAVSSGDAILTPRITRELLNRHMLSPVASPRQRAARQRLDDLSPREREVADLVSQGLTNAEIAQRLVLAPDSVKKNVTRILTKLDLRDRVQLVILMRDAQS$","Two-component system response regulator","Cytoplasm, Membrane","chitinase two-component response regulator","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[182-234]T$	Q9ZBU8_STRCO_Q9ZBU8;
PR00038	$\"[182-196]T$ $\"[196-212]T$ $\"[212-224]T$	HTHLUXR
PF00196	$\"[179-236]T$	GerE
SM00421	$\"[179-236]T$	HTH_LUXR
PS50043	$\"[175-240]T$	HTH_LUXR_2
PS00622	$\"[196-223]T$	HTH_LUXR_1

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[21-144]T$	Q82ES8_STRAW_Q82ES8;
PF00072	$\"[21-141]T$	Response_reg
SM00448	$\"[21-140]T$	REC
PS50110	$\"[22-144]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[155-240]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[16-148]T$	no description
PTHR23283	$\"[22-144]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF41	$\"[22-144]T$	TWO COMPONENT SENSOR AND REGULATOR HISTIDINE KINASE BACTERIA

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 4e-17. IPB000792 182-228***** IPB000673 (CheB methylesterase) with a combined E-value of 2.5e-11. IPB000673B 46-99 IPB000673C 100-130***** IPB005143 (Autoinducer binding domain) with a combined E-value of 3.2e-09. IPB005143B 182-225***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 4.6e-08. IPB001867A 74-87 IPB001867B 102-146***** IPB001789 (Response regulator receiver) with a combined E-value of 8.8e-07. IPB001789A 74-87 IPB001789B 122-132","Residues 21-144 are 64% similar to a (SENSORY TRANSDUCTION PHOSPHORYLATION REGULATOR DNA-BINDING TRANSCRIPTION REGULATION RESPONSE TWO-COMPONENT KINASE) protein domain (PD000039) which is seen in Q82ES8_STRAW.Residues 182-234 are 83% similar to a (DNA-BINDING TRANSCRIPTION REGULATION REGULATOR SENSORY PHOSPHORYLATION TRANSDUCTION RESPONSE TRANSCRIPTIONAL TWO-COMPONENT) protein domain (PD000307) which is seen in Q9ZBU8_STRCO.","","-54% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 1.2E_22);-54% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 1.2E_22);-44% similar to PDB:1YIO Crystallographic structure of response regulator StyR from Pseudomonas fluorescens (E_value = 7.1E_10);-44% similar to PDB:1ZN2 Low Resolution Structure of Response Regulator StyR (E_value = 7.1E_10);","Residues 21 to 141 (E_value = 9.2e-31) place ANA_0100 in the Response_reg family which is described as Response regulator receiver domain.Residues 172 to 224 (E_value = 4.5e-05) place ANA_0100 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 179 to 236 (E_value = 1.7e-16) place ANA_0100 in the GerE family which is described as Bacterial regulatory proteins, luxR family.","","two-component response regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0101","115022","113700","1323","6.72","-1.91","45695","ATGAGCCACGTTCTCGCAGTGCCCGAGCCGGCACACGTCTCCCGGGTCCCACGGACCCTCCTGGACCGGGTGGCTCAGTGGTGGCGCACCAGCGCCCTGACCCTGTGGGCGGTGGCCGGGGCCGCGGGCCTCTTCCAGCTGATGGTGCTGAACGTGGCCTCGTACACCTACCCGCACCTGCCCCTGCGAGGCTGGGTGATCGTCGCCCTGCTGCTCGCTGCTTCACTGGTGGCCCGACGCCGCTGGCCCCTCGCCGTCGTCATTGTCACGAGCCTGGCCTCGGGCGCCGTCGACCTGTGGGGGACGCGCGGCGGACTCAACCTGCTGTCCATGCTGGCCCTCTACGCCCTGCTCGTGGCCGCCCCCACCCGCGACCGAATCATCGGCTTCAGCATCAGCGCGCTGTGCACCCTCGTCCCCACGGCACTGGCCAAGTGGCCACAGGTGAGCACGTTGAGCCCGGGAATCCTCATCCTGGTCCTCGTGCTCGCGGTGGCCTCGATCTCCCGCTCACGCCGGGAGGCCCTGGAACACGGGGACGCCCAGCTGGCAGCACAGTCCGCCGAACATCGGCTGGTCGCCCAGCGCGACGCCGCCCGCCACCAGGCCCGGGTGGCGGCCGAGCTCCACGACTCCGTGGGCCACGCCCTGACCGCGATCATCGCCCTATCTGAGGGGATGCAGGGGGCCGGCGGCAGCCCACAGACAGATGAGGCCATTGACATGATGAACGCCCTGGCCCGCGAGGGTCTGGCCGACACCCGACGCGCCGTCGCCTCACTCCAGACGGCACCGGGCCCCTCCCCCGACGACGCCGAGACCACCGACCCCCTCACCGGCCGGGTCTTGGAGGGCCCGCAGTCCCCCTCGGGCGCAGCCGGCTGGGACCGGCTCGACGACCTGCTGACCACGGTGAGAGCCACCGGTATCAGTGCGGCTCTCACCGAGACCGGCAGGCGCCCCCTCGACGCCTCAAGCAGTCAGGCGCTCGGGGAGGTCGTCTATGTCGTCGTCCGGGAGGCCCTGACCAATGTCATGCGCCACGCCGAGGGCGCCACGCGCGTCGTCGTCTCCCTGGACCACGATCAGGCCGCCACCCGGATCACCGTGTCCGACGACGGTCGCGCCGCTCAGCCAGGCCACGCAGACGGCTTCCCGGGCTCGTCTCAGGCACCGGCGGCGGCCGGCCACGGGCTGGCGAACCTGGCAGCCGCGGTCGGTGAGCACGGCGGCACGCTGTCGGCCGGCCCCACAGCCGATGAGGGCGCATCCGGCTGGGTACTGCGCGCCCTCGTCCCCTTCCCGGAAGGTGCATCACGGTGA","MSHVLAVPEPAHVSRVPRTLLDRVAQWWRTSALTLWAVAGAAGLFQLMVLNVASYTYPHLPLRGWVIVALLLAASLVARRRWPLAVVIVTSLASGAVDLWGTRGGLNLLSMLALYALLVAAPTRDRIIGFSISALCTLVPTALAKWPQVSTLSPGILILVLVLAVASISRSRREALEHGDAQLAAQSAEHRLVAQRDAARHQARVAAELHDSVGHALTAIIALSEGMQGAGGSPQTDEAIDMMNALAREGLADTRRAVASLQTAPGPSPDDAETTDPLTGRVLEGPQSPSGAAGWDRLDDLLTTVRATGISAALTETGRRPLDASSSQALGEVVYVVVREALTNVMRHAEGATRVVVSLDHDQAATRITVSDDGRAAQPGHADGFPGSSQAPAAAGHGLANLAAAVGEHGGTLSAGPTADEGASGWVLRALVPFPEGASR$","Two-component system sensor kinase","Membrane, Cytoplasm","probable two-component sensor, putative","two-component system sensor kinase","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[329-435]T$	HATPase_c
SM00387	$\"[329-438]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[203-266]T$	HisKA_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[33-51]?$ $\"[57-77]?$ $\"[82-102]?$	transmembrane_regions

","BeTs to 7 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 1.6e-10. IPB011712A 200-217 IPB011712B 334-354","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 203 to 266 (E_value = 1.5e-12) place ANA_0101 in the HisKA_3 family which is described as Histidine kinase.Residues 329 to 435 (E_value = 4.6e-10) place ANA_0101 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","two-component sensor, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0102","115912","115019","894","11.46","15.58","31525","ATGAGCACCACCGCACCAGTCACACGTTCCACGGCAGGCCGGCCCCTCCGGCCCGCTCAGCACCCGTCAACGCTCCCCGGTCCCTCCGGCCCATCCACGACGCCGCAACCGACTATCCTGAGCCGGTCTGCTCCACCCGCTCCCCAGTCCCGCCCGTCGGTGCGAGCCGCCTGGTACTGGGAGAACCGCAAGGCCCCCAACCGGTGGTACTGGGTCGCCGTCACCATCCTGTGCTCCCTAGGCTCCCTGTCCGGCTACCTGCAGTACCGCAGCTACCGCAGCCAGTTCGAGGCTCAGGGCGCCACCTGGGAGATCACGTGGTCCCAGTCCACGCTCCTGCTCTCGATGCTGTTCCTGCCGCTGGCGCTGGGTGCCTTCGCCGCGCAGATCGCCAGCAGTGAGCACCAGGGAAGAAACTGGCAGAGAATGAGCGCCACCGGGCTGGAGACCGCCATGGTTGCGGGCAAGCTGCTGCACGGGCTCCAGGTCGCGGCTCTCACCACCGCGGTCCTGGCCCTGACCACCGCGGTGACGGGCCTCGCCCTGGGCTTCAACCTGGTGGGTCTGGTCGCCTACCTGCCGCGCTTCGCCGTCGTCGCGCTGGGAATGTGGGTCATCCTCACCTTCGTCACCTGGCTGGGCGCGGTCATGACGTCCTTCGCCACCACGATGTCCACCGTGCTGCTGAGCACCATTGCGGGGATGGCGATGCTTCTCGCGGCCCGACCGCTGAGTGTCCTCAACCCCGCAGCCTCACTGACCCGAACCACGTCCGCTATGAGCCCGGGCAACGTGGCCTCACCGGGCGCCGCAGCATTCGAGGGCGTCATCTGCCTGGTGTGGGTGGCCCTGCTGGCCCTGGCTCTGCGCCGCGCAGTGAGGCGACAGTCATGA","MSTTAPVTRSTAGRPLRPAQHPSTLPGPSGPSTTPQPTILSRSAPPAPQSRPSVRAAWYWENRKAPNRWYWVAVTILCSLGSLSGYLQYRSYRSQFEAQGATWEITWSQSTLLLSMLFLPLALGAFAAQIASSEHQGRNWQRMSATGLETAMVAGKLLHGLQVAALTTAVLALTTAVTGLALGFNLVGLVAYLPRFAVVALGMWVILTFVTWLGAVMTSFATTMSTVLLSTIAGMAMLLAARPLSVLNPAASLTRTTSAMSPGNVASPGAAAFEGVICLVWVALLALALRRAVRRQS$","Membrane protein","Periplasm, Membrane","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[69-89]?$ $\"[113-133]?$ $\"[164-184]?$ $\"[190-210]?$ $\"[220-240]?$ $\"[269-289]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[62-82]?$ $\"[101-123]?$ $\"[148-170]?$ $\"[184-204]?$ $\"[214-234]?$ $\"[277-297]?$	transmembrane_regions

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[224-266]T$	Q6HMF7_BACHK_Q6HMF7;
PF00005	$\"[122-300]T$	ABC_tran
PS50893	$\"[97-324]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[121-323]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[91-315]T$	no description
PTHR19222	$\"[97-314]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[97-314]T$	ABC TRANSPORTER

","BeTs to 16 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.4e-23. IPB005074C 111-158 IPB005074D 212-255***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.9e-19. IPB013563A 111-145 IPB013563C 221-248***** IPB005116 (TOBE domain) with a combined E-value of 2.4e-10. IPB005116A 129-145 IPB005116D 244-263***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3.3e-08. IPB010509B 122-147 IPB010509D 219-263***** IPB013283 (ABC transporter family E signature) with a combined E-value of 1.4e-06. IPB013283D 126-151","Residues 89-155 are 60% similar to a (ATP-BINDING PROTEIN CYDCD) protein domain (PDA1B3E1) which is seen in Q6ABD5_PROAC.Residues 90-192 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 93-326 are 45% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 95-284 are 46% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 96-192 are 50% similar to a (ATP-BINDING PHOSPHONATE ABC-TYPE PROTEIN) protein domain (PDA0J3O0) which is seen in Q6MPJ3_BDEBA.Residues 96-198 are 53% similar to a (ABC-TYPE ATP-BINDING) protein domain (PD253636) which is seen in Q9HQA8_HALN1.Residues 97-157 are 68% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 101-194 are 53% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 102-341 are 45% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 107-280 are 52% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 108-282 are 48% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 109-297 are 46% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 109-303 are 45% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 112-196 are 57% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187K3) which is seen in Q897D7_CLOTE.Residues 112-160 are 89% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9F2X6_STRCO.Residues 112-314 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 115-292 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD398054) which is seen in Q9CDL6_LACLA.Residues 115-282 are 52% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 126-302 are 43% similar to a (VEXC POLYSACCHARIDE VI ATP-BINDING INNER MEMBRANE BIOSYNTHESIS EXPORT) protein domain (PD416480) which is seen in VEXC_SALTI.Residues 135-284 are 45% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD784154) which is seen in Q88X92_LACPL.Residues 173-302 are 55% similar to a (LACF ATP-BINDING) protein domain (PD807654) which is seen in Q9RAV2_LACLA.Residues 181-306 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 199-317 are 48% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 200-320 are 55% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 203-282 are 53% similar to a (COMPONENT ABC ATPASE ATP-BINDING TRANSPORTER) protein domain (PDA0I0K5) which is seen in Q74HP7_LACJO.Residues 209-299 are 62% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18641) which is seen in Q8EG59_SHEON.Residues 211-282 are 63% similar to a (ATP-BINDING LONG TRANSPORTER ABC 331AA 298AA) protein domain (PD502979) which is seen in Q96ZV0_SULTO.Residues 218-304 are 57% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 219-312 are 60% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 224-282 are 67% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 224-266 are 93% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6HMF7_BACHK.","","-57% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 5.5E_30);-54% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.4E_25);-54% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.4E_25);-54% similar to PDB:1OXU Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.4E_25);-54% similar to PDB:1OXV Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.4E_25);","Residues 122 to 300 (E_value = 4.7e-52) place ANA_0104 in the ABC_tran family which is described as ABC transporter.","","transporter MutF","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0105","119460","118171","1290","5.49","-15.12","45873","GTGGGACCGGGACCCGACCCCACGCCGCTGAAGCCCACCCGGGATCCCGCATCAGTCATCCAGTCATCCCCGCGTTCATCCCCGACCGTTCTTGAAAGGCACCCCGTGACTCAGCGCACCGTCCTCGTTATCAACTCCGGCTCCTCCTCCATCAAGTACCAGCTGGTCGACCCCGACTCGGGCGCCTCGCTCGCCTCCGGCCTGGTGGAGCGCATCGGTGAGGAGACCGGCGCCATCACCCACAAGCACGGCGAGGAGCGCACCGAGATCACCGAGCCGGTCCCCGACCACGGCTTCGGCCTGTCCGAGGTGCTGCGCCTGTTCGAGGAGCAGGGCCCCTCGCTGGCCGACGCCCACATCGTGGCCGTGGGCCACCGGGTCGTCCAGGGCGGGCGCTACTTCTCCGGCCCGGCCCTCATCGACGACGACGTCGTGGCCCGGATCGAGCAGCTCGTGCCGCTGGGCCCGCTGCACAACCCCGCCCACCTCAAGGGCATCGAGGTGGGGCGCCGCCTCCTGTCCGACGTGCCGCACGTGGCCGTCTTCGACACCGCCTTCTTCCAGGACCTGCCCGAGGAGGCCGCCCGCTACGCCCTGGACCGCGAGGTCGCCGACACCTACTCCATCCGCCGCTACGGGGCTCACGGCACCAGCCACCAGTTCGTCTCCGGGGCGGTCTCCGAGCTCCTGGGGCGCGACGACCTCAAGCAGGTCGTCCTGCACCTGGGCAACGGGGCCTCGGCCTCGGCGGTCGTGGCCGGGCACGCCGTGGACACCTCCATGGGCCTGACCCCGCTGGAGGGCCTGGTCATGGGCGGGCGCACCGGCGACATCGACCCGGCCGCCGTCTTCCACCTGGCACGCGTGGCCGGCATGTCCATCGACGAGATCGACCACCTGTTCAACCGCGGCTCGGGCATGAAGGGCCTGGCCGGGGACAACGACATGCGCGAGGTGTGGAAGCGCATCGGCGCCGGTGAGCAGGAGGCCCGCGAGGCCATGGACATCTACCTGCACCGGCTCGTGAAGTACGTGGGCGCCTACACCGCCGTCATGGGAGGCCTGGACGCCCTGACCTTCACCGCCGGTATCGGCGAGAACGACGCGAACCTGCGCCGTGAGCTCGGCGAGCGCCTGGGCTTCATGGGTGTCAAGATCGACCAGGGGGTCAACGAGACCCGCTCCGACGAGCCGCGCGTCATCTCCACCCCGGACTCGAAGGTCACCGTGCTCGTGGTGCCCACCAACGAGGAGCTCGCCATCGCACGCCAGGCGCTCACCCTCATCTGA","VGPGPDPTPLKPTRDPASVIQSSPRSSPTVLERHPVTQRTVLVINSGSSSIKYQLVDPDSGASLASGLVERIGEETGAITHKHGEERTEITEPVPDHGFGLSEVLRLFEEQGPSLADAHIVAVGHRVVQGGRYFSGPALIDDDVVARIEQLVPLGPLHNPAHLKGIEVGRRLLSDVPHVAVFDTAFFQDLPEEAARYALDREVADTYSIRRYGAHGTSHQFVSGAVSELLGRDDLKQVVLHLGNGASASAVVAGHAVDTSMGLTPLEGLVMGGRTGDIDPAAVFHLARVAGMSIDEIDHLFNRGSGMKGLAGDNDMREVWKRIGAGEQEAREAMDIYLHRLVKYVGAYTAVMGGLDALTFTAGIGENDANLRRELGERLGFMGVKIDQGVNETRSDEPRVISTPDSKVTVLVVPTNEELAIARQALTLI$","Acetate kinase","Cytoplasm","acetate kinase","acetate kinase ","acetate kinase","","Poland B.W., Silva M.M., Serra M.A., Cho Y., Kim K.H., Harris E.M., Honzatko R.B. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 1993. 268(34):25334-25342. PMID: 8244965Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 2000. 296(2):569-577. PMID: 10669609","","","

InterPro
IPR000890
Family

Acetate and butyrate kinase
PR00471	$\"[41-52]T$ $\"[209-222]T$ $\"[237-258]T$ $\"[333-346]T$ $\"[355-371]T$ $\"[410-422]T$	ACETATEKNASE
PTHR21060	$\"[41-428]T$	FAMILY NOT NAMED
PF00871	$\"[40-423]T$	Acetate_kinase
PS01075	$\"[41-52]T$	ACETATE_KINASE_1
PS01076	$\"[237-254]?$	ACETATE_KINASE_2

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[138-411]T$	no description

InterPro
IPR004372
Family

Acetate kinase
PIRSF000722	$\"[39-429]T$	Acetate/propionate kinase
TIGR00016	$\"[36-429]T$	ackA: acetate kinase

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.40	$\"[39-219]T$	no description
PTHR21060:SF10	$\"[41-428]T$	gb def: Acetate kinase (EC 2.7.2.1) (Acetokinase)

","BeTs to 15 clades of COG0282COG name: Acetate kinaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0282 is --------vdrlbcefgh-nujx-twNumber of proteins in this genome belonging to this COG is 1","***** IPB000890 (Acetate and butyrate kinase) with a combined E-value of 1.3e-87. IPB000890A 41-52 IPB000890B 122-132 IPB000890C 155-166 IPB000890D 179-208 IPB000890E 210-221 IPB000890F 233-275 IPB000890G 301-316 IPB000890H 356-367 IPB000890I 412-422","Residues 41-82 are 78% similar to a (KINASE ACETATE TRANSFERASE ACETOKINASE PROPIONATE 2.7.2.- PROBABLE ACKA 3D-STRUCTURE SEQUENCING) protein domain (PD808637) which is seen in Q726S6_DESVH.Residues 107-166 are 68% similar to a (KINASE ACETATE TRANSFERASE ACETOKINASE PROPIONATE 2.7.2.- ACKA PROBABLE 3D-STRUCTURE SEQUENCING) protein domain (PD479864) which is seen in ACK1_NEIMB.Residues 175-232 are 77% similar to a (KINASE ACETATE TRANSFERASE ACETOKINASE PROPIONATE 2.7.2.- ACKA PROBABLE 3D-STRUCTURE SEQUENCING) protein domain (PD348124) which is seen in ACKA_MYCTU.Residues 261-372 are similar to a (KINASE ACETATE TRANSFERASE ACETOKINASE BUTYRATE PROBABLE BK BRANCHED-CHAIN ACID CARBOXYLIC) protein domain (PD003226) which is seen in Q82JD1_STRAW.Residues 383-428 are 80% similar to a (KINASE ACETATE TRANSFERASE ACETOKINASE PROPIONATE 2.7.2.- PROBABLE 3D-STRUCTURE SEQUENCING DIRECT) protein domain (PD135366) which is seen in Q8G5N7_BIFLO.","","-62% similar to PDB:1G99 AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA (E_value = 7.4E_81);-62% similar to PDB:1TUU Acetate Kinase crystallized with ATPgS (E_value = 7.4E_81);-62% similar to PDB:1TUY Acetate Kinase complexed with ADP, AlF3 and acetate (E_value = 7.4E_81);-57% similar to PDB:1X3M Crystal structure of ADP bound Propionate kinase (TdcD) from Salmonella typhimurium (E_value = 2.6E_65);-57% similar to PDB:1X3N Crystal structure of AMPPNP bound Propionate kinase (TdcD) from Salmonella typhimurium (E_value = 2.6E_65);","Residues 40 to 423 (E_value = 2.6e-168) place ANA_0105 in the Acetate_kinase family which is described as Acetokinase family.","","kinase (ackA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0106","121528","119474","2055","4.78","-33.88","71832","GTGGCGCGCAGTATCTACATCGCCTCACCCAACGCCGGAACCGGGAAGTCAACGGTGGCCCTCGGGCTGGTCTCCTGTCTGACCAAGGTGGTCGCCAAGGTCGGCGTCTTCCGCCCCTTCGTGGAGAGCCGTGAGGGCGATGCCTTCCTCAGCCTCCTGCTGAACCGTGCCGGCTCCACCACGCCCCCCGAGCAGTGCGTCGGCGCGACCTGGGACGAGTTCCACGCCGACCCCGAGGAGGCCCTGGCACGCATCGTCGACGCCTACCGGGCCATGGCGCGCGAGCACGACGTCGTCATCATCGACGGCTCGGACTTCACCGACGTCGCCGGCAACCCCGAGCTGGCCCTCAACGCCCGGGTAGCGGCCAACATCGGCGTCCCGGTGCTGCTGGTGGTCTCCGGGCAGAATGACGTGGAGGACGTCGTCGCCTCCGTGGAGGTCTCCATGGCCGAGATCGCCGACAACCACGCCCGCACCGTCGCGGTCGTGGCCAACAAGTGCCTGCCTGAGACCCGCCAGGCCGTCGGCGAGGCACTGACCGCCATCGAGGGCATCACCTCCACCACGCTGCCCGAGGTGCCGCTGCTGGCGGCCCCGGTGGTGCGCGAGGTGCTCGACGCCGTCGAGGGCACTCTCATCGCCGGTGACGAGACGCTGCTCGACCGCGAGGCCGAGTCCGTCCTCGTGTGCGCCATGGACGTCTCCCACGTCCTGGAGCGCCTGACCGCGGGACAGCTCGCCATCGTCCCGGCCGACCGCTCCGCCATGCTCATCTCCCTCATGGCGGCCCAGGCCTCCTCGAGCTTCCCGATCCTGTCGGGTCTCATCCTCAACGGCGGCTTCGAGGTGGCGCCCCACGCGCTGCGCCTCCTGGAGGGGCTGGACGTCAACATCCCGGTCATCACCTCCCCGCTGGACACCTTCGCCGCCGCCTCCGCAGCCGGCTCCCTGCAGGGCCTGCTCGCCCACGGCTCCGAGCGCAAGATCGACGTCGCCGTGACCACCTTCGAGCAGGAGGCCGACGTCGAGGCCCTCCTGTCGGCCCTGGAGGTCGAGCCCTCCGAAGTCGTCACCCCCATCATGTTCCAGGCCGAGCTGGTGGAGCGCTCGCGCACCAACCGCAAGACCATCGTCCTGCCCGAGCCCGACGACGACCGGGTCCTGCGCGCCGCCGACGCCATCCTGCGCCGCGGCATCGCCGACCTGGTGCTGCTGGGTGACGAGACCACGGTGCGGGCCCGCGCCACCGAGCTGGGCCTGGACATCGCCGCCGCCCGAGTCGTCGCCACCAACGACCCCGAGCTGCTGGAGAAGTACGCCGAGGAGTTCGCCCGCCTGCGCGCCAAGAAGGGCGTCACCCTCGAGCAGGCCCGCGAGAAGGTCCAGGACGTGTCCTACTTCGGCACGATGATGGTCCACATGGGAGACGCCGACGGCATGGTCTCGGGCGCCGCCCACACCACCGCCCACACGATCGTCCCCTCCTTCCAGATCATCAAGACCAAGCCGGGGACCTCCATCGTCTCCTCGGTCTTCCTCATGCTCCTGCAGGACCGGGTGCTCGTCTACGGCGACTGCGCCGTCAACCCCGAGCCCAACGCCGCCGAGCTGGCCGACATCGCCATCTCCTCGGCCGCCACCGCCCGCCAGTTCGGCGTCGAGCCGCGCGTGGCGATGCTGTCCTTCTCCACCGGGACCTCCGGCAAGGGCGCGGACGTGGACAAGGTCCGTGAGGCCACCGAGCTGGTGCGGGCCAAGGAGCCCGACCTCGCCGTCGAGGGCCCCATCCAGTACGACGCCGCCATCGACCCGACCGTGGCCGCCAAGAAGGCCCCGGACTCGCTCGTGGCCGGACGGGCCAACGTCTTCATCTTCCCGGACCTGTCCAGCGGCAACATCGGCTACAAGGCGGTCCAGCGCTCCTCGGGCGCCATCGCCATCGGCCCGGTCCTTCAGGGGCTCAACAAGCCGGTCAACGACCTCTCGCGCGGCGCCCTGGTGGAGGACATCATCAACACCGTCGCCATCACCGCCGTCCAGGCCCAGGGCTGA","VARSIYIASPNAGTGKSTVALGLVSCLTKVVAKVGVFRPFVESREGDAFLSLLLNRAGSTTPPEQCVGATWDEFHADPEEALARIVDAYRAMAREHDVVIIDGSDFTDVAGNPELALNARVAANIGVPVLLVVSGQNDVEDVVASVEVSMAEIADNHARTVAVVANKCLPETRQAVGEALTAIEGITSTTLPEVPLLAAPVVREVLDAVEGTLIAGDETLLDREAESVLVCAMDVSHVLERLTAGQLAIVPADRSAMLISLMAAQASSSFPILSGLILNGGFEVAPHALRLLEGLDVNIPVITSPLDTFAAASAAGSLQGLLAHGSERKIDVAVTTFEQEADVEALLSALEVEPSEVVTPIMFQAELVERSRTNRKTIVLPEPDDDRVLRAADAILRRGIADLVLLGDETTVRARATELGLDIAAARVVATNDPELLEKYAEEFARLRAKKGVTLEQAREKVQDVSYFGTMMVHMGDADGMVSGAAHTTAHTIVPSFQIIKTKPGTSIVSSVFLMLLQDRVLVYGDCAVNPEPNAAELADIAISSAATARQFGVEPRVAMLSFSTGTSGKGADVDKVREATELVRAKEPDLAVEGPIQYDAAIDPTVAAKKAPDSLVAGRANVFIFPDLSSGNIGYKAVQRSSGAIAIGPVLQGLNKPVNDLSRGALVEDIINTVAITAVQAQG$","Phosphate acetyltransferase","Cytoplasm, Membrane","Phosphate acetyltransferase(Phosphotransacetylase)","phosphate acetyltransferase ","phosphate acetyltransferase","","","","","

InterPro
IPR002505
Domain

Phosphate acetyl/butaryl transferase
PF01515	$\"[362-679]T$	PTA_PTB

InterPro
IPR004614
Domain

Phosphate acetyltransferase
TIGR00651	$\"[378-679]T$	pta: phosphate acetyltransferase

InterPro
IPR010766
Domain

DRTGG
PF07085	$\"[204-318]T$	DRTGG

noIPR
unintegrated

unintegrated
PTHR23406	$\"[429-682]T$	MALIC ENZYME-RELATED
PTHR23406:SF3	$\"[429-682]T$	PHOSPHATE ACETYLTRANSFERASE
signalp	$\"[1-32]?$	signal-peptide

","BeTs to 17 clades of COG0280COG name: PhosphotransacetylaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0280 is -o------vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 1","***** IPB002505 (Phosphate acetyl/butaryl transferase) with a combined E-value of 4e-90. IPB002505A 379-389 IPB002505B 464-515 IPB002505C 556-568 IPB002505D 589-632 IPB002505E 648-680***** IPB010766 (DRTGG) with a combined E-value of 8.4e-13. IPB010766B 646-681","Residues 5-137 are 69% similar to a (DETHIOBIOTIN SYNTHETASE TRANSFERASE PHOSPHATE ACETYLTRANSFERASE SYNTHASE LIGASE DTB DTBS BIOSYNTHESIS) protein domain (PD583611) which is seen in PTA_MYCTU.Residues 5-195 are 42% similar to a (PHOSPHATE ACETYLTRANSFERASE TRANSFERASE) protein domain (PD822881) which is seen in Q8G5N8_BIFLO.Residues 191-309 are 63% similar to a (TRANSFERASE PHOSPHATE ACETYLTRANSFERASE ACYLTRANSFERASE PHOSPHOTRANSACETYLASE CBS INORGANIC DOMAIN PROBABLE DOMAINS) protein domain (PD108213) which is seen in Q7U221_MYCBO.Residues 367-452 are 73% similar to a (TRANSFERASE PHOSPHATE ACETYLTRANSFERASE OXIDOREDUCTASE ACYLTRANSFERASE ENZYME PHOSPHOTRANSACETYLASE MALIC NADP-DEPENDENT MALATE) protein domain (PD650840) which is seen in Q7U221_MYCBO.Residues 453-546 are similar to a (TRANSFERASE PHOSPHATE ACETYLTRANSFERASE OXIDOREDUCTASE ACYLTRANSFERASE ENZYME PHOSPHOTRANSACETYLASE MALIC NADP-DEPENDENT MALATE) protein domain (PD319787) which is seen in PTA_SYNY3.Residues 543-657 are similar to a (TRANSFERASE PHOSPHATE ACETYLTRANSFERASE ACYLTRANSFERASE OXIDOREDUCTASE PHOSPHOTRANSACETYLASE ENZYME MALIC NADP-DEPENDENT MALATE) protein domain (PD002789) which is seen in Q6AGY8_BBBBB.","","-67% similar to PDB:1R5J Crystal Structure of a Phosphotransacetylase from Streptococcus pyogenes (E_value = 7.5E_81);-66% similar to PDB:1TD9 Crystal Structure of a Phosphotransacetylase from Bacillus subtilis (E_value = 4.2E_76);-66% similar to PDB:1XCO Crystal Structure of a Phosphotransacetylase from Bacillus subtilis in complex with acetylphosphate (E_value = 4.2E_76);-64% similar to PDB:1QZT Phosphotransacetylase from Methanosarcina thermophila (E_value = 4.1E_71);-64% similar to PDB:2AF3 Phosphotransacetylase from Methanosarcina thermophila soaked with Coenzyme A (E_value = 4.1E_71);","Residues 204 to 318 (E_value = 3.3e-25) place ANA_0106 in the DRTGG family which is described as DRTGG domain.Residues 362 to 679 (E_value = 2.9e-186) place ANA_0106 in the PTA_PTB family which is described as Phosphate acetyl/butaryl transferase.","","acetyltransferase (Phosphotransacetylase) (fragment)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0107","122703","121711","993","9.34","6.78","35194","ATGGCTCTCGTGCGCCGCTGGCTGTTGGCGGCGGCCAGCCTGGGACTGCTGGTCATCACTCTCAGCGGCACACTCCTGCCGCACCAGACCGAGATTCTGCGTTCACTGAGCCCAGCCGCCTCCGGCAGCGACGCCGGTCCCGGTCAGGTCTCGTTGCCACAGGCGGTCGAGGTGATCAAGAACCGCCATCCCGACGAGCCGGTCCTGTCGGCAAGGTGGGACACCGACGTCGTCGAGGTGCGGACCGAGCAAGGCACCTACGCGATTGATCCCTCCACCGGGCACGAGATCAGCAGGGCGTCGGCGGCACCGGTCTGGGTCGCCGTCCTGGACAACCTGCACCGCTGCCTGCTGTCCTGTCGGGGGCCCGGCCACGTGCACTGGATGTCCCAGGAGATCCCCCACACCGGCTGGTGGGCCGGCCAGCGGAGCCTGACCGTCGGGGGCCTGGTCGTGGCCACCGCTGGCGTGGTCCTCGTGGTCCTGACCGTCAGCGGGCTGCGCACATGGTGGCCGCTGCAGCGCCATCGACGCACAGCTCTGTCCTCCCACTGGCGCACTCAGCGCCTCTCCCGGGACACCGACCTGCTCAAGGCGGCCGGACTGGTCCTTCTCCCCCTGCTGTTCCTGTGGGGCTACTACGCCAGCGCGTTCAGTATCCGCCCCACCCAACCGGCCTCACCGGTCTCCATGACCGCTCACCAGTCCCCGGCGGAACCGACCAGCGCGGGCCGGGCCCAGGACATCGGGCCGCATCGCGCCGTCGCTGCAGCGCAGGAAGCGGGCGGCGGACAGGCGGTCGCCCTGTTCCTGCCTCAGCCGGGCGACCCGTCGTCGACCTACACGGTCTGGATCTCTCAAGGAGCACGGTTCGCCCCCCGGAAGTCCCCCGACGATGTCGCGGTGAGCATCGCAGTGAATGTCGACCCCGGAACCGGACGGACCACACTCCCCTCCACACCCGGCCACCGGCCGACCACTCAGGCGGACTAG","MALVRRWLLAAASLGLLVITLSGTLLPHQTEILRSLSPAASGSDAGPGQVSLPQAVEVIKNRHPDEPVLSARWDTDVVEVRTEQGTYAIDPSTGHEISRASAAPVWVAVLDNLHRCLLSCRGPGHVHWMSQEIPHTGWWAGQRSLTVGGLVVATAGVVLVVLTVSGLRTWWPLQRHRRTALSSHWRTQRLSRDTDLLKAAGLVLLPLLFLWGYYASAFSIRPTQPASPVSMTAHQSPAEPTSAGRAQDIGPHRAVAAAQEAGGGQAVALFLPQPGDPSSTYTVWISQGARFAPRKSPDDVAVSIAVNVDPGTGRTTLPSTPGHRPTTQAD$","Hypothetical protein","Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[7-27]?$ $\"[147-167]?$ $\"[195-215]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[57-77]?$ $\"[83-101]?$ $\"[111-131]?$	transmembrane_regions

InterPro
IPR002781
Family

Protein of unknown function DUF81
PF01925	$\"[31-276]T$	DUF81

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[21-43]?$ $\"[53-73]?$ $\"[94-114]?$ $\"[120-138]?$ $\"[199-219]?$ $\"[225-247]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 170-276 are similar to a (MEMBRANE INTEGRAL PROTEIN PLASMID INNER DUF81 PERMEASE PRECURSOR SIGNAL TOU2) protein domain (PD575902) which is seen in Q9KZC0_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 31 to 276 (E_value = 5.2e-26) place ANA_0109 in the DUF81 family which is described as Domain of unknown function DUF81.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0110","124248","124646","399","5.07","-5.01","13613","GTGCTGCCTGGGGCTGCGTCAACGGGGTGCCGCAGCGGTGCGCAGCAGCGTGGCGATCCCGGAGACGCCCAGGAAGATGAGTGCCGTTGCGGGCAGGGTTGCGCTGAGCAGGTGGTCCCAAAGAGCAGTGCGCTGGGTCGTCAGTCCGATCCCATGAAGCAGGCCGAGAGCGGCTGCTCCTGCGCCGATCGAGAGGATCGAGACCGCGGCTCGCAGCGCCCGTCTGGCAGCCGGCCAAGGAGTGATGAGCTGCAGCGGGGGCAGGGCCGCCCAGGCCGTGAGCCCGGCGATGCACCAGAGAAGTGCGCTCGAGGCGGGGGAGGCCTCTCCGAGCAGATTGCCAAGCTTCCCCAGGCCCACGCAGACGACCCAGATGACGGCGCAGTAGGCGACCAGTAG","VLPGAASTGCRSGAQQRGDPGDAQEDECRCGQGCAEQVVPKSSALGRQSDPMKQAESGCSCADREDRDRGSQRPSGSRPRSDELQRGQGRPGREPGDAPEKCARGGGGLSEQIAKLPQAHADDPDDGAVGDQ$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Sottrup-Jensen L. Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem. 1989. 264(20):11539-11542. PMID: 2473064Enghild J.J., Salvesen G., Thogersen I.B., Pizzo S.V. Proteinase binding and inhibition by the monomeric alpha-macroglobulin rat alpha 1-inhibitor-3. J. Biol. Chem. 1989. 264(19):11428-11435. PMID: 2472396Enghild J.J., Thogersen I.B., Roche P.A., Pizzo S.V. A conserved region in alpha-macroglobulins participates in binding to the mammalian alpha-macroglobulin receptor. Biochemistry 1989. 28(3):1406-1412. PMID: 2469470van Leuven F., Cassiman J.J., Van den berghe H. Human pregnancy zone protein and alpha 2-macroglobulin. High-affinity binding of complexes to the same receptor on fibroblasts and characterization by monoclonal antibodies. J. Biol. Chem. 1986. 261(35):16622-16625. PMID: 2430968Dodds A.W., Law S.K. The phylogeny and evolution of the thioester bond-containing proteins C3, C4 and alpha 2-macroglobulin. Immunol. Rev. 1998. 166:15-26. PMID: 9914899","","","

InterPro
IPR001599
Domain

Alpha-2-macroglobulin
PS00477	$\"[31-39]?$	ALPHA_2_MACROGLOBULIN

InterPro
IPR012307
Domain

Xylose isomerase-like TIM barrel
PF01261	$\"[111-326]T$	AP_endonuc_2

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.150	$\"[106-363]T$	no description
PTHR12110	$\"[201-371]T$	HYDROXYPYRUVATE ISOMERASE

","BeTs to 3 clades of COG1082COG name: Sugar phosphate isomerases/epimerasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1082 is a-m-k---v-r-bcef-----j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 84-129 are 69% similar to a (CATABOLISM MYO-INOSITOL IOLE MOCC RHIZOPINE IOLB ENDONUCLEASE CATABOLISMPROTEIN INOSITOL AGR_L_177GMP) protein domain (PD469793) which is seen in Q9KAH0_BACHD.Residues 108-357 are 43% similar to a (MLR7228) protein domain (PD464560) which is seen in Q986S5_RHILO.Residues 141-216 are similar to a (CATABOLISM MYO-INOSITOL IOLE MOCC RHIZOPINE IOLB ENDONUCLEASE CATABOLISMPROTEIN INOSITOL AGR_L_177GMP) protein domain (PD715929) which is seen in Q8ZK58_SALTY.Residues 234-309 are similar to a (CATABOLISM MYO-INOSITOL IOLE PLASMID MOCC RHIZOPINE IOLB CATABOLISMPROTEIN ENDONUCLEASE INOSITOL) protein domain (PD040390) which is seen in Q8ZK58_SALTY.Residues 316-357 are 76% similar to a (RHIZOPINE MODC CATABOLISM) protein domain (PDA137A0) which is seen in Q98LI7_RHILO.","","No significant hits to the PDB database (E-value < E-10).","Residues 111 to 326 (E_value = 8.2e-43) place ANA_0112 in the AP_endonuc_2 family which is described as Xylose isomerase-like TIM barrel.","","catabolism iolE","","1","","","Thu Jun 7 18:18:02 2007","Thu Jun 7 18:18:02 2007","Thu Jun 7 18:18:02 2007","","","Thu Jun 7 18:18:02 2007","Thu Jun 7 18:18:02 2007","Thu Jun 7 18:18:02 2007","","","","","","Thu Jun 7 18:15:13 2007","","Thu Jun 7 18:15:13 2007","","Thu Jun 7 18:15:13 2007","Thu Jun 7 18:15:13 2007","","","","","yes","","" "ANA_0113","127810","126155","1656","7.97","2.84","59696","ATGTCTCAGGGAGTCACGACGTCCCTGCGTGGACTCACCAGGGAAGAGCTCAACAAGGCGGTGGCCGAAACGCCGCCTTCGGGCAAGCACCGCGGCGTCATCGCCATCGCCGCCGTGGCCACGCTCGGCTCACTGCTCTTCGGCTACGACACCGGCGTCATCTCCGGCGCCCTGCCATACATGTACATGCCCCTTGGCGCCAAGGGCCTCCAGCTGACCTCCTTCGAGGAGGGCGCCATCGGTGGCACCCTGCTGGTCGGCGCGGCGCTGGGCGCGCTGCTGGGCGGCCTGATGTCGGACCGCTGGGGCCGGCGCCACAACATCACCGTCCTGGCCTTCCTGTTCTTCGCCGGCGCACTGGGCACCACGTTCGCCCCCAACGTCTGGGTCATGTACCCCTTCCGCGTCATCCTGGGCTTCGCCGTCGGAGCCGCCTCCGCGACGGTTCCCGTCTACCTGGCGGAGACGGCGCCCAAACGCATCCGCGGCTCCATCGTGGCCATCGACCAGCTCATGATCGTCACCGGCCAGCTGCTCGCCTTCTCGATGAACGCCATCATCAACTCCCTCCAGGGCGGCCCGCGGGTCACCATCGCTGAGGACCCCAGCGGGCACTTCGCCCCGAACACCTACGCCTTCGACGAGATCGCCAAGCTCCAGTCCTCCAAGGGCGGCCCGATGAGCGCAAACGAGTACCACGCCTTCCTCGACCAGCTCAGCATCAGCGCCGGTAACGGTGAGGCCTGGCGCTACATGCTGGTCCTGTGCTCTATCCCGGCCGTAGCCCTGTGGATCGGCATCCGCCTCATGCCCGAGTCCTCGCGCTGGTACCTGGCCAAGGAGCGCCTCTACGACGCCATCGGCGCCCTCAAGCGCGTGCGCGTCCCGGAGAAGGACGGCTCCATCGAGGACGAGATCATGGAGATGGTCGAGGCCCGCCGGCACGAGAAGGACGAGGAGTCCCAGCGCAAGGGCTTCAGCCACGTCATGGCCACGCCCTGGCTGCGCAAGCTGCTGCTGGTCGGCATCTTCCTGGCCGTGGTCAACCAGACCACCGGCGTCAACACCGTCATGTACTACGCCCCCAAGGTGCTGGAGTACGCCGGCATGTCCACCTCGGCCTCCATCACCGCGCAGGTGGCCAACGGCGTCATGTCGGTCATCGGCTCCGCCATCGGCGTCTGGCTCATCCTGAAGTTCCGGCGCCGCCAGGTCCTCATCGGCGACGTCATCGGCGTGGGCTTCACCCTGCTGGGCATCGCAGCGACCTTCCAGTTCTTCATCGCCCCGCACATGGCCAACCACACCACTCCGCCCACCTGGGCCGCCTATCTCATCCTCGGGCTCATGTCGGTCTTCATGCTCATCGTGCAGTCCTCCAACGGCACGATCGTGTGGACGATGATGGGTGAGATCTTCCCGGCCAACGTCCGCGGCATCATGAACGGCACGGCGATCTTCTGCATGTGGACCGCCAACGCCATCATCACCTGGACCTTCCCGCCCATGATGGAGACCCTGGGCGGCGGCATCACCTACACCATCTACGGCGTGCTCAACCTGGTCGTCGCCGTCGTCCTGTTCAAGATCATGCCGGAGACCAAGGACAAGTCCCTGGAGGAGATCGAGGTCGAGATGGAGAAGCTCTACTCCTGA","MSQGVTTSLRGLTREELNKAVAETPPSGKHRGVIAIAAVATLGSLLFGYDTGVISGALPYMYMPLGAKGLQLTSFEEGAIGGTLLVGAALGALLGGLMSDRWGRRHNITVLAFLFFAGALGTTFAPNVWVMYPFRVILGFAVGAASATVPVYLAETAPKRIRGSIVAIDQLMIVTGQLLAFSMNAIINSLQGGPRVTIAEDPSGHFAPNTYAFDEIAKLQSSKGGPMSANEYHAFLDQLSISAGNGEAWRYMLVLCSIPAVALWIGIRLMPESSRWYLAKERLYDAIGALKRVRVPEKDGSIEDEIMEMVEARRHEKDEESQRKGFSHVMATPWLRKLLLVGIFLAVVNQTTGVNTVMYYAPKVLEYAGMSTSASITAQVANGVMSVIGSAIGVWLILKFRRRQVLIGDVIGVGFTLLGIAATFQFFIAPHMANHTTPPTWAAYLILGLMSVFMLIVQSSNGTIVWTMMGEIFPANVRGIMNGTAIFCMWTANAIITWTFPPMMETLGGGITYTIYGVLNLVVAVVLFKIMPETKDKSLEEIEVEMEKLYS$","Sugar transporter, MFS superfamily","Membrane, Cytoplasm","sugar transporter homolog ydjK","sugar transporter; MFS superfamily","sugar transporter","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR003663
Family

Sugar transporter
PR00171	$\"[44-54]T$ $\"[132-151]T$ $\"[349-359]T$ $\"[447-468]T$ $\"[470-482]T$	SUGRTRNSPORT
TIGR00879	$\"[2-542]T$	SP: MFS transporter, sugar porter (SP) fami

InterPro
IPR005828
Family

General substrate transporter
PF00083	$\"[36-546]T$	Sugar_tr

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[95-112]?$	SUGAR_TRANSPORT_1
PS00217	$\"[137-162]T$	SUGAR_TRANSPORT_2

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[36-535]T$	MFS

noIPR
unintegrated

unintegrated
PTHR11600	$\"[31-194]T$ $\"[249-403]T$	SUGAR TRANSPORTER
PTHR11600:SF85	$\"[31-194]T$ $\"[249-403]T$	SUGAR TRANSPORTER
tmhmm	$\"[33-53]?$ $\"[78-98]?$ $\"[108-126]?$ $\"[132-154]?$ $\"[166-186]?$ $\"[249-267]?$ $\"[339-359]?$ $\"[378-398]?$ $\"[407-427]?$ $\"[441-459]?$ $\"[480-500]?$ $\"[510-528]?$	transmembrane_regions

","BeTs to 18 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","***** IPB005829 (Sugar transporter superfamily) with a combined E-value of 5.6e-37. IPB005829A 44-55 IPB005829B 131-178 IPB005829D 349-369 IPB005829E 531-542***** IPB003663 (Sugar transporter signature) with a combined E-value of 1.6e-21. IPB003663A 44-54 IPB003663B 132-151 IPB003663C 349-359 IPB003663D 447-468 IPB003663E 470-482","Residues 98-128 are 90% similar to a (TRANSMEMBRANE TRANSPORTER SUGAR RESISTANCE FAMILY MEMBRANE MULTIDRUG FACILITATOR MAJOR PROBABLE) protein domain (PD000082) which is seen in Q6AAJ7_PROAC.Residues 134-168 are 94% similar to a (TRANSMEMBRANE SUGAR TRANSPORTER GLUCOSE FAMILY PHOSPHATE GLYCOPROTEIN HEXOSE PERMEASE CARRIER) protein domain (PD860544) which is seen in Q6AAJ7_PROAC.Residues 169-227 are 72% similar to a (SUGAR TRANSPORTER FAMILY YFIG) protein domain (PD923410) which is seen in Q6AAJ7_PROAC.Residues 234-282 are 89% similar to a (TRANSMEMBRANE SUGAR TRANSPORTER GLUCOSE FAMILY GLYCOPROTEIN CARRIER ORGANIC MEMBER HEXOSE) protein domain (PD197893) which is seen in Q6AAJ7_PROAC.Residues 282-352 are 64% similar to a (SUGAR FAMILY TRANSPORTER) protein domain (PD945642) which is seen in Q6AAH6_PROAC.Residues 285-352 are 77% similar to a (SUGAR TRANSPORTER YFIG) protein domain (PD945641) which is seen in Q6AAJ7_PROAC.Residues 353-397 are 95% similar to a (SUGAR TRANSMEMBRANE TRANSPORTER GLUCOSE FAMILY GLYCOPROTEIN HEXOSE CARRIER MONOSACCHARIDE FACILITATED) protein domain (PD000712) which is seen in Q6AAJ7_PROAC.Residues 357-543 are 46% similar to a (TRANSMEMBRANE CG4797-PA RH09188P CG4797-PB SD10060P) protein domain (PD602677) which is seen in Q9W1J2_DROME.Residues 399-483 are similar to a (SUGAR TRANSMEMBRANE TRANSPORTER FAMILY METABOLITE PROBABLE SUGI INTEGRAL PHOSPHATE MEMBRANE) protein domain (PD261536) which is seen in Q6AAJ7_PROAC.Residues 489-540 are 92% similar to a (SUGAR TRANSMEMBRANE TRANSPORTER GLUCOSE FAMILY GLYCOPROTEIN HEXOSE CARRIER PERMEASE FACILITATED) protein domain (PD001518) which is seen in Q6AAJ7_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 36 to 546 (E_value = 1.2e-74) place ANA_0113 in the Sugar_tr family which is described as Sugar (and other) transporter.Residues 40 to 505 (E_value = 3.4e-24) place ANA_0113 in the MFS_1 family which is described as Major Facilitator Superfamily.","","transporter homolog ydjK (permease)","","1","","","","","","","","","","","Mon Aug 13 17:16:21 2007","","Mon Aug 13 17:16:21 2007","","","Mon Aug 13 17:16:21 2007","Mon Aug 13 17:16:21 2007","Mon Aug 13 17:16:21 2007","","Mon Aug 13 17:16:21 2007","Mon Aug 13 17:16:21 2007","","","","","yes","","" "ANA_0114","129277","127910","1368","5.12","-16.02","49207","GTGAGCACGAGGCCCTGCTCAGAGAGGTCATCAGACCTCATACTTCCCTCTTGTCAGGACAAAGGTGCTCTGATATCTTCCTGTGACGTCATTAACGACGGGTGTCTCCTGGGGCTTCCGGAGACACCTCCACACACACAGCAGCCGACAATGTTGTCGGGAAGGACCGTTATGGCCAATAAGTCAATACTGGGCATCGGAGTCATCTCCCTGGGCTGGATGGGACGGCTTCACTCCCGCAGCTACCGCGCCATCGCCGAGCGCTTCCCCGAGCTGGGGGTGACCCCACGGCTGGTCGCCGCCGCGGACCCGGTGGACGAGGTGCGTCAGGAGGCGGTGGACAACCTGGGCTTCGAGCGCGCCTACGCCGACTACCGCGACCTGCTGGCCGACCCCGAGGTGGAGGCCGTCTCCATCTGCGCCCCCAACTTCCTCCACCACGAGATGGCCCTGGCGGCCGTCGAGGCCGGCAAGCCCTTCTGGATCGAGAAGCCCATGGGGGTCAGCGCCGAGCAGTCCCGGCAGATCGCCCAGGCCGCCGAGAAGGCGGGGCTGATGACCGCCGTCGGCTTCAACTACCGCCACACCCCGGCCATCGAGTACCTGCGCTCCCTGGTACGCGGCGGCGAGCTCGGCCGGATCACGAACGTGCGCGTGTGGTTCATCGCCGACTACAACTCCTCCCCCATGGGGCCCCTGACCTGGCGGGCCTCGAAGGAGAAGGCCGGGGCCGGCGTCGTGCCCGACCTCATGAGCCACGGGGCGGACCTGGCCCAGTACATCGTGGGGCGCATCGCCTCGGTCACCGCGGTCACCGACACCTTCATCACTGAGCGCCCCATCCCCACCAAGATGGGCATCGGCCACTCGGGCTTCGAGATCGGCGACGATGTGGGCCCGGTGGAGAACGAGGACTACGTCTCCATGCTCGTGCGCTTCGAGAACGGCACCGTGGGGACCATGGAGTCCTCCCGCGTCAGCGTGGGACCGCGCGCCGAGTATGTCGTCGAGGTCTACGGCACGAAGGGCTCGGCCCGCTGGAACTTCGAGCGCCTCAACGAGCTGGAGATCTGCCCCGTGCTCGACGGCGGCGCCTCCCACGGCTACACCCGCGCCATGGCCGGCCCCCAGTGGGGCCAGTGGCAGCGCTTCCAGCCCGCCATCGGCACTTCCATGGGCTTTGACGACATGAAGGCCATCGAGGCCGCGCAGTTCATCGAGTCGATCCTCACCGGCAAACAGGTGGCCCCCTCGGCCGCCGACGCCTGGTGCGCCGCGGAGGTCGACGAGGCCGTCGTCGCCTCAGCAGCCGACGGCCAGTGGCACGAGATCCCCCGCGTCGAGGGACGCACCACCTTCGACGCCTGA","VSTRPCSERSSDLILPSCQDKGALISSCDVINDGCLLGLPETPPHTQQPTMLSGRTVMANKSILGIGVISLGWMGRLHSRSYRAIAERFPELGVTPRLVAAADPVDEVRQEAVDNLGFERAYADYRDLLADPEVEAVSICAPNFLHHEMALAAVEAGKPFWIEKPMGVSAEQSRQIAQAAEKAGLMTAVGFNYRHTPAIEYLRSLVRGGELGRITNVRVWFIADYNSSPMGPLTWRASKEKAGAGVVPDLMSHGADLAQYIVGRIASVTAVTDTFITERPIPTKMGIGHSGFEIGDDVGPVENEDYVSMLVRFENGTVGTMESSRVSVGPRAEYVVEVYGTKGSARWNFERLNELEICPVLDGGASHGYTRAMAGPQWGQWQRFQPAIGTSMGFDDMKAIEAAQFIESILTGKQVAPSAADAWCAAEVDEAVVASAADGQWHEIPRVEGRTTFDA$","Oxidoreductase","Cytoplasm","putative oxidoreductase","oxidoreductase","oxidoreductase domain protein","","","","","

InterPro
IPR000683
Domain

Oxidoreductase, N-terminal
PF01408	$\"[64-191]T$	GFO_IDH_MocA

InterPro
IPR004104
Domain

Oxidoreductase, C-terminal
PF02894	$\"[203-337]T$	GFO_IDH_MocA_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[54-226]T$	no description
PTHR22604	$\"[122-281]T$ $\"[302-454]T$	OXIDOREDUCTASES
PTHR22604:SF14	$\"[122-281]T$ $\"[302-454]T$	OXIDOREDUCTASE

","BeTs to 12 clades of COG0673COG name: Predicted dehydrogenases and related proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0673 is --mpk-yqvd-lbcefgh--uj----Number of proteins in this genome belonging to this COG is 5","***** IPB000683 (Oxidoreductase, N-terminal) with a combined E-value of 5.4e-14. IPB000683A 134-167","Residues 64-137 are 78% similar to a (OXIDOREDUCTASE 2-DEHYDROGENASE MYO-INOSITOL RELATED PROTEINS OXIDOREDUCTASE DEHYDROGENASES PLASMID PREDICTED BH0710) protein domain (PD599877) which is seen in Q6AAJ8_PROAC.Residues 64-139 are 61% similar to a (OXIDOREDUCTASE DEHYDROGENASE OXIDOREDUCTASE FAMILY GFO/IDH/MOCA PLASMID 1.-.-.- PROBABLE MYO-INOSITOL 2-DEHYDROGENASE) protein domain (PD336361) which is seen in Q826M7_STRAW.Residues 138-203 are 89% similar to a (OXIDOREDUCTASE DEHYDROGENASE OXIDOREDUCTASE FAMILY GFO/IDH/MOCA PROBABLE PLASMID MYO-INOSITOL 1.-.-.- 2-DEHYDROGENASE) protein domain (PD001155) which is seen in Q6AAJ8_PROAC.Residues 205-321 are 72% similar to a (OXIDOREDUCTASE DEHYDROGENASE OXIDOREDUCTASE FAMILY PLASMID MYO-INOSITOL GFO/IDH/MOCA 1.-.-.- 2-DEHYDROGENASE PREDICTED) protein domain (PD127410) which is seen in Q6AAJ8_PROAC.Residues 322-444 are 73% similar to a (OXIDOREDUCTASE 2-DEHYDROGENASE MYO-INOSITOL PROTEINS DEHYDROGENASES RELATED OXIDOREDUCTASE PREDICTED PLASMID BH0710) protein domain (PD472416) which is seen in Q6AAJ8_PROAC.","","-47% similar to PDB:2GLX Crystal Structure Analysis of bacterial 1,5-AF Reductase (E_value = 1.7E_19);-42% similar to PDB:1ZH8 Crystal structure of Oxidoreductase (TM0312) from Thermotoga maritima at 2.50 A resolution (E_value = 1.3E_14);-44% similar to PDB:1EVJ CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D (E_value = 2.9E_14);-44% similar to PDB:1H6A REDUCED PRECURSOR FORM OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS MOBILIS (E_value = 2.9E_14);-44% similar to PDB:1H6B REDUCED PRECURSOR FORM OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS MOBILIS COMPLEXED WITH GLYCEROL (E_value = 2.9E_14);","Residues 64 to 191 (E_value = 4e-31) place ANA_0114 in the GFO_IDH_MocA family which is described as Oxidoreductase family, NAD-binding Rossmann fold.Residues 203 to 337 (E_value = 0.02) place ANA_0114 in the GFO_IDH_MocA_C family which is described as Oxidoreductase family, C-terminal alpha/beta domain.","","oxidoreductase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0115","129318","130487","1170","7.30","1.30","41003","ATGGACTCCGGATCCCGCGGATCGTGCCGATCCGTGAGGCACAACGGTGTGGATGGGGAGACGTCTGCCGTGGAAGGACCTCGAGGACGAGGCGGGCGGGTCACGATCAGGACCGTCGCCGAACGTGCCGGTCGCTCCATCTCCACCGTCTCGGCGGCTCTCAACGGCTCCGACGGCGTCGCCGAGAAGACCCGTGGCGAGATCCTGCGCATCGCCTCCGAGCTCGGCTACCAGGCCGACCCGCGCGCCCAGTTCCTGCGCCGTAGCCACACCGGGCTCATCGGTGCCAGCTTCGCCATTGGGCAGGCCTACCAGGGCCTCATTGTGGACGGGCTCTTCCAGGCGGCCTCCGCCCTGGAGCACGCGCTGGTGCTGGCCACCTCCACCCCGCACCGCGATGTGGCCGACGGGCTGCGCTCACTGCTGCTCCAGCGCTGCGAGGGCCTCATCCTGGTCGACCCCGACTTCTCCGTGGACGCCCTGGCCAGCATCGGGGACCGTCCACCGGCGGTCCTCATCGGGACCAGTATCGAGATGGAGGACGTCGATGAGGTCCACTCACGTGACGACGTCGGTATCCAGATGCTCGTCGATCACCTGGTCGACACCGGGAGGCGCCGCATCACCCACGTGGACGGCGGGAGTCAGACCGCCGCGGGGCGACGCATCCAGAGGTTCGGCCAGGCCATGGAGAGCCGAGGGCTGGGACGAGGCGCGCGGGTGGTGCCCGGGGGAGGCGATGAGGACAGCGGTGCCAGGGCGGTCCACTACCTCATCGAGGCCGGTGAGCTGCCCGAGGCGCTCCTGTGCTTCAACGACCACTGCGCCGTCGGGGCTCTCATGGAGCTGCGCCGTCAAGGGGTGAGGGTGCCGCAGGACCTGGCCGTCACCGGCTACGACGGCATCCCGGTCACGGCCTCCTCGGCCTTCTCCCTGACCACGGTGCGACAGGACGCCCGCCTCATCGCCGAGGTGGCGGTCCGGGCGCTGCTGGTCCGGATGCACCCGGGTCAGGATGGCAAGATTCCGGCGGAGGTGGCCGGTGAGGACCGGCCTCTGGGGGCCGCCTCTACCGGGTGGTCCCCGAGCTCGTTGTCCGCGACACGACGGCCCCGCCGTGCGAGCGTCGGGCTGAGGCCTGTGCCTGATGCGGCACGCGGCCTACGGTAA","MDSGSRGSCRSVRHNGVDGETSAVEGPRGRGGRVTIRTVAERAGRSISTVSAALNGSDGVAEKTRGEILRIASELGYQADPRAQFLRRSHTGLIGASFAIGQAYQGLIVDGLFQAASALEHALVLATSTPHRDVADGLRSLLLQRCEGLILVDPDFSVDALASIGDRPPAVLIGTSIEMEDVDEVHSRDDVGIQMLVDHLVDTGRRRITHVDGGSQTAAGRRIQRFGQAMESRGLGRGARVVPGGGDEDSGARAVHYLIEAGELPEALLCFNDHCAVGALMELRRQGVRVPQDLAVTGYDGIPVTASSAFSLTTVRQDARLIAEVAVRALLVRMHPGQDGKIPAEVAGEDRPLGAASTGWSPSSLSATRRPRRASVGLRPVPDAARGLR$","LacI family transcriptional regulator","Cytoplasm, Membrane","Transcriptional regulators","K02529 LacI family transcriptional regulator","periplasmic binding protein/LacI transcriptional regulator","","Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 1992. 267(22):15869-15874. PMID: 1639817Vartak N.B., Reizer J., Reizer A., Gripp J.T., Groisman E.A., Wu L.F., Tomich J.M., Saier Jr M.H. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 1991. 142(9):951-963. PMID: 1805309","","","

InterPro
IPR000843
Domain

Bacterial regulatory protein, LacI
PF00356	$\"[34-59]T$	LacI
SM00354	$\"[33-103]T$	HTH_LACI
PS50932	$\"[34-88]T$	HTH_LACI_2

InterPro
IPR001761
Domain

Periplasmic binding protein/LacI transcriptional regulator
PF00532	$\"[88-350]T$	Peripla_BP_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[34-91]T$	no description
G3DSA:3.40.50.2300	$\"[189-334]T$	no description

InterPro
IPR008183
Family

Aldose 1-epimerase
PF01263	$\"[5-317]T$	Aldose_epim

InterPro
IPR014718
Domain

Glycoside hydrolase-type carbohydrate-binding, subgroup
G3DSA:2.70.98.10	$\"[11-316]T$	no description

","BeTs to 4 clades of COG2017COG name: Galactose mutarotase and related enzymesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2017 is ---p--y-vd-lb-e-gh-n-j----Number of proteins in this genome belonging to this COG is 1","***** IPB008183 (Aldose 1-epimerase) with a combined E-value of 6e-14. IPB008183B 49-79 IPB008183C 125-138 IPB008183D 175-187 IPB008183E 263-276","Residues 16-152 are 45% similar to a (ALDOSE 1-EPIMERASE ISOMERASE MUTAROTASE METABOLISM 1-EPIMERASE-LIKE UDP-GLUCOSE GALACTOSE ENZYME INCLUDES:) protein domain (PD127437) which is seen in Q8G4M0_BIFLO.Residues 54-96 are 65% similar to a (ALDOSE-1-EPIMERASE ISOMERASE YIHR YOXA ENZYME RELATED GALACTOSE STY3858 ALDOSE 1-EPIMERASE) protein domain (PD441589) which is seen in YIHR_ECOLI.Residues 114-307 are 45% similar to a (ALDOSE-1-EPIMERASE ISOMERASE) protein domain (PDA1D4N5) which is seen in Q6A8Z9_PROAC.","","-49% similar to PDB:2UVA CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400 (E_value = );-49% similar to PDB:2UVC CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE COMPLEXED WITH NADP+ FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400 (E_value = );-68% similar to PDB:1IN0 YAJQ PROTEIN (HI1034) (E_value = );-48% similar to PDB:1WXR Crystal structure of Heme Binding protein, an autotransporter hemoglobine protease from pathogenic Escherichia coli (E_value = );","Residues 5 to 317 (E_value = 8.9e-38) place ANA_0116 in the Aldose_epim family which is described as Aldose 1-epimerase.","","aldose-1-epimerase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0117","133198","132209","990","4.76","-21.18","34853","ATGCTCTCCATCGCCGTCATCGGTGCCGGCCGCATCGGCCACGTCCACGCCAAGACCATCGCCGCCCACCCCCAGGCCGAGCTCGCCCTGGTCTGCGACCCCTTCGAGGACGCGGCCGAGAAGCTCGCCGCCACCTACGGCGCCCGGTCCTGCAAGGACGCCGAGGAGGTCTTCGCCGACCCCGAGATCGAAGCCGTCATCGTCGGCTCCCCCACGCCGCTGCACATCCCCCACCTGCTGGCCGCCGCCAAGGCGGGCAAGGCGGTGCTGTGCGAGAAGCCGATCGCTCTGGACATGATGGACGTCGAGGCCGCCCAGGCCGAGCTCGATGCCGTCACGGTCCCCGTCATGTTCGGCTTCAACCGCCGCTTCGATCCCAGCTTCGCCGCCGCCCGCGCCGCGGTCGAGGCCGGCAAGATCGGCGATATCGAGCAGCTGACCATCATCAGCCGCGACCCGGCCGCCCCGCCGGCGGAGTACATCAAGGTCTCCGGCGGCATCTTCCGCGACATGACCATCCACGACTTCGACACCGCCCGCTTCTTCCTGGGTGAGATCGAGGAGGTCTACGCCGCCGGGCAGAACCTCGACCCGGCCCTGAAGGACACCGGCGACTTCGACGCCGCCGTCGTCACCCTCAAGGCAGCCTCGGGCGCCGTGGCCACGATCATCAACAACCGCCACTGCTCCTCCGGCTACGACCAGCGACTCGAGGCCTCGGGCCGCGAGGGCGCCCTGTTCGCCGAGAACATCCGCGCCACCACGGTGCGCCTGTCCAACGGCGAGGTCACCGACGCCCAGGAGCCCTACCTCGACTTCTTCCTGGAGCGCTACGCCGACGCCTACCGCATCGAGCTGAGCGCCTTCATCGAGGCCGTCGAGGCCGGCACCACGCCTCCCACCGGCATCGAGGACGCCATCGCCGCCCTGCGCCTGGCCGAGGCCGCCACGGAGTCGGCCCACTCCGGGCAGCCGGTGCGTCTGAGCTGA","MLSIAVIGAGRIGHVHAKTIAAHPQAELALVCDPFEDAAEKLAATYGARSCKDAEEVFADPEIEAVIVGSPTPLHIPHLLAAAKAGKAVLCEKPIALDMMDVEAAQAELDAVTVPVMFGFNRRFDPSFAAARAAVEAGKIGDIEQLTIISRDPAAPPAEYIKVSGGIFRDMTIHDFDTARFFLGEIEEVYAAGQNLDPALKDTGDFDAAVVTLKAASGAVATIINNRHCSSGYDQRLEASGREGALFAENIRATTVRLSNGEVTDAQEPYLDFFLERYADAYRIELSAFIEAVEAGTTPPTGIEDAIAALRLAEAATESAHSGQPVRLS$","Myo-inositol dehydrogenase","Cytoplasm","myo-inositol dehydrogenase; IdhA","myo-inositol 2-dehydrogenase ","Inositol 2-dehydrogenase","","","","","

InterPro
IPR000683
Domain

Oxidoreductase, N-terminal
PF01408	$\"[2-120]T$	GFO_IDH_MocA

InterPro
IPR004104
Domain

Oxidoreductase, C-terminal
PF02894	$\"[132-238]T$	GFO_IDH_MocA_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[1-146]T$	no description
PTHR22604	$\"[52-328]T$	OXIDOREDUCTASES
PTHR22604:SF14	$\"[52-328]T$	OXIDOREDUCTASE

","BeTs to 13 clades of COG0673COG name: Predicted dehydrogenases and related proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0673 is --mpk-yqvd-lbcefgh--uj----Number of proteins in this genome belonging to this COG is 5","***** IPB000683 (Oxidoreductase, N-terminal) with a combined E-value of 5.6e-20. IPB000683A 63-96 IPB000683B 174-184","Residues 1-66 are 60% similar to a (MYO-INOSITOL 2-DEHYDROGENASE SIMILAR DEHYDROGENASE OXIDOREDUCTASE) protein domain (PD745819) which is seen in Q6LK37_PHOPR.Residues 2-68 are 65% similar to a (OXIDOREDUCTASE DEHYDROGENASE OXIDOREDUCTASE FAMILY GFO/IDH/MOCA PLASMID 1.-.-.- PROBABLE MYO-INOSITOL 2-DEHYDROGENASE) protein domain (PD336361) which is seen in Q6AAJ5_PROAC.Residues 70-132 are 63% similar to a (OXIDOREDUCTASE DEHYDROGENASE OXIDOREDUCTASE FAMILY GFO/IDH/MOCA PROBABLE PLASMID MYO-INOSITOL 1.-.-.- 2-DEHYDROGENASE) protein domain (PD001155) which is seen in Q6AAJ5_PROAC.Residues 133-305 are 49% similar to a (OXIDOREDUCTASE 2-DEHYDROGENASE MYO-INOSITOL PLASMID) protein domain (PDA019N7) which is seen in Q6W1J0_RHISN.Residues 135-225 are similar to a (OXIDOREDUCTASE DEHYDROGENASE OXIDOREDUCTASE FAMILY PLASMID MYO-INOSITOL GFO/IDH/MOCA 1.-.-.- 2-DEHYDROGENASE PREDICTED) protein domain (PD127410) which is seen in Q6AAJ5_PROAC.Residues 223-277 are 74% similar to a (MYO-INOSITOL 2-DEHYDROGENASE OXIDOREDUCTASE DEHYDROGENASE INOSITOL OXIDOREDUCTASE PLASMID NAD-BINDING PEPTIDE SIMILAR) protein domain (PD330889) which is seen in Q8NL86_CORGL.","","-42% similar to PDB:2GLX Crystal Structure Analysis of bacterial 1,5-AF Reductase (E_value = 2.5E_14);","Residues 2 to 117 (E_value = 0.0016) place ANA_0117 in the DapB_N family which is described as Dihydrodipicolinate reductase, N-terminus.Residues 2 to 120 (E_value = 4.6e-33) place ANA_0117 in the GFO_IDH_MocA family which is described as Oxidoreductase family, NAD-binding Rossmann fold.Residues 132 to 238 (E_value = 3.5e-11) place ANA_0117 in the GFO_IDH_MocA_C family which is described as Oxidoreductase family, C-terminal alpha/beta domain.","","dehydrogenase; IdhA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0119","134492","133389","1104","5.00","-12.56","40542","ATGAACCCGAAAGAGAGCACAGAACCGATGAGCATCGACTACACCCCCGGACCCCTTCTCGACGCCGCCCGCAACACGCCCACCGCCCTGTGGAACGACTCAGCCGACCCCGACGAGCTGCGCCAGTCCATCTCCTTCGGTGGCGTCGGCGCCACCTGCAACCCCACTATCGCCTACACCTGCATCAACCAGCGCAAGGACGTGTGGCTCCCCCGCATCGCCGAGCTGGCCGAGGAGATGCCCGAGGCCACCGAGTCCGAGATCGGCTGGCAGGTCGTGCGCGAGATGAGCATCGAGGCCGCCACGCTGCTCGAGCCCATCTTCGAGGAGCACAAGGGCCGCAACGGTCGCCTGTCGATGCAGACCGACCCGCGCCTGGCCCGCAGCGCCAAGGCCCTGGCCGACCAGGCCGAGGAGTTCTCCAACCTGGCCAAGAACATCATCGTCAAGATCCCCGCCACCTCCGTGGGCGTCAAGGCCATCGAGGACGCCACCTACCGGGGCGTATCGGTCAACGTCACCGTCTCCTTCTCCGTGCCCCAGGCCGTGGCCACCGGTGAGGCCATCGAGCGCGGCCTCAAGCGCCGCGAGGCCGAGGGCAAGGACGTCTCCACCATGGGTCCGGTCGTCACCCTCATGGGCGGCCGCCTGGACGACTGGCTCAAGATCGTGGCCAAGCGGGACAAGCTCTTCATCGACCCCGGTCACCTGGAGTGGGGCGGCGTGGCCGCCCTCAAGCGCGCCTACCAGGAGTTCCAGGCCCGGGGCCTGCGCGCCCGCGTGCTGTCGGCCGCCTTCCGCAACGTGCTGCAGTGGTCCGAGCTGGTCGGCGGCGACCTGGTTGTCTCCCCGCCCTTCGCCTGGCAGAAGCTCATCAACGACTCCGACTACAAGGTCGTCGAGCGCATCAACGAGCCCGTGGCCCCCGAGATCATGGAGACGCTCCGGTCGATCCCCGAGTTCGTGCGCGCCTACGAGCCCGACGGCATGACGCCCGAGGAGTTCGACACCTTCGGCGCGACCCGCCGCACCCTGCGCGGCTTCCTCCAGGCCGACGCCGACCTGGACGCCCTGGTGCGCGACGTCATCATGCCCCAGCCCTGA","MNPKESTEPMSIDYTPGPLLDAARNTPTALWNDSADPDELRQSISFGGVGATCNPTIAYTCINQRKDVWLPRIAELAEEMPEATESEIGWQVVREMSIEAATLLEPIFEEHKGRNGRLSMQTDPRLARSAKALADQAEEFSNLAKNIIVKIPATSVGVKAIEDATYRGVSVNVTVSFSVPQAVATGEAIERGLKRREAEGKDVSTMGPVVTLMGGRLDDWLKIVAKRDKLFIDPGHLEWGGVAALKRAYQEFQARGLRARVLSAAFRNVLQWSELVGGDLVVSPPFAWQKLINDSDYKVVERINEPVAPEIMETLRSIPEFVRAYEPDGMTPEEFDTFGATRRTLRGFLQADADLDALVRDVIMPQP$","Transaldolase","Cytoplasm","putative transaldolase","transaldolase ","Transaldolase","","Miosga T., Schaaff-Gerstenschlager I., Franken E., Zimmermann F.K. Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase. Yeast 1993. 9(11):1241-1249. PMID: 8109173Reizer J., Reizer A., Saier Jr M.H. Novel phosphotransferase system genes revealed by bacterial genome analysis--a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system. Microbiology 1995. 141:961-971. PMID: 7773398","","","

InterPro
IPR001585
Family

Transaldolase
PTHR10683	$\"[115-294]T$	TRANSALDOLASE
PF00923	$\"[29-362]T$	Transaldolase

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[17-363]T$	no description

","BeTs to 17 clades of COG0176COG name: TransaldolaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0176 is --mp--yqvdrlbcefgh-nuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB001585 (Transaldolase) with a combined E-value of 1.8e-31. IPB001585A 50-61 IPB001585B 109-140 IPB001585C 148-202 IPB001585D 240-285","Residues 10-365 are similar to a (TRANSFERASE TRANSALDOLASE) protein domain (PDA0C6I6) which is seen in Q6AAL0_PROAC.Residues 99-161 are 67% similar to a (TRANSALDOLASE TRANSFERASE PENTOSE SHUNT PROBABLE TRANSALDOLASE ALDOLASE LYASE 4.1.2.- FRUCTOSE-6-PHOSPHATE) protein domain (PD692808) which is seen in Q829U5_STRAW.Residues 168-315 are 46% similar to a (TRANSALDOLASE TRANSFERASE PENTOSE SHUNT ISOMERASE GLYCOLYSIS GLUCONEOGENESIS TAL PHOSPHOGLUCOSE TRANSALDOLASE:TRANSALDOLASE) protein domain (PD009632) which is seen in TAL2_NOSPU.","","-46% similar to PDB:1I2N CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT N35A (E_value = 5.1E_11);-46% similar to PDB:1I2P CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT D17A (E_value = 5.1E_11);-46% similar to PDB:1I2R CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT S176A (E_value = 5.1E_11);-46% similar to PDB:1ONR STRUCTURE OF TRANSALDOLASE B (E_value = 5.1E_11);-46% similar to PDB:1UCW COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE (E_value = 5.1E_11);","Residues 29 to 362 (E_value = 6.3e-11) place ANA_0119 in the Transaldolase family which is described as Transaldolase.","","transaldolase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0120","135410","134619","792","6.53","-2.68","28886","ATGCTCGAGGCATTATCACGTCTGACACAGGCTCATCTCATGCCCGATTCAACATCCCCTTTCGCCCTCGACATCACGATCGACCGCGAGTCCAAGACGCCGCTGCACACGCAAATTTCCGAGCCGCTGGCCACACTCATCCTTGAAGGCACACTGCCCGCCGGTAGCCGCCTGGAGGACGAGCTCTCGATGGCCAAGCGACTGAAGGTCTCCCGCCCCACGGCGCGCCAAGCCCTTCAGCACCTGGTGGACCGCGGCCTGGTCAAGCGCCGTCGGGGCGTGGGCACGATCGTCTCCCCCATGCACGTCCACCGCCCGATGCAGCTGACGAGCCTGCTGTCAGACCTGTCCGCGGCTGGCCACACGACCTCCACGAGCGTGCTGGACTACGTCGAGCACGAGGCCGACGCCGAGGCCGCCGAGCACCTCGAGGTCGAGGAGGGCACCGCCGTCGTGACCTGCACCCGCATCCGCTGCGCCGACGGCGAGCCGATCGCGGTGCTGTCCAACCTCATGCCGGCAGCCATCGCCCCCACCCGTGAGGAGCTGGAGGCCGGAGGCCTCTACGACCTGCTGCGCGCCCAGGACGTCATCCCCACCACGGCCAAGCAGATCATCGGGGCCCGCAATGCCACCGCCCGCGAGGCCGACCTCCTCCACGAGCGGCGCCGCGCCGCCCTCATGACCGCCACCCGCATCACCTACGACCAGTCGGGCCGCATCATCGAGTACGGGCAGCACATCTACCGGGCCTCGCGCTACACCTTCGAGACCTCGCTGTTCTCCAGCTAG","MLEALSRLTQAHLMPDSTSPFALDITIDRESKTPLHTQISEPLATLILEGTLPAGSRLEDELSMAKRLKVSRPTARQALQHLVDRGLVKRRRGVGTIVSPMHVHRPMQLTSLLSDLSAAGHTTSTSVLDYVEHEADAEAAEHLEVEEGTAVVTCTRIRCADGEPIAVLSNLMPAAIAPTREELEAGGLYDLLRAQDVIPTTAKQIIGARNATAREADLLHERRRAALMTATRITYDQSGRIIEYGQHIYRASRYTFETSLFSS$","GntR-family transcriptional regulator","Cytoplasm","Transcriptional regulators","GntR-family transcriptional regulator","UbiC transcription regulator-associated domain protein","","Haydon D.J., Guest J.R. A new family of bacterial regulatory proteins. FEMS Microbiol. Lett. 1991. 63(2):291-295. PMID: 2060763Van aalten D.M., Dirusso C.C., Knudsen J., Wierenga R.K. Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. EMBO J. 2000. 19(19):5167-5177. PMID: 11013219Rigali S., Derouaux A., Giannotta F., Dusart J. Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies. J. Biol. Chem. 2002. 277(15):12507-12515. PMID: 11756427","","","

InterPro
IPR000524
Domain

Bacterial regulatory protein GntR, HTH
PR00035	$\"[58-72]T$ $\"[72-88]T$	HTHGNTR
PF00392	$\"[35-98]T$	GntR
SM00345	$\"[39-98]T$	HTH_GNTR
PS50949	$\"[33-101]T$	HTH_GNTR

InterPro
IPR011663
Domain

UbiC transcription regulator-associated
PF07702	$\"[118-255]T$	UTRA

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[28-101]T$	no description

","BeTs to 5 clades of COG2188COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2188 is ---------drlb-efg----j---wNumber of proteins in this genome belonging to this COG is 2","***** IPB011663 (UbiC transcription regulator-associated) with a combined E-value of 1.2e-15. IPB011663 58-98***** IPB000524 (Bacterial regulatory protein, GntR family) with a combined E-value of 1.4e-13. IPB000524 58-98","Residues 55-93 are 87% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR GNTR FAMILY REGULATOR GNTR-FAMILY REGULATORY) protein domain (PD069824) which is seen in Q8NTZ4_CORGL.Residues 156-232 are 64% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR FAMILY GNTR REGULATOR REPRESSOR GNTR-FAMILY) protein domain (PD004095) which is seen in Q6AC32_BBBBB.","","-55% similar to PDB:2P19 Crystal structure of bacterial regulatory protein of gntR family from Corynebacterium glutamicum (E_value = 2.7E_18);","Residues 35 to 98 (E_value = 9.4e-13) place ANA_0120 in the GntR family which is described as Bacterial regulatory proteins, gntR family.Residues 118 to 255 (E_value = 2.3e-41) place ANA_0120 in the UTRA family which is described as UTRA domain.","","regulators (PA3757)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0121","135629","136651","1023","5.12","-12.69","36798","GTGACCGAGGCGGTCGCGCCCGAGAGCTCGCCCGCAGCCGCCGGAAACGCCGACCGGCTCGACGTGCTCACCATCGGGCGCTGCGGCATCGACATCTACCCCCTTCAGGTCGGCGTCGGGCTGGAGGACGTGGAGAGCTTCGGCAAGTTCCTGGGCGGGAGCCCCACCAACGTGGCGGTGGCCGCCGCCCGCTACGGGCACCGCTCCGCCGTTGTCACCGGCGTGGGAAACGACCCCTTCGGGCGCTTCGTGCGCACCGAGATGCGCCGCCTGGGGGTCGACGACCGCCACGTCGTCACCAAGGCCGCCTACAACACCCCGGTCACCTTCTGCGAGATCTTCCCGCCGGATGACTTCCCCCTCTACTTCTACCGTGAGCCCTCGGCCCCCGACCTGGAGCTGACCTGGGAGGACCTGCCGCTGGAGGCCATTCGCGACGCCTCGATCTTCTGGATCTCGGTGACCGGCCTGAGCAAGGAGCCCTCGCGCTCGGCCCACCACGCGGCCCTGGGCACCCGCGACCGGCAGCGCTTCACGATCGCCGACCTCGACTACCGCCCCATGTTCTGGAAGGACAAGGAGACGGCCCACCGGGAGGTCTCTCGGATCCTTCCCAAGGTCACCGTCGCCATCGGCAACCGGGAGGAGTGTGAGGTCGCCGTCGGCGAGCGCGACCCCGAGCGGGCGGCCGACGCCCTCCTGGAGGCCGGCGTCGAGCTGGCCATCGTCAAGCAGGGCCTGGAGGGGACGTTGGCCAAGACCCGCACCGAGCGGGTGGAGATGCCCGTGACCTCGGTGGAGACGAAGAACGGCCTGGGAGCCGGGGACGCCTTCGGAGGGGCCATCTGCCACGGACTGCTGTCGGGCTGGTCCCTGGAGAAGACCATCTTCGCCGCCTCCACCGCAGGAGCGATCGTCTCCTCGCGACTGGAGTGCTCCACCGCCATGCCCACCGAGCCCGAGCTGCTCGAGCTCATGCGCGCCCGCCGCGACGAGGTCGCCCCGGGGCTGACGGACCTGTGA","VTEAVAPESSPAAAGNADRLDVLTIGRCGIDIYPLQVGVGLEDVESFGKFLGGSPTNVAVAAARYGHRSAVVTGVGNDPFGRFVRTEMRRLGVDDRHVVTKAAYNTPVTFCEIFPPDDFPLYFYREPSAPDLELTWEDLPLEAIRDASIFWISVTGLSKEPSRSAHHAALGTRDRQRFTIADLDYRPMFWKDKETAHREVSRILPKVTVAIGNREECEVAVGERDPERAADALLEAGVELAIVKQGLEGTLAKTRTERVEMPVTSVETKNGLGAGDAFGGAICHGLLSGWSLEKTIFAASTAGAIVSSRLECSTAMPTEPELLELMRARRDEVAPGLTDL$","Sugar kinase, ribokinase family","Cytoplasm","Sugar kinases, ribokinase family","PfkB domain protein","PfkB domain protein","","Sigrell J.A., Cameron A.D., Jones T.A., Mowbray S.L. Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures. Structure 1998. 6(2):183-193. PMID: 9519409","","","

InterPro
IPR011611
Domain

PfkB
PF00294	$\"[19-319]T$	PfkB

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[8-336]T$	no description
PTHR10584	$\"[23-326]T$	SUGAR KINASE RELATED
PTHR10584:SF34	$\"[23-326]T$	FRUCTOKINASE

","BeTs to 16 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 6","***** IPB002173 (Carbohydrate kinase, PfkB) with a combined E-value of 3.6e-07. IPB002173A 51-66 IPB002173B 269-282","Residues 52-93 are 83% similar to a (KINASE TRANSFERASE FRUCTOKINASE CARBOHYDRATE SYNTHASE ADP-HEPTOSE SUGAR 2.7.-.- 2.7.1.- PROBABLE) protein domain (PD001280) which is seen in Q6AAK8_PROAC.Residues 98-197 are 72% similar to a (KINASE CARBOHYDRATE) protein domain (PDA184C1) which is seen in Q6AAK8_PROAC.Residues 123-196 are 67% similar to a (KINASE CARBOHYDRATE TRANSFERASE FAMILY SUGAR RIBOKINASE KINASES KINASE PFKB) protein domain (PDA1F2F1) which is seen in Q8NTZ3_CORGL.Residues 200-306 are similar to a (KINASE TRANSFERASE RIBOKINASE SUGAR FRUCTOKINASE CARBOHYDRATE FAMILY PFKB ADENOSINE KINASE) protein domain (PD023180) which is seen in Q6AAK8_PROAC.Residues 209-333 are 49% similar to a (KINASE FAMILY CARBOHYDRATE PFKB) protein domain (PDA1D2Q6) which is seen in Q6LK43_PHOPR.","","-43% similar to PDB:1V19 2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS (E_value = 7.9E_19);-43% similar to PDB:1V1A 2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND 2-KETO-3-DEOXYGLUCONATE AND ADP (E_value = 7.9E_19);-43% similar to PDB:1V1B 2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND ATP (E_value = 7.9E_19);-43% similar to PDB:1V1S 2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS (CRYSTAL FORM 2) (E_value = 7.9E_19);-46% similar to PDB:1WYE Crystal structure of 2-keto-3-deoxygluconate kinase (form 1) from Sulfolobus Tokodaii (E_value = 1.5E_17);","Residues 19 to 319 (E_value = 1.3e-49) place ANA_0121 in the PfkB family which is described as pfkB family carbohydrate kinase.","","kinases, ribokinase family (AP001515)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0122","136662","137579","918","5.01","-10.37","32089","ATGAACGCATCATCCACCCCTGCCGCCTCCGCCTCGGGGCCGCGGCCGCTGACCGACGCCGTCACCGAGATCCGGGCCACCGACCCCGATCGCATCAGCCGGGCCCTGGCCCAGCGCCCCCGCGCCGACCTCGCCGGGGCCGGGCGCCTCATGGTCATCGCCTGCGACCACCCGGCCCGCGGGGCCCTGGGGGCCGGCGAGAGACCCCTGGCGATGGCCGACCGCGAGGACCTCCTGCGGCGCTGCATGACGGCCCTGTCCCGCCCCGGCGTCAACGGGTTCCTGGGAACGGCCGAGATCATCGAGGACCTGACCCTCCTGGGCGCCCTGGACGGCAAGCTCGTGTGGGGCTCGATGAACCGGATCGGCCTCCAGGGGGCCTCCTTCGAGATGGACGACCGCTTCGGCGCCTACGACGCTGACGGCATCGAGGCCTCCCACCTCGACGGCGGCAAGATGCTCACCCGCATCAACTACGCCGACCCCGCCAGCGCCGCCACCCTCGAGGCCAGCGCCAAGGCCATCGACTCCCTGTCCGAGCGTGGCCTGAATGCCATGATCGAGCCCTTCATCTCCCGCTGGGAGGACGACGGCCGCATCGTCAACGACCTCAGCGAGGAGGCCGTCATCCGCTCGATCAGCATCGCCCAGGCGCTGGGGCGCAGCTCGGCGCACACCTGGCTCAAGCTGCCCTGCGTCAGCGATCCCGTCTCGATGCGGCGCGTCATGGCCTCCACCTCCCTGCCCAGCCTCATCCTGGGCGGCGAGGTCTCCACCGACCCCGAGGCCACCCGCGCCTCCTGGGCGGCGGCCCTGGAGCTTCCCAATGTCAGGGGACTGGTCGTGGGCCGCTCCCTGCTCTACCCGGGCAATGACGACGTCGAGGCCGCCGTCGACGCCGCCGTCGCCCTGCTGTGA","MNASSTPAASASGPRPLTDAVTEIRATDPDRISRALAQRPRADLAGAGRLMVIACDHPARGALGAGERPLAMADREDLLRRCMTALSRPGVNGFLGTAEIIEDLTLLGALDGKLVWGSMNRIGLQGASFEMDDRFGAYDADGIEASHLDGGKMLTRINYADPASAATLEASAKAIDSLSERGLNAMIEPFISRWEDDGRIVNDLSEEAVIRSISIAQALGRSSAHTWLKLPCVSDPVSMRRVMASTSLPSLILGGEVSTDPEATRASWAAALELPNVRGLVVGRSLLYPGNDDVEAAVDAAVALL$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 50-289 are 73% similar to a (SCO6977 CGL0159) protein domain (PD318474) which is seen in Q6AAK7_PROAC.","","-40% similar to PDB:1GGZ CRYSTAL STRUCTURE OF THE CALMODULIN-LIKE PROTEIN (HCLP) FROM HUMAN EPITHELIAL CELLS (E_value = );-44% similar to PDB:1OJX CRYSTAL STRUCTURE OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE (E_value = );-44% similar to PDB:1OK4 ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COVALENTLY BOUND TO THE SUBSTRATE DIHYDROXYACETONE PHOSPHATE (E_value = );-44% similar to PDB:1OK6 ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE (E_value = );-44% similar to PDB:1W8R THE MECHANISM OF THE SCHIFF BASE FORMING FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE: STRUCTURAL ANALYSIS OF REACTION INTERMEDIATES (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0124","137724","138638","915","4.97","-19.00","33319","ATGGGCCACACCGACCGCACCGCTCAGTCCGAGACCTCGGACCAGTCCCACTACGTCATCCGCGCCGGAGAGCTCGCCCACGACGGCTACGAGCTGGACCTCACCCCGGAGCGGGCCGGCTGGGAGTGGTCCTCCCTGCGCGTGGTGGCGCTCGCTCCTGGGAAGCCCCTGACCGTGCCCGCCGGTGAGCACGAGTACCTCGTCCTGCCCCTGTCGGGAGGCTGCACCGTCCAGGCCGGCAGCGAGCGCCTCGAGGTGGCCGGGCGCGAGTCGGTCTTCACCGACATCACCGACTACGTCTACGTCCCCCGCCACACCGAGGTGACCCTCATCAGCGCCGGCGGCGCCCGCATCGCCCTTCCCGGCTCCAAGGCCACCACCGACAAGCCGCTGCGCTACTGCCCGCGCTCCGAGGTCGGCACCGGCCTGCGGGGGGCCGGCCCCTCCTCGCGCCAGGTCAACAACTACGCCCTGGGCAACGACGTCGAGACCTCCCACCTGCTGGCCTGCGAGGTCCTGACCCCCGGAGGCAACTGGTCCTCCTACCCGCCCCACAAGCACGACGAGCACACCGAGGTCGAGCGGGTCCTGGAGGAGATCTACTACTACCAGGTCCGCGCCGGCGAGGGCGACGCCGAGGGCTTCGCGCTCCAGCGCATCTACCCCTCGCCCGGCCACGACATCGACGTGTGCACCGAGGTGCGCGGCGGCGACGTCGTCGTCATGCCCTACGGCTACCACGGCCCCTCCGTGGCCGCCCCCGGCTACGACCTCTACTACCTCAACGTCATGGCCGGCCCCGCCGAGGACTCCGTGTGGCTCATGACCGACGACCCCCACCACACCTGGGTGCGCCAGACCTGGGAGGGCCAGGAGGTTGACCCACGCCTGCCTATGACCCCCATGAACGACTAG","MGHTDRTAQSETSDQSHYVIRAGELAHDGYELDLTPERAGWEWSSLRVVALAPGKPLTVPAGEHEYLVLPLSGGCTVQAGSERLEVAGRESVFTDITDYVYVPRHTEVTLISAGGARIALPGSKATTDKPLRYCPRSEVGTGLRGAGPSSRQVNNYALGNDVETSHLLACEVLTPGGNWSSYPPHKHDEHTEVERVLEEIYYYQVRAGEGDAEGFALQRIYPSPGHDIDVCTEVRGGDVVVMPYGYHGPSVAAPGYDLYYLNVMAGPAEDSVWLMTDDPHHTWVRQTWEGQEVDPRLPMTPMND$","Myo-inositol catabolism protein IolB","Cytoplasm","myo-inositol catabolism iolB","K03337 myo-inositol catabolism protein IolB","Myo-inositol catabolism IolB domain protein","","Miwa Y., Fujita Y. Involvement of two distinct catabolite-responsive elements in catabolite repression of the Bacillus subtilis myo-inositol (iol) operon. J. Bacteriol. 2001. 183(20):5877-5884. PMID: 11566986","","","

InterPro
IPR010669
Domain

Myo-inositol catabolism IolB region
PF06845	$\"[34-286]T$	IolB

InterPro
IPR012185
Family

Myo-inositol catabolism IolB
PIRSF036628	$\"[18-289]T$	Myo-inositol catabolism protein IolB

noIPR
unintegrated

unintegrated
PD550483	$\"[30-284]T$	Q9KZH6_STRCO_Q9KZH6;

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 30-284 are 65% similar to a (IOLB MYO-INOSITOL CATABOLISM PROTEIN ATU4509 SIMILAR ENZYME INOSITOL INVOLVED LMO0384) protein domain (PD550483) which is seen in Q9KZH6_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 34 to 286 (E_value = 1.8e-39) place ANA_0124 in the IolB family which is described as Myo-inositol catabolism protein IolB.","","catabolism iolB","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0125","138692","140599","1908","5.10","-22.20","69086","ATGAGCAACGAAGCCTACGCCGGCACGATCCGCCTGACGGTCGCCCAGGCCACCATCCGTTTCCTGTCCAACCAGTACTCCGAGCGCGACGGCGTCGAGCAGCGCCTCATCGCCGGGGCCTTCGGCATCTTCGGCCACGGCAACGTGGCCGGCATCGGCCAGGCCCTCCTGCAGAACGAGATCGCCCGCGCCGACGGCGAGCAGGAGATGCCCTACATCATGCCCCGCAACGAGCAGGGGCAGGTGCACGCGGCCGCCGCCTTCGCCAAGACCACCAACCGCCTCCAGACCTACATGTGCACGGCCTCCATCGGCCCGGGCTCCCTCAACATGGTCACCGGGGCCGCCCTGGCCACCACCAACCGCCTGCCGGTGCTGCTCTTCCCCTCCGACCAGTTCGCCACCCGCGTCCCCGACCCCGTGCTCCAGCAGCTGGAGGACCCCACGAGCCTCGACGTCAGCGTCAATGATGCCTTCCGCCCCGTCTCGCGCTTCTTCGACCGCATCAACCGGCCCGAGCAGCTCATCCCCTCGCTGCTGAGCGCCATGCGCGTGCTCACCGACCCCGCCGAGACCGGCGCGGTCACCATCGCCATGCCCCAGGACGTCCAGGCCGAGGTCTTCGACTGGCCCGTGGAGCTGTTCCGCAAGCGCGTGTGGCACGTGCGCCGCCCGGTGCCCGAGCCCGCCGCCCTGGAGCGCGCCGTCGCCCTCATCAAGGCCGCCAAGCGCCCCCTCATCATCGCCGGCGGCGGCACCATCTACGCCGGAGCCAGCGAGGAGCTGCGCGCCCTGGCCACCGCCACCGGCATCCCGGTCGGCGACACCCAGGCCGGCAAGGGCGCCATCAACTTCGACCACCCCAGCGCCGTGGGCGGCGTGGGCTCCACCGGCTGCGACTCCGGCAACCACATCGCCGACAAGGCCGACCTCATCATCGGCGTGGGCACCCGCTACTCCGACTTCACCACGGCCTCCAAGACCCAGTTCAAGAACCCCGACGTGAAGTTCGTGAACATCAACGTCACCCCCTTCGACGCCGCCAAGGAGAGCGCCGAGATGGTGGTGGCCGACGCCCGCGAGGCCCTGGCGGCCCTGACAGAGGCGCTCGCGGACTACCGCGTCGAGGCGGCCTACTCCGAGGAGATCACCGCGGAGAAGGAGGCCTGGCTCAAGGCCACCGAGCGCTGCTACCACCTGGACCACGGGCCCCTGCCCGCCCAGACCGAGGTCTTCGGCGCCCTCAACGAGCTCATGGGGGAGGAGGACGTGGTCATCAATGCCGCCGGCTCCATGCCCGGCGACCTCCAGGCCCTGTGGCAGGCCCGCAGCCCGCTGCAGTACCACGTGGAGTACGCCTTCTCCTGCATGGGCTATGAGGTGCCCGCCGCCATGGGCGTCAAGCTCGCCCGCCCCGAGGCCGAGGTGGTCTCCATCGTGGGCGACGGCACCTACCAGATGCTCCCCATGGAGCTGGCCACCGTGGTCCAGGAGAACATCAAGGTCATCTACGTTCTGCTGCAGAACTACGGCTTCTGCTCCATCGGCGCCCTCTCGGAGTCCCGCGGCTCCCAGCGCTTCGGCACCAAGTACCGCCAGCGCGGCGAGGGCAGCCACCTGGCCGACGAGCAGGTCATCGACGGTGTCGACATTGCCGCCAACGCCCGCTCCTGGGGCCTGGAAGTCCTCGAGGTCCACACCATCGCGGAGTTCAAGGAGGCCTACCGCAAGGCCGAGGCCTCCGACCGTCCCACGATGATCCACATCGAGACCGACCTCTACGGCCCCAACCCGCCCGGCTCGAGCTGGTGGGACGTCCCGGTCTCGGGGGTCTCCGAGCTGGAGTCCACGCAGCGCGCCTATGAGGAGTACCTGCGTGACCGCAAGCCTCAGCGCCACTACCTGTAA","MSNEAYAGTIRLTVAQATIRFLSNQYSERDGVEQRLIAGAFGIFGHGNVAGIGQALLQNEIARADGEQEMPYIMPRNEQGQVHAAAAFAKTTNRLQTYMCTASIGPGSLNMVTGAALATTNRLPVLLFPSDQFATRVPDPVLQQLEDPTSLDVSVNDAFRPVSRFFDRINRPEQLIPSLLSAMRVLTDPAETGAVTIAMPQDVQAEVFDWPVELFRKRVWHVRRPVPEPAALERAVALIKAAKRPLIIAGGGTIYAGASEELRALATATGIPVGDTQAGKGAINFDHPSAVGGVGSTGCDSGNHIADKADLIIGVGTRYSDFTTASKTQFKNPDVKFVNINVTPFDAAKESAEMVVADAREALAALTEALADYRVEAAYSEEITAEKEAWLKATERCYHLDHGPLPAQTEVFGALNELMGEEDVVINAAGSMPGDLQALWQARSPLQYHVEYAFSCMGYEVPAAMGVKLARPEAEVVSIVGDGTYQMLPMELATVVQENIKVIYVLLQNYGFCSIGALSESRGSQRFGTKYRQRGEGSHLADEQVIDGVDIAANARSWGLEVLEVHTIAEFKEAYRKAEASDRPTMIHIETDLYGPNPPGSSWWDVPVSGVSELESTQRAYEEYLRDRKPQRHYL$","Acetolactate synthase, thiamine diphosphate-dependent","Cytoplasm","Thiamine pyrophosphate-requiring enzymes[acetolactate synthase, pyruvate dehydrogenase","putative acetolactate synthase","thiamine pyrophosphate enzyme, central region","","Arjunan P., Umland T., Dyda F., Swaminathan S., Furey W., Sax M., Farrenkopf B., Gao Y., Zhang D., Jordan F. Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. J. Mol. Biol. 1996. 256(3):590-600. PMID: 8604141Koga J., Adachi T., Hidaka H. Purification and characterization of indolepyruvate decarboxylase. A novel enzyme for indole-3-acetic acid biosynthesis in Enterobacter cloacae. J. Biol. Chem. 1992. 267(22):15823-15828. PMID: 1639814Polovnikova E.S., Mcleish M.J., Sergienko E.A., Burgner J.T., Anderson N.L., Bera A.K., Jordan F., Kenyon G.L., Hasson M.S. Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase. Biochemistry 2003. 42(7):1820-1830. PMID: 12590569","","","

InterPro
IPR000399
Family

TPP-binding enzymes
PIRSF001370	$\"[14-606]T$	Thiamine diphosphate-dependent enzyme, acetolactate synthase type

InterPro
IPR011766
Domain

Thiamine pyrophosphate enzyme, C-terminal TPP-binding
PF02775	$\"[428-589]T$	TPP_enzyme_C

InterPro
IPR012000
Domain

Thiamine pyrophosphate enzyme, central region
PF00205	$\"[232-366]T$	TPP_enzyme_M

InterPro
IPR012001
Domain

Thiamine pyrophosphate enzyme, N-terminal TPP binding region
PF02776	$\"[12-212]T$	TPP_enzyme_N

InterPro
IPR012276
Family

Myo-inositol catabolism decarboxylase IolD
PIRSF500070	$\"[8-634]T$	Myo-inositol catabolism protein IolD

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1220	$\"[224-390]T$	no description
G3DSA:3.40.50.970	$\"[10-223]T$ $\"[401-592]T$	no description
PTHR18968	$\"[272-531]T$ $\"[548-627]T$	THIAMINE PYROPHOSPHATE ENZYMES
PTHR18968:SF9	$\"[272-531]T$ $\"[548-627]T$	MALONIC SEMIALDEHYDE OXIDATIVE DECARBOXYLASE

","BeTs to 20 clades of COG0028COG name: Thiamine pyrophosphate-requiring enzymes acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylaseFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0028 is a-mpkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB000399 (Pyruvate decarboxylase) with a combined E-value of 8.6e-18. IPB000399B 462-472 IPB000399C 476-509","Residues 7-65 are 69% similar to a (TRANSFERASE ACETOLACTATE SYNTHASE) protein domain (PDA1D126) which is seen in Q6M8J5_CORGL.Residues 9-67 are 81% similar to a (THIAMINE PYROPHOSPHATE-REQUIRING SYNTHASE ENZYME ACETOLACTATE) protein domain (PDA120X9) which is seen in Q6AAK5_PROAC.Residues 10-56 are 72% similar to a (IOLD) protein domain (PDA1D124) which is seen in Q9A8Q4_CAUCR.Residues 11-218 are 75% similar to a (SYNTHASE ACETOLACTATE BIOSYNTHESIS LARGE SUBUNIT THIAMINE PYRUVATE PYROPHOSPHATE TRANSFERASE FLAVOPROTEIN) protein domain (PD000376) which is seen in Q82CK4_STRAW.Residues 11-58 are 85% similar to a (IOLD MYO-INOSITOL CATABOLISM ENZYME SEMIALDEHYDE OXIDATIVE THIAMINE DECARBOXYLASE MALONIC SUBTILIS) protein domain (PD864479) which is seen in Q8CJL4_STRCO.Residues 12-205 are 45% similar to a (THIAMINE ACETOLACTATE PYROPHOSPHATE SYNTHASE) protein domain (PD648192) which is seen in Q8TPF5_METAC.Residues 37-288 are 39% similar to a (ACETOLACTATE SYNTHASE) protein domain (PD742211) which is seen in Q82ND1_STRAW.Residues 38-244 are 46% similar to a (THIAMINE ACETOLACTATE SUBUNIT HOMOLOG PYROPHOSPHATE SYNTHASE LARGE) protein domain (PDA191J9) which is seen in O27639_METTH.Residues 69-324 are 43% similar to a (SYNTHASE LARGE ACETOLACTATE SUBUNIT) protein domain (PD386643) which is seen in Q9K659_BACHD.Residues 70-124 are 81% similar to a (IOLD ACETOLACTATE SYNTHASE THIAMINE SEMIALDEHYDE OXIDATIVE DECARBOXYLASE MALONIC ENZYME PYROPHOSPHATE-REQUIRING) protein domain (PD896228) which is seen in Q6AAK5_PROAC.Residues 72-284 are 43% similar to a (PYROPHOSPHATE TR THIAMINE FLAVOPROTEIN ALS SYNTHASE TRANSFERASE ACETOHYDROXY-ACID BRANCHED-CHAIN BIOSYNTHESIS) protein domain (PD123410) which is seen in ILVB_SCHPO.Residues 125-242 are 80% similar to a (IOLD ACETOLACTATE SYNTHASE THIAMINE SEMIALDEHYDE OXIDATIVE DECARBOXYLASE MALONIC ENZYME PYROPHOSPHATE-DEPENDENT) protein domain (PD611167) which is seen in Q6AAK5_PROAC.Residues 287-342 are 85% similar to a (SYNTHASE BIOSYNTHESIS ACETOLACTATE LARGE SUBUNIT ACID THIAMINE TRANSFERASE FLAVOPROTEIN MAGNESIUM) protein domain (PD587410) which is seen in Q6AAK5_PROAC.Residues 406-584 are 69% similar to a (SYNTHASE ACETOLACTATE BIOSYNTHESIS LARGE THIAMINE PYRUVATE SUBUNIT PYROPHOSPHATE TRANSFERASE ACID) protein domain (PD000397) which is seen in Q82CK4_STRAW.Residues 491-590 are 53% similar to a (ENZYME SEMIALDEHYDE OXIDATIVE THIAMINE IOLD PYROPHOSPHATE-REQUIRING PROTEIN DECARBOXYLASE MALONIC) protein domain (PD717418) which is seen in Q81QB5_BACAN.Residues 516-592 are 65% similar to a (THIAMINE TRANSFERASE ACETOLACTATE ENZYMES PYROPHOSPHATE-REQUIRING SYNTHASE) protein domain (PD932502) which is seen in Q8NTY9_CORGL.Residues 521-633 are 46% similar to a (IOLD PLASMID) protein domain (PD987981) which is seen in Q6W1J3_RHISN.Residues 535-591 are 82% similar to a (ACETOLACTATE SYNTHASE THIAMINE PYROPHOSPHATE-REQUIRING ENZYME) protein domain (PD653377) which is seen in Q6AAK5_PROAC.Residues 592-634 are 69% similar to a (THIAMINE PYROPHOSPHATE-REQUIRING SYNTHASE ENZYME ACETOLACTATE) protein domain (PD987999) which is seen in Q6AAK5_PROAC.","","-40% similar to PDB:1YBH Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide Chlorimuron Ethyl (E_value = 2.3E_28);-40% similar to PDB:1YHY Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Metsulfuron methyl (E_value = 2.3E_28);-40% similar to PDB:1YHZ Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Chlorsulfuron (E_value = 2.3E_28);-40% similar to PDB:1YI0 Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Sulfometuron methyl (E_value = 2.3E_28);-40% similar to PDB:1YI1 Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Tribenuron methyl (E_value = 2.3E_28);","Residues 12 to 212 (E_value = 1.2e-06) place ANA_0125 in the TPP_enzyme_N family which is described as Thiamine pyrophosphate enzyme, N-terminal TPP binding domain.Residues 232 to 366 (E_value = 2.3e-51) place ANA_0125 in the TPP_enzyme_M family which is described as Thiamine pyrophosphate enzyme, central domain.Residues 428 to 589 (E_value = 1.7e-40) place ANA_0125 in the TPP_enzyme_C family which is described as Thiamine pyrophosphate enzyme, C-terminal TPP binding domain.","","pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase] (AJ276296)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0126","140970","142463","1494","5.83","-12.74","53292","ATGAGAACCATTGCGCACTGGGTTGACGGAAAGTACTACGAGGGAAACCCGATCGGGCGCTTTGCCGTCGAGAACCCGGGGACCGGTGAGGTCGAGGCCGAGCTGCTCCAGGCCTCCGACGCCGACCTCGACCACGCCGTCGAGGTGGCGCGCCGTGCCCAGAAGGAGTGGGCGAAGGTCTCGCTGGCCAAGCGCACCGCCATCATGTTCCGCATGCGCCAGCTGGTCCTGGACCACCAGGACGAGATGGCCAAGATGATCGTGGCCGAGCACGGCAAGAACTACTCCGACGCCGTCGGCGAGATCCAGCGCGGGCGCGAGACCCTCGACTTCGCCACCGCCATCAACCTGGCCCTCAAGGGCGAGCACTCCTTCGACATCTCCACCGGCGTGGACATCCACACCCTGCGCCAGCCGGTCGGCGTCGTCGCCGGCATCTGCCCCTTCAACTTCCCGGCCATGGTGCCCATGTGGATGCACCCCATCGCCATCGCCACCGGTAACGCCTTCATCCTCAAGCCGGCCTCGGCCACGCCGTCTGCGGCCCTGCTGACGGCCGAGCTCTACAAGGAGGCCGGCCTGCCCGACGGCGTCTTCAACGTCGTCTCCGGCAACCGCACCATGGTCTCCAAGGTCCTCGAGCACCCCGGCATCGACGCGATCTCCTTCGTGGGCTCCACCCCGGTGGCCCACATCGTCCAGAACACCGGCGTCACCCACGGCAAGCGCGTCCAGGCCCTGGGCGGGGCGAACAACCACGCCATCGTCATGCCCGACTCCGACCTGGACTTCGCCGCCCAGCACATCTCCGCCGCCGCCTTTGGCGCCGCCGGCGAGCGCTGCATGGCCCTGCCCGTCGTCGTGGCCGTGGGCGGCTGCGGACCGGATCTGGCCCGCCGCGTCAAGGCCCACGCCGAGAAGATCAAGGTCGGCTACGGCATGGACGAGGGCATCGAGATGGGCCCGGTCATCGACGCCAAGTCCAAGGAGTTCATCACCGGACTCATCGACGACGCCGAGGCCAAGGGAGCCGAGGTCGTCCTCGACGGCCGTCCGCTGGTCATCCCCGGACACGAGAAGGGTCACTTCCTCGGCCCGACCATCGTGGACAACGTCTCCCTGGAGTCCTCGCTCTACACCGAGGAGGTCTTCGGGCCGGTGCTCGCCATCGTCCACACCGACACCTACGAGGAGGCCATCAAGCAGGTCAACTCCTCGCCCTTCGGCAACGGCGCGGCCATCTTTACCAATGACGGCGGCGTGGCTCGCCGCTTCGAGCTCGACGTCGAGGCCGGCATGGTGGGCATCAACGTGCCGATCCCGACGCCGGTGGCCTACTACTCCTTCGGCGGCTGGAAGGAGTCGCTCCTGGGTGACACCCACATCCACGGCCCCGAGGGCGTGCGGTTCTACACCCGTGCCAAGGCGGTGACCACCCGCTGGCCCTCGGAGAAGACCTACGCCGCGACCATGTCCTTCCAGCGCGAGGAGTGA","MRTIAHWVDGKYYEGNPIGRFAVENPGTGEVEAELLQASDADLDHAVEVARRAQKEWAKVSLAKRTAIMFRMRQLVLDHQDEMAKMIVAEHGKNYSDAVGEIQRGRETLDFATAINLALKGEHSFDISTGVDIHTLRQPVGVVAGICPFNFPAMVPMWMHPIAIATGNAFILKPASATPSAALLTAELYKEAGLPDGVFNVVSGNRTMVSKVLEHPGIDAISFVGSTPVAHIVQNTGVTHGKRVQALGGANNHAIVMPDSDLDFAAQHISAAAFGAAGERCMALPVVVAVGGCGPDLARRVKAHAEKIKVGYGMDEGIEMGPVIDAKSKEFITGLIDDAEAKGAEVVLDGRPLVIPGHEKGHFLGPTIVDNVSLESSLYTEEVFGPVLAIVHTDTYEEAIKQVNSSPFGNGAAIFTNDGGVARRFELDVEAGMVGINVPIPTPVAYYSFGGWKESLLGDTHIHGPEGVRFYTRAKAVTTRWPSEKTYAATMSFQREE$","Methylmalonate-semialdehyde dehydrogenase","Cytoplasm","methylmalonate-semialdehyde dehydrogenase","methylmalonate-semialdehyde dehydrogenase","methylmalonate-semialdehyde dehydrogenase","","Steele M.I., Lorenz D., Hatter K., Park A., Sokatch J.R. Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. J. Biol. Chem. 1992. 267(19):13585-13592. PMID: 1339433Zhang Y.X., Tang L., Hutchinson C.R. Cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces coelicolor. J. Bacteriol. 1996. 178(2):490-495. PMID: 8550471Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W., Harris R.A. CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. J. Biol. Chem. 1992. 267(27):19724-19729. PMID: 1527093Yoshida K.I., Aoyama D., Ishio I., Shibayama T., Fujita Y. Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis. J. Bacteriol. 1997. 179(14):4591-4598. PMID: 9226270","","","

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PF00171	$\"[12-477]T$	Aldedh

InterPro
IPR010061
Family

Methylmalonate-semialdehyde dehydrogenase
PTHR11699:SF27	$\"[48-496]T$	METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE
TIGR01722	$\"[4-481]T$	MMSDH: methylmalonate-semialdehyde dehydrog

InterPro
IPR012303
Family

NAD-dependent aldehyde dehydrogenase
PIRSF000147	$\"[20-485]T$	NAD-dependent aldehyde dehydrogenase

InterPro
IPR015590
Domain

Aldehyde Dehydrogenase_
PTHR11699	$\"[48-496]T$	ALDEHYDE DEHYDROGENASE-RELATED

noIPR
unintegrated

unintegrated
G3DSA:3.40.605.10	$\"[3-284]T$	no description

","No hits to the COGs database.","***** IPB002086 (Aldehyde dehydrogenase) with a combined E-value of 5.5e-68. IPB002086A 138-179 IPB002086B 195-206 IPB002086C 252-300 IPB002086D 363-416 IPB002086E 438-462***** IPB011264 (Betaine aldehyde dehydrogenase) with a combined E-value of 4.2e-53. IPB011264A 32-71 IPB011264C 136-174 IPB011264D 179-206 IPB011264E 244-297 IPB011264F 320-373 IPB011264G 375-413","Residues 2-486 are 45% similar to a (DEHYDROGENASE ALDEHYDE) protein domain (PD728494) which is seen in Q9RYT8_DEIRA.Residues 2-481 are 60% similar to a (ALDEHYDE DEHYDROGENASE PROBABLE) protein domain (PD723136) which is seen in Q9I5I2_PSEAE.Residues 5-475 are 49% similar to a (ALDEHYDE DEHYDROGENASE) protein domain (PD449341) which is seen in Q98DB0_RHILO.Residues 7-493 are 45% similar to a (BENZALDEHYDE DEHYDROGENASE) protein domain (PD722867) which is seen in Q9A5Q0_CAUCR.Residues 7-472 are 49% similar to a (F45H10.1) protein domain (PDA181A7) which is seen in O02266_CAEEL.Residues 7-481 are 49% similar to a (PHENYLACETALDEHYDE OXIDOREDUCTASE DEHYDROGENASE SEQUENCING DIRECT NAD PAD) protein domain (PDA0J2C9) which is seen in FEAB_ECOLI.Residues 7-458 are 47% similar to a (ALDEHYDE ALDY DEHYDROGENASE) protein domain (PDA193O6) which is seen in P94358_BACSU.Residues 7-482 are 48% similar to a (OXIDOREDUCTASE DEHYDROGENASE ALDEHYDE PLASMID) protein domain (PDA0J2D0) which is seen in Q6W1I3_RHISN.Residues 7-478 are 46% similar to a (MEIOTIC OXIDOREDUCTASE UP-REGULATED DEHYDROGENASE PROBABLE BADH MEIOSIS ALDEHYDE EXPRESSION NAD) protein domain (PDA0J2D1) which is seen in DHAB_SCHPO.Residues 7-437 are 46% similar to a (MMCL) protein domain (PDA0J2C7) which is seen in Q9X5T0_STRLA.Residues 7-204 are 51% similar to a (ALDEHYDE CYTOSOLIC DEHYDROGENASE) protein domain (PDA1A9N1) which is seen in Q6JA94_EEEEE.Residues 8-481 are 47% similar to a (1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE) protein domain (PD243617) which is seen in Q9RZC4_DEIRA.Residues 8-477 are 46% similar to a (DEHYDROGENASE VANILLIN) protein domain (PD723371) which is seen in Q84IP9_PSEPA.Residues 8-281 are 45% similar to a () protein domain (PDA0I442) which is seen in Q73WL2_MYCPA.Residues 23-282 are 48% similar to a () protein domain (PD948750) which is seen in Q73V72_MYCPA.Residues 23-451 are 41% similar to a (DEHYDROGENASE PROLINE) protein domain (PD575773) which is seen in Q52711_RHOCA.Residues 23-477 are 44% similar to a (ALDEHYDE NAD OXIDOREDUCTASE DEHYDROGENASE PROBABLE) protein domain (PD727097) which is seen in DHAL_PSESP.Residues 23-478 are 69% similar to a (DEHYDROGENASE OXIDOREDUCTASE ALDEHYDE SEMIALDEHYDE PROLINE NADP REDUCTASE GAMMA-GLUTAMYL PHOSPHATE GPR) protein domain (PD250846) which is seen in Q6D769_BBBBB.Residues 25-258 are 72% similar to a (SEMIALDEHYDE METHYLMALONIC DEHYDROGENASE ACID) protein domain (PD751435) which is seen in Q82CK3_STRAW.Residues 26-483 are 46% similar to a (OXIDOREDUCTASE SUCCINATE-SEMIALDEHYDE DEHYDROGENASES ALDEHYDE DEHYDROGENASE PROBABLE NAD-DEPENDENT) protein domain (PDA188E8) which is seen in Q8NM66_CORGL.Residues 38-451 are 44% similar to a (PREDICTED PROLINE DEHYDROGENASE) protein domain (PD297252) which is seen in Q9F7Q7_PRB01.Residues 50-418 are 43% similar to a (DEHYDROGENASE NAD METABOLISM PROLINE P5C OXIDOREDUCTASE DELTA-1-PYRROLINE-5-CARBOXYLATE) protein domain (PDA185E9) which is seen in PUT2_AGABI.Residues 62-477 are 41% similar to a (OXIDOREDUCTASE NAD DEHYDROGENASE ALDEHYDE) protein domain (PD069129) which is seen in DHA1_ENTHI.Residues 93-386 are 41% similar to a (DEHYDROGENASE AT5G62530 OXIDOREDUCTASE DELTA-1-PYRROLINE-5-CARBOXYLATE) protein domain (PD891633) which is seen in Q9FJJ2_ARATH.Residues 139-482 are 42% similar to a (YARROWIA LIPOLYTICA A STRAIN CLIB99 CHROMOSOME) protein domain (PD957719) which is seen in Q6CGN3_EEEEE.Residues 141-403 are 45% similar to a (ILV2-ADE17 1.2.1.- LIKE OXIDOREDUCTASE ALDEHYDE-DEHYDROGENASE) protein domain (PD502700) which is seen in YM00_YEAST.Residues 402-451 are 68% similar to a (ALDEHYDE NAD-DEPENDENT OXIDOREDUCTASE DEHYDROGENASES DEHYDROGENASE) protein domain (PD616244) which is seen in Q8NSX1_CORGL.Residues 440-481 are 95% similar to a (OXIDOREDUCTASE DEHYDROGENASE SEMIALDEHYDE ALDEHYDE METHYLMALONATE-SEMIALDEHYDE NAD-DEPENDENT OXIDATIVE DEHYDROGENASES METHYLMALONIC ACID) protein domain (PD968275) which is seen in Q6AAK3_PROAC.","","-62% similar to PDB:1T90 Crystal structure of methylmalonate semialdehyde dehydrogenase from Bacillus subtilis (E_value = 1.3E_111);-49% similar to PDB:1A4S BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER (E_value = 6.4E_55);-49% similar to PDB:1BPW BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER (E_value = 6.4E_55);-51% similar to PDB:2ESD Crystal Structure of thioacylenzyme intermediate of an Nadp Dependent Aldehyde Dehydrogenase (E_value = 1.0E_52);-51% similar to PDB:1EUH APO FORM OF A NADP DEPENDENT ALDEHYDE DEHYDROGENASE FROM STREPTOCOCCUS MUTANS (E_value = 3.9E_52);","Residues 12 to 477 (E_value = 1e-159) place ANA_0126 in the Aldedh family which is described as Aldehyde dehydrogenase family.","","dehydrogenase (mmsA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0127","142989","144605","1617","7.54","1.80","58307","ATGTCCACATCACCCAGTTCTGCGGTGCACTACACGCCGGAGAAGATCCGGGAGCTGGTCGACCAGACCCCCGCCTCAGGGCCGAAGCGCTCGCTCGGACTCATCGCCCTGGTCGCCACCCTCGGCTCGCTGCTCTTCGGATACGACACCGGCGTCATCTCCGGTGCCCTGCCCTACATGTACCTGCCGCACGGTGCCGACGGCCTGCAGATCACCTCCTGGGAGGAGGGCTGGATCGGCGGCCTGCTCTGCATCGGCGCCGCGCTCGGCGCCTCGGTCGGAGGCAAGCTCTCCGACAAGTACGGGCGCCGGCACAACATCATGCTCCTGGCCATCGTCTTCTTCATTGGGGCGCTGGGCTGCACGATCTCGCCCAACATCTGGGTCCTCTACTTCTTCCGGATCGTGCTGGGCTTCGCCGTCGGTGGTGCCTCGGCGATCGTTCCCGTCTTCCTTGGTGAGACGGCCCCCAAGCGCATTCGTGGCACCCTGGTGGCCGTGGACCAGATGATGATCGTCTTCGGCCAGTTCCTCGCCTTCTCTATGAACGCCGTCCTGGCCCGCATGCACGGCGGCCCGGAGGTCACCCTGGCCAACGACGTCGTCAACAAGTCCGGTGAGGTCGTCGCCAAGGCCGGCGATAAGGTCGCCTGGGAGACCGTGCAGCACTTCAGCAACGTCGTGGTCGAGTCCGGCAACGGCATGACCTGGCGCTACATGCTCGTCCTGGCCACTCTGCCCGCCGTCGCCCTGTGGTTCGGCATCCGCCTCATGCCGGAGTCCTCGCGCTGGTACGTTGCCAACCTGCGCATCGCCGAGGCCATCGGCTCTCTCAAGCGGGTGCGCGACGAGTCCAAGGACGGCTCCATCGCCGAAGAGGTCGATGAGATGCTGGAGATCCAGCGCAAGGAGGCCAACCAGGAGAAGTGGGGGCTGGCGCAGATCATGGGCGTCAAATGGACCCGCCACCTGCTCTTCATCGGCATCATCCTGGGTCTGGCCGACCAGGTCACCGGCATCAACACAGCCATGTACTACACGCCCAAGCTGCTCTCCGCGGCCGGCCTGCCCATGAGTGACGCGATCTCCCTCAACGTCGTCTCCGGATTCGTCTCCTTCGTGGGCTCCGCCATCGGCCTGTGGCTGGTCACCAAGTTCGCTCGCCGCCACGTGGGCATCTACCAGGAGGCCAGCATCGTGGTCTCCCTCGGGCTCCTGGCGGCAGTCTTCTACTTCCTCATCCAGCCCTACCAGGACTCCGACGGCAACATTACGGGAGCCCCCGCCTTCGCCCCCTACCTGGTGCTGCTCATCGTCTCGCTGTTCGTGTTCGCCAAGCAGTCCGGAACAGTCACCTGGGTCCTCATCGCGGAGATCTACCCCGCCAAGGTGCGCGGTACAGCGATGGGTCTGGCTGTGGGCACTCTGTGGATCGGCAACGCGATCGTCGCCGCGGTCTTCCCCGTCATGATGGAGAAGCTCGGAGGGGCGGGGACCTACCTCATCTTCTGCCTGTTGAACGTCCTGTCACTCATCTTCTACATGAAGTTCGTGCCCGAGACGAAGTACCACTCCTTGGAGGAGCTCGAGGTGCGCTTCGAGAAGGAGTACAGCTGA","MSTSPSSAVHYTPEKIRELVDQTPASGPKRSLGLIALVATLGSLLFGYDTGVISGALPYMYLPHGADGLQITSWEEGWIGGLLCIGAALGASVGGKLSDKYGRRHNIMLLAIVFFIGALGCTISPNIWVLYFFRIVLGFAVGGASAIVPVFLGETAPKRIRGTLVAVDQMMIVFGQFLAFSMNAVLARMHGGPEVTLANDVVNKSGEVVAKAGDKVAWETVQHFSNVVVESGNGMTWRYMLVLATLPAVALWFGIRLMPESSRWYVANLRIAEAIGSLKRVRDESKDGSIAEEVDEMLEIQRKEANQEKWGLAQIMGVKWTRHLLFIGIILGLADQVTGINTAMYYTPKLLSAAGLPMSDAISLNVVSGFVSFVGSAIGLWLVTKFARRHVGIYQEASIVVSLGLLAAVFYFLIQPYQDSDGNITGAPAFAPYLVLLIVSLFVFAKQSGTVTWVLIAEIYPAKVRGTAMGLAVGTLWIGNAIVAAVFPVMMEKLGGAGTYLIFCLLNVLSLIFYMKFVPETKYHSLEELEVRFEKEYS$","Sugar transporter, MFS superfamily","Membrane, Cytoplasm","sugar transporter homolog ydjK","sugar transporter","sugar transporter","","Saenz H.L., Augsburger V., Vuong C., Jack R.W., Gotz F, Otto M. Inducible expression and cellular location of AgrB, a protein involved in the maturation of the staphylococcal quorum-sensing pheromone. Arch. Microbiol. 2000. 174(6):452-455. PMID: 11195102Zhang L., Gray L., Novick R.P., Ji G. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 2002. 277(38):34736-34742. PMID: 12122003","","","

InterPro
IPR003663
Family

Sugar transporter
PR00171	$\"[43-53]T$ $\"[131-150]T$ $\"[335-345]T$ $\"[434-455]T$ $\"[457-469]T$	SUGRTRNSPORT
TIGR00879	$\"[1-529]T$	SP: MFS transporter, sugar porter (SP) fami

InterPro
IPR005828
Family

General substrate transporter
PF00083	$\"[35-533]T$	Sugar_tr

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[94-111]T$	SUGAR_TRANSPORT_1
PS00217	$\"[136-161]T$	SUGAR_TRANSPORT_2

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[285-491]T$	no description

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[35-522]T$	MFS

noIPR
unintegrated

unintegrated
PTHR11600	$\"[34-193]T$ $\"[237-389]T$	SUGAR TRANSPORTER
PTHR11600:SF85	$\"[34-193]T$ $\"[237-389]T$	SUGAR TRANSPORTER
tmhmm	$\"[32-52]?$ $\"[71-91]?$ $\"[106-126]?$ $\"[132-152]?$ $\"[167-187]?$ $\"[235-255]?$ $\"[323-343]?$ $\"[362-382]?$ $\"[397-415]?$ $\"[425-445]?$ $\"[466-488]?$ $\"[494-514]?$	transmembrane_regions

","BeTs to 20 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","***** IPB005829 (Sugar transporter superfamily) with a combined E-value of 8.6e-32. IPB005829A 43-54 IPB005829B 130-177 IPB005829D 335-355 IPB005829B 434-481***** IPB003663 (Sugar transporter signature) with a combined E-value of 1.1e-16. IPB003663A 43-53 IPB003663B 131-150 IPB003663E 457-469 IPB003663D 109-130","Residues 94-127 are 85% similar to a (TRANSMEMBRANE TRANSPORTER SUGAR RESISTANCE FAMILY MEMBRANE MULTIDRUG FACILITATOR MAJOR PROBABLE) protein domain (PD000082) which is seen in Q6AAJ7_PROAC.Residues 130-336 are 43% similar to a (SUGAR SUGAR-PROTON TRANSMEMBRANE SYMPORTER) protein domain (PD702144) which is seen in Q8A1Q3_BACTN.Residues 133-167 are 85% similar to a (TRANSMEMBRANE SUGAR TRANSPORTER GLUCOSE FAMILY PHOSPHATE GLYCOPROTEIN HEXOSE PERMEASE CARRIER) protein domain (PD860544) which is seen in Q6AAJ7_PROAC.Residues 226-270 are similar to a (TRANSMEMBRANE SUGAR TRANSPORTER GLUCOSE FAMILY GLYCOPROTEIN CARRIER ORGANIC MEMBER HEXOSE) protein domain (PD197893) which is seen in Q6AAJ7_PROAC.Residues 271-338 are 61% similar to a (SUGAR TRANSPORTER YFIG) protein domain (PD945641) which is seen in Q6AAJ7_PROAC.Residues 385-470 are 62% similar to a (SUGAR TRANSMEMBRANE TRANSPORTER FAMILY METABOLITE PROBABLE SUGI INTEGRAL PHOSPHATE MEMBRANE) protein domain (PD261536) which is seen in Q6AAJ7_PROAC.Residues 451-522 are 55% similar to a (TRANSMEMBRANE TRANSPORTER SUGAR PHOSPHATE FAMILY ORGANIC FACILITATOR MAJOR MEMBRANE MFS) protein domain (PD073361) which is seen in Q7UF68_RHOBA.Residues 478-529 are 69% similar to a (SUGAR TRANSMEMBRANE SUGI) protein domain (PD958019) which is seen in Q73UB9_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 533 (E_value = 2.3e-85) place ANA_0127 in the Sugar_tr family which is described as Sugar (and other) transporter.Residues 39 to 492 (E_value = 1.5e-23) place ANA_0127 in the MFS_1 family which is described as Major Facilitator Superfamily.Residues 454 to 522 (E_value = 6.5e-08) place ANA_0127 in the MFS_1 family which is described as Major Facilitator Superfamily.","","transporter homolog ydjK","","1","","","","","","","","","","","Mon Aug 13 17:15:52 2007","","Mon Aug 13 17:15:52 2007","","","Mon Aug 13 17:15:52 2007","Mon Aug 13 17:15:52 2007","Mon Aug 13 17:15:52 2007","","Mon Aug 13 17:15:52 2007","Mon Aug 13 17:15:52 2007","","","","","yes","","" "ANA_0129","144788","146068","1281","9.97","9.03","43671","ATGAACCCGCATCCGCCGCGCAGCGCGCCACCCGCTCCGCTCCGCCTCCGCCTGTACGCATGGGCGGCAGGTCTGTTCCTCGGCGCCCTGGAAGGGGCGCTGGCTATCGAGGTCGCCGGCGCGCGCGGCGCCGCTCTGCCCCTGCTCGGTGCCGTCGCTGCGGCGATGGTGCTGGGAACCGTCACCGGCCGCCCCCTCGCCCGGTACTTGGGGCGACGGAGAATGGGCCTGCTCATGGGAGGTCTGGCAGTGCTGGGCGCCGGGGTCGCAGCCGGGCTCGGCGGCGTCGTCGGCCTGATCGGGGCCGGCCTGGTGGGCCTTGCCGTGGGTGGGGTGCTCGTTGTGGCGCCACTGGTGTGCCACGAGCTCTCCCTGTGCGGGCACAAGCGGCTCATGCCGCAGGCCATGGCTCTCGGCCCGGCCGCGGCCGGCGTCGTGGTCCTGGCGGCCTGGTGGACGCCCTCGCCGCTCTTCATCGCCTGGGCGATGGTCGCCGTCGCCGCGCTGATCTACCTGGCCTGCTCCCTGCTCCTGCCCGAGAGCCCGGTCTGGCTGGTGCGGCAGGGGCGCGACGTCGAGGCCTTCGAGGCGCTGCGCCGCCTGCACGGGACCCTGGAGGCCTCCGTGGCCATCGACTGGACCCGGCTGGACGCGGAGATGATGGCCGAGCAGCAAGCCATGTCTCCCGCTGAGCTGCGAGTGCCCGAGGTGCGTGCCGCCGTGCTCACCGGCGCGGTCCTCATCATCGCCCAAGAGGCGCCCCTGGGGGCGGCGGCCCTGGTCCTCGCCCCGCTGATCGCCACCGAGCTCGGCCTTGCATCCGTAGCGATCGCGGTGAGCGCCGCGACCTGGATGGGACTGGCGCTCCTCGCTCTGGCGCTGGTGACCCGGGTCGAGCAGCTGCGCTTCCTGCGGGTGGTGCTGGGAACCGTCGTCGCCGTCCTGGGGGCCACCTTCCTGGTGACCGGCATGACCCTGGGGGGCGTGGGCGGCGCCTGGACGATCATCATCTCCCTGACGATCCTGGTCGCCAGTCAGTCGGTCCTGGTCCTGCCCGCCTGCCAGGGGGCGATCGACCCGCGGATCCCGCCCTGGCTGGTTGAGGCGCAGCGGCGCGCCTCGGCGACTGGGGGAGTCCTGGCGCGTGCCGGAGTCCTCCTGGCCTCACTGCTCATCGTGAGTTACCTCGGAACCCACGCCCTGTTCTGGGCGGCCTTCACGCTCTCGGTGCTCAGCGTCGCCGTCGTGCTCCTGCGCCTGCCGCGCGAGCTCAAGGTCTAG","MNPHPPRSAPPAPLRLRLYAWAAGLFLGALEGALAIEVAGARGAALPLLGAVAAAMVLGTVTGRPLARYLGRRRMGLLMGGLAVLGAGVAAGLGGVVGLIGAGLVGLAVGGVLVVAPLVCHELSLCGHKRLMPQAMALGPAAAGVVVLAAWWTPSPLFIAWAMVAVAALIYLACSLLLPESPVWLVRQGRDVEAFEALRRLHGTLEASVAIDWTRLDAEMMAEQQAMSPAELRVPEVRAAVLTGAVLIIAQEAPLGAAALVLAPLIATELGLASVAIAVSAATWMGLALLALALVTRVEQLRFLRVVLGTVVAVLGATFLVTGMTLGGVGGAWTIIISLTILVASQSVLVLPACQGAIDPRIPPWLVEAQRRASATGGVLARAGVLLASLLIVSYLGTHALFWAAFTLSVLSVAVVLLRLPRELKV$","Permease of the major facilitator superfamily","Membrane, Cytoplasm","Probable metabolite transport protein csbC,putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Paulsen I.T., Brown M.H., Skurray R.A. Proton-dependent multidrug efflux systems. Microbiol. Rev. 1996. 60(4):575-608. PMID: 8987357Henderson P.J., Maiden M.C. Homologous sugar transport proteins in Escherichia coli and their relatives in both prokaryotes and eukaryotes. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 1990. 326(1236):391-410. PMID: 1970645","","","

InterPro
IPR005828
Family

General substrate transporter
PF00083	$\"[162-251]T$	Sugar_tr

noIPR
unintegrated

unintegrated
PTHR11600	$\"[162-212]T$	SUGAR TRANSPORTER
PTHR11600:SF85	$\"[162-212]T$	SUGAR TRANSPORTER
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[47-67]?$ $\"[76-91]?$ $\"[97-119]?$ $\"[134-152]?$ $\"[158-178]?$ $\"[242-264]?$ $\"[270-292]?$ $\"[307-327]?$ $\"[333-353]?$ $\"[374-394]?$ $\"[400-420]?$	transmembrane_regions

","BeTs to 6 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","***** IPB005829 (Sugar transporter superfamily) with a combined E-value of 4.7e-06. IPB005829B 98-145 IPB005829C 177-186","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 162 to 251 (E_value = 2.4e-06) place ANA_0129 in the Sugar_tr family which is described as Sugar (and other) transporter.","","metabolite transport protein csbC, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0130","146144","147403","1260","5.71","-7.29","43738","ATGTCGTATGGTGGGGGTGTGGCCGCAAGAGTCCACTCGGCGGCCCGACGTCGTCGACACCTGACAGAGAGGCACCTGAGCATGACGAGCAACGAGGCAGTCCAGGCCTCAGAGACCACCGTGTCCATCCCCGAGACCATTCCTGACACCATGAAGGCCGCTGTCCTGCGGGACCACGAGGTCGGCCTGCAGATTGAGACCCTGCTCACGCCCCGACCCAAGAGCGGCGAGGTCCTCATCAAGGTGGCCGCCTGCGGGCTGTGCCACTCCGACCTCCACGTCATCGGTGGCGCCATCGCCTTCCCGCTGCCAGCGGTGCTCGGCCACGAGGTCTCCGGCACCATCGTGGAGCTCGGCCCCGGCAACGAGCACACCGGCCTGACGATCGGGCAGAAGGTGGCCGGCGGTTTCCTCATGCCCTGCGGCCAGTGTGACGCCTGCGCCTCGGGGCGTGACGAGCTGTGCGGCCCCTTCTTCGACCTCAACCGCCTCAAGGGCGTCTTCTACGACGGCACCACCCGCCTGGCCACCCCCGACGGCGAGCCGGTGGCCATGTACTCCATGGGTGGCCTGGCCGAGTACGCGGTCGTTCCCTCCACCGCGGTGGCCCCCGTGCCGGACACCATCGACATGGTGCCGGCCGCCATCCTGGGCTGCGCCGCCATGACCGGTTATGGGGCCGTGCGCCGCGGCGCCGACCTGCGCTACGGGGAGACCGTCGCCGTGGTCGCCACCGGCGGCGTGGGCACCAATATCGTCCAGATCGCCCGGGCCTTCGGCGCCAGTCAGGTCATCGCCATCGACGTTGATGACGAGAAGCTGGCCCCCATGCTCGACTACGGGGCTACGGCCGTGGTCAACTCCGTTACCCAGGACGCCCGTGAGGAGGTCTTCCGGCTTACCGGCGGCAAGGGAGTTGACGTCTCCTTCGAGGCCCTGGGCATCCCCGCCACGTGGACCACTGCCCTGGATGTCCTGTCCGATGGTGGTCGCATGGTGCCGATCGGCCTGGGGGCCGGCGTGCAGACCGCCGGGGTGGAGATCAACCGCACCGTGCGCCGCTCGCAGTCGATCCTCGGCTCCTACGGGGCGCGCACCCGCCAGGACCTGCCGGCTGTCGTCGACCTGGCCGACAAGGGTGTCATCAACTACCGCGATGTCGTCTCGCGCCGTCTACCGCTGGAGGAGGCCGGCGCCGGCTACACCGCGCTGCGCAACCGCGAGATCCAGGGGCGCGCCGTCGTCGACATGTCGCTGTGA","MSYGGGVAARVHSAARRRRHLTERHLSMTSNEAVQASETTVSIPETIPDTMKAAVLRDHEVGLQIETLLTPRPKSGEVLIKVAACGLCHSDLHVIGGAIAFPLPAVLGHEVSGTIVELGPGNEHTGLTIGQKVAGGFLMPCGQCDACASGRDELCGPFFDLNRLKGVFYDGTTRLATPDGEPVAMYSMGGLAEYAVVPSTAVAPVPDTIDMVPAAILGCAAMTGYGAVRRGADLRYGETVAVVATGGVGTNIVQIARAFGASQVIAIDVDDEKLAPMLDYGATAVVNSVTQDAREEVFRLTGGKGVDVSFEALGIPATWTTALDVLSDGGRMVPIGLGAGVQTAGVEINRTVRRSQSILGSYGARTRQDLPAVVDLADKGVINYRDVVSRRLPLEEAGAGYTALRNREIQGRAVVDMSL$","Zinc-containing alcohol dehydrogenase","Cytoplasm","alcohol dehydrogenase-like protein","alcohol dehydrogenase / formaldehyde dehydrogenase (glutathione) ","Alcohol dehydrogenase, zinc-binding domain protein","","Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Taneja B., Mande S.C. Conserved structural features and sequence patterns in the GroES fold family. Protein Eng. 1999. 12(10):815-818. PMID: 10556240","","","

InterPro
IPR002085
Family

Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695	$\"[63-137]T$ $\"[186-417]T$	ALCOHOL DEHYDROGENASE RELATED

InterPro
IPR013149
Domain

Alcohol dehydrogenase, zinc-binding
PF00107	$\"[236-379]T$	ADH_zinc_N

InterPro
IPR013154
Domain

Alcohol dehydrogenase GroES-like
PF08240	$\"[75-205]T$	ADH_N

noIPR
unintegrated

unintegrated
G3DSA:3.90.180.10	$\"[45-268]T$	no description
PTHR11695:SF38	$\"[63-137]T$ $\"[186-417]T$	ZINC-TYPE ALCOHOL DEHYDROGENASE-RELATED

","BeTs to 6 clades of COG1062COG name: Zn-dependent alcohol dehydrogenases, class IIIFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1062 is ------y---r-bcef-h-n-j----Number of proteins in this genome belonging to this COG is 1","***** IPB002328 (Zinc-containing alcohol dehydrogenase) with a combined E-value of 2.9e-44. IPB002328A 62-93 IPB002328B 104-131 IPB002328C 141-155 IPB002328D 189-227***** IPB011597 (GroES-related) with a combined E-value of 5e-44. IPB011597A 74-101 IPB011597B 104-131 IPB011597C 188-225 IPB011597D 237-281 IPB011597E 305-337***** IPB002364 (Quinone oxidoreductase/zeta-crystallin) with a combined E-value of 1.1e-16. IPB002364B 103-123 IPB002364C 189-216 IPB002364D 234-257","Residues 44-159 are 45% similar to a (ALCOHOL OXIDOREDUCTASE DEHYDROGENASE ZINC-CONTAINING) protein domain (PDA026Q7) which is seen in Q7UR69_RHOBA.Residues 51-97 are 76% similar to a (OXIDOREDUCTASE ZINC METAL-BINDING DEHYDROGENASE ALCOHOL NAD QUINONE PROBABLE CLASS ZINC-BINDING) protein domain (PD015380) which is seen in Q97VV5_SULSO.Residues 101-155 are 63% similar to a (OXIDOREDUCTASE ZINC METAL-BINDING DEHYDROGENASE ALCOHOL NAD PROBABLE FAMILY CLASS MULTIGENE) protein domain (PD304143) which is seen in Q9FFQ2_ARATH.Residues 253-314 are 64% similar to a (OXIDOREDUCTASE ZINC METAL-BINDING DEHYDROGENASE ALCOHOL NAD QUINONE TRANSFERASE SYNTHASE PROBABLE) protein domain (PD000104) which is seen in Q9HWM8_PSEAE.Residues 300-376 are similar to a (OXIDOREDUCTASE ZINC METAL-BINDING DEHYDROGENASE ALCOHOL SORBITOL 3-DEHYDROGENASE NAD L-THREONINE ZINC-BINDING) protein domain (PD583481) which is seen in Q9FFQ2_ARATH.","","-46% similar to PDB:1ADB CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES (E_value = 4.0E_31);-46% similar to PDB:1ADC CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES (E_value = 4.0E_31);-46% similar to PDB:1ADF CRYSTALLOGRAPHIC STUDIES OF TWO ALCOHOL DEHYDROGENASE-BOUND ANALOGS OF THIAZOLE-4-CARBOXAMIDE ADENINE DINUCLEOTIDE (TAD), THE ACTIVE ANABOLITE OF THE ANTITUMOR AGENT TIAZOFURIN (E_value = 4.0E_31);-46% similar to PDB:1ADG CRYSTALLOGRAPHIC STUDIES OF TWO ALCOHOL DEHYDROGENASE-BOUND ANALOGS OF THIAZOLE-4-CARBOXAMIDE ADENINE DINUCLEOTIDE (TAD), THE ACTIVE ANABOLITE OF THE ANTITUMOR AGENT TIAZOFURIN (E_value = 4.0E_31);-46% similar to PDB:1AXG CRYSTAL STRUCTURE OF THE VAL203->ALA MUTANT OF LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH COFACTOR NAD AND INHIBITOR TRIFLUOROETHANOL SOLVED TO 2.5 ANGSTROM RESOLUTION (E_value = 4.0E_31);","Residues 75 to 205 (E_value = 7.4e-37) place ANA_0130 in the ADH_N family which is described as Alcohol dehydrogenase GroES-like domain.Residues 236 to 379 (E_value = 5.7e-37) place ANA_0130 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase.","","dehydrogenase-like protein (adh)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0131","148281","147574","708","11.83","34.82","27316","GTGCAGGGACGCACGACTCATGGTCAGGCGGACCTGCTCTACACACACCGAGAGGAACACTCACATGACCGCCACCATCACCGAGCACCCCACCCAGACCGTCGAGACCACCGCTGCCGCCACCGCCACCCAGGCGACCACCGGCACGCAGACCGACGCCAACCGCCTCACCTTCGCCGTCGCCATGATCGCCGTCATGTTCGCCGTCATGGTCATGTCGGTCGTCGGCGCCGTCACCGGCATCCCGACCCTCATGTTCGCCTCCTCCGTCCTGGCCGCGATCACCATGGGCGTGGGCATCTACACCGGCATCAACCTCCTCGAGGCCCGCTGAGCGTAGACGACTCCAACGAGCTCGCTAGAGCTCCGCCGGATCCGGACCACGCATCACAAGCAACGCAGGCCCCGGACCCAGCCCGACAAGGGCGCAGAAACAACGAGGCTGCGCGGCCAAGGAAGCCCGCGCAGCCATGGCAAACCCGAGGGGCACCACACAAGCGGCGCCCCTCTTCTCATATCCCCCTCCCCACAACGCAGACGGAACCAGGCCTCGCGCGACTCCGCTCACTGCTGGCGCACCCCTCCCCGCAAAGCGGACACCACCCTCCCGAACGGCACAGGAACGGCCGAGATGTCCATATCGGACACAAAGGCGAACTTCGAGCTCACGCCACCGATAAGAAACCGCATGATTCCGCGGTTCCATGA","VQGRTTHGQADLLYTHREEHSHDRHHHRAPHPDRRDHRCRHRHPGDHRHADRRQPPHLRRRHDRRHVRRHGHVGRRRRHRHPDPHVRLLRPGRDHHGRGHLHRHQPPRGPLSVDDSNELARAPPDPDHASQATQAPDPARQGRRNNEAARPRKPAQPWQTRGAPHKRRPSSHIPLPTTQTEPGLARLRSLLAHPSPQSGHHPPERHRNGRDVHIGHKGELRAHATDKKPHDSAVP$","Hypothetical protein","Cytoplasm, Extracellular","similar to splicing factor/activator protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","***** IPB013957 (Protein of unknown function DUF1777) with a combined E-value of 2.5e-06. IPB013957A 23-66 IPB013957A 47-90 IPB013957A 27-70 IPB013957A 33-76 IPB013957A 57-100 IPB013957A 31-74 IPB013957A 35-78 IPB013957A 59-102 IPB013957A 37-80 IPB013957A 62-105 IPB013957A 51-94 IPB013957A 17-60 IPB013957A 19-62 IPB013957A 34-77 IPB013957A 39-82 IPB013957A 29-72 IPB013957A 36-79 IPB013957A 42-85 IPB013957A 21-64 IPB013957A 50-93 IPB013957A 25-68 IPB013957A 75-118 IPB013957A 46-89 IPB013957A 43-86 IPB013957A 64-107 IPB013957A 48-91 IPB013957A 53-96 IPB013957A 13-56 IPB013957A 63-106 IPB013957A 15-58 IPB013957A 28-71 IPB013957A 41-84 IPB013957A 66-109 IPB013957A 11-54 IPB013957A 7-50 IPB013957A 26-69 IPB013957A 44-87 IPB013957A 55-98","No significant hits to the ProDom database.","","-42% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = );-42% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = );-42% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = );-42% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = );-42% similar to PDB:2J01 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 2 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE I. (E_value = );","No significant hits to the Pfam 21.0 database.","","to splicing factor-activator protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0132","148583","150253","1671","5.32","-18.54","59539","ATGGCGGGCAACGCCGAGAGATGGCGTCATCGCCGGCCGGCAGGGCGGAAGGCGGCCGGTTGCCGCCCCGGCTATTCTGTTCCGGTGACGACCAGCCAGACTTCTTCCAGCGCCGTCGGCCCCGTCCTCGTGGTGGACTTCGGCGCCCAGTACGCCCAGCTCATCGCCCGCCGCGTGCGCGAGGCCGGTGTCTACTCCGAGATCGTGCCCCACTCCATGGATGCCGCCGCCATGCTGGACAAGCGGCCTTCGGCCATCATCCTCTCCGGCGGCCCCTCCTCGGTCTACGCCGACGGCGCCCCCTCCGTTGACCCGGCCCTCTTCGACGCTGGAGTGCCGGTCCTGGGCATCTGCTACGGATTCCAGGCCATGGCCCAGGCCCTGGGCGGAACGGTCGGGCGCACCGGCACCCGCGAGTACGGGCACACCCCCGCCCGCGTGGCTGAGGGCTCCTGCCTGTTCGACGGCACCCCGGACGACCAGGTGGTGTGGATGAGTCACGGCGACGCGGTCCAAGCCGCCCCCGAGGGCTTCACCGTCACCGCCTCCACCTCCCAGACGCCGGTGGCAGCCTTCGAGAACCCGGGCCGCCGGCTCTACGGATTGCAGTGGCACCCCGAGGTCCTCCACTCCGAGCACGGGCAGGCCGCCCTGGTCAACTTCCTGCACAAGGAGGCGGGGCTACCGGCCACCTGGACGCCGGACAACATCATCGACGAGCAGGTGGCCCGCATCCGCGAGCAGGTGGGCGACGCTCACGTCATCTGCGGCCTGAGCGGGGGAGTGGACTCCTCCGTGGCCGCTGCCCTCGTCCACCGCGCCATCGGCGACCAGCTCACCTGCATCTTCGTCGATCATGGCCTGCTGCGCGCCGGCGAGCGCGAGCAGGTCGAGCACGACTACGCCGAAGGCATGGGCATCCGCGTCATCACGGTCGACGAGACCGAGCGCTTCCTGAGTGCCCTGGCCGGCGTCACCGAGCCGGAGGCCAAGCGCAAGATCATCGGCCGGGAGTTCATCCGCTCCTTCGAGGCTGCCCAGCGCCGGGTCATCGAGGCCGTGGGCGCCGAGGGCGGTGAGATCCGCTTCCTGGTCCAGGGGACCCTGTATCCCGACGTCGTCGAGTCCGGCGGGGGAGAGGGCGCCGCCAACATCAAGAGCCACCACAACGTGGGCGGCCTGCCAGAAGACCTCGACTTCGAGCTCATCGAGCCGCTGCGCGAGCTGTTCAAGGACGAGGTGCGCGCCATCGGCCGCGAGCTGGGCGTGCCGGAGAAGATCGTCGCCCGCCAGCCCTTCCCTGGGCCGGGGCTGGGCATTCGTGTCATTGGCGAGGTGACGGCCGAGAACCTGCGTGTGCTGCGGGCCGCCGACGCCATCGCCCGCGAGGAGCTCACCGCCGCTGGGCTCGACGACGAGATCTGGCAGTGCCCGGTGGTGCTGCTGGCCGACGTGCGCTCCGTGGGGGTGCAGGGTGATGGGCGCACCTACGGTCACCCCATTGTTCTGCGGCCGGTCAGCAGCGAGGACGCCATGACCGCGGACTGGACCCGCCTGCCCTACGATGTCCTGGCACGCATCTCCAACCGGATCACCAACTCCGTGCCGGAGGTCAACCGGGTGGTGCTCGACTGCACGAGCAAGCCCCCGGGCACCATCGAGTGGGAGTGA","MAGNAERWRHRRPAGRKAAGCRPGYSVPVTTSQTSSSAVGPVLVVDFGAQYAQLIARRVREAGVYSEIVPHSMDAAAMLDKRPSAIILSGGPSSVYADGAPSVDPALFDAGVPVLGICYGFQAMAQALGGTVGRTGTREYGHTPARVAEGSCLFDGTPDDQVVWMSHGDAVQAAPEGFTVTASTSQTPVAAFENPGRRLYGLQWHPEVLHSEHGQAALVNFLHKEAGLPATWTPDNIIDEQVARIREQVGDAHVICGLSGGVDSSVAAALVHRAIGDQLTCIFVDHGLLRAGEREQVEHDYAEGMGIRVITVDETERFLSALAGVTEPEAKRKIIGREFIRSFEAAQRRVIEAVGAEGGEIRFLVQGTLYPDVVESGGGEGAANIKSHHNVGGLPEDLDFELIEPLRELFKDEVRAIGRELGVPEKIVARQPFPGPGLGIRVIGEVTAENLRVLRAADAIAREELTAAGLDDEIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWTRLPYDVLARISNRITNSVPEVNRVVLDCTSKPPGTIEWE$","GMP synthase/glutamine amidotransferase","Cytoplasm","GMP synthase [glutamine-hydrolyzing](Glutamineamidotransferase) (GMP synthetase)","GMP synthase ","GMP synthase, large subunit","","Weng M.L., Zalkin H. Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. J. Bacteriol. 1987. 169(7):3023-3028. PMID: 3298209Nyunoya H., Lusty C.J. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. J. Biol. Chem. 1984. 259(15):9790-9798. PMID: 6086650","","","

InterPro
IPR000991
Domain

Glutamine amidotransferase class-I
PF00117	$\"[43-225]T$	GATase

InterPro
IPR001317
Domain

Carbamoyl-phosphate synthase, GATase region
PR00099	$\"[42-56]T$ $\"[83-97]T$ $\"[113-129]T$	CPSGATASE

InterPro
IPR001674
Domain

GMP synthase, C-terminal
PF00958	$\"[462-555]T$	GMP_synt_C
TIGR00884	$\"[236-556]T$	guaA_Cterm: GMP synthase, C-terminal domain

InterPro
IPR004506
Family

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
PF03054	$\"[252-274]T$	tRNA_Me_trans

InterPro
IPR004739
Domain

GMP synthase, N-terminal
TIGR00888	$\"[42-229]T$	guaA_Nterm: GMP synthase, N-terminal domain

InterPro
IPR006220
Domain

Anthranilate synthase component II/delta crystallin
PR00097	$\"[86-95]T$ $\"[113-124]T$ $\"[201-214]T$	ANTSNTHASEII

InterPro
IPR011702
Domain

Glutamine amidotransferase superfamily
PR00096	$\"[86-95]T$ $\"[113-124]T$ $\"[201-214]T$	GATASE

InterPro
IPR012998
Active_site

Glutamine amidotransferase, class I, active site
PS00442	$\"[113-124]T$	GATASE_TYPE_I

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[231-430]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.300.10	$\"[447-556]T$	no description
G3DSA:3.40.50.880	$\"[42-230]T$	no description
PTHR11922	$\"[41-556]T$	GMP SYNTHASE-RELATED
PTHR11922:SF2	$\"[41-556]T$	GMP SYNTHASE

","BeTs to 24 clades of COG0519COG name: GMP synthase - PP-ATPase domainFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0519 is aompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB001674 (GMP synthase, C terminal) with a combined E-value of 1.7e-233. IPB001674A 42-68 IPB001674B 107-122 IPB001674C 160-195 IPB001674D 200-219 IPB001674E 245-293 IPB001674F 312-347 IPB001674G 363-376 IPB001674H 390-444 IPB001674I 477-518 IPB001674J 530-556***** IPB006220 (Anthranilate synthase component II signature) with a combined E-value of 2.2e-27. IPB006220A 42-56 IPB006220B 86-95 IPB006220C 113-124 IPB006220E 158-170 IPB006220F 201-214***** IPB001317 (Carbamoyl-phosphate synthase protein GATase domain signature) with a combined E-value of 4.9e-25. IPB001317A 42-56 IPB001317B 83-97 IPB001317C 113-129 IPB001317D 160-177***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 3.2e-13. IPB000991A 113-130 IPB000991B 198-208***** IPB004506 (tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase) with a combined E-value of 7.8e-08. IPB004506A 253-283***** IPB011697 (Peptidase C26) with a combined E-value of 5.1e-07. IPB011697B 111-120 IPB011697C 196-209***** IPB002474 (Carbamoyl-phosphate synthase, small chain) with a combined E-value of 2.8e-06. IPB002474D 84-95 IPB002474E 113-146","Residues 59-130 are 88% similar to a (GLUTAMINE SYNTHASE AMIDOTRANSFERASE BIOSYNTHESIS LIGASE GMP SYNTHETASE CTP CHAIN COMPONENT) protein domain (PD000306) which is seen in Q6A6X1_PROAC.Residues 138-184 are 83% similar to a (GMP GLUTAMINE AMIDOTRANSFERASE BIOSYNTHESIS SYNTHASE LIGASE GLUTAMINE-HYDROLYZING PURINE SYNTHETASE ATP-BINDING) protein domain (PD349562) which is seen in GUAA_STRAW.Residues 191-227 are 83% similar to a (GLUTAMINE AMIDOTRANSFERASE GMP SYNTHASE BIOSYNTHESIS COMPONENT II ANTHRANILATE LIGASE SYNTHETASE) protein domain (PD095787) which is seen in Q6AD51_BBBBB.Residues 254-312 are 66% similar to a (GMP BIOSYNTHESIS SYNTHASE SYNTHETASE LIGASE ATP-BINDING GLUTAMINE-HYDROLYZING PURINE AMIDOTRANSFERASE GLUTAMINE) protein domain (PD780029) which is seen in Q6CU71_EEEEE.Residues 255-312 are 86% similar to a (LIGASE BIOSYNTHESIS GMP ATP-BINDING SYNTHASE GLUTAMINE AMIDOTRANSFERASE TRNA SYNTHETASE METHYLTRANSFERASE) protein domain (PD034321) which is seen in GUAA_CORGL.Residues 288-339 are 73% similar to a (GMP AMIDOTRANSFERASE GLUTAMINE BIOSYNTHESIS SYNTHETASE ATP-BINDING GLUTAMINE-HYDROLYZING PURINE SYNTHASE LIGASE) protein domain (PDA1C488) which is seen in GUA1_BACTN.Residues 349-442 are 91% similar to a (GMP BIOSYNTHESIS GLUTAMINE AMIDOTRANSFERASE SYNTHASE SYNTHETASE LIGASE GLUTAMINE-HYDROLYZING ATP-BINDING PURINE) protein domain (PD003340) which is seen in GUAA_BIFLO.Residues 443-556 are similar to a (GMP BIOSYNTHESIS GLUTAMINE AMIDOTRANSFERASE SYNTHASE SYNTHETASE LIGASE GLUTAMINE-HYDROLYZING PURINE ATP-BINDING) protein domain (PD036620) which is seen in GUAA_CORDI.","","-64% similar to PDB:1GPM ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE (E_value = 5.4E_143);-69% similar to PDB:2DPL Crystal Structure of the GMP synthase from Pyrococcus horikoshii OT3 (E_value = 3.9E_85);-51% similar to PDB:2D7J Crystal Structure Analysis of Glutamine Amidotransferase from Pyrococcus horikoshii OT3 (E_value = 1.4E_26);-51% similar to PDB:1WL8 Crystal structure of PH1346 protein from Pyrococcus horikoshii (E_value = 1.9E_26);-54% similar to PDB:2A9V Crystal structure of (np_394403.1) from THERMOPLASMA ACIDOPHILUM at 2.45 A resolution (E_value = 2.5E_23);","Residues 43 to 225 (E_value = 6.8e-56) place ANA_0132 in the GATase family which is described as Glutamine amidotransferase class-I.Residues 237 to 278 (E_value = 5.9e-05) place ANA_0132 in the NAD_synthase family which is described as NAD synthase.Residues 252 to 274 (E_value = 6.2e-10) place ANA_0132 in the tRNA_Me_trans family which is described as tRNA methyl transferase.Residues 253 to 381 (E_value = 0.0037) place ANA_0132 in the ExsB family which is described as ExsB.Residues 462 to 555 (E_value = 1.8e-55) place ANA_0132 in the GMP_synt_C family which is described as GMP synthase C terminal domain.","","synthase [glutamine-hydrolyzing] (Glutamineamidotransferase) (GMP synthetase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0134","150977","151843","867","4.62","-9.08","29605","ATGTCGTACCCTCCTCAGTCCGTCCCTCCCCAGCAGTACCCGCCTCAAGATCAGGTTCCTGTGCCCATTCAGCAAGCGCCTGCGCCAGTAAAGAAGGGGCGCAACACCGTGGGCATCGTTGCTCTGGTGATGGCGATCATCGGGTTCATCTTCGCCTGCGTCCCTGGCGCGCTCATCGTCGGCTGGATTCTGCTGCCAATCTCCTTCATCGTCGGTTTGGTGGGTCTCTTCCGGAAGGGGGAGGTGATCTGGCCTGCAATCACCGCGGTGATCGTCTCGGTTGTCGGAACTGTCGTCGGCGTCTTCGTCTTCCTTGTGGTTGTGAGCAACGCTGTCGATGAGGCGATGTCCTCTACGAGCGCGGTCTCTGCGGCGCCGGCTCCCGATGGGGCGTCGTCGAACTCAGGAGGATCGAGTGCTGCGGACTCCGCACAGGGAAAGACTCGGGAGAACCCCTACCCGCTCCGTACCGAGATCTCCAGCAAGGAATGGAAAGTGGTCATCAACTCGGTCACTTTCAAGGCTGACGATCAGGTCGCCGCGGCCAACCAGCTCAATGACCCTCCCGCTGAAGGGAAGGAATACGTTCTCATCAACTACACCGCCACCTACATCGGCAACGACCCAAGCGGAGACACACCTGCTTTTGTGCTGGTCGACTTCGTGACGGTGGATGGTGTCACCGTCGATGGGGCCGACTCCCTCGCCGTCGCCCCGGATGCCATCGATACTCTGACCACGCTGTACAACGGGGCCAGCGTCTCAGGCAACGTTGTGCGCGCGGTGCCGTCGGCCAACGCCCAGGACGGGGTTCTTGCGGTGACCCCCGGTCTTCTCGCCGACAAGGTCTTCGTCGCGGTGAAGTGA","MSYPPQSVPPQQYPPQDQVPVPIQQAPAPVKKGRNTVGIVALVMAIIGFIFACVPGALIVGWILLPISFIVGLVGLFRKGEVIWPAITAVIVSVVGTVVGVFVFLVVVSNAVDEAMSSTSAVSAAPAPDGASSNSGGSSAADSAQGKTRENPYPLRTEISSKEWKVVINSVTFKADDQVAAANQLNDPPAEGKEYVLINYTATYIGNDPSGDTPAFVLVDFVTVDGVTVDGADSLAVAPDAIDTLTTLYNGASVSGNVVRAVPSANAQDGVLAVTPGLLADKVFVAVK$","Hypothetical protein","Membrane, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Kota J., Ljungdahl P.O. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J. Cell Biol. 2005. 168(1):79-88. PMID: 15623581","","","

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[31-194]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[36-56]?$ $\"[58-78]?$ $\"[84-106]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[194-214]?$ $\"[235-253]?$ $\"[259-293]?$ $\"[302-322]?$ $\"[365-385]?$	transmembrane_regions

","BeTs to 6 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","No significant hits to the Blocks database.","Residues 282-350 are 57% similar to a () protein domain (PD851703) which is seen in Q8G5V3_BIFLO.Residues 282-350 are 57% similar to a () protein domain (PD851703) which is seen in Q8G5V3_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0136","154256","153114","1143","7.69","2.63","40850","ATGTTGACCGTCTTCCTGTATCAAGTACTCAGGCTCTTGCGAGACCGGGTCCTGCTCGTGTGGACGCTCGGCTTCCCCGTCGTCCTGTCCCTCATCTTCATGGCGATGTTCTCCAACCTGGACAAGGTCTACGAGGCCACCCCCATGAGCTTCGGCGTCGTCCAGGACGAGGCCTACCGGACCGCTCCGGGGCTGGACGCCGTCGTGGAGCGCATCTCCGCCGACGACGCCGATCATCACCTCATCACGAAGGTCACCCACTCCACGGTCGCGCAGGCCGAGACCGCCGCGAAGCGGGGAGAGACCAACGGGTACCTCGCCGTCGAGGGCAGCGATCCTGTGCTGCACGTGACTCAGCAGGGCAACGAGGCCGAGACGACTCGGGTGCTGCGAGTGGTCATGGACTCCTACCTCCAGAGGCGGGCCGAGTATGTGGCCCTGGCCAAGGCGGGGGCGGCTCCTGAGAAGCTGGCCGCGCTGGAGACCGATCAGGCCTTCACCCGTTCGATCTCGGTGACGCCCTCCCCGGTCAAGCCGCAGACCCCCTACTACTTCGCGCTGCTGGCCTTCGCCTGCGGCATGGGGACGACCGTGGCCATGGTGGCTGTGAAGGGGACTATGGCTGTCTCGCCGGTGGGCGCCCGGCAGACCTTGGCGGGTCTGCCCCGCTGGAAGGTCCTGACGGCCACGCTCGCGGCCTCCTGGGTGTGCGTGTTCGTCTGCCTGCTCCTCGCTTTCGCCTTCATGGCCTCGGTCGTGGGTGTGGACTTCGGGCCCCATGTGCTGCTGTGCCTCGTGGCGATCGGGGTGTGCAGCCTCATGGCGAGCGCGGTGGGCGCCGCCCTGGGGACGCTGGCCCGCCTGGAGATCGGGATGATCTCCGGCTTCACATCCCTGCTGTCACTGTTCACCGGCCTGTACGGGCCCGCATCCCAGTCCCTGGCCAGCTCCATCGAGCAGCACGCACCGCTGCTGGCGCAGGCCAATCCCCTGTGGCAGACGGCCCGCTGCTTCTACGGGCTCCTGTACTACGACTCTCTGGCGCCCTTCGCCCGCAGCTGCGCAGTCCTGCTGGGCATGACGTGCCTGTTCCTGACCATCGCCCTGATCCGCGCCAGGAGGATGACCCATGAGCACCTTTAA","MLTVFLYQVLRLLRDRVLLVWTLGFPVVLSLIFMAMFSNLDKVYEATPMSFGVVQDEAYRTAPGLDAVVERISADDADHHLITKVTHSTVAQAETAAKRGETNGYLAVEGSDPVLHVTQQGNEAETTRVLRVVMDSYLQRRAEYVALAKAGAAPEKLAALETDQAFTRSISVTPSPVKPQTPYYFALLAFACGMGTTVAMVAVKGTMAVSPVGARQTLAGLPRWKVLTATLAASWVCVFVCLLLAFAFMASVVGVDFGPHVLLCLVAIGVCSLMASAVGAALGTLARLEIGMISGFTSLLSLFTGLYGPASQSLASSIEQHAPLLAQANPLWQTARCFYGLLYYDSLAPFARSCAVLLGMTCLFLTIALIRARRMTHEHL$","ABC-type multidrug transport system, permease component","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[20-40]?$ $\"[183-203]?$ $\"[231-251]?$ $\"[261-281]?$ $\"[290-310]?$ $\"[350-370]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-380 are 46% similar to a () protein domain (PD849642) which is seen in Q8G5V2_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0137","155241","154258","984","5.24","-9.97","35439","ATGGACGGCGAGGATGAGAGCCACGAGGCGGGCCTGGCGGTGGAGGTCGACTCCCTGGTCAAGCGCTATGGGGAGCTGGTCGCGGTGGACGGACTGTCTCTGACGATCCCGCGCGGTCAGGTGCTGGGGCTGCTCGGCCCCAACGGCTCGGGCAAGACGACGACGATCAGCTGCATCCTTCAGCTACTCACCTACGACAAGGGCTCGATCCGCGTCTTCGGTGAGCCGATGACGCCCACCTCCTACGGTCTCAAGCGTCGCATCGGCGTGGTGCCTCAGGATGTCGCCGTCTTCGATGAGCTCACGGTGGCGGAGAACGTCAACGCCTTCTGCGCCCTCTACGTGCGCGATCGCGCCGAGAGGCGCCGCCTGGTGGCCGAGGCGATCGCCTTCGTCGGTCTGGAGAAGTTCGTGAGGTTCAAGCCCAAGAAGCTCTCCGGCGGCCTGCTGCGCCGCCTCAACATCGCCTGCGGCATCGCCCACGGCCCCGACCTCATCTTCCTCGATGAGCCCACAGTCGCCGTCGACCCGCAGAGCCGGGGCGCCATTCTCGAGGGCATCAAGCGTCTCAACGAGCGCGGTGCCACCGTCATCTACACGAGCCACTACATGGAGGAGGTGGAGCAGCTGTGCGACCGGATCGTCATTATGGACCGCGGCCGTCAGGTGGCCTCCGGTACCTCCGACGAGCTCAAGGCCATGATCGGCACCGGTGAGCGCATCCGGGTGGAGGTCGTCGACCCCGCCCCGCTGGGCGAGGAGGCCCTGGAGGGCCTGCGCCGCCTGGAGCATGTGCGCACGGCCGCCTACCTGGACGGTGAGGTGCTCATCGAGTGCTCCCCCGGGGCTCACAACCTCACCGATGTCATGAGGGCGCTGGATGCCGCGGGGGCGACCTGCGGCCGGGTGACCTCCGAGCCCCCGACCCTCAACGACGTCTTCCTGGAGATCACCGGGCGGGCCCTGCGAGACGAGGCGGCCTGA","MDGEDESHEAGLAVEVDSLVKRYGELVAVDGLSLTIPRGQVLGLLGPNGSGKTTTISCILQLLTYDKGSIRVFGEPMTPTSYGLKRRIGVVPQDVAVFDELTVAENVNAFCALYVRDRAERRRLVAEAIAFVGLEKFVRFKPKKLSGGLLRRLNIACGIAHGPDLIFLDEPTVAVDPQSRGAILEGIKRLNERGATVIYTSHYMEEVEQLCDRIVIMDRGRQVASGTSDELKAMIGTGERIRVEVVDPAPLGEEALEGLRRLEHVRTAAYLDGEVLIECSPGAHNLTDVMRALDAAGATCGRVTSEPPTLNDVFLEITGRALRDEAA$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Membrane","ABC-type multidrug transport system, ATP-asecompoment CAC0241","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[145-187]T$	Q8G5V1_BIFLO_Q8G5V1;
PF00005	$\"[39-220]T$	ABC_tran
PS50893	$\"[14-244]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[38-221]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[8-231]T$	no description
PTHR19222	$\"[14-254]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[14-254]T$	ABC TRANSPORTER

","BeTs to 14 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 8.1e-28. IPB013563A 28-62 IPB013563C 142-169 IPB013563D 196-248***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.4e-20. IPB005074C 28-75 IPB005074D 133-176***** IPB005116 (TOBE domain) with a combined E-value of 1.8e-17. IPB005116A 46-62 IPB005116B 86-103 IPB005116C 145-158 IPB005116D 165-184 IPB005116E 198-211***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 5.8e-11. IPB010509B 39-64 IPB010509D 140-184","Residues 1-231 are 44% similar to a (GLP_38_64512_71054 ATP-BINDING) protein domain (PDA0H565) which is seen in Q7R1F8_EEEEE.Residues 5-88 are 59% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 8-77 are 60% similar to a (MEMBRANE ATP-BINDING) protein domain (PDA0I3N6) which is seen in Q6NK67_CORDI.Residues 9-136 are 53% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 9-166 are 50% similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 11-236 are 47% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 12-246 are 42% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 14-231 are 46% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 14-242 are 47% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 14-91 are 57% similar to a (BVIB ATP-BINDING ATP BINDING) protein domain (PD195204) which is seen in Q9ZGP8_BUTFI.Residues 14-220 are 43% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD756741) which is seen in Q8A5R4_BACTN.Residues 14-113 are 52% similar to a (ABC-TYPE ATP-BINDING) protein domain (PD253636) which is seen in Q9HQA8_HALN1.Residues 19-243 are 43% similar to a (C24F3.5 ATP-BINDING) protein domain (PD574736) which is seen in Q21213_CAEEL.Residues 21-237 are 44% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 22-217 are 50% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 23-114 are 52% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 23-114 are 56% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187K3) which is seen in Q897D7_CLOTE.Residues 25-224 are 46% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 25-178 are 44% similar to a (ATP-BINDING OPPD OLIGOPEPTIDE) protein domain (PDA11396) which is seen in Q7P513_BBBBB.Residues 25-221 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 27-179 are 48% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 27-202 are 46% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 28-144 are 50% similar to a (GLP_574_64573_57809 ATP-BINDING) protein domain (PD990707) which is seen in Q7R6B9_EEEEE.Residues 28-112 are 55% similar to a (ATP-BINDING PROTEIN CYDCD) protein domain (PDA1B3E1) which is seen in Q6ABD5_PROAC.Residues 29-231 are 47% similar to a (ATP-BINDING SYSTEM ABC A1A2) protein domain (PD459661) which is seen in Q97BE5_THEVO.Residues 29-221 are 40% similar to a (ATP-BINDING CG1494-PA) protein domain (PD310846) which is seen in Q9VRG3_DROME.Residues 32-105 are 59% similar to a (ATP-BINDING PHOSPHONATE ABC-TYPE PROTEIN) protein domain (PDA0J3O0) which is seen in Q6MPJ3_BDEBA.Residues 34-78 are 86% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8G5V1_BIFLO.Residues 44-220 are 47% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD738131) which is seen in Q830L1_ENTFA.Residues 79-144 are 80% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER PROBABLE ATP BINDING) protein domain (PD931522) which is seen in Q8G5V1_BIFLO.Residues 92-216 are 49% similar to a (AMV130) protein domain (PD706071) which is seen in Q9EMR9_AMEPV.Residues 93-231 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 94-244 are 47% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 125-223 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 132-202 are 54% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in YRBF_HAEIN.Residues 133-232 are 58% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 133-224 are 48% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 133-230 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J201) which is seen in Q73M59_TREDE.Residues 144-235 are 64% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 145-187 are 93% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q8G5V1_BIFLO.Residues 268-322 are 70% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER RESISTANCE ABC-TYPE MULTIDRUG COMPONENT DAUNORUBICIN SYSTEM) protein domain (PD694176) which is seen in Q8G5V1_BIFLO.","","-54% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 1.7E_31);-53% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 7.5E_27);-54% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 5.3E_25);-54% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 5.3E_25);-52% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 2.0E_24);","Residues 39 to 220 (E_value = 6.1e-59) place ANA_0137 in the ABC_tran family which is described as ABC transporter.","","multidrug transport system, ATP-ase compoment CAC0241 (drra)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0138","155459","156571","1113","7.07","0.22","38978","GTGCTGCTGTGCGGTTGCCTCCTGCTGGTCCTGCTCGTGGGGCAGGTGAAGACGGCCGCCGTGATCTGGCTGATCGCGGCCGTGACCATCGCCGGCCTGAGTATGAGCACCGACCAGCGACAGTGGGGGATCGCCGCGCCGGCCGCCTACCTCCTGGTGGGAGCCCTCTCAACGGACTCCGTGACCGGGGCGCCGCTGGTCGTCTACGTCCTGGCCCGTCTCGGTGCGCTCACGACCCGGCGTGCGCGAATGACGGCGGTAGCCGCCTGCATTCCCTTCGTGGCCGCCGTTGCCGCCCGGGTTCGGGACACTCCCGTGCTGGCCCTCGCTCTGGCGGTCTGCGCTCTCGCGGCCCTCCTCGCGCTGCGCACCGTCCAGGAGGAGGCGGCGCGAAGGAGCCTGCACGTGGTGCGCGACGACCTGCGTGAGAAGGTCCTCACCCTTCAGGACACGAACGCCCAGCTGCTCCAGGCCCAGGACTACGAGCTGCGCGCCGCCGCCCTGGCCGAACGCACCCGCATCGCCCGCGAGATCCACGACGGCGTCGGCCACCTCCTGACCCGCCTCCTGCTGCAGGTCAAGGCCCTCCAGGTCGTCCACCGCGAGGAGCCCGGCGTCGTCGCCGACCTCACTACCCTGGACGGTGGCCTGGACGAGGCCCTCGACTCCATGCGCCGCTCCGTCCACGCCCTGTCCGACGACGGCGAGGAGCTGGCCACCTCCCTCAACATGCTGGGCTCGCGCTGCGGCATCGACTCCGTGAGCGTCGACTGCTCCACCGAGGCCGAGCTGCCGGCAGTGGTGGCGCGCTGCGTCGTGGCCGTCGTGCGCGAGGCCCTGACCAACGCCGCCCGCCACGGTGGGGCCCGCTCGGCCCGCGTGGCCGTCAACGACTACCCTGCGTTCTGGCAGGTGACCGTTGACAATGACGGCATCGTCCCCGCCGAGGGAGAGCCGGCCGCCGCTGGCCGCGGCGGCTCGGGCCTGGGCCTGCGCTCCATGACGGAGCGGGTCGAGGCCCTGGGTGGCCGGGTGCGCATCACCCCGCGGCCACGGTTCACGGTCTTCGTCACGATCCCCAAGGACGGACAAGGGAAAGAAGGAACATCATGA","VLLCGCLLLVLLVGQVKTAAVIWLIAAVTIAGLSMSTDQRQWGIAAPAAYLLVGALSTDSVTGAPLVVYVLARLGALTTRRARMTAVAACIPFVAAVAARVRDTPVLALALAVCALAALLALRTVQEEAARRSLHVVRDDLREKVLTLQDTNAQLLQAQDYELRAAALAERTRIAREIHDGVGHLLTRLLLQVKALQVVHREEPGVVADLTTLDGGLDEALDSMRRSVHALSDDGEELATSLNMLGSRCGIDSVSVDCSTEAELPAVVARCVVAVVREALTNAARHGGARSARVAVNDYPAFWQVTVDNDGIVPAEGEPAAAGRGGSGLGLRSMTERVEALGGRVRITPRPRFTVFVTIPKDGQGKEGTS$","Two-component system sensor kinase","Membrane, Cytoplasm","histidine kinase sensor of two-component system","histidine kinase sensor of two-component system","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[225-360]T$	no description
PF02518	$\"[267-362]T$	HATPase_c
SM00387	$\"[267-363]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[170-236]T$	HisKA_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide

","BeTs to 5 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 1.5e-18. IPB011712A 169-186 IPB011712B 272-292","Residues 179-243 are 59% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM TRANSFERASE 2.7.3.- SENSORY TRANSDUCTION NITRATE/NITRITE) protein domain (PD288674) which is seen in Q8G5V0_BIFLO.","","-51% similar to PDB:1GVF STRUCTURE OF TAGATOSE-1,6-BISPHOSPHATE ALDOLASE (E_value = );","Residues 170 to 236 (E_value = 1.1e-15) place ANA_0138 in the HisKA_3 family which is described as Histidine kinase.Residues 267 to 362 (E_value = 1.1e-13) place ANA_0138 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","kinase sensor of two-component system","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0139","156568","157248","681","4.72","-11.84","24034","ATGAGGGTCCTCATCGTCGACGACGACGCGCTCGTCGCCCAGTCCCTGTCCACGATCCTGTCGGTCGAGGACGACGTCGAGGTCGTCGGTCTGGGCTGCTCGGGCCCCGAGGCCATCGAGCGCTACCGGGAGCTGACCCCCGACATCCTCCTCATGGACATCCAGATGCCCGGCGGGGACGGGCTCAGTGCGGCCGAGCGGATTCTGGCCGAGGACGCCGGGGCGCGCATCGTCTTCCTCACCACCTTCTCCGACGACGAGTACATCGTGCGAGCCCTCAAGATGGGGGCGCGTGGCTACCTCATCAAGCAGGACGTCGCCCAGGTCGCCCCGGCGCTGCGCTCCGTCATGGCCGGGGTCTGCGTCCTGGAGGGGGAGGTGCTCGAGCGCAGCACCACCATGGGCCTTGGCGGGCGTACCGGAGGGCGGGGACCGACCGAGGAGGGTCCGGGACCGACCGCCAAGGACCTGCGGAGCACGGCTTTTGCGGCCCTGACCGACCGCGAGTACGAGGTCGTCGAGGCCGTGGCCGAGGGACTGGACAACGCCGAGGCCGCGGCGCGGCTGTTCATGAGTGAGGGCACGGTGCGCAACCACATCAGTGCGATCCTGGCCAAGCTCGGCCTGCGTAACCGCACCCAGGTCGCAGTCATGTACTACCGCTCCGCGCAGGCCGGGTGA","MRVLIVDDDALVAQSLSTILSVEDDVEVVGLGCSGPEAIERYRELTPDILLMDIQMPGGDGLSAAERILAEDAGARIVFLTTFSDDEYIVRALKMGARGYLIKQDVAQVAPALRSVMAGVCVLEGEVLERSTTMGLGGRTGGRGPTEEGPGPTAKDLRSTAFAALTDREYEVVEAVAEGLDNAEAAARLFMSEGTVRNHISAILAKLGLRNRTQVAVMYYRSAQAG$","Two-component system response regulator","Cytoplasm","response regulator of two-component system","putative two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[165-218]T$	Q8G5U9_BIFLO_Q8G5U9;
PR00038	$\"[165-179]T$ $\"[179-195]T$ $\"[195-207]T$	HTHLUXR
PF00196	$\"[162-219]T$	GerE
SM00421	$\"[162-219]T$	HTH_LUXR
PS50043	$\"[158-223]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[1-116]T$	Q73RE0_TREDE_Q73RE0;
PF00072	$\"[1-114]T$	Response_reg
SM00448	$\"[1-113]T$	REC
PS50110	$\"[2-103]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[156-225]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[1-103]T$	no description
PTHR23283	$\"[1-121]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF46	$\"[1-121]T$	OSMOLARITY TWO-COMPONENT SYSTEM PROTEIN SLN1

InterPro
IPR007712
Family

Plasmid stabilization system
PF05016	$\"[5-91]T$	Plasmid_stabil

InterPro
IPR012753
Family

Addiction module toxin, RelE/StbE
TIGR02385	$\"[4-91]T$	RelE_StbE: addiction module toxin, RelE/Stb

","BeTs to 5 clades of COG3041COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3041 is --------------e-ghs-u-----Number of proteins in this genome belonging to this COG is 1","***** IPB004386 (Conserved hypothetical protein 53) with a combined E-value of 7.4e-13. IPB004386 45-70","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 91 (E_value = 1e-08) place ANA_0140 in the Plasmid_stabil family which is described as Plasmid stabilisation system protein.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0141","158126","159100","975","4.75","-15.12","34233","ATGCTGCTGTGGAGCGTCATAGATCCTCGAGGCGTGTGGGAGGTGACGTCCTCCTGGCAGTTCCGAAACCCTGAGGCTAATGAGCCGTCCGATAGTGCCTTCGCGGTGCAGCGGTTCTTTGCCTTTATCAGTCTTCTGGTGATTGTGGGTGGTGCATTCTTTTTTGTGTCGGCATCGCACAGGAATGCGAGCGCCCGTGCGACTGATGATGCGAGTGTTCGTGAAGCTGATAGTGCCACTCCTTATGTGTACCCAAACATTTATTCGTCGAGTGATGGTGAGGGTAGTGATGGATATGCTGAGACGACCGTGACTCCGTCTCCGGTTGATCCTTTCCCGTCAGCTTCTACGACTGCCGTGGGATCTGGGGAGCCGGTTGTCCTTTTCAAGCCGGTTCTCGAGGGTGCGGCCGGTGAGCAGAAATCGGACTCCTCGGTCAGCATCGGCGTCGACGCCTTCTATTACTCTTGGCTGCCCGGTGACCATCCGAGTGCCTTCGCTGCGGCAAGCGTCGTCGACTCCAAGGTCGCCTTGGGGACACTCGATCCCGCCCAAGCGACCACGGCCAGTGGTGGAGAATCGGCGCTGGGTGAGGGGGCTGCGATTATTGTCCGGATGACAAAGGCGGTGTGCGCCGTCACGTCGGTATCGGTCGAAGAGTATGAGAAGGGCATTCAGATCGCTGTCTATGGGGTCACTGATCCGGCCCGCTGCGGGCAGACAACCGAGGGTGCTTACGTCGCCATCCCGCTCACCGATGAGCAGGTGGCGAAGGCGCGCAGCTACGAGGCTCCCGCCTACCATCCTCTGGACGACTCCGAGCTGAAGTACGGGGGGCAGAGTTCCTCCAAGGGGAAGTACAGCCCGACCATCTTCCAGGCTCGTAGCCGTGCCAAGCTCTCCGAGGTATGGCAGTCAGAGGAGACAGACCGCCAGCTGACGCCTCATGTGCTTCTGCCTCGCAGTGCCGGCTAA","MLLWSVIDPRGVWEVTSSWQFRNPEANEPSDSAFAVQRFFAFISLLVIVGGAFFFVSASHRNASARATDDASVREADSATPYVYPNIYSSSDGEGSDGYAETTVTPSPVDPFPSASTTAVGSGEPVVLFKPVLEGAAGEQKSDSSVSIGVDAFYYSWLPGDHPSAFAAASVVDSKVALGTLDPAQATTASGGESALGEGAAIIVRMTKAVCAVTSVSVEEYEKGIQIAVYGVTDPARCGQTTEGAYVAIPLTDEQVAKARSYEAPAYHPLDDSELKYGGQSSSKGKYSPTIFQARSRAKLSEVWQSEETDRQLTPHVLLPRSAG$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[39-59]?$	transmembrane_regions

InterPro
IPR013094
Domain

Alpha/beta hydrolase fold-3
PF07859	$\"[93-294]T$	Abhydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[29-316]T$	no description
PTHR23024	$\"[84-208]T$	MEMBER OF 'GDXG' FAMILY OF LIPOLYTIC ENZYMES

","No hits to the COGs database.","***** IPB013094 (Alpha/beta hydrolase fold-3) with a combined E-value of 1.4e-26. IPB013094A 91-104 IPB013094B 124-144 IPB013094C 162-181 IPB013094E 260-290***** IPB002168 (Lipolytic enzyme) with a combined E-value of 2.6e-18. IPB002168A 91-105 IPB002168B 108-150 IPB002168C 159-172","Residues 77-172 are similar to a (ESTERASE CAIFJ4 LIPASE CANDIDA HYDROLASE FUNCTION FAMILY ALBICANS EXPORTED PE-PGRS) protein domain (PD087172) which is seen in Q98KZ8_RHILO.Residues 187-265 are similar to a (HYDROLASE ESTERASE LIPASE 3.1.1.- PROBABLE LIPASE/ESTERASE CARBOXYLESTERASE PLASMID ACETYL 3.1.-.-) protein domain (PD087155) which is seen in Q8NUS5_STAAW.","","-46% similar to PDB:1JJI The Crystal Structure of a Hyper-thermophilic Carboxylesterase from the Archaeon Archaeoglobus fulgidus (E_value = 4.5E_13);-45% similar to PDB:2C7B THE CRYSTAL STRUCTURE OF ESTE1, A NEW THERMOPHILIC AND THERMOSTABLE CARBOXYLESTERASE CLONED FROM A METAGENOMIC LIBRARY (E_value = 4.6E_10);","Residues 93 to 294 (E_value = 2e-42) place ANA_0142 in the Abhydrolase_3 family which is described as alpha/beta hydrolase fold.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0143","160296","162809","2514","4.85","-42.34","89622","ATGGAAACCTACGAGATCGACCACCTCGCCGCCGTCCGCGCTCTCGCCCCCGAGTGCATGGTGCTGCTGCGCTCCAATGGCGCCTTCCCCTTGACTGAGCCGGGCGAGATCGCCCTGTTCGGATCCGGTGCGCGGCACACCATCAAGGGCGGAACCGGCAGCGGAGACGTCAACTCCCGCCACGTCACCACCATCGAGGAGGGGCTGGAGGCGGCCGGCTTCACCATCGTCACCCGGCCCTGGCTGGAGGCCTACGACCGTATCCGTCTCCGGGCCCACCAGGACTTCATTGTCGGTATCAGGGCCGAGGCCGCCAAGCGCGGCGTCCCCGCCATCATGGTCGGCATGGGCTCGGTCATGCCCGAGCCGGAGTACACGATCCCCCTCGATGTCCAGGCCGGCACCGACCCGCACGCAGCCGTCTACATCCTGTCCCGAACCTCCGGGGAAGGCAGCGACCGCACCCCCGAGGCGGGAGACCTCAGACTCACCGACACCGAGATCCGCGACATTCTCGACCTCAACGGGCGCTTCGAGCGGTTCCTCCTCGTGCTCAACGTGGGTGGCGTCGTCGACCTCAGCCCGCTGGGCGACGTTGCCAACATCCTGCTGCTCTCCCAGCTCGGCGCGACCGTCGGCGACGCCTTCGCCGACGTCCTCCTGGGGCGGACCTACCCCTCCGGAAAGCTCGCCACCACCTGGGCCGCCTGGGACGAGGACGACCAGATCGGCGACTTCGGCGACCCGGACGACACTCACTACCGCGAGGGCGTCTACGTCGGCTACCGCTTCTACGACTCGACCGGCAAGGAGCCGCTCTTCCCCTTCGGATTCGGCCTGGGCTACACGACCTTCGACGTCCAGATCCGCCAGGTGAGCCTCGACGGCGCCCGCGTGAGCATCGACATCGATGTCACCAATACCGGCGGCTACCCGGGCAAGGAGGCCATCCAGGTCTACGCCAGTGTGCCTGCCGGACGCCTCGACCAGCCGCTCCAGGCGCTGGCCGGCTTCACGAAGACCGACGAGATCACCCCCGGCGCCACGGCACGGATCAGCGTCGACGTCGATCTGACCGACCTGGCCTCCTACGACGAGGCCGCCCGTGCCACGGTCCTGGAGGCCGGGCGCTACATGCTGCGGGCGGGAACCTCCAGCCGGCAGCTGAGTCCCGTCGCCGTCGTCGAGCTCGCCCAGGACGCAACCGTGCGACACCTCACCGGTGACCTGGGGGAGCCCGGCTTCAGCGATTGGAAGCCCGAGGCGCCGGCGGTCCTCGACATTCCGGCCGGCCTGCCGGTGCTCACCGTCGACCCGGCCGACCTGCGCCTGCCGGACCACGCCGAGCCCGATGAGCAGGCAGCGCCGGAGGACGTCAGGCAGGCCCTCACCCTGGCCCGGGGGCTCTCCGACGACGAGCTCATCGACACCGTCTTGGGCGACTACCGCCGCGGCGAGGAGTCTGGTTCCATCGTCGGGGCCGCCTCCACCACCGTCATCGGCGCGGCGGGACAGACCACCACCCGGATCCCCGGCCTGCCCAGCATCATCATGGCCGACGGGCCCGCCGGACTGCGCCTGGCCCCCACCTACGGCGTCGACGCCGAGGGCCCCTTCTCACTGGGCGACTCCAGCCTGCCCGCCACCTTCCTCGAGCTCATGGACGACGCCGGACGTGAGGCCCTCGGCATCGCCGACGAGCCAGAACCCCGCGAACCTGCCGAGATCCGTGAGCAGTACGCCACCGCCATCCCCATCGGCACTGCGCTCGCCCAGTCCTGGAACCCTGCGCTGGTCGAGCAACTCGGCGACGTCGTCGGGGCCGAGATGGAGCGCTTCGGCATTCACCTCTGGCTCGCCCCCGCCTTCAACCTGCACCGCAGCGTCCTGTGCGGACGCAACTTCGAGTACCTCTCCGAGGACCCGCTGCTGGCCGGACGCCTCGCCGCCGCCATCACCCACGGGGTCCAGTCCCACCCGGGGCGGGGCGTGACCATCAAACATCTGGCCTGCAACAACCAGGAGACCAATCGCCTCAACTCCAACAGTCGGGTCAGCCCCCGAGCCCTGCGCGACCTCTACCTGCGCGCCTTCGAGATCTGCGTGCGCCAGGCCCGCCCCGCCGCCGTCATGACCTCCTACAACCTCATCAACGGCGTCCACACCTCCGAGTCGGCCCAGCTGCTCGAGGTGATCCTGCGCCGGGAGTGGGGCTTCGACGGACTGGTCATGACCGACTGGGTCGTCGACGGCATGACCCGCAGCGACATGAAGCACCCGCGCGCCACCGCGGCCGCCACCATCAAGGCAGGTAACGAGCTCTTCATGCCCGGAGGCGAGACGGACCGGGAGAACCTCCTGGCGGCCCTTGAGCGAGGGAGCGCAGGCCGCGGGCCGGATGGCCGGATCGCGCCGGAAGACGGAGGCGTGAGTCTGACACGGGGCGAGCTCGAGAAGCAGGCTGCCCGCGTTATCCGCGCGGCCTGGAGGATAGCCACGATCTCGACATCCTGA","METYEIDHLAAVRALAPECMVLLRSNGAFPLTEPGEIALFGSGARHTIKGGTGSGDVNSRHVTTIEEGLEAAGFTIVTRPWLEAYDRIRLRAHQDFIVGIRAEAAKRGVPAIMVGMGSVMPEPEYTIPLDVQAGTDPHAAVYILSRTSGEGSDRTPEAGDLRLTDTEIRDILDLNGRFERFLLVLNVGGVVDLSPLGDVANILLLSQLGATVGDAFADVLLGRTYPSGKLATTWAAWDEDDQIGDFGDPDDTHYREGVYVGYRFYDSTGKEPLFPFGFGLGYTTFDVQIRQVSLDGARVSIDIDVTNTGGYPGKEAIQVYASVPAGRLDQPLQALAGFTKTDEITPGATARISVDVDLTDLASYDEAARATVLEAGRYMLRAGTSSRQLSPVAVVELAQDATVRHLTGDLGEPGFSDWKPEAPAVLDIPAGLPVLTVDPADLRLPDHAEPDEQAAPEDVRQALTLARGLSDDELIDTVLGDYRRGEESGSIVGAASTTVIGAAGQTTTRIPGLPSIIMADGPAGLRLAPTYGVDAEGPFSLGDSSLPATFLELMDDAGREALGIADEPEPREPAEIREQYATAIPIGTALAQSWNPALVEQLGDVVGAEMERFGIHLWLAPAFNLHRSVLCGRNFEYLSEDPLLAGRLAAAITHGVQSHPGRGVTIKHLACNNQETNRLNSNSRVSPRALRDLYLRAFEICVRQARPAAVMTSYNLINGVHTSESAQLLEVILRREWGFDGLVMTDWVVDGMTRSDMKHPRATAAATIKAGNELFMPGGETDRENLLAALERGSAGRGPDGRIAPEDGGVSLTRGELEKQAARVIRAAWRIATISTS$","Beta-glucosidase","Cytoplasm, Extracellular","Beta-glucosidase A (Gentiobiase) (Cellobiase)(Beta-D-glucoside glucohydrolase)","beta-glucosidase ","Beta-glucosidase","","Varghese J.N., Hrmova M., Fincher G.B. Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 1999. 7(2):179-190. PMID: 10368285","","","

InterPro
IPR001764
Domain

Glycoside hydrolase, family 3, N-terminal
PR00133	$\"[510-526]T$ $\"[732-750]T$	GLHYDRLASE3
PF00933	$\"[510-777]T$	Glyco_hydro_3

InterPro
IPR002772
Domain

Glycoside hydrolase, family 3, C-terminal
PF01915	$\"[20-262]T$	Glyco_hydro_3_C

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.300	$\"[460-793]T$	no description
G3DSA:3.40.50.1700	$\"[7-285]T$	no description

","BeTs to 10 clades of COG1472COG name: Beta-glucosidase-related glycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1472 is --------vdrlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB001764 (Glycoside hydrolase, family 3, N-terminal) with a combined E-value of 2.4e-29. IPB001764A 624-672 IPB001764B 714-747***** IPB002772 (Glycoside hydrolase, family 3, C-terminal) with a combined E-value of 2.1e-09. IPB002772A 732-747 IPB002772B 8-26 IPB002772C 274-285***** IPB011658 (PA14) with a combined E-value of 4.4e-07. IPB011658A 697-746","Residues 28-160 are 49% similar to a (GLYCOSIDASE HYDROLASE BETA-GLUCOSIDASE GLUCOHYDROLASE DEGRADATION CELLULOSE CELLOBIASE BETA-GLUCOSIDASE-RELATED GENTIOBIASE GLUCOSIDE) protein domain (PD482647) which is seen in Q60038_THENE.Residues 254-293 are 72% similar to a (BETA-GLUCOSIDASE HYDROLASE GLYCOSIDASE GLUCOHYDROLASE PRECURSOR CELLOBIASE SIGNAL GENTIOBIASE BETA-D-GLUCOSIDE PROBABLE) protein domain (PD706916) which is seen in BGLS_AGRTU.Residues 305-383 are 59% similar to a (BETA-GLUCOSIDASE HYDROLASE GLYCOSIDASE PERIPLASMIC PRECURSOR BETA-XYLOSIDASE GLUCOHYDROLASE SIGNAL GENTIOBIASE BETA-D-GLUCOSIDE) protein domain (PD001971) which is seen in Q60038_THENE.Residues 488-793 are 57% similar to a (HYDROLASE BETA-GLUCOSIDASE GLYCOSIDASE PRECURSOR CELL SIGNAL BETA-HEXOSAMINIDASE BETA-XYLOSIDASE GLUCOHYDROLASE BETA-N-ACETYLGLUCOSAMINIDASE) protein domain (PD001132) which is seen in Q9F3Y0_BBBBB.Residues 580-765 are 44% similar to a (SACCHAROMYCOPSIS P22507 BETA-GLUCOSIDASE FIBULIGERA) protein domain (PDA1C2V5) which is seen in Q6CEN3_EEEEE.Residues 582-778 are 45% similar to a () protein domain (PDA1C2V3) which is seen in Q7SGM9_NEUCR.","","No significant hits to the PDB database (E-value < E-10).","Residues 20 to 284 (E_value = 6e-21) place ANA_0143 in the Glyco_hydro_3_C family which is described as Glycosyl hydrolase family 3 C terminal domain.Residues 510 to 777 (E_value = 2.3e-76) place ANA_0143 in the Glyco_hydro_3 family which is described as Glycosyl hydrolase family 3 N terminal domain.","","A (Gentiobiase) (Cellobiase) (Beta-D-glucoside glucohydrolase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0143.1","162857","163126","270","8.19","1.63","9997","ATGCCGACGATCAAGCCAGTATCAGATCTGAGGAGCTACACCGACGTTCTTAAGGATGTTGCGGAGGGCTCGCCTGTTTTCCTCACTAAGAATGGTCATGGGAGGTACGTCCTTCTCGATATGAAGGACTATGACCGCATTAAGGCGGGTCGTCGTCTCCTCCGAGAGGTCGAGGCGGGTCGGATTTCTGGTGAGGAGCAAGGGTGGGTTAGTGCTGCAGACGTGCGTGCGCACTTCGTCGCACGGCGGGATTCCGCCCATGAGTGCTGA","MPTIKPVSDLRSYTDVLKDVAEGSPVFLTKNGHGRYVLLDMKDYDRIKAGRRLLREVEAGRISGEEQGWVSAADVRAHFVARRDSAHEC$","Prevent-host-death family protein","Cytoplasm","","","","","","","","

InterPro
IPR006442
Family

Prevent-host-death protein
TIGR01552	$\"[4-55]T$	phd_fam: prevent-host-death family protein

InterPro
IPR007712
Family

Plasmid stabilization system
PF05016	$\"[5-97]T$	Plasmid_stabil

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","Residues 5 to 97 (E_value = 1.3e-09) place ANA_0143.2 in the Plasmid_stabil family which is described as Plasmid stabilisation system protein.","","","","1","","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:14 2007","Tue Aug 14 19:06:14 2007","Tue Aug 14 19:06:14 2007","Tue Aug 14 19:06:03 2007","","Mon Aug 20 17:58:40 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Mon Aug 20 17:58:40 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Tue Aug 14 19:06:03 2007","Mon Aug 20 17:58:40 2007","","Tue Aug 14 19:06:03 2007","","Tue Aug 14 19:06:03 2007","yes","","" "ANA_0144","163530","163895","366","5.12","-3.58","12979","ATGGCGCTGACACTTCAAGCACGTGAGACCTTCACCAGGCTGTTCGGGGTGGAGCCCCAACCTCACCCCACGGACCCCGAGCTGTTCGACATCCTCCAGAACGGGATCTTCGACGAGGCCTTCTCCACGGGCGTCCTCACCGACGTCGAGCGCGAGCTCATCAGCCTCGTGGCCATCGCCGCCATCGGCGCCACCACCCAGCTGCGCCCGCACGTGGCCGGGGCGATCCGGGCCGGTTCCTCCCGCCAGAAGGTGGCCGCCGCCCTGGTCCAGGTCATGCCCTACATCGGCGGCCCCTACGCCCTGCCCGGCCTGGTCCTCGTGGCCCGCTATGACGAGAGCGCCTCCGCAGAGGTCTACCGCTGA","MALTLQARETFTRLFGVEPQPHPTDPELFDILQNGIFDEAFSTGVLTDVERELISLVAIAAIGATTQLRPHVAGAIRAGSSRQKVAAALVQVMPYIGGPYALPGLVLVARYDESASAEVYR$","Gamma-carboxymuconolactone decarboxylase","Cytoplasm","4-carboxymuconolactone decarboxylase","hypothetical protein predicted by Glimmer/Critica","Carboxymuconolactone decarboxylase","","Eulberg D., Lakner S., Golovleva L.A., Schlomann M. Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity. J. Bacteriol. 1998. 180(5):1072-1081. PMID: 9495744","","","

InterPro
IPR003779
Domain

Carboxymuconolactone decarboxylase
PF02627	$\"[26-111]T$	CMD

","BeTs to 10 clades of COG0599COG name: Uncharacterized ACR, homolog of gamma-carboxymuconolactone decarboxylase subunitFunctional Class: S [Function unknown]The phylogenetic pattern of COG0599 is a-mp--y-vdrlbc-f-hsn-j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 111 (E_value = 1.1e-13) place ANA_0144 in the CMD family which is described as Carboxymuconolactone decarboxylase family.","","decarboxylase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0145","164360","163953","408","9.04","2.40","14958","ATGATCCCCCGGCCTCGCTCCGCCTGCCCGATCAACCGCAGCCTCGAGATGCTCGGCGACCGGTGGAGCCTGCTGATTCTGCGAGACATCGTCCTGCACGACCGGCGCTCCTTCCGCGAGCTGCTCACCGGCAGCGAGGAGGGCATCAGCGCCCCTGTCCTGTCCCGCCGACTGACCGACCTGGTGGAGGCGGGTTTCCTCACGAAGAATGAGGTCGCCCGGGGCAAGCAGGGGAGGTACTCGCTGACCGAGCAGGGCCTGGCGACGGTCCCACTGCTGATCGAGCTCGGTCGTCTCGGCGCACGCATCGACCCGTCAACCGCCCCCAACGCCCCCAGGATCGGCACGGATCCCGACGACCTCGCCAGGCGCATCGCCGTCCTGCGCGAGGCTCATCTCACTGATTAG","MIPRPRSACPINRSLEMLGDRWSLLILRDIVLHDRRSFRELLTGSEEGISAPVLSRRLTDLVEAGFLTKNEVARGKQGRYSLTEQGLATVPLLIELGRLGARIDPSTAPNAPRIGTDPDDLARRIAVLREAHLTD$","Transcriptional regulator, HxlR family","Cytoplasm","transcriptional regulatory protein","putative transcriptional regulator","helix-turn-helix, HxlR type","","Yasueda H., Kawahara Y., Sugimoto S. Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression. J. Bacteriol. 1999. 181(23):7154-7160. PMID: 10572115Huffman J.L., Brennan R.G. Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr. Opin. Struct. Biol. 2002. 12(1):98-106. PMID: 11839496","","","

InterPro
IPR002577
Domain

Helix-turn-helix, HxlR type
PF01638	$\"[17-107]T$	DUF24
PS51118	$\"[9-108]T$	HTH_HXLR

","BeTs to 13 clades of COG1733COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1733 is aomp-z---drlbcefghs-uj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","Residues 9-69 are 73% similar to a (REGULATOR TRANSCRIPTIONAL TRANSCRIPTION MLR1873 RSC0816 VNG0704C MB1754C SCO6223 STGU REGULATORY) protein domain (PD155022) which is seen in Q98JM7_RHILO.","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 107 (E_value = 6.2e-06) place ANA_0145 in the DUF24 family which is described as HxlR-like helix-turn-helix.","","regulatory protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0146","164474","165499","1026","6.08","-3.58","35327","GTGAAGGCCTTCGTCCTGAAGAAGTACGGCCACCCTCTGAGTGCCGTCGACATGCCCGTTCCCGAGCCCGGACCCCATCAGGTCCTGGTGCGGATGGTCGCCTCCGGCGTCAATCACGCCGATGAGCGCACCCGCACCGGTGAGTTCAAGGCCGTCTTCCGGCTCGACCTGCCCAAGGTGATGGGAGGGGAGCTGAGCGGTGAGGTGGTCGCCGTCGGCTCTCAGGTCGCAGGGCTCGCCGTCGGCGATCAGGTCTACGGCTACACCGGCGTGGTGGCGATGGGGACCTGGGCCGAGTTCGTCGTCATCGATGCCGACGCCCTCGCCCCCGCACCCCGGAGTATCTCTCTGGCTCAGGCGGCCTCCCTGCCGGTCGTCGCCCTGACCGCATGGCAGTCGCTGGTGACGATCGGCCGCCTCCAGCCGGGCCAGACGGTCCTGGTTCACGGCGGCGCCGGCGGAGTGGGGTCGGCCGTCATCCAGCTCGCCAAGCACCTGGGAGCCACTGTCGCCACCACGGCCTCGGCCTCCAGCGCCGACACCGTCAGGCAGCTCGGCGCGGACATCATCATCGACTACCGCAGTGAGGACTTCGTCCAGCGCCTGGCGGAGACCCCGGTGGACATCGTCGTCGACACCCAGGGCGGCGAGATCACCTCACGGTCCTTCCAGGTCCTGCGTCCGGGCGGGATCGTGGTGGGTATCGCCGGCACCCCCGACCCGTCACTGGCCGATCAGGCCGGCGCCGGGCCGCTGGTCAAGGTCGCGCTGTCCGCCCTCAGCCTCAAGGTGCGCCGCCAGGCCAGCAAGCTCGGCGTGCGCTACCGCTTCCTGTTCATCGAACCTGACGGAGAGGCCCTGCGCACCATCGCCGGACTCGTGGACGACGGCGTCATCCAGCCCGTCGTCGACCGGATCCTGCCCTTCGAGCAGACCCTCGCCGCACTCGACCAGCTGCTGGCCGGCGGAACCCGCGGCAAGGTCCTCGTGGCCACCAGCGAGCAGGAGGTCACCGCTCATGCCTGA","VKAFVLKKYGHPLSAVDMPVPEPGPHQVLVRMVASGVNHADERTRTGEFKAVFRLDLPKVMGGELSGEVVAVGSQVAGLAVGDQVYGYTGVVAMGTWAEFVVIDADALAPAPRSISLAQAASLPVVALTAWQSLVTIGRLQPGQTVLVHGGAGGVGSAVIQLAKHLGATVATTASASSADTVRQLGADIIIDYRSEDFVQRLAETPVDIVVDTQGGEITSRSFQVLRPGGIVVGIAGTPDPSLADQAGAGPLVKVALSALSLKVRRQASKLGVRYRFLFIEPDGEALRTIAGLVDDGVIQPVVDRILPFEQTLAALDQLLAGGTRGKVLVATSEQEVTAHA$","Alcohol dehydrogenase, zinc-binding","Cytoplasm, Membrane","zinc-binding oxidoreductase Atu5447","alcohol dehydrogenase; zinc-binding","Alcohol dehydrogenase, zinc-binding domain protein","","Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Taneja B., Mande S.C. Conserved structural features and sequence patterns in the GroES fold family. Protein Eng. 1999. 12(10):815-818. PMID: 10556240","","","

InterPro
IPR002085
Family

Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695	$\"[12-337]T$	ALCOHOL DEHYDROGENASE RELATED

InterPro
IPR002364
Family

Quinone oxidoreductase/zeta-crystallin
PS01162	$\"[143-164]T$	QOR_ZETA_CRYSTAL

InterPro
IPR013149
Domain

Alcohol dehydrogenase, zinc-binding
PF00107	$\"[142-274]T$	ADH_zinc_N

InterPro
IPR013154
Domain

Alcohol dehydrogenase GroES-like
PF08240	$\"[25-111]T$	ADH_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[105-307]T$	no description
PTHR11695:SF34	$\"[12-337]T$	ALCOHOL DEHYDROGENASE, ZINC-CONTAINING

","BeTs to 8 clades of COG0604COG name: NADPH:quinone reductase and related Zn-dependent oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0604 is -o-p-zyq-drlb-efghs--j----Number of proteins in this genome belonging to this COG is 4","***** IPB002364 (Quinone oxidoreductase/zeta-crystallin) with a combined E-value of 7e-37. IPB002364B 57-77 IPB002364C 95-122 IPB002364D 141-164***** IPB011597 (GroES-related) with a combined E-value of 2.7e-32. IPB011597A 24-51 IPB011597B 58-85 IPB011597C 94-131 IPB011597D 144-188 IPB011597E 206-238***** IPB002328 (Zinc-containing alcohol dehydrogenase) with a combined E-value of 5.1e-16. IPB002328A 12-43 IPB002328B 58-85 IPB002328D 95-133","Residues 139-197 are similar to a (OXIDOREDUCTASE ZINC METAL-BINDING DEHYDROGENASE ALCOHOL NAD QUINONE TRANSFERASE SYNTHASE PROBABLE) protein domain (PD000104) which is seen in Q82NU0_STRAW.Residues 216-330 are similar to a () protein domain (PDA134R8) which is seen in Q74LD4_LACJO.","","-45% similar to PDB:1IYZ Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH (E_value = 6.1E_19);-45% similar to PDB:1IZ0 Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH (E_value = 6.1E_19);-44% similar to PDB:2CF2 ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE (E_value = 7.9E_19);-45% similar to PDB:1YB5 Crystal structure of human Zeta-Crystallin with bound NADP (E_value = 2.3E_18);-42% similar to PDB:2J8Z CRYSTAL STRUCTURE OF HUMAN P53 INDUCIBLE OXIDOREDUCTASE (TP53I3,PIG3) (E_value = 8.8E_18);","Residues 25 to 111 (E_value = 3.9e-20) place ANA_0146 in the ADH_N family which is described as Alcohol dehydrogenase GroES-like domain.Residues 142 to 274 (E_value = 6.2e-24) place ANA_0146 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase.","","oxidoreductase Atu5447 (fragment)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0147","165492","166373","882","9.00","4.14","31771","ATGCCTGAGACCGACGGCACCACCATGATCGATGGGCCCATCACCCGGTGGACCTCCGCTCCCACCCGGCACCTGCCGGTGAGAGGAGAGTCCTTCGCCTACCGGGACCTCGGGGGCGACTCCGGAAGGCCGCCCATCGTCCTGCTCGCCCACCTCGGGGCCACCCTCGACGAGTGGGACCCCCGCGTCGTCGAGGCGCTCGCCGAAGGCCGCCGCGTCATTGCGGTCAACCTGCCGGGCATCGGCTCCTCCACCGGGAACGTCCCACGAACCATCAAAGGGATGGCCGGTGCCGCACGGGCCTTCATCTCCGAGCTTGGTCTGACCCGGATCGACCTCATGGGCTTCTCCCTGGGAGGCTTCGTGGCCCAGCAGGTCACTCTTGACGCCCCGAAGCTGGTCCGACGACTCGTCCTGGCCGGAACCGGTCCCGCAGGAGGCGAGGGGATCGACCGGCCCACCGGAGCCGCCTACGTCTACCACGACATGCTGCGCGGAGTGCTCGCCCGCACCGACGCCAAAGAGTTCCTCTTCTTCCCGCGCACCCCTGACGGCAAGGCTGCAGCGCGCGACTACCTCGCCCGGATTCACGAACGAGTCATGGATCGGGACTCCCCGATCACCTTGAAAGCCTTCCGCACTCAGATCGCCGCCATCAAGGCATGGGGGCGCCAGCAGCCACAGGACCTGTCCAGGATCACGGCCCCCACGCTGATCGCCAACGGGGACCACGACCGCATGGTCCCCACCCCGTTGTCTGAGGACATGCACCGGCGGATCCCCGGCAGCACCCTGGTCATCTACCCCGGGGCAGGCCACGGCGGTGTCTTCCAGTACCACCGGGAGTTCATCCCCACGCTGCTGGACCACCTCGACTCCTGA","MPETDGTTMIDGPITRWTSAPTRHLPVRGESFAYRDLGGDSGRPPIVLLAHLGATLDEWDPRVVEALAEGRRVIAVNLPGIGSSTGNVPRTIKGMAGAARAFISELGLTRIDLMGFSLGGFVAQQVTLDAPKLVRRLVLAGTGPAGGEGIDRPTGAAYVYHDMLRGVLARTDAKEFLFFPRTPDGKAAARDYLARIHERVMDRDSPITLKAFRTQIAAIKAWGRQQPQDLSRITAPTLIANGDHDRMVPTPLSEDMHRRIPGSTLVIYPGAGHGGVFQYHREFIPTLLDHLDS$","Hydrolase or acyltransferase (alpha/beta hydrolase superfamily)","Cytoplasm, Extracellular","cultivar specificity protein W78","hydrolase; alpha/beta fold family","alpha/beta hydrolase fold","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[71-289]T$	Abhydrolase_1

InterPro
IPR003089
Family

Alpha/beta hydrolase
PR00111	$\"[70-85]T$ $\"[113-126]T$ $\"[127-140]T$ $\"[237-251]T$	ABHYDROLASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[20-292]T$	no description
PTHR10992	$\"[29-291]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF17	$\"[29-291]T$	VALACYCLOVIR HYDROLASE

","BeTs to 17 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","***** IPB000639 (Epoxide hydrolase signature) with a combined E-value of 4.8e-17. IPB000639B 70-85 IPB000639C 113-126 IPB000639D 127-140 IPB000639E 235-251 IPB000639F 268-290***** IPB003089 (Alpha/beta hydrolase fold signature) with a combined E-value of 5.7e-15. IPB003089A 70-85 IPB003089B 113-126 IPB003089C 127-140 IPB003089D 237-251","Residues 2-146 are 47% similar to a (HYDROLASE) protein domain (PD796301) which is seen in Q9K3H6_STRCO.Residues 19-291 are 40% similar to a (ENZYME LIPOLYTIC) protein domain (PD730177) which is seen in Q8TMG8_METAC.Residues 23-140 are 51% similar to a (HYDROLASE BLR7809 BLR7810 PROBABLE) protein domain (PD701794) which is seen in Q89CI8_BRAJA.Residues 25-142 are 51% similar to a (CARBOXYLESTERASE CARBOXYLASE) protein domain (PD535844) which is seen in Q93HH2_STRAW.Residues 29-283 are 49% similar to a (64C2.070) protein domain (PD842961) which is seen in Q872K6_NEUCR.Residues 29-293 are 41% similar to a (HYDROLASE POSSIBLE) protein domain (PDA115G1) which is seen in Q6NCW9_RHOPA.Residues 34-144 are 68% similar to a (HYDROLASE ALPHA/BETA ENOL-LACTONE FOLD PEROXIDASE HYDROLASE FAMILY AMINOPEPTIDASE 3-OXOADIPATE BETA-KETOADIPATE) protein domain (PD036710) which is seen in Q9KJF9_RHILE.Residues 35-146 are 53% similar to a (ESTERASE2) protein domain (PD055009) which is seen in O66382_ACEPA.Residues 40-274 are 40% similar to a (HYDROLASE) protein domain (PD105081) which is seen in O54172_STRCO.Residues 43-142 are 52% similar to a (BETA-KETOADIPATE HYDROLASE ENOL-LACTONE HYDROLASE) protein domain (PD745856) which is seen in Q9RWS2_DEIRA.Residues 45-273 are 41% similar to a (HYDROLASE) protein domain (PD732145) which is seen in Q826V8_STRAW.Residues 45-147 are 54% similar to a (BIOH) protein domain (PD445098) which is seen in Q9AJM9_BBBBB.Residues 62-291 are 44% similar to a (HYDROLASE ALPHA/BETA 2-HYDROXYMUCONIC SEMIALDEHYDE PLASMID ACID MUSCULUS HOMOLOG 2-HYDROXY-6-OXO-6-PHENYLHEXA-24-DIENOATE MUS) protein domain (PD330619) which is seen in Q52532_PSESP.Residues 63-284 are 43% similar to a (HYDROLASE OR ALPHA/BETA TRANSFERASE ACYLTRANSFERASES PREDICTED ACYLTRANSFERASE SUPERFAMILY HYDROLASES) protein domain (PD611613) which is seen in Q8R776_THETN.Residues 95-145 are 68% similar to a (NODULATION RELATED) protein domain (PDA199Y9) which is seen in Q8P939_XANCP.Residues 146-229 are 65% similar to a (PEROXIDASE HYDROLASE OXIDOREDUCTASE ALPHA/BETA NON-HAEM POSSIBLE FAMILY FOLD SPECIFICITY 1.11.1.-) protein domain (PD857451) which is seen in Q8UJN0_AGRT5.Residues 232-273 are 71% similar to a (HYDROLASE ALPHA/BETA FOLD FAMILY HYDROLASE DEPOLYMERASE ENOL-LACTONE PEROXIDASE TRANSFERASE POSSIBLE) protein domain (PD588112) which is seen in Q9KJF9_RHILE.","","No significant hits to the PDB database (E-value < E-10).","Residues 71 to 289 (E_value = 6.6e-21) place ANA_0147 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","specificity protein W78","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0148","166471","167250","780","5.80","-4.71","27246","GTGACGACGCAGCCCTACCTCTCACGGCAGGTCACCCTCACCGTCCAGGGGCAGAGGCTCGGGGGACTGGCCTACGTCCCGCGCACGGCGTCGTCGGCCCCCGCGCCCCTGGTCATCTGCTGCCACGGCATGGAGGGCTCCCACACCCGCGTCGCCCCCATGGCCCGGCGCTTCGCCGCGGCCGGGGCCGTGGCCATCTGCTTCGACTTCCGCGGGGGCGGCGGCAGCGCCAGCCAGGGTGAGACCACCGCGATGTCGGCCCTGACCGAGCTGGCCGACCTCGAAGCCGTCCTCACTGCCGCCTGCGCCTGGCCGGAGGTCGACGCCTCCCGGGTCGCCCTGTTCGGGCTGAGCTTGGGCGGAGCGGTCGCAGCGCTCGCGGCCGCCCGCCACCCGCAGCGGATCACCGCCCTGACCCTGTGGTACCCGGCTCTGCGGCTGGGGGAGAACCTGCGCGCCGCCTTCCACACTCCGGCGGCCGTTCCCGAGGAGTTCGACTGGGCGGGCACCCGCCTGGGGCGCGCCTACGCCGTCGACGGCTGGAATCTGGAGGTCGGGGCCGAGCTGGCCACCTACCGCCGCCCCGTCCTCATCGTCCACGGGGACCAGGACCGCGCCGTGCCCATCGAGGTCTCCCGGGCCGCCGTGAGCGCCACCCCTGACGCCGAGCTCGTCACCATTCCCGGCGCCGCCCACGGCTTCGGCGACGCCAACTGGGAGGAGGCCATGCGCCGCACCATCGGCTTCCTGGCCTGGAACGGGGTCCTCGAGGAGGACTGA","VTTQPYLSRQVTLTVQGQRLGGLAYVPRTASSAPAPLVICCHGMEGSHTRVAPMARRFAAAGAVAICFDFRGGGGSASQGETTAMSALTELADLEAVLTAACAWPEVDASRVALFGLSLGGAVAALAAARHPQRITALTLWYPALRLGENLRAAFHTPAAVPEEFDWAGTRLGRAYAVDGWNLEVGAELATYRRPVLIVHGDQDRAVPIEVSRAAVSATPDAELVTIPGAAHGFGDANWEEAMRRTIGFLAWNGVLEED$","Alpha-beta superfamily hydrolase","Cytoplasm, Extracellular","CinII, putative","hydrolase; putative","dienelactone hydrolase","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[188-251]T$	Abhydrolase_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[21-250]T$	no description
PTHR10992	$\"[28-251]T$	ALPHA/BETA HYDROLASE RELATED

","BeTs to 3 clades of COG1073COG name: Hydrolases of the alpha/beta superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1073 is ao--kzy-vdrlb-efg-s--j-i--Number of proteins in this genome belonging to this COG is 1","***** IPB003089 (Alpha/beta hydrolase fold signature) with a combined E-value of 2.4e-17. IPB003089A 62-77 IPB003089B 114-127 IPB003089C 128-141 IPB003089D 196-210***** IPB000639 (Epoxide hydrolase signature) with a combined E-value of 1.1e-11. IPB000639B 62-77 IPB000639C 114-127 IPB000639D 128-141 IPB000639E 194-210***** IPB002410 (Prolyl aminopeptidase (S33) family signature) with a combined E-value of 3.9e-06. IPB002410A 38-46 IPB002410B 65-76 IPB002410C 114-128","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 20 to 254 (E_value = 3.2e-05) place ANA_0148 in the DLH family which is described as Dienelactone hydrolase family.Residues 188 to 251 (E_value = 8.5e-07) place ANA_0148 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0149","167350","168159","810","6.18","-4.18","30160","GTGAGCGCACACGAGACAACAGACCTGACCAGTGTCAGCAAGACGATGCTGTTGACCCTCCATGCCAGGGCGGAGCACACGCTCTCCGACCGGCCGCGCTTCACTGACCCCGCCGCGGTCGAGCTCGTCTCCCGGCTCGACTACGACTTCACCATGGCGAGTCAGGACCGGCTCATGGCCGACGGCGTCGTGCTGCGCACCCTCACGCTCGACCCGCTCGTGGCCGGCTACCTGGACACCCACCCCGGCTGCACGGTGGTCAACATCGCCTGTGGGCTCGACACCCGCTTCCAGCGCCTCGACGACGGGCGCGTCACCTGGTACGACCTCGACCTGCCTGACGTCATCGCGCTGCGGCGCCGGCTGCTCGAGGACGGCGAGCGTCACCGCACCATTGCCGCCTCCGCCCTCGACCCCGACTGGCCCGACCAGCTGGGGGAGATGAGCCGCCACGTGCTCGTCATCATCGAAGGACTGAGCATGTACCTCGAGCAGGAGGAGGTGCGCACGCTCCTGGACATCATCGCTGGGCGCCTGCCCGGTGCGACCGTCCTCATCGAGGTCATGCCCCGCCTGTTCCAGAAGTACGGCCGGGAGCGCTCAGTGGAGGACGCGGGGGCGCGCTACACCTACGGCTGCTCCAGCGCCGCCGAGTTTCGCCGCACGGTGGCCCCCGGCTACACGCTGCTCCACGACGTCCCCTTCACCCGCACCATCGCGCGCTACCATCCCCTGCTCGTGCCTCTGACGCGGCTACCGCTGGTGGGCAGACTCTCCGAGCGCATCGTGGTGCTGCGGGCGCCGGCCTGA","VSAHETTDLTSVSKTMLLTLHARAEHTLSDRPRFTDPAAVELVSRLDYDFTMASQDRLMADGVVLRTLTLDPLVAGYLDTHPGCTVVNIACGLDTRFQRLDDGRVTWYDLDLPDVIALRRRLLEDGERHRTIAASALDPDWPDQLGEMSRHVLVIIEGLSMYLEQEEVRTLLDIIAGRLPGATVLIEVMPRLFQKYGRERSVEDAGARYTYGCSSAAEFRRTVAPGYTLLHDVPFTRTIARYHPLLVPLTRLPLVGRLSERIVVLRAPA$","O-methyltransferase involved in polyketide biosynthesis","Cytoplasm","tetracenomycin C synthesis protein tcmP","O-methyltransferase-like protein","O-methyltransferase domain protein","","","","","

InterPro
IPR003455
Domain

O-methyltransferase, N-terminal
PF02409	$\"[5-99]T$	Omt_N

","BeTs to 4 clades of COG3315COG name: O-Methyltransferase involved in polyketide biosynthesisFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG3315 is ----------r-b--fgh---j----Number of proteins in this genome belonging to this COG is 2","***** IPB003455 (Protein of unknown function DUF142) with a combined E-value of 1.7e-19. IPB003455A 10-44 IPB003455B 86-119 IPB003455C 150-163","Residues 9-218 are 57% similar to a (METHYLTRANSFERASE TRANSFERASE O-METHYLTRANSFERASE POLYKETIDE SYNTHESIS TETRACENOMYCIN 2.1.1.- TCMP OMT O-METHYLTRANSFERASE-RELATED) protein domain (PD039622) which is seen in Q8TKD5_METAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 99 (E_value = 1.2e-15) place ANA_0149 in the Omt_N family which is described as O-methyltransferase N-terminus.","","C synthesis protein tcmP","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0150","168904","168440","465","4.87","-9.84","16716","ATGAGCAGCGAGTCGCGGACGCCTCCGCCCGCATCCGCAACCGGTATGCCGAAGTCCTGGAACGCCTCGGCCGCTGATCGGGCAGAGATGGTCGAGTACCTGACGCTCGAGGACGCACTGTCACTCATTGAGGACCTCGCTGTGGGACCGGTCCGGGATCTCGGCCTGCTCGACTCGGCGCTGCACCGACCTGCGACCATGCTCTGGGGACACGACGCTTACGCCACAATCGACGAGAAGGCGGCGGCGCTGCTCGATTCCCTGGTCCGCAATCATCCACTGGTAGATGGCAACAAGCGCCTGGGGTGGTTGGCCACGCTGGTCTTCCTGGACATCAACGGCCACTGGGTCGAGGCTCCCGACGACGACGCCTACCGGCTGGTGATGGACGTCGCCGCTGGGAAGCTCTCACTCAAGGAGATCACTGCTGCCCTGTCTCAATGGCACGGCCGCGACTCGGAATAG","MSSESRTPPPASATGMPKSWNASAADRAEMVEYLTLEDALSLIEDLAVGPVRDLGLLDSALHRPATMLWGHDAYATIDEKAAALLDSLVRNHPLVDGNKRLGWLATLVFLDINGHWVEAPDDDAYRLVMDVAAGKLSLKEITAALSQWHGRDSE$","Death-on-curing family protein","Cytoplasm","death on curing protein","K07341 death on curing protein","death-on-curing family protein","","Lehnherr H., Maguin E., Jafri S., Yarmolinsky M.B. Plasmid addiction genes of bacteriophage P1: doc, which causes cell death on curing of prophage, and phd, which prevents host death when prophage is retained. J. Mol. Biol. 1993. 233(3):414-428. PMID: 8411153","","","

InterPro
IPR006440
Family

Death-on-curing protein
PF05012	$\"[32-145]T$	DOC
TIGR01550	$\"[27-147]T$	DOC_P1: death-on-curing family protein

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 91-148 are 64% similar to a (ON DEATH DOC CURING DEATH-ON-CURING PLASMID P1 BACTERIOPHAGE FAMILY PROBABLE) protein domain (PD015546) which is seen in Q73V70_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 32 to 145 (E_value = 1.7e-10) place ANA_0150 in the DOC family which is described as Prophage maintenance system killer protein.","","on curing protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0151","168167","168496","330","11.70","8.38","11650","ATGGGGCACTGGCCCGGTGCTGGCCTGGTGCTGGCCTGGTCCCGGTCTGGCACTGGCGCGGCACTGGACCGACACGAGGCCTGGGCGGCCGGTCTCGACGGGGACATCCTGCGCGTTGGGGGACAGGAATCCGGTCCCCGACGGCGTCGAATGCCCCCGGCCGGAAGGACACGCACCCGGCCGTGCGGAATGTCCCCGATGGCGCCGGACGCCCGGGCCTGGAGGCGTGCATCTCCAGGCCGAGAGGCCGACGCCGTGTCCCGCCGTGCTGCTCTATTCCGAGTCGCGGCCGTGCCATTGAGACAGGGCAGCAGTGATCTCCTTGAGTGA","MGHWPGAGLVLAWSRSGTGAALDRHEAWAAGLDGDILRVGGQESGPRRRRMPPAGRTRTRPCGMSPMAPDARAWRRASPGREADAVSRRAALFRVAAVPLRQGSSDLLE$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[223-382]T$	AAA

InterPro
IPR011704
Domain

ATPase associated with various cellular activities, AAA-5
PF07728	$\"[226-384]T$	AAA_5

InterPro
IPR013982
Domain

AICARFT/IMPCHase bienzyme, formylation region
SM00798	$\"[46-298]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[199-331]T$	no description

","BeTs to 6 clades of COG1401COG name: GTPase subunit of restriction endonucleaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1401 is --m-k--q-d--bce-----u-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 198-474 are 67% similar to a (ENDONUCLEASE ATP-BINDING RESTRICTION ENZYME 5-METHYLCYTOSINE-SPECIFIC DOMAIN HYDROLASE PLASMID LLAI.2 RELATED) protein domain (PD006385) which is seen in Q6GKL9_STAAR.","","No significant hits to the PDB database (E-value < E-10).","Residues 226 to 384 (E_value = 4.3e-33) place ANA_0152 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0153","170899","172014","1116","9.17","9.28","41979","ATGACAGCCGCCCTGCCCGGCCGGGCGCGGGACGGGGTTCCCGGCCGACCGCACCAGCGTGGTCCCAGCACCGTCCTGCTCAAGAACGTCTACTACATGCTCGCCTACGCCTTCAAGGCCCTGGAGACCGGCGAGCACCGGCGCCTGGCGGCCGAGGACTTCGAGCATGTCCATGACATGCTCGCCGCGATCCTGGCCGGTGGGCTGGACAACCAGCGCCGACGCGGTTTCGAGCGGGACTATCAGCCCTTCAACGAGGACCTGACGGTGGTGCGGGGACGCATCGACCCGGCCGCCACGATGCGTCTGAGGGCGCGCCGCAGGAGCCTGGTGCGCTGCGGATACGACGAGCGCACCGAGAACACCCTCATGAACCGGCTCCTCAAGACAGCCGCCCTGCGTCTGATCCTGCACGGCGACGTCGCCTCGGCCCGCCGGAAGCGTCTGAAGTCCACACTGCTCGTCATGGGCGACGTCGAGGTGATGAGCGTCGGGGACCTGCGCCAGCTGCACTGGGACAGCTTGCGCTTCCACCGCGGTAACCGCTCCTACCGGCTGCTCATGGGCGTGTGCCGGCTCGTCCTGGACGAGCGGCTGCTCAGTGGCACCGACGGCGCGGTCAGCCTCGCCGACTTCCTCGACCCCCAGGAGCTGAGCGCCCTGTACGAGCGCTTCGTCCTGGCCTACTTCCGCCGCCACCACCCCCACCTGCGCGCCGGTGCTCCCTGGGTGAGCGGCGGCATCGAGGACGCCCCGGTCTTCCTCCCGGGACTGCACACCGACATCGTCCTGACCGGGCCGGAGCGGACCCTCATCATCGACACCAAGTGCTACGGGCGCATCCTCGGCTCCCGCTACGACAAGTCGATCCTGTCCCCAGCCAACCGCAACCAGATCTACAGCTACGTCATGCATGAGGCCAGTGACCCCCGGCAGTCCGGGCGTGAGGTCGCCGGCATGCTGCTCTACGCCCAGACCGCCGTCGACCCGCCGGTCCGCGAGACCTGGACCGAGACCGGGCACCGCTTCCACGTGCGCACCCTCGACCTGGACCGGGACTTCACCGAGATCGCCGTACAGCTCGACGACGTCGCTGCCCTGCTCGCGTCAATCTGA","MTAALPGRARDGVPGRPHQRGPSTVLLKNVYYMLAYAFKALETGEHRRLAAEDFEHVHDMLAAILAGGLDNQRRRGFERDYQPFNEDLTVVRGRIDPAATMRLRARRRSLVRCGYDERTENTLMNRLLKTAALRLILHGDVASARRKRLKSTLLVMGDVEVMSVGDLRQLHWDSLRFHRGNRSYRLLMGVCRLVLDERLLSGTDGAVSLADFLDPQELSALYERFVLAYFRRHHPHLRAGAPWVSGGIEDAPVFLPGLHTDIVLTGPERTLIIDTKCYGRILGSRYDKSILSPANRNQIYSYVMHEASDPRQSGREVAGMLLYAQTAVDPPVRETWTETGHRFHVRTLDLDRDFTEIAVQLDDVAALLASI$","McrBC 5-methylcytosine restriction system component","Cytoplasm","mcrC, putative","hypothetical protein","McrBC 5-methylcytosine restriction system component-like","","","","","

noIPR
unintegrated

unintegrated
PD360097	$\"[57-302]T$	Q6GKL8_STAAR_Q6GKL8;

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 57-302 are 53% similar to a (MCRC RESTRICTION ENZYME MA2118 SYSTEM CJ0140 SEQUENCING DIRECT MODULATOR POSSIBLE) protein domain (PD360097) which is seen in Q6GKL8_STAAR.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0154","172140","173777","1638","5.15","-27.03","59714","ATGCTGCGCGTTGGGGGACAGGAATCCGGTCCCCGACGGCGTCGAAGGTCCCCGTCCGCACAGAAATGTCCCCGGCCGCGGGGGAGGACTGGCAGCATCGGAACCGTGACCGAGAACCACGCCCAGCCCAGCCCCGCCAACCCGGACGACGTCGTCAACCCCCTCCTGCTCCAGGCCTTCGCCTGGGACCTGCCCGCCGACTCCACCCACTGGCGCCTCCTGGCGGACAATGCCGCCCTCCTGGCCGACTGCGGGGTGAGTTCGGTGTGGCTGCCTCCCGCCTATAAGGGCCAGGCCGGTGTGGAGGACGTCGGCTACGGCGTCTACGACACCTACGACCTGGGCGAGTTCGACCAGAAGGGCACCGTCCCCACCAAGTACGGCACCAAGGAGGACTACCTCGCCGCCATCGAGGCCCTGCACGCGGCCGGCATCAGCGTCGTGGCGGACATCGTCCTCAACCACCGCATGGGCGGGGACGCCACCGAGGTCGTGCGTGCCACGCCCGCCGACCCCCACGACCGCACGCGCACCATTGGTGAGACCGAGGAGATTACGGCCTGGACCCGCTACACCTTCCCGGGGCGCGCCGGCGCCTACTCGGACTTCACCTGGGACTGGACCTGCTTCCATGGCACCGACTGGGACGAGGCCCGTCACCAGCAGGGCGTCTGGCTCTTCGAGGGCAAGCAGTGGAACGAGAACGTCAATGACGAGTTCGGCAACTACGACTACCTCATGGGCTCTGATGTCCACGTTATCGACCCCGCCGTCAGCGCCGAGATGGACCGTTGGGGGCGCTGGTACGTGGAGACCACCGGCGTCGACGGTCTGCGCCTGGACGCACTCAAGCACGTCGGCGCCGATTTCTTCGCCCGCTGGCTGCCCGAGCTGCGCCGCGCCACCGGCCGCGCCCTGCCGGCCGTGGGCGAGTACTGGTCCCACGACGTCGCCGAGCTGGAGGGCTACCTGGAGGCCGTGCCCTTCATGAGCCTGTTCGACGTCCCCCTCCACTTCCACCTGCACGCGGCCTCCACCTCCAATGGCGACGTCGACCTGACCCGGCTCTTCGAGGGCACCCTCGTGGCCGCCGACCCCGCGCGCGCCGTCACCTTCGTGGAGAACCACGACACCCAGCCGGGCCAGTCCCTGGCCTCCACCATCGAGCCCTGGTTCAAGCCCTCGGCCTACGCCCTCATCCTGCTGCGCGAAGCTGGAACCCCCTGCGTCTTCTGGGGCGACCTGTTCGGCACGCCCGAGACCGGCGACCTGCCGGCCGTCACCGAGCTGCCGCTGCTCATGACCATGCGACGCGCCCTGGCCCACGGCCCCCAGCACGACGCCCTCGACGACCCCGACGTCGTCGGCTTCGCGCGCGAGGGCGACGAGGCCCACCCCGGCTCCGGGCTCGCCGTCGTCCTGTCCGACCGCAGGGCCGCCACTAAGCGTCTCCACGTCGGGGCGCGGCACGCCGGCGAGCAATGGATCTGCGTCCTGGGCGGGCACGAGCCGGTCACCGTCGCCGAGGACGGCAGCGTGGAGCTGCCCGTGTCCGACGGCGGCCTGAGCGTCTACGCGCCGCAGGCCGCCCGGCCGATCCTGGACAGTGCCGAGCAGCACCTCCTGCGTCAGCGCTGA","MLRVGGQESGPRRRRRSPSAQKCPRPRGRTGSIGTVTENHAQPSPANPDDVVNPLLLQAFAWDLPADSTHWRLLADNAALLADCGVSSVWLPPAYKGQAGVEDVGYGVYDTYDLGEFDQKGTVPTKYGTKEDYLAAIEALHAAGISVVADIVLNHRMGGDATEVVRATPADPHDRTRTIGETEEITAWTRYTFPGRAGAYSDFTWDWTCFHGTDWDEARHQQGVWLFEGKQWNENVNDEFGNYDYLMGSDVHVIDPAVSAEMDRWGRWYVETTGVDGLRLDALKHVGADFFARWLPELRRATGRALPAVGEYWSHDVAELEGYLEAVPFMSLFDVPLHFHLHAASTSNGDVDLTRLFEGTLVAADPARAVTFVENHDTQPGQSLASTIEPWFKPSAYALILLREAGTPCVFWGDLFGTPETGDLPAVTELPLLMTMRRALAHGPQHDALDDPDVVGFAREGDEAHPGSGLAVVLSDRRAATKRLHVGARHAGEQWICVLGGHEPVTVAEDGSVELPVSDGGLSVYAPQAARPILDSAEQHLLRQR$","Alpha-amylase","Cytoplasm, Extracellular","amyS","alpha-amylase ","alpha amylase, catalytic region","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","Some of the required catalytic sites were not detected in this domain. It is probably inactive. Check the literature (PMID: 9283074) for details.","","

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[54-417]T$	Alpha-amylase

InterPro
IPR006589
Domain

Glycosyl hydrolase, family 13, subfamily, catalytic region
SM00642	$\"[54-442]T$	Aamy

InterPro
IPR013776
Family

Alpha-amylase, thermostable
PIRSF001021	$\"[32-531]T$	Alpha-amylase, thermostable type

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[53-445]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[55-157]T$ $\"[198-525]T$	AMYLASE
PTHR10357:SF9	$\"[55-157]T$ $\"[198-525]T$	ALPHA-AMYLASE

","BeTs to 9 clades of COG0366COG name: GlycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0366 is ---p--y-vdrlbcefg----j----Number of proteins in this genome belonging to this COG is 7","***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 2.5e-22. IPB006589A 76-93 IPB006589B 127-155 IPB006589C 274-285 IPB006589D 371-380***** IPB006046 (Alpha-amylase signature) with a combined E-value of 1.2e-19. IPB006046B 144-155 IPB006046C 275-286 IPB006046D 307-325 IPB006046E 367-379***** IPB006048 (Alpha amylase, C-terminal all-beta domain) with a combined E-value of 1.8e-15. IPB006048B 128-156 IPB006048C 271-286 IPB006048E 365-386***** IPB004193 (Glycoside hydrolase, family 13, N-terminal) with a combined E-value of 6.5e-08. IPB004193D 141-155 IPB004193E 268-281","Residues 56-163 are similar to a (ALPHA-AMYLASE GLYCOSIDASE HYDROLASE PRECURSOR SIGNAL CARBOHYDRATE METABOLISM GLUCANOHYDROLASE CALCIUM-BINDING 14-ALPHA-D-GLUCAN) protein domain (PD031991) which is seen in Q9CG59_LACLA.Residues 165-227 are 55% similar to a (ALPHA-AMYLASE GLYCOSIDASE HYDROLASE CYTOPLASMIC AMYLASE CARBOHYDRATE GLUCANOHYDROLASE PRECURSOR 14-ALPHA-D-GLUCAN METABOLISM) protein domain (PD868023) which is seen in AMY_BACLI.Residues 232-299 are 64% similar to a (HYDROLASE GLYCOSIDASE ALPHA-AMYLASE PRECURSOR SIGNAL CALCIUM-BINDING METABOLISM CARBOHYDRATE GLUCANOHYDROLASE 14-ALPHA-D-GLUCAN) protein domain (PD000173) which is seen in Q8U916_AGRT5.Residues 309-412 are 73% similar to a (ALPHA-AMYLASE GLYCOSIDASE HYDROLASE PRECURSOR SIGNAL CARBOHYDRATE METABOLISM CALCIUM-BINDING GLUCANOHYDROLASE 14-ALPHA-D-GLUCAN) protein domain (PD001604) which is seen in AMY_BACAM.Residues 413-525 are 63% similar to a (ALPHA-AMYLASE GLYCOSIDASE HYDROLASE CYTOPLASMIC AMYLASE CARBOHYDRATE GLUCANOHYDROLASE PRECURSOR 14-ALPHA-D-GLUCAN METABOLISM) protein domain (PD005779) which is seen in AMY_BACAM.","","-63% similar to PDB:1OB0 KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE (E_value = 1.1E_129);-63% similar to PDB:1BLI BACILLUS LICHENIFORMIS ALPHA-AMYLASE (E_value = 1.5E_129);-63% similar to PDB:1VJS STRUCTURE OF ALPHA-AMYLASE PRECURSOR (E_value = 4.8E_128);-61% similar to PDB:1HVX BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE (E_value = 2.2E_125);-61% similar to PDB:1E3X NATIVE STRUCTURE OF CHIMAERIC AMYLASE FROM B. AMYLOLIQUEFACIENS AND B. LICHENIFORMIS AT 1.92A (E_value = 6.1E_123);","Residues 54 to 442 (E_value = 5.5e-66) place ANA_0154 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.Residues 124 to 152 (E_value = 1e-08) place ANA_0154 in the Glyco_hydro_70 family which is described as Glycosyl hydrolase family 70.",""," ","","1","","","","","","","","","","","","","Thu Aug 16 12:51:06 2007","Thu Aug 16 12:51:06 2007","","Thu Aug 16 12:51:06 2007","Thu Aug 16 12:51:06 2007","Thu Aug 16 12:51:06 2007","","Thu Aug 16 12:51:06 2007","Thu Aug 16 12:51:06 2007","","","","","yes","","" "ANA_0155","173888","174481","594","4.78","-10.14","20507","ATGCCCGCTTTCCATGCGCCCACCGATCAGAGGACCGACAAGGCCGTCGCCGTCTTCATCGCCCCCGGGCTGGAGGAGGTCGAGGCGCTGGCGACCGTGGACATCCTCTTCCGCGCCGGTATCCCCACGACGATGATCTCTGTGACTCCCGAGCGGGCCGTCGTCTCCTCCCACAACATCGTCGTCACCTGTGACCTCGCCCTGGCCGAGGCGAACCTGGACGACTACGACATGCTCGTCCTGCCCGGCGGCATCCCCGGCACCCCCAACCTCAAGGCCGTCGAGCCCCTCATGGCCGCGGTCACCGAGCGGGTGCGCACCGGCCGGCCCGTGGCCGCGATCTGCGCCGCCCCCTCGATCCTGGCCGAGCTGGGCCTGCTCGAGGGCCGCCAGGCGACGTCGAACCCCGGCTTCGTGGGCGTGCTCGCCGAGCACGGCGCGCAGGTCAGCCAGGCCGCCGTCGTCACAGACGGCCCCGTCATCACCTCCCGCGGCATGGGAACCGCCATCGACTTCGGCTTGGAGATCGTGCGCCACTACCTGGGCGAGGAGGCCGTCGACGACGTCAAGGCCAAGATCGTCTACCAGGGCTGA","MPAFHAPTDQRTDKAVAVFIAPGLEEVEALATVDILFRAGIPTTMISVTPERAVVSSHNIVVTCDLALAEANLDDYDMLVLPGGIPGTPNLKAVEPLMAAVTERVRTGRPVAAICAAPSILAELGLLEGRQATSNPGFVGVLAEHGAQVSQAAVVTDGPVITSRGMGTAIDFGLEIVRHYLGEEAVDDVKAKIVYQG$","ThiJ family intracellular protease/amidase","Cytoplasm","4-methyl-5(beta-hydroxyethyl)-thiazolemonophosphate synthesis protein","K03152 4-methyl-5(b-hydroxyethyl)-thiazole monophosphate biosynthesis","DJ-1 family protein","","Nagakubo D., Taira T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M., Ariga H. DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras. Biochem. Biophys. Res. Commun. 1997. 231(2):509-513. PMID: 9070310Mizote T., Tsuda M., Nakazawa T., Nakayama H. The thiJ locus and its relation to phosphorylation of hydroxymethylpyrimidine in Escherichia coli. Microbiology 1996. 142:2969-2974. PMID: 8885414","","","

InterPro
IPR002818
Domain

ThiJ/PfpI
PF01965	$\"[42-181]T$	DJ-1_PfpI

InterPro
IPR006287
Family

DJ-1
TIGR01383	$\"[15-192]T$	not_thiJ: DJ-1 family protein

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[11-197]T$	no description
PTHR11019	$\"[47-194]T$	THIJ/PFPI
PTHR11019:SF4	$\"[47-194]T$	THIJ-RELATED

","BeTs to 15 clades of COG0693COG name: Putative intracellular protease/amidaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0693 is aompkzyq-dr-bcefghs-uj--twNumber of proteins in this genome belonging to this COG is 2","***** IPB002818 (Family of unknown function ThiJ/PfpI) with a combined E-value of 1.9e-07. IPB002818A 75-86 IPB002818B 111-121","Residues 14-178 are 63% similar to a (PROTEASE MONOPHOSPHATE FAMILY BIOSYNTHESIS THIJ/PFPI INTRACELLULAR 4-METHYL-5B-HYDROXYETHYL-THIAZOLE ENZYME I HYDROLASE) protein domain (PD002258) which is seen in Q8XIP8_CLOPE.Residues 14-189 are 54% similar to a (P0665D10.11) protein domain (PD297664) which is seen in Q9FTQ5_EEEEE.","","-53% similar to PDB:2AB0 Crystal Structure of E. coli protein YajL (ThiJ) (E_value = 2.9E_21);-52% similar to PDB:1P5F Crystal Structure of Human DJ-1 (E_value = 3.2E_20);-52% similar to PDB:1PDV Crystal structure of human DJ-1, P 31 2 1 space group (E_value = 3.2E_20);-52% similar to PDB:1PDW Crystal structure of human DJ-1, P 1 21 1 space group (E_value = 3.2E_20);-52% similar to PDB:1PS4 crystal structure of DJ-1 (E_value = 3.2E_20);","Residues 42 to 181 (E_value = 1.3e-28) place ANA_0155 in the DJ-1_PfpI family which is described as DJ-1/PfpI family.","","monophosphate synthesis protein (D39747)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0156","174932","174561","372","7.93","1.55","13295","ATGGTTGAGACAGCATGCTCCGTACTCATGAGCCTGATCCTGAGCGTGACCGGCATCCTCCTCGTGGTGCTGGGACGCCGGATGGCGAAGCGCAGGCTCCCGCCGAACTCGTGGGCGGGAGTGCGTTACGAGATCGCGCTGCACTCCGAGGAGAACTGGTACACGATGCAGGCCTGGTGCGCGGCGGCGACTGTGGGACTGGGTGTGGTTCTCCTCGACTCAGCAGTCCTCTTCGCCGTTCAGGCGGCCATGCATGAGACGATCTCGATCCTGATCCCCATGGCCATCATGCTGGTTCAGATGGCTGCCGGTATCGCATTCCTTCACGTTCAGGCCCGCAGGTGCGCCGCGGAGCTGACACAGAGCGCATAG","MVETACSVLMSLILSVTGILLVVLGRRMAKRRLPPNSWAGVRYEIALHSEENWYTMQAWCAAATVGLGVVLLDSAVLFAVQAAMHETISILIPMAIMLVQMAAGIAFLHVQARRCAAELTQSA$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[58-80]?$ $\"[90-110]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-48% similar to PDB:1V4V Crystal Structure Of UDP-N-Acetylglucosamine 2-Epimerase From Thermus Thermophilus HB8 (E_value = );-60% similar to PDB:2NN6 Structure of the human RNA exosome composed of Rrp41, Rrp45, Rrp46, Rrp43, Mtr3, Rrp42, Csl4, Rrp4, and Rrp40 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0157","175606","175109","498","4.56","-7.08","16514","ATGAGCAGCACCTCTTCCACGACGTCGCCCGACGACGCCGGCAGCACCAGCACCGAGGCGACCGGCGAGGACGCCACCAGGCCCTTCCCTGCCGCCGGAGACACCCAGCCCCTGACCTCACCGGTGACTCAGCCCGCGGCTGAGCCAGCAGTTGAACCGGAGACTCAGCCGGTCACCATGCCACTGCCCACCTCCGAGGAGGCCGGTGCGGAGGCGGCGTCCACGGACTCGGCGCCTGCGTCCTCGACGCCCGGCCCGGTGTGGAGCGCCGGGACGATCGCCGACCGGGACCGACCTCAGGCACCCCAGGACATCAAGGGCTCGACTCTCCTGTGGGGGGCCTTCCTGCTCCTGGTGGGTGGACTGCTCATCGCGGCGGGCCTGGGGCTGCGCTTCGACTTCACGACGACGGCCATCGCCTGCCTGGCGGGTCTGGGGGTTCTGCTCGTGGTCGCCGCCCTCATCCCTAAGGGGCGCCGCAGCGCCAAGAAGTCCTGA","MSSTSSTTSPDDAGSTSTEATGEDATRPFPAAGDTQPLTSPVTQPAAEPAVEPETQPVTMPLPTSEEAGAEAASTDSAPASSTPGPVWSAGTIADRDRPQAPQDIKGSTLLWGAFLLLVGGLLIAAGLGLRFDFTTTAIACLAGLGVLLVVAALIPKGRRSAKKS$","Possible membrane receptor","Membrane, Periplasm, Extracellular","EPPT protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[109-131]?$ $\"[137-155]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-67% similar to PDB:2GRX Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0158","177744","175681","2064","7.12","0.58","72322","ATGAACGACAAGCCCACTTCCCCGTCTGACGGTGGTTCCCCCACCGGTTCCGATTCCTCTGACTCCTCCGCATCCTTCCCCTCTTCCAACACACAGGGTGCCGACGGCGCCCAGCGCGATTCCCGGCAGGGAGCGCAGCACGGACCGCAGCCGGGTCCCGCGCCCTCCTTCCAGCAGTACGGCGGCCCCCAGCCCGGGCCTCAGGGCGGATCGACTCACCGCTTCTTCGACTCCCTGCGCGGCTCGGGCCTCATGCGCACCAATGAGCGCTGGGTCGCGGGCGTGGCCGGTGGCGTGGCCTACCGCTTCGACCTGGACCCCACCCTGGTGCGTTGCGTGTGGGTGGTGCTCTCGCTCTTCGCCGGTGTCGGGCTGGTCCTCTACGGCATGGCCTGGGCCCTTCTGCCCGAGGAGTCCGATGGGCGCATCCACCTGGAGGAGGCCCTCTCCGGCCGTTTCAACGCAGGGCTGGCGGGCGCCATCGGGATGACGATCATCGGTATGTCGACATTCGGTAGCGGTTTCATCCCCAACTGGTACGTCCATGAGGCGGGGATCGCCGCCGCCCTGTGGCCCCTGTTCTGGCTGGGGCTGTTCATCCTCGGCATCGTCTTCCTCATCCGCCGCGCCCAGGACCGGCGCGCGCGCCGGAAGGCCGCTCGAGGCCCTCGGGGCCCCCAGCCCTGGCAGGCCCCCGCTCCCGGTGCCGCGCAGACACCGGGCAGCCGCCCCGGCGTCCAGGCCGGCGGCTTCGCATCGGCCTGGGACTCCTCAGCGCCCGGCTCCGGCACCCCGGCCTTCAACCAGTCGGCCGGCGGACAGAGCTGGCAGAGCCGCTCCTACCGGCAGCGCCCGCCGTACCAGCCAATGCCTATGCCGGTCCGCCCGGCGCGCCCGCGCCGTCCCGGCCCCGGTTCCTCACTGTCGCTGGCGGTCCTGGGGCTGGGGCTCCTGACCGCGGCGGGCGTCTGGTACGCCACGGTGACCCACCACCTGGGTCTGCTCCAGGGTCAGTTCATCCTCATCGGCATCCTGGTCGCCCTCCTGGGAGCGGGCATCGTCGTCAGTGGCCTGCGTCGTCGGCACGGAGGCTGGATGACGGTGCTGGGCTGGCCGGTCCTGTTCGTCGTTGCGATCCCCGCGCTGGCCACCGCCTCGATCGTCCCCACGAGCCTGGCCCGCATGCCCTTCGAGAGCCTCAGGAACGCAACCACCGCCACCTCGAGCACGGTGACCTGGCAGGAGCTGACGGCATCGGCCAGCAGCGGCAGCGTCACCCGCAACAAGGACATTGGTGACCTCACCCTGGATCTGCGCGGCATGCCCGCCACGGAGGCCAGCAAGCTCTCCACCATCACCACCCACCTCGACGTCGGCACCCTGCGCATCAAGACCGACACCGACCAGCGGGTGGAGGTCAGGGCCGACGTCGACATGGGAGCGATCGACTCACAGGTCTCCCGGGCCTGGACCGTCAACGGCCGCCAGATGAATCAGGACGACGAGGGCCCACGCACCTATGACGCGACTGGCAAGACCATCCCCGCTTACAGCAACTCCAGCGGCGGGCTGAACACCAAGCGCACCCTGGCCTCCCCCAACAGTGACGACCAGCGGCCGCAGATCACCATCAACGCCTCGGTGGACACCGGGACGATCAACATCGAGGAGCGCAGCAACACCGCCTCCTGGTACGGCAACGTCGAGGAGCCCGTGTGGATCGTCAGCATGTGGTTCGACGAGAAGGGCGATGCCCACGGTGACGACCTGCCAGTTCCGGGCATGAACCACCCGGCCATCACGGCCAAGGACGCTGAGACCTGCATCCGCACGGCCCACGAGAGCGTGAACGAGGACGACCGCAGCGAGGACGTCGGGTGGAGCAACCTGTCCGACCTGACCTCTGCGGAGCGTGCCTCCTACGACTCCTGCGTGCAAAGGGCCCTGTCCGGGCAGGGAGCCGCGCAGCCCAGTGCGAGCCCGAGCCCCTCCGGGGCGGCCGCTGCGACACCGTCCCCGACTCCCACCAAGCAGTCCGCTACGGCCAGCCCGACAGCCGGCTGA","MNDKPTSPSDGGSPTGSDSSDSSASFPSSNTQGADGAQRDSRQGAQHGPQPGPAPSFQQYGGPQPGPQGGSTHRFFDSLRGSGLMRTNERWVAGVAGGVAYRFDLDPTLVRCVWVVLSLFAGVGLVLYGMAWALLPEESDGRIHLEEALSGRFNAGLAGAIGMTIIGMSTFGSGFIPNWYVHEAGIAAALWPLFWLGLFILGIVFLIRRAQDRRARRKAARGPRGPQPWQAPAPGAAQTPGSRPGVQAGGFASAWDSSAPGSGTPAFNQSAGGQSWQSRSYRQRPPYQPMPMPVRPARPRRPGPGSSLSLAVLGLGLLTAAGVWYATVTHHLGLLQGQFILIGILVALLGAGIVVSGLRRRHGGWMTVLGWPVLFVVAIPALATASIVPTSLARMPFESLRNATTATSSTVTWQELTASASSGSVTRNKDIGDLTLDLRGMPATEASKLSTITTHLDVGTLRIKTDTDQRVEVRADVDMGAIDSQVSRAWTVNGRQMNQDDEGPRTYDATGKTIPAYSNSSGGLNTKRTLASPNSDDQRPQITINASVDTGTINIEERSNTASWYGNVEEPVWIVSMWFDEKGDAHGDDLPVPGMNHPAITAKDAETCIRTAHESVNEDDRSEDVGWSNLSDLTSAERASYDSCVQRALSGQGAAQPSASPSPSGAAAATPSPTPTKQSATASPTAG$","Phage shock protein C, PspC","Membrane, Periplasm","PspC domain family","phage shock protein C; PspC","PspC domain protein","","","","","

InterPro
IPR007168
Domain

PspC
PF04024	$\"[81-140]T$	PspC

noIPR
unintegrated

unintegrated
tmhmm	$\"[114-136]?$ $\"[157-177]?$ $\"[187-207]?$ $\"[308-328]?$ $\"[338-358]?$ $\"[368-388]?$	transmembrane_regions

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[362-453]T$	HATPase_c
SM00387	$\"[362-454]T$	HATPase_c

InterPro
IPR007168
Domain

PspC
PF04024	$\"[53-109]T$	PspC

noIPR
unintegrated

unintegrated
tmhmm	$\"[81-101]?$ $\"[150-170]?$ $\"[175-193]?$ $\"[207-227]?$ $\"[236-258]?$	transmembrane_regions

","BeTs to 7 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 9.4e-13. IPB011712A 275-292 IPB011712B 367-387 IPB011712C 401-410","Residues 190-357 are 55% similar to a (KINASE SENSOR SYSTEM TWO-COMPONENT COMPONENT TWO HISTIDINE KINASES TRANSDUCTION SYSTEM) protein domain (PD323223) which is seen in Q9KY73_STRCO.Residues 374-451 are 70% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM SENSORY TRANSFERASE TRANSDUCTION 2.7.3.- TWO) protein domain (PD005700) which is seen in Q8G3V7_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 53 to 109 (E_value = 1.5e-09) place ANA_0159 in the PspC family which is described as PspC domain.Residues 362 to 453 (E_value = 2e-11) place ANA_0159 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","histidine kinase sensor of two component system","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0160","179249","180034","786","5.85","-8.22","27542","TTGCTTTGTCTCCTTGGGCCGCACCCGGCCCCTCACTCCTCGATCACCCCACGTCATCACCAGGAAGACCCCATGGCTGACACGCCCGCCGGTACCACCACAGACCACCACCAGCCCGCCGATGCGAGCGCGTCCCTGCGGGTCCTGGTCGTCGACGACCACGCCCTGGTCCGCTCCGGGGTGCGCTCCGAGCTGACCGCCCACGCCCCCGACCTCGACGTCATCGCCGAGGCCGACGACGTCGAGGGCGCCATCGCCGCCGTCCACGCCCTGCGGCCCGACGTCGTCCTGCTCGATGTCCACCTGCCCGGCGGCAACGGCGGGGGAGGGGCCGAGGTCGTCGCCTCCTGCCACGACGTCCCCGAGACGCGCTTCCTGGCCCTGAGCGTCTCGGACGCCAGCGACGACGTCGTCGGCGTCATCCGGGCCGGCGCCCGCGGCTACGTCACCAAGGCGATCTCCACCGAGGACCTGGCCCAGGCCGTGCGGCGTGTGGCCGCTGGAGACGCCGCCTTCTCCCCGCGCCTGGCCGGATTCGTCCTGGACGCCTTCGGTGCCGGAGCGGGCGAGGTGGCCGTGGCCGACACCGAGCTCGACCGCCTCTCGGCGCGCGAGCGGGAGGTCATGCGACTCATCGCCCGCGGCTACACCTACAAGGAGTGCGCCTCCGAGCTGTTCATCTCGGTCAAGACCGTCGAGACCCACGTCTCCGCGGTCCTGCGCAAGCTCCAGCTGTCCAACCGCAACGAGCTCACCCGCTGGGCCGTGGCCCGCCGCATCGTGTAG","LLCLLGPHPAPHSSITPRHHQEDPMADTPAGTTTDHHQPADASASLRVLVVDDHALVRSGVRSELTAHAPDLDVIAEADDVEGAIAAVHALRPDVVLLDVHLPGGNGGGGAEVVASCHDVPETRFLALSVSDASDDVVGVIRAGARGYVTKAISTEDLAQAVRRVAAGDAAFSPRLAGFVLDAFGAGAGEVAVADTELDRLSAREREVMRLIARGYTYKECASELFISVKTVETHVSAVLRKLQLSNRNELTRWAVARRIV$","Two-component system response regulator","Cytoplasm","response regulator of two-component system","putative two-component system response regulator","regulatory protein, LuxR","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[200-258]T$	Q8G3V8_BIFLO_Q8G3V8;
PR00038	$\"[201-215]T$ $\"[215-231]T$ $\"[231-243]T$	HTHLUXR
PF00196	$\"[198-255]T$	GerE
SM00421	$\"[198-255]T$	HTH_LUXR
PS50043	$\"[194-259]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[46-165]T$	Q6NJ16_CORDI_Q6NJ16;
PF00072	$\"[46-163]T$	Response_reg
SM00448	$\"[46-162]T$	REC
PS50110	$\"[47-166]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[190-261]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[33-179]T$	no description
PTHR23283	$\"[38-170]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF40	$\"[38-170]T$	TWO-COMPONENT SENSOR HISTIDINE KINASE BACTERIA

InterPro
IPR004388
Domain

Sua5/YciO/YrdC/YwlC
TIGR00057	$\"[12-237]T$	TIGR00057: Sua5/YciO/YrdC/YwlC family prote

InterPro
IPR006070
Domain

SUA5/yciO/yrdC, N-terminal
PF01300	$\"[27-225]T$	Sua5_yciO_yrdC
PS51163	$\"[19-227]T$	YRDC

InterPro
IPR012200
Family

RNA-binding protein, YrdC
PIRSF004931	$\"[18-235]T$	RNA-binding protein, YrdC type

noIPR
unintegrated

unintegrated
G3DSA:3.90.870.10	$\"[7-240]T$	no description
PTHR17490	$\"[32-171]T$ $\"[192-252]T$	SUA5

","No hits to the COGs database.","***** IPB006070 (SUA5/yciO/yrdC, N-terminal) with a combined E-value of 2.3e-24. IPB006070A 29-72 IPB006070B 143-155***** IPB004388 (Sua5/YciO/YrdC/YwlC protein family) with a combined E-value of 1.3e-22. IPB004388A 34-63 IPB004388B 94-104 IPB004388C 146-156","Residues 1-232 are 41% similar to a (SUA5-RELATED) protein domain (PD260139) which is seen in Q9RTA3_DEIRA.Residues 4-237 are 41% similar to a (SPCC895.03C) protein domain (PD977854) which is seen in O94530_SCHPO.Residues 5-148 are 45% similar to a (GLP_680_34352_35572) protein domain (PDA1D445) which is seen in Q7QZP0_EEEEE.Residues 5-237 are 47% similar to a (TRANSLATION FACTOR) protein domain (PDA187I4) which is seen in Q7UPX2_RHOBA.Residues 15-148 are 52% similar to a () protein domain (PDA199K3) which is seen in Q6AL59_BBBBB.Residues 16-237 are 48% similar to a (SSO0664 ORF-C09_003) protein domain (PDA189O4) which is seen in Q9UX54_SULSO.Residues 16-237 are 50% similar to a (SUA5 TRANSLATION FACTOR) protein domain (PD977850) which is seen in Q8RD96_THETN.Residues 16-139 are 53% similar to a (SE1713) protein domain (PD977849) which is seen in Q8CRN1_STAEP.Residues 17-237 are 46% similar to a (SUA5 SUPERFAMILY-RELATED) protein domain (PD977847) which is seen in Q6L0H3_PICTO.Residues 17-233 are 46% similar to a () protein domain (PD977851) which is seen in Q9WZV6_THEMA.Residues 20-237 are 45% similar to a (SUA5 RELATED) protein domain (PD977848) which is seen in Q9HLC7_THEAC.Residues 20-148 are similar to a (FAMILY TRANSLATION SUA5/YCIO/YRDC/YWLC FACTOR SUA5/YCIO/YRDC SUA5 YRDC CASUA5 YCIO CANDIDA) protein domain (PD329321) which is seen in Q6A8B7_PROAC.Residues 22-148 are 62% similar to a (CPE2200) protein domain (PD977844) which is seen in Q8XIC1_CLOPE.Residues 22-240 are 45% similar to a () protein domain (PD977845) which is seen in Q8EM64_OCEIH.Residues 22-240 are 45% similar to a (SMC00984) protein domain (PDA18780) which is seen in Q92RK2_RHIME.Residues 22-148 are 57% similar to a (SUA5) protein domain (PD977853) which is seen in Q898Y2_CLOTE.Residues 22-142 are 62% similar to a (SUA5 TRANSLATION PREDICTED FACTOR) protein domain (PD977852) which is seen in Q97F70_CLOAB.Residues 25-237 are 47% similar to a (SUA5/YCIO/YRDC FAMILY) protein domain (PD977855) which is seen in Q9A316_CAUCR.Residues 28-148 are 53% similar to a (GLR3274) protein domain (PDA1A2G3) which is seen in Q7NG99_GLOVI.Residues 29-237 are 50% similar to a (YWLC) protein domain (PD977846) which is seen in YWLC_BACSU.Residues 29-240 are 50% similar to a (SUA5/YCIO/YRDC/YWLC DOMAIN FAMILY:SUA5) protein domain (PDA185X9) which is seen in Q6NAV3_RHOPA.","","-44% similar to PDB:1JCU Solution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicum (E_value = 9.4E_16);","Residues 27 to 225 (E_value = 2.7e-45) place ANA_0161 in the Sua5_yciO_yrdC family which is described as yrdC domain.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0162","180939","182189","1251","9.97","10.53","43939","GTGAAGGTCTACCTCCTGGTCATGGCCATTGCTGCGGCGACCACCTACGTGGCCGTGCCGATCATCCGGCACATCGCCCTGGTGGGTAACGCGCTGACCCCCGTGCGGGCCCGCGACGTCCACTCCACGCCCATCCCACGCCTGGGCGGCGTGGCCATGTTCTTCGGCCTGTTCTCAGCGATCTCCGTGGCCTCCACGATCCCCTACCTCTCCGACGTCATCGACTCCAGTGCCTGGGCGGTGGTCCTGGGGGCGGGACTGGTGTGCCTGCTCGGCGTCGTCGACGACCTGTGGGAGCTGGACTGGATGACCAAGCTCGCCGGCCAGATCCTAGCCGCCGGCGTTATGGCCTGGCAGGGCGTCCAGCTCCTCACCTTCCCGGTGGCCGGGCTGACGATCGGCTCCTCGCGCCTGTCCCTCATCTCCACCGTCATCGTCGTGGTGGCCGCCATCAACGCCGTCAACTTCGTCGACGGGCTCGACGGGCTCGCGGCCGGCATCATCGGGATCGGCTCGACCGCCTTCTTCCTGTACACCTACGTCTTGACCCGCGCCACGAGCCCGGGCTCCTACAGCTCCCTGGCCGCCACCATCGTGGCCGCGCTCATCGGCGTGTGCGTGGGCTTCCTGCCCCACAACTTCAACCCCGCCACCATCTTCATGGGCGACTCCGGGGCGATGCAGCTGGGACTGGTCTCAGCCGCCTCCACCATCATCGTCACCGGGCAGATCGACCCCGGCAGCTTCGACGGCTCGCGCGCCCTGCCCGCCTTCATGCCGATCCTCCTGCCATTGGCGGTCCTCCTGCTGCCACTGACCGACATGATGATGGCGATCGTGCGCCGCACCCGGAAGGGGCTGAGTCCCACCCACCCCGACCGCATGCACATGCACCACCGGCTCCTGGCCGCCGGGCACTCCCACCGCCGCGCGGTGCTGGTCATGTACCTGTGGGCGGCGGTCGCCTCCTTCCCCGTGGCCGCCATGGCCTTCTTCCCCCTGCCCTGGGTGCTGGCGGGGCTCGCCCTCGCGGTGCTGTTCGCCTTCGTCGTCACCGTCGACCTCATGCCCGGGGTGCGCCACGGCCTGCGCTCGGCGCTGCGCCGTCGCCAGGACCGCCCCGAGCAGCGGATCGTCATCTCCCGCAACGTCTCAGGAACTGGTGAAGTGACGCGCCCGGCCGAGGGGCAGGCGCCGCAGGGGAACGCCCTGCAGGTGTCGCACGGTTCGCCTGAAAGGACCCGCCAGTGA","VKVYLLVMAIAAATTYVAVPIIRHIALVGNALTPVRARDVHSTPIPRLGGVAMFFGLFSAISVASTIPYLSDVIDSSAWAVVLGAGLVCLLGVVDDLWELDWMTKLAGQILAAGVMAWQGVQLLTFPVAGLTIGSSRLSLISTVIVVVAAINAVNFVDGLDGLAAGIIGIGSTAFFLYTYVLTRATSPGSYSSLAATIVAALIGVCVGFLPHNFNPATIFMGDSGAMQLGLVSAASTIIVTGQIDPGSFDGSRALPAFMPILLPLAVLLLPLTDMMMAIVRRTRKGLSPTHPDRMHMHHRLLAAGHSHRRAVLVMYLWAAVASFPVAAMAFFPLPWVLAGLALAVLFAFVVTVDLMPGVRHGLRSALRRRQDRPEQRIVISRNVSGTGEVTRPAEGQAPQGNALQVSHGSPERTRQ$","Glycosyl transferase, family 4","Membrane, Cytoplasm, Extracellular","possible undecaprenyl-phosphatealpha-N-acetylglucosaminyltransferase","putative teichoic acid linkage unit synthesis (synthesis of undecaprenylpyrophosphate-N-aetylglucosamine ) ","glycosyl transferase, family 4","","","","","

InterPro
IPR000715
Family

Glycosyl transferase, family 4
PTHR22926	$\"[23-370]T$	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
PF00953	$\"[78-243]T$	Glycos_transf_4

noIPR
unintegrated

unintegrated
PTHR22926:SF2	$\"[23-370]T$	GLYCOSYL TRANSFERASE
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[51-71]?$ $\"[76-94]?$ $\"[108-128]?$ $\"[138-156]?$ $\"[162-182]?$ $\"[191-211]?$ $\"[252-272]?$ $\"[313-333]?$ $\"[339-359]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[51-71]?$ $\"[83-103]?$ $\"[117-137]?$	transmembrane_regions

InterPro
IPR000568
Family

ATPase, F0 complex, subunit A
PR00123	$\"[125-141]T$ $\"[210-232]T$ $\"[270-285]T$	ATPASEA
PTHR11410	$\"[88-261]T$	ATP SYNTHASE SUBUNIT 6
PF00119	$\"[59-285]T$	ATP-synt_A
TIGR01131	$\"[49-287]T$	ATP_synt_6_or_A: ATP synthase F0, A subunit

InterPro
IPR006162
PTM

Phosphopantetheine attachment site
PS00012	$\"[242-257]?$	PHOSPHOPANTETHEINE

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[64-84]?$ $\"[123-143]?$ $\"[149-171]?$ $\"[214-234]?$ $\"[240-260]?$ $\"[265-283]?$	transmembrane_regions

","BeTs to 16 clades of COG0356COG name: F0F1-type ATP synthase a subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0356 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB000568 (H+-transporting two-sector ATPase, A subunit) with a combined E-value of 2.7e-31. IPB000568A 122-163 IPB000568B 188-232 IPB000568C 263-285","Residues 119-194 are 72% similar to a (ION CF0 TRANSMEMBRANE HYDROGEN A ATP SYNTHASE SUBUNIT CHAIN CHLOROPLAST) protein domain (PD866702) which is seen in Q6AG64_BBBBB.Residues 201-241 are 78% similar to a (ION CF0 TRANSMEMBRANE HYDROGEN ATP A SYNTHASE SUBUNIT CHAIN ATPASE) protein domain (PD010746) which is seen in Q6AG64_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 59 to 285 (E_value = 1e-33) place ANA_0164 in the ATP-synt_A family which is described as ATP synthase A chain.","","synthase F0, A subunit (atpB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0165","183806","184015","210","8.66","0.91","6983","ATGTCCCTCACCGCGCTCGCATACGTCGGCTACGGCCTGGCCACGCTCGGCCCGGGCATCGGCATCGGCCTGCTCGTCGGCAAGACCCAGGAGGCCACGGCCCGTCAGCCCGAGGTGGCCGGACGCCTGTTCACCAACATGATTATCGGCGCGGGCATGGTCGAGGCCCTCGGCCTCATCGGCTTCGTCCTTCCGCTCGTCGTCAAGTGA","MSLTALAYVGYGLATLGPGIGIGLLVGKTQEATARQPEVAGRLFTNMIIGAGMVEALGLIGFVLPLVVK$","ATP synthase F0, C subunit","Membrane, Extracellular","H+-ATPase c subunit","hypothetical protein predicted by Glimmer/Critica","ATP synthase F0, C subunit","","Cross R.L., Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004. 576(1):1-4. PMID: 15473999Rappas M., Niwa H., Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci 2004. 5(2):89-105. PMID: 15078220Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001. 410(6831):898-904. PMID: 11309608Wilkens S., Zhang Z., Zheng Y. A structural model of the vacuolar ATPase from transmission electron microscopy. Micron 2005. 36(2):109-126. PMID: 15629643Fillingame R.H., Angevine C.M., Dmitriev O.Y. Mechanics of coupling proton movements to c-ring rotation in ATP synthase. FEBS Lett. 2003. 555(1):29-34. PMID: 14630314Inoue T., Forgac M. Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain. J. Biol. Chem. 2005. 280(30):27896-27903. PMID: 15951435Harrison M., Durose L., Song C.F., Barratt E., Trinick J., Jones R., Findlay J.B. Structure and function of the vacuolar H+-ATPase: moving from low-resolution models to high-resolution structures. J. Bioenerg. Biomembr. 2003. 35(4):337-345. PMID: 14635779","","","

InterPro
IPR000454
Family

ATPase, F0 complex, subunit C
PR00124	$\"[6-25]T$ $\"[27-42]T$ $\"[44-69]T$	ATPASEC
PS00605	$\"[34-55]T$	ATPASE_C

InterPro
IPR002379
Family

ATPase, F0/V0 complex, subunit C
G3DSA:1.20.20.10	$\"[1-67]T$	no description
PF00137	$\"[6-63]T$	ATP-synt_C

InterPro
IPR005953
Family

ATPase, F0 complex, subunit C, bacterial and chloroplast
TIGR01260	$\"[14-68]T$	ATP_synt_c: ATP synthase F0, C subunit

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[48-68]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB000454 (Eubacterial/plasma membrane H+-transporting two-sector ATPase, C subunit) with a combined E-value of 2.3e-26. IPB000454 10-64","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 69 (E_value = 1.3e-16) place ANA_0165 in the ATP-synt_C family which is described as ATP synthase subunit C.","","c subunit (atpE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0167","184012","184599","588","4.76","-10.02","21036","GTGATGCTTCCCCTGGCTGCCGAGGGCGGGCAGGGCGGAGGCACAGCCTTCATCCTTCCCCCGCTCTATGAGATCTTCTGGGCGGCGATCGTCCTCCTGCTCATCCTCCTGGTGGTGGGCCGCTACGCCCTGCCCCGGCTCTACGCCGTGCTGGACGAGCGGGCCCAGCGCATCCAGGAGGGCCTCGACCTGGCCGACAAGGCCAAGCAGGACCAGGCCGACGCCGAGAAGCGCGCCACCCGGCTCGTGGACGAGGCCCGTCGCGAGGCCGCCCGCATCCGCGACAACGCCCAGGGCGAGGCCAAGGAGATCGTCGCCAAGGCCCGCGCCGACGCCCAGGCGGAGGCCGCCGGCATCATCGAGGGCGCTCAGCGTCAGATCCTGGCCGAGAAGCAGGCCGCGCAGATCTCGCTGCGCACCGACGTCGGCATGCTCGCCTCCACCCTGGCCGAGCGCATCGTTGGTGAGCAGCTGAGCGACACCGCCCTGTCTGAGCGGGTCATCGACCGCTTCCTCGACGAGCTCGAGACCATGGAGTCGGTCGATGGGCTCGACGCCGTCGCCTCCTCTGCGGAGGCGACGCGGTGA","VMLPLAAEGGQGGGTAFILPPLYEIFWAAIVLLLILLVVGRYALPRLYAVLDERAQRIQEGLDLADKAKQDQADAEKRATRLVDEARREAARIRDNAQGEAKEIVAKARADAQAEAAGIIEGAQRQILAEKQAAQISLRTDVGMLASTLAERIVGEQLSDTALSERVIDRFLDELETMESVDGLDAVASSAEATR$","ATP synthase F0, B subunit","Cytoplasm, Membrane","protein with similarity to ATP synthase B chain","ATP synthase F0; B subunit","ATP synthase F0, B subunit","","Cross R.L., Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004. 576(1):1-4. PMID: 15473999Rappas M., Niwa H., Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci 2004. 5(2):89-105. PMID: 15078220Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001. 410(6831):898-904. PMID: 11309608Carbajo R.J., Kellas F.A., Runswick M.J., Montgomery M.G., Walker J.E., Neuhaus D. Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005. 351(4):824-838. PMID: 16045926","","","

InterPro
IPR002146
Family

ATPase, F0 complex, subunit B/B', bacterial and chloroplast
PF00430	$\"[24-155]T$	ATP-synt_B

InterPro
IPR005864
Family

ATPase, F0 complex, subunit B, bacterial
TIGR01144	$\"[28-175]T$	ATP_synt_b: ATP synthase F0, B subunit

noIPR
unintegrated

unintegrated
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[19-39]?$	transmembrane_regions

","BeTs to 7 clades of COG0711COG name: F0F1-type ATP synthase b subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0711 is -------qv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB002146 (sub) with a combined E-value of 5e-11. IPB002146 30-80","Residues 132-195 are 64% similar to a (CF0 SYNTHASE HYDROGEN CHAIN ION ATP TRANSMEMBRANE B I SUBUNIT) protein domain (PD887585) which is seen in Q9K4D7_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 155 (E_value = 5.8e-20) place ANA_0167 in the ATP-synt_B family which is described as ATP synthase B/B' CF(0).","","with similarity to ATP synthase B chain","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0168","184809","185411","603","7.57","1.36","22159","GTGGACGAGCGCGTCGTCGACCTGCTCAGCGCCATGGTCCGCGGCCGCTGGTCCAAGGCAGTCGACCTGGTCTCCGCCCTCCACGACCTGGGCATCGAGGCGATCCTCGCCGGCGCCCACGCGGGCGGCTCGGCGGAGGAGATCGAGCAGCAGCTCTTCGAGGTCCACGAGCAGATCGCCGACAACCGCGAGCTGCGCGAGGCCCTGACCCCCTCACGCCGCACCAGTACCGAGGCCCGGGTCCGCCTGGCCGAGTCCGTCTTCGCGCCCCACATCAGCGCCCCCGCCATGAGCCTGGTGAACTGGTGCGTGCGGCACCACGCCGAGGGCGGACCTCTGCGCAACCTGCGCCGCGTCGTCGAGCTGGCCGCCGAGATGCGCCGGCGCACCATCGTCGACGTCGTCACCGCCATCCCCATGACCTCCGCCCAGGAGGAGCGCCTGCGCACCATCCTGGAGCGCCGCCTGGGCACCAGGATCGACCTCAACTGCGAGGTCGACTCCGCGGTCATCGGCGGAGCCCGCATCTCGACGCGGAACTACGTCATGGACCGCACCGTGCGCAGCGCCGTCGCCGAGCTGCGCACCCGCCTGGCGGGCTAG","VDERVVDLLSAMVRGRWSKAVDLVSALHDLGIEAILAGAHAGGSAEEIEQQLFEVHEQIADNRELREALTPSRRTSTEARVRLAESVFAPHISAPAMSLVNWCVRHHAEGGPLRNLRRVVELAAEMRRRTIVDVVTAIPMTSAQEERLRTILERRLGTRIDLNCEVDSAVIGGARISTRNYVMDRTVRSAVAELRTRLAG$","ATP synthase F1, delta subunit","Cytoplasm","ATP synthase F1, delta subunit","ATP synthase F1; delta subunit","ATP synthase F1, delta subunit","","Cross R.L., Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004. 576(1):1-4. PMID: 15473999Rappas M., Niwa H., Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci 2004. 5(2):89-105. PMID: 15078220Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001. 410(6831):898-904. PMID: 11309608Carbajo R.J., Kellas F.A., Runswick M.J., Montgomery M.G., Walker J.E., Neuhaus D. Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005. 351(4):824-838. PMID: 16045926","","","

InterPro
IPR000711
Family

ATPase, F1 complex, OSCP/delta subunit
PTHR11910	$\"[34-199]T$	ATP SYNTHASE DELTA CHAIN
PF00213	$\"[132-198]T$	OSCP
TIGR01145	$\"[27-198]T$	ATP_synt_delta: ATP synthase F1, delta subu

","BeTs to 7 clades of COG0712COG name: F0F1-type ATP synthase delta subunit (mitochondrial oligomycin sensitivity protein)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0712 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 1-83 are 54% similar to a (ATP DELTA HYDROLASE CF1 SYNTHESIS SYNTHASE CHAIN SUBUNIT H-ATPASE HYDROGEN) protein domain (PD035418) which is seen in Q9K4D6_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 33 to 198 (E_value = 0.00014) place ANA_0168 in the OSCP family which is described as ATP synthase delta (OSCP) subunit.","","synthase F1, delta subunit (atpH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0169","185517","187148","1632","5.01","-20.31","58791","ATGGCAGAGCTGACCATCAGGCCCGAGGAGATCCGCTCGGCCCTGAACGAGTTCGCCGAGTCCTACAAGCCCGCCGAGGTCGCGGCCGAGGAGGTCGGGCACGTCGTCTTCGCCGCTGACGGCATCGCGCACGTCGAGGGCCTGCCCGGCGTCATGGCCAACGAGCTGCTCACCTTCGAGGACGGCACCGCCGGCCTGGCCATGAACCTCGAGGAGCGCCGGATCGGCGTCGTCGTCCTGGGCTCCTTCGACGGCATCGACGAGGGCCAGGTTGTGCGCCGCACCGGCGAGGTCCTCTCCGTGCCCGTGGGTGACGCCTACCTGGGCCGCGTCGTCGACCCGCTGGGCCGGCCCATCGACGGCCTGGGCGAGATCGAGGCCGAGGGGCGCCGCGCCCTGGAGCTCCAGGCACCCGGCGTCATGGCCCGCAAGTCCGTCCACGAGCCCCTCCAGACCGGGCTCAAGGCCATCGACTCGATGATCCCGATCGGCCGCGGCCAGCGCCAGCTCATCATCGGTGACCGCCAGACCGGCAAGACCGCCATCGCCCTGGACACCATCCTCAACCAGAAGGAGGCCTGGGAGTCCGGCGACCCGAACAAGCAGGTGCGCTGCATCTACGTGGCCACCGGCCAGAAGGGCTCCACCATCGCCGCCGTGCGCGCCACCCTGGAGGAGCGCGGCGCCCTGGAGTACACCACCATCGTGGCCTCACCGGCCTCCGACCCGGCCGGCTTCAAGTACCTGTCGCCCTACACGGGCTCGGCCATCGGCCAGCACTGGATGTACCAGGGCAAGCACGTCCTCATCGTCTTCGACGACCTGTCCAAGCAGGCCGAGGCCTACCGCGCCGTCTCCCTGCTGCTGCGCCGTCCGCCGGGCCGCGAGGCCTACCCCGGTGACGTCTTCTACCTCCACTCGCGTCTGCTGGAGCGCTGCTCCAAGCTCTCCGACGAGCTGGGGGCGGGCTCCATGACCGGGCTGCCGATCATCGAGACCAAGGCCAACGACGTCTCGGCCTACATCCCCACCAACGTCATCTCCATCACCGACGGGCAGATCTTCCTCCAGTCCGACCTGTTCAACGCCGACCAGCGCCCCGCCGTCGACGTCGGCATCTCCGTGTCCCGCGTGGGCGGCGCAGCCCAGGTCAAGGCCATGAAGAAGGTCGCCGGAACCCTCAAGATCACCCTGGCGCAGTACCGCTCCATGCAGGCCTTCGCCATGTTCGCTTCCGACCTGGACGCCGCCACCCGCGCCCAGCTCACCCGCGGTGAGCGCCTCATGGAGCTGCTCAAGCAGCCCCAGTACACGCCCTACCCGGTGGCTGAGCAGGTCGCCAGCGTCTGGGCCGGCACCAAGGGCTACCTCGACGACATCGACGTCTCCGACGTCCTGCCCTTCGAGGCCGCCTTCCTGGACCACCTGCGGCGCAACACCGACATCCTCGACACCATCGAGTCCACCGGTCAGCTCACTGACGAGACCGAGGAGGCCCTGGTCAAGGCCGTTGAGGCCTTCCGGCGCACCTTCGCCTCCGGTGAGCAGATGCTGGGCGCCCAGGTCGCCGAGCCCGAGGAGGAGCCCGCCGCCGAGAGGACCACCGAGCAGCTCGTGGTCAAGAGGGGCTGA","MAELTIRPEEIRSALNEFAESYKPAEVAAEEVGHVVFAADGIAHVEGLPGVMANELLTFEDGTAGLAMNLEERRIGVVVLGSFDGIDEGQVVRRTGEVLSVPVGDAYLGRVVDPLGRPIDGLGEIEAEGRRALELQAPGVMARKSVHEPLQTGLKAIDSMIPIGRGQRQLIIGDRQTGKTAIALDTILNQKEAWESGDPNKQVRCIYVATGQKGSTIAAVRATLEERGALEYTTIVASPASDPAGFKYLSPYTGSAIGQHWMYQGKHVLIVFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCSKLSDELGAGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNADQRPAVDVGISVSRVGGAAQVKAMKKVAGTLKITLAQYRSMQAFAMFASDLDAATRAQLTRGERLMELLKQPQYTPYPVAEQVASVWAGTKGYLDDIDVSDVLPFEAAFLDHLRRNTDILDTIESTGQLTDETEEALVKAVEAFRRTFASGEQMLGAQVAEPEEEPAAERTTEQLVVKRG$","ATP synthase F1, alpha subunit","Cytoplasm","ATP synthase F1, alpha subunit","ATP synthase F1; alpha subunit ","ATP synthase F1, alpha subunit","","Cross R.L., Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004. 576(1):1-4. PMID: 15473999Rappas M., Niwa H., Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci 2004. 5(2):89-105. PMID: 15078220Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001. 410(6831):898-904. PMID: 11309608Wilkens S., Zhang Z., Zheng Y. A structural model of the vacuolar ATPase from transmission electron microscopy. Micron 2005. 36(2):109-126. PMID: 15629643Leyva J.A., Bianchet M.A., Amzel L.M. Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). Mol. Membr. Biol. 2003. 20(1):27-33. PMID: 12745923Antes I., Chandler D., Wang H., Oster G. The unbinding of ATP from F1-ATPase. Biophys. J. 2003. 85(2):695-706. PMID: 12885621","","","

InterPro
IPR000194
Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding
PF00006	$\"[152-376]T$	ATP-synt_ab
PS00152	$\"[367-376]T$	ATPASE_ALPHA_BETA

InterPro
IPR000793
Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
PF00306	$\"[388-491]T$	ATP-synt_ab_C

InterPro
IPR004100
Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal
PF02874	$\"[28-96]T$	ATP-synt_ab_N

InterPro
IPR005294
Family

ATPase, F1 complex, alpha subunit
PTHR15184:SF3	$\"[206-539]T$	ATP SYNTHASE ALPHA SUBUNIT MITOCHONDRIAL
TIGR00962	$\"[5-513]T$	atpA: ATP synthase F1, alpha subunit

noIPR
unintegrated

unintegrated
G3DSA:1.20.150.20	$\"[384-517]T$	no description
G3DSA:2.40.30.20	$\"[28-97]T$	no description
G3DSA:3.40.50.300	$\"[98-383]T$	no description
PTHR15184	$\"[206-539]T$	ATP SYNTHASE

","BeTs to 16 clades of COG0056COG name: F0F1-type ATP synthase alpha subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0056 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB000194 (H+-transporting two-sector ATPase, alpha/beta subunit, central region) with a combined E-value of 6.1e-86. IPB000194A 108-120 IPB000194B 152-187 IPB000194C 252-263 IPB000194D 265-314 IPB000194E 323-371","Residues 4-121 are 58% similar to a (CF1 ALPHA HYDROLASE F0F1-ATPASE CHAIN ION ATP ATP-BINDING SYNTHESIS) protein domain (PD969833) which is seen in Q7UH05_RHOBA.Residues 40-133 are 52% similar to a (ION ATP F1 CF1 ALPHA SYNTHASE HYDROGEN HYDROLASE MITOCHONDRION ATP-BINDING) protein domain (PD483875) which is seen in Q8W9T4_MESVI.Residues 40-126 are 54% similar to a (ATP CF1 ALPHA SYNTHASE HYDROLASE ION ATP-BINDING SUBUNIT SYNTHESIS) protein domain (PD617115) which is seen in Q9AHX2_CARRU.Residues 41-130 are 63% similar to a (ATP CF1 ALPHA SYNTHASE HYDROLASE ATP-BINDING SUBUNIT SYNTHESIS) protein domain (PD072244) which is seen in O31082_METBA.Residues 47-119 are 58% similar to a (ION CF1 ALPHA HYDROGEN HYDROLASE ATP ATPASE ATP-BINDING SUBUNIT SYNTHESIS) protein domain (PD268148) which is seen in Q9GS23_TRYBB.Residues 101-131 are 96% similar to a (ATP ION HYDROLASE SYNTHESIS ATP-BINDING SYNTHASE CF1 HYDROGEN BETA SUBUNIT) protein domain (PD484054) which is seen in Q6RVY0_BIFAN.Residues 133-220 are similar to a (ATP ION HYDROLASE ATP-BINDING SYNTHESIS SYNTHASE SUBUNIT HYDROGEN CF1 BETA) protein domain (PD507040) which is seen in Q6A8C5_PROAC.Residues 184-226 are 90% similar to a (ATP ION CF1 HYDROLASE ATP-BINDING SYNTHESIS ALPHA SYNTHASE CHAIN SUBUNIT) protein domain (PD695509) which is seen in ATPA_MYCTU.Residues 228-269 are 97% similar to a (ATP ION CF1 HYDROLASE SYNTHESIS ATP-BINDING ALPHA SYNTHASE HYDROGEN CHAIN) protein domain (PD881004) which is seen in Q6AG60_BBBBB.Residues 270-347 are similar to a (ATP ION HYDROLASE SYNTHESIS ATP-BINDING SYNTHASE SUBUNIT HYDROGEN CF1 BETA) protein domain (PD000090) which is seen in Q73X57_MYCPA.Residues 348-378 are identical to a (ATP ION HYDROLASE CF1 SYNTHESIS ATP-BINDING ALPHA SYNTHASE HYDROGEN CHAIN) protein domain (PD000108) which is seen in Q83G89_TROWT.Residues 379-510 are 52% similar to a (ALPHA SYNTHASE CHAIN ATP) protein domain (PDA19208) which is seen in Q6F204_MESFL.Residues 392-511 are similar to a (ATP ION HYDROLASE SYNTHESIS ATP-BINDING SYNTHASE CF1 HYDROGEN BETA SUBUNIT) protein domain (PD587400) which is seen in Q6RVY0_BIFAN.","","-73% similar to PDB:1SKY CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3 (E_value = 1.2E_158);-71% similar to PDB:1FX0 Crystal structure of the chloroplast F1-ATPase from spinach (E_value = 2.6E_158);-71% similar to PDB:1KMH Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin (E_value = 2.6E_158);-77% similar to PDB:2HLD Crystal structure of yeast mitochondrial F1-ATPase (E_value = 1.4E_156);-76% similar to PDB:2F43 Rat liver F1-ATPase (E_value = 7.4E_153);","Residues 28 to 96 (E_value = 1.8e-15) place ANA_0169 in the ATP-synt_ab_N family which is described as ATP synthase alpha/beta family, beta-barrel domain.Residues 152 to 376 (E_value = 1.7e-112) place ANA_0169 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain.Residues 388 to 491 (E_value = 1.9e-30) place ANA_0169 in the ATP-synt_ab_C family which is described as ATP synthase alpha/beta chain, C terminal domain.","","synthase F1, alpha subunit (atpA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0170","187150","188094","945","5.45","-6.80","34500","GTGGCAGGAAACCAGCGCGTCTACAAGCAGCGCATTCGATCGACCCAGACCCTCCAGAAGGTGTTCCGGGCGATGGAGCTCATCGCCTCGTCCCGGATCGGGCAGGCGCGCCGCAACGCGCAGGAGGCCTCGCCCTACGATCACGCCCTGAGCCAGGCGGTGGCCGCGCTGGGGACCTACTCCCGCTTCGAGCACCCCATCACCCAGGAGCGCACCGATACCAAGCGCGTGGCGATCCTCGTGGTCACCTCTGACCGCGGCATGGCCGGCGCCTACTCGGCCACCATCCTGCGCGAGACCGGCCGCCTTATCGAGGAGCTGGTCAAGGAGGGCAAGGAGCCGGTGATCTTCACCTTCGGCCGGCGCGCCCAGAGCTACTTCAGCTTCCGGGGCACGCCGATTGAGTTCTCCTGGACCGGGCAGTCGGACCGCCCCAGCAACGAGGCCATCGAGGAGGTGGCCACCACCCTGCTGGACTACTTCCTCCAGCCGGCCGAGGCCGGCGGCGTCGCCGAGGTCCACATCGTCTTCACCCGCTACGTCTCGATGGTCTCCCAGGTCCCCGAGGTGCGTCGCATGCTGCCGCTCAAGGTGGTCGACGTCGAAGGGGCCGGCGAGCTCGACGACGCCGGTAACGAGGCCCTGGAGAAGGAGCTGGCGGCCAAGCACGGCGGCTCCATGCCGCTGTACGAGTTCGAGCCCGGGCCCTCCGAGGTGCTCGACGCCCTCCTGACCCGCTACATGGGCTCGCGCATCCGCAACGCCCTGCTGCAGTCGGCCGCCTCCGAGCTGGCCAGCCGTCAGCAGGCCATGCACACGGCCACGGACAACGCCGAGGACCTCATCATCACCTACACCCGCCTGGCCAACGCGGCCCGCCAGGGCGACATCACCCAGGAGATCACGGAGATCGTCTCGGGTGCCGACGCCCTGGGGTCCGAATAG","VAGNQRVYKQRIRSTQTLQKVFRAMELIASSRIGQARRNAQEASPYDHALSQAVAALGTYSRFEHPITQERTDTKRVAILVVTSDRGMAGAYSATILRETGRLIEELVKEGKEPVIFTFGRRAQSYFSFRGTPIEFSWTGQSDRPSNEAIEEVATTLLDYFLQPAEAGGVAEVHIVFTRYVSMVSQVPEVRRMLPLKVVDVEGAGELDDAGNEALEKELAAKHGGSMPLYEFEPGPSEVLDALLTRYMGSRIRNALLQSAASELASRQQAMHTATDNAEDLIITYTRLANAARQGDITQEITEIVSGADALGSE$","ATP synthase F1, gamma subunit","Cytoplasm","ATP synthase F1, gamma subunit","ATP synthase F1; gamma subunit ","ATP synthase F1, gamma subunit","","Cross R.L., Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004. 576(1):1-4. PMID: 15473999Rappas M., Niwa H., Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci 2004. 5(2):89-105. PMID: 15078220Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001. 410(6831):898-904. PMID: 11309608Feniouk B.A., Junge W. Regulation of the F0F1-ATP synthase: the conformation of subunit epsilon might be determined by directionality of subunit gamma rotation. FEBS Lett. 2005. 579(23):5114-5118. PMID: 16154570","","","

InterPro
IPR000131
Family

ATPase, F1 complex, gamma subunit
PR00126	$\"[74-93]T$ $\"[171-188]T$ $\"[258-277]T$ $\"[289-310]T$	ATPASEGAMMA
PTHR11693	$\"[6-208]T$ $\"[230-312]T$	ATP SYNTHASE GAMMA CHAIN
PF00231	$\"[3-311]T$	ATP-synt
TIGR01146	$\"[2-311]T$	ATPsyn_F1gamma: ATP synthase F1, gamma subu
PS00153	$\"[297-310]T$	ATPASE_GAMMA

noIPR
unintegrated

unintegrated
G3DSA:3.40.1380.10	$\"[28-270]T$	no description
PTHR11693:SF10	$\"[6-208]T$ $\"[230-312]T$	ATP SYNTHASE GAMMA CHAIN, SODIUM ION SPECIFIC

","BeTs to 16 clades of COG0224COG name: F0F1-type ATP synthase gamma subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0224 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB000131 (H+-transporting two-sector ATPase, gamma subunit) with a combined E-value of 1e-52. IPB000131A 6-37 IPB000131B 90-124 IPB000131C 169-196 IPB000131D 258-310","Residues 24-311 are 64% similar to a (ATP GAMMA SYNTHASE HYDROLASE SUBUNIT CHAIN ION SYNTHESIS CF1 HYDROGEN) protein domain (PD001150) which is seen in Q6RVY6_BIFBR.Residues 64-168 are 66% similar to a (ATP GAMMA SYNTHASE HYDROLASE SUBUNIT CHAIN F0F1-TYPE ION ATPG SECTOR) protein domain (PDA1E010) which is seen in ATPG_MYCTU.","","-51% similar to PDB:1FS0 COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI (E_value = 5.4E_19);-42% similar to PDB:1MAB RAT LIVER F1-ATPASE (E_value = 3.7E_12);-42% similar to PDB:2F43 Rat liver F1-ATPase (E_value = 3.7E_12);-42% similar to PDB:1BMF BOVINE MITOCHONDRIAL F1-ATPASE (E_value = 1.9E_11);-42% similar to PDB:1COW BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH AUROVERTIN B (E_value = 1.9E_11);","Residues 3 to 311 (E_value = 5.6e-91) place ANA_0170 in the ATP-synt family which is described as ATP synthase.","","synthase F1, gamma subunit (atpG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0171","188188","189624","1437","4.86","-24.58","51860","ATGGCTGACACCACCACCCCCGGGACGGGACGCATCACCCGCATCATCGGCGCCGTCGTCGACGTCGAGTTCCCGCCTGATGCGATCCCGGCGATGTACAACGCCCTCAAGGTGACCGTCCAGGCCACCAGCGCCGGCGAGGAGCCGCACGAGATCACCCTGGAGGTCGCCCAGCACCTGGGTGACAACATCGTGCGCACGATCTCCCTCAAGCCCACCGACGGCCTCGTGCGCGGCACGCAGGTGCGCGACACCGGCGCGCCGATCTCCGTGCCCGTGGGCGACGTGACCAAGGGCCACGTCTTCAACGTCACCGGCGACGTCCTCAACCTTGGCCCCGGCGAGCAGCTGGAGATCACCGAGCGCTGGCCCATCCACCGCCAGCCCCCGGCCTTCGACCAGCTCGAGTCCAAGGAGCAGATGTTCGAGACCGGCATCAAGGTCATCGACCTGCTCACCCCCTACGTGCAGGGCGGCAAGATCGGCCTGTTCGGCGGCGCCGGCGTGGGTAAGACCGTCCTCATCCAGGAGATGATTCAGCGCGTGGCCCAGAACCACGGCGGTGTCTCCGTGTTCGCCGGCGTGGGGGAGCGCACCCGTGAGGGCAACGACCTCATCGTCGAGATGGACGAGGCCGGCGTGTTCGACAAGACCGCCCTGGTCTTCGGCCAGATGGACGAGCCGCCGGGCACGCGTCTGCGCGTGGCCCTGTCCGCCCTGACGATGGCCGAGTACTTCCGCGACGTCCAGCACCAGGACGTGCTGCTGTTCATCGACAACATCTTCCGCTTCACCCAGGCCGGCTCCGAGGTCTCCACGCTGTTGGGCCGCATGCCCTCGGCCGTGGGCTACCAGCCCAACCTGGCCGACGAGATGGGCCAGCTCCAGGAGCGCATCACCTCCGCCGGCGGCCACTCCATCACCTCCCTGCAGGCGATCTACGTGCCCGCCGACGACTACACCGACCCGGCGCCGGCGACGACCTTCGCCCACCTGGACGCCACCACCGAGCTCAGCCGTGAGATCGCCTCGCGAGGCATCTACCCGGCCGTGGACCCGCTGACCTCCACCTCGCGCCTGCTGGCCCCCGGCTACGTGGGCCAGGAGCACTACGACGTCGCCACCCGCGTGAAGTCCATCCTCCAGAAGAACAAGGAGCTCCAGGACATCATCGCGATCCTCGGTGTCGACGAGCTCGGCGAGGAGGACAAGGTGACGGTGGCCCGCGCCCGCCGCATCGAGCAGTTCCTGTCCCAGAACACCTACATGGCGGAGAAGTTCACCGGCGTGGCCGGCTCCACCGTGCCGCTGTCGGAGACCATCGAGGCCTTCCGGCGCATCTGCGACGGTGACTACGACCACCTGCCGGAGCAGGCCTTCTTCAACATCGGTGGCATCGAGGACCTCGAGCGTCGCGCCGCCGAGCTCAACGCCTGA","MADTTTPGTGRITRIIGAVVDVEFPPDAIPAMYNALKVTVQATSAGEEPHEITLEVAQHLGDNIVRTISLKPTDGLVRGTQVRDTGAPISVPVGDVTKGHVFNVTGDVLNLGPGEQLEITERWPIHRQPPAFDQLESKEQMFETGIKVIDLLTPYVQGGKIGLFGGAGVGKTVLIQEMIQRVAQNHGGVSVFAGVGERTREGNDLIVEMDEAGVFDKTALVFGQMDEPPGTRLRVALSALTMAEYFRDVQHQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGQLQERITSAGGHSITSLQAIYVPADDYTDPAPATTFAHLDATTELSREIASRGIYPAVDPLTSTSRLLAPGYVGQEHYDVATRVKSILQKNKELQDIIAILGVDELGEEDKVTVARARRIEQFLSQNTYMAEKFTGVAGSTVPLSETIEAFRRICDGDYDHLPEQAFFNIGGIEDLERRAAELNA$","ATP synthase F1, beta subunit","Cytoplasm","ATP synthase F1, beta subunit","ATP synthase F1; beta subunit ","ATP synthase F1, beta subunit","","Cross R.L., Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004. 576(1):1-4. PMID: 15473999Rappas M., Niwa H., Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci 2004. 5(2):89-105. PMID: 15078220Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001. 410(6831):898-904. PMID: 11309608Wilkens S., Zhang Z., Zheng Y. A structural model of the vacuolar ATPase from transmission electron microscopy. Micron 2005. 36(2):109-126. PMID: 15629643Leyva J.A., Bianchet M.A., Amzel L.M. Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). Mol. Membr. Biol. 2003. 20(1):27-33. PMID: 12745923Antes I., Chandler D., Wang H., Oster G. The unbinding of ATP from F1-ATPase. Biophys. J. 2003. 85(2):695-706. PMID: 12885621","","","

InterPro
IPR000194
Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding
PF00006	$\"[144-358]T$	ATP-synt_ab
PS00152	$\"[349-358]T$	ATPASE_ALPHA_BETA

InterPro
IPR000793
Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
PF00306	$\"[371-478]T$	ATP-synt_ab_C

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[157-420]T$	AAA

InterPro
IPR004100
Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal
PF02874	$\"[12-86]T$	ATP-synt_ab_N

InterPro
IPR005722
Family

ATPase, F1 complex, beta subunit
PTHR15184:SF8	$\"[9-390]T$	ATP SYNTHASE BETA SUBUNIT
TIGR01039	$\"[8-476]T$	atpD: ATP synthase F1, beta subunit

noIPR
unintegrated

unintegrated
G3DSA:1.10.1140.10	$\"[361-476]T$	no description
G3DSA:2.40.10.170	$\"[9-88]T$	no description
G3DSA:3.40.50.300	$\"[89-360]T$	no description
PTHR15184	$\"[9-390]T$	ATP SYNTHASE

","BeTs to 16 clades of COG0055COG name: F0F1-type ATP synthase beta subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0055 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB000194 (H+-transporting two-sector ATPase, alpha/beta subunit, central region) with a combined E-value of 2.4e-94. IPB000194A 98-110 IPB000194B 144-179 IPB000194C 237-248 IPB000194D 251-300 IPB000194E 305-353***** IPB011113 (Rho termination factor, RNA-binding) with a combined E-value of 4.7e-08. IPB011113C 147-175 IPB011113E 251-278 IPB011113H 338-377","Residues 19-86 are 82% similar to a (ATP ION HYDROLASE SYNTHESIS BETA ATP-BINDING SYNTHASE CF1 HYDROGEN SUBUNIT) protein domain (PD536374) which is seen in Q6AG58_BBBBB.Residues 124-170 are 95% similar to a (ATP ION HYDROLASE ATP-BINDING SYNTHESIS SYNTHASE SUBUNIT HYDROGEN CF1 BETA) protein domain (PD507040) which is seen in Q6RVY5_BIFBR.Residues 171-197 are identical to a (ATP ION HYDROLASE SYNTHESIS BETA ATP-BINDING SYNTHASE CF1 HYDROGEN SUBUNIT) protein domain (PD690277) which is seen in Q6RVY5_BIFBR.Residues 198-238 are 97% similar to a (ATP ION HYDROLASE SYNTHESIS BETA ATP-BINDING SYNTHASE CF1 HYDROGEN SUBUNIT) protein domain (PD692862) which is seen in Q6AG58_BBBBB.Residues 239-319 are similar to a (ATP ION HYDROLASE SYNTHESIS ATP-BINDING SYNTHASE SUBUNIT HYDROGEN CF1 BETA) protein domain (PD000090) which is seen in Q8G7B3_BIFLO.Residues 322-422 are 52% similar to a (SUBUNIT ATP ION A HYDROLASE HYDROGEN V-TYPE SYNTHESIS SYNTHASE VACUOLAR) protein domain (PD186754) which is seen in O00779_DICDI.Residues 326-366 are 92% similar to a (ATP ION HYDROLASE SYNTHESIS BETA ATP-BINDING SYNTHASE CF1 HYDROGEN SUBUNIT) protein domain (PD856741) which is seen in Q6RVY2_BIFAN.Residues 367-457 are similar to a (ATP ION HYDROLASE SYNTHESIS ATP-BINDING SYNTHASE CF1 HYDROGEN BETA SUBUNIT) protein domain (PD587400) which is seen in Q6A8C7_PROAC.Residues 367-476 are 57% similar to a (ATP HYDROLASE ION BETA ATP-BINDING SYNTHESIS CF1 SYNTHASE HYDROGEN CHAIN) protein domain (PD544470) which is seen in ATPB_MYCPU.","","-80% similar to PDB:1SKY CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3 (E_value = 3.4E_170);-76% similar to PDB:1FX0 Crystal structure of the chloroplast F1-ATPase from spinach (E_value = 4.1E_160);-76% similar to PDB:1KMH Crystal Structure of spinach chloroplast F1-ATPase complexed with tentoxin (E_value = 4.1E_160);-75% similar to PDB:2HLD Crystal structure of yeast mitochondrial F1-ATPase (E_value = 6.8E_155);-76% similar to PDB:1MAB RAT LIVER F1-ATPASE (E_value = 4.4E_154);","Residues 12 to 86 (E_value = 6.3e-27) place ANA_0171 in the ATP-synt_ab_N family which is described as ATP synthase alpha/beta family, beta-barrel domain.Residues 144 to 358 (E_value = 1.7e-95) place ANA_0171 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain.Residues 371 to 478 (E_value = 1.6e-41) place ANA_0171 in the ATP-synt_ab_C family which is described as ATP synthase alpha/beta chain, C terminal domain.","","synthase F1, beta subunit (atpD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0172","189670","189936","267","4.48","-7.40","8925","ATGGCCTTACATGTTGAGGTGGTCTCGCCGGCGGGCGAGGCCTGGACCGGTGAGGCGACGCAGGTCTCCGTACCCCTGATTAACGGGGAGCTGGGGATCCTGCCGGGTCGTCAGCCCCTCGTGGCGGTCCTGGGGGCCGGTCCGGTGCGGCTGAGTCCCATCGACGGCGAGATGTGCAGTATCGAGGTGTCCGGCGGCTTCTGCTCCGTGGACCACGACGTCATCACGATCGCCGCCGACCACGTGAAGCAGGGCGCGGAGGCCTGA","MALHVEVVSPAGEAWTGEATQVSVPLINGELGILPGRQPLVAVLGAGPVRLSPIDGEMCSIEVSGGFCSVDHDVITIAADHVKQGAEA$","ATP synthase F1, epsilon subunit","Cytoplasm","ATP synthase, Delta/Epsilon chain, beta-sandwichdomain","ATP synthase; epsilon chain ","H+-transporting two-sector ATPase, delta/epsilon subunit","","Cross R.L., Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004. 576(1):1-4. PMID: 15473999Rappas M., Niwa H., Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci 2004. 5(2):89-105. PMID: 15078220Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001. 410(6831):898-904. PMID: 11309608Hong S., Pedersen P.L. ATP synthases: insights into their motor functions from sequence and structural analyses. J. Bioenerg. Biomembr. 2003. 35(2):95-120. PMID: 12887009","","","

InterPro
IPR001469
Family

ATPase, F1 complex, delta/epsilon subunit
PD000944	$\"[8-81]T$	Q6RVY3_BIFAN_Q6RVY3;
G3DSA:2.60.15.10	$\"[1-88]T$	no description
PTHR13822	$\"[3-81]T$	ATP SYNTHASE DELTA/EPSILON CHAIN
PF02823	$\"[2-80]T$	ATP-synt_DE_N

noIPR
unintegrated

unintegrated
PTHR13822:SF2	$\"[3-81]T$	ATP SYNTHASE EPSILON CHAIN

","No hits to the COGs database.","***** IPB001469 (H+-transporting two-sector ATPase, delta/epsilon subunit) with a combined E-value of 4.6e-16. IPB001469A 7-51 IPB001469B 63-88","Residues 8-81 are similar to a (ATP SYNTHASE EPSILON ION CF1 HYDROLASE SYNTHESIS SUBUNIT CHAIN HYDROGEN) protein domain (PD000944) which is seen in Q6RVY3_BIFAN.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 84 (E_value = 7e-11) place ANA_0172 in the ATP-synt_DE_N family which is described as ATP synthase, Delta/Epsilon chain, beta-sandwich domain.","","synthase, Delta-Epsilon chain, beta-sandwich domain","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0174","189940","190356","417","8.61","2.60","15600","ATGGGGCAGCACGTGTGGATGGTCGTGGCGATTGCCGTCACCGTCCTCGTGCTGCTGGCAGGCGGGTTCCTGCTGCGTTTGCGCTACCTGGCCGGGCAAGTCGGCTCCTTCGAGTGCGCCCTGCGTCCCCGCGGGGCGCAGCGCTGGCTGAGCGGGGTGGCCTCCTTCCAGCTCGACTCCCTGGAGTGGTATCGCCTCGTGTCCTTCTCCACCAGGCCGTCGCGCTCATGGAGCCGCTTAAACCTGGAGCTCTCCGAGGCACGGCGCCGCCGGGAGCAGGGGCGCGTCGTCGAGGTGCACTGTGTGGACGCCACCCGCAGCCCGGAGGGCTTCGACCTGGCCATGATGGAGGAGTCCCACTCGGCGCTGATCGCCTGGGTGGAGTCCGCCGCCCCTGAGCAGCCCCGGCTCTTCTGA","MGQHVWMVVAIAVTVLVLLAGGFLLRLRYLAGQVGSFECALRPRGAQRWLSGVASFQLDSLEWYRLVSFSTRPSRSWSRLNLELSEARRRREQGRVVEVHCVDATRSPEGFDLAMMEESHSALIAWVESAAPEQPRLF$","Putative secreted protein","Membrane, Periplasm, Cytoplasm","putative secreted protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PD031809	$\"[35-130]T$	Q9K4D3_STRCO_Q9K4D3;
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

InterPro
IPR002793
Family

Protein of unknown function DUF91
PD013521	$\"[4-231]T$	Q6AHG7_BBBBB_Q6AHG7;
PF01939	$\"[1-231]T$	DUF91

","BeTs to 7 clades of COG1637COG name: Predicted nuclease of the RecB familyFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1637 is -om-kz----r---------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 4-231 are similar to a (UPF0286 SSO2208 ST2290 APE0957 RECB PH0128 CE1318 RV1321/MT1363 VNG0171C MK0507) protein domain (PD013521) which is seen in Q6AHG7_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 231 (E_value = 1.9e-88) place ANA_0175 in the DUF91 family which is described as Protein of unknown function DUF91.","","nuclease of the RecB family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0176","191391","192647","1257","7.45","2.50","44252","ATGCCCGCCGCCCGCACGTCCTCCGCAACGCTGCCGACCGAGGTGAGCCTGGCCCGCATCATCTCCCAGGGCCTCGTCCCGGCCACCTCCGCGCCCGACGTCGTCGCGGCAGTGTCCCGCCAGCTCGCCATCCAGGGCCAGCAGGTCTCCGCCGTCCCCCACGCCCTGCTCGTGCGCGCCCCGGCCGCCACCTCGGCCGACGTCGAGGCGGCCTTCGCGCGAGGCGACCTGGTTCGCTCCTGGCCCATGCGCGGCACCGTCCACATCACCACCGCCGCCGACCACCACTGGCTGCGGGCCGCCCTCATGCACCGCACCGACGCCTGGGTGCGGAACAGCGAGAAGGCTTACGGCGTCGATACCGCCCTGTGCGAGCGCGCCGCCGAGGTGGCCCTGGGCCTCATCGAGGACCAGGGCCCGCTGACGCGCTCGGTGCTGCTGGCGGCCTGGCAGGAGGCCGGCCTCATGGAGGCCTTCCGTGGTGAGGACGTCTCGGCCTACCGGCGCCGCCACCTCCTGGTGCGCCTCCAGCGCGAGGGGATCCTCGTCCAGGGTCCGCGGTCCGGCAACGAGCACCTCGTCATGGACGCACGCCACCTGCCCGACGCCGACTCCGGGCCCGCAGGGGCCGACGTCGCCCACGGCGGGAGCGGCCACCGCGCCGCCTGCGCGCACATCGCCTACCGCTACGCGACCAGCCACGGCCCGGTTGGCGCCGAGGACCTGGCCCGCTGGACCACACTGCCCAAGACGCAGGCCGCCCGCGCCCTGGAGGACGCCGTCGAGCTGGGGGAGGAGCAGGCCCCAGCCGCGGTTAATGCTGCCGGTGAGTCGGCCGGGCCCCGTGTCCCGCTCGTGCGCGCGGTCGCCGAGGGCGGGGCCCGCGGAGGCCTGCGCCCGCTCGGTCCCGGCGAGTCGGCCCCGAAGACCGGCCTGCTCTACATGCGCGCCGACCTGCCCGACCTGCTGTCCGCCCACCGCAGCGCCGCGCAGGCCACGCACTTCCTGGGCTCCTTCGACGAGCTGCACGTGGGCTACAAGGACCGCTCCTGCCTCACCGATGAGGACGGTGAGCGCCTCATCTGCCCGGCGAGCAACGGCATGTTCCGCCCGATCCTGGTGGACCGCGGCCGACTCGTCGCTGTGCGGCCGGTCGGGGAGGGCCTGCTGTGGAAGGGCGGGGCGGCGCCGTCGGCGCGCGTGGAGCGAGACGTCAACCGGGCCGTCTCCCGCATGGAGCAGCGCCTGGCCGGGTGA","MPAARTSSATLPTEVSLARIISQGLVPATSAPDVVAAVSRQLAIQGQQVSAVPHALLVRAPAATSADVEAAFARGDLVRSWPMRGTVHITTAADHHWLRAALMHRTDAWVRNSEKAYGVDTALCERAAEVALGLIEDQGPLTRSVLLAAWQEAGLMEAFRGEDVSAYRRRHLLVRLQREGILVQGPRSGNEHLVMDARHLPDADSGPAGADVAHGGSGHRAACAHIAYRYATSHGPVGAEDLARWTTLPKTQAARALEDAVELGEEQAPAAVNAAGESAGPRVPLVRAVAEGGARGGLRPLGPGESAPKTGLLYMRADLPDLLSAHRSAAQATHFLGSFDELHVGYKDRSCLTDEDGERLICPASNGMFRPILVDRGRLVAVRPVGEGLLWKGGAAPSARVERDVNRAVSRMEQRLAG$","Superoxide dismutase, copper/zinc binding","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","Schinina M.E., Barra D., Bossa F., Calabrese L., Montesano L., Carri M.T., Mariottini P., Amaldi F., Rotilio G. Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis. Arch. Biochem. Biophys. 1989. 272(2):507-515. PMID: 2751312Parge H.E., Hallewell R.A., Tainer J.A. Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(13):6109-6113. PMID: 1463506Schinina M.E., Barra D., Simmaco M., Bossa F., Rotilio G. Primary structure of porcine Cu,Zn superoxide dismutase. FEBS Lett. 1985. 186(2):267-270. PMID: 3891411Van Camp W., Bowler C., Villarroel R., Tsang E.W., Van Montagu M., Inze D. Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1990. 87(24):9903-9907. PMID: 2263641","","","

InterPro
IPR001424
Domain

Superoxide dismutase, copper/zinc binding
PS00332	$\"[215-226]?$	SOD_CU_ZN_2

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 19-265 are 38% similar to a (SCO2204 CGL0375 LIN0820 SCO5027 LMO0824) protein domain (PD584819) which is seen in Q721Z1_LISMF.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0177","192741","193991","1251","4.79","-25.99","42929","ATGAGCAACGAAGCCATGCAGGTCCGCGCACTGCGGGGACGCGTCGTCACCCCCGACCACATCATCGACGATGGGGTGGTTGTCCTGTCGGGATCCCACATCGCGTGGGTCGGGCCCGCCGACCAGGCCGCCCGGGCCGGCTTCACAGACGCCGTCGAGCAGGCGCAGGCCGCACCCGAGGGCGGTTACCTCCTGCCGGGACTGGTGGACGTCCACTGCCACGGTGGGGGCGGTGAGTCCTTCCCCAACGCCGAGACCGCCGAGCAGGCGATGGTCTCCGTGCTCGAGCACCGCCGCTTCGGCACCACCTCGCTCGTGGCCTCCTGCGTGACGGCCGCCCCCGAGGTCCTGCGCGCACGCACCCGCGTCCTGGCAGGGCTGTGCGAGGACGGCGAGCTCGCCGGCATCCACTTCGAGGGGCCCTTCGTCTCGGTGGAGCGCTGCGGCGCCCAGGACCCCACCTACATCATCGACCCCGACGCCGACCTGACCCGCGAGCTCATCGAACTCGGCGGCGGGCACGTCGTCACCATGACGATCGCCCCGGAGAAGCCCGGCATCACCGGTGACGACGGCGTCAACGCAGCCCTCATCGAGGGAGGGGCGCTGCCCTCCTTCGGGCACACCGACTCCGAAGCCGCCCCCGTGCGCGCCGCCCTGGCCGACGCCGCCGCCCGCATCGCCGAGCGCCTCGAGGCCGGCGAGCCGGTCCGCGCGCCGCGCTCGACCGCCACTCACCTGTTCAACGGCATGCGCCCCATGCACCACCGCACGCCCGGGCCCGTGCCCGAGTTCCTGGCGGCCGCCCAGCGCGGCGAATGCGTCCTCGAGATGATCGGCGACGGCGTGCACCTCAGCCCCGCCATCGTCCTGGACATGTTCGAGACCCTGGGGCGCGATAACGTCGTCCTGGTCACCGACGCCATGGCCGCGGCCGGCATGGCCGACGGCGACTACGTGCTCGGCTCCCAGCCGGTCACCGTGGCCGACGGCGTCGCCCGCCTCACCGAGGGTGGCGCGATCGCCGGGGGAACCGCCCACCTCATCGACGTCGTGCGCACCACCTGGCAGGGGGGAGTCGACCTGGTCGACGCCGTCTACGCCGCCAGCGTCCAGGGCGCCCAGATCCTAGGCGACCCAACCGTGGGGGCGTTGCGGGCGGGCCTGTGGGCCGACGTCGTCGTCACCGACGCGGAGCTGCGGCCCGTCACCGTGCTGCGCCGCGGCGAGGCGGTGGAGCCCGCCGCCTGA","MSNEAMQVRALRGRVVTPDHIIDDGVVVLSGSHIAWVGPADQAARAGFTDAVEQAQAAPEGGYLLPGLVDVHCHGGGGESFPNAETAEQAMVSVLEHRRFGTTSLVASCVTAAPEVLRARTRVLAGLCEDGELAGIHFEGPFVSVERCGAQDPTYIIDPDADLTRELIELGGGHVVTMTIAPEKPGITGDDGVNAALIEGGALPSFGHTDSEAAPVRAALADAAARIAERLEAGEPVRAPRSTATHLFNGMRPMHHRTPGPVPEFLAAAQRGECVLEMIGDGVHLSPAIVLDMFETLGRDNVVLVTDAMAAAGMADGDYVLGSQPVTVADGVARLTEGGAIAGGTAHLIDVVRTTWQGGVDLVDAVYAASVQGAQILGDPTVGALRAGLWADVVVTDAELRPVTVLRRGEAVEPAA$","N-acetylglucosamine-6-phosphate deacetylase","Cytoplasm, Extracellular","N-acetylglucosamine-6-phosphate deacetylase","N-acetylglucosamine-6-phosphate deacetylase ","N-acetylglucosamine-6-phosphate deacetylase","","Nygaard P., Duckert P., Saxild H.H. Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis. J. Bacteriol. 1996. 178(3):846-853. PMID: 8550522Holm L., Sander C. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 1997. 28(1):72-82. PMID: 9144792","","","

InterPro
IPR006680
Domain

Amidohydrolase 1
PF01979	$\"[63-397]T$	Amidohydro_1

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.140	$\"[68-378]T$	no description
PTHR11113	$\"[1-219]T$ $\"[237-416]T$	N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE

","BeTs to 10 clades of COG1820COG name: N-acetylglucosamine-6-phosphate deacetylaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1820 is --------vdrlb-efghs--j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB011550 (Amidohydrolase-like) with a combined E-value of 3.2e-06. IPB011550A 61-74","Residues 97-378 are 57% similar to a (DEACETYLASE N-ACETYLGLUCOSAMINE-6-PHOSPHATE HYDROLASE 6-P GLCNAC METABOLISM CARBOHYDRATE PROBABLE NAGA N-ACETYLGALACTOSAMINE-6-PHOSPHATE) protein domain (PD591458) which is seen in Q8NMD3_CORGL.","","-43% similar to PDB:1UN7 THE 3-D STRUCTURE OF THE N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE, NAGA, FROM BACILLUS SUBTILIS: A MEMBER OF THE UREASE SUPERFAMILY (E_value = 9.8E_30);-42% similar to PDB:1O12 Crystal structure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution (E_value = 2.0E_22);-43% similar to PDB:1YMY Crystal Structure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 (E_value = 4.9E_21);-43% similar to PDB:1YRR Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution (E_value = 4.9E_21);","Residues 63 to 397 (E_value = 7.7e-06) place ANA_0177 in the Amidohydro_1 family which is described as Amidohydrolase family.","","deacetylase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0178","194638","194114","525","4.72","-12.82","19400","ATGACGACTCTTGAAATGCTCATTGACGTTCTGTTCCGCTCCCGAGAGCGCTTCGACCGCGCCTTTGATGGCGTCACGCTCGAGCAGGCCAACACCCGGCCCGCCCCGGACCTCGCGCCCCGCATCGACTCCCTGACCTGGCTGGCCTGGCACACGGCCCGCGAGCTCGACATCCAGGTCGCGCCCCTGGCGGGCGTCGAGCCCGTCTGGGTCACCGGCGGCCACCGGGAGCGCTTCGCCCTGCCCCTGCCCGACGACACCGAGGACTGGCACCACACGCCCGAGCAGGCCGCCCAGGTCGTCGTCAGCGACCTCGGTCTTCTCTTCTCCTACCTCGACGACGCCTACGCTCTGGCCACCACCTACCTGCGCTCCCTCACGCCGGAGGGGCTCGACGACGTCATCGACGACTCCTGGGACCCACCCGTCACTCGGGCCGTGCGCCTGGCCTCAGTCATCGACGACGCCGCCCAGCACTCCGGCCAGGCCATCTACACCCGCCGCCTCCTGGGCCTGCCGGGCTAA","MTTLEMLIDVLFRSRERFDRAFDGVTLEQANTRPAPDLAPRIDSLTWLAWHTARELDIQVAPLAGVEPVWVTGGHRERFALPLPDDTEDWHHTPEQAAQVVVSDLGLLFSYLDDAYALATTYLRSLTPEGLDDVIDDSWDPPVTRAVRLASVIDDAAQHSGQAIYTRRLLGLPG$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 9-170 are similar to a (SCO7269 SMU.1615C MB0451) protein domain (PD098493) which is seen in Q8DSY9_STRMU.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0182","195724","194882","843","5.21","-9.41","30245","ATGAAATTAGAAAGACGCAGCATTATTGCTGCCATAGTTTTGGTTCTGATCCTCACAGCCCCCTCCCTCCGAGCCGACGACCAGGCCGACAACACTCCTGGGACCAGACTAGGGGCAAGAAACCTCGACGGTGGCAGCGAGGCCTATGGGGAGGTGACTGAGACCATCCCTCAAGAGAGTGCGCCGGATTCTGGTGGGCCTCCGTCTCAGGAGCGTCCGACCGTTCAGGCTTCGGATCCGTCGATGTGGGAGGAGCAGTCGCATCGGGAGTGCTCGCCGGAGAAGGACGCCTACGGGCTGGACAAGTACAAGTGCAACCTGGCCACCCTCAACCGCCCCGGCGGGCCCGACCAACCCACCAACACTGACAGTGGTGGCCGTACGGTCACGGTCACCACCCGCCAGGCCGCCACCCTGATCGCCTCGGGCTCGGGCATCACCCGCCAGCCCCCAGGCCCCAAGGTCATCATCTCCAAGGCCTTCATCGTCTACACCAACCCCAGCCCCCAGCACCAGACCACCACCATCCTGGGCACCTCCATCGAGGTGGAGTTCACCCCCACCTCCTACACCTGGGGCTGGGGAGACGGCACCACCACAACCACCACCGACCCCGGCGCCCCCTACCCCCACCAGACCGTCACCCACCACTACCAGCACACCGCCACCGGAGTCACCACCACCCTGACCACCACCTGGACCACCAGGTACCGCCCCACCGGCGAGAGCCAGTGGCGACCCATCGAGGGCACCATCACCACCACCGAGACCTCCACCCCCTACGACCTGGTCCGCATCGTCACCTACCTCACCGACGACGCAGAAGAAGCCCAAGGCCACTAA","MKLERRSIIAAIVLVLILTAPSLRADDQADNTPGTRLGARNLDGGSEAYGEVTETIPQESAPDSGGPPSQERPTVQASDPSMWEEQSHRECSPEKDAYGLDKYKCNLATLNRPGGPDQPTNTDSGGRTVTVTTRQAATLIASGSGITRQPPGPKVIISKAFIVYTNPSPQHQTTTILGTSIEVEFTPTSYTWGWGDGTTTTTTDPGAPYPHQTVTHHYQHTATGVTTTLTTTWTTRYRPTGESQWRPIEGTITTTETSTPYDLVRIVTYLTDDAEEAQGH$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-25]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[39-57]?$	transmembrane_regions

InterPro
IPR002376
Domain

Formyl transferase, N-terminal
G3DSA:3.40.50.170	$\"[94-288]T$	no description
PF00551	$\"[94-271]T$	Formyl_trans_N

InterPro
IPR002912
Domain

Amino acid-binding ACT
PF01842	$\"[14-79]T$	ACT

InterPro
IPR004810
Family

Formyltetrahydrofolate deformylase
PR01575	$\"[16-42]T$ $\"[48-60]T$ $\"[95-117]T$ $\"[117-144]T$ $\"[241-263]T$ $\"[263-288]T$	FFH4HYDRLASE
PIRSF036480	$\"[11-290]T$	Formyltetrahydrofolate deformylase
TIGR00655	$\"[14-289]T$	PurU: formyltetrahydrofolate deformylase

noIPR
unintegrated

unintegrated
PTHR10520	$\"[172-289]T$	PHOSPHORIBOSYLAMINE-GLYCINE LIGASE-RELATED
PTHR10520:SF7	$\"[172-289]T$	FORMYLTETRAHYDROFOLATE DEFORMYLASE

","BeTs to 13 clades of COG0788COG name: Formyltetrahydrofolate hydrolaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0788 is -o-----q-dr-bcefghs-uj----Number of proteins in this genome belonging to this COG is 1","***** IPB004810 (Formyltetrahydrofolate deformylase signature) with a combined E-value of 2.3e-75. IPB004810A 16-42 IPB004810B 48-60 IPB004810C 95-117 IPB004810D 117-144 IPB004810E 241-263 IPB004810F 263-288 IPB004810F 198-223","Residues 15-75 are 70% similar to a (FORMYLTETRAHYDROFOLATE DEFORMYLASE HYDROLASE UPF0237 TRANSCRIPTIONAL CLEAVAGE SYSTEM PHOSPHATASE GLYCINE PHOSPHOSERINE) protein domain (PD407153) which is seen in Q6AD84_BBBBB.Residues 15-147 are 50% similar to a (PURU) protein domain (PD764804) which is seen in Q8D2I4_WIGBR.Residues 69-149 are 54% similar to a (PURU) protein domain (PDA1A8I9) which is seen in Q9X7F7_METCH.Residues 87-144 are 68% similar to a (FORMYLTETRAHYDROFOLATE HYDROLASE DEFORMYLASE) protein domain (PDA1B616) which is seen in Q6A6Z6_PROAC.Residues 176-279 are similar to a (TRANSFERASE FORMYLTRANSFERASE METHIONYL-TRNA PHOSPHORIBOSYLGLYCINAMIDE BIOSYNTHESIS METHYLTRANSFERASE FORMYLTETRAHYDROFOLATE DEFORMYLASE HYDROLASE TRANSFORMYLASE) protein domain (PD001209) which is seen in Q6AD84_BBBBB.Residues 176-269 are 55% similar to a (TRANSFERASE 5_apos;-PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE) protein domain (PD234962) which is seen in Q9XAT1_RHILE.Residues 245-289 are 73% similar to a (FORMYLTETRAHYDROFOLATE DEFORMYLASE HYDROLASE FORMYL-FH4 METABOLISM PLASMID PURINE ONE-CARBON PROBABLE BIOSYNTHESIS) protein domain (PD237291) which is seen in Q8GAI2_ARTNI.","","-59% similar to PDB:1MEJ Human Glycinamide Ribonucleotide Transformylase domain at pH 8.5 (E_value = 5.2E_13);-59% similar to PDB:1MEN complex structure of human GAR Tfase and substrate beta-GAR (E_value = 5.2E_13);-59% similar to PDB:1MEO human glycinamide ribonucleotide Transformylase at pH 4.2 (E_value = 5.2E_13);-59% similar to PDB:1NJS human GAR Tfase in complex with hydrolyzed form of 10-trifluoroacetyl-5,10-dideaza-acyclic-5,6,7,8-tetrahydrofolic acid (E_value = 5.2E_13);-59% similar to PDB:1RBM Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid (E_value = 5.2E_13);","Residues 14 to 79 (E_value = 3e-10) place ANA_0184 in the ACT family which is described as ACT domain.Residues 94 to 271 (E_value = 1.5e-42) place ANA_0184 in the Formyl_trans_N family which is described as Formyl transferase.","","deformylase (fragment)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0185","198634","198512","123","12.41","13.14","4569","ATGAAGGTTCGAGCCTCGATCCGGTCCCTGGCCAAGCAGCCGGGGTCCAAGGTGGTCCGACGCCGCGGCCACACCTACGTCATCAACAAGAAGAACCCCCGCCTCAAGGCCCGCCAGGGCTGA","MKVRASIRSLAKQPGSKVVRRRGHTYVINKKNPRLKARQG$","Ribosomal protein L36","Extracellular, Cytoplasm","ribosomal protein L36","hypothetical protein predicted by Glimmer/Critica","ribosomal protein L36","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000473
Family

Ribosomal protein L36
PD002101	$\"[1-39]T$	Q6NFL5_CORDI_Q6NFL5;
PF00444	$\"[1-40]T$	Ribosomal_L36
TIGR01022	$\"[1-40]T$	rpmJ_bact: ribosomal protein L36

","BeTs to 10 clades of COG0257COG name: Ribosomal protein L36Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0257 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 1-39 are similar to a (RIBOSOMAL L36 50S CHLOROPLAST RIBONUCLEOPROTEIN SEQUENCING B DIRECT MITOCHONDRION MITOCHONDRIAL) protein domain (PD002101) which is seen in Q6NFL5_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 40 (E_value = 1.2e-05) place ANA_0185 in the Ribosomal_L36 family which is described as Ribosomal protein L36.","","protein L36 (rpmJ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0186","199107","198715","393","10.08","8.82","14535","GTGCGGGCGGGGTGGGTCTGTGGGCCCGCACCCGCCGGGGCCCACGGCGCAGCACGTTCGCAGCCGCTCCCCTCTCAGCACCGCTGCCGGTACTCGTTCACCACGTCAGTTCTCACATTCACCCCCTTCCAAGGAGCTCGTATGCGTCCTGGGATCCACCCCAGTTACCAGCCCATCGTCTTTCGTGACAAGTCCGCAGGCTTCGCCTTCCTGACCCGTTCGACCCTGACGTCGTCGGAGACCATCGAGTGGGAGGACGGCAACACCTACCCGGTCTACGACGTCGAGGTCTCCAGCGCCTCGCACCCGTTCTGGACCGGCCAGGGCCGCATCCTGGACACGGCCGGCCGGGTGGAGAAGTTCGAGCGCCGCTACGGCAAGCGCAAGCGGTAG","VRAGWVCGPAPAGAHGAARSQPLPSQHRCRYSFTTSVLTFTPFQGARMRPGIHPSYQPIVFRDKSAGFAFLTRSTLTSSETIEWEDGNTYPVYDVEVSSASHPFWTGQGRILDTAGRVEKFERRYGKRKR$","Ribosomal protein L31","Extracellular","50S ribosomal protein L31 type B-2","putative ribosomal protein L31","ribosomal protein L31","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR002150
Family

Ribosomal protein L31
PR01249	$\"[49-66]T$ $\"[92-107]T$ $\"[107-125]T$	RIBOSOMALL31
PF01197	$\"[48-128]T$	Ribosomal_L31
TIGR00105	$\"[47-129]T$	L31: ribosomal protein L31
PS01143	$\"[96-117]T$	RIBOSOMAL_L31

","BeTs to 16 clades of COG0254COG name: Ribosomal protein L31Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0254 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB002150 (Ribosomal protein L31) with a combined E-value of 1.6e-28. IPB002150A 48-67 IPB002150B 87-125","Residues 48-126 are similar to a (RIBOSOMAL L31 50S TYPE RIBONUCLEOPROTEIN B CHLOROPLAST B-2 B-1 RPME) protein domain (PD003785) which is seen in R31C_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 48 to 128 (E_value = 5.7e-17) place ANA_0186 in the Ribosomal_L31 family which is described as Ribosomal protein L31.","","ribosomal protein L31 type B-2 (rpmE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0187","199417","199112","306","11.45","11.66","11593","ATGGCCAAGAAGTCCAAGATCGCCGCCGAGCTGCGGCGCCAGCAGGTGGTGGAGCGTTACGCCGAGCGCCGCGCCGAGCTCAAGCGGGCCTCGGTCAACCCTCACCTGAGCCAGGACGAGCGCGATGAGGCGATGGCGGCGCTGCACGCGCTGCCGCGAGACGCCTCCCCCACTCGCCTGCGTCGGCGTGACGTGGTGGACGGTCGTCCGCGCGGACACCTGCGCGTCACCGGGACCTCCCGGGTGCGCTTCCGCGAGATGGCGCTGCGCGGCGAGCTGCCGGGCATCGTCAAGTCCTCCTGGTAG","MAKKSKIAAELRRQQVVERYAERRAELKRASVNPHLSQDERDEAMAALHALPRDASPTRLRRRDVVDGRPRGHLRVTGTSRVRFREMALRGELPGIVKSSW$","Ribosomal protein S14","Cytoplasm, Extracellular","ribosomal protein S14p/S29e","30S ribosomal protein S14","ribosomal protein S14","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Chan Y.L., Suzuki K., Olvera J., Wool I.G. Zinc finger-like motifs in rat ribosomal proteins S27 and S29. Nucleic Acids Res. 1993. 21(3):649-655. PMID: 8441676","","","

InterPro
IPR001209
Family

Ribosomal protein S14
PTHR19836	$\"[1-101]T$	30S RIBOSOMAL PROTEIN S14
PF00253	$\"[46-100]T$	Ribosomal_S14

noIPR
unintegrated

unintegrated
G3DSA:4.10.830.10	$\"[41-101]T$	no description
PTHR19836:SF1	$\"[1-101]T$	CHLOROPLAST 30S RIBOSOMAL PROTEIN S14

","BeTs to 19 clades of COG0199COG name: Ribosomal protein S14Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0199 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001209 (Ribosomal protein S14) with a combined E-value of 3.5e-16. IPB001209 62-101","No significant hits to the ProDom database.","","-58% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.4E_14);-58% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.4E_14);-58% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 5.2E_14);-58% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 5.2E_14);-58% similar to PDB:2AVY Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 30S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 5.2E_14);","Residues 46 to 100 (E_value = 2.8e-10) place ANA_0187 in the Ribosomal_S14 family which is described as Ribosomal protein S14p/S29e.","","protein S14p-S29e (rpsN)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0188","199590","199417","174","11.27","10.39","6606","ATGAGCGGAGCCAAGGGCAAGGACCTGCGGCCGATCATCAAGATGGTCTCCACCGCGGGGACGGGCCACACCTACGTGACCCGCAAGAACCGCCGCAACACCCCTGACCGGCTGGTGCTGCGCAAGTTCGATCCGGTGGTGCGCCGGCACGTGGAGTACAAGGAGTCGCGCTGA","MSGAKGKDLRPIIKMVSTAGTGHTYVTRKNRRNTPDRLVLRKFDPVVRRHVEYKESR$","Ribosomal protein L33","Extracellular","ribosomal protein L33","K02913 large subunit ribosomal protein L33","ribosomal protein L33","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Kruft V., Kapp U., Wittmann-Liebold B. Characterization and primary structure of proteins L28, L33 and L34 from Bacillus stearothermophilus ribosomes. Biochimie 1991. 73(7):855-860. PMID: 1742360Sharp P.M. Identification of genes encoding ribosomal protein L33 from Bacillus licheniformis, Thermus thermophilus and Thermotoga maritima. Gene 1994. 139(1):135-136. PMID: 8112583","","","

InterPro
IPR001705
Family

Ribosomal protein L33
PD002595	$\"[10-57]T$	Q6A5U7_PROAC_Q6A5U7;
PF00471	$\"[10-57]T$	Ribosomal_L33
TIGR01023	$\"[1-57]T$	rpmG_bact: ribosomal protein L33
PS00582	$\"[25-44]T$	RIBOSOMAL_L33

","BeTs to 18 clades of COG0267COG name: Ribosomal protein L33Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0267 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001705 (Ribosomal protein L33) with a combined E-value of 1.5e-19. IPB001705 25-57","Residues 10-57 are similar to a (RIBOSOMAL L33 50S RIBONUCLEOPROTEIN CHLOROPLAST TYPE SEQUENCING DIRECT RNA-BINDING TRNA-BINDING) protein domain (PD002595) which is seen in Q6A5U7_PROAC.","","-80% similar to PDB:1P85 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 4.3E_13);-80% similar to PDB:1P86 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 4.3E_13);-80% similar to PDB:1VS6 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 50s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 4.3E_13);-80% similar to PDB:1VS8 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 4.3E_13);-80% similar to PDB:2AW4 Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 50S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 4.3E_13);","Residues 10 to 57 (E_value = 1.4e-13) place ANA_0188 in the Ribosomal_L33 family which is described as Ribosomal protein L33.","","protein L33 (rpmG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0189","199925","199587","339","11.12","12.61","12583","ATGTCAGCGAGGTTGCCGGCAAAGTCATCCGAGGGATCGGTCACGAGGTCCTCCAGCAGAGTTGACGAAACTGAGAATCATTCTTATATCATGCTCGTCATGACCACCTACTGCCAAGTCACGGGGGCCCGGCCTGTCTTCGGCCGGTCCGTCTCCCACTCCCACAAGCGCACGCCCCGGCGCTGGGATCCCAACCTGCAGCGCAAGCGCTACTGGGTGCCCTCCCTGGGGCGCACCGTGCGCCTGACGGTGTCCGCCAAGGGCATCCGCACGATCGACAAGCTGGGCATCGACGTCGTCGTGGCTCAGATGCTTGCCCGAGGGGAGAAGCTGTCATGA","MSARLPAKSSEGSVTRSSSRVDETENHSYIMLVMTTYCQVTGARPVFGRSVSHSHKRTPRRWDPNLQRKRYWVPSLGRTVRLTVSAKGIRTIDKLGIDVVVAQMLARGEKLS$","Ribosomal protein L28","Cytoplasm, Periplasm","50S ribosomal protein L28-1","ribosomal protein L28","ribosomal protein L28","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001383
Family

Ribosomal protein L28
PF00830	$\"[38-96]T$	Ribosomal_L28
TIGR00009	$\"[34-91]T$	L28: ribosomal protein L28

","BeTs to 18 clades of COG0227COG name: Ribosomal protein L28Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0227 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001383 (Ribosomal protein L28) with a combined E-value of 5.2e-16. IPB001383 34-67","Residues 34-69 are similar to a (RIBOSOMAL L28-2 50S) protein domain (PD614562) which is seen in R28B_MYCTU.Residues 37-90 are similar to a (RIBOSOMAL L28 50S CHLOROPLAST PEPTIDE SEQUENCING DIRECT TRANSIT PRECURSOR L28) protein domain (PD003595) which is seen in Q8FR24_COREF.Residues 71-111 are similar to a (RIBOSOMAL 50S L28 L28-2) protein domain (PD418397) which is seen in Q6A5U8_PROAC.","","-70% similar to PDB:2I2T Crystal Structure of Ribosome with messenger RNA and the Anticodon stem-loop of P-site tRNA. This file contains the 50s subunit of one 70s ribosome. The entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 2.3E_17);-70% similar to PDB:2I2V Crystal Structure of Ribosome with messenger RNA and the Anticodon stem-loop of P-site tRNA. This file contains the 50s subunit of one 70s ribosome. The entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 2.3E_17);-42% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 2.3E_17);-42% similar to PDB:2J01 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 2 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE I. (E_value = 2.3E_17);-42% similar to PDB:2J03 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 4 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE II. (E_value = 2.3E_17);","Residues 38 to 96 (E_value = 8.4e-26) place ANA_0189 in the Ribosomal_L28 family which is described as Ribosomal L28 family.","","ribosomal protein L28-1 (rpL28)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0190","200167","201087","921","4.69","-23.55","32056","ATGCCCTCCACCTGCCCCACCTGCTCCCTACGGGAGGTCCTGGCCGCCGTCGCCCAGGACCGCGCCGCCCAGGACCCGGGCGGCACCACCGTCATCCTCCTGCCGGCGGCCATCGAGCTCGCCCACCTCCTGCCCGGCCTGGCCGAGGAGCTCGCCGGCACCGGCGTCAGACTGGCCGGAGCCGCCCACGTCCTGGACGCCACCACCGCCCTGGACGAGCTCCTCGAGCACCGCCAGCTGAGCGCCTTCCCCGGCGACACCCGCTGCACGGGCGCCGTCCACCTGACCAACCTCGGATACGCCGACCTCGTCCTGGCCCTGGGGCGCGATGAGGACCCCGCCGGGGCCGACCTCATCGAGCACCTGCGCCCCCACGACGCCCTCCTGCTCCCAGGCCTCGACGCACCCCTCCTGGAGACCCTCACCACCCTCACCCATGACGCCGCCGCCTCCTTGAGCCGCATCCACCCCGCCACCACCAGCGCCTGGGGCGGCCCCGATGAGCACGGCGTGTGGACCCTCGACCTCAGCGCCTCCCTGCCCTTCCACCCCGAGCGCCTGCGCTCCCTCGTCGTTGAGCTCGCCGGTCAGGGCCTGTGCGCTCGCGGCTGCTTCTGGCTGCCCAGCCGTCCCGGTCGGGTCTGCACCTGGGAGGTCGCCGGAGGCGCCGTGAGCGTCGGCGACGCCGGTACCTGGGCGGAGGTCCCGGCCGCCCCCTCCGGTGCCGACGACGACGCGGCCGGCGAGCCCCGCTGCCATCTCGTGGTCACCGGTGTCGGGGACGAGGAGATGCGCGAGCAGGTGCGCCGCGCCTTCTCCCGGATCCTCCTGCGCCCCGAGGAGATGGCCCAGGCCCTGGCCTGGATCGGTGCCGACGACGGCCTGGGCGACTGGTTCGGGCAGGAGGACCCGGAGGGCTGA","MPSTCPTCSLREVLAAVAQDRAAQDPGGTTVILLPAAIELAHLLPGLAEELAGTGVRLAGAAHVLDATTALDELLEHRQLSAFPGDTRCTGAVHLTNLGYADLVLALGRDEDPAGADLIEHLRPHDALLLPGLDAPLLETLTTLTHDAAASLSRIHPATTSAWGGPDEHGVWTLDLSASLPFHPERLRSLVVELAGQGLCARGCFWLPSRPGRVCTWEVAGGAVSVGDAGTWAEVPAAPSGADDDAAGEPRCHLVVTGVGDEEMREQVRRAFSRILLRPEEMAQALAWIGADDGLGDWFGQEDPEG$","G3E family GTPase","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PTHR13748	$\"[167-284]T$	COBW-RELATED
PTHR13748:SF4	$\"[167-284]T$	COBALAMIN SYNTHESIS PROTEIN, PUTATIVE

","BeTs to 4 clades of COG0523COG name: Putative GTPases (G3E family)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0523 is ------yq-dr-bcefg-snuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-45% similar to PDB:1K5C Endopolygalacturonase I from Stereum purpureum at 0.96 A resolution (E_value = );-45% similar to PDB:1KCC Endopolygalacturonase I from Stereum purpureum complexed with a galacturonate at 1.00 A resolution. (E_value = );-45% similar to PDB:1KCD Endopolygalacturonase I from Stereum purpureum complexed with two galacturonate at 1.15 A resolution. (E_value = );-39% similar to PDB:1UAY Crystal Structure of Type II 3-Hydroxyacyl-CoA Dehydrogenase from Thermus thermophilus HB8 (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0191","201387","202697","1311","5.98","-8.68","46077","ATGACCGCGCAAGCCGTCACCCCGTCCCTGAACCAGCCGCTGGCCGAGCTCGACCCGGACATCGCCGGGGTCCTCACCGGCGAGCTCGCCCGCCAGCGCGAGACCCTGGAGATGATCGCCTCGGAGAACTTCGTTCCCCGGGCCGTCCTGGAGTGCCAGGGCTCGGTCCTGACCAACAAGTACGCGGAGGGCTACCCGGGCCGCCGCTACTACGGCGGCTGCGAGGTCGTCGACGTCGCCGAGTCCCTGGCCATCGAGCGCGCCAAGGCCGTCTTCGACGCCGAGTGGGCCAACGTCCAGCCCCACTCCGGAGCCCAGGCCAACGCCGCCGTCCTCCACGCCCTGGCCACCCCCGGCGACACCCTCCTGGGCCTGTCCCTGGCCCACGGCGGCCACCTCACCCACGGCATGAAGATCAACTTCTCCGGCAAGAACTACAACGCCACCGCTTACGGCGTGGACGAGACCACCATGCGCATCGAGATGGACCAGGTGCGCGAGGCCGCCCTGCGCGAGCGCCCCGCGGTCATCATCGCCGGCTGGTCGGCCTACCCCCGCCACCTCGACTTCGCCGCCTTCCGCTCCATCGCCGACGAGGTCGGCGCCGCCCTGTGGGTGGACATGGCCCACTTCGCCGGGCTCGTTGCCGCCGGCCTGCACCCCAACCCCGTCCCGCACGCCGACGTCGTGTCCACCACCGTCCACAAGACCCTGGGCGGCCCCCGCTCCGGCATGCTCCTGTCCAGCCGCGCCGAGCAGTGGGGCAAGAAGCTCAACTCCGCCGTCTTCCCCGGCCAGCAGGGCGGCCCCCTCATGCACGTCATCGCCGCCAAGGCCGTGGCCATGAAGATCGCCGGCACCGAGGAGTTCCGCGAGCGCCAGGAGCGCACCGTGCGCGGCGCCGCCATCATCGCCGAGCGTCTGGGGGCCGACGACGTCAAGGCCGCCGGCGTCAGCCTGGTCACCGGCGGCACCGACGTCCACCTGGTGCTGGTGGACCTGCGCGACTCCTCCCTGGACGGCCAGCAGGCCGAGGACCTCCTGCACACCGCCGGCATCACGGTCAACCGCAACGCCGTCCCCTTCGACCCACGTCCCCCGCGCGTCACCTCCGGCCTGCGCATCGGCACCCCCGCCCTGGCCACCCGCGGCTTCGGCGAGGCCGAGTTCACCGAGGTCGCCGACATCATCGCCGCCACCCTCGTCCACGGCGCCGCCGGCACTGCCGACGACGAGACCCTGGCCGCCCTGCGCGGTCGCGTGCGCGCCCTGACCGACGCCTTCCCCCTCTACCCGGGGCTGGCCCAGTGA","MTAQAVTPSLNQPLAELDPDIAGVLTGELARQRETLEMIASENFVPRAVLECQGSVLTNKYAEGYPGRRYYGGCEVVDVAESLAIERAKAVFDAEWANVQPHSGAQANAAVLHALATPGDTLLGLSLAHGGHLTHGMKINFSGKNYNATAYGVDETTMRIEMDQVREAALRERPAVIIAGWSAYPRHLDFAAFRSIADEVGAALWVDMAHFAGLVAAGLHPNPVPHADVVSTTVHKTLGGPRSGMLLSSRAEQWGKKLNSAVFPGQQGGPLMHVIAAKAVAMKIAGTEEFRERQERTVRGAAIIAERLGADDVKAAGVSLVTGGTDVHLVLVDLRDSSLDGQQAEDLLHTAGITVNRNAVPFDPRPPRVTSGLRIGTPALATRGFGEAEFTEVADIIAATLVHGAAGTADDETLAALRGRVRALTDAFPLYPGLAQ$","Serine hydroxymethyltransferase","Cytoplasm","serine hydroxymethyltransferase","serine hydroxymethyltransferase ","Glycine hydroxymethyltransferase","","Snell K., Baumann U., Byrne P.C., Chave K.J., Renwick S.B., Sanders P.G., Whitehouse S.K. The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase. Adv. Enzyme Regul. 2000. 40:353-403. PMID: 10828359Usha R., Savithri H.S., Rao N.A. The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases. Biochim. Biophys. Acta 1994. 1204(1):75-83. PMID: 8305478Trivedi V., Gupta A., Jala V.R., Saravanan P., Rao G.S., Rao N.A., Savithri H.S., Subramanya H.S. Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism. J. Biol. Chem. 2002. 277(19):17161-17169. PMID: 11877399Alexander F.W., Sandmeier E., Mehta P.K., Christen P. Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families. Eur. J. Biochem. 1994. 219(3):953-960. PMID: 8112347John R.A. Pyridoxal phosphate-dependent enzymes. Biochim. Biophys. Acta 1995. 1248(2):81-96. PMID: 7748903","","","

InterPro
IPR001085
Family

Glycine hydroxymethyltransferase
PIRSF000412	$\"[12-433]T$	Serine/glycine hydroxymethyltransferase
PTHR11680	$\"[16-436]T$	SERINE HYDROXYMETHYLTRANSFERASE
PF00464	$\"[14-397]T$	SHMT
PS00096	$\"[228-244]T$	SHMT

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[43-295]T$	no description

","BeTs to 26 clades of COG0112COG name: Glycine hydroxymethyltransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0112 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001085 (Glycine hydroxymethyltransferase) with a combined E-value of 1.9e-157. IPB001085A 39-93 IPB001085B 107-136 IPB001085C 189-242 IPB001085D 256-293 IPB001085E 317-363","Residues 18-66 are 89% similar to a (SERINE TRANSFERASE HYDROXYMETHYLTRANSFERASE PHOSPHATE PYRIDOXAL METABOLISM ONE-CARBON SHMT METHYLASE METHYLTRANSFERASE) protein domain (PD498026) which is seen in Q73WG1_MYCPA.Residues 22-104 are 90% similar to a (SERINE TRANSFERASE HYDROXYMETHYLTRANSFERASE PHOSPHATE PYRIDOXAL METABOLISM ONE-CARBON SHMT METHYLASE METHYLTRANSFERASE) protein domain (PD497395) which is seen in GLYA_COREF.Residues 137-221 are 87% similar to a (SERINE TRANSFERASE HYDROXYMETHYLTRANSFERASE PHOSPHATE PYRIDOXAL METABOLISM ONE-CARBON SHMT METHYLASE METHYLTRANSFERASE) protein domain (PD499089) which is seen in GLYA_COREF.Residues 222-363 are 88% similar to a (SERINE TRANSFERASE HYDROXYMETHYLTRANSFERASE PHOSPHATE PYRIDOXAL METABOLISM ONE-CARBON SHMT METHYLASE METHYLTRANSFERASE) protein domain (PD604370) which is seen in GLYA_CORGL.Residues 367-401 are 91% similar to a (SERINE TRANSFERASE HYDROXYMETHYLTRANSFERASE PHOSPHATE PYRIDOXAL METABOLISM ONE-CARBON SHMT METHYLASE METHYLTRANSFERASE) protein domain (PD001547) which is seen in GLYA_MYCLE.Residues 372-436 are 64% similar to a (SERINE METHYLTRANSFERASE TRANSFERASE HYDROXYMETHYLTRANSFERASE) protein domain (PDA0X5M0) which is seen in Q8G5H8_BIFLO.","","-61% similar to PDB:2DKJ Crystal Structure of T.th.HB8 Serine Hydroxymethyltransferase (E_value = 5.4E_103);-59% similar to PDB:1KKJ Crystal Structure of Serine Hydroxymethyltransferase from B.stearothermophilus (E_value = 2.7E_99);-59% similar to PDB:1KKP Crystal Structure of Serine Hydroxymethyltransferase complexed with Serine (E_value = 2.7E_99);-59% similar to PDB:1KL1 Crystal Structure of Serine Hydroxymethyltransferase Complexed with Glycine (E_value = 2.7E_99);-59% similar to PDB:1KL2 Crystal Structure of Serine Hydroxymethyltransferase Complexed with Glycine and 5-formyl tetrahydrofolate (E_value = 2.7E_99);","Residues 14 to 397 (E_value = 4.1e-220) place ANA_0191 in the SHMT family which is described as Serine hydroxymethyltransferase.","","hydroxymethyltransferase (glyA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0192","202694","203590","897","5.41","-6.99","30583","GTGAGGGCTCCCTGGAACGGGGCGGCCCGAGTCCTGGACGGCAAGGCCACGGCCGCCGCCCTCAAGGCCGAGCTCAAGGAGCGCGTCGCGGTACTGCGCGAGCGCGGCGTCACCCCCGGCCTGGGCACGGTCCTGGTGGGGGAGGACCCCGGCAGCGTCAAGTACGTCGCCGGCAAGCACGCCGACTGCGCCGAGGTCGGCATCCTCTCCATCCGCGAGGACCTGCCGGCCACCGCCACCCAGGCCGAGGTTGAGGCCGCCGTCGACCGCCTCAATGCGGATGACGCCTGCACCGGCTACATCGTCCAGCTCCCGCTGCCGGCGGGCGTGGACACCAACGCGATCCTGGAGCGCGTCGACCCGGCCAAGGACGCCGACGGCCTGCACCCCACCAACCTGGGGCGCCTGGTGCTGCGGGCCTCGGGGCCCATCGACTCGCCCCTGCCCTGCACGCCGCGCGGCTGCATCGAGCTCATGGAGCGCCACGGCATCGACCTGGCCGGCCGTAACGTGTGCGTCGTCGGCCGCGGGGTCACGGTGGGCCGCTCCATCGGCCTGCTCCTGGGACGCAAGGACGTCAACGCCACCGTGGACATCTGCCACACCGGCACCACGGACCTGGCCGAGCACGTGCGCCGGGCTGACGTCGTCATCTCGGCGGCCGGCAGCCCCGGCATCATCACCCCGGAGATGGTCGCCCCCGGCGCCGTCGTCCTGGATGTGGGCGTCTCGCGCGTCGTCGACCCCGCTACCGGCAAGGGCCGCATCGCCGGTGACGTCGCTGACGGCGTCGACGAGGTGGCCTCCTGGCTCTCGCCCAACCCCGGCGGCGTGGGCCCCATGACCCGCGCCCTGCTGCTGGCCAACGTGGTCGAGACCGCGGAGCGCTCGCTCTGA","VRAPWNGAARVLDGKATAAALKAELKERVAVLRERGVTPGLGTVLVGEDPGSVKYVAGKHADCAEVGILSIREDLPATATQAEVEAAVDRLNADDACTGYIVQLPLPAGVDTNAILERVDPAKDADGLHPTNLGRLVLRASGPIDSPLPCTPRGCIELMERHGIDLAGRNVCVVGRGVTVGRSIGLLLGRKDVNATVDICHTGTTDLAEHVRRADVVISAAGSPGIITPEMVAPGAVVLDVGVSRVVDPATGKGRIAGDVADGVDEVASWLSPNPGGVGPMTRALLLANVVETAERSL$","Methenyltetrahydrofolate cyclohydrolase","Cytoplasm","bifunctional protein (methylenetetrahydrofolatedehydrogenase and methenyltetrahydrofolate","methenyltetrahydrofolate cyclohydrolase ","Methenyltetrahydrofolate cyclohydrolase","","Barlowe C.K., Williams M.E., Rabinowitz J.C., Appling D.R. Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme. Biochemistry 1989. 28(5):2099-2106. PMID: 2541774Price B.D., Laughon A. The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase. Biochim. Biophys. Acta 1993. 1173(1):94-98. PMID: 8485162","","","

InterPro
IPR000672
Domain

Tetrahydrofolate dehydrogenase/cyclohydrolase
PD002300	$\"[28-138]T$	Q6ADF1_BBBBB_Q6ADF1;
PR00085	$\"[39-61]T$ $\"[80-107]T$ $\"[115-136]T$ $\"[164-184]T$ $\"[215-244]T$ $\"[271-289]T$	THFDHDRGNASE
PF00763	$\"[10-126]T$	THF_DHG_CYH
PF02882	$\"[129-298]T$	THF_DHG_CYH_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.192.10	$\"[5-136]T$	no description
G3DSA:3.40.50.720	$\"[142-279]T$	no description
PTHR10025	$\"[19-296]T$	METHYLENETETRAHYDROFOLATE DEHYDROGENASE FAMILY MEMBER

","BeTs to 21 clades of COG0190COG name: 5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0190 is -o-p--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000672 (Tetrahydrofolate dehydrogenase/cyclohydrolase) with a combined E-value of 2.7e-96. IPB000672A 39-68 IPB000672B 75-127 IPB000672C 149-188 IPB000672D 214-244 IPB000672E 254-290","Residues 28-138 are similar to a (METHYLENETETRAHYDROFOLATE HYDROLASE DEHYDROGENASE CYCLOHYDROLASE BIFUNCTIONAL FOLD OXIDOREDUCTASE METHENYLTETRAHYDROFOLATE BIOSYNTHESIS INCLUDES:) protein domain (PD002300) which is seen in Q6ADF1_BBBBB.Residues 146-230 are similar to a (METHYLENETETRAHYDROFOLATE DEHYDROGENASE HYDROLASE CYCLOHYDROLASE BIFUNCTIONAL OXIDOREDUCTASE METHENYLTETRAHYDROFOLATE FOLD BIOSYNTHESIS INCLUDES:) protein domain (PD316754) which is seen in Q6A6Z2_PROAC.Residues 232-298 are similar to a (METHYLENETETRAHYDROFOLATE HYDROLASE DEHYDROGENASE CYCLOHYDROLASE BIFUNCTIONAL FOLD METHENYLTETRAHYDROFOLATE OXIDOREDUCTASE BIOSYNTHESIS INCLUDES:) protein domain (PD638816) which is seen in Q6ADF1_BBBBB.","","-56% similar to PDB:2C2X THREE DIMENSIONAL STRUCTURE OF BIFUNCTIONAL METHYLENETETRAHYDROFOLATE DEHYDROGENASE-CYCLOHYDROLASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.5E_63);-56% similar to PDB:2C2Y THREE DIMENSIONAL STRUCTURE OF BIFUNCTIONAL METHYLENETETRAHYDROFOLATE DEHYDROGENASE-CYCLOHYDROLASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.5E_63);-49% similar to PDB:1B0A 5,10, METHYLENE-TETRAHYDROPHOLATE DEHYDROGENASE/CYCLOHYDROLASE FROM E COLI. (E_value = 4.6E_36);-49% similar to PDB:1A4I HUMAN TETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE (E_value = 4.4E_31);-49% similar to PDB:1DIA HUMAN METHYLENETETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE COMPLEXED WITH NADP AND INHIBITOR LY249543 (E_value = 4.4E_31);","Residues 10 to 126 (E_value = 6.5e-52) place ANA_0192 in the THF_DHG_CYH family which is described as Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain.Residues 129 to 298 (E_value = 5.6e-85) place ANA_0192 in the THF_DHG_CYH_C family which is described as Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain.","","protein (methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase) (NADP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0193","203633","205375","1743","5.61","-15.77","61987","ATGACGGACGAGTCCCACGGCGCCCATCCCTCCCATCCTGACCACCCCACCCATCCGGCTGAGTCGGCAGGCTCCACGAGCTCCTCGGAGCCTGAGCCGGCTCAGCCGGAGGTGTGTCCGCCGGCCCCTGGGGACGCGGCGCCGGTGGCGCCCTCGCCGGACGCGACCGGCTCCCAGGACCCGCAGCCGCACAGGACCGGCCTGCGGCGTCGGACCTTGATCCTCAGCGCGGCCGGCGCCGGCGCTCTCATCGTGGGCGGAGCCGTCCTGGTGCGCTGCTCCACGGGGCGCCGGAGCTCGCCGAAGCCCACGGCCACCGACTCGCCGGCCTCGGCCGCCTACCGCCCCGCCTACCACTACAGCCCCGCCACGGGGAATCTCGCCGACCCCAACGGCCTGGTCCTCTACGAGGGCGAGTACCACCTCTTCCACCAGCAGGACGGCACCTGGGCCCACGCGATCAGCCCTGACATGGTGCACTGGAAGCGCCAGGGGACGGCCCTGAAGCACGACGCGCAGGGCCTGGCCATGTCCGGCAGCTGCGTCGTCGACGGCGCCGACACCTCCGGCCTGGTCGCCGGCGGCGGCATGGTGGCCGTCTACACCTCCACCCAGGGCGGTGAGGCCCAGTCCCTGGCCTACTCCACCGACCGGGGGAGGAGCTGGCGGCGCTTCTCCGGCAACCCCGTCATCCCCAACGACGGGCGCAAGGACTTCCGCGACCCCAAGGTCTTCTGGCACGAGGACTCCAAGGCCTGGATCATGATCGTCTCCGCCGGGGACCACGTCTCCCTCTTCCGCTCCACCGACCTCAAGGCCTGGAGACACGCCAGCGACTTCGGCCAGGGCATCGGCTCGCACGCCGCCGTATGGGAGTGCCCCGACCTCTTCCCCCTGACCGACTCCAGCGACGGGCGCACCCGCTGGGTCGTGACCCTCTCGGTGGGAGCCAACGAGGAGACGGCCGGCTCCACCGCCCAGTACTTCATCGGCGACTTCGACGGCTCCGTCTTCTTCCCCGAGGACCGCGACACCCGCTTCACCGACGTCGGCCAGGACTTCTACGCCGCCCAGAGCTTCGAGCACATCGAGGGCCGCCGCGTGTGGATGGCCTGGCTGGGCAACTGGAACTACCCCTACTCGCTTCCCACCGGGGAGTGGCGCGGTGAGATGAGCATCCCGCGCGAGCTGTCCCTGACCACCATCGGCGGCAAGCGCACCCTCGTGCAGAAACCCATCCCCGAGCTCGACGCCCTGCGCGGGCGGGCCACCGACCTCTCCGGCCTCAAGGCCACCGACACGGTGACGGCTCTAGGCTCGGGCCGCACGGTCGAGATCGACTTGACGTTGGACGTCTCCCAGGCCTCTGAGGCCTGGCTGGGACTGGCCCGCGGCACAGTCGATGGCAAGACCCAGGAGATGCGCGTCGGCGTCGACATCTCGGCCGGCACCCTCTACCTCGACCGCACCGACGGAGGGCTTACACAGGTCGACGGCAAGGACGAGGGGACCACCACCGACTTCGCCCTGCGCCGCCAGACGCAGTACCGCCCCACCGGCTCCACAGTGCGTCTGCACCTCTACCTGGACCGCTCCAGCCTCGAGGTCTTCGTCGACGACGGCGCCACCGTCGGCAGCCTCCTGGTCTTCACCGACCCCTCCTGCCAGGAGATCGTCCTGGGCGCCAAGGGCACGGCCACCATCACGTCGGGAAGCCTCACCCCTCTGGCCGCAGCCCTGTAA","MTDESHGAHPSHPDHPTHPAESAGSTSSSEPEPAQPEVCPPAPGDAAPVAPSPDATGSQDPQPHRTGLRRRTLILSAAGAGALIVGGAVLVRCSTGRRSSPKPTATDSPASAAYRPAYHYSPATGNLADPNGLVLYEGEYHLFHQQDGTWAHAISPDMVHWKRQGTALKHDAQGLAMSGSCVVDGADTSGLVAGGGMVAVYTSTQGGEAQSLAYSTDRGRSWRRFSGNPVIPNDGRKDFRDPKVFWHEDSKAWIMIVSAGDHVSLFRSTDLKAWRHASDFGQGIGSHAAVWECPDLFPLTDSSDGRTRWVVTLSVGANEETAGSTAQYFIGDFDGSVFFPEDRDTRFTDVGQDFYAAQSFEHIEGRRVWMAWLGNWNYPYSLPTGEWRGEMSIPRELSLTTIGGKRTLVQKPIPELDALRGRATDLSGLKATDTVTALGSGRTVEIDLTLDVSQASEAWLGLARGTVDGKTQEMRVGVDISAGTLYLDRTDGGLTQVDGKDEGTTTDFALRRQTQYRPTGSTVRLHLYLDRSSLEVFVDDGATVGSLLVFTDPSCQEIVLGAKGTATITSGSLTPLAAAL$","Levanase","Extracellular, Periplasm, Cellwall","levanase precursor","levanase ","Levanase","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR001362
Family

Glycoside hydrolase, family 32
SM00640	$\"[119-541]T$	Glyco_32

InterPro
IPR013148
Domain

Glycosyl hydrolases family 32, N-terminal
PF00251	$\"[119-412]T$	Glyco_hydro_32N

InterPro
IPR013189
Domain

Glycosyl hydrolase family 32, C-terminal
PF08244	$\"[446-541]T$	Glyco_hydro_32C

noIPR
unintegrated

unintegrated
G3DSA:2.60.120.560	$\"[413-576]T$	no description
tmhmm	$\"[73-91]?$	transmembrane_regions

","BeTs to 5 clades of COG1621COG name: Beta-fructosidases (levanase/invertase)Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1621 is ------y-v--lb-e-gh--------Number of proteins in this genome belonging to this COG is 5","***** IPB013148 (Glycosyl hydrolases family 32, N terminal) with a combined E-value of 1.5e-12. IPB013148A 351-366 IPB013148B 525-551***** IPB001362 (Glycoside hydrolase, family 32) with a combined E-value of 6.1e-10. IPB001362 118-146","Residues 114-259 are 66% similar to a (HYDROLASE GLYCOSIDASE INVERTASE SUCROSE-6-PHOSPHATE PRECURSOR SIGNAL BETA-FRUCTOFURANOSIDASE ACID TRANSFERASE WALL) protein domain (PD581674) which is seen in SACC_BACSU.Residues 171-261 are 53% similar to a (GLYCOSIDASE HYDROLASE EXOINULINASE PRECURSOR SIGNAL EXO-INULINASE SUCROSE:SUCROSE 1-FRUCTOSYLTRANSFERASE TRANSFERASE) protein domain (PDA1E406) which is seen in Q6S3E2_ASPNG.Residues 205-262 are 63% similar to a (GLYCOSIDASE HYDROLASE INVERTASE MULTIGENE BETA-FRUCTOFURANOSIDASE FAMILY PRECURSOR GLYCOPROTEIN SACCHARASE SIGNAL) protein domain (PD761343) which is seen in Q93T55_BBBBB.Residues 260-420 are 61% similar to a (HYDROLASE GLYCOSIDASE INVERTASE SUCROSE-6-PHOSPHATE PRECURSOR SIGNAL ACID BETA-FRUCTOFURANOSIDASE TRANSFERASE WALL) protein domain (PD186064) which is seen in Q8RLU2_PAEPO.","","-49% similar to PDB:1Y4W Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21 (E_value = 7.8E_68);-49% similar to PDB:1Y9G Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose (E_value = 7.8E_68);-49% similar to PDB:1Y9M Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 (E_value = 7.8E_68);-43% similar to PDB:1UYP THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA (E_value = 2.9E_30);-43% similar to PDB:1W2T BETA-FRUCTOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH RAFFINOSE (E_value = 6.5E_30);","Residues 119 to 412 (E_value = 8.9e-93) place ANA_0193 in the Glyco_hydro_32N family which is described as Glycosyl hydrolases family 32 N terminal.Residues 446 to 541 (E_value = 1.5e-08) place ANA_0193 in the Glyco_hydro_32C family which is described as Glycosyl hydrolases family 32 C terminal.","","precursor ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0194","206984","205476","1509","5.16","-14.13","55043","ATGCAGATCCAGCGCGTCTCCAACCCCAATGCGCCGTCGGGCACCAACTCGATGCCCGAGCAGCTCACGATGCCGGAGATCTCCAACGGCTTCCCGGCCACAAGCGAGGACGTGTGGGTGTGGGACACCTGGACGCTGACTGACGAGGCCGCCCACCAGATCTCCTACAACGGCTGGGAGATCGCCTTCTCCCTGGTGGCCGACCGGCACGCCGGCTACACCTTCGACGACCGCCACACCCACGCGCGACTGGGCTTCTTCTACCGCAAGGCCGGCACGCAGACCTCCTCGGCCGACGGCGCGAACAGCTCCAACGGCGGGTGGATCTACGGGGGGCACGTCTTCCCCGACGGCGCCTCCGGCTCGATCTTCGAGGACCAGAGCTTCACGGCCCAGACCGAGTGGTCCGGCTCGGCCCGCCTCATGGAGGGCAACAAGATCCGCATGTTCTACACCTCGGTGGCCTTCTACAACACCACCACCGGCGGCAGCGGCGACGGGGGCTACGGTCAGGACGGCAACAACGCGGCCTCCAAGCCCTACGACCCGCGGATCGTGCAGTCCGAGGGACGCATCTACGCTGACGAGAACGGCGTGTGGCTCACCGGGTTCCGCACCCAGCACCAGCTTCTCGTCCCGGACGGCAAGTACTACCAGACCCGTGAGCAGAACCCGGGCGTGAACTTCCGCGACCCCTTCACCTTCCGCGACCAGAACAACCCCTCGGACCCCACCGAGTACATGGTCTTCGAGGGCAACTCGGCCTTCGTCCGTGAGCAGCAGTACGTCGACGCCGCGGCCAAGGCCGGTCAGAACACCGCTGTGGCCACCTGCACCGCGGAGGACCTCGGCTACGAGCAGGGCGACCCCAAGGCCGAGACGGTCGAGTCGGTCAACCAGCGCGGCGGCCGCTACCAGCTGGCCAACGTGGGTCTGGCCCGGGCCAAGAACAAGGCGATGACCCAGTGGGAGTACCTGCCTCCGCTGCTGAGCGGCAACTGCGTCAACGATCAGACTGAGCGGCCGCAGATCTACTTCCAGGACGGCAAGTACTACCTGTTCACGATCTCGCACCGGGAGACCTACGCCGACGGGCTCCAGGGCCCCGAGGGCGTCTACGGCTTCGTGGGCGACGGGCTGCGAAGCGACTACAAGCCGCTCAACCAGAACACGGGTATCGCACTGGGCAACCCCATCAACCTCAACTTCAACCCGGGCAAGCCCTACTCGCCAGACTTCAACCAGAGCCCGTACACCTTCCAGTCCTACTCGCACTACGTCATGCCCGGCGGCCTGGTGGAGTCCTTCATCGACTCCATCGGCGGCAACAAGGACGGCAACCCGGTGCGTGGAGGCTCGCTGGCCCCGACGGTGAAGCTCACCATCTCCGGGGACACCACCTCGGTGGACCGCACCTACGGCACCAACGGCTTGGGGGGCTTCGCGGACATCCCCTCCGACAGGGCCCGCTCCAACGGCGGTGACACCCGCCCGCAGCGCCTGAAGTAG","MQIQRVSNPNAPSGTNSMPEQLTMPEISNGFPATSEDVWVWDTWTLTDEAAHQISYNGWEIAFSLVADRHAGYTFDDRHTHARLGFFYRKAGTQTSSADGANSSNGGWIYGGHVFPDGASGSIFEDQSFTAQTEWSGSARLMEGNKIRMFYTSVAFYNTTTGGSGDGGYGQDGNNAASKPYDPRIVQSEGRIYADENGVWLTGFRTQHQLLVPDGKYYQTREQNPGVNFRDPFTFRDQNNPSDPTEYMVFEGNSAFVREQQYVDAAAKAGQNTAVATCTAEDLGYEQGDPKAETVESVNQRGGRYQLANVGLARAKNKAMTQWEYLPPLLSGNCVNDQTERPQIYFQDGKYYLFTISHRETYADGLQGPEGVYGFVGDGLRSDYKPLNQNTGIALGNPINLNFNPGKPYSPDFNQSPYTFQSYSHYVMPGGLVESFIDSIGGNKDGNPVRGGSLAPTVKLTISGDTTSVDRTYGTNGLGGFADIPSDRARSNGGDTRPQRLK$","Fructosyltransferase","Extracellular","Levansucrase/Invertase superfamily","levansucrase ","Levansucrase","AAG09737","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR003469
Family

Glycoside hydrolase, family 68
PF02435	$\"[1-485]T$	Glyco_hydro_68

","No hits to the COGs database.","***** IPB003469 (Glycoside hydrolase, family 68) with a combined E-value of 4.5e-36. IPB003469A 243-259 IPB003469B 323-358","Residues are similar to a () protein domain () which is seen in .","","-63% similar to PDB:1W18 CRYSTAL STRUCTURE OF LEVANSUCRASE FROM GLUCONACETOBACTER DIAZOTROPHICUS (E_value = 3.2E_139);-41% similar to PDB:1OYG Crystal structure of Bacillus subtilis levansucrase (E_value = 2.2E_23);-41% similar to PDB:1PT2 Crystal structure of levansucrase (E342A) complexed with sucrose (E_value = 1.1E_22);-45% similar to PDB:1LML LEISHMANOLYSIN (E_value = 1.1E_22);-42% similar to PDB:2OZL Human pyruvate dehydrogenase S264E variant (E_value = 1.1E_22);","Residues 1 to 485 (E_value = 1.4e-145) place ANA_0194 in the Glyco_hydro_68 family which is described as Levansucrase/Invertase.","","superfamily ","","1","","","","","","","","","","","","Wed Aug 1 13:16:43 2007","Wed Aug 1 13:16:43 2007","","","Wed Aug 1 13:16:43 2007","Wed Aug 1 13:16:43 2007","Wed Aug 1 13:16:43 2007","","Wed Aug 1 13:16:43 2007","Wed Aug 1 13:16:43 2007","","","","","yes","","" "ANA_0195","207250","207417","168","8.27","1.13","5603","ATGGTGGGGGAGGCGCTGGGGGAAGGTGCCTCATCGGCGAGCGCAGTGGTGCCGGACCCGGCCACCAGGAGTCCGAGCGTCAGCGCCACGGCCAGTCGTCTGCGACGGGCGCGGAACGAAGTGTGTGTCACGGTCATTGTCCGTACTGTCCTTACTCATGAGGGATGA","MVGEALGEGASSASAVVPDPATRSPSVSATASRLRRARNEVCVTVIVRTVLTHEG$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0196","207722","208915","1194","5.06","-8.43","39682","GTGAGTATCATTCCCATCCGTCTGCGACGGTTATCCGCACCAACATCCGCTCTCCTGGCTGCGCTCGCCCTGGCTGCAGCCGGTCCGGCTGTGGCTGCCCCGGCATCGAACACAGCTGGGCAGTCCACCACCTCTCTGCGCAACACCTCCACGGTGAGCGCTCAGAGCCTCGCCCAGATGGTCGCCGGTCCGAAGGCGACAGTCTCCAACGCATCCGTCTCCGGCAAGGACGTCCAGATCGGCACGGTCAAGGGACTGCCTGGTGACGGCAACGCCATCACCGAGGGGGTTGCCCTATCCACCGGCTCCCTTATCGACCCCGATCCCACTGCCGACTCCGATACTGACATCACCCGCTCCGCCGTCCTGGGACCCAACGACGCCCTGGACACCACCGGTGACTTCGGCGTCGTCGAGGATCCGGCGGGACTGGCCAAGGTGGCCGGCACCGACGTCTACGACGAGGCCGTCCTGGAGTTCGACGTCACCGCCACCAGCTCCACCATCGTCCTCTACTACAGCCTCGGCTCCGAGGAGTACGCCGGCGCCACCGAGGGCACCCCGGCCTCCTGGCAGTCGCGCGGATACAAAGACCCGCTGAGCATCCAGGTCAACGGCACCGAGTGCGCCCACGTCCCCGGCACGCAGACGGCCGTGAGCGCCGCCTCGATCAACGAGTCCTCCAACGCCGCCTACTACACGGCCAATGTCTCGGGACACACCCCGGGACAGATCCCCGTGGAGTTCAACGGCTACACCTCCGCCCTGCCCTGCCAGGCCTCCGTCACCCCGGGGCAGAAGGTGCACGTGCGCGTGGCCATCGCCGACGCCCAGGACGGCCAGCTCGACTCCACGGTGCTCCTGCGCACCCAGGGACTGGGCTTCACCGACAAGCCGATCACCGACCCCTGCAACGCCAAGGCCGGCAGCTGTGACATCCCCGGCAACAGCAACGGCTCCAACGGGGCGAAGAACGGCAAGGACTCCGCCACTCCGCCCGGTCAGGGCAAGCCGGGCGTGACCGACTACAGCGTCGCCTCGCCCACCGCGAGCCCCAAGAAGACGGTGGCCGGTCTGCCCCTGACCGGAACCCAGGCGCTCTTCCTGGGAGGCATCGCCCTGCTGCTCCTGGCCGGCGGTGGTGTCGCGCTCATGCTGCGCCGTCGTCGCCTAACCGGCTCTGAGGCCGGCTGA","VSIIPIRLRRLSAPTSALLAALALAAAGPAVAAPASNTAGQSTTSLRNTSTVSAQSLAQMVAGPKATVSNASVSGKDVQIGTVKGLPGDGNAITEGVALSTGSLIDPDPTADSDTDITRSAVLGPNDALDTTGDFGVVEDPAGLAKVAGTDVYDEAVLEFDVTATSSTIVLYYSLGSEEYAGATEGTPASWQSRGYKDPLSIQVNGTECAHVPGTQTAVSAASINESSNAAYYTANVSGHTPGQIPVEFNGYTSALPCQASVTPGQKVHVRVAIADAQDGQLDSTVLLRTQGLGFTDKPITDPCNAKAGSCDIPGNSNGSNGAKNGKDSATPPGQGKPGVTDYSVASPTASPKKTVAGLPLTGTQALFLGGIALLLLAGGGVALMLRRRRLTGSEAG$","LPXTG-motif cell wall anchor domain","Extracellular, Periplasm, Cellwall","Gram positive anchor domain protein","conserved hypothetical protein","LPXTG-motif cell wall anchor domain","","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
PF00746	$\"[351-389]T$	Gram_pos_anchor
TIGR01167	$\"[358-390]T$	LPXTG_anchor: LPXTG-motif cell wall anchor
PS50847	$\"[359-396]T$	GRAM_POS_ANCHORING

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[366-386]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 38-299 are 42% similar to a (HEMAGGLUTININ-RELATED) protein domain (PDA1A0T4) which is seen in Q6ACZ1_BBBBB.","","-38% similar to PDB:1HG8 ENDOPOLYGALACTURONASE FROM THE PHYTOPATHOGENIC FUNGUS FUSARIUM MONILIFORME (E_value = );-46% similar to PDB:1YGA CRYSTAL STRUCTURE OF Saccharomyces cerevisiae YN9A PROTEIN, NEW YORK STRUCTURAL GENOMICS CONSORTIUM (E_value = );-38% similar to PDB:1JJ2 Fully Refined Crystal Structure of the Haloarcula marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution (E_value = );-38% similar to PDB:1K73 Co-crystal Structure of Anisomycin Bound to the 50S Ribosomal Subunit (E_value = );-38% similar to PDB:1K8A Co-crystal structure of Carbomycin A bound to the 50S ribosomal subunit of Haloarcula marismortui (E_value = );","Residues 351 to 389 (E_value = 1.3e-05) place ANA_0196 in the Gram_pos_anchor family which is described as Gram positive anchor.","","positive anchor domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0197","209236","209012","225","8.63","1.86","7970","ATGGAACCCGACGACGCCCGGGCGCCGCGCAGCGCCCGACGAGTCGGCGTGTGGATGGCGGTTATCGTCATCGCCGCCGCCTTGCCCGTGCTGGCTCAGACCTCGCTGCTGTCCCGCGTCAGCACCCTGTTGTGGCTGGCCTCCATGCCGCTGTGCATCCTGGGCTGTGCGATGCTGGCCAAGGAGCTGGCGGCGCGTCGCGCCTCCCGGCCGGAGGAGGACTGA","MEPDDARAPRSARRVGVWMAVIVIAAALPVLAQTSLLSRVSTLLWLASMPLCILGCAMLAKELAARRASRPEED$","Hypothetical protein","Cytoplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[41-61]?$	transmembrane_regions

InterPro
IPR001792
Domain

Acylphosphatase
PD001884	$\"[17-82]T$	Q9KSA4_VIBCH_Q9KSA4;
PR00112	$\"[13-28]T$ $\"[34-59]T$	ACYLPHPHTASE
PF00708	$\"[10-71]T$	Acylphosphatase
PS51160	$\"[13-101]T$	ACYLPHOSPHATASE_3
PS00150	$\"[18-28]T$	ACYLPHOSPHATASE_1

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.100	$\"[2-101]T$	no description
PTHR10029	$\"[14-100]T$	ACYLPHOSPHATASE

","BeTs to 12 clades of COG1254COG name: AcylphosphatasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1254 is a-mpkz--vd-lb-efgh---j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB001792 (Acylphosphatase) with a combined E-value of 1.4e-25. IPB001792A 13-63 IPB001792B 65-100***** IPB011125 (HypF Zn-finger) with a combined E-value of 3.1e-09. IPB011125A 15-51","Residues 7-85 are 55% similar to a (HYDROLASE ACYLPHOSPHATASE) protein domain (PD704844) which is seen in Q8PTD8_METMA.Residues 17-82 are similar to a (HYDROLASE ACYLPHOSPHATASE HYDROGENASE MATURATION HYPF PHOSPHOHYDROLASE ACYLPHOSPHATE ACYLPHOSPHATASE ISOZYME TYPE) protein domain (PD001884) which is seen in Q9KSA4_VIBCH.","","-63% similar to PDB:1V3Z Crystal Structure of Acylphosphatase from Pyrococcus horikoshii (E_value = 4.4E_13);-63% similar to PDB:1W2I CRYSTAL STRUCTUORE OF ACYLPHOSPHATASE FROM PYROCOCCUS HORIKOSHII COMPLEXED WITH FORMATE (E_value = 4.4E_13);-64% similar to PDB:2GV1 NMR solution structure of the Acylphosphatase from Eschaerichia Coli (E_value = 6.4E_12);-62% similar to PDB:1ULR Crystal structure of tt0497 from Thermus thermophilus HB8 (E_value = 9.2E_11);-62% similar to PDB:1Y9O 1H NMR Structure of Acylphosphatase from the hyperthermophile Sulfolobus Solfataricus (E_value = 1.2E_10);","Residues 10 to 101 (E_value = 1.9e-10) place ANA_0198 in the Acylphosphatase family which is described as Acylphosphatase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0199","209553","210434","882","5.33","-9.35","31965","ATGGACCTATCGTCTCAGGCTCAGGGCCGAGCGCGTAGGCTTGCCGCCATGCGTATCGCCACCGTCAACGTCAACGGCATCCGGGCCGCCGCCCGCAAGGGCATGGGGGAGTGGCTCGCCGCCTCCGCCCCCGACATCCTCCTGCTCCAGGAGGTCCGAGCCGACGAGCAGATCGCCGTCGACCTCCTGCCCGGCTACGAGGCCGCCATCTGGCCCTGCCGTATCAAGGGGCGTGCGGGCGTGGGCGTCGCCGTGCGCGAGGGCGGCCCGGCCACTCTCGGCGAGCTGCGCTACGGCGTTGCCGCTGCCGGCACCGAGGAGCCCGACGTCGACTCCGGCCGCTGGCTCGAGGCCGACCTGAGCCTCGCCGGCCTCGACGGCGTCGAGCAGCTCACCGTCATCTCCGCCTACCTGCATTCCGGCCAGCTGGGCACCGAGAAGATGGACCAGAAGTACGCCCACCTCGAGCTCGTCGATGCCCGCATGGCCGAGCTCCTGGCCGCCGCCCGTGATGGTGGGTCCCAGGTTGTCATGGCCGGGGACCTCAACGTGGTGCGCTCCGAGCGTGACATCAAGAACTGGAAGCCCAACCACAACAAGATCGCCGGCGTCATGGATGAGGAGATCGCCCACTTGGAGGGCTGGTTCGCCTCCGGCTGGGTGGACGCCTCGCGCCACCTCGTGGGGGATGAGGAGCAGGGGCCCTACACGTGGTGGTCCCAGCGCGGCAAGGCCTTCGACAACAACACCGGCTGGCGGATCGACTACCAGGTCCTCACCCCCGCCCTGGCCGAGCGGGCCCACAGCGTCACCGTGGACCGGGCGCCCGACTACGCCTCGCGCTGGTCCGACCATGCCCCGCTCGTCGTCGAGTACCGCTGA","MDLSSQAQGRARRLAAMRIATVNVNGIRAAARKGMGEWLAASAPDILLLQEVRADEQIAVDLLPGYEAAIWPCRIKGRAGVGVAVREGGPATLGELRYGVAAAGTEEPDVDSGRWLEADLSLAGLDGVEQLTVISAYLHSGQLGTEKMDQKYAHLELVDARMAELLAAARDGGSQVVMAGDLNVVRSERDIKNWKPNHNKIAGVMDEEIAHLEGWFASGWVDASRHLVGDEEQGPYTWWSQRGKAFDNNTGWRIDYQVLTPALAERAHSVTVDRAPDYASRWSDHAPLVVEYR$","Exodeoxyribonuclease III","Cytoplasm, Extracellular","possible exodeoxyribonuclease","putative exodeoxyribonuclease ","exodeoxyribonuclease III Xth","","Dlaki M. Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases. Trends Biochem. Sci. 2000. 25(6):272-273. PMID: 10838565","","","

InterPro
IPR004808
Family

Exodeoxyribonuclease III xth
PTHR22748	$\"[66-293]T$	AP ENDONUCLEASE
TIGR00633	$\"[17-293]T$	xth: exodeoxyribonuclease III (xth)

InterPro
IPR005135
Domain

Endonuclease/exonuclease/phosphatase
PF03372	$\"[17-292]T$	Exo_endo_phos

noIPR
unintegrated

unintegrated
G3DSA:3.60.10.10	$\"[17-292]T$	no description

","BeTs to 17 clades of COG0708COG name: Exonuclease IIIFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0708 is a-mp--y--drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB000097 (AP endonuclease, family 1) with a combined E-value of 9.2e-42. IPB000097A 17-29 IPB000097B 44-53 IPB000097D 174-208 IPB000097E 236-283","Residues 17-292 are 57% similar to a (EXODEOXYRIBONUCLEASE III HYDROLASE EXONUCLEASE ENDONUCLEASE I DNA DEOXYRIBONUCLEASE DNASE LYASE) protein domain (PD002469) which is seen in Q6AGQ6_BBBBB.Residues 19-181 are 48% similar to a (EXODEOXYRIBONUCLEASE POSSIBLE) protein domain (PD808542) which is seen in Q8G4J1_BIFLO.Residues 238-292 are 69% similar to a (EXODEOXYRIBONUCLEASE EXONUCLEASE HYDROLASE III) protein domain (PD875259) which is seen in Q6NIY3_CORDI.","","-51% similar to PDB:2JC5 APURINIC APYRIMIDINIC (AP) ENDONUCLEASE (NAPE) FROM NEISSERIA MENINGITIDIS (E_value = 3.2E_34);-42% similar to PDB:1BIX THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES (E_value = 3.7E_14);-42% similar to PDB:1E9N A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIMIDINIC ENDONUCLEASE, APE1, AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM (E_value = 3.7E_14);-42% similar to PDB:1HD7 A SECOND DIVALENT METAL ION IN THE ACTIVE SITE OF A NEW CRYSTAL FORM OF HUMAN APURINIC/APYRIDINIMIC ENDONUCLEASE, APE1, AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM (E_value = 3.7E_14);-42% similar to PDB:2ISI Crystal structure of Ape1 from Homo sapiens in a new crystal form complexed with a ligand (E_value = 3.7E_14);","Residues 17 to 292 (E_value = 8.2e-35) place ANA_0199 in the Exo_endo_phos family which is described as Endonuclease/Exonuclease/phosphatase family.","","exodeoxyribonuclease (exoA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0200","211898","210504","1395","5.73","-4.12","47745","ATGAACGGCATTCTCACCGGATTCTTCGGCGCCATCGTCGAGGCCTGGGCCCAGCTGCGCATCGGCAAGCTGAGGGTCCTGCTGTCGCTGGTGGGTGTGGCGGCGGCGGTGGCGGCCATGACCTTCGTCATCGCCCTGGGTCAGGTCTCCGTCGACGCCATCAACAAGGCCAGCGAGAAGTACACCGGCCGCCCGGGCACGGTGACGATCAACGTCAGCCCCACCGGCAAGGGCCTGGACCAGGCCCTCCAGGCCGACGACGCCCCCGAGGCGAGCGCCGGCGGCGACTCAGGTGCCAGCGGCGGCAGCGACGGTGCGGGCGGTACCGGTGGCGCAGGTAGTGCGGGCGGAGACTCCACGACCAGCGCTGCGACCGCGGCGAAGATCTCCACGGCGATGAACAGCTTCGTCGAGCGCTACGAGATCAAGTCCTGGGCAACGACCTACACCTCCAACGTCCGCTTCTCCTTCCCCGACGGCGCTCGGAGCGTGCCCACCCAGACCGTGAGCCTGAGCTACGGGCTCCTGCACCACAAGACCGTCTCCCAGGGGCGCTGGTTCACCGCACAGGACGAGGACGACCTCTCCCCGAGCATGGTCGTCACCCAGGGCTTCCTCGACGCCATGGGGATCCAGCAGCTCACCGAGCCGGTCACCATCACCTCCTTCTCCCCGGTGCAGACCTCCTTCACGATCGTCGGCGTCCTGGAGGCGGAGGACCTCTCCCTCATCGGCTGCAGCGGCGACCCCGAGCGGGACGCGGGCCTGCCGTGCACCCAGCCCGTGACCGCCTTCGCCCTCAACACGCCCTATGAGCACTGGCTGCCCAAGGACGCCGCCCGCCCCGCCCCCACGCTGGAGATCTGGGCCGGTCAGGGCGGCGCGAAGGAGGTCGCCAGCCTGGCCAAGAAGGACCTGGACGCGCGCTTCGGTCAGGGATCGACCCAGGCCGAGGACAACCTCCAGGGCGGCGGCTTCAGCTCCAGCGCGAACACCTTCACCCAGGTGGTCACGGCCGCCGGAGTGTTCGTCATGCTGCTGGGGGCCCTGAGCCTGGTCAACATCTCACTGGTGACCGTGCGCCAACGCATTCACGAGATCGGGGTGCGGCGATCCTTCGGGGCGACGAGCCGACGCATCTTCTTCTCCATCATGCTGGAGTCGGTGGTGGCCACCGTCGTCGCCGGCGTCGTCGGCATCGGGATCGCCATCGTAGGGATGCGCGTCATGCCGCTGAGCGCCTTCCTCGGCATCCCGGTGACCACGACCCCGCCCTTCCCCATGGTGGCGGCTGTCATCGGCCTGGTCGCGGCCACCGCCGTGGGCGCGCTGGCGGGCATCATCCCGGCGATCGTGGCCACCCGCATCCGGCCGATCGACGCGATCCGCTACTGA","MNGILTGFFGAIVEAWAQLRIGKLRVLLSLVGVAAAVAAMTFVIALGQVSVDAINKASEKYTGRPGTVTINVSPTGKGLDQALQADDAPEASAGGDSGASGGSDGAGGTGGAGSAGGDSTTSAATAAKISTAMNSFVERYEIKSWATTYTSNVRFSFPDGARSVPTQTVSLSYGLLHHKTVSQGRWFTAQDEDDLSPSMVVTQGFLDAMGIQQLTEPVTITSFSPVQTSFTIVGVLEAEDLSLIGCSGDPERDAGLPCTQPVTAFALNTPYEHWLPKDAARPAPTLEIWAGQGGAKEVASLAKKDLDARFGQGSTQAEDNLQGGGFSSSANTFTQVVTAAGVFVMLLGALSLVNISLVTVRQRIHEIGVRRSFGATSRRIFFSIMLESVVATVVAGVVGIGIAIVGMRVMPLSAFLGIPVTTTPPFPMVAAVIGLVAATAVGALAGIIPAIVATRIRPIDAIRY$","ABC-type transport protein involved in lipoprotein release, permease component","Membrane, Cytoplasm","probable permease/ATP-binding fusion ABCtransporter, putative","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF214","","Pugh E.L., Wakil S.J. Studies on the mechanism of fatty acid synthesis. XIV. The prosthetic group of acyl carrier protein and the mode of its attachment to the protein. J. Biol. Chem. 1965. 240(12):4727-4733. PMID: 5321311Wong H.C., Liu G., Zhang Y.M., Rock C.O., Zheng J. The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 2002. 277(18):15874-15880. PMID: 11825906","","","

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[283-458]T$	FtsX

InterPro
IPR006162
PTM

Phosphopantetheine attachment site
PS00012	$\"[114-129]?$	PHOSPHOPANTETHEINE

noIPR
unintegrated

unintegrated
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[26-46]?$ $\"[339-359]?$ $\"[380-412]?$ $\"[431-453]?$	transmembrane_regions

","BeTs to 13 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 283 to 458 (E_value = 5.3e-27) place ANA_0200 in the FtsX family which is described as Predicted permease.","","permease-ATP-binding fusion ABC transporter, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0201","212686","211895","792","6.65","-1.38","27977","GTGAGCGGGCTGCTGGAGCTGCGGGAGATCACCCGCACCTTCACCGTTCCCGACTCCGAGCCCCTGCAGATCCTCACGGGAGTCAATCTGAGCGTCTCCCCCGGTGAGCACGTGGCCATCGTGGGACGGTCGGGAACGGGAAAGTCCACCCTGCTCAACATCCTGGGTCTCATCGACAAGCCGACATCGGGCCACTACACGCTCTCGGGCACCGACACCTCCCGGCTCGGGGAGAGCCGCCGCGCCCACCGGCGGGGACAGACCTTCGGCTTCGTCTTCCAGTCCTTCAACCTCATCCCAGGACTGACCACCACCGAGAACGTGGCGGCACCCCTCCTGTACGACACCGGCAGGGCCTTCTGGACCCGCAGCGCACGGGCCGCCGAGCTGCTGGAGGCCGTGGGCCTGGGTGACAAGGTGGGCTCGCCCATCTCGCGCCTGTCGGGAGGCGAGCAGCAGCGGGTGGCCATCGCCAGGGCGCTGTCGCGCCGCCCCAGCGTCATCCTGGCCGACGAGCCCACCGGCGCCCTCGACGTCGATACCGGCAACTCGGTCATGACGCTCCTAGAGCGTCAGTGCGCCGAGAACGGTGCCGCCCTCATCATCATCACGCACGACCTGGCCGTGGCCGGCCGCGCTCACACCCAGTACCGGCTCGATCACGGCACCCTGACCCCGATCTCCGTCATGCGTCGCCAGGTCGGCAGCCTGGAGGAGTTCGGTGAGGTCGTCACCACCCCTCCGACATCCCCCTACCCGTCTGAGCCCACCAGCCACGAAGGAGCCTCATGA","VSGLLELREITRTFTVPDSEPLQILTGVNLSVSPGEHVAIVGRSGTGKSTLLNILGLIDKPTSGHYTLSGTDTSRLGESRRAHRRGQTFGFVFQSFNLIPGLTTTENVAAPLLYDTGRAFWTRSARAAELLEAVGLGDKVGSPISRLSGGEQQRVAIARALSRRPSVILADEPTGALDVDTGNSVMTLLERQCAENGAALIIITHDLAVAGRAHTQYRLDHGTLTPISVMRRQVGSLEEFGEVVTTPPTSPYPSEPTSHEGAS$","ABC-type transport protein involved in lipoprotein release, ATPase component","Membrane, Cytoplasm","macrolide ABC efflux protein","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[146-189]T$	Q92CI5_LISIN_Q92CI5;
PF00005	$\"[35-222]T$	ABC_tran
PS50893	$\"[5-246]T$	ABC_TRANSPORTER_2
PS00211	$\"[147-161]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[34-225]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-225]T$	no description
PTHR19222	$\"[5-225]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32	$\"[5-225]T$	ABC TRANSPORTER

","No hits to the COGs database.","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.2e-35. IPB005074C 24-71 IPB005074D 135-178 IPB005074E 199-219***** IPB005116 (TOBE domain) with a combined E-value of 4.5e-20. IPB005116A 42-58 IPB005116B 87-104 IPB005116C 147-160 IPB005116D 167-186***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 5.3e-20. IPB013563A 24-58 IPB013563C 144-171***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.3e-18. IPB010509B 35-60 IPB010509D 142-186***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.3e-08. IPB010929K 22-66 IPB010929M 144-190","Residues 2-132 are 56% similar to a (LIPOPROTEIN ATP-BINDING RELEASING SYSTEM LOLD) protein domain (PDA0I1Q0) which is seen in Q7UH39_RHOBA.Residues 4-113 are 57% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 4-140 are 49% similar to a (PHNL ATP-BINDING) protein domain (PDA1B9K8) which is seen in Q6RCD1_PSEST.Residues 13-226 are 39% similar to a (ATP-BINDING) protein domain (PD727310) which is seen in Q8FQ82_COREF.Residues 17-225 are 44% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 24-217 are 42% similar to a (ATP-BINDING ABC PROTEIN TRANSPORTER) protein domain (PD995669) which is seen in Q73R06_TREDE.Residues 24-202 are 51% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 25-206 are 48% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 25-76 are 80% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8RAL4_THETN.Residues 25-210 are 47% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 25-178 are 45% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 29-205 are 50% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 30-207 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 38-213 are 44% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 93-207 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 122-210 are 56% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA184H5) which is seen in Q6W139_RHISN.Residues 123-210 are 53% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 123-206 are 58% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 125-226 are 59% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 126-205 are 55% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 126-207 are 59% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 127-212 are 60% similar to a (BLR8070 ATP-BINDING) protein domain (PD727315) which is seen in Q89BS8_BRAJA.Residues 131-189 are 69% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD436020) which is seen in Q9A7G4_CAUCR.Residues 132-219 are 55% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 139-205 are 59% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 146-189 are 86% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q92CI5_LISIN.Residues 149-226 are 64% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.","","-64% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 2.7E_42);-64% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 6.1E_42);-55% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 1.0E_25);-52% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 3.5E_21);-52% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 5.0E_20);","Residues 35 to 222 (E_value = 9.5e-51) place ANA_0201 in the ABC_tran family which is described as ABC transporter.","","ABC efflux protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0202","213750","212683","1068","4.96","-9.67","36526","ATGGAGGACGCCGTGAAGCGCTTCGTCTGGCCCGCCCTCAAGACCCTCATCGCGGTGGTCGTCGCTGTCGCCCTGGTGAAGATCGCCTTCTTCCCCTCGCAGAACGACGGCACCACCGCTGACATCTCCCCCGGTTACGCCGCCGACGTCAAGACCGTCCCCGTGACCAAAGGCAGCATCTCGAACACGGTCTCGGTCAAGGGTCACATCGTTCAGGACGCCACGGTCGAGGTCCAGGCCGACCTGGCCGGCGTGGTGGACTCGGTCGCCGTGGAGAAGGACACCCAGGTCAGTGCCGGTGACCCGCTGCTCTACATCAAGCACTCCGAGTCCCAGCCCCCGGTGACCAAGACCGATGAGAGCGGCAACGTCACCCAGACCCCGACCGAGGACAAGGTCACCTGGTCCACGATCTACGCCCCCGTCAGCGGCACCGTGACCCCCAAGGTCCTCAAGCAGCAGGAGACCGGCGTCGGCGTCGTCGTGGCCACCATCACCCCCGCGACCTACTCGGCCACCGGCACCGTCAGCGCCGCGCAGCAGTACCGGCTCACCAACGCGCCCACTGCCGCGACCCTGACCCTGGAAGGGGGCCCGGCGCCCTTCCAGTGCAACAACCTCAAGGTCGGTACCAAGGCCTCCACCTCCACGACCACCGGCGGGGACGGCTCGACGACGACCACCTCCGGTGACGGCACCAGCGTGGAGATGCGCTGCGCGGTTCCCGGCGACCAGAAGGTCTTCGCCGGTATGCCGGTGACCATCAGCGTTGACGCCGGCAGCGCCTCAGAGGCCCTGATGGTTCCGGTCACCGCCGTGGAGGGCAAGGTCGGCTCGGGCTTCGTGTGGCTGGTGCCCGAGTCCGGGGACGCCTCCAAGGCGGTCAAGACCGCTGTGAAGCTGGGGATCACGGACGGTACGAACATCCAGATCACGGCCGGTCTCAAGGCCGACCAGCAGGTCCTGCAGTTCGTCCCCAACAAGGACACGCGCCGCACCGGGACGCCGGACACCTGCGAGCCGGACAACTCCGCCTGCTACGACTCCGAAGGCAAGGAGATCCTGTGA","MEDAVKRFVWPALKTLIAVVVAVALVKIAFFPSQNDGTTADISPGYAADVKTVPVTKGSISNTVSVKGHIVQDATVEVQADLAGVVDSVAVEKDTQVSAGDPLLYIKHSESQPPVTKTDESGNVTQTPTEDKVTWSTIYAPVSGTVTPKVLKQQETGVGVVVATITPATYSATGTVSAAQQYRLTNAPTAATLTLEGGPAPFQCNNLKVGTKASTSTTTGGDGSTTTTSGDGTSVEMRCAVPGDQKVFAGMPVTISVDAGSASEALMVPVTAVEGKVGSGFVWLVPESGDASKAVKTAVKLGITDGTNIQITAGLKADQQVLQFVPNKDTRRTGTPDTCEPDNSACYDSEGKEIL$","Biotin-requiring enzyme","Extracellular, Periplasm, Membrane","efflux transporter, RND family, MFP subunit,putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Shenoy B.C., Xie Y., Park V.L., Kumar G.K., Beegen H., Wood H.G., Samols D. The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis. J. Biol. Chem. 1992. 267(26):18407-18412. PMID: 1526981Russell G.C., Guest J.R. Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim. Biophys. Acta 1991. 1076(2):225-232. PMID: 1825611","","","

InterPro
IPR000089
Domain

Biotin/lipoyl attachment
PF00364	$\"[74-106]T$	Biotin_lipoyl

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[15-33]?$	transmembrane_regions

","BeTs to 10 clades of COG0845COG name: Membrane-fusion proteinFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0845 is -------qvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB006143 (Secretion protein HlyD) with a combined E-value of 4.5e-06. IPB006143A 78-107 IPB006143C 138-154","No significant hits to the ProDom database.","","-47% similar to PDB:2J0F STRUCTURAL BASIS FOR NON-COMPETITIVE PRODUCT INHIBITION IN HUMAN THYMIDINE PHOSPHORYLASE: IMPLICATION FOR DRUG DESIGN (E_value = );-51% similar to PDB:1BF2 STRUCTURE OF PSEUDOMONAS ISOAMYLASE (E_value = );","Residues 74 to 106 (E_value = 2.2e-05) place ANA_0202 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme.","","transporter, RND family, MFP subunit, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0203","215210","213933","1278","4.93","-24.30","44670","ATGACCAACGATGCTCCCGTCTTCGCCCCTGCACTGAGCCCCCAGGAGGGCGCCGAGGCCGCGACCGCCCTGTTCCGCGAGGTCTTCGAGGCCGAGCCCGACGGGGTGTGGTACGCCCCCGGGCGCGTCAACATCATTGGCGAGCACACTGACTACAACGGCGGCCTGGCTCTGCCCATCGCCCTGCCCCACCGGGCGCACCTGGCGCTGCGGCGCCGCGAGGACCGCGTCGTGCGCCTGGTCTCCCCCCAGACCCGGGAGAAGGTCGACGTCATGGACCTCGACACGATCGGTCCGAAGGGAACCCCCGGGGAGGTGGCGCACTGGGCCTCCTACATCGCCGGCGTCGCCTGGTCCCTGGAGCGCGACGGCTTCGAGAACCTGCCCGGCTTCGACGCCGCACTCGTCTCCTGCGTGCCCTTGGGAGGCGGACTGTCCTCCTCAGCGGCCCTGGAGTGCTCGGCGGCCGTCGCCATTGACGAGGTCGCGCACCTGGGCCTGGCCGGGACTGCGCAGGAGCCCGACGACGCCGGGCGCGCCCGCCTGGTGACCAACTGCGTGCGCACGGAGAACGAGATGGCCGGGGCCCCCACCGGCGGCATGGACCAGTCGGCCTCCATGCGCTGCCGCGAGGGTCACGCCCTGGAGCTGGACTGCCGCGACGGCTCGGTGACCCACGTGCCCTTCGACCTGGCCGCCGAGGGCCTGGCCCTCCTGGTCATCGACACCAAGGCCAAGCACTCTCTGGACGATGGCCAGTACGGGGCCAGGCGAGCGGCCTGCGAGCGGGCCGCTGAGATCCTTGGGGTGGAGCTCCTGGCGGACATCGCGATCGAGGACCTGTCCGGCGCCCTGGAGCGCCTCGCGGCCACCGACGGCGACGACGCCGACGAGCTGGTCAAGCGCACCCGCCACGTTGTCACCGAGATCGACCGCACCCGCCGGCTCGTGGCGCTTCTGCAGGACGGGCAGCCCCTGCGCGGGGCGAAGCTCGCCGAGGCGGGCAGGCTCATGGACGCCTCGCACGAGTCACTGCGTGTGGACTACGAGTGCACCTGCCCCGAGCTGGACGTGGCCGTGGAGGCGGCCCGCGCCGCCGGCGCCCACGGGGCGCGCATGACCGGCGGCGGATTCGGCGGCTCGGCGATCGCCCTGGTGGACGCCGACGCCGTCCACGACGTGGCCCGCGCCGTGACCGAGGCCTACCGCCGTGAGGGCTTCAACCCGCCGGCCTTCCTCGACGCGGTTCCCGCCGCCCCGGCCGGCAGGCTCGCCTGA","MTNDAPVFAPALSPQEGAEAATALFREVFEAEPDGVWYAPGRVNIIGEHTDYNGGLALPIALPHRAHLALRRREDRVVRLVSPQTREKVDVMDLDTIGPKGTPGEVAHWASYIAGVAWSLERDGFENLPGFDAALVSCVPLGGGLSSSAALECSAAVAIDEVAHLGLAGTAQEPDDAGRARLVTNCVRTENEMAGAPTGGMDQSASMRCREGHALELDCRDGSVTHVPFDLAAEGLALLVIDTKAKHSLDDGQYGARRAACERAAEILGVELLADIAIEDLSGALERLAATDGDDADELVKRTRHVVTEIDRTRRLVALLQDGQPLRGAKLAEAGRLMDASHESLRVDYECTCPELDVAVEAARAAGAHGARMTGGGFGGSAIALVDADAVHDVARAVTEAYRREGFNPPAFLDAVPAAPAGRLA$","Galactokinase","Cytoplasm","galactokinase","galactokinase ","galactokinase","","Tsay Y.H., Robinson G.W. Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase. Mol. Cell. Biol. 1991. 11(2):620-631. PMID: 1846667Lee M., Leustek T. Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene. Arch. Biochem. Biophys. 1999. 372(1):135-142. PMID: 10562426","","","

InterPro
IPR000705
Family

Galactokinase
PR00473	$\"[41-59]T$ $\"[109-120]T$ $\"[130-148]T$ $\"[301-315]T$	GALCTOKINASE
PIRSF000530	$\"[17-424]T$	Galactokinase
TIGR00131	$\"[18-424]T$	gal_kin: galactokinase
PS00106	$\"[41-52]T$	GALACTOKINASE

InterPro
IPR006203
Domain

GHMP kinase, ATP-binding region
PS00627	$\"[139-150]?$	GHMP_KINASES_ATP

InterPro
IPR006204
Domain

GHMP kinase
PF00288	$\"[132-210]T$	GHMP_kinases_N

InterPro
IPR006206
Family

Mevalonate and galactokinase
PR00959	$\"[39-63]T$ $\"[137-159]T$ $\"[190-209]T$ $\"[370-387]T$	MEVGALKINASE

InterPro
IPR013750
Domain

GHMP kinase, C-terminal
PF08544	$\"[315-404]T$	GHMP_kinases_C

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[16-241]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.890	$\"[302-401]T$	no description
PTHR10457	$\"[107-406]T$	MEVALONATE KINASE/GALACTOKINASE
PTHR10457:SF6	$\"[107-406]T$	GALACTOKINASE 1

","BeTs to 9 clades of COG0153COG name: GalactokinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0153 is ----k-y-v-rlb-e-gh------t-Number of proteins in this genome belonging to this COG is 2","***** IPB000705 (Galactokinase) with a combined E-value of 1.8e-84. IPB000705A 39-62 IPB000705B 104-116 IPB000705C 130-151 IPB000705D 189-222 IPB000705E 254-268 IPB000705F 301-313 IPB000705G 334-361 IPB000705H 370-383***** IPB006203 (GHMP kinase, ATP-binding region) with a combined E-value of 3.5e-20. IPB006203A 39-54 IPB006203B 139-153 IPB006203C 371-380***** IPB013750 (GHMP kinase, C-terminal) with a combined E-value of 3.5e-06. IPB013750A 46-54 IPB013750B 137-150","Residues 112-183 are 68% similar to a (KINASE TRANSFERASE ATP-BINDING BIOSYNTHESIS 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL CMK ISOPRENE 4-CYTIDINE-5_apos;-DIPHOSPHO-2-C-METHYL-D-ERYTHRITOL GALACTOSE HOMOSERINE) protein domain (PD008614) which is seen in Q8G508_BIFLO.Residues 201-321 are 69% similar to a (KINASE GALACTOSE METABOLISM TRANSFERASE ATP-BINDING GALACTOKINASE CARBOHYDRATE MUS MUSCULUS CDNA) protein domain (PD329027) which is seen in GAL1_STRLI.","","-44% similar to PDB:1WUU crystal structure of human galactokinase complexed with MgAMPPNP and galactose (E_value = 2.6E_33);-42% similar to PDB:1PIE Crystal Structure of Lactococcus lactis Galactokinase Complexed with Galactose (E_value = 1.7E_21);-39% similar to PDB:1S4E Pyrococcus furiosus galactokinase in complex with galactose, ADP and magnesium (E_value = 3.3E_12);-36% similar to PDB:2CZ9 Crystal Structure of galactokinase from Pyrococcus horikoshi (E_value = 3.3E_12);-36% similar to PDB:2DEI Crystal Structure of galaktokinase from Pyrococcus horikoshii with AMP-PNP and galactose (E_value = 3.3E_12);","Residues 132 to 210 (E_value = 9.6e-09) place ANA_0203 in the GHMP_kinases_N family which is described as GHMP kinases N terminal domain.Residues 315 to 404 (E_value = 3.4e-14) place ANA_0203 in the GHMP_kinases_C family which is described as GHMP kinases C terminal.","","(galK) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0204","216315","215284","1032","5.84","-5.45","35775","GTGACCCGCACACATTACCGTGTCACCTCCCTGTTATCCCAGCCGGGAGCGCAGCACGAGCGGGATGAGTGTGCCACGACCGACCGAACGGGCGGAACAACGGCACCACCGACGCCTGTGCGACTCTGTGCGGGAACGTGCGAACATGGCGTTTTCGGCGCCGAGGTCTGGCAGACTGGCCCCATGCAACCCGGCCCTTCAGCCTCCACCGTCGGATCGCCCCGCCCGGCCCCAATGCTCGCCCGTCAACGCCAGGAGCACATCCTGGAACGGGTCGCGGCCACTGGCGGCGTCCGGGTGGCCGACGTCGTCGAGGAGCTGGGGATCTCCGAGATGACCGTGCGCCGTGACATCACCGAGCTGGTCACCCAGGGGCTGGTCGAACGCGTCCACGGCGGGGCGGTGGCGGCCGGCCCCACCACCCTCGAGCCGCGATTCACCGCCAAGTCGACCCTCAATCTGGAGGCCAAGCGCCGCATCGGCCAGGCCGCGGCCGCCATGGTCCGCCCCGGGGACTCCCTGGCGCCGTCGGCCGGGACCACCACGCTGGCACTCGCCCAGGCCCTGACTGAGCTGGAGCACTTCCCCACCCTGACCGTCATCACGAACTCGCTGCCCGCCGCTCAGGTGCTCTTTGACGCTGCCGATGCCGCCCGCGCCGAGAACCGCGACGCCCCCACGGTGGTCATCACCGGCGGTGAGCGCACGCCGTCGAACGCCCTGGTGGGCCTGGTTGCGGTCGACGCGCTGCGCACGATGCGTGTGGAGTGGGTCTTCCTGGGCGCCCACGGCTTCACTCCTGAGGCCGGGCTCATGACCCCCAACCTGCAGGAGGCCTCCGCCAACCAGGCGCTGGTCGCCGCCGGGCGCACGGTGGTGGCCACGCTGGACTCCTCCAAGTGGGGGGTCCTGGGGCTGCGCTCCTTCTGCGCCACCCGGGACATCGGGGTCCTGGTGACCGAGGCCGAGCCCGACGCCGACGGCGTCGACGCGCTCACGCAGGCCGGTACCCGCCTGACCATCGCCACCTGA","VTRTHYRVTSLLSQPGAQHERDECATTDRTGGTTAPPTPVRLCAGTCEHGVFGAEVWQTGPMQPGPSASTVGSPRPAPMLARQRQEHILERVAATGGVRVADVVEELGISEMTVRRDITELVTQGLVERVHGGAVAAGPTTLEPRFTAKSTLNLEAKRRIGQAAAAMVRPGDSLAPSAGTTTLALAQALTELEHFPTLTVITNSLPAAQVLFDAADAARAENRDAPTVVITGGERTPSNALVGLVAVDALRTMRVEWVFLGAHGFTPEAGLMTPNLQEASANQALVAAGRTVVATLDSSKWGVLGLRSFCATRDIGVLVTEAEPDADGVDALTQAGTRLTIAT$","Transcriptional regulator, DeoR family","Cytoplasm","Transcriptional regulators of sugar metabolism","transcriptional regulator; DeoR family","regulatory protein, DeoR","","Beck von Bodman S., Hayman G.T., Farrand S.K. Opine catabolism and conjugal transfer of the nopaline Ti plasmid pTiC58 are coordinately regulated by a single repressor. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(2):643-647. PMID: 1731335Ray W.K., Larson T.J. Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12. Mol. Microbiol. 2004. 51(3):813-826. PMID: 14731281","","","

InterPro
IPR001034
Domain

Bacterial regulatory protein, DeoR N-terminal
PR00037	$\"[102-116]T$ $\"[116-134]T$	HTHLACR
PF08220	$\"[84-140]T$	HTH_DeoR
SM00420	$\"[84-136]T$	HTH_DEOR
PS51000	$\"[81-136]T$	HTH_DEOR_2
PS00894	$\"[84-118]T$	HTH_DEOR_1

InterPro
IPR014036
Domain

Bacterial regulatory protein, DeoR
PF00455	$\"[154-321]T$	DeoR

","BeTs to 9 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K [Information storage and processing--Transcription] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is 4","***** IPB001034 (Bacterial regulatory protein, DeoR family) with a combined E-value of 3e-43. IPB001034A 96-134 IPB001034B 156-189 IPB001034C 197-205 IPB001034E 281-321***** IPB000524 (Bacterial regulatory protein, GntR family) with a combined E-value of 2.9e-06. IPB000524 97-137","Residues 79-135 are 66% similar to a (TRANSCRIPTIONAL DNA-BINDING TRANSCRIPTION REGULATOR REGULATION DEOR-FAMILY) protein domain (PD978395) which is seen in Q82MA5_STRAW.Residues 79-164 are 53% similar to a (DNA-BINDING RIORF65 TRANSCRIPTION REGULATION PLASMID) protein domain (PD978397) which is seen in Q9KWB9_AGRRH.Residues 80-174 are 56% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR DEOR FAMILY REGULATOR OPERON) protein domain (PD469489) which is seen in Q986T2_RHILO.Residues 163-276 are 64% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR DEOR FAMILY OPERON REGULATOR) protein domain (PD002430) which is seen in Q9K3N4_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 76 to 137 (E_value = 0.0031) place ANA_0204 in the GntR family which is described as Bacterial regulatory proteins, gntR family.Residues 84 to 135 (E_value = 0.0031) place ANA_0204 in the HTH_11 family which is described as HTH domain.Residues 84 to 140 (E_value = 6.4e-22) place ANA_0204 in the HTH_DeoR family which is described as DeoR-like helix-turn-helix domain.Residues 154 to 321 (E_value = 2e-22) place ANA_0204 in the DeoR family which is described as Bacterial regulatory proteins, deoR family.","","regulators of sugar metabolism","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0205","216394","217056","663","6.20","-4.72","23367","ATGCAGATCCCCGCACCAGACGCGCACCAGTGCGTCATCGGTGTGGCCATCGCCCTGCCCTCCCACTATGCCGCCCAGGTGCGAGCGGTGCGGGAGGCCGCGGGGGATCCTCTGGCCGAAGTCGTGCCGCCCCACATCACGCTGCTGCCGCCCACGGCCGTCGACGTCGACGCCCTCGATGAGATCATGCAGCACCTGCGCGATGTGGCCGCCGGGACGACCCCCTTCAAGGTGCGGCTGGACGAGGTCGGCACCTTCCGGCCCGTCAGCCCCGTGGTCTACCTCGGTCTGCGCAGCGGCGCAGAGGAGTGCAACCTCCTTCAGATGCGGGTCCGCGACCGCTGGGGACCCCTGGCCCGTTCGCTCAGCTTCCCCTTCCACCCGCACGTGACCCTGGCCCACGAGATCGCCGAGGACGGCCTCGACACCGCAGCCAGAAAGGGAGCTGACCTCACCATGGACTTCACTGTCACCAAGCTTCATCTCTACCGCCACCGCAGCCGGCCCGCCGGCCACGGCGATAGCCAGTGCCCGGCTTCGGAAGGGGGCTGGGACGTCGTGTCCGCCTTCGCCTTCGGGGGCTCCCTGGCCCCTGACGCCTCCGCTGACCCTACGGCGAGAGCAGTACCGGTGCTTCCGACGACTCCGGCGGTGTCGGCATGA","MQIPAPDAHQCVIGVAIALPSHYAAQVRAVREAAGDPLAEVVPPHITLLPPTAVDVDALDEIMQHLRDVAAGTTPFKVRLDEVGTFRPVSPVVYLGLRSGAEECNLLQMRVRDRWGPLARSLSFPFHPHVTLAHEIAEDGLDTAARKGADLTMDFTVTKLHLYRHRSRPAGHGDSQCPASEGGWDVVSAFAFGGSLAPDASADPTARAVPVLPTTPAVSA$","2'-5' RNA ligase","Cytoplasm","putative secreted protein","2';5' RNA ligase","2',5' RNA ligase","","Arn E.A., Abelson J.N. The 2'-5' RNA ligase of Escherichia coli. Purification, cloning, and genomic disruption. J. Biol. Chem. 1996. 271(49):31145-31153. PMID: 8940112Mazumder R., Iyer L.M., Vasudevan S., Aravind L. Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily. Nucleic Acids Res 2002. 30(23):5229-5243. PMID: 12466548","","","

InterPro
IPR014051
Domain

Phosphoesterase, HXTX
PF02834	$\"[17-93]T$	2_5_RNA_ligase

noIPR
unintegrated

unintegrated
G3DSA:3.90.1140.10	$\"[15-172]T$	no description

","BeTs to 5 clades of COG1514COG name: 2'-5' RNA ligaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1514 is a-mpkz-qvd--b-ef-----j----Number of proteins in this genome belonging to this COG is 1","***** IPB014051 (Phosphoesterase, HXTX) with a combined E-value of 8e-08. IPB014051A 42-55 IPB014051B 122-134","Residues 13-207 are 55% similar to a (SECRETED) protein domain (PD308889) which is seen in Q82HU2_STRAW.Residues 41-132 are 51% similar to a (LIGASE RNA 2_apos;-5_apos; 6.5.1.- UPF0097 ABC PERMEASE TRANSPORTER LIGASE PROTEIN) protein domain (PD007497) which is seen in Q6HLV6_BACHK.","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 93 (E_value = 3.1e-11) place ANA_0205 in the 2_5_RNA_ligase family which is described as 2',5' RNA ligase family.","","secreted protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0206","217053","218075","1023","10.06","9.08","35614","ATGATCGAGCGCGTCAAGGAGCTGCTGGAGGCCGGGCGGCGCACGCGGATCGGCCGGGCCCTGATCCGCTACGGAACGGCGCGCGGCGCGCTCATGGCCGGAGGAATCGCCTACACGGGCATGTTCTCCGTCTTCGCCGTCCTCGTCATCGGTGTGAGCATACTCATGGCGATGCTCGGTCGGTACCCCAGCATCCGGGCGGCCGTCGTGGACTCCATCAACTCCCTGCTGCCCGGTGTCATCGACACCGGCAACGGGAAGGGGTTGGTCTCGGTCGAGCAGCTGACGCTCTCCTCGGCGCTCAACCTGGGATCGGTGCTGGCGGCCGGGGCCTTCATCTACTCGGTCATCAGCCTTATGGGCACCCTCAAGATCGCCTTGCGAGCCATGTTCGGACTGGTCAATCCCGTCATGAGACCGGTGGTCGGGCAGCTGGCGAATCTCGCGGGCTTCCTCATCATCGTGGCCGGAGTACTGGTGACCGCCGTCGCCTCGGTGGTGACGACGACGCTGTCGGGCAGTGTCGGTCGCTCCCTGGGCCTGCCGCAGTCGCTGACCGGAACCGGGGCGTGGGTGATGACGCTCCTGCTGTCCTTCCTCATCGACACCGGTGTCCTGGCATTCCTCATCACCATGTGCGGGATCCGCCCTCCCCGGCGCGACCTGCTGCAGGGCTGCATGCTGGGCGCCTTCGCGCTGGGTGTGCTGCGCCAGGTGGGAACCGGGGCGGTCGGCTCGGTGACGCGCAACCCGCTGCTGGCCTCCTTCGCCGCCATCGCCGTCCTCATCCTGTGGCTGCACCTGACCAGCCGCGTCGTGCTGCTCGTGGCGGCCTGGATGGCCAACCCGCCGCTGCCCCGCGACGTCGGCCACCCCGACGAAGTCCACGCCCACGAGCGCCCCAACTACGTGACGCTCTCCGTGCCCGAGACCCTGGCCTGGCCCCGCCAGTCCATCACCGGCAGCCTCGAGGCGGACCCGACGGCGCACCCCGACTACGTCCCCCCGGTGCCGATCCCGTGA","MIERVKELLEAGRRTRIGRALIRYGTARGALMAGGIAYTGMFSVFAVLVIGVSILMAMLGRYPSIRAAVVDSINSLLPGVIDTGNGKGLVSVEQLTLSSALNLGSVLAAGAFIYSVISLMGTLKIALRAMFGLVNPVMRPVVGQLANLAGFLIIVAGVLVTAVASVVTTTLSGSVGRSLGLPQSLTGTGAWVMTLLLSFLIDTGVLAFLITMCGIRPPRRDLLQGCMLGAFALGVLRQVGTGAVGSVTRNPLLASFAAIAVLILWLHLTSRVVLLVAAWMANPPLPRDVGHPDEVHAHERPNYVTLSVPETLAWPRQSITGSLEADPTAHPDYVPPVPIP$","Ribonuclease BN","Membrane, Cytoplasm","narrowly conserved hypothetical membraneprotein, putative","hypothetical protein","ribonuclease BN","","","","","

InterPro
IPR004664
Domain

Ribonuclease BN
PF03631	$\"[25-287]T$	Ribonuclease_BN

noIPR
unintegrated

unintegrated
tmhmm	$\"[21-55]?$ $\"[105-127]?$ $\"[148-168]?$ $\"[187-209]?$ $\"[229-249]?$ $\"[255-275]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB004664 (Ribonuclease BN) with a combined E-value of 6.8e-11. IPB004664A 23-46 IPB004664C 255-279","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 25 to 287 (E_value = 4.7e-06) place ANA_0206 in the Ribonuclease_BN family which is described as Ribonuclease BN-like family.","","conserved hypothetical membrane protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0207","218720","219937","1218","5.00","-17.57","41519","GTGACTGATATTTCTGGCAACCCTGGCAAGTCCGATCGCGCCGTACAGCCCGACAGCTCGGCGCCGGCCATTCACGCCATCATTCCCGCAGGCGGTGCGGGCACCCGGCTGTGGCCGCTCAGCCGACGCCACCGCCCCAAGTTCCTCCTCGACCTCACCGGGGCCGGCCGCAGCCTCCTGCAGGACACCGTTGAGCGCCTGGCCCCACTGACCGCCACCATGACGGTCGTCACCGGCGTCGCCCACATCGCCGCCGTGGCCGACCAGCTCCCGAGCATCCCGCTCGACAACCTCCTGGCCGAGCCCTCCCCGCGCGACTCCATGGCGGCCATCGGCCTGGCCGCCGCCGTCATCGCCCACCGCCACGGGCGAGACGCCGTCGTCGGCTCCTTCGCCGCCGACCACACCGTGGCCGACCGGGTCGCCTTCGCCGACGCCGTGCGCCAGGCCGCCCGCCTGGCCGAGCAGGGCTGGGTGGTCACCATCGGGATCGAGGCCACCGGCCCCTCGACCGCCTTCGGCTACATCCACGCCGGCGACCCCACCGACGTGCCCGGGGCCCCCGACGGACGCCGGGTCCTGGGCTTCACCGAGAAGCCCGACGCCGACACCGCCGCCGCCTACCTGGCCACCGGCGACTACCGCTGGAACGCCGGCATGTTCGTGGTCCGCGCCGGCGTCCTCCTCGACCACCTCGCCGAGCTCAGGCCCCAGCTGGCCCAGGGCATCGAGGCCATCGCCGCCGTCTGGGACGCCCCCGAGCGCGAGGAGGTCCTGGCCGAGCGCTGGCCCGCCCTGGAGAAGATCGCCATCGACCACGCCATCGCCGAGCCGGTGGCCGCCGCCGGGGGAGTGGCCACCGTGCCGGTCTCCATGGGCTGGAACGACGTCGGCGGCTTCGACGCCCTGACCGACCTCGTCCCGCCGCGCACCCAGGGCCCGGCCACCGGTGCCGGAGTGCTCGACGATGTCGACGGGTCTACTGGCGCCGCCGGCGACGCCGCCCCCGCGACCCTCCGTGCAGAGATCCGGGCCCTTGACTCCGACGGCGCCCTCATCGCCTCCACCTCCGGACGCACAGTGGTGCTCCTGGGAGTGCCGGGCACCGTCGTCGTCGATACTCCCGACGCCCTCCTGGTCACCACCCCCGAACACGCCCAGGACGTCAAGGGCGTCGTTGACGCCCTCAAGGCGGCCGGCCGAGAGGACCTGCTCTAG","VTDISGNPGKSDRAVQPDSSAPAIHAIIPAGGAGTRLWPLSRRHRPKFLLDLTGAGRSLLQDTVERLAPLTATMTVVTGVAHIAAVADQLPSIPLDNLLAEPSPRDSMAAIGLAAAVIAHRHGRDAVVGSFAADHTVADRVAFADAVRQAARLAEQGWVVTIGIEATGPSTAFGYIHAGDPTDVPGAPDGRRVLGFTEKPDADTAAAYLATGDYRWNAGMFVVRAGVLLDHLAELRPQLAQGIEAIAAVWDAPEREEVLAERWPALEKIAIDHAIAEPVAAAGGVATVPVSMGWNDVGGFDALTDLVPPRTQGPATGAGVLDDVDGSTGAAGDAAPATLRAEIRALDSDGALIASTSGRTVVLLGVPGTVVVDTPDALLVTTPEHAQDVKGVVDALKAAGREDLL$","Mannose-1-phosphate guanylyltransferase (GDP)","Cytoplasm","mannose-1-phosphate guanylyltransferase","mannose-1-phosphate guanylyltransferase (GDP) ","Mannose-1-phosphate guanylyltransferase (GDP)","","Jensen S.O., Reeves P.R. Domain organisation in phosphomannose isomerases (types I and II). Biochim. Biophys. Acta 1998. 1382(1):5-7. PMID: 9507048","","","

InterPro
IPR001538
Domain

Mannose-6-phosphate isomerase, type II, C-terminal
PF01050	$\"[347-402]T$	MannoseP_isomer

InterPro
IPR005835
Domain

Nucleotidyl transferase
PF00483	$\"[25-313]T$	NTP_transferase

InterPro
IPR013794
Domain

Mannose-6-phosphate isomerase, type II
PD002664	$\"[132-239]T$	Q88M00_PSEPK_Q88M00;

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[24-263]T$	no description
PTHR12526	$\"[24-315]T$ $\"[338-402]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF1	$\"[24-315]T$ $\"[338-402]T$	MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE

","BeTs to 12 clades of COG0836COG name: Mannose-1-phosphate guanylyltransferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0836 is ao--k--qvd---cefg-s-uj----Number of proteins in this genome belonging to this COG is 1","***** IPB001538 (Mannose-6-phosphate isomerase, type II) with a combined E-value of 5.9e-56. IPB001538A 26-50 IPB001538C 143-177 IPB001538D 196-238 IPB001538E 280-317***** IPB005835 (Nucleotidyl transferase) with a combined E-value of 2.9e-10. IPB005835A 27-41 IPB005835B 188-200","Residues 132-239 are 61% similar to a (TRANSFERASE MANNOSE-1-PHOSPHATE NUCLEOTIDYLTRANSFERASE ISOMERASE PYROPHOSPHORYLASE GUANYLYLTRANSFERASE GDP-MANNOSE MANNOSE-6-PHOSPHATE GDP PHOSPHOMANNOSE) protein domain (PD002664) which is seen in Q88M00_PSEPK.Residues 228-303 are 66% similar to a (TRANSFERASE MANNOSE-1-PHOSPHATE ISOMERASE NUCLEOTIDYLTRANSFERASE PYROPHOSPHORYLASE GUANYLYLTRANSFERASE GDP-MANNOSE GDP MANNOSE-6-PHOSPHATE PHOSPHOMANNOSE) protein domain (PD959980) which is seen in Q6AGP8_BBBBB.","","-39% similar to PDB:2CU2 Crystal structure of mannose-1-phosphate guanyltransferase from Thermus thermophilus HB8 (E_value = 6.0E_16);-55% similar to PDB:2H08 crystal structure of human phosphoribosyl pyrophosphate synthetase 1 mutant Y146M (E_value = 6.0E_16);","Residues 25 to 313 (E_value = 1.6e-34) place ANA_0207 in the NTP_transferase family which is described as Nucleotidyl transferase.Residues 347 to 402 (E_value = 1.2e-08) place ANA_0207 in the MannoseP_isomer family which is described as Mannose-6-phosphate isomerase.","","guanylyltransferase (GDP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0208","220729","221829","1101","5.43","-4.67","37914","ATGAAGAAGGCCTGCTCCGCGATGACGCTCGGCGCGGCTGTGGCCCTGGTCCTGGCCGCCTGCGGGACGCCACCGGCCCAGCGGCCCGCCCGCAACCTCGAGGGCGCCAAGAACTTCACCGCCTGCATGCTCTCCGACGAGGGCGGATTCGACGACCACTCCTTCAACGAGTCCGGCAAGAAGGGCCTGGACCGGGCCGGCAAGGAGCTGGGAGTCAAGACCATTGCCGTGCAGTCGGAGAACTCGGCCGACTACGCCACCAACATTTACGCGCTCATTCAGCAGAACTGCAAGCTCGTCATCGGCGTCGGCTTCAACATCGCCGCCGACCTGACCGAGTCGGCCAAGGCCAACCCCGACATCCAGTTCGCCCTCATCGACGCCTCCTTCATCGGCGCCGACGGCAAGCCCGCCACCCTGCCCAATACCAAGCCGCTGCTGTTCAAGACGGCCGAGGCCGCCTACCTGGCCGGATACGCCGCCGCCGGTACCTCCCGCACCGGGGTCGTGGGCACCTACGGCGGCAAGCCCCTGCCCACCGTCCAGATCTTCATGGACGGCTTCGCCAAGGGCGTGGCCCGCTACAACCAGGACACCGGCGCCCAGGTCCAGGTCAAGGGCTGGGACACCACCACCGGCAAGGGCGGATCCTTCGTCGGCAACTTCACCGACGCCGCCAAGGGCCAGGCCATCACCGAGCAGTTCATTTCCCAGGGCGCGGACATCATCATGCCGGTGGCCGGCCCCGTCGGCCAGGGCACGCTGTCCTCCGTGCGCCAGAAGAACGACGCCGGGGGCACCAACGCCGTCATCTGGGTCGACTCCGACGGCTACACCTCCTCCGGTGACGGCAGCATCATCATGACCTCCGTGGTCAAGGAGATCGGCAACTCGGTCTTCGACACCGTCAAGAACGCCTCCGAGGGGAGATTCTCCTCCGAGCCCTACATCGGAACCCTCAAGAACAACGGGGTGGCCGCCGCACCCTTCCACGACTTCGACTCTCGGGTGCCGGCGCCGGTCAAGGCCAGGCTCGAGGAGCTGCGAGGCCAGATCATCGACGGGTCCCTCGACGTCTCCACCCCCTACGACCCCTCCTGA","MKKACSAMTLGAAVALVLAACGTPPAQRPARNLEGAKNFTACMLSDEGGFDDHSFNESGKKGLDRAGKELGVKTIAVQSENSADYATNIYALIQQNCKLVIGVGFNIAADLTESAKANPDIQFALIDASFIGADGKPATLPNTKPLLFKTAEAAYLAGYAAAGTSRTGVVGTYGGKPLPTVQIFMDGFAKGVARYNQDTGAQVQVKGWDTTTGKGGSFVGNFTDAAKGQAITEQFISQGADIIMPVAGPVGQGTLSSVRQKNDAGGTNAVIWVDSDGYTSSGDGSIIMTSVVKEIGNSVFDTVKNASEGRFSSEPYIGTLKNNGVAAAPFHDFDSRVPAPVKARLEELRGQIIDGSLDVSTPYDPS$","Surface lipoprotein","Extracellular, Periplasm","Surface lipoprotein","K07335 basic membrane protein A and related proteins","basic membrane lipoprotein","","Roessler D., Hauser U., Wilske B. Heterogeneity of BmpA (P39) among European isolates of Borrelia burgdorferi sensu lato and influence of interspecies variability on serodiagnosis. J. Clin. Microbiol. 1997. 35(11):2752-2758. PMID: 9350727Ogura M., Ohshiro Y., Hirao S., Tanaka T. A new Bacillus subtilis gene, med, encodes a positive regulator of comK. J. Bacteriol. 1997. 179(20):6244-6253. PMID: 9335269","","","

InterPro
IPR003760
Family

Basic membrane lipoprotein
PF02608	$\"[10-293]T$	Bmp

noIPR
unintegrated

unintegrated
PS51257	$\"[1-21]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","BeTs to 10 clades of COG1744COG name: Surface lipoproteinFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1744 is ao--kz--vd-lb--f-----j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB003760 (Basic membrane lipoprotein) with a combined E-value of 1.5e-19. IPB003760A 48-63 IPB003760B 142-162 IPB003760C 236-248 IPB003760E 313-326***** IPB008107 (Mycoplasma P48 major surface lipoprotein signature) with a combined E-value of 4.4e-18. IPB008107D 148-164 IPB008107E 167-184 IPB008107F 187-200 IPB008107H 289-305","Residues 49-208 are 66% similar to a (LIPOPROTEIN MEMBRANE PRECURSOR SIGNAL BASIC TRANSPORTER PALMITATE ABC FAMILY ANTIGEN) protein domain (PD022289) which is seen in Q6A701_PROAC.Residues 228-361 are 64% similar to a (LIPOPROTEIN MEMBRANE SIGNAL PRECURSOR BASIC TRANSPORTER PALMITATE ABC FAMILY ANTIGEN) protein domain (PD004667) which is seen in Q6A701_PROAC.","","-39% similar to PDB:2FQW PnrA from Treponema pallidum as purified from E. coli (bound to inosine) (E_value = 2.9E_14);-39% similar to PDB:2FQX PnrA from Treponema pallidum complexed with guanosine (E_value = 2.9E_14);-39% similar to PDB:2FQY PnrA from Treponema pallidum complexed with adenosine. (E_value = 2.9E_14);","Residues 10 to 361 (E_value = 1.3e-32) place ANA_0208 in the Bmp family which is described as Basic membrane protein.","","lipoprotein (lipoprotein)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0209","221887","223416","1530","5.02","-23.80","54259","GTGAAGCTTGAGCTGCGCGGGATCACGAAGGCCTTCGGGCCGCTCGTGGCCAACGACCATATCGACTTAACCGTCGAACCCGGCCAGATCCACGCCCTCCTGGGCGAGAACGGCGCGGGCAAGTCCACGCTCATGAACGTCCTCTACGGCCTCCACCAGCCCGACGCCGGAGAGATCCTCATCGACGACGAGCCCGTCACCTTCTCCGGGCCGGGCGACGCCGTGGCCGCCGGCATCGGCATGGTCCACCAGCACTTCATGCTCGTGCCCGTCTTCACCGTGGCCGAGTCCGTCGCCCTGGGCTACGAGCCGGTCGGGTCGCTGGGGCTCATCAACACCGGCGCCGCCGCCGCCAAGGTCACCGAGATCTCCCGCCGCTTCGGCTTCGACGTCGACCCCCACGCCCTCATCGAGGATCTGCCCGTGGGCGTCCAGCAGCGCGTGGAGATCATCAAGGCCCTGGCCAGAGACGCCAAGGTCCTCATCCTCGACGAGCCCACCGCCGTGCTCACCCCGCAAGAGACCGACGAGCTCATCACCATCATGCGCGAGCTCAAGGCCTCGGGCACCTCCATCGTCTTCATCACCCACAAGCTGCGCGAGATCCGCGAGGTCGCCGACACCATCACCGTCATCCGCCGCGGCCGCGTCGTCGGCACCGCCGAGCCCACCGCCTCGGCCGCCGAGCTCGCCGGCCTCATGGTCGGCCACGACGTCTCCTTGACCGTCGACAAGCCCCCGGCGGCCCCCGGGGATGACGGGCTCACCCTGGAGGGCATCAGCCTCATCGAGGACGGCACCACCCTGCTTGAGGACATCGACCTGCACGTGCGCGCCGGCGAGATCCTCGCCATCGCCGGCGTCCAGGGCAACGGCCAGACCGAGCTGAGCGAGGTTATCCTCGGGCTGCGTCCGCCCACCGCCGGCTCCATCGCCTTCGACGGTCAGGACGTCACCCGCCACACGGTGCGCCGCCGCCTGCGAGCCGGACTGGGCTTCGTGCCCGAGGACCGCACCACCGACGGCATGGTCGCTGAGCTCTCCGTCGCCGAGAACATGGTCCTGGACCGCTACGACGACCCCGCCCTGGGGCGGGGCCCGTCACTGTCCCCGACGCGCGTGCGCCACGCCGCCCACCGGATGCGCGAGGAGTTCGACGTGCGCGTCACCGACGTCGACGACGCCATCTCCACCCTCTCGGGAGGCAACCAGCAGAAGGCCATCCTCGCCCGCGAGCTCTCCCGGCCCCTCAAGGTCCTCGTCGCCTCCCAGCCCACCCGAGGCCTGGACGTGGGCTCCATCGAGTTCGTCCACCAGCGCATCGTCGCCGAGCGGGACACCGGCACCGCCGTCCTCATCATCTCCTCCGAGCTCGACGAGATCTACGCCCTGGCCGACCGCATCGCCGTCATGTACCGCGGACGGATCGTCGGCACCGTCCCGGCTGACACCGCCCGCGACGCCCTGGGCCTCATGATGGCCGGCACCCCCGCCGAGCAGGCCCTCGACCCTCAGGAGCAGACACGATGA","VKLELRGITKAFGPLVANDHIDLTVEPGQIHALLGENGAGKSTLMNVLYGLHQPDAGEILIDDEPVTFSGPGDAVAAGIGMVHQHFMLVPVFTVAESVALGYEPVGSLGLINTGAAAAKVTEISRRFGFDVDPHALIEDLPVGVQQRVEIIKALARDAKVLILDEPTAVLTPQETDELITIMRELKASGTSIVFITHKLREIREVADTITVIRRGRVVGTAEPTASAAELAGLMVGHDVSLTVDKPPAAPGDDGLTLEGISLIEDGTTLLEDIDLHVRAGEILAIAGVQGNGQTELSEVILGLRPPTAGSIAFDGQDVTRHTVRRRLRAGLGFVPEDRTTDGMVAELSVAENMVLDRYDDPALGRGPSLSPTRVRHAAHRMREEFDVRVTDVDDAISTLSGGNQQKAILARELSRPLKVLVASQPTRGLDVGSIEFVHQRIVAERDTGTAVLIISSELDEIYALADRIAVMYRGRIVGTVPADTARDALGLMMAGTPAEQALDPQEQTR$","Sugar ABC transporter ATP-binding component","Cytoplasm, Membrane","ABC-type sugar","sugar ABC transporter ATP-binding protein ","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[139-182]T$ $\"[399-441]T$	Q6A702_PROAC_Q6A702;
PF00005	$\"[28-215]T$ $\"[280-474]T$	ABC_tran
PS50893	$\"[3-239]T$ $\"[255-498]T$	ABC_TRANSPORTER_2
PS00211	$\"[399-413]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[27-216]T$ $\"[279-475]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[3-229]T$ $\"[255-487]T$	no description
PTHR19222	$\"[3-302]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12	$\"[3-302]T$	SUGAR ABC TRANSPORTER

","BeTs to 11 clades of COG3845COG name: ABC-type uncharacterized transport systems, ATPase componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG3845 is ao--kz--vd-lb--f-----j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 4e-26. IPB005074C 17-64 IPB005074D 128-171 IPB005074E 191-211***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 5.3e-24. IPB013563A 17-51 IPB013563C 137-164 IPB013563D 450-502 IPB013563C 396-423***** IPB005116 (TOBE domain) with a combined E-value of 1.2e-12. IPB005116A 35-51 IPB005116B 77-94 IPB005116D 160-179 IPB005116E 193-206***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.5e-09. IPB010929K 15-59 IPB010929M 137-183 IPB010929A 27-46 IPB010929E 452-504 IPB010929K 267-311***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.3e-09. IPB010509B 28-53 IPB010509D 135-179 IPB010509B 280-305 IPB010509D 394-438","Residues 5-101 are 53% similar to a (PM1309 ATP-BINDING) protein domain (PD390268) which is seen in Q9CLC9_PASMU.Residues 15-229 are 43% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 15-221 are 44% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 15-246 are 41% similar to a (GLP_38_64512_71054 ATP-BINDING) protein domain (PDA0H565) which is seen in Q7R1F8_EEEEE.Residues 272-320 are 75% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9HR21_HALN1.Residues 19-229 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 19-217 are 47% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 21-198 are 47% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 254-506 are 42% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 399-487 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 84-162 are 63% similar to a (ATP-BINDING TRANSPORTER SUGAR PROBABLE ABC) protein domain (PDA188W0) which is seen in Q6AQG3_BBBBB.Residues 128-197 are 67% similar to a (ATP-BINDING TRANSPORTER SUGAR ABC PROTEIN RIBOSE) protein domain (PDA18787) which is seen in Q98GG8_RHILO.Residues 130-197 are 60% similar to a (ATP-BINDING TRANSPORTER ABC RIBOSE) protein domain (PDA18784) which is seen in Q987E7_RHILO.Residues 137-347 are 42% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 399-441 are 90% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q97L59_CLOAB.Residues 143-219 are 63% similar to a (SUGAR ABC ATP ATP-BINDING BINDING) protein domain (PDA0I5K8) which is seen in Q982N2_RHILO.Residues 143-316 are 44% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA106Q1) which is seen in Q73R37_TREDE.Residues 145-239 are 60% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD476601) which is seen in Q89GD9_BRAJA.Residues 198-304 are 53% similar to a (ATP-BINDING SYSTEM ABC RIBOSE) protein domain (PD513759) which is seen in Q8ZTS1_PYRAE.Residues 252-311 are 68% similar to a (ATPASE ATP-BINDING) protein domain (PD101630) which is seen in O06761_MYCFE.Residues 253-474 are 40% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 254-506 are 42% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 255-337 are 57% similar to a (ABC ATP TRANSPORTER ATP-BINDING BINDING) protein domain (PDA0J3R3) which is seen in Q97VF4_SULSO.Residues 270-331 are 61% similar to a (ATP-BINDING COMPONENT ABC RIBOSE/GALACTOSE TRANSPORTER) protein domain (PDA0K5J6) which is seen in Q6MUL8_MYCMS.Residues 272-320 are 75% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9HR21_HALN1.Residues 396-500 are 57% similar to a (ATP-BINDING SUGAR ABC TRANSPORTER) protein domain (PDA0I778) which is seen in Q98JJ1_RHILO.Residues 396-493 are 67% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 399-455 are 91% similar to a (ATP-BINDING ABC SUGAR TRANSPORTER TRANSPORTER PLASMID PROBABLE MGLA COMPONENT ATP) protein domain (PD022456) which is seen in Q6A702_PROAC.Residues 399-487 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 399-496 are 54% similar to a (PROBABLE ATP-BINDING ABC TRANSPORTER ATP BINDING) protein domain (PD763654) which is seen in Q8G625_BIFLO.Residues 399-441 are 90% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q97L59_CLOAB.Residues 442-495 are 67% similar to a (ATP-BINDING SYSTEM ABC RIBOSE) protein domain (PDA0I954) which is seen in Q8ZTS1_PYRAE.Residues 457-493 are 83% similar to a (ATP-BINDING ABC SUGAR TRANSPORTER TRANSPORTER RIBOSE COMPONENT SYSTEM PLASMID RBSA) protein domain (PD716721) which is seen in Q6AGP5_BBBBB.","","-55% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.5E_22);-55% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.5E_22);-55% similar to PDB:1OXU Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.5E_22);-55% similar to PDB:1OXV Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.5E_22);-55% similar to PDB:1OXX Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.2E_21);","Residues 28 to 215 (E_value = 6.6e-51) place ANA_0209 in the ABC_tran family which is described as ABC transporter.Residues 280 to 474 (E_value = 8.6e-21) place ANA_0209 in the ABC_tran family which is described as ABC transporter.","","sugar (aldose)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0210","223413","224732","1320","9.36","6.58","45168","ATGAGCACCCCCACCACCGGCTCCAGCACCGAAGCGACCCCGACGCCCCCGCCCGAGGACCACCCCGAGGAGCAGACCAAGCACGGCCCGAGCGGCCAGGGCGCCCTGCTGCGGCAGATCGCCTCCTCACCGGCCATCGTCGGGCTGCTCGCGGTCCTGACCGCCCTGATCCTCAGCTCGATCCTCATCCTCGCGGCCGACTCCGAGGTGCGCTACACCGCCACCTACCTGCTCAACCGCCCCGGCGACTTCCTCCACGCCACCGCCTCCACCCTGAGCGAGGCCTACAGCTCCCTGCTGCGTGGTGCCCTCTTCGACTGGCGCGCCACCACGGGCGTGCGCATGATCCGCCCCATCACCGACACCCTGACCAACGCCACCCCGCTCATCATCGCCGGGCTCGGCATGGCGGTGGCCTTCCGAGCCGGCCTGTTCAACATCGGCGGCCAGGGGCAGATGATCCTCGGGGCGATCACCGCCTGCTACGTGGGCATCGCCTGGAACCTGCCCCCGGTGGCCCACCTGCTCGTGGCCGTCGTCGGGGCGGGTCTGGGAGGGCTGGTGTGGGGCGGCATCGCCGGCGTCCTCAAGGCCCGCACTGGCGCCAACGAGGTGATCGTGACGATCATGCTCAACTCCATTGCCGCCCACCTGCTGTCCCAGGTGCTCAGCCTCAAGGCCTTCAATGGTGAGGGGGAGACCGGCAACCGCAAGTCCCTGACCGTGGCGGATACCGCCCAGTACCCCTGGCTGGCCGGTGACTCCTTCCGCCTCCACGCCGGTTTCCTCCTGGCCCTGCTGGTCGCCGTGGCCGTGTGGTGGCTCATGGAGCGCTCCCGCCTCGGCTTCCAGCTGCGGGCCACCGGCCTCAACGCCGACGCCGCCCGCACCGCCGGCATGAGCGTTCCCTGGGTGACGAGCCTGGTCATGATGATCTCCGGCGCCCTGTGCGGGCTGGCCGCCACCGCGCCGGTCCTGGGTACCCAGAAGAGCATGGACGAGTCCGTCGTGGGCACTATCGGCTTCGACGCCATCACGGTGGCGCTCCTGGGCCGCTCCCGCCCCGTGGGGACCGTGCTGGCCGGCCTGCTTTTCGGGGCGCTGCGCGCCGGTGGGACTGCCATGCAGGCGGCCCCGGGAACCCACATCAAGATCGTCCTGGTCCTGCAGTCCACGATCGTGCTGTTCATCGCCGCGCCGCCCCTGATCCGGGCCATCTTCCGGCTCCCGGAGCGCCGCGACACCCTCGGCGGCACCGCCCCGTCCCCCGCCTCAGTGCCGGCCGCAGCCCCGGCCGCTCCCGCCGCGAAGGAGGCCTGA","MSTPTTGSSTEATPTPPPEDHPEEQTKHGPSGQGALLRQIASSPAIVGLLAVLTALILSSILILAADSEVRYTATYLLNRPGDFLHATASTLSEAYSSLLRGALFDWRATTGVRMIRPITDTLTNATPLIIAGLGMAVAFRAGLFNIGGQGQMILGAITACYVGIAWNLPPVAHLLVAVVGAGLGGLVWGGIAGVLKARTGANEVIVTIMLNSIAAHLLSQVLSLKAFNGEGETGNRKSLTVADTAQYPWLAGDSFRLHAGFLLALLVAVAVWWLMERSRLGFQLRATGLNADAARTAGMSVPWVTSLVMMISGALCGLAATAPVLGTQKSMDESVVGTIGFDAITVALLGRSRPVGTVLAGLLFGALRAGGTAMQAAPGTHIKIVLVLQSTIVLFIAAPPLIRAIFRLPERRDTLGGTAPSPASVPAAAPAAPAAKEA$","Sugar ABC transporter permease component","Membrane, Cytoplasm","permease protein of sugar ABC transporteralr5367","K02057 simple sugar transport system permease protein","inner-membrane translocator","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR001851
Family

Bacterial inner-membrane translocator
PF02653	$\"[118-398]T$	BPD_transp_2

noIPR
unintegrated

unintegrated
tmhmm	$\"[45-65]?$ $\"[84-104]?$ $\"[125-145]?$ $\"[176-196]?$ $\"[205-225]?$ $\"[256-276]?$ $\"[301-323]?$ $\"[385-403]?$	transmembrane_regions

","BeTs to 11 clades of COG1079COG name: Uncharacterized ABC-type transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1079 is ao--kz--vd-lb--f-----j--twNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 95-155 are similar to a (ABC PERMEASE TRANSPORTER TRANSPORTER SUGAR MEMBRANE PLASMID SYSTEM PROBABLE PROTEIN) protein domain (PD257674) which is seen in Q6AGP4_BBBBB.Residues 282-418 are 48% similar to a (APE2587) protein domain (PD281716) which is seen in Q9Y8P6_AERPE.","","-64% similar to PDB:1KOB TWITCHIN KINASE FRAGMENT (APLYSIA), AUTOREGULATED PROTEIN KINASE DOMAIN (E_value = );","Residues 118 to 398 (E_value = 1.9e-55) place ANA_0210 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component.","","protein of sugar ABC transporter alr5367 (rbsC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0211","224736","226028","1293","10.45","11.60","43882","ATGAGCGCATCAACCGCTTCCGCCGACTCTCACGCCGTAACCGCATCGGATGCCTCCGCGCCCGCGACGGCGGCGCCCATGGATCTGAAGATCCCGATCACCGGCGTCGTCGTGCTCCTCCTGCAGGGGCTCATGGCTCTGGGGGCCCGCGGCTCGACGACCTTCGACCTGACCGCCTCCTCCGACCTCTTCCGGCTCGGGGCCCCCGAGCTCAACGCGCGCCTGATCATCCTCACCACCGCCGTGATCGTCGCGGCGGCCACCGCCGTCGCCTTCGACCGCTCCCGGCGCCGCAGCAGGATCCCCACCTGGGCCGCCGTCCTCATCGGCGTCGGATTCGTCCTGGCCTTCCTGGCCTGGGCCGGGGCCGGAAGCCGCGGCGTCATCCCCCTGGTGACCATCCTGTCCTCCGCGCTGGGACTGAGCGTCCCCCTCGTCTACGGCTCACTGGCCGGGATCATCGGGGAGCGCTCGGGCACCATCAACATCGCCATCGAGGGCCAGCTCCTGGGCGGGGCCTTCCTGGGGGCCGTCGTCGCCTCGGCCTGCTCCAACCCCTGGGTGGGAATCCTGGCCGCCCCCGTGGCCGGAGTCCTCGTGGCCCTCCTCCTGGCCCTGTTCGGCCTGCGCTACCGGGTCAACCAGATCGTCGTCGGCGTCGTCCTCAACGTCCTGGTCTCCGGACTCACCGGCTTCCTGTTCTCCACCTTCCTGTCCTCCAGCCCCAGCCTCAACCGGGCCCTGCGCCTGCCCACCCTGGCGGTGCCGCTGCTGTCCCGGATCCCGATCATCGGGCCGGTCCTCTTCCACCAGACGATCCTCGTCTACCTCATGTACGCGGCCGTGGCGGTCCTGTCCGTCATGCTGTTCCGCTCCCGGTGGGGGCTGAGGCTGCGGGCCTGCGGTGAGCATCCCAAGGCCGCCGACACCGTCGGCATCAACGTCATGCGCACCCGCGTGGCCAACCTGGCCCTGGCCGGGGCGCTCGCGGGACTGGGAGGGGCCTTCTTCACCGTCGGCTCGGGCCTGTCCTTCGAGAACGACATGACCGCAGGCAACGGCTACATCGCCCTGGCCGCCATGATCCTGGGCGCCTGGCGGCCCCTGGGATCGTTGGGGGCGGCCCTGCTGTTCGGCTTCGCCACCTCCGTGGCCCAGACCCTGCCGGTCATCGGCAGCTCGGTCTCACCGGACATCATCTCCATGATCCCCTACATCGTCACGATCCTGGCGGTGGCCGGATTCGTGGGCAAGGTGCGTGCGCCGGCCGCCGAGGGGGTGCCCTACCCGTGA","MSASTASADSHAVTASDASAPATAAPMDLKIPITGVVVLLLQGLMALGARGSTTFDLTASSDLFRLGAPELNARLIILTTAVIVAAATAVAFDRSRRRSRIPTWAAVLIGVGFVLAFLAWAGAGSRGVIPLVTILSSALGLSVPLVYGSLAGIIGERSGTINIAIEGQLLGGAFLGAVVASACSNPWVGILAAPVAGVLVALLLALFGLRYRVNQIVVGVVLNVLVSGLTGFLFSTFLSSSPSLNRALRLPTLAVPLLSRIPIIGPVLFHQTILVYLMYAAVAVLSVMLFRSRWGLRLRACGEHPKAADTVGINVMRTRVANLALAGALAGLGGAFFTVGSGLSFENDMTAGNGYIALAAMILGAWRPLGSLGAALLFGFATSVAQTLPVIGSSVSPDIISMIPYIVTILAVAGFVGKVRAPAAEGVPYP$","Sugar ABC transporter permease component","Membrane, Cytoplasm","uncharacterized ABC-type transport system,permease component","K02057 simple sugar transport system permease protein","inner-membrane translocator","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR001851
Family

Bacterial inner-membrane translocator
PF02653	$\"[134-412]T$	BPD_transp_2

noIPR
unintegrated

unintegrated
tmhmm	$\"[33-53]?$ $\"[72-92]?$ $\"[101-121]?$ $\"[127-147]?$ $\"[157-177]?$ $\"[183-205]?$ $\"[215-235]?$ $\"[272-290]?$ $\"[323-345]?$ $\"[351-369]?$ $\"[371-393]?$ $\"[399-417]?$	transmembrane_regions

InterPro
IPR002125
Domain

CMP/dCMP deaminase, zinc-binding
PF00383	$\"[11-116]T$	dCMP_cyt_deam_1
PS00903	$\"[64-104]?$	CYT_DCMP_DEAMINASES

InterPro
IPR006262
Family

Cytidine deaminase, homotetrameric
PIRSF001250	$\"[9-137]T$	Cytidine deaminase

noIPR
unintegrated

unintegrated
G3DSA:3.40.140.10	$\"[4-137]T$	no description
PTHR11644	$\"[20-136]T$	CYTIDINE DEAMINASE

","BeTs to 12 clades of COG0295COG name: Cytidine deaminaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0295 is -o---zy-vdrlb-e-gh---j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB013171 (Cytidine and deoxycytidylate deaminase, zinc-binding region) with a combined E-value of 1.9e-14. IPB013171A 24-36 IPB013171B 37-50 IPB013171D 95-106 IPB013171E 123-136","Residues 9-131 are 53% similar to a (HYDROLASE CYTIDINE DEAMINASE) protein domain (PD532709) which is seen in Q8VMU9_METCH.Residues 29-106 are similar to a (CYTIDINE DEAMINASE HYDROLASE AMINOHYDROLASE CDA ZINC CYTIDINE/DEOXYCYTIDINE CDD 3D-STRUCTURE CEREVISIAE) protein domain (PD021108) which is seen in Q6AGP2_BBBBB.","","-54% similar to PDB:2D30 Crystal Structure of Cytidine Deaminase Cdd-2 (BA4525) from Bacillus Anthracis at 2.40A Resolution (E_value = 3.7E_18);-56% similar to PDB:1ZAB Crystal Structure of Mouse Cytidine Deaminase Complexed with 3-Deazauridine (E_value = 6.3E_18);-56% similar to PDB:2FR5 Crystal Structure of Mouse Cytidine Deaminase Complexed with Tetrahydrouridine (E_value = 6.3E_18);-56% similar to PDB:2FR6 Crystal Structure of Mouse Cytidine Deaminase Complexed with Cytidine (E_value = 6.3E_18);-57% similar to PDB:1UWZ BACILLUS SUBTILIS CYTIDINE DEAMINASE WITH AN ARG56- ALA SUBSTITUTION (E_value = 8.3E_18);","Residues 11 to 116 (E_value = 2.4e-22) place ANA_0213 in the dCMP_cyt_deam_1 family which is described as Cytidine and deoxycytidylate deaminase zinc-binding region.","","deaminase (AJ237978)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0214","226500","227846","1347","4.89","-17.09","45829","GTGACCGTCCCCGCCGCACCGCCGGCCGTCGAGCCCTTCGACGCCGTCGACGTCATCGCCGCCAAGCGCGACGGCGCCGCCCTGACCGACGCCCAGATCGACTGGGTCGTGGAGGCCTACACCCGCGGCGCCGTCGCCGAGGAGCAGATGAGTGCCTTGGCCATGGCAATCTACCTGCGCGGCATGAGCCGGGCCGAGATCGCCCGCTGGACCGAGGCCATGATCGCCTCCGGGGAGCGCATGGACTTCTCCAGCCTGCCCCGCCCCACAGCGGACAAGCACTCCACCGGGGGAGTGGGGGACAAGATCACCCTGCCGCTGGCGCCGCTCGTGGCCGTCTTCGGCGTGAGCGTCCCCCAGCTGTCCGGACGCGGCCTCGGGCACACCGGCGGCACCCTGGACAAGCTGGAGTCCATCCCCGGCTGGCGGGCTGACCTCACGGGCGAGGAGATCGCGACGATGCTCGGCGCCGACGGCCCCGGCGCCGTCATCTGCGCCGCCGGGGCGGGACTGGCCCCCGCCGACAAGCGCCTCTACGCCCTGCGCGACACCACCGCCACCGTCTCCTGCGTCCCTCTCATCGCCTCCTCGATCATGTCCAAGAAGATCGCCGAGGGGACCGGCGCCCTCGTCCTGGATGTCAAGGTCGGCTCGGGCGCCTTCATGAAAGAGATCGGCCAGGCCCGCGAGCTCGCCTCCACCATGGTGGCCCTGGGCACCGACGCCGGCGTGACCACCCGCGCCCTGCTCACCGACATGTCCACCCCGCTCGGGCTCACCGCAGGCAACGCCCTCGAGGTCGCCGAGTCCCTCGAGGTGCTCGCCGGCGGGGGACCGGCCGACGTCGTCGACCTCACCGTGGCCCTGGCCCTGGAGATGTGCGCCGCCGCCGGCAGACCCGTCGAGGAGGACCAGGCCCGAGCCGCCCTGGCCGACGGGCGCGCCATGGACATCTGGCGCGACATGATCTCCCGCCAGGGAGGCGACCCGGACGCGCCCCTGCCCCTCGCCCCGGAGACCGAGACCGTCACCGCCCCGGCCGACGGGGTCCTCACCACCCTGGACGCCCTCGCCGTCGGGGTGGCCGCCTGGCGCCTCGGGGCCGGGCGGGCCCGCAAGGAGGACCCGGTCCAGGCCGTCGCCGGCGTCACCATGCACGCCAAACCGGGCGACGAGGTACGCGCCGGCCAACCGCTGCTCACCCTGCACACCGCCACCCCCGAGCGCTTCACCCGCGCCCGGGAGGCGCTCGCGGGTGGCATCGTCATCTCCGAGGCCGGATCGCCGGAAGCGGCCGACGCCGTGGCCCGCCGGGAGCGCGGCGTCATCCTGGAGCGCATCGGATGA","VTVPAAPPAVEPFDAVDVIAAKRDGAALTDAQIDWVVEAYTRGAVAEEQMSALAMAIYLRGMSRAEIARWTEAMIASGERMDFSSLPRPTADKHSTGGVGDKITLPLAPLVAVFGVSVPQLSGRGLGHTGGTLDKLESIPGWRADLTGEEIATMLGADGPGAVICAAGAGLAPADKRLYALRDTTATVSCVPLIASSIMSKKIAEGTGALVLDVKVGSGAFMKEIGQARELASTMVALGTDAGVTTRALLTDMSTPLGLTAGNALEVAESLEVLAGGGPADVVDLTVALALEMCAAAGRPVEEDQARAALADGRAMDIWRDMISRQGGDPDAPLPLAPETETVTAPADGVLTTLDALAVGVAAWRLGAGRARKEDPVQAVAGVTMHAKPGDEVRAGQPLLTLHTATPERFTRAREALAGGIVISEAGSPEAADAVARRERGVILERIG$","Thymidine phosphorylase","Cytoplasm","thymidine phosphorylase","thymidine phosphorylase ","pyrimidine-nucleoside phosphorylase","","Pugmire M.J., Ealick S.E. The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. Structure 1998. 6(11):1467-1479. PMID: 9817849Walter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W., Krenitsky T.A., Ealick S.E. Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution. J. Biol. Chem. 1990. 265(23):14016-14022. PMID: 2199449","","","

InterPro
IPR000053
Family

Pyrimidine-nucleoside phosphorylase
PIRSF000478	$\"[1-440]T$	Thymidine phosphorylase/pyrimidine-nucleoside phosphorylase
PTHR10515	$\"[5-443]T$	THYMIDINE/PYRIMIDINE-NUCLEOSIDE PHOSPHORYLASE
TIGR02644	$\"[15-424]T$	Y_phosphoryl: pyrimidine-nucleoside phospho
PS00647	$\"[122-137]T$	THYMID_PHOSPHORYLASE

InterPro
IPR000312
Domain

Glycosyl transferase, family 3
PD001864	$\"[89-329]T$	Q82HZ3_STRAW_Q82HZ3;
G3DSA:1.20.970.10	$\"[13-79]T$	no description
G3DSA:3.40.1030.10	$\"[79-356]T$	no description
PF00591	$\"[87-316]T$	Glycos_transf_3
PF02885	$\"[14-79]T$	Glycos_trans_3N

InterPro
IPR013102
Domain

Pyrimidine nucleoside phosphorylase, C-terminal
PF07831	$\"[350-424]T$	PYNP_C

","BeTs to 10 clades of COG0213COG name: Thymidine phosphorylaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0213 is a-m-k---vdrlb-e-g----j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB000053 (Thymidine/pyrimidine-nucleoside phosphorylase) with a combined E-value of 9.6e-79. IPB000053A 18-32 IPB000053B 46-79 IPB000053C 91-102 IPB000053D 109-135 IPB000053E 178-220 IPB000053F 310-328","Residues 22-79 are 82% similar to a (PHOSPHORYLASE TRANSFERASE GLYCOSYLTRANSFERASE THYMIDINE PYRIMIDINE-NUCLEOSIDE ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE TDRPASE TRYPTOPHAN BIOSYNTHESIS) protein domain (PD584685) which is seen in Q9AK36_STRCO.Residues 89-329 are 84% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE TRYPTOPHAN BIOSYNTHESIS PHOSPHORYLASE THYMIDINE PYRIMIDINE-NUCLEOSIDE TDRPASE) protein domain (PD001864) which is seen in Q82HZ3_STRAW.Residues 276-403 are 45% similar to a (TP TDRPASE PHOSPHORYLASE THYMIDINE FACTOR RENEWAL 3D-STRUCTURE STEM-CELL TRANSFERASE SEQUENCING) protein domain (PD891582) which is seen in TYPH_HUMAN.Residues 340-403 are 76% similar to a (PHOSPHORYLASE THYMIDINE TRANSFERASE GLYCOSYLTRANSFERASE TDRPASE DEOA PYRIMIDINE PYRIMIDINE-NUCLEOSIDE THYMIDINE-NUCLEOSIDE PROBABLE) protein domain (PD982606) which is seen in Q73UC9_MYCPA.Residues 345-428 are 77% similar to a (PHOSPHORYLASE TRANSFERASE GLYCOSYLTRANSFERASE THYMIDINE PYRIMIDINE-NUCLEOSIDE PYRIMIDINE NUCLEOSIDE PYNP 3D-STRUCTURE TDRPASE) protein domain (PD385219) which is seen in Q9AK36_STRCO.","","-64% similar to PDB:1BRW THE CRYSTAL STRUCTURE OF PYRIMIDINE NUCLEOSIDE PHOSPHORYLASE IN A CLOSED CONFORMATION (E_value = 1.0E_101);-60% similar to PDB:2DSJ Crystal structure of project ID TT0128 from Thermus thermophilus HB8 (E_value = 2.5E_87);-55% similar to PDB:2J0F STRUCTURAL BASIS FOR NON-COMPETITIVE PRODUCT INHIBITION IN HUMAN THYMIDINE PHOSPHORYLASE: IMPLICATION FOR DRUG DESIGN (E_value = 3.1E_77);-58% similar to PDB:1AZY STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE (E_value = 2.0E_76);-58% similar to PDB:1OTP STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE (E_value = 2.0E_76);","Residues 14 to 79 (E_value = 3.2e-14) place ANA_0214 in the Glycos_trans_3N family which is described as Glycosyl transferase family, helical bundle domain.Residues 87 to 316 (E_value = 3.2e-11) place ANA_0214 in the Glycos_transf_3 family which is described as Glycosyl transferase family, a/b domain.Residues 350 to 424 (E_value = 1.1e-28) place ANA_0214 in the PYNP_C family which is described as Pyrimidine nucleoside phosphorylase C-terminal domain.","","phosphorylase (TDRPASE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0215","227843","228646","804","10.78","10.83","28467","ATGACCACGCCCCGACCGGTGGACCCCGCCATCGTCGCCCGAGCCGTCAACTCCAGGCTGCGAGTGGGCCGCCTCACCCAGGCGGGCCAGGCCATCACCCTGACCCAGACCGACGCCACCACCTGCGGGCCCACCTGCCTCCTGGCAGCCCACCTGCTCCTGGTGCCCGGCGAGCGCGCAGCCGTGACGGACGACCTCGCCCAGGAGATGACCGCCTCGCCACCCGGCCGGGAGGGCAAGCACCTGCTGTCCGTCCTGTCCCGCCAGCAGCTGCGTCTCCAACGAGCCATGAATGTCCGCGGCCTGGGGGTCCTGCCCTGGCCGAAGGCGCTGGGTTCCACGCCCTGGTCCGTGGCCCGGCAGATGACCGGGATCGCGAGCACCTGCACTCCGGGCGGAGGGCGCCGTCGCTACACGGTGAGGTGGGTGAGCGACCGTGGCCCCGCCTGGGGCGGTGAGGTCGCCTCGATCCGAGATGCGCTGGCAAGCGGACTCCCGGTCATCCTGGTCGCCGGCGGCCCGCTCGTCCTCGACGACGTCTCCGAGGGCGAGCCCACGGCGAGGGCGAGGCTGCGCACCTCCCTGGCCCGGACCCCGGCCGTGCCCCGCCACTACGTCCTGGCCCTGCCCTGGCAGACCATCGGGCAGGACGACCCCGGTGAGGGGCGCGCGCACATCTACGAGCCCTCCAGCGGATCCGTGCGAGCTCTCGACCTGACTGCCCCGCGCGATCCACGCCGCCCCGGCCCCCGCGAGCTCGGCAACTGGCCCCGCGTCCTCGCCGTCATCGCGCCCGAGAACTGA","MTTPRPVDPAIVARAVNSRLRVGRLTQAGQAITLTQTDATTCGPTCLLAAHLLLVPGERAAVTDDLAQEMTASPPGREGKHLLSVLSRQQLRLQRAMNVRGLGVLPWPKALGSTPWSVARQMTGIASTCTPGGGRRRYTVRWVSDRGPAWGGEVASIRDALASGLPVILVAGGPLVLDDVSEGEPTARARLRTSLARTPAVPRHYVLALPWQTIGQDDPGEGRAHIYEPSSGSVRALDLTAPRDPRRPGPRELGNWPRVLAVIAPEN$","Hypothetical protein","Periplasm, Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0216","228724","228954","231","9.01","1.40","8200","ATGTCGACTGTCAGCCATGATGAGAGTCTCCGGGATATTCAGCGAGCCCTGGCGATCATGATCTTCACCGTCGGAGTCCTCGGGGCGGTGGCGATCCTGTCGGTTCCCTTCGCCATCGGCCTGTACGGTCTACATGGATTATGGCTCCCGGTGGTTCTCCTCATTCCGCTCGTCCTGCAGGCGTGGGCGCTTCGCGTCCTGCGCCGGGCAGAGTCGACGTTGCCCGGATGA","MSTVSHDESLRDIQRALAIMIFTVGVLGAVAILSVPFAIGLYGLHGLWLPVVLLIPLVLQAWALRVLRRAESTLPG$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-63]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[47-67]?$	transmembrane_regions

InterPro
IPR002915
Family

Deoxyribose-phosphate aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase
PF01791	$\"[6-214]T$	DeoC

InterPro
IPR011343
Family

Deoxyribose-phosphate aldolase
PIRSF001357	$\"[5-215]T$	Deoxyribose-phosphate aldolase
PTHR10889	$\"[4-213]T$	DEOXYRIBOSE-PHOSPHATE ALDOLASE
TIGR00126	$\"[6-213]T$	deoC: deoxyribose-phosphate aldolase

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[6-215]T$	no description

","BeTs to 15 clades of COG0274COG name: Deoxyribose-phosphate aldolaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0274 is -omp-z-qvdrlbce-gh---j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002915 (Deoxyribose-phosphate aldolase) with a combined E-value of 3.9e-46. IPB002915A 12-32 IPB002915B 57-66 IPB002915C 76-91 IPB002915D 122-131 IPB002915E 146-155 IPB002915F 178-188 IPB002915G 202-211","Residues 7-91 are similar to a (ALDOLASE DEOXYRIBOSE-PHOSPHATE LYASE DEOXYRIBOALDOLASE SCHIFF BASE DERA PHOSPHODEOXYRIBOALDOLASE PROBABLE 3D-STRUCTURE) protein domain (PD005801) which is seen in Q6NJX0_CORDI.Residues 98-170 are 82% similar to a (ALDOLASE DEOXYRIBOSE-PHOSPHATE LYASE DEOXYRIBOALDOLASE SCHIFF BASE DERA PHOSPHODEOXYRIBOALDOLASE PROBABLE 3D-STRUCTURE) protein domain (PDA02223) which is seen in Q6NJX0_CORDI.Residues 175-213 are 92% similar to a (ALDOLASE DEOXYRIBOSE-PHOSPHATE LYASE DEOXYRIBOALDOLASE SCHIFF BASE DERA PHOSPHODEOXYRIBOALDOLASE PROBABLE 3D-STRUCTURE) protein domain (PDA172U9) which is seen in Q6NJX0_CORDI.","","-58% similar to PDB:1O0Y Crystal structure of Deoxyribose-phosphate aldolase (TM1559) from Thermotoga maritima at 1.9 A resolution (E_value = 4.1E_35);-55% similar to PDB:1J2W Tetrameric Structure of aldolase from Thermus thermophilus HB8 (E_value = 9.2E_35);-55% similar to PDB:1UB3 Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8 (E_value = 9.2E_35);-53% similar to PDB:1MZH QR15, an Aldolase (E_value = 1.9E_27);-49% similar to PDB:1N7K Unique tetrameric structure of deoxyribose phosphate aldolase from Aeropyrum pernix (E_value = 4.9E_20);","Residues 6 to 214 (E_value = 7.2e-64) place ANA_0217 in the DeoC family which is described as DeoC/LacD family aldolase.","","aldolase (deoC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0218","229664","231004","1341","5.83","-8.47","46675","GTGCGTCGTCGCACGTCACCGCACCTCACGGACGGGCCCGGCATAGCGGCCGGGCCCGTCGTCGTCCCCTTCGGTATGCAGCAGGAAGGATCGCCTCAACTTGCCAAGTTTCGGGTCTCCGAAACTATACTCGGCTCTATGAGAACCATCCCCAGTATGAGTCGCCGCAGCGCCGCGGCGCTTGCCTGCCTCGCCCTGTCCGCTCCCGCCCTGGCTGCCTGTGGTCACAGCTCGACCTCGGCCGACGCCGCGGGAACGGTCAAGGCGGTCGCCTCCACCACGCAGATCTGCGACTACATCACCCAGCTCGCCAGCGGCGACGCCTCCAGTGATCTCTCCTTCGACCGCACCGGCGCGGACGGCAAGACCCAGCACTTCGGAGCCGACGCAGCCAAGGCCAAGTCCCACCTCACGCTCACCTGCCTGCTGGCCCCCAACGCCTCAGCGCATGAGCACGACATGACCACGGCCCAGTCCAAGGCCTTGTCCGAGGCGGATCTCTTCTTCGTCTCCGGCGTCGACCTCGAGCACTTCCTGGACTCCGCCGTCGACTCCTCCGGCTTCAAGGGCACCATGGTGGTGACCTCCGGGGTCGCTGGGGCCGCCGACGTCGATGACCTGGCCGCCCAGAAGAAGAAGGAGGAGGCCAAGCCCTACAAGGTCGACCGGGGCAGCGCCAAGGTCGAGGTCGCCAAGTGGCCCTTCCCGCCGGAGGAGGGCGAGAGCGAGCCCGAGTTCCGCTTCGACCCGCACGTGTGGACCTCACCGAAGAACGCCATCGTCCAGGTCACCAACATCGGCGCCGCCCTGGAGAAGGCCGCCCCCGACCAGGCCGGCGTCTTCCGCAGCCACGTGGACGCCTACGTCGCCAAGCTCAAGAAGCTCGACGAATGGGCCGCAGGCTCCCTCAACTCGGTACCCCAGGACAAGCGGGTCCTGTTCACCAGCCACGACGCCTTCGGCTACTTCAGCAAGGAGTTCGGCGTGAAGTTCGAGGGTGCCGCCCTGTCCGACTTCAACGCCCAGCAGGACGCCACCGCCGACAAGATCCAGCAGACCGCGGACAAGGTCAAGTCCTCCGGGGCCGTGGCCATCTTCGCTGAGAACTCCAACAACCCCAAGTCCATCCAGAAGGTCGCCGAGGTCGCCGGAGTCAAGGCGGTCATCGGTGATGAGGCCCTCTACGGCGACTCCCTGGGGACCCCCGGATCCGACGGCGAGACCTACATCGGCTCCATCCTCCACAACGTCTCCAACCTCACCAAGGCCTGGGGCGGCACGGTCACCGAGATTCCTGCCGACCTCGCCCAGTGGAGCCCCAAGGCCTCCGACGTCAAGTGA","VRRRTSPHLTDGPGIAAGPVVVPFGMQQEGSPQLAKFRVSETILGSMRTIPSMSRRSAAALACLALSAPALAACGHSSTSADAAGTVKAVASTTQICDYITQLASGDASSDLSFDRTGADGKTQHFGADAAKAKSHLTLTCLLAPNASAHEHDMTTAQSKALSEADLFFVSGVDLEHFLDSAVDSSGFKGTMVVTSGVAGAADVDDLAAQKKKEEAKPYKVDRGSAKVEVAKWPFPPEEGESEPEFRFDPHVWTSPKNAIVQVTNIGAALEKAAPDQAGVFRSHVDAYVAKLKKLDEWAAGSLNSVPQDKRVLFTSHDAFGYFSKEFGVKFEGAALSDFNAQQDATADKIQQTADKVKSSGAVAIFAENSNNPKSIQKVAEVAGVKAVIGDEALYGDSLGTPGSDGETYIGSILHNVSNLTKAWGGTVTEIPADLAQWSPKASDVK$","Zinc/manganese transport system substrate-binding protein","Membrane, Periplasm","adhesin, probable nmb0586 , putative","K02077 zinc/manganese transport system substrate-binding protein","periplasmic solute binding protein","","","","","

InterPro
IPR006127
Family

Periplasmic solute binding protein
PF01297	$\"[62-425]T$	SBP_bac_9

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1980	$\"[78-288]T$ $\"[291-426]T$	no description

","BeTs to 15 clades of COG0803COG name: ABC-type Mn/Zn transport system, periplasmic Mn/Zn-binding (lipo)protein (surface adhesin A)Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0803 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 4","***** IPB006129 (Adhesin B signature) with a combined E-value of 7.9e-34. IPB006129A 86-107 IPB006129C 159-178 IPB006129D 248-267 IPB006129E 306-323 IPB006129G 357-374 IPB006129I 403-421***** IPB006127 (Periplasmic solute binding protein) with a combined E-value of 3.5e-31. IPB006127A 142-176 IPB006127B 249-284 IPB006127C 311-328***** IPB006128 (Adhesin family signature) with a combined E-value of 1.4e-21. IPB006128C 159-176 IPB006128D 306-327 IPB006128E 361-379 IPB006128F 390-409","Residues 77-180 are 55% similar to a (LIPOPROTEIN ABC PERIPLASMIC ZINC BINDING PRECURSOR SIGNAL TRANSPORTER TRANSPORTER METAL-BINDING) protein domain (PD002751) which is seen in Q6NJ01_CORDI.Residues 288-400 are 79% similar to a (LIPOPROTEIN ABC PERIPLASMIC ZINC PRECURSOR SIGNAL TRANSPORTER BINDING TRANSPORTER METAL-BINDING) protein domain (PD002761) which is seen in Q6NJ01_CORDI.","","-42% similar to PDB:1TOA PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM (E_value = 6.2E_22);-42% similar to PDB:1K0F Crystal structure of Zn(II)-free T. pallidum TroA (E_value = 8.1E_22);-43% similar to PDB:1PSZ PNEUMOCOCCAL SURFACE ANTIGEN PSAA (E_value = 1.0E_19);-52% similar to PDB:1XVL The three-dimensional structure of MntC from Synechocystis 6803 (E_value = 1.9E_18);-40% similar to PDB:2O1E Crystal Structure of the Metal-dependent Lipoprotein YcdH from Bacillus subtilis, Northeast Structural Genomics Target SR583 (E_value = 7.6E_12);","Residues 62 to 425 (E_value = 3.2e-47) place ANA_0218 in the SBP_bac_9 family which is described as Periplasmic solute binding protein family.","","probable nmb0586 , putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0219","231013","231840","828","8.96","3.39","29069","ATGACAGACCCCCGTGATCGCACTCCCGCGATGACCTCCCCGACCACCCTGACCGCTGCTGCCGAACCAGTCGTCACCCTGGAGGACGCCTCCTTCTCCTACGGCTCCACCACCGTGCTCACCGGTGTCACTGGTCGGGTCCCGGCCGGGCAGGCCCTCGCCCTCGTGGGTCCCAACGGCTCGGGCAAGACGACACTCATGCGGGCACTGCTCGGCATGGTGACCGTCAGCAGGGGCCGGGTGCGTGTCAACGGGGCGGCACCGGGCAGAGCGCCACGGGGGTCCGTCGGATACGTTCCTCAGCTCAGCGACCTCGACCCCACCTTCCCCGTCACCGTGCGGGAGGTGGTCCAGATGGGCATGTACTCCCAGCTCGGCATCCTGCGGCGCCCTGGTGCCGAGGCCCGTCGTCGGGCGCTGGAGGCCCTTGAGAGCGTGGGTCTGGCCGACCGCGCCGACAGGCGCTTCGGCACCCTGTCCGGCGGCCAGCAGCAGCGCGTCCTCGTGGCCCGCTGCGTGGCCGCCCGGCCCCGCCTCATCCTCCTCGATGAGCCCTTCAACGGCCTGGACCAGCCCAACCGGGACGCCCTGCTGTCCATCATCACTGACCTCAAGGACCAGGGCATCTCCCTGGTCATCTCCACCCACGACCTCGTTCTGGCCCAGGAGACCTGCGAGCAGGCGGCCCTCCTGGCCGGACGGCAGATCGCATTCGGCCCGCGCGACGACGTGCTCGTGGCCCGCTACATCGACGAGGCCTACGGCGGCCACGGCACCACCCGGCTGCTGGGACTCCGTTCCGGCGCGGGCACGCAGGAGCCGTCATGA","MTDPRDRTPAMTSPTTLTAAAEPVVTLEDASFSYGSTTVLTGVTGRVPAGQALALVGPNGSGKTTLMRALLGMVTVSRGRVRVNGAAPGRAPRGSVGYVPQLSDLDPTFPVTVREVVQMGMYSQLGILRRPGAEARRRALEALESVGLADRADRRFGTLSGGQQQRVLVARCVAARPRLILLDEPFNGLDQPNRDALLSIITDLKDQGISLVISTHDLVLAQETCEQAALLAGRQIAFGPRDDVLVARYIDEAYGGHGTTRLLGLRSGAGTQEPS$","Zinc/manganese transport system ATP-binding protein","Membrane, Periplasm","Zinc transport system ATP-binding protein troB","K02074 zinc/manganese transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[159-201]T$	Q6NJ00_CORDI_Q6NJ00;
PF00005	$\"[50-234]T$	ABC_tran
PS50893	$\"[25-258]T$	ABC_TRANSPORTER_2
PS00211	$\"[159-173]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[49-251]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[18-261]T$	no description
PTHR19222	$\"[25-245]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 16 clades of COG1121COG name: ABC-type Mn/Zn transport systems, ATPase componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1121 is aom-kz-qvd-lbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 4.1e-30. IPB005074C 39-86 IPB005074D 147-190***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 5.6e-22. IPB013563A 39-73 IPB013563C 156-183***** IPB005116 (TOBE domain) with a combined E-value of 1.5e-19. IPB005116A 57-73 IPB005116C 159-172 IPB005116D 179-198 IPB005116E 212-225***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.2e-19. IPB010509B 50-75 IPB010509D 154-198***** IPB010929 (CDR ABC transporter) with a combined E-value of 5.1e-08. IPB010929K 37-81 IPB010929M 156-202","Residues 2-237 are 42% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 3-197 are 43% similar to a (ATP-BINDING ABC SYSTEM) protein domain (PDA078N5) which is seen in Q6NED2_CORDI.Residues 13-103 are 52% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 19-127 are 46% similar to a (ATP-BINDING ABC PROTEIN CATION TRANSPORTER) protein domain (PD961539) which is seen in Q72FW0_DESVH.Residues 22-85 are 66% similar to a (COBALT ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PDA0I1O9) which is seen in Q7NNW9_GLOVI.Residues 24-125 are 51% similar to a (PM1309 ATP-BINDING) protein domain (PD390268) which is seen in Q9CLC9_PASMU.Residues 25-111 are 52% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3N9) which is seen in Q6A7M6_PROAC.Residues 25-121 are 51% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD735025) which is seen in Q8G5L4_BIFLO.Residues 25-224 are 48% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 25-240 are 48% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 31-216 are 47% similar to a (ATP-BINDING/PERMEASE ABC TOXIN TRANSPORTER ATP-BINDING PLASMID) protein domain (PD416779) which is seen in Q82YJ4_ENTFA.Residues 35-121 are 52% similar to a (LIPOPROTEIN ATP-BINDING RELEASING SYSTEM LOLD) protein domain (PDA0I1Q0) which is seen in Q7UH39_RHOBA.Residues 37-218 are 50% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 38-180 are 51% similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 40-86 are 72% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9YD57_AERPE.Residues 41-231 are 47% similar to a (ATP-BINDING SECRETION PROBABLE ABC TOXIN TRANSPORTER) protein domain (PDA0C7R3) which is seen in Q7UXT8_RHOBA.Residues 45-222 are 43% similar to a (ATP-BINDING NEQ299) protein domain (PDA186D0) which is seen in Q74MU8_NANEQ.Residues 50-218 are 46% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 50-244 are 50% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 91-244 are 52% similar to a (COMPONENT ABC ATPASE ATP-BINDING TRANSPORTER) protein domain (PDA0I0K5) which is seen in Q74HP7_LACJO.Residues 114-216 are 52% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 145-224 are 62% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 145-216 are 66% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.Residues 146-216 are 62% similar to a (ATP-BINDING TRANSPORTER ABC-TYPE ABC) protein domain (PD891090) which is seen in Q73Y59_MYCPA.Residues 146-205 are 68% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8FAX9_ECOL6.Residues 147-253 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 147-241 are 50% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.Residues 153-231 are 56% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA198U3) which is seen in Q72IT9_THET2.Residues 157-228 are 65% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 158-244 are 52% similar to a (APRD ATP-BINDING) protein domain (PDA0I303) which is seen in Q89EV0_BRAJA.Residues 159-245 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 159-201 are 88% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6NJ00_CORDI.","","-51% similar to PDB:2NQ2 An inward-facing conformation of a putative metal-chelate type ABC transporter. (E_value = 8.3E_21);-47% similar to PDB:1JI0 Crystal Structure Analysis of the ABC transporter from Thermotoga maritima (E_value = 1.7E_18);-49% similar to PDB:1L7V Bacterial ABC Transporter Involved in B12 Uptake (E_value = 1.1E_17);-45% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 1.5E_17);-50% similar to PDB:2ONK ABC transporter ModBC in complex with its binding protein ModA (E_value = 1.5E_17);","Residues 50 to 234 (E_value = 1.5e-53) place ANA_0219 in the ABC_tran family which is described as ABC transporter.","","transport system ATP-binding protein troB (troB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0220","231837","232895","1059","9.19","3.64","35883","ATGAGTGAGGCGATGACGCTCTTCAGCCAGGCCCTCGAGCAGCTGCGCCTGGCGGCCCTCAACATCCCCGGGCTCACCGAGCTGGCGACGTACCCCTTCCTCTTCCGCCCCCTGGTGATGGTGGTGCTTCTGGGCGTCGTCGCCGGCGTCATCGGTGTCATCGTCAACCTGCGCAGCGCCGAGTTCAGCGCCGAGGCCATGGTCCACGCCGTCTTCCCCGGGATCGTCGCCGGCGCCGTCTACTGGGGGATCGACGCGATCATCCCGGCGGCCTCCGTTGTCGCCGTCGCCGCGGCCGTGGTGCTGACCATCGTCTCGCACCGTTCGCATCGGGGGGAGGCCTCCGAGGCCGGCACCGCCGTCGTCCTCACCAGCTTCTTCTCCGTCGGGCTCATCCTGTCCCTGGCCAAGGGCGACATGTCCGGCCAGCTCGAGGCCCTCATGTTCGGCCGCCTCCTGGAGGTCACCGATGAGCGCCTCGCCCAGGCGCTCATCGTGTGCGCCGTCGCACTGCTGCTCATTGCGGCGACCTGGAAGGAGCAGGTGGCCTACGCCTTCGACCGCACCGGCGCCCGCGCCTCCGGGCTGAGACTCCTCGCACTGGACCTGGTCCTCAACACCGCCATCGCTGCCGCGGTGGTCTCCGCTTCGACGGCGGTGGGGATCCTCCTGGTCATCGGCTACCTCGTTATCCCCGGTGCGACGGCGCGCGTTCTCGCCTCCCGGGTTCGCACCATGGTCCTGGTCGCCATCGCCGTGGGTGTGGGCGGGGGATACCTGGGCATGCTGCTCATGGCCCTACCCGGGACCTCCGACAAGCCGATCTCACCGCAGGCCACCGTGGCCCTGGTGATGACCAGCATCCTCCTAGTTGCCGTCAGCGTCTCAACCGCGCGCGAAAGGCTGCGCGGGCCGGATCGGCGGGCCGGCTCGGCGCAGTCCGCAACAGCTGGGGCGACCTCGACGACGGTAGGTGCGAAGGCCAGTGCCAATCCCATCGGGGGACCGGAGGGCTCGGCGAGTACCGTGACCCCGGCGACTGAGAGGAGCCGGGTATGA","MSEAMTLFSQALEQLRLAALNIPGLTELATYPFLFRPLVMVVLLGVVAGVIGVIVNLRSAEFSAEAMVHAVFPGIVAGAVYWGIDAIIPAASVVAVAAAVVLTIVSHRSHRGEASEAGTAVVLTSFFSVGLILSLAKGDMSGQLEALMFGRLLEVTDERLAQALIVCAVALLLIAATWKEQVAYAFDRTGARASGLRLLALDLVLNTAIAAAVVSASTAVGILLVIGYLVIPGATARVLASRVRTMVLVAIAVGVGGGYLGMLLMALPGTSDKPISPQATVALVMTSILLVAVSVSTARERLRGPDRRAGSAQSATAGATSTTVGAKASANPIGGPEGSASTVTPATERSRV$","Zinc/manganese transport system permease protein","Membrane, Cytoplasm","hydrophobic membrane protein, putative","K02075 zinc/manganese transport system permease protein","ABC-3 protein","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR001626
Family

ABC-3
PF00950	$\"[30-296]T$	ABC-3

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[126-304]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-52]?$	signal-peptide
tmhmm	$\"[37-57]?$ $\"[62-82]?$ $\"[86-106]?$ $\"[116-136]?$ $\"[160-178]?$ $\"[193-215]?$ $\"[221-241]?$ $\"[246-266]?$ $\"[280-298]?$	transmembrane_regions

","BeTs to 8 clades of COG1108COG name: ABC-type Mn2+/Zn2+ transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1108 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB001626 (ABC transporter, family 3) with a combined E-value of 5.9e-24. IPB001626A 48-75 IPB001626C 186-196 IPB001626D 205-236","Residues 32-114 are similar to a (MEMBRANE SYSTEM ABC TRANSMEMBRANE) protein domain (PD968871) which is seen in Q6NIZ9_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 30 to 296 (E_value = 1.5e-31) place ANA_0220 in the ABC-3 family which is described as ABC 3 transport family.","","membrane protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0221","232892","233782","891","11.05","9.85","31168","ATGAGAATCGGCTTCGACATCCTCCTGCTGCCCATCATTGAGGTCCTTCTCATGGGGCTCCTGGCCGGGCTCGTGGGGGCGCTTGCACTGGTTCATCGCCGGATCTTCTTCACCGAGTCACTCACTCACGCGACCTTCCCCGGAGCGATCGTCGGCGTGGTCACCGCCGCCTGGTTCTCGCGGGCGGTTCTCGGTCAGCGCGCCGACTTCACCCTCCTGTCGGCGCTGGTGCTGGTGGGAGCCGCCTTCATGTGCCTGCCGATGATCTGGCTCATGCGGCGACTGTCCCAGGTCCCCGGGATCTCCTCCCAGTCTGCCGCCGGCGTTGTCCTCACCTTCGGATTCGCCCTGGGCTACTTCCTCAACAAGTGGTTCGCCCCGCTGCCGATCAAGGTGGACTCCTTCCTGGCCGGATCCGTGCTCAACGTCAACCGGGTCGATGTCATTGCCGTCGGCGTCGTCCTGGTGATGACGGTCCTCGTGCTCCTGGTGGCCGGGCGGTTCCTCACCTTCTACAGCTTCGACCCGCTGGGGTATCGCGCCAGCGGGCTGAACCCCGCCTGGGCCGAGGGGACCGTCATGGTCATGATCACCCTGACCATCGTGATGCTCGTTCCCGCCGTCGGCACGATTCTGCCCATCGCGCTCATCGCCGCGCCCGCGGCCGCGCTGGCGCCGTGGACGCGAACCATGCGGCACCTGCTCATCGGCGCCCCGATTCTCGGTGCGGCGACGTCCCTGGCCGGGCTGTTGATCGCGGTGCAGCTGAGCCTGTCTGCCGGCGGAGTCATCGCGGTGACCTCCGGGGTGGTCTACCTGGTCTCGGCCCTGGTCCACTGGGCCGCGATGAGCGGAGCCTGGGTTCGAGTGCCGCTGCTACGCAGGGGATGA","MRIGFDILLLPIIEVLLMGLLAGLVGALALVHRRIFFTESLTHATFPGAIVGVVTAAWFSRAVLGQRADFTLLSALVLVGAAFMCLPMIWLMRRLSQVPGISSQSAAGVVLTFGFALGYFLNKWFAPLPIKVDSFLAGSVLNVNRVDVIAVGVVLVMTVLVLLVAGRFLTFYSFDPLGYRASGLNPAWAEGTVMVMITLTIVMLVPAVGTILPIALIAAPAAALAPWTRTMRHLLIGAPILGAATSLAGLLIAVQLSLSAGGVIAVTSGVVYLVSALVHWAAMSGAWVRVPLLRRG$","Zinc/manganese transport system permease protein","Membrane, Cytoplasm","putative ABC transporter integral membranesubunit","K02075 zinc/manganese transport system permease protein","ABC-3 protein","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR001626
Family

ABC-3
PF00950	$\"[132-279]T$	ABC-3

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[40-60]?$ $\"[70-90]?$ $\"[99-119]?$ $\"[125-143]?$ $\"[148-168]?$ $\"[191-225]?$ $\"[235-253]?$ $\"[259-279]?$	transmembrane_regions

","BeTs to 15 clades of COG1108COG name: ABC-type Mn2+/Zn2+ transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1108 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB001626 (ABC transporter, family 3) with a combined E-value of 3.1e-18. IPB001626A 22-49 IPB001626D 193-224","Residues 7-272 are 66% similar to a (MEMBRANE SYSTEM ABC TRANSMEMBRANE) protein domain (PD966281) which is seen in Q6NIZ8_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 279 (E_value = 4.2e-13) place ANA_0221 in the ABC-3 family which is described as ABC 3 transport family.","","ABC transporter integral membrane subunit (troC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0222","234322","233852","471","7.38","0.60","17423","TTGTCGCCTTTCTTCTATGACGCCCCGGCCAGCGCCCTTAGCGTTCTGGTCATGAGCAGCACCAACTACACTGAGACATTCATCCGAGTCGCCGAGGACTGCCCGGTGCAGGACGCACAGGAGCCTCCTGCTGGCCCGAAGGGCAAGCCCCCGACGATCGCCCTCCTCCAGTACCGGCTCCTCAGCGAGCGCCCCTATGAGCTGACCTCCGACGACCTGCTGTTCGAGGTGCACGCCATTCGTCAGAACATTGAGCCTCCGGAGCGGGCTGCCCAGCGGGAGGCCTTCTTCGCCAAGCCCCAGGCCTGCCTGCGCTCCTCACCGTTGGCCAAGCGCTACGGCTGGGGCTTTCACCACGATGGCCAGGGCCGGGTGGCGCTGGTCCCTCAGGGCTCGACACGCTACCAGGAGCTCTCAGATGACACCTCACTCACCCAGTTGAAAGCCATGCGCTCGCGCCGCGCCTCCTGA","LSPFFYDAPASALSVLVMSSTNYTETFIRVAEDCPVQDAQEPPAGPKGKPPTIALLQYRLLSERPYELTSDDLLFEVHAIRQNIEPPERAAQREAFFAKPQACLRSSPLAKRYGWGFHHDGQGRVALVPQGSTRYQELSDDTSLTQLKAMRSRRAS$","Hypothetical protein","Periplasm, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 16-155 are 65% similar to a (BLL7858) protein domain (PD797167) which is seen in Q89CD9_BRAJA.","","-47% similar to PDB:1WPW Crystal Structure of IPMDH from Sulfolobus tokodaii (E_value = );-39% similar to PDB:2IUY CRYSTAL STRUCTURE OF AVIGT4, A GLYCOSYLTRANSFERASE INVOLVED IN AVILAMYCIN A BIOSYNTHESIS (E_value = );-39% similar to PDB:2IV3 CRYSTAL STRUCTURE OF AVIGT4, A GLYCOSYLTRANSFERASE INVOLVED IN AVILAMYCIN A BIOSYNTHESIS (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0223","234374","235234","861","8.37","4.29","31335","ATGTCAGCCGATCCGGACTGCGGTCCACGTCAGTCCCCGATCCATCCGCAGGAGCGCACAGGGGTGCTGGTACCGGACAACCTCACCCGCTACGGCGCGCACTGGCTGGCACCCGATCCCACAGTGGCCGACGTCGTCGACCAGTACTGGTACGTCTCATGGAACCTGGGCGACCAGAGCGTGGACCAGCGGATCATCGACGCCCCGGCCGTGACCCTGACGGTGGAGGAGGGCGACGTTCCCGCGCCTCTGGTGATTACCGGAGTTCAGACCCGTGCCTGGCACCGCACGATTCAGGGTCGTGGAAGGGTCTTCGCCATACGGCTGCGACCGGCGGGACTCGCCGTCCTCGGCGCGCTGTCGCCCCAGCACCTGGCCAACACCACGCTTCCCCTGACCGAGAAGCTCGACGCTGAACTGCACGCACTCATGCGCAGGGTCGCAACCTACCCCACGCCCCAAACCCGCGCCCAGGCCGCCGATGAGGCGATCCGGGAGCGGCTGGCCGACCACCGGCCCTCTGAGAGCGGCCTTCTGGCCAACAGGGTGGTCGATGAGCTGCGTTCCCGGCTTCACCGGCGCACTGGCGACTCCCTGCCTGCGGCTCTGCACGTCAGTGAGCGCACGATCCAGCGCTGCCTGCGCGCCACCCTGGGACGCGGGCCGAGATGGGTGGGGCACCGCATCAGGCTCCAGGAGGTGGTTCTGGCACTCACGGCGCGCCCTGAGGCCGACCTGGCCACGATCGCCGCAGACCTCGGCTTCGCCGACCAGTCTCACCTGTCGGGTGCCTTCAGAACCGCCTGCGGACTGAGCCCCAGCGCCTATCGGCGCAGTCTTGAGGCTCTCATCAACGGATGA","MSADPDCGPRQSPIHPQERTGVLVPDNLTRYGAHWLAPDPTVADVVDQYWYVSWNLGDQSVDQRIIDAPAVTLTVEEGDVPAPLVITGVQTRAWHRTIQGRGRVFAIRLRPAGLAVLGALSPQHLANTTLPLTEKLDAELHALMRRVATYPTPQTRAQAADEAIRERLADHRPSESGLLANRVVDELRSRLHRRTGDSLPAALHVSERTIQRCLRATLGRGPRWVGHRIRLQEVVLALTARPEADLATIAADLGFADQSHLSGAFRTACGLSPSAYRRSLEALING$","Transcriptional regulator, AraC family ","Cytoplasm","putative AraC-family transcriptional regulator","putative transcriptional regulator","helix-turn-helix- domain containing protein, AraC type","","Gallegos M.T., Michan C., Ramos J.L. The XylS/AraC family of regulators. Nucleic Acids Res. 1993. 21(4):807-810. PMID: 8451183Henikoff S., Wallace J.C., Brown J.P. Finding protein similarities with nucleotide sequence databases. Meth. Enzymol. 1990. 183:111-132. PMID: 2314271Parker L.L., Hall B.G. Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12. Genetics 1990. 124(3):455-471. PMID: 2179047Bustos S.A., Schleif R.F. Functional domains of the AraC protein. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(12):5638-5642. PMID: 8516313","","","

InterPro
IPR000005
Domain

Helix-turn-helix, AraC type
PR00032	$\"[246-261]T$ $\"[261-277]T$	HTHARAC
PF00165	$\"[233-278]T$	HTH_AraC
SM00342	$\"[193-277]T$	HTH_ARAC
PS01124	$\"[181-279]T$	HTH_ARAC_FAMILY_2
PS00041	$\"[230-273]?$	HTH_ARAC_FAMILY_1

noIPR
unintegrated

unintegrated
PTHR11019	$\"[181-279]T$	THIJ/PFPI
PTHR11019:SF11	$\"[181-279]T$	ARAC FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN

","BeTs to 9 clades of COG2207COG name: AraC-type DNA-binding domain-containing proteinsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2207 is --------v-rlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000005 (Helix-turn-helix, AraC type) with a combined E-value of 4.1e-11. IPB000005 246-277***** IPB003313 (Arac protein, arabinose-binding/dimerisation) with a combined E-value of 1.2e-06. IPB003313F 241-281","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 233 to 278 (E_value = 1.7e-06) place ANA_0223 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, AraC family.","","AraC-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0224","237077","235266","1812","5.19","-18.00","63898","GTGTTTGGAAACACCAGTGAGGAGCGTCATTGTGAGCGTTTCCAGAAGTTATCGCGCGGTACCGTCGCAGATATGACCCGAAGCCCTGAAGATGTGTACGACGACGTTGCCGTGGACGCGTGGATCCAGGACGATCCGGATCCCGTCACCCGCGCCGAGCTCACTGAGCTGCTGAGCGCCGCCCGCTCTCATGGCGAGCAGGCCCAGGCAGCTCGCAGGGCACTCAGCGACGCCTTCAGCGGCACCCTCGCCTTCGGCACGGCCGGCCTACGAGGCCGCCTGGGCGGCGGCCCCAACCGGATGAACCGGGTCGTCGTCATCCGCGCCGCGGCGGGGCTGTCCGCTTACCTCAAGGACCGTCTCGGTGAGGGTTTCAGCGTCGTCATCGGCTACGACGCCCGCCACAACTCCAAGCAGTTCGCCCTCGATACGGCCGCGGTCGTCACCGGTGCGGGCGGTCGGGCCATTCTCTTCGAGTCGCACTGCCCGACCCCGGTACTCGCCTTCGCGCTGCGGCGCCTGGAGGCCGACGCCGGCGTCATGGTGACGGCCTCGCACAACCCTCCCCAGGACAACGGCTACAAGGTCTACCTGGGCGGGAGGGCCGTGACCGACTCAGGTCAGGGGGCCCAGATCGTTCCCCCCTATGACAGCCAGATCGCTGCGGCGATCGACGCCGTCGGCCCGGTCAGCTCCGTACCCCGCCCGCAGTCGGGCTGGGAGACGGTCGACCCGGAGATCCGGGAGGAGTACATCGAGCGGGCCGCTCAGGCGGCTCGGATGACGGCCCCCGCCCCGGTGAAGATCGTGTTGACGGCGATGCACGGCGTGGGTGGGGCCACCTGCCGTGAGGTGCTCGCGCGAGCCGGGTTCACCGACGTCGTCGAGGTGGCTGAACAGTTCGAGCCGGATCCGGACTTCCCGACGGTCACCTTCCCCAACCCGGAGGAGCCCGGGGCGCTGGACCTGGCGCTGGACAAGGCCCGGCAGGTCGAGGCGGACCTGGTGATCGCCAACGATCCCGATGCGGATCGTTGCTCCGCCGCCATCCCGGACGAGGACGCTCCCGGCGGCTGGCGTCAGCTGACGGGCGATGAGGTCGGCGCGCTCCTGGGTGAGCAGGCCGCCGAGCTGGCCGCTTTCGCCGGCAACGGGGTCCTGGCCTGTTCCGTGGTCTCCTCCCGCCTGCTGCGCCGGATCGCCCAGTCCCACGGCTTGGGCTTCCGCCGCACCCTGACGGGCTTCAAGTGGATCAGCCGTGAGCCAGGCCTGGTCTTCGGCTACGAGGAGGCCCTGGGCTACTGCGTCGATCCTGCCGCGGTGCGGGACAAGGACGGCATCTCCGCCTCCGTGCGGTTGGCGGTGCTGACCTCCGTGCTCAAGCAGCAGGGCCGGACCTTGCAGGATCTGCTCGACCGGCTCGCGCGGGAGCACGGGCTGCACGCCACGAGCCCGTTGAGCATGCGAGTCGAGGACCTTGACATCATCACCAGCACCATGGAGCGTCTGCGTTCGGGCGGGGCACCGGCCAAGCTCGCCGGTTCCCCGATCACCAAGACGGTGGATCTGCTCGACGGCATCTCGGACGGCAACGGCGGCACCCTTCCCCCCACGAACGGCCTGGTGTGGGTGACGGCCTCGGATGACCGGGTGGTCGTGCGACCCTCAGGGACCGAGCCCAAGCTCAAGTGCTACTGCGAGGTGATTCTGCCGACGAATGACACTCCGGTGGCCCAGGTTCGGGAGGCGGCCGCTGAGCGCCTGGAGGCCATCAAGGCCGACCTGCGCGGAATCCTGGGGATCGCCGCCTGA","VFGNTSEERHCERFQKLSRGTVADMTRSPEDVYDDVAVDAWIQDDPDPVTRAELTELLSAARSHGEQAQAARRALSDAFSGTLAFGTAGLRGRLGGGPNRMNRVVVIRAAAGLSAYLKDRLGEGFSVVIGYDARHNSKQFALDTAAVVTGAGGRAILFESHCPTPVLAFALRRLEADAGVMVTASHNPPQDNGYKVYLGGRAVTDSGQGAQIVPPYDSQIAAAIDAVGPVSSVPRPQSGWETVDPEIREEYIERAAQAARMTAPAPVKIVLTAMHGVGGATCREVLARAGFTDVVEVAEQFEPDPDFPTVTFPNPEEPGALDLALDKARQVEADLVIANDPDADRCSAAIPDEDAPGGWRQLTGDEVGALLGEQAAELAAFAGNGVLACSVVSSRLLRRIAQSHGLGFRRTLTGFKWISREPGLVFGYEEALGYCVDPAAVRDKDGISASVRLAVLTSVLKQQGRTLQDLLDRLAREHGLHATSPLSMRVEDLDIITSTMERLRSGGAPAKLAGSPITKTVDLLDGISDGNGGTLPPTNGLVWVTASDDRVVVRPSGTEPKLKCYCEVILPTNDTPVAQVREAAAERLEAIKADLRGILGIAA$","Phosphomannomutase","Cytoplasm","YhxB","putative phosphomannomutase ","phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I","","Dai J.B., Liu Y., Ray Jr W.J., Konno M. The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution. J. Biol. Chem. 1992. 267(9):6322-6337. PMID: 1532581Zielinski N.A., Chakrabarty A.M., Berry A. Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase. J. Biol. Chem. 1991. 266(15):9754-9763. PMID: 1903398","","","

InterPro
IPR005841
Family

Phosphoglucomutase/phosphomannomutase
PR00509	$\"[178-192]T$ $\"[266-285]T$ $\"[333-348]T$	PGMPMM
PS00710	$\"[179-188]T$	PGM_PMM

InterPro
IPR005844
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I
PF02878	$\"[82-231]T$	PGM_PMM_I

InterPro
IPR005845
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II
PF02879	$\"[249-359]T$	PGM_PMM_II

InterPro
IPR005846
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III
PF02880	$\"[363-474]T$	PGM_PMM_III

noIPR
unintegrated

unintegrated
G3DSA:3.40.120.10	$\"[72-231]T$ $\"[268-349]T$ $\"[361-483]T$	no description
PTHR22573	$\"[144-596]T$	PHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF2	$\"[144-596]T$	PHOSPHOGLUCOMUTASE

","BeTs to 26 clades of COG1109COG name: PhosphomannomutaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1109 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB005841 (Phosphoglucomutase/phosphomannomutase) with a combined E-value of 1e-13. IPB005841B 127-137 IPB005841D 178-188 IPB005841G 272-281 IPB005841I 334-345 IPB005841M 548-560","Residues 40-117 are 67% similar to a (PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOGLUCOMUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE FAMILY PROBABLE MUTASE PHOSPHORYLATION METAL-BINDING MAGNESIUM) protein domain (PD688253) which is seen in Q9AD82_STRCO.Residues 116-181 are 68% similar to a (PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOGLUCOMUTASE MUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE MAGNESIUM METAL-BINDING PHOSPHORYLATION PHOSPHOGLUCOSAMINE PHOSPHOMUTASE) protein domain (PD475365) which is seen in Q6A712_PROAC.Residues 183-235 are 64% similar to a (PHOSPHOMANNOMUTASE ISOMERASE MUTASE PHOSPHOGLUCOMUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE MAGNESIUM METAL-BINDING PHOSPHOGLUCOSAMINE PHOSPHORYLATION FAMILY) protein domain (PD000667) which is seen in Q6NJW9_CORDI.Residues 183-252 are 62% similar to a (PHOSPHOMANNOMUTASE) protein domain (PDA0Z9N9) which is seen in Q6AGN7_BBBBB.Residues 270-365 are similar to a (PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOGLUCOMUTASE MUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE MAGNESIUM METAL-BINDING PHOSPHORYLATION PHOSPHOGLUCOSAMINE FAMILY) protein domain (PD000778) which is seen in Q9AD82_STRCO.Residues 385-431 are 80% similar to a (PHOSPHOGLUCOMUTASE ISOMERASE PHOSPHOMANNOMUTASE METAL-BINDING MAGNESIUM PHOSPHORYLATION PGM GLUCOSE PHOSPHOMUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE) protein domain (PD853029) which is seen in Q6AGN7_BBBBB.Residues 432-514 are 73% similar to a (PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOGLUCOMUTASE PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE FAMILY PROBABLE MUTASE METAL-BINDING PHOSPHORYLATION MAGNESIUM) protein domain (PD394215) which is seen in Q9AD82_STRCO.Residues 527-596 are 68% similar to a (MUTASE PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOMANNOSE PROBABLE PMMB) protein domain (PD873701) which is seen in Q6NJW9_CORDI.","","-39% similar to PDB:1TUO Crystal structure of putative phosphomannomutase from Thermus Thermophilus HB8 (E_value = 1.3E_20);-40% similar to PDB:1WQA Crystal Structure of Pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with Mg2+ (E_value = 6.2E_15);-46% similar to PDB:1K35 Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa (E_value = 1.9E_11);-46% similar to PDB:1P5D Enzyme-ligand complex of P. aeruginosa PMM/PGM (E_value = 1.9E_11);-46% similar to PDB:1P5G Enzyme-ligand complex of P. aeruginosa PMM/PGM (E_value = 1.9E_11);","Residues 82 to 231 (E_value = 3e-48) place ANA_0224 in the PGM_PMM_I family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I.Residues 249 to 359 (E_value = 4e-06) place ANA_0224 in the PGM_PMM_II family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II.Residues 363 to 474 (E_value = 0.00041) place ANA_0224 in the PGM_PMM_III family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0225","237307","238062","756","5.04","-9.09","27192","ATGAGTACACGCGAGTCCTACCGCAAGGGGCCAGTGGTGCTGCGCGGCACCCAGATCCCCACCCAGACTACCGACGCGCGACTGCTGAGCAGTGACGCCGACGCCGACTGGCTCCACGCCGACCCGTGGCGGGTCATGCGCATCCAGGCGGAGTTCGTCGAGGGCTTCGGAGCCTTGGCGGAGCTGGGGCCGGCCATCAGCGTCTTCGGCTCGGCACGCACCAAACCCGAGGACCCTACCTATCGCATGGCCATGGAGGTCGGCGCCGGGCTGGCGCGCGCCGGCTACGCCGTCATCACCGGAGGCGGCCCGGGCATGATGGAGGCCGCCAACCGTGGGTGCCATGAGGCCGGCGGGACCTCAGTGGGCCTGGGCATCGAGCTGCCCCACGAGCAGGGCATGAACGAGTACGTCGATCTCGGGGTCAACTTCCGCTACTTCTTCGCCCGCAAGACCATGTTCGTCAAGTACTCCGACGGATTCGTCGTCATGCCCGGCGGGATGGGGACCCTCGACGAGCTCTTCGAGGCCCTCACTCTGGTTCAGACTCAGAAGATCTCCTCCTTCCCCATCGTCCTGGTGGACAGCGGTTACTGGGGTGGGCTGCTGGAGTGGCTGCGCACCACGATGATCGAGCGCGGCATGATCTCTGCCAGCGACCCCGACCTGCTGCACGTCGTCGACGATGCTGAGGAGGCTGTGGACTACGTGGTCAGCGCGGCCCGTCGGCTGCGCGACGGCCGGGCGGGGGCGTGA","MSTRESYRKGPVVLRGTQIPTQTTDARLLSSDADADWLHADPWRVMRIQAEFVEGFGALAELGPAISVFGSARTKPEDPTYRMAMEVGAGLARAGYAVITGGGPGMMEAANRGCHEAGGTSVGLGIELPHEQGMNEYVDLGVNFRYFFARKTMFVKYSDGFVVMPGGMGTLDELFEALTLVQTQKISSFPIVLVDSGYWGGLLEWLRTTMIERGMISASDPDLLHVVDDAEEAVDYVVSAARRLRDGRAGA$","Rossmann fold nucleotide-binding protein","Cytoplasm","Predicted Rossmann fold nucleotide-bindingprotein","hypothetical protein","conserved hypothetical protein 730","","","","","

InterPro
IPR005269
Family

Conserved hypothetical protein 730
PF03641	$\"[107-240]T$	Lysine_decarbox
TIGR00730	$\"[64-240]T$	TIGR00730: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.450	$\"[63-239]T$	no description

","BeTs to 16 clades of COG1611COG name: Predicted Rossmann fold nucleotide-binding proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1611 is a--pk-yqvdrlb-efghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB005269 (Conserved hypothetical protein 730) with a combined E-value of 3.3e-46. IPB005269A 64-112 IPB005269B 143-189 IPB005269A 94-142","Residues 68-149 are similar to a (FAMILY DECARBOXYLASE EXPORTED NUCLEOTIDE-BINDING FOLD PREDICTED ROSSMANN CC0810 TLL1830 CT0458) protein domain (PD294994) which is seen in Q6NHZ7_CORDI.Residues 150-199 are 84% similar to a (DECARBOXYLASE LYSINE FAMILY DECARBOXYLASE-LIKE NUCLEOTIDE-BINDING FOLD PREDICTED ROSSMANN SIMILAR EXPORTED) protein domain (PD005712) which is seen in Q6MD50_PARUW.Residues 183-224 are 71% similar to a (PLASMID) protein domain (PD975827) which is seen in Q937Z9_MYCAV.","","-71% similar to PDB:1WEK Crystal structure of the conserved hypothetical protein TT1465 from Thermus thermophilus HB8 (E_value = 2.7E_52);-50% similar to PDB:1WEH Crystal structure of the conserved hypothetical protein TT1887 from Thermus thermophilus HB8 (E_value = 2.3E_14);-49% similar to PDB:1T35 CRYSTAL STRUCTURE OF A HYPOTHETICAL PROTEIN YVDD- A PUTATIVE LYSINE DECARBOXYLASE (E_value = 7.5E_10);-50% similar to PDB:1RCU X-RAY STRUCTURE OF TM1055 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET VT76 (E_value = 9.8E_10);","Residues 107 to 240 (E_value = 3.4e-58) place ANA_0225 in the Lysine_decarbox family which is described as Possible lysine decarboxylase.","","Rossmann fold nucleotide-binding protein (AL160371)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0226","238168","238335","168","6.66","-0.07","5739","ATGGCTGCCATGAAGCCCCGGACCGGAGACGGCCCCCTCGAAGTCGTCAAGGAAGGCCGCGCCATCATCATGCGGGTTCCGCTTGAGGGTGGTGGTCGACTCGTCCTCGAGATCACGGCCGATGAGGTCAAGGCACTCGGAGAGGCCCTGGCCAACGCCAAGATCTGA","MAAMKPRTGDGPLEVVKEGRAIIMRVPLEGGGRLVLEITADEVKALGEALANAKI$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-50 are similar to a (CALMODULIN-LIKE MB1243 ML1067 SCO5145 CGL1114 U1756N) protein domain (PD027920) which is seen in Q9FBL3_STRCO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0227","239170","238484","687","5.70","-2.58","24142","ATGTGGCTCGAGGGGTGCGCCTGGCACCCCGCAGCAGAAGAAAGGCTCACAGTGAGTGCGGACAAGACGCTGAGCTGGTCCTACACGGAGGACTTCACCGCGGAGGACGAGGCCACCGCCCAGGCCCGCATACGCGGGCTCGAGCTCGGCATCACCCCGGTGTCCTCGGGGACCGGAGCGGCGCTGCGGATGTTGGCCGCCTCAGTGGGAGCCAAGTCCGTGGCCGAGGTCGGCACCGGCACCGGTGTCTCGGGTCTGTGGCTGCTGGGCGGCATGGGCACTGACGGGGTCCTCACCACGATCGACGTCGAGCCCGAGCTCCAGCGCGAGGCGCGTCGCGCCTTCGACGGGGCCGGCTACCCCTCCTCGCGCACCCGCATCATCCAGGGTCGGGCCTCGGACGTCATGCCCCGGATGGCGGCCCGCTCCTACGACATGGTGGTGCTCGACGTCGCCCCGGAGGAGGCGATCCTCCTGGCCTCCAACGCCCTGCGGATGCTGCGCCCCGGCGGGGTCCTGGCCGTCACTCGGGCCCTGTGGAACGACCACGTGGCCGACCCGGCCCGCCGCGACGTCACCACCGTGGCAGCCCGCGAGCTCGGCAAGGCGCTGCGGGCCTCCCGCGCGCTGCTGACCACGCTGCTGCCCGTCGGAGACGGCCTGCTCGTCTCCGTGCGCCAGACCTGA","MWLEGCAWHPAAEERLTVSADKTLSWSYTEDFTAEDEATAQARIRGLELGITPVSSGTGAALRMLAASVGAKSVAEVGTGTGVSGLWLLGGMGTDGVLTTIDVEPELQREARRAFDGAGYPSSRTRIIQGRASDVMPRMAARSYDMVVLDVAPEEAILLASNALRMLRPGGVLAVTRALWNDHVADPARRDVTTVAARELGKALRASRALLTTLLPVGDGLLVSVRQT$","O-methyltransferase, family 3","Cytoplasm","probable methyltransferase","probable methyltransferase ","O-methyltransferase, family 3","","Pospiech A., Bietenhader J., Schupp T. Two multifunctional peptide synthetases and an O-methyltransferase are involved in the biosynthesis of the DNA-binding antibiotic and antitumour agent saframycin Mx1 from Myxococcus xanthus. Microbiology 1996. 142:741-746. PMID: 8936303","","","

InterPro
IPR002935
Family

O-methyltransferase, family 3
PTHR10509	$\"[13-227]T$	O-METHYLTRANSFERASE

InterPro
IPR013216
Domain

Methyltransferase type 11
PF08241	$\"[75-175]T$	Methyltransf_11

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[52-215]T$	no description
PIRSF005841	$\"[20-228]T$	Caffeoyl-CoA 3-O-methyltransferase

","BeTs to 10 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 6","***** IPB002935 (O-methyltransferase, family 3) with a combined E-value of 2.8e-23. IPB002935A 52-99 IPB002935C 193-226","Residues 20-123 are 64% similar to a (METHYLTRANSFERASE TRANSFERASE O-METHYLTRANSFERASE) protein domain (PDA1B5N8) which is seen in Q6AFP7_BBBBB.Residues 25-227 are 44% similar to a (METHYLTRANSFERASE PROBABLE TRANSFERASE) protein domain (PD833222) which is seen in Q8G5R4_BIFLO.Residues 25-113 are 53% similar to a (METHYLTRANSFERASE TRANSFERASE) protein domain (PDA1B5N9) which is seen in Q6AA19_PROAC.Residues 35-91 are 61% similar to a (METHYLTRANSFERASE TRANSFERASE PROBABLE 2.1.1.- O-METHYLTRANSFERASE) protein domain (PD703834) which is seen in Q9CCA7_MYCLE.Residues 54-180 are 48% similar to a (METHYLTRANSFERASE TRANSFERASE O-METHYLTRANSFERASE CAFFEOYL-COA BIOSYNTHESIS TRANS-CAFFEOYL-COA LIGNIN CCOAOMT CCOAMT 3-O-METHYLTRANSFERASE) protein domain (PD002981) which is seen in O67476_AQUAE.Residues 54-92 are 89% similar to a (METHYLTRANSFERASE TRANSFERASE) protein domain (PD898028) which is seen in Q82IL5_STRAW.Residues 65-224 are 48% similar to a (METHYLTRANSFERASE TRANSFERASE O-METHYLTRANSFERASE) protein domain (PD733743) which is seen in Q870E1_EEEEE.Residues 98-191 are 58% similar to a (METHYLTRANSFERASE TRANSFERASE CGL1119 PROBABLE O-METHYLTRANSFERASE) protein domain (PD891317) which is seen in Q6NHY7_CORDI.Residues 124-190 are 62% similar to a (METHYLTRANSFERASE TRANSFERASE O-METHYLTRANSFERASE CAFFEOYL-COA 3-O-METHYLTRANSFERASE TRANS-CAFFEOYL-COA BIOSYNTHESIS LIGNIN CCOAOMT CCOAMT) protein domain (PD245993) which is seen in Q6AFP7_BBBBB.","","-45% similar to PDB:2AVD Crystal Structure of Human Catechol-O-methyltransferase domain containing 1 (E_value = 2.0E_14);","Residues 24 to 227 (E_value = 4.2e-09) place ANA_0227 in the Methyltransf_3 family which is described as O-methyltransferase.Residues 75 to 175 (E_value = 0.00022) place ANA_0227 in the Methyltransf_11 family which is described as Methyltransferase domain.","","methyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0229","239279","240178","900","4.47","-32.22","32045","GTGTTCGGCATCAACGGAAATGAGTTCCTCGTCATCATCCTGGTGGCGGTGATCGTGGTGGGGCCGCAGCGCTTGCCCGAGTACACCCGCAAGCTCACGCAGCTGGTGCGCCAGCTCAGGGTGTTCCTGGACAATGCGCGCAGCCAGATCGCCGAGGAAGTCGGCCCCGAGATGGCCGACCTGGACCTGTCCAGCCTCGATCCGCGCCAGTACGACCCGCGCAAGATCGTGCGCGATGCCCTGGGGGAGGACATCGACGCCATCCGCGAGGACCTCGCCCACCCCTTCCGCTCCGTCGGCTCAGCCGCCAAGGAGATGTCCGACGACGCCGCACAGGCTGTCAACGACGTGGTCAAGAAGGATCGGGCCTCGTCGCTGAGCAAGCAGATCGAGGCCAAGCGCGACGAGCGGCTGGCCGAGAAGGACACCGAGAAGGCTGAGAACACCGAGAGCACTGAGGGCGCCGAGAACGCTGAGGGCCCGCAGAGTGCTGAGCAGCCCCCCGCCACTGCGCCGCGGGGAGTGCTCCAGCAGGCCGACGACGTCGAGCATGCCGTCGAGGCCGAGGCCGAGACTGATGCTGGGTCGGTCGAGTCGGCTGAAGGGGCTGAGCCGGAGAAGACAGAGCCCGAGCAGTCCGGGGAGGCCGAGGTCGCCGAGGACCCGGAGAGCACTGAGCAGCCGGAGCAGTCCGACCGTCCGGCCGAGCCGGTTGAGGTCCCGACAAGCCTGGTCGAGCCGCAGGCCGCTGCCGCCGGTGAGGATGCAGGGGACGCCACCGCGGCGGGTGATGACTCCCGTAATCGCGTGCACCCTCTATCGCCGCGTGACATCGTGCGAGCCGCCAACGCCGCCGCCCGCACCCGCGCCGAGGCCGCGCGTATCGCCGTCGACTTCTGA","VFGINGNEFLVIILVAVIVVGPQRLPEYTRKLTQLVRQLRVFLDNARSQIAEEVGPEMADLDLSSLDPRQYDPRKIVRDALGEDIDAIREDLAHPFRSVGSAAKEMSDDAAQAVNDVVKKDRASSLSKQIEAKRDERLAEKDTEKAENTESTEGAENAEGPQSAEQPPATAPRGVLQQADDVEHAVEAEAETDAGSVESAEGAEPEKTEPEQSGEAEVAEDPESTEQPEQSDRPAEPVEVPTSLVEPQAAAAGEDAGDATAAGDDSRNRVHPLSPRDIVRAANAAARTRAEAARIAVDF$","Twin-arginine translocation protein, TatB","Cytoplasm, Extracellular","twin-arginine translocation protein TatB,putative","hypothetical protein","twin-arginine translocation protein, TatB subunit","","Sargent F., Bogsch E.G., Stanley N.R., Wexler M., Robinson C., Berks B.C., Palmer T. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 1998. 17(13):3640-3650. PMID: 9649434Berks B.C., Sargent F., Palmer T. The Tat protein export pathway. Mol. Microbiol. 2000. 35(2):260-274. PMID: 10652088","","","

InterPro
IPR003998
Family

Twin-arginine translocation protein TatB
PR01506	$\"[1-21]T$ $\"[21-40]T$ $\"[40-58]T$	TATBPROTEIN
TIGR01410	$\"[2-80]T$	tatB: twin arginine-targeting protein trans

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide

","No hits to the COGs database.","***** IPB003998 (Bacterial sec-independent translocation TatB protein signature) with a combined E-value of 3.5e-11. IPB003998A 1-21 IPB003998B 21-40***** IPB003369 (Bacterial sec-independent translocation protein mttA/Hcf106) with a combined E-value of 7.8e-08. IPB003369 4-41","Residues 21-93 are 61% similar to a (TRANSLOCATION TWIN COMPONENT PROTEIN ARGININE COMPLEX) protein domain (PDA0U3Y1) which is seen in Q6AA17_PROAC.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","translocation protein TatB, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0230","241414","240272","1143","4.98","-13.58","39807","ATGACGCAACCGACTCATGACGCCGTCATGGAGGCGCTGGCCAGGGTCATCGACCCCGAGCTGCACCGCCCCATCACCGACCTGGGAATGGTCTCCACCGTTGACATCGCCGAGGACGGCGTGGTCAGCGTCGAGGTGCTCCTGACCGTGGCCGGGTGCCCCTTGAAGGACACCATCACCGCCGACACCCGGCGCGAGGTCAGCACCGTCGAGGGTGTCACCGAGGTGCAGGTGAGCCTGGGCGTCATGAACGACGAGCAGAAGGCCGAGCTGCGGCGCCGCCTGCGCGGAGGGGCCGCCGAACCGGTGGTTCCCTTCACTCAGCCGGGCAACCTCACCCGGGTCTACGCCGTCACCTCCGGCAAGGGAGGGGTCGGCAAGTCCTCGGTGACTGCGAACCTCGCCGCCGCCATGGCCGCCCAGGGCCTGAGCGTGGGCGTGGTAGACGCCGACATCTACGGCTTCTCCATCCCCCGCATGCTGGGGGTGGACCGGGTGCCCACCCAGCTCGACGGCATGATCGTGCCGCCGGTGGCCCACGGGGTGAAGGTCATCTCCATCGGCATGTTCGTGGAGGACAAGCAGCCGGTTGTGTGGCGCGGCCCCATGCTGCACCGCGCCGTCCAGCAGTTCCTGTCCGATGTGTTCTGGGGCGACCTGGACGTCCTGCTGCTGGACCTGCCGCCTGGCACCGGCGACGTGACGATCTCCGTGGCCCAGCTGCTCCCGAACGCCGAGATTCTCGTGGTCACCACCCCGCAGACGGCCGCCGCCGAGGTCGCAGAGCGCACCGGCCTCATCGCCACCCAGACGCACCAGAAGGTGGTGGGCGTCATCGAGAACATGTCCTACATGCCCCAGCCCGACGGCTCACGCCTGGAGATCTTCGGCTCCGGCGGGGGCGAGATCGTCAGCGCCTCCTTGAGCGAGACCCTCGGCTACGAGGTGCCGCTGCTGGCCCAGCTGCCGCTGGACATCCGCCTGCGCGAGGGCTCCGACACCGGTCTGCCGGCCACCGTGGCCCAGGACGGCAAGCCGGCCGCCGACGCCCCCGCAGCCCTGGAGCTGTCCGCTGTGGCCCAGCGCCTGACTCACCGCTCCCGCGGCCTGGCCGGCAAGAGCCTGGGGGTCACCCCGGCCTGA","MTQPTHDAVMEALARVIDPELHRPITDLGMVSTVDIAEDGVVSVEVLLTVAGCPLKDTITADTRREVSTVEGVTEVQVSLGVMNDEQKAELRRRLRGGAAEPVVPFTQPGNLTRVYAVTSGKGGVGKSSVTANLAAAMAAQGLSVGVVDADIYGFSIPRMLGVDRVPTQLDGMIVPPVAHGVKVISIGMFVEDKQPVVWRGPMLHRAVQQFLSDVFWGDLDVLLLDLPPGTGDVTISVAQLLPNAEILVVTTPQTAAAEVAERTGLIATQTHQKVVGVIENMSYMPQPDGSRLEIFGSGGGEIVSASLSETLGYEVPLLAQLPLDIRLREGSDTGLPATVAQDGKPAADAPAALELSAVAQRLTHRSRGLAGKSLGVTPA$","ATP-binding protein involved in chromosome partitionin","Cytoplasm","Mrp protein homolog","K03593 ATP-binding protein involved in chromosome partitioning","protein of unknown function DUF59","","Olivera E.R., Minambres B., Garcia B., Muniz C., Moreno M.A., Ferrandez A., Diaz E., Garcia J.L., Luengo J.M. Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: the phenylacetyl-CoA catabolon. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(11):6419-6424. PMID: 9600981","","","

InterPro
IPR000808
Family

Mrp
PS01215	$\"[217-233]T$	MRP

InterPro
IPR002744
Domain

Protein of unknown function DUF59
PD005595	$\"[5-87]T$	Q82IM1_STRAW_Q82IM1;
PF01883	$\"[5-80]T$	DUF59

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[112-363]T$	no description
PTHR23264	$\"[152-350]T$	NUCLEOTIDE-BINDING PROTEIN NBP35(YEAST)-RELATED
PTHR23264:SF4	$\"[152-350]T$	MRP-RELATED NUCLEOTIDE-BINDING PROTEIN

","BeTs to 23 clades of COG0489COG name: ATPases involved in chromosome partitioningFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0489 is aompkzyqvdr-bcefghsnujx---Number of proteins in this genome belonging to this COG is 3","***** IPB000808 (Mrp family) with a combined E-value of 2.1e-71. IPB000808A 112-151 IPB000808B 197-233 IPB000808C 253-285 IPB000808D 302-337***** IPB002744 (Protein of unknown function DUF59) with a combined E-value of 6.7e-20. IPB002744A 9-31 IPB002744B 42-67 IPB002744C 257-281***** IPB002586 (Cobyrinic acid a,c-diamide synthase) with a combined E-value of 3.5e-19. IPB002586A 116-149 IPB002586B 216-238***** IPB003348 (Anion-transporting ATPase) with a combined E-value of 1.5e-06. IPB003348A 117-153","Residues 5-87 are similar to a (MRP ATP-BINDING HOMOLOG ACID PHENYLACETIC DEGRADATION PAAD PROTEIN COMPLEX RING) protein domain (PD005595) which is seen in Q82IM1_STRAW.Residues 157-213 are 82% similar to a (ATP-BINDING MRP NUCLEOTIDE-BINDING HOMOLOG BINDING FAMILY ATPASE CHROMOSOME MRP/NBP35 PROTEIN) protein domain (PD587968) which is seen in Q9FBK6_STRCO.Residues 236-299 are similar to a (ATP-BINDING MRP HOMOLOG NUCLEOTIDE-BINDING BINDING FAMILY ATPASE CHROMOSOME MRP/NBP35 PROTEIN) protein domain (PD092650) which is seen in MRP_MYCLE.","","-50% similar to PDB:2PH1 Crystal structure of nucleotide-binding protein AF2382 from Archaeoglobus fulgidus, Northeast Structural Genomics Target GR165 (E_value = 2.0E_18);","Residues 5 to 80 (E_value = 1.6e-26) place ANA_0230 in the DUF59 family which is described as Domain of unknown function DUF59.","","protein homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0231","242057","241485","573","5.19","-5.54","21861","ATGCCTGACCAGCTCGACCAGCCCTTGCCCGACAGTCGCCTGCGGTGGCTGCGCAGGACGCATCCGGCCCACGCCTCGCGCTCGGACGGCTTCGGCCGCTTCGCCGAGGCCACCGCCCGCTTCATGGGCTCGCCCAAGTTCGTGCTCTACATGACGATCTTCGTCGCTGTGTGGATCGTGGCGAACCTCATCCTGGCCAAGATGCAGCAGGCCTGGGACCCCTACCCCTTCATCCTGCTCAACCTGGCCTTCTCCACCCAGGCCTCCTACTCGGCCCCCCTCATCATGCTGGCCCAGAACCGGCAGGACGACCGTGACCGGGTTACCGCCGAGCAGGACCGCCAGCGCGCCCAGCGCAACCTGGAGGACACCGAGTTCCTCACCCGGGAGATCGCCGCCCTGCGCCTGGCCATGAACGACGTCGCCACCCGCGACTTCGTGCGCAGCGAACTTCGCGACATGCTCAGCGAGATCCTCGCCGAGGAGCGCCTCACCCGTGAAGAGATCGCCGAGTTCCAGGACAGCGGCGACGACGAGCCCAGCACCACTCCTGGACAGCGCACCGCCCAGTGA","MPDQLDQPLPDSRLRWLRRTHPAHASRSDGFGRFAEATARFMGSPKFVLYMTIFVAVWIVANLILAKMQQAWDPYPFILLNLAFSTQASYSAPLIMLAQNRQDDRDRVTAEQDRQRAQRNLEDTEFLTREIAALRLAMNDVATRDFVRSELRDMLSEILAEERLTREEIAEFQDSGDDEPSTTPGQRTAQ$","Predicted membrane protein [Function unknown]","Cytoplasm","putative integral membrane protein","hypothetical protein","protein of unknown function DUF1003","","","","","

InterPro
IPR010406
Family

Protein of unknown function DUF1003
PF06210	$\"[20-150]T$	DUF1003

noIPR
unintegrated

unintegrated
tmhmm	$\"[47-65]?$ $\"[75-97]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 33-168 are 47% similar to a (SMB20255 DRA0362 PLASMID) protein domain (PD542031) which is seen in Q92WT4_RHIME.Residues 72-154 are similar to a (MEMBRANE PROBABLE INTEGRAL LP_1807 CT1691 GBS2003 SAG2047 MLR4962 SMU.1307C AGR_C_3054P) protein domain (PD394069) which is seen in Q73WV9_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 20 to 150 (E_value = 1e-49) place ANA_0231 in the DUF1003 family which is described as Protein of unknown function (DUF1003).","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0232","243342","242050","1293","4.86","-21.75","46845","GTGGAGAACACCAGGACGCGCACGACCAGCAGGGTTTTTGTGGCCCGCCTCATCGGCACCTCCGTCTTCGATCCCTTGGGCGATGAGGTGGGCAAGGTCCATGACGTCGTCGTCCTGCTGCAGATGCGCGGAGAACCCAGAGCCGTCGGCTTCGTCATCGAGGTCTCCAGCCGGCGCCGCGTCTTCCTGCCCCTGTCGAGGATCACCGCCATCGAGCCCGGAGCCGTCATCACCACGGGCCTGATGAACATCCGCCGCTTCACCCAGCGCCACGTGGAGACCCTGGTCGTCGGCGAGCTGCTAGACCGGGTGGTCACCATGCGCGACGGCTCGGGCAACGTCACGGTGCGCGACGTGGCCATCGAGCGCGACCGCGGCATGGACTGGAAGGTGACCCGCCTGTTCGTCCAGCGGGCCTCCTCAGGCCCTCTGGGCCTGCGCCGCGGGGAGACCTTCACGGTGCGCCCCGACGAGGTCAGCGGCCTGGCCGCCAGCGCCGACCAGCAGGGTGCCACCGCACTACTGGCCACTCTGGAGGACCTCAAGCCCGCCGACCTGGCCGACGTCATGCGCGACCTGCCCCAGGACAGCCAGATGCGCGTGGCCGCAGAGCTGACCGATGAGCGCCTGGCCGACGTCCTGGAGGAGCTCGGCAACGAGGACGCCGTCGCCCTCCTGTCCCGCCTGGAGGCCGGGCGCGCCGCCCACGTCCTGGACGCCATGCAGCCCGATGACGCCGCCGACCTGGTCGCCGATCTGCCCCAGCTCAAGGCCACCGAGCTGCTGGGCCTCATGGAGCCCGAGGAGGCCGAGGACGTGCGCCGCCTCATGGCCTACGACGACTACACCGCCGGCGGCCTGATGACCACCGAGCCGATCATCCTGCCCCCCGAGTCGACGGTGGCGACCTTCCTGGCCCAGTCCCGCAAGGCCGAGGTCCCTCCCGCCCTGGCCGCCATCGGCTTCGTGTGCCGCCCGCCCCTGGAGTCCCCCACCGGCAAGTTCGTGGGCATGATCCACTTCCAGAGGGCCCTGCGCGAGCGCCCCCAGCGCATGGTCGGCTCCATCGTGGACACCGACGTCGACTCCGTGCGCCCCGAGGACTCCATCGGTACCGTCACCCGCCTGCTGGCCACCTACAACCTGACGGCCCTGCCGGTCCTCGACGACGCCGGACGCCTGCTGGGCGCCGTCAGTGTCGACGACGTCCTGGACCACCTCATGCCCGACGACTGGCGCGTGGCCGACGAGGCCGTCACCGACGAGACGATCGAGAGGGGCGCCAATGCCTGA","VENTRTRTTSRVFVARLIGTSVFDPLGDEVGKVHDVVVLLQMRGEPRAVGFVIEVSSRRRVFLPLSRITAIEPGAVITTGLMNIRRFTQRHVETLVVGELLDRVVTMRDGSGNVTVRDVAIERDRGMDWKVTRLFVQRASSGPLGLRRGETFTVRPDEVSGLAASADQQGATALLATLEDLKPADLADVMRDLPQDSQMRVAAELTDERLADVLEELGNEDAVALLSRLEAGRAAHVLDAMQPDDAADLVADLPQLKATELLGLMEPEEAEDVRRLMAYDDYTAGGLMTTEPIILPPESTVATFLAQSRKAEVPPALAAIGFVCRPPLESPTGKFVGMIHFQRALRERPQRMVGSIVDTDVDSVRPEDSIGTVTRLLATYNLTALPVLDDAGRLLGAVSVDDVLDHLMPDDWRVADEAVTDETIERGANA$","Mg/Co/Ni transporter MgtE","Cytoplasm, Extracellular","Mg/Co/Ni transporter MgtE (contains CBS domain)","MgtE intracellular region","MgtE intracellular region","","Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 2004. 113(2):274-284. PMID: 14722619Carr G., Simmons N., Sayer J. A role for CBS domain 2 in trafficking of chloride channel CLC-5. Biochem. Biophys. Res. Commun. 2003. 310(2):600-605. PMID: 14521953Hebeisen S., Biela A., Giese B., Muller-Newen G., Hidalgo P., Fahlke C. The role of the carboxyl terminus in ClC chloride channel function. J. Biol. Chem. 2004. 279(13):13140-13147. PMID: 14718533","","","

InterPro
IPR000644
Domain

Cystathionine-beta-synthase
PF00571	$\"[286-408]T$	CBS
SM00116	$\"[360-408]T$	CBS

InterPro
IPR006668
Domain

MgtE intracellular region
PF03448	$\"[156-284]T$	MgtE_N

noIPR
unintegrated

unintegrated
PTHR11911	$\"[342-404]T$	INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED
PTHR11911:SF5	$\"[342-404]T$	INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED

","BeTs to 13 clades of COG2239COG name: Mg/Co/Ni transporter MgtE (contains CBS domain)Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2239 is --m-----v-r-bc-fg-sn-jxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 8-210 are similar to a (TRANSPORTER CBS MG2 CONTAINS DOMAIN MGTE MAGNESIUM DOMAINS INTRACELLULAR SCO5154) protein domain (PD206942) which is seen in Q6AFP3_BBBBB.Residues 187-287 are 55% similar to a (TRANSPORTER MAGNESIUM MG2 MGTE CATION CBS MG TRANSMEMBRANE DOMAIN DIVALENT) protein domain (PD303837) which is seen in Q9FBK4_STRCO.Residues 288-361 are 77% similar to a (TRANSPORTER CBS MG2 CONTAINS MGTE MAGNESIUM DOMAIN DOMAINS MB1264C INTRACELLULAR) protein domain (PD708221) which is seen in Q82IM3_STRAW.Residues 368-415 are 75% similar to a (TRANSPORTER CONTAINS MGTE CBS MG2 MAGNESIUM DOMAIN MB1264C INTRACELLULAR SCO5154) protein domain (PDA045X7) which is seen in Q8FQD5_COREF.","","-45% similar to PDB:2OUX Crystal structure of the soluble part of a magnesium transporter (E_value = 4.6E_14);","Residues 156 to 284 (E_value = 5.4e-28) place ANA_0232 in the MgtE_N family which is described as MgtE intracellular domain.Residues 286 to 408 (E_value = 5.2e-14) place ANA_0232 in the CBS family which is described as CBS domain pair.","","transporter MgtE (contains CBS domain)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0233","243381","244229","849","8.20","1.42","29642","ATGGGTCCGTACCGCGTGCCCGCGCGTGCGACGATAGCCCCCATGAACGCCAATCCGAGCTCGTTGTCCTCCCTGACCTCGTCCAGTGGTGGTGTCATGCCCCAGGGGGAGGAGGTGGCCTCCTTCGCGACCTACCCCGAGGCGCAGGGAGCAGTGGACGCCCTGTCGGATCAGGGCTTCCCGGTGCAGCACCTGGCGATTATCGGCACCGACCTGCGTCAGGTCGAGCGCATCACTGGACGCATGAGCTGGGGACGTGCAGCGATGTCGGGAGCCATGAACGGCCTGTGGATCGGGGTGTTCTTCGGCATCATCATGTCGGTGGCCGGTAGCAGCGGCCCCAGGCTCAACTTCTGGGCCTGCGTCCTGCTGGGGGTGCTGTGGGGCATCGTCTTCCAGCTCTTCAGCTACGCACTGACCCGGGGGCGGCGTGACTTCACCTCCATCAGCCAGGTTGTGGCCTCGCGCTACTCCATCATCGCCGCCCGGGAGATTCGCGAGGCCAGCCAGGCTCTGGCCGATGTCCCGGGCAACCTTGCGCGCGGGGGAGGAGCGCTGCGGCGCTCCCAGGAGCGGCGTCGGGCGAGGGAGGAGGCCCCTGGGCCCACAGCCTTCGGATCGCGCCCCGATGAGCAGCCCCGCTTCGGGGTGCGTCTGCCGCAGCCCGGCAGCGACGCTCCTGAGCGGACCTCCACCGCAGCGGCCGGCCCTGCCTCCGGCGCCCCGGCCGCTGCCGAGGACTACGACCCCTTCCTGCGTCCCTCGCGATCAGAGGATCACAAGGAGTCGGGGGCCTCGGCGTCGTCGCAGGAGCCCGGCGATGAGACTGGCTCCGGTAGCCGGGGTTGA","MGPYRVPARATIAPMNANPSSLSSLTSSSGGVMPQGEEVASFATYPEAQGAVDALSDQGFPVQHLAIIGTDLRQVERITGRMSWGRAAMSGAMNGLWIGVFFGIIMSVAGSSGPRLNFWACVLLGVLWGIVFQLFSYALTRGRRDFTSISQVVASRYSIIAAREIREASQALADVPGNLARGGGALRRSQERRRAREEAPGPTAFGSRPDEQPRFGVRLPQPGSDAPERTSTAAAGPASGAPAAAEDYDPFLRPSRSEDHKESGASASSQEPGDETGSGSRG$","Hypothetical membrane protein","Membrane, Extracellular","Hypothetical membrane protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[91-109]?$ $\"[115-135]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 34-172 are similar to a (TRANSMEMBRANE MEMBRANE PROBABLE) protein domain (PD603173) which is seen in Q6AFP2_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0234","244259","245107","849","6.64","-2.73","30489","ATGAGCATTCCGGTGGGGCTGTCGACAGCCTGCGTGGTTCCCGGCAGTGTTCCAGAGACCTTCGCCATCGCCCAGGAGCTGGGCTACGACGGCGTCGAGATCATGGTCTGGAGTGAGAAGGCATCCCAGGATGCCATCCGGTTGGCGGCTCTGGTGGAGAAGCATGATCAGCCGGTACTGGCGGTCCACGCTCCCACGCTGCTGGTGACCCGCGGGGTTTTCGGTGCCGATCCGTGGGACAAGGTGGATCGCTCCATCGAGCTGGCCCACTACCTCGAGGCGCCCACGGTGGTGCTGCACCCGCCCTTCTTCTGGCAGACCCGTTACGCGCGCTCCTTCATCGCCGGGGTCGCGCAGCGCGAGGCGACCACGGGCATCCACCTGGCGGTGGAGAACATGTTCACCTGGCGGCCCCGCCACGCCCACTCCACGCGAGACTTCCAGGCATACTCGCCCACCTGGGACCCGGTGGGGCAGGGCTACAAGTCGGTGACGCTGGACATCTCCCACGCCGCCACCTCCGGCTCCGACGCCCTGGCCATGGCCCGTGCGCTGGGGCCCACGCTGCGCCACCTGCACCTGACTGACGGTGTGCCCGGGCCCTTGGATGACCACCTGCTGCCCGGGCAGGGCAACCAGGACTGCGCAGGGGTTCTCAAGCACCTGGTGGCCACCGGTTTCGAGGCCGGTGGGGGACAGGTCGTCGTCGAGGTGACCACCCGGTCCATGACGGCCTCCCAGCGTCTCGAGGGCCTCGCCAGCGCGCTGGCCTTCGCCCGTGAGCACCTGGAGGGTGGGGAGCCGGCTCACATTCCCGAGCCGACCCGCAAACGCTACCGCCGTTCCTGA","MSIPVGLSTACVVPGSVPETFAIAQELGYDGVEIMVWSEKASQDAIRLAALVEKHDQPVLAVHAPTLLVTRGVFGADPWDKVDRSIELAHYLEAPTVVLHPPFFWQTRYARSFIAGVAQREATTGIHLAVENMFTWRPRHAHSTRDFQAYSPTWDPVGQGYKSVTLDISHAATSGSDALAMARALGPTLRHLHLTDGVPGPLDDHLLPGQGNQDCAGVLKHLVATGFEAGGGQVVVEVTTRSMTASQRLEGLASALAFAREHLEGGEPAHIPEPTRKRYRRS$","Sugar phosphate isomerase/epimerase","Cytoplasm","AP endonuclease, family 2 family","hypothetical protein","Xylose isomerase domain protein TIM barrel","","Fry J., Wood M., Poole P.S. Investigation of myo-inositol catabolism in Rhizobium leguminosarum bv. viciae and its effect on nodulation competitiveness. Mol. Plant Microbe Interact. 2001. 14(8):1016-1025. PMID: 11497462","","","

InterPro
IPR012307
Domain

Xylose isomerase-like TIM barrel
PF01261	$\"[21-213]T$	AP_endonuc_2

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.150	$\"[8-269]T$	no description

","BeTs to 6 clades of COG1082COG name: Sugar phosphate isomerases/epimerasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1082 is a-m-k---v-r-bcef-----j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 1-117 are 65% similar to a (ENDONUCLEASE PRECURSOR SIGNAL RV0498/MT0518/MB0509 AP FAMILY SCO3347 ML2432) protein domain (PD116509) which is seen in Q82EA1_STRAW.Residues 5-260 are 40% similar to a () protein domain (PDA083L4) which is seen in Q74FT9_GEOSL.Residues 118-263 are 59% similar to a (ENDONUCLEASE PRECURSOR SIGNAL RV0498/MT0518/MB0509 AP FAMILY ML2432) protein domain (PD669951) which is seen in Y498_MYCTU.Residues 161-227 are 65% similar to a (ENDONUCLEASE FRLC AP FAMILY ENDONUCLEASE Y4FM BLL4545 PHOSPHATE AF1279 PREDICTED) protein domain (PD113359) which is seen in YX47_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 21 to 213 (E_value = 3.4e-19) place ANA_0234 in the AP_endonuc_2 family which is described as Xylose isomerase-like TIM barrel.","","endonuclease, family 2 family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0235","246100","245114","987","6.68","-4.14","34553","GTGAGCACCCCAGCCGGCCACGAGCCCGACACCCATTCCCACCACCACTCCCACCATCAGTCCCACGGCCACTCGCACAACCACGGCGCCGGGGCCTCACGAGGTCGTCTCCTGGTCGCCCTGTGCCTGTCGACCACGGTCCTGGTGGCCGAGATCGTCAGCGCCCTTGTCACCGGATCGCTGGCGCTGCTGGCCGACGCCGGGCACATGCTCACCGACGTCGCCGGCCTGGCCATGGCCCTGACGGCCGCCCAGCTGTCCACGCGTCCGGCCACGGACCGCTCCACCTGGGGCATGCGTCGCGCTGAGGTCATCGGGGCCGCGCTCCAGGCGGGCATGCTCGCCGTCGTCGGGCTCTTCGTGGCCTTCAAGGCGGTTCACAACCTGCTGGTAGCCCCGCAGGTCGAGGCCTCGGGCATGCTCGTCATGGGTGTCATCGGCCTGGCCGCCAACGTCATCGCGCTGCTGGTCCTCTCTGGCGGCCGGGGGCATGACGGACACGGCGAGAACCTCAACATGAGGGCCGCCCTGCTGGAGGTCCTCAATGACGCCCTGGGATCAGTGGGCGTCATCATCGCTGCCGCCGTCGTGGCCCGCACCGGCTGGACGCGGGCCGACGCCGTGGCCTCCCTGCTCATCGCCGTCCTCATCCTGCCCCGGGCGGTGACGCTGCTGCGCTCGGCCCTGGCGGTGCTCATGGACTTCACTCCCCGGGAGCTGGACCTGGCGCAGGTGCGCTCGCACATGCTCGGCATCGACCACGTCGAGGAGGTCCACGACCTGCATGCCTGGACCGTCGCCTCGGGCATGCCGGTACTGACCGCGCACGTCGTCGTGCGCAACGAGTGCCTGCGCGACGGTCACACCGAGGAGATCCTCGACCGGCTCCAGAACTGCGTGGCCGAGCACTTCCCGGTCAGGATCCAGCACGCGACCCTCCAGCTCGAGCCCGTCTCGCACCTCGAGCACGAGGCCGCCTACTGCTAG","VSTPAGHEPDTHSHHHSHHQSHGHSHNHGAGASRGRLLVALCLSTTVLVAEIVSALVTGSLALLADAGHMLTDVAGLAMALTAAQLSTRPATDRSTWGMRRAEVIGAALQAGMLAVVGLFVAFKAVHNLLVAPQVEASGMLVMGVIGLAANVIALLVLSGGRGHDGHGENLNMRAALLEVLNDALGSVGVIIAAAVVARTGWTRADAVASLLIAVLILPRAVTLLRSALAVLMDFTPRELDLAQVRSHMLGIDHVEEVHDLHAWTVASGMPVLTAHVVVRNECLRDGHTEEILDRLQNCVAEHFPVRIQHATLQLEPVSHLEHEAAYC$","Cation efflux protein","Membrane, Cytoplasm","cation efflux system protein","K03295 cation efflux system protein; CDF family","cation diffusion facilitator family transporter","","Xiong A., Jayaswal R.K. Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus. J. Bacteriol. 1998. 180(16):4024-4029. PMID: 9696746Kunito T., Kusano T., Oyaizu H., Senoo K., Kanazawa S., Matsumoto S. Cloning and sequence analysis of czc genes in Alcaligenes sp. strain CT14. Biosci. Biotechnol. Biochem. 1996. 60(4):699-704. PMID: 8829543Conklin D.S., Mcmaster J.A., Culbertson M.R., Kung C. COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae. Mol. Cell. Biol. 1992. 12(9):3678-3688. PMID: 1508175","","","

InterPro
IPR002524
Family

Cation efflux protein
PTHR11562	$\"[14-328]T$	CATION EFFLUX PROTEIN/ ZINC TRANSPORTER
PF01545	$\"[37-322]T$	Cation_efflux
TIGR01297	$\"[33-320]T$	CDF: cation diffusion facilitator family tr

noIPR
unintegrated

unintegrated
tmhmm	$\"[37-55]?$ $\"[61-83]?$ $\"[104-123]?$ $\"[137-159]?$ $\"[180-202]?$ $\"[208-228]?$	transmembrane_regions

","BeTs to 10 clades of COG1230COG name: Co/Zn/Cd efflux system componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1230 is ----k-yqvdrlb-ef-hsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002524 (Cation efflux protein) with a combined E-value of 1.5e-38. IPB002524A 47-87 IPB002524B 89-128 IPB002524C 179-192 IPB002524D 255-266 IPB002524C 202-215","Residues 36-98 are similar to a (CATION EFFLUX TRANSPORTER SYSTEM ZINC FAMILY TRANSMEMBRANE RESISTANCE COBALT-ZINC-CADMIUM METAL) protein domain (PD001602) which is seen in ZITB_SALTY.Residues 219-265 are 78% similar to a (ZINC EFFLUX TRANSPORTER CATION SYSTEM TRANSMEMBRANE RESISTANCE FAMILY CZCD COBALT-ZINC-CADMIUM) protein domain (PD095382) which is seen in Q9X7Q7_STRCO.Residues 266-326 are similar to a (EFFLUX COBALT-ZINC-CADMIUM PLASMID RESISTANCE PROBABLE PERMEASE CATION CATION-EFFLUX) protein domain (PDA110S0) which is seen in Q70K49_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 37 to 322 (E_value = 1.4e-76) place ANA_0235 in the Cation_efflux family which is described as Cation efflux family.","","efflux system protein (efflux)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0236","246468","246097","372","6.61","-1.89","13023","ATGACGATGAAACATGGGCTGCTGCCCGAGGACCGCCCCCAGGACCACGGTGCTGTGCGCGAGGCCTCCACCGTGGCCTCCCTGCTCGATGTCCTGGGGGACGCCACCCGCCTGGCGATCCTGCGCCACCTCCACGGCGGCGAGCACCGGGTGGTGGAGCTGACCGAGCACCTGGGCCTGGCCCAGTCGACCGTCTCCCAGCACCTGGCGATCCTGCGCAGCGCCGGTCTCATCTCCAGCCACTCCCACGGACGGGCCAACGTCAGCCGGATCGAGAACCCCGAGGCCATCGAGCAGGTCCTGGCCGCTGCCGAGTCCTTGGCCGCCGTCATCTCCGCGGACGGAGTGAGCCGGGGCAAGGAGCCGCAGTGA","MTMKHGLLPEDRPQDHGAVREASTVASLLDVLGDATRLAILRHLHGGEHRVVELTEHLGLAQSTVSQHLAILRSAGLISSHSHGRANVSRIENPEAIEQVLAAAESLAAVISADGVSRGKEPQ$","Transcriptional regulator, ArsR family","Cytoplasm","transcriptional regulator, ArsR family","putative transcription regulator","regulatory protein, ArsR","","Morby A.P., Turner J.S., Huckle J.W., Robinson N.J. SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 1993. 21(4):921-925. PMID: 8451191Bairoch A. A possible mechanism for metal-ion induced DNA-protein dissociation in a family of prokaryotic transcriptional regulators. Nucleic Acids Res. 1993. 21(10):2515-2515. PMID: 8506147Eicken C., Pennella M.A., Chen X., Koshlap K.M., VanZile M.L., Sacchettini J.C., Giedroc D.P. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins. J. Mol. Biol. 2003. 333(4):683-695. PMID: 14568530Cook W.J., Kar S.R., Taylor K.B., Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J. Mol. Biol. 1998. 275(2):337-346. PMID: 9466913Busenlehner L.S., Pennella M.A., Giedroc D.P. The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 2003. 27(2):131-143. PMID: 12829264Liu T., Nakashima S., Hirose K., Shibasaka M., Katsuhara M., Ezaki B., Giedroc D.P., Kasamo K. A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPx-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II). J. Biol. Chem. 2004. 279(17):17810-17818. PMID: 14960585","","","

InterPro
IPR001845
Domain

Bacterial regulatory protein, ArsR
PR00778	$\"[29-44]T$ $\"[61-76]T$ $\"[76-91]T$	HTHARSR
PF01022	$\"[34-80]T$	HTH_5
SM00418	$\"[27-106]T$	HTH_ARSR
PS50987	$\"[17-111]T$	HTH_ARSR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[10-100]T$	no description

","BeTs to 13 clades of COG0640COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0640 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB001845 (Bacterial regulatory protein, ArsR family) with a combined E-value of 2.8e-16. IPB001845 47-91","Residues 25-86 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL ARSR FAMILY REGULATOR REGULATOR REPRESSOR RESISTANCE) protein domain (PD001992) which is seen in Q6A8D7_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 34 to 80 (E_value = 8.8e-15) place ANA_0236 in the HTH_5 family which is described as Bacterial regulatory protein, arsR family.","","regulator, ArsR family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0237","248158","246533","1626","4.88","-31.91","58537","ATGGCATCGACTTCTCCCGCAGACAACCGCCCGTCCGACGAGACCCCCGACTCCTCGCAGGAAGCTCCCCAGTCCTTGGCGGCGCGAGGCTCCAACCGGTCCCGCCAGCCCGAGAACCAGGCCTTCCGTGACTTCATCGGCTCGGGGTGGGGGCCGCGTCCCGAAGGCCTGCCCACCCGCAGCGAGGCGGCTCCCTGGGCGGCCGCCCGCCGTGAGGCCCTCGGCAGGCTCTTCCCCGGCGAGCGTCTGGTGCTCCCCGCCGGCGCGCTCAAGGTGCGCAACAACGACTGCGACTACCGGTTCAGGCCCCACAGCGCCTTCGCCCACCTGGCCGGAACCGGCACGGACTTCGAGCCGGATGCCGTGCTCGTCCTGGACCCCCTCACCGAGCCGAGTCAGGACGCCGGTTCCCCGGACGGCTCCGATGACACCGACGACGTCGCCCCGACGCATGAGGCAGTCCTCTACTTCCGGCCCCGGGCCTCGCGATCCAGCCAGGAGTTCTACGGTGACCCCCGCTACGGCGAGCTGTGGGTGGGGGTGCGGCCCTCCCTGGAGGAGGTCGAGGCCTCCACCGGCATGCGCTGCGCCCACATCGACTCCCTGCCCGACGCGCTGGCCAAGGATGCCGGTCCCGACGCGGTGCAGCTGCGCGTCGTCGCCGAGGCCGATGAGTCCGTCACCGCTCTGGTGACCACCACGCGGGAGAAGGTCGGGCTGCAGACCGGCCAGGGCGCCGCGGAGGTGGACGCCGGTCTGGCCGAGGCCGCCAGCGAGCTGCGCCTGGTCAAGGACCCCTGGGAGATCGACCAGCTGCGTGCCGCCGTCGCCGCCACCAAGGCCGGCTTCGACGACCTCATCCGCTCCATCCCCCGGGCCCGCGGCCACTGGCGCGGTGAGCGGGTCCTGGAGGGGGCCTTCGGGGCCAAGGCCCGCGAGGAGGGCAACGGCCTGGGCTATGACACGATCGCCGCGGCCGGCAACCACGCCAACACCCTGCACTGGATCAACAACGACGGCGCCGTCGAGCCCGGCCAGCTGGTCCTGGTGGACGCCGGCGTCGAGGTCGACTCCCTCTACACCGCTGACGTCACTCGCACGATCCCGGTCGATGGTCGCTTCACCGAGGCTCAGCGCCGGATCTACCAGGCGGTTCTCGACGCCGCCGACGCCGCCTTCGCCCGTGCGGGCACCCCGGGCTGCCGCTTCAAGGACGTCCACGCCGCCGCCATGGAGGTGATCGCCGCCCGCCTCGAGGAGTGGGGGATGCTGCCCGAGGGCGTCAGCGCAGCCGACTCCCTGGCCCCCGAAGGCCAGTACCACCGGCGCTGGATGGTGCACGGCACCAGCCACCATCTGGGCCTGGATGTCCACGACTGCGCCCAGGCGCGCCGCGAGATGTACATGGAGGCCGAGCTCAAGCCGGGCATGTGCTTCACCATCGAACCGGGACTGTACTTCCGCGAGGACGACCTGCTGGTGCCCGCCGAGATGCGCGGCACGGGCGTGCGCATCGAGGACGACGTCGTGGTGCGCGAGGACGGCAGCGTGGAGCGCCTCACTCAGGACGTGCCCCGCACTGTGGAGGAGGTCGAGGCCTGGGTGAGCGGGCTCATCGCCAACTGA","MASTSPADNRPSDETPDSSQEAPQSLAARGSNRSRQPENQAFRDFIGSGWGPRPEGLPTRSEAAPWAAARREALGRLFPGERLVLPAGALKVRNNDCDYRFRPHSAFAHLAGTGTDFEPDAVLVLDPLTEPSQDAGSPDGSDDTDDVAPTHEAVLYFRPRASRSSQEFYGDPRYGELWVGVRPSLEEVEASTGMRCAHIDSLPDALAKDAGPDAVQLRVVAEADESVTALVTTTREKVGLQTGQGAAEVDAGLAEAASELRLVKDPWEIDQLRAAVAATKAGFDDLIRSIPRARGHWRGERVLEGAFGAKAREEGNGLGYDTIAAAGNHANTLHWINNDGAVEPGQLVLVDAGVEVDSLYTADVTRTIPVDGRFTEAQRRIYQAVLDAADAAFARAGTPGCRFKDVHAAAMEVIAARLEEWGMLPEGVSAADSLAPEGQYHRRWMVHGTSHHLGLDVHDCAQARREMYMEAELKPGMCFTIEPGLYFREDDLLVPAEMRGTGVRIEDDVVVREDGSVERLTQDVPRTVEEVEAWVSGLIAN$","Xaa-Pro aminopeptidase","Cytoplasm, Extracellular","Xaa-Pro aminopeptidase I","Xaa-Pro aminopeptidase ","Xaa-Pro aminopeptidase","","Wilce M.C., Bond C.S., Dixon N.E., Freeman H.C., Guss J.M., Lilley P.E., Wilce J.A. Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(7):3472-3477. PMID: 9520390","","","

InterPro
IPR000994
Domain

Peptidase M24, catalytic core
G3DSA:3.90.230.10	$\"[262-541]T$	no description
PTHR10804	$\"[311-421]T$ $\"[444-538]T$	PROTEASE FAMILY M24 (METHIONYL AMINOPEPTIDASE, AMINOPEPTIDASE P)
PF00557	$\"[270-522]T$	Peptidase_M24

InterPro
IPR001131
Domain

Peptidase M24B, X-Pro dipeptidase, cataltyic core
PS00491	$\"[447-459]T$	PROLINE_PEPTIDASE

InterPro
IPR007865
Domain

Peptidase M24B, X-Pro dipeptidase/aminopeptidase N-terminal
PF05195	$\"[62-208]T$	AMP_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.350.10	$\"[59-261]T$	no description
PTHR10804:SF17	$\"[311-421]T$ $\"[444-538]T$	XAA-PRO DIPEPTIDASE PEPD/PEPQ(E.COLI)

","BeTs to 24 clades of COG0006COG name: Xaa-Pro aminopeptidaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0006 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB007865 (Aminopeptidase P, N-terminal) with a combined E-value of 2.4e-61. IPB007865A 257-287 IPB007865B 319-333 IPB007865C 348-386 IPB007865D 447-459 IPB007865E 473-487 IPB007865F 502-520***** IPB001714 (Methionine aminopeptidase-1 signature) with a combined E-value of 2.3e-06. IPB001714D 471-483","Residues 74-208 are 62% similar to a (AMINOPEPTIDASE HYDROLASE XAA-PRO P II DIPEPTIDASE X-PRO PROLINE MANGANESE I) protein domain (PD011173) which is seen in Q8G4M8_BIFLO.Residues 258-318 are 75% similar to a (AMINOPEPTIDASE I HYDROLASE XAA-PRO II P X-PRO METAL-BINDING MANGANESE PEPP) protein domain (PD646725) which is seen in Q6AFP1_BBBBB.Residues 319-379 are 86% similar to a (AMINOPEPTIDASE HYDROLASE COBALT METHIONINE PROTEASE DIPEPTIDASE XAA-PRO PEPTIDASE P PROLINE) protein domain (PD556587) which is seen in Q6AA10_PROAC.Residues 399-458 are 58% similar to a (AMINOPEPTIDASE HYDROLASE COBALT METHIONINE PROTEASE DIPEPTIDASE PEPTIDASE XAA-PRO MAP M) protein domain (PD289122) which is seen in AMP1_STRCO.Residues 420-476 are 82% similar to a (AMINOPEPTIDASE HYDROLASE DIPEPTIDASE XAA-PRO P PROLINE II X-PRO PROLIDASE MANGANESE) protein domain (PD580674) which is seen in Q6AFP1_BBBBB.","","-41% similar to PDB:1A16 AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU (E_value = 8.7E_29);-41% similar to PDB:1JAW AMINOPEPTIDASE P FROM E. COLI LOW PH FORM (E_value = 8.7E_29);-41% similar to PDB:1M35 Aminopeptidase P from Escherichia coli (E_value = 8.7E_29);-41% similar to PDB:1N51 Aminopeptidase P in complex with the inhibitor apstatin (E_value = 8.7E_29);-41% similar to PDB:1W2M CA-SUBSTITUTED FORM OF E. COLI AMINOPEPTIDASE P (E_value = 8.7E_29);","Residues 62 to 223 (E_value = 1.8e-14) place ANA_0237 in the AMP_N family which is described as Aminopeptidase P, N-terminal domain.Residues 270 to 522 (E_value = 7.4e-56) place ANA_0237 in the Peptidase_M24 family which is described as metallopeptidase family M24.","","aminopeptidase I (pepP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0238","249296","248226","1071","6.29","-7.06","37998","GTGTCCACCACGCGGCGCGCCGCCGACACCCCAATCCGCTTCGGGGTGATCGGCGCCGGTTTCATCGCCCGCTGGTTCGCCGAGGCAGTCGCCCGCGAGCCGGGTGCCCAGATCGTGGCCGTCACCTCCGCCCACCGCGAGCGCGCCGAAGCCTTCGCCACCGAGCACGGAGTTCCGCATGCCTATGCCTCGCTTAAGGAGATGCTCACCGCCCACGGCCCGGGCTCGCAGGACCCGATCGACGTCATCCATGTGGGCTCCCCCAACTCCCTGCACGCGCAGCACGCGATCGCGGCCCTGGAGGCCGGTTTTCACGTGGTAGTGGAGAAGCCCTTCGCCCTGACGCGCTCGCAGGCCGAGGCGATGGTGGAGGCGGCGCAGGCGGCCGACCGCTTTCTCATGGAGGGGTGGCTGTCCGCCTTCGAGCCCGGGGTGGCTCGGCTACGTGAGCACCTGCCGCGGCTGGGGCAGCTGCACCGGGTGGTGCTGTCCAAGGAGCAGTTCTCCTCGCGGATGGAGGTCTACCGCTCCGGTGGCCTACCGCCGGCCTTCAATCCGGCTCTGGGCGGCGGCTCCCTCATGGACCTGGGCATCTACCCGGTCAGCCTGGCCATTCACCTCTTCGGTGAGCCGGACCGGGTGACGGCTACGGGAACGTTGCTGGAGCATGGTGTGGACGCACGGGGCACGGTGGTCCTGTCCTACGACTGCGGTGAGCACGCCGGGCTAGAGGTCGTCTGCCTGCACTCCAAGACCTCCCCGGGAATGGAGTCGAGCTTCGCCGGGGACCATGACGTGCTGAGCATTGACGACTGCCAGTGGCCTCGGCGCATCGAGCTGCGCGGCCCGGCGGCAGCGACGGGCACGGGTGAGGACCTGTCGGTCGAGCGCGGCGCTGAGGCGCCCGGTCACCAGCTCGCCTACGAGCTGGCCGAGGTGTGCCGCCTGGTGCGTGCCGGCGCGCGCCAGTCCGATCTGCACCCGCTGAGCCGCTGTGTGGCGGCGGTCGGGGTTCTGCAGGAGGCACGCCGCCAGGTGGGGGTGCGCTTCCCGGCCGATGAGCAGGGCTGA","VSTTRRAADTPIRFGVIGAGFIARWFAEAVAREPGAQIVAVTSAHRERAEAFATEHGVPHAYASLKEMLTAHGPGSQDPIDVIHVGSPNSLHAQHAIAALEAGFHVVVEKPFALTRSQAEAMVEAAQAADRFLMEGWLSAFEPGVARLREHLPRLGQLHRVVLSKEQFSSRMEVYRSGGLPPAFNPALGGGSLMDLGIYPVSLAIHLFGEPDRVTATGTLLEHGVDARGTVVLSYDCGEHAGLEVVCLHSKTSPGMESSFAGDHDVLSIDDCQWPRRIELRGPAAATGTGEDLSVERGAEAPGHQLAYELAEVCRLVRAGARQSDLHPLSRCVAAVGVLQEARRQVGVRFPADEQG$","Oxidoreductase","Cytoplasm","ygjR protein","putative oxidoreductase","oxidoreductase domain protein","","","","","

InterPro
IPR000683
Domain

Oxidoreductase, N-terminal
PF01408	$\"[12-137]T$	GFO_IDH_MocA

InterPro
IPR004104
Domain

Oxidoreductase, C-terminal
PF02894	$\"[165-258]T$	GFO_IDH_MocA_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[2-170]T$	no description
PTHR22604	$\"[62-346]T$	OXIDOREDUCTASES
PTHR22604:SF15	$\"[62-346]T$	DIMERIC DIHYDRODIOL DEHYDROGENASE

","BeTs to 12 clades of COG0673COG name: Predicted dehydrogenases and related proteinsFunctional Class: RThe phylogenetic pattern of COG0673 is --tKYqVCEB--uj-------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 260-364 are 52% similar to a (PLASMID) protein domain (PD988803) which is seen in Q6W1L0_RHISN.Residues 401-508 are 61% similar to a (OXIDOREDUCTASE YGJR 1.-.-.- OXIDOREDUCTASE GFO/IDH/MOCA FAMILY YULF SPY0441 B.SUBTILIS SPYM3_0310) protein domain (PD407148) which is seen in Q6LQM3_PHOPR.Residues 426-492 are 61% similar to a (OXIDOREDUCTASE DEHYDROGENASE OXIDOREDUCTASE FAMILY PLASMID MYO-INOSITOL GFO/IDH/MOCA 1.-.-.- 2-DEHYDROGENASE PREDICTED) protein domain (PD127410) which is seen in Q82AY9_STRAW.","","-46% similar to PDB:2HO3 Crystal structure of Oxidoreductase, Gfo/Idh/MocA family from Streptococcus pneumoniae (E_value = 2.0E_21);-46% similar to PDB:2HO5 Crystal structure of Oxidoreductase, Gfo/Idh/MocA family from Streptococcus pneumoniae (E_value = 2.0E_21);-43% similar to PDB:1YDW X-RAY STRUCTURE OF GENE PRODUCT FROM ARABIDOPSIS THALIANA AT4G09670 (E_value = 3.0E_17);-48% similar to PDB:2GLX Crystal Structure Analysis of bacterial 1,5-AF Reductase (E_value = 1.8E_14);-51% similar to PDB:1H6A REDUCED PRECURSOR FORM OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS MOBILIS (E_value = 1.3E_12);","Residues 261 to 386 (E_value = 3.5e-37) place ANA_0238 in the GFO_IDH_MocA family which is described as Oxidoreductase family, NAD-binding Rossmann fold.Residues 267 to 384 (E_value = 0.00034) place ANA_0238 in the NAD_binding_3 family which is described as Homoserine dehydrogenase, NAD binding domain.Residues 414 to 507 (E_value = 0.021) place ANA_0238 in the GFO_IDH_MocA_C family which is described as Oxidoreductase family, C-terminal alpha/beta domain.","","protein ","","1","","","Wed Aug 1 14:48:55 2007","","Wed Aug 1 14:48:55 2007","","","Wed Aug 1 14:48:55 2007","Wed Aug 1 14:48:55 2007","Wed Aug 1 14:48:55 2007","","","","","","Wed Aug 1 14:48:14 2007","Wed Aug 1 14:48:14 2007","Wed Aug 1 14:48:14 2007","","Wed Aug 1 14:48:14 2007","Wed Aug 1 14:48:14 2007","","","","","yes","","" "ANA_0240","249384","250229","846","5.59","-10.21","30007","GTGCGTATCGACCCCCACACCCACTCGGCCTGCTCCGACGGCACCGACTCGCCCGCCGGGCTCATGGCTCAGGCGGCCGCGGCCGGCCTCGACGTCGTCGGCCTGACCGACCACGACACGATGGCCGGATGGCAGGAGGCGGCCCGGGCCGTCCCGGATACCGGCGTCGCCCTGCTGCGCGGCACCGAGATCTCCTGCGCCGCTGACGGGGTCACCCTCCATCTGCTGTCTTACCTGCACCGGGCCGATGATGCCGGGCTGGAGGCCGCCTTCGCCCGCGCCCGCCGCTCGCGCGACAGCCGGGCGCAGCAGATGGTCGAGCGCCTCAGCGAGGACTACCCGCTCACCTGGGAGGACGTCCTGTCCCAGTCGACCGACTCCCACACGATCGGCCGGCCCCATATCGCCGACGCCCTCGTAGCGGCCGGCTCCTTCCCCGATCGCAACGCCGCCTTCGCCGGGCCGCTGGCCACCTCCTCGCCCTACTATGTCCACCACTGGGCGCTGGACCCGGTGGAGGCCTGCCGCCTGGTGCGCGCCGCCGGTGGGGTCCCGGTGGCGGCCCACCCGCGCGCCGCCTCCCGCCAACGCCGCCTCGTGCCCGATGAGACCTTCGCCCAGATGGCCGAGGCCGGCCTGGCGGCCCTGGAGATGAACCATCGCGACCAGGGCCCCGAGCAGCGCGAGCAGGTTCGCCTCCTGGCTCAGCGCCTGGGGCTGGGGCTGTCGGGGGCCTCGGACTACCACGGCACCGGGAAGCCCAACCGCCTGGGGGAGAACCTCATGCCGCCCGAGCTGCTGGAACAGATCCTCGACGAGGGCGCCCTCGACCTCGTCCGACCCTGA","VRIDPHTHSACSDGTDSPAGLMAQAAAAGLDVVGLTDHDTMAGWQEAARAVPDTGVALLRGTEISCAADGVTLHLLSYLHRADDAGLEAAFARARRSRDSRAQQMVERLSEDYPLTWEDVLSQSTDSHTIGRPHIADALVAAGSFPDRNAAFAGPLATSSPYYVHHWALDPVEACRLVRAAGGVPVAAHPRAASRQRRLVPDETFAQMAEAGLAALEMNHRDQGPEQREQVRLLAQRLGLGLSGASDYHGTGKPNRLGENLMPPELLEQILDEGALDLVRP$","Metal-dependent phosphoesterase (PHP family)","Cytoplasm","PHP domain protein","hypothetical protein","PHP C-terminal domain protein","","","","","

InterPro
IPR003141
Domain

Polymerase and histidinol phosphatase, N-terminal
SM00481	$\"[3-68]T$	POLIIIAc

InterPro
IPR004013
Domain

PHP, C-terminal
PF02811	$\"[3-252]T$	PHP

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.140	$\"[1-83]T$	no description

","BeTs to 11 clades of COG0613COG name: Predicted metal-dependent phosphoesterases (PHP family)Functional Class: RThe phylogenetic pattern of COG0613 is aMt--qVce--h---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 168-256 are 67% similar to a (TRPH PHP DOMAIN PHOSPHOESTERASE METAL-DEPENDENT PREDICTED FAMILY ENZYMES ENZYME PHOSPHOESTERASES) protein domain (PD696630) which is seen in Q8G7Z5_BIFLO.Residues 279-363 are 64% similar to a (PHP TRPH PHOSPHOESTERASE METAL-DEPENDENT DOMAIN FAMILY PREDICTED ENZYMES ENZYME PHOSPHOESTERASES) protein domain (PD022188) which is seen in Q6AFP0_BBBBB.","","-50% similar to PDB:1EQQ SINGLE STRANDED DNA BINDING PROTEIN AND SSDNA COMPLEX (E_value = );-52% similar to PDB:1QVC CRYSTAL STRUCTURE ANALYSIS OF SINGLE STRANDED DNA BINDING PROTEIN (SSB) FROM E.COLI (E_value = );-41% similar to PDB:1YEY Crystal Structure of L-fuconate Dehydratase from Xanthomonas campestris pv. campestris str. ATCC 33913 (E_value = );-41% similar to PDB:2HNE Crystal structure of l-fuconate dehydratase from xanthomonas campestris pv. campestris str. ATCC 33913 (E_value = );-41% similar to PDB:2HXT Crystal structure of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and D-erythronohydroxamate (E_value = );","Residues 116 to 365 (E_value = 1.2e-18) place ANA_0240 in the PHP family which is described as PHP domain.","","domain protein","","1","","","Wed Aug 1 14:43:21 2007","","Wed Aug 1 14:43:21 2007","","","Wed Aug 1 14:43:21 2007","Wed Aug 1 14:43:21 2007","Wed Aug 1 14:43:21 2007","","","Wed Aug 1 14:43:21 2007","","","Wed Aug 1 14:43:21 2007","","Wed Aug 1 14:43:21 2007","","Wed Aug 1 14:43:21 2007","Wed Aug 1 14:43:21 2007","","","","","yes","","" "ANA_0241","250286","250915","630","6.04","-0.82","21624","ATGCTGCAGTCCGTCTTCGACACCACGGTCTTCGCCACGACCTTCACAACGCTCCTGGTCATTCAGGACCCCCTGGGCGCCATCCCGATCTTCCTGTCCCTGACCTCGCGGCAGACGCCCCCGGAGCGCGCCGCCTCCGCGCGCCAGGCCACAGTGGTCTCCTTCGCCGTCATCGTGCTCTTCGCGGCCTTCGGACGCTACATCCTGAAGTTCCTGGGGATCTCGGTACCCTCCCTCCAGGTGGCCGGCGGACTGCTGCTGCTCCTGGTGGCCCTGGAGCTGCTGACCGACAAGGTCGATGAGAGCCCCGACCCCGAGGCCGTCACTGCCAACGCCGCCCTCGTGCCCCTGGGCACGCCCCTGCTGGCCGGACCCGGCGCCATCGTCGCGGCGATGGTCGCCGTGGACACCACCGGAGGCGGGGTGGCCGGGTGGGTCTCCGTGACGGCCGCGATCATCGGCACGCACATCGCCATCTGGGCCTCGCTGCGCTTCTCCCTGGGGCTCAACCGGGTGCTGGGCACCTCCGGCATCCGGATCCTCACCCGGGTCATGGGACTGCTCCTGGCGGCCATCGCCGTCCAGATCATGGCCGACGGCGTCTTCGCCTTCCTGGAGACCCGCCTCTGA","MLQSVFDTTVFATTFTTLLVIQDPLGAIPIFLSLTSRQTPPERAASARQATVVSFAVIVLFAAFGRYILKFLGISVPSLQVAGGLLLLLVALELLTDKVDESPDPEAVTANAALVPLGTPLLAGPGAIVAAMVAVDTTGGGVAGWVSVTAAIIGTHIAIWASLRFSLGLNRVLGTSGIRILTRVMGLLLAAIAVQIMADGVFAFLETRL$","Multiple antibiotic resistance protein marC","Membrane, Cytoplasm","membrane protein, putative","K05595 multiple antibiotic resistance protein","multiple antibiotic resistance (MarC)-related protein","","","","","

InterPro
IPR002771
Family

Multiple antibiotic resistance (MarC)-related proteins
PF01914	$\"[8-205]T$	MarC
TIGR00427	$\"[2-201]T$	TIGR00427: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[44-66]?$ $\"[72-92]?$ $\"[113-135]?$ $\"[141-163]?$ $\"[184-204]?$	transmembrane_regions

","BeTs to 15 clades of COG2095COG name: Integral membrane proteins of the MarC familyFunctional Class: S [Function unknown]The phylogenetic pattern of COG2095 is a-mpkz-q-d--b-efghsnuj-it-Number of proteins in this genome belonging to this COG is 2","***** IPB002771 (Multiple antibiotic resistance (MarC)-related proteins) with a combined E-value of 3e-31. IPB002771A 76-96 IPB002771B 116-129 IPB002771C 169-201","Residues 21-75 are 67% similar to a (MEMBRANE TRANSMEMBRANE ANTIBIOTIC MULTIPLE MARC RESISTANCE UPF0056 TRANSPORTER PROTEIN FAMILY) protein domain (PD006289) which is seen in Q8A5G9_BACTN.Residues 111-201 are 70% similar to a (MEMBRANE TRANSMEMBRANE ANTIBIOTIC MULTIPLE MARC RESISTANCE UPF0056 PROTEIN FAMILY TRANSPORTER) protein domain (PD341950) which is seen in Q82IN1_STRAW.","","-62% similar to PDB:1QPN QUINOLINATE PHOSPHORIBOSYL TRANSFERASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH NCNN (E_value = );-62% similar to PDB:1QPO QUINOLINATE PHOSPHORIBOSYL TRANSFERASE (QAPRTASE) APO-ENZYME FROM MYCOBACTERIUM TUBERCULOSIS (E_value = );-62% similar to PDB:1QPQ Structure of Quinolinic Acid Phosphoribosyltransferase from Mycobacterium Tuberculosis: A Potential TB Drug Target (E_value = );-62% similar to PDB:1QPR QUINOLINATE PHOSPHORIBOSYLTRANSFERASE (QAPRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH PHTHALATE AND PRPCP (E_value = );","Residues 8 to 205 (E_value = 2e-53) place ANA_0241 in the MarC family which is described as MarC family integral membrane protein.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0242","252911","250983","1929","6.63","-4.20","69193","TTGCCGTGCGTGAAGCACAGCCGTGACATCGACCACGCCGACGGCGCACCTCCCCATCCAGACAGGCCATCATCATGTTTTCCCGCTACGCTGACGGCGTCCACGGTTGCCCGGTCGTCAGATGGACTCAGATATGACTCACGATCGGCTGCCACATCCGACGGCGCCAACGCCCACGCAGCGCACCCGACCGTGCGCGCGAGCGACAGCCGCGCCGGACCGGTTCAACCTGATCAGAAGACAAGGAACCTCGTGAGCAACGAGCACCACGGGGCCGACGCCGTCGAGCCCGACCACAACTCCACAGACGACCAGACCACCCTCGAGAGCGCCAACGCCGCTGCCGGCACCACTGGCGCTACGTCCGGGATCATCGAGACGGCCGGCGCCCACGCCCCCGTCCTGGATGAGGCCACTCCCGACATCACCGACGAGGGCGCCCAAACCGACCTGAGCCGCAAGACCTTCGCCGACTTCGGTGTCGAGCCGGAGATCTGCGAGGCCCTGGACGCCAAGGGCATCACCCACCCCTTCCCCATCCAGGCCCTCACCCTGCCGGTGGCCCTGGAGGGGCAGGACATCATCGGTCAGGCCAAGACCGGCACCGGCAAGACCCTGGGCTTCGGCATCCCCCTGCTCATGGACACCCTGGGCCCCGGGGAGGAGGGCTGGGACGAGGATCCCGCCTCCGGCAGCCCCCAGGCCCTGGTCATCCTGCCCACCCGCGAGCTGGCCAAGCAGGTCGCCGAGGAGCTGTCCACAGCTGCCGCCAAGCGCACCGTGCGCATCGTCCAGGTCTACGGCGGGCGCGCCTACGAGCCCCAGATCGAGGACCTCGAGCGAGGAGCCGAGGTCGTCGTGGGCACGCCCGGCCGCCTCATCGACCTCATGGAGCGTGGCGTGCTGGACCTGGCTCACGTCACCACTGTCGTCCTGGACGAGGCCGACGAGATGCTGGATCTGGGCTTCCTGCCGGACGTGGAGAAGATCCTGGCCCGCACCCGCGCCGACCGGCACACGATGCTCTTCAGCGCCACCATGCCCGGGGCCGTGGTCGCCCTGGCGCGCCGCTACATGACCCGCCCCACCCACATCCGCGCCCAGGACCCGGGCGACGAGGGCATGACCGTCCAGACGGTCCAGCAGGTCGTCTACCGCACCCACTCGATGAACAAGGTGGAGGTCGTCTCCCGGATCCTCCAGGCCGAGGGGCGCGGGCGCACCATCATCTTCGCACGCACCAAGCGCACGGCGGCCCGGGTGGCCGACGACCTGCGCGCCCGAGGTTTCGCCACCGGGGCCCTGCACGGCGACCTCGGCCAGGGGGCCCGCGAGCAGGCCCTGCGCGCCTTCCGCAACAACAAGGTGGACGTCCTGGTGGCCACCGACGTGGCCGCCCGGGGCATCGACGTCGACGACGTCACCCACGTCATCAACTACCAGTGCCCCGAGGACGAGAAGATCTACGTCCACCGCATCGGGCGCACCGGACGCGCCGGCAACTCCGGCACGGCGGTCACCTTCGTGGACTGGGACGACGTGCCGCGCTGGCGGATCATCGCCAAGGCTCTGGGCCTGCCCATCGAGGAGCCGGTGGAGACCTACCACACCAGCGAGCACCTGTTCTCCGACCTGTCGATCCCGGAGAAGGTCACCGGCCGCCTGCCCCGTCACAAGCGCACCCTGGAGGGGCTCGACGCCGAGGAGATCGAGGACCTGGGTGAGACCGGCAAGCGTGGGCGCAAGCAGTCCGGCCGGCAGGGCGGGCGCTCGGAGCGCGGCCGGGGCCGCGGCGGCAGGGGCGCCAAGGACTCCAAGCGCGGTGAGCGCTCCCGGCGCTCCGCCGACGGCGAGGCCAAGCCCCGGCGCAAGCGCACCCGTAAGCGCACGCGCGGTGGCCGCCCGGTTGACGGGACCACCGGCGAGTAG","LPCVKHSRDIDHADGAPPHPDRPSSCFPATLTASTVARSSDGLRYDSRSAATSDGANAHAAHPTVRASDSRAGPVQPDQKTRNLVSNEHHGADAVEPDHNSTDDQTTLESANAAAGTTGATSGIIETAGAHAPVLDEATPDITDEGAQTDLSRKTFADFGVEPEICEALDAKGITHPFPIQALTLPVALEGQDIIGQAKTGTGKTLGFGIPLLMDTLGPGEEGWDEDPASGSPQALVILPTRELAKQVAEELSTAAAKRTVRIVQVYGGRAYEPQIEDLERGAEVVVGTPGRLIDLMERGVLDLAHVTTVVLDEADEMLDLGFLPDVEKILARTRADRHTMLFSATMPGAVVALARRYMTRPTHIRAQDPGDEGMTVQTVQQVVYRTHSMNKVEVVSRILQAEGRGRTIIFARTKRTAARVADDLRARGFATGALHGDLGQGAREQALRAFRNNKVDVLVATDVAARGIDVDDVTHVINYQCPEDEKIYVHRIGRTGRAGNSGTAVTFVDWDDVPRWRIIAKALGLPIEEPVETYHTSEHLFSDLSIPEKVTGRLPRHKRTLEGLDAEEIEDLGETGKRGRKQSGRQGGRSERGRGRGGRGAKDSKRGERSRRSADGEAKPRRKRTRKRTRGGRPVDGTTGE$","ATP-dependent RNA helicase","Cytoplasm","Superfamily II DNA and RNA helicases","putative ATP-dependent RNA helicase","DEAD/DEAH box helicase domain protein","","Schmid S.R., Linder P. D-E-A-D protein family of putative RNA helicases. Mol. Microbiol. 1992. 6(3):283-292. PMID: 1552844Linder P., Lasko P.F., Ashburner M., Leroy P., Nielsen P.J., Nishi K., Schnier J., Slonimski P.P. Birth of the D-E-A-D box. Nature 1989. 337(6203):121-122. PMID: 2563148Wassarman D.A., Steitz J.A. RNA splicing. Alive with DEAD proteins. Nature 1991. 349(6309):463-464. PMID: 1825133","","","

InterPro
IPR000629
Domain

ATP-dependent helicase, DEAD-box
PS00039	$\"[311-319]T$	DEAD_ATP_HELICASE

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[283-516]T$	no description

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[424-500]T$	Helicase_C
SM00490	$\"[419-500]T$	HELICc
PS51194	$\"[394-540]T$	HELICASE_CTER

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[178-355]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[173-383]T$	DEXDc

InterPro
IPR014014
Domain

DEAD-box RNA helicase Q motif
PS51195	$\"[154-182]T$	Q_MOTIF

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[185-365]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[141-369]T$ $\"[375-545]T$	no description
PTHR10967	$\"[154-539]T$ $\"[555-616]T$	DEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF51	$\"[154-539]T$ $\"[555-616]T$	ATP-DEPENDENT RNA HELICASE

","BeTs to 20 clades of COG0513COG name: Superfamily II DNA and RNA helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: K [Information storage and processing--Transcription],JThe phylogenetic pattern of COG0513 is a-mp--yq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 4","***** IPB012562 (GUCT) with a combined E-value of 3e-89. IPB012562A 177-216 IPB012562B 230-248 IPB012562C 265-298 IPB012562D 311-331 IPB012562E 339-351 IPB012562G 444-498***** IPB000629 (ATP-dependent helicase, DEAD-box) with a combined E-value of 2.5e-80. IPB000629A 173-213 IPB000629B 236-248 IPB000629C 284-295 IPB000629D 307-330 IPB000629E 462-503***** IPB005580 (DbpA RNA binding domain) with a combined E-value of 1.1e-55. IPB005580A 212-250 IPB005580B 310-359 IPB005580C 469-521***** IPB012541 (DBP10CT) with a combined E-value of 2.6e-51. IPB012541A 177-217 IPB012541B 232-270 IPB012541C 291-345 IPB012541D 407-441 IPB012541E 470-524***** IPB005034 (Protein of unknown function DUF283) with a combined E-value of 1.8e-11. IPB005034C 285-319 IPB005034F 449-503***** IPB013701 (DEAD/H associated) with a combined E-value of 4.2e-09. IPB013701A 168-211 IPB013701G 405-425 IPB013701H 450-483***** IPB002121 (HRDC domain) with a combined E-value of 9.7e-06. IPB002121F 461-500","Residues 140-217 are 55% similar to a (HELICASE HYDROLASE ATP-BINDING DEAD DDX24 POLYPEPTIDE RNA ATP-DEPENDENT BOX DEAD-BOX) protein domain (PD355390) which is seen in Q6VEU8_RAT.Residues 158-199 are 80% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT BOX HELICASE DEAD DEAD-BOX FAMILY) protein domain (PD285395) which is seen in Q6A841_PROAC.Residues 200-290 are similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT FACTOR DNA BOX RNA-BINDING 3.6.1.-) protein domain (PD410733) which is seen in Q6A841_PROAC.Residues 291-340 are 80% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT BOX RNA-BINDING DEAD DEAD-BOX INITIATION) protein domain (PD000276) which is seen in Q6A841_PROAC.Residues 347-402 are 80% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT FACTOR INITIATION DEAD RNA-BINDING BOX) protein domain (PD186348) which is seen in Q82IN5_STRAW.Residues 407-471 are 90% similar to a (HELICASE ATP-BINDING HYDROLASE DNA ATP-DEPENDENT RNA EXCISION FACTOR B REPAIR) protein domain (PD000033) which is seen in Q8FRH5_COREF.Residues 474-509 are 91% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT BOX RNA-BINDING DEAD DEAD-BOX HELICASE) protein domain (PD035460) which is seen in Q7TX01_MYCBO.Residues 511-567 are 70% similar to a (HELICASE RNA ATP-DEPENDENT ATP-BINDING HYDROLASE RHLE PROBABLE DEAD HELICASES II) protein domain (PD348339) which is seen in Q9FBJ2_STRCO.","","-60% similar to PDB:1HV8 CRYSTAL STRUCTURE OF A DEAD BOX PROTEIN FROM THE HYPERTHERMOPHILE METHANOCOCCUS JANNASCHII (E_value = 2.1E_69);-55% similar to PDB:2I4I Crystal Structure of human DEAD-box RNA helicase DDX3X (E_value = 1.1E_62);-55% similar to PDB:2DB3 Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa (E_value = 1.8E_60);-66% similar to PDB:2GXQ HERA N-terminal domain in complex with AMP, crystal form 1 (E_value = 1.5E_51);-66% similar to PDB:2GXS HERA N-terminal domain in complex with AMP, crystal form 2 (E_value = 1.5E_51);","Residues 178 to 355 (E_value = 8.3e-63) place ANA_0242 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 424 to 500 (E_value = 3.1e-33) place ANA_0242 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","II DNA and RNA helicases","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0244","252855","253601","747","5.33","-7.64","27010","ATGGGGAGGTGCGCCGTCGGCGTGGTCGATGTCACGGCTGTGCTTCACGCACGGCAAGACCTGGATACGATGGTGGCCATGTCCCAGATGCCGACACCGTCACCTCAGCCCAACGCCTCCATCCCGATGCAGGTTGGTCCCCACGAGCTGTCCGTCGTCGGCGTCGTCGCGATCTCCCGGACGGCGGCCTGCACCCGCTACGCCAAGGATGCCGACCGGGCACCGCGGATGAGGGCTCGGGTCGACCTGCTGCGCATGAGTGCCTGGGAGGTCGCCTCCTTCGACCGGGTCGTGGAGCTGGCCGCGACCCACGGCATCGACGCCCTCGGGGCGGCCGAACGCTTCACCGACGTGCTGGGCGACTTCGACGAGCGACTGCGGCCACTGGACTGGGCCGAGCGCCTGCTCAAGACCTACATCACCTTCGGGCTGCTCATCGACTTCGGGATGGCGCTGAGCGAGTCCCTGGACGACCCCTTGCATAGCGGACTCATTCATGAGCTCAGCCAGGACCCGATCGGCACGTACGCCGTCGCCGAGCTGGAGGAGGTCGTCGCGGCCGACCCTCAGCTGGCCGCCCGACTGGGGCTGTGGGGCCGGCGCGTCATCGGTGAGGAGATCGGGACCTTCCAGAGGCTCCTGGGGCAGTTCCCCGAGCTTCTCGGCCAGATGGCGCAGGAGCAGCTCCACTCAGTACTGTCCCAGGGGGCGGTCTCGCGTATGAGAGGGCTGGGCCTGAGGGTCTGA","MGRCAVGVVDVTAVLHARQDLDTMVAMSQMPTPSPQPNASIPMQVGPHELSVVGVVAISRTAACTRYAKDADRAPRMRARVDLLRMSAWEVASFDRVVELAATHGIDALGAAERFTDVLGDFDERLRPLDWAERLLKTYITFGLLIDFGMALSESLDDPLHSGLIHELSQDPIGTYAVAELEEVVAADPQLAARLGLWGRRVIGEEIGTFQRLLGQFPELLGQMAQEQLHSVLSQGAVSRMRGLGLRV$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 32-246 are 48% similar to a (SCO5167 MB3236C) protein domain (PD116103) which is seen in Q73UQ5_MYCPA.","","-64% similar to PDB:1FNT CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST IN COMPLEX WITH THE PROTEASOME ACTIVATOR PA26 FROM TRYPANOSOME BRUCEI AT 3.2 ANGSTROMS RESOLUTION (E_value = );-64% similar to PDB:1G0U A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE (E_value = );-64% similar to PDB:1G65 CRYSTAL STRUCTURE OF EPOXOMICIN:20S PROTEASOME REVEALS A MOLECULAR BASIS FOR SELECTIVITY OF ALPHA,BETA-EPOXYKETONE PROTEASOME INHIBITORS (E_value = );-64% similar to PDB:1JD2 Crystal Structure of the yeast 20S Proteasome:TMC-95A complex: A non-covalent Proteasome Inhibitor (E_value = );-64% similar to PDB:1RYP CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS RESOLUTION (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0245","254422","253748","675","12.30","30.27","22546","GTGTCAGTAGGTCAGCCTACGGCGCGCCATGAGCATGGCGGCGCCTGTCGCACCAGTGCCCAGCACCATCCAGGCTGCGGTCGTCCCCGCACCGGTCTGGGCGAGGGTGGAGCGACCTGCGGTGGCGGTACCCTGCTGGCCGGAAGCAGCCTGCTCGCGGGGAGCGGCGGCCTGCTCACCGGGGACATTCGCGGCGCCCTGGGGAGCGCTCTCCTCGGCGGCCGCGGGGGCGCCTCCCTCAGAGGACTGCTCGGGGGCCGCCGGGGCCTGCTGCTCGGGAGCAGCCTCGGAGCCAGCGGAATCGCCCTGCTGCTGCTCAGCCTGGTTCTGCTGGGGCTGCTCGGCCGGAGCCTCCGGCTTGTTCTCCTGCTGCGCCGCGGCGTTGTCGGCGCCCGGAGCCTGGGGAGCGGTCTTGCCCGCATCCTCCGCGGGAGCAGGCGCAGGGGCGGGGGCCGGAGCCGGCTTGTTGCCTTCAGGGTTGGGGGCAGCCGGGGAGGGGGTGTCGGGCTGAGGAGCCTCGGCCTTCGCGTCACCGGCCTGGGACGCCGACTGCTCGGCGACAGGAGCCGGGTCCGTCTCAGCAGCAGCCGCACCGACCGGGACGACGGACAGGGCAACGGCCGCAGACGCAGCCATCCATACGCTTCGCTTCATGGGAACTCCTTGAGGACTTGA","VSVGQPTARHEHGGACRTSAQHHPGCGRPRTGLGEGGATCGGGTLLAGSSLLAGSGGLLTGDIRGALGSALLGGRGGASLRGLLGGRRGLLLGSSLGASGIALLLLSLVLLGLLGRSLRLVLLLRRGVVGARSLGSGLARILRGSRRRGGGRSRLVAFRVGGSRGGGVGLRSLGLRVTGLGRRLLGDRSRVRLSSSRTDRDDGQGNGRRRSHPYASLHGNSLRT$","Hypothetical protein","Extracellular, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[96-116]?$ $\"[122-142]?$	transmembrane_regions

InterPro
IPR000408
Repeat

Regulator of chromosome condensation, RCC1
PF00415	$\"[270-290]T$	RCC1
PS50012	$\"[271-322]T$	RCC1_3

noIPR
unintegrated

unintegrated
G3DSA:2.130.10.30	$\"[197-400]T$	no description
PTHR22870	$\"[243-383]T$	REGULATOR OF CHROMOSOME CONDENSATION
PTHR22870:SF20	$\"[243-383]T$	UVB-RESISTANCE PROTEIN-RELATED
tmhmm	$\"[159-179]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 270 to 290 (E_value = 1.8e-05) place ANA_0246 in the RCC1 family which is described as Regulator of chromosome condensation (RCC1).","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0247","256002","255742","261","8.69","2.14","9086","ATGCGCGCATGTATAGTCGAGCCATCCTCCACGTCTCCATTTCGTGGAGACTCACCACGGAAAGGAGCTCTCATGAGCGACAACGGAACCTTTGACAGGATCGCCGGCAAGACCAAGGAGGCCGCGGGCAAGGTCACTGGCAACAAGGAGACCGAGACCGAGGGCAAGCTCCAGCAGGCCGAAGGCAAGATCAAGGAGGTCGCCGAGGACGCCAAGGACGCCATCAAGGGTGCGGTGAACCACCTCAAGGGCGACAAGTAA","MRACIVEPSSTSPFRGDSPRKGALMSDNGTFDRIAGKTKEAAGKVTGNKETETEGKLQQAEGKIKEVAEDAKDAIKGAVNHLKGDK$","CsbD family protein","Periplasm, Extracellular","Ej97D protein-related protein","hypothetical protein predicted by Glimmer/Critica","CsbD family protein","","Pragai Z., Harwood C.R. Regulatory interactions between the Pho and sigma(B)-dependent general stress regulons of Bacillus subtilis. Microbiology 2002. 148:1593-1602. PMID: 11988534","","","

InterPro
IPR008462
Family

CsbD-like
PF05532	$\"[25-77]T$	CsbD

","No hits to the COGs database.","***** IPB008462 (CsbD-like) with a combined E-value of 1.1e-24. IPB008462 25-76 IPB008462 32-83 IPB008462 18-69","Residues 25-76 are similar to a (SIGMAB-CONTROLLED NCU09057.1 PLASMID GENE PRODUCT NEUROSPORA YJBJ CRASSA SA0772 SPR1626) protein domain (PD053107) which is seen in Q8KMT9_ENTFA.","","No significant hits to the PDB database (E-value < E-10).","Residues 25 to 77 (E_value = 2.1e-19) place ANA_0247 in the CsbD family which is described as CsbD-like.","","protein-related protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0248","256194","257642","1449","5.96","-2.41","49854","ATGAGCAGTGCACCTGCGGACGTTCCCGCCGCCACTCGCGTCGAGAACGCCGGTCTTGACGTCATCTCCGAGTCTGATCGCAAGGGGCGGCCGAGCGATCTCTTCATGCCCTGGTTCGCGGCCAACATCTCCGTCCTGGGACTGTCCTGGGGTGCCTGGGTCCTCGGATTCGGACTGTCCTTCTGGCAGGCGGTCGTTGCGGGCAGCGTTGGCGTCATCGTCTCCTTCCTCCTGTGCGGTGTCGTGGCCGTCCTGGGCAAACGAGGCAGCGCCCCCACCCTGGCGCTGTCCCGAGCGGCCTTCGGCTACAACGGCAATCGCCTGTCCGCGGCCCTGTCCTGGATCCTCACGGTCGGCTGGGAGACCGTCCTGTGCGTCTCTGCCACCCTGGCCTCGGCCACGGTGTTCCAGGCCCTGGGTTGGCACAACCAGGTCGGTGCCCAGATCCTGGGCTTCCTGCTCACTGTTGGCCTGGCTGCCAGCGCCGGTATTCTCGGCTTCGAGGCGATCATGAGGGTTCAGACCTGGATCACCTGGGCCACCGGTGTCCTCACCATCATCTACCTCGTCCTCGTCGCTCCCCAGATCAGTGTCGACAAGATCTTGGCCCTGCCGTCGGGCGGCCCTGCGGCCTTCATCGGAGCCCTGGTCATGGTGGCCACCGGCTTCGGCCTCGGTTGGGTCAATGCCGCCGCCGACTACTCCCGCTACCTGCCCCGCAGGGCCTCGACAGCCGGCGTCATCGGCTGGACCACGCTGGGATCGGCACTGCCCTGCGTGGTGCTCGTCTTCTTCGGCATCCTCCTGGTGGGCTCCGACGCCGAGCTCGGCCAGGCCATCAACACCGACCCCATCGGCGCTCTGACCACGATCCTGCCCACGTGGTTCCTCATCCCCTTCGCGGTCGTCGCCATCCTGGGATTGGCTGGCGGCATCATCATGGACCTGTACTCCTCGGGCCTGTCTCTCCTGGCGACCGGCCTGCCCGTGCGCCGACACGTGGCCACCTCCATCGACGCCACCATCATGACCGTGGGCACCATCGCCGTCATCTTCGGCGCTGATGACTTCCTCGGTCCCTTCCAAGGGTTCCTCACCACTCTCGGGGTCGTCGTCGCCGCCTGGGCCGGAGTCATGGTCGCCGAGGTCATTCTGCGCAAGCGCGACTACGACGAGGAAGCCCTCTTCACGCCCGACGGCGTCTACGGCTCAGTCAACTGGGAGGCCATCGCCCTGGTGGCTGCCGGTTCCGTCGTCGGCTGGGGGCTGGTCGTCAACTCGGCTGCCTCCTGGTTGTCCTGGCAGGGCTACCTGCTCGGGCCTCTCGGGGGGCGCGACGGGGCCTGGGCTGGAGCCAACCTCGGTGTGCTGGTCGCTCTGCTCATCGGTGTGCTCGGGCACCTTGTCCTCGGCCGAGGCCGGGTGGCCCGCCAGGAGGCCCGTTCGTGA","MSSAPADVPAATRVENAGLDVISESDRKGRPSDLFMPWFAANISVLGLSWGAWVLGFGLSFWQAVVAGSVGVIVSFLLCGVVAVLGKRGSAPTLALSRAAFGYNGNRLSAALSWILTVGWETVLCVSATLASATVFQALGWHNQVGAQILGFLLTVGLAASAGILGFEAIMRVQTWITWATGVLTIIYLVLVAPQISVDKILALPSGGPAAFIGALVMVATGFGLGWVNAAADYSRYLPRRASTAGVIGWTTLGSALPCVVLVFFGILLVGSDAELGQAINTDPIGALTTILPTWFLIPFAVVAILGLAGGIIMDLYSSGLSLLATGLPVRRHVATSIDATIMTVGTIAVIFGADDFLGPFQGFLTTLGVVVAAWAGVMVAEVILRKRDYDEEALFTPDGVYGSVNWEAIALVAAGSVVGWGLVVNSAASWLSWQGYLLGPLGGRDGAWAGANLGVLVALLIGVLGHLVLGRGRVARQEARS$","Permease for cytosine/purines, uracil, thiamine, allantoin","Membrane, Cytoplasm","probable transmembrane protein, putative","permease for cytosine/purines; uracil; thiamine; allantoin","permease for cytosine/purines, uracil, thiamine, allantoin","","","","","

InterPro
IPR001248
Family

Permease for cytosine/purines, uracil, thiamine, allantoin
PF02133	$\"[21-440]T$	Transp_cyt_pur

noIPR
unintegrated

unintegrated
tmhmm	$\"[34-54]?$ $\"[64-86]?$ $\"[110-130]?$ $\"[149-167]?$ $\"[177-197]?$ $\"[211-231]?$ $\"[246-268]?$ $\"[291-313]?$ $\"[334-354]?$ $\"[360-380]?$ $\"[410-430]?$ $\"[449-471]?$	transmembrane_regions

","BeTs to 7 clades of COG1457COG name: Purine-cytosine permease and related proteinsFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG1457 is ---pk-y-----b-ef-h-n------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 22-130 are similar to a (PERMEASE CYTOSINE ALLANTOIN TRANSMEMBRANE TRANSPORTER PURINE-CYTOSINE CEREVISIAE FAMILY SACCHAROMYCES STRAIN) protein domain (PD025109) which is seen in Q6AA41_PROAC.Residues 131-206 are 55% similar to a (TRANSPORT-PROTEIN FOR PERMEASE CYTOSINE/PURINES) protein domain (PDA039B5) which is seen in Q6AA41_PROAC.Residues 211-324 are similar to a (PERMEASE CYTOSINE PURINE-CYTOSINE KINASE TRANSMEMBRANE SENSORY TRANSFERASE PHOSPHORYLATION TRANSDUCTION FAMILY) protein domain (PD608088) which is seen in Q6AA41_PROAC.Residues 327-446 are 66% similar to a (TRANSPORT-PROTEIN FOR PERMEASE CYTOSINE/PURINES) protein domain (PDA039D2) which is seen in Q6AA41_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 21 to 440 (E_value = 3.5e-11) place ANA_0248 in the Transp_cyt_pur family which is described as Permease for cytosine/purines, uracil, thiamine, allantoin.","","transmembrane protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0249","257729","258523","795","5.92","-5.92","27437","ATGGAAGGCGCCCACCAGATCGCCCGACGCACCGGCGCGCCTCGCCACGATCTCCTGGTGGTCCTGGGGTCCGGCGCTGCTGACGCCCTGGCTTCCTGGGGTGAGCCGGCTGCGAGCCTGCGCCTGTCCGACCTGCCCGGGGTCATGCTCCCGGTCGCGCCGGGACATGAGGACCGCCTTGACTCCTATGTCGTCGCTCGTGGCCGGAAGGTGGGCGGACAAGAGGATGGGGGAGAGCGGCGCGTCCTCGTGGCTCGCGGACGGACCCACCTCTACGAGGGTCGCGGGCCCGGACCGGTGGTCGCCCTGTCCCGTGTCGCGGCTGCAGCCGGCGTACGTGGCGCCGTCCTGGTCAACGCCGGCGGCTGCCTGCGCGGCTGGCACATCGGCGAGGTCATGACGATCACCGATCACCTCAACCTCACCGGCTCCTCACCCTTCGACGGCCCGGTCTTCACTGACGTGCGCAGTGTGTGGGACGACGAGCTTGCTGACGTCCTGCGCGGTGTCACAGAGAGGTCAGGCGTCTATGCCGCTGTGCGTGGGCCGGAGTATCAGACCATGGCGGAGACGCGAATGCTGGAGTCCGCCGGTGCCGACTGCGTAGGCATGTCCACCGTTCTGGAGGCCATCGCCCTGCACCACCTCGGGGTGCGCGTGGCCGGCATGAGCGTCGTCTCCGACCTGTCCTTCGCGCAGGCGCCCACCGATCCCGACGAGGTCATCCGACTCGTGGTCGGTGCGCACACGACGATCGCCGCCGGCATCGAGGCGGTGCTGGCGGCGATGTCGTGA","MEGAHQIARRTGAPRHDLLVVLGSGAADALASWGEPAASLRLSDLPGVMLPVAPGHEDRLDSYVVARGRKVGGQEDGGERRVLVARGRTHLYEGRGPGPVVALSRVAAAAGVRGAVLVNAGGCLRGWHIGEVMTITDHLNLTGSSPFDGPVFTDVRSVWDDELADVLRGVTERSGVYAAVRGPEYQTMAETRMLESAGADCVGMSTVLEAIALHHLGVRVAGMSVVSDLSFAQAPTDPDEVIRLVVGAHTTIAAGIEAVLAAMS$","Purine nucleoside phosphorylase","Cytoplasm","2.4.2.1","purine nucleoside phosphorylase ","Purine-nucleoside phosphorylase","","Ealick S.E., Rule S.A., Carter D.C., Greenhough T.J., Babu Y.S., Cook W.J., Habash J., Helliwell J.R., Stoeckler J.D., Parks Jr R.E. Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J. Biol. Chem. 1990. 265(3):1812-1820. PMID: 2104852Della Ragione F., Takabayashi K., Mastropietro S., Mercurio C., Oliva A., Russo G.L., Della Pietra V., Borriello A., Nobori T., Carson D.A., Zappia V. Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA. Biochem. Biophys. Res. Commun. 1996. 223(3):514-519. PMID: 8687427Seeger C., Poulsen C., Dandanell G. Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli. J. Bacteriol. 1995. 177(19):5506-5516. PMID: 7559336","","","

InterPro
IPR001369
Family

Purine phosphorylase, family 2
PTHR11904	$\"[15-229]T$	METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE
PF00896	$\"[15-262]T$	Mtap_PNP

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1580	$\"[4-263]T$	no description
PTHR11904:SF9	$\"[15-229]T$	PURINE NUCLEOSIDE PHOSPHORYLASE

","BeTs to 16 clades of COG0005COG name: Purine nucleoside phosphorylaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0005 is aompkzyqv-rlbcef--s--j----Number of proteins in this genome belonging to this COG is 2","***** IPB001369 (Purine (and other) phosphorylase, family 2) with a combined E-value of 2.8e-18. IPB001369A 16-26 IPB001369D 174-214","Residues 2-84 are 50% similar to a (PHOSPHORYLASE TRANSFERASE GLYCOSYLTRANSFERASE NUCLEOSIDE PURINE PNP INOSINE I PURINE-NUCLEOSIDE XANTHOSINE) protein domain (PD860101) which is seen in Q73UD9_MYCPA.Residues 180-260 are 61% similar to a (PHOSPHORYLASE TRANSFERASE GLYCOSYLTRANSFERASE PURINE NUCLEOSIDE 5_apos;-METHYLTHIOADENOSINE PNP MTA METHYLTHIOADENOSINE INOSINE) protein domain (PD003195) which is seen in Q729W7_DESVH.","","-47% similar to PDB:1G2O CRYSTAL STRUCTURE OF PURINE NUCLEOSIDE PHOSPHORYLASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH A TRANSITION-STATE INHIBITOR (E_value = 4.9E_31);-47% similar to PDB:1I80 CRYSTAL STRUCTURE OF M. TUBERCULOSIS PNP IN COMPLEX WITH IMINORIBITOL, 9-DEAZAHYPOXANTHINE AND PHOSPHATE ION (E_value = 4.9E_31);-47% similar to PDB:1N3I Crystal Structure of Mycobacterium tuberculosis PNP with transition state analog DADMe-ImmH (E_value = 4.9E_31);-48% similar to PDB:1C3X PURINE NUCLEOSIDE PHOSPHORYLASE FROM CELLULOMONAS SP. IN COMPLEX WITH 8-IODO-GUANINE (E_value = 4.1E_30);-48% similar to PDB:1QE5 PURINE NUCLEOSIDE PHOSPHORYLASE FROM CELLULOMONAS SP. IN COMPLEX WITH PHOSPHATE (E_value = 4.1E_30);","Residues 15 to 262 (E_value = 8.1e-15) place ANA_0249 in the Mtap_PNP family which is described as Phosphorylase family 2.","","(pnpI) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0250","258943","258563","381","5.45","-4.85","13912","ATGACCGACACCACCCGTACCGGTGCCGACTTCGACGCGAGCTACCTGCGCACCTGGACTGAGCCCGACGCCGATCAGCGCCGTGCACTCATCGAGCAGATGTGGGCCCCGCACGGGTCGCTGCACATCTCCTCACCCGCCTTGACCGTCACAGGAACAGCCGACATCGCTGAGCACATCAACCGCGTCCACAACGACCGCATTGCAGGTCAGGGCCTGACCTTCAGCTATGACCAGCGCATGGAGTCCGGCGACGCACTATTGCTGCGCTGGTCGATGACCGCCCCAAGCGGCGACGTCGTAGGGCGCGGAGTCGACACCGTCTTCCGCGACGTCGACGGCAAGGTGACGCACGCCTACATGTTCATGGGCGTGAACTGA","MTDTTRTGADFDASYLRTWTEPDADQRRALIEQMWAPHGSLHISSPALTVTGTADIAEHINRVHNDRIAGQGLTFSYDQRMESGDALLLRWSMTAPSGDVVGRGVDTVFRDVDGKVTHAYMFMGVN$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 43-126 are similar to a () protein domain (PD938446) which is seen in Q6ADW7_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0252","259028","259621","594","6.27","-3.93","21270","ATGAGCCCTCGCGATCCAGGTCCGACGCGCGCCGCCATCCTCGACGCCGCTGCAACGCTGCTCGAGGACAGGGGACCTGAGTCGGTGACGCTGCGCGCCGTTGGCGAGGCTGCCGGCGTGTCCCGCTCGGCGCCCTATCGTCACTACGCGGACAAGGCTGCGCTCATGCGTGCCCTGGCGGGACGGACCCTGCGGCAGATCGCAGAGCGGATTCGTCATGGTGCGGAGCGGCACCGGGGAGTGCGACAGCGGCTGCGCGCCGGTTGCTGGGCCTATATCGACTACGCAGTCGAGTGCCCCCACCACTACCAGCTGGTCTTCGGGGACGCCCCGATTGCGGAGCCGGACCCCGGGCTGGAGGAGGCCGCCGACGACGCCATGGCTGCCGTCGGCGAGCTCGTTGCCCAGGCCCAGGGAGCCGGTCTGCTGCGACCCGGCCCCACTCGTGAGATCGCCACCGTCATCTGGGTTCTGCTTCATGGGCTCGCTGCCCTGCAGATCACGGGTCATCTCCATGAGCCCCGGACCATTGACGGCGATGAGCATCTTGCGGAGCTGCTGGACCTGGCCCTGGAGCAGCTGCGCCCCGTGTGA","MSPRDPGPTRAAILDAAATLLEDRGPESVTLRAVGEAAGVSRSAPYRHYADKAALMRALAGRTLRQIAERIRHGAERHRGVRQRLRAGCWAYIDYAVECPHHYQLVFGDAPIAEPDPGLEEAADDAMAAVGELVAQAQGAGLLRPGPTREIATVIWVLLHGLAALQITGHLHEPRTIDGDEHLAELLDLALEQLRPV$","Transcriptional regulator, TetR family","Cytoplasm","putative TetR-family transcriptional regulator","transcriptional regulator; TetR family","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[13-26]T$ $\"[34-57]T$	HTHTETR
PF00440	$\"[13-59]T$	TetR_N
PS50977	$\"[7-67]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[6-70]T$	no description

","BeTs to 12 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 1.3e-16. IPB001647 13-55***** IPB013572 (Tetracycline transcriptional repressor MAATS-type, C-terminal) with a combined E-value of 6.5e-06. IPB013572B 34-56","Residues 14-60 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL FAMILY REGULATOR TETR REGULATOR TETR-FAMILY REGULATORY) protein domain (PD000384) which is seen in Q9A690_CAUCR.","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 59 (E_value = 6.5e-14) place ANA_0252 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","TetR-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0253","259717","261153","1437","5.17","-16.48","51304","ATGACAACTGATGCAAAGACGCCCAACCAGGCTGTCACGACCCGCACCGAATCCGACTCCATGGGCACCATCGAGGTGGACGCCAACCGCTACTGGGGGGCCCAGACCGAGCGGAGCCTGCACAACTTCGATATCGGCCGCGAGACCTTCGTGTGGGGCCGCCCCATGATCAAGGCCCTGGGGATCCTCAAGAAGTCCGCCGCCCTGGCCAACGCTGAGCTCGGCGAGCTGCCCGCCGACATCGCCGAGCTCATCGCCAAGGCCGGCGATGAGGTCATCGCCGGTGACCTCGACGCCGAGTTCCCGCTCGTGGTCTTCCAGACCGGCTCGGGCACCCAGTCCAACATGAACTCCAACGAGGTCATCTCCAACCGCGCCATTGAGCTGGCCGGCGGCGAGCGCGGCTCCAAGACCCCGGTCCACCCCAACGACCACGTCAACCGCGGCCAGTCCTCCAACGACACCTTCCCCACGGCCATGCACATCGCCGTCGTCAACGAGCTGGCCGCCATGTACCCGCGCGTCCAGCAGCTGCGCGACACCCTGGACGCCAAGGCCAAGGCCTACGCCGAGGTCGTCATGGTGGGGCGCACCCACCTGCAGGACGCCACCCCCATCACCCTGGGGCAGGTCATCAGCGGGTGGGTCGCCCAGATCGACTTCGCCCTCGATGGCATCCGCTACGCCGACTCCCGCGCCCGTGAGCTCGCCATCGGCGGGACCGCCGTCGGCACCGGCCTCAACGCCCACCCGGACTTCGGCGCCCTGTGCGCCAAGAAGATCTCCGAGGAGACCGGCATCGAGTTCACCCAGGCGGACAACCTCTTCGCCGCCCTGGGCGCCCACGACGCCCTGGTCCAGGTCTCCGGCGCCCTGCGAGTCCTGGCCGACGCCCTCATGAAGATCGCCAACGACGTGCGCTGGTACGCCTCCGGCCCCCGCAACGGCATCGGCGAGCTCATCATCCCGGAGAATGAGCCCGGCAGCTCGATCATGCCCGGCAAGGTCAACCCCACCCAGTGCGAGGCCATGACCATGGTGGCCACGAAGGTCTTCGGCAACGACGCCACCGTCGGCTTCGCCGGCTCCCAGGGCAACTTCCAGCTCAACGTCTTCAAGCCGGTCATGGCCTGGTGCGTCCTGGAGTCCATCCAGCTCCTGGGTGACACCTGCGTCTCCTTCGACACCAACTGCGCCTACGGCATCGAGCCCAACACCGAGCGGATCAAGGCCAACCTGGAGACCAACCTCATGCAGGTCACCGCCCTCAACCGCCACATCGGCTACGACAAGGCCTCCAAGATCGCCAAGAACGCGCACCACAAGGGCCTGTCCCTGCGTGAGTCCGCCCTCGAGCTCGGCTTCGTCACCGCTGAGGAGTTCGACAAGTGGGTCGTGCCCATGGACATGACCCACCCCAGCGCCGCTGAGGACTGA","MTTDAKTPNQAVTTRTESDSMGTIEVDANRYWGAQTERSLHNFDIGRETFVWGRPMIKALGILKKSAALANAELGELPADIAELIAKAGDEVIAGDLDAEFPLVVFQTGSGTQSNMNSNEVISNRAIELAGGERGSKTPVHPNDHVNRGQSSNDTFPTAMHIAVVNELAAMYPRVQQLRDTLDAKAKAYAEVVMVGRTHLQDATPITLGQVISGWVAQIDFALDGIRYADSRARELAIGGTAVGTGLNAHPDFGALCAKKISEETGIEFTQADNLFAALGAHDALVQVSGALRVLADALMKIANDVRWYASGPRNGIGELIIPENEPGSSIMPGKVNPTQCEAMTMVATKVFGNDATVGFAGSQGNFQLNVFKPVMAWCVLESIQLLGDTCVSFDTNCAYGIEPNTERIKANLETNLMQVTALNRHIGYDKASKIAKNAHHKGLSLRESALELGFVTAEEFDKWVVPMDMTHPSAAED$","Fumarate hydratase, class II","Cytoplasm","fumarate hydratase, class II","fumarate hydratase","fumarate hydratase, class II","","Woods S.A., Schwartzbach S.D., Guest J.R. Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 1988. 954(1):14-26. PMID: 3282546","","","

InterPro
IPR000362
Domain

Fumarate lyase
PR00149	$\"[146-164]T$ $\"[191-207]T$ $\"[282-309]T$ $\"[328-344]T$	FUMRATELYASE
PF00206	$\"[22-353]T$	Lyase_1
PS00163	$\"[328-337]T$	FUMARATE_LYASES

InterPro
IPR003031
Domain

Delta crystallin
PR00145	$\"[145-167]T$ $\"[186-206]T$ $\"[328-344]T$	DCRYSTALLIN

InterPro
IPR005677
Family

Fumarate hydratase, class II
TIGR00979	$\"[14-472]T$	fumC_II: fumarate hydratase, class II

noIPR
unintegrated

unintegrated
PD727516	$\"[14-37]T$	FUMC_DEIRA_Q9RR70;
G3DSA:1.10.275.10	$\"[12-150]T$	no description
G3DSA:1.10.40.30	$\"[419-478]T$	no description
G3DSA:1.20.200.10	$\"[151-418]T$	no description
PTHR11444	$\"[14-473]T$	ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF1	$\"[14-473]T$	ASPARTATE AMMONIA LYASE

","BeTs to 17 clades of COG0114COG name: FumaraseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0114 is -o---zy--dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB003031 (Delta crystallin signature) with a combined E-value of 6.2e-58. IPB003031A 145-167 IPB003031B 186-206 IPB003031C 237-253 IPB003031D 282-306 IPB003031E 328-344 IPB003031F 423-442***** IPB000362 (Fumarate lyase) with a combined E-value of 3.1e-14. IPB000362 328-353***** IPB009049 (Argininosuccinate lyase) with a combined E-value of 9.3e-07. IPB009049C 192-229","Residues 19-458 are 73% similar to a (LYASE ADENYLOSUCCINATE ARGININOSUCCINATE BIOSYNTHESIS ARGININE ASAL ARGINOSUCCINASE ASPARTATE AMMONIA-LYASE ASL) protein domain (PD000660) which is seen in Q6CCT2_EEEEE.Residues 144-442 are 41% similar to a (LYASE PROBABLE) protein domain (PD757944) which is seen in Q9HY92_PSEAE.Residues 144-348 are 45% similar to a (LYASE PROBABLE) protein domain (PDA1B3O3) which is seen in Q9HY93_PSEAE.Residues 146-348 are 46% similar to a (LYASE ADENYLOSUCCINATE) protein domain (PDA1A6R3) which is seen in Q701W7_AAAAA.","","-74% similar to PDB:1VDK Crystal structure of fumarase from thermus thermophilus HB8 (E_value = 1.5E_154);-72% similar to PDB:1YFM RECOMBINANT YEAST FUMARASE (E_value = 1.0E_142);-71% similar to PDB:1FUO FUMARASE C WITH BOUND CITRATE (E_value = 1.3E_142);-71% similar to PDB:1FUP FUMARASE WITH BOUND PYROMELLITIC ACID (E_value = 1.3E_142);-71% similar to PDB:1FUQ FUMARASE WITH BOUND PYROMELLITIC ACID (E_value = 1.3E_142);","Residues 22 to 353 (E_value = 3.7e-156) place ANA_0253 in the Lyase_1 family which is described as Lyase.","","hydratase, class II (fumC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0255","261384","263210","1827","5.53","-7.67","63086","ATGAACCTGCCACGACGCACCATCCTTGCCGCCCTGCCCGCCACCGCGGGGCTCTTGGGCCTGGGAGCCTGCTCCACCGGAGAAGCCACCGCGCAGGCCTCCTCCACGGCCTCGTCGCAGGCTTCCACCGATGCCAAACTCGCCCTGGACTCCGCCGCCTGGCGCTACGACGCCGACCACAAGGTCTACTACCAGCTGGGGCTGCGCTACGTGGCCATGCCCCAGGCCTCGGACTACGAGACCCTGGGCATCTACGTGCCCGGTGCCTACTTCACCGGCAAGGACAACGGAAATGGCACCTACACGGTCGCCGTCAACGCCTCGGGCGCCGTCGGCAGCTTCACCGCTGCCACCGCACCCACCGTCTTCCCGGTCAACACCCCGGGATACTCCGCCCAGAAGCCGCCCACCGAGTACTCCTACGACACCATCAAGGCCTACATGGAGGCCGGCTTCATCTACGTCCACGCCGGTCTGCGCGGCAAGGACTCCAACTCCCAGACCTACTCCGGCAACGCGCCCTGGGGCGTCGCCGACCTCAAGGCCGCCGTGCGCTACCGGCGCTACAACTCCGCCGCCGTACCCGGCGACGCCGCGAAGGTCTATGTCTTCGGGCACAGCGGGGGAGGGGCGCAGAGCGCCGTCGCCGGAGCCTCCGGGGACAGCGAGCTGTTCGCCCCCTACCTGGCCGTCCTGGGGGCCGCCACCACTGACACCAGCGGCAAGGCCCTGTCCGATGCCGTGGCCGGAGCCATGTGCTGGTGCCCGATCACTAGCCTGGACAGCGCCAACGCCGCCTACGAGTGGAACATGGGGCAGTTCGCCTCCTCCGACACCCGGGCCGAGGGTACCTGGACGCGGGCCTACTCCCAGGACCTCGCCGCCGCCTTCCCCGCCTACCTCAATGGGCTGAAGCTCACCGACTCCCAGGGCAAGCCTCTGACCCTGGAATCCTCGTCCCAGGGCACCTTCCTGTCGGGCTCCTACTACGACCACCTCGTGGCGGTCATCCAGAAGTCCCTCAACGACTTCCTGGCGGCCACCACCTTCCCCTACACGTCCTCCTCCACCGAGATGGCGGGGATGGAGCCCAGCGGCGGCGGGGCGCCGTCGGGAACCCCGCCCAGCGACGGTGGCGGCACGCCCCCCAAGGGCGGGAAACCCGGAAGCGGCGGTCAGGGCAGCGCCGAGTCCACCACCTACAAGACGGTGGAGGAGTACATCGCCGCCCTCAACTCCTCCTCCCAGTGGGTCACCTACGACGCCTCCAAGAAGACCGCGACGATCACCGGCCTGCAGGGCTTCGTCGCCTCCCAGAAGAACGCCTCCAAGGACGTGGGGGCCTTCGACGGCGTGGGCCGCGCCCAGACCGAGAACCTCGTCATGGGCTCGGGGGAGAACAAGCAGCACTTCTCCTCCCTGAGCCGCGAGGTCATCTCCAAGGGGCAGTCCAGGTACTCGGGGCTGTCGGGCTGGAACAAGGACTACGGCGTCGCCGCCTACGAGAAGGACCTGGCCGCCAAGGACTCGGTCGGCACCGACATGGTCACGCGCGTGGCGATGTACGACCCCCTGTACTACCTCACCCAGGACTCCAAGGGTCGGGGCAGCTCCACCATCGCCCCCGCCTGGCGCATCCGTACCGGCATCACGCAGGGCGACACGGCCTCCACCGTCGAGGTGAACCTTGCCCTGGCGCTTCAGCAGGCTGGAGCCGGCAGCGTCGACTTCGCCACTATCTGGGGACAGGGGCACACGATGGCCGAGCTGACCGGCACCGGTGAGGAGAACTTCATCGCCTGGGTGACCAAGCAGGCGGCCTCCTGA","MNLPRRTILAALPATAGLLGLGACSTGEATAQASSTASSQASTDAKLALDSAAWRYDADHKVYYQLGLRYVAMPQASDYETLGIYVPGAYFTGKDNGNGTYTVAVNASGAVGSFTAATAPTVFPVNTPGYSAQKPPTEYSYDTIKAYMEAGFIYVHAGLRGKDSNSQTYSGNAPWGVADLKAAVRYRRYNSAAVPGDAAKVYVFGHSGGGAQSAVAGASGDSELFAPYLAVLGAATTDTSGKALSDAVAGAMCWCPITSLDSANAAYEWNMGQFASSDTRAEGTWTRAYSQDLAAAFPAYLNGLKLTDSQGKPLTLESSSQGTFLSGSYYDHLVAVIQKSLNDFLAATTFPYTSSSTEMAGMEPSGGGAPSGTPPSDGGGTPPKGGKPGSGGQGSAESTTYKTVEEYIAALNSSSQWVTYDASKKTATITGLQGFVASQKNASKDVGAFDGVGRAQTENLVMGSGENKQHFSSLSREVISKGQSRYSGLSGWNKDYGVAAYEKDLAAKDSVGTDMVTRVAMYDPLYYLTQDSKGRGSSTIAPAWRIRTGITQGDTASTVEVNLALALQQAGAGSVDFATIWGQGHTMAELTGTGEENFIAWVTKQAAS$","Tannase","Extracellular","lipoprotein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-24]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-24]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 70-342 are 46% similar to a (LP_2956 FN0616) protein domain (PD680073) which is seen in Q8RFS1_FUSNN.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0257","263315","263701","387","7.52","0.85","12994","ATGCTGACCGCCGCAATGGTCCTCGCCGTCCTGGCCGCCGCACTCCACGTCCTCATCTTCTACATGGAGTCCATCGCCTGGGAGGGGCCTCTGGCCCGCAAGACCTTCGGGGGCACGCCCGAAGAGGCCAGGCCGCACGCCTTCTACGCCTTCAACCAGGGCTTCTACAACCTCTTCCTGGCCCTCCAGGCGCTGACCGGAGTCGCCCTGGCGGCCCTGGGGCACGTGGAGCTCGGCGCCGCCCTCATCCTGGCTGGCACTGGAGCCATGCTGGCGGCCGCCGTGGTCCTGGCCCTGGCCTCAGCTCCGCACCGTGGCGCAGCTGCCAAGCAGGGGATCCTCCCGCTACTGGCGGTCTCCTGCACCATCGCAGCACTGCTGGGCTAA","MLTAAMVLAVLAAALHVLIFYMESIAWEGPLARKTFGGTPEEARPHAFYAFNQGFYNLFLALQALTGVALAALGHVELGAALILAGTGAMLAAAVVLALASAPHRGAAAKQGILPLLAVSCTIAALLG$","Hypothetical membrane protein","Membrane, Cytoplasm","Hypothetical membrane protein","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF1304","","","","","

InterPro
IPR009732
Family

Protein of unknown function DUF1304
PF06993	$\"[3-127]T$	DUF1304

noIPR
unintegrated

unintegrated
PD076489	$\"[19-68]T$	Q6MK99_BDEBA_Q6MK99;
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[55-75]?$ $\"[80-100]?$ $\"[106-126]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 127 (E_value = 5.1e-24) place ANA_0257 in the DUF1304 family which is described as Protein of unknown function (DUF1304).","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0258","264499","263732","768","7.03","0.07","27275","ATGCGCGAGAGTCCCCACGACAGGCGCCGCACGATACTGCGCGCCCTGAGCCCCACCACGGTCCACAGTGTGCAGGCGCTGTCCCGGCTGACCGGGGTCTCGGTCATCACCATCCGTCGGGACCTGGCAGAGCTGGCGCATGAGGGCCTGGTGACCCGGGTCCACGGCGGGGCTCTGCGTGCACCGCGCCGTGGAGCCGCCCGACCGGCCTCCATGCGTCGCAGGCAGGATGTGGAGATCAAGCGCCGTCTGGCGCAGGCCACTGCCGAGCTCATCGAGGACGGGGAGGCGGTCATCATCGACTCGGGGACCACCTGCGAGATGGTGGCTGAGCAGCTGGCCGGCCGCGACATCCGGGTTCTGTGCCTGTCGCTGGGAGCAGGGGCGGCAGTGGCCTCCGTGCGTGGAGCCGCGGTGACCATCGCGGGCGGCCCGGTGGATCCGGAGTCCCTCTCCCTGTTCTCCGCTGAGGCGGTCGAGGCGGTGCGCGCGTTCCGCGCCGACGTCGCGGTCCTGTCCACCTGCGCCGTGTCCACCCATGAGGGCATGACCGTCATGGAGTCCGACGACGCGATGGTCAAGCGCGCCATCATGGCCTCCTCCACCCGACGCGTTCTGCCGACCGCACCGAGCAAGATCACCCAGACCAACACCTACCGGTTCGGGCGTATCGAGGACCTCGACACGCTGCTGACAACAAGCCAGATCGACCCCGAGGCACTCGAGGAGCTGCGGGGAGTCGGGGTTGACGTCGTCCTGTGCGACTAA","MRESPHDRRRTILRALSPTTVHSVQALSRLTGVSVITIRRDLAELAHEGLVTRVHGGALRAPRRGAARPASMRRRQDVEIKRRLAQATAELIEDGEAVIIDSGTTCEMVAEQLAGRDIRVLCLSLGAGAAVASVRGAAVTIAGGPVDPESLSLFSAEAVEAVRAFRADVAVLSTCAVSTHEGMTVMESDDAMVKRAIMASSTRRVLPTAPSKITQTNTYRFGRIEDLDTLLTTSQIDPEALEELRGVGVDVVLCD$","Transcriptional Regulator, DeoR family","Cytoplasm","Transcriptional regulators of sugar metabolism","putative transcriptional regulator","regulatory protein, DeoR","","Beck von Bodman S., Hayman G.T., Farrand S.K. Opine catabolism and conjugal transfer of the nopaline Ti plasmid pTiC58 are coordinately regulated by a single repressor. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(2):643-647. PMID: 1731335Ray W.K., Larson T.J. Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12. Mol. Microbiol. 2004. 51(3):813-826. PMID: 14731281","","","

InterPro
IPR001034
Domain

Bacterial regulatory protein, DeoR N-terminal
PR00037	$\"[26-40]T$ $\"[40-58]T$	HTHLACR
PF08220	$\"[8-64]T$	HTH_DeoR
SM00420	$\"[8-60]T$	HTH_DEOR
PS51000	$\"[5-60]T$	HTH_DEOR_2
PS00894	$\"[8-42]?$	HTH_DEOR_1

InterPro
IPR013982
Domain

AICARFT/IMPCHase bienzyme, formylation region
SM00798	$\"[33-249]T$	no description

InterPro
IPR014036
Domain

Bacterial regulatory protein, DeoR
PF00455	$\"[78-233]T$	DeoR

","BeTs to 9 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K [Information storage and processing--Transcription] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is 4","***** IPB001034 (Bacterial regulatory protein, DeoR family) with a combined E-value of 1e-44. IPB001034A 20-58 IPB001034B 80-113 IPB001034D 139-156 IPB001034E 193-233***** IPB000524 (Bacterial regulatory protein, GntR family) with a combined E-value of 2.4e-07. IPB000524 21-61","Residues 8-105 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR DEOR FAMILY REGULATOR OPERON) protein domain (PD469489) which is seen in Q986T2_RHILO.Residues 87-183 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR DEOR FAMILY OPERON REGULATOR) protein domain (PD002430) which is seen in Q8NU41_CORGL.Residues 189-252 are similar to a (SUGAR REGULATORS TRANSCRIPTIONAL PROTEINS DNA-BINDING TRANSCRIPTION REGULATORY BACTERIAL REGULATION FAMILY) protein domain (PD791657) which is seen in Q8NU41_CORGL.","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 59 (E_value = 0.0028) place ANA_0258 in the HTH_11 family which is described as HTH domain.Residues 8 to 64 (E_value = 7.2e-11) place ANA_0258 in the HTH_DeoR family which is described as DeoR-like helix-turn-helix domain.Residues 78 to 233 (E_value = 6.2e-21) place ANA_0258 in the DeoR family which is described as Bacterial regulatory proteins, deoR family.","","regulators of sugar metabolism (glpR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0259","264709","265149","441","4.75","-12.59","16132","ATGCCGTACCTCGACCACGTCGCCATCTGGGTCGCCGACCTCGACAGCGCCCGCGACTTCTACTCCCACTGGTTTGACGGGCATGCCAACGGTCTCTACGAGAACCCCAGGACCGGCCTGCGCACCCACATCCTCCACTTCGCCGAGACGCCCGCGGGCGAGCGGGGGACCCGCCTGGAGATCATGACCCGTCCGGAGCTGGCCGAGGGGCGCGAGGCCGCCGGGCTGGGGTGGGCTCACGTCTCTTTTGGCCTGCCGGGGCGCGAAGACGTCGACCGCCTGGCTTCCTACATGTCGGAAGCCGGTGTGCCGGTCGTCGACGGACCTCGCGAGACCGGCGACGGGTACTACGAGGCCACCGTGCTTGACCCCGAGGGCAACCGCGTCGAGCTCGTTGCCTCCGACTACTCCGACGACGTCGCCCTGCGCCCGGCCTTCTGA","MPYLDHVAIWVADLDSARDFYSHWFDGHANGLYENPRTGLRTHILHFAETPAGERGTRLEIMTRPELAEGREAAGLGWAHVSFGLPGREDVDRLASYMSEAGVPVVDGPRETGDGYYEATVLDPEGNRVELVASDYSDDVALRPAF$","Glyoxylase family protein","Cytoplasm","glyoxylase family protein","glyoxylase family protein ","Glyoxalase/bleomycin resistance protein/dioxygenase","","Kim N.S., Umezawa Y., Ohmura S., Kato S. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 1993. 268(15):11217-11221. PMID: 7684374Harayama S., Rekik M. Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J. Biol. Chem. 1989. 264(26):15328-15333. PMID: 2670937Asturias J.A., Eltis L.D., Prucha M., Timmis K.N. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases. J. Biol. Chem. 1994. 269(10):7807-7815. PMID: 8126007Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 1995. 270(5238):976-980. PMID: 7481800","","","

InterPro
IPR004360
Domain

Glyoxalase/bleomycin resistance protein/dioxygenase
PF00903	$\"[3-131]T$	Glyoxalase

InterPro
IPR011588
Domain

Glyoxalase/extradiol ring-cleavage dioxygenase
PD002334	$\"[7-131]T$	Q8L185_BBBBB_Q8L185;

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.10	$\"[4-143]T$	no description

","BeTs to 6 clades of COG0346COG name: Lactoylglutathione lyase and related lyasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0346 is aom-kzy--drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","Residues 4-101 are 59% similar to a (LYASE FAMILY LACTOYLGLUTATHIONE GLYOXYLASE GLYOXALASE ACETYLTRANSFERASE LIN0429 YYAH TRANSFERASE BH0282) protein domain (PD353558) which is seen in Q734N2_BACC1.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 131 (E_value = 1.6e-14) place ANA_0259 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0260","265235","266290","1056","7.80","2.99","37802","GTGGGGGCAGCTCGTCGATACCTTCGACGTGTCGATGGTGAGCACCTGGGTGTTTGCTTTCAATCCTGCACCAATCGCCTTGGGAAAGCCTGCCACCCGGCAGATCGGCAGATGGTGGCTGGTACGGTGGCAATACGCCATCGGGCCGCACCGCCTAAGGCCATGAGAGGACACCCGGCACCCGCAATGAGCAGCACCATTACCTTTGATGCCGTCACCAAGTCGTACCCGGCCGGGAAGGGCTCCGGAACCGGTTCCCCCGCCGTCGACTCCTTCACCGCCCGTATCGAGGCCGGCACCACCACCGTCCTGCTGGGATCGTCCGGCTGTGGCAAGACGACCCTGCTGCGCATGGTCAACCGCATGGTGGAGCCCTCCAGCGGCCGGGTCCTCATCGATGACGAGGACGTTGCCACCCGCGATGCCGTGGCCCTGCGTCGCTCCATCGGCTACGTCATGCAGAACGCGGGGCTGCTGCCGCACCGGCGCGTCATCGACAACATCACCCTCGTACCCCGCCTCCAGGGTGCCGACCGCCACGACGCCCGGTGCCGGGCCCTCGAGCTCATGGACATGCTCGACCTCGACCGCGACCTGGCCGGGCGCTACCCCCACCAGCTCTCCGGCGGCCAGGCCCAGCGGGTCGGGGTCGCCCGGGCACTGGCCGCCGATCCTGAGGTGCTCCTCATGGACGAGCCCTTCGGCGCTGTCGACCCGCTCGTGCGCCGCGACCTCCAGCGCGAGATGGCCCGCATCCAGGCCGAGTTGGGGAAGACCATCATCTTCGTCACCCACGATGTCGATGAGGCCCTTGCCCTGGGCGACGAGATCATCCTCCTGCGCGAAGGCGCCCAGGTCGCCCAGCGCGGCAGCGGCCCCCAGCTGCTGGCCCACCCGGCCGATGACTTCGTCGCCCGCTTCCTCGGCCTCGACGACGCCGCCCGCCAGCTTCAGCTCACGGACGTCGCCGAGTCCCGGATCGTCCTGGACCGGGCCGGCCGCGCCGTCGGGCGCCTGGCCGACGAATCCTGCCCGAAGGCGGAGGAACGGGCATGA","VGAARRYLRRVDGEHLGVCFQSCTNRLGKACHPADRQMVAGTVAIRHRAAPPKAMRGHPAPAMSSTITFDAVTKSYPAGKGSGTGSPAVDSFTARIEAGTTTVLLGSSGCGKTTLLRMVNRMVEPSSGRVLIDDEDVATRDAVALRRSIGYVMQNAGLLPHRRVIDNITLVPRLQGADRHDARCRALELMDMLDLDRDLAGRYPHQLSGGQAQRVGVARALAADPEVLLMDEPFGAVDPLVRRDLQREMARIQAELGKTIIFVTHDVDEALALGDEIILLREGAQVAQRGSGPQLLAHPADDFVARFLGLDDAARQLQLTDVAESRIVLDRAGRAVGRLADESCPKAEERA$","ABC-type glycine betaine/L-proline/carnitine/choline transport system, ATPase component","Cytoplasm, Membrane","PROV-like protein","K05847 osmoprotectant transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[206-249]T$	Q7X3N9_LEIXX_Q7X3N9;
PF00005	$\"[99-283]T$	ABC_tran
PS50893	$\"[67-308]T$	ABC_TRANSPORTER_2
PS00211	$\"[207-221]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[98-283]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[64-311]T$	no description
PTHR19222	$\"[67-331]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF48	$\"[67-331]T$	GLYCINE BETAINE/L-PROLINE ABC TRANSPORTER

","BeTs to 8 clades of COG1125COG name: ABC-type proline/glycine betaine transport systems, ATPase componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1125 is a--------drlb-ef----uj--t-Number of proteins in this genome belonging to this COG is 2","***** IPB005116 (TOBE domain) with a combined E-value of 4.8e-31. IPB005116A 106-122 IPB005116B 147-164 IPB005116C 207-220 IPB005116D 227-246 IPB005116E 261-274***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 9.2e-29. IPB013563A 88-122 IPB013563C 204-231 IPB013563D 259-311***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 5.2e-27. IPB005074C 88-135 IPB005074D 195-238 IPB005074E 259-279***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.8e-14. IPB010509B 99-124 IPB010509D 202-246","Residues 57-176 are 48% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3N7) which is seen in Q92T99_RHIME.Residues 63-233 are 40% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 67-281 are 45% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 69-265 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 81-240 are 45% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 83-154 are 64% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I309) which is seen in Q9AM85_RIEAN.Residues 85-286 are 48% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 89-137 are 81% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q6AAQ8_PROAC.Residues 90-183 are 53% similar to a (BG:DS00797.5 CG31731-PA ATP-BINDING) protein domain (PD266009) which is seen in Q9NKF0_DROME.Residues 99-267 are 52% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 201-322 are 52% similar to a (PROBABLE ATP-BINDING ABC TRANSPORTER ATP BINDING) protein domain (PD763654) which is seen in Q8G625_BIFLO.Residues 202-265 are 67% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 203-281 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD195520) which is seen in Q822T7_CHLCV.Residues 203-277 are 57% similar to a (ATP-BINDING TRANSPORTER ABC OLIGOPEPTIDE) protein domain (PDA189L6) which is seen in Q8TRD5_METAC.Residues 203-283 are 64% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 203-277 are 61% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA184H5) which is seen in Q6W139_RHISN.Residues 204-288 are 54% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 204-296 are 55% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 204-266 are 63% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q8DEB0_VIBVU.Residues 206-249 are 88% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q7X3N9_LEIXX.Residues 266-309 are 77% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER SUGAR COMPONENT ATPASE MEMBRANE PROBABLE PLASMID) protein domain (PD001887) which is seen in Q6NKD5_CORDI.Residues 266-351 are 59% similar to a (ATP-BINDING SUBUNIT ABC TRANSPORTER) protein domain (PD956621) which is seen in Q6AAQ8_PROAC.","","-53% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 7.9E_38);-54% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 6.9E_34);-54% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 6.9E_34);-51% similar to PDB:1G29 MALK (E_value = 2.6E_33);-54% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 1.7E_32);","Residues 99 to 283 (E_value = 8.8e-57) place ANA_0260 in the ABC_tran family which is described as ABC transporter.","","protein (proV)","","1","","","","","","","","","","","Mon Aug 13 18:16:48 2007","","Mon Aug 13 18:16:48 2007","","","Mon Aug 13 18:16:48 2007","Mon Aug 13 18:16:48 2007","Mon Aug 13 18:16:48 2007","","Mon Aug 13 18:16:48 2007","Mon Aug 13 18:16:48 2007","","","","","yes","","" "ANA_0262","266287","266991","705","9.20","4.32","23919","ATGAGCTGGGTCCTGGCCAACCTGCCCACCATCGCCGGCCACCTGCTGGCCCACCTGCTCCAGGCGGTTCCCGCGATCGTCGCCTCCTTCGTCCTGGCGATCCCCATTGCCCGGCTGGCCCGCGTGGCCCGGCCGTTGCGAGCCCTGCTGGTGACCGGTTCCTCGCTGCTCTACGCCGTCCCCTCCCTGGCCCTGTTCGTCATCCTCCCCATCATCCTGGCCACCGGCATCCGCGACCCGCTCAACGTCATCGTGGCCCTGACCCTCTACGGGCTGGCGCTCCTGGTTCCGGCCACCGCCGACGCGCTCGACGCCGTTGACGCCCGTGTCCTGGACGCCGCCACCGCCATGGGCATGGGGCGACTGCGCTGCTTCCTCACCGTCGAGCTGCCGCTGGCGGGCCCCGCGATCCTCACGGGCCTGCGCGTGGTGACGGTCTCGACGATCTCACTGACCACTGTCGGGGCGGTCCTCGGTGTGCGCAGCCTCGGCTGGCTGTTCACCGACGGCTTCCAGCGCGGCATCACCGCGGAGATCGTCACTGGGCTGGTCGCCACCGCGGCCCTGGCCCTCGTCCTGGACGGGCTCGTCCTCGCTCTGGGGCGGCTGTGCCTGCCCTGGACCTGGAAGCGCGCCGGCGACGCCGGGGCAGTCCCTGCCGGAGCCTGCGCAGCCGCCTCGAACAGTCAGGAGGGCAAGGCGTGA","MSWVLANLPTIAGHLLAHLLQAVPAIVASFVLAIPIARLARVARPLRALLVTGSSLLYAVPSLALFVILPIILATGIRDPLNVIVALTLYGLALLVPATADALDAVDARVLDAATAMGMGRLRCFLTVELPLAGPAILTGLRVVTVSTISLTTVGAVLGVRSLGWLFTDGFQRGITAEIVTGLVATAALALVLDGLVLALGRLCLPWTWKRAGDAGAVPAGACAAASNSQEGKA$","ABC-type glycine betaine/L-proline/carnitine/choline transport system, permease component","Membrane, Cytoplasm","PROW-like protein","binding-protein-dependent transport systems inner membrane component","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[15-206]T$	BPD_transp_1
PS50928	$\"[15-202]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[19-39]?$ $\"[54-74]?$ $\"[80-100]?$ $\"[143-165]?$ $\"[179-201]?$	transmembrane_regions

","BeTs to 6 clades of COG1174COG name: ABC-type proline/glycine betaine transport systems, permease componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1174 is a--------drlb-ef----uj--t-Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 54-133 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q6AAQ9_PROAC.Residues 135-181 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORT SYSTEM PROBABLE BETAINE GLYCINE ABC-TYPE TRANSPORTER) protein domain (PD704458) which is seen in Q8FU54_COREF.","","No significant hits to the PDB database (E-value < E-10).","Residues 15 to 206 (E_value = 1.6e-11) place ANA_0262 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","protein (proWX)","","1","","","","","","","","","","","Mon Aug 13 18:17:15 2007","","Mon Aug 13 18:17:15 2007","","","Mon Aug 13 18:17:15 2007","","Mon Aug 13 18:17:15 2007","","Mon Aug 13 18:17:15 2007","Mon Aug 13 18:17:15 2007","","","","","yes","","" "ANA_0263","267048","267668","621","10.83","6.64","20945","ATGGGGATCGGCCCGCTGCTGGTCCAGCATGTCCTCTACTCCCTGGCCGGTGTCCTCATCGCCGCCCTCATCGGGGTCCCCGCCGGCTGGTGGGTAGGGCACACTGGACGTGGGCGCACCTGGGTGCAACCGCTCAGCGGCACGGCCCGCTCCCTGCCCACCCTCGGCCTCATCACGCTGTTCGGCCTCGTTCTCGGGGTCGGCCTGAGCGCCCCCATGATCGCCTTCGTCATCCTGGCCCTACCCAGTGTCCTGGCCGGAGCCATGAGCGGGGTGCGGGCGGCCTCAGCCATGGCCGTCGACGGCGCCCGGGCCAGCGGCATGAGCGAGCTGCAGGTGCTGGGCCGGGTCGAGATCCCGCTGGGGGCGCCGCTGCTCGTCGGTGGGCTGCGCTCGGCCAGCCTCCAGGTCATCTCCACCGCCACACTGGCCGCCTACACCGGCGCCGGCGGGCTCGGCCGACTCATGTTCCTGGGCCTCAAGACCCAGGACTACGTCATGATGCTCTCCTCGGCGCTCCTGGTCATCTCCCTGGCCCTGGCCTCCGAGGCCGTCTTCGCCCTCATCCAATGGGGGGTCACGCCCCCAGGTGCCCGGCAGCACCGGAAGGAATCAGCATGA","MGIGPLLVQHVLYSLAGVLIAALIGVPAGWWVGHTGRGRTWVQPLSGTARSLPTLGLITLFGLVLGVGLSAPMIAFVILALPSVLAGAMSGVRAASAMAVDGARASGMSELQVLGRVEIPLGAPLLVGGLRSASLQVISTATLAAYTGAGGLGRLMFLGLKTQDYVMMLSSALLVISLALASEAVFALIQWGVTPPGARQHRKESA$","ABC-type glycine betaine/L-proline/carnitine/choline transport system, permease component","Membrane, Extracellular","PROZ-like protein","K05846 osmoprotectant transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[7-195]T$	BPD_transp_1
PS50928	$\"[7-186]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[52-72]?$ $\"[78-98]?$ $\"[113-131]?$ $\"[137-159]?$ $\"[169-189]?$	transmembrane_regions

","BeTs to 8 clades of COG1174COG name: ABC-type proline/glycine betaine transport systems, permease componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1174 is a--------drlb-ef----uj--t-Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 47-121 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q6NKD7_CORDI.","","-59% similar to PDB:1DY0 MURINE ENDOSTATIN, CRYSTAL FORM II (E_value = );-59% similar to PDB:1DY1 MURINE ENDOSTATIN, CRYSTAL FORM III (E_value = );-59% similar to PDB:1KOE ENDOSTATIN (E_value = );-41% similar to PDB:1V9N Structure of Malate Dehydrogenase from Pyrococcus horikoshii OT3 (E_value = );-43% similar to PDB:1CWV CRYSTAL STRUCTURE OF INVASIN: A BACTERIAL INTEGRIN-BINDING PROTEIN (E_value = );","Residues 7 to 195 (E_value = 5.6e-16) place ANA_0263 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","protein ","","1","","","","","","","","","","","Mon Aug 13 18:17:38 2007","","Mon Aug 13 18:17:38 2007","","","Mon Aug 13 18:17:38 2007","","Mon Aug 13 18:17:38 2007","","Mon Aug 13 18:17:38 2007","Mon Aug 13 18:17:38 2007","","","","","yes","","" "ANA_0264","267665","268654","990","5.49","-5.11","34329","ATGACTGCACCGTCCCACTCGCGCCCCGGCAAGCAGCTGACGCGACGCGGCCTGCTGGCCGGCGTCGGTGCGACCGCCGGCTTGCTCGCCCTGAGCGCCTGCTCCGACACCGACCCCTTCGCCGTCGACCAAGCATCGGGAGGCTACTCCGGCGGCCCGATCATCATCGGCAGCCAGCAGTACTACTCCAACGAGATCATCGCCGAGCTCTACGCCCAGATGATGGAGAAGACGGGCCTGACCGTCACCCGCCAGTACCAGATCGGCCAGCGGGAGGTCTACCTGCCCGAGCTCGAGGCCGGCAAGATCCACGTCATCCCCGAGTACGGCGGCAACCTGCTGGAGTACTACAGCAAGACCTCCGCCTCAGGCAGTCCCACCGCCACCGCGACCCCCTCCCGTGCCGCCGGTGATACCGCCTCCATCCAGGACACCCTGCTGAGGACCCTGCCGCACTCGCTGACCGTCCTGAACCCGGCCGAGGCGACGGATCAGGACTCCCTGACCGTCACCAAGGCCACCGCCCAGGCCCACTCCCTGACCTCCATCGGCGACCTGGCCTCACTGGGGCGGCCCATTACGATCGCCGCGAACTCGGAGTTCACCACCCGCCCCTACGGCCCCAAGGGCCTCAAGGCCGTCTACGGCGTCGACGCCTCCGTCACGCCGGTGGAGGACTCCGGCGGGCCTCTGACCGTCAAAGCCCTCACCGACGGCACCGTCGACGTTGCCGACATCTACTCCTCCGATCCCGCCATCGGGGCCAAGGACCTCGTCATCCTGTCCGACCCCCAGATGCTCATCCTCCCGCAGAACGTCACCCCGCTGGTCTCCGCCTCACTGCCGGCCATCGCGGCCACCGCCATCAACCGGGTCTCGGCCCTGCTGACCCCCGACGAGCTGCGCTCCCTCAACCAGCGCTCCACCGGCGAGAAGCTCAGCTCCAAGACCATCGCCACCGACTGGCTCACCTCCAAGAAGCTGCTCTGA","MTAPSHSRPGKQLTRRGLLAGVGATAGLLALSACSDTDPFAVDQASGGYSGGPIIIGSQQYYSNEIIAELYAQMMEKTGLTVTRQYQIGQREVYLPELEAGKIHVIPEYGGNLLEYYSKTSASGSPTATATPSRAAGDTASIQDTLLRTLPHSLTVLNPAEATDQDSLTVTKATAQAHSLTSIGDLASLGRPITIAANSEFTTRPYGPKGLKAVYGVDASVTPVEDSGGPLTVKALTDGTVDVADIYSSDPAIGAKDLVILSDPQMLILPQNVTPLVSASLPAIAATAINRVSALLTPDELRSLNQRSTGEKLSSKTIATDWLTSKKLL$","ABC-type glycine betaine/L-proline/carnitine/choline transport system, substrate-binding component","Membrane, Periplasm, Extracellular","PROX-like protein","K05845 osmoprotectant transport system substrate-binding protein","Substrate-binding region of ABC-type glycine betaine transport system","","Kempf B., Bremer E. OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. J. Biol. Chem. 1995. 270(28):16701-16713. PMID: 7622480Kappes R.M., Kempf B., Kneip S., Boch J., Gade J., Meier-wagner J., Bremer E. Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis. Mol. Microbiol. 1999. 32(1):203-216. PMID: 10216873","","","

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[13-33]T$	TAT_signal_seq: Tat (twin-arginine transloc

InterPro
IPR007210
Domain

Substrate-binding region of ABC-type glycine betaine transport system
PF04069	$\"[52-325]T$	OpuAC

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[47-217]T$	no description
signalp	$\"[1-34]?$	signal-peptide

","BeTs to 7 clades of COG1732COG name: Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system (osmoprotectant binding protein)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1732 is ao-------drlb-ef----uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 63-186 are 58% similar to a (ABC TRANSMEMBRANE TRANSPORTER GLYCINE PERMEASE BINDING TRANSPORTER PERIPLASMIC LIPOPROTEIN BETAINE/CARNITINE/CHOLINE) protein domain (PD009904) which is seen in Q6NK80_CORDI.Residues 193-264 are 72% similar to a (ABC TRANSMEMBRANE TRANSPORTER GLYCINE PERMEASE BINDING TRANSPORTER PERIPLASMIC LIPOPROTEIN BETAINE/CARNITINE/CHOLINE) protein domain (PD854862) which is seen in Q8FU56_COREF.Residues 267-328 are 61% similar to a (SUBSTRATE-BINDING GLYCINE ABC-TYPE TRANSPORT BETAINE PROX-LIKE) protein domain (PD886833) which is seen in Q6AAR1_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 52 to 325 (E_value = 1.4e-56) place ANA_0264 in the OpuAC family which is described as Substrate binding domain of ABC-type glycine betaine transport system.","","protein ","","1","","","","","","","","","","","Mon Aug 13 18:17:57 2007","","Mon Aug 13 18:17:57 2007","","","Mon Aug 13 18:17:57 2007","","Mon Aug 13 18:17:57 2007","","Mon Aug 13 18:17:57 2007","Mon Aug 13 18:17:57 2007","","","","","yes","","" "ANA_0265","268813","269436","624","4.53","-9.05","20403","ATGTCCGTCCCCTCCATCTCCATCATCGGCGCCGGCAACATCGGATCAGCGGTCGCGGGTCTGGCGGTCAAGGCCGGTGCCAGTACTCAGGTCGTGGTGCGCGACGCCTCCAAGGCCACCGACCTGTCGGGCGTCGACGTCGCCGAGATCGGTTCACCCCTGACCGGTGACATCGTTGTCCTCGCCCTGCCCTACGCCGCCATCGACGAGGTCATTGCCACCTACGGCGCACAGGCCTTCGCCGGCAAGGTCGTCGTCGACCCGACCAACCCCCTGGACTTCACCACTCTCGACTCTCTCGTCCCGGCCGGTAGCTCCGCGAGCGCCGAGCTCGCAGCAAAGCTCCCGGACGCCCAGGTGGTCAAGGCCTTCAACACCGTCTTCGCCGCCGTCCTGGCGAGCGGCACCATCGGCGCCCGCCCGGCCACCGTCCTGGCCGCCTCCGACTCCGCAGAGGCCAAGGCGGGCCTGCGCTCCTTCGTCGAGGCCGCCGGACTGGCGTGGGCCGACGCCGGCGAGCTCAAGCGGGCAGAGCGTATGGAGGCACTCGGGGCACTGAACATCGCCCTGGGTGTCACGGAGCAGGTCGCTTGGACCGGCGGCCTCGCCGTCGTGTCAGAGTGA","MSVPSISIIGAGNIGSAVAGLAVKAGASTQVVVRDASKATDLSGVDVAEIGSPLTGDIVVLALPYAAIDEVIATYGAQAFAGKVVVDPTNPLDFTTLDSLVPAGSSASAELAAKLPDAQVVKAFNTVFAAVLASGTIGARPATVLAASDSAEAKAGLRSFVEAAGLAWADAGELKRAERMEALGALNIALGVTEQVAWTGGLAVVSE$","NADP oxidoreductase, coenzyme F420-dependent","Cytoplasm, Extracellular","putative reductase","predicted dinucleotide-binding enzyme","NADP oxidoreductase, coenzyme F420-dependent","","","","","

InterPro
IPR004455
Family

NADP oxidoreductase, coenzyme F420-dependent
PF03807	$\"[5-185]T$	F420_oxidored

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[4-204]T$	no description
PTHR14239	$\"[4-200]T$	DUDULIN-RELATED

","BeTs to 5 clades of COG2085COG name: Predicted dinucleotide-binding enzymesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2085 is aom--------l------s--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 114-205 are similar to a (OXIDOREDUCTASE DINUCLEOTIDE-BINDING 1.-.-.- ENZYME YQFE PREDICTED ENZYMES) protein domain (PD874142) which is seen in Q8NR04_CORGL.Residues 116-188 are 63% similar to a (REDUCTASE TRANSMEMBRANE PLASMID PHYDE ENRICHED OXIDOREDUCTASE LIBRARY DUDULIN PROSTATE F420-DEPENDENT) protein domain (PD580440) which is seen in Q7B6G1_STRHY.","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 131 (E_value = 0.001) place ANA_0265 in the NAD_Gly3P_dh_N family which is described as NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus.Residues 5 to 185 (E_value = 1.5e-21) place ANA_0265 in the F420_oxidored family which is described as NADP oxidoreductase coenzyme F420-dependent.","","reductase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0266","269607","269969","363","7.04","0.11","13319","ATGGCGCCCGACCCCTATAGCCGCAGCTGCCCCTCACGCGGCCTGCTCAAGTCGCTCGGCGACCTGTGGACCGTGCTCGTCGTCGGGGCGCTTCACGAAGCGGGCCGGCCGCAACGCTTCAAGGAGATATCGACCCGCGTCGACGGTATCTCCACCAAGATGCTCACCCAGACCCTCAGGGGCCTTGAGCGTGATGGACTCATCGAGCGCCATCAGTACCCTGAGATCCCGCCGCGAGTGACCTACGAGCTCACCGACTCAGGCAAGGGGCTGGCGGAGGCGCTGGCTCACGTCGAGACCTGGGCCACTGAGCACCTCGGCGCTGTCAGCCAGGCCCGGGCGCGCTACGACGCCGAGCACTGA","MAPDPYSRSCPSRGLLKSLGDLWTVLVVGALHEAGRPQRFKEISTRVDGISTKMLTQTLRGLERDGLIERHQYPEIPPRVTYELTDSGKGLAEALAHVETWATEHLGAVSQARARYDAEH$","Transcriptional regulator, HxlR type","Cytoplasm","transcriptional regulatory protein","transcriptional regulator","helix-turn-helix, HxlR type","","Yasueda H., Kawahara Y., Sugimoto S. Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression. J. Bacteriol. 1999. 181(23):7154-7160. PMID: 10572115Huffman J.L., Brennan R.G. Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr. Opin. Struct. Biol. 2002. 12(1):98-106. PMID: 11839496","","","

InterPro
IPR002577
Domain

Helix-turn-helix, HxlR type
PD004032	$\"[39-76]T$	Q82PF6_STRAW_Q82PF6;
PF01638	$\"[18-110]T$	DUF24
PS51118	$\"[10-110]T$	HTH_HXLR

","BeTs to 13 clades of COG1733COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1733 is aomp-z---drlbcefghs-uj----Number of proteins in this genome belonging to this COG is 4","***** IPB002577 (Protein of unknown function DUF24) with a combined E-value of 2.2e-26. IPB002577 39-86","Residues 39-76 are similar to a (TRANSCRIPTIONAL REGULATOR REGULATOR FAMILY MARR PREDICTED UPF0087 PLASMID REGULATORY PROBABLE) protein domain (PD004032) which is seen in Q82PF6_STRAW.","","-58% similar to PDB:1YYV Putative transcriptional regulator ytfH from Salmonella typhimurium (E_value = 1.9E_16);-56% similar to PDB:2FSW Crystal Structure of the Putative Transcriptional Regualator, MarR family from Porphyromonas gingivalis W83 (E_value = 1.4E_11);-54% similar to PDB:2HZT Crystal Structure of a putative HTH-type transcriptional regulator ytcD (E_value = 5.3E_11);-58% similar to PDB:1Z7U Crystal Structure of the Putitive Transcriptional Regulator of MarR Family from Enterococcus faecalis V583 (E_value = 3.4E_10);","Residues 18 to 110 (E_value = 2.3e-28) place ANA_0266 in the DUF24 family which is described as HxlR-like helix-turn-helix.Residues 58 to 95 (E_value = 3.5e-05) place ANA_0266 in the PadR family which is described as Transcriptional regulator PadR-like family.","","regulatory protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0267","270600","270010","591","7.37","0.41","21017","ATGAGCGGCCTGGGGATGATCTGGGCCCAGGACATCACCGGCGTCCTGGGGGCCGACGGCGGCATGCTGTGGCGCGTGCCGGCGGACTTCGCCCACTTCAAGGCCACGACCATGGGCTGCGGGCTGGTCATGGGGCGCACCACCTGGGAATCACTGGGAGGCCCCTTGCCCGGGCGGCGCAATGTGGTTCTCACCCGTGACCGCTCCTGGCGGGCCGAGGGGGCGGTCCGTGCCGGCTCGCTGCGCGAGGGGCTCTCGCTGGCGGCGCGGGGCCTGGCCGCTGAGCTGGGCCGCGACCCCCGTGACGGGGATGCTGCGGGGCTGCCCCGCCTGTGGGTCATCGGTGGCGGGAGCGTCTACGAGCAGGCGCTGGCTGACGGCCTGCCTGATGTGCTCGTCGTCAGCGTCCTGGACCTGGATGCCACGCAGCGGGCCCGCGAGCGCGGCCTGCCCGACTCGGCGCTCGTGCGCGCGCCGGGGATCAGCACTCAGGAGTGGGCCATCGATCCGGCCCTCTCCGACCCGCGGGGGCAGTGGCGCCCCACATCCGGGGACGCGCGCTGGCGCGTGGAGACCTGGCGGCACCTGTAG","MSGLGMIWAQDITGVLGADGGMLWRVPADFAHFKATTMGCGLVMGRTTWESLGGPLPGRRNVVLTRDRSWRAEGAVRAGSLREGLSLAARGLAAELGRDPRDGDAAGLPRLWVIGGGSVYEQALADGLPDVLVVSVLDLDATQRARERGLPDSALVRAPGISTQEWAIDPALSDPRGQWRPTSGDARWRVETWRHL$","Dihydrofolate reductase","Cytoplasm, Extracellular","dihydrofolate reductase","dihydrofolate reductase ","dihydrofolate reductase region","","Trimble J.J., Murthy S.C., Bakker A., Grassmann R., Desrosiers R.C. A gene for dihydrofolate reductase in a herpesvirus. Science 1988. 239(4844):1145-1147. PMID: 2830673Oefner C., D. Arcy A., Winkler F.K. Crystal structure of human dihydrofolate reductase complexed with folate. Eur. J. Biochem. 1988. 174(2):377-385. PMID: 3383852Smith S.L., Patrick P., Stone D., Phillips A.W., Burchall J.J. Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence. J. Biol. Chem. 1979. 254(22):11475-11484. PMID: 500653Bolin J.T., Filman D.J., Matthews D.A., Hamlin R.C., Kraut J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. J. Biol. Chem. 1982. 257(22):13650-13662. PMID: 6815178Cowman A.F., Lew A.M. Antifolate drug selection results in duplication and rearrangement of chromosome 7 in Plasmodium chabaudi. Mol. Cell. Biol. 1989. 9(11):5182-5188. PMID: 2601715","","","

InterPro
IPR001796
Domain

Dihydrofolate reductase region
PR00070	$\"[15-25]T$ $\"[29-37]T$ $\"[42-53]T$ $\"[110-124]T$	DHFR
PF00186	$\"[3-195]T$	DHFR_1

InterPro
IPR012259
Family

Dihydrofolate reductase
PIRSF000194	$\"[3-183]T$	Dihydrofolate reductase
PTHR11549:SF1	$\"[15-92]T$ $\"[108-124]T$	DIHYDROFOLATE REDUCTASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.430.10	$\"[4-195]T$	no description
PTHR11549	$\"[15-92]T$ $\"[108-124]T$	DIHYDROFOLATE REDUCTASE
signalp	$\"[1-17]?$	signal-peptide

","BeTs to 13 clades of COG0262COG name: Dihydrofolate reductaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0262 is ------y-vdrlb-efghsn-j-i-wNumber of proteins in this genome belonging to this COG is 1","***** IPB001796 (Dihydrofolate reductase) with a combined E-value of 4.4e-32. IPB001796A 7-37 IPB001796B 42-53 IPB001796C 54-66 IPB001796D 111-120","Residues 1-66 are 72% similar to a (DIHYDROFOLATE REDUCTASE OXIDOREDUCTASE NADP METABOLISM ONE-CARBON TYPE SYNTHASE RESISTANCE PLASMID) protein domain (PD000692) which is seen in DYR_MYCLE.","","-54% similar to PDB:1DF7 DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND METHOTREXATE (E_value = 8.3E_21);-54% similar to PDB:1DG5 DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND TRIMETHOPRIM (E_value = 8.3E_21);-54% similar to PDB:1DG7 DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND 4-BROMO WR99210 (E_value = 8.3E_21);-54% similar to PDB:1DG8 DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH (E_value = 8.3E_21);-53% similar to PDB:2CIG DIHYDROFOLATE REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS INHIBITED BY THE ACYCLIC 4R ISOMER OF INH-NADP A DERIVATIVE OF THE PRODRUG ISONIAZID. (E_value = 3.2E_20);","Residues 3 to 195 (E_value = 8.7e-17) place ANA_0267 in the DHFR_1 family which is described as Dihydrofolate reductase.","","reductase (folA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0268","271490","270597","894","5.50","-7.43","32788","GTGAGCGCAGTCGGCAGTGCCGGCGAGCCCTCGCCATCGGCCGGTCAGTACCCGGTGCTGGCGCGGATGGGGCTCGTCCCTCCGCCAGGCGTAGACGTCGCCTATGAGAACCTCCTGGCCGAGGTTCTGACCAACGGGGCCGCGAAGTCCGACCGTACCGGCACTGGGACGCGTTCGCTCTTCGCCCGCCAGCTGCGCTACGACCTGCGCCGCGGCTTTCCGCGTATCACCACGAAGTTCGTGGCCATGAAGGCCGTCAAGGGTGAACTGCTGTGGTTCTTGCGCGGGGAGACGAACGTGCGCTGGCTCCAGGAGCGGGGAATCACGATCTGGGACGAGTGGGCCGATGACTCCGGTGAGCTGGGGCCGGTCTACGGCTCGCAGTGGCGCTCCTGGCCCACCCGGGACGGGGGCGCGATCGATCAGATCGCCGGGCTCATCGACACGCTGCGTACCGACCCGGACTCACGGCGCATGCTGGTGTCGGCCTGGAACGTCTCCGAGCTGGGGTCCATGGCGCTGGCCCCCTGCCACGCCTTCTTCCAGTGCTACGTGGCCGACGGCCGTCTGAGCCTGCAGATCTACCAGCGCAGCGCCGACCTGTTCCTGGGGGTGCCCTTCAACATCGCCTCTTACGCGCTGCTGGCCCACATGCTCGCCCAGCAGGCGGATCTGGAGCCCGGTGAGCTCATCTGGACCGGCGGGGACTGCCACATCTACGACAACCACGTCGAGCAGGTCCGCACCCAGCTCTCCCGGGTGCCCAGCGCCCACCCCTTCCCCACGCTGCGCCTGGAGCGGGCCGAGTCCATCGACTCCTACGACATGGACGACATCGACGCCTCCCAGGGCTACGAGCACCACCCCACGATCAAGGCCCCGGTCGCGGTATGA","VSAVGSAGEPSPSAGQYPVLARMGLVPPPGVDVAYENLLAEVLTNGAAKSDRTGTGTRSLFARQLRYDLRRGFPRITTKFVAMKAVKGELLWFLRGETNVRWLQERGITIWDEWADDSGELGPVYGSQWRSWPTRDGGAIDQIAGLIDTLRTDPDSRRMLVSAWNVSELGSMALAPCHAFFQCYVADGRLSLQIYQRSADLFLGVPFNIASYALLAHMLAQQADLEPGELIWTGGDCHIYDNHVEQVRTQLSRVPSAHPFPTLRLERAESIDSYDMDDIDASQGYEHHPTIKAPVAV$","Thymidylate synthase","Cytoplasm","thymidylate synthase","thymidylate synthase ","Thymidylate synthase","","Benkovic S.J. On the mechanism of action of folate- and biopterin-requiring enzymes. Annu. Rev. Biochem. 1980. 49:227-251. PMID: 6996564Ross P., O. Gara F., Condon S. Cloning and characterization of the thymidylate synthase gene from Lactococcus lactis subsp. lactis. Appl. Environ. Microbiol. 1990. 56(7):2156-2163. PMID: 2117882Hardy L.W., Finer-Moore J.S., Montfort W.R., Jones M.O., Santi D.V., Stroud R.M. Atomic structure of thymidylate synthase: target for rational drug design. Science 1987. 235(4787):448-455. PMID: 3099389Kaneda S., Nalbantoglu J., Takeishi K., Shimizu K., Gotoh O., Seno T., Ayusawa D. Structural and functional analysis of the human thymidylate synthase gene. J. Biol. Chem. 1990. 265(33):20277-20284. PMID: 2243092","","","

InterPro
IPR000398
Domain

Thymidylate synthase, C-terminal
PD001180	$\"[201-297]T$	Q8G3T9_BIFLO_Q8G3T9;
PR00108	$\"[73-94]T$ $\"[146-165]T$ $\"[172-187]T$ $\"[190-216]T$ $\"[228-245]T$	THYMDSNTHASE
G3DSA:3.30.572.10	$\"[32-297]T$	no description
PF00303	$\"[30-297]T$	Thymidylat_synt

noIPR
unintegrated

unintegrated
PTHR11549	$\"[87-297]T$	DIHYDROFOLATE REDUCTASE
PTHR11549:SF2	$\"[87-297]T$	BIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE

","BeTs to 14 clades of COG0207COG name: Thymidylate synthaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0207 is a-m---y--drlb-efghsn-j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB000398 (Thymidylate synthase) with a combined E-value of 4.1e-107. IPB000398A 73-107 IPB000398B 119-132 IPB000398C 137-171 IPB000398D 182-222 IPB000398E 223-259 IPB000398F 274-297","Residues 35-112 are 78% similar to a (SYNTHASE THYMIDYLATE METHYLTRANSFERASE NUCLEOTIDE BIOSYNTHESIS TRANSFERASE TSASE TS DIHYDROFOLATE REDUCTASE-THYMIDYLATE) protein domain (PD582817) which is seen in Q73VZ2_MYCPA.Residues 50-200 are 46% similar to a (METHYLTRANSFERASE SYNTHASE TRANSFERASE BIOSYNTHESIS NUCLEOTIDE THYMIDYLATE TSASE TS) protein domain (PD511678) which is seen in TYSY_FUSNN.Residues 120-201 are 50% similar to a (METHYLTRANSFERASE TRANSFERASE BIOSYNTHESIS NUCLEOTIDE THYMIDYLATE SYNTHASE TSASE TS SYNTHETASE THYA) protein domain (PD971771) which is seen in TYSY_VIBPA.Residues 172-200 are 93% similar to a (SYNTHASE THYMIDYLATE METHYLTRANSFERASE NUCLEOTIDE BIOSYNTHESIS TRANSFERASE TSASE TS DIHYDROFOLATE REDUCTASE-THYMIDYLATE) protein domain (PD937168) which is seen in Q6AFI0_BBBBB.Residues 201-297 are 77% similar to a (SYNTHASE THYMIDYLATE METHYLTRANSFERASE NUCLEOTIDE BIOSYNTHESIS TRANSFERASE TSASE TS DIHYDROFOLATE REDUCTASE-THYMIDYLATE) protein domain (PD001180) which is seen in Q8G3T9_BIFLO.","","-77% similar to PDB:2TSC STRUCTURE, MULTIPLE SITE BINDING, AND SEGMENTAL ACCOMODATION IN THYMIDYLATE SYNTHASE ON BINDING D/UMP AND AN ANTI-FOLATE (E_value = 3.1E_93);-77% similar to PDB:1QQQ CRYSTAL STRUCTURE ANALYSIS OF SER254 MUTANT OF ESCHERICHIA COLI THYMIDYLATE SYNTHASE (E_value = 9.0E_93);-77% similar to PDB:1AN5 E. COLI THYMIDYLATE SYNTHASE IN COMPLEX WITH CB3717 (E_value = 1.2E_92);-77% similar to PDB:1AOB E. COLI THYMIDYLATE SYNTHASE COMPLEXED WITH DDURD (E_value = 1.2E_92);-77% similar to PDB:1AXW E. COLI THYMIDYLATE SYNTHASE IN COMPLEX WITH METHOTREXATE (MTX) AND 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP) (E_value = 1.2E_92);","Residues 30 to 297 (E_value = 6.5e-131) place ANA_0268 in the Thymidylat_synt family which is described as Thymidylate synthase.","","synthase (thyA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0269","272185","271487","699","10.16","6.43","23792","GTGAACACCTCCCACTCCGGGCGCTCCACAGCGCTGGAACGTGCCCTCGACAAGGCCATCGCCATCCCGGCCTCCCGCATCGAGGAGCGCGTCGCACGGATGCGCCGGGACCGCCCCGGGGCCGACACCGCCGAGCTCGTCGAGATGGCCGGCTCCCGATTCCGGCGGGACGCGGGGCTGTCATCGGGGGCCGTCGGAGCCTCCGCGGCCATCCCGGCCATCGGAACCGGTGCGGCCGCAGCTCTGACAGTCGGCCAGAGCGCCGCCTTCATGGCCTCGGCCGTCACCTATGTTCTGACTGTCGCGGAGATCCAGGGGGTGCACGTCGTCGACGCCGAGCGCCGTCGGGCTCTGGTCCTCTCCGCCCTCCTGGGCAAGGAGGGCTCCGAGGCGGTTCAGGGCCAGCTGGGTCTGTCCTCGATGTTCTGGGCGGCTCAGGTGCTCATGCAGATGCCGCTGCCGTCGGTGAAGTCGATCAACGCCCGCCTCATCAAGCGGGTGGCCAAGCGCTCGGCCGCCAAGGGCGGGGCGCTGGCGCTGGGGCGTCTCCTCCCCTTCGGGATCGGGGCCGCCATCGGCTGGTCGGGGGGCCGGGCGCTGGCCAACCAGGTCATCGAGGGGGCGCAGGCGGCCCTGGGACCAGAGCTCACTGCGCGAGGCTACGTCGACAGCCCCGATGTCGAGGTGATCGAGGCGTGA","VNTSHSGRSTALERALDKAIAIPASRIEERVARMRRDRPGADTAELVEMAGSRFRRDAGLSSGAVGASAAIPAIGTGAAAALTVGQSAAFMASAVTYVLTVAEIQGVHVVDAERRRALVLSALLGKEGSEAVQGQLGLSSMFWAAQVLMQMPLPSVKSINARLIKRVAKRSAAKGGALALGRLLPFGIGAAIGWSGGRALANQVIEGAQAALGPELTARGYVDSPDVEVIEA$","Membrane protein","Membrane, Cytoplasm","POSSIBLE MEMBRANE PROTEIN","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 12-213 are 57% similar to a (MEMBRANE POSSIBLE) protein domain (PD122940) which is seen in Q7U0A5_MYCBO.","","-54% similar to PDB:2HQ1 Crystal Structure of ORF 1438 a putative Glucose/ribitol dehydrogenase from Clostridium thermocellum (E_value = );-65% similar to PDB:2A2M Crystal structure of (np_812058.1) from Bacteroides thetaiotaomicron VPI-5482 at 1.88 A resolution (E_value = );-65% similar to PDB:2A2O Crystal structure of (np_812058.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 2.16 A resolution (E_value = );","No significant hits to the Pfam 21.0 database.","","MEMBRANE PROTEIN","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0270","272927","272259","669","6.31","-4.57","23975","ATGAGGAGAGCCGGGCCACCGCCTGGCTCGCCGAGCACTGACCCGCGTCGTCATCACGCCCCGATCACTCACGGGTCCCACACGGATCACACACGGATCACTGACTGTGCGCTGCGTCGCCCAGCGGCGTTATTCCCGTGCTGCGCCCCTGTCCGCCAGTGGCGCAGCACGGGGCTGTACGCCGATTCCACCGCCGAGTCTCACCCGGTTTCATGGCACGATCAGGCCATGAGCACTTCTAACACAGCCGCTTCCGCCCCTAACGCCGTGTGGGCCGAGCGCGCGGGCACCCGTCAGTACATCGGCCGCAACTCCTCGGGCGCTGAGGTCCGCATCGGGATGGGCCCGGGCGAGTTCTCCCCCGGTGAGCTGATGAAGATCGCGCTGGCCACCTGCAACACCCTGTCCGCCGATCACCGTCTGGCCAAGGCCCTGGGCGAGGACTTCGAGGCCACCGTGGGCTGCTCGACCGTCAAGAACGACGCCGAGGAGCGCTACGAGTCCTTCCAGGTCGAGATCGTCACTGACCTGTCCTCCCTCGACGCCGAGCAGCGCGAGCTGCTCAGCCAGCGGGTCGCCAGCGCCGTGGACCGTCACTGCACCGTGGGCCACACCATCGAGCACGGCGCTTCCTACACGACGACGATCGTCGACCCCAACGAGGACTGA","MRRAGPPPGSPSTDPRRHHAPITHGSHTDHTRITDCALRRPAALFPCCAPVRQWRSTGLYADSTAESHPVSWHDQAMSTSNTAASAPNAVWAERAGTRQYIGRNSSGAEVRIGMGPGEFSPGELMKIALATCNTLSADHRLAKALGEDFEATVGCSTVKNDAEERYESFQVEIVTDLSSLDAEQRELLSQRVASAVDRHCTVGHTIEHGASYTTTIVDPNED$","OsmC family protein","Periplasm, Extracellular","conserved hypothetical protein","hypothetical protein","OsmC family protein","","Gordia S., Gutierrez C. Growth-phase-dependent expression of the osmotically inducible gene osmC of Escherichia coli K-12. Mol. Microbiol. 1996. 19(4):729-736. PMID: 8820643Mongkolsuk S., Praituan W., Loprasert S., Fuangthong M., Chamnongpol S. Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli. J. Bacteriol. 1998. 180(10):2636-2643. PMID: 9573147","","","

InterPro
IPR003718
Family

OsmC-like protein
PF02566	$\"[102-215]T$	OsmC

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 90-205 are 50% similar to a () protein domain (PDA0U4H3) which is seen in Q8G3U0_BIFLO.Residues 119-217 are similar to a (RV2923C/MT2992/MB2948C CGL1062) protein domain (PD711177) which is seen in YT23_MYCTU.","","-50% similar to PDB:2F2E Crystal Structure of PA1607, a Putative Transcription Factor (E_value = );-39% similar to PDB:1PQW Putative enoyl reductase domain of polyketide synthase (E_value = );","Residues 102 to 215 (E_value = 1.7e-09) place ANA_0270 in the OsmC family which is described as OsmC-like protein.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0271","273393","272887","507","5.61","-1.81","17555","ATGAGGAAGACCATCACCATCACCTATCCCGCATCTCCAGTACGCACCGCGCAGATGCTCGCCGACCCCTCCTACCAGGAGACACGGGTCTCACGGGCCGGGCTCGACAACGCCTCGGTGGACGTCGCCCAGCGAGGCCAGGGCTTCGTGGCCACCATCGCCGGAAGCATCCAGCCCTCCCAGCTGCCCTCGGTCGCCTCGAGGTTCGTGCGCTCGGCGGTGTCCTTCTCCGTAGCCGAGTCCTGGGGCGAGCCGAAGGATGACGGCTCACGCTCCGGCGGCTACGACGTGACGGTCAAGAACGCCCCGGTCAAGGTCAGTGCCACCTCCACCATGGCTCCCGCCGCGGAGTCCGCCGGTGAGGCCACCACCGTCACCGTCGACGTCGACCTCAAGGTCACTGTGCCACTGGTCGGCAAGGCCATCGAGGAGAAGGCCATGGGCATGGTGGGCCGCGTCGTCGCCGATGAGGAGAGCCGGGCCACCGCCTGGCTCGCCGAGCACTGA","MRKTITITYPASPVRTAQMLADPSYQETRVSRAGLDNASVDVAQRGQGFVATIAGSIQPSQLPSVASRFVRSAVSFSVAESWGEPKDDGSRSGGYDVTVKNAPVKVSATSTMAPAAESAGEATTVTVDVDLKVTVPLVGKAIEEKAMGMVGRVVADEESRATAWLAEH$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0273","273570","275045","1476","5.79","-12.15","53209","GTGCCTAATCTTCTGCCTAGCGCCTTGAGAGACGCAGTCGACCTCGCCGAGGCCGACCTTGACTGGATCCACCAGCTGGTGGCCGACTGGCAGCTGATTGCGGACCTATCCACCTCTGACCTGGTGCTGTGGGTGCGTACCCGTGCGGGGCGCTTCATCGCTGCGGGCCACACCCGCCCCTCGGGGGGAACCACCGTCCACCTCGAGGACGTCGTCGGGCGGCGCATGCCGGCCTCGCGTGAGGCCAAGGCCATGGAATCACTGTCCACCGCCCAGATCCAGGACGCGGCCGAGCCCTACTGGACCGGTACCGCCGCGGTCCAGGAGGAGTACATCCCGGTCGTTCACGCCGGTACGCCGATCGCCGTCGTGACTCGGGAGACCTCGGTGGGCGTTATCCGGGGCGGGCGCATCGTTGAACGGGAGATGGAGGAGATCGCCGAGGTCCTGTGCCAGATGACCGCCTCGGGCGACTTCCCCATCCAGGGCGCCGGCACCACGATCCGCCACGGCACGCCGCGCGTGGCCGACGGCGTCCTGCGTCTGGACGAGGAGGGGCGGATCGTCTACGTCAGCCCCAACGGGCGCTCCTGCTTCCACCGCCTGGGCATCGAGGGCGAGTTGGAGGGGATCCTGCTGGCCGAGGCCGTCACCTCGATCATTCCCGCCCGTACCCCCGTCGATGAGACGCTGGCCGTGGTCCTCATGGGGAGGCAGGCCTGGCTCACCGAGGTCGAGGTCGGGGGAGTGTTCCTGTCTGTGCGCTCCATCCCCCTGACGCGCAAGGGGCGCCGTTCCGGGGCAGTGCTCCTGGTGCGCGACGTCACCGAGGTGCGTCGGCGCGAGCAGGTCCTGCTCAACAAGGACGCCACCATCCGGGAGGTCCACCACCGGGTCAAGAACAACCTGCAGACCGTCTCGGCGCTGCTGCGTATGCAGGCCCGCCGTGCCTCGAACGAGGAGACCCGCCAGGCTCTGTCCGAGGCCGAGCGTCGGGTGACCACCATTGCCACCGTCCACGACGCTTTGAGCCACAACGTCAATGAGCATGTGGACTTCGATGAGGTCTTCTCCTCCATCCTGCGCATGGCCGCGGTCGTGGCCACGCCCACGGGCGAGGTCAGCACCAAGCTGGAGGGCTCCTTCGGAGTGGTCGACGCTGACACGGCGCAGGCGCTGGCCACGGTGCTGGCCGAGCTTGTGACCAACGCCGTCGAGCACGGCCTCGATGGCCGCGACGGCCGCGTGACGGTCACGGCCCACCGTGACGAGGACCGGCTCGAGGTCCACGTGATGGACAACGGTGCGGGCCTGGCGCCGGACACCCTCATGACCGGACTGGGAACACGGATCGTCACCACGCTTGTGCGCGGGGAACTGCGCGGGGTCATTGATTGGGAGCCTCTGAGCGGAGGGGGCACCGACGTCGTCATTCATGCCCGCCTTCATCAGCGGGCTGCCAGGGCTGAAGCCTGA","VPNLLPSALRDAVDLAEADLDWIHQLVADWQLIADLSTSDLVLWVRTRAGRFIAAGHTRPSGGTTVHLEDVVGRRMPASREAKAMESLSTAQIQDAAEPYWTGTAAVQEEYIPVVHAGTPIAVVTRETSVGVIRGGRIVEREMEEIAEVLCQMTASGDFPIQGAGTTIRHGTPRVADGVLRLDEEGRIVYVSPNGRSCFHRLGIEGELEGILLAEAVTSIIPARTPVDETLAVVLMGRQAWLTEVEVGGVFLSVRSIPLTRKGRRSGAVLLVRDVTEVRRREQVLLNKDATIREVHHRVKNNLQTVSALLRMQARRASNEETRQALSEAERRVTTIATVHDALSHNVNEHVDFDEVFSSILRMAAVVATPTGEVSTKLEGSFGVVDADTAQALATVLAELVTNAVEHGLDGRDGRVTVTAHRDEDRLEVHVMDNGAGLAPDTLMTGLGTRIVTTLVRGELRGVIDWEPLSGGGTDVVIHARLHQRAARAEA$","Two-component system sensor kinase","Cytoplasm, Membrane","histidine kinase","signal transduction histidine kinase","histidine kinase, dimerisation/phosphoacceptor","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[347-479]T$	no description
PF02518	$\"[388-483]T$	HATPase_c
SM00387	$\"[388-484]T$	HATPase_c

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[294-484]T$	HIS_KIN

InterPro
IPR011495
Domain

Histidine kinase, dimerisation/phosphoacceptor
PF07568	$\"[294-374]T$	HisKA_2

InterPro
IPR013656
Domain

PAS fold-4
PF08448	$\"[172-280]T$	PAS_4

noIPR
unintegrated

unintegrated
PTHR23283	$\"[250-478]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF8	$\"[250-478]T$	SENSORY TRANSDUCTION HISTIDINE KINASE

","BeTs to 9 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","No significant hits to the Blocks database.","Residues 16-286 are 56% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM TRANSFERASE 2.7.3.- PROBABLE COMPONENT TWO) protein domain (PD125692) which is seen in Q6AD94_BBBBB.Residues 288-335 are 89% similar to a (KINASE HISTIDINE TRANSDUCTION SENSORY SENSOR TRANSFERASE 2.7.3.- PHOSPHORYLATION TWO-COMPONENT REGULATOR) protein domain (PD428398) which is seen in Q7TWZ2_MYCBO.Residues 292-476 are 45% similar to a (KINASE HISTIDINE TRANSDUCTION SENSORY SENSOR PLASMID PHOSPHORYLATION SIGNAL KINASE COMPONENT) protein domain (PD115206) which is seen in Q9A7N7_CAUCR.Residues 336-394 are 61% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM TRANSFERASE 2.7.3.- TWO PROBABLE COMPONENT) protein domain (PD714323) which is seen in Q6A8A3_PROAC.Residues 399-482 are 70% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM SENSORY TRANSFERASE TRANSDUCTION 2.7.3.- TWO) protein domain (PD005700) which is seen in Q6AD94_BBBBB.Residues 399-478 are 60% similar to a (KINASE HISTIDINE SENSOR TRANSFERASE FACTOR TWO-COMPONENT RSBW B 2.7.3.- ANTI-SIGMA) protein domain (PD524641) which is seen in Q8G5J8_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 172 to 280 (E_value = 4.5e-07) place ANA_0273 in the PAS_4 family which is described as PAS fold.Residues 294 to 374 (E_value = 3.4e-28) place ANA_0273 in the HisKA_2 family which is described as Histidine kinase.Residues 388 to 483 (E_value = 1.2e-16) place ANA_0273 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0274","275392","275144","249","8.20","1.81","9008","ATGGACTGGCGCAGCCAAGCCGCATGTCTCACCGTTGACCCGGAGCTCTTCTTCCCCGTGGGGAACACAGGTCCCGCCATTGCCCAGATCGCCAAGGCAAAAGAGGTGTGCGGCCGCTGTGAGGTGGTGGACACGTGCCTGAAGTGGGCGCTGGAGAACGGTCAGGATGCAGGCGTCTGGGGAGGCATGAGCGAGGACGAGCGCCGTTCCCTCAAGCGCAGGGCGGCCCGGGCCCGCCGGTCCTCCTGA","MDWRSQAACLTVDPELFFPVGNTGPAIAQIAKAKEVCGRCEVVDTCLKWALENGQDAGVWGGMSEDERRSLKRRAARARRSS$","Transcription factor WhiB","Periplasm, Cytoplasm","WhiB-type transcription regulator","transcription factor WhiB","transcription factor WhiB","","","","","

InterPro
IPR003482
Family

Transcription factor WhiB
PF02467	$\"[3-71]T$	Whib

","No hits to the COGs database.","***** IPB003482 (Transcription factor WhiB) with a combined E-value of 4.5e-16. IPB003482A 36-46 IPB003482B 46-62 IPB003482C 68-75","Residues 1-67 are similar to a (REGULATORY TRANSCRIPTIONAL REGULATOR WHIB-LIKE TRANSCRIPTION PROBABLE WHIB-FAMILY FACTOR WHIB WHIB3) protein domain (PD008027) which is seen in Q6AD95_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 71 (E_value = 7.2e-35) place ANA_0274 in the Whib family which is described as Transcription factor WhiB.","","transcription regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0275","278853","275599","3255","7.84","8.31","112748","ATGAAGGAGGGGACGCTCCTGCGGCTGGGGAACAGCGTGCTCGAGCTGCGTAGGCGCCCCTGTGACCTGGTGGTGGCGGCACCTGCAACGTCGGGATCGTCAACGGCGTGGTTGATGGCGGGCTCACTGGTCTGTGTCCTGGTCATGGCCGGCTCGGCGGTCATCGCGCTCAGGACGGGGAGCCGCGGCGCGATGGGCATGGTCATGGTGGCGCCGATGGTCGCGATGACGATCATGCGCCTGGTGCCCTTCCTGCAACAACGGAGAACCCAGCGCGCCGGGCGCACCGGGCGGGCCGGTGGAGGCCGATGGCACGCTCGCCGGCGCCGCCGGGGCGGCCGACCGGGTTGGAGGCGCGGAGAGCCGGACCCTGCCACGATGCTGCTGGCCGTCGCCGCGCGCTCCAGCATGTCTCAGTCCGTCCATGGCCCCCAGGCCGAGGGCTCGACGACGCCCGCCTCCGCCGGTCAGGAGAACCTGGCCGCATGGAGTGCCGGGCGACGACGACGCTGCGTCCTGTCGCTCTGCGACGGTGAGAGCCTGGCCCTGGTGGGCAGGAGCGCTGGCAGTGCGCTCAGATGGTGGTGCGCCCAGCTCCTGGCCCGCGATGAGGTCCGGTTGACCATACTGGATGTCCCACCGGGTGCCCCGTCGGATGAACGCGCCGGCTATCGGGGCGGTGTGGAGCGTGAGGAGACAGGCGACCGGCTGGGGGTCCGCCTCTCCTGGGGCCCGCAGGCCCACCCTCGCTGCGCGCAGATAGTGACCTGCTCTCATGACGGGGTCCCACCCCAGGCGCTGAGCACGCGGCCCGCTCCGGATGGGGCGCCGTCGTGCTCACCGACCTGGTGGGGGGCGGTTTGTCACCTGAGCCGCTCCCGGATCAGGTCACCACGCGGGTCCTCGTCCCAGGCCGAAGGCATTCCCGATCTGGTCCCCCTCAGCACGGTCATGGACGACCTCGACGCCCACGAGCTGCGGGCACGGTGGGAGGATCAGACGCACTCGCCGGCCCGGGGCGCGCAGGCGCTGTCGGCAGTGCTCGGAGTGGGAGTACGAGGACCGGTGCGTGCCGACCTGGTGGCGGACGGTCCGCACGCCCTGCTGGCCGGGACCACGGGCTCAGGCAAGTCCGAGCTGCTCATCTCGTGGCTGGTGCAGCTGGCGCTGAGCCGAGCGCCGGATCGCCTCACCCTGGTCCTCGTCGACTACAAGGGCGGCGCCGCCTTCGGCCCTCTGGCCGGCCTGCCGCACACGGCCGGGGTGCTGACGGATCTGGATCCCGCCGGCACCCAGCGCGCCCTGTCCTCCTTGGAGGCCGAGGTGCGCCGCCGCGAGCGGATCCTGGCCGCACACGGCGCCAAGGACCTGTCCTGCCTGCCACCGCAGGTTGTCGTGCCCGATCTGGTGGTAGCGGTGGACGAGTTCGCCACCTTGGCCGGCGAGCACGCAGAGGTCCTGGAGTCCCTGGTGCGTATCGCCGCCCAAGGGCGCAGCCTGGGAATCCACCTCATTCTGGCCACGCAGCGCCCTCAGGGGGCAATATCCCCGGCGATTCGGGCCAACACCTCCTTACGAGTGTGCCTGCGGGTGCTCGACGCCGCTGACTCCCGGGACGTCCTGGGACACGACGGGGCCGCCCGGCTCGGTCATCATCCCGGCAGGGTCCTGGTCAGTGGCGCCGGCGGCGCTCAAGACAGCGCCGCTGACCGGCAAGGTCTCGGCGACGGGGCCAGTGGTTCTCCCGACCCTGGCAGTCAGGTGCTTCAGGCCCCCTGGTGCGGCTCGGCGAGTGAGGTTCAGGGGATCGTCGACCTCATCTCACGGGCAGCCGAGGGTCACGCCGCCCCGTGGCGTCCCTGGGCGCCGGCCCTGCCCACCTCGATCAGCGCGGCCGGGGCACTCGAGCTGGTTCGGCTCCGAGGCCCCCAGGCACCGAGTGAGCGTGAGGAGCAGGAGCCGCTGGTCACGGCCGACCCTGCCGACCACGCTCCACTGTCCGGGCACGACGATGACCGTCTTCTCCTGGCCGTGACCGACCTTCCTCGCCGGCAGAGCCTGGGGGTGTGGCAGTGGCGGGTCACTCGCCCGCTGCTGGTCCTCGGGGCCCCGAGGTCGGGGCGCTCCACTCTCGTTGCCTCCGCAGCGACGGCGGCGCTGGGCTCGGGCAGAGGGGTGCACCTGTGCGGCTTCGCTCCCACAACCACTATCGCCTCCGACCAGACCACGGACATGGCCTGCTCCGTGCGCGGGCTCCTCAGCCACCCCGGGCTGGGCACCGTGGTCGGTACGGAGGACCCGCGACGTCTGACCCGGCTGTGGGGACTCGCCGCCAGCGGACACCTCGGCGGGGACCTATTGTGCCTCGACAACGTCGACGCTCTCGTCCCGACAATTGATGAGGTGCTGGGACCCGGCCAGGGCAACGCCCTGTTGGAGGCCGTCATCCGTACCGCCTCCGCGACGGGCACTCCCCTGCTGCTGACCGCCCCCTTGGCAGCCTCCACCTCCCGATGGGCCGCCTCCATGGGGCTCAGGCTGGTTCTCGGTGCGGCCACCGGCACACAGGCCGCTCTCGCTGGTCTTCCACGCGGGGTGGTCACCGGCGGCGCCCCGGGGCGCGGCGTCATCCTGGACGGGGCGACGACAACCGCCTGCCAGATCGTGCTCCGTGAGGACTGCCCGGGATCCGCCTGCGAGCGCAACGTCGGCCACGCGCTACGACTCGAACCACTGCCGACCCGGCCCACCTGGGAGGACGTCCCAGAGGGCACCTGGGCTGTGGGAGGGGACGCGGCTGCACCCGTCGCGCTTCCGGCTCACACCAGCGTCCTGGTCACTGGGCCGCCCGGCTCGGGGCGCTCCACGGCACTGCGAGCACTGGCCCGGGCGATGGCCTCCGACCCCCTCGTCGTTGACGACCTGGACCTGGCGGACATCACCACGACCACTCAGGTGGAGGCCGCGCTAGCACGCTCCGAGGTGGTCCTGGCCTCCGCCTCGACGGAGAAGGTCGCCACGACCTTCCGCGGCCCGATCTCCACCATGCGTGAGCGTGAGGCACTCGTCGTGCTGTGGCCCGGCATGCGCCCTGCCGATCAGGCCGCCGGCATCTCCTTGCGGACGGTCACCGACCCCAGAGCGATGACGCTGCCCGGTCGTGGAGCACTCGTCTATCGCGGAACGTGCCTGCCCATTCAGATCGTGCTGCCCCAGCCCGAAGACGACGATCATCCTATTGAATGCCCTGTTTAA","MKEGTLLRLGNSVLELRRRPCDLVVAAPATSGSSTAWLMAGSLVCVLVMAGSAVIALRTGSRGAMGMVMVAPMVAMTIMRLVPFLQQRRTQRAGRTGRAGGGRWHARRRRRGGRPGWRRGEPDPATMLLAVAARSSMSQSVHGPQAEGSTTPASAGQENLAAWSAGRRRRCVLSLCDGESLALVGRSAGSALRWWCAQLLARDEVRLTILDVPPGAPSDERAGYRGGVEREETGDRLGVRLSWGPQAHPRCAQIVTCSHDGVPPQALSTRPAPDGAPSCSPTWWGAVCHLSRSRIRSPRGSSSQAEGIPDLVPLSTVMDDLDAHELRARWEDQTHSPARGAQALSAVLGVGVRGPVRADLVADGPHALLAGTTGSGKSELLISWLVQLALSRAPDRLTLVLVDYKGGAAFGPLAGLPHTAGVLTDLDPAGTQRALSSLEAEVRRRERILAAHGAKDLSCLPPQVVVPDLVVAVDEFATLAGEHAEVLESLVRIAAQGRSLGIHLILATQRPQGAISPAIRANTSLRVCLRVLDAADSRDVLGHDGAARLGHHPGRVLVSGAGGAQDSAADRQGLGDGASGSPDPGSQVLQAPWCGSASEVQGIVDLISRAAEGHAAPWRPWAPALPTSISAAGALELVRLRGPQAPSEREEQEPLVTADPADHAPLSGHDDDRLLLAVTDLPRRQSLGVWQWRVTRPLLVLGAPRSGRSTLVASAATAALGSGRGVHLCGFAPTTTIASDQTTDMACSVRGLLSHPGLGTVVGTEDPRRLTRLWGLAASGHLGGDLLCLDNVDALVPTIDEVLGPGQGNALLEAVIRTASATGTPLLLTAPLAASTSRWAASMGLRLVLGAATGTQAALAGLPRGVVTGGAPGRGVILDGATTTACQIVLREDCPGSACERNVGHALRLEPLPTRPTWEDVPEGTWAVGGDAAAPVALPAHTSVLVTGPPGSGRSTALRALARAMASDPLVVDDLDLADITTTTQVEAALARSEVVLASASTEKVATTFRGPISTMREREALVVLWPGMRPADQAAGISLRTVTDPRAMTLPGRGALVYRGTCLPIQIVLPQPEDDDHPIECPV$","Cell division protein FtsK/SpoIIIE","Cytoplasm, Membrane","3C3.20c protein","FHA domain containing protein","cell divisionFtsK/SpoIIIE","","Begg K.J., Dewar S.J., Donachie W.D. A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 1995. 177(21):6211-6222. PMID: 7592387","","","

InterPro
IPR002543
Domain

Cell divisionFtsK/SpoIIIE
PF01580	$\"[328-513]T$	FtsK_SpoIIIE
PS50901	$\"[353-538]T$	FTSK

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[363-533]T$ $\"[694-895]T$ $\"[940-1074]T$	AAA

noIPR
unintegrated

unintegrated
PTHR22683	$\"[332-549]T$	SPORULATION PROTEIN RELATED
PTHR22683:SF1	$\"[332-549]T$	DNA TRANSLOCASE FTSK
tmhmm	$\"[37-57]?$ $\"[67-85]?$	transmembrane_regions

","BeTs to 14 clades of COG1674COG name: DNA segregation ATPase FtsK/SpoIIIE and related proteinsFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG1674 is ---------drlb-efghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB002543 (Cell divisionFtsK/SpoIIIE protein) with a combined E-value of 2.8e-24. IPB002543A 365-378 IPB002543B 424-450 IPB002543C 490-519 IPB002543A 942-955","Residues 326-403 are 64% similar to a (SCO2975 ATP-BINDING) protein domain (PDA0D108) which is seen in Q9L060_STRCO.Residues 354-403 are 70% similar to a (ATP-BINDING) protein domain (PD838416) which is seen in Q82D83_STRAW.Residues 359-457 are similar to a (ATP-BINDING CELL DIVISION DNA FTSK TRANSMEMBRANE TRANSLOCASE DNA-BINDING CHROMOSOME PARTITION) protein domain (PD002076) which is seen in Q9L0T6_STRCO.Residues 490-558 are 70% similar to a (ATP-BINDING CELL DIVISION FTSK DNA TRANSMEMBRANE TRANSLOCASE DNA-BINDING CHROMOSOME PARTITION) protein domain (PD037665) which is seen in Q9L0T6_STRCO.","","-45% similar to PDB:2IUT P. AERUGINOSA FTSK MOTOR DOMAIN, DIMERIC (E_value = 2.3E_15);-45% similar to PDB:2IUU P. AERUGINOSA FTSK MOTOR DOMAIN, HEXAMER (E_value = 2.3E_15);-43% similar to PDB:2IUS E. COLI FTSK MOTOR DOMAIN (E_value = 2.2E_13);","Residues 328 to 513 (E_value = 3.3e-35) place ANA_0275 in the FtsK_SpoIIIE family which is described as FtsK/SpoIIIE family.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0276","278968","279324","357","9.43","6.25","12666","ATGACGGCGGGAGACCAAGGGATCGCTGAGGACCTCGCCGCGGCCCAGGAGGGCGCCGTCCCTGACGGCCATTACCAGGCCCAGGTCGGGACCGTCCAGGACGGCAAGGTGCCACGGGCCGGCCACGGCGGCCAGAGCCGCGTCCGCTGCCGCCTCACCTGCCGAGCGTCGGAACAACGAGGACGAGGCCTCTCCCGGCAGGAACGAGTGGAGGTCCAGGACGTCGGCGGTAGAGCTCATTCGTCCAGAATCGCCGTAGGGGCTCGTTGCGTCATTTTCAGGCAATCCCGGGTGTGGACAACCTCGCCGTTCGGGGATGCTCATGGTCACTGTGGACACTGGCGCAACCCGGTGTGA","MTAGDQGIAEDLAAAQEGAVPDGHYQAQVGTVQDGKVPRAGHGGQSRVRCRLTCRASEQRGRGLSRQERVEVQDVGGRAHSSRIAVGARCVIFRQSRVWTTSPFGDAHGHCGHWRNPV$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0277","279349","281805","2457","5.48","-20.13","88821","ATGACTGACACCGATGCGCCTCGCGGCTCCGCTCCCGCCCCGGCTCTCTCCTCGGCACGCTCCGATCAGCGCGGCCCCGTGGATCTGAGTGCCATCCCCTCCGCCGCCCGGGAGCGCTGGAGCGAGCTGGTGCGTGACATCGAGGCCGCCCGCGACGCCTACTACAACGCCATCGATGCCGAGAGCCCCCTGTCCGACGCCGACTACGACCTCCTCTACCGTGAGCTGGAGGGGCTGGAGGCGGCTTACCCCCTCCTGGCCCGAGCCGGATCACCGACCCGCTCCGTGGGCGGGCGCGCCGTCACCGACTTCGCCCCCGCCCCGCACCACGAGCGCATGTACTCCCTTCAGGATGTCTTCTCCCTCGACGAGGTCCAGGAGTGGGCCGAGCGCATGGTCGCTGAGACCGGGGTCGGTGACGACGAGCTCGCCATGACCGCCGAGGTCAAGATCGACGGCCTGGCCGTAGCCCTGACCTACGAGGACGGCATCCTCACCCGGGCCGCTACCCGGGGGGACGGCACCACCGGTGAGGACGTCACCGGCAATGTGCGCACCATCGCCTCGGTCCCCCTGGTCCTGGCCGGCGACGCCCACCCCTCCCTGCTCGAGGTGCGCGGCGAGGTCTACTTCCCCACCCAGGAGTTCGAGGCCTTCAACGAGGAGCGCCGAACCCTCAACCTGCAGCGGCAGGCCGACGGCGCCCCCCTCCTGCAGGTCTTCGCCAACCCGCGCAACGCGGCTGCCGGCTCGCTGCGCCAGAAGAACCCCGCCGTTACCGCTTCCCGGCCCCTGGCGATGATCGCCCACGGGGTCGGTGCGATCACCCCTGCACCGGGGGAGAGGCTCCCTACCCGCCAGCACGAGTGGTATGAGCTGCTGGCCGGCTGGGGGCTGGCGGTATCCCCCTACAACGCCGTGGTGAGGGGACGCGCCGAGCGCGAGGCCTACATCGAGCGCTACGCCACCCACCGCCACGACCTCATCCACGAGATCGACGGCATCGTCTTCAAGCTCGACGACCACTCCCTTCAGCGCCGCCTGGGGCACACCTCCCGAGTGCCCCGCTGGGCCACCGCCTACAAGTACCCGCCCGAGGAGGTACGCACCCGGTTGCTGGACATCGCCGTCCAGGTCGGGCGCACCGGTCGCGTCACGCCCTTCGGCATGATGGAGCCGGTCCTGGTCGCCGGCTCGACGGTGGCACGCGCCACCCTTCACAACGCCACCGAGGTGGCCCGCAAGGGCGTGCGCATCGGCGACATGGTCATCGTGCGCAAGGCCGGCGACGTCATCCCCGAGATCCTCGGGCCGGTCGCCGACCTGCGTGACGGCAGCGAGAGGGACTTCGTCATGCCGACGCACTGCCCGTCCTGCGGCACCGAGCTGGCGCCGGCCAAGGCCGGCGACGTCGACCTGCGCTGCCCTAATACCCGGTCCTGCCCCGCCCAGCTCACTGAGCGGATCGCTCACATCGGTTCCCGGGGCGCCCTCGACGTCGAAGGGCTGGGAGACGAGGCCGCCGGCGCCCTGACCCGACCCGACGCCGGACGCCGTGAGGCCCTGACCGCGCTCGCGGCGGGGCGGAGCCTGGAGACCGAAGGCGGACGACTCAGCCTGCCGCCCGGCGAGCTCGACTCCCTCCACGTCTCCCAGCGGGTGGAGGCCGTTGAGGAGCTCCTGAGGCAGGCGGGGATCACCGAGCAGACACCGGTGCTCACCGGCGAGGCCGCCCTGTTCGACCTGACCGAGGACGACCTGCGCGAGGTCTTCGTCTGGCGCCCCGTCTCCCGTCGCGGGGTCCCCACCGGGGACTGGCGCCTGAGCCGGTTCTTCTGGACCAAGCAGACCTATGACGCCGACGGACGGGTCAAGAAGGCGACGGTGCCGGGGAAGAACGCCACCGCCATGCTCTCCCAGCTCCGCCAGGCCCGCAGCCGCCCGCTGTGGCGCATCCTGGTGGCCCTGTCGGTGCGCCACGTCGGTCCTACGGCCGCTCGGGCCCTGGCGGCGCGCTTCAGGTCCTTGGAGGCCCTGTGTCAGGCCGATGTCGCCGAGCTGGCCGAGGTCGACGGTGTCGGCCCCACCATTGCCGAGTCCTGGGTCAGGTGGCGTGAGGTCGACTGGCACCGCGAGATCCTCAGCCGCTGGGAGGCCGCCGGGGTCCGTACCTGGGAGGAGGACTCGGAGGAGCAGGAGGAGCCGGCGCGGACCCTGGAGGGCCTGACCGTCGTCGTCACCGGCTCCCTGGAGGGATTCACCCGGGACAGCGCCAAGGAGGCCATCGTCTCGCGCGGCGGCAAGGCATCGGGCAGCGTCTCGAAGAAGACGAGCTTCGTCGTCGTGGGGGACAAGGCGGGCTCCAAGGAGACCAAGGCCCGCGAGCTGGGACTGACGATCCTTGACGAGGAGGGCTTCGTGGCGCTCCTGGAAGGCGGACCCCAGGCGGTCTCCTGA","MTDTDAPRGSAPAPALSSARSDQRGPVDLSAIPSAARERWSELVRDIEAARDAYYNAIDAESPLSDADYDLLYRELEGLEAAYPLLARAGSPTRSVGGRAVTDFAPAPHHERMYSLQDVFSLDEVQEWAERMVAETGVGDDELAMTAEVKIDGLAVALTYEDGILTRAATRGDGTTGEDVTGNVRTIASVPLVLAGDAHPSLLEVRGEVYFPTQEFEAFNEERRTLNLQRQADGAPLLQVFANPRNAAAGSLRQKNPAVTASRPLAMIAHGVGAITPAPGERLPTRQHEWYELLAGWGLAVSPYNAVVRGRAEREAYIERYATHRHDLIHEIDGIVFKLDDHSLQRRLGHTSRVPRWATAYKYPPEEVRTRLLDIAVQVGRTGRVTPFGMMEPVLVAGSTVARATLHNATEVARKGVRIGDMVIVRKAGDVIPEILGPVADLRDGSERDFVMPTHCPSCGTELAPAKAGDVDLRCPNTRSCPAQLTERIAHIGSRGALDVEGLGDEAAGALTRPDAGRREALTALAAGRSLETEGGRLSLPPGELDSLHVSQRVEAVEELLRQAGITEQTPVLTGEAALFDLTEDDLREVFVWRPVSRRGVPTGDWRLSRFFWTKQTYDADGRVKKATVPGKNATAMLSQLRQARSRPLWRILVALSVRHVGPTAARALAARFRSLEALCQADVAELAEVDGVGPTIAESWVRWREVDWHREILSRWEAAGVRTWEEDSEEQEEPARTLEGLTVVVTGSLEGFTRDSAKEAIVSRGGKASGSVSKKTSFVVVGDKAGSKETKARELGLTILDEEGFVALLEGGPQAVS$","DNA ligase, NAD-dependent","Cytoplasm","DNA ligase, NAD-dependent","DNA ligase; NAD-dependent ","DNA ligase, NAD-dependent","","Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Aravind L., Walker D.R., Koonin E.V. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res. 1999. 27(5):1223-1242. PMID: 9973609Provvedi R., Dubnau D. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol. Microbiol. 1999. 31(1):271-280. PMID: 9987128Doherty A.J., Serpell L.C., Ponting C.P. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 1996. 24(13):2488-2497. PMID: 8692686","","","

InterPro
IPR001357
Domain

BRCT
PF00533	$\"[734-810]T$	BRCT
SM00292	$\"[736-813]T$	BRCT
PS50172	$\"[734-811]T$	BRCT

InterPro
IPR001679
Family

NAD-dependent DNA ligase
TIGR00575	$\"[43-806]T$	dnlj: DNA ligase, NAD-dependent
PS01055	$\"[150-179]T$	DNA_LIGASE_N1
PS01056	$\"[379-394]T$	DNA_LIGASE_N2

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[653-672]T$ $\"[685-704]T$	HhH1

InterPro
IPR004149
Domain

Zinc-finger, NAD-dependent DNA ligase C4-type
PF03119	$\"[454-483]T$	DNA_ligase_ZBD

InterPro
IPR004150
Domain

NAD-dependent DNA ligase, OB-fold
PD003944	$\"[366-439]T$	Q8FPZ7_COREF_Q8FPZ7;
PF03120	$\"[368-449]T$	DNA_ligase_OB

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[367-439]T$	no description

InterPro
IPR013839
Domain

NAD-dependent DNA ligase, adenylation
PF01653	$\"[34-366]T$	DNA_ligase_aden

InterPro
IPR013840
Domain

NAD-dependent DNA ligase, N-terminal
SM00532	$\"[35-497]T$	LIGANc

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.20	$\"[645-727]T$	no description
G3DSA:1.10.287.610	$\"[31-95]T$	no description
G3DSA:3.30.470.30	$\"[154-300]T$	no description
G3DSA:3.40.50.10190	$\"[732-810]T$	no description
PIRSF001604	$\"[33-813]T$	DNA ligase (NAD), LigA type
PTHR11107	$\"[31-548]T$ $\"[625-813]T$	BRCT DOMAIN-CONTAINING PROTEIN

","BeTs to 18 clades of COG0272COG name: NAD-dependent DNA ligase (contains BRCT domain type II)Functional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0272 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001679 (NAD-dependent DNA ligase) with a combined E-value of 3.7e-176. IPB001679A 56-92 IPB001679B 93-131 IPB001679C 147-191 IPB001679D 200-211 IPB001679E 241-257 IPB001679F 348-398 IPB001679G 452-461 IPB001679H 481-504 IPB001679I 627-676 IPB001679J 754-803***** IPB013725 (DNA replication factor C-terminal) with a combined E-value of 8.3e-16. IPB013725A 727-755 IPB013725B 756-781 IPB013725C 781-813","Residues 39-363 are 61% similar to a (DNA LIGASE NAD REPAIR REPLICATION NAD-DEPENDENT POLYDEOXYRIBONUCLEOTIDE SYNTHASE NAD LIGASE) protein domain (PD550531) which is seen in DNLJ_STRCO.Residues 249-364 are 46% similar to a (DNA LIGASE NAD REPAIR REPLICATION) protein domain (PD711119) which is seen in Q83HX4_TROW8.Residues 366-439 are 86% similar to a (DNA LIGASE NAD REPAIR REPLICATION NAD-DEPENDENT POLYDEOXYRIBONUCLEOTIDE SYNTHASE NAD LIGASE) protein domain (PD003944) which is seen in Q8FPZ7_COREF.Residues 441-655 are 55% similar to a (LIGASE DNA) protein domain (PD987136) which is seen in Q6A7A2_PROAC.Residues 459-727 are 49% similar to a (DNA LIGASE REPAIR NAD REPLICATION NAD-DEPENDENT POLYDEOXYRIBONUCLEOTIDE SYNTHASE NAD LIGASE) protein domain (PD041672) which is seen in Q8NR20_CORGL.Residues 733-806 are 62% similar to a (DNA LIGASE REPAIR REPLICATION POLYDEOXYRIBONUCLEOTIDE ATP-BINDING SYNTHASE RECOMBINATION NAD NAD) protein domain (PD799442) which is seen in DNLJ_THEFI.Residues 739-783 are 93% similar to a (DNA LIGASE REPLICATION NAD REPAIR NAD-DEPENDENT POLYDEOXYRIBONUCLEOTIDE SYNTHASE NAD SUBUNIT) protein domain (PD002763) which is seen in Q8FPZ7_COREF.","","-56% similar to PDB:2OWO Last Stop on the Road to Repair: Structure of E.coli DNA Ligase Bound to Nicked DNA-Adenylate (E_value = 2.0E_88);-55% similar to PDB:1V9P Crystal Structure Of Nad+-Dependent DNA Ligase (E_value = 5.8E_88);-55% similar to PDB:1DGS CRYSTAL STRUCTURE OF NAD+-DEPENDENT DNA LIGASE FROM T. FILIFORMIS (E_value = 1.5E_83);-58% similar to PDB:1ZAU Adenylation domain of NAD+ dependent DNA ligase from M.tuberculosis (E_value = 5.9E_64);-53% similar to PDB:1TAE Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal (E_value = 2.7E_53);","Residues 34 to 366 (E_value = 6.8e-124) place ANA_0277 in the DNA_ligase_aden family which is described as NAD-dependent DNA ligase adenylation domain.Residues 368 to 449 (E_value = 1e-45) place ANA_0277 in the DNA_ligase_OB family which is described as NAD-dependent DNA ligase OB-fold domain.Residues 454 to 483 (E_value = 4.7e-12) place ANA_0277 in the DNA_ligase_ZBD family which is described as NAD-dependent DNA ligase C4 zinc finger domain.Residues 734 to 810 (E_value = 6.2e-17) place ANA_0277 in the BRCT family which is described as BRCA1 C Terminus (BRCT) domain.","","ligase, NAD-dependent (ligA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0278","283718","281892","1827","5.12","-17.07","63362","ATGAGCAGCAATACTTCCCCCACTGGTGCGCAGCACCAGGGAGAAGCCTCCCAGAGCGAGACCACTGTGCTCAGCACGCCCTATGGGCAGCCCGAAGGCGTGCGTCGTCAGTCCGTCTTCCAGGCGGCTGCGCGAGCCGCGGGACCGCATGCGCATTCCGCTGGCACCGCCGCAGGCGTGATGAGCGCGGAGCAGAGCAGCACCGAGGAGATCGAGGCGGTCGCCCCGGCAGCGGCCTCAGAACCGGTCTCCAGCAGCGAGCCGACCCTCAAGGATGCTTCGCGCACCGAGCGCACCGAGGTCACTGCCGGCACCGACCGTCCCTCCGCAGTCGTCCCGGCCCCCTCCTCCTTCCCGGCGGTCACATCCCCCGAGGCGGAGTCGTCCCGGGAGGAGCCCCGGCGTCGTCGCCGCTGGCCCCTGGGGGTCGCGGCCGCCGCGCTGCTCCTGCTGGGCGTCGTCGGCGCCGGAGGCTATGCCTACGCCGCCCACTACGACGGCCGGGCCGTCCCGGGGACCACCGTGGCCGGCACCGACGTCTCCGGCAAGAGCCGGCAGGAGATCGTGGCGACCATTGAGGAGCGCGCCAAGAACACCAAGGTCGGCATCTCCGGAGACGTCACCGCCAGCGCCTCCCTGGCAGACCTGGGAACCACCGTGGACGCCCAGGCCACCGCTGACGCCGTCATGGCCCGGGGTGACACGCTCGGCGAGAAGCTCCGCGCCCTGGTCTCCCAGGGCAAGAGCGAGGTCCCGGTGGTCTCCACCACTGACAAGACCAAGGTGAGCGGCTACGCCACCTCCCTGATCCCCGAGGACCGTGCCAAGGCACGCAACGCCACCGTGATCCTCAGCGAGGACGGCACCACCTTCACCACCACGAGCTCGGCCAAGGGCTCCTCCCTGGACGCCAACGCCCTGGCCCAGGCCGCGCAGAAGGCCGCCACGTCCCTGGACTCGGCATCGATCTCCCTGAAGATCACGGACGCCGCGCCGAAGGTCTCCGACTCCGACGCCCAGAAGGTCGCTGACAAGGCCAACAGCTGGGTCTCCCAGGACGTCACCATCACCATGGGTGAGGACTCCTACACGGCGGAGAACACGGACAAGGCCTCGTGGATCAAGATCACCAACTCGACCGAGTCCGCCCCGACCATCACCGTGGACTCCTCAAAGGTCTCTCAGTGGGTCAAGTCACAGGCTGAGGAGGCCAGTTCCGAGCCCGTCACCGGCGAACGTAACGTCAATGCCAGCGGCCAGGTGGTCTCCACCCCGACCGAGGCCAAGGACGGCAAGACCGTCAACAACGCCGACGCGGTGACCACCGCGATCACGCAGTCCCTGGGCAGCAACAAGGCCTACTCCGGCTCCTTTGAGGCGACGACGGTCAAGGCGGAGTGGAAGGAGCGCACCATCGCCAATGGTGCGGAGAAGCTGCCCTACCAGGCCGCTCCGGGTGAGAAGTGGGTCGACCTCAACCTGTCGAACAAGACGGTGACCGCCTACGAGGGGGCGACCGTCGTGCACGGCCCGGTCTCCATTGTCGACGGCGCCGCCGAGACCCCGACGGTGACCGGCACCTACAAGGTCTACCTGCAGTACGAGTCCCAGACCATGCGCGGTGAGAACGCCGACGGCTCCCCCTACGTCGCCGAGAACGTCCCGTGGGTGAGCTACTTCTACAGCGGCTACGCCTTCCACGGCGCGGGATGGCGCTCCAGCTTCGGGTACTCCGATTCCCACGGCTGCGTCAACATGCCGGTCTCCGAGGCGCAGTGGATCTACAACTGGGTCGATACGAACACGGTGGTCCAGAGCCACTACTGA","MSSNTSPTGAQHQGEASQSETTVLSTPYGQPEGVRRQSVFQAAARAAGPHAHSAGTAAGVMSAEQSSTEEIEAVAPAAASEPVSSSEPTLKDASRTERTEVTAGTDRPSAVVPAPSSFPAVTSPEAESSREEPRRRRRWPLGVAAAALLLLGVVGAGGYAYAAHYDGRAVPGTTVAGTDVSGKSRQEIVATIEERAKNTKVGISGDVTASASLADLGTTVDAQATADAVMARGDTLGEKLRALVSQGKSEVPVVSTTDKTKVSGYATSLIPEDRAKARNATVILSEDGTTFTTTSSAKGSSLDANALAQAAQKAATSLDSASISLKITDAAPKVSDSDAQKVADKANSWVSQDVTITMGEDSYTAENTDKASWIKITNSTESAPTITVDSSKVSQWVKSQAEEASSEPVTGERNVNASGQVVSTPTEAKDGKTVNNADAVTTAITQSLGSNKAYSGSFEATTVKAEWKERTIANGAEKLPYQAAPGEKWVDLNLSNKTVTAYEGATVVHGPVSIVDGAAETPTVTGTYKVYLQYESQTMRGENADGSPYVAENVPWVSYFYSGYAFHGAGWRSSFGYSDSHGCVNMPVSEAQWIYNWVDTNTVVQSHY$","ErfK/YbiS/YcfS/YnhG family protein","Extracellular, Cellwall","ErfK/YbiS/YcfS/YnhG family","hypothetical protein","ErfK/YbiS/YcfS/YnhG family protein","","","","","

InterPro
IPR005490
Family

ErfK/YbiS/YcfS/YnhG
PF03734	$\"[485-606]T$	ErfK_YbiS_YhnG

noIPR
unintegrated

unintegrated
tmhmm	$\"[143-163]?$	transmembrane_regions

","BeTs to 5 clades of COG1376COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1376 is --------v-r-bcefg--n-j----Number of proteins in this genome belonging to this COG is 1","***** IPB005490 (ErfK/YbiS/YcfS/YnhG) with a combined E-value of 5.4e-13. IPB005490C 564-607","Residues 8-471 are 37% similar to a (NRRL STRAIN LACTIS KLUYVEROMYCES E CHROMOSOME Y- Y-1140) protein domain (PDA0F960) which is seen in Q6CPZ4_EEEEE.Residues 164-568 are 47% similar to a () protein domain (PD721135) which is seen in Q8G566_BIFLO.Residues 345-604 are 40% similar to a (FAMILY EXPORTED UNCHARACTERIZED CONTAINING SECRETED LP_0536 PROTEIN ERFK ERFK/YBIS/YCFS/YNHG) protein domain (PD564962) which is seen in Q88Z40_LACPL.Residues 560-602 are 67% similar to a (SIGNAL PRECURSOR ERFK/YBIS/YCFS/YNHG ERFK EXPORTED YBIS PERIPLASMIC FAMILY YCFS ERFK/SRFK) protein domain (PD398654) which is seen in Q55969_SYNY3.","","-41% similar to PDB:1ZAT Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution (E_value = 1.9E_11);-40% similar to PDB:2HKL Crystal structure of Enterococcus faecium L,D-transpeptidase C442S mutant (E_value = 2.7E_10);","Residues 485 to 606 (E_value = 1.4e-06) place ANA_0278 in the ErfK_YbiS_YhnG family which is described as ErfK/YbiS/YcfS/YnhG.","","family ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0280","283943","284449","507","4.89","-8.40","17857","ATGAGGCTGTGTGAGATCGCACGAATCTGGTATCGGTTCAGTTTCGCAGGGCCCCGTGGGCGTGGCGTCCACGTCCCTCCTGCGGGGCAAGAATGGGGCAAGGATGTCGATGAGGGCAGGTCCCTCGCCGTCGAACCCGCCGCGACGTGTTGTCGCCGTGATACGGCCGTAGCCCGGCTCGACCCGGCTAGACTCCACACCATGTCTGCTATTTCCACTGATGAGGTCGCACGTGTCGCGGCACTGGCTCGGGTCGCCCTGAGCGATGAGGAGGTGTCGCGCCTGGCCGGAGAGCTGGACGCGGTCGCCTCCTCCTTCGCCAGGGTCACGAGCGTGGTCACGCCCGACCTGCCTGCGACCTCCCACCCCGTGCCCCTGACCAACGTGCTGCGTGAGGACGTTCCGGCCCCCACGCTCGACGTCGACGAGCTCCTGGCCGGCGCGCCGGCCAGCGAGGACTCCATGTTCCTCGTTCCGCAGATCCTGGGGGAGGACTCCGCCTCATGA","MRLCEIARIWYRFSFAGPRGRGVHVPPAGQEWGKDVDEGRSLAVEPAATCCRRDTAVARLDPARLHTMSAISTDEVARVAALARVALSDEEVSRLAGELDAVASSFARVTSVVTPDLPATSHPVPLTNVLREDVPAPTLDVDELLAGAPASEDSMFLVPQILGEDSAS$","Glutamyl-tRNA(Gln) amidotransferase subunit C","Cytoplasm","Glutamyl-tRNA(Gln) amidotransferase subunit C(Glu-ADTsubunit C)","glutamyl-tRNA(Gln) amidotransferase; C subunit","glutamyl-tRNA(Gln) amidotransferase, C subunit","","Curnow A.W., Hong K., Yuan R., Kim S., Martins O., Winkler W., Henkin T.M., Soll D. Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(22):11819-11826. PMID: 9342321","","","

InterPro
IPR003837
Family

Glu-tRNAGln amidotransferase, C subunit
PF02686	$\"[87-158]T$	Glu-tRNAGln
TIGR00135	$\"[71-163]T$	gatC: glutamyl-tRNA(Gln) and/or aspartyl-tR

","BeTs to 12 clades of COG0721COG name: Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunitFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0721 is aom--z-qvdrlbc-f---nujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003837 (Glu-tRNAGln amidotransferase, C subunit) with a combined E-value of 5.8e-23. IPB003837A 71-115 IPB003837B 130-163","Residues 71-162 are similar to a (C SUBUNIT AMIDOTRANSFERASE LIGASE 6.3.5.- BIOSYNTHESIS GLUTAMYL-TRNAGLN GLU-ADT TRANSFERASE ASPARTYL/GLUTAMYL-TRNAASN/GLN) protein domain (PD009162) which is seen in GATC_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 87 to 158 (E_value = 1.4e-15) place ANA_0280 in the Glu-tRNAGln family which is described as Glu-tRNAGln amidotransferase C subunit.","","amidotransferase subunit C (Glu-ADTsubunit C) (Gln)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0281","284446","285987","1542","4.94","-20.82","53344","ATGAGCGCTCACAGCACCAACGCCCTGGCCGACCTGATCAGGAGCAGCGCCGCCGAGCAGGCCGCGGCCCTGGCGGCGGGGGAGGTCTCCTCACGCGAGCTCACCCAGGCCCACCTCGATCGCATCGCCGCTGTCGACGGCGCTGTCGGTGCCTTCCTCGACGTCGATGCCGAGTGCGCCCTGAGCCAGGCCGACGCCGCCGACGCCGCCCGCAAGGAGGGCCAGGCGACCAGCGAGCTGACCGGCGTGCCGGTGGCCGTCAAGGACCTCATCGTCACCCGAGGCCAGGTCACCACCGCCGCCTCACGGATCCTCGAGGGATGGGTGCCGCCCTATGACGCCACCCTCGTGCGCAACCTGCGCGCCGCCCGCACCCCGATCCTGGGCAAGACCAATCTCGACGAGTTCGCCATGGGCGGCTCCACCGAGCACTCGGCCTTCGGACGCACCGCCAACCCCTGGGACCTGGGCCGCATCCCGGGAGGATCCTCGGGTGGCTCAGCCGCGGCCGTGGGCGCCTACGAGGCCCCCGTGGCCGTGGGCACCGACACCGGGGGCTCGATCCGCCAGCCCGCGGCCGTCACCGGCACGGTCGGCGTCAAGCCGACCTACGGCACGGTCTCGCGCTTCGGCGTCATCGCTATGGCCTCCTCCCTCGACACGCCGGGCCCCATGGCCCGTACGGTGCTGGACACCGCTCTACTGCACGACGTCATCGCCTCTCACGACCCGCTGGACTCGACCTCGCTGCCGGACGCCCCGCGCGACATGGCTGCCGTGGTCCGGGCCGCCCAGGAGGGAAGGGACCTGACCGGACTGCGAGTCGGCGTCATCTCCGAGCTCGACGGCGGAGAGGGCTACCACGACGGCGTCGTGGCCTCCTTCCACGCCGCCCTGGAGCTGCTCGAGGCGGCTGGCGCGCAGGTGGAGACCGTCTCCCTGCCGCACCTGGAGTACGCGCTGGACGCCTACTACCTCATCATGCCCGCCGAGGCCTCCTCCAACCTGGCCCGCTACGACGGGATGCGTTACGGCCTGCGGGTCGAACCGACGTCGGGACCCGTCACCGCCGAGACCGTCATGGCGGCCACCCGCGGAGCAGGCTTCGGCGACGAGGTCAAGCGCCGCATCATCCTGGGCACCCACGTGCTGTCGGCCGGCTACTACGACGCCTACTACGGCTCGGCCCAGAAGGTGCGCACTCTCGTGCAGCGCGACTTCGCCGCCGCCTGGGACAAGGCGGACATCCTCGTCTCGCCCACCGCCCCGGTGACGGCCTACCGCTTTGGGGAGAAGGACGACCCGCTGGCGATGTACAAGCTGGACGTGACCACGATCCCGGCCAACCTCGCGGGGGTCCCCGGCATGAGCCTGCCCTCGGGCCTGAGTGATGACGGGCTTCCGGTGGGCTTCCAGATCCTGGCGCCGCAGAGGGCCGATGACCGCCTGTACCGCGTGGGTGCCGTCCTGGAGGCCGCGCTGGAGGAGACATGGGGGGCGCCGCTGCTGTCGCGTGCGCCCGAGCTGGAGGAGACACGATGA","MSAHSTNALADLIRSSAAEQAAALAAGEVSSRELTQAHLDRIAAVDGAVGAFLDVDAECALSQADAADAARKEGQATSELTGVPVAVKDLIVTRGQVTTAASRILEGWVPPYDATLVRNLRAARTPILGKTNLDEFAMGGSTEHSAFGRTANPWDLGRIPGGSSGGSAAAVGAYEAPVAVGTDTGGSIRQPAAVTGTVGVKPTYGTVSRFGVIAMASSLDTPGPMARTVLDTALLHDVIASHDPLDSTSLPDAPRDMAAVVRAAQEGRDLTGLRVGVISELDGGEGYHDGVVASFHAALELLEAAGAQVETVSLPHLEYALDAYYLIMPAEASSNLARYDGMRYGLRVEPTSGPVTAETVMAATRGAGFGDEVKRRIILGTHVLSAGYYDAYYGSAQKVRTLVQRDFAAAWDKADILVSPTAPVTAYRFGEKDDPLAMYKLDVTTIPANLAGVPGMSLPSGLSDDGLPVGFQILAPQRADDRLYRVGAVLEAALEETWGAPLLSRAPELEETR$","Glutamyl-tRNA(Gln) amidotransferase subunit A","Cytoplasm, Extracellular","glutamyl-tRNA(Gln) amidotransferase, A subunit","glutamyl-tRNA(Gln) amidotransferase subunit A ","glutamyl-tRNA(Gln) amidotransferase, A subunit","","","","","

InterPro
IPR000120
Family

Amidase
PTHR11895	$\"[25-495]T$	AMIDASE
PF01425	$\"[33-484]T$	Amidase
PS00571	$\"[161-192]T$	AMIDASES

InterPro
IPR004412
Family

Glutamyl-tRNA(Gln) amidotransferase A subunit
TIGR00132	$\"[20-496]T$	gatA: glutamyl-tRNA(Gln) and/or aspartyl-tR

noIPR
unintegrated

unintegrated
G3DSA:3.90.1300.10	$\"[11-495]T$	no description
PTHR11895:SF7	$\"[25-495]T$	GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A

","BeTs to 21 clades of COG0154COG name: Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidasesFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0154 is aom--zyqvdrlbc-f---nujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000120 (Amidase) with a combined E-value of 5.6e-35. IPB000120 152-206","Residues 27-250 are 51% similar to a (SPAC869.01) protein domain (PD249540) which is seen in Q9URY4_SCHPO.Residues 27-321 are 53% similar to a (AMIDASE HYDROLASE AF1954) protein domain (PDA1A737) which is seen in YJ54_ARCFU.Residues 39-470 are 76% similar to a (SUBUNIT A AMIDASE AMIDOTRANSFERASE GLUTAMYL-TRNAGLN LIGASE 6.3.5.- HYDROLASE BIOSYNTHESIS GLU-ADT) protein domain (PD038838) which is seen in Q6AEE8_BBBBB.Residues 80-258 are 53% similar to a (ADR051CP) protein domain (PD992426) which is seen in Q75A67_ASHGO.Residues 182-240 are 66% similar to a (AMIDASE) protein domain (PD933539) which is seen in Q7VU19_BORPE.Residues 397-459 are 79% similar to a (A SUBUNIT AMIDOTRANSFERASE LIGASE 6.3.5.- GLUTAMYL-TRNAGLN GLU-ADT BIOSYNTHESIS TRANSFERASE AMIDASE) protein domain (PD858007) which is seen in Q6NHQ1_CORDI.Residues 449-491 are 79% similar to a (A SUBUNIT AMIDOTRANSFERASE LIGASE 6.3.5.- GLUTAMYL-TRNAGLN AMIDASE GLU-ADT BIOSYNTHESIS TRANSFERASE) protein domain (PD002554) which is seen in GATA_CORGL.Residues 465-509 are 82% similar to a (AMIDOTRANSFERASE 6.3.5.- A TRANSFERASE GLUTAMYL-TRNAGLN LIGASE SUBUNIT) protein domain (PD992419) which is seen in Q6A8P5_PROAC.","","-56% similar to PDB:2DF4 Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Mn2+ (E_value = 3.2E_86);-56% similar to PDB:2DQN Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Asn (E_value = 3.2E_86);-56% similar to PDB:2F2A Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln (E_value = 3.2E_86);-56% similar to PDB:2G5H Structure of tRNA-Dependent Amidotransferase GatCAB (E_value = 3.2E_86);-56% similar to PDB:2G5I Structure of tRNA-Dependent Amidotransferase GatCAB complexed with ADP-AlF4 (E_value = 3.2E_86);","Residues 33 to 484 (E_value = 2.9e-187) place ANA_0281 in the Amidase family which is described as Amidase.","","amidotransferase, A subunit (gatA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0282","285984","287480","1497","5.02","-18.78","53642","ATGAGTGACACGCTGATGGACTTCGACGAGGCCGTTCGTCGCTACGACCCGGTCCTGGGACTCGAGGTGCACGTCGAGCTGGGGACCGCCACCAAGATGTTTGACGCCGCCCCCAACGTCTTCGGCGCTCAGCCCAACACGATGGTGACCCCGACGTCAGTGGGCCTTCCCGGCGCGCTGCCGGTGGTCAACGCCCGCGGTGTGGAGTACGCCATCCGTATCGGCCTCGCCCTGGGCTGCGAGATCGCGCAGTCCTGCCGCTTCGCCCGGAAGAACTACTTCTATCCGGACCTGGCCAAGGACTTCCAGACCTCCCAGTCCGATGAGCCCATCGCCTACGACGGCGCCCTGGAGATCGAGATGGAGGACGGCTCCTTATTCACCATCCCGATCGAGCGGGCCCACATGGAGGAGGACGCCGGTAAGAACACGCACATCGGGGGTGCCGACGGCCGTATCGAGGGCGCCAGCCACTCCCTGGTGGACTACAACCGCGCCGGCGTGCCGCTGGTGGAGATCGTCACCCGCCCCATCGAGGGCACCGGTGCCAGGGCGCCTCAGGTCGCCGCCGCCTATGTGCGCACCCTGCGCGACATCTTCCGTGCCCTGGGCGTCTCCGAGGCGCGCATGGAGCGCGGCAACGTGCGCGCTGACGTCAACGTCTCCCTGCGCGAGTCGCCCGACGCGCCGCTGGGCACCCGCACCGAGACCAAGAACGTCAACACCTTCCGTGGGATCGAGCAGGTCGTCCGGTACGAGATCCAGCGTCAGGCCGCCATCCTGGCCGCCGGGGGAGAGGTGCTTCAGGAGACCCGTCACGGCCAGGCCGACGGCACTACCCGTGCCGGTCGCGTCAAGTCCGACGCCGATGACTACCGCTACTTCCCCGAGCCGGACCTGGTTCCGGTGGCGCCCAGCCGCGAATGGGTCGAGGAGATCCGTGCGGGGCTGCCCGAGATGCCTGCGGCCAAGCGTCGTCGTCTCAAGGCCGAGTGGGGCCTGAGTGACACTGAGATGCGTGATGTCGTCAACGCCGGGGCGCTTGAGCTCATCGAGGCCACCGCGGCAGCGGGGATCACCGGCCAGGCCGCCCGCAAGTGGTGGATGGGTGAGCTCTCCCGCAGGGCCAAGGAACAGGAGACCGCCCTGGAGGAGATGGCTGTCACGCCCGAGCAGATCGCCGAGCTGCAAGGGCTGGTGGATTCCGGTCGCCTGACTGACAAGCTCGCCCGACAGGTTCTCGAAGGGGTTCTGGCCGGCGAAGGTGATCCTGAGGCCGTGGCCGCCGCTCGTGGGCTCGAGGTTGTCTCCGACGACTCCGCGCTGCTGGCCGCCGTGGACGAGGCTCTCGCCGCCAACCCGGACGTGGCGGACAAGATCCGCGGCGGCAAGGTTCAGGCGGCAGGCGCCATCGTCGGAGCCGTCATGAAGGCGACCCGCGGCCAGGCCGACGCCAAGCGCGTACGCGAGCTCGTCATGGAGCGCGTGCAGGGCTGA","MSDTLMDFDEAVRRYDPVLGLEVHVELGTATKMFDAAPNVFGAQPNTMVTPTSVGLPGALPVVNARGVEYAIRIGLALGCEIAQSCRFARKNYFYPDLAKDFQTSQSDEPIAYDGALEIEMEDGSLFTIPIERAHMEEDAGKNTHIGGADGRIEGASHSLVDYNRAGVPLVEIVTRPIEGTGARAPQVAAAYVRTLRDIFRALGVSEARMERGNVRADVNVSLRESPDAPLGTRTETKNVNTFRGIEQVVRYEIQRQAAILAAGGEVLQETRHGQADGTTRAGRVKSDADDYRYFPEPDLVPVAPSREWVEEIRAGLPEMPAAKRRRLKAEWGLSDTEMRDVVNAGALELIEATAAAGITGQAARKWWMGELSRRAKEQETALEEMAVTPEQIAELQGLVDSGRLTDKLARQVLEGVLAGEGDPEAVAAARGLEVVSDDSALLAAVDEALAANPDVADKIRGGKVQAAGAIVGAVMKATRGQADAKRVRELVMERVQG$","Glutamyl-tRNA(Gln) amidotransferase subunit B","Cytoplasm","glutamyl-tRNA(Gln) amidotransferase, B subunit","glutamyl-tRNA(Gln) amidotransferase subunit B ","glutamyl-tRNA(Gln) amidotransferase, B subunit","","Curnow A.W., Hong K., Yuan R., Kim S., Martins O., Winkler W., Henkin T.M., Soll D. Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(22):11819-11826. PMID: 9342321","","","

InterPro
IPR003789
Domain

GatB/Yqey
PF02637	$\"[349-496]T$	GatB_Yqey

InterPro
IPR004413
Family

Glutamyl-tRNA(Gln) amidotransferase B subunit
PTHR11659	$\"[23-498]T$	GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B (MITOCHONDRIAL AND PROKARYOTIC) PET112-RELATED
TIGR00133	$\"[12-497]T$	gatB: glutamyl-tRNA(Gln) and/or aspartyl-tR
PS01234	$\"[163-177]T$	GATB

InterPro
IPR006075
Domain

GatB N-terminal region
PF02934	$\"[13-264]T$	GatB_N

InterPro
IPR006107
Domain

GatB, central region
PF01162	$\"[280-348]T$	GatB

","BeTs to 21 clades of COG0064COG name: Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit (PET112 homolog)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0064 is aom--zyqvdrlbc-f---nujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003789 (GatB/Yqey) with a combined E-value of 2.7e-105. IPB003789A 19-30 IPB003789B 45-80 IPB003789C 88-102 IPB003789D 129-145 IPB003789E 161-185 IPB003789F 213-223 IPB003789G 232-257 IPB003789H 280-300 IPB003789I 316-343 IPB003789J 471-485","Residues 20-141 are similar to a (SUBUNIT B AMIDOTRANSFERASE LIGASE 6.3.5.- BIOSYNTHESIS ASPARTYL/GLUTAMYL-TRNAASN/GLN ASP/GLU-ADT E GLUTAMYL-TRNAGLN) protein domain (PD617852) which is seen in GATB_STRCO.Residues 159-246 are 89% similar to a (SUBUNIT B AMIDOTRANSFERASE LIGASE 6.3.5.- BIOSYNTHESIS ASPARTYL/GLUTAMYL-TRNAASN/GLN ASP/GLU-ADT GLUTAMYL-TRNAGLN E) protein domain (PD002690) which is seen in GATB_BIFLO.Residues 247-331 are 84% similar to a (SUBUNIT B AMIDOTRANSFERASE LIGASE 6.3.5.- BIOSYNTHESIS ASPARTYL/GLUTAMYL-TRNAASN/GLN ASP/GLU-ADT E GLUTAMYL-TRNAGLN) protein domain (PD018234) which is seen in Q6AEE9_BBBBB.Residues 383-494 are 85% similar to a (SUBUNIT B AMIDOTRANSFERASE LIGASE 6.3.5.- BIOSYNTHESIS ASPARTYL/GLUTAMYL-TRNAASN/GLN ASP/GLU-ADT GLUTAMYL-TRNAGLN E) protein domain (PD309942) which is seen in GATB_MYCTU.","","-55% similar to PDB:2DF4 Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Mn2+ (E_value = 1.2E_85);-55% similar to PDB:2DQN Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Asn (E_value = 1.2E_85);-55% similar to PDB:2F2A Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln (E_value = 1.2E_85);-55% similar to PDB:2G5H Structure of tRNA-Dependent Amidotransferase GatCAB (E_value = 1.2E_85);-55% similar to PDB:2G5I Structure of tRNA-Dependent Amidotransferase GatCAB complexed with ADP-AlF4 (E_value = 1.2E_85);","Residues 13 to 264 (E_value = 2e-125) place ANA_0282 in the GatB_N family which is described as PET112 family, N terminal region.Residues 280 to 348 (E_value = 3.3e-30) place ANA_0282 in the GatB family which is described as PET112 family, C terminal region.Residues 349 to 496 (E_value = 3.7e-49) place ANA_0282 in the GatB_Yqey family which is described as GatB/Yqey domain.","","amidotransferase, B subunit (gatB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0283","287808","289196","1389","5.20","-14.11","48838","ATGGTTCAGCCCAGTCCCAGTTACACCGTCGCCCTGTACCTCGAGGTGCCCGCCTCCCAGAAGGCGGTGGCCCGCCTGGTCGACACTGCCACTGCGACTGGTGCCATCGTCACCGGCGTCGACGTGGCCGACTCCGACGGCGACAAGCTCACCGTCAATCTCACGGCGGACACCCGGGACTCCAAGCACCGCAACGAGCTGGTTGCCAAGTTGGAGGAGATTGACGGCGTCGTCGTCCGCAACGTCGGCGACTCGACCTTCCTGACTCACGTCGGAGGCAAGATCGAGATCGCTAGCAAGTACCCGATTCACAACCGTCGTGACCTGGCCCGTGTCTACACCCCCGGAGTGGCCCGCGTCTGCAAGGCCATCTACGACCACCCCGAGCGCGCCCGGATGCTCACCATCAAGAAGAACACCGTCGCCGTCGTCACCGACGGGACCGCGGTCTTGGGGCTGGGGGACATCGGCCCATCCGCAGCCATGCCCGTCATGGAGGGCAAGGCCGTTCTGTTCAAGCAGTTCGGCAACGTGGACGCCTGGCCGGTGGCCCTGGACACGAAGGACCCCGAGGAGATCATCTCCATCGTCAAGGCCATCGCCCCGGCCTACGGCGGCATCAACCTGGAGGACATCGCCGCCCCCAAGTGCTTCGACATCGAGGCCCGCCTGCGCGAGGAGCTCGACATCCCGGTCTTCCACGACGATCAGCACGGTACCGCCATCGTGACCCTGGCGGCCCTCATCAACGCTCTGAAGATCGTGGGCAAGAAGATCGAGGACGTGCGCATCGTCCTGTCCGGTGTCGGTGCGGCCGGCAGCGCCATCGCCAAGCTGCTCATGGCGCACGGCGCCACGGACATCGTCGGCTACGGGCGCACCGGAGCCTTGTCCGCGGCGAACACCGAGGGGATGAACGAGCACCGCAAGTGGCTGGCAGAGAACACCAACCCGCGTCAGGTGACCGGCTCCCTCAAGGAGGGCCTCAAGGGGGCCGACGTCTTCATCGGGGTCTCCTCGGGCAACCTGCTCGAGCCCGAGGACCTGGAGGTCATGAACGACGGCGCCATCGTCTTCGCCATGGCTAACCCGATCCCGGAGGTCGACCCGATCCGCGCGGCCGACTACGCCGCCGTGGTGGCGACCGGACGCTCGGACTTCCCCAACCAGATCAACAATGTCCTGGCCTTCCCCGGGCTCTTCCGAGGTCTGCTGGACACCGGGATCACCGACATCTCCACCGAACTGCTGCGGGCCGCGTCGACCGGTATCGCCTCGGTGATCGCCGATGACGAGATCAGCCCCGTGTACATCATCCCCGGCGCCTTCGACACCCGGGTCGCCGACGCCGTGGCCAAGGCGGTCCGCAAGTTCGCTGAGACGGAGTGA","MVQPSPSYTVALYLEVPASQKAVARLVDTATATGAIVTGVDVADSDGDKLTVNLTADTRDSKHRNELVAKLEEIDGVVVRNVGDSTFLTHVGGKIEIASKYPIHNRRDLARVYTPGVARVCKAIYDHPERARMLTIKKNTVAVVTDGTAVLGLGDIGPSAAMPVMEGKAVLFKQFGNVDAWPVALDTKDPEEIISIVKAIAPAYGGINLEDIAAPKCFDIEARLREELDIPVFHDDQHGTAIVTLAALINALKIVGKKIEDVRIVLSGVGAAGSAIAKLLMAHGATDIVGYGRTGALSAANTEGMNEHRKWLAENTNPRQVTGSLKEGLKGADVFIGVSSGNLLEPEDLEVMNDGAIVFAMANPIPEVDPIRAADYAAVVATGRSDFPNQINNVLAFPGLFRGLLDTGITDISTELLRAASTGIASVIADDEISPVYIIPGAFDTRVADAVAKAVRKFAETE$","Malate dehydrogenase (oxaloacetate-decarboxylating)","Cytoplasm","NAD-dependent malic enzyme (NAD-ME)","malate dehydrogenase (oxaloacetate-decarboxylating) ","Malate dehydrogenase (oxaloacetate-decarboxylating)","","","","","

InterPro
IPR001891
Family

Malic oxidoreductase
PIRSF000106	$\"[56-461]T$	Malic enzyme
PS00331	$\"[233-249]T$	MALIC_ENZYMES

InterPro
IPR012301
Domain

Malic enzyme, N-terminal
PF00390	$\"[92-235]T$	malic

InterPro
IPR012302
Domain

Malic enzyme, NAD-binding
PF03949	$\"[237-460]T$	Malic_M

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.10380	$\"[70-234]T$	no description
G3DSA:3.40.50.720	$\"[235-459]T$	no description
PTHR23406	$\"[86-459]T$	MALIC ENZYME-RELATED
PTHR23406:SF2	$\"[86-459]T$	MALIC ENZYME

","BeTs to 19 clades of COG0281COG name: Malic enzymeFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0281 is ao-pkzy-vdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB001891 (Malic oxidoreductase) with a combined E-value of 2.5e-11. IPB001891E 208-253 IPB001891H 382-422","Residues 84-135 are 80% similar to a (OXIDOREDUCTASE ENZYME MALIC MALATE NADP-DEPENDENT NAD-DEPENDENT DEHYDROGENASE NAD DECARBOXYLATING DEHYDROGENASE) protein domain (PD064098) which is seen in Q9L1U4_STRCO.Residues 112-282 are 41% similar to a (OXIDOREDUCTASE MALATE) protein domain (PDA194W1) which is seen in Q6LKB1_PHOPR.Residues 138-278 are 43% similar to a (ENZYME OXIDOREDUCTASE MALIC) protein domain (PD730559) which is seen in Q875H8_MUCCI.Residues 139-181 are 93% similar to a (OXIDOREDUCTASE ENZYME MALIC MALATE NADP-DEPENDENT NAD-DEPENDENT DEHYDROGENASE NAD DECARBOXYLATING DEHYDROGENASE) protein domain (PD968981) which is seen in MAOX_BACST.Residues 191-236 are similar to a (OXIDOREDUCTASE ENZYME MALIC MALATE NADP-DEPENDENT NAD-DEPENDENT DEHYDROGENASE NAD DEHYDROGENASE DECARBOXYLATING) protein domain (PD005834) which is seen in MAOX_BACST.Residues 207-333 are 49% similar to a (ENZYME OXIDOREDUCTASE NAD-DEPENDENT MALIC) protein domain (PDA0S886) which is seen in Q6A9C2_PROAC.Residues 237-289 are 75% similar to a (ENZYME OXIDOREDUCTASE MALIC) protein domain (PDA0S877) which is seen in Q8R7R6_THETN.Residues 239-281 are 90% similar to a (OXIDOREDUCTASE ENZYME MALIC MALATE NADP-DEPENDENT NAD-DEPENDENT DEHYDROGENASE NAD NADP-ME NADP) protein domain (PD553255) which is seen in Q717I9_TRIVA.Residues 267-373 are 62% similar to a (OXIDOREDUCTASE ENZYME MALIC MALATE NADP-DEPENDENT DEHYDROGENASE NAD-DEPENDENT NADP NAD NADP-ME) protein domain (PD001213) which is seen in Q59826_STRBO.Residues 377-444 are similar to a (OXIDOREDUCTASE ENZYME MALIC MALATE NADP-DEPENDENT DEHYDROGENASE NAD-DEPENDENT NAD NADP NADP-ME) protein domain (PD361637) which is seen in Q8CX62_OCEIH.","","-71% similar to PDB:2A9F Crystal structure of a putative malic enzyme ((S)-malate:NAD+ oxidoreductase (decarboxylating)) (E_value = 2.0E_103);-69% similar to PDB:1VL6 Crystal structure of NAD-dependent malic enzyme (TM0542) from Thermotoga maritima at 2.61 A resolution (E_value = 3.5E_92);-69% similar to PDB:2HAE Crystal structure of a putative malic enzyme (malate oxidoreductase) (E_value = 3.5E_92);-65% similar to PDB:1WW8 Crystal Structure of malic enzyme from Pyrococcus horikoshii Ot3 (E_value = 1.6E_89);-42% similar to PDB:1LLQ Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide (E_value = 8.8E_19);","Residues 92 to 235 (E_value = 3e-74) place ANA_0283 in the malic family which is described as Malic enzyme, N-terminal domain.Residues 237 to 460 (E_value = 5.2e-86) place ANA_0283 in the Malic_M family which is described as Malic enzyme, NAD binding domain.","","malic enzyme (NAD-ME) (NAD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0284","289870","289313","558","10.47","5.64","19562","GTGCCTGCTTCCACTCGTGGCGCCAAGCGCCCTCGTTCCGGATCCGACATCGTGACCAGCCCGTCGGCTCGCATCGTGCTGGCCGTCCTACGGATCGTCGTCGGCTTCATTTTCCTGTGGACCTTCCTGGACAAGACGTTCGGCCTCGGATTCTCCACCCCTCGTCAGATGGCCTGGATCCACGGAGGTCAGCCCGCCCAGGGCTTCATCAAGGGCGTGGCAGTTCACAGCCCCTTTGGGAGCGCCTTCGAGTTGCTGGCCAACCCGGTCGGGGACTGGCTGTTCATGGCTGGGATGCTCGGGGTGGGCGTCGCCCTGACTATGGGCATTGGGCTCAAGGTGAGCGCATTCGCGGCCTCAGCACTCATGGTGCCGTTGTATCTGGCCCTGTGGCCCATCGGCACCGGAGGTACCGAGAACGCCGCGACCAACCCCCTGGTCGATCTTCACTGGGTTCTGACTCTGTCTGCCATCCTGTTCGCCCTGACTCGGGCCGGCGATACCCTGGGGCTGGGCGCCTGGTGGTCTCGTCTGGTCGGGGACTCCTGGCTGCGCTGA","VPASTRGAKRPRSGSDIVTSPSARIVLAVLRIVVGFIFLWTFLDKTFGLGFSTPRQMAWIHGGQPAQGFIKGVAVHSPFGSAFELLANPVGDWLFMAGMLGVGVALTMGIGLKVSAFAASALMVPLYLALWPIGTGGTENAATNPLVDLHWVLTLSAILFALTRAGDTLGLGAWWSRLVGDSWLR$","Integral membrane protein","Membrane, Extracellular","probable integral membrane protein SCJ12.13c","integral membrane protein SCJ1213c","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-48]?$	signal-peptide
tmhmm	$\"[21-43]?$ $\"[89-109]?$ $\"[114-134]?$ $\"[153-175]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-185 are 57% similar to a (MEMBRANE SCJ12.13C INTEGRAL) protein domain (PD312887) which is seen in Q9RI45_STRCO.","","-57% similar to PDB:2FZW Structure of the binary complex of the E67L mutant of human glutathione-dependent formaldehyde dehydrogenase with NAD(H) (E_value = );","No significant hits to the Pfam 21.0 database.","","integral membrane protein SCJ12.13c","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0288","296162","297547","1386","7.83","4.61","49453","GTGACTCATAGCGACCTCCCTGCCACTCCATCGGACAACGGCCACGAACCGAGTCTCGATGCCGATCGGCTCATGCAACAGTCCGACGTCGTGCTGCACCTGGGACGGCTCATGCTCGCTGCCGGTGCCGGCTCCTACCGCATCAAGTCCTCCATGGCCAGAGCCGCTTCGGCTGTTGGGCTCGACCGCCACGAGGCGACCGTGACGATGACCGAGATCGTCACTTCCTCCTACGTCGGCAACCGTTTCCGTACCGAGGCCTGCGAAGTGCGTCGGGTCGGCGTCAACGTCGGTCGCTTGGAGGCGCTGCGCCGCATCGTCCACGACCTGCGAGCACATGAGACCGTCGAGCACCTCGAGGCCAGGCTTCAACAGGTCGAGAAGATGCATGCGCGCTACAACGCCTTCACCAACGCGGCAGCCTCGGGTGTGGCCTGTGCCGGATTCTGCTTCCTCAACAAGGGCGGTTGGGTGGAGTGTCTGACGGTCCTCGTCGCGGCCTTCCTCGGACAGTTCGTTCGCCGGCAGATGCTGGAGCGCCACTATCAGCACTTCTTCACCTGGCTCGTCTGCGGAGTTGCGGCCTCCGGCACCTACATGGGCATCGTGACAGCCCTGAACGCCACTGGCGTGGTGGCGGGAAACCACCAGGGCGGCATCATCTCGGCGATCCTCTTCCTCATTCCTGGTTTCCCCATGGTCACCGCCATGCTCGACCTGTTCCGACAGGACTTCTCCTCGGCCCTGTCACGCAGCGCCTACGTGCTCATGGTCATGGCTGCGGCCGGCGTCGCCGTGTGGACCGTGACCTTCATCTTCCGCTGGGATGTTGCCGCGGCCAGCGGCAGCACGCTCGACGGTCCTCTCCTCTACGTTCTGCGCTGCTTCTGCTCCTTCATCGCCGCCTACGGATTCGCCATGCTGTTCAACGCAGGCGTGAAGGCCAGCATGCTGGCTGCAGTGGTCGGGGCTCTGGCTAATACCGGCAGACTGCTTCTCATTGACGTCTTCCACGTGCCATGGCAGCTCGCAGTGGGCCTGGCCGCGGTCACGATCGGCCTGCTCGCCCAGCTCTTCGTCTCCCGCGCCTCCCTGTCCCGGGTGGCTCTGTCCGTTCCCGCCGTCGTCATCATGATCCCCGGAGTCCCCTTCTACCGAGCCATCTCCGCGCTCAACACGCTCTCCGTGGACAAGCTCGGCGTCGACGTCGGCGAGGCGGCCACGAACCTGGCTGAGGTCTTCTTCGTCATCACCGCTATCGGTGTGGGGCTGGCCTTGGCGCGTATCATCACCGATCACAACTGGCGTCACGACGTCGCCACCTCCGGGCACATCACGCTGCCTCGCACACACGTCGAGGCGGTGGAGCAGCCTCTGGAGGTCTGA","VTHSDLPATPSDNGHEPSLDADRLMQQSDVVLHLGRLMLAAGAGSYRIKSSMARAASAVGLDRHEATVTMTEIVTSSYVGNRFRTEACEVRRVGVNVGRLEALRRIVHDLRAHETVEHLEARLQQVEKMHARYNAFTNAAASGVACAGFCFLNKGGWVECLTVLVAAFLGQFVRRQMLERHYQHFFTWLVCGVAASGTYMGIVTALNATGVVAGNHQGGIISAILFLIPGFPMVTAMLDLFRQDFSSALSRSAYVLMVMAAAGVAVWTVTFIFRWDVAAASGSTLDGPLLYVLRCFCSFIAAYGFAMLFNAGVKASMLAAVVGALANTGRLLLIDVFHVPWQLAVGLAAVTIGLLAQLFVSRASLSRVALSVPAVVIMIPGVPFYRAISALNTLSVDKLGVDVGEAATNLAEVFFVITAIGVGLALARIITDHNWRHDVATSGHITLPRTHVEAVEQPLEV$","Threonine/serine exporter family protein, ThrE","Membrane, Cytoplasm","integral membrane protein, putative","hypothetical protein","protein of unknown function DUF1212","","","","","

InterPro
IPR010619
Family

Protein of unknown function DUF1212
PF06738	$\"[34-230]T$	DUF1212

noIPR
unintegrated

unintegrated
tmhmm	$\"[155-173]?$ $\"[188-208]?$ $\"[218-238]?$ $\"[253-275]?$ $\"[289-309]?$ $\"[319-339]?$ $\"[345-365]?$ $\"[370-388]?$ $\"[407-427]?$	transmembrane_regions

","BeTs to 3 clades of COG2966COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2966 is ------------b-e-gh--u-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 58-177 are 62% similar to a (MEMBRANE TRANSMEMBRANE STRUCTURAL INTEGRAL PROTEIN EXPORT CARRIER IPF13607 CANDIDA EXPORTER) protein domain (PD036296) which is seen in Q6A9Z3_PROAC.Residues 212-340 are 57% similar to a (MEMBRANE INTEGRAL) protein domain (PD718375) which is seen in Q890F4_LACPL.","","No significant hits to the PDB database (E-value < E-10).","Residues 34 to 230 (E_value = 1.3e-32) place ANA_0288 in the DUF1212 family which is described as Protein of unknown function (DUF1212).","","membrane protein, putative","","1","","","","","","","","","","","Mon Aug 13 18:21:31 2007","","","","","Mon Aug 13 18:21:31 2007","","Mon Aug 13 18:21:31 2007","","Mon Aug 13 18:21:31 2007","Mon Aug 13 18:21:31 2007","","","","","yes","","" "ANA_0289","299419","297653","1767","10.04","20.83","61601","ATGGTCCTGGACTACCTGTTGGACAACCCGGTTGTCATCGTCCTGCTCATGGTTGGCTCCGGGATGCTGCTCTGGCGCGCCAGGCGCGGGAGCATACGCATCCCGGCAGCGGCCCTTCTGGTCTGCAGCACCGCACTGCTGATCTGGAAAGTGGCGCACGCCAATGTCCTCCACCATCTGGCCGGCAACGCGGTTCTCGTCCTATTCCTCCTGGTCGGCGCCGGGATGCTGCTCGGGCACATCAAGATCAAGGGCGTGAGCCTGGGCGCAGCGGCCGTCCTGTTCAGCGGCATCGCGCTGGCGGCGTGGGGAGCGTCAGCCTCCACCCCGATTGAGGTTCCCAAGGAGCTGGGAACCCTGGGGCTGGCGATCTTCACCTTCGCCATCGGCATCCAGTCCGGACCGAACTTCTTCCACGTCATCCGAACCGCCGGCGGGCCGTTGGCGATCCTCCTGGGCGTTCTGGGCGTGGCGGCTCTGGCGGCCGTGGGCATGGGGCGTCTTCTCGGTCTCAAGGCGGCGATGATCGCGGGAGCCTTCGCCGGCGCCGTCACGAACACCCCCGCCCTGGCCGCAGCAGGTAACGCCGCCGCCATGGCCGGTGACAAGGCAGGACCGGGTGACGCAACCGTGGCCTATGCCGTCACCTACCTCTACGGTGTCATCGGCATGCTGTTCTTCTGTCTGCTGGCGCTGCGCTACCGGCGCAGCGACAAGGACACTCCCTCCCCTCTCATCAACCGCACCATCCGGGTGGAGCGCGAGGACGGCCCGCTCCTGGGCAACATCGTTGAGACCATCTCGGGACAGCTGCGGTTCTCTCGTCTGCGCCGGGGTGAGAAGGGGCCGATCACCCGGCCGAAGAATGACGACCGGCTGTACAAGGACGACCTCATCACCGTCGTCGGCACCCAGGACGCCGTCAACCAGGCGATCAAAGCGGTGGGCCACGGCTCCTCGCACTCACTCATTGAGGACCGCAAGTATCTCGACTTCCGCCGGATCACAGTCTCGGACCCGAAGCTGGCCGGCCGTACCATCGGTGAGCTGGATATCGACAGCCGTTTCGGGGCAACGATCTCGCGGGTACGCCGCGGCGACGTCGACATGGTGGGCACCCCGGACCTGGTGCTTCAGCAGGGAGACCGGGTGCGCGTCGTCGGCCCGACCGGGCGCATGAAGGATATTTCCACGTACTTCGGCGACTCCTCGCGCGGCCTGTCCTCTATCAACCCGGTGGCGCTGGGCCTGGGGATGGCACTGGGCATCGTCATCGGTGAGTGGAAGTTCCTCACGCCTACCGGAGCGACCTTCTCCATCGGATCGGCTGCCGGAACACTGCTGATCGGACTCATCTTCGGACGCATTGGCCGCATCGGGAAGTTCGTGACCGCCATGCCCTTCACTGCCACGGCGGTGCTGTCGGAGTTCGGGCTCCTGGTCTTCCTGGCCCAGGCGGGTACGAAGGCCGGTGGGGAGATCGCGCATGCCTTCACCGGTGGTGACTGGTGGAGGATCTTCGTCACCGGTTTCGTCGTCACCACCATCGTCGGACTGGGGATTTACGTCTCCATGCGCTGGATCGTCAAGATGGGTGGGACTCGCCTGTCAGGCCTCATCGGTGGCGCCCAGACCCAGCCGGCGATTCTGGCCTTCGCCAACGAGCGCACCGGCGCCGACCCGCGGGTGGCGCTGGGGTACGCGATGGTCTACCCCGTGGCGATGATCGTCAAGATCTTCATTGCGCAGGTCCTCGGCGGGCTGTGA","MVLDYLLDNPVVIVLLMVGSGMLLWRARRGSIRIPAAALLVCSTALLIWKVAHANVLHHLAGNAVLVLFLLVGAGMLLGHIKIKGVSLGAAAVLFSGIALAAWGASASTPIEVPKELGTLGLAIFTFAIGIQSGPNFFHVIRTAGGPLAILLGVLGVAALAAVGMGRLLGLKAAMIAGAFAGAVTNTPALAAAGNAAAMAGDKAGPGDATVAYAVTYLYGVIGMLFFCLLALRYRRSDKDTPSPLINRTIRVEREDGPLLGNIVETISGQLRFSRLRRGEKGPITRPKNDDRLYKDDLITVVGTQDAVNQAIKAVGHGSSHSLIEDRKYLDFRRITVSDPKLAGRTIGELDIDSRFGATISRVRRGDVDMVGTPDLVLQQGDRVRVVGPTGRMKDISTYFGDSSRGLSSINPVALGLGMALGIVIGEWKFLTPTGATFSIGSAAGTLLIGLIFGRIGRIGKFVTAMPFTATAVLSEFGLLVFLAQAGTKAGGEIAHAFTGGDWWRIFVTGFVVTTIVGLGIYVSMRWIVKMGGTRLSGLIGGAQTQPAILAFANERTGADPRVALGYAMVYPVAMIVKIFIAQVLGGL$","Aspartate-alanine antiporter","Membrane, Cytoplasm","Predicted permease","predicted permease","YidE/YbjL duplication","","Anantharaman V., Koonin E.V., Aravind L. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J. Mol. Biol. 2001. 307(5):1271-1292. PMID: 11292341","","","

InterPro
IPR006037
Domain

TrkA-C
PF02080	$\"[331-401]T$	TrkA_C
PS51202	$\"[235-317]T$ $\"[318-402]T$	RCK_C

InterPro
IPR006512
Domain

YidE/YbjL duplication
PF06826	$\"[67-233]T$ $\"[414-587]T$	Asp-Al_Ex
TIGR01625	$\"[72-219]T$ $\"[419-573]T$	YidE_YbjL_dupl: YidE/YbjL duplication

noIPR
unintegrated

unintegrated
signalp	$\"[1-54]?$	signal-peptide
tmhmm	$\"[10-25]?$ $\"[35-53]?$ $\"[59-81]?$ $\"[86-106]?$ $\"[120-138]?$ $\"[148-168]?$ $\"[209-229]?$ $\"[410-430]?$ $\"[436-454]?$ $\"[464-484]?$ $\"[503-523]?$ $\"[563-585]?$	transmembrane_regions

","BeTs to 4 clades of COG2985COG name: Predicted permeaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2985 is -o------------e-gh--------Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 270-400 are 61% similar to a (MEMBRANE PERMEASE) protein domain (PD993002) which is seen in Q6A666_PROAC.Residues 341-400 are 71% similar to a (POTASSIUM UPTAKE TRKA SYSTEM TRANSMEMBRANE TRK CHANNEL HOMOLOG IONIC MEMBRANE) protein domain (PD013953) which is seen in Q74EE6_GEOSL.Residues 474-588 are 53% similar to a (MEMBRANE UPF0199 TRANSMEMBRANE YIDE PERMEASE YBJL PREDICTED UPTAKE POTASSIUM TRKA) protein domain (PD008628) which is seen in Y4I3_YERPE.","","No significant hits to the PDB database (E-value < E-10).","Residues 67 to 233 (E_value = 5.6e-31) place ANA_0289 in the Asp-Al_Ex family which is described as Predicted Permease Membrane Region.Residues 331 to 401 (E_value = 1.1e-14) place ANA_0289 in the TrkA_C family which is described as TrkA-C domain.Residues 414 to 587 (E_value = 1.2e-33) place ANA_0289 in the Asp-Al_Ex family which is described as Predicted Permease Membrane Region.","","permease ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0290","299731","301515","1785","5.09","-25.06","63747","ATGACACGCGAAGACGCTCCCGCACGTCAGGACCACCAGGTCATGACAGGCGCCCAGGCTCTGGTGCGCGCGCTGGAGGAGCTAGGCGTCACAGACATCTTCGGGATGCCGGGCGGCGCCATCCTGCCCTTCTACGACCCCCTGCTCGCCTCGACGAAGATCCGTCACGTCTTGGTGCGCCACGAGCAGGGCGCTGGTCATGCCGCCGAGGGATACGCCATGGTCACCGGTCGTCCCGGGGTGTGCGTCGCCACCTCCGGCCCCGGCGCCACCAACCTCATCACCCCCATCGGTGACGCCCACATGGACTCCGTGCCCATGCTGGCCATCACCGGGCAGGTCGGAAGCCGCGGAATCGGGACGGACGCCTTCCAGGAGGCCGACATCGTCGGGGCCACGATGCCCTTCGTCAAGCACTCCTTCCTCATCACCAGTGCCGAGGACATCGTCCCGTGCGTGGCTGAGGCCTTCCACATCGCCTCCACCGGACGCCCCGGTCCGGTCCTCATCGACATCTCCAAGGATGCCCAGGAGGGGCTCACCGAGTTCGCGTGGCCCCCGGCCCGGGACCTGCCCGGCTACCGCCTGCCAGGCAAGCCCAACCAGCGGCGCCTGGCCCAGGCCGCCGAGGTGATCTCCGCGGCCGAGCGACCCGTCCTCTACCTGGGCGGTGGCCTGAACCGGGCGCAGGTTCCCACCGAGGACCTCACTGAGCTCATCGAGCTCATCGGAGCGCCCTTCGTCACCACCCTGACCGCCCTGGACGTCATGCCCAGTGAGCACTCGCTCAACCTGGGGATGCCCGGCATGCACGGTACCGTGGCCGCCGTCGGGGCGTTGCAGCGGGCCGACGTCGTCGTCTGCCTGGGAGCCCGCTTCGATGACCGCGTCACCGGCAAGCCGGACACCTTCGCCACCAAGGCCTCGGTGATCCACGTCGACGTCGACCCCGCCGAGATCTCCAAGATCCGCACCGCCGACGTCCCGATCGTCGGGGACCTGGCCGACGTCGTTCCCGCGCTGAGCGCTGAGTTCCGCGACCACGTCGCCGCTGAGGGGCGGGTGGACATCGCCCCGTGGCGCCGTGAGATCGAGCGCATCCAGGCCACCTACCCCACGGGCTGGACCGACACCGACGACGGACTGCTTCAGCCCCAGGAGGTCATCACCCATCTTGATCGGGCGGCCTCCGAGGACACCATCTGGGTTACAGGCGTGGGACAGCACCAAATGTGGGCGGCGCACTACCTCACCTTCCGCCGTCCGCACACCTGGCTCAACTCGGCCGGCGCCGGCACCATGGGCTATGGCCTGCCCGCCGCCATGGGTGCCAAGGAGGCCTGCCCCGACCGGCCAGTGTGGCTGATCGACGGGGACGGATGCTTCCAGATGACCAACCAGGAGCTGGCCACCTGCACCCTCAACAACATCCCCATCAAGGTCGCCATCATCAACAACTCCTCGCTGGGGATGGTGCGGCAGTGGCAGACGCTGTTCTACGGGCAGCGCTACTCCAACACCGACCTGCATACCGGGGCCGGAACGAAGCGGATTCCCGACTTCGTCAAGATGGCCGAGGCCTACGGGGCCGTTGGGCTGCGGTGTGAGCGCCTGGAGGACCTGGACGACGTCATCGCCCAGGCCAATGCCATCAACGACCGCCCCGTCGTCGTCGACTTCATCGTCTCCGCGGACGCCCAGGTGTGGCCCATGGTCGCGGCCGGGGTATCCAACGACGAGATCCAGCACGCCCGCGGCATGAGCCCGGTGTGGGAAGAGGAGTGA","MTREDAPARQDHQVMTGAQALVRALEELGVTDIFGMPGGAILPFYDPLLASTKIRHVLVRHEQGAGHAAEGYAMVTGRPGVCVATSGPGATNLITPIGDAHMDSVPMLAITGQVGSRGIGTDAFQEADIVGATMPFVKHSFLITSAEDIVPCVAEAFHIASTGRPGPVLIDISKDAQEGLTEFAWPPARDLPGYRLPGKPNQRRLAQAAEVISAAERPVLYLGGGLNRAQVPTEDLTELIELIGAPFVTTLTALDVMPSEHSLNLGMPGMHGTVAAVGALQRADVVVCLGARFDDRVTGKPDTFATKASVIHVDVDPAEISKIRTADVPIVGDLADVVPALSAEFRDHVAAEGRVDIAPWRREIERIQATYPTGWTDTDDGLLQPQEVITHLDRAASEDTIWVTGVGQHQMWAAHYLTFRRPHTWLNSAGAGTMGYGLPAAMGAKEACPDRPVWLIDGDGCFQMTNQELATCTLNNIPIKVAIINNSSLGMVRQWQTLFYGQRYSNTDLHTGAGTKRIPDFVKMAEAYGAVGLRCERLEDLDDVIAQANAINDRPVVVDFIVSADAQVWPMVAAGVSNDEIQHARGMSPVWEEE$","Acetolactate synthase large subunit","Cytoplasm","acetolactate synthase, large subunit,biosynthetic type","acetolactate synthase large subunit ","acetolactate synthase, large subunit, biosynthetic type","","Arjunan P., Umland T., Dyda F., Swaminathan S., Furey W., Sax M., Farrenkopf B., Gao Y., Zhang D., Jordan F. Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. J. Mol. Biol. 1996. 256(3):590-600. PMID: 8604141Koga J., Adachi T., Hidaka H. Purification and characterization of indolepyruvate decarboxylase. A novel enzyme for indole-3-acetic acid biosynthesis in Enterobacter cloacae. J. Biol. Chem. 1992. 267(22):15823-15828. PMID: 1639814Polovnikova E.S., Mcleish M.J., Sergienko E.A., Burgner J.T., Anderson N.L., Bera A.K., Jordan F., Kenyon G.L., Hasson M.S. Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase. Biochemistry 2003. 42(7):1820-1830. PMID: 12590569","","","

InterPro
IPR000399
Family

TPP-binding enzymes
PIRSF001370	$\"[17-576]T$	Thiamine diphosphate-dependent enzyme, acetolactate synthase type
PS00187	$\"[442-461]?$	TPP_ENZYMES

InterPro
IPR011766
Domain

Thiamine pyrophosphate enzyme, C-terminal TPP-binding
PF02775	$\"[405-560]T$	TPP_enzyme_C

InterPro
IPR012000
Domain

Thiamine pyrophosphate enzyme, central region
PF00205	$\"[205-341]T$	TPP_enzyme_M

InterPro
IPR012001
Domain

Thiamine pyrophosphate enzyme, N-terminal TPP binding region
PF02776	$\"[15-185]T$	TPP_enzyme_N

InterPro
IPR012846
Family

Acetolactate synthase, large subunit, biosynthetic
PIRSF500108	$\"[15-588]T$	Acetolactate synthase, large subunit
TIGR00118	$\"[15-585]T$	acolac_lg: acetolactate synthase, large sub

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1220	$\"[205-342]T$	no description
G3DSA:3.40.50.970	$\"[6-203]T$ $\"[356-565]T$	no description
PTHR18968	$\"[246-581]T$	THIAMINE PYROPHOSPHATE ENZYMES
PTHR18968:SF13	$\"[246-581]T$	ACETOLACTATE SYNTHASE

","BeTs to 20 clades of COG0028COG name: Thiamine pyrophosphate-requiring enzymes acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylaseFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0028 is a-mpkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB000399 (Pyruvate decarboxylase) with a combined E-value of 4.8e-28. IPB000399A 84-95 IPB000399B 439-449 IPB000399C 453-486","Residues 11-226 are 60% similar to a (BIOSYNTHESIS AEL305CP THIAMINE TRANSFERASE BRANCHED-CHAIN AMINO MAGNESIUM PYROPHOSPHATE FLAVOPROTEIN ACID) protein domain (PDA198E6) which is seen in Q758Q8_ASHGO.Residues 12-224 are 43% similar to a (DOMAIN THIAMINE PYROPHOSPHATE-BINDING) protein domain (PDA102F3) which is seen in Q6SGZ3_BBBBB.Residues 14-116 are 51% similar to a (PYRUVATE INDOLE-3-PYRUVATE DECARBOXYLASE) protein domain (PDA191K2) which is seen in Q7NIX5_GLOVI.Residues 15-175 are 41% similar to a (BLR7248) protein domain (PDA1D3V4) which is seen in Q89E39_BRAJA.Residues 15-196 are 62% similar to a (CAILV2 ACETOLACTATE CANDIDA SYNTHASE ALBICANS) protein domain (PDA191K0) which is seen in Q6BJI8_EEEEE.Residues 15-196 are 63% similar to a (BIOSYNTHESIS THIAMINE TRANSFERASE BRANCHED-CHAIN YMR108W AMINO CEREVISIAE ACETOLACTATE MAGNESIUM PYROPHOSPHATE) protein domain (PDA191K1) which is seen in Q6FN19_EEEEE.Residues 15-425 are 46% similar to a (SYNTHASE LARGE ACETOLACTATE SUBUNIT) protein domain (PD386643) which is seen in Q9K659_BACHD.Residues 15-210 are 54% similar to a (THIAMINE ACETOLACTATE PYROPHOSPHATE SYNTHASE) protein domain (PD648192) which is seen in Q8TPF5_METAC.Residues 15-196 are 63% similar to a (3D-STRUCTURE THIAMINE ALS TRANSFERASE BRANCHED-CHAIN MITOCHONDRION AMINO AHAS ACETOLACTATE MAGNESIUM) protein domain (PD123412) which is seen in ILVB_YEAST.Residues 16-175 are 87% similar to a (SYNTHASE ACETOLACTATE BIOSYNTHESIS LARGE SUBUNIT THIAMINE PYRUVATE PYROPHOSPHATE TRANSFERASE FLAVOPROTEIN) protein domain (PD000376) which is seen in Q82JM2_STRAW.Residues 16-216 are 44% similar to a (CARBOXYETHYL SYNTHASE ARGININE) protein domain (PDA1A2Y0) which is seen in Q6TA05_STRCL.Residues 16-259 are 48% similar to a (VALINE SENSITIVE ACETOLACTATE SUBUNIT SYNTHASE III) protein domain (PD648205) which is seen in Q8KTR7_CANTP.Residues 16-264 are 55% similar to a (PYROPHOSPHATE TR THIAMINE FLAVOPROTEIN ALS SYNTHASE TRANSFERASE ACETOHYDROXY-ACID BRANCHED-CHAIN BIOSYNTHESIS) protein domain (PD123410) which is seen in ILVB_SCHPO.Residues 18-217 are 55% similar to a (THIAMINE ACETOLACTATE SUBUNIT HOMOLOG PYROPHOSPHATE SYNTHASE LARGE) protein domain (PDA191J9) which is seen in O27639_METTH.Residues 18-206 are 47% similar to a (SPBC725.04) protein domain (PDA1D4P3) which is seen in Q9Y7M1_SCHPO.Residues 19-126 are 67% similar to a (MJ0663 THIAMINE PYROPHOSPHATE) protein domain (PDA1D502) which is seen in Y663_METJA.Residues 21-256 are 42% similar to a (ACETOLACTATE SYNTHASE) protein domain (PD742211) which is seen in Q82ND1_STRAW.Residues 25-576 are 37% similar to a (LYASE DECARBOXYLASE BENZOYLFORMATE) protein domain (PDA0T8N0) which is seen in Q7NTF5_CHRVO.Residues 53-251 are 49% similar to a (ORF60X1) protein domain (PD750771) which is seen in O31007_VIBAN.Residues 186-374 are 46% similar to a () protein domain (PDA1D4I5) which is seen in Q73U56_MYCPA.Residues 261-322 are 83% similar to a (SYNTHASE BIOSYNTHESIS ACETOLACTATE LARGE SUBUNIT ACID THIAMINE TRANSFERASE FLAVOPROTEIN MAGNESIUM) protein domain (PD587410) which is seen in ILVB_MYCTU.Residues 327-581 are 49% similar to a (ACETOLACTATE SUBUNIT SYNTHASE LARGE) protein domain (PD777184) which is seen in Q8A609_BACTN.Residues 328-562 are 44% similar to a (LYASE ACETOLACTATE SUBUNIT HOMOLOG ILVB-5 SYNTHASE LARGE) protein domain (PD525912) which is seen in Q97UP3_SULSO.Residues 380-590 are 70% similar to a (SYNTHASE ACETOLACTATE BIOSYNTHESIS LARGE THIAMINE PYRUVATE SUBUNIT PYROPHOSPHATE TRANSFERASE ACID) protein domain (PD000397) which is seen in Q8FPX3_COREF.Residues 399-581 are 58% similar to a (ACETOLACTATE SUBUNIT SYNTHASE LARGE) protein domain (PD716021) which is seen in Q9RU76_DEIRA.Residues 513-556 are 81% similar to a (ACETOLACTATE SUBUNIT LARGE SYNTHETASE SYNTHASE) protein domain (PD930271) which is seen in Q82JM2_STRAW.Residues 518-575 are 68% similar to a (TRANSFERASE ACETOLACTATE SUBUNIT SYNTHASE LARGE) protein domain (PDA1B2N3) which is seen in Q6NHN4_CORDI.Residues 557-594 are 89% similar to a (SYNTHASE ACETOLACTATE SUBUNIT BIOSYNTHESIS LARGE THIAMINE TRANSFERASE BRANCHED-CHAIN AMINO MAGNESIUM) protein domain (PD981888) which is seen in ILVB_MYCLE.","","-59% similar to PDB:1YBH Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide Chlorimuron Ethyl (E_value = 3.8E_126);-59% similar to PDB:1YHY Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Metsulfuron methyl (E_value = 3.8E_126);-59% similar to PDB:1YHZ Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Chlorsulfuron (E_value = 3.8E_126);-59% similar to PDB:1YI0 Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Sulfometuron methyl (E_value = 3.8E_126);-59% similar to PDB:1YI1 Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Tribenuron methyl (E_value = 3.8E_126);","Residues 15 to 185 (E_value = 7.6e-92) place ANA_0290 in the TPP_enzyme_N family which is described as Thiamine pyrophosphate enzyme, N-terminal TPP binding domain.Residues 205 to 341 (E_value = 2.7e-57) place ANA_0290 in the TPP_enzyme_M family which is described as Thiamine pyrophosphate enzyme, central domain.Residues 405 to 560 (E_value = 6e-75) place ANA_0290 in the TPP_enzyme_C family which is described as Thiamine pyrophosphate enzyme, C-terminal TPP binding domain.","","synthase, large subunit, biosynthetic type (ilvB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0291","301521","302033","513","6.70","-0.85","18522","GTGAGCGAGAAGCACACCCTGTCCGTCCTGGTGGAGAACAAGCCCGGCGTCCTGACCCGGGTCTCGGCGCTGTTCACGCGCCGGGGCTTCAACATCCACTCCCTGGCCGTGGGGCCCACCGAGCACGAGGACATCTCGCGTATCACGGTGATCGCCGACGCCGAGGGACTGGCCATGGAACAGGTCACCAAGCAGCTCAACAAGCTGGTCAACGTCCTCAAGATCGTCGAGCTCGACCCCGACACCTCGGTCGAGCGCGAGCTCTACCTCATCAAGGTGCACGCCGATGACGCCAATCGCACGGCGGTGCTCCAGGTCGTCGACCTGTTCCGCGCCCACGTCGTGGACGTCGCCCCCACGTCGGTGGTCATTGAGACCATCGGCTCAGAATCCAAGGTCAAGGCTCTACTGACGGCTCTCCAGCCGTACGGTGTCAAAGAGATTGTCCAGTCCGGTGCCGTGGCGATCACGCGCGGCCCACGATCCATCACCGATCAACTCAAGGAGAAGTGA","VSEKHTLSVLVENKPGVLTRVSALFTRRGFNIHSLAVGPTEHEDISRITVIADAEGLAMEQVTKQLNKLVNVLKIVELDPDTSVERELYLIKVHADDANRTAVLQVVDLFRAHVVDVAPTSVVIETIGSESKVKALLTALQPYGVKEIVQSGAVAITRGPRSITDQLKEK$","Acetolactate synthase small subunit","Cytoplasm","acetolactate synthase, small subunit","acetolactate synthase small subunit ","acetolactate synthase, small subunit","","Chipman D.M., Shaanan B. The ACT domain family. Curr. Opin. Struct. Biol. 2001. 11(6):694-700. PMID: 11751050","","","

InterPro
IPR002912
Domain

Amino acid-binding ACT
PF01842	$\"[5-71]T$	ACT

InterPro
IPR004789
Family

Acetolactate synthase, small subunit
PD002844	$\"[4-78]T$	Q9RFQ7_STRCM_Q9RFQ7;
TIGR00119	$\"[3-160]T$	acolac_sm: acetolactate synthase, small sub

","BeTs to 17 clades of COG0440COG name: Acetolactate synthase, small subunitFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0440 is a-m-kzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB004789 (Acetolactate synthase, small subunit) with a combined E-value of 5.1e-68. IPB004789A 4-55 IPB004789B 64-93 IPB004789C 100-144","Residues 4-78 are similar to a (SMALL SUBUNIT SYNTHASE ACETOLACTATE ACID TRANSFERASE SYNTHASE LYASE BIOSYNTHESIS AMINO) protein domain (PD002844) which is seen in Q9RFQ7_STRCM.Residues 79-128 are 68% similar to a (SMALL SUBUNIT SYNTHASE ACETOLACTATE ACID TRANSFERASE SYNTHASE LYASE BIOSYNTHESIS III) protein domain (PD002971) which is seen in Q6NHN3_CORDI.","","-66% similar to PDB:2PC6 Crystal structure of putative acetolactate synthase- small subunit from Nitrosomonas europaea (E_value = 3.1E_31);-66% similar to PDB:2FGC Crystal structure of Acetolactate synthase- small subunit from Thermotoga maritima (E_value = 3.4E_30);-63% similar to PDB:2F1F Crystal structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from E. coli (E_value = 1.4E_28);","Residues 5 to 71 (E_value = 8.1e-12) place ANA_0291 in the ACT family which is described as ACT domain.","","synthase, small subunit (ilvN)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0292","302043","303074","1032","4.98","-17.19","37182","ATGGCAGCTGAGAAGTTCTACGACGACGACGCCGACCTGTCCGTCATCCAGTCCAAGAAGGTCGCCGTCATCGGCTACGGTTCCCAGGGGCACGCTCACGCTCTGAACCTGCGCGACTCCGGTGTGGAGGTCGTTGTCGGCCTGCGCGAGGGCTCGGCCTCTGTGGCTAAGGCTGAGGAGGCGGGCCTGCCCGTCAAGCCGATCGCCGAGGCCGTGGCCTGGGCCGACGTCGTCACCGTCCTGGCCCCCGACCAGGTGCAGGCCACCCTCTACCGCGAGGAGATCGAGCCGAACATCAAGGCTGGCTCCGCCCTCCTGTTCTCCCACGGCTTCAACATCCACTTCGGCTACATCAAGCCGTCGGCGGACATTGACGTCGTCATGGTGGCTCCCAAGGGACCCGGCCACACCGTGCGCCGCGAGTTCGAGTCCGGCCGAGGCGTGCCCGTGCTCGTCTGTGTGGAGCAGGACGCCTCGGGCACCGCCTGGGACCTCGTCCTGTCCTACGCCAAGGCCATCGGCGGTACCCGCGCCGGCGCCATCAAGACCACCTTCCGTGAGGAGACCGAGACCGACCTCTTCGGTGAGCAGTCGGTCCTGTGCGGTGGCGTCTCCAAACTCATCCAGTACGGCTTCGAGACCCTGGTCGAGGCCGGCTACCAGCCCGAGATGGCCTACTTCGAGGTCTGCCACGAGATGAAGCTCATCGTGGACCTCATCAACGAGGGCGGTATCTCCAAGCAGCGCTGGTCCTGCTCCGACACCGCTGAGTACGGCGACTACGTCTCCGGCCCGCGCGTCATCACCCCCGAGGTCAAGGAGCACATGAAGGAGGTCCTGTCCGACATCCAGGACGGCACCTTCGCCAAGCGCTTCATGGACGACCAGGCCGCCGGCGCTCCGGAGTTCAAGAAGCTCCGGGCCGAGGGTGAGGCGCACCCCATCGAGGCCGCCGGCCGCGAGGTGCGTTCCATGTTCGCCTGGCGCGCCGACGTCGACAAGGACTACACCGAGGGCTCCGTGGCTCGCTGA","MAAEKFYDDDADLSVIQSKKVAVIGYGSQGHAHALNLRDSGVEVVVGLREGSASVAKAEEAGLPVKPIAEAVAWADVVTVLAPDQVQATLYREEIEPNIKAGSALLFSHGFNIHFGYIKPSADIDVVMVAPKGPGHTVRREFESGRGVPVLVCVEQDASGTAWDLVLSYAKAIGGTRAGAIKTTFREETETDLFGEQSVLCGGVSKLIQYGFETLVEAGYQPEMAYFEVCHEMKLIVDLINEGGISKQRWSCSDTAEYGDYVSGPRVITPEVKEHMKEVLSDIQDGTFAKRFMDDQAAGAPEFKKLRAEGEAHPIEAAGREVRSMFAWRADVDKDYTEGSVAR$","Ketol-acid reductoisomerase","Cytoplasm","ketol-acid reductoisomerase","ketol-acid reductoisomerase ","ketol-acid reductoisomerase","","Biou V., Dumas R., Cohen-Addad C., Douce R., Job D., Pebay-Peyroula E. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. EMBO J. 1997. 16(12):3405-3415. PMID: 9218783","","","

InterPro
IPR000506
Domain

Acetohydroxy acid isomeroreductase C-terminal
PF01450	$\"[185-330]T$	IlvC

InterPro
IPR013023
Family

Acetohydroxy acid isomeroreductase
TIGR00465	$\"[16-330]T$	ilvC: ketol-acid reductoisomerase

InterPro
IPR013116
Domain

Acetohydroxy acid isomeroreductase, catalytic
PF07991	$\"[15-179]T$	IlvN

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[3-183]T$	no description
PIRSF000117	$\"[5-336]T$	Ketol-acid reductoisomerase, archaeal/bacterial type
PTHR21371	$\"[81-341]T$	FAMILY NOT NAMED
PTHR21371:SF1	$\"[81-341]T$	SUBFAMILY NOT NAMED

","BeTs to 19 clades of COG0059COG name: Ketol-acid reductoisomeraseFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0059 is a-m-k-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000506 (Acetohydroxy acid isomeroreductase) with a combined E-value of 2e-148. IPB000506A 19-44 IPB000506B 57-91 IPB000506C 112-162 IPB000506D 170-221 IPB000506E 237-277 IPB000506F 313-323","Residues 6-33 are 92% similar to a (REDUCTOISOMERASE KETOL-ACID OXIDOREDUCTASE ACID ISOMEROREDUCTASE ACETOHYDROXY-ACID BRANCHED-CHAIN ALPHA-KETO-BETA-HYDROXYLACIL BIOSYNTHESIS AMINO) protein domain (PDA0G4M6) which is seen in ILVC_MYCTU.Residues 34-88 are 69% similar to a (REDUCTOISOMERASE OXIDOREDUCTASE ACETOHYDROXY-ACID BRANCHED-CHAIN KETOL-ACID ALPHA-KETO-BETA-HYDROXYLACIL BIOSYNTHESIS ACID ISOMEROREDUCTASE AMINO) protein domain (PD881313) which is seen in ILVC_BRUSU.Residues 34-115 are 79% similar to a (OXIDOREDUCTASE NADP DEHYDROGENASE REDUCTOISOMERASE 6-PHOSPHOGLUCONATE PENTOSE SHUNT UTILIZATION GLUCONATE KETOL-ACID) protein domain (PD378363) which is seen in ILVC_LEPIN.Residues 34-115 are 78% similar to a (REDUCTOISOMERASE KETOL-ACID ACID ACETOHYDROXY-ACID BRANCHED-CHAIN BIOSYNTHESIS AMINO ALPHA-KETO-BETA-HYDROXYLACIL ISOMEROREDUCTASE NADP) protein domain (PD781231) which is seen in ILVC_PSEPK.Residues 118-325 are similar to a (REDUCTOISOMERASE KETOL-ACID ACID OXIDOREDUCTASE ACETOHYDROXY-ACID BRANCHED-CHAIN BIOSYNTHESIS AMINO ALPHA-KETO-BETA-HYDROXYLACIL ISOMEROREDUCTASE) protein domain (PD002380) which is seen in Q6AEP2_BBBBB.","","-74% similar to PDB:1NP3 Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa (E_value = 1.1E_111);-54% similar to PDB:1YRL Escherichia coli ketol-acid reductoisomerase (E_value = 1.3E_40);-54% similar to PDB:1QMG ACETOHYDROXYACID ISOMEROREDUCTASE COMPLEXED WITH ITS REACTION PRODUCT DIHYDROXY-METHYLVALERATE, MANGANESE AND ADP-RIBOSE. (E_value = 3.4E_25);-54% similar to PDB:1YVE ACETOHYDROXY ACID ISOMEROREDUCTASE COMPLEXED WITH NADPH, MAGNESIUM AND INHIBITOR IPOHA (N-HYDROXY-N-ISOPROPYLOXAMATE) (E_value = 3.4E_25);","Residues 14 to 111 (E_value = 0.0033) place ANA_0292 in the CoA_binding family which is described as CoA binding domain.Residues 15 to 179 (E_value = 3.5e-118) place ANA_0292 in the IlvN family which is described as Acetohydroxy acid isomeroreductase, catalytic domain.Residues 185 to 330 (E_value = 3.1e-77) place ANA_0292 in the IlvC family which is described as Acetohydroxy acid isomeroreductase, catalytic domain.","","reductoisomerase (ilvC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0293","304413","303154","1260","9.17","8.21","42692","ATGAAGCACGTCGGACTGCTGGTCCTGGGCTCCTTCATCAACTCGCTGGGAACGGGCCTGAGCGCCTTCGGCCTGGCCGTCGTCGTGCTGCGCGTCTACGGGACGGCATCCTCAGTGGCAGCCGTCCAGATGAGCGCCTTCGCCCCCATTGTTCTTCTGGCACCCCTGGCCGGGGTCCTCGCAGACCGCTACGACCGCCGCCTGATGATGATGATCGGTGACGCCGGCTCGATTCTCGGGCTGGGCGTCATCCTGACGGCCCTGTCCTCGCCCCGGCCCTCCTTGGGCTGGATCTGCGCAGGAGCCGTCACCTCCTCCTGCCTGGCGGCCCTGACCGAGCCGGCGCTGCGGGCCAGCGTCACCGACCTGGTGACCGAGGAGGACTACGTGCGCTCCTCCGGTCTGCTCCAGCTCGCCTCCGCTGCCAAGTACCTGCTGGCGCCGGCCGCGGCGGGGTTCCTCATGCCTCTTGTCGGCCCCCGGGGTCTCGTGCTGCTGGACGCCAGCACCTGCCTGGTCACCGTGGCGTGCACCATGACAGTGCGCCAGGCTCTGGCAGCAGGTGCCTCGCAACGCGCAGCGTCCCAGCCCGGTGACGACCGCGACGTCATAGCGGGCTGGAGGACCATCATTGCCTCCCCCGGTCTGCGTACCCTCGTGACTCTCATGATGCTGGCGACCCTCTCCATCGGAGTCATCCAGGTTCTCATCAAGCCGATTCTCCTGCCCACCGTGAGCACCGCCGAGATGGGGGTGGTCGAGACGGTGGCCGCCACCGGCATGCTCGTGGGCGCGGCCCTGGTCACGGCCTGGAAGAGCGCCCAGCCCACGACACTGCTTGCCGCAGGGCTGGCCGGAACCGGCGCCGCCATGGCGCTGGTCCCCCTGGGGCCGGGCGCCTGGTGGGTGGCCGCCTGCGGCTTCCTCACCTTCGCCTGCCTGCCCCTGTCCCAGGCGGGTGCGGAGGTCCTGGTGCGCACGCAGGTCGACAACACTCGGCAGGCACGCACCTGGGGCACGATCAGCCTGGTCACCCAGATGGGCTACCTGGTGGCCTACCTGTGCTCCGGGGCACTGGTGGACCATGTGCTCCAGCCCCTGCTAGAGCCCGGACGGTCGCTGTCCACCAGTGTGGGAGCCGTCGTCGGCATCGGCCCGGGACGCGGCGCCGCCCTGCTCGTGGGCCTCATGGGCGCGGTCATGGCCCTGGTAGCTCTCACCGTTCGCCTCCAGCGACGCCGGCTCGCCTCACCCCAGTAG","MKHVGLLVLGSFINSLGTGLSAFGLAVVVLRVYGTASSVAAVQMSAFAPIVLLAPLAGVLADRYDRRLMMMIGDAGSILGLGVILTALSSPRPSLGWICAGAVTSSCLAALTEPALRASVTDLVTEEDYVRSSGLLQLASAAKYLLAPAAAGFLMPLVGPRGLVLLDASTCLVTVACTMTVRQALAAGASQRAASQPGDDRDVIAGWRTIIASPGLRTLVTLMMLATLSIGVIQVLIKPILLPTVSTAEMGVVETVAATGMLVGAALVTAWKSAQPTTLLAAGLAGTGAAMALVPLGPGAWWVAACGFLTFACLPLSQAGAEVLVRTQVDNTRQARTWGTISLVTQMGYLVAYLCSGALVDHVLQPLLEPGRSLSTSVGAVVGIGPGRGAALLVGLMGAVMALVALTVRLQRRRLASPQ$","Macrolide-efflux protein","Membrane, Cytoplasm","macrolide-efflux protein, putative","K08217 MFS transporter; DHA3 family; macrolide efflux protein","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[7-361]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[6-363]T$ $\"[389-419]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF7	$\"[6-363]T$ $\"[389-419]T$	PERMEASE-RELATED
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[31-53]?$ $\"[68-88]?$ $\"[94-112]?$ $\"[219-239]?$ $\"[245-267]?$ $\"[277-295]?$ $\"[301-319]?$ $\"[340-360]?$ $\"[388-408]?$	transmembrane_regions

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[15-28]T$ $\"[36-59]T$	HTHTETR
PF00440	$\"[15-61]T$	TetR_N
PS50977	$\"[9-69]T$	HTH_TETR_2
PS01081	$\"[27-58]T$	HTH_TETR_1

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[2-61]T$	no description

","No hits to the COGs database.","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 1.6e-18. IPB001647 15-57***** IPB013571 (Tetracycline transcriptional regulator QacR-related, C-terminal) with a combined E-value of 3.2e-11. IPB013571A 9-59***** IPB013573 (Tetracycline transcriptional regulator YcdC-like, C-terminal) with a combined E-value of 4.2e-08. IPB013573B 36-77","Residues 15-68 are 75% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL FAMILY REGULATOR TETR REGULATOR TETR-FAMILY REGULATORY) protein domain (PD000384) which is seen in Q737Y5_BACC1.Residues 98-201 are similar to a (DNA-BINDING TRANSCRIPTION REGULATION TRANSCRIPTIONAL REGULATOR FAMILY TETR ACRR) protein domain (PD533793) which is seen in Q737Y5_BACC1.","","-48% similar to PDB:2IBD Crystal structure of Probable transcriptional regulatory protein RHA5900 (E_value = 2.5E_10);","Residues 15 to 61 (E_value = 4.8e-20) place ANA_0294 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator, TetR family (methyl)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0295","305147","306214","1068","5.18","-14.41","37333","ATGACGCAGACCATCAAGCTGGCAGTAATCCCGGGTGACGGCATCGGTAAGGAGGTCGTCCCCGAAGGGCTCAAGGTCCTCGAGCGAGCGCTGGAGGGAACCGGGGTCACGGTCCGTCCCACCACCTTCGACCTGGGGGCCGAGCGCTGGCACCGCACCGGCCAGACCCTCACCGATGAGGATCTCGAGGCCATCAAGGCCCATGACGCCATTCTGCTGGGAGCCGTCGGCGATCCCTCCGTCCCCTCCGGCGTGCTCGAGCGCGGCTTGCTCCTGCGCCTGCGCTTCGCCTTGGACCACTACGTCAACCTGCGTCCCTCGGTGTACTACCCGGGCGTGCCGACGCCGTTGGCCGATCCCGGCGACATCGACTTCGTCGTGGTGCGCGAGGGCACCGAGGGCCTCTACTGCGGTAACGGCGGCGTCGTGCGCCAGGGCACGGCGCACGAGATCGCCACCGAGGTCAGCGTCAACACGGCCTACGGGGTGGAGCGCCTGGTCCGCTACGCCTTCGCCAAGGCCCAGGCCAGGGCGGCCAAGCACCTCACCCTCGTCCACAAGCACAACGTGCTCGTCCACGCCGGCGACCTGTGGCGGCGCACCGTGGAGGCCGTCGGCACCGAGTACCCCGAGGTCGCCGTCGACTACTGCCACGTGGACGCCGCCACCATCTACATGGTGACCGACCCCGGCCGCTTCGACGTCATCGTCACCGACAACCTCTTCGGAGACATCCTCACCGATGAGGCCGGCGCTGTCACCGGCGGCATCGGCCTGTCGGCCTCGGGCAACATCAATCCCGAGAGGGCCTTCCCCTCCATGTTTGAGCCCGTCCACGGCTCGGCCCCGGACATCGCCGGTCAGGGCAAGGCGGACCCGACGGCCACGATCAGCGCGGTGGCCCTCATGCTCGACCACCTCGGGCTGCCCGAGGTCGCGGCGAAGGTCGAGGCCGGAGTCACTGCGGACATGGCCACTCGGCGCGGCGGCGGCCAGCGCTCCACCAGCCAGATCGGTGACGCCATCGCCGAGGCGGTGACGGCCGGGGTCGATACGTCATCGCTTTGA","MTQTIKLAVIPGDGIGKEVVPEGLKVLERALEGTGVTVRPTTFDLGAERWHRTGQTLTDEDLEAIKAHDAILLGAVGDPSVPSGVLERGLLLRLRFALDHYVNLRPSVYYPGVPTPLADPGDIDFVVVREGTEGLYCGNGGVVRQGTAHEIATEVSVNTAYGVERLVRYAFAKAQARAAKHLTLVHKHNVLVHAGDLWRRTVEAVGTEYPEVAVDYCHVDAATIYMVTDPGRFDVIVTDNLFGDILTDEAGAVTGGIGLSASGNINPERAFPSMFEPVHGSAPDIAGQGKADPTATISAVALMLDHLGLPEVAAKVEAGVTADMATRRGGGQRSTSQIGDAIAEAVTAGVDTSSL$","3-isopropylmalate dehydrogenase","Cytoplasm","3-isopropylmalate dehydrogenase (Beta-IPMdehydrogenase)(IMDH) (3-IPM-DH)","3-isopropylmalate dehydrogenase ","3-isopropylmalate dehydrogenase","","Hurley J.H., Thorsness P.E., Ramalingam V., Helmers N.H., Koshland Jr D.E., Stroud R.M. Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 1989. 86(22):8635-8639. PMID: 2682654Cupp J.R., McAlister-Henn L. NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae. J. Biol. Chem. 1991. 266(33):22199-22205. PMID: 1939242Imada K., Sato M., Tanaka N., Katsube Y., Matsuura Y., Oshima T. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution. J. Mol. Biol. 1991. 222(3):725-738. PMID: 1748999Zhang T., Koshland Jr D.E. Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase. Protein Sci. 1995. 4(1):84-92. PMID: 7773180Tipton P.A., Beecher B.S. Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases. Arch. Biochem. Biophys. 1994. 313(1):15-21. PMID: 8053675","","","

InterPro
IPR001804
Family

Isocitrate/isopropylmalate dehydrogenase
G3DSA:3.40.718.10	$\"[6-346]T$	no description
PTHR11835	$\"[43-348]T$	DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE
PF00180	$\"[6-342]T$	Iso_dh
PS00470	$\"[240-259]T$	IDH_IMDH

noIPR
unintegrated

unintegrated
PIRSF000107	$\"[3-352]T$	3-isopropylmalate dehydrogenase
PTHR11835:SF7	$\"[43-348]T$	3-ISOPROPYLMALATE DEHYDROGENASE

","BeTs to 19 clades of COG0473COG name: Isocitrate/isopropylmalate dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0473 is a-m-k-yqvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB001804 (Isocitrate/isopropylmalate dehydrogenase) with a combined E-value of 7.7e-58. IPB001804A 10-19 IPB001804B 94-106 IPB001804C 124-138 IPB001804D 181-192 IPB001804E 234-265 IPB001804F 279-306","Residues 1-79 are 60% similar to a (TARTRATE DEHYDROGENASE OXIDOREDUCTASE NAD TDH PROBABLE) protein domain (PDA1F2I5) which is seen in TTUC_ECOLI.Residues 1-343 are 79% similar to a (DEHYDROGENASE OXIDOREDUCTASE 3-ISOPROPYLMALATE NAD ISOCITRATE IMDH BETA-IPM 3-IPM-DH BIOSYNTHESIS LEUCINE) protein domain (PD186037) which is seen in LEU3_STRCO.Residues 2-342 are 48% similar to a (ADL214CP) protein domain (PDA188O9) which is seen in Q75AY4_ASHGO.Residues 10-138 are 50% similar to a (OXIDOREDUCTASE ISOCITRATE DEHYDROGENASES) protein domain (PDA0U7O6) which is seen in Q7V9S5_PROMA.Residues 120-168 are 69% similar to a (C2207) protein domain (PD734013) which is seen in Q8FGV2_ECOL6.","","-72% similar to PDB:1W0D THE HIGH RESOLUTION STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS LEUB (RV2995C) (E_value = 2.8E_107);-72% similar to PDB:2G4O anomalous substructure of 3-ISOPROPYLMALATE DEHYDROGENASE (E_value = 2.8E_107);-56% similar to PDB:1WAL 3-ISOPROPYLMALATE DEHYDROGENASE (IPMDH) MUTANT (M219A)FROM THERMUS THERMOPHILUS (E_value = 4.8E_51);-53% similar to PDB:1DPZ STUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD711 (E_value = 1.1E_50);-56% similar to PDB:1DR0 STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD708 (E_value = 1.8E_50);","Residues 6 to 342 (E_value = 5.6e-98) place ANA_0295 in the Iso_dh family which is described as Isocitrate/isopropylmalate dehydrogenase.","","dehydrogenase (Beta-IPM dehydrogenase)(IMDH) (3-IPM-DH) (3-IPM-DH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0296","306282","306935","654","4.51","-14.86","21707","ATGTCGCTACTCGGTCCCCGACGTCGGACAGCCGTCTGCCTCCTGCTCGCCGGTCTCACCGGTCTGTGTGGGTGCGACGTCCTGACCGATGCCCCACTGACCGACTCTGAGATGTCCGCCTTCCTGGCCGAGGCGGACTCACGCGCCACCCGATCGCGGGGACATGCTTTCCAGGCGACTGCGGTGGCGGCAGCGGATCAACGCTCCGCCATCACGGGGGCCCTGTCGCTCTCCCGGATCCGGAGCGACGCCGCTGTGGAGGCCGCGACGCTGGCCACAAGGGCCGCAGTGGTGGCGAGTGACCTGAGTCCGGCCGAGTCCGCCGGCCTTGAGGTTGCGAGGTCGGTGCTCGACCAGGCGATGCAGGGCGAGGACGTCGAGGCGATCACGACGGCGCTCACGAACCTTCGTGACGCCGTGGCTGCGGCCGAGTCCGCGGTCTCCTCCCGGCGCTCGTCTCAGGACCGGGCGGCTGCGCCCGGGGAGGAGAGCTCGACAGGAGTTCCTGGCAGGGGAGGGGACGGCGAGTCCGCAGAGGCAGACCGGCCGGGGGAGGGGGAGCCCGAGTCTCCCGCCCAGGTCGGCACCCCGTCCGATAGCGAGCCATCGGCCCCCCAAGACTCCGCTGAACCGGCCCAGGGATCGTCCTCTTGA","MSLLGPRRRTAVCLLLAGLTGLCGCDVLTDAPLTDSEMSAFLAEADSRATRSRGHAFQATAVAAADQRSAITGALSLSRIRSDAAVEAATLATRAAVVASDLSPAESAGLEVARSVLDQAMQGEDVEAITTALTNLRDAVAAAESAVSSRRSSQDRAAAPGEESSTGVPGRGGDGESAEADRPGEGEPESPAQVGTPSDSEPSAPQDSAEPAQGSSS$","Hypothetical protein","Extracellular, Periplasm, Cytoplasm","mKIAA0845 protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[10-28]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0297","307797","306970","828","7.17","0.54","27725","ATGAGTTCCGTTCATCGCCCCTCGGTCAGCGCTCATCGGCCGGGCCCTCGAGCCCGGTTCGCCCGGGGTGTGGTGGCCGGCACAGTCCTCCTGACCGGGGTGAGCGGATGTGCACAGGTGGATTTGGATCAGCTCTCCGGGTCGGTGTCAGGGCCTGCCTCCCCTTCCGCGGCACCGCATTCCTCGACGGCTCCGCCCCGGATGGTGATGCCCACCGCGCTGCCGACCGCCCAGGCCACGGCCGCGGCCGCGCTCACGGTCAGCTTCCCGGACCTTCCCGGCTACACCGCCTCCACCGCGCCCCCGACCTCCACGAGCACCCCGCACGGGAGCACCACCTCTACCAGGCCCGCGACGGCGTCAACCCCGGAGGCATCCTGGTCGCGCTCCTACGCCTCGACCTCCTCCGGATGCCAGGTGAGCGCCGAGGTGACCAGCGCAGCGGCGCTGCTCGTCACCGGCGGCGATGACCGCGCCCTGTCCGAGCACTGGTCCACCTCCTTGGCGGGGACCTACCCGGACTACCGGCAAACCGGTCGAGAGGAGCTCACGGCGACGAACCACTCCGCACCCTATGCCGGTATCGCCACCGCCTTCAGCGCCAGCCTCCGTGGTTCCCGGGTCGCGGGGAGGGCCTTCGTGCGGGTGTGGTCGGCCGACGGCGCAGCCGTATCAGTGACCCAGGTCTGTCAGCAGGGGGTCTTCGACGAGGCGGCGTGGGACGCCGTCCTTCACGACATCGCCGTGGACGGCCTGTCGGGTCAGTCCCGCTGGCCCACGAAGGCGGCACCCGGGTCTGAGACGCCGGCTGCCTCCACCACCGGATGA","MSSVHRPSVSAHRPGPRARFARGVVAGTVLLTGVSGCAQVDLDQLSGSVSGPASPSAAPHSSTAPPRMVMPTALPTAQATAAAALTVSFPDLPGYTASTAPPTSTSTPHGSTTSTRPATASTPEASWSRSYASTSSGCQVSAEVTSAAALLVTGGDDRALSEHWSTSLAGTYPDYRQTGREELTATNHSAPYAGIATAFSASLRGSRVAGRAFVRVWSADGAAVSVTQVCQQGVFDEAAWDAVLHDIAVDGLSGQSRWPTKAAPGSETPAASTTG$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0298","307884","309059","1176","5.04","-15.94","42137","ATGCCCGAGACAGACGCCACCTCAACCGACTTCGCATCCACCTCCTTGGCTCGCGCCGCCGAGGTCCCCGTCCCGCAGGCCGATGCGCTCGCCGGTCGATTCCCCCTGACCGCCAATCCCTCTCCCGTCGCTGACGACGAACGGGAAGCGGTCCTGGCGAGCCTCCACTTCGGTAACGCCTTCACCGACCACATGGCTCACGCCCGTTGGAGGCAGGGCGAGGGGTGGGGCGACTACGGCGTCATTCCCTACGGCAGCCTCAGCCTGTCCCCGGCCGCCGCTGTGCTCCACTACGGCCAGGAGGTCTTCGAGGGCATCAAGGCCTACCGGCACGAGGACGGATCGGTGTGGACCTTCCGCCCCCGCTACAACGCGGCGCGCCTTAACGCCTCCGCCCGGCGCATGGCTCTGCCCGAGCTGGCGGAGGAGGACTTCGTGGCCTCCCTGGTGGATCTGGTGCGCGCCGACGCCGCCTGGGTGCCCTCAGGTGAGGGCGAGTCCCTCTACCTGCGCCCCTTCGCCTTCGCCTCCGAGGCCTTCCTGGGCGTGCGCCCCGCCGCTGTGGTGGACTACTACGTCATCGCCTCTCCCGCCGGCTCCTACTTCCCTCACGGCCTGGAGCCCGTCTCCATCTGGGTGACCACCGAGTACCACCGCGCCGGACGCGGAGGGACCGGGGCGGCCAAGACCGGAGGCAACTACGCCTCCTCCCTGCTTCCCCAGCAGGAGGCCTACGCGCAGGGCTGCGACCAGGTCTGCTTCCTCGACGACGTCTCGCAGAAGAACATCGAGGAGCTCGGCGGCATGAACCTCATGGTCGTCGACGCCGACGGGACCGTGCGCACACCGCGCCTGACCGGGACGATCCTCGAGGGCTGCACCCGCAGCGCCATCATCCGCCTGCTGCGCGACTCCGGGCGGAATGTCGTGGAGGAGACCATCAGCCTTCAGGGACTGCTCGCAGACATCGAGTCGGGCCGGGTCAATGAGGTCTTCGCCTGTGGAACCGCCGCCGTCGTCGTGCCTCTGGGGCATCTCAAGGGCGAGGGCTTCGACGCCCGCATCGAGGGCAGCGAGGTCACCCGGCAGATTCACGACCGGCTCACCGCCATTCAGACCGGCCGCGCCGAGGATCCCTACGGGTGGATGTATCAGCTCGTGCCTCCTCGTTCATAA","MPETDATSTDFASTSLARAAEVPVPQADALAGRFPLTANPSPVADDEREAVLASLHFGNAFTDHMAHARWRQGEGWGDYGVIPYGSLSLSPAAAVLHYGQEVFEGIKAYRHEDGSVWTFRPRYNAARLNASARRMALPELAEEDFVASLVDLVRADAAWVPSGEGESLYLRPFAFASEAFLGVRPAAVVDYYVIASPAGSYFPHGLEPVSIWVTTEYHRAGRGGTGAAKTGGNYASSLLPQQEAYAQGCDQVCFLDDVSQKNIEELGGMNLMVVDADGTVRTPRLTGTILEGCTRSAIIRLLRDSGRNVVEETISLQGLLADIESGRVNEVFACGTAAVVVPLGHLKGEGFDARIEGSEVTRQIHDRLTAIQTGRAEDPYGWMYQLVPPRS$","Branched-chain amino acid aminotransferase","Cytoplasm","branched-chain amino acid aminotransferase","branched-chain amino acid aminotransferase ","branched-chain amino acid aminotransferase","","Green J.M., Merkel W.K., Nichols B.P. Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme. J. Bacteriol. 1992. 174(16):5317-5323. PMID: 1644759Sugio S., Petsko G.A., Manning J.M., Soda K., Ringe D. Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry 1995. 34(30):9661-9669. PMID: 7626635Okada K., Hirotsu K., Sato M., Hayashi H., Kagamiyama H. Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution. J. Biochem. 1997. 121(4):637-641. PMID: 9163511","","","

InterPro
IPR001544
Family

Aminotransferase, class IV
PD001961	$\"[248-364]T$	Q8PC84_XANCP_Q8PC84;
PTHR11825	$\"[60-387]T$	SUBGROUP IIII AMINOTRANSFERASE
PF01063	$\"[78-369]T$	Aminotran_4

InterPro
IPR005786
Family

Branched-chain amino acid aminotransferase II
PIRSF006468	$\"[27-387]T$	Branched-chain amino acid aminotransferase, BCAT1 type
PTHR11825:SF2	$\"[60-387]T$	BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE
TIGR01123	$\"[76-386]T$	ilvE_II: branched-chain amino acid aminotra

noIPR
unintegrated

unintegrated
G3DSA:3.20.10.10	$\"[233-373]T$	no description
G3DSA:3.30.470.10	$\"[28-222]T$	no description

","BeTs to 20 clades of COG0115COG name: Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyaseFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0115 is aom---yqvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB001544 (Aminotransferase, class IV) with a combined E-value of 7.5e-41. IPB001544A 97-109 IPB001544B 119-128 IPB001544C 169-182 IPB001544D 219-234 IPB001544E 263-272 IPB001544F 282-302 IPB001544G 330-343","Residues 28-87 are 60% similar to a (AMINOTRANSFERASE PROBABLE TRANSFERASE BRANCHED-CHAIN ACID AMINO) protein domain (PD809168) which is seen in Q8G5Z9_BIFLO.Residues 62-150 are 56% similar to a (AMINOTRANSFERASE ACIDS PROBABLE TRANSFERASE BRANCHED-CHAIN AMINO) protein domain (PD388665) which is seen in Q9HEB7_NEUCR.Residues 76-153 are 74% similar to a (AMINOTRANSFERASE TRANSFERASE ACID AMINO BRANCHED-CHAIN LYASE BRANCHED-CHAIN-AMINO-ACID PYRIDOXAL PHOSPHATE BIOSYNTHESIS) protein domain (PD330724) which is seen in Q8PNW2_XANAC.Residues 156-217 are 79% similar to a (AMINOTRANSFERASE TRANSFERASE BRANCHED-CHAIN AMINO ACID BRANCHED-CHAIN-AMINO-ACID PYRIDOXAL PHOSPHATE BIOSYNTHESIS BCAT) protein domain (PD867021) which is seen in Q8XGX6_RALSO.Residues 248-364 are 66% similar to a (AMINOTRANSFERASE TRANSFERASE ACID AMINO BRANCHED-CHAIN LYASE BRANCHED-CHAIN-AMINO-ACID PYRIDOXAL PHOSPHATE BIOSYNTHESIS) protein domain (PD001961) which is seen in Q8PC84_XANCP.","","-49% similar to PDB:2COG Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate (E_value = 3.0E_49);-49% similar to PDB:2COI Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with gabapentin (E_value = 3.0E_49);-49% similar to PDB:2COJ Crystal structure of reduced human cytosolic branched-chain aminotransferase complexed with gabapentin (E_value = 3.0E_49);-48% similar to PDB:2ABJ Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCl, and pyridoxal 5' phosphate. (E_value = 1.1E_48);-52% similar to PDB:2HDK Crystal Structure of Cys315Ala-Cys318Ala Mutant of Human Mitochondrial Branched Chain Aminotransferase (E_value = 9.6E_48);","Residues 78 to 369 (E_value = 1.2e-104) place ANA_0298 in the Aminotran_4 family which is described as Aminotransferase class IV.","","amino acid aminotransferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0299","309239","310375","1137","5.53","-8.08","40199","ATGACTCAGTCCCTCCTACCAGAACCCGAAAGCAGTCCGATTGAAAAGGGCGATGCTGAAGCCGCCTCGTCAGGGGCCGACACGACCTCGGCGCGCGGTGCAGGCAGCGTCCTGCGCCGTCCCGGACGAGGATGGAGGATCGCCCTTCTCAGTGTCCTGGCGATCTTCCTGGTTCTGACCCTGGCCACAGGAGGCCTGGCCCTGTGGGTGCGACACTCCATCGCCTCCGGCATCGAGTTCATCGCCGATCCCTTCGCGGGCATTCCCGCACGGGCCCCGCAGCAGAAGGTGGCCGCGGGCGAGGAACCGGCTGTCAACATCCTGGTCCTGGGGACCGACTCGCGCACCTCCGCCTCCGACCCCTCCCAGTGGAAGGAGGGGGCCCAGCGCACGGACGCGATCATGATCGTTCAGGTCAGCGGAGACCGGAAGACGGTCTCAGTCATGTCGATCCCCCGTGACTCATGGGTGGAGATCCCCGGTCACGGCCAGGGGAAGATCAACGCCGCCTACTCCTACGGGGGGCCCTCGCTGACGATCCACACCGTGGAGAACCTCACCGGCATCCACATCGACCACTTCGCGGTGGCGAACTTCGAGTCCTTCGTCGCCCTGACCGACGAGATCGGTGGGGTGCGCATCAACCTCAAGACGCCTCAGACACTCGCCGGCAAGGAACTCGGCGCAGGGGCCCAGGTACTCGACGGGCAGCAGGCCCTGGCCTACACCCGCGAGCGCTCCTCCCTGCCCAACGGGGACTTCGACCGCGTCAAGCGCCAGCAGACCTGGATGCGCTCCATCGTGAGCAGGGTCCTGACCAACGGCACCATGAGCAGTCCCACGGCTCTGTACTCCTTCCTCAAGACCGCCTCGCGGACAGTCGCCGTGGACGAGTCCTTCACGCTCAACCAGATGCAGTCCCTGGCCCTGGAGACGCGCCACCTCCACAGCAACGACATCGCCTTCATGACCGTGCCGACCGCCGGTACGGGAACCTCCACGGACGGGCAGTCCATCGTCACGCTCGACGCCGACGCGGACACCCCCTTGTTCAATGCCTTCGCCGAGGACCGGGTGAGCACCTACCTCACCGAGCACCCCGACGCCGTTGAGCTGCTCCCCGCCACGGTGAACTAG","MTQSLLPEPESSPIEKGDAEAASSGADTTSARGAGSVLRRPGRGWRIALLSVLAIFLVLTLATGGLALWVRHSIASGIEFIADPFAGIPARAPQQKVAAGEEPAVNILVLGTDSRTSASDPSQWKEGAQRTDAIMIVQVSGDRKTVSVMSIPRDSWVEIPGHGQGKINAAYSYGGPSLTIHTVENLTGIHIDHFAVANFESFVALTDEIGGVRINLKTPQTLAGKELGAGAQVLDGQQALAYTRERSSLPNGDFDRVKRQQTWMRSIVSRVLTNGTMSSPTALYSFLKTASRTVAVDESFTLNQMQSLALETRHLHSNDIAFMTVPTAGTGTSTDGQSIVTLDADADTPLFNAFAEDRVSTYLTEHPDAVELLPATVN$","Cell envelope-related transcriptional attenuator","Membrane, Cytoplasm","Transcriptional regulator","cell envelope-related transcriptional attenuator","cell envelope-related function transcriptional attenuator, LytR/CpsA family","","","","","

InterPro
IPR004474
Domain

Cell envelope-related transcriptional attenuator
PF03816	$\"[130-273]T$	LytR_cpsA_psr
TIGR00350	$\"[129-273]T$	lytR_cpsA_psr: cell envelope-related functi

noIPR
unintegrated

unintegrated
signalp	$\"[1-67]?$	signal-peptide
tmhmm	$\"[49-69]?$	transmembrane_regions

","BeTs to 7 clades of COG1316COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1316 is --------vdrlbc----------t-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","Residues 147-212 are similar to a (TRANSCRIPTIONAL REGULATOR LYTR FAMILY TRANSCRIPTION REGULATOR CPSA MEMBRANE ANTITERMINATOR MEMBRANE-BOUND) protein domain (PD003150) which is seen in Q745J4_MYCPA.Residues 260-340 are 64% similar to a (TRANSCRIPTIONAL REGULATOR MEMBRANE FAMILY CPSA REGULATOR LYTR POSSIBLE ENVELOPE-RELATED CELL) protein domain (PD372113) which is seen in Q8NSD6_CORGL.","","-52% similar to PDB:2HG4 Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS. (E_value = );-46% similar to PDB:2HVZ Solution structure of the RRM domain of SR rich factor 9G8 (E_value = );-51% similar to PDB:1H4I METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE (E_value = );-51% similar to PDB:1H4J METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE D303E MUTANT (E_value = );-59% similar to PDB:1K3V Porcine Parvovirus Capsid (E_value = );","Residues 130 to 273 (E_value = 2.9e-66) place ANA_0299 in the LytR_cpsA_psr family which is described as Cell envelope-related transcriptional attenuator domain.","","regulator ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0300","310451","311758","1308","5.28","-13.71","46799","ATGACTGACACGACTGAAGTAGCCGACGTCGCGGTCATCGGGCTGGGGTACATCGGCCTGCCCACGGCAGCGGTCCTGGCCCGCGCCGGGCTCGACGTCGTCGGGGTGGACCGGATCCGGGAACGTGTCGAGGCCGTCAACCGCGGAGAGCTTCCCTTCCTCGAGGAGGGGCTGGCCACCGTGCTGGCCGAACAGGTCGAGGCCGGCCGCCTGCGCGCCCAAATGGAGACGCCCTCGGCACGGACCTACATCATCGCGGTGCCGACCCCGTTGATGGGCTCGGACCACGCGGCCGATCTGTCCCTGGTGGAGGCCGCTACCAGGCAGATCGCCCCTCGTCTCACAGGGGGAGAGCTCATCGTCCTGGAGTCGACCTGCCCGCCCGGTACCACTCGCGCCCTGGCTGAGGCGATCGGCTCGATGCGCCCGGACCTGTCCACGGACGGCAGCGGCGCACGGCCCCAGGTGCATCTGTCCTACTGCCCCGAACGCGTGCTGCCCGGGCGCATCATGACGGAGATGGTGACCAACTCCCGGGTCATCGGCGGCCTGACCCCCGAGGCCTCGCACCTGGCCAGAGACCTGTACGCCACCTTCTGCGCCGGCGAGCTGGTCCTGACCGACGCCACCACCGCCGAGATGACCAAACTGACGGAGAACTCCTTCCGTGACCTCAACATCGCCTTCGCCAACGAGCTGGCCCTTGTCTGCGAGCGGGTCGGGGTGGATGTCTGGGAACTCGTCGACCTGGCCAACCGCCATCCGCGGGTGAGCATTCTGCAGCCGGGCCCCGGCGTGGGCGGCCACTGCATCGCCGTGGACCCCTGGTTCCTGGTGTCCAGCGCTCCGGAGGAGACCCGGCTCATCCGCACGGCCCGCCAGGTCAATGACTCCCGGCCGGCCCACTACGTCGGGCGCATCCTTGAGGCGATGGAGCCCTTCTCCTCGCCGATCGTGGCGGTACTCGGCCTGACCTTCAAGGCCGATGTCGATGACCTGCGCCAGTCGCCGGCGCTTGCGATCACTGAGCAGGTTGCCGCCGCCGCGCCCCATGCCCGGGTGCTGGTGGCTGAGCCGCACGCCAAGGAGCTCCCGGCGTCTTTGGCGCGGTGGGACAACGTGCGGCTGACCGGGTGGCGGCAGGCCGTCGAACAGGCTGATGTCGTGGCGGTGCTGGTTGGCCACCAGGAGTTCGCCGACCTTGATCCGCACCTGCTCGAGGGGCGCAGAGTCATCGACGCCACGGGGTTCTGGCGCGCCCGAGAGCCCCAGCTGACGGGTAGAAGGACATGGGCGGCAGGCGTCTGA","MTDTTEVADVAVIGLGYIGLPTAAVLARAGLDVVGVDRIRERVEAVNRGELPFLEEGLATVLAEQVEAGRLRAQMETPSARTYIIAVPTPLMGSDHAADLSLVEAATRQIAPRLTGGELIVLESTCPPGTTRALAEAIGSMRPDLSTDGSGARPQVHLSYCPERVLPGRIMTEMVTNSRVIGGLTPEASHLARDLYATFCAGELVLTDATTAEMTKLTENSFRDLNIAFANELALVCERVGVDVWELVDLANRHPRVSILQPGPGVGGHCIAVDPWFLVSSAPEETRLIRTARQVNDSRPAHYVGRILEAMEPFSSPIVAVLGLTFKADVDDLRQSPALAITEQVAAAAPHARVLVAEPHAKELPASLARWDNVRLTGWRQAVEQADVVAVLVGHQEFADLDPHLLEGRRVIDATGFWRAREPQLTGRRTWAAGV$","UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase","Cytoplasm","UDP-N-acetyl-D-mannosaminuronic aciddehydrogenase VC0918","UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase ","UDP-glucose/GDP-mannose dehydrogenase","","Roychoudhury S., May T.B., Gill J.F., Singh S.K., Feingold D.S., Chakrabarty A.M. Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa. J. Biol. Chem. 1989. 264(16):9380-9385. PMID: 2470755Campbell R.E., Sala R.F., van de Rijn I., Tanner M.E. Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol. J. Biol. Chem. 1997. 272(6):3416-3422. PMID: 9013585","","","

InterPro
IPR001732
Domain

UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03721	$\"[8-201]T$	UDPG_MGDP_dh_N

InterPro
IPR014026
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation
PF00984	$\"[209-301]T$	UDPG_MGDP_dh

InterPro
IPR014027
Domain

UDP-glucose/GDP-mannose dehydrogenase, C-terminal
PF03720	$\"[320-414]T$	UDPG_MGDP_dh_C

InterPro
IPR014028
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding
PTHR11374	$\"[169-421]T$	UDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC DEHYDROGENASE

InterPro
IPR014360
Family

UDP-glucose/GDP-mannose dehydrogenase
PIRSF000124	$\"[8-435]T$	UDP-glucose/GDP-mannose dehydrogenase

InterPro
IPR014687
Family

UDP-N-acetyl-D-mannosaminuronate dehydrogenase
PIRSF500136	$\"[8-423]T$	UDP-N-acetyl-D-mannosaminuronate dehydrogenase

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.220	$\"[209-295]T$	no description
G3DSA:3.40.50.1870	$\"[298-431]T$	no description
G3DSA:3.40.50.720	$\"[8-199]T$	no description
PTHR11374:SF4	$\"[169-421]T$	UDP-N-ACETYL-D-MANNOSAMINURONIC ACID DEHYDROGENASE
signalp	$\"[1-27]?$	signal-peptide

","BeTs to 8 clades of COG0677COG name: UDP-N-acetyl-D-mannosaminuronate dehydrogenaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0677 is --m-k---v-----efghs--j----Number of proteins in this genome belonging to this COG is 2","***** IPB001732 (UDP-glucose/GDP-mannose dehydrogenase) with a combined E-value of 6.8e-82. IPB001732A 9-20 IPB001732B 33-62 IPB001732C 80-90 IPB001732D 119-129 IPB001732E 158-183 IPB001732F 207-258 IPB001732G 265-274 IPB001732H 319-357","Residues 1-274 are 39% similar to a (LMBL) protein domain (PD824343) which is seen in Q54365_STRLN.Residues 10-70 are 68% similar to a (DEHYDROGENASE UDP-GLUCOSE OXIDOREDUCTASE 6-DEHYDROGENASE NAD 3-HYDROXYISOBUTYRATE BIOSYNTHESIS UDP-GLUCOSE/GDP-MANNOSE UDP-GLCDH UDPGDH) protein domain (PD398280) which is seen in Q9KTI4_VIBCH.Residues 68-413 are 40% similar to a (DEHYDROGENASE UDP-GLUCOSE/GDP-MANNOSE FAMILY UDP-GLUCOSE-6-DEHYDROGENASE) protein domain (PD102173) which is seen in Q93N63_COXBU.Residues 80-197 are 46% similar to a (DEHYDROGENASE NUCLEOTIDE-SUGAR) protein domain (PDA0X8E9) which is seen in Q9FBM9_STRCO.Residues 118-341 are 44% similar to a (DEHYDROGENASE UDP-N-ACETYL-D-MANNOSAMINURONIC ACID) protein domain (PD836650) which is seen in Q8DPX4_STRR6.Residues 160-192 are 87% similar to a (DEHYDROGENASE OXIDOREDUCTASE 1.1.1.- ACID UDP-N-ACETYL-D-MANNOSAMINE UDP-N-ACETYL-D-MANNOSAMINURONIC NAD UDP-MANNAC ENZYME POLYSACCHARIDE) protein domain (PD874019) which is seen in Q7VKN5_HAEDU.Residues 160-302 are 53% similar to a (CALS8) protein domain (PDA1C8Y3) which is seen in Q8KNF6_MICEC.Residues 195-242 are 83% similar to a (DEHYDROGENASE OXIDOREDUCTASE UDP-GLUCOSE/GDP-MANNOSE POLYSACCHARIDE 1.1.1.- BIOSYNTHESIS ACID UDP-N-ACETYL-D-MANNOSAMINE NAD FAMILY) protein domain (PD683562) which is seen in Q74C21_GEOSL.Residues 220-297 are 76% similar to a (UDP-GLUCOSE DEHYDROGENASE 6-DEHYDROGENASE OXIDOREDUCTASE NAD UDP-GLCDH UDPGDH UDP-GLC SUGAR NUCLEOTIDE) protein domain (PD001282) which is seen in O26924_METTH.Residues 244-297 are similar to a (DEHYDROGENASE OXIDOREDUCTASE UDP-GLUCOSE/GDP-MANNOSE POLYSACCHARIDE 1.1.1.- BIOSYNTHESIS ACID UDP-N-ACETYL-D-MANNOSAMINE NAD FAMILY) protein domain (PDA0A7T9) which is seen in Q9RMD5_ACILW.Residues 258-401 are 44% similar to a (NDP-N-ACETYL-D-GALACTOSAMINURONIC OXIDOREDUCTASE DEHYDROGENASE ACID 1.1.1.-) protein domain (PDA0U115) which is seen in Q8PXR2_METMA.Residues 317-418 are 60% similar to a (DEHYDROGENASE OXIDOREDUCTASE 1.1.1.- UDP-N-ACETYL-D-MANNOSAMINE NAD UDP-MANNAC ACID UDP-N-ACETYL-D-MANNOSAMINURONIC NDP-N-ACETYL-D-GALACTOSAMINURONIC LIPOPOLYSACCHARIDE) protein domain (PD598697) which is seen in EPD2_RALSO.","","-44% similar to PDB:1MFZ Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa (E_value = 2.6E_25);-44% similar to PDB:1MUU 2.0 A crystal structure of GDP-mannose dehydrogenase (E_value = 2.6E_25);-44% similar to PDB:1MV8 1.55 A crystal structure of a ternary complex of GDP-mannose dehydrogenase from Psuedomonas aeruginosa (E_value = 2.6E_25);-43% similar to PDB:2O3J Structure of Caenorhabditis Elegans UDP-Glucose Dehydrogenase (E_value = 6.7E_21);-42% similar to PDB:1DLI THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION (E_value = 3.7E_11);","Residues 7 to 45 (E_value = 7e-06) place ANA_0300 in the NAD_binding_2 family which is described as NAD binding domain of 6-phosphogluconate dehydrogenase.Residues 8 to 201 (E_value = 6.6e-59) place ANA_0300 in the UDPG_MGDP_dh_N family which is described as UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain.Residues 9 to 38 (E_value = 1.7e-05) place ANA_0300 in the DAO family which is described as FAD dependent oxidoreductase.Residues 10 to 51 (E_value = 1.1e-05) place ANA_0300 in the ApbA family which is described as Ketopantoate reductase PanE/ApbA.Residues 209 to 301 (E_value = 1.2e-44) place ANA_0300 in the UDPG_MGDP_dh family which is described as UDP-glucose/GDP-mannose dehydrogenase family, central domain.Residues 320 to 414 (E_value = 1.5e-16) place ANA_0300 in the UDPG_MGDP_dh_C family which is described as UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain.","","acid dehydrogenase VC0918 (ECA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0303","311740","314949","3210","6.96","-0.44","113992","ATGGGCGGCAGGCGTCTGAGACGTCTCATCGGTGCGGCTGTGCGCGGCGTGCACCGGCCCCGACTCAGCGTCATCGTCCGAGCAGCGGGGGCCGGTCCTCACCTGGAAGGGGCCATCCGCTCCGTACTCAACCAGACCTTCAGGGACCTGGAGGTCCTGGTCGTCGTCGGTCCGGGGGCCGATGCGCTGAGCTCCGGTGAGCAGGTGGCCACCGGCCTGTCCGCCAGGGACCGGCGCGTCCGGGTCGTGTCCTGCGACCCGGACGATCACCGGGGCGCTGGCCCGGATGGCTGGCTGGATACCGCCCTGAAACGAGCCAGGGGAGGCCTGGTGACCGTCATTGACGGTGGGGATGGGATGGTCGCCGGTGCCTGCCAGTCGATGATTGAGTGCCTGGAGCGGTCGGGCTCCGACGTCGTCGTCGCGCGCTCGCGGTCCTTGACACTGGCAACCGGGGCCGGGCAGGGGGCGGGACCTCCCCGCGCGCCTCGTCTCGCGCAGCCGCTGGCTCGGGTGCCCGAGGCGGTTGAGGAGCTGGTGGCCGGCGCGGTCATGGCGCGCCGAAGGCTGTGGGCACCGCCGAGACGGCCTCGAGTGCTCCGCGCCCCCGCCGTGTCACTGCCCGCCAGGGCCCTCGCGGTGCTTCTGGCCGCGACCCGGATGGACGTCCTGGATGAGGAGGTCTACACCTGGCGCGCAGGCTCTGCGGCCCGTGGCCTCAGTGCGGACACGGATCCCGTCGGCCTCCTGGCGGAGGTGGACGCTTTGGCGCAGCTGGCCGCCGACGCCCCGGAGGCGGTGCGTCGGAGCCTGGTCGCCGGACGCCTGAGTCGGGACCTGGTTCGTCTGGCCGAGGTCGCGCACCGGGAGGGGGCCGACTTCGCCAGCAGGCTCCGCCGCACTGCGAAGAGAGTGCTCGCCGATGCCGACGACCTCGTGTGGGAGGCGGTCGGGCTGCTCGACCGACTGGTGCTGTGGCTCCTCATCCAGGACGAGCCGGCCGGCGCCGTGGAGCTCGAGGAGCTGATCGGCAGACGCTGCGAGGACCTGGGCCACCTTCCCCTGACCATCGAGGCGGGCACCGTGCGCCCCGAGCCTGCTCTCCTGGAAGGGGCCCCGGTGCCCCGCCGACTCACCGAGATCCGGGACGCCGACTTAAGACTGCATGTCGGTGTCGACGCGGTGCGCTGGCTGGGCCCCAGGACCCTGGAGGTACGCGGATGCGCCTGGGTCTGGGGGCTCGACCCAGGCCTGATCGACCGCCCGACCGTCGAGGTGGTCGATGAGACCGGACGAGTTCGAGGCCGTGCCCAGGCTGATCGTTGTGAGGCCCCCCGAGCCGACCTGGAGGCCGGCGACCCGTGCCGCTCCTACCTCACCTCGGGGATCGTGGTGCGTCTGCAGGTCGAAGCGGGCCGCCCCTCCTGGTTCCGGGTGGTGACCCGCGTTGCCGGGCGAGAGGTGCGGGCATGGATGCCGCAACCGGCCGGCTCCAGCAGGAGGCACCTGGCGCCGCCGGAGACCGGGCAGCATCTGGAGGCGCGCGGTCAGCGGGGGCTGCTCCAGGTCGCCCCGGCGCCGAGCGGGATCCGGGGGAGCGAGGCGCGGCCCGGCGGGGAGATCGACGTCGTGCTCCTCTGCGCGCGTCTGGACACTGACGCAACGCTGGAGCTGAGCGGAACGGTGGCGCCGGCCCCGGATGGGCTGGATATCGTCCTGGGCGGCAGGGCCGCCGAGGCTCGGGCGATGACGGTGCCGGCCGTCCTGGCCCCTGGCGGCGGCTGGTCGGCAAGCATCGATCTGGCTGATCCCGACGTCGAGCTGGCGACCTACCCGCTGAGCTGGAGCACCGTATCGCAGGACGAGCCCGGCAACCGGATCAAGGGAGCCTGCCTGGCCGGAGAAGGGATCGACGGTCCGGCCACCGAGGTTCCCATCGCCGCGGCGCCCACTAGCTCCGCGGCGGAACCCGATAGCGACGTCACCGGGGCGGATGCCGGGCGCCCGGCGCGCCGCGCGCGGATCCTCACCCGCACGGACGGCTCCGTGGCCGTTGCTGTCATCCCTCCGCTGACTCCTGGCGAGCGCTCACGACGGGGCCACCGGCTCCTCATCGAGCGCGAGGCGGGCCCCCTGAGACCGGGAGTGTTCCTGGAGTCCTTCGGTGGACGCAGCGCGGGAGACAACCCGGCCGCCATCTGCGAGGACCTGGCGGCCCACGGCGTGGGAGCGCCCCTGTGGTGGTCGGTTGTCGACGGGACGGTTCGCGTGCCGGCGGGCGCGTGCCCCGTCGTCGTCGGATCCCCGCAGTGGGTGGAGGCGCTGCGCACCTCACGTGTCATCGTCACCAACGACCACCTCCCCTCCTGGTTCTCCAAGCGTGAGGGCCAGTACCTGCTCCAGACCTGGCACGGCACTCCGATCAAGAAGCTGTTGCACGACGCGCCGAGAGCCGTCACCCTGAGATACCGGCGACTCATGGACCGCCAGGTTCCCCAGTGGGACCTGCTGCTGGCCCAGAGCCCGCAGGCCGGTCGGCGCCTTCAACAGGCACTGGGATACTGCGGGCCGGTTCGGGTGGGGGAGTACCCCCGCAACGTGAGGCTGCTCGGAGGCGCTGAAGTACGGCGACGGGTGCGCCACGAGCTCGGTATCGCTCCGGGACAGCCCGTCATTCTCTACGCCCCGACCTGGCGCGAGAGCCTGCGGCCCTCGACGGGTGCAGCCGGCTGCGCCGCCGCGCACGGGCCGGGACCTGTGGGGGCGCTGGACGGGCCGCGTCTGGCTGAGCTCCTCGATGCGGTGGTCCTGATGCGCAGCCACCACATGAACCGGGTCGGATGTGTCCCAGGGATGATCGATGTCAGTGGGTACCCGAGTGTCGAGGAACTCATGCTGGCGGCCGACATCCTGGTCTCGGACTACTCGAGCATCTTCTTCGACTTCGCTCTGACCGGGAAACCGGCAGTGGTCTACGCACCCGACCTGGCCTCCTACCGAGATGTCGAAAGGGGCCTGTACGGTGACTGGCCCCTGGGCTCGGGGCTGCCGGTCGCCGCCGACCACGATGAGCTCGCATCCCACCTGCAGCGGCTCCTCGGCGACATCGACGTCGCTGAGGGGTGCCACTCCCCACTGGAGGTGGAACCCGTGCCGATCCTGGACAACCTCACGTGGATCCGGGGATGGATCGCTCGTTTCCTGAGCTGA","MGGRRLRRLIGAAVRGVHRPRLSVIVRAAGAGPHLEGAIRSVLNQTFRDLEVLVVVGPGADALSSGEQVATGLSARDRRVRVVSCDPDDHRGAGPDGWLDTALKRARGGLVTVIDGGDGMVAGACQSMIECLERSGSDVVVARSRSLTLATGAGQGAGPPRAPRLAQPLARVPEAVEELVAGAVMARRRLWAPPRRPRVLRAPAVSLPARALAVLLAATRMDVLDEEVYTWRAGSAARGLSADTDPVGLLAEVDALAQLAADAPEAVRRSLVAGRLSRDLVRLAEVAHREGADFASRLRRTAKRVLADADDLVWEAVGLLDRLVLWLLIQDEPAGAVELEELIGRRCEDLGHLPLTIEAGTVRPEPALLEGAPVPRRLTEIRDADLRLHVGVDAVRWLGPRTLEVRGCAWVWGLDPGLIDRPTVEVVDETGRVRGRAQADRCEAPRADLEAGDPCRSYLTSGIVVRLQVEAGRPSWFRVVTRVAGREVRAWMPQPAGSSRRHLAPPETGQHLEARGQRGLLQVAPAPSGIRGSEARPGGEIDVVLLCARLDTDATLELSGTVAPAPDGLDIVLGGRAAEARAMTVPAVLAPGGGWSASIDLADPDVELATYPLSWSTVSQDEPGNRIKGACLAGEGIDGPATEVPIAAAPTSSAAEPDSDVTGADAGRPARRARILTRTDGSVAVAVIPPLTPGERSRRGHRLLIEREAGPLRPGVFLESFGGRSAGDNPAAICEDLAAHGVGAPLWWSVVDGTVRVPAGACPVVVGSPQWVEALRTSRVIVTNDHLPSWFSKREGQYLLQTWHGTPIKKLLHDAPRAVTLRYRRLMDRQVPQWDLLLAQSPQAGRRLQQALGYCGPVRVGEYPRNVRLLGGAEVRRRVRHELGIAPGQPVILYAPTWRESLRPSTGAAGCAAAHGPGPVGALDGPRLAELLDAVVLMRSHHMNRVGCVPGMIDVSGYPSVEELMLAADILVSDYSSIFFDFALTGKPAVVYAPDLASYRDVERGLYGDWPLGSGLPVAADHDELASHLQRLLGDIDVAEGCHSPLEVEPVPILDNLTWIRGWIARFLS$","Glycosyl/glycerophosphate transferase involved in teichoic acid biosynthesis","Cytoplasm, Extracellular","putative glycosyltransferase","teichoic acid biosynthesis domain protein","CDP-glycerol glycerophosphotransferase","","Fitzgerald S.N., Foster T.J. Molecular analysis of the tagF gene, encoding CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase of Staphylococcus epidermidis ATCC 14990. J. Bacteriol. 2000. 182(4):1046-1052. PMID: 10648531","","","

InterPro
IPR007554
Family

CDP-glycerol glycerophosphotransferase
PF04464	$\"[879-1062]T$	Glyphos_transf

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[20-145]T$	no description

","BeTs to 4 clades of COG1887COG name: Putative glycosyl/glycerophosphate transferases involved in teichoic acid biosynthesis TagF/TagB/EpsJ/RodCFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1887 is --m-k------lb-------------Number of proteins in this genome belonging to this COG is 1","***** IPB007554 (CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase) with a combined E-value of 3.9e-13. IPB007554E 889-899 IPB007554F 969-1002","Residues 779-866 are 61% similar to a (TEICHOIC ACID BIOSYNTHESIS TRANSFERASE GLYCOSYL GLYCOSYLTRANSFERASE B WALL F CELL) protein domain (PD135736) which is seen in Q8CJZ1_STRCO.Residues 891-1037 are 51% similar to a (TEICHOIC ACID BIOSYNTHESIS TRANSFERASE B GLYCOSYLTRANSFERASE GLYCOSYL WALL F CELL) protein domain (PD007030) which is seen in Q8CJZ1_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 879 to 1062 (E_value = 9e-23) place ANA_0303 in the Glyphos_transf family which is described as CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase.","","glycosyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0304","315214","315606","393","5.59","-2.61","14895","ATGAAGCGCGTGATTACCTATGGCACATATGACCTGCTCCACTATGGTCATATTGCATTGCTGAAGCGTGCGCGAGCGCTGGGGGACTTCCTGATGGTGGCGCTGTCCAGTGATGAGTTCAATGCCGGAAAGGGTAAGCAGGCCTACTTCTCCTACGAGGAGCGCAAGGTGATGCTCGAAGCCATCCGGTATGTCGATCTCGTGGTGCCCGAGATGACCTGGGGGCAGAAGACCGAGGATATCGCCAAATACGGTATTGATGTCTTCGTCATGGGGGACGACTGGAACGGCGAGTTCGACGACCAGCTCAAGGGGCTGTGTGAGGTCGTCTACCTCCCGCGGACTCCCGAGGTATCAACGACTCGGATCAAGAGTGATATGCGCCTGGGCTGA","MKRVITYGTYDLLHYGHIALLKRARALGDFLMVALSSDEFNAGKGKQAYFSYEERKVMLEAIRYVDLVVPEMTWGQKTEDIAKYGIDVFVMGDDWNGEFDDQLKGLCEVVYLPRTPEVSTTRIKSDMRLG$","Glycerol-3-phosphate cytidylyltransferase","Cytoplasm","glycerol-3-phosphate cytidylyltransferase ,CDP-glycerol pyrophosphorylase (teichoic acid","glycerol-3-phosphate cytidylyltransferase ","glycerol-3-phosphate cytidylyltransferase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR004820
Domain

Cytidylyltransferase
PF01467	$\"[5-126]T$	CTP_transf_2

InterPro
IPR004821
Domain

Cytidyltransferase-related
TIGR00125	$\"[3-68]T$	cyt_tran_rel: cytidyltransferase-related do

InterPro
IPR006409
Family

Glycerol-3-phosphate cytidylyltransferase
TIGR01518	$\"[4-127]T$	g3p_cytidyltrns: glycerol-3-phosphate cytid

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[1-127]T$	no description

noIPR
unintegrated

unintegrated
PTHR10739	$\"[4-127]T$	CHOLINE/ETHANOLAMINE PHOSPHATE CYTIDYLYLTRANSFERASE

","BeTs to 10 clades of COG0615COG name: CytidylyltransferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane] Functional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0615 is aompkzyq---lb-------------Number of proteins in this genome belonging to this COG is 3","***** IPB001980 (Lipopolysaccharide core biosynthesis protein signature) with a combined E-value of 1.3e-22. IPB001980A 2-20 IPB001980B 20-41 IPB001980C 53-77 IPB001980D 85-101 IPB001980E 104-126","Residues 2-98 are 56% similar to a (ADP-HEPTOSE SYNTHASE) protein domain (PDA186D6) which is seen in Q7M9U1_WOLSU.Residues 3-127 are 50% similar to a (CYTIDYLYLTRANSFERASE TRANSFERASE CTP-PHOSPHOETHANOLAMINE CTP:ETHANOLAMINE NUCLEOTIDYLTRANSFERASE) protein domain (PD729236) which is seen in Q84JV7_CHLRE.Residues 3-94 are 57% similar to a (CYTIDYLYLTRANSFERASE TRANSFERASE NUCLEOTIDYLTRANSFERASE PHOSPHOETHANOLAMINE) protein domain (PD737934) which is seen in Q84X92_HORVD.Residues 9-127 are 85% similar to a (TRANSFERASE GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE NUCLEOTIDYLTRANSFERASE CYTIDYLTRANSFERASE BIOSYNTHESIS TEICHOIC ACID D TAGD) protein domain (PD001938) which is seen in Q8G7N8_BIFLO.","","-83% similar to PDB:2B7L Crystal Structure of CTP:Glycerol-3-Phosphate Cytidylyltransferase from Staphylococcus aureus (E_value = 3.8E_47);-81% similar to PDB:1COZ CTP:GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE FROM BACILLUS SUBTILIS (E_value = 2.3E_44);-81% similar to PDB:1N1D Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol (E_value = 2.3E_44);","Residues 5 to 126 (E_value = 2.7e-26) place ANA_0304 in the CTP_transf_2 family which is described as Cytidylyltransferase.","","cytidylyltransferase , CDP-glycerol pyrophosphorylase (teichoic acid biosynthesis protein D) homolog tagD (gct)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0305","315747","319736","3990","7.00","0.08","146436","ATGAGTAAGGATACTGTTCTCAGAAAAATGGGGCGTGCCGTTTCCGGCCGCCTGCAGCTGCCGGCCACCACCCGGCTGGTGCGCTATGCCGCCGCCAGGGAGTACGAGGACGGTAACCTGGCTGAGGCAAAGCGTCTGTATGAAAAACTCTCTGAGAGCGGCCACGACACGGCCAGCCGGCTGCGGCTGGGAGTCATCGCTGAGCGTCAGGAACGGTTCGAGGCGGCCTTGAGGACCTACACCGAGGTGGCCGACCGCGACCCCTCCTGCGGAGAGGCCTTCTACCGTGCCGGCTGCCTCCTCAAGCGTCAGGACGATCCGGAGGGGGCCTCCGTCTTCTTCTCGCGGGCCCTCTCCTCGGGGGTGCGGGACCGGCGCTACTCGGAGAATCTGCTCGCCTGCCTGCCCGCGAGCACCCCGCAGTGGCAGCGCCTGGAGGTTCTGCTCTCCGGACTGCCGGAGCACGAGAACGACGCCGCCTGGCTGCGCAAGCTCCTTCAGGCTCAGCTTCACCTGGGGCTCAACGGGCCGGCCAGGTGCACCCTGGACGCCCTGGCCGACATCGACGAGCTCAGCGCGCAGGAGCTCTTCGAGCAGGGGGTCATCGCCCACCGTGAGGGTGATCGGGCCTCCGCCGCCACCAGCTTCGCCGCCGCCTGCAAGGCCGCCGGAGGAAAGGCCTGCAGCAAGGGACCGGCCCAGTTCGCGTGCTCCCGGGGAGACTGGAGGCTGGCGGCCGAGCTCTTCGAGATCTACCCGGGCGAGGGGATGACGAGGGTGGAGCGGGCCTACGAGCTGGCCTACTGCCTGGACCGTCTGCGCGAGCACGAGCGGGCACAAGGACAGTACGCCCTGGCCGCCTCACTGGACACCGGCAACGGGAACACTCTTTACAAGCTGGGACTCGCCTCGGAACGTGTCGGCGACCTCGCCACCGCGGAGCGCTCGTACCAGGAGGCCTTGCGGACGCTCAAGAAGCCCGCACGCAGCTGGTGGAACTATCGCCGTGGGGTCTGCCTGGCAAGGCTGGGACGCCACGACGAGGCGCTGGCCTCCTTCTGGGCCTACCTGGGACCGGCCCCGCGCGGGCTGGCATCGGTGTCCAAGCAGCTGGCCAGCACGGGCTTCCTCGACCTGGTCCGCGCGAAGAGCACGCCCCCGCCTCGGCAGCGGCCGGAGGACCTGGTCGAGTCCACCATCAGTGACATCATGCTCGGCCTTCACGAGGCTCTCAGCTCCCACGGCGCTCCGGGCGGTTCCGGCAGCGGCACGGAGGTCCCGCCGGCCGCAGCGCAGACTGCCGCTCAGTCCATCCGGCATGTCCTCCCGCTGGTTCTCAAGGGGGACCGGAATCACCGCCTGGTCCTGGCCCAGCTGGCCCAGGACGCCGGGCAGGTGGAGCTCGCCTGCGAGATCCTCGAGCAGGCCGAGGAGTTCGGCTGCAAGGACGGGCTGGACCCACTGGCCTATGGACGCACCGCGACAGCCGCCCGCAACATCCGCTACGCCGAGGCCCTGGAGGTCCTTCCCGTCAGCCCCCACCTGGTGCTGTGGGAGTCCAACCATGGCGCCTCGATCGGCTGCCACCCCCTGGCCATCTTCCGCTGGATGGTGGACCGGCCAGAGTACTCCCACCTCATCCACGTGTGGGCCGTCAATGACCTGGGCGCCATCCCCGCGGATCTGCTGGGGCGTCGCAACGTCGTCTTCGTCCCCCTGCACAGCACCGAGTACATGCAGTACCTCGCCACCGCCGGGTACCTCGTCAACAACGTCTCCTTCGCTCCCTACTTCGTGCGCCGCCGCGAGCAGCGCTACCTCAACACCTGGCACGGCACCCCCTTCAAGACCCTGGGACGGTCCATGCGGGGAGGTCTGCTCGACTACGAGAACCTGCAGCGCAACTTCCAGCTGAGCACCACGCTCATGGCGCCCAATGAGCTCACCCGATGGGCGCTGGTGGAGGACCATGATCTGCTCGACGTCTACCGGGGCCGCACCATCGTCGCCGGCTCCCCCCGACTGGACACCTCGCTGACGATGAGCGCCCAGGAGCGCACGGCGCTGCGAGGTCGCCTGGGACTCGCTGAGGACGATGAGCGCCGTCTGGTCCTGTTCGCCCCCACCTGGCGCGGCGGGGTCAGCAAGCGAGAGCTGGACCGCGAGGCCCTGGTCGCCGACCTGACCGCCATGGCCTCCCGTGACGACGTGCTCGTGGTCTACCGCGCCCACCGTCTGTCCGAGAAGCTGCTGGCCGGCGTCGATCTGCCGGTGAGCGTCGTCCCCAAGGACATCGACACCAATGAGCTGCTGGCCGCCGTCGACGTCCTGGTGACCGACTACTCCTCTATCCTCTTCGACTTCCTGCCCCAGAAGCGCCCCATCGTGCTCTACATGCACGACATCGAGGAGTACCGGGCCGAACGGGGCCTGTACCTTGATCCTGGGGAGGTCCCCGGGCTGGCCTGTTATGACCGCGCTGAGCTGGCCTCAGCCATCGGGCGTGCCCTGGCCGGAGAGGGGGTCGCACCCCAGAAGGCCCTCGACCGGTACTGCCCCTACGAGGACGGACAGGCCTCGTCACGCCTGGCCCGAGCCTTCTTCGACGACGACCTCGACCACGGACGGCAGGCGATCATCAGGGACCACTCCCTCGAGCCCGCGTCTGGCGACGGTTCCCGCAGACGCCGTACCCTCCTGTTTCACGCCTCCATGATCCCCAACGGGATCGCCTCCGCCCTCCTGGCTCTCCTGGAGGCGCTCGATCCGAACCTCTACTCGGTCAACCTCATTGTTGAGCCCTCTGTCCTGCGCAACAACGAGGACCGTCAGGAGATCTTCCGACGCCTGCCCCGCCACGTCCATGTCATCTGTAAGCCCGGGGCCGCGCCCTGGCGGATCCACGAACGGGCCTGCGTCAACGACTTCGCCCGGCACCCCGATGCCTTCACCTCGCAGAGCTTCTGGGACTGCTACTGGGCCTACTACGAGCGCGAGACGCGCCGTATCCTGGGCGACTTCGTGCCCGACGCCGCCATCGAGTACGACGGCTATGCCGAGACGTGGGTCTCGCTCATCGCTGCCTGGGGTCGCCGCGGATCGCGCACCTCCTGCTACCAGCACAACCAGATGGACAACGAGTACCGGGACAAGTACCCGGGCCTCAAGCGCGTCTTCACCCTCTACAGCGCTGTCGACGCCGTCGTCGCCGTCAGCCCGGGACTGGCCCGCCACAACCGCAGCGGGCTGGCCGGCCTGGGTATCGACCTCACCCAGCACCAGCTCTCGGCCCGCAACCTCCTGAACGTCGAGCGGGTCCGCCGCGGGGCGCAGGCACCGGCCCCGGAGGCCTTCACCACCCTGAAGAACGAGCACGACGTCGTCCTTGCCACCATGGGGCGGATGTCGATGGAGAAGAACCAGGCGGCTCTCATCGAGGCGCTCGCCCTTCTGCGTAAGCAGGACGGCACCGAGGGCGGCGGCGCTCAGGGACTGAACGTCGGCCTGGCGATCGTCGGCTCCGGGGTGCTCGAGGCGACGCTGCGGGCCAGGATCGACTCCCTGGGACTGTGCGGGCACGTTGAGCTGCTGGGACAGATGGACAACCCGTTCCCGGTCCTGGGAGGAGCCGACCTGTTCGTCCTGCCCTCCCTGCACGAGGGGCAGCCGGTCACCCTGCTGGAGGCGATGACGCTGGGAACCGGGGTCGTGGCCTCCGACCTTCCGGGCAACCGGGAGCTGATCGACCTCGGATACGGGGTTCTGAGCGGCACCTCGCCCCAGGACATCGCCCAGGCGATCCGCTCGGCACTGGCCGATCCCCGCCTCGCCCACGGAGCCTTCGACGTCACCGAGCACAACGCGCGCTCACTGCGGGACACCCTGGAGGCAGTGCTCGGCCCCGAGGCACTCCAGCAGCAGCCCCAGGGGAAGACGGCTTCCAAGAGGCGGCGGCGCAAGCGGGCGGCCTCGCGAGGGAAGCCCGCATGA","MSKDTVLRKMGRAVSGRLQLPATTRLVRYAAAREYEDGNLAEAKRLYEKLSESGHDTASRLRLGVIAERQERFEAALRTYTEVADRDPSCGEAFYRAGCLLKRQDDPEGASVFFSRALSSGVRDRRYSENLLACLPASTPQWQRLEVLLSGLPEHENDAAWLRKLLQAQLHLGLNGPARCTLDALADIDELSAQELFEQGVIAHREGDRASAATSFAAACKAAGGKACSKGPAQFACSRGDWRLAAELFEIYPGEGMTRVERAYELAYCLDRLREHERAQGQYALAASLDTGNGNTLYKLGLASERVGDLATAERSYQEALRTLKKPARSWWNYRRGVCLARLGRHDEALASFWAYLGPAPRGLASVSKQLASTGFLDLVRAKSTPPPRQRPEDLVESTISDIMLGLHEALSSHGAPGGSGSGTEVPPAAAQTAAQSIRHVLPLVLKGDRNHRLVLAQLAQDAGQVELACEILEQAEEFGCKDGLDPLAYGRTATAARNIRYAEALEVLPVSPHLVLWESNHGASIGCHPLAIFRWMVDRPEYSHLIHVWAVNDLGAIPADLLGRRNVVFVPLHSTEYMQYLATAGYLVNNVSFAPYFVRRREQRYLNTWHGTPFKTLGRSMRGGLLDYENLQRNFQLSTTLMAPNELTRWALVEDHDLLDVYRGRTIVAGSPRLDTSLTMSAQERTALRGRLGLAEDDERRLVLFAPTWRGGVSKRELDREALVADLTAMASRDDVLVVYRAHRLSEKLLAGVDLPVSVVPKDIDTNELLAAVDVLVTDYSSILFDFLPQKRPIVLYMHDIEEYRAERGLYLDPGEVPGLACYDRAELASAIGRALAGEGVAPQKALDRYCPYEDGQASSRLARAFFDDDLDHGRQAIIRDHSLEPASGDGSRRRRTLLFHASMIPNGIASALLALLEALDPNLYSVNLIVEPSVLRNNEDRQEIFRRLPRHVHVICKPGAAPWRIHERACVNDFARHPDAFTSQSFWDCYWAYYERETRRILGDFVPDAAIEYDGYAETWVSLIAAWGRRGSRTSCYQHNQMDNEYRDKYPGLKRVFTLYSAVDAVVAVSPGLARHNRSGLAGLGIDLTQHQLSARNLLNVERVRRGAQAPAPEAFTTLKNEHDVVLATMGRMSMEKNQAALIEALALLRKQDGTEGGGAQGLNVGLAIVGSGVLEATLRARIDSLGLCGHVELLGQMDNPFPVLGGADLFVLPSLHEGQPVTLLEAMTLGTGVVASDLPGNRELIDLGYGVLSGTSPQDIAQAIRSALADPRLAHGAFDVTEHNARSLRDTLEAVLGPEALQQQPQGKTASKRRRRKRAASRGKPA$","CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase","Cytoplasm, Extracellular","CDP-Glycerol:Poly(glycerophosphate)glycerophosphotransferase family","teichoic acid biosynthesis protein","CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Davis S.C., Tzagoloff A., Ellis S.R. Characterization of a yeast mitochondrial ribosomal protein structurally related to the mammalian 68-kDa high affinity laminin receptor. J. Biol. Chem. 1992. 267(8):5508-5514. PMID: 1531984Tohgo A., Takasawa S., Munakata H., Yonekura H., Hayashi N., Okamoto H. Structural determination and characterization of a 40 kDa protein isolated from rat 40 S ribosomal subunit. FEBS Lett. 1994. 340(1):133-138. PMID: 8119397Ouzonis C., Kyrpides N., Sander C. Novel protein families in archaean genomes. Nucleic Acids Res. 1995. 23(4):565-570. PMID: 7899076","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[1113-1278]T$	Glycos_transf_1

InterPro
IPR001440
Repeat

Tetratricopeptide TPR_1
PF00515	$\"[57-90]T$ $\"[294-327]T$ $\"[334-353]T$	TPR_1

InterPro
IPR001865
Family

Ribosomal protein S2
PS00962	$\"[162-173]?$	RIBOSOMAL_S2_1

InterPro
IPR007554
Family

CDP-glycerol glycerophosphotransferase
PF04464	$\"[689-869]T$	Glyphos_transf

InterPro
IPR011990
Domain

Tetratricopeptide-like helical
G3DSA:1.25.40.10	$\"[21-135]T$ $\"[175-361]T$	no description

InterPro
IPR013026
Domain

Tetratricopeptide region
SM00028	$\"[57-90]T$ $\"[91-124]T$ $\"[294-327]T$	TPR
PS50293	$\"[57-124]T$ $\"[260-363]T$	TPR_REGION

noIPR
unintegrated

unintegrated
PTHR12526	$\"[897-960]T$ $\"[981-1319]T$	GLYCOSYLTRANSFERASE

","No hits to the COGs database.","***** IPB007554 (CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase) with a combined E-value of 2.1e-12. IPB007554E 701-711 IPB007554F 775-808***** IPB001296 (Glycosyl transferase, group 1) with a combined E-value of 9.2e-12. IPB001296B 1216-1248","Residues 529-676 are similar to a (TEICHOIC ACID BIOSYNTHESIS TRANSFERASE GLYCOSYL GLYCOSYLTRANSFERASE B WALL F CELL) protein domain (PD135736) which is seen in Q6UYC4_ACTPL.Residues 625-695 are 58% similar to a (TEICHOIC BIOSYNTHESIS ACID) protein domain (PD822563) which is seen in Q88ZN9_LACPL.Residues 703-833 are similar to a (TEICHOIC ACID BIOSYNTHESIS TRANSFERASE B GLYCOSYLTRANSFERASE GLYCOSYL WALL F CELL) protein domain (PD007030) which is seen in Q6UYC4_ACTPL.Residues 851-1084 are 50% similar to a (REPEAT TEICHOIC ACID TPR BIOSYNTHESIS SYNTHASE CPS2D C3694) protein domain (PD697338) which is seen in Q6UYC4_ACTPL.","","No significant hits to the PDB database (E-value < E-10).","Residues 57 to 90 (E_value = 90) place ANA_0305 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 294 to 327 (E_value = 327) place ANA_0305 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 334 to 353 (E_value = 0.019) place ANA_0305 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 689 to 869 (E_value = 2.8e-35) place ANA_0305 in the Glyphos_transf family which is described as CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase.Residues 1113 to 1287 (E_value = 4.3e-25) place ANA_0305 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","glycerophosphotransferase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0306","319733","321577","1845","5.85","-11.69","67696","ATGACGGGCCCCCACGGGTCACAGCCCACAGCGGCTCGCCAGGGTGCGGTCTGCGCCCCGATGCCGGCCGGCAAGCCCTCGGCGGAGCTGGGGGAGATCCTCCAGCAGGTCCTCCAAGGGCTGTCCCGCGGGGAGGAGTCCGGAGCAGCGCCCCGTGTCGCCGTGCTCCTGGACCGCCCTCAGCCCCACCTGAGTAACTGGCTCGGGGCGGCGCTGGGAGCGTGCGAGCTGATCGTCTGCTCAATGCGGGACGAGCAGGACGAGCAGGACGGGTGCGCGGAGGCGGAACCAGTGGAGTACTCCGGTCTCATCGGTCTGGCCCGAGTGGTTGGCTTCACGAACCAGGTCGACCTGCACCAGGCCCTGGCCACTCACGGCCGGTTCGACGTCCTCGTGGACGCACTCACCCACAGCCCGGGCATGCGCGCTACGTCCGCCCAGTTGTTCATCGGTATTGTCCGCGACGGCGGGTACTACGTCGCCATCGATGGTGCGGCGCTGGGCGAGAGCCTCAACACCGCTGGGCTCATCGCCCGGGCCTCGCGCAGCCTCGCCGGCCTGCACGGAGCCGCGGGGGAGCTGAGTGGGGACGAACGGTCCTACGGTGAGCAGGTGGCCGCACTGACCGTCCTCGACGGCGGTGTCGTGCTGCGTAAACGAGGAGACGGATTCGTCAAGCTCCGATACGCCGAGACCCCGCCGATCCTGTCCGCCCGCTACGGCGAGTCCTGGGGGCGGTCACTGGAGACCCTCCCCGCCCGGGTCACCCCGCTGGAGGTCATTGGCGTCACCAACAACCCGGGATTGTGCGCCAAGAGGTTTCCGCGCGAGAACCGCATCCCCGAGACCTCCGTCCTGGAGTACCGGGACGTGTGCGTCGCCCCCCGTCAGGTGCTTGTCAAGGATCATCTCCTGCTGCCCAACACCTTCCGCCTGGCCACGACCAAGCGGCTGGTCAACACGGCGCTGAAGGAACTCAACCACTACTACGCCGCGCCCACGGTCGATACGCAGTCGGCTCCCAGACGTGAAGGAACCTTCTTCTACCTGGACATCGAGTACAACCGGCACTTCGGCCACTTCATGACCGAGGTCGTTCCCAGGCTCTACGCCTGGGAGCTGGCGCGGGCGACGCACCCCGACATCCGGATCCTCACCAACAGCAGGGCCGACCGCGGCCGTCCCCCTGCCTACCAGCGCATCCTCCTGGAGGCCTACGGCATCGACGACGACCTGGTCGAGGTCATCACCTCCCCGGTGAAGGTCGACACCCTCGTGTGCGCCATGCCCCTCATGCAGAACGGGCGATTCGCCGACCCGGCTCTGGCCTCAACCTGCCACCGGCTGCGTGACGGCCTGCTGGAGCGATCAACCCCCAACGACAAGCCCCAGCGCAGGCTCTTCATCTCCCGCAAACCCGACATGTGGCGCGAGTGCCTCAACGGCAGTCAGGTCGAGGAGTGCTTCGCCCGCAGGGGCTTCACCATCATCCGGCCCGAGGGCCATTCCATCGTGGAGCAGGCCCGCATGTTCTACGAGGCCGACGTCGTGGCCGGGTACATCGGCTCGGCCCTGTACAACATCATGTTCGCGCGCCGCCCGATCGACGTCATCGGTTTCATCAACCAGTCCTACCTGGCCACCAACGAGTACCTCATCTGCTCGGTCCTCGGCCACCGCCTGCACCTGTTCTACGGTGATGAGATCACCGATGGCAGGGGAAAGGACTGCGAGGGCCGGGACCTGGGAGTCACCAACCGGGACTACGTCTTCAACATCGAGCGCGACGGCGACCAGCTCGACGAGCTGCTCGACTCCCTGGAGGAGACATGGGGGGAGTCATGA","MTGPHGSQPTAARQGAVCAPMPAGKPSAELGEILQQVLQGLSRGEESGAAPRVAVLLDRPQPHLSNWLGAALGACELIVCSMRDEQDEQDGCAEAEPVEYSGLIGLARVVGFTNQVDLHQALATHGRFDVLVDALTHSPGMRATSAQLFIGIVRDGGYYVAIDGAALGESLNTAGLIARASRSLAGLHGAAGELSGDERSYGEQVAALTVLDGGVVLRKRGDGFVKLRYAETPPILSARYGESWGRSLETLPARVTPLEVIGVTNNPGLCAKRFPRENRIPETSVLEYRDVCVAPRQVLVKDHLLLPNTFRLATTKRLVNTALKELNHYYAAPTVDTQSAPRREGTFFYLDIEYNRHFGHFMTEVVPRLYAWELARATHPDIRILTNSRADRGRPPAYQRILLEAYGIDDDLVEVITSPVKVDTLVCAMPLMQNGRFADPALASTCHRLRDGLLERSTPNDKPQRRLFISRKPDMWRECLNGSQVEECFARRGFTIIRPEGHSIVEQARMFYEADVVAGYIGSALYNIMFARRPIDVIGFINQSYLATNEYLICSVLGHRLHLFYGDEITDGRGKDCEGRDLGVTNRDYVFNIERDGDQLDELLDSLEETWGES$","Capsular polysaccharide biosynthesis protein","Cytoplasm","hypothetical protein","capsular polysaccharide biosynthesis protein-like","Capsular polysaccharide biosynthesis protein-like","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 345-526 are 48% similar to a (BH3368) protein domain (PD298535) which is seen in Q9K7J3_BACHD.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0308","321574","323499","1926","6.94","-0.77","71887","ATGAGCTCGCCGGAGACCCGCACCTCGCCTCGGACGGCCCCCGAGCTGCGGCGAGCCCTGTGGCACCTGCGTCACTCAGGGCTGTCGGGGCTGCGTGAGCACCTGCGCCGTCGTCGGGCCACCGCCTGGGCCCGCCCCCGCCGATGGGCCTCCAAGAGACGGGGCCGGACGCTCCTGCCAGACTGGCCGCTGCCCACACCCCAGGAGACCGGGCCCCGTCACGACGTGACCGTCGGGGTGATCGCCGACGAGTTCACGGCGCTCGCCCTGGGCTACGAGTGGCGCTCGGTGCCCCTGACCCCCACCGGTTGGCGCGAGCAGGTCGAGCAGACCCCCATCGACCTCCTCTTCGTGGAGTCCGCCTGGCACGGCAACGACGACGCCTGGCGCTTCCAGGTCATCGGCTCCCAGGGACCCTCGGGCCACCTGAGGGACATGGTTACCGTGCTGCGGGACCGAGGAGTGCCGACGGTCTTCTGGAACAAGGAGGATCCCGCCCACTACGACGAGGCCATCGAGACCGCACGCCTCTTCGACTGGGTCTTCACCACCGATGAGGCGATGGTGGAGCACTACCGGCGCGACCTGGGACATGACCGCATCGGGATCCTGCCCTTCGCCGCCCAGCCCGCGATCCACAACCCGATCCGCCTGCTGGACGAGGCGGGGCGTCCCGCGCCCCTGAGGGATGTCGCCTTCGCCGGCACCTATTTCGCTCACAAGTACCCCGAGCGGCGCGAGCAGATGGAGATCGTCCTGGGCGGCGCCCACGACGTCGCGGCACGCCTGCCCCGTGGGCTGGACATCTTCTCCCGGTACCTTGACGGTGACGACACCTACCAGTTCCCACCCCCCTGGGACTCACACGTGCGAGGCAGCCTCACCTACACCCAGATGCTCAGCGCCTACCGCGCCTACGCCGTCTTCCTCAACGTCAGCTCCGTGGTGGACAGCCCCTCCATGCTGCCGCGCCGCGTCATCGAGGTCCTGGCCTGTGGTACTCCCGTGGTGAGCACCCCGACGCCGGCCATCGACCGCCTGCTGCCCGCAGGCGCCCTGGCCAAGGTCACCGACCGCGCCCAGGCAGGGCACACCGTGCGCGCGCTCGTGACCAACCCGGTCCTCGGGGAGTACATGACCTACCTGGCGCAACGGGAGATCTGGAGCCGGCACACCTACAGCCACCGCGTGGAGACCGTGCTGCGAGCCGTCGGCATGGGGGAGCGGGTCAGGCCCCGCCCCACCATCGCACCGCTGGTGTCCACCATCCGGCCCGAGCAGATCGACCACGTCCTTGGGACCCTGGCCGGTCAGCAGCAGGTGACGATGGCCCCGGTCATCCTCACCCACGGTTTCACCGCCCCAGCCGCCAGCAGGGCCCGGGCTCGCGAGCTGGGCCTGGAGATCGACTGGGTCACCGCCGAGACCAGCACTCCCTTGGGGGGCTGCTACAACCTCATGCTCTCGCGGGTCGAGGCCGACTACATCGCCAAGATGGACGACGACGACCTCTACGGCGATCACTACCTCTTCGAGTCCCTCGCGGCGGCCGACTACGCTCGTGCCGAGGTCGTGGGCAAGCACGCCCACTACCTGCACCTGACGGGCCCGGACCTGACGGTGCTGCGCTTCGCCGACTGGGAGCACCGCTATACGACTTTCGTCTCCGGGCCGACCCTGGTGGCTCGAGCGGACCTGGCGCGCGAGGTGACTTTTCCCGAGACGACCACCGGTGAGGACACCGGTTTCCTCAGTGACTGCGCACGCGCCGGGGCCCGTATCTATTCGGCCTCCCGGTTCGGGTTCGTCCAACGGAGAGGGACGACTTTCGGACACACCTGGGACATCTCCAACGCGGAGGTGCTGGCTACGTCCACCATTAGTCATTGGGGACCGCCCCACGAAATGGAGATGCCCACCTCATGA","MSSPETRTSPRTAPELRRALWHLRHSGLSGLREHLRRRRATAWARPRRWASKRRGRTLLPDWPLPTPQETGPRHDVTVGVIADEFTALALGYEWRSVPLTPTGWREQVEQTPIDLLFVESAWHGNDDAWRFQVIGSQGPSGHLRDMVTVLRDRGVPTVFWNKEDPAHYDEAIETARLFDWVFTTDEAMVEHYRRDLGHDRIGILPFAAQPAIHNPIRLLDEAGRPAPLRDVAFAGTYFAHKYPERREQMEIVLGGAHDVAARLPRGLDIFSRYLDGDDTYQFPPPWDSHVRGSLTYTQMLSAYRAYAVFLNVSSVVDSPSMLPRRVIEVLACGTPVVSTPTPAIDRLLPAGALAKVTDRAQAGHTVRALVTNPVLGEYMTYLAQREIWSRHTYSHRVETVLRAVGMGERVRPRPTIAPLVSTIRPEQIDHVLGTLAGQQQVTMAPVILTHGFTAPAASRARARELGLEIDWVTAETSTPLGGCYNLMLSRVEADYIAKMDDDDLYGDHYLFESLAAADYARAEVVGKHAHYLHLTGPDLTVLRFADWEHRYTTFVSGPTLVARADLAREVTFPETTTGEDTGFLSDCARAGARIYSASRFGFVQRRGTTFGHTWDISNAEVLATSTISHWGPPHEMEMPTS$","Glycosyltransferase","Cytoplasm","conserved hypothetical protein","hypothetical protein","Uncharacterized protein-like","","","","","

noIPR
unintegrated

unintegrated
PTHR12526	$\"[322-433]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF41	$\"[322-433]T$	GLYCOSYLTRANSFERASE

","BeTs to 4 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","Residues 104-283 are 58% similar to a (DOMAIN BCBI ECBI SPORE ACBIV ACBI POSSIBLE) protein domain (PD332890) which is seen in Q81K25_BACAN.Residues 286-347 are 67% similar to a (DOMAIN BCBI ECBI SPORE ACBIV ACBI POSSIBLE) protein domain (PD350871) which is seen in Q81K25_BACAN.Residues 512-618 are 50% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE PREDICTED ECBJ OB2081) protein domain (PD583236) which is seen in Q97IM6_CLOAB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0309","323496","325904","2409","6.51","-7.61","86555","ATGAACGCCCGCAGCACCGAGACCTTGCACGTCATCATCATCGGTTCCGCAGGTGGTCAGGACACACTCGACTCTCTTGGCCAGGACTCGCCCGAAGGCGGGATCGTCCCCATCGGCTGCCCCGACCCGGCCGGGCTGGACCAGGTCCTACGCCCCCTGGCCGCAGGGACCCGGGTCCTGCTCCTCAAGGCAGGAGACCGCCTCGAGCCGGGCTATCTCACCTCAGTGGCCCAGCACGGCACCAGCAGCGCCGTCGTCCTCACCCCGACCGTGACCATCCGCCCCGACGGTACCCGCGACGAGCGGCTGCAATGGCGCTTCAAGCACGGTAGCCGCACCGCTGACCTGACCGTGGAGCCCCACATCTTCCCCGACACCGTCAGCGGAGCGGTGCTCACCATCCCCCGCCACGGCCTGCAGGGCTGGGGCGGATCGGGTGCCCTCGACGGCATGGATGACGCCTTCGGCGCTGAGCCCACCACTTCTGATGACGAGAACACCGCCCTGAGCGGGCTCATCGCCCACATCATGGCCACCGGTAACCGGGTGGGTCTCCACGACGGCCCGGCCGTCATCCGCCACACCCCCAAGCCCCCCGGCCCCTGGGACAGGATCGACCACTACCGCCACCTGCTGGGCACGGTGCTGCCGGCGTGGCTGCAGGCAGGAAGCCCCCCACCGGCCTGGGTGCACCAGCTCATCATCCACCGCCTCATCCAGGTCACCGATGCCGACCGCGGGCTGCGCTACCCCTCGGCAGGACTCACGGCCGCCGAGCGTGCCGAGGTGGCCCAGCTGCTGCGTGCTGTCACCCGACGTCTCCCCGCCTCCCAGATCGAGGTGTACTGCTCCACGCCGCTGGCCGTGGGCCGTCGCACCGCCCTGGTCGCCATGGCCGCCGGCCCCATGCCTGCCCCGATCCTGCCCTCGGGACGCAGGTTCCGCAGCGACCAGAAGGCCACCTACTTCTACACCGGCGACATGCCCCAGGAGCAGTGGAAGGTTGATGGCGCCTGGGCCCAGCCGACCAGCGCCAAGACAGTCGATCACCGCTACTTCGACGACGTGGTCCTCCACGAGCGCATCGTCTGGCTGCCCAAGGGCCAGATCACCGCCGTCATCGACGATCAGGAGCTCCCAGTGGCCCCCTACCGGGGCGACCCCAGGCCGCCTCAGACGCCACCGGGGCGAGGCCGCCCAGAAGGGGCCTCATCCGGGCTGCGTCGGCGCCTGGCCCGGCTCCTGAGCCCCACCGGCGCGCAGGACGACCAGCGATCCGGCGGTACGTCACCGGCCCCGGAGGCATCTTCCGCGGCGTCCTCCACGACCTCCGTGGCCTCCTCCTCAGCGCCCACGCCGTACACCGCCTCATCCCCCTCCGACTGGCCCCGCACCTGGCTCTACATGGACCGCCATGACAGCGCCGGCGACAACGCCGAGCCGCTGTACCGCTACGCCCGCACCCATGCACCCAGCGTCAGGCACATCTTCGTCATTGAGCGCAGCTGCCCGGACTGGGAGCGCCTCGCACAGGACGGCTTCGTCCTGCTGGACCCGACCGGTCCCGGATTCGACGCCGCCTGGAGCGGTGCCGAGACCATCCTCCTGTCCGATATCGGCGACCCGCTCATCGCGGGCCGGCTCACCGGAGCGGGAGTCGGCCCCGACCAGCGCCTCGTCTTCCTCCAGCACGGCGTGACCATGCGCGACATGTGGCGCTGGTTCAACGGCGCCCGCCTGGACGTCGTCGTGTGCGCCACTGCCGCCGAGCAGGCCGGGCTGACTGCCGACCACACCTCCTACACCCTCACCGACCGAGAGGTCTGGCGCACCGGCTTCCCCCGCCACGACCACCTCCACAGCCTGCTGGGACGCGAGCGCGACAGCATCCTGCTGGCCCCCACCTGGGACCCCGAGGTCTCACGCGCCCTGGAGTGCGACCCCGACGCCGTCGGACTCCTCAGCGCGCTCTACCGGCCCTGGCTCGAGCTGGCCGCGGGCCTGACCCAGGCCGGTCACCGCACCGTCCTGTTCGCCCACCCCAAGCTGGTGCTGCACGCACCCGAGTGGTTCAGGGCCCTGGGCGTGCCCGCGGTCACCGGTCGCGACCTGCCCGAGACCCTGGTCCGCTCCTGGGCAGTCGTCTCGGACCGCTCATCCGTCCTCGACGAGGGCATGATCGCCGGCTGCGTCGGCATCGTCTGGGACCCTCGAGGGCGGCCGGACACGGACCGCTACCGCGCCCGTCACGAGGCCATCGGAGCTATCGGCGCCGACACCTCTGCGCAGGTGCATCAGGCGGTGGGGGACGTCGTCGCCGGCCGAGTCACCGCCCCTGAGGACCTCCTCCTGCTCGACGCCGGAGCCTGCGCCCGCCTGACCGCGCTGCTCCGACGCGACATGATCTGA","MNARSTETLHVIIIGSAGGQDTLDSLGQDSPEGGIVPIGCPDPAGLDQVLRPLAAGTRVLLLKAGDRLEPGYLTSVAQHGTSSAVVLTPTVTIRPDGTRDERLQWRFKHGSRTADLTVEPHIFPDTVSGAVLTIPRHGLQGWGGSGALDGMDDAFGAEPTTSDDENTALSGLIAHIMATGNRVGLHDGPAVIRHTPKPPGPWDRIDHYRHLLGTVLPAWLQAGSPPPAWVHQLIIHRLIQVTDADRGLRYPSAGLTAAERAEVAQLLRAVTRRLPASQIEVYCSTPLAVGRRTALVAMAAGPMPAPILPSGRRFRSDQKATYFYTGDMPQEQWKVDGAWAQPTSAKTVDHRYFDDVVLHERIVWLPKGQITAVIDDQELPVAPYRGDPRPPQTPPGRGRPEGASSGLRRRLARLLSPTGAQDDQRSGGTSPAPEASSAASSTTSVASSSAPTPYTASSPSDWPRTWLYMDRHDSAGDNAEPLYRYARTHAPSVRHIFVIERSCPDWERLAQDGFVLLDPTGPGFDAAWSGAETILLSDIGDPLIAGRLTGAGVGPDQRLVFLQHGVTMRDMWRWFNGARLDVVVCATAAEQAGLTADHTSYTLTDREVWRTGFPRHDHLHSLLGRERDSILLAPTWDPEVSRALECDPDAVGLLSALYRPWLELAAGLTQAGHRTVLFAHPKLVLHAPEWFRALGVPAVTGRDLPETLVRSWAVVSDRSSVLDEGMIAGCVGIVWDPRGRPDTDRYRARHEAIGAIGADTSAQVHQAVGDVVAGRVTAPEDLLLLDAGACARLTALLRRDMI$","Glycosyl/glycerophosphate transferase involved in teichoic acid biosynthesis","Cytoplasm, Membrane","hypothetical protein","putative glycosyl/glycerophosphate transferase involved in teichoic acid biosynthesis TagF/TagB/EpsJ/RodC","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 466-521 are similar to a (TEICHOIC BIOSYNTHESIS ACID MINOR GALACTOSAMINE-CONTAINING TRANSFERASE GLYCOSYLTRANSFERASE EPSJ FCS2 GGAB) protein domain (PD794166) which is seen in Q82T92_NITEU.Residues 557-636 are similar to a (TEICHOIC BIOSYNTHESIS ACID MINOR GALACTOSAMINE-CONTAINING TRANSFERASE GLYCOSYLTRANSFERASE EPSJ FCS2 GGAB) protein domain (PD139282) which is seen in Q82UV2_NITEU.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0310","325904","327148","1245","10.05","14.82","46389","ATGCGGGCCCCGCTGGCGGGGACCCCGCGGATGCGCCGCCGCCCGTCCCTGGTCAGCCTCGTCATCCCCGTCTACGGGGTGGCCCCTTACCTGGCCCGCTTCCTGAGCTCGCTCGACGCCCAGGACCACCCGCACGACCGTCTTCAGGTCGTGCTCGTCCTGGACGGGGCCTGCGACGACTCACCGAGGGCCTGCCGGAGCTGGGCGCGGCGAACCGACCTCGACGTCGAGATCGTCGAGACGGACAACGGCGGACAGGGCCGTGCCCGAAACCTCGGGATGGAGCGGGCCCGGGGACAGTGGATCGGCTTCCCCGATCCCGATGACTGGCTCGCCCCCGACTTCCTCACCCGGCTCCTGGCTGCCAGACGCCGCGGCGACGTCCTCCTGGCCGGCCGCACCCTCATCCACCAGGACGGTGCTGAGATCCCCCACCCCCTCGACTTCCGCTTCCAGGGCGGGACCGTCCGGGTCGACGCCGCCCGGCAGCCGCAGGCCATCCAGCTCTCCGTCCACGAGTGCCTCATCCGGGCCGACCGGGCGCTCGCGGCCCGGTTCCCGGAGGACCGTGAGGCCCCCACCTTCGAGGACGCCCTCTACCTGGGGCGTATCCGCAGCCGCTGGGGCCGGATCGTCTACGTGCCCGAGGCCGTCTACCACTATGACAAGCGGGTCGCAGGCGACTCCGCGGTTCAGACCGCCTGGTCGCGGCCGGGCCGCTACGTCGCTCAGATGCGCACGCGCTACCACGCCCTTCTCGATGCCGCCGGTGGGGCGCCCTGGGCTCAGCAGACGATCCTGTACGACCTGGGCTGGTACTTCGGGGTCGTCGACGCCGGCCGGATGCCCACTGATCCGCCCGGACTGGGGCAGGTGCACGCGGCTGAGATGCGTGGGCTGGCGCAGCGCCTCGACTCCGAGCAGATCCTCCGCAGCCCTTGGGGGAACCTCGGTGCCCGGGACCGGGCCCGCCTTCTGCTGTGGAAAGGCCGACCCGAGGTGGCGGTGGTGCGTGACGGCGAGGTCATCGAGCTGTGTACCGTCGAGCCCGCCGGCCGGCAGGCGGAGCCCCTTCGCTACGCAGGGACCGACGTCGGCTGGGTCCTCACCGGAGCCGAGGCGGCGCAGCGCTACTCCGGTGCAGACGTCCCCCGCGTCCCTCTGTGGCCCCGCCGACCCCGGCTGGCCGAGCCGCGCCCGGCCGGGACAGGGCGCCTTCGCAGGCTGCTGCGGCGTCGTCGCTGA","MRAPLAGTPRMRRRPSLVSLVIPVYGVAPYLARFLSSLDAQDHPHDRLQVVLVLDGACDDSPRACRSWARRTDLDVEIVETDNGGQGRARNLGMERARGQWIGFPDPDDWLAPDFLTRLLAARRRGDVLLAGRTLIHQDGAEIPHPLDFRFQGGTVRVDAARQPQAIQLSVHECLIRADRALAARFPEDREAPTFEDALYLGRIRSRWGRIVYVPEAVYHYDKRVAGDSAVQTAWSRPGRYVAQMRTRYHALLDAAGGAPWAQQTILYDLGWYFGVVDAGRMPTDPPGLGQVHAAEMRGLAQRLDSEQILRSPWGNLGARDRARLLLWKGRPEVAVVRDGEVIELCTVEPAGRQAEPLRYAGTDVGWVLTGAEAAQRYSGADVPRVPLWPRRPRLAEPRPAGTGRLRRLLRRRR$","Glycosyl transferase, family 2","Cytoplasm","Glycosyl transferase, family 2, putative","galactosamine-containing minor teichoic acid biosynthesis protein","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[19-186]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[17-221]T$	no description
PTHR22916	$\"[24-250]T$	GLYCOSYLTRANSFERASE
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 18-121 are 50% similar to a (TRANSFERASE GLYCOSYL TRANSFERASE GROUP FAMILY) protein domain (PDA0X5V4) which is seen in Q74D16_GEOSL.Residues 25-121 are 57% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL FAMILY TRANSFERASE GROUP SYNTHASE BIOSYNTHESIS 2.4.1.- 2.-.-.-) protein domain (PD000196) which is seen in Q56046_STRTR.Residues 52-125 are 51% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE) protein domain (PD832699) which is seen in Q88W89_LACPL.","","No significant hits to the PDB database (E-value < E-10).","Residues 19 to 186 (E_value = 4e-27) place ANA_0310 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","transferase, family 2, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0311","327976","327200","777","5.12","-9.64","28686","ATGCACAGTGAGGAAAGCACCATGACAGCAGGACGAATCACGGTCTACGGCTCTTGCGTGGCCAGGGACGTGGCCGGTGAGATGGAGCGGCGGGGTTGGAGCGTGGAGCGTTACATCGCCCGCCAGTCCCTCATCAGTGCGGGGTGCCCGGCCGACGTCGGCGACGTCGATCTGTCCCTGCTCAGGTCATCCTTCGCCCGTCGGTCCTTCCTGTCCGACATGGTGGGCAACCTGGAGGCGCAGCTAACGGCCGTCGCCTCCTACACCGACCTCCTGCTGTGGGACCTGACCGATGAGCGCCTCGGCGTCCTGGAGACCTCCCCCGGGACCTTCCTGACGCGTTCGACCGAGGCGCTGACGGCCGGCCTCTACGAGGGGCTTCCCGCCAGGTTCCTCGAGCTGGGGACGGCCGAGCACCTGCACCTGTGGCGGCCGGCCCTGCTGCGTTTCCACGCCCTCCTGGAGCGGCTCGACCTGGCGAGGCGGACAATCCTCATCAACGTTCCCTGGGCGACGCGGACCACCTCGGGGATGTCCACCGTCCCGAGCTGGGGGCAGACGGCCATGGAGGCCAACTGGGTCATGACCCGCTACATCGAGCTGGTCTACCAGGAGACCGACCTGCGGATTCTGCAGGTGCCCGACGAGCTCGTGGTGGCCGACGACGCGCACCGCTGGGGGGCCGCCCCCTTCCACTACGCCGGCTCCCTGTACTCCTGGGTCGCCGACGAGTTAGAGATCTCCCTGGCACCGCGCAGCCTCGCCCCGGCGCTGTGA","MHSEESTMTAGRITVYGSCVARDVAGEMERRGWSVERYIARQSLISAGCPADVGDVDLSLLRSSFARRSFLSDMVGNLEAQLTAVASYTDLLLWDLTDERLGVLETSPGTFLTRSTEALTAGLYEGLPARFLELGTAEHLHLWRPALLRFHALLERLDLARRTILINVPWATRTTSGMSTVPSWGQTAMEANWVMTRYIELVYQETDLRILQVPDELVVADDAHRWGAAPFHYAGSLYSWVADELEISLAPRSLAPAL$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0312","328924","327980","945","8.56","4.09","33459","ATGACATCGGATGGCGACTCGTCGGCCGCTGTCATGACCGCGGCCGAGGGTCACGAGGCCGGCATCGGCACCGCCACCGTCGTCGTCGACGAGATCGGGGTGAGCTACCGGGCGCCCTCCACGGACGCCGAGGATCTGCGCGCCGCCTCCGTGGCGCAGAAGATCGTCATGGGGATGACTGGGCACAGGCCGAAAGTGAGGGTCGAGGCCCTCAAGAACATCTCCTTCGTGGCTCGCGCCGGGGAGTCGATCGGGATCCTGGGGCGCAACGGGGCGGGGAAGTCCACGCTGCTGCGCGTCATGGGCGGCTTGGAGACGCCGACCTCGGGAACAGTGAGCGCCCGTTCCACCCCGGTGCTCCTGGGCGTCAACGCGGCCCTCGTCCCGGACCTGTCCGGCGAGCGCAATGTGCGCCTGGGCTGCCTGGCCATGGGGCTGACTCCCCAGCAGATCGAGGCGATCATCCCGGAGGTCATTGAGTTGGCCGGGATCGGGAAGGCCATCTACCGCCCGATGAAGACCTATTCCTCGGGAATGGCCTCACGTCTGCGGTTCGCGATCGCCGCCGCGGCGAACCCGGACATCCTCCTCATCGACGAGGCCCTGTCCACCGGTGACGCCGCGTTCAAGGAGCGCAGCGAGATCAAGATGACCGAACTGCGGCGCGCCGCCGGGACGGTGTTCATCGTCAACCATGCCGCGCAGGTCATTGAGGAGATGTGCACCCGGGCTCTGTGGCTCATGGATGGCGAGCTCATCGGTGACGGTCCGGGACCCCAGATCGCCCACGACTACCGCTGGTGGTCCTGGAACATCGCCAAGAACAAGCCGGACAAGGCCGCCACGATCCTGGCCGAGTGCCGGGAGAAGTGGAAACCGGCGGGAGTGCGGATCCAACGCTCGGAGAGCCGCACCCTGCCCTACCGACACGCTCGAGGAGTATGA","MTSDGDSSAAVMTAAEGHEAGIGTATVVVDEIGVSYRAPSTDAEDLRAASVAQKIVMGMTGHRPKVRVEALKNISFVARAGESIGILGRNGAGKSTLLRVMGGLETPTSGTVSARSTPVLLGVNAALVPDLSGERNVRLGCLAMGLTPQQIEAIIPEVIELAGIGKAIYRPMKTYSSGMASRLRFAIAAAANPDILLIDEALSTGDAAFKERSEIKMTELRRAAGTVFIVNHAAQVIEEMCTRALWLMDGELIGDGPGPQIAHDYRWWSWNIAKNKPDKAATILAECREKWKPAGVRIQRSESRTLPYRHARGV$","Techoic acid ABC transporter, ATP-binding protein","Cytoplasm, Membrane","techoic acid ABC transporter, ATP-bindingprotein","techoic acid ABC transporter; ATP-binding protein ","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[175-212]T$	Q47591_ECOLI_Q47591;
PF00005	$\"[81-250]T$	ABC_tran
PS50893	$\"[46-274]T$	ABC_TRANSPORTER_2
PS00211	$\"[175-189]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[80-258]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[68-306]T$	no description
PTHR19222	$\"[27-36]T$ $\"[66-266]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF2	$\"[27-36]T$ $\"[66-266]T$	SIALIC ACID ABC TRANSPORTER

","BeTs to 12 clades of COG1134COG name: ABC-type polysaccharide/polyol phosphate transport system, ATPase componentFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1134 is a------q--rlbc-fghsnujx---Number of proteins in this genome belonging to this COG is 2","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.1e-21. IPB005074C 70-117 IPB005074D 163-206***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3.3e-12. IPB013563A 70-104 IPB013563C 172-199***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3e-10. IPB010509B 81-106 IPB010509D 170-214***** IPB005116 (TOBE domain) with a combined E-value of 1.3e-09. IPB005116A 88-104 IPB005116D 195-214***** IPB013283 (ABC transporter family E signature) with a combined E-value of 7.8e-06. IPB013283D 85-110","Residues 25-153 are 53% similar to a (ATP-BINDING COMPONENT ATP-TRANSPORTER PLASMID) protein domain (PDA0J3M3) which is seen in Q6QW96_AZOBR.Residues 52-224 are 46% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 62-153 are 57% similar to a (EXPORTER LIPOPOLYSACCHARIDE) protein domain (PDA0J3N8) which is seen in Q6AEK2_BBBBB.Residues 67-154 are 63% similar to a (ATP-BINDING TEICHOIC ABC ACID TRANSPORTER) protein domain (PD727857) which is seen in Q88ZH4_LACPL.Residues 68-198 are 58% similar to a (BLL4315 ATP-BINDING) protein domain (PD728322) which is seen in Q89M78_BRAJA.Residues 68-257 are 45% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 70-151 are 62% similar to a (ATP-BINDING POLYSACCHARIDE ABC TRANSPORTER) protein domain (PD611236) which is seen in Q8TRJ8_METAC.Residues 71-252 are 46% similar to a (VEXC POLYSACCHARIDE VI ATP-BINDING INNER MEMBRANE BIOSYNTHESIS EXPORT) protein domain (PD416480) which is seen in VEXC_SALTI.Residues 71-115 are 77% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q7W260_BORPA.Residues 75-198 are 54% similar to a (ABC-TYPE TRANSPORTER) protein domain (PDA190W2) which is seen in Q692K7_YEREN.Residues 198-251 are 77% similar to a (ATP-BINDING ABC TRANSPORTER ACID EXPORT TRANSPORTER POLYSACCHARIDE TEICHOIC COMPONENT SYSTEM) protein domain (PD336368) which is seen in Q9EWH8_STRCO.","","-44% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 1.5E_16);-46% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.3E_14);-46% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.3E_14);-46% similar to PDB:1OXU Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.3E_14);-46% similar to PDB:1OXV Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.3E_14);","Residues 81 to 250 (E_value = 2e-26) place ANA_0312 in the ABC_tran family which is described as ABC transporter.","","acid ABC transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0313","329918","329004","915","10.09","10.14","34516","ATGAGCAGGGCGTCCTGGGCCCCGTGGTCCGATGGGCAGCCGTTCTGGGGCGGCAGCTCGGAGGTCAGTGTCAGCGTCGTCGAGCTCAGCGAGCTCTACCCGGTGGGCCGGCGCCCGCCGCTGGGGGCCTACATCCGCCAGCTCTGGCAGCGCCGGCACTTCATCTGGGCCGACGCCCGGGCCAAGGCCCTGGGCTCTCAACGGGGCACCTTCCTGGGCAACGCCTGGCTCATCGCCAAGCCGATGCTCGACGCGATCGTCTACTTCCTGGTCTTCGGTCTGCTTCTGCAGACGAGCCGCGGTATTGACAACTTCATCGGCTACCTCATCATCGGCGTCACGTTCTTCCCGCCGCTGCAGCGGGCGGTCACCGGTGGCAGCCAGGTGATCGTCACCGGCAGGAACCTCATTCGAGGCTTCTCCTTCCCTCGGGCCGCCCTGCCCGCGTCGTACACGATTCGCAGCGCGATCGACCTGGTCCCGCCGATGATCGCGCTCCTCGTCCTCGTGGTGGTTCTTCCTCCTCACGCCTGGCCGAGCTGGCACTGGGTCCTCATCGTCCCGGTCCTGGCGCTTCAGGTGCTCCTGAGCCTGGGACTGACGCTGGCGACCTCCCGTATCACGACGACGATCCCGGACATGCGCAACATCTGGCCCTTCCTGACTCAGTTCTGGTTCTACGCCTCGGGAGTCTTCTTCTCCTACGAACGGTTCATCCATCACCCGGTGATGCTGCGGGCCATGGACCTCAATCCCGGTTACCTCATCATCACGATGTACCGGGAGGCGATCCTGTACCAGCGTGTTCCGCAGCCGCGCATGTGGCTCATCCTCAGTGCCTGGTCGCTGGGGCTGACCGCCGTGTCCTTCGTGTTCTTCTGGGAGAAGGAGGAAGCCTACGGTGTCGAGCGCTGA","MSRASWAPWSDGQPFWGGSSEVSVSVVELSELYPVGRRPPLGAYIRQLWQRRHFIWADARAKALGSQRGTFLGNAWLIAKPMLDAIVYFLVFGLLLQTSRGIDNFIGYLIIGVTFFPPLQRAVTGGSQVIVTGRNLIRGFSFPRAALPASYTIRSAIDLVPPMIALLVLVVVLPPHAWPSWHWVLIVPVLALQVLLSLGLTLATSRITTTIPDMRNIWPFLTQFWFYASGVFFSYERFIHHPVMLRAMDLNPGYLIITMYREAILYQRVPQPRMWLILSAWSLGLTAVSFVFFWEKEEAYGVER$","Techoic acid ABC transporter, permease protein","Membrane, Cytoplasm","putative ABC transporter integral membraneprotein","K01992 ABC-2 type transport system permease protein","ABC-2 type transporter","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[53-265]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
tmhmm	$\"[76-96]?$ $\"[102-120]?$ $\"[159-179]?$ $\"[185-205]?$ $\"[217-235]?$ $\"[274-294]?$	transmembrane_regions

","BeTs to 6 clades of COG1682COG name: ABC-type polysaccharide/polyol phosphate export systems, permease componentFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1682 is a------q--rlbc-fghsnujx---Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 72-214 are 60% similar to a (ABC PERMEASE TRANSPORTER MEMBRANE INTEGRAL TRANSPORTER SYSTEM ACID ABC-TRANSPORTER O-ANTIGEN) protein domain (PD002060) which is seen in Q9EWH9_STRCO.Residues 217-301 are 55% similar to a (MEMBRANE ABC TRANSPORTER COMPONENT INTEGRAL) protein domain (PD600731) which is seen in Q82DA1_STRAW.","","-42% similar to PDB:2B42 Crystal structure of the Triticum xylanse inhibitor-I in complex with bacillus subtilis xylanase (E_value = );-41% similar to PDB:1T6E Crystal Structure of the Triticum aestivum xylanase inhibitor I (E_value = );-41% similar to PDB:1T6G Crystal structure of the Triticum aestivum xylanase inhibitor-I in complex with aspergillus niger xylanase-I (E_value = );","Residues 53 to 265 (E_value = 3.5e-07) place ANA_0313 in the ABC2_membrane family which is described as ABC-2 type transporter.","","ABC transporter integral membrane protein (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0314","331537","329915","1623","9.40","13.42","57840","ATGCCTGAGCCCTGGCGCGGCCGGAGCGCACGGGCGCTCAGCATCGGGGCCGGTGAGCACGAGCTGCGCCGGGCGCTGTCGGCGTTCATCGCCGACCGACCGGACTGCGCCGGTGACGCGCTGAGCCGGGCGGTACCACGATCGGCCCTTGGCCGCCGGCTCGCCGCCGAGATGGCGATCCACCTGGGGTCGGCGGAGCGCAGGCATCTTGACGCCAAGGGCCTGAGCCCCGCGGTGCGCGCGCGGGACCTGTGGTCCCGGGGCCACCTGAGCGCCGCACTCAGCACACTGGAGGCAGCGCCCGTCTCCGGGGCGCTGCGGGCCCGTCTGCGTTCCCAGCTCGCCATGATGAGCCCGGGCTTTCACCTGCCCCGATTGTCCCCCTCACCGGGCTGGACCGCTCCTGACCCCGGCGAGCCGCTGCGAGTGCTTCACCTGCTGACCAGCTCACTGCCCCACACCCAGTCCGGCTACACCGTGCGCTCGCACGCACTCCTTCAGGCGCAGTGCGACGCCGGCATCGACGTGCGGGCGGTGACCCGCATCGGCTACCCCGTCATCATCGGCAGACCCTCGGCTCAGGCCACTGACGTCGTCGACGCAGTCACCTACCGGCGGCTTCTGCCCGCGCGCACCCAGGCCGCGCCGATAGCCCGGCTGACTCAGATGAGCCGCCTGCTGGCGCGGGAGGTGGAGGCGTTCCGCCCCCACGTGCTGCACACGACCACCAACTACGTCAACGCCCTGGTCACCCAGGCGGTGGCGCGCTCCTACGGTCTGCCCTGGGTCTACGAGATGCGAGGGGTACTGGAGTGCACCTGGGTGGCTTCCAGGCCGGTGGGTCAGCAGGCCGAGGCACTGGGCTCCGAGCGCTTCGCGCTGCTACGGGCCAAGGAGGCCGAGATGGCCCGGTGGGCCGACGCCGTCGTCGTCCTCTCACGGGTCCAGGCCCAGGACCTCGCGGCCCGAGGAGTCGAGCCCGGCCGGATCACGGTCATACCCAACGCCGTGGAGCAGGATGTCCTCAACGCCACTAGGTACTCGCCGGCAGATGCCCGCCAAAGGCTGGGACTGTCCCCCGACGGTCTGTGGGTGGGCAGCGTCTCCTCCCTGGTGGGTTACGAGGGCTTCGACGTGCTCCTGCGGGCCGTGGCGCTCTGCCGCGCTCGAGGGGTCGACGTGCGGTGCGCCGTCGTGGGTGACGGGGTCAGCCGCCCCGGGCTGGTGGCCCTGGCCGGAGAGCTGGGGCTGGAGGCCTCGGTGTGCGTCCTTCCCGGACGGGTGGAGCGCGCCACGGCCCTGGACTGGTACCAGGCCCTGGACGTCTTCTGCGTGCCGAGGCTGGATACGCCGGTGTGCCGGCTGGTGACGCCGCTCAAGCCGATGACGGCGATGGCGCTGGGGCGGCCGGTGGTGGTCTCCGACCTTCCCGCGCTCAGCGAGCTCACCGCCGCAGCGACGAATCGGTCCTTCCCGGCCGGGGACGTGGAGGCGCTCAGCCGAGTGCTGACTGGTATGGCGTCTGGAGATCCCCTGCCCTCAACGCCCTCAACGCATCAGCCGCTGCCCACCTGGAGCGGCAACGCAGTCCGTCAGGCCGAGATCTACAAGGAGCTGGTATGA","MPEPWRGRSARALSIGAGEHELRRALSAFIADRPDCAGDALSRAVPRSALGRRLAAEMAIHLGSAERRHLDAKGLSPAVRARDLWSRGHLSAALSTLEAAPVSGALRARLRSQLAMMSPGFHLPRLSPSPGWTAPDPGEPLRVLHLLTSSLPHTQSGYTVRSHALLQAQCDAGIDVRAVTRIGYPVIIGRPSAQATDVVDAVTYRRLLPARTQAAPIARLTQMSRLLAREVEAFRPHVLHTTTNYVNALVTQAVARSYGLPWVYEMRGVLECTWVASRPVGQQAEALGSERFALLRAKEAEMARWADAVVVLSRVQAQDLAARGVEPGRITVIPNAVEQDVLNATRYSPADARQRLGLSPDGLWVGSVSSLVGYEGFDVLLRAVALCRARGVDVRCAVVGDGVSRPGLVALAGELGLEASVCVLPGRVERATALDWYQALDVFCVPRLDTPVCRLVTPLKPMTAMALGRPVVVSDLPALSELTAAATNRSFPAGDVEALSRVLTGMASGDPLPSTPSTHQPLPTWSGNAVRQAEIYKELV$","Glycosyl transferase, group 1","Cytoplasm, Membrane","Glycosyl transferases group 1, putative","glycosyl transferase; group 1","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[349-503]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[142-503]T$	GLYCOSYLTRANSFERASE

","BeTs to 18 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","Residues 135-354 are 49% similar to a (TRANSFERASE TRANSFERASES GLYCOSYL GROUP) protein domain (PD846232) which is seen in Q82UY1_NITEU.","","No significant hits to the PDB database (E-value < E-10).","Residues 349 to 523 (E_value = 4.4e-13) place ANA_0314 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","transferases group 1, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0315","332909","331635","1275","9.95","13.20","45359","ATGCGCATTCTTCTGCTCACTCACTACTGGGCACCAGAGGTCGGGGCTCCTCAACGCCGCTGGAACCGGCTGGCCGAGGCGCTGAACTCCCGGGGCCATGAGCTGGCGGTGCTGGCTCCGGCCCCCCACTACCCGGGCGGTCGTCTCCTGCCAGGCGGAGGGGCCCACGTGGCTGGTTCGATCAGACGGGACGTCACCGGAGCCATGGTGCATCGCACGATCTTCCGTCCCTACGGCAACGCCGTGTGCGGACGCGGAGTCGATCAGATGGTCACGGCGGCCGACTCCGTGCGCCTGGGGGTAGCACGCTTTCGGGGAGATAACCGTCCCGACGTCATCCTCGGATCGGTACCGGGGCTCCCCACCCTTCCGGCTGCGCTCGCCGTCGGGAGGGTCCTGCACCGTCCCGTCGTGGTGGAGCTGCGAGACGCCTGGCCGGACCTGCTCCTGTCAGCCGGGCAGTGGTCCGAGCCGGCCGCCTGTCCATCGGCCGTGGCGCAGGCCCGCCGGGTCCGCGGGATGAACGTTGTCAGCCGGGGTACGCGCAGCCTCCTGCCGCCCCTGATCACCCGCCTGGAGCAGGAGGCCGCGGCCGTGGTGACGACGACCGACTCCTTCGCCCGGGTCCTGCGCTCCCGCGGGGTACGCCACGTGGTGACGGTGCGCAACACCGGTGCCACGGTGCCGATGGAAAGGACGGGGGCCGGCCGACACCGCCCGAACGGCGCCCTGAACGTGCTCTACCTGGGAACAGTGGGGCGCGCTCAGGGGCTGGGCTTCGCGGTAAGGGCCGCGCACATCGCTCAGCGCAACGGCACCCCGGTGGTACTGCGGATCGTCGGCGACGGCGCGCAGCTCCAGGAGGTGGCAGCCCTGGCCCGCAGGCTCGGGGCCCCGGTTGAGATCCATCCCCCTGTGCCCTGGAGTGAGGTGGCTCAGCACTACGCCTGGGCTGATACGGCTCTGGTGAGCCTCCAGAACTGGCCGGCCATGTGTGTGACAGTCCCGTCCAAGCTCTACGAGATCATGTCTGCCGGAGTGCACGTGTGCGCCTCGGTGGACGGGGAGGCCCGGCGCATCGTGGAGGACGCCGGCTGCGGTGACGTCACTGCCCCGCAGGACCCGCAGGCCCTGGCCTCCTTGTGGAGCACGCTGGCCGCCGACCACAGCCGTCTGGACGTGACGGGTGGACGACGCTGGCTGGCGGACCACGCCGACGCCGAGGTCATGACCGACCGCTATGAGTCCCTCCTGAGGCAGGTGGCCGGTGACTGA","MRILLLTHYWAPEVGAPQRRWNRLAEALNSRGHELAVLAPAPHYPGGRLLPGGGAHVAGSIRRDVTGAMVHRTIFRPYGNAVCGRGVDQMVTAADSVRLGVARFRGDNRPDVILGSVPGLPTLPAALAVGRVLHRPVVVELRDAWPDLLLSAGQWSEPAACPSAVAQARRVRGMNVVSRGTRSLLPPLITRLEQEAAAVVTTTDSFARVLRSRGVRHVVTVRNTGATVPMERTGAGRHRPNGALNVLYLGTVGRAQGLGFAVRAAHIAQRNGTPVVLRIVGDGAQLQEVAALARRLGAPVEIHPPVPWSEVAQHYAWADTALVSLQNWPAMCVTVPSKLYEIMSAGVHVCASVDGEARRIVEDAGCGDVTAPQDPQALASLWSTLAADHSRLDVTGGRRWLADHADAEVMTDRYESLLRQVAGD$","Glycosyl transferase, group 1","Cytoplasm, Membrane","lipopolysaccharide biosynthesis protein,putative","glycosyl transferase; group 1","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[230-400]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-161]T$ $\"[179-421]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF8	$\"[2-161]T$ $\"[179-421]T$	GLYCOSYLTRANSFERASE

","BeTs to 11 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 230 to 400 (E_value = 0.00034) place ANA_0315 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","biosynthesis protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0316","334295","332913","1383","10.00","19.97","48035","ATGTCTCTTCCTGGCAACCCTTGTCAGGACGCTCTTATCAACGCATCGAATTCTTTATCCGCGCCTGCTCCTGATAGGGATCGCATCCGCTGCACTCATTCAGCTGACCGCCTGGTACGTGACATGCCGCTACTGGCCGTGGGCCTCCACGCGGACCATGCCCTTCGTCATCGTGGCTGGGGCCGGGTTCGCACTGGGGTCCAGCTTCCTCGACCTCGCCACACAGGTCCGCCTCCTGCCGTGGAGCGCAGCCCTGGCTGGGTCTGCCGTCGCGGTGGCGGATCAGTGGCGGCACCGACTGAGATGGCAGGCTCAGGCGCGACGGGCCCTGGAGACGGCCTCATGACCACCCTGCTTCTGAGCGGGCTCGCCCTGACGGCGGCTGTCTGCGCCTCCTTGACCGCAGCGGTGATTCCACTTCTGCGGAGGGCCCGCGTCATTGATGTTCCCGGGGACAGATCCCTTCACAAGACGCCTGTTCCCCGCGGTGGTGGTCTCGCCATTGTCCTGTCCGCCTCGCTGGCCACCTGGGCGACCGTACTGGCTGCGGTGCACCGGCACGACACGGTTCACTCACTGACCGGTCTCGGCCTCGCGCTCATGGGGCTGGCGACCGTGCTGGCCTTTGCGCTGCTCGGGCTGATCGAGGATCTGTTTTCCGTGTCGGTCAGGACTCGCCTGGTTCTCCAGCTCGCCCTGGGGGCAGGACTCGGGCTGGTGGCACACAGTACCTTCGAGGTCTCACTGTGGTGGACTCCGGCGATCTGCGTGAGCACCGCCGCGCTGGTCAACGCCACGAACTTCATGGACGGCGCTAACGGCCTGGCCTGCAGCCACGCCCTGATGACCTCCCTGTGGTACGTCCAGGTGGCGATCCTCGCCCCGGTTCCCGGGCTGGGGCTCGTCATGGTCTCGGTGGCCGGCGCATGCCTTGGTTTCCTGCCCTTCAACACGCCTCGTGCCAAGGTGTTCCTGGGTGACTCCGGTTCCTACGCCCTGGGCGGCGCCTGGGCCTTCTCGGTCACGGCCTGCCTGGCCCAGGGTGTGGCCGTGGAGGCGGCGCTCGCCCCTGTCCTCGTGCTTCTGGCGGATACCGGCTATACCCTGTGGAAGCGGCTGAGAGCGGGCCAGTGCTGGTACGCGCCTCACCGGCTTCACGTCTATCAGCGCCTGGTCTGTGCCGGCTGGCCGCACTGGGCGTCGGCCCTCCTGGTGACCCTGGCCGCGGCGTCGTGCTCGGCTCTGGCGTCAGGCAGCCTTCTGACCCGCAGCCGGCTCTGGATGCCCCAGGTCGCCATGGCAGCAGTCCTGATCCTCTATCTGAAGATGCCCTCCATCATCGGAGCCCCCAATCCCTTCCCCACCCCTCGACGGGCGAGGTGA","MSLPGNPCQDALINASNSLSAPAPDRDRIRCTHSADRLVRDMPLLAVGLHADHALRHRGWGRVRTGVQLPRPRHTGPPPAVERSPGWVCRRGGGSVAAPTEMAGSGATGPGDGLMTTLLLSGLALTAAVCASLTAAVIPLLRRARVIDVPGDRSLHKTPVPRGGGLAIVLSASLATWATVLAAVHRHDTVHSLTGLGLALMGLATVLAFALLGLIEDLFSVSVRTRLVLQLALGAGLGLVAHSTFEVSLWWTPAICVSTAALVNATNFMDGANGLACSHALMTSLWYVQVAILAPVPGLGLVMVSVAGACLGFLPFNTPRAKVFLGDSGSYALGGAWAFSVTACLAQGVAVEAALAPVLVLLADTGYTLWKRLRAGQCWYAPHRLHVYQRLVCAGWPHWASALLVTLAAASCSALASGSLLTRSRLWMPQVAMAAVLILYLKMPSIIGAPNPFPTPRRAR$","Glycosyl transferase, family 4","Membrane, Cytoplasm, Extracellular","lipopolysaccharide core biosynthesis protein","lipopolysaccharide core biosynthesis protein","glycosyl transferase, family 4","","Perham R.N. The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes. Biochem. Soc. Trans. 1990. 18(2):185-187. PMID: 2199259Marsh J.J., Lebherz H.G. Fructose-bisphosphate aldolases: an evolutionary history. Trends Biochem. Sci. 1992. 17(3):110-113. PMID: 1412694Berry A., Marshall K.E. Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett. 1993. 318(1):11-16. PMID: 8436219","","","

InterPro
IPR000715
Family

Glycosyl transferase, family 4
PTHR22926	$\"[138-460]T$	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
PF00953	$\"[199-343]T$	Glycos_transf_4

InterPro
IPR000771
Family

Ketose-bisphosphate aldolase, class-II
PS00602	$\"[42-54]?$	ALDOLASE_CLASS_II_1

noIPR
unintegrated

unintegrated
tmhmm	$\"[122-142]?$ $\"[163-183]?$ $\"[193-215]?$ $\"[225-245]?$ $\"[251-269]?$ $\"[290-310]?$ $\"[329-363]?$ $\"[399-417]?$ $\"[423-441]?$	transmembrane_regions

","BeTs to 21 clades of COG0472COG name: UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N- acetylglucosamine-1-phosphate transferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0472 is --m-k-yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB003524 (Phospho-N-acetylmuramoyl-pentapeptide transferase) with a combined E-value of 3.6e-33. IPB003524A 143-169 IPB003524B 196-235 IPB003524C 264-276 IPB003524D 305-342","Residues 305-398 are 55% similar to a (TRANSFERASE PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE TRANSMEMBRANE SYNTHESIS PHOSPHOTRANSFERASE CELL DIVISION UDP- PEPTIDOGLYCAN MURNAC-PENTAPEPTIDE) protein domain (PD001416) which is seen in Q7U8Z9_SYNPX.","","No significant hits to the PDB database (E-value < E-10).","Residues 199 to 343 (E_value = 7.1e-13) place ANA_0316 in the Glycos_transf_4 family which is described as Glycosyl transferase family 4.","","core biosynthesis protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0317","334905","335324","420","5.41","-3.63","15988","ATGAAACGCATCATCACCTACGGCTCCTTCGATCTGCTTCACTACGGGCACATCGAGCTGCTGCGCCGGGCCAAGGCTATGGGGGACTATCTCATCGTCGCTCTATCGACCGATGAGTTCAGCGCTTCCAAGGGGAAACGTGCCTACTTCTCCTATGAGCAGCGCAAGGCGATGCTTGAGGCCGTCCGCTATGTCGACATGGTCGTTCCTGAACGGACCTGGGGTCAGAAGAGCCGGGACATCGACGAGTACGGCATCGACGTCTTCGTCATCGGCGATGACTGGATCGGCACCTTCGACGAGCAGCTTGAAGGACGCTGCGAGATCGCCTACCTCCCGCGGACCCCGGAGATCGGCTCCGCTCAGGGACGGCCGTGCCGCGAGGGGCGGGAGGACGCTCAGGAGGCTCTCGTGCGGTGA","MKRIITYGSFDLLHYGHIELLRRAKAMGDYLIVALSTDEFSASKGKRAYFSYEQRKAMLEAVRYVDMVVPERTWGQKSRDIDEYGIDVFVIGDDWIGTFDEQLEGRCEIAYLPRTPEIGSAQGRPCREGREDAQEALVR$","Glycerol-3-phosphate cytidylyltransferase","Cytoplasm","glycerol-3-phosphate cytidylyltransferase","glycerol-3-phosphate cytidylyltransferase ","glycerol-3-phosphate cytidylyltransferase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR004820
Domain

Cytidylyltransferase
PF01467	$\"[5-95]T$	CTP_transf_2

InterPro
IPR004821
Domain

Cytidyltransferase-related
TIGR00125	$\"[3-68]T$	cyt_tran_rel: cytidyltransferase-related do

InterPro
IPR006409
Family

Glycerol-3-phosphate cytidylyltransferase
TIGR01518	$\"[4-127]T$	g3p_cytidyltrns: glycerol-3-phosphate cytid

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[1-122]T$	no description

noIPR
unintegrated

unintegrated
PTHR10739	$\"[4-115]T$	CHOLINE/ETHANOLAMINE PHOSPHATE CYTIDYLYLTRANSFERASE

InterPro
IPR002509
Domain

Polysaccharide deacetylase
PF01522	$\"[84-211]T$	Polysacc_deac_1

noIPR
unintegrated

unintegrated
PS51257	$\"[1-17]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-19]?$	signal-peptide

","BeTs to 8 clades of COG0726COG name: Predicted xylanase/chitin deacetylaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0726 is ---pk-y-vdrlbcefg-s-uj----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 78-193 are 50% similar to a (DEACETYLASE POLYSACCHARIDE) protein domain (PD966910) which is seen in Q73H54_WOLPM.Residues 90-276 are 46% similar to a (DEACETYLASE POLYSACCHARIDE HYDROLASE DEGRADATION 3.5.1.- XYLAN NODULATION SIGNAL PRECURSOR CHITOOLIGOSACCHARIDE) protein domain (PD389393) which is seen in Q8R8J1_THETN.Residues 92-214 are similar to a (ML2649) protein domain (PD934004) which is seen in Q73RZ2_MYCPA.Residues 216-277 are 69% similar to a (ML2649) protein domain (PD395482) which is seen in Q73RZ2_MYCPA.","","-46% similar to PDB:2J13 STRUCTURE OF A FAMILY 4 CARBOHYDRATE ESTERASE FROM BACILLUS ANTHRACIS (E_value = 2.1E_14);-50% similar to PDB:1NY1 CRYSTAL STRUCTURE OF B. SUBTILIS POLYSACCHARIDE DEACETYLASE NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET SR127. (E_value = 3.1E_10);-50% similar to PDB:1W17 STRUCTURE OF BACILLUS SUBTILIS PDAA, A FAMILY 4 CARBOHYDRATE ESTERASE. (E_value = 3.1E_10);-50% similar to PDB:1W1A STRUCTURE OF BACILLUS SUBTILIS PDAA IN COMPLEX WITH NAG, A FAMILY 4 CARBOHYDRATE ESTERASE. (E_value = 3.1E_10);-50% similar to PDB:1W1B STRUCTURE OF BACILLUS SUBTILIS PDAA WITH CADMIUM, A FAMILY 4 CARBOHYDRATE ESTERASE. (E_value = 3.1E_10);","Residues 84 to 211 (E_value = 2.9e-30) place ANA_0318 in the Polysacc_deac_1 family which is described as Polysaccharide deacetylase.","","deacetylase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0320","337235","336594","642","5.11","-8.89","23491","ATGACTACAGTGGCTCCCGTGAGCAAGCAGATGACTACCTCTGACCCGCTGGTGTGGATCGACTGTGAGATGACGGGCCTGGACCAGAGCGCCGACGCGCTCATCGAGGTCGCCGTCGTCGTCACCGACTATGAGCTCAAGCCCCTGGCTGAGGGAATCGATGTGCTCATCAAGCCCCCCGCCGCCGCGCTGGAGCAGATGGACGACTACGTGCGCACCATGCACACCTCCTCGGGCCTGCTGGCCGCGCTGGAGGACGGAGTGACCATGGAGACTGCCCGCACCACGGTCCTGGACTATGTGACCTCCCTGGTGCCCGAGCCGCGCACCGCCCAGCTCGCGGGCAACTCCGTGGGCACGGACAAGGCGTTCCTGGCCCGCGACATGCCCGATCTCATCAAGCACCTCCACTACCGGATCGTGGATGTCTCCTCCCTCAAGGAGCTGGCCAAGCGCTGGTACCCCAGGACCTTCTTCCACGCACCGAAGAAGGCCGGCGGGCACCGCGCGCTGGCGGACATCCTGGAGTCCATCGACGAGCTGCGCTACTACCGCGAGGTGCTGTTCCCCAGCGGGGAGGGCCCCAGCTCCCAGGAGTGCAAGGACGTGGCCGAGCGGATCCTCAGCACACCCACCAGGTGA","MTTVAPVSKQMTTSDPLVWIDCEMTGLDQSADALIEVAVVVTDYELKPLAEGIDVLIKPPAAALEQMDDYVRTMHTSSGLLAALEDGVTMETARTTVLDYVTSLVPEPRTAQLAGNSVGTDKAFLARDMPDLIKHLHYRIVDVSSLKELAKRWYPRTFFHAPKKAGGHRALADILESIDELRYYREVLFPSGEGPSSQECKDVAERILSTPTR$","Oligoribonuclease","Cytoplasm","Oligoribonuclease","oligoribonuclease ","Exonuclease, RNase T and DNA polymerase III","","Koonin E.V., Deutscher M.P. RNase T shares conserved sequence motifs with DNA proofreading exonucleases. Nucleic Acids Res. 1993. 21(10):2521-2522. PMID: 8506149","","","

InterPro
IPR006055
Domain

Exonuclease
SM00479	$\"[16-190]T$	EXOIII

InterPro
IPR013520
Domain

Exonuclease, RNase T and DNA polymerase III
PF00929	$\"[17-181]T$	Exonuc_X-T

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[8-192]T$	no description
PTHR11046	$\"[15-211]T$	OLIGORIBONUCLEASE, MITOCHONDRIAL

","BeTs to 8 clades of COG1949COG name: Oligoribonuclease (3'->5' exoribonuclease)Functional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG1949 is ------y---r---efghsn------Number of proteins in this genome belonging to this COG is 1","***** IPB013520 (Exonuclease, RNase T and DNA polymerase III) with a combined E-value of 3e-19. IPB013520A 18-28 IPB013520B 121-130 IPB013520C 137-155***** IPB006055 (Exonuclease) with a combined E-value of 1.3e-10. IPB006055A 18-28 IPB006055B 167-181","Residues 14-52 are 79% similar to a (OLIGORIBONUCLEASE 3.1.-.- HYDROLASE NUCLEASE EXONUCLEASE PROBABLE MITOCHONDRIAL SMALL CGI-114 OLIGORIBONUCLEASE) protein domain (PD477405) which is seen in Q6AEG5_BBBBB.Residues 55-164 are similar to a (OLIGORIBONUCLEASE 3.1.-.- HYDROLASE NUCLEASE EXONUCLEASE PROBABLE MITOCHONDRIAL OLIGORIBONUCLEASE YLR059C SMALL) protein domain (PD011165) which is seen in Q6AEG5_BBBBB.","","-59% similar to PDB:1J9A OLIGORIBONUCLEASE (E_value = 9.2E_32);-60% similar to PDB:1YTA Crystal Structure of Oligoribonuclease, the lone essential exoribonuclease in Escherichia coli (E_value = 3.5E_31);-60% similar to PDB:2GBZ The Crystal Structure of XC847 from Xanthomonas campestris: a 3-5 Oligoribonuclease of DnaQ fold family with a Novel Opposingly-Shifted Helix (E_value = 6.0E_31);","Residues 17 to 181 (E_value = 4.2e-17) place ANA_0320 in the Exonuc_X-T family which is described as Exonuclease.","","(CGI) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0321","337387","339906","2520","6.19","-5.75","88344","ATGTCCCACAGCCCCGACCCCCGTCACCTCGGAAGCTCCTACATCATGGAGACCCGGATCGGTGCGGGTGCCCAAGGAGAGGTCTGGCGCGGTCGGCGTACGGACTCTCGCGAGACCTTGGCCTTCAAGGTGCTGCGTGCGGACCTGGTGGAGAATCCCGACGTCGTGGAGCGCTTCATCAAGGAGCGCTCCACTCTGCTGCGGGTGCGCAGTCCCTATGTCGTCGCCATTCGTGACGTCGTCATCGAGGGTTCCACTTTCGCGATCGTCATGGACTATGTCAACGGTGGTGACCTGCGAGATCTGCTGAGGGCATACGGCTGCCTACCGCCTGCGCAGGTGGCGTCCCTGGGGACGCGTATCGCTCAGGGACTGTCCTCGGTTCATCAGGCCGGCGTGATCCACCGGGACATCAAGCCTGCCAACGTCCTGCTCAGCTCTCGCCCCAGCCGGGGCGGCGACCCGGCTGAGACGGTCATCGTCGGGGTCGCGCCCGGAGGGGAGGTGCCCGAGACTGTTGTGCCCCGACTCGCAGACTTCGGGGTGGCGCGCATCTGCGACACCTTCTCCGCCTCCCACATCACGGGGGCCATCGGTACACCGCTGTACATGGCGCCGGAGATCCTGTCGCTGCAGGCCCCGACCTCGGCGGCCGACATCTATTCACTGGGTATCATGCTCTACGAGATGGTGTGTGGGACGACGCCGTTCGTGGGGCAACCCGCCCAGCTGCTCAGCCAGCACGCCCGGCGTGACGCGGGCCGGCCCCAGGGGGTGCCCGACCCGTTGTGGGAGCTCATCGCCTCGATGATCTCCAAGCAGCCCGACATGCGTCCTTCGAGTGAGGACGTCGCCCAGCGTCTGGACGTCATGCAGTCCACTCTGGCCGGTCTGCCGGCCGCACCGCGGCTCGCCTCGCCCCCGCAATCAACGGTCTCGCTCGTTCCCTACGACTGGGAGGCCCTGCCTCCTGCGGCTCCCGAAGCTCCTGCGGCCCCGCCGGCGACGCTGCCGACTCCCTCGGCGACCCCGGCCACGATGCCCTTCGCCCCGGATGCACCGACCCTGGTGAGTGGGCAGCAGTACGTCCCCGGCCCCGGACAGGCTCCTGTCAGCCCGGGGACGGCAGGGACCGCGGGCTTCACCGTTCCGGCGATGCCGACCGGCCCCGGTGTCTCCGACCCCTCTGCGCCCGCTTTCTACAGTCAACCGGGCCCGCAGTACCCGGAGGCTGCGACGGGTGGTCCGCAGACCGGAGTGCGTCGGCGGTGGTGGCGGCGCCGGTGGGTGGCTGTGGCTGCCGTGGTCACGGTCCTGGCAGTGGTGGGGGCGAGCGCGACCTGGTGGTACTTCTTCTCCGGAGTGCAGACCGGCAAAAGGTGGGCGGTGGAGCTGCCTGCTGGCAACGGTGTCCGCGAGGACCTGCGCTATTCGTCGGTTTCCGACCCCGTCCTGTCCGCAGACGGGACCACGATGGCCTACTATCACGATAGCAAGACGCGCCTTGTGGATCTCACGAAGAGCACGACGACGCCGGTGTGGAGCGGTGAGTGCGACAAGACCCTCCCCTGGGTCGGTGGCTCGATGCTCTGTACCAAGTCCAGTGACGACGAGTCCACGGTGGTCGGGGCTGCGGGCAAGACCTCCAAGGCGCCTTTCTCCAAGGGCTCCTTCTACATCGGCGCGACACCCGACCTCGGCATCGTGTCCGACAAGGGGGAGTCCTCCGACGGAGGCTCCATGAAGGCCTACGACGCATCTGGCAAGGAGAAATGGACCGCTTCGGGTCATTATGAGGCAGGCCGGGTCGACAACGGTTTCATCCTCACCTACGAGAACAAGTCGCGACAGTTCCAGGTGCTGTCGGCCAAGACCGGTGAGGTGCTCGTCTCCGAGCCCGGCAAGCAGCAGGGCTCGGACCTCGATGAGGACTCTCGATTCCCTGGCGGTTTCAATATCGAGTCCGGGCCGGAGGCCTTCTCCCGAGTGACGTCCTCAGGCGCCACGATCTACAAGGCCAACGGCAGCGAGGCGGCAACCGTCTCAGGCAAGTTCTCGGAGAAGCACTGGTGGGCTGCGTCAGCACCACTGGATGCCTCCTCACTGAAAGACGCCTACTCCTCCTTGGCCAAGGCATCGTCCTCGACCACCCCGGTCATCGGTTCCAACGGCACGGTCAACGTCGTTATCAATACGAGCGCCTGCACGGCCGAGGTCGGCAGCAAGAAGCTCGCGCTGCCTGAGTTCTCGCAGCGTGAGGGCTGCCACATCAGACCCATCGGGCTACTCAGTGACGGGCAGGTGCTGATCGAGGTCGGAAGGCCGAGCATATGGGACAGTGAACCGGGCAACCTCGTCGTCGCCGTGTCACCCGAGACGGGCAAGGTCGGCTGGAAGACCCCCGGAGCCTATGCTGGCACCGTTGTTCCCGCCGAGGGCCAGAGCGAAGCCCGTCTCCTGGCGGTACAGGGCTCCTCTTTCAACTTCGACCTGGTGATCTCCCGCATCACCAGCAAGTAG","MSHSPDPRHLGSSYIMETRIGAGAQGEVWRGRRTDSRETLAFKVLRADLVENPDVVERFIKERSTLLRVRSPYVVAIRDVVIEGSTFAIVMDYVNGGDLRDLLRAYGCLPPAQVASLGTRIAQGLSSVHQAGVIHRDIKPANVLLSSRPSRGGDPAETVIVGVAPGGEVPETVVPRLADFGVARICDTFSASHITGAIGTPLYMAPEILSLQAPTSAADIYSLGIMLYEMVCGTTPFVGQPAQLLSQHARRDAGRPQGVPDPLWELIASMISKQPDMRPSSEDVAQRLDVMQSTLAGLPAAPRLASPPQSTVSLVPYDWEALPPAAPEAPAAPPATLPTPSATPATMPFAPDAPTLVSGQQYVPGPGQAPVSPGTAGTAGFTVPAMPTGPGVSDPSAPAFYSQPGPQYPEAATGGPQTGVRRRWWRRRWVAVAAVVTVLAVVGASATWWYFFSGVQTGKRWAVELPAGNGVREDLRYSSVSDPVLSADGTTMAYYHDSKTRLVDLTKSTTTPVWSGECDKTLPWVGGSMLCTKSSDDESTVVGAAGKTSKAPFSKGSFYIGATPDLGIVSDKGESSDGGSMKAYDASGKEKWTASGHYEAGRVDNGFILTYENKSRQFQVLSAKTGEVLVSEPGKQQGSDLDEDSRFPGGFNIESGPEAFSRVTSSGATIYKANGSEAATVSGKFSEKHWWAASAPLDASSLKDAYSSLAKASSSTTPVIGSNGTVNVVINTSACTAEVGSKKLALPEFSQREGCHIRPIGLLSDGQVLIEVGRPSIWDSEPGNLVVAVSPETGKVGWKTPGAYAGTVVPAEGQSEARLLAVQGSSFNFDLVISRITSK$","Serine/threonine protein kinase","Membrane, Periplasm","Serine/threonine protein kinase pkaA","serine/threonine protein kinase ","protein kinase","","Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995. 9(8):576-596. PMID: 7768349Hunter T. Protein kinase classification. Meth. Enzymol. 1991. 200:3-37. PMID: 1835513Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth. Enzymol. 1991. 200:38-62. PMID: 1956325Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988. 241(4861):42-51. PMID: 3291115Knighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991. 253(5018):407-414. PMID: 1862342","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[14-282]T$	Q81ZW6_STRAW_Q81ZW6;
PF00069	$\"[14-288]T$	Pkinase
PS50011	$\"[14-295]T$	PROTEIN_KINASE_DOM

InterPro
IPR000897
Domain

GTP-binding signal recognition particle SRP54, GTPase
PS00300	$\"[759-772]?$	SRP54

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[133-145]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[81-286]T$	no description
PTHR22986	$\"[13-149]T$ $\"[174-287]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES
tmhmm	$\"[430-452]?$	transmembrane_regions

","BeTs to 10 clades of COG0515COG name: Serine/threonine protein kinasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0515 is -o-p-zyq-drlbcefghs--j-i-wNumber of proteins in this genome belonging to this COG is 10","***** IPB000961 (Protein kinase C-terminal domain) with a combined E-value of 3.8e-26. IPB000961A 13-47 IPB000961B 72-103 IPB000961C 116-158 IPB000961D 196-237***** IPB001772 (Kinase-associated, C-terminal) with a combined E-value of 6.8e-16. IPB001772A 11-42 IPB001772B 74-128 IPB001772D 207-246***** IPB000095 (PAK-box/P21-Rho-binding) with a combined E-value of 3.1e-13. IPB000095D 97-143 IPB000095E 180-224***** IPB000959 (POLO box duplicated region) with a combined E-value of 3e-11. IPB000959C 120-159 IPB000959D 200-254***** IPB003527 (MAP kinase) with a combined E-value of 4.1e-11. IPB003527C 109-159 IPB003527D 214-256***** IPB000861 (PKN/rhophilin/rhotekin rho-binding repeat) with a combined E-value of 4.9e-09. IPB000861D 92-145 IPB000861E 202-251***** IPB010513 (Ribonuclease 2-5A) with a combined E-value of 5.8e-09. IPB010513D 124-145 IPB010513E 219-239***** IPB002219 (Protein kinase C, phorbol ester/diacylglycerol binding) with a combined E-value of 2.2e-08. IPB002219C 72-104 IPB002219D 180-231***** IPB001180 (Citron-like) with a combined E-value of 1e-06. IPB001180A 110-146 IPB001180B 199-208","Residues 1-399 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796289) which is seen in Q9S2A6_STRCO.Residues 1-239 are 45% similar to a (CELL DIVISION KINASE SERINE/THREONINE-PROTEIN TRANSFERASE MITOSIS ATP-BINDING HOMOLOG CONTROL CYCLE) protein domain (PDA1A0C7) which is seen in CDC2_CAEEL.Residues 1-312 are 45% similar to a (KINASE SERINE-THREONINE) protein domain (PDA1D4F7) which is seen in Q6A9T0_PROAC.Residues 1-286 are 44% similar to a (ATP-BINDING AGCP10418) protein domain (PDA0J0F6) which is seen in Q7QGN6_EEEEE.Residues 1-299 are 45% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA2 PROBABLE TRANSFERASE REPEAT ATP-BINDING) protein domain (PD848557) which is seen in PKNA_BIFLO.Residues 1-308 are 45% similar to a () protein domain (PDA046H8) which is seen in Q73YC5_MYCPA.Residues 1-281 are 46% similar to a (SERINE/THREONINE-PROTEIN KINASE PROBABLE TRANSFERASE PKNJ TRANSMEMBRANE ATP-BINDING) protein domain (PD063660) which is seen in PKNJ_MYCTU.Residues 2-286 are 46% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE WD SERINE/THREONINE ATP-BINDING) protein domain (PD288091) which is seen in Q9RDS3_STRCO.Residues 2-247 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN PPKA TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA025J8) which is seen in Q7UT84_RHOBA.Residues 3-281 are 45% similar to a (KINASE SER/THR P08458 SPS1 CEREVISIAE YDR523C SACCHAROMYCES) protein domain (PDA0B8H6) which is seen in Q6C9X8_EEEEE.Residues 3-284 are 46% similar to a (KINASE STE20-LIKE ATP-BINDING DON3) protein domain (PD609771) which is seen in Q8NJX3_USTMA.Residues 4-284 are 46% similar to a (KINASE RELATED ATP-BINDING SEVERIN) protein domain (PDA0F7C6) which is seen in Q7SFV7_NEUCR.Residues 4-145 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN REGULATOR SERINE/THREONINE) protein domain (PD843536) which is seen in Q9L096_STRCO.Residues 5-308 are 43% similar to a (BLR3604 KINASE TRANSFERASE ATP-BINDING) protein domain (PD828726) which is seen in Q89P79_BRAJA.Residues 5-298 are 44% similar to a (AFR724CP ATP-BINDING) protein domain (PDA101P3) which is seen in Q751V1_ASHGO.Residues 5-310 are 39% similar to a (KINASE SERINE/THREONINE-PROTEIN SERINE/THREONINE KINASE) protein domain (PD745593) which is seen in Q9RUY7_DEIRA.Residues 6-298 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNA TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5E6) which is seen in Q7UX63_RHOBA.Residues 6-288 are 46% similar to a (SERINE/THREONINE-PROTEIN KINASE REPEAT PROBABLE TRANSFERASE WD PKWA ATP-BINDING) protein domain (PD110150) which is seen in PKWA_THECU.Residues 6-308 are 44% similar to a (KINASE SER/THR TRANSFERASE ATP-BINDING) protein domain (PD126531) which is seen in O54229_STRGT.Residues 6-290 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD820279) which is seen in Q81ZY2_STRAW.Residues 6-286 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD141352) which is seen in O54230_STRGT.Residues 6-390 are 40% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE-THREONINE ATP-BINDING) protein domain (PD319602) which is seen in Q9K3W7_STRCO.Residues 6-288 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING SERINE/THREONINE-SPECIFIC PROBABLE) protein domain (PDA1D2S2) which is seen in Q7UFH1_RHOBA.Residues 7-288 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD298418) which is seen in Q9X8G8_STRCO.Residues 7-289 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA010X1) which is seen in Q7UKY9_RHOBA.Residues 7-289 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA10189) which is seen in Q7UKJ3_RHOBA.Residues 7-288 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796214) which is seen in Q81ZX4_STRAW.Residues 7-259 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD239091) which is seen in Q9KJN8_MYXXA.Residues 8-311 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD842227) which is seen in Q81ZZ0_STRAW.Residues 8-316 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756057) which is seen in Q81ZV7_STRAW.Residues 8-288 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD724652) which is seen in Q81ZW8_STRAW.Residues 8-291 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD498679) which is seen in Q8Z111_SALTI.Residues 8-300 are 41% similar to a (KINASE SERINE/THREONINE-PROTEIN MAP TRANSFERASE ATP-BINDING) protein domain (PD324666) which is seen in Q9N9B1_LEIMA.Residues 8-103 are 55% similar to a (KINASE SERINE/THREONINE-PROTEIN REPEAT TRANSFERASE 2.7.1.- WD ATP-BINDING PROBABLE) protein domain (PDA19784) which is seen in Q7UWP5_RHOBA.Residues 8-281 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD975784) which is seen in Q7NPK1_GLOVI.Residues 8-297 are 48% similar to a (KINASE SERINE/THREONINE) protein domain (PDA1A7D8) which is seen in Q6AE50_BBBBB.Residues 9-281 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA10203) which is seen in Q7UIJ7_RHOBA.Residues 9-237 are 45% similar to a (KINASE P27636 SERINE/THREONINE-PROTEIN TRANSFERASE CDC15 CEREVISIAE ATP-BINDING SACCHAROMYCES YAR019C) protein domain (PDA0F8T8) which is seen in Q6FWK3_EEEEE.Residues 10-298 are 46% similar to a (KINASE PKNB SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5H6) which is seen in Q7UFU9_RHOBA.Residues 10-280 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING PLASMID) protein domain (PD756391) which is seen in Q820A7_STRAW.Residues 10-291 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA191E0) which is seen in Q8DLN7_SYNEL.Residues 10-301 are 45% similar to a (KINASE SERINE/THREONINE) protein domain (PD456344) which is seen in Q98IK2_RHILO.Residues 10-304 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA1A878) which is seen in Q72IA2_THET2.Residues 10-275 are 46% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA TRANSFERASE ATP-BINDING PROBABLE) protein domain (PDA188K3) which is seen in PKNA_MYCLE.Residues 10-279 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD810446) which is seen in Q895P6_CLOTE.Residues 10-281 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE KINASE ATP-BINDING) protein domain (PD828286) which is seen in Q9RRH3_DEIRA.Residues 12-301 are 49% similar to a (SIMILAR DEBARYOMYCES HANSENII DEHA0C16181G) protein domain (PD991318) which is seen in Q6C3K8_EEEEE.Residues 12-236 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD727335) which is seen in Q86JX3_DICDI.Residues 12-316 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756060) which is seen in Q81ZY9_STRAW.Residues 12-302 are 42% similar to a (KINASE REPEAT TPR SERINE/THREONINE ATP-BINDING PKN8) protein domain (PD280760) which is seen in Q9XBP6_MYXXA.Residues 12-299 are 43% similar to a (KINASE TRANSFERASE ATP-BINDING MOS) protein domain (PD267193) which is seen in Q9GRC0_ASTPE.Residues 13-296 are 46% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE TPR PHOSPHORYLATION REPEAT PKN1 ATP-BINDING) protein domain (PD052299) which is seen in PKN1_MYXXA.Residues 13-298 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D3Y0) which is seen in Q7UVF2_RHOBA.Residues 14-230 are 44% similar to a (KINASE CELL DIVISION SERINE/THREONINE-PROTEIN 3D-STRUCTURE CYCLE TRANSFERASE PHOSPHORYLATION PLSTIRE ATP-BINDING) protein domain (PD470147) which is seen in CDK6_HUMAN.Residues 14-294 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796751) which is seen in Q81ZW2_STRAW.Residues 14-247 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE CAMP ATP-BINDING CAMP-DEPENDENT NUCLEAR) protein domain (PD061517) which is seen in O00843_PARPR.Residues 14-288 are 45% similar to a (CELL DIVISION SERINE/THREONINE-PROTEIN CONTROL KINASE CYCLE TRANSFERASE 2.7.1.- MITOSIS ATP-BINDING) protein domain (PDA0F8T7) which is seen in CC15_YEAST.Residues 14-288 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D5J2) which is seen in Q7UZ75_RHOBA.Residues 14-303 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA0Z806) which is seen in Q7NLM6_GLOVI.Residues 14-284 are 48% similar to a (ORYZA SIMILAR 36I5.3 RICE. SATIVA ATP-BINDING) protein domain (PD808911) which is seen in Q86IX1_DICDI.Residues 14-287 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING PROBABLE SERINE-THREONINE) protein domain (PD736072) which is seen in Q8G6Q0_BIFLO.Residues 14-295 are 48% similar to a (KINASE PKN9 SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD268676) which is seen in Q9XBP3_MYXXA.Residues 14-282 are 56% similar to a (KINASE ATP-BINDING TRANSFERASE SERINE/THREONINE-PROTEIN RECEPTOR PHOSPHORYLATION SERINE/THREONINE TYROSINE-PROTEIN REPEAT CELL) protein domain (PD000001) which is seen in Q81ZW6_STRAW.Residues 14-291 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA19096) which is seen in Q7UJC1_RHOBA.Residues 14-316 are 45% similar to a (SERINE/THREONINE-PROTEIN KINASE PKN3 TRANSFERASE ATP-BINDING) protein domain (PD316927) which is seen in PKN3_MYXXA.Residues 14-311 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA0K9H0) which is seen in Q7NMV0_GLOVI.Residues 14-278 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA0H1H6) which is seen in Q7UJD9_RHOBA.Residues 15-302 are 41% similar to a (KINASE RECEPTOR TRANSFERASE TYROSINE-PROTEIN ATP-BINDING TYROSINE) protein domain (PD566768) which is seen in Q8WSM2_SCHMA.Residues 15-237 are 44% similar to a (KINASE DJFGFR1 TRANSFERASE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD611563) which is seen in Q8MY86_DUGJA.Residues 15-288 are 46% similar to a (KINASE TRANSFERASE TYROSINE-PROTEIN ATP-BINDING F11E6.8) protein domain (PD247428) which is seen in Q9XVQ7_CAEEL.Residues 15-236 are 42% similar to a (SERINE/THREONINE-PROTEIN KINASE MEK1 MEIOSIS TRANSFERASE ATP-BINDING MEIOSIS-SPECIFIC) protein domain (PDA0I4P9) which is seen in MEK1_SCHPO.Residues 15-289 are 45% similar to a (KINASE FOCAL TRANSFERASE ADHESION TYROSINE-PROTEIN ATP-BINDING) protein domain (PD996867) which is seen in Q7Z1D3_LYTVA.Residues 17-292 are 42% similar to a (T20L15_160 AT5G01890/T20L15_160 ATP-BINDING) protein domain (PD280913) which is seen in Q9LZV7_ARATH.Residues 17-244 are 46% similar to a (KINASE DIVISION CELL SERINE/THREONINE-PROTEIN TRANSFERASE RELATED ATP-BINDING CYCLE 2-RELATED) protein domain (PD849176) which is seen in Q86ZH1_NEUCR.Residues 18-275 are 40% similar to a (KINASE SERINE/THREONINE-PROTEIN REPEAT TRANSFERASE TPR 2.7.1.- ATP-BINDING) protein domain (PDA0F980) which is seen in Q7URL4_RHOBA.Residues 18-291 are 43% similar to a (KINASE TRANSFERASE ATP-BINDING) protein domain (PD325465) which is seen in Q9LRY7_ARATH.Residues 19-237 are 47% similar to a (KINASE STRESS-RESPONSIVE PRKSD ATP-BINDING) protein domain (PD087289) which is seen in O62571_SUBDO.Residues 19-284 are 45% similar to a (KINASE 1-LIKE RESPONSIVE ATP-BINDING STRESS) protein domain (PD099489) which is seen in O61125_DICDI.Residues 19-237 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING MAP) protein domain (PD290024) which is seen in Q9P8J0_PNECA.Residues 19-239 are 44% similar to a (KINASE R11E3.1 TRANSFERASE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD278557) which is seen in Q9TYX4_CAEEL.Residues 19-286 are 44% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE APOPTOSIS HIPPO ATP-BINDING) protein domain (PD727337) which is seen in HPO_DROME.Residues 19-307 are 38% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING PPKA) protein domain (PDA1D587) which is seen in Q7UMX3_RHOBA.Residues 19-238 are 45% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE ATP-BINDING SHK2) protein domain (PD078766) which is seen in SHK2_SCHPO.Residues 20-284 are 44% similar to a (KINASE LIKE NEUROSPORA RELATED STE20- B16M17.090 Q871H9 DON3 CRASSA) protein domain (PDA064R7) which is seen in Q6C8H9_EEEEE.Residues 20-144 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA18944) which is seen in Q7UPN1_RHOBA.Residues 20-305 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN ACR142WP TRANSFERASE ATP-BINDING) protein domain (PDA0A7Q6) which is seen in Q75CE9_ASHGO.Residues 20-277 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD500022) which is seen in Q8YMH9_ANASP.Residues 20-236 are 43% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN ANK ATP-BINDING TRANSFERASE GLP_39_28978_30531) protein domain (PD959207) which is seen in Q7R3P5_EEEEE.Residues 20-282 are 45% similar to a (P0418B08.10 OJ1740_D06.39) protein domain (PDA10665) which is seen in Q69P46_EEEEE.Residues 20-240 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D464) which is seen in Q7UW31_RHOBA.Residues 20-237 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PDA0G6B9) which is seen in Q6MAN0_PARUW.Residues 20-286 are 43% similar to a (KINASE GLA-LIKE TRANSFERASE TYROSINE-PROTEIN) protein domain (PD627181) which is seen in Q8T6I3_HALRO.Residues 20-283 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA08789) which is seen in Q7UL45_RHOBA.Residues 20-316 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN PKN10 TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA043E6) which is seen in Q7UGA2_RHOBA.Residues 20-314 are 40% similar to a (KINASE SERINE/THREONINE-PROTEIN GLP_28_16955_18661 TRANSFERASE ATP-BINDING) protein domain (PDA08641) which is seen in Q7R1Q1_EEEEE.Residues 20-299 are 41% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE BRASSINOSTEROID ATP-BINDING INSENSITIVE) protein domain (PD595107) which is seen in Q84ZJ8_EEEEE.Residues 20-313 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA1D4Q5) which is seen in Q7ULK7_RHOBA.Residues 20-291 are 45% similar to a (KINASE TRANSFERASE TYROSINE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD289861) which is seen in Q9Y1Y3_EEEEE.Residues 20-282 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING MAP) protein domain (PDA18314) which is seen in Q93WR7_MEDVA.Residues 20-292 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE TRANSCRIPTION ATP-BINDING DNA-BINDING SERINE-THREONINE REGULATION) protein domain (PDA1B2W7) which is seen in Q6PV87_BBBBB.Residues 23-278 are 45% similar to a (PKND) protein domain (PDA18730) which is seen in Q73UI1_MYCPA.Residues 29-275 are 45% similar to a () protein domain (PD454795) which is seen in Q9AQ02_BBBBB.Residues 40-240 are 44% similar to a (KINASE CAMP-DEPENDENT SERINE/THREONINE-PROTEIN CATALYTIC TRANSFERASE ATP-BINDING SUBUNIT) protein domain (PD750451) which is seen in Q9BMY6_TOXGO.Residues 48-284 are 45% similar to a (KINASE CBS138 CANDIDA SEQUENCE K SERINE/THREONINE-PROTEIN GLABRATA STRAIN ATP-BINDING TRANSFERASE) protein domain (PD957660) which is seen in Q6FMF3_EEEEE.Residues 52-284 are 45% similar to a (SERINE/THREONINE-PROTEIN KINASE YKL101W PROBABLE ATP-BINDING TRANSFERASE) protein domain (PD095148) which is seen in KKK1_YEAST.Residues 56-250 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING KINASE-LIKE) protein domain (PDA198D0) which is seen in Q8S1B9_EEEEE.Residues 62-155 are 51% similar to a (AGCP11047 KINASE TRANSFERASE ATP-BINDING) protein domain (PDA19076) which is seen in Q7Q3B5_EEEEE.Residues 78-299 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE F24O1.13 ATP-BINDING) protein domain (PD235013) which is seen in Q9MAV2_ARATH.Residues 87-310 are 41% similar to a () protein domain (PD743406) which is seen in Q8G5T5_BIFLO.Residues 92-237 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING PENTATRICOPEPTIDE REPEAT-CONTAINING PPR) protein domain (PDA18435) which is seen in Q7XB71_EEEEE.Residues 110-243 are 44% similar to a (YARROWIA LIPOLYTICA STRAIN C CLIB99 CHROMOSOME) protein domain (PD950595) which is seen in Q6CAU2_EEEEE.Residues 112-281 are 42% similar to a (KINASE TYROSINE-PROTEIN TRANSFERASE C03B1.5 ATP-BINDING X CHROMOSOME) protein domain (PD092556) which is seen in YX05_CAEEL.","","-47% similar to PDB:1MRU Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB. (E_value = 1.2E_32);-48% similar to PDB:1O6Y CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.4E_31);-48% similar to PDB:2FUM Catalytic domain of protein kinase PknB from Mycobacterium tuberculosis in complex with mitoxantrone (E_value = 1.4E_31);-45% similar to PDB:2H34 Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE (E_value = 3.8E_26);-47% similar to PDB:2H6D Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain) (E_value = 4.4E_22);","Residues 14 to 288 (E_value = 1.3e-50) place ANA_0321 in the Pkinase family which is described as Protein kinase domain.Residues 14 to 138 (E_value = 2.1e-09) place ANA_0321 in the Pkinase_Tyr family which is described as Protein tyrosine kinase.Residues 204 to 288 (E_value = 1.7e-05) place ANA_0321 in the Pkinase_Tyr family which is described as Protein tyrosine kinase.","","protein kinase pkaA (fragment)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0322","342593","339993","2601","9.06","13.45","91487","GTGGGGCGCTCACCGGACAGCGACGTTCAGATCGTCCACCCCTTGGTCTCCCGCACCCATCTCCAGGTGACCCCCACCCCAACGGGATGGGCAGTGAGGTGCCAGGGACGTAACGGCATGCTCGTCAACGGGACCGTGACGCGCGAGGCACTCGTGACTCAGGGCACTCGCATCCAGCTGGGCGACGCCTCCGGGCCGGCGCTGGGGCTCACTCCGATCGTCTCCGGCAGCGCGGCCCAGACCGGCGCCCCCATCCAGTCCCAGCCGATGGGACAGCCCGCTCCGTCTGCGTCAAGCGCCCCCTTCATCCCGTCACAGCCGAGTGCGGCCTCCGCGCCCCAAGCCGCTCCCCTCCAGCGTCCAGTCAGCCCGGCCCCAGCCCTCTCGGCGCAGTCCGCGCCCGTGCCCCAGGCCATGGCATCGGCATCCTCAGCTGCCACCTACGTGGCACCCCCGGGCCGCCCGGCGCCGCCCTCATCGAGCTCAGCGAGCTCGGGAGCCTTCCCCACCTCGAGGCACACGGTCACGTCCTTCCGTGTCACCTCCTCAGGCACCATCGGGCGCGCGCCCGACAACACCCTGGTCCTGGATGACCCGCTCATCTCCAAGCACCACGCCCGTATCGACGTCTCCTCCAGCGGAATGGTCGTCACCGACCTGGGATCCACCAACGGCCTGTATGTCGCCGGGCAGCGCGTGTCACAGGTCCAGGTCACCCAGCCCGTGCTCATCGGTCTGGGATCGACCTTCATCGCCCTGAGCCCGGATGGTCTGTGCGAGGTCCAGGTCGCGGGCGGAGCCGGCGGAGAGCTGGTGGGCAAGGACCTGACCTTCCGCGTCAACAACGGCAGCATGACGCTGCTCGACGGCATCTCCTTCTCCCTGCCTGGCAACGAGCTGCTGGCCGTCGTCGGCCCGTCGGGAGCAGGGAAGTCGACGCTGCTCAAGGCCCTCACCGGTGAGCAGAAGGCCCAGGAGGGCCAGGTTCTCTTCAACGGGCTGGACGTGTACGAGCACTACCCGGTCATGCGCAACAAGATCGGCGTGGTCCCCCAGAGCGACGTCATTCACTCGGCCCTCACTGTCCGCAAGACCCTTGAGTACGCCGCTGAGCTGCGTTTCGCCAAGGACGTGTCCAAGGCCGAGCGGCGCCGGCGCATCGCCGAGGTACTGGAGGATCTTGACCTGACCGCGCATGTGGACAAGCGGGTCAAGAAGCTCTCCGGAGGACAGCGCAAGCGGGTCTCCACCGCCATCGAGCTGCTAACACGCCCCAGCCTCCTGTTCCTCGACGAGCCCACCTCCGGCCTGGACCCCCAGCTGGACCGAGACGTCATGGACCTGTTGGCGTCCCTGGCTCACGGCACCCGTCCTGGTGACACCGGCCGCACGGTCGTCGTCGTCACCCACAATGAGAACCACATTGACCGTGCGGACAAAGTCCTCATCCTGGCGGCGGGCGGCAAGCCGGTCTACTACGGCTCCCCCCGAGAGGTGCTCCCCTACTTCCGCCAGAGGCTCAACGAGATCGCCTCTCAGGGCCGCCTGCTGCTCAACACGCCGAAAGGCACCCTCCCCGACCCGCCCGCCGTGGACGGCTACGCCGATGTCTACGCCCTCATCCGTAACCACACCGCGGAGCTGCGTCAGTACATGGAGGCCACGGTGCCCTCGACGCGGCGCGGAGGGGCTCCCGCAGCGGCTGCGGGACCGGCGACGCAGGAGAAGCCGCCCAAGCAGCAGTCCGTGCTCAGGCAGGTCTCGACCCTCGTACGGCGCCAGCTGAGGATCGTGGCGGCGGACCCGTCCTACCTCGCCTTCATGCTGTTGCTGCCCATCATCATGGGACTGCTGACCAAGGCGATCGAGGGCAGCGACGGCTTCGCGGTCCCCCACTACCCGGAGCCCACTGCCCCGACGCCGGAGAACCCCACTCCCCCGATCATCAAGTACTCCAGCCAGGCACTGCAGCTGTTGGTCATTCTCATCACCGGGGCGGCGTTCTCCGGGATGTCGGCGACCATTCGTGACCTCATCGGGGAGCGGGACGTCTTCCTGCGGGAGAAGGCCGTCGGTCTGAGATCCGGGGCCTACCTGTTCTCCAAGGCGACCATTCTGGCGCTCATCACCACTATCCAGACCGCGCTGATGATGGGCATCGCCCTGGCCCTCAACAAGGGTCCCTCAGATGCCGTCATCCTGGAGGGGTGGCCGGGTCTGGAGCTGGCCTTCTGCTGCTGGGCCGTCGCCTTCGTCTCCGGGCTCCTGGGGCTGGCGGTCTCCGCGATGGTCTCCTCCTCCGAGCAGGTCATGCCGGTCCTGGTGGTCTCCATCATGGCCCAGCTGGTCCTGTCCGGCGGCATCATTCCGATCGCGGGGCGGGCGGTCTTCGAGCAGCTCGCCTGGTTCATGCCATCGCGGTGGGGTTACGCGATGGCCTCCTCCACCCTGGAGATGCTCGCCATCCTGCCCAACCGCCACGACGCACTGTGGAAGCACGAGACCGCGCAGTGGCTGACGGACTACGGCCTACTCTCAGCCATCGGCTTGGCCTGCATGGTGATGTGCTACGTCGCCCTGGCCCGTCGCGGGCGTCGCTGA","VGRSPDSDVQIVHPLVSRTHLQVTPTPTGWAVRCQGRNGMLVNGTVTREALVTQGTRIQLGDASGPALGLTPIVSGSAAQTGAPIQSQPMGQPAPSASSAPFIPSQPSAASAPQAAPLQRPVSPAPALSAQSAPVPQAMASASSAATYVAPPGRPAPPSSSSASSGAFPTSRHTVTSFRVTSSGTIGRAPDNTLVLDDPLISKHHARIDVSSSGMVVTDLGSTNGLYVAGQRVSQVQVTQPVLIGLGSTFIALSPDGLCEVQVAGGAGGELVGKDLTFRVNNGSMTLLDGISFSLPGNELLAVVGPSGAGKSTLLKALTGEQKAQEGQVLFNGLDVYEHYPVMRNKIGVVPQSDVIHSALTVRKTLEYAAELRFAKDVSKAERRRRIAEVLEDLDLTAHVDKRVKKLSGGQRKRVSTAIELLTRPSLLFLDEPTSGLDPQLDRDVMDLLASLAHGTRPGDTGRTVVVVTHNENHIDRADKVLILAAGGKPVYYGSPREVLPYFRQRLNEIASQGRLLLNTPKGTLPDPPAVDGYADVYALIRNHTAELRQYMEATVPSTRRGGAPAAAAGPATQEKPPKQQSVLRQVSTLVRRQLRIVAADPSYLAFMLLLPIIMGLLTKAIEGSDGFAVPHYPEPTAPTPENPTPPIIKYSSQALQLLVILITGAAFSGMSATIRDLIGERDVFLREKAVGLRSGAYLFSKATILALITTIQTALMMGIALALNKGPSDAVILEGWPGLELAFCCWAVAFVSGLLGLAVSAMVSSSEQVMPVLVVSIMAQLVLSGGIIPIAGRAVFEQLAWFMPSRWGYAMASSTLEMLAILPNRHDALWKHETAQWLTDYGLLSAIGLACMVMCYVALARRGRR$","ABC-type multidrug transport system, ATPase component","Periplasm, Membrane, Extracellular","ABC transporter, ATP-binding protein","ABC transporter; ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[1-61]T$ $\"[184-245]T$	FHA
SM00240	$\"[1-47]T$ $\"[183-233]T$	FHA
PS50006	$\"[1-47]T$ $\"[184-233]T$	FHA_DOMAIN

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[407-449]T$	Q9AJX1_STRCO_Q9AJX1;
PF00005	$\"[298-487]T$	ABC_tran
PS50893	$\"[271-512]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[297-497]T$	AAA

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[585-818]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.20	$\"[1-62]T$ $\"[182-253]T$	no description
G3DSA:3.40.50.300	$\"[276-500]T$	no description
PTHR19241	$\"[186-533]T$ $\"[563-839]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19241:SF6	$\"[186-533]T$ $\"[563-839]T$	ABC TRANSPORTER
tmhmm	$\"[598-618]?$ $\"[704-724]?$ $\"[743-763]?$ $\"[773-793]?$ $\"[841-861]?$	transmembrane_regions

","BeTs to 9 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 6.2e-36. IPB005074C 287-334 IPB005074D 395-438 IPB005074E 464-484***** IPB010929 (CDR ABC transporter) with a combined E-value of 7.5e-24. IPB010929K 285-329 IPB010929L 334-386 IPB010929M 404-450 IPB010929A 297-316 IPB010929B 341-387 IPB010929C 389-422***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 6.5e-20. IPB013563A 287-321 IPB013563C 404-431***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.2e-13. IPB010509B 298-323 IPB010509D 402-446***** IPB005116 (TOBE domain) with a combined E-value of 5.3e-10. IPB005116A 305-321 IPB005116C 407-420 IPB005116D 427-446","Residues 185-249 are 67% similar to a (ATP-BINDING KINASE DOMAIN FHA TRANSCRIPTION ABC ZINC-FINGER NUCLEAR TRANSPORTER TRANSFERASE) protein domain (PD001303) which is seen in Q8DJ88_SYNEL.Residues 271-499 are 48% similar to a (ATP-BINDING SYSTEM ABC A1A2) protein domain (PD459661) which is seen in Q97BE5_THEVO.Residues 274-347 are 60% similar to a (ATP-DEPENDENT PROBABLE YFL028C ATP-BINDING TRANSPORTER) protein domain (PD951805) which is seen in YFC8_YEAST.Residues 274-405 are 54% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18601) which is seen in Q73JC4_TREDE.Residues 274-484 are 48% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 275-466 are 51% similar to a (ATP-BINDING AFR326WP) protein domain (PDA187V1) which is seen in Q753I6_ASHGO.Residues 276-503 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD738128) which is seen in Q8G833_BIFLO.Residues 278-419 are 52% similar to a (DPP1 ATP OLIGOPEPTIDE ATP-BINDING ABC TRANSPORTER BINDING) protein domain (PD955106) which is seen in Q6L102_PICTO.Residues 278-459 are 52% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 278-492 are 44% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 278-438 are 52% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD738131) which is seen in Q830L1_ENTFA.Residues 279-478 are 45% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 280-487 are 44% similar to a (ATP-BINDING ABC PROTEIN TRANSPORTER) protein domain (PD995669) which is seen in Q73R06_TREDE.Residues 280-443 are 52% similar to a (ATP-BINDING/PERMEASE ABC TOXIN TRANSPORTER ATP-BINDING PLASMID) protein domain (PD416779) which is seen in Q82YJ4_ENTFA.Residues 281-476 are 46% similar to a (ATP-BINDING ABC PRECURSOR TRANSPORTER SIGNAL) protein domain (PDA0X2Z3) which is seen in Q6MM73_BDEBA.Residues 283-496 are 50% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 284-363 are 58% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I309) which is seen in Q9AM85_RIEAN.Residues 285-440 are 46% similar to a (ATP-BINDING OPPD OLIGOPEPTIDE) protein domain (PDA11396) which is seen in Q7P513_BBBBB.Residues 286-428 are 52% similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 286-487 are 46% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 287-439 are 50% similar to a (C56E6.5) protein domain (PD145750) which is seen in Q18900_CAEEL.Residues 287-502 are 46% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 287-477 are 46% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 287-396 are 52% similar to a (GH24286P ATP-BINDING CG9663-PA) protein domain (PD305172) which is seen in Q8MRL3_DROME.Residues 288-392 are 58% similar to a (ABC ATP TRANSPORTER ATP-BINDING BINDING) protein domain (PDA0J3R3) which is seen in Q97VF4_SULSO.Residues 288-338 are 78% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9AJX1_STRCO.Residues 290-468 are 43% similar to a (ATP-BINDING) protein domain (PD845659) which is seen in Q82AF2_STRAW.Residues 291-506 are 47% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 294-471 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 298-452 are 49% similar to a (ATP-BINDING CG1494-PA) protein domain (PD310846) which is seen in Q9VRG3_DROME.Residues 354-401 are 70% similar to a (ATP-BINDING TRANSPORTER ABC TRANSMEMBRANE RESISTANCE CASSETTE GLYCOPROTEIN MULTIDRUG CANDIDA MEMBER) protein domain (PD000665) which is seen in Q740L9_MYCPA.Residues 383-487 are 62% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 384-452 are 60% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 386-452 are 69% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 387-491 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 401-500 are 53% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 406-470 are 63% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 407-449 are 93% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9AJX1_STRCO.Residues 474-632 are 42% similar to a (ATP-BINDING ABC TRANSPORTER TRANSMEMBRANE PROBABLE TRANSPORTER PLASMID) protein domain (PD041849) which is seen in Q7TZN0_MYCBO.Residues 656-766 are 53% similar to a (ATP-BINDING) protein domain (PDA0V9L3) which is seen in Q73Y57_MYCPA.Residues 658-768 are 53% similar to a (ABC PERMEASE TRANSPORTER MEMBRANE ATP-BINDING TRANSPORTER TRANSMEMBRANE PROTEIN COMPONENT INTEGRAL) protein domain (PD115342) which is seen in Q73UA2_MYCPA.Residues 769-838 are 68% similar to a (ATP-BINDING ABC TRANSPORTER TRANSMEMBRANE PROBABLE TRANSPORTER) protein domain (PDA004P0) which is seen in Q740L9_MYCPA.","","-50% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 8.3E_24);-52% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 2.7E_22);-52% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 2.7E_22);-52% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 2.7E_22);-52% similar to PDB:2AWN Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg) (E_value = 2.7E_22);","Residues 1 to 61 (E_value = 2.8e-07) place ANA_0322 in the FHA family which is described as FHA domain.Residues 184 to 245 (E_value = 1.1e-09) place ANA_0322 in the FHA family which is described as FHA domain.Residues 298 to 487 (E_value = 5.3e-57) place ANA_0322 in the ABC_tran family which is described as ABC transporter.Residues 585 to 818 (E_value = 4.6e-16) place ANA_0322 in the ABC2_membrane family which is described as ABC-2 type transporter.","","transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0323","344791","343160","1632","8.31","5.53","59455","ATGTATGACGTCACCCTCGACACCCTCGACCAGATCGCCGCGACCTGCCTCGCGCTCGGCGTCGATCGCCACTGCCTGTCATCCGCAGAGCTGGCCGTGCTTCCCACTCAGCCCGTCGAGCCTCTCGACCTTTCGCAGATACGCAGGCTCATCCTCGACGGCGAGGATCCTCTTGGCCAGGCATTCTGCACTGCGCGCACCGCCGAGGAGCGTCGACCACGCGGGCAGACATTCACTCCCGCCCCCATTGTTCGTTCCATGTTGGAGTGGACGAAAGGACGCGTGACCCCGGCCCGCGTGGTTGATCCCGGCTGCGGTTCCGGTCGATACATTCTGGCTGCCCTACGCGCCTTCCCACACGCGGTCGGGCTCGCATCCGACCTTGACCCTTACGCCACCCTCATGACTCGCGCCAACGCTCGTGTCCTGGGACTCGAATCGCGTCTCAAGGTCATCGTCGGCGACTATCGTGCGCTCAGACTGCCCAAGATCGAGGGGGTCACGCTCTTCCTTGGGAACCCACCGTATGTCCGACACCATAACATTGATGCTCGTTGGAAGACCTGGCTCGGTGCGACGGCCTCACAGATGGGCATGAAGGCGAGCAAGCTCTCCGGTCTGCACGCCCACTTCTTCCTGGCGACCGCACTCTACGCTCAGGCCGGAGACATCGGCTCCTTCATCACCAGCTCGGAATGGCTCGACGTCAACTACGGTCAGCTCATTCGCGAGCTCCTCATCGGCCCTCTCTCCGTGTCGAGCCTCCACATCCTGAGCCCGACGAGTCTGCCGTTCGGTGACGCCACCGTTACCGGTGCCATTACCTGCTTCGAGGTCGGCGCAAACGCCCCTGAGGTGCAGATCCAGACCGTCGATAGTGTTGACGCGCTCGGTGATCTCTCCACCGGATTCCCCGTCTCGCGTCAGCGCCTCGCCGAGACATCCCGCTGGTCAGTCATCACCCGAGTGACTCCGAGGCTCCCCGACGGCTACGTTGAGCTTGGAGAGCTCGCACGCGTCCACCGAGGCACCGTCACAGGAGCGAACAAGATATGGGTCACTCCTCGCGACGCCGTTGACCTTCCTGACGATCTTCTCTTCCCGGCGATCACCCGCGCACGCGAGCTCTTCGCCGCGGGTGAGCGCTTGTCAACCTCCGATGACCTCAAGGCAGTCATCGACCTTCCTACCGATCTGGACATCCTCGACGAACCCGACAGGAAGAGAGTCGATCGCTTCCTGCGCAAAGCGAAGCGGCTCGGTGTCGCCAACGGCTACGTGGCTCGCAATCGACGCGCATGGTGGAGCATCGGCCTGTCCTCTCCGGCACCCATCCTGACGACCTACATGGCGCGGCGGCCTCCCGCGTTCGTGAGGAACGCGGTCGATGCCCGTCACATCAACATCGCTCACGGAATCTACCCGAGGGAAACCATGAGCGACTCGGATCTCGACGCCCTCGCCGCGTACCTGCGTGTCAACGTGTCGACGACTAGCGGTCGCACCTATGCTGGAGGTTTGACAAAGTTCGAGCCACGAGAAATGGAGCGTCTGGTGGTTCCAGACCTCCCATTGCTCCGCGACAAGGGCCGTCATGACTCACGTAGCGCCGCCGAGATAGTCGGAGTCTGA","MYDVTLDTLDQIAATCLALGVDRHCLSSAELAVLPTQPVEPLDLSQIRRLILDGEDPLGQAFCTARTAEERRPRGQTFTPAPIVRSMLEWTKGRVTPARVVDPGCGSGRYILAALRAFPHAVGLASDLDPYATLMTRANARVLGLESRLKVIVGDYRALRLPKIEGVTLFLGNPPYVRHHNIDARWKTWLGATASQMGMKASKLSGLHAHFFLATALYAQAGDIGSFITSSEWLDVNYGQLIRELLIGPLSVSSLHILSPTSLPFGDATVTGAITCFEVGANAPEVQIQTVDSVDALGDLSTGFPVSRQRLAETSRWSVITRVTPRLPDGYVELGELARVHRGTVTGANKIWVTPRDAVDLPDDLLFPAITRARELFAAGERLSTSDDLKAVIDLPTDLDILDEPDRKRVDRFLRKAKRLGVANGYVARNRRAWWSIGLSSPAPILTTYMARRPPAFVRNAVDARHINIAHGIYPRETMSDSDLDALAAYLRVNVSTTSGRTYAGGLTKFEPREMERLVVPDLPLLRDKGRHDSRSAAEIVGV$","Adenine-specific DNA methylase","Cytoplasm","XamI DNA methyltransferase","hypothetical protein","hypothetical protein","","Cheng X. Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 1995. 24:293-318. PMID: 7663118Loenen W.A., Daniel A.S., Braymer H.D., Murray N.E. Organization and sequence of the hsd genes of Escherichia coli K-12. J. Mol. Biol. 1987. 198(2):159-170. PMID: 3323532Narva K.E., Van Etten J.L., Slatko B.E., Benner J.S. The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases. Gene 1988. 74(1):253-259. PMID: 3248728Lauster R. Evolution of type II DNA methyltransferases. A gene duplication model. J. Mol. Biol. 1989. 206(2):313-321. PMID: 2541254Timinskas A., Butkus V., Janulaitis A. Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases. Gene 1995. 157(1):3-11. PMID: 7607512Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E., Schildkraut I., Saenger W. Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(23):10957-10961. PMID: 7971991","","","

InterPro
IPR002296
Family

N6 adenine-specific DNA methyltransferase, N12 class
PR00507	$\"[75-91]T$ $\"[100-114]T$ $\"[167-179]T$	N12N6MTFRASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[77-312]T$	no description
PIRSF000403	$\"[46-542]T$	Modification methylase (adenine-specific), M.HincII type
PTHR18895	$\"[78-186]T$	METHYLTRANSFERASE

","BeTs to 3 clades of COG0827COG name: Adenine-specific DNA methylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0827 is --m-k-----rlb----h--uj---wNumber of proteins in this genome belonging to this COG is 1","***** IPB002296 (N12 class N6 adenine-specific DNA methyltransferase signature) with a combined E-value of 8.4e-11. IPB002296A 75-91 IPB002296B 100-114 IPB002296C 167-179","Residues 27-177 are 46% similar to a (METHYLTRANSFERASE TRANSFERASE HEMK 2.1.1.- METHYLASE PROTOPORPHYRINOGEN OXIDASE RIBOSOMAL L11 ADENINE-SPECIFIC) protein domain (PD001640) which is seen in Q7WCE2_BORPA.Residues 58-277 are similar to a (METHYLTRANSFERASE XAMI TRANSFERASE RESTRICTION SYSTEM ADENINE-SPECIFIC MODIFICATION METHYLASE SALI DNA) protein domain (PD113380) which is seen in Q8PJU4_XANAC.Residues 334-523 are similar to a (METHYLTRANSFERASE TRANSFERASE METHYLASE MODIFICATION ADENINE-SPECIFIC RESTRICTION SYSTEM DNA XAMI PROBABLE) protein domain (PD134887) which is seen in MTX1_XANCR.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","DNA methyltransferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0326","345821","347422","1602","5.21","-13.55","55885","ATGCCCGCTCCTGTCCCCTCGCGCCACTCTCAGGATGACGCGCCCGTCTCCTCCCTGAGTCGCGCTCAGCTCCTCGATGTCCTGTCCGACCTGGTCCGGGACCTCGAGCGCCTCGACCTGGCCCTGAGTGCCGACGGCGTCGAGGCTGCGCGCACATTGCGCGACGGTCTCATCGGACAGGTCCGTGACCAGGTTGTTCCCCGCCTGCAGGATGCCGATATCCCGTCCATCGTGGTGATCGGGGGGTCCACGGGTGCGGGGAAGTCCACGCTCGTCAACTCCGTGCTCGGCCAGGAGGTCTCCGTTGCCGGAGTGCTCAGGCCCACCACACGAACCCCGGTTCTGGTGGCCAATCCGGAGGACGTGGACTCACTGTCCGAGCACCCTCTGACCCAGGTGTGTCGGCAGGAGGTCTCCGCTGCCATTCCGGCTGGCCTGGCCCTGATCGATGCCTCGGACCTGGACTCCGTGCACGAGGCCAACCGGGCTCTGGCTGGAAGGCTGCTGGAGGCGGCCGACCTGTGGCTGTTCGTCACCACCGCGGCGCGTTACGGCGATCAGACGCCGTGGACGACGCTGGAGGAGGCCGCGCGCCGTGAGACTCCCATCGGTGTGGTTCTCAACCGGGTGCCGGCGAGGATTCTGCCCGAGGTGCGTCGGGATCTCATCACCCGCCTGCAGGGGCTGGGACTGTCGGAGGCGCCCTTCTTCGTCGTGCCGGACGCCGGGCCGCACGAGGGGCTCCTATCGGGTGACGGCGTCAGCGAGCTGCGCGACTGGCTGCAGCTCCTGGCTGGGCGTCACCGCGCAGCCGGTCTCGTGCGTCGTACCGGCAGAGGGGTGTGGAGCACTCTGCGCGCCGACCTGGAGCGCCTGGCCGACGACGTCGACGCCCAGAACGCGGTGGCCGAGGAGCTGGAGAGAACCTGCCAGGAGCTGAGGGAGACCGCCATTGAGGCGTTGAGCGCCGACATCAGGGCTGGTTCAGCGGGCCAGGGCGCCACTGCCACCAGATGGATCACTCTGGCCTCCTCCGGAGGTCCGCTCGCCTCGCTGGCCCAGGGGGGCAAGTTGCGCAGGGGATTCCTGGGACGGGCGGACAAGGCTCGCGCCGAGGGGCTTTCCCAGCTGGCCAACGATGCCCGCCAGGCCCTGGCCAACCAGCTTCAGGCAGCCATCGTTGCCTTGAGCGCCGAGGCTCGCAGGGCCTGGGCCGAGGTGGGGGCCGAGGAGCGCGCGCACAAGATTCTGGGGCAGGGTGACGACGCGGTCGCGACCATTGAGGCCTGGGTCGGCTACCTGGAGGCCAATATCGAGAGTCCGCAGGATATCCGTAGACTGAGCCCTGGCAGTGTCATCGACCTTCTCATCTCCGCTGCAGCCGGTGTCGACGGGGCCGTGTCGGCCGCCAGACGCCTGGGACTGGAGGAGCAGACCGCTCAGGCCGGTGCCCTTCTGGTGGAAGCGGTCACCGAGGCGCTGACTGCCACAGTCCCCAAGGGGGCGGCCACCTCGCTCGCCCCCGCCCCTGGGTTCGCCGCTGCGCTGCGTCTGCGCTCGGGCGAGCTCAAGCCCTTCACCCGTCCCGGAGCCACAGCATGA","MPAPVPSRHSQDDAPVSSLSRAQLLDVLSDLVRDLERLDLALSADGVEAARTLRDGLIGQVRDQVVPRLQDADIPSIVVIGGSTGAGKSTLVNSVLGQEVSVAGVLRPTTRTPVLVANPEDVDSLSEHPLTQVCRQEVSAAIPAGLALIDASDLDSVHEANRALAGRLLEAADLWLFVTTAARYGDQTPWTTLEEAARRETPIGVVLNRVPARILPEVRRDLITRLQGLGLSEAPFFVVPDAGPHEGLLSGDGVSELRDWLQLLAGRHRAAGLVRRTGRGVWSTLRADLERLADDVDAQNAVAEELERTCQELRETAIEALSADIRAGSAGQGATATRWITLASSGGPLASLAQGGKLRRGFLGRADKARAEGLSQLANDARQALANQLQAAIVALSAEARRAWAEVGAEERAHKILGQGDDAVATIEAWVGYLEANIESPQDIRRLSPGSVIDLLISAAAGVDGAVSAARRLGLEEQTAQAGALLVEAVTEALTATVPKGAATSLAPAPGFAAALRLRSGELKPFTRPGATA$","ABC transporter","Cytoplasm","possible ATP-binding protein","putative ABC transporter","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[77-210]T$	no description

","BeTs to 3 clades of COG2262COG name: GTPasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2262 is -om-kz-qvdrlbcefghsn-j-i--Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 59-334 are 41% similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PD318046) which is seen in Q9KYI8_STRCO.Residues 68-113 are 86% similar to a (TRANSMEMBRANE GTPASE GTP-BINDING MEMBRANE 3.6.5.- COILED COIL HYDROLASE MITOCHONDRION OUTER) protein domain (PD590957) which is seen in Q93HK4_STRAW.Residues 105-339 are 48% similar to a (ATP-BINDING POSSIBLE SCC61A.06C ABC TRANSPORTER) protein domain (PD871710) which is seen in Q9KYI7_STRCO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0327","347473","348921","1449","6.88","-0.65","51754","GTGCTCGACGCCGCGCACCTCGATGCCCGGCTGAACGCGGTTCGAGAAGCCCTGCGCCTGTGCCCCACGGAGGTTCCGGCCTCGCTGTCGATTCCTGCCCACAAGGCGCTCGATGCCGTGGCCCAGCGTCTGGCGCTGGGAGTGGATCACACCGTCGTAGCGCTCTTCGGGGGCACCGGCTCGGGCAAGTCGTCGCTGTTCAACGCCTTGACCCAGCTGAACTTCGCAGATGTCGGCGCGCGTCGCCCCACGACGTCACGGGCCGCCGCCTGCTCCTGGGGCGACGACGCCGGCCCGCTCCTGGACTTCCTCGGGGTCTCCTCGGAACGGCGAATCCGGAGGGACTCGATCCTTGACGGCGAGGACCAGGGCTCCATGTCCGGTCTGGTCCTGCTCGACGTTCCCGACTACGACTCGGTGACGACGGAGCATTCCCTACAGGTGGATCGCCTCGTTCCGCTGGCGGACATCCTCGTGTGGGTGGTCGATCCTCAGAAGTATGCCGACGCGGCTCTGCACGACGGCTACCTGCGCGGACTGGGTGCTCGTCAGGAGGACATGCTCGTCCTGGTCAACCAGGTGGATACCCTCCCGGAGAGCGGCTTGGCGAGTCTGCTCGACGACGTCGGGTCTCTTCTCAAGGACGACGGGCTCAGCCAGGTTCAGGTGCTCCCGGTCTCGGCCGTGCGCGGCGACAACCTTGACGTCGTGCGCAGCATGCTGCGCCAGCGCGTCGCACGGGAGTCCAACGCGGCACGCACGGCCTCGGCCGAGCTCGACGCGATCACCCGTCGTCTGCGTCCCACGGTGGCCCGCGACAAGGTGGAGCTCGATGCCGAGCTCACCGAGGAGACCACTAAGGTGCTGCTGCAGGCTTCCGGCGCCCAGGCGGTGGAGGACTCGGTGAGGGCCGGGCTGTCCAGGGTGCTGCCCAGGGCCCTGGCCCGTCCCGAACCGCCCTCGCGCACGGCAGTGTCCTCGGCCCACTCCACCTGGGTCCACCGCACCTCGCAGGGGCTGCCGCCCACGTGGGCTCGGAGTCTGGAGGCCTCCGTCGCCTCCCCGGAGACCTTGGCGGGGCAGACCGCCGAGGCGGTCGGTTCCGTGGCGCTGCCGGGGCACCGCCAGCCGCTGATCGACCTGCTGTGGTGGGGAGGCCTGCTCATGGTGCTCGGCGGGGTGTCGTGGCTGACCGCCTCCGTGGTGCGAGAGGGGCTCGAGGTCCTGCACCGCAGCATCGAGATCGCCCCGGTCTGCCTCATCGTCGTCGGACTCCTGGCGCTCCTGATCGCCACGGTGCGCCGGCGCAGCAGAGCGCGCCGCGAGGCGCAGCGCTATGGGCAACGGGTGCGTGACCGCCTGGAGTCCGTGGTTGAGCGAGGACTGAGCCGGCCGGCCGCCAAGGTTCTGGACAAGCACCGGGTGCTGCAATCGGCTCTGGGGCTCTAA","VLDAAHLDARLNAVREALRLCPTEVPASLSIPAHKALDAVAQRLALGVDHTVVALFGGTGSGKSSLFNALTQLNFADVGARRPTTSRAAACSWGDDAGPLLDFLGVSSERRIRRDSILDGEDQGSMSGLVLLDVPDYDSVTTEHSLQVDRLVPLADILVWVVDPQKYADAALHDGYLRGLGARQEDMLVLVNQVDTLPESGLASLLDDVGSLLKDDGLSQVQVLPVSAVRGDNLDVVRSMLRQRVARESNAARTASAELDAITRRLRPTVARDKVELDAELTEETTKVLLQASGAQAVEDSVRAGLSRVLPRALARPEPPSRTAVSSAHSTWVHRTSQGLPPTWARSLEASVASPETLAGQTAEAVGSVALPGHRQPLIDLLWWGGLLMVLGGVSWLTASVVREGLEVLHRSIEIAPVCLIVVGLLALLIATVRRRSRARREAQRYGQRVRDRLESVVERGLSRPAAKVLDKHRVLQSALGL$","ABC transporter","Cytoplasm, Membrane","putative ATP-binding membrane protein","putative ABC transporter","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[52-252]T$	no description
tmhmm	$\"[381-403]?$ $\"[409-431]?$	transmembrane_regions

","BeTs to 3 clades of COG1159COG name: Predicted GTPases, Era/HflX familyFunctional Class: RThe phylogenetic pattern of COG1159 is -m-k-QVCEBRhujgpolinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 24-395 are 51% similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PD318046) which is seen in Q9KYI8_STRCO.Residues 146-284 are 47% similar to a (ATP-BINDING POSSIBLE SCC61A.06C ABC TRANSPORTER) protein domain (PD871710) which is seen in Q93HK4_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","ATP-binding membrane protein","","1","","","Fri Aug 10 17:37:40 2007","","Fri Aug 10 17:37:40 2007","","","Fri Aug 10 17:37:40 2007","Fri Aug 10 17:37:40 2007","Fri Aug 10 17:37:40 2007","","","","","","Fri Aug 10 17:37:40 2007","Fri Aug 10 17:37:40 2007","Fri Aug 10 17:37:40 2007","","Fri Aug 10 17:37:40 2007","Fri Aug 10 17:37:40 2007","","","","","yes","","" "ANA_0328","350365","349805","561","4.85","-10.85","20093","ATGAGTGAGACCTCCCTATCGCCCGCGCTGACACGCGCCTTCGAGGATCGCGTCGACCTGGGTTCCTGGGCGGGCTTCACCTCGTCGCTGGCCCGGTTCCTCGACGAGGTGTGCAGGCCGCCCGCGCAGCGGGGAGAATCCGTCGAGGCCGCCATTGACCCCTCCGGCGGTACCCTGCTGCTGACCGCCCCGCTCCCCATGGTCAAGCCCGAGGAGCTGGTTCCCCAGGGGCGCTGGTCGCAGCTGCTGACACGATTGTCCCTGATCACTCCACCCGTTCCTTCCCCAGACCTGCCAGGCGTGGTCCTCGTCGGCCGCTCCGACGGCATCGAAGTCTCACTGCCTGAGCTCGATGCGCAGGGACGGGTGCTGCTGGGCCCCACCGAGCGCAGAATCCTGGGGGCGATCGGCTGGCATGAGAGCCATCACGTCTTCGCCAGGCTGCTGTCCGACGCAGACGAGACCGCCGACCTGGTGACCCGCATCCTCATCGAGGTGCTCGAGGTCGCCCATCCTGCAGACCTCGACTACCTCCTGCGCGCACACTCCGACATCAGCTGA","MSETSLSPALTRAFEDRVDLGSWAGFTSSLARFLDEVCRPPAQRGESVEAAIDPSGGTLLLTAPLPMVKPEELVPQGRWSQLLTRLSLITPPVPSPDLPGVVLVGRSDGIEVSLPELDAQGRVLLGPTERRILGAIGWHESHHVFARLLSDADETADLVTRILIEVLEVAHPADLDYLLRAHSDIS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0329","349090","349812","723","4.78","-13.87","25501","ATGACTCGTCAGCTCGACCTCACCGTTCAGGGCGTCGTCGGAACCAATCCGGTCCTGTCCCGCGTCGGGGATAATGCCCGTCCCTACTGCCGTTTCCGTGTCGCCGTCACTCCGACCTACCGCACTGAGCAGGGCTGGAACAATGCCGAGACGATCTGGTTCACCGCCAAGGCGTGGGGCCAGCTCGCCGCCAATCTGAGCCACTCCCTGCGCAAGGGGGACGCAGTCCTGCTCACCGGACGCTTCTCCCAGGAGTCCTGGGAGAGCAACGGCAGGAAGCACGAGACCAACGTCATCACGCTTCAGGCCGCCGGTCACGACCTGACCAGGGGGGAGTCCCGCTTCGCGCGCGTCAGAGCCGCGGAGTCGGCGCCGTCGGCCTCCTCCGGGGCGGGAACCGGTGATGCCGAGCTCGAGCCCGGTGGCGAGGAGCGCGTCCCGTCGGATCACTGGGAGGTTGAGGTGGCGGCCTCGGGCGTCTCGGCTTCACCGGCCCCGGGGACTGGAGGCCCCCGGGATTTCGCAGAGTCCACCGAGTCCACCGAGCTCAGTGAGTCCACCGAGTCCACCGGGCTTGGTCAGTCCAGCGCGACGCACGCGCAGAGCCCTGAGTCCTTCGTCATCGATCCGGCCTGTGCGCGCACTGAGGATCAGACCGGGGAGCCGTGGCCCGTCTACGAGCTCGCTGATGATCTCGTCGAGCAGGCCGTGGGGGTCAGCTGA","MTRQLDLTVQGVVGTNPVLSRVGDNARPYCRFRVAVTPTYRTEQGWNNAETIWFTAKAWGQLAANLSHSLRKGDAVLLTGRFSQESWESNGRKHETNVITLQAAGHDLTRGESRFARVRAAESAPSASSGAGTGDAELEPGGEERVPSDHWEVEVAASGVSASPAPGTGGPRDFAESTESTELSESTESTGLGQSSATHAQSPESFVIDPACARTEDQTGEPWPVYELADDLVEQAVGVS$","Single-strand binding protein","Periplasm, Cytoplasm","single-strand binding protein subfamily","single-strand binding protein","single-strand binding protein","","Meyer R.R., Laine P.S. The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev. 1990. 54(4):342-380. PMID: 2087220","","","

InterPro
IPR000424
Family

Single-strand binding protein/Primosomal replication protein n
PF00436	$\"[7-107]T$	SSB
PS50935	$\"[1-110]T$	SSB

InterPro
IPR011344
Family

Single-strand binding protein
PTHR10302	$\"[39-88]T$	SINGLE-STRANDED DNA-BINDING PROTEIN, SSB
TIGR00621	$\"[2-212]T$	ssb: single-strand binding protein

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[1-118]T$	no description

","BeTs to 15 clades of COG0629COG name: Single-stranded DNA-binding proteinFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0629 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB011344 (Single-strand binding protein) with a combined E-value of 2.1e-10. IPB011344B 49-101***** IPB000424 (Single-strand binding protein) with a combined E-value of 6e-07. IPB000424B 62-90","Residues 6-110 are 54% similar to a (DNA DNA-BINDING REPLICATION SINGLE-STRAND BINDING HELIX-DESTABILIZING SSB REPAIR SINGLE-STRANDED MB2505C) protein domain (PD372220) which is seen in Q6A791_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 7 to 107 (E_value = 2.4e-08) place ANA_0329 in the SSB family which is described as Single-strand binding protein family.","","binding protein subfamily (ssb)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0330","350581","351270","690","9.69","7.17","25758","ATGATCCGCTTCAACCACGTCTCGAAGGTCTATGACCGGGGGATGCGTCCGGCGCTCGACGACGTCGACATCAAGATCAATCGTGACGAGTTCGTGTTCCTTGTCGGCGCTTCGGGATCGGGCAAGTCGACCTTCTTGAGGCTGGTCATCCGGGAGGAGCGCCCCACCAAGGGACGTATCCACGTGCTGGGCCGCGATCTGTCGAAGATCTCCTCGTGGAAGGTGCCCCAGCTGCGGCAGGAGATCGGCTTCGTCTTCCAGGACTTCCGGCTCCTGGACAACAAGACCGTCCTGGAGAACGTGGCGCTGGCCTCCCAGGTGATCGGTAAGCCGCGCCACTACATCCTCTCCGCTGTGCCCGAGGCCCTCGACCTGGTGGGGCTGGCGGGCAAGGAGAGGCGTCTGCCGCATGAGCTCTCCGGGGGTGAGCAGCAGCGTGTGGCGATCGCCCGTGCCATGGTCAACCGGCCCAAGCTCCTCCTGGCCGATGAGCCCACTGGGAACCTGGACCCCTCGACGTCGGTCGGGATCATGCGTCTGCTTGACCGCATCAACCGGCAGGGGACCACGGTCGTCATGGCGACTCACGACGACGAGATCGTCGACCAGATGCGTAAACGCGTCATCGAGCTCAAGGGCGGCGAGGTCGTGCGCGACCAGGACCGCGGCGTCTACGGCTCGGACCGCTGA","MIRFNHVSKVYDRGMRPALDDVDIKINRDEFVFLVGASGSGKSTFLRLVIREERPTKGRIHVLGRDLSKISSWKVPQLRQEIGFVFQDFRLLDNKTVLENVALASQVIGKPRHYILSAVPEALDLVGLAGKERRLPHELSGGEQQRVAIARAMVNRPKLLLADEPTGNLDPSTSVGIMRLLDRINRQGTTVVMATHDDEIVDQMRKRVIELKGGEVVRDQDRGVYGSDR$","Cell division ATP-binding protein FtsE","Cytoplasm, Membrane","cell division ATP-binding protein","cell division ATP-binding protein FtsE","cell division ATP-binding protein FtsE","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[138-181]T$	Q9L1S6_STRCO_Q9L1S6;
PF00005	$\"[29-214]T$	ABC_tran
PS50893	$\"[2-227]T$	ABC_TRANSPORTER_2
PS00211	$\"[139-153]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[28-215]T$	AAA

InterPro
IPR005286
Family

Cell division ATP-binding protein FtsE
TIGR02673	$\"[1-215]T$	FtsE: cell division ATP-binding protein Fts

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-217]T$	no description
PTHR19222	$\"[2-224]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF36	$\"[2-224]T$	FILAMENTATION TEMPERATURE SENSITIVE CELL DIVISION PROTEIN FTSE

","BeTs to 9 clades of COG2884COG name: Predicted ATPase involved in cell divisionFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG2884 is ---------drlb-efghsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 5e-33. IPB005074C 18-65 IPB005074D 127-170 IPB005074E 190-210***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 6.5e-31. IPB013563A 18-52 IPB013563B 82-95 IPB013563C 136-163***** IPB005116 (TOBE domain) with a combined E-value of 5.5e-25. IPB005116A 36-52 IPB005116B 80-97 IPB005116C 139-152 IPB005116D 159-178***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.5e-16. IPB010509B 29-54 IPB010509D 134-178***** IPB010929 (CDR ABC transporter) with a combined E-value of 3.9e-07. IPB010929K 16-60 IPB010929M 136-182 IPB010929A 28-47","Residues 1-197 are 47% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 2-216 are 48% similar to a (ATP-BINDING ABC PRECURSOR TRANSPORTER SIGNAL) protein domain (PDA0X2Z3) which is seen in Q6MM73_BDEBA.Residues 10-216 are 46% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 14-101 are 60% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD616033) which is seen in Q8PV90_METMA.Residues 16-196 are 46% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 18-216 are 48% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 19-181 are 49% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 19-160 are 47% similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 19-219 are 49% similar to a (ATP-BINDING SYSTEM ABC A1A2) protein domain (PD459661) which is seen in Q97BE5_THEVO.Residues 19-219 are 55% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 19-114 are 63% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I309) which is seen in Q9AM85_RIEAN.Residues 19-69 are 84% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q83HI4_TROW8.Residues 19-200 are 51% similar to a (ATP-BINDING/PERMEASE ABC TOXIN TRANSPORTER ATP-BINDING PLASMID) protein domain (PD416779) which is seen in Q82YJ4_ENTFA.Residues 22-198 are 46% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 23-202 are 49% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 30-197 are 50% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 32-217 are 48% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 59-196 are 49% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 85-124 are 72% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT MEMBRANE ATPASE AMINO ACID SYSTEM) protein domain (PD007166) which is seen in Q6A809_PROAC.Residues 86-217 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 99-216 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K1H6) which is seen in Q73MA6_TREDE.Residues 118-219 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 119-216 are 57% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 123-181 are 74% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD436020) which is seen in Q9A7G4_CAUCR.Residues 124-211 are 61% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 126-196 are 68% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 126-197 are 63% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q7N062_PHOLL.Residues 126-197 are 63% similar to a (ATP-BINDING TRANSPORTER COBALT ABC PROTEIN) protein domain (PD944400) which is seen in Q72D73_DESVH.Residues 126-196 are 70% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.Residues 127-219 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 127-223 are 53% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 127-221 are 53% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 136-217 are 62% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z9) which is seen in Q8DM53_SYNEL.Residues 138-181 are 95% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9L1S6_STRCO.Residues 138-222 are 55% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 139-219 are 60% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD957735) which is seen in Q73JF3_TREDE.Residues 139-212 are 62% similar to a (BLR8070 ATP-BINDING) protein domain (PD727315) which is seen in Q89BS8_BRAJA.Residues 139-217 are 54% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 140-216 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA106Q1) which is seen in Q73R37_TREDE.Residues 141-207 are 66% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.","","-61% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 1.2E_35);-61% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 2.7E_35);-56% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 4.0E_31);-56% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 2.2E_29);-55% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.8E_28);","Residues 29 to 214 (E_value = 2.8e-62) place ANA_0330 in the ABC_tran family which is described as ABC transporter.","","division ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0331","351283","352200","918","9.38","7.12","32971","GTGAGACTGCGTTTCGTCCTGTCGGAGACCGCCAAGGGCATGTACCGGAACCTGGCGATGACGGTGTCCGTGATTCTCGTCGCCTTCGTGTCGCTGCTCTTCGTCGGGGCCTCGTCGCTGCTGCAGAGCCAGATCTCGACCATGAAGGGCGACTGGTACGACAAGGTCGAGGTCTCGGTCTACATGTGCCCCAAGTCGTCGGCCTCCTCCAACTGCGCCAATGGCGAGGCCACCGCCGCTCAGATCAGCGAGGTTGAGAACCTCATCACCAGCGGCGCCCCCTCCGGCTACGTCAAGTCCTACCAGATGGAGACCAAGGCCCAGGCCTACCAGAATTTCATGAAGGCCTATGCCAAGTCCGCCGTCGGGAGGAACGCGACGGAGGACATGATGCCCGTGTCCTTCCGCATCAAGCTCAAGGACGCCGAGAACTACAAGCTGGTGGCCGAGCAGTTCGAGGGGCACAGTGGCGTGGAGCGCGTGGTGGACCAGCGCTCCACCCTCGAGCCGCTCTTCCTCGTGATGAACCGGGCCTCCTGGATCACGGGAGGGCTGGCGACCATCATGGCGGTGGCCGCGGTGCTGCTCATCTCGACGACCATCAGGCTGTCGGCCATGTCCCGCTCCCGGCAGACGGGGATCATGCGTCTGGTGGGGGCCTCGAACCTCTTCATCCAGCTGCCCTTCATCCTCGAAGGGGTCATTGCCGCCCTCACCGGGGCGATTCTCGCCGTGGCCACGTTGTGGGTGGGAGTGCGCTACGTCGTGGAGGGGTGGCTCGCCTCCTCCATCTCCTTCACGAGCGCCTTCATCAGTACCAGGGATGTCCTCCTCCTGTCGCCCTGGCTGATTCTGGCCGCCATCGCCCTGGCCGCGGTCTCCTCCGCCTTGTCTCTGTCCAAGTACACGAGGATCTGA","VRLRFVLSETAKGMYRNLAMTVSVILVAFVSLLFVGASSLLQSQISTMKGDWYDKVEVSVYMCPKSSASSNCANGEATAAQISEVENLITSGAPSGYVKSYQMETKAQAYQNFMKAYAKSAVGRNATEDMMPVSFRIKLKDAENYKLVAEQFEGHSGVERVVDQRSTLEPLFLVMNRASWITGGLATIMAVAAVLLISTTIRLSAMSRSRQTGIMRLVGASNLFIQLPFILEGVIAALTGAILAVATLWVGVRYVVEGWLASSISFTSAFISTRDVLLLSPWLILAAIALAAVSSALSLSKYTRI$","Cell division protein FtsX","Membrane, Cytoplasm, Extracellular","FtsX-like protein involved in cell division","K02004","protein of unknown function DUF214","","","","","

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[132-303]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[178-196]?$ $\"[217-246]?$ $\"[252-272]?$ $\"[277-297]?$	transmembrane_regions

","BeTs to 9 clades of COG2177COG name: Cell division proteinFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG2177 is ---------drlb-efghsn-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 9-215 are 60% similar to a (DIVISION CELL FTSX ABC PERMEASE MEMBRANE TRANSPORTER TRANSMEMBRANE CELL-DIVISION FTSX) protein domain (PD011562) which is seen in Q6AEL6_BBBBB.","","-47% similar to PDB:1W2V THE 3-DIMENSIONAL STRUCTURE OF A THERMOSTABLE MUTANT OF A XYLANASE (XYN10A) FROM CELLVIBRIO JAPONICUS (E_value = );","Residues 132 to 303 (E_value = 1.2e-17) place ANA_0331 in the FtsX family which is described as Predicted permease.","","protein involved in cell division (ftsX)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0332","352207","353523","1317","5.19","-12.40","45674","ATGCTGTCTCGTCTGTTCCTGCGCCGCTCACGCCGGCGTGCCGCAGTCTGCGCCCTGGCCGCCGCCAGCCTCGTCTTCTTCTACTCTGGGGACATCTCCCTGGCTGATGAGCGGGATGACGCCGTTGCCAAGCAGAATGAGGCGGAGCGCAAGCAGCAGCAGGTGATGTCCTCGCTGGAGGGGGTCAGCGCCGATCTGGGGCAGGCCTACATCTCACTTCAGAACGCCCAGGCCTCGTTGAGCACTGCGGAGACGCAGCTGACCACTGCTGAGACGACTCTGGCCGCCAAGGAGAGGGAGCAGCAGATCGCCAGTGACCGCTTGAGTACGGCGCAGAGCAGCCTGGAGACGGTCAAGAAGGAGTCCGAGGCATCTAAGAAGACGGCTGAGGAGACCTCCGACTCGGTGGCGGAGATCGTCGTGTCCACCTATCAGGGGGATAACTCGGTGACCTCCTGGAGCTATGTTCTCGGCTCGCAGGACGTCGAGGAGCTCAGCCAGCGAGCCTCAGCGGTTGAGATCGGCTCAGGGGTCCAGGAGGCGGTACTGTCTGCCGCCGAGGTCGAGCGTGCTCAGAACGCCAACCGTGAGGCCAGGCAGAATGCTGCCACCACGCGAGTCAGCACGCTCAAGACCGAGGCCGACACCGCAGAGGCGAACGCCAAGTCGGCCCGGGACGCGGCCAAGACCAAGCGGGACGAGGTCGCCAAGCTGACGGCGCAGAAGAAGTCGGCCGCCGAGGCGCTGGAGAGCCGTAAGAGCGATCTGCAGTCCCAGCTCAACCAGGCCAACGCCGATGCCGCGGCAGCGGCCGCACGAGTCGCCCAGATCGACGCCGCCAACCGAGCAGCGGCCAGCGCTGGAACAATGCCCTCGGTCCCCGCGAGCTCGATCGGCGCCGACTCCCTGGGAAGCGGGTACATCGGACACCCGATCACCGGCCCGCTCGAGGTGACCTCGCCCTTCGGGTACCGCGTCCACCCGGTTACCGGTGTCGCCACAGGGCACCAGGGGGTCGACTTCGCCGCGAGTGAGGGGACGCCCCAGTACGCGGCGGTCTCCGGAGTGGCCACCTACTGGGACTCCGAGTCCTGCGGCATCGGCATTGACATCAACGGTGGCATCATTGACGGGCACTCCTACGTCATCACCCTGTGCCACCTCTCCTCGCGCAGCATCGCCGACGGCCAGCAGGTCAAGCGCGGTGACGTCGTCGGCGCGACCGGCTCCACCGGTTACGCGACCGGAGCGCACGTCCACTTCCAGGTGGCCCAGGACGGGGCGTACATCGACCCGATGTCCCTGCCCGGCTTCTAG","MLSRLFLRRSRRRAAVCALAAASLVFFYSGDISLADERDDAVAKQNEAERKQQQVMSSLEGVSADLGQAYISLQNAQASLSTAETQLTTAETTLAAKEREQQIASDRLSTAQSSLETVKKESEASKKTAEETSDSVAEIVVSTYQGDNSVTSWSYVLGSQDVEELSQRASAVEIGSGVQEAVLSAAEVERAQNANREARQNAATTRVSTLKTEADTAEANAKSARDAAKTKRDEVAKLTAQKKSAAEALESRKSDLQSQLNQANADAAAAAARVAQIDAANRAAASAGTMPSVPASSIGADSLGSGYIGHPITGPLEVTSPFGYRVHPVTGVATGHQGVDFAASEGTPQYAAVSGVATYWDSESCGIGIDINGGIIDGHSYVITLCHLSSRSIADGQQVKRGDVVGATGSTGYATGAHVHFQVAQDGAYIDPMSLPGF$","Peptidase, M23/M37 family","Extracellular, Periplasm","M23/M37 peptidase domain protein protein","peptidase; M23/M37 family","peptidase M23B","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR002886
Family

Peptidase M23B
PTHR21666:SF7	$\"[3-100]T$ $\"[264-435]T$	M23/M37 PEPTIDASE FAMILY MEMBER
PF01551	$\"[334-432]T$	Peptidase_M23

noIPR
unintegrated

unintegrated
PTHR21666	$\"[3-100]T$ $\"[264-435]T$	PEPTIDASE-RELATED
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

InterPro
IPR000037
Family

SmpB protein
PD004488	$\"[29-153]T$	SSRP_BIFLO_Q8G540;
PF01668	$\"[27-95]T$	SmpB
TIGR00086	$\"[28-171]T$	smpB: SsrA-binding protein
PS01317	$\"[47-59]T$	SSRP

noIPR
unintegrated

unintegrated
G3DSA:2.40.280.10	$\"[21-149]T$	no description

","BeTs to 18 clades of COG0691COG name: tmRNA-binding proteinFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0691 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000037 (SmpB protein) with a combined E-value of 2.1e-53. IPB000037A 29-74 IPB000037B 123-171","Residues 29-153 are similar to a (SSRA-BINDING RNA-BINDING SMALL B TMRNA-BINDING SMPB 3D-STRUCTURE HOMOLOG SSRA BTMRNA-BINDING) protein domain (PD004488) which is seen in SSRP_BIFLO.","","-57% similar to PDB:1P6V Crystal structure of the tRNA domain of transfer-messenger RNA in complex with SmpB (E_value = 8.7E_19);-57% similar to PDB:2OB7 Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM (E_value = 8.7E_19);-56% similar to PDB:1J1H Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus (E_value = 4.8E_17);-56% similar to PDB:1K8H NMR Structure of Small Protein B (SmpB) from Aquifex aeolicus (E_value = 6.2E_17);-55% similar to PDB:1ZC8 Coordinates of tmRNA, SmpB, EF-Tu and h44 fitted into Cryo-EM map of the 70S ribosome and tmRNA complex (E_value = 3.1E_16);","Residues 27 to 95 (E_value = 1.4e-31) place ANA_0333 in the SmpB family which is described as SmpB protein.","","protein (smpB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0335","355667","354921","747","6.42","-5.21","27389","ATGAACCAAAAGTCGGACAATGGGGCCATGCAGATCTCCCGCGGTGTCATGTCCGGCCTTACCACCACCCCGATGACTCAGTCATCCACGGCGATCGCCGAGATCAAGAACTACATTCTCACCAAGGGTCTGCATCCTGGAGATGCGTTGCCCACCGAGTCCCAGCTGTGCACCGACCTGGGAGTATCCCGCTCCTCCGTCCGCGAGGCCGTCCGCACCCTCGTCGCCCTCGACATCGTCGAAGTACGCCACGGACACGGCATGTTCGTCGGCCAGGTCTCCATGCGCCCCATGGTCGAGTCCCTCATCTTCAAAGGCCTCCTCAACCCCGGAGACGACCACCGCGGACTACGAGACATCGTCGAAGTACGCATCACCCTCGACAACGCCCTGGCCGAACCCGTCACCCACGCCTGGCACAACCGCCACGACCCCGAGCTCGACACCCTCGTCGACAACATCGAGCACCTCGCCTCACAAGGCAAGCTCTTCACCGACCAGGACCGCCGCTTCCACACCCGCCTACTCGAACCCCTCGACAACCACCTCTACCTCCACCTCACCGAAGCCTTCTGGGCCATCCACACCCTCACCGTCCCCCTCCTGGACGCCCCCAAGCTCGAAGACCTCACCAGCACCGCCAAAGCCCACCGAGCCATGCTCCAAGCCGCCCACGCCGGAGACACCCCCGCCTACCACCAAGCCATCACCGACCACTACGCCCCACTCCTCGCCGTCCTCTCCTGA","MNQKSDNGAMQISRGVMSGLTTTPMTQSSTAIAEIKNYILTKGLHPGDALPTESQLCTDLGVSRSSVREAVRTLVALDIVEVRHGHGMFVGQVSMRPMVESLIFKGLLNPGDDHRGLRDIVEVRITLDNALAEPVTHAWHNRHDPELDTLVDNIEHLASQGKLFTDQDRRFHTRLLEPLDNHLYLHLTEAFWAIHTLTVPLLDAPKLEDLTSTAKAHRAMLQAAHAGDTPAYHQAITDHYAPLLAVLS$","Transcriptional regulator, GntR-family","Cytoplasm","Transcriptional regulators","GntR-family transcriptional regulator","regulatory protein GntR, HTH","","Haydon D.J., Guest J.R. A new family of bacterial regulatory proteins. FEMS Microbiol. Lett. 1991. 63(2):291-295. PMID: 2060763Van aalten D.M., Dirusso C.C., Knudsen J., Wierenga R.K. Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. EMBO J. 2000. 19(19):5167-5177. PMID: 11013219Rigali S., Derouaux A., Giannotta F., Dusart J. Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies. J. Biol. Chem. 2002. 277(15):12507-12515. PMID: 11756427","","","

InterPro
IPR000524
Domain

Bacterial regulatory protein GntR, HTH
PR00035	$\"[50-64]T$ $\"[64-80]T$	HTHGNTR
PF00392	$\"[27-90]T$	GntR
SM00345	$\"[31-90]T$	HTH_GNTR
PS50949	$\"[25-93]T$	HTH_GNTR

InterPro
IPR011711
Domain

GntR, C-terminal
PF07729	$\"[119-242]T$	FCD

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[20-93]T$	no description

","BeTs to 8 clades of COG2186COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2186 is ---------dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is 2","***** IPB000524 (Bacterial regulatory protein, GntR family) with a combined E-value of 5.7e-16. IPB000524 50-90***** IPB011711 (GntR, C-terminal) with a combined E-value of 7.4e-16. IPB011711A 47-77 IPB011711B 217-228***** IPB011663 (UbiC transcription regulator-associated) with a combined E-value of 9.4e-13. IPB011663 50-90","Residues 46-85 are 85% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR GNTR FAMILY REGULATOR GNTR-FAMILY REGULATORY) protein domain (PD069824) which is seen in Q6NJ95_CORDI.Residues 91-240 are 44% similar to a (DNA-BINDING TRANSCRIPTION REGULATION GNTR) protein domain (PD794773) which is seen in Q9CK70_PASMU.Residues 146-243 are 62% similar to a (DNA-BINDING TRANSCRIPTION REGULATION REGULATORY TRANSCRIPTIONAL FAMILY GNTR REGULATORS PROTEINS NEDR) protein domain (PD632195) which is seen in NEDR_MICVI.","","-45% similar to PDB:2DI3 Crystal structure of the transcriptional factor CGL2915 from Corynebacterium glutamicum (E_value = 1.9E_10);","Residues 27 to 90 (E_value = 1.4e-18) place ANA_0335 in the GntR family which is described as Bacterial regulatory proteins, gntR family.Residues 119 to 242 (E_value = 0.00022) place ANA_0335 in the FCD family which is described as FCD domain.","","regulators (AL132991)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0336","357624","356905","720","6.21","-7.21","26484","ATGACGACGCCCGCCACTCAAGCAGAGGCCACGATGGCCGAGATCAAGAACTACATCCTGCGCTCCGGCCTGCAGATGGGTGATGCGTTGCCCACCGAGTCCCAGCTGTGCACCGACCTGGGAGTATCCCGCTCCTCCGTCCGCGAGGCCGTCCGCACCCTCGTCGCCCTCGACATCGTCGAAGTACGCCACGGACACGGCATGTTCGTCGGCCAGGTCTCCATGCGCCCCATGGTCGAGTCCCTCATCTTCAAAGGCCTCCTCAACCCCGGAGACGACCACCGCGGACTACGAGACATCGTCGAAGTACGCATCACCCTCGACAACGCCCTGGCCGAACCCGTCACCCACGCCTGGCACAACCGCCACGACCCCGAGCTCGACACCCTCGTCGACAACATCGAGCACCTCGCCTCACAAGGCAAGCTCTTCACCGACCAGGACCGCCGCTTCCACACCCGCCTACTCGAACCCCTCGACAACCACCTCTACCTCCACCTCACCGAAGCCTTCTGGGCCATCCACACCCTCACCGTCCCCCTCCTGGACGCCCCCAAGCTCGAAGACCTCACCAGCACCGCCAAAGCCCACCGAGCCATGCTCCAAGCCGCCCACGCCGGAGACACCCCCGCCTACCACCAAGCCATCACCGACCACTACGCCCCACTCCTCGCCGTCCTCACACACCCCGTAGAGAACTCCTCCGTCAGGGCGGGATAG","MTTPATQAEATMAEIKNYILRSGLQMGDALPTESQLCTDLGVSRSSVREAVRTLVALDIVEVRHGHGMFVGQVSMRPMVESLIFKGLLNPGDDHRGLRDIVEVRITLDNALAEPVTHAWHNRHDPELDTLVDNIEHLASQGKLFTDQDRRFHTRLLEPLDNHLYLHLTEAFWAIHTLTVPLLDAPKLEDLTSTAKAHRAMLQAAHAGDTPAYHQAITDHYAPLLAVLTHPVENSSVRAG$","Transcriptional regulator, GntR-family","Cytoplasm","Transcriptional regulators","GntR-family transcriptional regulator","regulatory protein GntR, HTH","","Haydon D.J., Guest J.R. A new family of bacterial regulatory proteins. FEMS Microbiol. Lett. 1991. 63(2):291-295. PMID: 2060763Van aalten D.M., Dirusso C.C., Knudsen J., Wierenga R.K. Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. EMBO J. 2000. 19(19):5167-5177. PMID: 11013219Rigali S., Derouaux A., Giannotta F., Dusart J. Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies. J. Biol. Chem. 2002. 277(15):12507-12515. PMID: 11756427","","","

InterPro
IPR000524
Domain

Bacterial regulatory protein GntR, HTH
PR00035	$\"[30-44]T$ $\"[44-60]T$	HTHGNTR
PF00392	$\"[7-70]T$	GntR
SM00345	$\"[11-70]T$	HTH_GNTR
PS50949	$\"[5-73]T$	HTH_GNTR

InterPro
IPR011711
Domain

GntR, C-terminal
PF07729	$\"[99-222]T$	FCD

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[8-73]T$	no description

","BeTs to 8 clades of COG2186COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2186 is ---------dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is 2","***** IPB000524 (Bacterial regulatory protein, GntR family) with a combined E-value of 5.5e-16. IPB000524 30-70***** IPB011711 (GntR, C-terminal) with a combined E-value of 6.9e-16. IPB011711A 27-57 IPB011711B 197-208***** IPB011663 (UbiC transcription regulator-associated) with a combined E-value of 9.1e-13. IPB011663 30-70","Residues 27-65 are 84% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR GNTR FAMILY REGULATOR GNTR-FAMILY REGULATORY) protein domain (PD069824) which is seen in Q8NMC7_CORGL.Residues 71-228 are 44% similar to a (DNA-BINDING TRANSCRIPTION REGULATION GNTR) protein domain (PD794773) which is seen in Q9CK70_PASMU.Residues 126-223 are 62% similar to a (DNA-BINDING TRANSCRIPTION REGULATION REGULATORY TRANSCRIPTIONAL FAMILY GNTR REGULATORS PROTEINS NEDR) protein domain (PD632195) which is seen in NEDR_MICVI.","","-47% similar to PDB:2DI3 Crystal structure of the transcriptional factor CGL2915 from Corynebacterium glutamicum (E_value = 5.7E_12);","Residues 7 to 70 (E_value = 1.1e-16) place ANA_0336 in the GntR family which is described as Bacterial regulatory proteins, gntR family.Residues 99 to 222 (E_value = 0.00022) place ANA_0336 in the FCD family which is described as FCD domain.","","regulators (AL132991)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0337","355814","356968","1155","5.29","-10.49","41301","GTGAGCGGCTTGCCGCTACAGCGCTCACAGTGCAACAGTTACGGCATGTCTCGCACGCATGAGGAGCTCCCTGCCCGTCCTGCCTACGACAGTGCCACCGCCGCTCTGCTCGAGCGCATCGAGTCGCTCGGCGTCTTCGGAACCATGACGGTGCAGAAGATCCCGAGCTGGCGCGTACCGGCTGACGAGGTCCGGGCGAGTTTTCTGCTCAAGCACCCCGACATCGACCTGGAGGACGTGGACGTCCTTCGTCAGGATGGGACGAGACTTCCCGCCGCGGTTGCACGAAGCGCCCAGGGTGCCTGCGTGGGCCGCCCCGGCCCCCTGTTCCTCTCTCTGCACGGGGGAGGGCTGGTGATGGGGTGCCGTTTCAATGGCCTGTCGACCGTTGTCCCGTGGCTGCGGCGGTACGGGGGCGTCATCGTCAGCCCCGAGTACCGTCTGGCTCCCGAGGATCCGGCACCGGCCGGCGTCGAGGACTGCTACACCACGCTGTGCTGGGCGGTCGAGCACGCCGAGGAGCTCGGTGCTGATCCGGAGCGCGTCATCGTCGTCGGGCCGAGCGCCGGGGGAGGGCTGAGCGCCGGCACGCTGCTCATCTCGCGAGACAGGCGGGGCCCGGTGGTTCTCGGCGGGCTGCTGGACTACCCCATGCTGGATGACCGCACCGGCATGCCGCACTGGCAGGGCTCGGTCTCAGCGCGTCAGTACCCGGACGACGGCACCTGGCCGACGGCGTACAACAATGTTGCCTGGGATGCTGCCCTGGGGGAGCGGCGAGGTACGGACCTGGTCACCCCCTACGAGGCCCCCGCCCGTGCCACGTGGTTGGGTGGGCTGCCACCGCTGTTCATCTCAGTGGCCTCCGCCGAGGTCTTCCGGGACGAGGATGTCGCCTTCGCCTCTGGGGTGTGGCGTGATGGTGGTGATGCCGAGCTGCATGTCTACCCCGGGGGCACCCACGCCATGGAGTTCGTCAACGCGCGATGGCTCGCACGCGGACTTACGGCAGCACGCGACCTGTGGGTGGACAGGTTGCTTCGACCGGAGGACCCGCGCCTCAATGTCGTGGCCGTGGCGCAGGCCGGCACCTATCCCGCCCTGACGGAGGAGTTCTCTACGGGGTGTGTGAGGACGGCGAGGAGTGGGGCGTAG","VSGLPLQRSQCNSYGMSRTHEELPARPAYDSATAALLERIESLGVFGTMTVQKIPSWRVPADEVRASFLLKHPDIDLEDVDVLRQDGTRLPAAVARSAQGACVGRPGPLFLSLHGGGLVMGCRFNGLSTVVPWLRRYGGVIVSPEYRLAPEDPAPAGVEDCYTTLCWAVEHAEELGADPERVIVVGPSAGGGLSAGTLLISRDRRGPVVLGGLLDYPMLDDRTGMPHWQGSVSARQYPDDGTWPTAYNNVAWDAALGERRGTDLVTPYEAPARATWLGGLPPLFISVASAEVFRDEDVAFASGVWRDGGDAELHVYPGGTHAMEFVNARWLARGLTAARDLWVDRLLRPEDPRLNVVAVAQAGTYPALTEEFSTGCVRTARSGA$","Esterase/lipase","Cytoplasm, Extracellular","esterase","hypothetical protein","Alpha/beta hydrolase fold-3 domain protein","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR013094
Domain

Alpha/beta hydrolase fold-3
PF07859	$\"[110-325]T$	Abhydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[17-353]T$	no description
PTHR23024	$\"[73-327]T$	MEMBER OF 'GDXG' FAMILY OF LIPOLYTIC ENZYMES
PTHR23024:SF25	$\"[73-327]T$	UNCHARACTERIZED ENZYME

","BeTs to 10 clades of COG0657COG name: Esterase/lipaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0657 is a--p--y-vdrlbcefg-s--j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB013094 (Alpha/beta hydrolase fold-3) with a combined E-value of 1.6e-30. IPB013094A 108-121 IPB013094B 141-161 IPB013094C 184-203 IPB013094E 291-321***** IPB002168 (Lipolytic enzyme) with a combined E-value of 8.5e-18. IPB002168A 108-122 IPB002168B 125-167 IPB002168C 181-194***** IPB010468 (Hormone-sensitive lipase, N-terminal) with a combined E-value of 1.8e-08. IPB010468K 130-156 IPB010468L 157-183","Residues 146-184 are 76% similar to a (HYDROLASE ESTERASE LIPASE 3.1.1.- PROBABLE LIPASE/ESTERASE PRMC3 ACETYL CARBOXYLESTERASE FAMILY) protein domain (PD409736) which is seen in Q8PDG3_XANCP.Residues 202-296 are 54% similar to a (HYDROLASE ESTERASE LIPASE 3.1.1.- PROBABLE LIPASE/ESTERASE CARBOXYLESTERASE PLASMID ACETYL 3.1.-.-) protein domain (PD087155) which is seen in O52556_AMYMD.","","-42% similar to PDB:1LZK BACTERIAL HEROIN ESTERASE COMPLEX WITH TRANSITION STATE ANALOG DIMETHYLARSENIC ACID (E_value = 4.1E_27);-42% similar to PDB:1LZL Bacterial Heroin Esterase (E_value = 4.1E_27);-40% similar to PDB:2C7B THE CRYSTAL STRUCTURE OF ESTE1, A NEW THERMOPHILIC AND THERMOSTABLE CARBOXYLESTERASE CLONED FROM A METAGENOMIC LIBRARY (E_value = 8.0E_15);-41% similar to PDB:1JJI The Crystal Structure of a Hyper-thermophilic Carboxylesterase from the Archaeon Archaeoglobus fulgidus (E_value = 3.0E_14);-38% similar to PDB:1EVQ THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS (E_value = 6.8E_14);","Residues 110 to 325 (E_value = 8e-44) place ANA_0337 in the Abhydrolase_3 family which is described as alpha/beta hydrolase fold.","","(estA) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0338","357650","359575","1926","7.26","1.42","69171","ATGATCGGCTCGTCACCCACAGATGTGACTTTCATCTCTTTATCTGTGATGGCGGTTGCCTGCGGTGCGGATGCTCTGTTCATGGTGCTGCTTCTCTTGATGTTGGCCATGGTTCTTGCCCTGTCAATCATTGTTGATCACTACGATGTGATTCCGCTCGTCGAACGGCTCGCCCCGGCAGTGGGGCGGGAGTTGCGACTGTCTTGCCTGCGAGGTTGTGAGTGGTCTGGACGCCCTGACTTCTGCTACAGTCATCCTACCAACGTCAGACATAAGACGTCAGACATCAGGAGAGAATCAATGGCGATCACGACTCCGGCCGGCTCCAGCCGCCGGGACTTCATCAGGCTGACCGGCACCCTCGGAATGGCTGCTGGTCTGGCCGTCAGCCTTGCGGCCTGCGGCGGTAAGGGCAAGGCCTCGGGTGGCGCGAAGGCCAGCGGCATGGCTGCCGATCAGGAGGTCACCCACAAGGACGGTGTCATCACCGCAGGTATTTCCTACGAGCTGGGCACCAACGGCTACGACCCGATGACGACGTCGTCGGCTCTGACGGTCGCTGCCAACTGGCACACTCTGGAGGGGCTCACCGAGCTCCACCCGGCCACCCGGGAGGTGTACGCGGCTCTGGCGGCGGAGATGCCCAAGAAGGTGGATGACACCACCTATGAGGTCGCGCTGCGTAAGGATGCGAAGTTCTCCGACGGCTCGGCCGTGACTGCCGACGACGTCGTCTTCTCCTTCACGCGCGTGCTCGACCCGGCCAACAAGTCGCTGTACTCCCAGTTCCTGCCCTTCATCGACAAGGTGGAGGCCAAGGATGCGGGCACGGTGACCATTAAGCTCAAGTACGCCTTCTCTCTGGTGGCGGAGCGTCTGAGCGTGGTCAAGATCGTCCCCAAGGCGATCGTTGAGGCGGACGCCAAGAAGTTCGACATGAGCCCCACTGGAAGCGGTCCCTACAAGATGACCGACAACGGTGCCGGCAGCCAGAAGGTCGTCTTCGAGCGCAACGACAAGTACAACGGTCCTCGCCCGGCGCTGGCCAAGTCCATGACCTGGCAGATCCTGCCCGACGACACCACCCGCACCAACGCGATGAGCTCCAGTTCCGTGCAGGCCATCGACGCCGTTCCGGCAGCCAACCTCAAGACGCTCAAGGACCCGGTCAAGGTGGCGGCGCAGCAGGGCTTCGGGCTGCTCTTCGCCATGTTCAACCACACCACCTTCTCCAACGTCAAGGCCCGGCAGGCGGTGCTCTACGCGCTGGACTACGCCAAGATCTGCAACACCGGCATGGCCGGCCTGGCGACGCCGGCGACCTGTTTCGTCCAGGACGGGCACCCCGCGTACAAGAAGGCCAAGACGGTCTACTCCAAGGACGCGGCCAAGGCCAAGTCGCTCCTGGCGGAGGCCGGCATCACGACTATCAACCTGCTGTGCACGGACCACGGCTGGTTCTCGGCCGTCAGGCCCATCATCCGTGAGAACCTCGAGGCCCTGGGGGTGACGGTCAAGTACGACGAGAAGAAGTCCGCGGACACCTACTCCTTCATCGACTCCGGACAGGGCACGTGGGACGTGCTGATCGCTCCCGGAGACCCCTCGGTCTTCGGCAATGACGCGGACCTGCTCATGCGCTGGTGGTACGGCGGTGACGTGTGGACCGAGACCCGGATGCACTGGAAGGGTTCGGAGAGTCAGGTCGCGGTCCAGAAGCTGCTGGAGGAAGCGGTCAAGCTGGAGGGTGACAAGCAGGTCGCCAAGTGGCAGGAGATCTTCGACAAGCTCTCCGAGGAGGTGCCGCTCTACCCGATCTTCCACCGCAAGGCTCCAACGGCTTATGACTCGACGACGTTGGAGAACTTCAAGCCCATCGCGCTGACCGGCCTGTCCTTCGTGGGGACGGGGTCGTCCAAGTCCTGA","MIGSSPTDVTFISLSVMAVACGADALFMVLLLLMLAMVLALSIIVDHYDVIPLVERLAPAVGRELRLSCLRGCEWSGRPDFCYSHPTNVRHKTSDIRRESMAITTPAGSSRRDFIRLTGTLGMAAGLAVSLAACGGKGKASGGAKASGMAADQEVTHKDGVITAGISYELGTNGYDPMTTSSALTVAANWHTLEGLTELHPATREVYAALAAEMPKKVDDTTYEVALRKDAKFSDGSAVTADDVVFSFTRVLDPANKSLYSQFLPFIDKVEAKDAGTVTIKLKYAFSLVAERLSVVKIVPKAIVEADAKKFDMSPTGSGPYKMTDNGAGSQKVVFERNDKYNGPRPALAKSMTWQILPDDTTRTNAMSSSSVQAIDAVPAANLKTLKDPVKVAAQQGFGLLFAMFNHTTFSNVKARQAVLYALDYAKICNTGMAGLATPATCFVQDGHPAYKKAKTVYSKDAAKAKSLLAEAGITTINLLCTDHGWFSAVRPIIRENLEALGVTVKYDEKKSADTYSFIDSGQGTWDVLIAPGDPSVFGNDADLLMRWWYGGDVWTETRMHWKGSESQVAVQKLLEEAVKLEGDKQVAKWQEIFDKLSEEVPLYPIFHRKAPTAYDSTTLENFKPIALTGLSFVGTGSSKS$","Peptide/nickel transport system substrate-binding protein","Membrane, Periplasm, Cellwall","ABC-type transporter, periplasmic component","K02035 peptide/nickel transport system substrate-binding protein","extracellular solute-binding protein, family 5","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670","","","

InterPro
IPR000914
Family

Bacterial extracellular solute-binding protein, family 5
PF00496	$\"[205-555]T$	SBP_bac_5
PS01040	$\"[211-233]?$	SBP_BACTERIAL_5

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[109-132]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.10.105.10	$\"[394-608]T$	no description
G3DSA:3.90.76.10	$\"[160-319]T$	no description
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[10-44]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 110-216 are 71% similar to a (PERIPLASMIC COMPONENT SECRETED ABC-TYPE SYSTEM DIPEPTIDE/OLIGOPEPTIDE/NICKEL ABC SYSTEM TRANSPORTER TRANSPORTER) protein domain (PD714624) which is seen in Q6NJ97_CORDI.Residues 227-303 are 72% similar to a (ABC PERIPLASMIC TRANSPORTER BINDING OLIGOPEPTIDE OLIGOPEPTIDE-BINDING TRANSPORTER PEPTIDE SOLUTE-BINDING PROTEIN) protein domain (PD588987) which is seen in Q7VL18_HAEDU.Residues 298-379 are 79% similar to a (ABC PERIPLASMIC TRANSPORTER BINDING OLIGOPEPTIDE OLIGOPEPTIDE-BINDING TRANSPORTER PEPTIDE SOLUTE-BINDING PROTEIN) protein domain (PD000753) which is seen in Q8NMC6_CORGL.Residues 396-444 are 73% similar to a (ABC PERIPLASMIC TRANSPORTER BINDING OLIGOPEPTIDE OLIGOPEPTIDE-BINDING TRANSPORTER PEPTIDE PROTEIN SOLUTE-BINDING) protein domain (PD001217) which is seen in Q8NMC6_CORGL.Residues 448-509 are 72% similar to a (PERIPLASMIC COMPONENT SECRETED ABC-TYPE SYSTEM DIPEPTIDE/OLIGOPEPTIDE/NICKEL ABC SYSTEM TRANSPORTER TRANSPORTER) protein domain (PD885519) which is seen in Q8NMC6_CORGL.Residues 510-632 are 75% similar to a (PERIPLASMIC COMPONENT SECRETED ABC-TYPE SYSTEM DIPEPTIDE/OLIGOPEPTIDE/NICKEL ABC SYSTEM TRANSPORTER TRANSPORTER) protein domain (PD660794) which is seen in Q8NMC6_CORGL.","","-38% similar to PDB:1UQW CRYSTAL STRUCTURE OF YLIB PROTEIN FROM ESCHERICHIA COI (E_value = 9.8E_19);-40% similar to PDB:1XOC The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide. (E_value = 7.0E_17);-41% similar to PDB:1DPP DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE (E_value = 2.6E_11);-46% similar to PDB:1UIU Crystal structures of the liganded and unliganded nickel binding protein NikA from Escherichia coli (Nickel unliganded form) (E_value = 2.6E_11);-46% similar to PDB:1UIV Crystal structures of the liganded and unliganded nickel binding protein NikA from Escherichia coli (Nickel liganded form) (E_value = 2.6E_11);","Residues 205 to 555 (E_value = 5.4e-66) place ANA_0338 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 Middle.","","transporter, periplasmic component","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0339","359783","360748","966","9.00","2.67","34820","GTGTCCAACCTCATCCGCCTGATCGGACGGCGCCTGGTCGCGCTGCCGGTCATGGTGCTGGGCGTGACGCTGCTCGTCTTCGTCGTCATGTCGTTCTCCTCGGCGGACCCGGCGCGTCTCGCGCTGGGCGAGTCGGCCACGCCAGACGCCCTCGAGCAGTACCGAGTCGCCCATCATCTCAACGATCCCCTTCTCAAGCGGTTCTGGGAGTACCTCCTGGGTCTGATCCACGGCGACCTCGGTACCTCCTTCACCGGCGTCAAGATCACCGGCATGGTGGCCGATGCGTTCCCGATCACGCTCCAGCTGACCTTCATCGGAATCTTCGTCGCCGTCATCGTGGCCACGGTCCTGGGCATTACGGCGGCCCTCTACCGCGACAAGTGGCAGGACCAGGTCATCCGCGTCATCTCCATCGCCTCCCTGGCCACCCCGTCCTTCTGGCTCGCCCTGCTGCTCATTCAGTGGTTCTCCGACATCCCGGGGGGAACGGGGACCTTCCCCGCGCTGGTGTCCGAGTGGGTTCCCTTCAGCGAGGATCCGGGAACGTACCTCAATCAGATCTTCCTGCCGGCACTGGCCATCGCGGTGCCCAACGCCGGCTCGCTCACCCGTGTGGTGCGTACCGCCATGGTTGAGGAGCTCGACCGCGACTACGTGCGCACCGCCATCGGCGGCGGTATTCCCAAGAACGTCGTCGTGGCCCGCAACGTGCTGCGCAACGCGCTCATTACTCCGCTGACCGTGCTGGGACTGCGCATCGGCTACGCCATGGGAGGTGCCGTCGTCATCGAGATGATCTTCAACATCAAGGGAATGGGCCAGCTCATCTTCCAGGGCATCACCCGCAACGACGTGAACATCGTCCAGGGCGTCTCCATCACGGTGGCACTGGCCTTCATCATCATCAACATCGTCGTTGACATGCTCTACGTCCTCGTCAACCCACGAATCAGGAGCATCTGA","VSNLIRLIGRRLVALPVMVLGVTLLVFVVMSFSSADPARLALGESATPDALEQYRVAHHLNDPLLKRFWEYLLGLIHGDLGTSFTGVKITGMVADAFPITLQLTFIGIFVAVIVATVLGITAALYRDKWQDQVIRVISIASLATPSFWLALLLIQWFSDIPGGTGTFPALVSEWVPFSEDPGTYLNQIFLPALAIAVPNAGSLTRVVRTAMVEELDRDYVRTAIGGGIPKNVVVARNVLRNALITPLTVLGLRIGYAMGGAVVIEMIFNIKGMGQLIFQGITRNDVNIVQGVSITVALAFIIINIVVDMLYVLVNPRIRSI$","Peptide/nickel transport system permease protein","Membrane, Cytoplasm","ABC-type transporter, permease components","K02033 peptide/nickel transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Kota J., Ljungdahl P.O. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J. Cell Biol. 2005. 168(1):79-88. PMID: 15623581","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[97-320]T$	BPD_transp_1
PS50928	$\"[97-311]T$	ABC_TM1

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[17-173]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[12-32]?$ $\"[105-125]?$ $\"[137-157]?$ $\"[183-203]?$ $\"[250-270]?$ $\"[294-314]?$	transmembrane_regions

","BeTs to 20 clades of COG0601COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0601 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 5-79 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER OLIGOPEPTIDE TRANSPORTER SYSTEM MEMBRANE PEPTIDE DIPEPTIDE) protein domain (PD856780) which is seen in Q6M2I9_CORGL.Residues 80-157 are 58% similar to a (NICKEL ABC PERMEASE TRANSMEMBRANE TRANSPORTER) protein domain (PD990188) which is seen in Q8TKE8_METAC.Residues 81-230 are 45% similar to a (FOR SIMILAR PEPTIDES ABC PERMEASE TRANSMEMBRANE TRANSPORTER) protein domain (PD762760) which is seen in Q8G560_BIFLO.Residues 89-133 are 77% similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER OLIGOPEPTIDE SYSTEM TRANSPORTER PEPTIDE MEMBRANE DIPEPTIDE) protein domain (PD857696) which is seen in Q7VL17_HAEDU.Residues 127-192 are similar to a (TRANSMEMBRANE ABC-TYPE PERMEASE INTEGRAL SYSTEM MEMBRANE OLIGOPEPTIDE SYSTEM DIPEPTIDE/OLIGOPEPTIDE/NICKEL TRANSPORTER) protein domain (PD877055) which is seen in Q8NMC5_CORGL.Residues 193-230 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER OLIGOPEPTIDE TRANSPORTER SYSTEM PEPTIDE MEMBRANE DIPEPTIDE) protein domain (PD289919) which is seen in Q6NJ98_CORDI.Residues 247-292 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER OLIGOPEPTIDE SYSTEM TRANSPORTER PEPTIDE MEMBRANE DIPEPTIDE) protein domain (PD007336) which is seen in Q6NJ98_CORDI.","","-48% similar to PDB:1W0I ARABIDOPSIS THALIANA MITOCHONDRIAL KAS (E_value = );-48% similar to PDB:2IX4 ARABIDOPSIS THALIANA MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE HEXANOIC ACID COMPLEX (E_value = );","Residues 97 to 320 (E_value = 1.4e-44) place ANA_0339 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter, permease components (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0340","360748","362898","2151","6.02","-9.43","76235","ATGCTGCACCGCTCCACACTGGATAAGGCCTCGCGGCCCGGGCTGCGCTTCCAGGGCTGGAAGGCGCTTCCTGTCGGCTCCAAGATCGCCATCATCGTGCTGGGCCTCATCGCCCTGGTCGCCATCCTGGCTCCCATCATCGCCCCCTACTCTCCCGGTGCCACCGGGTTGGCGGAGACCAAGACGACCTCCTACATCGAGGGCGTCGGTGAGGTGACCTCCTCCGATCCGGTCGTCGCCCCGTCCGCGTCTCACCTGTTCGGGACGGACGGCACCGGTCGTGACATCTTCTCCCGTGCCGTCTACGGCGCCAGGGTCTCGCTGGTCGTGGGCCTGACGGCCACCGGTCTGGCCCTTGTGGTGGCCTCGGTCCTCGGGGCCGTTGCCGCCACGTCGCGCAAGTGGATCGCTGAGACCCTCATGCGCGTGCTCGACGTCGTCATGTCCTTCCCCGGCATCGCTCTGGCGGCCGTCCTCGTCTCGGCGATGTCGACCCGCCTGCCGATGCTGCCGGTCATCATCGTCTCCATCGGCATCCTCTACATCCCCCAGCTCACCCGCGTGGTGCGTGCCAACATCATCTCCCAGTTCGGGGAGGACTATGTGGCCGCCTCCAAGGTGATGGGGGCCCCGGTGCCGTGGATCCTGCTCAAGCACGTGGCCCGCAACTGCATCGCCCCGATCATGGTCTTCGCAACCGTCCTGGTGGCCGACGCGATCGTCTTCGAGGCCTCGCTGTCCTTCATCGGCGCGGGCATCAAGTCCGTCAACACCCCGACCTGGGGCAACATGCTCTCCGAGGGCAAGGAGCTGCTCCTGTCGGGCCACTGGTGGCCGACCTTCTTCCCCGGCCTGCTCATCCTCATCACCACCCTGTGCCTCAACGTCCTGTCCGAGGGACTGACCGATGCGATGGCCTCGCCGCGCATCAAGGCCAAGCCCGATGTTCAGGCCGATGAGGAGGCCATGGAGGCTCAGGAGACCCTGAACGCCTGGGACGACGCCGCCGAGGCGGTGGTCGCCAACGCCTCCGTCGCCGACGGGGACGACGCCGACAACGGGCTGAGCTCTCTGACCGGCGTTGTCGCCCCTGCGACAGAGGACGTTCCCCTGTCCGAGCGGCTCAGCTCCCTGCGGGTGGCCGAGCTTGCCCGGCGGGACCGCCTGGTCTACGAGGACACCGGCGAGGATCCGGTTCTGGAGGTCAAGAACCTCACGATCGCCTTCCCCGAGCAGCACGGTGAGGTCAACATCGTCGATGGCGTCTCCTTCTCCGTGCGTCCGGGCGAGACCATGGGCCTGGTGGGGGAGTCCGGCTGCGGTAAGTCCATCAGCTCGATGGCCGTCATGGGGCTGCTGCCCCCCTCGGCCCGGATCTCCGGTGAGATCCTCTTCAAGGGACGCAACATCCTTGAGATGACGCCGGCCGAGCACAACGCGCTGCGCGGTCACGAGATGAGCATGGTCTACCAGGACGCTCTGTCCTCACTGAACCCCTCCATGCTCATCCGCACTCAGATGGCCCAGCTCAGCGCGCGCGGAGGCACCCGCAGTGCCGAAGAGCTGCTCGAGCTGGTGGGGCTCGACCCCAAGCGCACGCTGCGCAGCTACCCGCACGAGCTCTCCGGCGGTCAGCGTCAGCGCGTTCTCATCGCCATGGCGCTGACCCGTGACCCCTCCCTGGTCCTGGCCGACGAGCCGACGACCGCGCTGGACGTGACCGTTCAGAAGCAGGTCATCGACCTGCTCAACGAGCTGCGTGAGAAGCTCGGCTTCGCGATGGTCTTCGTCTCGCACGACCTGGCCCTCGTGGCCAAGCTGGCCCACCGGATCACGGTGATGTACGCGGGCCAGGTGGTTGAGCAGGCGCCCACCAGCGAGCTGCTGGCCAACCCGGTTCACGAGTACACCCGCGGCCTTCTCGGTGCGGTGCTCTCCATCGAGGCCGGCTCCAAGCGACTCCACCAGGTGCGAGGGGTCGTCCCCTCACCCAGCGAGTTCGTCAAGGGAGACCGGTTCGCGCCGCGATCGGCCCACCCGACGGTCGGACTTGAGACCCGTCCGGTGCTCAAGCCCGTGCCGGGCACGACGGAGCACAGCTACGCCATCACCCCCGAGCTCGAGGCTCTGCTCGCGAAGGAGAAGCACTGA","MLHRSTLDKASRPGLRFQGWKALPVGSKIAIIVLGLIALVAILAPIIAPYSPGATGLAETKTTSYIEGVGEVTSSDPVVAPSASHLFGTDGTGRDIFSRAVYGARVSLVVGLTATGLALVVASVLGAVAATSRKWIAETLMRVLDVVMSFPGIALAAVLVSAMSTRLPMLPVIIVSIGILYIPQLTRVVRANIISQFGEDYVAASKVMGAPVPWILLKHVARNCIAPIMVFATVLVADAIVFEASLSFIGAGIKSVNTPTWGNMLSEGKELLLSGHWWPTFFPGLLILITTLCLNVLSEGLTDAMASPRIKAKPDVQADEEAMEAQETLNAWDDAAEAVVANASVADGDDADNGLSSLTGVVAPATEDVPLSERLSSLRVAELARRDRLVYEDTGEDPVLEVKNLTIAFPEQHGEVNIVDGVSFSVRPGETMGLVGESGCGKSISSMAVMGLLPPSARISGEILFKGRNILEMTPAEHNALRGHEMSMVYQDALSSLNPSMLIRTQMAQLSARGGTRSAEELLELVGLDPKRTLRSYPHELSGGQRQRVLIAMALTRDPSLVLADEPTTALDVTVQKQVIDLLNELREKLGFAMVFVSHDLALVAKLAHRITVMYAGQVVEQAPTSELLANPVHEYTRGLLGAVLSIEAGSKRLHQVRGVVPSPSEFVKGDRFAPRSAHPTVGLETRPVLKPVPGTTEHSYAITPELEALLAKEKH$","Peptide/nickel transport system ATP-binding protein","Membrane, Cytoplasm","ABC transporter, ATP-binding protein andpermease protein","K02031 peptide/nickel transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[104-311]T$	BPD_transp_1
PS50928	$\"[104-298]T$	ABC_TM1

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[540-583]T$	Q8NMC4_CORGL_Q8NMC4;
PF00005	$\"[429-617]T$	ABC_tran
PS50893	$\"[400-641]T$	ABC_TRANSPORTER_2
PS00211	$\"[541-555]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[428-618]T$	AAA

InterPro
IPR013563
Domain

Oligopeptide/dipeptide ABC transporter, C-terminal
PF08352	$\"[620-685]T$	oligo_HPY

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[394-650]T$	no description
PTHR19222	$\"[400-676]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28	$\"[400-676]T$	OLIGOPEPTIDE ABC TRANSPORTER
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[29-49]?$ $\"[108-128]?$ $\"[143-163]?$	transmembrane_regions

","BeTs to 15 clades of COG0444COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0444 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is 2","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.2e-71. IPB013563A 418-452 IPB013563B 486-499 IPB013563C 538-565 IPB013563D 593-645***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.6e-17. IPB005074C 418-465 IPB005074D 529-572***** IPB005116 (TOBE domain) with a combined E-value of 4.4e-15. IPB005116A 436-452 IPB005116C 541-554 IPB005116D 561-580 IPB005116E 595-608***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4e-11. IPB010509B 429-454 IPB010509D 536-580","Residues 143-220 are 84% similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q6NJ99_CORDI.Residues 143-239 are 60% similar to a (PROBABLE INNER MEMBRANE SYSTEM COMPONENT BINDING-PROTEIN- TRANSMEMBRANE DEPENDENT) protein domain (PD877965) which is seen in Q7WHK5_BORBR.Residues 240-305 are 87% similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER OLIGOPEPTIDE TRANSPORTER SYSTEM PEPTIDE MEMBRANE DIPEPTIDE) protein domain (PD672238) which is seen in Q6NJ99_CORDI.Residues 394-530 are 51% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD263317) which is seen in Q9KKK3_VIBCH.Residues 398-624 are 45% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 398-637 are 49% similar to a (ATP-BINDING SYSTEM ABC A1A2) protein domain (PD459661) which is seen in Q97BE5_THEVO.Residues 398-443 are 73% similar to a (ATP-BINDING PEPTIDE ABC SAPD TRANSPORTER SYSTEM TRANSPORTER OLIGOPEPTIDE COMPONENT ABC-TYPE) protein domain (PD684577) which is seen in Q8DKD3_SYNEL.Residues 399-537 are 55% similar to a (ATP-BINDING) protein domain (PDA1B1R2) which is seen in Q7M969_WOLSU.Residues 399-554 are 49% similar to a (DPP1 ATP OLIGOPEPTIDE ATP-BINDING ABC TRANSPORTER BINDING) protein domain (PD955106) which is seen in Q6L102_PICTO.Residues 399-510 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD305427) which is seen in Q9KKK3_VIBCH.Residues 399-571 are 55% similar to a (ATP-BINDING OPPD OLIGOPEPTIDE) protein domain (PDA11396) which is seen in Q7P513_BBBBB.Residues 399-488 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I322) which is seen in Q6AD99_BBBBB.Residues 399-601 are 46% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 400-599 are 44% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 400-631 are 43% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 400-646 are 44% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 415-599 are 46% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 419-473 are 94% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8NMC4_CORGL.Residues 426-501 are 60% similar to a (ATP-BINDING ABC TRANSPORTER PLASMID) protein domain (PDA0I326) which is seen in Q930F2_RHIME.Residues 444-510 are 73% similar to a (ATP-BINDING PEPTIDE ABC TRANSPORTER) protein domain (PD703348) which is seen in Q83AM6_COXBU.Residues 481-611 are 52% similar to a (ATP-BINDING ATPASE SYSTEM ABC COMPONENT ABC-TYPE YNTD) protein domain (PD861225) which is seen in Q7CQQ3_SALTY.Residues 491-611 are 51% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA184H5) which is seen in Q6W139_RHISN.Residues 498-599 are 55% similar to a (ATP-BINDING SYSTEM ABC) protein domain (PDA18612) which is seen in Q7MAH4_WOLSU.Residues 517-621 are 62% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 519-631 are 52% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 523-629 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 524-620 are 57% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 525-622 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 526-599 are 70% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 526-585 are 61% similar to a (ATPASE ATP-BINDING OPPF) protein domain (PDA184A1) which is seen in Q9LAT3_LISMO.Residues 526-610 are 65% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z9) which is seen in Q8DM53_SYNEL.Residues 526-600 are 54% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q7VP45_HAEDU.Residues 526-583 are 63% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD436020) which is seen in Q9A7G4_CAUCR.Residues 526-630 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K5M4) which is seen in Q897H9_CLOTE.Residues 527-621 are 60% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 531-611 are 74% similar to a (ATP-BINDING TRANSPORTER ABC OLIGOPEPTIDE) protein domain (PDA185B9) which is seen in Q9X0U7_THEMA.Residues 534-631 are 53% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 535-613 are 58% similar to a (ATP-BINDING TRANSPORTER ABC OLIGOPEPTIDE) protein domain (PDA189L6) which is seen in Q8TRD5_METAC.Residues 538-624 are 63% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 539-629 are 57% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 539-631 are 59% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 540-628 are 56% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 540-583 are 97% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q8NMC4_CORGL.Residues 540-606 are 59% similar to a (COMPONENT ABC ATPASE ATP-BINDING TRANSPORTER) protein domain (PDA0I0K5) which is seen in Q74HP7_LACJO.Residues 540-652 are 53% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.Residues 541-632 are 55% similar to a (PROBABLE ATP-BINDING ABC TRANSPORTER ATP BINDING) protein domain (PD763654) which is seen in Q8G625_BIFLO.Residues 648-702 are 78% similar to a (ATP-BINDING ABC-TYPE PERMEASE ATPASE TRANSPORTER MEMBRANE PROTEINS SYSTEM DIPEPTIDE/OLIGOPEPTIDE/NICKEL COMPONENT) protein domain (PD740554) which is seen in Q8NMC4_CORGL.","","-53% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.9E_26);-53% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.9E_26);-53% similar to PDB:1OXU Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.9E_26);-53% similar to PDB:1OXV Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.9E_26);-53% similar to PDB:1OXX Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 9.4E_26);","Residues 104 to 311 (E_value = 8.8e-27) place ANA_0340 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.Residues 429 to 617 (E_value = 9.4e-55) place ANA_0340 in the ABC_tran family which is described as ABC transporter.Residues 620 to 685 (E_value = 9.9e-15) place ANA_0340 in the oligo_HPY family which is described as Oligopeptide/dipeptide transporter, C-terminal region.","","transporter, ATP-binding protein and permease protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0341","362898","363725","828","6.81","-0.62","29640","ATGTCATCCAACACGTCTGCATCGTCCTCATGGAGCGAGGACCAGCCGGTCGTCGAGCTCAAGAACGTCAACGTCATCCACAAGTCCCGCACCGGTGGCCTGTTCAACCCGGACACGGTTCACGCGGTCAACGACGTCTCGCTGAGCGTCAAGCGCGGAGAGACGCTGGGACTCGTGGGGGAGTCGGGGTGCGGCAAGTCCACCACCGCCCGAGTCATGGTGGGGCTGCAGCCGGTCACCTCCGGTGAGGTCATCTTCAAGGGCCGTCCGTTGGGGCGCTCGGCCTCGGACCGTCGTGAGCTCGGGCGCAGCATCTCGGTGGTCTTCCAGGACCCGGCCACGGCCCTCAACCCGCGCATGATCGTGCACGACGCGCTCATCGACCCGCTCAACGTCCACGGAATCGGCTCGCCGAAGGAACGTGAGGCCAAGGTGCGCGACCTGCTCCACCTGGTCGGGCTGCCCCCCAGCGCACTCAATGTGCTGCCTCGGCAGATCTCCGGTGGTCAGCGCCAGCGCGTCGCCATCGCCCGAGCGCTCGCCCTGGACCCCGACATCATCGTGGCCGACGAGCCCACCTCCGCCCTGGACGTCTCGGTGCGCGCCCAGGTGCTCAACCTCCTCCAGGACCTCAAGGCCTCCTTGGGACTGGGGCTGGTGTTCATCAGTCACGACATCAACACGGTGCGCTACGTCTCGGACCGGATCGCCGTCATGTACTTCGGCAAGATCCTCGAGCTCAACACCACCGAGGAGATCTTCAACAATCCTCAGGAGGAGTACACGCGCACTCTGCTGTCGGCAGTGCCCTCACTGCTCGATGTCTGA","MSSNTSASSSWSEDQPVVELKNVNVIHKSRTGGLFNPDTVHAVNDVSLSVKRGETLGLVGESGCGKSTTARVMVGLQPVTSGEVIFKGRPLGRSASDRRELGRSISVVFQDPATALNPRMIVHDALIDPLNVHGIGSPKEREAKVRDLLHLVGLPPSALNVLPRQISGGQRQRVAIARALALDPDIIVADEPTSALDVSVRAQVLNLLQDLKASLGLGLVFISHDINTVRYVSDRIAVMYFGKILELNTTEEIFNNPQEEYTRTLLSAVPSLLDV$","Peptide/nickel transport system ATP-binding protein","Membrane, Cytoplasm","ABC-type transporter, ATPase component","K02032 peptide/nickel transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[165-208]T$	Q82BU6_STRAW_Q82BU6;
PF00005	$\"[53-242]T$	ABC_tran
PS50893	$\"[20-266]T$	ABC_TRANSPORTER_2
PS00211	$\"[166-180]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[52-251]T$	AAA

InterPro
IPR013563
Domain

Oligopeptide/dipeptide ABC transporter, C-terminal
PF08352	$\"[245-272]T$	oligo_HPY

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[12-275]T$	no description
PTHR19222	$\"[18-272]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28	$\"[18-272]T$	OLIGOPEPTIDE ABC TRANSPORTER

","BeTs to 16 clades of COG1124COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1124 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 4.1e-80. IPB013563A 42-76 IPB013563B 105-118 IPB013563C 163-190 IPB013563D 218-270***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.2e-32. IPB005074C 42-89 IPB005074D 154-197 IPB005074E 218-238***** IPB005116 (TOBE domain) with a combined E-value of 1.9e-22. IPB005116A 60-76 IPB005116C 166-179 IPB005116D 186-205 IPB005116E 220-233***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1e-18. IPB010509B 53-78 IPB010509D 161-205***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.9e-06. IPB010929K 40-84 IPB010929M 163-209 IPB010929C 148-181","Residues 16-271 are 49% similar to a (ATP-BINDING SYSTEM ABC A1A2) protein domain (PD459661) which is seen in Q97BE5_THEVO.Residues 17-196 are 46% similar to a (ATP-BINDING OPPD OLIGOPEPTIDE) protein domain (PDA11396) which is seen in Q7P513_BBBBB.Residues 17-130 are 62% similar to a (ABC ATP TRANSPORTER ATP-BINDING BINDING) protein domain (PDA0J3R3) which is seen in Q97VF4_SULSO.Residues 17-126 are 55% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18601) which is seen in Q73JC4_TREDE.Residues 22-98 are 55% similar to a (ATP-BINDING PHOSPHONATE ABC-TYPE PROTEIN) protein domain (PDA0J3O0) which is seen in Q6MPJ3_BDEBA.Residues 28-253 are 44% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 30-261 are 44% similar to a (ATP-BINDING ABC PROTEIN TRANSPORTER) protein domain (PD995669) which is seen in Q73R06_TREDE.Residues 34-187 are 50% similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 36-235 are 49% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 36-177 are 46% similar to a (DPP1 ATP OLIGOPEPTIDE ATP-BINDING ABC TRANSPORTER BINDING) protein domain (PD955106) which is seen in Q6L102_PICTO.Residues 37-253 are 47% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 42-154 are 55% similar to a (ATP-BINDING) protein domain (PDA1B1R2) which is seen in Q7M969_WOLSU.Residues 42-239 are 44% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD738128) which is seen in Q8G833_BIFLO.Residues 43-261 are 48% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 43-208 are 49% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 43-196 are 49% similar to a (ATP-BINDING ABC PRECURSOR TRANSPORTER SIGNAL) protein domain (PDA0X2Z3) which is seen in Q6MM73_BDEBA.Residues 45-91 are 85% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8NMC3_CORGL.Residues 45-224 are 49% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 46-120 are 59% similar to a (ATP-BINDING ABC TRANSPORTER PLASMID) protein domain (PDA0I326) which is seen in Q930F2_RHIME.Residues 48-226 are 51% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 50-238 are 43% similar to a (ATP-BINDING NEQ299) protein domain (PDA186D0) which is seen in Q74MU8_NANEQ.Residues 102-239 are 49% similar to a (ATP-BINDING ATPASE SYSTEM ABC COMPONENT ABC-TYPE YNTD) protein domain (PD861225) which is seen in Q8ZDB8_YERPE.Residues 108-149 are 76% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER OLIGOPEPTIDE PEPTIDE COMPONENT DIPEPTIDE ATPASE SYSTEM) protein domain (PD469406) which is seen in Q6NJA0_CORDI.Residues 110-236 are 53% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA184H5) which is seen in Q6W139_RHISN.Residues 141-247 are 58% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 142-253 are 56% similar to a (COMPONENT ABC ATPASE ATP-BINDING TRANSPORTER) protein domain (PDA0I0K5) which is seen in Q74HP7_LACJO.Residues 143-235 are 63% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 144-256 are 54% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 151-236 are 67% similar to a (ATP-BINDING TRANSPORTER ABC OLIGOPEPTIDE) protein domain (PDA185B9) which is seen in Q9X0U7_THEMA.Residues 152-224 are 73% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 152-209 are 60% similar to a (ATPASE ATP-BINDING OPPF) protein domain (PDA184A1) which is seen in Q9LAT3_LISMO.Residues 152-235 are 61% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z9) which is seen in Q8DM53_SYNEL.Residues 153-246 are 58% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 158-225 are 66% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q87LE8_VIBPA.Residues 159-245 are 58% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 159-258 are 57% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 163-246 are 61% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 163-238 are 59% similar to a (ATP-BINDING TRANSPORTER ABC OLIGOPEPTIDE) protein domain (PDA189L6) which is seen in Q8TRD5_METAC.Residues 164-256 are 58% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 164-262 are 57% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J201) which is seen in Q73M59_TREDE.Residues 165-253 are 57% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 165-263 are 55% similar to a (COMPONENT METHYL M-REDUCTASE COENZYME ATP-BINDING) protein domain (PD462863) which is seen in Q93RF2_TREMD.Residues 165-257 are 56% similar to a (PROBABLE ATP-BINDING ABC TRANSPORTER ATP BINDING) protein domain (PD763654) which is seen in Q8G625_BIFLO.Residues 165-208 are identical to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q82BU6_STRAW.Residues 165-275 are 54% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.","","-58% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 5.5E_33);-57% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 7.2E_33);-57% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 7.2E_33);-57% similar to PDB:1G29 MALK (E_value = 2.7E_32);-57% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 3.0E_31);","Residues 53 to 242 (E_value = 3e-63) place ANA_0341 in the ABC_tran family which is described as ABC transporter.Residues 245 to 272 (E_value = 3.5e-07) place ANA_0341 in the oligo_HPY family which is described as Oligopeptide/dipeptide transporter, C-terminal region.","","transporter, ATPase component (dppF)","","1","","","","","","","","","","","","","Wed Aug 1 15:31:23 2007","","","Wed Aug 1 15:31:23 2007","Wed Aug 1 15:31:23 2007","Wed Aug 1 15:31:23 2007","","Wed Aug 1 15:31:23 2007","Wed Aug 1 15:31:23 2007","","","","","yes","","" "ANA_0342","363923","364843","921","4.96","-12.92","32091","ATGGACAACCGTTTCACCGGCGTCATCCCGCCGGTCGTCACCCCTTTCACCGCCGCGGGCGAGGTTGACTTCGACAGCCTGGACAAGGTCGTCGAGCACCTCATCGCCGGTGGTGTCAACGGCCTGTTCGCCCTGGGGTCCTCCGGAGAGGTCGCTTACCTCACCGACGCCCAGCGCGACGCCGTCATCGAGCGGGTCGTCAAGGCTGCGGCAGGACGCGTCCCGGTGCTCGCCGGTGCCATCGACACCACCGCCCACCGGGTCATTGACCAGGCTCGTCGGGCAGCCGCCCTGGGCGCTGAGGCGATCGTGGCCACCTGCCCGTTCTACGCGCTCAACGACGCCGAGGAGATCAAGGCTCACTTCCGCGCCATCGCCGCGGCCATCGACGTCCCCGTCTTCGCCTACGACGTCCCCGTGCGCCTTGGCGGCGCGAAGCTCGGTTGCGAGCTGCTCGTCGAGCTGGGCAAGGAGGGTGTCCTGGCCGGTGTCAAGGACTCCTCCGGCAACGACGTCGCCTTCCGCAGGCTGGTGGCCGCCAATGAGGCCGCGGGCCACCCCCTGGCCCTTCTGACCGGCCACGAGTGCGTCGTCGACGGCATGCTGCTGCTGGGTGCCGACGGCCTCGTCCCCGGGTACGGCAACGTGGACCCGGTCCGCTACGCCGAGATGTGGAAGGCCTCCCGCGAGGGGGCGTGGGACGAGGTGCGCCGTCTCCAGGACGAGGTCTGCGTCGGCTTCGAGATCGTCTTCGTGCCCCAGGGCCGTTCGGCCGACGCGACCGGCATCGGCGCCTTCAAGACCGCCATGGAGGCTATCGGGATCATCGCCACCAACGAGATGGCCTTCCCCGTCAAGGCGCTCGAGGGCGAGACCAAGGAACGGGTCCTGGAGATCGTCAAGGCCCAGGGCCTCATCTGA","MDNRFTGVIPPVVTPFTAAGEVDFDSLDKVVEHLIAGGVNGLFALGSSGEVAYLTDAQRDAVIERVVKAAAGRVPVLAGAIDTTAHRVIDQARRAAALGAEAIVATCPFYALNDAEEIKAHFRAIAAAIDVPVFAYDVPVRLGGAKLGCELLVELGKEGVLAGVKDSSGNDVAFRRLVAANEAAGHPLALLTGHECVVDGMLLLGADGLVPGYGNVDPVRYAEMWKASREGAWDEVRRLQDEVCVGFEIVFVPQGRSADATGIGAFKTAMEAIGIIATNEMAFPVKALEGETKERVLEIVKAQGLI$","Dihydrodipicolinate synthetase","Cytoplasm","dihydrodipicolinate synthase family protein","dihydrodipicolinate synthase family protein ","dihydrodipicolinate synthetase","","Mirwaldt C., Korndorfer I., Huber R. The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. J. Mol. Biol. 1995. 246(1):227-239. PMID: 7853400Murphy P.J., Trenz S.P., Grzemski W., De Bruijn F.J., Schell J. The Rhizobium meliloti rhizopine mos locus is a mosaic structure facilitating its symbiotic regulation. J. Bacteriol. 1993. 175(16):5193-5204. PMID: 8349559","","","

InterPro
IPR002220
Family

Dihydrodipicolinate synthetase
PD001859	$\"[7-75]T$	Q6NJA1_CORDI_Q6NJA1;
PR00146	$\"[38-59]T$ $\"[74-92]T$ $\"[106-122]T$ $\"[131-148]T$	DHPICSNTHASE
PIRSF001365	$\"[5-305]T$	Dihydrodipicolinate synthase
PTHR12128	$\"[1-306]T$	DIHYDRODIPICOLINATE SYNTHASE
PF00701	$\"[4-304]T$	DHDPS

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[5-306]T$	no description

","BeTs to 22 clades of COG0329COG name: Dihydrodipicolinate synthase/N-acetylneuraminate lyaseFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0329 is aompkz-qv-rlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB002220 (Dihydrodipicolinate synthetase) with a combined E-value of 8.1e-52. IPB002220A 7-16 IPB002220B 30-80 IPB002220C 99-142 IPB002220D 192-218 IPB002220B 22-72","Residues 7-75 are 82% similar to a (LYASE DIHYDRODIPICOLINATE SYNTHASE BIOSYNTHESIS DHDPS LYSINE DIAMINOPIMELATE N-ACETYLNEURAMINATE ACID ALDOLASE) protein domain (PD001859) which is seen in Q6NJA1_CORDI.Residues 126-200 are 78% similar to a (LYASE DIHYDRODIPICOLINATE SYNTHASE BIOSYNTHESIS DHDPS LYSINE DIAMINOPIMELATE ACID N-ACETYLNEURAMINATE DEHYDRATASE) protein domain (PD485872) which is seen in Q6NJA1_CORDI.Residues 205-306 are 66% similar to a (DIHYDRODIPICOLINATE SYNTHASE LYASE ALDOLASE FAMILY DAPA SYNTHASE/N-ACETYLNEURAMINATE) protein domain (PDA165T5) which is seen in Q8FWP0_BRUSU.Residues 224-304 are 64% similar to a (LYASE DIHYDRODIPICOLINATE SYNTHASE BIOSYNTHESIS DHDPS LYSINE DIAMINOPIMELATE N-ACETYLNEURAMINATE DEHYDRATASE PROBABLE) protein domain (PD213669) which is seen in Q6A699_PROAC.","","-44% similar to PDB:2EHH Crystal structure of dihydrodipicolinate synthase from aquifex aeolicus (E_value = 1.3E_22);-41% similar to PDB:1DHP DIHYDRODIPICOLINATE SYNTHASE (E_value = 7.3E_21);-41% similar to PDB:1YXC Structure of E. coli dihydrodipicolinate synthase to 1.9 A (E_value = 7.3E_21);-41% similar to PDB:1YXD Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A (E_value = 7.3E_21);-41% similar to PDB:2ATS Dihydrodipicolinate synthase co-crystallised with (S)-lysine (E_value = 7.3E_21);","Residues 4 to 304 (E_value = 2.3e-38) place ANA_0342 in the DHDPS family which is described as Dihydrodipicolinate synthetase family.","","synthase family protein (dapA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0343","365013","366053","1041","5.09","-13.00","34565","ATGAGTCAGGATGTCCTCCCACCCAACCCCCTTGCTCCATTGCCATCTCCGTCCGATCGGGCGCCGCTCGTCGTCGGACTCGACCTGGGCGGCACCAAGATGGCCGCCGCACTGGTCGACTCCGGAGGGACCCTGCAAGGACCGGTGAGCTCCTGCCCGACCCCGGCTCACGAGGGCCCCACCGCCATGCTCAATGCCATCAGCGGCCTGATCGCGACGGTCGTCGAGACCGGAACGCACCAGGAGCCAGGCAAGGCCGCGGCAATCACGGCGGTCGGAATCGGTACCGCCGGCGTCGTCGACGTCGAGCGAGGGACCATCCTGTCGGCCACCGACGCCATCACCGGATGGGCCGGCACGCAGGTCGCCGCCGGCGTTCGCGAGCGGCTCGCCGCCCAGGGGCTGGGTGAGCTGCCGATCCACGTCGAGAACGACGTCGACGCCTACGCCGCCGGAGAGGCCTGGCTCGGTGCCGGCACCGGGGCCGAGGTCGTCCTCATGGTGGCGGTGGGCACCGGGGTCGGCGGCGCCCTCGTACTCGATGGGCGAACCCGCAGGGGCGCCCATCACGTGGCCGGCGAGATCGGCCACGTCCCCGTCCCCGGGGCCCAGGGCGAGCCCTGCACCTGCGGCAGGACGGGGCACCTGGAGGGCGTCACCGCCGGACCCCAGATCCACCGCCGTTACCTGGCCAAGGGCGGAGACCCCGACGTTCCCGACGCCCGCGGGGTTGAGGAGCGCGCCGCTGCCGGGGACGACATCGCCGCGGAGGTCTACCGCGACTCGGCCACCTGCCTGGGCAGAGCCCTGGCAGGACTGGTCACCGTGATCGACCCCGACGTCGTCGTCGTCTCCGGCGGCCTGGCCCGCGCCGGTGACCTGTGGTGGGAGCCCCTGCGGCAGACCTTCGCCGCAGAGATCATCGACCCCCTGGCCCCCATCAAGATCCTTCCCGCCACCCTGGGGACTACCGCGCCGATCGTCGGTGCGGCTCGCGGCGCCCTTGCCCTGGCCGCCTGCAACGACAACCACCGCCCCTAG","MSQDVLPPNPLAPLPSPSDRAPLVVGLDLGGTKMAAALVDSGGTLQGPVSSCPTPAHEGPTAMLNAISGLIATVVETGTHQEPGKAAAITAVGIGTAGVVDVERGTILSATDAITGWAGTQVAAGVRERLAAQGLGELPIHVENDVDAYAAGEAWLGAGTGAEVVLMVAVGTGVGGALVLDGRTRRGAHHVAGEIGHVPVPGAQGEPCTCGRTGHLEGVTAGPQIHRRYLAKGGDPDVPDARGVEERAAAGDDIAAEVYRDSATCLGRALAGLVTVIDPDVVVVSGGLARAGDLWWEPLRQTFAAEIIDPLAPIKILPATLGTTAPIVGAARGALALAACNDNHRP$","Transcriptional regulator; glucokinase","Cytoplasm","Transcriptional regulator","glucokinase; putative ","ROK family protein","","Titgemeyer F., Reizer J., Reizer A., Saier Jr M.H. Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 1994. 140:2349-2354. PMID: 7952186","","","

InterPro
IPR000600
Family

ROK
PF00480	$\"[26-225]T$	ROK
PS01125	$\"[170-197]?$	ROK

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.160	$\"[145-331]T$	no description
G3DSA:3.30.420.40	$\"[11-144]T$	no description
PTHR18964	$\"[95-342]T$	ROK FAMILY
PTHR18964:SF37	$\"[95-342]T$	GLUCOSE KINASE

","BeTs to 11 clades of COG1940COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1940 is ao-p-z-qvdrlbce-gh---j--t-Number of proteins in this genome belonging to this COG is 5","***** IPB000600 (ROK family) with a combined E-value of 1.9e-18. IPB000600A 26-33 IPB000600B 139-153 IPB000600C 168-179 IPB000600D 192-198 IPB000600E 208-217","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 225 (E_value = 3.6e-23) place ANA_0343 in the ROK family which is described as ROK family.","","regulator ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0344","366147","366839","693","5.23","-8.44","23683","ATGCACCCCGTTCTGGAACGCCTCAAGGGAGGACTCATCGCCTCCGCCCAGGCCTACCCGGGTGAGCCCATGCGCGACCCCCGCACCATGGACCAGGTGGCCCAGGCCTGCGTCGCCGGCGGCGCCGTCGGCATCCGCGCACAGGGGCTGGCGGACCTGGCCCTCATCTGCCAGCACGTCGACGTCCCCGTCATTGGCCTGTGGAAGGACGGCCACGACGGCGTCTTCATCACTCCGACCCTCACCCACGCCATCGCCGTGGCCGCCACCGGAAGCCAGATCGTGGCGCTGGACGGCACCCGGCGCCCCCGCCCCGATGGGTTGAGTCTGGCCCAGACCGTCGAGGGGCTGCGGGCGGCCCGCCCCGAGGTCCTCATCATGGCTGACTGCGGCTCCCTGGATGACGCCAAGGCCGCCCAAGATGCGGGAGTGGACGTCCTGGGGACCACCCTGGCCGGCTACACCGGGGAGCGTCCCAAGACCGAGGGGCCCGACCTCGAGCTCGTTGACCAGGTCGCCGGTATCGCGGAGGTTCCGTTGGTGGTTGAGGGCAGGGTCCACACGCCCGCGCAGGCGGCTGCCGCCATGGAGCACGGGGCCTTCGCCGTCGTGGTTGGTACTGCCATCACCCACCCGACGACCATCACCTCCTGGTTCGCCAGCGCGCTGCCCGGCGCCCTGTGGAAGGACTGA","MHPVLERLKGGLIASAQAYPGEPMRDPRTMDQVAQACVAGGAVGIRAQGLADLALICQHVDVPVIGLWKDGHDGVFITPTLTHAIAVAATGSQIVALDGTRRPRPDGLSLAQTVEGLRAARPEVLIMADCGSLDDAKAAQDAGVDVLGTTLAGYTGERPKTEGPDLELVDQVAGIAEVPLVVEGRVHTPAQAAAAMEHGAFAVVVGTAITHPTTITSWFASALPGALWKD$","N-acylglucosamine-6-phosphate 2-epimerase","Cytoplasm","5.1.3.9","N-acylglucosamine-6-phosphate 2-epimerase ","N-acylglucosamine-6-phosphate 2-epimerase","","","","","

InterPro
IPR007260
Family

Putative N-acetylmannosamine-6-phosphate epimerase
PF04131	$\"[30-225]T$	NanE

","BeTs to 4 clades of COG3010COG name: Putative N-acetylmannosamine-6-phosphate epimeraseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG3010 is -----------l--e-gh------t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 4-160 are 77% similar to a (2-EPIMERASE N-ACETYLMANNOSAMINE-6-PHOSPHATE ISOMERASE EPIMERASE CARBOHYDRATE MANNAC-6-P METABOLISM KINASE ENZYME INCLUDES:) protein domain (PD691126) which is seen in Q6A6A0_PROAC.Residues 162-219 are 73% similar to a (N-ACETYLMANNOSAMINE-6-PHOSPHATE 2-EPIMERASE ISOMERASE EPIMERASE METABOLISM CARBOHYDRATE MANNAC-6-P) protein domain (PD931497) which is seen in Q6A6A0_PROAC.Residues 164-223 are 68% similar to a (2-EPIMERASE N-ACETYLMANNOSAMINE-6-PHOSPHATE EPIMERASE ISOMERASE CARBOHYDRATE MANNAC-6-P METABOLISM KINASE ENZYME INCLUDES:) protein domain (PD023458) which is seen in NANE_ECO57.","","-54% similar to PDB:1YXY Crystal Structure of putative N-acetylmannosamine-6-P epimerase from Streptococcus pyogenes (APC29713) Structural genomics, MCSG (E_value = 7.3E_33);-47% similar to PDB:1Y0E Crystal structure of putative ManNAc-6-P epimerase from Staphylococcus aureus (strain N315) (E_value = 3.6E_24);","Residues 30 to 225 (E_value = 1.7e-62) place ANA_0344 in the NanE family which is described as Putative N-acetylmannosamine-6-phosphate epimerase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0345","366979","367323","345","8.15","0.91","12003","ATGCGTAGCGTTGCCAGAAGTGGCACCACACAAGGGTGTCCGTCCACGATCGAGAGGGAAGACATGTCCGTCAACCGCACCGAGCTCATCGCCGCCATCGCCGAGAAGGCCGGCCTGACCAAGACCGACGCCGACGCCTTCCTGGGAGCCTTCCAGGATGTCCTCGTTGAGAACGTCGCCAAGGGTGAGGCCGTGAAGATCACCGGCCTCATGGGTATCGAGCGCGTCGAGCGTGCCGCACGCACTGGCCGCAACCCCCGCACCGGTGAGGAGATTCAGATCCCCGCCGGCTACGGTGTCAAGGTCACCGTCGGCTCCTCGCTGAAGAAGGCTGTCGCCGAGTGA","MRSVARSGTTQGCPSTIEREDMSVNRTELIAAIAEKAGLTKTDADAFLGAFQDVLVENVAKGEAVKITGLMGIERVERAARTGRNPRTGEEIQIPAGYGVKVTVGSSLKKAVAE$","Histone-like bacterial DNA-binding protein","Cytoplasm","DNA-binding protein Hu","K03530 DNA-binding protein HU-beta","histone family protein DNA-binding protein","","Drlica K., Rouviere-Yaniv J. Histonelike proteins of bacteria. Microbiol. Rev. 1987. 51(3):301-319. PMID: 3118156Pettijohn D.E. Histone-like proteins and bacterial chromosome structure. J. Biol. Chem. 1988. 263(26):12793-12796. PMID: 3047111Wang S.L., Liu X.Q. The plastid genome of Cryptomonas phi encodes an hsp70-like protein, a histone-like protein, and an acyl carrier protein. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(23):10783-10787. PMID: 1961745Friedman D.I. Integration host factor: a protein for all reasons. Cell 1988. 55(4):545-554. PMID: 2972385Neilan J.G., Lu Z., Kutish G.F., Sussman M.D., Roberts P.C., Yozawa T., Rock D.L. An African swine fever virus gene with similarity to bacterial DNA binding proteins, bacterial integration host factors, and the Bacillus phage SPO1 transcription factor, TF1. Nucleic Acids Res. 1993. 21(6):1496-1496. PMID: 8464748Tanaka I., Appelt K., Dijk J., White S.W., Wilson K.S. 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature 1984. 310(5976):376-381. PMID: 6540370","","","

InterPro
IPR000119
Family

Histone-like bacterial DNA-binding protein
PD000945	$\"[33-112]T$	DBH1_BIFLO_P17615;
G3DSA:4.10.520.10	$\"[24-112]T$	no description
PF00216	$\"[24-113]T$	Bac_DNA_binding
SM00411	$\"[24-113]T$	BHL

","BeTs to 18 clades of COG0776COG name: Bacterial nucleoid DNA-binding proteinFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0776 is ---p---qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000119 (Histone-like bacterial DNA-binding protein) with a combined E-value of 2.7e-17. IPB000119 62-112","Residues 33-112 are similar to a (DNA-BINDING DNA REGULATION HU HOST INTEGRATION FACTOR TRANSCRIPTION CONDENSATION RECOMBINATION) protein domain (PD000945) which is seen in DBH1_BIFLO.","","-65% similar to PDB:1EXE SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1. (E_value = 5.0E_17);-62% similar to PDB:1WTU TRANSCRIPTION FACTOR 1, NMR, MINIMIZED AVERAGE STRUCTURE (E_value = 9.4E_16);-64% similar to PDB:1HUE HISTONE-LIKE PROTEIN (E_value = 2.1E_15);-64% similar to PDB:1HUU DNA-BINDING PROTEIN HU FROM BACILLUS STEAROTHERMOPHILUS (E_value = 2.1E_15);-61% similar to PDB:1P51 Anabaena HU-DNA cocrystal structure (AHU6) (E_value = 8.8E_14);","Residues 24 to 113 (E_value = 9.7e-34) place ANA_0345 in the Bac_DNA_binding family which is described as Bacterial DNA-binding protein.","","protein Hu (hs1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0346","367379","367501","123","5.82","-0.90","4351","GTGTGGCAACGGGCCGAATCATGTTCTCGCCGCGGTGCCCTCCTCATCTGCCTGATGATGCACGGGCAGGTTCTCCGGGAGGACGTCGGAAACGGTGATCTCCTCCTTGCGGCGGAGGGATGA","VWQRAESCSRRGALLICLMMHGQVLREDVGNGDLLLAAEG$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[163-206]T$	Q737Q7_BACC1_Q737Q7;
PF00005	$\"[58-239]T$	ABC_tran
PS50893	$\"[33-263]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[57-248]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[27-264]T$	no description
PTHR19222	$\"[33-272]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[33-272]T$	ABC TRANSPORTER

","BeTs to 16 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.8e-20. IPB005074C 47-94 IPB005074D 152-195***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.6e-19. IPB013563A 47-81 IPB013563C 161-188 IPB013563D 215-267***** IPB005116 (TOBE domain) with a combined E-value of 5e-10. IPB005116A 65-81 IPB005116D 184-203***** IPB013283 (ABC transporter family E signature) with a combined E-value of 7.4e-07. IPB013283D 62-87","Residues 37-139 are 53% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 38-96 are 67% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 41-142 are 50% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 45-228 are 43% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 46-236 are 44% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 47-251 are 43% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 48-97 are similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q6AEK4_BBBBB.Residues 48-275 are 40% similar to a (ATP-BINDING CG1494-PA) protein domain (PD310846) which is seen in Q9VRG3_DROME.Residues 51-264 are 41% similar to a (LANTIBIOTIC SYSTEM MERSACIDIN TRANSPORTER) protein domain (PDA0G5T2) which is seen in Q7UG09_RHOBA.Residues 62-248 are 43% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 63-251 are 50% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 63-221 are 50% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 103-163 are 63% similar to a (ATP-BINDING ABC SYSTEM TRANSPORTER TRANSPORTER) protein domain (PD931498) which is seen in Q8G3S7_BIFLO.Residues 110-206 are similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA1A2W6) which is seen in Q6A6S1_PROAC.Residues 115-250 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 143-247 are 50% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 161-250 are 60% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 163-206 are 86% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q737Q7_BACC1.Residues 165-252 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K5M6) which is seen in Q6A6H8_PROAC.Residues 165-248 are 58% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 209-280 are similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I9A2) which is seen in Q6AEK4_BBBBB.Residues 222-276 are 74% similar to a (ATP-BINDING SYSTEM ABC TRANSPORTER) protein domain (PD732582) which is seen in Q8G3S7_BIFLO.","","-58% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 6.2E_32);-51% similar to PDB:2ONK ABC transporter ModBC in complex with its binding protein ModA (E_value = 6.7E_18);-51% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.9E_17);-51% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.9E_17);-51% similar to PDB:1OXU Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.9E_17);","Residues 58 to 239 (E_value = 1e-39) place ANA_0347 in the ABC_tran family which is described as ABC transporter.","","protein of ABC transporter system","","1","","","","","","","","","","","Mon Aug 13 18:25:34 2007","","Mon Aug 13 18:25:34 2007","","","Mon Aug 13 18:25:34 2007","Mon Aug 13 18:25:34 2007","Mon Aug 13 18:25:34 2007","","Mon Aug 13 18:25:34 2007","Mon Aug 13 18:25:34 2007","","","","","yes","","" "ANA_0348","368467","370074","1608","9.11","11.09","55425","ATGGTGCTGACCGGCGCCGTCGGACTGGGGCTCAAGGCCGACCCTGACGTCATCATGCTGGTTCTCGGGGCTCTCGGGGCGCTGCTGATGGCCGGTTGGGCCGTGGTGCCACTGCTCGTCACCGGGGTCGACTCCACCCTGGACCCCCGCGCCATGGCGGCCTGGACCGCTCCGTCCAGAGGGCTGGCGCTCGGCCTGCTGGCCGCCGGCGCCCTGGGAATCCCCGGTTGCCTCACGGCTGCCGTCTGTCTCATTCCGGTCCTCACCTGGCTGCTGGCGGGCCAGTTCGCAGCGGCGCTCCTGGCGCTGCTGTGCGCTCCGGCCGCCCTGGCCACCTGCGTCCTGCTGTCCCGGATCATCGTGACAGCCGTAGGCGTCTCCGCCTCACGCCGGGGGCGTGAGGCGACAGCGATCATCACCTTCGTCGCCTTCATGGTGTGCACACAGCTGCCGAATCTGATCCCCCGAATCCTCGGGGACGATCCCTCCGATTTTCTTCAACGGCTCAATGGTGCCGCCAAGGTCATGGGGCTGAGCCCCTTTGGGTGGACCTTCTCGGCCCCCGGTCTCATGGCCACCGGATCCGTGATGCCGGCTCTGGCTCTGGCGATCGTCGCCTGGGTCCTCCCCGTGATCCTGTTTCCCCTGTGGCAGCGCGTGGTGGGCAAGGTGATGACCTCTCCGGGGACGTCACACACCCGGATGCGGGCATACGCAGCCAGTAGCACGGGATCCAATGCGCGGCAGCAGGGCCTACCCGACGTGCTGCCGTGGGCCCGCAGACTCGGCGCCTCCCTGCCTGCGCCCGCCGCTGCTGTGGCGGCCCGCAGCCTGCGCTACTGGCGCACCGATCCCAGGTACCTGGTTCAGTTTCTGTCCGTCCTGATTCTGCCCGTTGTGCTCGTCCTGGGGCCTGCTCTCAACTCCAGCCGATTCGCCGCCGGCGACAACGGTCAGCCGGTGGACATCAGCTTCGCCCTCGGACACGCCCCGGCCCCGCTGCTGTTCATGGCGCCCGCCCTGGCCGTCTTCATGGGATGGGCGATCCACGATGACCTCGGCCTGGACTCCACCGCCCTGTGGAGTCATATCAGCGCCGGTATCAGCGGAGCGCACGACCGTCTGGGGCGGGTAGTCGGTGCGGCCGTGTGGCAGGTCCCCGCACTGGTTGCTATCGACCTGCTCATGGTCGTGTGGACGGGACGATGGGATGCGCTCCCCGCCGTCACCGGTGCCTGCCTGGCCCTCTACGGCTGCGCGCTGGCCTGGTCCTGCCTGACCAGTGTCCTGCTGCCCTACGAGACGCTCGCCCCAGGGGACAGTCCCATGCGTTCGCGGACCTCGGGCACGGCCTTCCTGGCCGCGCTCATTCAGATGGCGGCAATCCTGCTTCTGCTGGCCGTGTGCTCCCCGGTCCTGGGGGCTGCGGTCTACAGCGTCGTCCAAGGCGCGCCGGTGTGGGGGTGGGTGGCGCTCGTCGCGGGGGTCGTGTGGTGCGGTCTGCTGCTCTGGGGTGGAGTCGTCGTCGGCGGGCGGATGCTGGACCGGCGAGGACCACAGGTTCTTGCCACGATCCGTAGCTGGCCGGGACACTCCCAGCCGGTGTGA","MVLTGAVGLGLKADPDVIMLVLGALGALLMAGWAVVPLLVTGVDSTLDPRAMAAWTAPSRGLALGLLAAGALGIPGCLTAAVCLIPVLTWLLAGQFAAALLALLCAPAALATCVLLSRIIVTAVGVSASRRGREATAIITFVAFMVCTQLPNLIPRILGDDPSDFLQRLNGAAKVMGLSPFGWTFSAPGLMATGSVMPALALAIVAWVLPVILFPLWQRVVGKVMTSPGTSHTRMRAYAASSTGSNARQQGLPDVLPWARRLGASLPAPAAAVAARSLRYWRTDPRYLVQFLSVLILPVVLVLGPALNSSRFAAGDNGQPVDISFALGHAPAPLLFMAPALAVFMGWAIHDDLGLDSTALWSHISAGISGAHDRLGRVVGAAVWQVPALVAIDLLMVVWTGRWDALPAVTGACLALYGCALAWSCLTSVLLPYETLAPGDSPMRSRTSGTAFLAALIQMAAILLLLAVCSPVLGAAVYSVVQGAPVWGWVALVAGVVWCGLLLWGGVVVGGRMLDRRGPQVLATIRSWPGHSQPV$","Putative integral membrane transport protein","Membrane, Cytoplasm","putative integral membrane transport protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[19-41]?$ $\"[62-93]?$ $\"[99-121]?$ $\"[171-191]?$ $\"[197-217]?$ $\"[287-307]?$ $\"[330-350]?$ $\"[380-402]?$ $\"[408-430]?$ $\"[451-481]?$ $\"[487-507]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 39-441 are 42% similar to a (MEMBRANE INTEGRAL PERMEASE ABC ABC-TYPE PROTEIN ASSOCIATED TRANSPORTER COMPONENTS TRANSPORTER) protein domain (PD324911) which is seen in Q6AEK5_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","integral membrane transport protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0349","370215","370955","741","4.81","-15.45","26139","GTGCAGCTAGTCATTCTGGATTCCGCGCAGGCGATCGCACAGCGGGCGGCCGACGAGATCGAGGCGCTGCTCAAGGACAAACCGGCAGCCGTGCTGGGAACCGCGACGGGCTCCTCGCCTCTGCCCCTGTACGACGAGCTCACTGCCCGCTGCGCCGCTGGCCGCCTCAGCTTCGCCGAGGTCACCGGATTCATGCTCGACGAGTACGTCGGCCTGCCCGCAGGCCACCCGGAGCGCTACGCCACCTTCATGGAGACCAACCTGCGCTCCCGCGTTGACATGCGCCCCGGCGCCCTCCACGGCCCGGACGCGCTGAGCGAAGACCTTGAGGCCGCCTGCCGGGACTACGAGGCGCAGATGGCTGCGGCCGGATACTGCGACCTGCAGATCCTCGGCATCGGCTCCGATGGGCACATCGGGTTCAACGAGCCCGGCGGCGCCCTCGACTCGCGCACGCACCTGGGCGAGCTCCATGAGCAGACCCGCCGGGACAACGCCCGCTTCTTCGGCGGCGACGTCGAGGCCGTGCCCACCCAGTGCATCACCCAGGGGCTAGCCACCATCATGGAGGCCCGCAAGCTGGTCCTCATCGCCACCGGCGAGGGCAAGGCCGAGGCCATCGCCCAGCTCGTCGAGGGGGAGGTCAGCGCCCAGTGGCCGGCGACCGTCATGCAGCGTCACGACGACGCCCTTGTCCTGGTCGATCCCGCCGCCGCCAGCCGGCTCACCTCGACGCACTGA","VQLVILDSAQAIAQRAADEIEALLKDKPAAVLGTATGSSPLPLYDELTARCAAGRLSFAEVTGFMLDEYVGLPAGHPERYATFMETNLRSRVDMRPGALHGPDALSEDLEAACRDYEAQMAAAGYCDLQILGIGSDGHIGFNEPGGALDSRTHLGELHEQTRRDNARFFGGDVEAVPTQCITQGLATIMEARKLVLIATGEGKAEAIAQLVEGEVSAQWPATVMQRHDDALVLVDPAAASRLTSTH$","Glucosamine-6-phosphate isomerase","Cytoplasm","Glucosamine-6-phosphate deaminase(Glucosamine-6-phosphate isomerase) (GNPDA) (GlcN6P","glucosamine-6-phosphate isomerase ","glucosamine-6-phosphate isomerase","","Oliva G., Fontes M.R., Garratt R.C., Altamirano M.M., Calcagno M.L., Horjales E. Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Structure 1995. 3(12):1323-1332. PMID: 8747459","","","

InterPro
IPR004547
Family

Glucosamine-6-phosphate isomerase
PTHR11280	$\"[19-242]T$	GLUCOSAMINE-6-PHOSPHATE ISOMERASE
TIGR00502	$\"[1-245]T$	nagB: glucosamine-6-phosphate isomerase
PS01161	$\"[120-138]?$	GLC_GALNAC_ISOMERASE

InterPro
IPR006148
Domain

Glucosamine/galactosamine-6-phosphate isomerase
PF01182	$\"[16-245]T$	Glucosamine_iso

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1360	$\"[1-242]T$	no description

","BeTs to 12 clades of COG0363COG name: 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0363 is ------y-v-rlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 2","***** IPB004547 (Glucosamine-6-phosphate isomerase) with a combined E-value of 7.7e-78. IPB004547A 31-73 IPB004547B 116-168 IPB004547C 184-238","Residues 12-139 are 51% similar to a (6PGL 3D-STRUCTURE HYDROLASE 6-PHOSPHOGLUCONOLACTONASE) protein domain (PD750531) which is seen in 6PGL_THEMA.Residues 31-242 are similar to a (ISOMERASE DEAMINASE GLUCOSAMINE-6-PHOSPHATE HYDROLASE METABOLISM CARBOHYDRATE GNPDA GLCN6P PHOSPHATE GLUCOSAMINE-6-) protein domain (PD006132) which is seen in NAGB_STRAW.","","-62% similar to PDB:2BKV STRUCTURE AND KINETICS OF A MONOMERIC GLUCOSAMINE-6-PHOSPHATE DEAMINASE: MISSING LINK OF THE NAGB SUPERFAMILY (E_value = 4.5E_44);-62% similar to PDB:2BKX STRUCTURE AND KINETICS OF A MONOMERIC GLUCOSAMINE-6-PHOSPHATE DEAMINASE: MISSING LINK OF THE NAGB SUPERFAMILY (E_value = 4.5E_44);-57% similar to PDB:1NE7 HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE (E_value = 1.8E_40);-56% similar to PDB:1CD5 GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER (E_value = 1.7E_38);-56% similar to PDB:1DEA STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION (E_value = 1.7E_38);","Residues 16 to 245 (E_value = 6e-57) place ANA_0349 in the Glucosamine_iso family which is described as Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase.","","deaminase (Glucosamine-6-phosphate isomerase) (GNPDA) (GlcN6P deaminase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0350","371048","371413","366","6.12","-0.91","12763","ATGACAGACGTCCTCGCCAGTGCCGATCCCGGATCGCCCGGAGCCCCGACAGACCCGGCCACCGAGCCCACCCAGGGCGTCGGTACGGCTGTCCTGGAGCGCGACGAGCTCCAGACGACCGACGACGGCGACGCCGACCGCTTCGCCCACTACGTCCGCAAGGACAAGATCGCCGCGGCCGCTGTCACCGGGCGTCCCGTCGTCGCCCTGTGCGGCAAGGTGTGGACGCCCGGGCGCGACCCGTCGAAGTACCCGGTGTGCCCCACCTGCAAGTCCATCTACGAGGAGATGCGTAACGGGGAGGGCTCCGGCGACGGCAAGGGGCCGCGTTTCCCCCGCTTCCCGTTCGGGCGAGGCGGTCGGTGA","MTDVLASADPGSPGAPTDPATEPTQGVGTAVLERDELQTTDDGDADRFAHYVRKDKIAAAAVTGRPVVALCGKVWTPGRDPSKYPVCPTCKSIYEEMRNGEGSGDGKGPRFPRFPFGRGGR$","Hypothetical protein","Extracellular, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 28-97 are 74% similar to a (SCO2947 U1764C CGL1916 MB2727C ML1016) protein domain (PD028488) which is seen in Q9L1U7_STRCO.","","-94% similar to PDB:2C31 CRYSTAL STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH THE COFACTOR DERIVATIVE THIAMIN-2-THIAZOLONE DIPHOSPHATE AND ADENOSINE DIPHOSPHATE (E_value = );-75% similar to PDB:2GJ0 Cycloviolacin O14 (E_value = );-46% similar to PDB:2GU2 Crystal Structure of an Aspartoacylase from Rattus norvegicus (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0351","371410","373233","1824","8.60","5.40","65662","GTGAACGCCGCCCGCGGCGGCCAGGCGACCCACCCCACCCCGACGCGAGCCTCGACGTCGGCGGCCCAGAACCTCTCCCCGGCCTACCCGCGCCGCGCCGCCTGGGGGACCGCCGGTTCGCTGCGTGCCTGGCAGGCCGCTGCGCTCGCGCAGTACCTGGAGACGATGCCCCAGGACTTCCTTGCGGTGGCCACCCCCGGGGCCGGCAAGACGACCTTCGCACTGCGAGTGGCCACCGAGCTGCTCAGTTCCGCAGACGTCCACAAGGTGACGATCGTCTGCCCCACTGAGCACCTCAAGTACCAGTGGGCCGAGGCCGCCGCCCGCGTCGGCATCCATATCGACCCCTCCTACTCCAACTCCCAGGGGGCACTCGGCTCGCGCTTCGACGGCGTCGCCCTGACCTACGCCCAGGTGGCCGCCAACGCCAACCTGCACCGCGCCCGCACCGACCAGGCCCGCACTCTGGTCATCCTCGACGAGATCCACCATGGGGGAGACGCCCTGAGCTGGGGAGACGCGATCCGGGAGGCCTTCACCCCGGCGCGGAGGCGACTGGCCCTGACCGGAACGCCCTTCCGCTCCGACACCTCCCCGATCCCCTTCGTGCGGTACAAGGAGGACGCCTCCGGGGCGAAACGCTCCCAGGCGGACTACTCCTACGGCTACTCCGACGCGCTGCGCGACGGAGTCGTGCGCCCGGTGATGTTCATGTCCTACTCGGGGCAGATGCGGTGGCGCACCAAGGCCGGCGACGAGGTCGCGGCGCGCCTGGGCGAGCCCCTCACCAAGGACCTGGAGTCCCAGGCCTGGCGCACCGCGCTCGACCCGGCGGGGGAGTGGATCCCCGCGGTCCTGGCCGCCGCCGACCAGCGCCTGACCGAGGTGCGCCGCCAGGTCCCCGACGCCGGAGCCCTCGTCATCGCCTCCGACCAGGCCAAGGCCCGCGCCTACGCCAAGCAGCTGCGCGCCATCACCGGCGAGGCCCCCACCGTGGTCCTCTCCGACGACAACGGTGCCTCCAGCCGCATCGAGGCCTTCTCCGCCTCCACCGACCGCTGGCTGGTGGCCGTGCGTATGGTCTCCGAGGGAGTGGACGTGCCCCGTCTGGCCGTGGGCGTCTACGCCACCTCCACCTCCACCCCGCTCTTCTTCGCCCAGGCCGTGGGGCGCTTCGTGCGCTCGCGGGCGAGGGGCGAGACTGCCTCGGTGTTCCTCCCGTCGGTCACGCCGCTGCTGGCCCTGGCCGGCGAGATGGAGGTGGCCCGCGACCATGTCCTGAGCCGCCCCGACTCGGCGGCGCAGGAGGACGCCCTGTTCAGCCCCGAGGACCGGCTCCTCGCCGAGGCCAACAAGACTGAGAACGCCTCGGCCGAGCTGCTGCCGGGCTTCGAGGCCATGGATAGCCAGGCCGAGTTCGACCGGGTGCTCTTCGACGGCGGCGAGTTCGGCACCGGTGCCATGGTGGGCAGTATCGAGGAGCAGGAGTACCTGGGGCTGCCCGGTCTGCTGGAGCCCGAGCAGGTGACCGCCCTGCTGCGCCAGCGCCAGGACAAGCAGATCGCCTCCCAGAAGAAGCAGGCCGCCGCTGAGGCGCAGAGGCGGAAGAACTCAGGCGTCGACGACGCCCGGCGGCGGGCAGCGGCCCGTAAGGAGCTCTCCCAGCTGGTGGCCGCCTGGGCCCGCCGCTCGAGCCAGCCCCACGGCGTCGTCCACAACGAGCTCAGGCGTGTGTGCGGGGGACCGGAGGTCGCGGCCGCCTCCACCGAGGAGATCGAGAAGCGCATCCAGACCCTGCGACGCTGGTTCGTCGGCAAGCGCTGA","VNAARGGQATHPTPTRASTSAAQNLSPAYPRRAAWGTAGSLRAWQAAALAQYLETMPQDFLAVATPGAGKTTFALRVATELLSSADVHKVTIVCPTEHLKYQWAEAAARVGIHIDPSYSNSQGALGSRFDGVALTYAQVAANANLHRARTDQARTLVILDEIHHGGDALSWGDAIREAFTPARRRLALTGTPFRSDTSPIPFVRYKEDASGAKRSQADYSYGYSDALRDGVVRPVMFMSYSGQMRWRTKAGDEVAARLGEPLTKDLESQAWRTALDPAGEWIPAVLAAADQRLTEVRRQVPDAGALVIASDQAKARAYAKQLRAITGEAPTVVLSDDNGASSRIEAFSASTDRWLVAVRMVSEGVDVPRLAVGVYATSTSTPLFFAQAVGRFVRSRARGETASVFLPSVTPLLALAGEMEVARDHVLSRPDSAAQEDALFSPEDRLLAEANKTENASAELLPGFEAMDSQAEFDRVLFDGGEFGTGAMVGSIEEQEYLGLPGLLEPEQVTALLRQRQDKQIASQKKQAAAEAQRRKNSGVDDARRRAAARKELSQLVAAWARRSSQPHGVVHNELRRVCGGPEVAAASTEEIEKRIQTLRRWFVGKR$","DNA or RNA helicase of superfamily II","Cytoplasm, Periplasm","SdrA","hypothetical protein","type III restriction enzyme, res subunit","","Gorbalenya A.E., Koonin E.V., Donchenko A.P., Blinov V.M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989. 17(12):4713-4730. PMID: 2546125","","","

InterPro
IPR006935
Family

Type III restriction enzyme, res subunit
PF04851	$\"[38-194]T$	ResIII

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[37-216]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[51-210]T$	HELICASE_ATP_BIND_1

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 21-114 are similar to a (HELICASE ATP-BINDING HYDROLASE TRANSCRIPTION ATP-DEPENDENT RNA ACTIVATOR REGULATION SUBUNIT HEPA) protein domain (PD040095) which is seen in Q6AF06_BBBBB.Residues 61-272 are 43% similar to a (HELICASE DOMAIN C-TERMINAL) protein domain (PD911672) which is seen in Q7U8D2_SYNPX.Residues 63-458 are 34% similar to a (ENDONUCLEASE NHN PLASMID) protein domain (PD849979) which is seen in Q82YG2_STRAW.Residues 115-215 are similar to a (ATP-BINDING HELICASE RNA SDRA OR DNA VPA1393 II SUPERFAMILY SCO2936) protein domain (PD942943) which is seen in Q73VM8_MYCPA.Residues 219-395 are similar to a (HELICASE ATP-BINDING RNA SDRA OR DOMAIN DNA VPA1393 II SUPERFAMILY) protein domain (PD784757) which is seen in Q6AF06_BBBBB.Residues 219-264 are 68% similar to a (HELICASE RNA) protein domain (PDA0D978) which is seen in Q6A9B5_PROAC.Residues 247-279 are 90% similar to a (ATP-BINDING SDRA SCO2936) protein domain (PD883298) which is seen in Q9S3Y6_STRCO.Residues 396-491 are 67% similar to a (ATP-BINDING HELICASE RNA SDRA OR DNA II SUPERFAMILY SCO2936 ALANINE) protein domain (PD839029) which is seen in Q6AF06_BBBBB.Residues 551-602 are 69% similar to a (ATP-BINDING SDRA HELICASE OR RNA DNA II SUPERFAMILY SCO2936 ALANINE) protein domain (PD839024) which is seen in Q6NGU2_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 38 to 194 (E_value = 2.1e-07) place ANA_0351 in the ResIII family which is described as Type III restriction enzyme, res subunit.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0352","375441","374029","1413","5.19","-14.92","49083","GTGAACAGCTACGCGCCCTCTACCGATTCCACCGCCGCCTCCATGGACGTGTCGGCGGCCTCAACCTCCCTGCTGACCGACATGTACGAGCTCACGATGCTGCAAGGAGCACTGGCATCGGGGGCCGCCTCACGGCGCAGCGTCTTCGAGCTCTTCGGCCGCAGTTTGCCCGGGTCGCGCCGCTTCGGTGTCGTCGCAGGCACCGGTCGGCTGCTGGACGCCGTCGAGGCCTTCACATTCACCGCCGCCCAGATCGACTTCCTGCACCGCACCGAGGTCGTCAACGACGAGACCCTGGACTTCCTGCGCGACTACCGCTTCTCCGGGACGATCCGCGGCTACGCCGAGGGCGAGTGCTACTTCGCCGGTTCCCCGCTGCTAACCGTGGAAGGCACATTCGCAGAGGCCTGCATCCTGGAGACCCTGGCCCTGTCGATCTACAACTACGACTGCGCCGTCGCCGCAGCCGCCTCCCGCATGACTATCGCCGCCCACGGGCGTCCTTGTGTGGACTTCGGGGCGCGCCGAGCCCACGAGCAGGCGGCCGTCGCCGCGGCCAGGGCCTCGGTCGTCGGTGGTTTCGTGGGAACGAGCAACCTGGAGGCGGGGCTCCTCTACGGCATTCCCACGGTGGGGACGTCGGCCCACTCCTTCACCCTCCTGCACGACACCGAGGAGGAGGCCTTCGCCGCGCAGGTGGCCAGCCTTGGACCGAGCACCACGATCCTGGTGGACACCTACGACATCGCCACCGGCGTGGAGCGGGCGGTCAAGGCGGCCCGCGCCGCAGGCGGTGAGCTCGGGGCGGTGCGCCTGGACTCCGGTGACCTGGTGGCCGAGGCCTTCAAGGTGCGCGCCCAGCTCGACGCCCTGGGGGCGACCTCGACGAGGATCACCGTCACCAACGACCTCGACGAGCACGCCATCGCGGCGCTGGGAGCGGCCCCCGTGGACTCCTACGGCGTGGGCACCAAGCTCGTGACGGGCTCGGGGCGCCCGACCGCGGCACTCGTCTACAAGCTGGTGGAGCGCGAGGGCGCCGACGGCACCATGGAGGAGGTCGCCAAGTTCTCCTCGGGCGGCAAGTCCACCGTGGGCGGCCGCAAGTGGGCCGGCCGCATCCTGACCCCCGAGGGCACGGCCGCCGAGGAGCTTGTGGTCGCCTCCAGCTCGCAGGATGAGGGGATGTCGGCGTTGAGCCAGGCCGGTGCCCGGCCGCTTCAGGTGCTTCTGGTCGATGAGGGCCGGATCGTCGAGGAGCACCGCGGCAAGGAGGCCTTGAGCGCCGCGGCGGAGCGGCACCGGGCATCGCGCGCCGAGCTCCCCTACGACGCCTGGCGTCTGAGCGACGGCGAGTCGGCGCTGCCAACCCGCCACGTCGACCTCGACGGGCGAGGCGCCACCCGACGCTGA","VNSYAPSTDSTAASMDVSAASTSLLTDMYELTMLQGALASGAASRRSVFELFGRSLPGSRRFGVVAGTGRLLDAVEAFTFTAAQIDFLHRTEVVNDETLDFLRDYRFSGTIRGYAEGECYFAGSPLLTVEGTFAEACILETLALSIYNYDCAVAAAASRMTIAAHGRPCVDFGARRAHEQAAVAAARASVVGGFVGTSNLEAGLLYGIPTVGTSAHSFTLLHDTEEEAFAAQVASLGPSTTILVDTYDIATGVERAVKAARAAGGELGAVRLDSGDLVAEAFKVRAQLDALGATSTRITVTNDLDEHAIAALGAAPVDSYGVGTKLVTGSGRPTAALVYKLVEREGADGTMEEVAKFSSGGKSTVGGRKWAGRILTPEGTAAEELVVASSSQDEGMSALSQAGARPLQVLLVDEGRIVEEHRGKEALSAAAERHRASRAELPYDAWRLSDGESALPTRHVDLDGRGATRR$","Nicotinate phosphoribosyltransferase","Cytoplasm","nicotinate phosphoribosyltransferase, putative","nicotinate phosphoribosyltransferase","putative nicotinate phosphoribosyltransferase","","","","","

InterPro
IPR006405
Family

Nicotinate phosphoribosyltransferase related
TIGR01513	$\"[23-460]T$	NAPRTase_put: putative nicotinate phosphori

InterPro
IPR007229
Family

Nicotinate phosphoribosyltransferase and related
PTHR11098:SF1	$\"[1-420]T$	NICOTINATE PHOSPHORIBOSYLTRANSFERASE
PF04095	$\"[167-367]T$	NAPRTase

noIPR
unintegrated

unintegrated
G3DSA:3.20.140.10	$\"[24-390]T$	no description
PTHR11098	$\"[1-420]T$	NICOTINATE PHOSPHORIBOSYLTRANSFERASE

","BeTs to 13 clades of COG1488COG name: Nicotinic acid phosphoribosyltransferaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1488 is ao-pkzyqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB007229 (Nicotinate phosphoribosyltransferase and related) with a combined E-value of 5.5e-52. IPB007229A 19-53 IPB007229B 131-149 IPB007229C 166-179 IPB007229D 194-225 IPB007229E 267-298 IPB007229F 320-329","Residues 33-97 are 73% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE NICOTINATE PHOSPHORIBOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE-LIKE PHOSPHORIBOSYLTRANSFERASE ACID NICOTINIC Y54G2A.17 PROTEIN) protein domain (PD289342) which is seen in Q9S2G4_STRCO.Residues 116-171 are 82% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE NICOTINATE PHOSPHORIBOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE-LIKE PHOSPHORIBOSYLTRANSFERASE NICOTINIC ACID Y54G2A.17 RIKEN) protein domain (PD008895) which is seen in Q6A753_PROAC.Residues 197-229 are 90% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE NICOTINATE PHOSPHORIBOSYLTRANSFERASE BIOSYNTHESIS NUCLEOTIDE NAPRTASE PYRIDINE PHOSPHORIBOSYLTRANSFERASE-LIKE ACID) protein domain (PD427103) which is seen in Q6A753_PROAC.Residues 236-342 are 78% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE NICOTINATE PHOSPHORIBOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE-LIKE NICOTINIC ACID PHOSPHORIBOSYLTRANSFERASE PROTEIN RIKEN) protein domain (PD468412) which is seen in Q6AEK7_BBBBB.","","-50% similar to PDB:2F7F Crystal structure of Enterococcus faecalis putative nicotinate phosphoribosyltransferase, NEW YORK STRUCTURAL GENOMICS CONSORTIUM (E_value = 8.9E_51);-41% similar to PDB:2I14 Crystal structure of nicotinate-nucleotide pyrophosphorylase from Pyrococcus furiosus (E_value = 7.7E_10);","Residues 167 to 367 (E_value = 4.3e-06) place ANA_0352 in the NAPRTase family which is described as Nicotinate phosphoribosyltransferase (NAPRTase) family.","","phosphoribosyltransferase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0353","375480","375809","330","5.42","-4.13","11967","ATGAGCACCTCGTTGCCCGTTGCGGAACCGGAGATCCTGGAGGAGTCGCGCGTCCGTGCCCAGCGCCTGTGGTGCACCGTGGTTCACGACGACCCGGTCAACACGATGAGCTATGTGACCTGGGTGTTCCACTCCTACTTCGGTTTCTCGCTGCCTGTGGCCGAGGCGCGGATGATGCAGGTGCACACCGCCGGCCGTGCCGTGGTCTCCCGGGGAGCCCGCGAGCGCATGGAGGTCGATGTCACGGCGATGCACGGATACGGCCTGCGCGCCACCATCGAGCCCGTGGGTGACGACGCCGGTGCTGACGACTCTTCAGGAGGGCGCTGA","MSTSLPVAEPEILEESRVRAQRLWCTVVHDDPVNTMSYVTWVFHSYFGFSLPVAEARMMQVHTAGRAVVSRGARERMEVDVTAMHGYGLRATIEPVGDDAGADDSSGGR$","ATP-dependent Clp protease adaptor protein clpS","Cytoplasm, Extracellular","ATP-dependent Clp protease adaptor protein clpS","ATP-dependent Clp protease adaptor protein ClpS","ATP-dependent Clp protease adaptor protein ClpS","","Guo F., Esser L., Singh S.K., Maurizi M.R., Xia D. Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA. J. Biol. Chem. 2002. 277(48):46753-46762. PMID: 12235156Uchiumi T., Hori K., Nomura T., Hachimori A. Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding. J. Biol. Chem. 1999. 274(39):27578-27582. PMID: 10488095Dougan D.A., Reid B.G., Horwich A.L., Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 2002. 9(3):673-683. PMID: 11931773","","","

InterPro
IPR003769
Domain

Adaptor protein ClpS, core
PF02617	$\"[18-93]T$	ClpS

InterPro
IPR014719
Domain

Ribosomal protein L7/L12, C-terminal/adaptor protein ClpS-like
G3DSA:3.30.1390.10	$\"[16-96]T$	no description

","BeTs to 7 clades of COG2127COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2127 is ---------dr--cefg-snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003769 (Protein of unknown function DUF174) with a combined E-value of 5.8e-14. IPB003769 30-80","Residues 24-94 are similar to a (PROTEASE CLPS CLP ATP-DEPENDENT ADAPTOR DUF174) protein domain (PD624753) which is seen in CLPS_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 93 (E_value = 7.7e-21) place ANA_0353 in the ClpS family which is described as ATP-dependent Clp protease adaptor protein ClpS.","","Clp protease adaptor protein clpS","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0354","375809","376495","687","4.68","-15.31","24822","ATGCGCGCCTTCCGCCGAGTCCCCGAGGGACTGGTCTGCGGTCTCGACGACTGGGAGCGCGAGCTGCTGGCCAGGCTGGCCCTGGAGGTGAGGGCCCTTCTCCAGGCGGATGCTCCCCCCACCCAGGGGGCCGGTCAGCCCGAGGCATCCTTATCGCCGCGCCCCGAGTCGGTGCGCCCGGGGGAGAGCGAGCGGGACCGTGAGGTCCTGGAGGCCCTGGACTTCGACCTCGATGCGCCGACCAACCGCGTTCACGTCGGCAGCCCGAGCGCGGACCCTGTTATCGCTGTCCTGCTCCCGCAGGCCTCGGAGGATCCCATCACCTCGATGGAGGTCAGCAGCCTGACTCGCGCGCGCCTGCGGGGTGACAAGGTCGACCGCCTGGCGCGCCTGGCCGCCGAGCTGCGGGCGCCGTCGGGCCCTGAGGGAACGGTGCTTGTGGCCCCGGGCCAGGAGTCCGACTGGCTGGGGGCGAGCAATGATATCCGGCTCGTGCTGGCCCAGCGCCTGGGCATCGAGTCGGCTCAGGATGCCGAGCACGTTCACTCCGTCGCCTTCCAGGAGGCCCCCGAGGAGGAGACGTCTCGCGAGCAGTGGTACCGGGGGACGGCGCTCGTCTACGACATGATCACCTGGTGGCAGGAATCACTGATATCCGCGCTGTTCGGGGGCACAGGGCCCGCATAG","MRAFRRVPEGLVCGLDDWERELLARLALEVRALLQADAPPTQGAGQPEASLSPRPESVRPGESERDREVLEALDFDLDAPTNRVHVGSPSADPVIAVLLPQASEDPITSMEVSSLTRARLRGDKVDRLARLAAELRAPSGPEGTVLVAPGQESDWLGASNDIRLVLAQRLGIESAQDAEHVHSVAFQEAPEEETSREQWYRGTALVYDMITWWQESLISALFGGTGPA$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0355","376505","377389","885","5.26","-9.42","30845","GTGAATGATGCTCCGATCGGGATGTTCGACTCTGGGGTCGGTGGCCTCACCGTCGCCCGTTCTGTCCTCGACCAACTGCCCCAAGAGCAGGTGCTGTACATCGGGGACACGGCCAACAGTCCCTACGGTCCCCGGGACATCGCTGAGGTCCGGTCCCTGGCTCTGGGCATCATGGACGAGCTCGTGGACCGCGGGGTCAAGCTGCTCGTCATCGCCTGCAACACCGCCTCGGCGGCGGTCCTGCATGATGCGCGGGAGCGCTACACCCTGGGGCGGGGCGTCCCGGTCATCGAGGTCATCCACCCGGCGGCACGTACCGCGGCCCGAGTGACCCGCAACGGCAAGGTGGGGCTGATCGCCACCCGCGGGACGGTCGACTCGCGCGCTTACGACGACGCCCTCCAGGCCGTTCCCGGCGTCGAGCTCGTCTCACAGGCGTGCCCGCGCTTCGTCGAGCTGGCCGAGCGGGGGGTGACTACCGGCCCCGAGGTGCTCGACGTCGCCGAGGAGTACCTGGCCCCCATCAAGGCCGCAGGCGTGGACACCCTCATCCTCGGCTGCACCCACTACCCACTGCTGGTGGGGCCGATCTCCTACGTCATGGGGCGGGACGTGACCCTGGTGACCTCCTCGGACGAGACCGCCAAGGACGTCTACCGGGCGCTGGCCGGCAAGAACCTTCTGCGTGGTCCCGATGCCCCTGAACCGCGCCATGACTTCGCCTCCACTGGTGATCCCGAGGCATTCTCCGTCCTGGCCCGGCGTTTCCTGGGGCCCGAGGTCACTGCCGTTGAGCACGTCGCCTTCTCCTCTGAGACAGCCGGCGCCCCTGCCGGGTTGCCTCACCCTCCCTCACCTCCCACCTCCCATCAAGGAACTGCATGA","VNDAPIGMFDSGVGGLTVARSVLDQLPQEQVLYIGDTANSPYGPRDIAEVRSLALGIMDELVDRGVKLLVIACNTASAAVLHDARERYTLGRGVPVIEVIHPAARTAARVTRNGKVGLIATRGTVDSRAYDDALQAVPGVELVSQACPRFVELAERGVTTGPEVLDVAEEYLAPIKAAGVDTLILGCTHYPLLVGPISYVMGRDVTLVTSSDETAKDVYRALAGKNLLRGPDAPEPRHDFASTGDPEAFSVLARRFLGPEVTAVEHVAFSSETAGAPAGLPHPPSPPTSHQGTA$","Glutamate racemase","Cytoplasm","glutamate racemase","glutamate racemase ","glutamate racemase","","Gallo K.A., Knowles J.R. Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus. Biochemistry 1993. 32(15):3981-3990. PMID: 8385993","","","

InterPro
IPR001920
Family

Asp/Glu racemase
PF01177	$\"[5-223]T$	Asp_Glu_race
PS00923	$\"[70-78]T$	ASP_GLU_RACEMASE_1
PS00924	$\"[183-193]T$	ASP_GLU_RACEMASE_2

InterPro
IPR004391
Family

Glutamate racemase
TIGR00067	$\"[4-259]T$	glut_race: glutamate racemase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1860	$\"[4-153]T$	no description
PTHR21198	$\"[2-277]T$	GLUTAMATE RACEMASE

","BeTs to 13 clades of COG0796COG name: Glutamate racemaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0796 is -------q-drlbcefgh-nuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB001920 (Asp/Glu racemase) with a combined E-value of 3.9e-36. IPB001920A 6-36 IPB001920B 64-81 IPB001920C 116-125 IPB001920D 181-197","Residues 5-100 are 83% similar to a (GLUTAMATE RACEMASE ISOMERASE WALL PEPTIDOGLYCAN SYNTHESIS CELL ASPARTATE RACEMASES:GLUTAMATE MURI) protein domain (PD004303) which is seen in MURI_CORGL.Residues 102-163 are 74% similar to a (GLUTAMATE RACEMASE ISOMERASE WALL PEPTIDOGLYCAN SYNTHESIS CELL ASPARTATE RACEMASES:GLUTAMATE HP0549) protein domain (PD004566) which is seen in Q6A758_PROAC.Residues 171-257 are 76% similar to a (GLUTAMATE RACEMASE ISOMERASE WALL PEPTIDOGLYCAN SYNTHESIS CELL MURI ASPARTATE RACEMASES:GLUTAMATE) protein domain (PD086961) which is seen in MURI_CORGL.","","-61% similar to PDB:1ZUW Crystal structure of B.subtilis glutamate racemase (RacE) with D-Glu (E_value = 4.4E_52);-58% similar to PDB:1B73 GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS (E_value = 5.3E_37);-58% similar to PDB:1B74 GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS (E_value = 5.3E_37);","Residues 5 to 223 (E_value = 3.2e-83) place ANA_0355 in the Asp_Glu_race family which is described as Asp/Glu/Hydantoin racemase.","","racemase (murI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0357","377386","378183","798","4.75","-16.98","27853","ATGAGACTCACGATCATCGGATGCTCCGGCTCCATGTCGGGCCCCCAGTCCTCGGCCTCCTCCTACCTGGTGCAGGCCGACGGAGTCGACGCCGACGGCGCGGTGCGCACCTACTCGATCGTGCTGGACCTCGGGCCCGGGTCGATGGGGCAGCTGCTGCGCCACCTCGATCCCGCCGAGCTCGACGCCATTGCGATCTCCCACTGCCACGCCGATCACATGGTGGACCTGGTGGGCATGCACGTCTACCGACGCTGGCTGCCCACCGGGGCGCTCGGGCCGGTGGCCTGCCTGGGGCCCTCGGAGCTGCTGGAGCGCCTCCAGGGGGTCGACGGCGTCCCGCCCAGTGAGCGCTACGCCACGGAATTCGGCTTCGTCACCGCCGTACCCGGCCGGTCCTACAGTGTGGGCCCCCTCGTGATCTCCCCCTTCGAAGCGCTCCACCCCGTGGAGGCCTACGGCTACCGGATCGAGGGCCCCAGCGAGGAGGATCCCTCCCGGCAGGTCAGCCTGGCCTTCACCGGGGACACTGATATCTGCCAGACGATGAGCGACATGGCTCAGGGCGTGGACCTCCTCCTGGCCGAGGCGGCCTTCGTCGAGGGCCGCGACACCGTGGGCGGCATGCACATGACGGGGCGTCGCGCCGGCGAGCTCGCCGCTCAGGCCGGTGCGGGGCACCTGGTCCTCACCCATATCCAGCCCTGGACGGATCCGGCCGTGCCCCTCAAGGAGGCCGCAGCCGTCTACTCCGGCCCGTTGGAGGCAGCGACGGCGGACGCCGTCTGGGAGCTGTGA","MRLTIIGCSGSMSGPQSSASSYLVQADGVDADGAVRTYSIVLDLGPGSMGQLLRHLDPAELDAIAISHCHADHMVDLVGMHVYRRWLPTGALGPVACLGPSELLERLQGVDGVPPSERYATEFGFVTAVPGRSYSVGPLVISPFEALHPVEAYGYRIEGPSEEDPSRQVSLAFTGDTDICQTMSDMAQGVDLLLAEAAFVEGRDTVGGMHMTGRRAGELAAQAGAGHLVLTHIQPWTDPAVPLKEAAAVYSGPLEAATADAVWEL$","Metal-dependent hydrolase of the beta-lactamase superfamily III","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","Metal-dependent hydrolase of the beta-lactamase superfamily III-like","","Carfi A., Pares S., Duee E., Galleni M., Duez C., Frere J.M., Dideberg O. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 1995. 14(20):4914-4921. PMID: 7588620","","","

InterPro
IPR001279
Domain

Beta-lactamase-like
PF00753	$\"[18-74]T$	Lactamase_B

noIPR
unintegrated

unintegrated
G3DSA:3.60.15.10	$\"[1-265]T$	no description
PTHR12553	$\"[39-264]T$	RIBONUCLEASE Z
PTHR12553:SF7	$\"[39-264]T$	ARYLSULFATASE

","BeTs to 13 clades of COG1234COG name: Metal-dependent hydrolases of the beta-lactamase superfamily IIIFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1234 is aompkzy-vdrlbce--h---j-it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 123-204 are 52% similar to a (ENDONUCLEASE Z TRNA HYDROLASE ZINC RIBONUCLEASE RNASE METAL-BINDING PROCESSING NUCLEASE) protein domain (PD352433) which is seen in Q82D21_STRAW.Residues 210-264 are similar to a (HYDROLASE TRNA ENDONUCLEASE Z METAL-DEPENDENT RNASE RIBONUCLEASE ZINC PERIPLASMIC ARYLSULFATASE) protein domain (PD430307) which is seen in Q9S2H3_STRCO.","","-42% similar to PDB:1ZKP 1.5A Resolution Crystal Structure of a Metallo Beta Lactamase Family Protein, the ELAC Homolgue of Bacillus anthracis, a Putative Ribonuclease (E_value = 5.8E_16);-43% similar to PDB:2CBN CRYSTAL STRUCTURE OF ZIPD FROM ESCHERICHIA COLI (E_value = 1.4E_14);","Residues 18 to 74 (E_value = 1.6e-06) place ANA_0357 in the Lactamase_B family which is described as Metallo-beta-lactamase superfamily.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0358","378180","378710","531","9.70","3.87","19293","GTGAGCGCTGACGGGCACGATCGCCCCGCACCGCGCAGAACGGTCTCCTTCACCCCGGCTCTTCCCGACGGGGTGGACTGCCCCTGGACCCGGGGAAGACGGACGCGTTGGTGGCTGGTGGTTCCCGCCGACCTGGCGGCGGTGGTCCTCGTGGCCCTGTTCGGTGCCGCCTCCACCCGCAGCCTGGGGGAGGTTCCCGCCTCCCTGTGGCAGGCGGGGGCGGCCCTCCTCGTCGCCTGGGGCGTGACCTGGCTCGTGCGGCGCTCTCACCCCGATCACCTGGAGATGGCGCTGCCCGAGGGGCTCATCGTCGTGGGTGTCAGCTGGGTGGTCTGGACCGCGTTGCGCCAGGTGGCATCCGCCTTCGACAACGTGTCCGCCATGGTCTCCTGGGCGGTGATGACCGGGGCCTTCCTCCTGGTGTTCCTGGGCGGATGGAGATGGCTCTACGGCTACGTGCGCGCCCACGACTCCCTGACCCCCAAGCCCGTGGCGCGGCGCCTCGCCGAGCAGGAGAGGGAGTCCAGCTAG","VSADGHDRPAPRRTVSFTPALPDGVDCPWTRGRRTRWWLVVPADLAAVVLVALFGAASTRSLGEVPASLWQAGAALLVAWGVTWLVRRSHPDHLEMALPEGLIVVGVSWVVWTALRQVASAFDNVSAMVSWAVMTGAFLLVFLGGWRWLYGYVRAHDSLTPKPVARRLAEQERESS$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[38-60]?$ $\"[66-86]?$ $\"[101-121]?$ $\"[127-149]?$	transmembrane_regions

InterPro
IPR002637
Family

Ham1-like protein
PTHR11067	$\"[23-234]T$	INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN
PF01725	$\"[25-229]T$	Ham1p_like
TIGR00042	$\"[24-230]T$	TIGR00042: non-canonical purine NTP pyropho

noIPR
unintegrated

unintegrated
G3DSA:3.90.950.10	$\"[24-234]T$	no description
PTHR11067:SF1	$\"[23-234]T$	HAM1 PROTEIN-RELATED

","BeTs to 23 clades of COG0127COG name: Xanthosine triphosphate pyrophosphataseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0127 is aompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB002637 (Ham1-like protein) with a combined E-value of 7.2e-27. IPB002637A 24-37 IPB002637B 91-114 IPB002637C 171-216","Residues 24-222 are 69% similar to a (HYDROLASE HAM1 HOMOLOG TRIPHOSPHATE PYROPHOSPHATASE FAMILY XANTHOSINE NUCLEOSIDE-TRIPHOSPHATASE RIBOSOMAL INOSINE) protein domain (PD218601) which is seen in HAM1_STRCO.","","-55% similar to PDB:1K7K crystal structure of RdgB- inosine triphosphate pyrophosphatase from E. coli (E_value = 1.8E_34);-46% similar to PDB:1VP2 Crystal structure of Putative Xanthosine triphosphate pyrophosphatase/HAM1 protein homolog (TM0159) from Thermotoga maritima at 1.78 A resolution (E_value = 5.0E_21);-50% similar to PDB:1V7R Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3 (E_value = 1.8E_10);","Residues 25 to 229 (E_value = 4.5e-63) place ANA_0360 in the Ham1p_like family which is described as Ham1 family.","","purine NTP pyrophosphatase, rdgB-HAM1 family (rdgB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0361","381082","380276","807","5.90","-3.91","28366","ATGACAACTGCCCCCTTCACCCGCAAGGACGGCCGCGCCGTCGACGAGTTGCGTCCTGTGACCATGACCCGCCACTGGCTCGACCACGCCGAGGGATCGGTCCTGGTGACCTTCGGGCGCACCCGGGTCCTGTGCGCCGCCTCCTTCACTGAGGGCGTCCCGCACTGGCGCAAGGGCAGTGGCGAGGGCTGGGTGACCGCCGAGTACGCCATGCTCCCCCGGGCCGGCTCGGAGCGCTCCGGCCGGGAGTCCGTGAGGGGCAAGGTCGGCGGCCGCACCCACGAAATCTCCCGCCTCATCGGCCGCAGCCTGCGCGGCATCATCGACGTCGCCGCACTGGGTGAGAACACGATCGCCCTGGACTGCGACGTGCTGCAGGCCGACGGCGGCACCCGCACCGCGGCGATCACCGGCGCCTACGTGGCCCTGGCCGACGCCGTCGCCTGGGGCACGCAGCGCGGCCTCATCAAGGCCCGCCCCGGCAGGCCCGTGCTCTCCGACTCCCTGTCGGCCATCTCGGTGGGGATCATCGACGGCGTTCCCTGCCTCGACCTGCCCTACGAGGAGGACGTGCGCGCCCAGACCGATATGAATGTCGTCCAGACCGGGGACGGGCGCTTCATCGAGGTTCAGGGCACCGCCGAGCATGCCCCCTTCGACCGCTCCGAGCTCGGAGAGCTGCTCGACCTGGCCGCCACCGGCAACAGCCGTCTGGCGGCGCTCCAGCGCCAGGCCCTAGCCGGCCCCAGCGGTGAGCCCTTCACCGTGTCCTCGGCGGACTCCTCGCCCCAGTCCACGCAGGCCTGA","MTTAPFTRKDGRAVDELRPVTMTRHWLDHAEGSVLVTFGRTRVLCAASFTEGVPHWRKGSGEGWVTAEYAMLPRAGSERSGRESVRGKVGGRTHEISRLIGRSLRGIIDVAALGENTIALDCDVLQADGGTRTAAITGAYVALADAVAWGTQRGLIKARPGRPVLSDSLSAISVGIIDGVPCLDLPYEEDVRAQTDMNVVQTGDGRFIEVQGTAEHAPFDRSELGELLDLAATGNSRLAALQRQALAGPSGEPFTVSSADSSPQSTQA$","Ribonuclease PH","Cytoplasm","ribonuclease PH","ribonuclease PH ","ribonuclease PH","","Kelly K.O., Deutscher M.P. Characterization of Escherichia coli RNase PH. J. Biol. Chem. 1992. 267(24):17153-17158. PMID: 1512253","","","

InterPro
IPR001247
Domain

Exoribonuclease
PF01138	$\"[16-149]T$	RNase_PH
PF03725	$\"[167-234]T$	RNase_PH_C

InterPro
IPR002381
Family

Ribonuclease PH
TIGR01966	$\"[8-247]T$	RNasePH: ribonuclease PH
PS01277	$\"[122-135]T$	RIBONUCLEASE_PH

noIPR
unintegrated

unintegrated
PTHR11953	$\"[8-146]T$	RIBONUCLEASE PH RELATED

","BeTs to 16 clades of COG0689COG name: RNase PHFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0689 is a-mpkzyq-dr-b-efghsn-jx---Number of proteins in this genome belonging to this COG is 1","***** IPB002381 (Ribonuclease PH) with a combined E-value of 6.7e-118. IPB002381A 8-46 IPB002381B 47-70 IPB002381C 88-142 IPB002381D 169-210","Residues 12-69 are similar to a (PH RIBONUCLEASE NUCLEOTIDYLTRANSFERASE TRANSFERASE TRNA RNASE PROCESSING) protein domain (PDA1E2N1) which is seen in Q8DLA4_SYNEL.Residues 12-47 are 77% similar to a (PH NUCLEOTIDYLTRANSFERASE TRNA RIBONUCLEASE TRANSFERASE RNASE PROCESSING EXONUCLEASE EXOSOME HYDROLASE) protein domain (PD186441) which is seen in RNPH_RALSO.Residues 71-116 are similar to a (PH NUCLEOTIDYLTRANSFERASE TRNA RIBONUCLEASE TRANSFERASE RNASE PROCESSING PROBABLE HYDROLASE 3D-STRUCTURE) protein domain (PD858583) which is seen in Q8G7I0_BIFLO.Residues 117-146 are similar to a (PH NUCLEOTIDYLTRANSFERASE TRNA RIBONUCLEASE TRANSFERASE RNASE PROCESSING PROBABLE HYDROLASE 3D-STRUCTURE) protein domain (PDA0X5G8) which is seen in RNPH_MYCTU.Residues 160-197 are 81% similar to a (PH NUCLEOTIDYLTRANSFERASE TRNA RIBONUCLEASE TRANSFERASE RNASE PROCESSING HYDROLASE PROBABLE 3D-STRUCTURE) protein domain (PD592123) which is seen in Q8FMU8_COREF.Residues 198-235 are similar to a (PH NUCLEOTIDYLTRANSFERASE TRNA RIBONUCLEASE TRANSFERASE RNASE PROCESSING PROBABLE HYDROLASE 3D-STRUCTURE) protein domain (PD709796) which is seen in Q8G7I0_BIFLO.","","-73% similar to PDB:1R6L Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa (E_value = 3.8E_71);-73% similar to PDB:1R6M Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa In Complex With Phosphate (E_value = 3.8E_71);-74% similar to PDB:1UDN Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus (E_value = 2.8E_66);-73% similar to PDB:1UDQ Crystal structure of the tRNA processing enzyme RNase PH T125A mutant from Aquifex aeolicus (E_value = 1.1E_65);-73% similar to PDB:1UDO Crystal structure of the tRNA processing enzyme RNase PH R86A mutant from Aquifex aeolicus (E_value = 1.4E_65);","Residues 16 to 149 (E_value = 1.2e-44) place ANA_0361 in the RNase_PH family which is described as 3' exoribonuclease family, domain 1.Residues 167 to 234 (E_value = 1.1e-15) place ANA_0361 in the RNase_PH_C family which is described as 3' exoribonuclease family, domain 2.","","PH (rph)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0362","381236","381529","294","5.55","-2.57","11233","ATGACCTATGTCAACATCACCGCACTGACCTTCCCCGAGGGCGCCCAGGCCGAGATCGAGAAGCGCTTCGCCGCCCGGAAGCGAGGCGTTGACACCTCACAGGGCTTTCAGGGCTTCGAGCTGCTGCGCCCGCTGGTCGGAGAGGACCGCTACTTCGTGGTGACCCGGTGGGACAGGCGCGAGGACTACGAGCGCTGGAGCGCGGCGCGGCCCGCCGGCGGGCACGAGGACGACAAGCGCCGAGGCATGAGCGTGGAGGTCCTCGGCTTCGAGGTCGTCCAGCACGAGGAGTGA","MTYVNITALTFPEGAQAEIEKRFAARKRGVDTSQGFQGFELLRPLVGEDRYFVVTRWDRREDYERWSAARPAGGHEDDKRRGMSVEVLGFEVVQHEE$","Antibiotic biosynthesis monooxygenase","Cytoplasm","Uncharacterized enzyme involved in biosynthesisof extracellular polysaccharides","hypothetical protein","Antibiotic biosynthesis monooxygenase","","Sciara G., Kendrew S.G., Miele A.E., Marsh N.G., Federici L., Malatesta F., Schimperna G., Savino C., Vallone B. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis. EMBO J. 2003. 22(2):205-215. PMID: 12514126","","","

InterPro
IPR007138
Domain

Antibiotic biosynthesis monooxygenase
PF03992	$\"[11-74]T$	ABM

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.900	$\"[2-93]T$	no description

","BeTs to 6 clades of COG2329COG name: Uncharacterized enzyme involved in biosynthesis of extracellular polysaccharidesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2329 is -o-p-z---dr-b--f-----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 3-57 are similar to a (TB11.2 ENZYME YHGC INVOLVED UNCHARACTERIZED EXTRACELLULAR BIOSYNTHESIS POLYSACCHARIDES TRAP DR0272) protein domain (PD901134) which is seen in Q8NMA1_CORGL.Residues 58-96 are similar to a (ENZYME INVOLVED UNCHARACTERIZED EXTRACELLULAR BIOSYNTHESIS POLYSACCHARIDES) protein domain (PDA108W3) which is seen in Q8NMA1_CORGL.","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 74 (E_value = 5e-08) place ANA_0362 in the ABM family which is described as Antibiotic biosynthesis monooxygenase.","","enzyme involved in biosynthesis of extracellular polysaccharides","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0363","381711","382343","633","8.00","1.37","22831","ATGAGAAGTAAGGAGGCGAGCCACGTGGGAGTCGATACCGGACGAGTTCGTCAGATGAGCGAGCAGCTGCGTAGCACCGGGATGCTCGTTATTCCGGAGTCCCCGATGCGTCTCTGGGGAAGCCTTCTGGGCTGCGTCGGCTTCACCGCGCTGGGGGTCGGGATCATTCTGATCGCGAATCAGTCGAGCTCCCCGCTCCTCTACATTCTCGCTGGCATCGCCTGTATCGGTTTCTTCGGCGTCATCGGTATCCCCGGCATGATGAGGAAGATCATCCTCCGCAGTCGGCTGGTGGTGACGTCTGAGGGGCTGCGTCTGGAACGGCGCAACATCGTCAATGAGTCGGCACGCTGGGCGGATATCGCCGAGTTCTTCGGGCAGGAAGTCACTCCCGACAGTGGCACACAAGCACAGCTGGTGATCGGCTACACCCTGACGCCGTTGGGACAGCAGATGCGCCGTCAGGACGCGACCACCGCCCAGCTGGGCCAGCAGATCAATGAGGTTGCCGACCGTGGGATGGGCAAGGAGGAGCGCGTCTACCTTCCTGCCACCTTGGAGGGCAGTAAGGAGGACCTGCTGGTCCTGCTTCAACAGGCGCACCAGTTCTACAGCGCACCGGGTGGCGTCTAG","MRSKEASHVGVDTGRVRQMSEQLRSTGMLVIPESPMRLWGSLLGCVGFTALGVGIILIANQSSSPLLYILAGIACIGFFGVIGIPGMMRKIILRSRLVVTSEGLRLERRNIVNESARWADIAEFFGQEVTPDSGTQAQLVIGYTLTPLGQQMRRQDATTAQLGQQINEVADRGMGKEERVYLPATLEGSKEDLLVLLQQAHQFYSAPGGV$","Hypothetical protein","Cytoplasm, Membrane","","","","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[38-60]?$ $\"[66-86]?$	transmembrane_regions

InterPro
IPR000866
Domain

Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
PF00578	$\"[6-138]T$	AhpC-TSA

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[4-147]T$	no description

noIPR
unintegrated

unintegrated
PTHR10681	$\"[1-158]T$	PEROXIREDOXIN
PTHR10681:SF5	$\"[1-158]T$	BACTERIOFERRITIN COMIGRATORY PROTEIN

","BeTs to 18 clades of COG1225COG name: PeroxiredoxinFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1225 is -o-p-zyqvdr-bcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000866 (Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen) with a combined E-value of 6.8e-11. IPB000866A 33-52 IPB000866B 70-84","Residues 2-76 are 57% similar to a (KINASE BIOSYNTHESIS SIMILAR CBK1P SERINE/THREONINE-PROTEIN ATP-BINDING TRANSFERASE WALL CELL) protein domain (PD952568) which is seen in Q75JU5_DICDI.Residues 4-50 are 74% similar to a (PEROXIDASE ANTIOXIDANT PEROXIREDOXIN BACTERIOFERRITIN COMIGRATORY OXIDOREDUCTASE ALKYL REDUCTASE HYDROPEROXIDE THIOREDOXIN) protein domain (PD000498) which is seen in Q7N3G9_PHOLL.Residues 13-111 are 53% similar to a (AHPC/TSA FAMILY) protein domain (PDA0X206) which is seen in Q6MUH8_MYCMS.Residues 19-77 are 65% similar to a (MEROZOITE CAPPING 20H10.090 MCP1) protein domain (PD508137) which is seen in Q871K9_NEUCR.Residues 54-143 are 47% similar to a (YARROWIA CADOT5 LIPOLYTICA CANDIDA E STRAIN SILENCING CHROMOSOME TELOMERIC CLIB99) protein domain (PD897994) which is seen in Q6C5B6_EEEEE.Residues 83-151 are similar to a (PEROXIDASE ANTIOXIDANT BACTERIOFERRITIN PEROXIREDOXIN COMIGRATORY ALKYL REDUCTASE HYDROPEROXIDE OXIDOREDUCTASE THIOREDOXIN) protein domain (PD000721) which is seen in Q8FMW2_COREF.","","-56% similar to PDB:2CX3 Crystal structure of a bacterioferritin comigratory protein peroxiredoxin from the Aeropyrum pernix K1 (form-1 crystal) (E_value = 1.4E_16);-56% similar to PDB:2CX4 Crystal structure of a bacterioferritin comigratory protein peroxiredoxin from the Aeropyrum pernix K1 (form-2 crystal) (E_value = 1.4E_16);-57% similar to PDB:2A4V Crystal Structure of a truncated mutant of yeast nuclear thiol peroxidase (E_value = 6.2E_12);","Residues 5 to 157 (E_value = 1e-17) place ANA_0368 in the Redoxin family which is described as Redoxin.Residues 6 to 138 (E_value = 1.4e-46) place ANA_0368 in the AhpC-TSA family which is described as AhpC/TSA family.","","(bcp) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0369","384956","384600","357","8.83","1.18","12468","GTGCAACCGGCCGCTGCGCCAGAAGTCTTGACCCGCGCACGCCGGCTCGGCAGGTACGTCCTTGCTTCGGCACGTGCTGCGACCCCAGGCCCCTTCGGGCCGACGACGTTGAAGGAAGATGAGGAGATACGTATGACACGCAACATCCACACCATGACCACCATGACGACTCCGGCCACCGGGCCGGCAGCCACTGACGCTCTGGCCGACGAGGCCGCCATCAGGGAGCTGTTCGCCGCCCGCGCGGAGCTCGCCTCTCTGGGGGCAACCACCTCCCCCTCGCGCCTCGAGCGGGCGCTGGAGCGCCTGGAGGCGGCGCAGCAGGCCTCGCGGCAAACACTCGCCCAGGCCGCCTGA","VQPAAAPEVLTRARRLGRYVLASARAATPGPFGPTTLKEDEEIRMTRNIHTMTTMTTPATGPAATDALADEAAIRELFAARAELASLGATTSPSRLERALERLEAAQQASRQTLAQAA$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0372","385991","385479","513","11.90","21.13","18362","GTGAGCTCTCAAACCCGCGGGCCGCGTATCACCGCCGCGCAGCGCTACTGGGCATCCATGGCCGCCATCGTCGTCGGAACCGTTCTTGCCGCAGGCATTCTTGGAGGAACCGTCTCGATACTCACCGGAGCCCGGGCCGGCCGCAGCAGCATGTGGGGCGGCATGGTGGTCGCGCTCATCATGCTGGCGGGCTGGACCCTCGGCACCCGGGTGCGCGACCGCAAGAAGCTCGACCTGCCCCTGTGGCACCGTCTCACCGAGGAGCAGGCGGCCACACTGAAGCAGTACCACCAGTGGTCTCGCACCGGCCGCATCGAGCAGGACGACGACGCCAAGCGCACTTCCGCCGGGCGGAGCGGCCATCGCAGCAGCGGGCGGACCGGCGCTGGCGCATCGAAGACAGCGCCGTCGAGGAGGTCCTCTTCGAGCGGCGCGATGTCGAAACGCGACCGCGCCCGTGCCGCCGACGTGCGCCGTCGCAGGCAAGGCCGCGAGGGCCATTCATCGCACTGA","VSSQTRGPRITAAQRYWASMAAIVVGTVLAAGILGGTVSILTGARAGRSSMWGGMVVALIMLAGWTLGTRVRDRKKLDLPLWHRLTEEQAATLKQYHQWSRTGRIEQDDDAKRTSAGRSGHRSSGRTGAGASKTAPSRRSSSSGAMSKRDRARAADVRRRRQGREGHSSH$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[21-43]?$ $\"[49-69]?$	transmembrane_regions

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[114-323]T$	ATP_GRASP

InterPro
IPR005185
Family

Protein of unknown function DUF307
PIRSF028777	$\"[1-123]T$	Uncharacterised conserved protein
PF03733	$\"[3-59]T$ $\"[67-123]T$	DUF307

noIPR
unintegrated

unintegrated
PS51257	$\"[1-29]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[2-20]?$ $\"[26-46]?$ $\"[56-76]?$ $\"[82-104]?$	transmembrane_regions

","BeTs to 3 clades of COG3304COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG3304 is ----------r---e-gh---j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 70-120 are similar to a (MEMBRANE INTEGRAL YCCF PROTEIN POSSIBLE PREDICTED INNER UNCHARACTERIZED Y2731 TLL0814) protein domain (PD021079) which is seen in Q8FR43_COREF.Residues 70-120 are similar to a (MEMBRANE INTEGRAL YCCF PROTEIN POSSIBLE PREDICTED INNER UNCHARACTERIZED Y2731 TLL0814) protein domain (PD021079) which is seen in Q8FR43_COREF.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 59 (E_value = 1.8e-21) place ANA_0374 in the DUF307 family which is described as Domain of unknown function (DUF307).Residues 67 to 123 (E_value = 1.2e-20) place ANA_0374 in the DUF307 family which is described as Domain of unknown function (DUF307).","","membrane protein (COG3304)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0375","389031","387550","1482","8.43","4.76","52351","ATGGACCCGGTTGCACATCACCGCGAGCCCGCCCCCGCATCGGATACCTCACCCGCCCCTCCCCCTCGGCCCCGGCACGACGGCCCCGAGGATCCGGGAGGCCCCGACAACCAGGGGCGTGTCACCGCGCTGGAACGCCGCATGAACCGACGTCACCTCATGATGATCAGCTTCGGCGGGGTCATCGGCACGGGACTGTTTCTCTCAACCGGCAACACGATCCACCAGGCCGGCCCCTTGGGGACCGTGCTGGCATACTCCATCGGCGCCGTCATCGTCTACCTGGTCATGCTGTGCCTGGGAGAGCTGAGCGTTGCGATGCCCTTCACCGGCGCCTTCCATGTCTACGCCCGCCAGTACCTGGGGCCGGCCACGGGTTTCGTCACTGCCGTCCTGTACTGGCTCACGTGGACGGTCGCCCTGGGAAGTGAGTTCACCGGCGCGGCGATCATCATGTACGGGTGGTTCCCGGGCGTTCCGGTATGGGTGTGGGCGGCCGCCTTCATCGTCCTGGTCCTTGTGCTCAACATGGTCTCGGTCCGGGTCTTCGCCGAGGCAGAGACTGTGCTGTCCGGGATCAAGGTGGCGGCCATCATCGTGTTCATCGCTCTGGGCACGGCCGCAATCGTCGGGCTGCTGCCCTATGAGGGGCACCGCTCGCTCCTGGGGCTGACGAATCTGTACCGGGACGGTCTCTTCCCCAACGGCTTCGGCGCGGTGTTCACCACGATCCTGGCCGTCAACTTCGCTTTCTCCGGCACCGAGCTCATCGGCATCACCGCCGGGGAGGTCGAGGATCCGGGCACCACTGTTCCGCGCGCGATCCGGGCGACCCTGGCCCGACTGGCCATCTTCTTCATCGGCTCAATCATCATCATCGCAGCGCTGATCCCGTGGGAGAAGGCCGGAGTCGAGGAGAGTCCCTTCGTGACGGTCCTGTCCAGAATCGGCGTGCCCTACGCCGGGGGCCTCATGAACATCGTCATTCTGGCTGCGATCCTGTCGGCGGCGAACTCGGGGCTCTACGCCTCGACCCGCATGCTGTGGTCGCTGGCCAATGAGGGCACTCTGCCCAAGGTCCTGGCGCGCACTAATCGCTTCGGGGTGCCTGCCCTGGCGATGGGTCTGTCCATGGTCGGCGGGCTGGCCTCGCTGCTGACCTCGACCTATGCGGCCTCCACGGTCTACCTGGTCCTTGTGTCAGTCTCCGGTCTCGCCGTCGTCCTGGTCTGGGTGGTTATTGCCGCATGCCACCTGTCCTTCCGACGGCGCTGGCTCGCTGAGGGCCGCAGCCTTGAGGACCTGGCCTACCGGGCTCCCGGATATCCGTGGGTCTCGATCGCGGCGCTGGGGCTGTCTATGGCCTCGTGCCTGCTCATCGTCTTCGACCCCGAGCAGCGCGCCGGCCTGGCGATCACCGCCGTCTTCCTCGTGGTCTGCTACGTGGGCTACTGGGGAGTCAACCGCCGCGTCAGCCTGTGA","MDPVAHHREPAPASDTSPAPPPRPRHDGPEDPGGPDNQGRVTALERRMNRRHLMMISFGGVIGTGLFLSTGNTIHQAGPLGTVLAYSIGAVIVYLVMLCLGELSVAMPFTGAFHVYARQYLGPATGFVTAVLYWLTWTVALGSEFTGAAIIMYGWFPGVPVWVWAAAFIVLVLVLNMVSVRVFAEAETVLSGIKVAAIIVFIALGTAAIVGLLPYEGHRSLLGLTNLYRDGLFPNGFGAVFTTILAVNFAFSGTELIGITAGEVEDPGTTVPRAIRATLARLAIFFIGSIIIIAALIPWEKAGVEESPFVTVLSRIGVPYAGGLMNIVILAAILSAANSGLYASTRMLWSLANEGTLPKVLARTNRFGVPALAMGLSMVGGLASLLTSTYAASTVYLVLVSVSGLAVVLVWVVIAACHLSFRRRWLAEGRSLEDLAYRAPGYPWVSIAALGLSMASCLLIVFDPEQRAGLAITAVFLVVCYVGYWGVNRRVSL$","Amino acid transporter","Membrane, Cytoplasm","amino acid transport protein","K03293 amino acid transporter; AAT family","amino acid permease-associated region","","Weber E., Chevallier M.R., Jund R. Evolutionary relationship and secondary structure predictions in four transport proteins of Saccharomyces cerevisiae. J. Mol. Evol. 1988. 27(4):341-350. PMID: 3146645Vandenbol M., Jauniaux J.C., Grenson M. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases. Gene 1989. 83(1):153-159. PMID: 2687114Reizer J., Finley K., Kakuda D., MacLeod C.L., Reizer A., Saier Jr M.H. Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria. Protein Sci. 1993. 2(1):20-30. PMID: 8382989","","","

InterPro
IPR002293
Family

Amino acid/polyamine transporter I
PTHR11785	$\"[42-490]T$	AMINO ACID TRANSPORTER

InterPro
IPR004840
Family

Amino acid permease
PS00218	$\"[77-108]T$	AMINO_ACID_PERMEASE_1

InterPro
IPR004841
Domain

Amino acid permease-associated region
PF00324	$\"[52-485]T$	AA_permease

noIPR
unintegrated

unintegrated
PIRSF006060	$\"[42-493]T$	High-affinity amino acid transporter
PTHR11785:SF22	$\"[42-490]T$	AMINO ACID TRANSPORTER-RELATED
tmhmm	$\"[54-74]?$ $\"[84-106]?$ $\"[121-141]?$ $\"[160-180]?$ $\"[195-215]?$ $\"[231-251]?$ $\"[279-299]?$ $\"[318-338]?$ $\"[367-387]?$ $\"[397-419]?$ $\"[440-462]?$ $\"[468-488]?$	transmembrane_regions

","BeTs to 5 clades of COG0833COG name: Amino acid transportersFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0833 is ------y----lb-ef----u-----Number of proteins in this genome belonging to this COG is 2","***** IPB004840 (Amino acid permease) with a combined E-value of 8.2e-66. IPB004840A 51-79 IPB004840B 176-195 IPB004840C 249-287 IPB004840D 331-370","Residues 45-149 are 58% similar to a (SIMILAR CANDIDA GLABRATA CAGL0E01089G) protein domain (PDA048N6) which is seen in Q6C9P9_EEEEE.Residues 55-92 are 92% similar to a (TRANSMEMBRANE PERMEASE AMINO ACID AMINO-ACID TRANSPORTER STRAIN AROMATIC LYSINE-SPECIFIC CHROMOSOME) protein domain (PD078045) which is seen in Q8G671_BIFLO.Residues 61-263 are 40% similar to a (SIMILAR VALINE/TYROSINE/TRYPTOPHAN A PERMEASE TRANSMEMBRANE AMINO-ACID) protein domain (PD837283) which is seen in Q86ZL7_PODAN.Residues 94-157 are similar to a (TRANSMEMBRANE AMINO ACID PERMEASE TRANSPORTER AMINO-ACID ANTIPORTER CATIONIC FAMILY PROBABLE) protein domain (PD284669) which is seen in Q8G671_BIFLO.Residues 178-250 are similar to a (TRANSMEMBRANE PERMEASE AMINO ACID AMINO-ACID TRANSPORTER AROMATIC LYSINE-SPECIFIC STRAIN PROBABLE) protein domain (PD031626) which is seen in Q88XC2_LACPL.Residues 178-250 are 65% similar to a (AMINO-ACID TRANSMEMBRANE METABOLISM ARGININE ROCE PERMEASE) protein domain (PD945979) which is seen in ROCE_BACSU.Residues 179-250 are 56% similar to a (TRANSMEMBRANE ACID AMINO ROCE PERMEASE) protein domain (PD640376) which is seen in O25661_HELPY.Residues 309-374 are similar to a (TRANSMEMBRANE AMINO ACID PERMEASE TRANSPORTER AMINO-ACID ANTIPORTER CATIONIC PROBABLE FAMILY) protein domain (PD004899) which is seen in Q88XC2_LACPL.Residues 376-443 are 75% similar to a (TRANSMEMBRANE PERMEASE AMINO ACID AMINO-ACID TRANSPORTER STRAIN AROMATIC LYSINE-SPECIFIC CHROMOSOME) protein domain (PD286223) which is seen in Q8PMN5_XANAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 52 to 493 (E_value = 2.6e-129) place ANA_0375 in the AA_permease family which is described as Amino acid permease.","","acid transport protein (rocE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0376","389030","390058","1029","5.01","-10.46","36067","ATGCCTGAGACGCTACCGGTGCCGCCTCGAGCTATTCGATACCGTGTCGCAATGCGAACGCTCTCGGAATCCGCCACGTCCTTCGGGCGAGAGCCGGTCCGGTTGTCTGATCTGCTGGACCGAGGTCCGGTCGTCCTCGACGGGGCAATGGGGACCGAGCTCGACGCCTGCGGGGTCAACACCCGCAACGCGCTGTGGTCGGCGCGTGCGCTCACCACGGCGCCCGACGTCGTGCGCGAGGTGCACTCCGAGTACCTGGATGCAGGGGCTCGCGTCATCACCACCAACACGTACCAGGCCACGCTTCCGGCGCTGGTCCGCTCCGGGGAGGATGCCGCCGGAGCAAGGCGGGTCATCGCAGCCGGCGCCCGCCTGGCCAAGGAGGCGGCCCGCCAGTTCGGCAATGAGCATCCCGAGGAGCCGGTGCTCGTCGCCGGAGGGCTCGGGCCGTATGGGGCCTATCTGGCTGATGGCAGCGAGTACACCGGTGCCTACGGCATCGACATCCTTGAGGACCCCGGTTTCCAGGAGGTTCACCTGCCGCGCATCGAGGTGCTGGTGGGGGAGGGGGTCGACCTGTTCGCCCTGGAGACGCTTCCGCGACTGGATGAAGCGCGGGCGCTCGCCTCCATGGTCACGGCCCTCGCCCCTCAGGCCCAGTGCTGGGTCTCCTTCCAGGTGCGCCCCGACGGCGCCACTCTTGCTGACGGCACGCCGCTGGCCGAGGCGGCGGTCTGGGCCGCGCAGGAGGAGATAGTCGTCGCGGTCGGCATCAACTGCGTGGCCCCGGGCGTCGTCGTCCGCGCGCTGCCGGTACTGCGTGCGGCGACCGACAAACCGCTGGTGGCCTACCCCAATGCGGGCGATCTCTACGACCCGGCAACCAAGACCTGGCAGTCCACAGGTGACGGGGCTGGAATCCCGGAGCTGGCGCCCTCATGGATCGCCGAAGGGGTTCGGCTCGTCGGCGGCTGCTGCCGCACCCGGCCGGCCCAGATCCGCCAGCTCGCCCGCGCGGTCTGCCCCTAG","MPETLPVPPRAIRYRVAMRTLSESATSFGREPVRLSDLLDRGPVVLDGAMGTELDACGVNTRNALWSARALTTAPDVVREVHSEYLDAGARVITTNTYQATLPALVRSGEDAAGARRVIAAGARLAKEAARQFGNEHPEEPVLVAGGLGPYGAYLADGSEYTGAYGIDILEDPGFQEVHLPRIEVLVGEGVDLFALETLPRLDEARALASMVTALAPQAQCWVSFQVRPDGATLADGTPLAEAAVWAAQEEIVVAVGINCVAPGVVVRALPVLRAATDKPLVAYPNAGDLYDPATKTWQSTGDGAGIPELAPSWIAEGVRLVGGCCRTRPAQIRQLARAVCP$","Homocysteine S-methyltransferase","Cytoplasm","homocysteine S-methyltransferase","homocysteine S-methyltransferase ","homocysteine S-methyltransferase","","Thanbichler M., Neuhierl B., Bock A. S-methylmethionine metabolism in Escherichia coli. J. Bacteriol. 1999. 181(2):662-665. PMID: 9882684Chen L.H., Liu M.L., Hwang H.Y., Chen L.S., Korenberg J., Shane B. Human methionine synthase. cDNA cloning, gene localization, and expression. J. Biol. Chem. 1997. 272(6):3628-3634. PMID: 9013615Garrow T.A. Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J. Biol. Chem. 1996. 271(37):22831-22838. PMID: 8798461","","","

InterPro
IPR003726
Domain

Homocysteine S-methyltransferase
G3DSA:3.20.20.330	$\"[35-340]T$	no description
PF02574	$\"[44-342]T$	S-methyl_trans
PS50970	$\"[32-340]T$	HCY

noIPR
unintegrated

unintegrated
PTHR21091	$\"[71-340]T$	METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
PTHR21091:SF4	$\"[71-340]T$	5-METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE

","BeTs to 4 clades of COG2040COG name: Homocysteine/selenocysteine methylase (S-methylmethionine-dependent)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2040 is ------y---r-bce------j----Number of proteins in this genome belonging to this COG is 1","***** IPB003726 (Homocysteine S-methyltransferase) with a combined E-value of 9.8e-25. IPB003726A 75-95 IPB003726B 255-261 IPB003726C 318-341","Residues 44-92 are 71% similar to a (METHYLTRANSFERASE TRANSFERASE HOMOCYSTEINE S-METHYLTRANSFERASE METHIONINE OXIDOREDUCTASE FLAVOPROTEIN FAD S- 5-METHYLTETRAHYDROFOLATE--HOMOCYSTEINE) protein domain (PD741711) which is seen in Q88XC1_LACPL.Residues 46-109 are 62% similar to a (HOMOCYSTEINE METHYLTRANSFERASE TRANSFERASE S-METHYLTRANSFERASE POSSIBLE) protein domain (PD320864) which is seen in Q9N8X6_EEEEE.Residues 157-240 are 64% similar to a (METHYLTRANSFERASE TRANSFERASE HOMOCYSTEINE S-METHYLTRANSFERASE S- METHYLMETHIONINE:HOMOCYSTEINE ZINC METHIONINE BIOSYNTHESIS SMM:HCY) protein domain (PD695728) which is seen in Q88XC1_LACPL.Residues 253-340 are similar to a (METHYLTRANSFERASE TRANSFERASE METHIONINE HOMOCYSTEINE 5-METHYLTETRAHYDROFOLATE--HOMOCYSTEINE S-METHYLTRANSFERASE SYNTHASE OXIDOREDUCTASE FLAVOPROTEIN FAD) protein domain (PD009874) which is seen in Q88XC1_LACPL.","","-38% similar to PDB:1Q7M Cobalamin-dependent methionine synthase (MetH) from Thermotoga maritima (Oxidized, Monoclinic) (E_value = 1.8E_10);-38% similar to PDB:1Q7Q Cobalamin-dependent methionine synthase (1-566) from T. maritima (Oxidized, Orthorhombic) (E_value = 1.8E_10);-38% similar to PDB:1Q7Z Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima (Cd2+ complex) (E_value = 1.8E_10);-38% similar to PDB:1Q85 Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima (Cd2+ complex, Se-Met) (E_value = 1.8E_10);-38% similar to PDB:1Q8A Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima (Cd2+:L-Hcy complex, Se-Met) (E_value = 1.8E_10);","Residues 44 to 342 (E_value = 2.2e-76) place ANA_0376 in the S-methyl_trans family which is described as Homocysteine S-methyltransferase.","","S-methyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0377","390144","390662","519","5.19","-5.55","19258","ATGTCTTCCGACGCCGACATCGTTGTCCTCTCGCTCCTTGCCGAGCAGCCGCGCCATGGCTACGACCTCGATCGGGTCATCGAGCAGCGCGGCTACCGTCAGTGGACCTCCCTGGCCTTCTCCTCCGTCTACTACCTCCTCAAGCGCCTGTCGGAGCGGGGGCTCCTCGAGCCCGACGAGGGATCTCAGGGACGGCGCACCGTCTTCCGCGTCACCGAGGCCGGGCGCCGCGAGCTGAGACAGGCCGCCGGTGAACGTGTCCTCGCCCCGGCTCCGCCTTCCGCCGGTGTGCTCCCGGCGCTCAACGCCTATAGCCGACTCGACGATCCTGCGCTCGCGGCCCTCCTCGCGCAGCGCGCCGAGGCACTCCTCGGCAGGCTCGATGAGCTGCGCGCCCTGCGCGCCCAGGTCGACGAGGAGCACGCCCTGGCCATCTTCGACTACGAGATCCTGCGCCAGGAAGCGGATCTCGCCTGGACTCGATCCCTTCTCAAGAAAGCAGACAGTGATGAGGACTGA","MSSDADIVVLSLLAEQPRHGYDLDRVIEQRGYRQWTSLAFSSVYYLLKRLSERGLLEPDEGSQGRRTVFRVTEAGRRELRQAAGERVLAPAPPSAGVLPALNAYSRLDDPALAALLAQRAEALLGRLDELRALRAQVDEEHALAIFDYEILRQEADLAWTRSLLKKADSDED$","Transcriptional regulator, PadR family","Cytoplasm","transcriptional regulator, PadR family domainprotein","transcriptional regulator PadR-like family","transcriptional regulator PadR family protein","","Gury J., Barthelmebs L., Tran N.P., Divies C., Cavin J.F. Cloning, deletion, and characterization of PadR, the transcriptional repressor of the phenolic acid decarboxylase-encoding padA gene of Lactobacillus plantarum. Appl. Environ. Microbiol. 2004. 70(4):2146-2153. PMID: 15066807","","","

InterPro
IPR005149
Family

Transcriptional regulator PadR-like
PF03551	$\"[6-82]T$	PadR

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[3-89]T$	no description

","BeTs to 9 clades of COG1695COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1695 is aompkz--vdrlb-e-g----j----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","Residues 9-76 are 74% similar to a (TRANSCRIPTIONAL FAMILY PADR REGULATOR REGULATOR PREDICTED PADR-LIKE PLASMID PYRIDOXAL REGULATORY) protein domain (PD230683) which is seen in Q6LZC9_METMP.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 82 (E_value = 3e-09) place ANA_0377 in the PadR family which is described as Transcriptional regulator PadR-like family.","","regulator, PadR family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0378","393983","391284","2700","5.10","-38.88","98871","GTGACCTCCCAGACTGCTCCGGCCCTCAACGCGATGCTCGACGCCCTCATTCCGGCTGACGATCCCGAGCGCGTCCCCGACCCCGAGGAGGTCTACCTGGCCTTCTCAAGCTGGGCGGAGACGACCGGCCGCCCCCTCTACCCGCACCAGGACGAGGCGCTGTCGGAGATCCTGGAGGACCGCCACGTCATCGCCGCCACCCCGACCGGTTCGGGCAAGTCGATGATCGCGCTGGCAGCCCACACCGCCTCCCTGGCCCGCGGGGGCCGCTCCTACTACACGGCACCGCTCAAGGCCCTGGTCAGTGAGAAGTTCTTCGAGCTGGTGCACCTGTTCGGGGCCGATAACGTCGGCATGGTCACCGGGGACACCTCCATCAACGCCGCCGCCCCGATCATCTGCTGCACCGCGGAGATCCTGGCCAACCAGTCCCTGCGCGAGGGCGAGGACATGGATGTGGACTGCGTCATCATGGACGAGTTCCACTATTACGCCGACCCGCAGCGCGGCTGGGCCTGGCAGGTGCCCCTCCTGGAGCTGCCCCAGGCGCAGATGGTGCTGCTGTCGGCCACACTGGGCGACGTCTCCTTCTTCGTGCGGGACCTGCGCGAGCGCACGGGCCGCGAGGTCGCCGTCGTCGACGACGCCGTGCGGCCGGTTCCGTTGGAGATGGAGTACGTCGTCGAGCCGATCGGTGAGCTGCTTCAGCGCCTGGTGGGTCAGGACAAGGCGCCGGTCTATGTCGTTCACTTCTCCCAGAAGGAGGCGGTGGAGCGGGCGACCTCCCTGCTGAGCGTGGACCTGGTGCCCAAGTCCCGCAAGGCCGAGGTGGTGGAGGCGCTCGGCGACTTCCGCTTCGGGGGCGGTTTCGGAGCCACGCTCTCGCGGCTGCTGCGCGCCGGGATCGGCGTGCACCACGCGGGCATGCTGCCGCGCTACCGGCGGCTGGTGGAGCGCCTGGCCCGCGAGGGCCTGCTGTCCGTCATCTGCGGTACTGACACGCTCGGGGTGGGGATCAACGTGCCGATCCGCTCAGTGGTCATGACCTCCCTGGTGAAGTTCGACGGCTCCAAGGAGCGCCACCTCACCGCTCGCGAGTTCCACCAGATCGCCGGGAGGGCGGGGCGCGCCGGCTTCGACACCCGCGGCTACGTCTCCGTCCAGGCCCCCGAGCACGTCATCGAGAACGCCAAGGCGCTGGCCAAGGCCGGCGACGACGAGCGCAAGCGCCGCAAGATCGTGCGTAAGAAGGCCCCTGAGGGGCGCGTCAACTGGACGGACAAGACCTTCGAGCGGCTGCGCGACGCGGCCCCGGAGACACTGACCAGCCAGTTCCAGGTCACCACCACCATGGTGCTCAACCTCATGGAGCGCGCCGGTGACCCGGTGGCGGCGATGGCGGAACTGCTGGAGCGCGCCCACGAGCCCGAGGCCCAGCGGCGTCGCCACGTGCGCCGCGCTCTGGAGATCTACCTGTCCCTGCGCACGGCGGGGGTCCTCACGCATGTCTCCAGCGCCCAAGCCGCCGCCGATGGGCGCCCCCGGTTGCGCCTGGCGGTGGACCTGCCGGCCGACTTCGCCCTCAACCAGCCCCTGGCGCCCTTCGCCCTGGCGGCCATGGACCTGCTGAACGTGGAGGCCCCGGAGCACACGGTCGACGTCGTCAGCGTCGTCGAGGCCACCCTGGACGATCCGCGTCCGCTGCTCTACGCCCAGCAGCGTGCCGCCCGCGGCGAAGCGATCGCCGCGATGAAGGCCGAGGGGATGGACTACGAGGAGCGCATGGCCGCCCTGGAGGAGGTCACCTGGCCCCAGCCGCTGGCCGAGCTACTCACTCCTGCTCTGGAGATGTACAAGCAGGCCAACCCATGGATCGCCGAGCACGAGCTGGCGCCGAAGTCAGTGGTGCGCGAGATGGTGGAGAACGCGATGACCTTCTCCGACCTCATCTCCCGCCACGAGCTGGGCCGCAGCGAGGGCGTGGTGCTGCGCTACCTGACCGACGCCTACCGGGCGCTGCGCCAGGTCGTGCCCGAGGAGCACCGCACTCCTGAAGTGGTCGAGCTCATCGACTGGCTGGGGGCACTCGTGCGCGCCGTCGACTCCTCCCTACTCGATGAGTGGGAGGCGCTCGGTCAGGCGCAGGCGGGCAAGGCCGGCGAGGCCGCCGGCCTGCTGGAGGGCGACCGTCCCGGCGCGGACGACTCATCCGGGGTGGAGCGGGCCTTCGGCGCGGACGAGGACGGGACGGTGGCCTTCACTCGCAACCGTCACGCCTTCCGAGTGGCGGTGCGCCGGGAGATGTTCCGGCGCGTGGAGCTCATGGCGCGCGACGACGTCGAGGCACTGGGCCGTCTGGACGCCTCCTCCGGCTGGGGCGAGGACCGCTGGGACGAGGTGCTGGGCCGCTACTGGGACGAGTACGACTGGATCGGCACCGACACCTCGGCTCGGGCGATCTCGCTGGCGCCGCTCGACGAGGCCCCCGATGAGACGGCCCTGGCGGCAGCCGGGGTCAGTGAGCGCCTCCGCGAGGCCCTGGAGGCCTCCGGCAAGCAGGTGTGGCTGGCCACGCAGGTCCTGGAGGACCCCGACGGCGATCACGACTGGCGGCTGACGGCCCTGGTGGATCTTGCCGAGTGCGACCGGGAGGGGCGCGCGGTCGTCCACCTGCTGTCCGTGGGCCCGCAGCAGGGTTAA","VTSQTAPALNAMLDALIPADDPERVPDPEEVYLAFSSWAETTGRPLYPHQDEALSEILEDRHVIAATPTGSGKSMIALAAHTASLARGGRSYYTAPLKALVSEKFFELVHLFGADNVGMVTGDTSINAAAPIICCTAEILANQSLREGEDMDVDCVIMDEFHYYADPQRGWAWQVPLLELPQAQMVLLSATLGDVSFFVRDLRERTGREVAVVDDAVRPVPLEMEYVVEPIGELLQRLVGQDKAPVYVVHFSQKEAVERATSLLSVDLVPKSRKAEVVEALGDFRFGGGFGATLSRLLRAGIGVHHAGMLPRYRRLVERLAREGLLSVICGTDTLGVGINVPIRSVVMTSLVKFDGSKERHLTAREFHQIAGRAGRAGFDTRGYVSVQAPEHVIENAKALAKAGDDERKRRKIVRKKAPEGRVNWTDKTFERLRDAAPETLTSQFQVTTTMVLNLMERAGDPVAAMAELLERAHEPEAQRRRHVRRALEIYLSLRTAGVLTHVSSAQAAADGRPRLRLAVDLPADFALNQPLAPFALAAMDLLNVEAPEHTVDVVSVVEATLDDPRPLLYAQQRAARGEAIAAMKAEGMDYEERMAALEEVTWPQPLAELLTPALEMYKQANPWIAEHELAPKSVVREMVENAMTFSDLISRHELGRSEGVVLRYLTDAYRALRQVVPEEHRTPEVVELIDWLGALVRAVDSSLLDEWEALGQAQAGKAGEAAGLLEGDRPGADDSSGVERAFGADEDGTVAFTRNRHAFRVAVRREMFRRVELMARDDVEALGRLDASSGWGEDRWDEVLGRYWDEYDWIGTDTSARAISLAPLDEAPDETALAAAGVSERLREALEASGKQVWLATQVLEDPDGDHDWRLTALVDLAECDREGRAVVHLLSVGPQQG$","ATP-dependent helicase","Cytoplasm","Superfamily II DNA and RNA helicases","putative helicase","DEAD/DEAH box helicase domain protein","","Gorbalenya A.E., Koonin E.V., Donchenko A.P., Blinov V.M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989. 17(12):4713-4730. PMID: 2546125","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[296-378]T$	Helicase_C
SM00490	$\"[292-378]T$	HELICc
PS51194	$\"[230-437]T$	HELICASE_CTER

InterPro
IPR002048
Domain

Calcium-binding EF-hand
PS00018	$\"[355-367]?$	EF_HAND_1

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[47-198]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[42-223]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[54-210]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[46-214]T$	no description
PTHR11752	$\"[46-392]T$ $\"[431-481]T$	HELICASE SKI2W
PTHR11752:SF2	$\"[46-392]T$ $\"[431-481]T$	HELICASE SKI2W

","BeTs to 8 clades of COG1204COG name: Predicted helicasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1204 is aompkzyq------------------Number of proteins in this genome belonging to this COG is 1","***** IPB012961 (DSH, C-terminal) with a combined E-value of 5.9e-48. IPB012961A 62-108 IPB012961B 139-193 IPB012961C 212-226 IPB012961E 300-341 IPB012961F 365-380 IPB012961G 436-457***** IPB004179 (Sec63 domain) with a combined E-value of 8.2e-12. IPB004179E 326-355 IPB004179F 366-383***** IPB013701 (DEAD/H associated) with a combined E-value of 1.7e-08. IPB013701A 37-80 IPB013701D 143-170","Residues 68-136 are 85% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT FACTOR DNA BOX RNA-BINDING 3.6.1.-) protein domain (PD410733) which is seen in Q6A5X1_PROAC.Residues 137-231 are 77% similar to a (HELICASE HYDROLASE ATP-BINDING RNA DNA II SUPERFAMILY DEAD OR BOX-LIKE) protein domain (PD285135) which is seen in Q6NGT5_CORDI.Residues 233-320 are 77% similar to a (HELICASE ATP-BINDING HYDROLASE RNA 3.6.1.- CEREVISIAE DNA ATP-DEPENDENT SKI2 STRAIN) protein domain (PD100066) which is seen in Q8NP92_CORGL.Residues 322-400 are 83% similar to a (HELICASE ATP-BINDING HYDROLASE RNA 3.6.1.- ATP-DEPENDENT NUCLEAR DNA CEREVISIAE PROBABLE) protein domain (PD007814) which is seen in Q6A5X1_PROAC.Residues 401-895 are 65% similar to a (HELICASE HYDROLASE ATP-BINDING RNA DNA II SUPERFAMILY DEAD OR BOX-LIKE) protein domain (PD323994) which is seen in Q9KZJ3_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 43 to 194 (E_value = 4.6e-06) place ANA_0378 in the ResIII family which is described as Type III restriction enzyme, res subunit.Residues 47 to 198 (E_value = 1e-18) place ANA_0378 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 296 to 378 (E_value = 1.3e-09) place ANA_0378 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","II DNA and RNA helicases (SKI2W)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0379","390652","391287","636","5.47","-5.83","23119","ATGAGGACTGACATCAAGAAGGACCGCAAGGACCTGTACCTGCCGGGGCGAGCCGACTTCACGGAGGTGGACGTACCGGCCATGACCTACTTGGCCATCGACGGCCACGGAGACCCCAACACCTCACCGGCCTACGCCACCGCGATCCAGGCGCTCTACGCGGGCGCCTACGCGATCCGTGCCGTGCTGAAGAAACGAACCGGCGATGACTTCGTCGTCGGCCCCCTGGAGGGACTGTGGACGAGCGCCGACAATGCGGCTTTCGTCGCCGGTGACAAGGGGGAGTGGGACTGGACCATGATGCTCCCCCTGCCCGAGGCGGTCTCCTCGCAGGACATCGCCGAGGGGCTGGCGCAGGCGGCGCGCAAGAAGCCGGAGCTGCCCGTCTCCGCTCTCAAGGAGCTCTCTCTGAGCGAGGGCAGGTCGCTGCAGATCCTCCACGTGGGCACGTACGACGACGAGGCCCCCACTCTGGCGCGTCTGCACGACGAGGTCATGCCGCGCCTCGGCCTCACCTGGAACGGGCCCCACCACGAGATCTACCTCAGCGACCCCAGGCGCGTGGCACCGGAGAGGATGAAAACCGTCCTGCGCCAGCCGGTCAGGTCCGTCGCGGAAGCCAACGAGGCGGGTTAA","MRTDIKKDRKDLYLPGRADFTEVDVPAMTYLAIDGHGDPNTSPAYATAIQALYAGAYAIRAVLKKRTGDDFVVGPLEGLWTSADNAAFVAGDKGEWDWTMMLPLPEAVSSQDIAEGLAQAARKKPELPVSALKELSLSEGRSLQILHVGTYDDEAPTLARLHDEVMPRLGLTWNGPHHEIYLSDPRRVAPERMKTVLRQPVRSVAEANEAG$","Uncharacterized conserved protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","conserved hypothetical protein","","","","","

InterPro
IPR008319
Family

Uncharacterised conserved protein UCP031644
PIRSF031644	$\"[1-204]T$	Uncharacterised conserved protein

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 25-124 are similar to a (LMO2083 YCDC LP_3071 CYTOSOLIC SMU.1470C MA1133 LIN2189) protein domain (PD400417) which is seen in Q8TRP2_METAC.Residues 144-202 are 67% similar to a (DNA-BINDING TRANSCRIPTIONAL TRANSCRIPTION REGULATION REGULATOR FAMILY REGULATOR MERR ARAC PROBABLE) protein domain (PD219988) which is seen in Q8TRP2_METAC.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0380","394077","395273","1197","4.67","-31.89","44085","ATGGACCCCCGTGCCCGCATCGAGGCCTTCCTCGCCGACTACGTCGCTGCCCACGCCGAGGTCAAGCCGCTCTTCGACAACCGGAAAGAGAACGGAGCAGAGGATCCATTCTCCGCGTGGTACGCGAAGCTGGAAGAACTCCGCGCAGCTCATCAGATGGAGAGGTCACTTAAGGGCGACATCGCCGGTATCTCTGCGCCGGGAACTTCCCACCTGGGAACGATCACGATTGAGCGCATCGAGGTCTACGGCAACATGGCCAGGGCGAGGCTCACACGAGAAATCCGTTCCTATGGGCGCCCCATCATCGAGATGATGCTGGTTCGCGTTAGCGACGACTGGCGCATCGACACCATTGACGACTACCGCGAGGAGCCGGGCTCCCCACTGGTGGACAAGGACGTGCTCGAGGCCTGGAAGGCCGCCGCCGATAAGACGGAGCCGATGGAGGCCCAGCACAAGGAGGACATGCCGGACCCCGCGGCCGTGTTCTCCGCCTCCTGGGCCTGCGAGGCGCTCAGCGAGGACTACATCGAGGTCTTCCTCAGCGACACCATGGAGTGGCGCGAGGAGGACGGTGATGAGAACGACCCGGAGACCTACGCCGCTGTACGAGCCAGGGCCATCGCTGAGATGTACCGCAATGCTGAGGTTGGACCGGTCGAGATTCAGGAGATCGGCCAGTTCCCGCACGGCAGCTACCTGGCGGCGGGAGACCCCTTCGGAGAGATGTGCCTGTGCGCCCTCAAGGTCGAGCCCGGTGTGGCGCGGGCTCAGGCCCTGCTCACCACGCTGGGTGGTGAGCGGTGCGTGGCCGCGCTGCGCGTCATCCTCGCGGACCGTGAGCCGGTGCAGTGGAAGCACGCGATCGTCATGACGGCATCGGCGCGCTCCACGGACGTCAGTTCGTGGCATGAGGTGGACACCAGGTCGGGTAACGGCACCATCGCCGACGCCGACGCCTACTTCGGCATGACCCACCGGCAGTACTCCATCGTGGAGCGGCAGGAGGAACAGACCTTCCTCATGGATCCGGGGTCGGGTCCCATTGGTGCCTCGACCTCCTCCGGACGGCAGTACGGCGTCGCCCAGGCCTACTGGGGTCTGGATGAGGATGACCGGCCCGTTCAGCTGGTGCTCGACCACCAGGAGCTCTGGGCGCCTGCCGACCCGCCCGAGGCCACGACCGGGGCCTGA","MDPRARIEAFLADYVAAHAEVKPLFDNRKENGAEDPFSAWYAKLEELRAAHQMERSLKGDIAGISAPGTSHLGTITIERIEVYGNMARARLTREIRSYGRPIIEMMLVRVSDDWRIDTIDDYREEPGSPLVDKDVLEAWKAAADKTEPMEAQHKEDMPDPAAVFSASWACEALSEDYIEVFLSDTMEWREEDGDENDPETYAAVRARAIAEMYRNAEVGPVEIQEIGQFPHGSYLAAGDPFGEMCLCALKVEPGVARAQALLTTLGGERCVAALRVILADREPVQWKHAIVMTASARSTDVSSWHEVDTRSGNGTIADADAYFGMTHRQYSIVERQEEQTFLMDPGSGPIGASTSSGRQYGVAQAYWGLDEDDRPVQLVLDHQELWAPADPPEATTGA$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0381","395397","396944","1548","8.06","2.34","53239","ATGGATGCCCTCGCCGCTCAGCTCGAGGCCGTCTCGGACTGGATCACGCTCCACATCACCATGTGGGTGCTCGTCGGTACCGGGATCCTGCTGACCGCCCGCACCGGTTTCGTGCAGCTCCGCCGCCTGCCGGACATGTTCCGCCAGGTGGCCGGATCGCGCTCCGGGGCTCAAGGAGGCATCTCCTCCTTCCAGGCCTTCACGATTTCCCTGGCCGCCCGTGTGGGCATCGGTAATGTCTTCGGAGTGGCTGCCGCCCTCATCTTGGGCGGCCCCGGTGCGATCTTCTGGATGTGGGTGGTCGCCCTGGTCGGTATGGCCACCGCTTTCTTCGAGGCGACCCTGGCCCAGATGTTCAAGGTCCGTCACTCCGATGGCTCCTTCCGTGGCGGGCCCGCCTACTACATGGCGCGCGGGATGCGCAGCCGTCCCCTGGGGGTTGCCTTCGCGGGGCTGACGATCTTCACCTGCGGCTTCTCCATCATCATGGTCCAGTCCAACGCCGTCGCCGGGGTGATCGGCCCGGATTCCCCGCTGCACCTGCGCCCAAGCGTCGCCGCCGCGGTGCTGGTGGGACTGGCCGCTCTGGTCATCCTGGGGGGAGTGCGCCGGGTCGCCCGCGTCACCGAGTGGATGGCGCCGATCATGGCCCTGGTCTACGTCGTCATGGCCGTTGTCATCGTCGCTCTCCACATCACTCAGCTCCCGGGGCTGCTGGCTACGATCGTCTCCTCGGCCTTCGGCCCGATGCCCTTCGCCGGAGGGGTGACCGGAGGCATCATCGCCGCCCTGACCAACGGGACCCGCCGCGGCCTGTTCTCCAACGAGGCCGGGCAGGGCACCGCCCCCTTCGCCGCCGCCACCGCCACCGTGGCCCACCCCGTTCAGCAGGGCCTCATCCAGTCCCTCGGAGTGTTCGTCGACACCATCATCGTGTGCACCGCGACCGCCTTCATCATCCTGGTCTCCGGCGTCTACAGCCCCGCCCTCGTCCAGGCCGGCACGCTGACCCCCAACGCCGCGGCAACCTTGACCTCCGACGCCGTCGCCGCCACCCTCGGCAGCTGGACGGCCATTCCCATGGCCATCGTCATCTTCGTCCTGGCCTTCTCCTCCATCATCGCCGCGGCCACCTACTCCGAGGTCTCCATGACCTTCATCTCCGAGCGGCCCGAGTGGCGCTGGCTGCCCCGGCTCGTCTCGGTGGCCTCCACCGGGCTGGGAGCCCTTGCCACTCTGACCGTCGTGTGGAACACCGTCGACATCACCATGGCCGTCATGACCCTGACCAACCTGGTCGCCCTCATCTGGCTCGCCCGCTGGGGAGTGGGGGCGCTCAAGGACTGGGACGCCCAGCGCGCGGCGGGACGAGTCGCCCCCCTGTTCAACGGCGTGGGCAACCCCTATCTGCCCGGCGACCTCCCCGGTGACGTCTGGACCGGCGAGAGGACCCACCTGGCCGAGGCGGACAGCACCGCAGACGACGTCGTTCCCGCAGCAACCCCGGCCAGCAGCCAGCCCGCCGCCTCGACAGGAGCCGACGCATGA","MDALAAQLEAVSDWITLHITMWVLVGTGILLTARTGFVQLRRLPDMFRQVAGSRSGAQGGISSFQAFTISLAARVGIGNVFGVAAALILGGPGAIFWMWVVALVGMATAFFEATLAQMFKVRHSDGSFRGGPAYYMARGMRSRPLGVAFAGLTIFTCGFSIIMVQSNAVAGVIGPDSPLHLRPSVAAAVLVGLAALVILGGVRRVARVTEWMAPIMALVYVVMAVVIVALHITQLPGLLATIVSSAFGPMPFAGGVTGGIIAALTNGTRRGLFSNEAGQGTAPFAAATATVAHPVQQGLIQSLGVFVDTIIVCTATAFIILVSGVYSPALVQAGTLTPNAAATLTSDAVAATLGSWTAIPMAIVIFVLAFSSIIAAATYSEVSMTFISERPEWRWLPRLVSVASTGLGALATLTVVWNTVDITMAVMTLTNLVALIWLARWGVGALKDWDAQRAAGRVAPLFNGVGNPYLPGDLPGDVWTGERTHLAEADSTADDVVPAATPASSQPAASTGADA$","Sodium/alanine symporter","Membrane, Cytoplasm","sodium/alanine symporter","K03310 alanine or glycine:cation symporter; AGCS family","amino acid carrier protein","","MacLeod P.R., MacLeod R.A. Identification and sequence of a Na(+)-linked gene from the marine bacterium Alteromonas haloplanktis which functionally complements the dagA gene of Escherichia coli. Mol. Microbiol. 1992. 6(18):2673-2681. PMID: 1447975Kamata H., Akiyama S., Morosawa H., Ohta T., Hamamoto T., Kambe T., Kagawa Y., Hirata H. Primary structure of the alanine carrier protein of thermophilic bacterium PS3. J. Biol. Chem. 1992. 267(30):21650-21655. PMID: 1400476","","","

InterPro
IPR001463
Family

Sodium:alanine symporter
PR00175	$\"[90-112]T$ $\"[183-201]T$ $\"[211-230]T$ $\"[305-323]T$ $\"[358-380]T$ $\"[418-438]T$	NAALASMPORT
PF01235	$\"[43-458]T$	Na_Ala_symp
TIGR00835	$\"[19-449]T$	agcS: amino acid carrier protein
PS00873	$\"[90-105]T$	NA_ALANINE_SYMP

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[14-33]?$ $\"[54-74]?$ $\"[80-100]?$ $\"[145-165]?$ $\"[184-202]?$ $\"[212-232]?$ $\"[242-264]?$ $\"[310-330]?$ $\"[358-378]?$ $\"[399-417]?$ $\"[423-443]?$	transmembrane_regions

","BeTs to 12 clades of COG1115COG name: Na+/alanine symporterFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1115 is ----k----d-lb-efgh-nu--it-Number of proteins in this genome belonging to this COG is 3","***** IPB001463 (Sodium:alanine symporter) with a combined E-value of 1.1e-92. IPB001463A 62-112 IPB001463B 185-232 IPB001463C 267-298 IPB001463D 367-379 IPB001463E 416-456","Residues 8-80 are 64% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE FAMILY ACID AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD685428) which is seen in Q8EN00_OCEIH.Residues 96-129 are 79% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID AMINO FAMILY CARRIER SODIUM:ALANINE PERMEASE PROBABLE) protein domain (PD961883) which is seen in Q9HXZ0_PSEAE.Residues 270-323 are 83% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD681215) which is seen in Q9CNA4_PASMU.Residues 353-421 are 57% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD170825) which is seen in Q81XD8_BACAN.","","No significant hits to the PDB database (E-value < E-10).","Residues 43 to 458 (E_value = 1.6e-133) place ANA_0381 in the Na_Ala_symp family which is described as Sodium:alanine symporter family.","","symporter (ORF8)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0382","396941","398395","1455","8.29","3.06","50803","ATGAACCTCACCAGTATCGAGAACCTGCTCAACTCCGTCGACGACTTCTTCTACACCTATCTTCTGACCGCCCTGCTCATCCTGGCCGGCATCTACCTGACCGCACGTAGCCGCCTGGTTCAGCTGCGCCACTTCGGCACCATGGTCAACTCGCTGTCCGGATCCCGATCCGGCGCGCAGGGCGGTATCTCCTCCTTCCAGGCCTTCGCCGTAGGACTGGCCGCGCGCGTCGGCATCGGCAACATCGCCGGAGTCGCCCTGGCCATTGTGGCCGGCGGCCCCGGCGCCCTGCTCTGGATGTGGGTCGTCGCCCTCATCGGCATGGCCACCAGCTTCGTGGAGTCCACACTCGCCCAGATCTTCAAGGAGCGCGGCCGGGACTTCACCTTCCGCGGGGGCCCGGCCTACTACATCAAGAACGGCCTGGGCTCGCCCCTGTGGGGCAAGATCTTCGCCGCCATCTGCATCGTCTCAGTCGGCGTGACGGTGGTCATGGTGCAGACGAACTCGCTGGCCCAAGTCATCACCGTCACCGTCCCCAGCGTCTCGGCCTGGATGGTCGGGGTCTTCCTCGTCCTGCTGACCGCACCCGTGGTCCTGGGTGGGGTCCGGCTCGTGGCCCGCGTCGCGGAGTGGCTGGCCCCCATCATGGCGCTGGCCTACGTGCTCATGGCCGTGGTGGTCATCATCCTCAACATCGGTAGGCTCCCCGAGGTCCTGGGGAGCGTCTTCGAAGGGGCCTTCGGTCTCAACCAGGCCCTGTTCGGCACCGCCGGAGGAGTCCTCGCGGCGCTGCTCAACGGCGTGCGCCGCGGCCTGTTCTCCAACGAGGCCGGGCTCGGAACCGTCCCCAATGCCGCCGGCACCGCGACCGTCGCCCACCCTGTGCGACAGGGCCTCATCCAGTCCTTCGGCGTCTTCGTCGACACGATCCTCGTGTGCACGGCCACCGGCCTGCTCATCCTCCTGACCACCAAGACCTACCACCCCGGCGACGACTCCCTGGTCGGAGCGATCCTCACCCAGCAGGCCGTTGCCGAGCACCTGGGGCCCTGGACCACCTGGCCCATGGTGGTGCTCATCTTCGTCCTGGTCTTCTCCACGGTGCTGGGCTGCTACTCCTACGCGCAGGTCAACGTCAACTTCCTGGGCGGAGAACGACGGGCCGAGCAGATCTTCGGGATCCTCCTGACTGCTGCGGCCTTCGGTGGCACCGTCCTGACCCTGCCCGTCGTCTGGGCTCTGTCCGACATCGCCCTGGGGCTCCTGGGCGTGCTCAACCTCGTCGTCATCATCCGGCTGGCCCCCTGGGTCATAGGAGCCCTGCGGGACTTCGAGTCCCAGCGTGCCCGGGGCATCACCGAGCCCGCCTTCGTAGGCCACGGCAACTCCCTCCTGCCCGGAGACGTGGTCCCCGGCATCTGGGAGCCCGACGACGTGGCGAAGCGGGGCTGA","MNLTSIENLLNSVDDFFYTYLLTALLILAGIYLTARSRLVQLRHFGTMVNSLSGSRSGAQGGISSFQAFAVGLAARVGIGNIAGVALAIVAGGPGALLWMWVVALIGMATSFVESTLAQIFKERGRDFTFRGGPAYYIKNGLGSPLWGKIFAAICIVSVGVTVVMVQTNSLAQVITVTVPSVSAWMVGVFLVLLTAPVVLGGVRLVARVAEWLAPIMALAYVLMAVVVIILNIGRLPEVLGSVFEGAFGLNQALFGTAGGVLAALLNGVRRGLFSNEAGLGTVPNAAGTATVAHPVRQGLIQSFGVFVDTILVCTATGLLILLTTKTYHPGDDSLVGAILTQQAVAEHLGPWTTWPMVVLIFVLVFSTVLGCYSYAQVNVNFLGGERRAEQIFGILLTAAAFGGTVLTLPVVWALSDIALGLLGVLNLVVIIRLAPWVIGALRDFESQRARGITEPAFVGHGNSLLPGDVVPGIWEPDDVAKRG$","Sodium/alanine symporter","Membrane, Cytoplasm","sodium/alanine symporter","K03310 alanine or glycine:cation symporter; AGCS family","amino acid carrier protein","","MacLeod P.R., MacLeod R.A. Identification and sequence of a Na(+)-linked gene from the marine bacterium Alteromonas haloplanktis which functionally complements the dagA gene of Escherichia coli. Mol. Microbiol. 1992. 6(18):2673-2681. PMID: 1447975Kamata H., Akiyama S., Morosawa H., Ohta T., Hamamoto T., Kambe T., Kagawa Y., Hirata H. Primary structure of the alanine carrier protein of thermophilic bacterium PS3. J. Biol. Chem. 1992. 267(30):21650-21655. PMID: 1400476","","","

InterPro
IPR001463
Family

Sodium:alanine symporter
PR00175	$\"[92-114]T$ $\"[184-202]T$ $\"[212-231]T$ $\"[306-324]T$ $\"[354-376]T$ $\"[414-434]T$	NAALASMPORT
PF01235	$\"[42-456]T$	Na_Ala_symp
TIGR00835	$\"[18-445]T$	agcS: amino acid carrier protein

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[16-35]?$ $\"[56-76]?$ $\"[82-102]?$ $\"[146-166]?$ $\"[182-202]?$ $\"[212-234]?$ $\"[248-266]?$ $\"[304-324]?$ $\"[358-378]?$ $\"[393-413]?$ $\"[419-439]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB001463 (Sodium:alanine symporter) with a combined E-value of 1.9e-97. IPB001463A 64-114 IPB001463B 186-233 IPB001463C 268-299 IPB001463D 363-375 IPB001463E 412-452","Residues 99-131 are 90% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID AMINO FAMILY CARRIER SODIUM:ALANINE PERMEASE PROBABLE) protein domain (PD961883) which is seen in Q6ANS1_BBBBB.Residues 274-333 are 85% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD681215) which is seen in Q7P3Z5_BBBBB.Residues 340-418 are 60% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD170825) which is seen in Q8FP18_COREF.","","No significant hits to the PDB database (E-value < E-10).","Residues 42 to 456 (E_value = 2e-128) place ANA_0382 in the Na_Ala_symp family which is described as Sodium:alanine symporter family.","","symporter (ORF8)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0383","398401","399876","1476","7.08","0.25","50476","ATGGCACCTCTGGGGGGCATCTCATGGATGGGCCAGGTCGACGCCGTCCTGGCCTCCGTCTCCGACATGCTCTACTCCTGGGGCCTCATGTGGCTCCTCATCGGGGCGGGCATCTTCTTCACCGTCAGGACCCGGGGCGTCCAAGTGCGGCACACCGACGCGATCGCCGCCTCAGTGATCGGCTCCCGCGACGGCAGCCACGGCGGCATCACCTCCTTCCAGGCCTTCGCCGTCGGACTGGCCTGCCGGGTGGGGACCGGCAATATCGTCGGGGTCGCCCTGGCGCTCATCCTGGGCGGGCCCGGAGCCGTGCTGTGGATGTGGCTCGTGGCGATCCTGGGAACCGCCACTGCCTTCAGCGAGGCCACGCTCGCCCAGCTGTTCAAGGTGCGTCGCCCCGACGGCACCTTCCGCGGCGGTCCCGCCTACTACATTTCGCGAGGACTGGGGCTGCCGATCCTGGGCGGGGTCTTCGCCGTCGTCTTCCTCATCGCCAACGGCCTGGTCATGCCCATGGTGCAGGCCAACGCCATCACCGCCTCCCTGCAGGGGGCCGGAGGGCTCTCACCGAGTCTGGGAGCCGTCCTCGTCGTGGCCCTGACCGCGCCGGTCCTCCTGGGAGGCCTGCGCGCCATGGCCCGCGTGGCGGAGTACCTGGCCCCGTTCATGGCGCTGGCCTACCTGGTGCTCGTTCTGGCCATCCTCCTGACCCACCCCGTCCAGGCCCTCGAGGCGCTGACCTCCATCATCGAGGGCGCCTTCGGCCTGCGCCAGGGGCTGGGCGGCCTGGCCGGCGGGATGACCGCGGCGCTGCTCAACGGCGTGCGCCGCGGCCTGTTCTCCAATGAGGCGGGACTGGGAGGAGCCGCCTGCGCCGCTGGCTCAGCCACCGTGAGCCACCCCGTCCAGCAGGGATTCATTCAGGCCTTCGGGGTCGTGGTGGACACCCTGTTCGTCTGCACGGCGACGGCGCTGGCGATCTTGGTCGCCGGAGCAGACGTCCTCCATCCCGGGGTGAGCGCCAAGGAGAGTGCGGGAACCCTGACCCAGGACGCCATCGCCCACCTCGTGGGGGAGTGGAGCCGCTGGCCCATGGCGCTGCTCGTCGTCGTCCTGGCCTACACCACCATCATCGGAGCCTTCTCCTACGCCCAGGTCTGCCTCGACTACCTCACCGACCGCCCCGGGGTCTCGCGCGCGCTCCAGATCGGCGCCGTCGTCTGCGCCGGCGTCGGCAGCGTGCAGCAGCTGACCACAGTGTGGACCCTGGCGGATGTGCTCCTGGGGCTGGGCGCCATCATCAACCTCGTGGCGCTGGTGCTCCTGAGCCGGTGGGTCGTCGGTGCGCTCAGGGACTGGGAGGCCAGGCGGGGCATGTCAACTGCGGAGGGCGGCCAGTCGGTCTTCCGCGGGGACTCCGAGTATCTTCCAGCACCCCTGCCGGAAGGCGCCTGGGAGCGGGCAGACGACCGGTAG","MAPLGGISWMGQVDAVLASVSDMLYSWGLMWLLIGAGIFFTVRTRGVQVRHTDAIAASVIGSRDGSHGGITSFQAFAVGLACRVGTGNIVGVALALILGGPGAVLWMWLVAILGTATAFSEATLAQLFKVRRPDGTFRGGPAYYISRGLGLPILGGVFAVVFLIANGLVMPMVQANAITASLQGAGGLSPSLGAVLVVALTAPVLLGGLRAMARVAEYLAPFMALAYLVLVLAILLTHPVQALEALTSIIEGAFGLRQGLGGLAGGMTAALLNGVRRGLFSNEAGLGGAACAAGSATVSHPVQQGFIQAFGVVVDTLFVCTATALAILVAGADVLHPGVSAKESAGTLTQDAIAHLVGEWSRWPMALLVVVLAYTTIIGAFSYAQVCLDYLTDRPGVSRALQIGAVVCAGVGSVQQLTTVWTLADVLLGLGAIINLVALVLLSRWVVGALRDWEARRGMSTAEGGQSVFRGDSEYLPAPLPEGAWERADDR$","Sodium/alanine symporter","Membrane, Cytoplasm","sodium/alanine symporter VC2356","K03310 alanine or glycine:cation symporter; AGCS family","amino acid carrier protein","","MacLeod P.R., MacLeod R.A. Identification and sequence of a Na(+)-linked gene from the marine bacterium Alteromonas haloplanktis which functionally complements the dagA gene of Escherichia coli. Mol. Microbiol. 1992. 6(18):2673-2681. PMID: 1447975Kamata H., Akiyama S., Morosawa H., Ohta T., Hamamoto T., Kambe T., Kagawa Y., Hirata H. Primary structure of the alanine carrier protein of thermophilic bacterium PS3. J. Biol. Chem. 1992. 267(30):21650-21655. PMID: 1400476","","","

InterPro
IPR001463
Family

Sodium:alanine symporter
PR00175	$\"[99-121]T$ $\"[190-208]T$ $\"[218-237]T$ $\"[312-330]T$ $\"[362-384]T$ $\"[422-442]T$	NAALASMPORT
PF01235	$\"[55-464]T$	Na_Ala_symp
TIGR00835	$\"[27-453]T$	agcS: amino acid carrier protein

noIPR
unintegrated

unintegrated
signalp	$\"[1-44]?$	signal-peptide
tmhmm	$\"[24-42]?$ $\"[76-98]?$ $\"[108-128]?$ $\"[149-169]?$ $\"[188-208]?$ $\"[218-236]?$ $\"[255-275]?$ $\"[366-386]?$ $\"[427-447]?$	transmembrane_regions

","BeTs to 12 clades of COG1115COG name: Na+/alanine symporterFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1115 is ----k----d-lb-efgh-nu--it-Number of proteins in this genome belonging to this COG is 3","***** IPB001463 (Sodium:alanine symporter) with a combined E-value of 2e-85. IPB001463A 71-121 IPB001463B 192-239 IPB001463C 274-305 IPB001463D 371-383 IPB001463E 420-460","Residues 27-103 are 67% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE FAMILY ACID AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD685428) which is seen in Q9HXZ0_PSEAE.Residues 106-138 are 87% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID AMINO FAMILY CARRIER SODIUM:ALANINE PERMEASE PROBABLE) protein domain (PD961883) which is seen in Q6ANS1_BBBBB.Residues 277-333 are 71% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD681215) which is seen in Q8NTU6_CORGL.Residues 348-426 are 63% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD170825) which is seen in Q8FP18_COREF.","","No significant hits to the PDB database (E-value < E-10).","Residues 55 to 464 (E_value = 3.8e-106) place ANA_0383 in the Na_Ala_symp family which is described as Sodium:alanine symporter family.","","symporter VC2356 (ORF8)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0384","400116","401711","1596","6.02","-4.38","55906","GTGCAACCGGTTCTGGCTTCCCTGAACAGTGCGGCATCCAGCGCAGGCAACAACTGGACCGCATCCTTGGAACGCTTCTTCGACGATGGCGCCAAGATCCTCGATGACGCCGCCGGGTACCTGTTCCTCTACCTGCTCGCCTGGCTGCTCGTGCTGGGAGGCCTGTACTTCACCGTGCGGACCGGATTCGTACAGCTGCGGCTCTTCCCCTACATGGTGCGGGCCATCACCTCCTCCCGTGACAGCAAGGAGGGCGGAATCTCCTCCTTCCAGGCCTTCGCCGTCGGGCTGGCCTCCCGCGTGGGCACCGGCAACATCGTGGGTGTGGCCATCGCCATCACCATGGGTGGCCCCGGCGCCGTGTTCTGGATGTGGGTCGTGGCGCTGGTGGGCATGGCCACCGGGTTCATCGAGGCCACCCTCGCTCAGCTCTACAAGGTCACCCACCCCGATGGCACCTTCCGCGGCGGCCCGGCCTACTACATCCAGCGCGGCCTGGGGTCCAAGCCCGCCGCCAAGCTCTTCGCCGTCGTCATCACCTTCGTCTTCGGTTTCGCCTACGAGGCCACCCAGGCCAACACGATCGCCGCCACGATGGAGAGCACCTTCCACGTCGAGCCGTGGATGACCGCCGTTGCACTGGTTGTCATCACCACGCCGATCATCTTCAAGGGCATCAAGTCGGTCGCTGCCGTCTCGGAGTGGCTCGTGCCGATCATGACGGTGGTCTACGCGCTCATCGCCGTGACCATCCTAGTGCTGCACGCCAGCGCGATCCCGGGTGCGATCTTCTCCATCCTCGAGGGCGCCTTCGGGCTCAACCAGGTCTTCGCGGGGACCGCAGGGGGATTCACCGCCGCACTTCTCAACGGCACCCGACGAGGCCTGTTCTCCAACGAGGCCGGCGAGGGATCGGTCCCCAACATCGCGGCCACCGCCACCGTTCCCCACCCGGTCCAGCAGGGATTCGTGCAGTCCCTGGGCGTCTTCGTCGACACGATCGTGGTGTGTACCGTCACCGCCCTCATCGTCCTGCTCTCCGGGGTCTACGACCCGGTGGCCGCTCAATCCGCCCCAGAGGTTGCCAATGGCGCCGCCAACACCCTGACCTCGGCATCAGTCACCAACGTCCTCGGTGGCTGGGCGCAGTACCTCATGGCCGTCATCATCTTCGTCTTCGCCTACTCCTCGCTCCTGGGCAACTACACCTACGCACAGGTCAACATGGACTACCTCCAGGGCAAGCAGCACAAGCACTACGCCCTGCGGGCCATGATCATCGTGGCCACCGCCGTCGGCTCCCTGTCCACCCTCACCTTCGTGTGGAGCCTGTCCGACCTCGTCATGGGGGCGATGACCGTCATCAACATGGTCTCCATCCTCGCCCTGGGAGGCTGGGCCTTTGGAGCCCTGCGCGACTGGGAGGCCCAGCGCCGCGCCGTCGAGGCCGGCGAGAAGGACGAGATCCGCTTCATCGCCACCGACAACCCCTACCTGCCCGGCACGCTCCCCGGAGACATCTGGGCGGCTGACGGCGCTGCCCACGCCGCCATCACGGAGCGTCGCGCCGCGCTCGAGGAGGCCTCGGGCAGCTGA","VQPVLASLNSAASSAGNNWTASLERFFDDGAKILDDAAGYLFLYLLAWLLVLGGLYFTVRTGFVQLRLFPYMVRAITSSRDSKEGGISSFQAFAVGLASRVGTGNIVGVAIAITMGGPGAVFWMWVVALVGMATGFIEATLAQLYKVTHPDGTFRGGPAYYIQRGLGSKPAAKLFAVVITFVFGFAYEATQANTIAATMESTFHVEPWMTAVALVVITTPIIFKGIKSVAAVSEWLVPIMTVVYALIAVTILVLHASAIPGAIFSILEGAFGLNQVFAGTAGGFTAALLNGTRRGLFSNEAGEGSVPNIAATATVPHPVQQGFVQSLGVFVDTIVVCTVTALIVLLSGVYDPVAAQSAPEVANGAANTLTSASVTNVLGGWAQYLMAVIIFVFAYSSLLGNYTYAQVNMDYLQGKQHKHYALRAMIIVATAVGSLSTLTFVWSLSDLVMGAMTVINMVSILALGGWAFGALRDWEAQRRAVEAGEKDEIRFIATDNPYLPGTLPGDIWAADGAAHAAITERRAALEEASGS$","Sodium/alanine symporter","Membrane, Cytoplasm","sodium/alanine symporter VC2356","K03310 alanine or glycine:cation symporter; AGCS family","amino acid carrier protein","","MacLeod P.R., MacLeod R.A. Identification and sequence of a Na(+)-linked gene from the marine bacterium Alteromonas haloplanktis which functionally complements the dagA gene of Escherichia coli. Mol. Microbiol. 1992. 6(18):2673-2681. PMID: 1447975Kamata H., Akiyama S., Morosawa H., Ohta T., Hamamoto T., Kambe T., Kagawa Y., Hirata H. Primary structure of the alanine carrier protein of thermophilic bacterium PS3. J. Biol. Chem. 1992. 267(30):21650-21655. PMID: 1400476","","","

InterPro
IPR001463
Family

Sodium:alanine symporter
PR00175	$\"[116-138]T$ $\"[207-225]T$ $\"[235-254]T$ $\"[329-347]T$ $\"[383-405]T$ $\"[443-463]T$	NAALASMPORT
PF01235	$\"[69-486]T$	Na_Ala_symp
TIGR00835	$\"[42-474]T$	agcS: amino acid carrier protein
PS00873	$\"[116-131]T$	NA_ALANINE_SYMP

noIPR
unintegrated

unintegrated
signalp	$\"[1-61]?$	signal-peptide
tmhmm	$\"[44-64]?$ $\"[85-100]?$ $\"[106-126]?$ $\"[171-189]?$ $\"[208-226]?$ $\"[241-263]?$ $\"[269-289]?$ $\"[327-347]?$ $\"[380-400]?$ $\"[421-443]?$ $\"[449-469]?$	transmembrane_regions

","BeTs to 12 clades of COG1115COG name: Na+/alanine symporterFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1115 is ----k----d-lb-efgh-nu--it-Number of proteins in this genome belonging to this COG is 3","***** IPB001463 (Sodium:alanine symporter) with a combined E-value of 2.4e-97. IPB001463A 88-138 IPB001463B 209-256 IPB001463C 291-322 IPB001463D 392-404 IPB001463E 441-481","Residues 58-120 are 74% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE FAMILY ACID AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD685428) which is seen in Q7N3C6_PHOLL.Residues 121-155 are 82% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID AMINO FAMILY CARRIER SODIUM:ALANINE PERMEASE PROBABLE) protein domain (PD961883) which is seen in Q9HXZ0_PSEAE.Residues 221-275 are 74% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE FAMILY ACID AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD005953) which is seen in Q7NRX8_CHRVO.Residues 294-349 are similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD681215) which is seen in Q8NTU6_CORGL.Residues 369-446 are 65% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/ALANINE ACID FAMILY AMINO CARRIER PERMEASE SODIUM:ALANINE D-ALANINE) protein domain (PD170825) which is seen in Q81XD8_BACAN.","","No significant hits to the PDB database (E-value < E-10).","Residues 69 to 486 (E_value = 8e-146) place ANA_0384 in the Na_Ala_symp family which is described as Sodium:alanine symporter family.","","symporter VC2356 (ORF8)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0385","401737","402561","825","4.96","-12.83","29655","ATGAAGATCGCGCGCTTCTCCACCGGTGACGAGCCCCGTTACGGCATCGTTCAGGGCCTGCCCGAGCATGAGGTCGCCTCGGGCGAGTCCGAGGGGCACCTCCTGGTCCTCAAGGGAGACCCCCTCTACTCCCTGCCCGAGGCCACTGGGGAGGTCGTCGAGCTGCGTGAGGCCCGGCTCCTGTCGCCGGTCATCCCGCGCTCCAAGGTCGTGGGGATCGGGAAGAACTACGGGGGCCACATCGCCGAGATGGGGGAGGACGAGCCGCCGCGCGACCCGGTGGTCTTCCTCAAGCCCAACACCTCCGTCATCGGCCCCGACGCTCCCATCGTCCTGCCCGCCTGGAGCGAGGAGGTTCACTACGAGGCCGAGCTCGCCGTCGTCATCAAGACCCTCGCCAAGGACGTCCCCGTGGAGCACGCCGACGACGTCATCCTGGGGTACACGGTCGCCAACGACGTCTCGGCCCGCGACCGCCAGCGCGCCGAGCCGCAGTGGGTGCGGGCCAAGGCCTTCGACACCTCCTGCCCCCTGGGGCCGTGGATCGAGGTTCCCGAGCCCGGCCGCGAGCCGCTCTTCTCACCCGGCGACGCGGTGGTGCGCGCCCGGGTCGATGGCCGCCTCGTCCAGGAGGGACGGACCGCTGACATGATCCGCTCGATTCCCGAGCTGGTCGCCTACATATCGACGATCTTCACCCTCCTGCCCGGTGACGTCATTCTCACCGGCACACCGGCCGGAGTTGGCGAGATCCGTCCCGGTCAGCGCGTCGAGGTCGAGGTCGAGGGCATCGGCTCCTTCTCCAACCCGGTGGTCCGTCGCTGA","MKIARFSTGDEPRYGIVQGLPEHEVASGESEGHLLVLKGDPLYSLPEATGEVVELREARLLSPVIPRSKVVGIGKNYGGHIAEMGEDEPPRDPVVFLKPNTSVIGPDAPIVLPAWSEEVHYEAELAVVIKTLAKDVPVEHADDVILGYTVANDVSARDRQRAEPQWVRAKAFDTSCPLGPWIEVPEPGREPLFSPGDAVVRARVDGRLVQEGRTADMIRSIPELVAYISTIFTLLPGDVILTGTPAGVGEIRPGQRVEVEVEGIGSFSNPVVRR$","Fumarylacetoacetate (FAA) hydrolas","Cytoplasm, Extracellular","possible 2-hydroxyhepta-2,4-diene-1,7-dioateisomerase in the fumarylacetoacetate hydrolase family","5-carboxymethyl-2-hydroxymuconate delta-isomerase ","5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase","","","","","

InterPro
IPR002529
Domain

Fumarylacetoacetate (FAA) hydrolase
PF01557	$\"[84-253]T$	FAA_hydrolase

noIPR
unintegrated

unintegrated
G3DSA:3.90.850.10	$\"[59-266]T$	no description
PTHR11820	$\"[59-272]T$	FUMARYLACETOACETATE HYDROLASE

","BeTs to 17 clades of COG0179COG name: 2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway)Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0179 is aompkzy--dr-bcefgh-nuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002529 (Fumarylacetoacetate (FAA) hydrolase) with a combined E-value of 5.4e-36. IPB002529A 70-103 IPB002529B 119-130 IPB002529C 140-160 IPB002529D 233-247","Residues 1-89 are 55% similar to a (5-OXO-125-TRICARBOXILIC-3-PENTEN ACID DECARBOXILASE) protein domain (PD956953) which is seen in Q6AEQ0_BBBBB.Residues 93-141 are 75% similar to a (ISOMERASE HYDROLASE FUMARYLACETOACETATE 2-HYDROXYHEPTA-24-DIENE-17-DIOATE FAMILY 5.3.3.- LYASE 4.1.1.- DECARBOXYLASE BIFUNCTIONAL) protein domain (PD731021) which is seen in Q6A7Z6_PROAC.Residues 143-215 are 65% similar to a (ISOMERASE HYDROLASE FUMARYLACETOACETATE 2-HYDROXYHEPTA-24-DIENE-17-DIOATE FAMILY 5.3.3.- FUMARYLACETOACETASE BIFUNCTIONAL LYASE CATABOLISM) protein domain (PD002459) which is seen in Q82JR2_STRAW.Residues 217-264 are 87% similar to a (ISOMERASE HYDROLASE 2-HYDROXYHEPTA-24-DIENE-17-DIOATE FUMARYLACETOACETATE FAMILY 5.3.3.- BIFUNCTIONAL LYASE 4.1.1.- DECARBOXYLASE) protein domain (PD888892) which is seen in Q6A7Z6_PROAC.","","-59% similar to PDB:2DFU Crystal structure of the 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase from Thermus Thermophilus HB8 (E_value = 1.0E_50);-58% similar to PDB:1WZO Crystal Structure of the HpcE from Thermus Thermophilus HB8 (E_value = 9.4E_41);-57% similar to PDB:1NR9 Crystal Structure of Escherichia coli 1262 (APC5008), Putative Isomerase (E_value = 2.8E_37);-53% similar to PDB:1GTT CRYSTAL STRUCTURE OF HPCE (E_value = 2.0E_35);-53% similar to PDB:1I7O CRYSTAL STRUCTURE OF HPCE (E_value = 2.0E_35);","Residues 84 to 253 (E_value = 1.9e-76) place ANA_0385 in the FAA_hydrolase family which is described as Fumarylacetoacetate (FAA) hydrolase family.","","2-hydroxyhepta-2,4-diene-1,7-dioate isomerase in the fumarylacetoacetate hydrolase family (FAA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0387","403546","402704","843","5.44","-6.91","29959","ATGTCCCCGTCCCTACATCCGGCGGCAGGTTCCACCAACCGCCGCCGATCTGCCCTCAGACTCCCCGTTGTTGCCGGCCTCAGCCTCGCTTTGGCCGTTCCGGCTCTCGCTGCGTGCCAGGACGAGTCCGGCCCCGCGCGCCCCAGTGCCTCCAGCAGTGCGTCATCATCCGCTAAAAAGTCGGACAAGAGTGCAGAACCATCGGAAAAGCCCTCCAAGGAGAGCAAGAACAGCAACGTCGAGTACGTTCCTTCATGGGAGTTCCCGCATTCCCACTCCGGTTGGAACGTGACCGTCTACGACGTCGACGGCAAGAACAAGATGGATAAGCAGAACGGCTGCGTGTTCACCGCGACGCAGAATCTGTACGCCCAGACCACGAAGGACGATCAGGCGGAGTCGGGCTATCAGGCAGATGCCGTCATCGACGCCTATCAGAAGTCGTCGGACTTCACGAACGTCTCCTTCGAGCCCACCAAGGACGATTCCACCCTGGTCAAGGACACCGACGGTCACGCCATCGAGACCAAGCGCCTGGACTTCACGTACACCGGAGCCGACCACAAGGACTACAAGCTCACCAGGGTCGTCCGTGTCTTCAGCACGGTGGGTAGGCCCGTCATGCTCCAGGGGATGTACGCCTGCCCCGTCAACGTCTACTCCTCCAGTGAGATGGAGGAACTGTTCAAGGCCACCCCGATCTCCAATCCTGGCCCGGCCGACATGGACGAGGGCAGCTCCAGCGATGGTGCCGGCAAGGACGGCAACGACGGCAAGAAGAGCGAGTCCGAGGACAAGAAGAGCGATGAGAAGAGCTCAGGAAGTTCTCCCAAGGACACCTGA","MSPSLHPAAGSTNRRRSALRLPVVAGLSLALAVPALAACQDESGPARPSASSSASSSAKKSDKSAEPSEKPSKESKNSNVEYVPSWEFPHSHSGWNVTVYDVDGKNKMDKQNGCVFTATQNLYAQTTKDDQAESGYQADAVIDAYQKSSDFTNVSFEPTKDDSTLVKDTDGHAIETKRLDFTYTGADHKDYKLTRVVRVFSTVGRPVMLQGMYACPVNVYSSSEMEELFKATPISNPGPADMDEGSSSDGAGKDGNDGKKSESEDKKSDEKSSGSSPKDT$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[21-39]?$	transmembrane_regions

InterPro
IPR000924
Family

Glutamyl-tRNA synthetase, class Ic
PR00987	$\"[32-44]T$ $\"[46-57]T$ $\"[61-74]T$ $\"[216-226]T$ $\"[232-240]T$	TRNASYNTHGLU
PTHR10119	$\"[32-538]T$	GLUTAMYL/GLUTAMINYL-TRNA SYNTHETASE
PF00749	$\"[28-348]T$	tRNA-synt_1c

InterPro
IPR004527
Family

Glutamyl-tRNA synthetase bacterial/mitochondrial
TIGR00464	$\"[28-535]T$	gltX_bact: glutamyl-tRNA synthetase

InterPro
IPR008925
Domain

Class I aminoacyl-tRNA synthetase, anticodon-binding
G3DSA:1.10.10.350	$\"[428-535]T$	no description

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[28-273]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.1160.10	$\"[274-358]T$	no description
PTHR10119:SF1	$\"[32-538]T$	GLUTAMYL-TRNA SYNTHETASE 1, 2, 3 (GLUTAMATE--TRNA LIGASE 1, 2, 3)

","BeTs to 26 clades of COG0008COG name: Glutamyl- and glutaminyl-tRNA synthetasesFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0008 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000924 (Glutamyl-tRNA synthetase signature) with a combined E-value of 1.5e-24. IPB000924A 32-44 IPB000924B 46-57 IPB000924C 61-74 IPB000924D 216-226 IPB000924E 232-240","Residues 31-77 are 97% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS GLUTAMYL-TRNA GLUTAMATE--TRNA GLURS GLUTAMINYL-TRNA GLUTAMINE--TRNA) protein domain (PD001595) which is seen in Q73VI4_MYCPA.Residues 83-147 are 81% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS GLUTAMYL-TRNA GLUTAMATE--TRNA GLURS GLUTAMINYL-TRNA GLUTAMINE--TRNA) protein domain (PD458103) which is seen in SYE_CORGL.Residues 153-252 are similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA GLUTAMYL-TRNA BIOSYNTHESIS ATP-BINDING GLUTAMATE--TRNA GLURS TRNA SYNTHETASE-RELATED) protein domain (PD406080) which is seen in SYE_BIFLO.Residues 263-335 are 90% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA GLUTAMYL-TRNA BIOSYNTHESIS ATP-BINDING GLUTAMATE--TRNA GLURS TRNA SYNTHETASE-RELATED) protein domain (PD130077) which is seen in SYE_STRAW.Residues 331-428 are 58% similar to a (SYNTHETASE GLUTAMYL-TRNA AMINOACYL-TRNA) protein domain (PDA1C4Z2) which is seen in Q6AEQ1_BBBBB.Residues 449-522 are 72% similar to a (SYNTHETASE LIGASE GLUTAMYL-TRNA AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS GLURS GLUTAMATE--TRNA GLUTAMATE-TRNA GLTS) protein domain (PD722450) which is seen in SYE_BIFLO.","","-51% similar to PDB:2O5R Crystal structure of Glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (Glutamate-tRNA ligase 1) (GluRS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution (E_value = 3.3E_73);-50% similar to PDB:1J09 Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP and Glu (E_value = 3.8E_69);-50% similar to PDB:1N75 Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP. (E_value = 3.8E_69);-50% similar to PDB:1N77 Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(Glu) and ATP. (E_value = 3.8E_69);-50% similar to PDB:1N78 Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(Glu) and glutamol-AMP. (E_value = 3.8E_69);","Residues 28 to 348 (E_value = 3.9e-108) place ANA_0388 in the tRNA-synt_1c family which is described as tRNA synthetases class I (E and Q), catalytic domain.","","synthetase (gltX)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0389","406413","405667","747","4.87","-10.16","26200","ATGTTCCTCACCCGCACCCCCTCCAGAGCTCGTCACCTCGCCCTGGTGGGGCTGGGCCTCGCAGCCAGTCTGGCGCTGAGCGCCTGCGGCCCCGCCCATAAGGGGCAGCTCACCGTCGAGCCCGCCGAAGCCTCCGCCGAGGCCAGCGAATCCAGTTCCCCCTCGCCGTCCCCAACACCGAGCCCGACCGCCTCACCGTCGACGCCTTCACCCTCGGCGACGACATGGACGGCACCGAGTGTCACGATCTCCAGCGAGGACTCGTCGGTCTGGACGCACGACGACGAACGCATCAAGAAGGACTCGGCCGGCCCTAACGGGACTATTGACGGCTACACGGTCAACGCCAACCCCGCCTGCTTCGGTTTTGTCTCCAGCGAAGCCGAGGAGAGGTTCTACACCCTCCGAGGAGTCGGAGACGACATTCAGTCCAAAGCGGCCCTCAAGAGTCAGCAGACGATCTTCTCCAATTATCAGACGACACAAGGGCCAAACCTCGTGGAGGCCGTCCGGGACGACAGCGGGACCTTCCCGGGCTATGAGGAGACCTTCTCCGTGACCGCCAACTTCTCCGACTCCCCCAACACGCCCATGGATGGATATCGTTTCGACAGGCGAGTGGGAGAGAAGGGGTTCACTTTCGAGGTCATGCTGCTGTGCCCTCAAGGCTCCCTCATCGGACTGGATCAGTGGCACACGATCCTGGGGGGCATCCGGATCCAGGGAATCGACGCCGGAGCCATGTAG","MFLTRTPSRARHLALVGLGLAASLALSACGPAHKGQLTVEPAEASAEASESSSPSPSPTPSPTASPSTPSPSATTWTAPSVTISSEDSSVWTHDDERIKKDSAGPNGTIDGYTVNANPACFGFVSSEAEERFYTLRGVGDDIQSKAALKSQQTIFSNYQTTQGPNLVEAVRDDSGTFPGYEETFSVTANFSDSPNTPMDGYRFDRRVGEKGFTFEVMLLCPQGSLIGLDQWHTILGGIRIQGIDAGAM$","Hypothetical protein","Extracellular, Periplasm","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-29]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[12-32]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-58% similar to PDB:1F9D Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellotetraose (E_value = );-58% similar to PDB:1F9O Crystal structure of the cellulase Cel48F from C. Cellulolyticum with the thiooligosaccharide inhibitor PIPS-IG3 (E_value = );-58% similar to PDB:1FAE Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellobiose (E_value = );-58% similar to PDB:1FBO Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellobiitol (E_value = );-58% similar to PDB:1FBW Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellohexaose (E_value = );","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0390","407262","406507","756","5.88","-6.00","26396","ATGCCCACCCGCCTGCGGCACCGTCACCGCGCAGGTCACGGCCCCTGCCGCACTCGCCTCCTCACCCTTGGACTGACCCTGATCGCAGCTCTCCCCCTTGGCGCCTGCGGCCCCGCACACAATGGACAGCTGACCGTCGAACCCGCCGGCGCCTCCTCCACGGCCACCTCCTCCAGCTCGGATGCGCCGTCCGCGACCCCGACGCCGTCGGCAACATCGTCCGCAACAGCCTGGACGGCCCCGAACGTCACGATCTCCAACGACACCACGGGTACCTGGCACCGGCAGGACGACATACTCGAGCATCCGGTCGAGACACCATCAAAAATCAGCCAGGCCTACAAGTTCGACGCAGGAGGCTGCCTAGCCATCATCTTCTACGACGCAAGCCAAACAATTCACGACGAAGGAAGAAGGGGTGGAGACAACCTCTCCTCCTCCACAAAGGTGCAGGAGACGATGTCCAACCACAGTTCCTTTGTGGTGGCCTCAGGTCCGACCTCCGTCAACGCCGTACGAGACGACAATGGGACGCTTCCCGGATACGAGATCGCATACACAGCCACTGTCACATATGCCAACGGCTCGACCGGTGACGTAGCGGGATATCGGTTCTTCCGGCAGATCAGCGATCCGGGTGTCACACTCGAAATCTTCCTCGAGTGCGCCCCGGACAATCTTGCCCCCTCCGACACATGGCACCAGTTCTTGTTCTCGACACGAGTGGAGGGACTCGATGCTGGGGCCATGGGATAG","MPTRLRHRHRAGHGPCRTRLLTLGLTLIAALPLGACGPAHNGQLTVEPAGASSTATSSSSDAPSATPTPSATSSATAWTAPNVTISNDTTGTWHRQDDILEHPVETPSKISQAYKFDAGGCLAIIFYDASQTIHDEGRRGGDNLSSSTKVQETMSNHSSFVVASGPTSVNAVRDDNGTLPGYEIAYTATVTYANGSTGDVAGYRFFRQISDPGVTLEIFLECAPDNLAPSDTWHQFLFSTRVEGLDAGAMG$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[21-39]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-42% similar to PDB:2IEM Solution structure of an oxidized form (Cys51-Cys198) of E. coli Methionine Sulfoxide Reductase A (MsrA) (E_value = );-43% similar to PDB:2UVG STRUCTURE OF A PERIPLASMIC OLIGOGALACTURONIDE BINDING PROTEIN FROM YERSINIA ENTEROCOLITICA (E_value = );-45% similar to PDB:1BH3 E1M, A116K MUTANT OF RH. BLASTICA PORIN (E_value = );-45% similar to PDB:1PRN REFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COMPARISON WITH THE PORIN FROM RHODOBACTER CAPSULATUS (E_value = );-61% similar to PDB:2O03 Crystal structure of FurB from M. tuberculosis- a Zinc uptake regulator (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0395","408906","408070","837","7.02","0.11","28967","GTGACGACCACGAGCCTGCCGGATGACGGAGCTAGGGACAGCGCTCCCTCTTCGTCAACCGAGTCACAGCCGAGTCCCGCTCCTCGTGAGAGCCGGCGAGGCCTCCTGGGAAGAGCCGCCCTGGCAACGACTGCAGGTCTCCTCGGTGCGGGCGCCGGCGCAGGAGCCGCCCACTGGCGGGACACCCACCTCTCCCCCACGGCAAGAACCGCCCCTCGCCCCGCGGGTCCCGGCGACCCGCTCGGAACGCGAGTGGTCTTCCAGACCGACGGGAAGTCCGGAAAGCTGGCGTTGACCTTCGACGACGGCCCGGACCCCCGTTGGACTCCACGGGTGCTTGACATGCTGGCGAGGTTGCACGTGCAGGCCACCTTCTTCGTCCTGGGCTCCGCGGTGCAGGCCCACCCCGAGCTGATCGCGCGAGAGGTCGCCGAGGGGCACGAGGTCGCCGTTCATAACTGGGTGCACACGGATGTCTACGGCGTGAGCTTCTCCGAGCTGAGCGACTCAGTGGAACGGACACGTGAGGCGATCATGGCCGCCGGCGCCCCATCTCCACGCCTGTGGCGGCCTCCCTACGGCCGGGTTGACGCGCCGGCCATGATGGTCGCCTCACTCAAGAAGATGGACCTGTTGCTGTGGAGCGTTCACACGCCCACTGCGGCGAAGGCCGCCGCCATCAAGGATGCTGCCGGCGCCGGGTCGGTGGTGCTGTGTCACGACGGGCGCACGCAGCCCTCCGAGGCCCTGTTCACCGCCTTGGAAGGAGGCGTGCGCTCGCTGCTGGAGCGAGGGCTTGCCGTGACGACGGGAAGTGACCTGCTGGCGCCCGCCTGA","VTTTSLPDDGARDSAPSSSTESQPSPAPRESRRGLLGRAALATTAGLLGAGAGAGAAHWRDTHLSPTARTAPRPAGPGDPLGTRVVFQTDGKSGKLALTFDDGPDPRWTPRVLDMLARLHVQATFFVLGSAVQAHPELIAREVAEGHEVAVHNWVHTDVYGVSFSELSDSVERTREAIMAAGAPSPRLWRPPYGRVDAPAMMVASLKKMDLLLWSVHTPTAAKAAAIKDAAGAGSVVLCHDGRTQPSEALFTALEGGVRSLLERGLAVTTGSDLLAPA$","Polysaccharide deacetylase","Cytoplasm, Periplasm","Unknown","polysaccharide deacetylase","polysaccharide deacetylase","","Freiberg C., Fellay R., Bairoch A., Broughton W.J., Rosenthal A., Perret X. Molecular basis of symbiosis between Rhizobium and legumes. Nature 1997. 387(6631):394-401. PMID: 9163424Mishra C., Semino C.E., McCreath K.J., de la Vega H., Jones B.J., Specht C.A., Robbins P.W. Cloning and expression of two chitin deacetylase genes of Saccharomyces cerevisiae. Yeast 1997. 13(4):327-336. PMID: 9133736Millward-Sadler S.J., Poole D.M., Henrissat B., Hazlewood G.P., Clarke J.H., Gilbert H.J. Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases. Mol. Microbiol. 1994. 11(2):375-382. PMID: 8170399","","","

InterPro
IPR002509
Domain

Polysaccharide deacetylase
PF01522	$\"[89-214]T$	Polysacc_deac_1

","BeTs to 11 clades of COG0726COG name: Predicted xylanase/chitin deacetylaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0726 is ---pk-y-vdrlbcefg-s-uj----Number of proteins in this genome belonging to this COG is 2","***** IPB002509 (Polysaccharide deacetylase) with a combined E-value of 9.3e-16. IPB002509A 99-109 IPB002509B 115-126 IPB002509C 146-156 IPB002509D 188-194","Residues 81-246 are 51% similar to a (CHITIN HYDROLASE DEACETYLASE) protein domain (PDA0L2T1) which is seen in Q7WYW6_BBBBB.Residues 82-276 are 44% similar to a (HYDROLASE SIGNAL ORFX YBAN PRECURSOR) protein domain (PD375585) which is seen in YBAN_BACSU.Residues 83-265 are 50% similar to a (NODB) protein domain (PD714855) which is seen in Q9RAN6_MESS7.Residues 84-217 are 58% similar to a (POLYSACCHARIDE FAMILY DEACETYLASE) protein domain (PDA186R3) which is seen in Q73CS3_BACC1.Residues 85-255 are 53% similar to a (DEACETYLASE POLYSACCHARIDE HYDROLASE DEGRADATION 3.5.1.- XYLAN NODULATION SIGNAL PRECURSOR CHITOOLIGOSACCHARIDE) protein domain (PD389393) which is seen in Q8E5Y7_STRA3.Residues 86-160 are 66% similar to a (DEACETYLASE PEPTIDOGLYCAN N-ACETYLGLUCOSAMINE) protein domain (PD530644) which is seen in Q897I0_CLOTE.Residues 88-215 are 55% similar to a (DEACETYLASE OLIGOSACCHARIDE) protein domain (PD761949) which is seen in Q8EPK0_OCEIH.Residues 95-160 are 60% similar to a () protein domain (PDA1C9P8) which is seen in Q72KC3_THET2.Residues 96-216 are 50% similar to a (DEACETYLASE POLYSACCHARIDE) protein domain (PD966910) which is seen in Q73H54_WOLPM.Residues 96-275 are 45% similar to a (POLYSACCHARIDE DEACETYLASE) protein domain (PD746781) which is seen in Q8DK37_SYNEL.","","-56% similar to PDB:2C1G STRUCTURE OF STREPTOCOCCUS PNEUMONIAE PEPTIDOGLYCAN DEACETYLASE (SPPGDA) (E_value = 1.8E_18);-56% similar to PDB:2C1I STRUCTURE OF STREPTOCOCCUS PNEMONIAE PEPTIDOGLYCAN DEACETYLASE (SPPGDA) D 275 N MUTANT. (E_value = 6.7E_18);-46% similar to PDB:2C71 THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A MAGNESIUM ION. (E_value = 2.0E_14);-46% similar to PDB:2C79 THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A COLBALT ION. (E_value = 2.0E_14);-55% similar to PDB:2CC0 FAMILY 4 CARBOHYDRATE ESTERASE FROM STREPTOMYCES LIVIDANS IN COMPLEX WITH ACETATE (E_value = 2.6E_14);","Residues 89 to 214 (E_value = 2.3e-34) place ANA_0395 in the Polysacc_deac_1 family which is described as Polysaccharide deacetylase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0396","409086","410720","1635","5.32","-22.99","59033","ATGCGCATCACTCCCCTGGGGGGCCTGGGCGAGGTCGGCCGCAACATGACCGTCTTCGAGTTGGACGGCAAGCTGCTCATCGTCGACTGCGGTGTGCTCTTCCCTGAGGAGGACCAGCCGGGTGTCGACCTCATCCTTCCTGACTTCTCCTCCATCGAGCACCGCATCGACGACGTCGTCGCCCTGGTCCTGACTCACGGGCACGAGGACCACATCGGGGGTGTGCCCTATCTGCTGCGCCTGCGTGAGGACATCCCCTTGGTGGGAAGCGAGCTCACGCTGGCCTTCGTGGAGGCCAAGCTCAAGGAGCACCGTATCCGTCCGGTGCTGCGTCAGGTCGTCGAGCACGAGGAGGTCTCCTACGGCCCCTTCGACCTGGAGTTCGTGGCCGTCAACCACTCCATCCCCGACGCCATGGCCGTCATGATCCGCACCGATGCCGGCAAGGTGCTGGCCACCGGTGACTTCAAGATGGACTCCCTGCCCATCGACGGGCGCATCACGGACCTGCGCTCCTTCGCCCGTTTCGGTGAGGAGGGTGTGGACCTGTTCTGCGTGGACTCCACCAACGCCGAGGTCCCGGGCATGGTGGGCCATGAGGGAGAGATCGGCCAGGTCCTGGACAACGTCTTCGCCGACTCCGACGGCCAGATCGTCGTGGCCTCCTTCGCCAGCCACGTCCACCGCGTCCAGCAGGTCCTCGACGCCGCCGCCCTGCACGACAGGCGGGTCGCCCTCGTGGGGCGCTCCATGGTGCGCAACATGGGGATCGCCGCCGAGCGCGGCTACCTCAAGGTCCCCGCCGGCGTCCTCATCGATGCTCGGGACATCACCTCGCTGCCCCCGCACGAGAGAGTCCTCATGGTCACCGGCTCTCAGGGAGAGCCCATGGCGGCCCTGTCCCGGATGGCCCACTCCGAGCACCGCAGCGTCACCATCGAGCCCGGGGACACCGTCATCTTCGCCTCCTCCCTCATCCCCGGCAACGAGAACTCCGTCTTCCGGGTCATCAACCAGCTCATGAGGCTGGGGGCACGCGTGGTCCACCAGGGCAACGCTAAGGTCCACGTCTCCGGGCACGCCTCCTCCGAGGAGCTGCTCCACGTCTACAACATCGTCCAGCCCCGCAACGTCATGCCCATCCATGGTGAGATTCGTCATCTGGTGGCTAATGGTGGGCTTGCCGTCAAGACGGGAATCGCCCCGGAGCGAGTCATGCTGTGTGAGGACGGCGTGGCCGTCGACCTGGAGGGTGGAGTGGCCCGTATCGCCGGCCAGGTGCCCTGCGGCTACATCTACGTCGACGGCTCCTCGGTGGGGGAGATCGACGAGGCCGAGCTCAAGGACCGCCGCATCCTGGCGGAGGAGGGTTTCGTCTCGGTCTACGCCGTGGTGGAGACCACGACTGGCACGATCCTGGCCGGCCCCCACATCCAGGCGCGGGGCGTGGCGGAGGACGACTCGGTCTTCGAGGAGATCCTTCCCGATGTGACCGAGGCCCTGTCGGCTGCGCTGGAGACCGGGAAGGCGGACGCCTACTCCCTCCAGCAGGTCATGCGCCGCACCCTGGGGCGCTGGATCGGGCGCCGCCTCAGGCGCCGTCCCATGATCGTCCCGGTCGTCATCGAGGCATAG","MRITPLGGLGEVGRNMTVFELDGKLLIVDCGVLFPEEDQPGVDLILPDFSSIEHRIDDVVALVLTHGHEDHIGGVPYLLRLREDIPLVGSELTLAFVEAKLKEHRIRPVLRQVVEHEEVSYGPFDLEFVAVNHSIPDAMAVMIRTDAGKVLATGDFKMDSLPIDGRITDLRSFARFGEEGVDLFCVDSTNAEVPGMVGHEGEIGQVLDNVFADSDGQIVVASFASHVHRVQQVLDAAALHDRRVALVGRSMVRNMGIAAERGYLKVPAGVLIDARDITSLPPHERVLMVTGSQGEPMAALSRMAHSEHRSVTIEPGDTVIFASSLIPGNENSVFRVINQLMRLGARVVHQGNAKVHVSGHASSEELLHVYNIVQPRNVMPIHGEIRHLVANGGLAVKTGIAPERVMLCEDGVAVDLEGGVARIAGQVPCGYIYVDGSSVGEIDEAELKDRRILAEEGFVSVYAVVETTTGTILAGPHIQARGVAEDDSVFEEILPDVTEALSAALETGKADAYSLQQVMRRTLGRWIGRRLRRRPMIVPVVIEA$","Hydrolase of the metallo-beta-lactamase superfamily","Cytoplasm","predicted hydrolase of themetallo-beta-lactamase superfamily","putative hydrolase of the metallo-beta-lactamase superfamily","beta-lactamase domain protein","","Carfi A., Pares S., Duee E., Galleni M., Duez C., Frere J.M., Dideberg O. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 1995. 14(20):4914-4921. PMID: 7588620","","","

InterPro
IPR001279
Domain

Beta-lactamase-like
PF00753	$\"[13-169]T$	Lactamase_B

InterPro
IPR011108
Domain

RNA-metabolising metallo-beta-lactamase
PF07521	$\"[347-386]T$	RMMBL

noIPR
unintegrated

unintegrated
G3DSA:3.60.15.10	$\"[1-189]T$	no description

","BeTs to 13 clades of COG0595COG name: Predicted hydrolase of the metallo-beta-lactamase superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0595 is -om-k---vdrlbc------ujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB011108 (RNA-metabolising metallo-beta-lactamase) with a combined E-value of 2.7e-19. IPB011108A 25-34 IPB011108B 59-77 IPB011108C 373-384","Residues 3-44 are 78% similar to a (HYDROLASE METALLO-BETA-LACTAMASE SUPERFAMILY FAMILY ZN-DEPENDENT UPF0036 PREDICTED 3.-.-.- LACTAMASE METAL) protein domain (PD467742) which is seen in Q8RAH0_THETN.Residues 61-86 are 96% similar to a (HYDROLASE METALLO-BETA-LACTAMASE SUPERFAMILY FAMILY ZN-DEPENDENT UPF0036 YCBL BETA-LACTAMASE-LIKE PREDICTED 3.-.-.-) protein domain (PD125043) which is seen in Q8G528_BIFLO.Residues 90-407 are 77% similar to a (HYDROLASE METALLO-BETA-LACTAMASE SUPERFAMILY FAMILY ZN-DEPENDENT UPF0036 PREDICTED METAL 3.-.-.- DEPENDENT) protein domain (PD006373) which is seen in Q82K88_STRAW.Residues 419-518 are 74% similar to a (HYDROLASE METALLO-BETA-LACTAMASE SUPERFAMILY FAMILY ZN-DEPENDENT UPF0036 METAL PREDICTED 3.-.-.- DEPENDENT) protein domain (PD039891) which is seen in Q6ADZ4_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 169 (E_value = 1.2e-20) place ANA_0396 in the Lactamase_B family which is described as Metallo-beta-lactamase superfamily.Residues 347 to 386 (E_value = 6.8e-10) place ANA_0396 in the RMMBL family which is described as RNA-metabolising metallo-beta-lactamase.","","hydrolase of the metallo-beta-lactamase superfamily (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0397","410739","411674","936","4.87","-14.74","32552","ATGACTCTCTTCCGGCCCGCATGCTTCATATCCACCGGATCCATCCTCATTGACATCCCCCTCCACGTCAGCCGTGTGCCGACGCCGGGAGGGGCGATCACCGGTGCGTCGTCGGGTCCGGTCGTGGGTGGCGGGTACACCGTGGTCTCGGCCGCAGCCCGTCAGGGCGTTCCCACGGCCCTGGCCGCCACCTTGGGAACCGGACCCAACTCCGCGCGGGTGCGTGAGTCGATGCGGCTGGACCGGGTCGAGCTGCTCGTCGAGGAGCTCGTCGGGGACATCGGCACCTGCACCACGCTTATCGAGCCCTCCGGCCGACGCACCTTCATCACCACCGCGGGCGTGGAGGGCGAGCCTCAGCGTGAGGATCTCGAGAGCCTCGACCTGAGGGCCGGGGACTGGGTCTACGCCACGGGCTACGATCTGGCCCACTACACGAGCCGCGGCATCCTGGCCGACTGGCTGCTGTCGATCCCCGACGGCGTCGGGCTGGTGATCGACCTTGGTCCGGTCCAGCCCGATATCCCGGACCAGGTGCTCCTACCGCTGCTGGGTCGAGCGACGATGCTGACCGGCAATGACTTGGAGATGAGCCGGCTCGAGGAACGCCTGGGTGGCATGAGGGCCATCCGGCAGGCGTGTCCGCAGGCACTGATCGTCCACCGTACCGGTGTCGACGGCTGTGTCCTCCATCCGGTGGGTGAGGCGGCGATCGAGGTTCCCGGTTTCGTGCGCGAGGTCGTGGACACCACGGGGGCGGGAGACACGCATACCGGTGTTCTGGTCGCCGGCCTTCTTGACGGACTCGATGTCGTTGAGGCGGCCAGGCGTGCCAACGCGGCCGCGGCCCACGCCGTCGCCTGCAGCGGCCCGGCCCAGGCCCCGCTGCGCGAGGAGATCGATGAGTTCCTCCGGGTATGCGATGAGAGGCTCTGA","MTLFRPACFISTGSILIDIPLHVSRVPTPGGAITGASSGPVVGGGYTVVSAAARQGVPTALAATLGTGPNSARVRESMRLDRVELLVEELVGDIGTCTTLIEPSGRRTFITTAGVEGEPQREDLESLDLRAGDWVYATGYDLAHYTSRGILADWLLSIPDGVGLVIDLGPVQPDIPDQVLLPLLGRATMLTGNDLEMSRLEERLGGMRAIRQACPQALIVHRTGVDGCVLHPVGEAAIEVPGFVREVVDTTGAGDTHTGVLVAGLLDGLDVVEAARRANAAAAHAVACSGPAQAPLREEIDEFLRVCDERL$","Ribokinase","Cytoplasm","ribokinase","putative sugar kinase","PfkB domain protein","","Sigrell J.A., Cameron A.D., Jones T.A., Mowbray S.L. Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures. Structure 1998. 6(2):183-193. PMID: 9519409","","","

InterPro
IPR011611
Domain

PfkB
PF00294	$\"[13-299]T$	PfkB

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[9-307]T$	no description
PTHR10584	$\"[12-301]T$	SUGAR KINASE RELATED
PTHR10584:SF16	$\"[12-301]T$	UNCHARACTERIZED
signalp	$\"[1-16]?$	signal-peptide

","BeTs to 12 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","Residues 7-257 are 49% similar to a (KINASE TRANSFERASE RIBOKINASE SUGAR FRUCTOKINASE CARBOHYDRATE FAMILY PFKB ADENOSINE KINASE) protein domain (PD023180) which is seen in Q98JW9_RHILO.Residues 10-258 are 43% similar to a (KINASE FAMILY CARBOHYDRATE SUGAR PROBABLE PFKB) protein domain (PD823422) which is seen in Q8CY55_BIFLO.Residues 93-193 are 55% similar to a (KINASE TRANSFERASE SUGAR YEGV SIMILAR) protein domain (PD035550) which is seen in Q7MY13_PHOLL.","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 299 (E_value = 5.8e-24) place ANA_0397 in the PfkB family which is described as pfkB family carbohydrate kinase.","","(sugar) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0398","416079","414736","1344","4.86","-21.29","45790","ATGCACTCCTCCACCTCTCTACCATCACCTTCACCAGGCTCCGCATGTCTCACCCGCAGGTCACGAGGACCGGCCCTGCTGACCGCCGTCGTTCTCACCGCATCCGTCGCCATGAACGGTTGCTCGACGAGTTCCGATCAGGCTGTGCCGGCTCAATCGCCGACTCCGTCCGCCTCCGCCAGCGTCGGCGGCTCGCAGGACGTGCACTTCACGGTGGGTTACGCCGGCGACGTCCTCATGCACATGCCGGTAATGGAATCCACTCCGGCAGGCTCAGGGGATATCACCGCCAACATCGCCGCTGAGACCCCCTGGGTCGAGGGCCTGGATCTGGCCCTGTGCGGGATGGAGGTACCTGTCGCTCCGGACGGGGTCTACTCGGGCTACCCCGCCTTCGGCACCTCTACCGAGGTCGTGGCCGCCTTGGCGAGATCCGGATGGGACGGCTGCGCGACCGCCTCCAACCACGCTGCGGACCGGGGGGAGTCCGGCGTCGTGGCCACCTTGGACGCCCTGGACGCTCACGGGATGGGCCACGCAGGCACCTACCGGAGCCGACAGGACGCCTCGGTCCCCTTCGCGCTCTACGAGCTTGAGCGGGGTGGGCGCACCGTGACCGTCGCCCAGATCTCCACGACCATGGACCTCAACGGCCTGGAGGATCCCACCGGCTACTCGGTGGCACTCAACGACGTCGGCGCCATCACGAAGGCGGCAACGTCGGCCCGTGCGGCGGGCGCCGACCTCGTCGTCGTCCAATCCCAGCTCGGTGAGGAGTACGAGACCACGCCCAACGACGCGCAGGTCTCCTATGCCCAGGCCCTGGCAGACAGCGGGCAGATCGACATCCTCTTCGGCGCTCACCCTCATGTGCCTCAGCCCGCCGAGAAGCTCTCCGGAGGAGTCGGGGGCAAGGGGATGTGGGTGTCGTACTCGGCCGGCAACTACATCTCGAACCAGGATGAGGAGTGCTGCGCCCCGCTGTCCGACGTCGGTCAGCTGGTCTGGGCCGACGTCACCTCCCACGCCGACGGCTCAGTGAGCGTGGACAAGCTGAACTGGCACCCGTTCACCATGGATCTCGCCGGTGGCTACAAGATCCGGGACCTGGCGGCGCTTCACAACGGTGAACGCTCTGCCGACCTGGGCCTGAGCACGGAGGAGATCGACCGGCGCTGGAACCTGCTGACCGCTCAGGTCAAGGACGCCTCGACCGTGTCCACCACACCGCCCAAGGCCACCGGACCGGCTCCGACGATTCCCAGCCGGGACGAGGTCATCACACGGGCAGGGGCCCACCCGGGCCCGCAGGGCACGGCATCGGCCTCCCCCTCACCACGATGA","MHSSTSLPSPSPGSACLTRRSRGPALLTAVVLTASVAMNGCSTSSDQAVPAQSPTPSASASVGGSQDVHFTVGYAGDVLMHMPVMESTPAGSGDITANIAAETPWVEGLDLALCGMEVPVAPDGVYSGYPAFGTSTEVVAALARSGWDGCATASNHAADRGESGVVATLDALDAHGMGHAGTYRSRQDASVPFALYELERGGRTVTVAQISTTMDLNGLEDPTGYSVALNDVGAITKAATSARAAGADLVVVQSQLGEEYETTPNDAQVSYAQALADSGQIDILFGAHPHVPQPAEKLSGGVGGKGMWVSYSAGNYISNQDEECCAPLSDVGQLVWADVTSHADGSVSVDKLNWHPFTMDLAGGYKIRDLAALHNGERSADLGLSTEEIDRRWNLLTAQVKDASTVSTTPPKATGPAPTIPSRDEVITRAGAHPGPQGTASASPSPR$","Poly-gamma-glutamate synthesis protein (capsule biosynthesis protein)","Extracellular, Periplasm","putative lipoprotein","K07282 poly-gamma-glutamate synthesis protein (capsule biosynthesis protein)","Putative enzyme of poly-gamma-glutamate biosynthesis (capsule formation)-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide

","BeTs to 4 clades of COG2843COG name: Putative enzyme of poly-gamma-glutamate biosynthesis (capsule formation)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG2843 is ---------drlb------n-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 110-181 are 69% similar to a (CAPA CAPSULE BIOSYNTHESIS LIPOPROTEIN PLASMID SYNTHESIS DOMAIN POLYGLUTAMATE POLY-GAMMA-GLUTAMATE YWTB) protein domain (PD135685) which is seen in Q9RCW9_STRCO.Residues 138-356 are 52% similar to a (HYDROLASE 5_apos;-NUCLEOTIDASE 2_apos;-PHOSPHODIESTERASE 2_apos;3_apos;-CYCLIC-NUCLEOTIDE UDP-SUGAR WALL SIGNAL CELL PEPTIDOGLYCAN-ANCHOR PRECURSOR) protein domain (PD002576) which is seen in Q6A8I1_PROAC.Residues 182-406 are 40% similar to a () protein domain (PD833906) which is seen in Q8G428_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","lipoprotein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0399","411832","414747","2916","5.28","-23.50","102183","ATGGCCAATCGTCGCACCACGAGAACAGCTGCGTCTTCATCAGGAACCGGCAGAGGGCGTAATCGAGGTGGCTCCGCTCCAGGGGCCGCTCCCTTCTCTGCGCCTGGAACCGGACCCTCTGGCGGACGCTACCGCCGCACCGGCTGGGCCTTTCTCATTCTGGCCCTCGCAGCGGTGCTGGCGCTGCGCGAGTGGTTCGGGATCTCCGGCGCCGCAGGCGATCTCCTGCACCACATCGCCGCGGGCCCTGTGGGTGTCCTGGGCATCTTCGTGCCCCCGCTCCTGGCGGCGCTGGGCGTCGCCATGCTGCGGGTCCACAACCTGGGGGCGGTGCACGCGCGGGTCTCCGTGGGCTGCCTGGGGCTGCTGACGGCTCTGACCGGAATGATCCAGGTCGGCAGCGGCAACCCGGTCCTCAAGAACAACCTCGGCGGACTGGAAGCAGCTGGGGGGCTGCTGGGATGGCTGGTGGGCTACCCCCTGGCGGCGCTGTTCTCCTCCGTGGGGGCCTTCATCCTGTTCATCCTCCTGACTGCGTTCTCCGCACTGGTCCTGTCCGGCAAGACTGTTGCCGAGATCCGTGAGCTGTTGGAGCAGCGCCGGGCCTCAGAGGGTGACAGCCCCGCCCAGGGCGCCGGTGGCATCGGTGACTCCCTGGCTCGGCGCCTGCTCGGACGCGCGCGTGGAAACGCTGGGCGAGCCGCCGCCTCGGGTGAGGACCCGGATCAGACGGCGCTCCTGGACTCCTACGACGGTGACGAGCCCTTCCGCTCCGCCTTGGAGGTGGAGGAGTCGGCTTCTCGTAAGCGGGGCAGCGGCCGGCGCAAGCGCTCGGCCGACCGGCAGGCCCAGCAGACGACGATCACCGAGCTCTTCGAGCCGGGCGGCGATCACGGTGCTCACTCCGGCAGCGAGGACTTCGTCATCCCGGACGTGGGCGAGGAGACCGACGTCATCGCCTCCCCGGCGCCCTCAGCCTCCTCTCCTGCTCGGAGCAGGCCCACCGGCTCGACAGGTGGCCCCGCGGCCTCCGGCCCAGTCTCAGGGGGACAGCGCAAACCCTCATCCGCCAAGCGCACGGCTACGAAGCCAGCTCCTCAGACACCGTCCGGTTTCGACGCCGTCACCGAGGAGACCCCCGAGGTCGTGCTCGAGGAGCCCGACCTCGCCGACCAGATCGCCATGGGCAACATGTCGTTGCCTGACGGCTCGACCTACACCCTGCCCGAGGACGCGCTGCTCGGTCCAGGGCCGGGACACTCCACCCGCACCCCCGCCAACGACGCCATCGTCGAGGCTCTGCAGAATGTCTTCGCCGAGTTCAACGTGGACGCCACGGTCACCGGCTACACACGCGGTCCTCAGGTCACCCGCTACGAGGTCCACCGGGGTCGGGGGGTCAACGTCTCCCGGATCACGGGGCTGGAGAAGAACATCGCCTACGCGGTGGCCTCCGACGAGATCCGTCTGCTCACCCCCATTCCGGGAAAGAGCGCCATTGGCATCGAGATCCCCAACAGCGACCGGGAGATGGTCAAGCTCGGCGACGTCCTGCGCTCCCAGGCCGCGCGCAAGCAGGCGCACCCGCTGGTGGTCGGGTTGGGCAAGAACGTTGAGGGCGACTACGTCGTCACCAACCTGGCCAAGACCCCGCACCTTCTGGTGGCCGGTCAGACCGGTTCGGGTAAGTCCTCCTTCGTCAACTCGATGATCACCTCGATCATGATGCGTGCCACGCCTGAGGAGGTGCGCATGGTGCTGGTGGACCCCAAGCGGGTGGAGCTGACCATCTACGAGGGCATCCCCCACCTCATCACGCCGATCATCACCTCCCCGAAGAAGGCGGCCGAGGCTCTGGAGTGGGTGGTGCGCGAGATGGACGCCCGCTACGACGACCTGGCCTCCTTCGGTTTCAAGCACATCGACGACTTCAACAAGGCAGTGCGGGCCGGAGAGGTCCAGCCCCTGCCGGGATCCCAGCGAGAGCTGAGCCCCTACCCCTACCTCCTGGTCGTCGTTGACGAGCTCGCCGACCTCATGATGACCGCCCCTAAGGACGTGGAGGCCTCCATCCAGCGCATCACCCAGCTGGCCCGCGCTGCCGGGATCCACCTGGTCCTGGCCACCCAGCGACCCGTCGCCCAGGTCGTCACCGGCCTCATCAAGTCCAACGTCCCCTCGCGCCTGGCCTTCGCCACGGCCTCCCAGCTGGACTCTCGGGTCATCCTCGACCAGAACGGGGCTGAGACGCTCACCGGCCAGGGTGACGCCCTCTACCTGGGCCCGGGCGCCTCGACGCCAGTGCGTATCCAGGGCTCGTGGGTCACCGAGTCCGAGATCCGCTCCGTCGTCGAGCACGTCAAGTCCCAGCTGACGCCCGAGTACCGCGAGGACGTCGTCGTCCCGGAGGTCAAGAAGCAGATCGACGAGGAGATCGGTGATGACATGGACCTGCTCCTGCAGGCCGCCGAGCTCATCATCTCCAGTCAGTTCGGCTCCACCTCCATGCTCCAGCGCAAGCTGCGCGTCGGCTTCGCCAAGGCCGGACGCCTCATGGACCTGCTCGAGTCGCGTGAGGTCGTCGGCCCCTCGGAGGGTTCCAAGGCCCGCGACGTCCTCGTCCAGCCCGAGCAGCTCGAGGAGACCCTGGCCTGGATCAAGGGCGAGGGCGGTGCGCCGGGAAGCGCTGAGAGTCCCGAAGCCCCTGACGCCTCTCAAGGCGAGCCCGATTCCGAGGCCCCGTCGGCTCCGGCCGCGAATGAGCCCCGTACTGCGGTCATGCCGTCGAACCGCTACAGCACGGATCCGTTGGAGGTCGCCTCGAGCCTGCCGGAGTCTGAGTCCTGGGACGACACCTCCGCCGATGAGGACTCCGAGGACGCCTGGTCGCTCACTGGCCGCGGCTCATCGTGGTGA","MANRRTTRTAASSSGTGRGRNRGGSAPGAAPFSAPGTGPSGGRYRRTGWAFLILALAAVLALREWFGISGAAGDLLHHIAAGPVGVLGIFVPPLLAALGVAMLRVHNLGAVHARVSVGCLGLLTALTGMIQVGSGNPVLKNNLGGLEAAGGLLGWLVGYPLAALFSSVGAFILFILLTAFSALVLSGKTVAEIRELLEQRRASEGDSPAQGAGGIGDSLARRLLGRARGNAGRAAASGEDPDQTALLDSYDGDEPFRSALEVEESASRKRGSGRRKRSADRQAQQTTITELFEPGGDHGAHSGSEDFVIPDVGEETDVIASPAPSASSPARSRPTGSTGGPAASGPVSGGQRKPSSAKRTATKPAPQTPSGFDAVTEETPEVVLEEPDLADQIAMGNMSLPDGSTYTLPEDALLGPGPGHSTRTPANDAIVEALQNVFAEFNVDATVTGYTRGPQVTRYEVHRGRGVNVSRITGLEKNIAYAVASDEIRLLTPIPGKSAIGIEIPNSDREMVKLGDVLRSQAARKQAHPLVVGLGKNVEGDYVVTNLAKTPHLLVAGQTGSGKSSFVNSMITSIMMRATPEEVRMVLVDPKRVELTIYEGIPHLITPIITSPKKAAEALEWVVREMDARYDDLASFGFKHIDDFNKAVRAGEVQPLPGSQRELSPYPYLLVVVDELADLMMTAPKDVEASIQRITQLARAAGIHLVLATQRPVAQVVTGLIKSNVPSRLAFATASQLDSRVILDQNGAETLTGQGDALYLGPGASTPVRIQGSWVTESEIRSVVEHVKSQLTPEYREDVVVPEVKKQIDEEIGDDMDLLLQAAELIISSQFGSTSMLQRKLRVGFAKAGRLMDLLESREVVGPSEGSKARDVLVQPEQLEETLAWIKGEGGAPGSAESPEAPDASQGEPDSEAPSAPAANEPRTAVMPSNRYSTDPLEVASSLPESESWDDTSADEDSEDAWSLTGRGSSW$","DNA segregation ATPase FtsK/SpoIIIE","Cytoplasm, Membrane","ftsK homolog","K03466 DNA segregation ATPase FtsK/SpoIIIE; S-DNA-T family","cell divisionFtsK/SpoIIIE","","Morett E., Segovia L. The sigma 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol. 1993. 175(19):6067-6074. PMID: 8407777Austin S., Kundrot C., Dixon R. Influence of a mutation in the putative nucleotide binding site of the nitrogen regulatory protein NTRC on its positive control function. Nucleic Acids Res. 1991. 19(9):2281-2287. PMID: 2041769Albright L.M., Huala E., Ausubel F.M. Prokaryotic signal transduction mediated by sensor and regulator protein pairs. Annu. Rev. Genet. 1989. 23:311-336. PMID: 2694934Austin S., Dixon R. The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent. EMBO J. 1992. 11(6):2219-2228. PMID: 1534752","","","

InterPro
IPR002078
Domain

RNA polymerase sigma factor 54, interaction
PS00675	$\"[553-566]?$	SIGMA54_INTERACT_1

InterPro
IPR002543
Domain

Cell divisionFtsK/SpoIIIE
PF01580	$\"[513-714]T$	FtsK_SpoIIIE
PS50901	$\"[540-740]T$	FTSK

noIPR
unintegrated

unintegrated
PTHR22683	$\"[420-830]T$	SPORULATION PROTEIN RELATED
PTHR22683:SF1	$\"[420-830]T$	DNA TRANSLOCASE FTSK
signalp	$\"[1-61]?$	signal-peptide
tmhmm	$\"[49-69]?$ $\"[79-101]?$ $\"[116-136]?$ $\"[142-162]?$ $\"[167-187]?$	transmembrane_regions

","BeTs to 15 clades of COG1674COG name: DNA segregation ATPase FtsK/SpoIIIE and related proteinsFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG1674 is ---------drlb-efghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB002543 (Cell divisionFtsK/SpoIIIE protein) with a combined E-value of 1.5e-35. IPB002543A 551-564 IPB002543B 608-634 IPB002543C 691-720","Residues 44-195 are 59% similar to a (DIVISION CELL FTSK TRANSMEMBRANE ATP-BINDING TRANSLOCASE DNA-BINDING CHROMOSOME DNA PARTITION) protein domain (PD152674) which is seen in FTSK_BIFLO.Residues 428-540 are 80% similar to a (DIVISION CELL ATP-BINDING FTSK DNA TRANSLOCASE TRANSMEMBRANE DNA-BINDING CHROMOSOME PARTITION) protein domain (PD006902) which is seen in Q6ADZ5_BBBBB.Residues 543-683 are similar to a (ATP-BINDING CELL DIVISION DNA FTSK TRANSMEMBRANE TRANSLOCASE DNA-BINDING CHROMOSOME PARTITION) protein domain (PD002076) which is seen in Q6A806_PROAC.Residues 679-755 are 79% similar to a (ATP-BINDING CELL DIVISION FTSK DNA TRANSMEMBRANE TRANSLOCASE DNA-BINDING CHROMOSOME PARTITION) protein domain (PD037665) which is seen in Q820U2_ENTFA.Residues 738-788 are 80% similar to a (DIVISION CELL ATP-BINDING FTSK DNA TRANSLOCASE TRANSMEMBRANE DNA-BINDING CHROMOSOME PARTITION) protein domain (PD470519) which is seen in Q6A806_PROAC.Residues 795-874 are 92% similar to a (DIVISION CELL ATP-BINDING FTSK DNA TRANSLOCASE TRANSMEMBRANE DNA-BINDING CHROMOSOME PARTITION) protein domain (PD006901) which is seen in FTSK_STRCO.","","-61% similar to PDB:2IUT P. AERUGINOSA FTSK MOTOR DOMAIN, DIMERIC (E_value = 7.0E_104);-62% similar to PDB:2IUS E. COLI FTSK MOTOR DOMAIN (E_value = 1.2E_100);-64% similar to PDB:2IUU P. AERUGINOSA FTSK MOTOR DOMAIN, HEXAMER (E_value = 1.4E_96);","Residues 513 to 714 (E_value = 8e-72) place ANA_0399 in the FtsK_SpoIIIE family which is described as FtsK/SpoIIIE family.","","homolog ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0400","416320","416943","624","11.27","9.93","22347","ATGAACGCCCCGACCGCCCCGGATGGCGCCGCGCCGTCAGAGCAGGCGCCGCTGCTCAACATCGCCAACGTCCTGACGGTGCTGCGCCTGCTGCTCGTGCCCGTCTTCATCTGGCTCTCTCTGCTGCCCGGGGACCGGGCCAGGCTCGCCGCAGTCGTGGTCTTTGTCGTGGCGGCCTTCACGGACCGCCTTGACGGCCAGCTGGCGCGCTCGTGGGGGCTGGTGACCTCCTTCGGCAAGATCGCCGACCCGATCGCGGACAAGGCGCTGACCCTGTCCGCCTTCGTTCTGCTGAGTATCAACCAACGACTGTGGTGGTGGGTCACCATCCTCATCGTCGTGCGCGAGCTCGGCATCACGGTTCTGCGCTTCTTCATGCTGCGCCGTGCCGTCATGGCGGCCTCGCGCGGCGGCAAGATCAAGACGACGCTGCAGATGGTGGGGCTGGTCGGGCTGCTCACGCCGTGGTCCATGCTCCTGCTTCCCGCGGGCCCGGCCGCGTTCCTGACTAAGACGGCCTACGTCATTGTGGCTGCGGCACTCATCGTCACGGTGGTGACTGGCCTGGACTATGTTCGCGAGGCGATGCGGCTGAGCCGTCAGAGTGGACGGAGCGGCCAGTGA","MNAPTAPDGAAPSEQAPLLNIANVLTVLRLLLVPVFIWLSLLPGDRARLAAVVVFVVAAFTDRLDGQLARSWGLVTSFGKIADPIADKALTLSAFVLLSINQRLWWWVTILIVVRELGITVLRFFMLRRAVMAASRGGKIKTTLQMVGLVGLLTPWSMLLLPAGPAAFLTKTAYVIVAAALIVTVVTGLDYVREAMRLSRQSGRSGQ$","CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase","Membrane, Cytoplasm, Extracellular","CDP-diacylglycerol--glycerol-3-phosphate3-phosphatidyltransferase","CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase ","CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase","","Nikawa J., Kodaki T., Yamashita S. Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae. J. Biol. Chem. 1987. 262(10):4876-4881. PMID: 3031032Hjelmstad R.H., Bell R.M. sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products. J. Biol. Chem. 1991. 266(8):5094-5134. PMID: 1848238","","","

InterPro
IPR000462
Family

CDP-alcohol phosphatidyltransferase
PF01066	$\"[52-194]T$	CDP-OH_P_transf
PS00379	$\"[65-87]T$	CDP_ALCOHOL_P_TRANSF

InterPro
IPR004570
Family

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
TIGR00560	$\"[19-202]T$	pgsA: CDP-diacylglycerol--glycerol-3-phosph

noIPR
unintegrated

unintegrated
PIRSF000847	$\"[19-203]T$	CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
PTHR14269	$\"[18-202]T$	CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED
PTHR14269:SF3	$\"[18-202]T$	CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE
signalp	$\"[1-47]?$	signal-peptide
tmhmm	$\"[19-39]?$ $\"[49-64]?$ $\"[105-127]?$ $\"[148-168]?$ $\"[174-192]?$	transmembrane_regions

","BeTs to 20 clades of COG0558COG name: Phosphatidylglycerophosphate synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0558 is aompkzyqv-rlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 4","***** IPB000462 (CDP-alcohol phosphatidyltransferase) with a combined E-value of 2.3e-18. IPB000462 51-98","Residues 61-96 are 86% similar to a (TRANSFERASE SYNTHASE CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE PHOSPHATIDYLTRANSFERASE PHOSPHATIDYLGLYCEROPHOSPHATE 3-PHOSPHATIDYLTRANSFERASE CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE 3- PHOSPHATIDYLSERINE) protein domain (PD329097) which is seen in Q8FPC5_COREF.Residues 106-158 are 77% similar to a (TRANSFERASE SYNTHASE CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE PHOSPHATIDYLGLYCEROPHOSPHATE PHOSPHATIDYLTRANSFERASE 3- 3-PHOSPHATIDYLTRANSFERASE PGP CDP-DIACYLGLYCEROL-GLYCEROL-3-PHOSPHATE TRANSMEMBRANE) protein domain (PD033022) which is seen in Q6ADZ6_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 52 to 194 (E_value = 1.1e-28) place ANA_0400 in the CDP-OH_P_transf family which is described as CDP-alcohol phosphatidyltransferase.","","3-phosphatidyltransferase (pgsA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0401","416966","417487","522","6.52","-1.70","17717","GTGATCGTGGATGCGCAGGGCGCCCAGGACCGTGTCCGCGTGGCGAAGGCTCTGCTGCAGGCCGCTGCGGACCACGGAGTGACTCTGGCGATCGCCGAGTCGCTGACGGGCGGGCAGGTCTCCTCCAGTCTGGTGGAGGTCTCCGGTGCCTCCCGTGTGCTCGTGGGAACGGTCGTGGCCTATGCCACCCGGATCAAGGCGCAGCTCCTCGGGGTCGATGCTGCGCACCTGGAGCGGACCGGGCCGGTGGACCGTGATGTCGCCCTGCAGATGGCGGATGGAGTACGCCGGCTCCTCGGGGCCGATGTGGGGCTGGCCACCACCGGGGTGGCCGGGCCGGGGCCGGCCGACGGTCATCCGGCCGGAACGGTCCATGTCGCGGTTGTTGCCCCATGGGGGCAGAGGCACCGCGAGCTGCACCTGGGCGGTGATCGCTCGCAGATCCGGTGCGCCACCGTGATGGAGGTGTGCGAGCTGGCCATCGGCTTCCTACAGAAGGACGAGTGTGGGCCGCAGCCCTGA","VIVDAQGAQDRVRVAKALLQAAADHGVTLAIAESLTGGQVSSSLVEVSGASRVLVGTVVAYATRIKAQLLGVDAAHLERTGPVDRDVALQMADGVRRLLGADVGLATTGVAGPGPADGHPAGTVHVAVVAPWGQRHRELHLGGDRSQIRCATVMEVCELAIGFLQKDECGPQP$","Competence/damage-inducible protein CinA","Cytoplasm","CinA protein","K03743 competence/damage-inducible protein CinA C-terminal domain","CinA domain protein","","Pearce B.J., Naughton A.M., Campbell E.A., Masure H.R. The rec locus, a competence-induced operon in Streptococcus pneumoniae. J. Bacteriol. 1995. 177(1):86-93. PMID: 7798154Martin B., Garcia P., Castanie M.P., Claverys J.P. The recA gene of Streptococcus pneumoniae is part of a competence-induced operon and controls lysogenic induction. Mol. Microbiol. 1995. 15(2):367-379. PMID: 7538190","","","

InterPro
IPR008136
Domain

CinA, C-terminal
PF02464	$\"[11-164]T$	CinA
TIGR00199	$\"[18-161]T$	cinA_cterm: competence/damage-inducible pro

InterPro
IPR012244
Family

Uncharacterised conserved protein CinA
PIRSF006161	$\"[13-168]T$	Uncharacterised protein related to CinA

noIPR
unintegrated

unintegrated
PD004924	$\"[32-158]T$	Q6ADZ7_BBBBB_Q6ADZ7;

","BeTs to 14 clades of COG1546COG name: Uncharacterized protein (competence- and mitomycin-induced)Functional Class: R [General function prediction only]The phylogenetic pattern of COG1546 is -o-----qvdrlbcefg-snuj---wNumber of proteins in this genome belonging to this COG is 1","***** IPB008136 (CinA, C-terminal) with a combined E-value of 5.4e-18. IPB008136 54-106","Residues 32-158 are 59% similar to a (CINA-LIKE CINA COMPETENCE-DAMAGE COMPETENCE/DAMAGE-INDUCIBLE INDUCIBLE COMPETENCE-DAMAGED DOMAIN YGAD CINA-RELATED COMPETENCE) protein domain (PD004924) which is seen in Q6ADZ7_BBBBB.","","-45% similar to PDB:2A9S The crystal structure of competence/damage inducible protein CihA from Agrobacterium tumefaciens (E_value = 6.3E_11);","Residues 11 to 164 (E_value = 3.3e-44) place ANA_0401 in the CinA family which is described as Competence-damaged protein.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0402","417649","418059","411","8.97","2.64","15022","ATGAACAACACGACTCACCCCCGCACCACTCGCCCGATCAACAACCGGATGCCGATGCGCCAGGGACCCGGGGCAGGGTACGGTGTGTCCGTGGACACCCCGAAGCACGAGAATGTCGTCCTGCGCCGCGAGATCGGAGAAGTCCTGCGCGGCGTCCGACAGCACCAGGGACGCACGCTGCGCGAGGTCTCCTCGCAGGCCCGTGTCTCCCTGGGATACCTCTCCGAGGTCGAGCGCGGTCAGAAGGAGGCCTCCTCCGAGCTGCTCGCCTCCATCTGCCAGGCGCTTGACGCCCCCCTGTCCATGGTGCTGCGTGAGGTCTCCGACCGCATCGCCCTGACCGAGGGCGTCATGATTCCGGACACGGTTCCCGATGAGCTCGTGCGTCAGCAGGGGGTCGCCCTGCGGTGA","MNNTTHPRTTRPINNRMPMRQGPGAGYGVSVDTPKHENVVLRREIGEVLRGVRQHQGRTLREVSSQARVSLGYLSEVERGQKEASSELLASICQALDAPLSMVLREVSDRIALTEGVMIPDTVPDELVRQQGVALR$","Transcriptional regulator, XRE family","Periplasm, Cytoplasm","possible DNA binding protein","hypothetical protein","helix-turn-helix domain protein","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[49-103]T$	HTH_3
SM00530	$\"[48-103]T$	HTH_XRE
PS50943	$\"[49-103]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[45-106]T$	no description

","BeTs to 8 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","Residues 45-105 are similar to a (TRANSCRIPTIONAL DNA-BINDING REGULATOR REGULATOR FAMILY PLASMID REPRESSOR TRANSCRIPTION REGULATORY CRO/CI) protein domain (PD000418) which is seen in Q6A905_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 49 to 103 (E_value = 2e-07) place ANA_0402 in the HTH_3 family which is described as Helix-turn-helix.","","DNA binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0403","418189","418407","219","4.87","-3.88","8056","GTGAAGCACTCGGAGTTCTGGAACGCCGTCGAGGCGGTCTTCGGTCCGGCCTACGGCCGGTCCCTGGCTCAGGATCTGGTTCTTCCGGGGCTGGGGGTGACCTGCGTGCAGGCGCTCGACGACGGAGTGGCCCCGGAGCGGGTCTGGGGTCTTCTGTGCGAGGAGACCGAGCGCTCGGATGCCGAGCGGTGGATCTTCCGCTCGGATCCGCGTCGCTGA","VKHSEFWNAVEAVFGPAYGRSLAQDLVLPGLGVTCVQALDDGVAPERVWGLLCEETERSDAERWIFRSDPRR$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0405","418675","419916","1242","6.14","-2.27","42905","ATGCCTGCTGCCAGCCAGACCCAGGACCGTTCCAAGGCCCTGGCCACAGCCCTCGCCCAGATCGACAAGAGCTTCGGTAAGGGATCCGTCATGCGCCTGGGGGACGAGTCCCGTCCTCCGGTCTCCGTCATCCCGACCGGGTCAGTCGCCCTCGATGTGGCTCTGGGAGTCGGAGGACTCCCGAGGGGACGCATCGTCGAGGTCTACGGGCCGGAGTCCTCCGGAAAGACCACCGTCGCCCTGCACGCCGTGGCCAGCGCGCAGAGGGCCGGCGGGAACGCGGCCTTCATCGACGCCGAGCACGCCCTCGACCCGGTCTACGCCAAGGCCCTGGGCGTCGACATTGACAACCTCCTGGTCTCACAGCCGGACACCGGGGAGCAGGCCCTGGAGATCACCGACATGCTGGTGCGCTCAGGAGGCCTGGACATCATCGTCATCGACTCCGTGGCGGCTCTGGTCCCCAAGGCTGAGATCGAGGGGGAGATGGGGGACTCCCACGTCGGTCTCCAGGCCCGCCTCATGAGCCAGGCGCTGCGCAAGATCACCGGTGCGCTGTCCTCCACCGGCACCACCGCCATCTTCATCAACCAGCTGCGCGAGAAGATCGGTGTGTTCTTCGGCAACCCCGAGACCACCACCGGTGGAAAGGCCCTGAAGTTCTACGCCTCCGTGCGCCTGGACGTGCGCCGCATCGGCGGGCTCAAGGACGGGGACCAGCCCGTGGGTAACCGCACCCGGGTCAAGGTCGTCAAGAACAAGATGGCGCCGCCCTTCAAGCAGGCCGAGTTCGACATCCTCTACGGCCAGGGCATCTCCCGCGAGGGCAGCCTCCTGGACCTGGGCGTGGACAACGGCGTGGTGCGCAAGTCGGGGGCCTGGTTCACCTACGGGGAGGACCAGCTCGGTCAGGGCAAGGAGAATGCCCGCAACTTCCTCAAGGACAACCCACAGTTGGCTGCCGAGATCGAGGAGAAAATCCTCGCCGCCCTGGGCATCGGTGAGCCCGGCCGCAAGGCCCGGGAGGCTGAGGAGCTCGCCGCTGCCGAGGCCGCCGTGGCCGCGGCAGCCGTCCCGGTGGAGAGCGCTGACACCGCCGCCACGAGCGCGGTCAAGAGCGCCCGAGGGCGCGGGAAGAAGACCGCCGCAACCGCCAAAGCAGCCAAGAGCGTGAAGACTCCCAAGGAGGCGTCGTCGGATGAGCCGGACACCATCTTCGGTGAGGAGGCCGGCGGGTTCTGA","MPAASQTQDRSKALATALAQIDKSFGKGSVMRLGDESRPPVSVIPTGSVALDVALGVGGLPRGRIVEVYGPESSGKTTVALHAVASAQRAGGNAAFIDAEHALDPVYAKALGVDIDNLLVSQPDTGEQALEITDMLVRSGGLDIIVIDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKITGALSSTGTTAIFINQLREKIGVFFGNPETTTGGKALKFYASVRLDVRRIGGLKDGDQPVGNRTRVKVVKNKMAPPFKQAEFDILYGQGISREGSLLDLGVDNGVVRKSGAWFTYGEDQLGQGKENARNFLKDNPQLAAEIEEKILAALGIGEPGRKAREAEELAAAEAAVAAAAVPVESADTAATSAVKSARGRGKKTAATAKAAKSVKTPKEASSDEPDTIFGEEAGGF$","Recombinase A","Cytoplasm","RecA protein (Recombinase A)","putative RecA protein","recA protein","","Selbitschka W., Arnold W., Priefer U.B., Rottschafer T., Schmidt M., Simon R., Puhler A. Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobium leguminosarum biovar viciae. Mol. Gen. Genet. 1991. 229(1):86-95. PMID: 1896024Roca A.I., Cox M.M. RecA protein: structure, function, and role in recombinational DNA repair. Prog. Nucleic Acid Res. Mol. Biol. 1997. 56:129-223. PMID: 9187054Karlin S., Weinstock G.M., Brendel V. Bacterial classifications derived from recA protein sequence comparisons. J. Bacteriol. 1995. 177(23):6881-6893. PMID: 7592482Eisen J.A. The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species. J. Mol. Evol. 1995. 41(6):1105-1123. PMID: 8587109Cerutti H., Osman M., Grandoni P., Jagendorf A.T. A homolog of Escherichia coli RecA protein in plastids of higher plants. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(17):8068-8072. PMID: 1518831","","","

InterPro
IPR001553
Family

RecA bacterial DNA recombination
PD000229	$\"[161-209]T$	RECA_BIFLO_Q8G4G9;
PR00142	$\"[41-63]T$ $\"[67-96]T$ $\"[98-127]T$ $\"[132-161]T$ $\"[170-199]T$ $\"[215-243]T$ $\"[248-277]T$ $\"[302-319]T$	RECA
TIGR02012	$\"[9-329]T$	tigrfam_recA: protein RecA
PS50162	$\"[40-203]T$	RECA_2
PS50163	$\"[204-277]T$	RECA_3
PS00321	$\"[218-226]T$	RECA_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[62-233]T$	AAA

InterPro
IPR013765
Domain

RecA
PF00154	$\"[12-333]T$	RecA

noIPR
unintegrated

unintegrated
G3DSA:3.30.250.10	$\"[274-332]T$	no description
G3DSA:3.40.50.300	$\"[31-273]T$	no description
PTHR22942	$\"[10-332]T$	RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER
PTHR22942:SF1	$\"[10-332]T$	DNA REPAIR PROTEIN RECA

","BeTs to 26 clades of COG0468COG name: RecA/RadA recombinaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0468 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001553 (RecA bacterial DNA recombination protein) with a combined E-value of 8.4e-176. IPB001553A 9-32 IPB001553B 46-99 IPB001553C 107-161 IPB001553D 194-236 IPB001553E 276-318","Residues 38-78 are 97% similar to a (DNA ATP-BINDING DNA-BINDING REPAIR RECOMBINATION DAMAGE SOS RECA RESPONSE RECOMBINASE) protein domain (PD007172) which is seen in RECA_MYCPA.Residues 44-295 are 45% similar to a (UVSX DNA RECOMBINATION REPAIR RECA-LIKE DAMAGE REPLICATION ATP-BINDING) protein domain (PD138437) which is seen in Q6J2M6_VVVVV.Residues 58-306 are 53% similar to a (DNA SOS DNA-BINDING RECOMBINASE DAMAGE REPAIR ATP-BINDING RECOMBINATION PLASMID RESPONSE) protein domain (PD089927) which is seen in Q935F3_SALTI.Residues 80-297 are 45% similar to a (ORF93) protein domain (PDA0C161) which is seen in Q6Y7M6_VVVVV.Residues 81-121 are 95% similar to a (DNA ATP-BINDING RECOMBINATION DNA-BINDING DAMAGE SOS RESPONSE RECA RECOMBINASE A) protein domain (PD103312) which is seen in RECA_SYNY3.Residues 93-200 are 56% similar to a (ATP-BINDING) protein domain (PD778556) which is seen in Q86HP2_DICDI.Residues 94-297 are 46% similar to a (GP201) protein domain (PD841289) which is seen in Q853A2_VVVVV.Residues 122-160 are 94% similar to a (DNA ATP-BINDING RECOMBINATION DNA-BINDING DAMAGE SOS RESPONSE RECA RECOMBINASE A) protein domain (PD894890) which is seen in RECA_MYCSM.Residues 161-209 are 95% similar to a (DNA ATP-BINDING RECOMBINATION DNA-BINDING DAMAGE SOS RESPONSE RECA RECOMBINASE A) protein domain (PD000229) which is seen in RECA_BIFLO.Residues 210-276 are 92% similar to a (DNA ATP-BINDING RECOMBINATION DNA-BINDING DAMAGE RECA SOS RESPONSE RECOMBINASE A) protein domain (PD493955) which is seen in RECA_AMYMD.Residues 280-317 are 92% similar to a (DNA RECOMBINATION ATP-BINDING DNA-BINDING DAMAGE SOS RESPONSE RECA RECOMBINASE A) protein domain (PD492971) which is seen in RECA_STRLI.","","-92% similar to PDB:1UBC Structure of Reca Protein (E_value = 1.7E_146);-92% similar to PDB:1UBE MsRecA-ADP Complex (E_value = 1.7E_146);-92% similar to PDB:1UBF MsREcA-ATPgS complex (E_value = 1.7E_146);-92% similar to PDB:1UBG MsREcA-dATP complex (E_value = 1.7E_146);-92% similar to PDB:2G88 MSRECA-dATP COMPLEX (E_value = 1.7E_146);","Residues 12 to 333 (E_value = 6.3e-238) place ANA_0405 in the RecA family which is described as recA bacterial DNA recombination protein.","","protein (Recombinase A)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0406","419916","420413","498","7.53","0.69","18143","ATGCCCTGGCTCATCCCTGACGCCCACACGCAAGCGGTCGAGGCGGCGCGGGAGATCGTCCTGCGCCGCCTGGACCGCAGCGCGGCTCCTCGCGCCGCCCTGGCCGAGCTCCTCGAGCGCAAGGAGGTGGACTCCCGTGTAGCCTCCGAGGTCCTTGACCGTCTGGAGGCCGCCGGAGTCATTGACGACACCGCCTACGCGGCCCGCCTCGCGCGCACCCGCTTCGCGGAGAAGGGGGCGGCCAGGCGGGCCATCGCCGAGGAACTGCGGCGCAAGGGACTGGGTGAGTCGGATGTCGCTCAGGCCCTGGATCAGATCAGCGCCGAGGACGAGGACTCAGCGGCGCTGGCGCTGGCTCGCAAGAAGCTCTCCGCCACCGGCCACCTGCCCTGGGAGGTGCGCCGGCGTCGCACCGAGGCCGTGCTGGGGCGCAAGGGCTACAGCCGGGACGTGACCATGCGGGCCATCGCTGCGGCTCACGCTGAGGAATTGGAATGA","MPWLIPDAHTQAVEAAREIVLRRLDRSAAPRAALAELLERKEVDSRVASEVLDRLEAAGVIDDTAYAARLARTRFAEKGAARRAIAEELRRKGLGESDVAQALDQISAEDEDSAALALARKKLSATGHLPWEVRRRRTEAVLGRKGYSRDVTMRAIAAAHAEELE$","Regulatory protein RecX","Cytoplasm","Regulatory protein recX","hypothetical protein predicted by Glimmer/Critica","regulatory protein RecX","","Vierling S., Weber T., Wohlleben W., Muth G. Transcriptional and mutational analyses of the Streptomyces lividans recX gene and its interference with RecA activity. J. Bacteriol. 2000. 182(14):4005-4011. PMID: 10869079","","","

InterPro
IPR003783
Family

Regulatory protein RecX
PF02631	$\"[38-158]T$	RecX

","BeTs to 3 clades of COG2137COG name: Uncharacterized BCRFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2137 is --------vdrlb-efgh-n----t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 38 to 158 (E_value = 1.6e-12) place ANA_0406 in the RecX family which is described as RecX family.","","protein recX","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0407","420479","422206","1728","6.20","-8.84","60137","ATGACCCAGGTGATTGCGGCCACTGGCGGCTCCGACGCTCCGATCGACCTCCACGCGTTGGCGGCCTCAGCGGGAATAGCCGCCGAGTACGTCATTCCCTATGGCCGCGATGTGGGCAAGATCGACCTGCGGGCGCTGGAATCCAGCCAGCACGTGAGCGGCGGTGGGGCGAGTAGCCCTCACTACGTCGTCGTCACTGCGATCACGCCGACGCCTTTCGGGGAGGGCAAGACCACCACGGCCATCGGACTGGCCCAGGGGCTCACCCGCTTGGGCCAGCAGGCAGTCCTGACTCTGCGCCAGTCGGCCATGGGCCCCACCTTCGGCATCAAGGGCGGAGCCGGAGGCTCCGGAGGCGCCCGCATCCTGCCGGCCGAGCGGATGAACCTGCACCTGACCGGCGACTTCCATGCCATCACCGCCGCCCACAACCTCCTGTCGGCGATGATCGACAACCACCTGCACCACGGCAATGAGCTCGACATTGACGAGCGCACCATCACCTGGCCCCGGGTGCTGGACGTCAACGACCGCGCCCTGCGCCATATCGTCACCGGCCTGGGGGCCAAGATCGATGGAGTCACCCGGCAGGCCTCCTTCGACATCACCCCGGCCAGCGAGCTCATGGTCATCATGTCGCTGGCCACGGACCTGTCCGACCTGCGCAGGCGCCTGGGGCGCATCGTCATCGGCCGAAGCCGTGGCGGGGAGTGGATCAGCGCCGAGGACCTCAAGGCAGCCGGGGCCATGTGCGCCGTCCTGCGCGATGCGCTTGAGCCCAATCTCCTGCGCACCGGCGAGGGCACCCCCGTCCTGGTCCATACGGGCCCCTTCGGCAATATTGCCACCGGATGCTCCTCGGTCATCGCCGACCGCGTCGCTGCGGCAGGAGCCCGCGACGGCGGCTACATCCTCACCGAGGCCGGCTTCGGATCCGACATGGGCCTGGAGCGTTTCATCGACCTCAAGTGCGCCGTCTCCGAGATGCACCCGAGCGTCGCCGTCGTCGTGGTCACCATCAGGGCGCTCAAGGCCCACAGCGGACGCCACCGCCTCGTCAGCGGCAAGGACCTGCCCGAGGAGATGCTCCAGGAGAACGTCGATGACGTGCGCGACGGCGCCGCCAACCTGCTCAAGCACCTGCAGATCGTGCGGGGCTTCGGCATCACCCCGGTCGTGGCCGTCAACGTCTTCCCCACCGACCACGACGCCGAGATCGAGGAGGTGACGCGTATCGCCGGCGACGCCGGAGCCCGGGTCGCGGTCTGCCACCCCGTCACCAGGGGAGGCGAGGGCTGCCTCGACCTGGCCGGAGCCGTCGTCGAGGCCTGCCAGGAGGCGGGAGAGCCAGCCAGCAGCCGACCCGCCTACGAGCCGCAGGACGACCTGCGCACCAAGATCTCCAAGCTCGCCGACCTCTACGGCGCCGACGGCGTGGACTACACCCCCGCCGCGAGCAGACTGCTGGAGGCCTACGAGCAGGCAGGCTTCGGCCACCTGCCCGTCATCGTCGCCAAGACCCCGCTGTCCCTGTCCGCTGAACCCGGCCGCAAGGGCGTGCCCACCGGGTGGCGCCTGCCGGTGCGCGAGGTGCGCCTGGCCGCGGGGGCCGGCTACGTCTACGCGATCTGCGGCAGCCTGTCGACCATGCCGGGGCTGCCGAGCCGGCCCGCCGCCGAGCGCATCGACGTCGACCTCGACACCGGGCAGATCGTGGGGCTGCGTTGA","MTQVIAATGGSDAPIDLHALAASAGIAAEYVIPYGRDVGKIDLRALESSQHVSGGGASSPHYVVVTAITPTPFGEGKTTTAIGLAQGLTRLGQQAVLTLRQSAMGPTFGIKGGAGGSGGARILPAERMNLHLTGDFHAITAAHNLLSAMIDNHLHHGNELDIDERTITWPRVLDVNDRALRHIVTGLGAKIDGVTRQASFDITPASELMVIMSLATDLSDLRRRLGRIVIGRSRGGEWISAEDLKAAGAMCAVLRDALEPNLLRTGEGTPVLVHTGPFGNIATGCSSVIADRVAAAGARDGGYILTEAGFGSDMGLERFIDLKCAVSEMHPSVAVVVVTIRALKAHSGRHRLVSGKDLPEEMLQENVDDVRDGAANLLKHLQIVRGFGITPVVAVNVFPTDHDAEIEEVTRIAGDAGARVAVCHPVTRGGEGCLDLAGAVVEACQEAGEPASSRPAYEPQDDLRTKISKLADLYGADGVDYTPAASRLLEAYEQAGFGHLPVIVAKTPLSLSAEPGRKGVPTGWRLPVREVRLAAGAGYVYAICGSLSTMPGLPSRPAAERIDVDLDTGQIVGLR$","Formate--tetrahydrofolate ligase","Cytoplasm","formate--tetrahydrofolate ligase","formate--tetrahydrofolate ligase ","Formate--tetrahydrofolate ligase","","Shannon K.W., Rabinowitz J.C. Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase. J. Biol. Chem. 1988. 263(16):7717-7725. PMID: 2836393Lovell C.R., Przybyla A., Ljungdahl L.G. Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum. Biochemistry 1990. 29(24):5687-5694. PMID: 2200509Radfar R., Shin R., Sheldrick G.M., Minor W., Lovell C.R., Odom J.D., Dunlap R.B., Lebioda L. The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica. Biochemistry 2000. 39(14):3920-3926. PMID: 10747779","","","

InterPro
IPR000276
Family

Rhodopsin-like GPCR superfamily
PS00237	$\"[306-322]?$	G_PROTEIN_RECEP_F1_1

InterPro
IPR000559
Domain

Formate-tetrahydrofolate ligase, FTHFS
PF01268	$\"[1-575]T$	FTHFS
PS00722	$\"[337-348]?$	FTHFS_2

noIPR
unintegrated

unintegrated
G3DSA:3.10.410.10	$\"[462-550]T$	no description
G3DSA:3.40.50.300	$\"[16-461]T$	no description
PTHR10025	$\"[14-575]T$	METHYLENETETRAHYDROFOLATE DEHYDROGENASE FAMILY MEMBER

","BeTs to 7 clades of COG2759COG name: Formyltetrahydrofolate synthetaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG2759 is ---p--y-v--l----g--n-j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB000559 (Formate-tetrahydrofolate ligase, FTHFS) with a combined E-value of 5.4e-215. IPB000559A 10-52 IPB000559B 58-88 IPB000559C 100-129 IPB000559D 130-156 IPB000559E 169-207 IPB000559F 244-295 IPB000559G 302-350 IPB000559H 362-409 IPB000559I 425-440 IPB000559J 453-477 IPB000559K 496-515 IPB000559L 516-554","Residues 29-187 are 80% similar to a (LIGASE FORMATE--TETRAHYDROFOLATE FORMYLTETRAHYDROFOLATE SYNTHETASE SYNTHASE FORMATE-TETRAHYDROFOLATE DEHYDROGENASE METHYLENETETRAHYDROFOLATE SYNTHASE C1-THF) protein domain (PD003089) which is seen in Q6ABS5_PROAC.Residues 200-364 are 75% similar to a (LIGASE FORMATE--TETRAHYDROFOLATE FORMYLTETRAHYDROFOLATE SYNTHETASE FORMATE-TETRAHYDROFOLATE SYNTHASE DEHYDROGENASE METHYLENETETRAHYDROFOLATE SYNTHASE C1-THF) protein domain (PD857102) which is seen in Q6ABS5_PROAC.Residues 366-421 are 76% similar to a (LIGASE FORMATE--TETRAHYDROFOLATE FORMYLTETRAHYDROFOLATE SYNTHETASE FORMATE-TETRAHYDROFOLATE SYNTHASE DEHYDROGENASE METHYLENETETRAHYDROFOLATE METHENYLTETRAHYDROFOLATE SYNTHASE) protein domain (PD341571) which is seen in Q6ABS5_PROAC.Residues 496-553 are 81% similar to a (LIGASE FORMATE--TETRAHYDROFOLATE SYNTHETASE FORMYLTETRAHYDROFOLATE FORMATE-TETRAHYDROFOLATE SYNTHASE DEHYDROGENASE METHYLENETETRAHYDROFOLATE METHENYLTETRAHYDROFOLATE SYNTHASE) protein domain (PD186204) which is seen in Q6ABS5_PROAC.","","-62% similar to PDB:1FP7 MONOVALENT CATION BINDING SITES IN N10-FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA (E_value = 1.3E_123);-62% similar to PDB:1FPM MONOVALENT CATION BINDING SITES IN N10-FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA (E_value = 1.3E_123);-62% similar to PDB:1EG7 THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA (E_value = 3.8E_123);","Residues 1 to 575 (E_value = 2.1e-230) place ANA_0407 in the FTHFS family which is described as Formate--tetrahydrofolate ligase.","","ligase (fhs)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0408","422619","422275","345","9.50","5.61","12506","ATGGCATCGGGCCGTCGCCCGCTGCGCTCGGCCAGCTGCACCACCACTGAGGCACAGGACATCGTGGCCTCTCACGGAATCGTCTTCCCGGCGATCGCCTCCTCCACGAAGAAGGCCGTCAAGGTCTTTGAGGAAACGGGGCTTCCCACCAAGCCCTTCACCCAGCACCTGGAGGACAAGTCCACGTTCTTCTTCCCACTGACCTACTTCGGGGCGGATGTGGGCGCCATCATGAAGCCGGCGACGGACGACCTGTGGGCCAACCGGGTGCCGGCCTCAACGCTGACGAAGTACAACGAGCAGGTCAACCTCCTGTTCAAGACGTCCAAGCACAAGAAGAGCTGA","MASGRRPLRSASCTTTEAQDIVASHGIVFPAIASSTKKAVKVFEETGLPTKPFTQHLEDKSTFFFPLTYFGADVGAIMKPATDDLWANRVPASTLTKYNEQVNLLFKTSKHKKS$","Hypothetical protein","Periplasm, Membrane","putative substrate binding protein","extracellular solute-binding protein; family 1","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","substrate binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0410","422558","423355","798","5.29","-7.00","27282","ATGTCCTGTGCCTCAGTGGTGGTGCAGCTGGCCGAGCGCAGCGGGCGACGGCCCGATGCCATCGGAATCTCCCTGGGGGCGGCCGTCGTCGGGAGACGGACTGTGGTGGTGGCCAGCTTCCTGGGATGGCGCAACGTACCTCTGGCCGCCATGGTCACCGAGGCCACCGGGCTGCCCTGCGTCGCGGCCAACGACGTGCGCGCCTTCGCCTACGCCGAGGCATGGTTCGGTGCCGGCCGTGGGAAGGACCCCTTCGCGATGGTCACCTTGGGGGCTGGAATCGGCTGCGGGGTCGTGGTGGCCGGTGAGGTCGTCTCCGGTGCGCAGGGGGCGGCCGGCAGTGTCGGGCACCTGCCGGTGGATCCCTCGGGGCCCAGCTGCGAGATCGGGCACCCCGGGTGCGCTCGGGCCCTCGCCTCGACCCCCGGGATCCTGCGGGCGGCCGCCGAGCACCTGGAGTGTGAGGCCGGCGAGCTGAGTCTCGATCTGCTCCTGAGTCCCGACATGCGTCGCCACAATGGCGTCGACGACGTCCTACGGCGTGCGGTGCTGGCGATCGGAAGGGTCGTGGGGACTCTCATCGCCTACGTCGATCCCGAGCTCGTCGTCGTCTCAGGGGAGGGGGTCGCCGTGGTGGAGACCTACCGCGAGGTCTTTGATGAGGAGGTGGGCGGTCTGCGGCACTGGGCCGCGGCGCCCGTGCCCGTCCTGCTGCGTCCCTTCGAGTTCGACGAGTGGGCGCGAGGGGCGGCCGCTCTGGCCCTGGATCAGTGGACGGTGGTCGCAGGCGGCCGGTGA","MSCASVVVQLAERSGRRPDAIGISLGAAVVGRRTVVVASFLGWRNVPLAAMVTEATGLPCVAANDVRAFAYAEAWFGAGRGKDPFAMVTLGAGIGCGVVVAGEVVSGAQGAAGSVGHLPVDPSGPSCEIGHPGCARALASTPGILRAAAEHLECEAGELSLDLLLSPDMRRHNGVDDVLRRAVLAIGRVVGTLIAYVDPELVVVSGEGVAVVETYREVFDEEVGGLRHWAAAPVPVLLRPFEFDEWARGAAALALDQWTVVAGGR$","Transcriptional regulator, ROK family","Cytoplasm","glucokinase","xylose operon repressor","ROK family protein","","Titgemeyer F., Reizer J., Reizer A., Saier Jr M.H. Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 1994. 140:2349-2354. PMID: 7952186","","","

InterPro
IPR000600
Family

ROK
PF00480	$\"[2-144]T$	ROK
PS01125	$\"[90-117]T$	ROK

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.160	$\"[65-262]T$	no description
PTHR18964	$\"[26-206]T$	ROK FAMILY
PTHR18964:SF37	$\"[26-206]T$	GLUCOSE KINASE

","BeTs to 9 clades of COG1940COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1940 is ao-p-z-qvdrlbce-gh---j--t-Number of proteins in this genome belonging to this COG is 5","***** IPB000600 (ROK family) with a combined E-value of 1e-10. IPB000600B 59-73 IPB000600C 88-99 IPB000600E 127-136","Residues 42-90 are similar to a (KINASE TRANSCRIPTIONAL TRANSFERASE REGULATOR FAMILY ROK GLUCOKINASE REPRESSOR SUGAR GLUCOSE) protein domain (PD212372) which is seen in Q9EWT7_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 144 (E_value = 2.3e-10) place ANA_0410 in the ROK family which is described as ROK family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0411","423454","424977","1524","7.36","1.79","53863","ATGAGTCGTCGCGCCACCATTGCCCTGTCGACCGCCGGCCTCCTGGCCGCCGGAGCCGCCCTCGCACTGGCCGTACGTCCGGCCCGCCATGACGTCCCCGACGTCGCCGCCGGCACGGGCAGCCGCCGTCCGCCCCGCGTCGTCATCGCCGGTGGCGGCTACGTCGGCTTCTGCGTCGCCCGGGCCCTGCGCGCCCAGCTCAACCTCGACCAGGTCGAGATCGCCATCATCGACTCGCGCGCCTACATGACCTACCAGCCCTTCCTGCCGGAGGTCGCGGCCGGCTCCATCCAGCCACGCCACGTCGTCGCGCCCCACCGCCGTAACCTCGACGGCGTCACCATCATCACCGGCGCCGTCACCGCCATCGACCACGCGGGCCGCACCGTCACCGTGCGTCCCCCGACCCCCCAGTCCACGCACGAGCCGGTCGAGCCCTACACCCTGACCTACGACCACCTCGTCATCGCCCTGGGCGCCGAGGCCCGCACCCTGCCGATTCCCGGTCTTGCGGAGCAGGCCATGGGCTTCAAGCAGGTCGAGGAGGCCACCGCCCTGCGCAACCGGGTCCTCACCCGCATCGAGGACGCCGCCTCCACCTGGGACACCGAGCGCCGCAGGCGCCTGCTCACCTTCGTCTTCGTCGGAGGAGGCTTCGCGGGCGTCGAGGCCATCGCCGAGCTGGAGGACATGGCACGCGCGACCGTGCGCACCATCCCTTCCATCGAGCAGCGCGACGTCCGCTTCGTCCTCGTCGAGGGCTCGCGCCGCATCCTGCCCGAGCTCACCGAGGAGCTCTCCGGCTACGGGCTGCAGCAGCTGCTTGAGCGCGGCATCGACGTGCGGCTCAACACCTTCCTCAACTCCTGCGTTGACGGTCACGTCGTCCTGTCCGACGGCACCGAGTTCGACGCCGACACCATCGTGTGGACCGCCGGCGTCAAGGCCGCCCCGGTGCTGCAGACCGCCTCCGACCTACCCATCGATGCCCGCGGCCGTGTCACCGCGCTGCCCACCCTCCAGGTGGCGCGCGACGGCGCGCCGGTCGAGGGAGCCTGGGCCGCCGGCGACTGCGCCGCCGTCCCGGACCTGACCTCCGAGGACCCCGAGGCCACCTGCGCCCCCACCGCCCAGCACGCGGTGCGTCAGGCCAAGCTGCTGGCCGACAACCTCGTGGCCGTCCTCGCCGCCGGGGACGAGAACGGTGTGCCTCTGAAGTCCTACGCGCACGCGAACCTGGGCACCGTGGCCTCCCTGGGCATCGGCAAGGGCGTCGCCCGCATCATGGGCCGGGACCTGCGCGGCTTCACCGCCTGGACCGCTCACCGCGGCTATCACGTCTACGCGATGCCGACCCTCAACCGGAAGGTGCGCATCATGATGGGCTGGCTGGCCGCCGTCGTCTTCCGTCGCGACCTGGCCTCCTTCGGCTCCATCGCCGAGCCCGGCGCGGCCTTTGCCACGGCGGCCCGTCACGACGCCGACCTCGCTGCCCGCCGCAAGGCCGCCGACAGCGGGTCCTGA","MSRRATIALSTAGLLAAGAALALAVRPARHDVPDVAAGTGSRRPPRVVIAGGGYVGFCVARALRAQLNLDQVEIAIIDSRAYMTYQPFLPEVAAGSIQPRHVVAPHRRNLDGVTIITGAVTAIDHAGRTVTVRPPTPQSTHEPVEPYTLTYDHLVIALGAEARTLPIPGLAEQAMGFKQVEEATALRNRVLTRIEDAASTWDTERRRRLLTFVFVGGGFAGVEAIAELEDMARATVRTIPSIEQRDVRFVLVEGSRRILPELTEELSGYGLQQLLERGIDVRLNTFLNSCVDGHVVLSDGTEFDADTIVWTAGVKAAPVLQTASDLPIDARGRVTALPTLQVARDGAPVEGAWAAGDCAAVPDLTSEDPEATCAPTAQHAVRQAKLLADNLVAVLAAGDENGVPLKSYAHANLGTVASLGIGKGVARIMGRDLRGFTAWTAHRGYHVYAMPTLNRKVRIMMGWLAAVVFRRDLASFGSIAEPGAAFATAARHDADLAARRKAADSGS$","NADH dehydrogenase, FAD-containing subunit","Cytoplasm","putative NADH dehydrogenase","putative NADH dehydrogenase ","NADH dehydrogenase","","Eggink G., Engel H., Vriend G., Terpstra P., Witholt B. Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J. Mol. Biol. 1990. 212(1):135-142. PMID: 2319593Ross R.P., Claiborne A. Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases. J. Mol. Biol. 1992. 227(3):658-671. PMID: 1404382Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Hanukoglu I., Gutfinger T. cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases. Eur. J. Biochem. 1989. 180(2):479-484. PMID: 2924777Hyde G.E., Crawford N.M., Campbell W.H. The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases. J. Biol. Chem. 1991. 266(35):23542-23547. PMID: 1748631Karplus P.A., Schulz G.E. Refined structure of glutathione reductase at 1.54 A resolution. J. Mol. Biol. 1987. 195(3):701-729. PMID: 3656429Schiering N., Kabsch W., Moore M.J., Distefano M.D., Walsh C.T., Pai E.F. Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607. Nature 1991. 352(6331):168-172. PMID: 2067577Mattevi A., Schierbeek A.J., Hol W.G. Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase. J. Mol. Biol. 1991. 220(4):975-994. PMID: 1880807Kuriyan J., Kong X.P., Krishna T.S., Sweet R.M., Murgolo N.J., Field H., Cerami A., Henderson G.B. X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(19):8764-8768. PMID: 1924336Stehle T., Ahmed S.A., Claiborne A., Schulz G.E. Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution. J. Mol. Biol. 1991. 221(4):1325-1344. PMID: 1942054Schulz G.E. Gene duplication in glutathione reductase. J. Mol. Biol. 1980. 138(2):335-347. PMID: 7411611","","","

InterPro
IPR001327
Domain

Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00070	$\"[211-313]T$	Pyr_redox

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07992	$\"[46-363]T$	Pyr_redox_2

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[43-170]T$ $\"[211-393]T$	no description
PTHR22915	$\"[45-468]T$	NADH DEHYDROGENASE-RELATED
PTHR22915:SF4	$\"[45-468]T$	NADH DEHYDROGENASE-RELATED
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","BeTs to 10 clades of COG1252COG name: NADH dehydrogenase, FAD-containing subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1252 is -o----y--drlbcefgh---j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 46-99 are 75% similar to a (NADH DEHYDROGENASE OXIDOREDUCTASE FLAVOPROTEIN PYRIDINE NUCLEOTIDE-DISULPHIDE DEHYDROGENASE REDUCTASE SULFIDE SULFIDE-QUINONE) protein domain (PD022954) which is seen in Q83N60_TROW8.Residues 166-269 are similar to a (NADH DEHYDROGENASE OXIDOREDUCTASE PYRIDINE NUCLEOTIDE-DISULPHIDE DEHYDROGENASE FAMILY UBIQUINONE MEMBRANE FLAVOPROTEIN) protein domain (PD342384) which is seen in Q8CJX7_STRCO.Residues 266-360 are 51% similar to a (OXIDOREDUCTASE DEHYDROGENASE NADH SUBUNIT OXIDASE PYRIDINE PLASMID NUCLEOTIDE-DISULPHIDE A PROBABLE) protein domain (PD689523) which is seen in DHNA_HAEIN.Residues 277-359 are similar to a (NADH DEHYDROGENASE OXIDOREDUCTASE PYRIDINE FLAVOPROTEIN REDUCTASE NUCLEOTIDE-DISULPHIDE SULFIDE-QUINONE DEHYDROGENASE SULFIDE) protein domain (PD338946) which is seen in Q83N60_TROW8.Residues 402-482 are similar to a (DEHYDROGENASE OXIDOREDUCTASE NADH TYPE DEHYDROGENASE) protein domain (PD346732) which is seen in Q9KYF1_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 46 to 363 (E_value = 1.3e-10) place ANA_0411 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 211 to 313 (E_value = 2.8e-09) place ANA_0411 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.","","NADH dehydrogenase (Y09899)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0412","425368","424982","387","4.00","-19.58","13376","ATGGCTCAGAGCGTGCGCGCCCACCTGCGCTACAGCATCGACCACGAGTGGCTGGAGGACGGTGAGCCCGCACGCGTGGGCATCACTACCGTCGCCGCCGATGCTCTCGGTGAGGTCGTCTTCATCGACCTGCCCGAGGTCGGCGCCCAGGTCGAGGCGGGCGAGCCCTGCGGCGAGCTCGAGTCGACCAAGTCCGTCTCGGACCTCGTCTCGCCCGTGAGCGGCACCGTCGTCGCCGTCAACGATGCGGTCGTCGACGAGCCGGGCACCATCAACGAGGACCCCTACGGTGCCGGCTGGCTGTTCACGGTGACGGTCAGCGCTGAGGGAGATCTGCTCAGCGCCCAGGACTACGCAGACAAGTTCGACGCCGTCGTCGACGGCTGA","MAQSVRAHLRYSIDHEWLEDGEPARVGITTVAADALGEVVFIDLPEVGAQVEAGEPCGELESTKSVSDLVSPVSGTVVAVNDAVVDEPGTINEDPYGAGWLFTVTVSAEGDLLSAQDYADKFDAVVDG$","Glycine cleavage system H protein","Cytoplasm","glycine cleavage system H protein","glycine cleavage system H protein","glycine cleavage system H protein","","Yeaman S.J. The 2-oxo acid dehydrogenase complexes: recent advances. Biochem. J. 1989. 257(3):625-632. PMID: 2649080Russell G.C., Guest J.R. Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim. Biophys. Acta 1991. 1076(2):225-232. PMID: 1825611Fujiwara K., Okamura-Ikeda K., Motokawa Y. Chicken liver H-protein, a component of the glycine cleavage system. Amino acid sequence and identification of the N epsilon-lipoyllysine residue. J. Biol. Chem. 1986. 261(19):8836-8841. PMID: 3522581Behal R.H., Browning K.S., Hall T.B., Reed L.J. Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 1989. 86(22):8732-8736. PMID: 2682658Priefert H., Hein S., Kruger N., Zeh K., Schmidt B., Steinbuchel A. Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J. Bacteriol. 1991. 173(13):4056-4071. PMID: 2061286","","","

InterPro
IPR002930
Family

Glycine cleavage H-protein
PTHR11715	$\"[7-127]T$	GLYCINE CLEAVAGE SYSTEM H PROTEIN
PF01597	$\"[9-125]T$	GCV_H
TIGR00527	$\"[4-123]T$	gcvH: glycine cleavage system H protein

InterPro
IPR003016
Binding_site

2-oxo acid dehydrogenase, lipoyl-binding site
PS00189	$\"[48-77]T$	LIPOYL

InterPro
IPR010916
Domain

TonB box, N-terminal
PS00430	$\"[1-109]?$	TONB_DEPENDENT_REC_1

noIPR
unintegrated

unintegrated
G3DSA:2.40.50.100	$\"[3-123]T$	no description

","BeTs to 17 clades of COG0509COG name: Glycine cleavage system H protein (lipoate-binding)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0509 is -o-pkzyqvdrlbcefg-sn-j-i--Number of proteins in this genome belonging to this COG is 1","***** IPB002930 (Glycine cleavage H-protein) with a combined E-value of 3.4e-33. IPB002930 45-99***** IPB003016 (2-oxo acid dehydrogenase, acyltransferase component, lipoyl-binding) with a combined E-value of 3.9e-10. IPB003016 48-80","Residues 14-84 are 64% similar to a (SYSTEM GLYCINE H CLEAVAGE) protein domain (PD969563) which is seen in Q6A8T6_PROAC.Residues 26-104 are similar to a (SYSTEM GLYCINE H CLEAVAGE HOMOLOGUE) protein domain (PD918781) which is seen in Q6MR34_BDEBA.Residues 28-94 are 64% similar to a (GLYCINE CLEAVAGE SYSTEM H H-PROTEIN GCVH PROTEIN SA0313 FAMILY MW0301) protein domain (PD472562) which is seen in Q831K4_ENTFA.Residues 48-120 are 60% similar to a (SYSTEM GLYCINE H CLEAVAGE LIPOYL PROBABLE) protein domain (PD632443) which is seen in Q7UPP1_RHOBA.","","-66% similar to PDB:1ZKO Crystal structure of Glycine cleavage system H protein (tm0212) from Thermotoga maritima at 1.65 A resolution (E_value = 2.2E_23);-66% similar to PDB:1ONL Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system (E_value = 6.5E_23);-63% similar to PDB:1DXM REDUCED FORM OF THE H PROTEIN FROM GLYCINE DECARBOXYLASE COMPLEX (E_value = 1.2E_21);-63% similar to PDB:1HPC REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE (E_value = 1.2E_21);-63% similar to PDB:1HTP REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX (E_value = 1.2E_21);","Residues 9 to 125 (E_value = 5.9e-49) place ANA_0412 in the GCV_H family which is described as Glycine cleavage H-protein.","","cleavage system H protein (gcvH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0413","426679","425414","1266","5.03","-20.06","44092","ATGAGCGAGCACACCGAGACCGGCGCAGCCGTCCTGCACACCACGCCCCTGCACCGCGTGCACACGGCCCTGGGCGCGTCCTTCACCGACTTCGGCGGCTGGCAGATGCCGTTGCGCTACACCTCTGACCTGGCCGAGCACCACGCGGTGCGCCGCAGCGCGGGGATCTTCGACCTGTCCCACATGGGTGAGGTCAAGGTCACCGGCCCCGAGGCGGGCGCCGCCCTGGACCACGCGCTCGTGGGGGCCCTGTCGGCCGTGGCGGTGGGGCGCGCCCGCTACACGATGATCGTCTCGCCCTCCGGCGGGGTCATCGACGACCTCATCGTCTACCACGTGGGCGACGAGGAGTACCTCGTGGTGCCCAACGCCGGCAACCGCGAGCGCGTCGCCGCCGAGCTGGTCGCCCGTTGCGCGGGCTTCGACTGCACGGTCGAGGACATCTCTCTGCGCACCTGCCTCATCGCCGTCCAGGGGCCGCGGGCGCAGGAGGTGCTCGTCGGCGTCGTCGAGTCCGGTGCCGCCATGCCCGGCGCCCTCAGGCCCCTTGAGGGCTCGGAGGAGGAAGACTGCGGACCAGACGTGCTGTGCGGTCCCACGCTCTTGGAGCGCCTGCGCTTCTACGCTGCCGTCAGGGCGACGGCGGCGGGGCACTCGGTGCTGCTGGCCCGTACCGGCTACACGGGTGAGGACGGCTTCGAACTGTTCTGCGGCGCGGAGGACGCCGTGGACCTGTGGACGGTCATCACCAGTGCCGCGGCGGCCCTGGAGCCCACCGTCATCGACGGCGAGCCGGTGCCGGCGCTGACCCCCTGCGGGCTGGCGGCGCGCGACTCTCTGCGACTGGAGGCCGGGATGCCCCTGTACGGGCACGAGCTCCACGAGGGGATGACGCCCTACGACGCAGGCCTGGGCATGGTGGTGCGGCTCAACAAGGGCGACTTCATCGGACGTGACGCCCTGGCCGCCCGGGCCGAGCAGGAGGGCACCGAGGGAACCTCGGTGCTGGTTCCCCTGACCGCTGAGGGTCGACGTGCGGCCCGGGCCGGTGCGCCGGTACTGGGCGACGACGGCGAGGTGCTCGGTACCGTGACCTCCGGCCTGCTGTCACCCACCCTGGGTCACCCCGTGGCCCTGGCGCTCCTGCGTCCCTGGAGTGAGGACGCCCCCGCCTGGCCCGTGGGCACGGTGCTCGTCGCCGACGTGCGCGGCAGGCCGCTGGAGGTCACGGTCGTCGCCTCCCCCTTCTACAAGCGGACCCGATAA","MSEHTETGAAVLHTTPLHRVHTALGASFTDFGGWQMPLRYTSDLAEHHAVRRSAGIFDLSHMGEVKVTGPEAGAALDHALVGALSAVAVGRARYTMIVSPSGGVIDDLIVYHVGDEEYLVVPNAGNRERVAAELVARCAGFDCTVEDISLRTCLIAVQGPRAQEVLVGVVESGAAMPGALRPLEGSEEEDCGPDVLCGPTLLERLRFYAAVRATAAGHSVLLARTGYTGEDGFELFCGAEDAVDLWTVITSAAAALEPTVIDGEPVPALTPCGLAARDSLRLEAGMPLYGHELHEGMTPYDAGLGMVVRLNKGDFIGRDALAARAEQEGTEGTSVLVPLTAEGRRAARAGAPVLGDDGEVLGTVTSGLLSPTLGHPVALALLRPWSEDAPAWPVGTVLVADVRGRPLEVTVVASPFYKRTR$","Glycine cleavage system T protein","Cytoplasm","glycine cleavage system T protein","glycine cleavage system T protein","glycine cleavage system T protein","","","","","

InterPro
IPR006222
Family

Glycine cleavage T protein (aminomethyl transferase)
PF01571	$\"[56-166]T$ $\"[203-246]T$ $\"[270-307]T$	GCV_T

InterPro
IPR006223
Family

Glycine cleavage system T protein
TIGR00528	$\"[12-419]T$	gcvT: glycine cleavage system T protein

InterPro
IPR013977
Domain

Glycine cleavage T-protein, C-terminal barrel
PF08669	$\"[313-414]T$	GCV_T_C

noIPR
unintegrated

unintegrated
PTHR13847	$\"[15-172]T$ $\"[201-418]T$	FAD NAD BINDING OXIDOREDUCTASES
PTHR13847:SF5	$\"[15-172]T$ $\"[201-418]T$	AMINOMETHYLTRANSFERASE

","BeTs to 15 clades of COG0404COG name: Glycine cleavage system T protein (aminomethyltransferase)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0404 is -o-pkzyqvdr-bcef--sn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB006222 (Glycine cleavage T protein (aminomethyl transferase)) with a combined E-value of 2.3e-68. IPB006222A 31-40 IPB006222B 51-62 IPB006222C 99-111 IPB006222D 147-174 IPB006222E 224-235 IPB006222F 273-306 IPB006222G 314-324 IPB006222H 362-373 IPB006222I 395-417","Residues 30-58 are 93% similar to a (GLYCINE CLEAVAGE SYSTEM TRANSFERASE T AMINOMETHYLTRANSFERASE AMINOTRANSFERASE METHYLTRANSFERASE GCVT MITOCHONDRIAL) protein domain (PD633190) which is seen in Q6A9R6_PROAC.Residues 59-157 are similar to a (TRANSFERASE GLYCINE CLEAVAGE SYSTEM T AMINOMETHYLTRANSFERASE AMINOTRANSFERASE METHYLTRANSFERASE SARCOSINE SUBUNIT) protein domain (PD003737) which is seen in Q6A9R6_PROAC.Residues 220-285 are 65% similar to a (GLYCINE TRANSFERASE CLEAVAGE SYSTEM T AMINOMETHYLTRANSFERASE AMINOTRANSFERASE SARCOSINE SUBUNIT METHYLTRANSFERASE) protein domain (PD370700) which is seen in Q6A9R6_PROAC.Residues 290-416 are 60% similar to a (TRANSFERASE GLYCINE CLEAVAGE SYSTEM T AMINOMETHYLTRANSFERASE AMINOTRANSFERASE SARCOSINE METHYLTRANSFERASE SUBUNIT) protein domain (PD280855) which is seen in GCST_STRCO.","","-53% similar to PDB:1YX2 Crystal Structure of the Probable Aminomethyltransferase from Bacillus subtilis (E_value = 1.2E_62);-51% similar to PDB:1WOO Crystal structure of T-protein of the Glycine Cleavage System (E_value = 1.9E_60);-51% similar to PDB:1WOP Crystal Structure of T-protein of the Glycine Cleavage System (E_value = 1.9E_60);-51% similar to PDB:1WOR Crystal Structure of T-protein of the Glycine Cleavage System (E_value = 1.9E_60);-51% similar to PDB:1WOS Crystal Structure of T-protein of the Glycine Cleavage System (E_value = 1.9E_60);","Residues 56 to 307 (E_value = 9.4e-56) place ANA_0413 in the GCV_T family which is described as Aminomethyltransferase folate-binding domain.Residues 313 to 414 (E_value = 1.1e-13) place ANA_0413 in the GCV_T_C family which is described as Glycine cleavage T-protein C-terminal barrel domain.","","cleavage system T protein (gcvT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0414","429631","426710","2922","5.75","-27.26","102643","ATGACGGCGCCCCACACACCCACGCGCTTCCTGGACCGGCACCTGGGCACGACGGGAGCGGACCTGGACACGGTTCTGACCAGCATCGGTGCCCGGAGCCTGGAGGACCTGGCCGTCCGGGTGGTCCCCACCACCCTGCCCGTCCTGGATCCCCCGCAGCAGCCCGAGCGCCCCGATGCCGTCGTCGGCGGGCTGAGCGAGGACGAGGCCGTCAGCGCGCTCAGGTCCCTGGCCGCCCTCAACGACCCGCACACCGAGATGATCGGGTGCGGTTACCACCCCACCATCACCCCCGCCATCATCGTGCGCGACGTCCTGTCCAATCCCGCTTGGACCACCGCCTACACCCCCTACCAGGCGGAGATCAGCCAGGGGCGACTGGAGGCCCAGCTGCTGTTCCAGACCGTCGTGGCCGATCTCACCGGCCTGCCGGTGGCCTGCACCTCCCTGCTGGATGAGGCCACGGCCGTGGCCGAGGCCGTCCTGCTCATGACGCGCGCGCACCGCGGCCCCGGCGCCCCCGTGCTCCTCGACTCCGGCCTGCACCCCCAGCTCATCGAGGTGGCCTCGGCCCGGGCCGAGGCCCTGGGCATCGACGTCGAGGTCGTCTGCATCTCCACGATCACCGAAGACGGCGCTCCCCTGACCGGCGCGGTCCTCGCCCACACCACCAGCCGCGGACTCGTCCAGGACCTCGCCGGTGCCGTCGCGGCCGTCCACGCCCGCGGCGGCCTGGTGGCAGTCGATGCCGACCCGCTGGCCCTGACGCTGCTGACCGAGCCGGGCGCCGTCGGCACGGACATCGCCGTCGGTACCGCGCAGCGCCTGGGGGTGCCCCTGTTCTTCGGAGGCCCCCACCCGGGCTTCATGTCCGTCACCGAGGCGCTGCGGCGCCAGCTGCCGGGACGCGTCGTCGGCGTCTCCCGAGACACCGAGGGCCGTGAGGCCTACCGCCTGGCCCTGCAGACCCGCGAGCAGCACATTCGCCGGGAGAAGGCCACCTCGAATATCTGCACCGCGCAGGCCCTGCTGGCGGTCGTGGCGGCCTTCTACGCGGTCTACCACGGTCCCGAGGGCCTGGTGTCCATCGCCGAGCACGTGCACCGCCGGGCCGAGCACCTGGCCGTCGGCGCCTGCGCGCTCGGGCTCGCCCTCGAGCACGAGGAGTTCTTCGACACGGTGAGCGTGCGCCTGCCCGGCGCCGCCCGCCAGGCCATCGAGCGCGCTGAGGCGCTGGGCTACAACCTGCGTCTGCTCGATGCCGACCACGTGGGCGTGAGCGTCAACGAGACCACCACCGATGACGACGTCACCACGGTCCTGCGGGCGCTCGCCGACTCCCTCCCCCGCGCCGCGCAGGATCCCGCCCCGGGCACCGACGGCGCCTCCCGGTTCCCCCTGCCCACCTCGCTGGCGCGCACGAGCACCTTCCTGACCCACCCGAGCTTCCACCGCCACCGCAGCGAGACCGCCCTCGTGCGCTACATCCGGCGGCTGGCGGACCGCGACCTCGCCCTCGACCGGACGATGATCCCGTTGGGCTCGTGCACCCTCAAGCTCAACGCGGCCGCGCAGTCGACCGTGTGGCTCAGCCCCGAGCTCGCCGGCATCCACCCCTACGCCCCCGCGACCCAGACGCGCGGCTGGCGCCTGCTGCTGGACGGTCTCGCCGACCGGCTGGCGCAGCTGACCGGCTACGACCGGTGCAGCCTGCAGCCGGCCTCCGGCGCCCAGGGCGAGCTCGCCGGCCTGCTGGCGGTGCGCGGCTACCTCCGGGCCACCGGGCAGCAGCAACGCGACCTCGTCCTGGTACCCGCCAGCGCCCACGGCACGAACGCCGCCTCGGCCGCCGGCGCCGGCTTCAGCGTCACGGTGGTCGCCACCGCCGAGGACGGCTCCATCGACGTCGACCACCTGCGCGAGCTCCTGGCCGAGTACGGTCAGCGCGTCGCGGCCATCATGCTCACGTACCCGTCCACCCACGGCGTCTTCGAGCCGCAGGTCACTGAGGTCACCGCCCTCGTCCACGACGCCGGCGGCCAGGTCTACATCGACGGCGCCAACCTCAACGCCCTCACGGGGCTGCTGCGCCCGGGTGACCTCGGTGGCGATGTGTCCCACCTCAACCTGCACAAGACCTTCGCCGTCCCTCACGGCGGCGGCGGCCCGGGCGTGGGGCCCGTCGTCGTCAAGGAGCACCTGGCCCCCTACCTTCCGGCCGGCCCCGCCGGATCGGCCCTCCCGACGGACGAGGACCACGACCGGGGCTTCGGCGGAGCAGCGGCCATGGGGGCCCGCTTCGGCTCGGCGGGGGTCATGCCGCTGGCCTGGACGTACCTGGCCACGCTCACCGACGCCGATCTGCGCCGGGTCACCCTCACGGCGCTGGCCCACGCGAGCTATCTCTCGCAGGCGCTCGCCGACGTCTTCCCCACCCTGTACACCCATCGCGGGCACGTGGCGCACGAGTGCGTCCTCGACCTGCGTGCACTCACCGCCGCCACCGGCGTGACCGCCGAGGACGTGGCCAAGAGGCTCATCGACTACGGGTTCCACGCGCCGACCCTCTCCTTCCCCGTGGCCGGCACGCTCATGGTCGAGCCCACCGAGTCCGAGCCCCTGACCGAGCTGGACCGCTTCATCGCGGCCATGCGCTCGATCCGTGCCGAGATCGACGAGGTCGCCTCGGGGGCCGTGGCGCTGGAGGACTCGGTGCTGCGCCGCTCGCCGCACACGCTGGCGGCCGTCACGGCCGAGCCCTGGAAGCGGCCCTACTCGCGCGCCACCGCGGCCTTCCCGCTGGCGGGCATGGAGACGGACAAGTACTTCCCCCCGGTCTCGCGGGTGGACAACGCGTGGGGCGACCGCCACCTGATGTGCACCTGCCCGCCACCCGATGCCTTCGAGGCGCACGAGGCCTGA","MTAPHTPTRFLDRHLGTTGADLDTVLTSIGARSLEDLAVRVVPTTLPVLDPPQQPERPDAVVGGLSEDEAVSALRSLAALNDPHTEMIGCGYHPTITPAIIVRDVLSNPAWTTAYTPYQAEISQGRLEAQLLFQTVVADLTGLPVACTSLLDEATAVAEAVLLMTRAHRGPGAPVLLDSGLHPQLIEVASARAEALGIDVEVVCISTITEDGAPLTGAVLAHTTSRGLVQDLAGAVAAVHARGGLVAVDADPLALTLLTEPGAVGTDIAVGTAQRLGVPLFFGGPHPGFMSVTEALRRQLPGRVVGVSRDTEGREAYRLALQTREQHIRREKATSNICTAQALLAVVAAFYAVYHGPEGLVSIAEHVHRRAEHLAVGACALGLALEHEEFFDTVSVRLPGAARQAIERAEALGYNLRLLDADHVGVSVNETTTDDDVTTVLRALADSLPRAAQDPAPGTDGASRFPLPTSLARTSTFLTHPSFHRHRSETALVRYIRRLADRDLALDRTMIPLGSCTLKLNAAAQSTVWLSPELAGIHPYAPATQTRGWRLLLDGLADRLAQLTGYDRCSLQPASGAQGELAGLLAVRGYLRATGQQQRDLVLVPASAHGTNAASAAGAGFSVTVVATAEDGSIDVDHLRELLAEYGQRVAAIMLTYPSTHGVFEPQVTEVTALVHDAGGQVYIDGANLNALTGLLRPGDLGGDVSHLNLHKTFAVPHGGGGPGVGPVVVKEHLAPYLPAGPAGSALPTDEDHDRGFGGAAAMGARFGSAGVMPLAWTYLATLTDADLRRVTLTALAHASYLSQALADVFPTLYTHRGHVAHECVLDLRALTAATGVTAEDVAKRLIDYGFHAPTLSFPVAGTLMVEPTESEPLTELDRFIAAMRSIRAEIDEVASGAVALEDSVLRRSPHTLAAVTAEPWKRPYSRATAAFPLAGMETDKYFPPVSRVDNAWGDRHLMCTCPPPDAFEAHEA$","Glycine dehydrogenase","Cytoplasm, Membrane","glycine dehydrogenase","glycine dehydrogenase ","glycine dehydrogenase","","Stauffer L.T., Fogarty S.J., Stauffer G.V. Characterization of the Escherichia coli gcv operon. Gene 1994. 142(1):17-22. PMID: 8181752","","","

InterPro
IPR003437
Family

Glycine cleavage system P-protein
PTHR11773	$\"[10-969]T$	GLYCINE DEHYDROGENASE
PF02347	$\"[12-444]T$	GDC-P
TIGR00461	$\"[13-962]T$	gcvP: glycine dehydrogenase

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[102-353]T$ $\"[549-788]T$	no description

","BeTs to 15 clades of COG1003COG name: Glycine cleavage system protein P (pyridoxal-binding), C-terminal domainFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1003 is -o-pkzyqvdr-bcef--sn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB003437 (Glycine cleavage system P-protein) with a combined E-value of 7e-112. IPB003437A 101-143 IPB003437B 572-623 IPB003437C 679-732 IPB003437D 766-816 IPB003437E 850-891 IPB003437A 524-566 IPB003437D 338-388","Residues 13-188 are 61% similar to a (GLYCINE SYSTEM CLEAVAGE OXIDOREDUCTASE DEHYDROGENASE DECARBOXYLASE SUBUNIT P-PROTEIN DECARBOXYLATING PHOSPHATE) protein domain (PD003559) which is seen in GCSP_MYCLE.Residues 282-484 are 63% similar to a (GLYCINE SYSTEM CLEAVAGE OXIDOREDUCTASE DEHYDROGENASE DECARBOXYLASE SUBUNIT P-PROTEIN DECARBOXYLATING PHOSPHATE) protein domain (PD408705) which is seen in GCSP_STRCO.Residues 468-605 are 67% similar to a (GLYCINE SYSTEM CLEAVAGE DEHYDROGENASE OXIDOREDUCTASE SUBUNIT DECARBOXYLASE PHOSPHATE PYRIDOXAL P-PROTEIN) protein domain (PD445371) which is seen in GCSP_SYNY3.Residues 630-685 are 80% similar to a (GLYCINE SUBUNIT SYSTEM CLEAVAGE OXIDOREDUCTASE DEHYDROGENASE DECARBOXYLASE P-PROTEIN DECARBOXYLATING PHOSPHATE) protein domain (PD690281) which is seen in GCSP_MYCTU.Residues 686-792 are 66% similar to a (GLYCINE SYSTEM CLEAVAGE OXIDOREDUCTASE DEHYDROGENASE SUBUNIT DECARBOXYLASE PHOSPHATE PYRIDOXAL P-PROTEIN) protein domain (PD003536) which is seen in Q9VH09_DROME.Residues 810-963 are 78% similar to a (GLYCINE SYSTEM CLEAVAGE OXIDOREDUCTASE DEHYDROGENASE SUBUNIT DECARBOXYLASE PHOSPHATE PYRIDOXAL P-PROTEIN) protein domain (PD471673) which is seen in GCSP_PROMM.","","-45% similar to PDB:1WYT Crystal structure of glycine decarboxylase (P-protein) of the glycine cleavage system, in apo form (E_value = 1.4E_48);-45% similar to PDB:1WYU Crystal structure of glycine decarboxylase (P-protein) of the glycine cleavage system, in holo form (E_value = 1.4E_48);-45% similar to PDB:1WYV Crystal structure of glycine decarboxylase (P-protein) of the glycine cleavage system, in inhibitor-bound form (E_value = 1.4E_48);","Residues 12 to 444 (E_value = 1.6e-166) place ANA_0414 in the GDC-P family which is described as Glycine cleavage system P-protein.","","dehydrogenase (gcvP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0415","429696","431468","1773","6.25","-6.88","63782","ATGGATGCAGCGCTCCGTGAGGCTCAGGTCGAGGACCATCAGCCGTGCATCTGGTCACGACGCTGCGCCAGGGCTGGGGCGGGGCCGCGCCGCCACCTACACTGCTCGGCGATGACCACACTGACCACCTCCGCCCCCGTTCTCGACGCCCGAGGCGGCCTGCCGCGCACCTACCACGTGCGCACGCTCGGCTGCCAGATGAACGTCCACGACTCCGAGCACATGGCGGGACTGCTGGAGAGAGCCGGCTACCTGCGCGTCGAGGACGTGCCCGAGGCCGCCGCCCGCGCCACCGACGCCGGCGACGGCGGGGCCGATGTCGTCATCATCAACACCTGCTCGGTGCGTGAGAACGCCGCCACCCGGCTCTTCGGCAACCTGGGCCAGCTCGCCGCCGTCAAGCGTGAGCGCCCCGGCATGCAGATCGCCGTGGCCGGCTGCCTGGCCCAGCAGATGGGGGAGGGGATCGTCGAGCGGGCCCCCTGGGTCGACGTCGTCTTCGGCACCCACAACCTCGACGTCCTGCCCGCCCTGCTCGAGCGCGCCCGGCACAACTCCGCGGCCGCCGTCGAGCTCGAGGAGTCCCTCAAGGTCTTCCCCTCCACCCTGCCCACCCGCCGCGAGTCCTCCTACGCCGCCTGGGTCTCCATCGCCGTGGGCTGCAACAACACCTGCACCTTCTGCATCGTGCCCTCCCTGCGCGGCAAGCAGCGCGACCGCCGCCCCGGCGACGTCCTGGCCGAGGTCGAGGCCGTCGCCGCGCAGGGCGCCATCGAGGTGACCCTCCTGGGGCAGAACGTCAACTCCTACGGGGTCGGCTTCGGGGACCGCGGCGCCTTCGCCAAGCTGCTGCGGGCGGCCGGCTCAGTCGAGGGCATCGAGCGCGTGCGCTTCACCAGCCCCCACCCCGCCGCCTTCACCGACGACGTCATCGAGGCCATGGCCACCACCGAGGCCGTCATGCCCAGCCTGCACATGCCCCTGCAGTCCGGGTCCGACCGGGTGCTGCGCGCCATGCGCCGCTCCTACCGCACCCAGCGCTTCCTGGGCATCCTGGACAAGGTCCGCGCCGTCATGCCCGAGGCCGCCATCACCACCGACATCATCGTCGGCTTCCCCGGCGAGACCGAGGAGGACTTCCAGGCCACCCTCGACGTCGTCGAGCAGGCCCGCTTCGCCTCGGCCTACACCTTCGAGTACTCCCCGCGCCCGGGCACCCCCGCCGCCGACCGCGACGACCAGGTCCCCACCGAGGTCGTCAAGGACCGCTACCGGCGGCTCGACGCGCTCGTGCGCCGCATCGCCCACGAGGAGAACGAGCGCCAGGAGGGGCGCGTCGTGGAGGTGCTCGTCGCCGAGGGCGAAGGGCGCCGGGATGCGGTCACCGCCCGCATCTCTGGGCGCGCCGCCGACAACCGCCTCGTCCACGTCGCCCTGCCCGAGGGCCTGGCCGAGGACGACTACGCCGGCGGGGCCCCGCGCCCCGGCGACATGGTCACTGTGCGCGTCACCCACGGCGCCCCCCACAACCTCATCGCCGACTCCGCCCGCTGCGGACGCGAGCTGGACCCGCGCGCCGCGGCCGCCAACGAGGCACTCAAGCCCGGCGACCGCCTTTGGCTCGACGACGGCCCCGCCCTGTTCCAGGTGCGACGCACCCGCGCCGGGGACGCCTGGGAGCGCCGCCAGGCCGAGGCCTGCGCCACGCCCGAGCCCGACACCGCCCCGGTGAGCCTGGGCCTGCCCACCCTGCGCGTGGGCGCACCGGTCTGA","MDAALREAQVEDHQPCIWSRRCARAGAGPRRHLHCSAMTTLTTSAPVLDARGGLPRTYHVRTLGCQMNVHDSEHMAGLLERAGYLRVEDVPEAAARATDAGDGGADVVIINTCSVRENAATRLFGNLGQLAAVKRERPGMQIAVAGCLAQQMGEGIVERAPWVDVVFGTHNLDVLPALLERARHNSAAAVELEESLKVFPSTLPTRRESSYAAWVSIAVGCNNTCTFCIVPSLRGKQRDRRPGDVLAEVEAVAAQGAIEVTLLGQNVNSYGVGFGDRGAFAKLLRAAGSVEGIERVRFTSPHPAAFTDDVIEAMATTEAVMPSLHMPLQSGSDRVLRAMRRSYRTQRFLGILDKVRAVMPEAAITTDIIVGFPGETEEDFQATLDVVEQARFASAYTFEYSPRPGTPAADRDDQVPTEVVKDRYRRLDALVRRIAHEENERQEGRVVEVLVAEGEGRRDAVTARISGRAADNRLVHVALPEGLAEDDYAGGAPRPGDMVTVRVTHGAPHNLIADSARCGRELDPRAAAANEALKPGDRLWLDDGPALFQVRRTRAGDAWERRQAEACATPEPDTAPVSLGLPTLRVGAPV$","2-methylthioadenine synthetase","Cytoplasm","2-methylthioadenine synthetase","hypothetical protein","RNA modification enzyme, MiaB family","","Sofia H.J., Chen G., Hetzler B.G., Reyes-spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 2001. 29(5):1097-1106. PMID: 11222759","","","

InterPro
IPR002792
Domain

Deoxyribonuclease/rho motif-related TRAM
PS50926	$\"[440-517]T$	TRAM

InterPro
IPR005839
Family

Protein of unknown function UPF0004
PTHR11918	$\"[56-461]T$	RADICAL SAM PROTEINS
TIGR00089	$\"[57-513]T$	TIGR00089: RNA modification enzyme, MiaB fa
PS01278	$\"[215-235]T$	UPF0004

InterPro
IPR006463
Family

tRNA-i(6)A37 modification enzyme MiaB
TIGR01574	$\"[57-516]T$	miaB-methiolase: tRNA-i(6)A37 thiotransfera

InterPro
IPR006638
Domain

Elongator protein 3/MiaB/NifB
SM00729	$\"[211-429]T$	Elp3

InterPro
IPR007197
Domain

Radical SAM
PF04055	$\"[215-387]T$	Radical_SAM

InterPro
IPR007449
Domain

ZipA, C-terminal FtsZ-binding region
SM00771	$\"[243-369]T$	no description

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[220-421]T$	no description

InterPro
IPR013848
Domain

Protein of unknown function UPF0004, N-terminal
PF00919	$\"[57-168]T$	UPF0004

","BeTs to 24 clades of COG0621COG name: 2-methylthioadenine synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0621 is aompkz-qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB005839 (Protein of unknown function UPF0004) with a combined E-value of 6.2e-84. IPB005839A 60-78 IPB005839B 105-115 IPB005839C 136-155 IPB005839D 215-239 IPB005839E 324-344 IPB005839F 360-401 IPB005839G 443-452***** IPB002792 (Deoxyribonuclease/rho motif-related TRAM) with a combined E-value of 2.2e-15. IPB002792A 225-235 IPB002792B 326-336 IPB002792C 367-376","Residues 77-182 are 70% similar to a (UPF0004 OXIDOREDUCTASE FE-S ENZYME MIAB 2-METHYLTHIOADENINE SYNTHETASE TRNA MODIFYING MIAB-LIKE) protein domain (PD037433) which is seen in Q82KC4_STRAW.Residues 175-214 are 82% similar to a () protein domain (PD918760) which is seen in Q83HG3_TROW8.Residues 188-262 are 85% similar to a (OXIDOREDUCTASE UPF0004 FE-S UPF0313 ENZYME 2-METHYLTHIOADENINE MIAB SYNTHETASE TRNA 1.8.-.-) protein domain (PD376491) which is seen in Q6NGR0_CORDI.Residues 264-343 are similar to a (UPF0004 OXIDOREDUCTASE FE-S ENZYME 2-METHYLTHIOADENINE MIAB SYNTHETASE TRNA MODIFYING MIAB-LIKE) protein domain (PD463325) which is seen in Q6A8Z7_PROAC.Residues 367-434 are 89% similar to a (UPF0004 OXIDOREDUCTASE FE-S ENZYME 2-METHYLTHIOADENINE MIAB SYNTHETASE TRNA MODIFYING MIAB-LIKE) protein domain (PD000690) which is seen in Q8FPD5_COREF.Residues 444-562 are 54% similar to a (UPF0004 TRNA RV2733C/MT2803/MB2752C METHYLTRANSFERASE MIAB METHYLTHIOTRANSFERASE 2-METHYLTHIOADENINE SCO5787 TRANSFERASE ML0989) protein domain (PD800169) which is seen in Q82KC4_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 57 to 168 (E_value = 1.1e-44) place ANA_0415 in the UPF0004 family which is described as Uncharacterized protein family UPF0004.Residues 215 to 387 (E_value = 3.1e-31) place ANA_0415 in the Radical_SAM family which is described as Radical SAM superfamily.","","synthetase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0416","431625","432230","606","5.65","-3.41","21595","GTGGACTCGAGAGAGAAGCTGGTTGAGGCGATGGCAGAGCTGATGTGGGAGCGTGGTTACAGCGCCACGAGCCCGCGAGCGGTTCGCGAGCTCTCCGGCGTCGGTCAGGGGAGCATGTATCACTACTTCCCGACCAAGCGGGATCTCGGGCTGGCAGCTCTGAATCACAACTGCCAGATCCAGCTGGATTCCTGGAAGGCCGCGCTCAAGGACCTTGAGGACCCGCTCGAGATCCTCACTGCCTACCTCACCCTCCCGCGTGATCCGCTCAAAGGCTGCCGAGTCGGTCGGATGGCGCAGGACAAGGCGGTAGTGGCTGATGACGGTCTTCGTCAGCCGGTCGCCGAGGCCTTCGCCCAGCTTCGCGAGATGCTGGCCGCTGTCATTCGCATGGCCAGGTCGCAGGGGCGTCTGCCGGCAGACCTTGAGCCGGACCACCTGGCTCGCACGATGGTCGCCGTCGTTCAGGGCGGTTACGTCCTGGCCATGGCCGAGCAGGACAGGGCCCCGTATGACGCGGCCTGTCAAGGTGCCCTCGAGCTGCTCCGCGTAGCGGCCGGGACCACCGGCGCGGCCCCTGGCGGCGACGGGTCCGCCTCCTCCTGA","VDSREKLVEAMAELMWERGYSATSPRAVRELSGVGQGSMYHYFPTKRDLGLAALNHNCQIQLDSWKAALKDLEDPLEILTAYLTLPRDPLKGCRVGRMAQDKAVVADDGLRQPVAEAFAQLREMLAAVIRMARSQGRLPADLEPDHLARTMVAVVQGGYVLAMAEQDRAPYDAACQGALELLRVAAGTTGAAPGGDGSASS$","Transcriptional regulator; TetR family","Cytoplasm","transcription regulator, TetR family Atu3075","transcriptional regulator; TetR family","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[7-20]T$ $\"[28-51]T$	HTHTETR
PF00440	$\"[7-53]T$	TetR_N
PS50977	$\"[1-61]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[2-53]T$	no description

","BeTs to 15 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 2.2e-14. IPB001647 7-49***** IPB013571 (Tetracycline transcriptional regulator QacR-related, C-terminal) with a combined E-value of 3.5e-06. IPB013571A 1-51","Residues 2-49 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REGULATORY TETR-FAMILY FAMILY TETR PROBABLE) protein domain (PDA130A7) which is seen in Q73ZH2_MYCPA.Residues 3-173 are 48% similar to a (TRANSCRIPTIONAL REGULATOR) protein domain (PDA0Y1N9) which is seen in Q6MH81_BDEBA.Residues 82-174 are similar to a (TRANSCRIPTION TRANSCRIPTIONAL DNA-BINDING REGULATION REGULATOR FAMILY TETR REGULATOR REGULATORY PROBABLE) protein domain (PD037338) which is seen in Q73ZH2_MYCPA.","","-51% similar to PDB:1SGM Crystal Structure of Hypothetical Protein YXAF (E_value = 1.3E_11);","Residues 7 to 53 (E_value = 3e-11) place ANA_0416 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator, TetR family Atu3075","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0417","432289","433293","1005","5.15","-12.87","35062","ATGACTATTCGTATCGGTATCAACGGCTTCGGACGTATCGGACGCACCTACCTGCGTGCTGCGCTGGCCGGCGCAGCGGACGTCGAGGTCGTTGCCGTCAACGACCTGACCGACGCAGGCACGCTGGCCACGCTCTTGGAGTGGGACTCAGTGGCCGGGCACCTCGACGGCGTTGCCGCCGACGGCGAGGACCTCGAAGTCGCAGGGCGGATCATCAAGGTCTTCTCCGAACCGGACCCGGCCAAGATTCCCTGGGGTGAGGTCGGGGCCGACGTCGTCATCGAGTCCACCGGATTCTTCGTCGACCGGGACAAGGCGGCCCAGCACCTCAAGGGAGGCGCCAAGAAGATCATCGTCTCCGCACCCGCCAAGGGCGACGTCCCCACCATCGTCCTGGGGGTCAACGACGGCCAGTTGGATGTCTCCGCCGCCGACGTGTTCTCCAACGGATCGTGCACCACCAACTCCCTGGCCCCGCTTGCCAGGGTCCTCCACGACGCCTTCGGGATCGAGAGCGGTCTCATGACGACGATCCACGCCTACACCGGGGACCAGCGGCTTCACGACGCACCTCACAAGGACCTGCGTCGGGCGCGCGCTGCCGCCGCCTCCATCGTTCCCACCTCCTCAGGGGCCGCCCGGGCCATCGGTCTGGTCATCCCCGAGCTCGACGGGCGCCTGACCGGCGCTGCCATGAGGGTTCCGGTCCCGGTCGGCTCGATTACCGACCTCACCGTGGTCACCTCCCGCCCGGCAACGGTTGAGGACGTCAATGCAGCTTTCCGCGAGGCTGCCGATCACGGGCCGCTGGCCGGCTACCTGCAGTACTCCCAGGCGCCGATCGTCTCCCACGACATCGTTGGCAACCCGCACTCCTCGATCTTCGATGCGCCCCTGACCGAGGTGATCGACGGCCAGGTCAAGGTCTTCGGATGGTACGACAACGAGTGGGGCTTCTCCAACCGCCTCGTGGAGTTCTCCCAGAGGATCGGTGAACAGCTCTGA","MTIRIGINGFGRIGRTYLRAALAGAADVEVVAVNDLTDAGTLATLLEWDSVAGHLDGVAADGEDLEVAGRIIKVFSEPDPAKIPWGEVGADVVIESTGFFVDRDKAAQHLKGGAKKIIVSAPAKGDVPTIVLGVNDGQLDVSAADVFSNGSCTTNSLAPLARVLHDAFGIESGLMTTIHAYTGDQRLHDAPHKDLRRARAAAASIVPTSSGAARAIGLVIPELDGRLTGAAMRVPVPVGSITDLTVVTSRPATVEDVNAAFREAADHGPLAGYLQYSQAPIVSHDIVGNPHSSIFDAPLTEVIDGQVKVFGWYDNEWGFSNRLVEFSQRIGEQL$","Glyceraldehyde-3-phosphate dehydrogenase, type I","Cytoplasm","glyceraldehyde-3-phosphate dehydrogenase, typeI","glyceraldehyde 3-phosphate dehydrogenase ","glyceraldehyde-3-phosphate dehydrogenase, type I","","Huang X.Y., Barrios L.A., Vonkhorporn P., Honda S., Albertson D.G., Hecht R.M. Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans. J. Mol. Biol. 1989. 206(3):411-424. PMID: 2716055Dugaiczyk A., Haron J.A., Stone E.M., Dennison O.E., Rothblum K.N., Schwartz R.J. Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle. Biochemistry 1983. 22(7):1605-1613. PMID: 6303388Berry M.D., Boulton A.A. Glyceraldehyde-3-phosphate dehydrogenase and apoptosis. J. Neurosci. Res. 2000. 60(2):150-154. PMID: 10740219Tatton W., Chalmers-redman R., Tatton N. Neuroprotection by deprenyl and other propargylamines: glyceraldehyde-3-phosphate dehydrogenase rather than monoamine oxidase B. J. Neural Transm. 2003. 110(5):509-515. PMID: 12721812","","","

InterPro
IPR000173
Family

Glyceraldehyde 3-phosphate dehydrogenase
PR00078	$\"[109-122]T$ $\"[146-164]T$ $\"[173-189]T$ $\"[229-246]T$ $\"[270-285]T$	G3PDHDRGNASE
PTHR10836	$\"[3-333]T$	GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
PF00044	$\"[3-152]T$	Gp_dh_N
PF02800	$\"[157-313]T$	Gp_dh_C

InterPro
IPR006424
Family

Glyceraldehyde-3-phosphate dehydrogenase, type I
TIGR01534	$\"[4-325]T$	GAPDH-I: glyceraldehyde-3-phosphate dehydro

noIPR
unintegrated

unintegrated
G3DSA:3.30.360.10	$\"[151-315]T$	no description

","BeTs to 18 clades of COG0057COG name: Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0057 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 3","***** IPB000173 (Glyceraldehyde 3-phosphate dehydrogenase) with a combined E-value of 1.1e-114. IPB000173A 4-15 IPB000173B 89-125 IPB000173C 146-188 IPB000173D 193-245 IPB000173E 291-326","Residues 83-133 are 84% similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GAPDH GLYCERALDEHYDE 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD000250) which is seen in Q9LPW0_ARATH.Residues 134-174 are 78% similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GLYCERALDEHYDE GAPDH 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD589901) which is seen in G3P2_STAEP.Residues 175-250 are similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GLYCERALDEHYDE GAPDH 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD000244) which is seen in G3P_STRAE.Residues 254-332 are 77% similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GLYCERALDEHYDE GAPDH 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD444561) which is seen in Q741C7_MYCPA.","","-68% similar to PDB:1CER DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION (E_value = 4.3E_86);-68% similar to PDB:2G82 High Resolution Structures of Thermus aquaticus Glyceraldehyde-3-Phosphate Dehydrogenase: Role of 220's Loop Motion in Catalysis (E_value = 4.3E_86);-72% similar to PDB:1HDG THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS RESOLUTION (E_value = 5.6E_86);-68% similar to PDB:1GD1 STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.8 ANGSTROMS RESOLUTION (E_value = 9.5E_86);-68% similar to PDB:2GD1 COENZYME-INDUCED CONFORMATIONAL CHANGES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILLUS (E_value = 9.5E_86);","Residues 3 to 152 (E_value = 3.3e-73) place ANA_0417 in the Gp_dh_N family which is described as Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain.Residues 3 to 33 (E_value = 6.3e-05) place ANA_0417 in the GFO_IDH_MocA family which is described as Oxidoreductase family, NAD-binding Rossmann fold.Residues 157 to 313 (E_value = 4.5e-98) place ANA_0417 in the Gp_dh_C family which is described as Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain.","","dehydrogenase, type I (gap)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0418","433494","433964","471","5.22","-7.66","17651","ATGCCCAGCTTCGACGCCAGCTCTGCTGCCGCCGCCACGGTCCCCAGGCCCGTGGACGTCGACCGTATCCACGAGTGCGTCAAACGACTGGGACTGCGCTACTTCATCGACGACGAGGGCGACATCGGCATCCCCTGGCGCTACGTCACCGTCCACGCCATCTTCCAGGACACCAGGGCCGTCCAGATGCGCGGAATCTGGCACCGCATCGCCGACACCGAGCACCTGACCCAGTTGCGCGCCCTGGTCGAGGACTGGAACACCACCCGTATCGGCCCCAAGGCCTACCTCACCGTCGCCGACGGCGGAGTCGTGCGTCTTCACGGCGAGTACACCTACCCCCTCGAGGCGGGAATGACGGACCGACAGCTCGAGGACTTCGTCTTCGGCGGCTGCCGGCTCATCGTCGCCCTCATGCACGAGGCCGAGGAGCAGTTCCCCGACGAGCTGCGCGGAAGCCTGGAGCCGTGA","MPSFDASSAAAATVPRPVDVDRIHECVKRLGLRYFIDDEGDIGIPWRYVTVHAIFQDTRAVQMRGIWHRIADTEHLTQLRALVEDWNTTRIGPKAYLTVADGGVVRLHGEYTYPLEAGMTDRQLEDFVFGGCRLIVALMHEAEEQFPDELRGSLEP$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 2-128 are 46% similar to a (SCO3659) protein domain (PD306749) which is seen in Q9X8S6_STRCO.Residues 9-128 are 49% similar to a (CGL2103) protein domain (PD721090) which is seen in Q8NNT4_CORGL.","","-44% similar to PDB:1MIO X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION (E_value = );-40% similar to PDB:1PKF Crystal Structure of Epothilone D-bound Cytochrome P450epoK (E_value = );-40% similar to PDB:1Q5D Epothilone B-bound Cytochrome P450epoK (E_value = );-40% similar to PDB:1Q5E Substrate-free Cytochrome P450epoK (E_value = );-61% similar to PDB:1FP4 CRYSTAL STRUCTURE OF THE ALPHA-H195Q MUTANT OF NITROGENASE (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0419","433964","434752","789","4.50","-23.84","28378","ATGCCCAGACTGCAACGCCTCACCGACTTCATCGCACGCCTCCTGGGCAAGGAGTGGGATGTACGGGCGCTGGACCACCGGCGCAGCAGCGGGCCGGTTGACTCCCAGAGCCGATCCGACGAGCCCCCGACCATCTCGCCGTACGTCACAGGTCACGTGGAACCCTCAGCTTCAGGGGAATTAGCCGACTCAACCACTCCGACCGACTCCAGTGGTCCATCGGAGCCGGCCAGGACAACCGCCTCGGCGCAGACCCTGGACGACTCACGCAGCTGGTCGAGCACATCAGGCCGACCGGAGGAGGAGCCGGCAGCGGGAGGACGGGGCGCCGACCGCTCGTCGGACCTGGAGTCGGCCGACGAGGAGCCCCAGGAGTTGACCCTGGCCCGGATCGAGTCCATGCTCACCGGCCCCATGGAGTACAACGTCCAGCTGACCGAGGACCGCGAGCACCCCTGCCTCCTGGGCACCTGGGACTCCTTCCCCTTCGTCATCGAGATTCCTGAGGGGCACGAGGGTTGGCTCCTGGTCTCCGGGGACTGGGAGGAGGCCGCCCCCGCCTCCCAGAGGGACGAGATCGCCGCCAGCGTCAACGACTGGAACCGGGACAAGTTCTTCCCCACCGTCGGCGTCATCGACACCCCCATCGGTCCGCTGGTGCGCGCCACCTACCTCACCGACCTGTCCGCCGGGGTCACCGACGCCCAGCTGCGCCTCCACCTGGACACGGCGCTGTCCGCCTGCACCCAGGCGCTCAGCCTCGTGGGCCCCCTCCTGCCGGAGATCTGA","MPRLQRLTDFIARLLGKEWDVRALDHRRSSGPVDSQSRSDEPPTISPYVTGHVEPSASGELADSTTPTDSSGPSEPARTTASAQTLDDSRSWSSTSGRPEEEPAAGGRGADRSSDLESADEEPQELTLARIESMLTGPMEYNVQLTEDREHPCLLGTWDSFPFVIEIPEGHEGWLLVSGDWEEAAPASQRDEIAASVNDWNRDKFFPTVGVIDTPIGPLVRATYLTDLSAGVTDAQLRLHLDTALSACTQALSLVGPLLPEI$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG0752COG name: Glycyl-tRNA synthetase, alpha subunitFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0752 is -------qv--lbcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-42% similar to PDB:1J5W Crystal structure of Glycyl-tRNA synthetase alpha chain (TM0216) from Thermotoga maritima at 1.95 A resolution (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0420","434758","435753","996","6.75","-1.12","36279","ATGAGCCCAGGGTCCCCGCGCGCCCCCCGTCTGCCCAGAGTCGTCGTCGTAGGTCCCACGGCCACCGGCAAGTCCGCCCTCGCCCTCGACCTTGCCGAGCGGATGCACTCCGACGAACCGGCGACCCGCGCCGAGATCATCAACGCCGACGCCTCCCTGCTCTACCGCGGCATGGACATCGGCACCGCCAAACCCAGCCCCGCCGAGCGGGCCCGCGTCCCCCATCACCAGATCGACGTCCTCACCGTCAGGGACAGGGCATCCGTGGCAGCCTTCCAACGCAGCGCCCGCGGAGACATCGACGCCGTCGAGTCACGGGGCCACCTGCCGATCATCGCCGGAGGCTCCGGCCTGTACGTGCGGGCCCTGACCGACGACCTCGACTTCCCCGGCACCGACCCGGCCGTGCGCAGCCGCCTGAGTGAGCGCGCCGAGCAGGAGGGGACCGCCGCCCTCCACGCCGAGCTGGCTCGCCTCGACCCGGCCGCCGCCGAGCGCGTCGAGACCTCCAACACCCGCAGGATCGTGCGAGCCCTGGAGGTCATCGAGATCACCGGCCGTCCCTTCTCCGCCTCCCTGCCCCGCTACGAGGACATCGCCCCCACCGTCCACATCGCCCTGCGCTGCGAGCGTCGGCTCCTGGACAAGCGCATCAACGAGCGGGCCCGCGCCATGTTCGACGGCGACCTCGTCGAGGAGGTGGAGGCCCTCATCGACCAGGGCATCCGGGAGGGGGAGACCGCCCCACGCGCCATCGGCTACGCCCAGGCGCTCGCGGTCATCGACGGGACCATGAGCGTACCCGAGGCGGTCGACTCCACCGCCCTGGCCACCCGCCAGCTCGCCTCCCGCCAGATCAAGTGGTTCCGGCGTGACCCACGGCTGCACTGGATCGACGTCGCCCTCACCGAGACCGGGCAGTGCACCGACTCCGAGCGCTCCCGGCTCACCCGGCGGGCATGGGAGTTCGTCAGCGAGCATCGCGGCGTCGCTTAG","MSPGSPRAPRLPRVVVVGPTATGKSALALDLAERMHSDEPATRAEIINADASLLYRGMDIGTAKPSPAERARVPHHQIDVLTVRDRASVAAFQRSARGDIDAVESRGHLPIIAGGSGLYVRALTDDLDFPGTDPAVRSRLSERAEQEGTAALHAELARLDPAAAERVETSNTRRIVRALEVIEITGRPFSASLPRYEDIAPTVHIALRCERRLLDKRINERARAMFDGDLVEEVEALIDQGIREGETAPRAIGYAQALAVIDGTMSVPEAVDSTALATRQLASRQIKWFRRDPRLHWIDVALTETGQCTDSERSRLTRRAWEFVSEHRGVA$","tRNA delta(2)-isopentenylpyrophosphate transferase","Cytoplasm","tRNA delta(2)-isopentenylpyrophosphatetransferase","tRNA delta(2)-isopentenylpyrophosphate transferase ","tRNA delta(2)-isopentenylpyrophosphate transferase","","Canaday J., Gerad J.C., Crouzet P., Otten L. Organization and functional analysis of three T-DNAs from the vitopine Ti plasmid pTiS4. Mol. Gen. Genet. 1992. 235(2):292-303. PMID: 1465104Boguta M., Hunter L.A., Shen W.C., Gillman E.C., Martin N.C., Hopper A.K. Subcellular locations of MOD5 proteins: mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms commingle in the cytosol. Mol. Cell. Biol. 1994. 14(4):2298-2306. PMID: 8139535","","","

InterPro
IPR002627
Family

tRNA isopentenyltransferase
PD004674	$\"[78-123]T$	MIAA_MYCLE_P46811;
PTHR11088	$\"[54-299]T$	TRNA DELTA(2)-ISOPENTENYLPYROPHOSPHATE TRANSFERASE-RELATED
PF01715	$\"[52-301]T$	IPPT
TIGR00174	$\"[13-303]T$	miaA: tRNA delta(2)-isopentenylpyrophosphat

InterPro
IPR011593
Domain

Isopentenyl transferase-like
PD005388	$\"[20-75]T$	MIAA_SHEON_Q8CX50;

noIPR
unintegrated

unintegrated
PTHR11088:SF21	$\"[54-299]T$	TRNA DELTA(2)-ISOPENTENYLPYROPHOSPHATE TRANSFERASE

","BeTs to 18 clades of COG0324COG name: tRNA delta(2)-isopentenylpyrophosphate transferaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0324 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB002627 (tRNA isopentenyltransferase) with a combined E-value of 3.3e-46. IPB002627A 14-49 IPB002627B 107-123 IPB002627C 160-187 IPB002627D 214-237 IPB002627E 278-290***** IPB002648 (Isopentenyl transferase) with a combined E-value of 7.9e-11. IPB002648A 13-56 IPB002648B 107-121 IPB002648D 270-289","Residues 20-75 are 75% similar to a (TRANSFERASE TRNA ATP-BINDING DELTA2-ISOPENTENYLPYROPHOSPHATE ISOPENTENYLTRANSFERASE IPP IPTASE IPPT ISOPENTENYL-DIPHOSPHATE:TRNA NUCLEOTIDYLTRANSFERASE) protein domain (PD005388) which is seen in MIAA_SHEON.Residues 70-143 are 74% similar to a (TRANSFERASE TRNA ATP-BINDING MIAA IPP IPTASE ISOPENTENYL-DIPHOSPHATE:TRNA ISOPENTENYLTRANSFERASE IPPT DELTA2-ISOPENTENYLPYROPHOSPHATE) protein domain (PD904821) which is seen in MIAA_MYCTU.Residues 78-123 are 80% similar to a (TRANSFERASE TRNA ATP-BINDING DELTA2-ISOPENTENYLPYROPHOSPHATE ISOPENTENYLTRANSFERASE IPP IPTASE IPPT ISOPENTENYL-DIPHOSPHATE:TRNA NUCLEOTIDYLTRANSFERASE) protein domain (PD004674) which is seen in MIAA_MYCLE.Residues 148-190 are 74% similar to a (TRANSFERASE TRNA ATP-BINDING DELTA2-ISOPENTENYLPYROPHOSPHATE ISOPENTENYLTRANSFERASE IPP IPTASE IPPT ISOPENTENYL-DIPHOSPHATE:TRNA NUCLEOTIDYLTRANSFERASE) protein domain (PD703751) which is seen in MIAA_STRAW.Residues 194-299 are 61% similar to a (TRANSFERASE TRNA ATP-BINDING DELTA2-ISOPENTENYLPYROPHOSPHATE ISOPENTENYLTRANSFERASE IPP IPTASE IPPT ISOPENTENYL-DIPHOSPHATE:TRNA NUCLEOTIDYLTRANSFERASE) protein domain (PD584724) which is seen in MIAA_MYCTU.","","-57% similar to PDB:1GXB ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH PYROPHOSPHATE AND MAGNESIUM (E_value = );-57% similar to PDB:1O17 ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD) (E_value = );-57% similar to PDB:1ZXY Anthranilate Phosphoribosyltransferase from Sulfolobus solfataricus in complex with PRPP and Magnesium (E_value = );-57% similar to PDB:1ZYK Anthranilate Phosphoribosyltransferase in complex with PRPP, anthranilate and magnesium (E_value = );-57% similar to PDB:2GVQ Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate (E_value = );","Residues 52 to 301 (E_value = 7.7e-104) place ANA_0420 in the IPPT family which is described as IPP transferase.","","delta(2)-isopentenylpyrophosphate transferase (miaA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0421","435764","436714","951","4.49","-26.48","32424","ATGCCGCACTCGACAGGCCTTCGCGGTCGTGAGCTCGTCAAGGGCCACGCGACCCTCAACGACTTCCTCATGCTGGTCGACCCCGGCTGCGAGGTCGCCATCAGCGGCGCCGACATCGCAGCGGTCTGCGACCGCCACAGCGGCATCGGCGCCGACGGCTTCGTGCGCGTCGTACGGACCACTGCCCTGCCCGGCGGCGGAGCCTTCGCCGCCTCCGTGCCCGAGGCCGAGTGGTTCATGGACTACTACCGCGCCGACGGAACCGTGGCCGAGATGTGCGGCAACGCCGCACGCCTGTTCGCCCACGTCCTGGACCGTGAGGGCCTGTGCCCCATCGCCGACGGCGAGTCCGTCACCATCGGCACACGCGGCGGGGCCCGCACCATCACCCGCCTGGGCGAGCTGTGGACTGTGGACATGGGGCCGGCCCGCCTGGCCAGCCCCGAGGAGGCCGAGGACGAGGGCTGGGACACGGCCGTCGACGTCCCCGGCCTGGACGGGCCGCGGGCCGCCCTGAGTGTGGAGATCGCCGGCCCCCACACCGTCGTCGCCCTGGGGGAGGAGAGTGAGCTCGAGGCGGCCGCCTTCGCCGGCCTCACCGACTCCGCGGACCCGGTTGCCTACGACCCCGCCCCCGAGGTCGGCACCAACCTCGAGCTCGTCGTGCCGCTGGGGGAGGAGACCGACCCCGACACCCAGTCATCGGTGGGTATCGTCCGTATGCGTGTCCTGGAGCGCGGCGTGGGGGAGTCCCTCTCCTACGGAGCGGGGTGCTGCGCCGTCGCCGTCGCCCTGCACGCCTGGACCGGTCCGGGCGCTCCCGAGGACTACCGACTGCTCGTTCCCGGCGGAGAGATCGGGGTCCACGTGGGCTCCGATCCCCTGGGTGCGGACAGCAGCGTGCTGCTGACCGGCCCGGCCACGATCACCGCGCGGATCACCGTCGCCTGA","MPHSTGLRGRELVKGHATLNDFLMLVDPGCEVAISGADIAAVCDRHSGIGADGFVRVVRTTALPGGGAFAASVPEAEWFMDYYRADGTVAEMCGNAARLFAHVLDREGLCPIADGESVTIGTRGGARTITRLGELWTVDMGPARLASPEEAEDEGWDTAVDVPGLDGPRAALSVEIAGPHTVVALGEESELEAAAFAGLTDSADPVAYDPAPEVGTNLELVVPLGEETDPDTQSSVGIVRMRVLERGVGESLSYGAGCCAVAVALHAWTGPGAPEDYRLLVPGGEIGVHVGSDPLGADSSVLLTGPATITARITVA$","Diaminopimelate epimerase","Cytoplasm","diaminopimelate epimerase","diaminopimelate epimerase ","Diaminopimelate epimerase","","","","","

InterPro
IPR001653
Family

Diaminopimelate epimerase
PF01678	$\"[12-146]T$	DAP_epimerase
TIGR00652	$\"[10-315]T$	DapF: diaminopimelate epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.10.310.10	$\"[10-149]T$	no description

","BeTs to 17 clades of COG0253COG name: Diaminopimelate epimeraseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0253 is a-m----qv-r-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB001653 (Diaminopimelate epimerase) with a combined E-value of 2e-29. IPB001653A 12-25 IPB001653B 48-57 IPB001653C 77-103 IPB001653D 136-151 IPB001653F 222-261 IPB001653G 303-313","Residues 14-57 are 77% similar to a (EPIMERASE DIAMINOPIMELATE ISOMERASE LYSINE BIOSYNTHESIS DAP DAPF) protein domain (PDA0M1T5) which is seen in Q73W21_MYCPA.Residues 209-309 are 47% similar to a (EPIMERASE DIAMINOPIMELATE ISOMERASE DAP LYSINE BIOSYNTHESIS 3D-STRUCTURE 3-EPIMERASE RIBULOSE-PHOSPHATE AT3G53580/F4P12_280) protein domain (PD005029) which is seen in DAP2_ANASP.Residues 209-309 are 47% similar to a (EPIMERASE DIAMINOPIMELATE ISOMERASE DAP LYSINE BIOSYNTHESIS 3D-STRUCTURE 3-EPIMERASE RIBULOSE-PHOSPHATE AT3G53580/F4P12_280) protein domain (PD005029) which is seen in DAP2_ANASP.","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 146 (E_value = 3.3e-13) place ANA_0421 in the DAP_epimerase family which is described as Diaminopimelate epimerase.","","epimerase (dapF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0422","436797","438218","1422","9.63","10.26","48686","ATGAGCCAGCCATCCACACGCTCCGCCGTCGGCGCCGTCCTGCCGACCGGCCTGATGCTCTTCGCCCTGTTCTTCGGGGCGGGCAACCTCATCTTCCCGCCTCTGCTGGGCGCCGCCTCGGGCAAGTCCTTCATTCCGGCCATGGGGGGCTTCCTCGCCACCGGGGTGCTCATGCCGCTCATCACCGTGGTCGCCGTCTCCGCATCCGGTGAGGGGATCCTGGGACTGGCTCGCAGAGTGGGACCACGATTCGGCACCGTCATGCCGCTGGCGGTCTATCTGGTGATCGGTCCTCTGACCGGTATCGCTCGTGCCGCCACGGTCGCTTACGAGCTGGCGACCCTTCCGGTGCTCGAGCTGCTGGGGATTCACCACTCCCGCCTGGCCCTGCTGGCGCATGTGACGGTGTTCATGGGGGTGTCCTTCAGCATCGCCCTCAGCCCGAGCCGCCTGGCCGACCGCGTCGGGCGCTGGCTCACTCCCGCCCTGCTGGCCCTGCTGGCCCTGCTGTGCGGGGCCGCCATCCTGATGTTCCCCAGCGTGGAGCGCGAGGCCGTCGGGGACTATGTGAGTCACCCCCTGACCACCGGGTTGACTCGGGGCTACCTCACCATGGACGTCCTGGCGGCCACCGTCTTCGGCGTCGTGGTCATCTCCTCCCTGCGCGAACGAGGCCTGTCCTCTTCCCGCGCTCTGGTGCGCAGCACGATCCTGTCCGGGGGTATCGCTGCCGCGCTCCTGGGGCTGGTGTACATCGGCCTGGCCGTCCTGGGAACCCACACCCGCGGGCGGATCACCGCCGACGCCGAGGAGGGCACCGAGTTGCTGAGCAAAGCGGCCTCCTCGACGCTGGGGGCCTTGGGCGTCGTCATCTTCGCCGCTATCGTCATCCTGGCCTGCCTGACCACCGCCGTGGGGCTGCTGGCCTCCTGGGCCGGATACGCCTACACCGCCTGGCCGGCCGTCTCCTTCAACCGGCAGCTCGCCGCCTGCACGATCGTCGCCTTCACCCTGGCCAACCTCGGACTGAATGCCATCCTCAAGATCGCGGGGCCGGTGACGTTCCTGCTCTATCCCCTCGTCATCGCCCTGGTGATCGTGACACTGATCGATGCCCTGGCGCCGGGACGGCTCAAGGCCGCCTACCGGTGGTGCGTGAGCACAGCGGGGATCCTCGGCTCCGTCTCCGCCATCATGGCCACCGGCTGGAAGGGCCCCAGCAGGCTGCTGGAGCGCGCCGGCCTGTGGAGCGACTCCTCCGGCTGGATCCTGCCGGTGCTCATCGCCCTGGTGATTGGGATCGCCCTGCTGATCGGCATCCTCCTGGACATCCGCTCCGGAGCCTGGTCCACGCCCGCCCCCGGGGAGCCTCCCAGCCGGGCTCAGCAGGACGTCGAGCACGCCGCGGCCTCACAGCTGTGA","MSQPSTRSAVGAVLPTGLMLFALFFGAGNLIFPPLLGAASGKSFIPAMGGFLATGVLMPLITVVAVSASGEGILGLARRVGPRFGTVMPLAVYLVIGPLTGIARAATVAYELATLPVLELLGIHHSRLALLAHVTVFMGVSFSIALSPSRLADRVGRWLTPALLALLALLCGAAILMFPSVEREAVGDYVSHPLTTGLTRGYLTMDVLAATVFGVVVISSLRERGLSSSRALVRSTILSGGIAAALLGLVYIGLAVLGTHTRGRITADAEEGTELLSKAASSTLGALGVVIFAAIVILACLTTAVGLLASWAGYAYTAWPAVSFNRQLAACTIVAFTLANLGLNAILKIAGPVTFLLYPLVIALVIVTLIDALAPGRLKAAYRWCVSTAGILGSVSAIMATGWKGPSRLLERAGLWSDSSGWILPVLIALVIGIALLIGILLDIRSGAWSTPAPGEPPSRAQQDVEHAAASQL$","Branched-chain amino acid transport system II carrier protein","Membrane, Cytoplasm","branched-chain amino acid transport system IIcarrier protein","branched-chain amino acid transporter","branched-chain amino acid transport system II carrier protein","","","","","

InterPro
IPR004685
Family

Branched-chain amino acid transport system II carrier protein
PF05525	$\"[9-440]T$	Branch_AA_trans
TIGR00796	$\"[17-425]T$	livcs: branched-chain amino acid transport

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[51-69]?$ $\"[90-110]?$ $\"[129-147]?$ $\"[162-182]?$ $\"[201-221]?$ $\"[236-256]?$ $\"[290-312]?$ $\"[327-347]?$ $\"[353-373]?$ $\"[383-403]?$ $\"[422-442]?$	transmembrane_regions

","BeTs to 7 clades of COG1114COG name: Branched-chain amino acid permeasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1114 is -----------lb-efgh-----it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 16-112 are similar to a (ACID AMINO BRANCHED-CHAIN CARRIER SYSTEM II CHAIN BRANCHED TRANSPORTER AMINO-ACID) protein domain (PD007051) which is seen in Q81T30_BACAN.Residues 263-353 are 63% similar to a (ACID AMINO BRANCHED-CHAIN CARRIER SYSTEM II CHAIN BRANCHED TRANSPORTER AMINO-ACID) protein domain (PD007729) which is seen in Q8FND2_COREF.","","No significant hits to the PDB database (E-value < E-10).","Residues 9 to 440 (E_value = 1.9e-124) place ANA_0422 in the Branch_AA_trans family which is described as Branched-chain amino acid transport protein.","","amino acid transport system II carrier protein (brnQ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0423","440365","439757","609","5.82","-3.87","21721","GTGAGCGAGCACTACTTCACCGCCTCCCCCGCCGTCGAGCCCGAGGAGCGCACCCACCGCTTCTCGATCCGTGGCGTCGAGCACACGGTGGTCACGGCCTCAGGCGTCTTCAGCGCCGACCGCCTCGACAAGGGCACCCAGGTCCTCCTCGATCACGTCCCCGATCCGGCCCAGACCGGCACGTTCCTCGACCTGGGCTGCGGATGGGGGCCGATCACGCTGGCCCTGGCCGGGGCCGCTCCGCAGGCACAGGTCCTGGCCACCGATGTCAACGAGCGCTCCCTGGCCCTGACCGCCCGCAACGCCGCTGCCGCAGGCCTGGACAACGTGCGGACCGCCCCGGCCGACGCACTGCTGGCCGAGCTGCGCCAGAGCTCGACGCCGGTGGATCTCATCTGGTCCAACCCTCCGGTGCGCATCGGCAAGGAAGCCCTGCACGCCCTGCTGCTGGACTGGCTGGCGCTGCTGTCCGACGACGGCGAGGCCTGGCTGGTGGTGCTCAAGAACCTGGGAGCCGACTCCCTGGCGACCTGGCTGAGGGACCAGGGCTGGGACGTGAGCCGGATGGCCTCCTCGAAGGGCTTCAGGGTCCTGCGAGTGCGCCGCTGA","VSEHYFTASPAVEPEERTHRFSIRGVEHTVVTASGVFSADRLDKGTQVLLDHVPDPAQTGTFLDLGCGWGPITLALAGAAPQAQVLATDVNERSLALTARNAAAAGLDNVRTAPADALLAELRQSSTPVDLIWSNPPVRIGKEALHALLLDWLALLSDDGEAWLVVLKNLGADSLATWLRDQGWDVSRMASSKGFRVLRVRR$","Methyltransferase","Cytoplasm","Protein","hypothetical protein","methyltransferase small","","","","","

InterPro
IPR007848
Domain

Methyltransferase small
PF05175	$\"[27-199]T$	MTS

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[6-202]T$	no description
PTHR18895	$\"[44-202]T$	METHYLTRANSFERASE

","BeTs to 9 clades of COG2813COG name: 16S RNA G1207 methylase RsmCFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG2813 is --m-k---vd-lb-efgh---j----Number of proteins in this genome belonging to this COG is 1","***** IPB013675 (Methyltransferase small, N-terminal) with a combined E-value of 9.7e-08. IPB013675C 25-69***** IPB003358 (Putative methyltransferase) with a combined E-value of 7.8e-06. IPB003358A 60-91 IPB003358B 104-117","Residues 1-62 are 62% similar to a () protein domain (PD752102) which is seen in Q8G4R9_BIFLO.Residues 23-164 are 54% similar to a (METHYLTRANSFERASE TRANSFERASE HEMK 2.1.1.- METHYLASE PROTOPORPHYRINOGEN OXIDASE RIBOSOMAL L11 ADENINE-SPECIFIC) protein domain (PD001640) which is seen in Q8TXG5_METKA.Residues 132-198 are 62% similar to a () protein domain (PD968535) which is seen in Q6AE06_BBBBB.","","-46% similar to PDB:1DUS MJ0882-A hypothetical protein from M. jannaschii (E_value = 2.2E_16);","Residues 27 to 199 (E_value = 2.1e-34) place ANA_0423 in the MTS family which is described as Methyltransferase small domain.Residues 63 to 162 (E_value = 0.0003) place ANA_0423 in the Methyltransf_12 family which is described as Methyltransferase domain.Residues 63 to 118 (E_value = 1.7e-06) place ANA_0423 in the Methyltransf_11 family which is described as Methyltransferase domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0423.1","440535","441425","891","11.12","12.07","31289","ATGAGCCGATACAAGGCTCTCGCAAAGGCGCTCAGCGGCTGGGCAATCTTGACGTTGGGGGTGACTCTTTCGATAGCGATCGCACAGGCTGTCGGATCCAGGACTGAGACCGGACCTGTATTCATTCGCGTGTCTCAGGCAGTTCTGGTCACATTGTTCGTTGTTCCCGCGATCGTGGCTTGTCGTCGTCTCCTTGACCGCAGGACTCTTGCCGGGATGGGCCTATCACGCCACTGGCCCGCCGCGGCCGCGACCGGGGTGGCCGTCGGTGTCGTGACCGGGGCTGTTGTGTGGACACCCGTGTTCTTGATCGGCTGGGCCCGGTTCGATCACCTCGAACCGGCGGCGCTCGCAACCTTCCTCGCAGTCAACGCGGTCGTCCTGCTACTGTACGAGGCATTGCCGGAGGAGATCGCGCTGCGCGGCTACGGGTGGTCGACTCTACGGGAAAGTTGGGGCCCGCTCGCGGCCACCATGACGATCACGGTTCTCTTCTGCCTCAGTACGGCGTTGAGCAATCTGATTCGAATGACGTCAACGCTCGTTCTGGGAGGCGGAACGACGGGCTTCTCTCTGGCGCCGAGCGGTAGCGACCCCTTTTTCTACATAGCTTTGCTGTTCGTCTTCGGTCTCACACTGGTTGCGGCCCGACGGATCCCACTACCGGGTGCGCTCACCTCTGCGATCGCCTTCCATCACACGTTTCTCACCATCAACCGCGTGCTTCTGGGCGGTCTTGGCTGGATCGACTCCGGGGTCGGGATCGGGTTCGCCGCGCCCGAGGTGCCCGCGATCAGCCTTGTGCACGCTGCGCTTGCCGGAGCTGTCTTCATGGTGGTGCGGCGGTGGCTGGAACGCCGTACAGCGGTTGTATCGAGGCGGGTAGCCTGA","MSRYKALAKALSGWAILTLGVTLSIAIAQAVGSRTETGPVFIRVSQAVLVTLFVVPAIVACRRLLDRRTLAGMGLSRHWPAAAATGVAVGVVTGAVVWTPVFLIGWARFDHLEPAALATFLAVNAVVLLLYEALPEEIALRGYGWSTLRESWGPLAATMTITVLFCLSTALSNLIRMTSTLVLGGGTTGFSLAPSGSDPFFYIALLFVFGLTLVAARRIPLPGALTSAIAFHHTFLTINRVLLGGLGWIDSGVGIGFAAPEVPAISLVHAALAGAVFMVVRRWLERRTAVVSRRVA$","Membrane protein","Membrane, Cytoplasm","","","","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[12-34]?$ $\"[40-60]?$ $\"[81-101]?$ $\"[152-172]?$ $\"[174-194]?$ $\"[200-215]?$ $\"[236-258]?$ $\"[264-284]?$	transmembrane_regions

InterPro
IPR001411
Family

Tetracycline resistance protein TetB
PR01036	$\"[23-47]T$ $\"[114-134]T$ $\"[144-168]T$	TCRTETB

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[20-501]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[24-462]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[2-211]T$ $\"[291-497]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57	$\"[2-211]T$ $\"[291-497]T$	DRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[21-43]?$ $\"[49-71]?$ $\"[81-101]?$ $\"[107-129]?$ $\"[144-164]?$ $\"[174-194]?$ $\"[240-258]?$ $\"[264-284]?$ $\"[299-321]?$ $\"[340-362]?$ $\"[371-393]?$ $\"[399-419]?$ $\"[448-468]?$ $\"[474-494]?$	transmembrane_regions

","BeTs to 23 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","Residues 18-188 are 47% similar to a () protein domain (PDA0D7S0) which is seen in Q72KK9_THET2.Residues 55-191 are 55% similar to a (TRANSLOCASE MEMBRANE ANTIPORTER INTEGRAL ANTIBIOTIC TRANSPORTER) protein domain (PD653719) which is seen in Q8KHB7_NOCAE.","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 462 (E_value = 3.5e-44) place ANA_0424 in the MFS_1 family which is described as Major Facilitator Superfamily.","","efflux protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0425","442136","443761","1626","5.74","-13.82","57516","GTGACCCATCACCACTCCAACACCCCCTCCACCCCCGAGGAGGCAGCAGACCTCCGCGACGACCGCGACGCCCATGAGGGCCGTGACGTTCACGACGTCCATGACGTTGTGGCCCGGGTCCTGTCCCGGACCGGAACCGCCCTGGCCTCCACCGCCGCCCAGCACGAGCGTGCCGGTGGGTACGCGGACGGCCTCGACGACGGCGCCCTGGAGCGGGAGGCCCGCGCCGCCCGCCGCCGCGTGGCCGGGCTGTCCACCGAACTGGAGGACGTCAGCGAGGTCGAGTACCGCCAGGTCCGTCTGGAGAAGGTGGTCCTGGTCGGCCTGGAGCTGCCCCGGTCGCCCGCCCCCTCGCGCGGCGCACCGGGTGCCAGCGGCCCGCAGGTGCATGACTCCCAGGACGCCGGAACCTCTCTGCGCGAGCTGGCCGCTCTGGCCGAGACTGCCGGCAGCGAGGTCCTCGACGCCCTCATCCAGAGGCGCGACCACCCCGATCCCGCCACCTACCTGGGCAGCGGCAAGGCTCACGAGCTGGCCGACGTCGTGGCCGCCGCCGGAGCCGACACGGTCATCGTCGACGGCGAGCTCGCCCCCTCCCAGCGCCGCGCCCTGGAGGACGTCGTCGGCGTCAAGGTCGTCGACCGCACCGCCCTCATCCTGGACATCTTCGCCCAGCACGCCAAGTCCCGTGAGGGCAAGGCCCAGGTCGAGCTCGCCCAGCTCGAGTACCTCCTGCCGCGCCTGCGCGGATGGGGCGAGTCCATGTCCCGACAGGCCGGAGGCCGCGTGGCCGCCGGTCAGGGCATCGGCTCACGCGGCCCCGGAGAGACCAAGATCGAGCTCGACCGGCGCCGCATCCGCCAGCGTATGGCCCGCCTGCGCCGCGAGATCCAGGCCATGGCGCCCTCACGCGAGACCAAACGGGGCTCGCGCCGACGCGGGGCCATCCCCTCGGTGGCGATCGCCGGTTACACCAACGCCGGCAAGTCCTCCCTCATGAACCGCCTCACCGAGGCCGGCATCATGGTTGAGGACGCCCTGTTCGCCACCCTCGACCCCACCGTCCGGCGGGCCGAGACCTCCGAAGGACGCACCTACACCCTCACTGACACCGTCGGTTTCGTGCGCAACCTGCCCCACGAGCTCATTGAGGCCTTCCGCTCCACCCTGGAGGAGGTGGCCGGGGCCGACCTCGTGCTGCACGTCGTCGATGCTGCCCACCCCGATCCCCTCAGCCAGGTGGCGGCCGTGCGCACCGTCCTGTCCGAGATCCCCGGCGCCCTGGACGTGCCCGAGCTCATCGTCCTGAACAAGACCGACCTCGCCGATGCCGTCACCCTGGCTGCGCTGCGCACCGGCCTGCCCGGGGCGGTCGCGGTCTCGGCCCGCACCGGGGAGGGGATCGAGGAGCTGCGCGCCCGCATCGAGCAGATGCTGCCCCACCCGCAGGTGAGCATCGACGTCGTGGTGCCCTACTCCCGTGGGGATCTCGTCTCCCGGGTCCACGCCGAGGGGGAGATCGACACGGTCGACTACATCGAGGCGGGCACTCACGTCGTCGCGCGCGTCGGTGCCGCCCTGGCGGCCGAGATCGAGGGCGCCGCCGCAGGCGTCACGGTCGGCTGA","VTHHHSNTPSTPEEAADLRDDRDAHEGRDVHDVHDVVARVLSRTGTALASTAAQHERAGGYADGLDDGALEREARAARRRVAGLSTELEDVSEVEYRQVRLEKVVLVGLELPRSPAPSRGAPGASGPQVHDSQDAGTSLRELAALAETAGSEVLDALIQRRDHPDPATYLGSGKAHELADVVAAAGADTVIVDGELAPSQRRALEDVVGVKVVDRTALILDIFAQHAKSREGKAQVELAQLEYLLPRLRGWGESMSRQAGGRVAAGQGIGSRGPGETKIELDRRRIRQRMARLRREIQAMAPSRETKRGSRRRGAIPSVAIAGYTNAGKSSLMNRLTEAGIMVEDALFATLDPTVRRAETSEGRTYTLTDTVGFVRNLPHELIEAFRSTLEEVAGADLVLHVVDAAHPDPLSQVAAVRTVLSEIPGALDVPELIVLNKTDLADAVTLAALRTGLPGAVAVSARTGEGIEELRARIEQMLPHPQVSIDVVVPYSRGDLVSRVHAEGEIDTVDYIEAGTHVVARVGAALAAEIEGAAAGVTVG$","GTP-binding protein","Cytoplasm","GTP-binding protein","K03665 GTP-binding protein HflX","GTP-binding protein, HSR1-related","","Vernet C., Ribouchon M.T., Chimini G., Pontarotti P. Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm. Genome 1994. 5(2):100-105. PMID: 8180467","","","

InterPro
IPR002917
Domain

GTP-binding protein, HSR1-related
PF01926	$\"[317-440]T$	MMR_HSR1

InterPro
IPR006073
Domain

GTP1/OBG
PR00326	$\"[319-339]T$ $\"[386-404]T$	GTP1OBG

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[316-481]T$	no description
PTHR10229	$\"[177-535]T$	GTP-BINDING PROTEIN HFLX

","BeTs to 16 clades of COG2262COG name: GTPasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2262 is -om-kz-qvdrlbcefghsn-j-i--Number of proteins in this genome belonging to this COG is 2","***** IPB006073 (GTP1/OBG GTP-binding protein family signature) with a combined E-value of 1.7e-23. IPB006073A 319-339 IPB006073B 340-358 IPB006073C 368-383 IPB006073D 386-404***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 2.4e-10. IPB002917 321-353","Residues 139-178 are 90% similar to a (GTP-BINDING HFLX PROTEASE GTPASE FOR LAMBDA REPRESSOR CII SUBUNIT PHAGE) protein domain (PD686546) which is seen in Q73W22_MYCPA.Residues 195-256 are similar to a (GTP-BINDING HFLX PROTEASE GTP BINDING GTPASE PROTEIN FOR LAMBDA REPRESSOR) protein domain (PD006242) which is seen in Q6AE07_BBBBB.Residues 321-353 are 96% similar to a (GTP-BINDING TRNA ENGA REPEAT GTPASE RNA-BINDING MODIFICATION TRME PROBABLE ERA) protein domain (PD000414) which is seen in Q82KD3_STRAW.Residues 356-404 are similar to a (GTP-BINDING HFLX PROTEASE GTP BINDING GTPASE PROTEIN FOR LAMBDA REPRESSOR) protein domain (PD009339) which is seen in Q6A8Z3_PROAC.Residues 406-473 are 67% similar to a (GTP-BINDING HFLX GTPASE ATP/GTP-BINDING GTP HFLX BINDING HYDROLASE POSSIBLE FAMILY) protein domain (PD759379) which is seen in Q6AE07_BBBBB.Residues 479-523 are 68% similar to a (GTP-BINDING HFLX GTPASE ATP/GTP-BINDING PROBABLE 3.1.5.- HYDROLASE BINDING GTP GTPASE) protein domain (PD020995) which is seen in Q6A8Z3_PROAC.","","-44% similar to PDB:1UDX Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8 (E_value = 9.0E_10);","Residues 317 to 440 (E_value = 1.7e-37) place ANA_0425 in the MMR_HSR1 family which is described as GTPase of unknown function.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0426","443866","445830","1965","5.79","-10.21","68545","ATGGGCGGCAGCCCCCGCCAGGGGCAGACCACCATGGCCCGGGAGGTCGCCCAGACCCTGGCCGACGGCACCCACCTTCTGGTGCAGGCCGGCACCGGGACAGGAAAGTCACTGGGCTACCTGGTCCCCGCCATGGTCCACGCCGTACAGGCCGGTGCCCGGGTCGTGGTCTCCACCGCCACCCTGGCCCTGCAACGGCAGATCCTCACCAAGGACGCGCCTCTGGCCGCCGATGCCGTCGAGCAGGTCACCGGCACCCGCCCCGAAGTGGCCCTGCTCAAGGGCTGGCAGAACTACCTGTGCCGCCACCGCCTGGACGGTGGCTACCCGCCGGAGGAGGACGAGGCCGCGCTCTTCGGCGTCGGGGACGCCATCGCCCAGCCGGCCGCCGGGCACGGGAGCGACGCGAGCCTGGGCGAGCAGGTGGTCCGCCTGCGCGAGTGGGCGGCCAGGACGGATACCGGTGACCGCGACGACCTTGTCCCCGGCGTCTCCCAGCGCGCCTGGGCCCAGGTCTCCGTCTCCCGGGCCGAGTGCCTGGGGCAGTCCTGCCCCCTGAAGTCCGAGTGCTTCCCCGAGTTGGCGCGCGCCGCCGCCTCCCGGGCCGATCTCGTGGTGACCAACCACGCCATGCTCGGCGTGGTCGTGGCCGGCAACCCCGGGGTCCTGCCCGACCACCAGGTCCTCATCGTCGACGAGGCCCACGAGCTGGCCGACCGCATCCGCTCCCAGGGCACCATCGCCCTGTCGGCGGCCGCCGTGGCGCGCACCGCCGCCACCGCCCGCAAGCACGCCTCCGTGCTGGTCAGCGAGCTGGAGTCCGCGGGCCAGACCCTCCAGCTCGCGCTGGCCGAGCTGCCCGACGGCCGCCTGGAGGCGCCCCTGCCCACCGTCCTGCACGATGCGCTCGTGCTCCTGGACGGCGCCGCCCGCCAGGTCGCCTCCGACGTGCGCGACCAGGCCCGCGCCCTGGGGCGCGACCGTTCCAGCGAGGCTGCCGGGGGCCTGGCGGTCGCCCGCACCGCTGTCGCGGACCTGGTCGACGCCCTGGACCGCATGACCTCGGACTCGGTGGCCCAGGGACGCGACGTGGCCTGGATCGAGCGTCCCCGCATGGGCGCCGAACCCCCACGCCTCCTCCTGGCCCCCATCGAGGTCGCCGGATCGGTGGCCGGCCACCTGCTCAACGGCCGCGCCAGCGTCATGACGTCGGCGACCCTCGCCCTGGGGGACAGCTTCGACCCCATGGCCCGCTCCCTGGGACTGACCCTGGCCGAGCAGCCCTGGAGAGGTCTCGACGTCGGCTCCCCCTTCGACTACCCCCGTCAGGGCATCCTCTATGTGGCTGCCCACCTGCCTCGCCCCGGCGCCGGCATCTCCGAGGCTGCCCTGGATGAGATGCTCGCCCTGGTCGAGGCCTCCGAAGGCGGCATGCTGGGCCTGTTCTCCTCCCGGCGCGCCGCCCAGGAGGCCGCCGAGGTGCTGCGCGGAGCCACCGACCTGCCCGTCTACGCCCAGGGCGACGACCAGCTGCCCACCCTGGTGCGGGCCTTCGCCGAGGACGAGGCGGCCTGCCTGGTGGGCACCCTCTCGCTGTGGCAGGGCGTGGACGTGCCCGGGCGCACCTGCCGCCTCGTCGTCATCGACCGCATCCCCTTCCCCCGGCCCGACGACCCGGTCGCCCAGGCCCGCACCGACGCCGTCGTGGCCGCCGGCGGCAATGGCTTCATGAGCGTATCGGCCACCCACGCGGCCCTGCTCCTGGCCCAGGGGGCGGGGCGCCTCATCCGCCGCAGCCAGGACCGCGGCGTCGTCGCCGTCCTGGACTCGCGTCTGCGCACGGCGCGCTACGGGGGCTTCCTCACCCGCTCCATGCCCGCCCTGTGGCCGACGACGAAGCCCGACGTGGTCCGTGCCGCCCTGAGGCGCCTGGCTTTGCGGACTGATGCCCCGGCGGAGGAGTGA","MGGSPRQGQTTMAREVAQTLADGTHLLVQAGTGTGKSLGYLVPAMVHAVQAGARVVVSTATLALQRQILTKDAPLAADAVEQVTGTRPEVALLKGWQNYLCRHRLDGGYPPEEDEAALFGVGDAIAQPAAGHGSDASLGEQVVRLREWAARTDTGDRDDLVPGVSQRAWAQVSVSRAECLGQSCPLKSECFPELARAAASRADLVVTNHAMLGVVVAGNPGVLPDHQVLIVDEAHELADRIRSQGTIALSAAAVARTAATARKHASVLVSELESAGQTLQLALAELPDGRLEAPLPTVLHDALVLLDGAARQVASDVRDQARALGRDRSSEAAGGLAVARTAVADLVDALDRMTSDSVAQGRDVAWIERPRMGAEPPRLLLAPIEVAGSVAGHLLNGRASVMTSATLALGDSFDPMARSLGLTLAEQPWRGLDVGSPFDYPRQGILYVAAHLPRPGAGISEAALDEMLALVEASEGGMLGLFSSRRAAQEAAEVLRGATDLPVYAQGDDQLPTLVRAFAEDEAACLVGTLSLWQGVDVPGRTCRLVVIDRIPFPRPDDPVAQARTDAVVAAGGNGFMSVSATHAALLLAQGAGRLIRRSQDRGVVAVLDSRLRTARYGGFLTRSMPALWPTTKPDVVRAALRRLALRTDAPAEE$","Rad3-related DNA helicase","Cytoplasm, Membrane","ATP-dependent helicase","helicase C2","DEAD/DEAH box helicase domain protein","","Gorbalenya A.E., Koonin E.V., Donchenko A.P., Blinov V.M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989. 17(12):4713-4730. PMID: 2546125","","","

InterPro
IPR006555
Domain

Helicase c2
SM00491	$\"[485-614]T$	HELICc2

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[6-261]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[1-301]T$	DEXDc

InterPro
IPR014013
Domain

Helicase superfamily 1 and 2 ATP-binding, DinG/Rad3-type
PS51193	$\"[1-295]T$	HELICASE_ATP_BIND_2

","BeTs to 12 clades of COG1199COG name: Rad3-related DNA helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1199 is -ompkzyq--rlb-efghsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB006555 (Helicase c2) with a combined E-value of 3.9e-36. IPB006555A 28-39 IPB006555B 228-241 IPB006555C 525-553 IPB006555D 590-611***** IPB010614 (DEAD_2) with a combined E-value of 3.2e-21. IPB010614A 8-48 IPB010614E 228-245 IPB010614I 576-626","Residues 12-50 are 79% similar to a (HELICASE ATP-DEPENDENT DING PROBABLE DNA FAMILY HYDROLASE HELICASE ATP-BINDING ENZYME) protein domain (PD462537) which is seen in Q73X78_MYCPA.Residues 57-172 are 62% similar to a (HELICASE ATP-DEPENDENT DNA DING PROBABLE FAMILY HELICASE HYDROLASE ENZYME DNA-BINDING) protein domain (PD329182) which is seen in Q73X78_MYCPA.Residues 179-230 are 67% similar to a (HELICASE ATP-DEPENDENT DING DNA PROBABLE FAMILY HELICASE ENZYME HYDROLASE DNA-BINDING) protein domain (PD567182) which is seen in Q8FMT4_COREF.Residues 379-521 are 63% similar to a (HELICASE ATP-DEPENDENT DNA DING PROBABLE FAMILY HELICASE HYDROLASE REPAIR ATP-BINDING) protein domain (PD403018) which is seen in DING_MYCTU.Residues 532-607 are 89% similar to a (HELICASE ATP-DEPENDENT DNA DING PROBABLE FAMILY HELICASE HYDROLASE REPAIR ATP-BINDING) protein domain (PD004168) which is seen in Q6A8Z2_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 261 (E_value = 2.2e-07) place ANA_0426 in the DEAD family which is described as DEAD/DEAH box helicase.","","helicase (dinG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0427","445949","446950","1002","5.43","-7.69","35209","GTGTCAGACCACATCACCACTACCGCTGAAGGCTCCTACCCCACCAACCGTTCCGGCCGCCCCTCCAAAGTCGCTGTCATCGGTGCCGGGGCCGTCGGCTCCACCCTCGCCTACGCCTGCGTGACCAAGGGTGTTGCCCGCGAGGTCGTGCTGCAGGACATCGTCAAGGAGAAGGTCGAGGCCGAGGCCCTCGACATCGCCCAGGGAATCCAGTTCACCTCCGCCGGCTCCGTCTCCGGCTCCGACGACCCCGAGATCTGCCGCGACGCGGACGTCATCGCCATCACCGCCGGCGCCAAGCAGAAGCCCGGCCAGTCCCGCCTCGAGCTGGCCGGCGCCACCGTCGGCATCATGGAGAAGATCCTCCCCAAGCTGGTCGAGGTCGCTCCCAACGCCATCTTCGTCCTCGTGGCCAACCCGGTGGACGTGGTGACCTACTGCGCTAAGAAGATCACCGGTCTGCCCGAGAACCAGGTCTTCGGCTCCGGCACGGTGCTGGACACCGCCCGGATGCGGTACCTCATCTCCCTGGAGACCGGCACGGCCGTCCAGAACATCCACGGCTACATCGCCGGTGAGCACGGCGACTCCGAGGTGCCCCTGTGGTCCTCCACCGAGATCGGCGGTGTGCCGATCACCCAGTGGGGCACCACCCTCGACGGCGGCGTGTTCGACGAGTCCAAGCGTGAGCGCATCGCCCACGACGTGGTCCGCTCCGCCTACCGCATCATCGAGGGCAAGGGCGCCACCAACTACGCCGTCGGCCTGGCCGTGCAGCGCATCATCGGCGCCGTCCTCAACGACGAGCAGCGGGTGCTCACCATCTCCCCGCTGCTGGACAACTGGCACGGCATCTCCGACGTGTGCATGGCCGTCCCCACGATCGTGGGACGTGAGGGCGCCGGGCGCCGCCTCGAGCTGCCCCTGACCCCCGAGGAGAAGGAGCGCCTGACCGCCTCCGCCGACCACCTGCGCGAGGTCGCACGCGGCCTGGGCTACTGA","VSDHITTTAEGSYPTNRSGRPSKVAVIGAGAVGSTLAYACVTKGVAREVVLQDIVKEKVEAEALDIAQGIQFTSAGSVSGSDDPEICRDADVIAITAGAKQKPGQSRLELAGATVGIMEKILPKLVEVAPNAIFVLVANPVDVVTYCAKKITGLPENQVFGSGTVLDTARMRYLISLETGTAVQNIHGYIAGEHGDSEVPLWSSTEIGGVPITQWGTTLDGGVFDESKRERIAHDVVRSAYRIIEGKGATNYAVGLAVQRIIGAVLNDEQRVLTISPLLDNWHGISDVCMAVPTIVGREGAGRRLELPLTPEEKERLTASADHLREVARGLGY$","L-lactate dehydrogenase","Cytoplasm","L-lactate dehydrogenase","L-lactate dehydrogenase ","L-lactate dehydrogenase","","Hannenhalli S.S., Russell R.B. Analysis and prediction of functional sub-types from protein sequence alignments. J. Mol. Biol. 2000. 303(1):61-76. PMID: 11021970","","","

InterPro
IPR001236
Family

Lactate/malate dehydrogenase
G3DSA:3.90.110.10	$\"[164-333]T$	no description
PF00056	$\"[22-162]T$	Ldh_1_N
PF02866	$\"[164-330]T$	Ldh_1_C

InterPro
IPR001557
Family

L-lactate/malate dehydrogenase
PR00086	$\"[23-47]T$ $\"[48-72]T$ $\"[135-155]T$ $\"[159-177]T$ $\"[189-202]T$	LLDHDRGNASE
PIRSF000102	$\"[23-333]T$	L-lactate/malate dehydrogenase

InterPro
IPR011304
Family

L-lactate dehydrogenase
TIGR01771	$\"[26-326]T$	L-LDH-NAD: L-lactate dehydrogenase
PS00064	$\"[191-197]?$	L_LDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[1-163]T$	no description
PTHR11540	$\"[20-333]T$	MALATE AND LACTATE DEHYDROGENASE
PTHR11540:SF3	$\"[20-333]T$	L-LACTATE DEHYDROGENASE

","BeTs to 20 clades of COG0039COG name: Malate/lactate dehydrogenasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0039 is aomp-zyqvdrlbce-ghs-ujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB011304 (L-lactate dehydrogenase) with a combined E-value of 1.9e-97. IPB011304A 32-72 IPB011304B 117-170 IPB011304C 171-209 IPB011304D 236-268 IPB011304E 287-324***** IPB001557 (L-lactate dehydrogenase) with a combined E-value of 2.7e-85. IPB001557A 22-62 IPB001557B 77-128 IPB001557C 139-193 IPB001557D 225-274 IPB001557E 286-331***** IPB000594 (UBA/THIF-type NAD/FAD binding fold) with a combined E-value of 4.6e-06. IPB000594 23-45","Residues 20-100 are similar to a (OXIDOREDUCTASE DEHYDROGENASE NAD GLYCOLYSIS L-LACTATE MALATE CYCLE TRICARBOXYLIC ACID L-LDH) protein domain (PD486729) which is seen in LDH2_BIFLO.Residues 101-202 are similar to a (OXIDOREDUCTASE DEHYDROGENASE NAD MALATE CYCLE TRICARBOXYLIC ACID GLYCOLYSIS L-LACTATE L-LDH) protein domain (PD000350) which is seen in LDH2_BIFLO.Residues 236-300 are 80% similar to a (OXIDOREDUCTASE DEHYDROGENASE NAD GLYCOLYSIS L-LACTATE L-LDH FAMILY MULTIGENE CHAIN MALATE) protein domain (PD000436) which is seen in LDH2_BIFLO.","","-76% similar to PDB:1LLD MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE (E_value = 2.0E_104);-76% similar to PDB:1LTH T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL (E_value = 2.0E_104);-64% similar to PDB:1A5Z LACTATE DEHYDROGENASE FROM THERMOTOGA MARITIMA (TMLDH) (E_value = 2.6E_67);-64% similar to PDB:1LLC STRUCTURE DETERMINATION OF THE ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS CASEI AT 3.0 ANGSTROMS RESOLUTION (E_value = 1.9E_65);-65% similar to PDB:1Y6J L-Lactate Dehydrogenase from Clostridium Thermocellum Cth-1135 (E_value = 1.9E_65);","Residues 20 to 39 (E_value = 0.00043) place ANA_0427 in the ThiF family which is described as ThiF family.Residues 22 to 162 (E_value = 2.2e-55) place ANA_0427 in the Ldh_1_N family which is described as lactate/malate dehydrogenase, NAD binding domain.Residues 164 to 330 (E_value = 1.7e-33) place ANA_0427 in the Ldh_1_C family which is described as lactate/malate dehydrogenase, alpha/beta C-terminal domain.","","dehydrogenase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0428","447812","447024","789","5.15","-9.63","27376","ATGAGCACCACAGCACGCCAGGGCGACTCACCCAACCCGGCGCCGCATGCTGGAGCCGGCAGCTCTGAGCAGATCAGCGCAGCAGCGGTCACGGAGGTCATCAACGACCTCGACAAGCGCGCCCGCGCGGTCTATGAGGCCGTCCGCGCGGCCATCGCCACCCACGGCTACCCGCCCTCACTGCGTGAGATCGGCGAGCAGGTGGGCCTGACCAGCCCCTCCTCCGTCAAGCACCAGCTGGACAAGCTCGAGCGCCTGGGCCTGGTGCGCCGAGACCCGAATCGGCCTCGGGCGATGGAGGTCGTCTGCGCCGACAGCGCACCGAGCGGCCGCGCGGCCACCCCCGGCAGCGCTCACGTCTCCTCTCTTGACTCCCCCAGCGTCCCCGGCGTCGAGGACGGGGAGGCGGTCGCCGTTCCGCTGGTGGGACGCATCGCCGCCGGGGCCCCGATCCTGGCCGAGCAGGAGGTCACCGATGTCATGGCCCTGCCCCGCCGCCTGACCGGCGAGGGCGAGCTCTTCATGCTGGAGGTGCACGGGGACTCGATGATTGAGGCCGCCATCTGCGACGGCGACTGGGTGGTGGTGCGCTCCCAGCCCGACGCGGCCAACGGCGAGATCGTGGCGGCCATGATCGAGGACGTCGACGGTGCCTCGGCCACGGTCAAGGTGCTCTCGCGACGCGACGGCCACCAGTGGCTGCTTCCCCGCAACTCCAGCTACGCCCCGATCGACGGAGACCAGGCCACGATCATGGGCAAGGTGGTCACGGTGCTGCGCGCCCTGTAG","MSTTARQGDSPNPAPHAGAGSSEQISAAAVTEVINDLDKRARAVYEAVRAAIATHGYPPSLREIGEQVGLTSPSSVKHQLDKLERLGLVRRDPNRPRAMEVVCADSAPSGRAATPGSAHVSSLDSPSVPGVEDGEAVAVPLVGRIAAGAPILAEQEVTDVMALPRRLTGEGELFMLEVHGDSMIEAAICDGDWVVVRSQPDAANGEIVAAMIEDVDGASATVKVLSRRDGHQWLLPRNSSYAPIDGDQATIMGKVVTVLRAL$","LexA repressor","Cytoplasm","LexA repressor","SOS-response transcriptional repressor; LexA ","LexA repressor","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Paetzel M., Dalbey R.E., Strynadka N.C. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature 1998. 396(6707):186-190. PMID: 9823901Bell C.E., Frescura P., Hochschild A., Lewis M. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. Cell 2000. 101(7):801-811. PMID: 10892750Luo Y., Pfuetzner R.A., Mosimann S., Paetzel M., Frey E.A., Cherney M., Kim B., Little J.W., Strynadka N.C. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell 2001. 106(5):585-594. PMID: 11551506Peat T.S., Frank E.G., Mcdonald J.P., Levine A.S., Woodgate R., Hendrickson W.A. The UmuD' protein filament and its potential role in damage induced mutagenesis. Structure 1996. 4(12):1401-1412. PMID: 8994967Mustard J.A., Little J.W. Analysis of Escherichia coli RecA interactions with LexA, lambda CI, and UmuD by site-directed mutagenesis of recA. J. Bacteriol. 2000. 182(6):1659-1670. PMID: 10692372Ferentz A.E., Walker G.C., Wagner G. Converting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C). EMBO J. 2001. 20(15):4287-4298. PMID: 11483531Mcdonald J.P., Peat T.S., Levine A.S., Woodgate R. Intermolecular cleavage by UmuD-like enzymes: identification of residues required for cleavage and substrate specificity. J. Mol. Biol. 1999. 285(5):2199-2209. PMID: 9925794Goldsmith M., Sarov-blat L., Livneh Z. Plasmid-encoded MucB protein is a DNA polymerase (pol RI) specialized for lesion bypass in the presence of MucA', RecA, and SSB. Proc. Natl. Acad. Sci. U.S.A. 2000. 97(21):11227-11231. PMID: 11016960Sutton M.D., Kim M., Walker G.C. Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage. J. Bacteriol. 2001. 183(1):347-357. PMID: 11114935","","","

InterPro
IPR006197
Family

Peptidase S24, LexA/MucA/RumA/RuvA
PR00726	$\"[174-184]T$ $\"[185-196]T$ $\"[217-229]T$	LEXASERPTASE

InterPro
IPR006198
Domain

Peptidase S24, S26A and S26B
PF00717	$\"[177-249]T$	Peptidase_S24

InterPro
IPR006199
Domain

LexA DNA-binding region
PF01726	$\"[34-98]T$	LexA_DNA_bind

InterPro
IPR006200
Family

Peptidase S24, LexA repressor
TIGR00498	$\"[34-262]T$	lexA: LexA repressor

InterPro
IPR011056
Domain

Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10	$\"[143-260]T$	no description

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[34-103]T$	no description

","BeTs to 10 clades of COG1974COG name: SOS-response transcriptional repressors (RecA-mediated autopeptidases)Functional Class: K [Information storage and processing--Transcription] Functional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1974 is --------vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 1","***** IPB006199 (LexA DNA-binding region) with a combined E-value of 2.4e-60. IPB006199A 37-87 IPB006199B 139-153 IPB006199C 174-220 IPB006199D 251-260***** IPB006197 (Repressor LexA serine protease (S24) family signature) with a combined E-value of 6.2e-12. IPB006197A 174-184 IPB006197B 185-196","Residues 56-262 are 44% similar to a (HYDROLASE REPRESSOR LEXA) protein domain (PDA1B7D2) which is seen in Q6A8Z1_PROAC.Residues 144-260 are 77% similar to a (REPRESSOR DNA HYDROLASE SOS LEXA AUTOCATALYTIC TRANSCRIPTION CLEAVAGE DNA-BINDING REGULATION) protein domain (PD001529) which is seen in LEXA_BIFLO.","","-45% similar to PDB:1JHH LEXA S119A MUTANT (E_value = 8.8E_17);-44% similar to PDB:1JHF LEXA G85D MUTANT (E_value = 2.6E_16);-51% similar to PDB:1JHC LEXA S119A C-TERMINAL TRYPTIC FRAGMENT (E_value = 4.1E_14);-49% similar to PDB:1JHE LEXA L89P Q92W E152A K156A MUTANT (E_value = 2.9E_12);","Residues 34 to 98 (E_value = 3.6e-22) place ANA_0428 in the LexA_DNA_bind family which is described as LexA DNA binding domain.Residues 177 to 249 (E_value = 2.8e-17) place ANA_0428 in the Peptidase_S24 family which is described as Peptidase S24-like.","","repressor (lexA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0428.1","447874","448776","903","11.62","18.11","31553","ATGTCGGTGGTCCGTGATCATCTTGGACATGACCAGCCTACCGGCGAGACGACCACGATTCAAACACATGTTCGAAGACGTGCTGGACGTGTCGCCCATCAGGCGCTAGTGTATCGAACAAGCGTTCGTCGAACATGTGTTCAGGAGGTTGCTGTGAGTGCCATCGCCATCCCGCTCCCGTCCCGCCAGAATTCTCGGGGGCGGACTGATGAGCCTGTCGCTGGGTCGGCCAGCGATCGGGGTGCCAGGCAGTCCTCCCGTCGGCCCAGGCTGAGGCTCGTCACTGACGACTTCGTCCCCGAGGTTCCTGTGCGGCGAAGCCTCGAGGGCGCGCGGCGTCCCGTGCCTGCATCCGCAGGCGTTGCGACACTGCCTGTGGTGTCGGAAATGCGTCGCCCTGTGGCGCCCGTGGCACTGCGGGGTGGTCGCACGGATCTGGAGCGCCTGGCTCCTCAGCACCCGGCAGTGCGGGCTGCCGGGCTGCGACGTGCTGCCCAGCAGGAGGGGATCCGGCGAGGCGGCGCCACTCAGAGTGTGGGCAAGAGAGAGCCCGTCGTGTCCCGCCCGCGGGAGGTGGCGGAGGTGGCGGTGCGCTCCAGGGCGGGGCTTCGGCTTCTTCGTGGCGGGCTCGCGGTCATCGTCGCGGCCTTCGTGCTTGCCTGTGGCGGACTGGTCGTCGGGGCTCTGGCGGGCCTGGTCTCTGCGGCCCCCGCCACGGCGGTTGCGCAGGTGTCGGCTGACACCACCACCACCGTTGTTCGTCCTGGTCAGTCCCTGTGGGACATCGCCGAGGCGAGCGGGACCTCGGACGTTCCGGGGATGGTGGCCCGGATCGCCGAGCTCAATGACCTCCAGGGAACCACCATCCGTGCCGGACAGACGCTTGAGATTCCTACGGCGTGA","MSVVRDHLGHDQPTGETTTIQTHVRRRAGRVAHQALVYRTSVRRTCVQEVAVSAIAIPLPSRQNSRGRTDEPVAGSASDRGARQSSRRPRLRLVTDDFVPEVPVRRSLEGARRPVPASAGVATLPVVSEMRRPVAPVALRGGRTDLERLAPQHPAVRAAGLRRAAQQEGIRRGGATQSVGKREPVVSRPREVAEVAVRSRAGLRLLRGGLAVIVAAFVLACGGLVVGALAGLVSAAPATAVAQVSADTTTTVVRPGQSLWDIAEASGTSDVPGMVARIAELNDLQGTTIRAGQTLEIPTA$","LysM domain containing protein","Membrane, Cytoplasm, Extracellular","","","","","Bateman A, Bycroft M.The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD).J Mol Biol. 2000 Jun;299(4):1113-9.PMID: 10843862","","","

InterPro
IPR002482
Domain

Peptidoglycan-binding LysM
PF01476	$\"[251-298]T$	LysM
SM00257	$\"[250-298]T$	LysM

noIPR
unintegrated

unintegrated
tmhmm	$\"[213-233]?$	transmembrane_regions

","BeTs to 4 clades of COG1388COG name: Predicted lytic murein transglycosylaseFunctional Class: NThe phylogenetic pattern of COG1388 is -----q--eB-h----o-IN-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","Residues 251 to 298 (E_value = 4.6e-08) place ANA_0428.1 in the LysM family which is described as LysM domain.","","","","1","","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:55 2007","Fri Aug 10 10:54:55 2007","Fri Aug 10 10:54:55 2007","Fri Aug 10 10:54:23 2007","","Mon Aug 20 18:01:25 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Mon Aug 20 18:01:25 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Fri Aug 10 10:54:23 2007","Mon Aug 20 18:01:25 2007","","Fri Aug 10 10:54:23 2007","","Fri Aug 10 10:54:23 2007","yes","","" "ANA_0429","448884","449339","456","7.32","0.74","16704","GTGCACTGCCCCTTCTGCCGTCATGACGGCTCACGCGTTGTCGACTCCCGGACCGCTGAGGACGGCACCTCCATCCGTCGTCGCCGTGAGTGTCAGCAGTGCGGGCGCCGATTCACCACTCTGGAGACCGCCAGCCTGTCGGTCCGCAAGCGCTCCGGCGTCGTCGAGCCCTTCAGTCGGGACAAGGTGGTGGTCGGAGTCAGGCGCGCCTGTCAGGGGCGTCCCGTCTCCGATGATCAGCTCGCGCTTCTGGCGCACCAGGTTGAGGAGGCCATTCGCGCGGGAGGTCAGGCGCTCGTCGACTCCCACGACGTCGGACTGGCGATCCTGGGCCCCTTGCGTGAGCTGGATCAGATCGCCTACCTGCGCTTCGCCTCGGTCTACTCCTCCTTCGACTCCCTGGAGGACTTCGATAAGGCCATCGCCGAACTGCGCAGTACTGAGGCGACCTGCTGA","VHCPFCRHDGSRVVDSRTAEDGTSIRRRRECQQCGRRFTTLETASLSVRKRSGVVEPFSRDKVVVGVRRACQGRPVSDDQLALLAHQVEEAIRAGGQALVDSHDVGLAILGPLRELDQIAYLRFASVYSSFDSLEDFDKAIAELRSTEATC$","Transcriptional regulator, NrdR family","Cytoplasm","transcriptional regulator, NrdR family","K07738 ATP-cone domain protein","ATP-cone domain protein","","Reichard P. From RNA to DNA, why so many ribonucleotide reductases?. Science 1993. 260(5115):1773-1777. PMID: 8511586","","","

InterPro
IPR003796
Family

Ribonucleotide reductase regulator NrdR-like
TIGR00244	$\"[1-144]T$	TIGR00244: transcriptional regulator, NrdR

InterPro
IPR005144
Domain

ATP-cone
PF03477	$\"[46-136]T$	ATP-cone
PS51161	$\"[46-136]T$	ATP_CONE

","BeTs to 12 clades of COG1327COG name: Predicted transcriptional regulator, consists of a Zn-ribbon and ATP-cone domainsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1327 is --------vdrlbcefghsn-j-i--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 13-148 are similar to a (UPF0168 CONE DOMAIN REGULATORY ATP YBAD TRANSCRIPTIONAL ORF RIBX ZN-RIBBON) protein domain (PD006144) which is seen in YO62_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 46 to 136 (E_value = 3.3e-26) place ANA_0429 in the ATP-cone family which is described as ATP cone domain.","","regulator, NrdR family (nrdR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0430","449423","450565","1143","7.70","2.60","41147","ATGCGCGTCCTCATCGTCTCCGACTGCTATTCGCCCAGGCTGGGCGGCATCGAGACTCAGGTGCGGGATCTCGCCCGCAACCTGAAGCTGGCCGGCCATGAGCCCGCCGTCGTCACCGCCACGCCGGTCGGTGACGGTCGTGGCCGTAGCGTCGAAAGGGCTGACGGCTTCCCTGTCTACCGCACCACCGCGCACCTGCCCAAGGAGCTGCCCGTTCACCCTCGAGCAGGCCGTGAGCTCGATGACCTCCTGTCCCGCCTGCGTCCCGACGTCGTTCACGCTCACGTCGGCGTCGTCTCACCCTTCGCCTGGTCCGGCATTGCTGCCGCCCGGCGAGCGCGGCTCCCGCTGGCCGTCACCTTCCACTGCGTCCTGGGACCCTGGGCGCGTGTGGCCGGAGCACTGGGGCCGGTCAGTCCTGTGCGGATGTGGCAGCGCGGCGGCGCCGACCTGACGGCCGTGTCCTCCATGCTCGCTGCCGACGTTCATCGTGCCGGGGCTGACGACCCTGTCACCGTTCTGCCCAACGGCATCACCGTTGAGAACTGGCGTCTGGAGCGCCCTGGTCCCCAGGAGCGACGGCCTCACCGGCCGGTCACGGTCGTGGCCTCCCTGCGATGGGTTGAGCGCAAGCGGCCCCTGCAGGTCGTGCGCGCCTTCGCTGAGGCCGTCAGGAGCGTTCCCGGCACCGATGCGCTCCTCAAGATCTATGGGGACGGTCCGCTGCGTGAGCGACTCACCCGGGAGGTTGCCGAGTCCGGCCTGGCCGACCGCATCGAGCTCGTGGGTCGTGTCGAACGCACTGAGCTCGCTCAGGCCTTCACGCACGCAGACATCTACCTGCAGACCTCGCCCGCCGAGTCCTTCGGTATCTCCACCCTGGAGGCCCGCAGCGCCGGGCTGGCCGTCGTCGCTCTGCGCTCCAGCGGAGTGCGCGACTTCATCACCGACGGTGTCGATGGCCTCCTCGCTGACGACGACGCCGGTCTGGGTCGCAAGCTCGCCACTCTCCTGGGGGACGACGAGCTCCTTGAGGGCATTAAGACCCACAACTATGAGAACGCCCCCTTGCCCGAGTGGGGCACTGTGGTGCAGATGCACGTCGATACCTACCGGCGTGCCATCGACCTGGCGGGTGCCTGA","MRVLIVSDCYSPRLGGIETQVRDLARNLKLAGHEPAVVTATPVGDGRGRSVERADGFPVYRTTAHLPKELPVHPRAGRELDDLLSRLRPDVVHAHVGVVSPFAWSGIAAARRARLPLAVTFHCVLGPWARVAGALGPVSPVRMWQRGGADLTAVSSMLAADVHRAGADDPVTVLPNGITVENWRLERPGPQERRPHRPVTVVASLRWVERKRPLQVVRAFAEAVRSVPGTDALLKIYGDGPLRERLTREVAESGLADRIELVGRVERTELAQAFTHADIYLQTSPAESFGISTLEARSAGLAVVALRSSGVRDFITDGVDGLLADDDAGLGRKLATLLGDDELLEGIKTHNYENAPLPEWGTVVQMHVDTYRRAIDLAGA$","N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein","Cytoplasm","N-acetylglucosaminyl-phosphatidylinositolbiosynthetic protein, putative","N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[185-354]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-345]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF44	$\"[2-345]T$	GLYCOSYLTRANSFERASE

InterPro
IPR005471
Domain

Transcriptional regulator IclR, N-terminal
PF09339	$\"[18-102]T$	HTH_IclR
SM00346	$\"[16-102]T$	HTH_ICLR
PS51077	$\"[16-75]T$	HTH_ICLR

InterPro
IPR014757
Domain

Transcriptional regulator IclR, C-terminal
PF01614	$\"[130-242]T$	IclR
PS51078	$\"[76-245]T$	ICLR_ED

noIPR
unintegrated

unintegrated
G3DSA:3.30.450.40	$\"[85-243]T$	no description

","BeTs to 10 clades of COG1414COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1414 is -o-----qvdr-b-efgh--uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 35-96 are 85% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR ICLR FAMILY REGULATORY PROBABLE REGULATOR) protein domain (PD287404) which is seen in Q82JR7_STRAW.Residues 97-237 are 46% similar to a (TRANSCRIPTIONAL TRANSCRIPTION REGULATORY DNA-BINDING REGULATION) protein domain (PD806167) which is seen in Q89SX5_BRAJA.Residues 97-200 are similar to a (TRANSCRIPTION DNA-BINDING REGULATOR REGULATION TRANSCRIPTIONAL ICLR REGULATORY FAMILY PROTEINS BACTERIAL) protein domain (PDA1F2S7) which is seen in Q82JR7_STRAW.Residues 97-235 are similar to a (TRANSCRIPTION REGULATION DNA-BINDING TRANSCRIPTIONAL REGULATOR ICLR FAMILY REGULATORY REPRESSOR REGULATOR) protein domain (PD282734) which is seen in Q8G4W3_BIFLO.Residues 206-243 are 84% similar to a (REGULATOR TRANSCRIPTIONAL DNA-BINDING TRANSCRIPTION REGULATION ICLR-FAMILY) protein domain (PD885053) which is seen in Q6A7Z8_PROAC.","","-46% similar to PDB:2G7U 2.3 A structure of putative catechol degradative operon regulator from Rhodococcus sp. RHA1 (E_value = 2.5E_13);-43% similar to PDB:2O0Y Crystal structure of putative transcriptional regulator RHA1_ro06953 (IclR-family) from Rhodococcus sp. (E_value = 3.2E_13);-40% similar to PDB:2IA2 The crystal structure of a putative transcriptional regulator RHA06195 from Rhodococcus sp. RHA1 (E_value = 4.4E_10);","Residues 18 to 102 (E_value = 1.4e-17) place ANA_0431 in the HTH_IclR family which is described as IclR helix-turn-helix domain.Residues 130 to 242 (E_value = 4e-25) place ANA_0431 in the IclR family which is described as Bacterial transcriptional regulator.","","transcriptional regulator (AP001514)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0432","451571","453064","1494","5.21","-17.25","52564","ATGGGAATGACTCTCGCCGAGAAGGTCTGGCGCGATCATGTGGTGTCCAAGGGTAGCGACGGCGCCCCCGACCTGCTGTACATCGACCTTCACCTGGTCCACGAGGTCACCAGCCCCCAGGCCTTCGAGGGGCTGCGTCTGGCCGGACGCCCGGTGCGTCGCCCCGACCTGACGATCGCCACCGAGGACCACAACACGCCCACTGTGGACATCGACCTGCCGATCGCCGATGTCACCAGCCGCGCTCAGATCGAGACCCTGCGTGCCAACTGCGCCGAGTTCGGGGTGCGGCTGCACTCCCTGGGCGACGCCGACCAGGGGATTGTCCACGCCGTCGGTCCGCAGCTGGGGCTGACCCAGCCCGGCATGACGGTGGTCTGCGGCGACTCCCACACCTCCACTCACGGCGCCTTCGGGGCCCTCGCCTTCGGTATTGGCACCTCCCAGGTCGAGCACGTCCTGGCCACCCAGACCCTGCCCATCGCCCCCTTCAAGACGATGAGCGTCACCATTGACGGGGACCTGCCCTCGGGCAGCGGGGCCAAGGACATCATCCTGGCCATCATCGCCAAGATCGGCACCAACGGGGCCCAGGGGCACGTCATCGAGTACCGTGGACGGGCCATCGAGCAGCTCTCGATGGAGGCCCGAATGACGATCTGCAATATGAGCATCGAGGGCGGGGCCCGGGCCGGCATGATCGCCCCGGACCAGACCACCTTCGACTACCTCAAGGGCCGTCCTCACGCCCCCGCCGGCGAGGACTGGGACGCCGCCGTGGAGTACTGGTCCAGCCTGCGCTCCGATCCCGACGCCGTCTTCGACACCGAGGTGGTGCTGCAGGCCGAGGACATCGAGCCCTTCGTCACCTGGGGCACCAATCCCGGGCAGGGCCTGCCGTTGTCCGCACGGGTCCCCGACCCCGAGGACATCGCCGACGCCACCGAGCGGCTGGCCGCCGAACGGGCCCTGGAGTACATGGACCTCGTACCGGGAACGCCCCTGCGCGACATCAAGGTCGACACCGTCTTCATCGGTTCGTGCACCAACGGCCGTATCGAGGACCTGCGGGCCGCCGCCGAGGTGGTGCGTGGGCGCAAGAAGGCTGAGGGGCTGCGCATGCTCGTGGTGCCGGCCTCGGCCCGAGTGCGTTTGCAGGCCGAGGCTGAGGGCCTGGACCGGGTCTTCACGAGCTTCGGTGCCGAGTGGCGCAACGCCGGCTGCTCCATGTGCCTGGCCATGAACCCCGACAAGCTCTCCTCCGGGGAGCGTGCGGCCTCCACCTCCAACCGCAACTTCGAGGGGCGTCAAGGAAAGGGCGGACGGACCCACCTCGTCTCGCCCGTCGTCGCCGCGGCCACCGCCGTGCGCGGGGCACTGTCGGCCCCGGGGGACCTGCCGCCGCGTCCGGAGGCCGCGCAGAACTCGGGTGATATCCCGACGGTCCCGGCGATTGCGCCGGTCTCCGCCGCGCCGGAGGCAACCGTCCAGTAG","MGMTLAEKVWRDHVVSKGSDGAPDLLYIDLHLVHEVTSPQAFEGLRLAGRPVRRPDLTIATEDHNTPTVDIDLPIADVTSRAQIETLRANCAEFGVRLHSLGDADQGIVHAVGPQLGLTQPGMTVVCGDSHTSTHGAFGALAFGIGTSQVEHVLATQTLPIAPFKTMSVTIDGDLPSGSGAKDIILAIIAKIGTNGAQGHVIEYRGRAIEQLSMEARMTICNMSIEGGARAGMIAPDQTTFDYLKGRPHAPAGEDWDAAVEYWSSLRSDPDAVFDTEVVLQAEDIEPFVTWGTNPGQGLPLSARVPDPEDIADATERLAAERALEYMDLVPGTPLRDIKVDTVFIGSCTNGRIEDLRAAAEVVRGRKKAEGLRMLVVPASARVRLQAEAEGLDRVFTSFGAEWRNAGCSMCLAMNPDKLSSGERAASTSNRNFEGRQGKGGRTHLVSPVVAAATAVRGALSAPGDLPPRPEAAQNSGDIPTVPAIAPVSAAPEATVQ$","3-isopropylmalate dehydratase large subunit","Cytoplasm","3-isopropylmalate dehydratase, large subunit","3-isopropylmalate dehydratase large subunit ","3-isopropylmalate dehydratase, large subunit","","Gruer M.J., Artymiuk P.J., Guest J.R. The aconitase family: three structural variations on a common theme. Trends Biochem. Sci. 1997. 22(1):3-6. PMID: 9020582","","","

InterPro
IPR001030
Domain

Aconitate hydratase, N-terminal
PD000511	$\"[107-463]T$	LEU2_MYCLE_O33123;
PR00415	$\"[83-96]T$ $\"[109-117]T$ $\"[120-133]T$ $\"[134-149]T$ $\"[196-209]T$ $\"[210-223]T$ $\"[287-301]T$ $\"[344-355]T$ $\"[400-413]T$	ACONITASE
PF00330	$\"[4-458]T$	Aconitase
PS00450	$\"[340-356]T$	ACONITASE_1
PS01244	$\"[400-413]T$	ACONITASE_2

InterPro
IPR004430
Domain

3-isopropylmalate dehydratase large subunit region
TIGR00170	$\"[1-466]T$	leuC: 3-isopropylmalate dehydratase, large

InterPro
IPR012095
Family

3-isopropylmalate dehydratase large subunit
PIRSF006442	$\"[3-468]T$	3-isopropylmalate dehydratase, large subunit

noIPR
unintegrated

unintegrated
G3DSA:3.30.499.10	$\"[3-166]T$ $\"[328-466]T$	no description
G3DSA:3.40.1060.10	$\"[167-282]T$	no description
PTHR11670	$\"[1-315]T$ $\"[340-460]T$	ACONITASE
PTHR11670:SF6	$\"[1-315]T$ $\"[340-460]T$	3-ISOPROPYLMALATE DEHYDRATASE

","BeTs to 18 clades of COG0065COG name: 3-isopropylmalate dehydratase large subunitFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0065 is aom-k-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001030 (Aconitate hydratase, N-terminal) with a combined E-value of 7.5e-97. IPB001030A 4-13 IPB001030B 117-151 IPB001030C 173-183 IPB001030D 196-245 IPB001030E 343-357 IPB001030F 380-433","Residues 1-46 are 91% similar to a (ISOMERASE 3-ISOPROPYLMALATE DEHYDRATASE LYASE SUBUNIT LARGE ALPHA-IPM IPMI 4FE-4S ISOPROPYLMALATE) protein domain (PD738556) which is seen in LEU2_BIFLO.Residues 4-98 are 56% similar to a (DEHYDRATASE LYASE SUBUNIT LARGE 3-ISOPROPYLMALATE) protein domain (PDA1A7J3) which is seen in Q7NW21_CHRVO.Residues 50-96 are 87% similar to a (ISOMERASE 3-ISOPROPYLMALATE DEHYDRATASE LYASE SUBUNIT LARGE IPMI ALPHA-IPM ISOPROPYLMALATE 4FE-4S) protein domain (PD581395) which is seen in Q73VI7_MYCPA.Residues 107-463 are similar to a (LYASE ISOMERASE ACONITATE 3-ISOPROPYLMALATE HYDRATASE IRON-SULFUR DEHYDRATASE 4FE-4S LARGE SUBUNIT) protein domain (PD000511) which is seen in LEU2_MYCLE.Residues 121-178 are 81% similar to a (ISOMERASE DEHYDRATASE LYASE SUBUNIT LARGE 3-ISOPROPYLMALATE BIOSYNTHESIS IRON-SULFUR IPMI ALPHA-IPM) protein domain (PD299828) which is seen in LEU2_CAUCR.Residues 124-302 are 44% similar to a (LYASE HYDRATASE ACONITATE) protein domain (PD690511) which is seen in Q8EQL5_OCEIH.Residues 124-307 are 44% similar to a (ACONITATE LYASE HYDRATASE) protein domain (PD995517) which is seen in Q6MIH9_BDEBA.Residues 193-341 are 68% similar to a (ISOMERASE IPMI DEHYDRATASE LYASE ALPHA-IPM ISOPROPYLMALATE SUBUNIT BIOSYNTHESIS LEUCINE LARGE) protein domain (PD582305) which is seen in LEU2_CAUCR.Residues 407-448 are 90% similar to a (ISOMERASE IPMI DEHYDRATASE LYASE ALPHA-IPM ISOPROPYLMALATE SUBUNIT BIOSYNTHESIS LEUCINE LARGE) protein domain (PD556812) which is seen in LEU2_AZOVI.","","-40% similar to PDB:1B0J CRYSTAL STRUCTURE OF ACONITASE WITH ISOCITRATE (E_value = 4.9E_23);-40% similar to PDB:1B0K S642A:FLUOROCITRATE COMPLEX OF ACONITASE (E_value = 4.9E_23);-40% similar to PDB:1B0M ACONITASE R644Q:FLUOROCITRATE COMPLEX (E_value = 4.9E_23);-40% similar to PDB:1C96 S642A:CITRATE COMPLEX OF ACONITASE (E_value = 4.9E_23);-40% similar to PDB:1C97 S642A:ISOCITRATE COMPLEX OF ACONITASE (E_value = 4.9E_23);","Residues 4 to 458 (E_value = 1.1e-229) place ANA_0432 in the Aconitase family which is described as Aconitase family (aconitate hydratase).","","dehydratase, large subunit (leuC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0433","453146","453799","654","5.51","-4.37","24080","GTGGACAAGTTCATCCGACACACCGGCATCGGCGCCCCGTTGCGGCGCAGCGCCGTCGACACCGACCAGATCATCCCGGCGGTGTATCTCAAGCGCATCACCCGCACGGGCTTCGACGACGCCCTGTTCGCCTCCTGGCGGGCCGGTGAGCCCGACTTCATTCTCAATCAGGAGGCCTACAAGCGGGCCTCGGTGCTCGTCGCCGGTCCCGACTTCGGCACGGGCTCCTCACGGGAGCATGCCGTGTGGGCGCTCAAGGACTACGGCTTCAAGGTCGTTCTGGCCCCCCGCTTCGCCGACATCTTCCGCGGCAACGCAGGCAAGCAGGGGCTGGTGGCCGGCGTGGTCTCCCAGGAGGACTGCGAGCAGCTGTGGAAGATCCTCGAGACCGAGCCGGGTACTGAGGTGACGGTGGACCTGGAGAACCGCACGGTCGAGGCCGGCTCCTTCCGCTGTGCCTTCTCCATCGACGACTACGTCCGCTGGATTCTCATGGAGGGGCTCGACGACATCTCCCTGACCCTCACCCAGGAGGACGCCATCCGCGCCTACGAGGAGGCTCGCCCGGCCTTCAAGCCGCGCACCCTGCCGGCCAAGCACCTGCCGGCCCAGGAGGTCGTCTCGGCCCGGGCCGCGGATATGCCTCGACCCTGA","VDKFIRHTGIGAPLRRSAVDTDQIIPAVYLKRITRTGFDDALFASWRAGEPDFILNQEAYKRASVLVAGPDFGTGSSREHAVWALKDYGFKVVLAPRFADIFRGNAGKQGLVAGVVSQEDCEQLWKILETEPGTEVTVDLENRTVEAGSFRCAFSIDDYVRWILMEGLDDISLTLTQEDAIRAYEEARPAFKPRTLPAKHLPAQEVVSARAADMPRP$","3-isopropylmalate dehydratase small subunit","Cytoplasm","3-isopropylmalate dehydratase, small subunit","3-isopropylmalate dehydratase small subunit ","3-isopropylmalate dehydratase, small subunit","","Lauble H., Stout C.D. Steric and conformational features of the aconitase mechanism. Proteins 1995. 22(1):1-11. PMID: 7675781Gruer M.J., Artymiuk P.J., Guest J.R. The aconitase family: three structural variations on a common theme. Trends Biochem. Sci. 1997. 22(1):3-6. PMID: 9020582Robbins A.H., Stout C.D. Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. Proc. Natl. Acad. Sci. U.S.A. 1989. 86(10):3639-3643. PMID: 2726740Lauble H., Kennedy M.C., Beinert H., Stout C.D. Crystal structures of aconitase with trans-aconitate and nitrocitrate bound. J. Mol. Biol. 1994. 237(4):437-451. PMID: 8151704Theil E.C. The IRE (iron regulatory element) family: structures which regulate mRNA translation or stability. Biofactors 1993. 4(2):87-93. PMID: 8347279","","","

InterPro
IPR000573
Domain

Aconitate hydratase, C-terminal
PF00694	$\"[1-119]T$	Aconitase_C

InterPro
IPR004431
Domain

3-isopropylmalate dehydratase small subunit region
TIGR00171	$\"[1-181]T$	leuD: 3-isopropylmalate dehydratase, small

InterPro
IPR012305
Family

3-isopropylmalate dehydratase small subunit
PIRSF001420	$\"[1-196]T$	3-isopropylmalate dehydratase, small subunit

noIPR
unintegrated

unintegrated
G3DSA:3.20.19.10	$\"[14-158]T$	no description
PTHR11670	$\"[35-195]T$	ACONITASE
PTHR11670:SF2	$\"[35-195]T$	3-ISOPROPYLMALATE DEHYDRATASE

","BeTs to 18 clades of COG0066COG name: 3-isopropylmalate dehydratase small subunitFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0066 is a-m-k-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000573 (Aconitate hydratase, C-terminal) with a combined E-value of 3.1e-30. IPB000573A 16-31 IPB000573B 65-105","Residues 28-57 are similar to a (ISOMERASE 3-ISOPROPYLMALATE DEHYDRATASE SUBUNIT SMALL LYASE IPMI ALPHA-IPM ISOPROPYLMALATE BIOSYNTHESIS) protein domain (PD018132) which is seen in Q8FPR2_COREF.Residues 58-91 are similar to a (LYASE ISOMERASE 3-ISOPROPYLMALATE SMALL SUBUNIT DEHYDRATASE ACONITATE HYDRATASE BIOSYNTHESIS IPMI) protein domain (PD001077) which is seen in Q6AFK6_BBBBB.Residues 65-146 are 57% similar to a (ACONITATE HYDRATASE LYASE ACONITASE ISOMERASE HYDRO-LYASE CITRATE B ACID 4FE-4S) protein domain (PD489052) which is seen in LEUD_AQUAE.Residues 92-199 are similar to a (DEHYDRATASE SMALL 3-ISOPROPYLMALATE SUBUNIT) protein domain (PD986445) which is seen in Q6AFK6_BBBBB.Residues 99-148 are similar to a (ISOMERASE 3-ISOPROPYLMALATE DEHYDRATASE SUBUNIT SMALL LYASE IPMI ALPHA-IPM ISOPROPYLMALATE BIOSYNTHESIS) protein domain (PD584304) which is seen in Q8FPR2_COREF.Residues 154-197 are similar to a (LEUD) protein domain (PD983697) which is seen in Q73VI8_MYCPA.Residues 154-195 are similar to a (DEHYDRATASE LYASE SUBUNIT SMALL 3-ISOPROPYLMALATE) protein domain (PDA1A334) which is seen in Q6NHK9_CORDI.","","-58% similar to PDB:2HCU Crystal Structure Of Smu.1381 (or LeuD) from Streptococcus Mutans (E_value = 6.4E_36);","Residues 1 to 119 (E_value = 3.6e-37) place ANA_0433 in the Aconitase_C family which is described as Aconitase C-terminal domain.","","dehydratase, small subunit (leuD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0434","454046","455368","1323","6.11","-9.08","47252","ATGGTCGACGGTCTGCTCCAGGTCGAGGGTGGTCGCCCGCTGACTGGTGAGATCACCGTCCGCGGAGCCAAGAACCTGGTTCCCAAGGCGATGGTGGCGGCGCTGCTGGGCTCGTCTCCCTCGGTGCTGCGCAATGTCCCGCTCATTCGTGACGTCGATGTTGTCTCGGGGCTGTTGAGCCTGCACGGGGTGAGCATCGACTACGACCAGCGCGAGGGCGTCCTCCAGCTGGACCCGTCCAAGGTCGAGTCGGCTCACATGGCTGATATCGACGCGCATGCCGGCTCTTCGCGCATCCCGATCCTCTTCTGCGGTCCGCTCCTGCACCGCCTGGGGGAGGCCTTCATCCCCGACCTGGGCGGGTGCCGCATCGGTGACCGCCCCATCGACTTCCACCTGGAGATTCTGCGCCAGTTCGGCGCCGCGGTGGACAAGCAGGCTCAGGGCATCCGGCTCACCGCGCCGCACGGTCTCAAGGGCACCGTCATCGAGCTTCCCTACCCCTCGGTCGGAGCCACCGAGCAGACCCTGCTCACCGCTGTGCGCGCTCACGGACTGACCGAGCTGCGCAACGCCGCCGTCGAGCCCGAGATCATGGACCTGGTCGACGTCCTGCAGAAGATGGGCGCCATCATCTCGGTGGACACCGACCGCACCATCCACGTCGAGGGCGTCGATGAGCTGTGCGGCTACACCCACTCGGCCCTGCCGGACCGCATTGAGGCCGCCTCCTGGGCCTCGGCTGCCCTGGCCACGCGCGGGGACGTGTTCGTGCGCGGAGCCCACCAGAGCCACATGACCACCTTCCTCAACACCTTCCGCAAGGTGGGAGGCGCCTTCGATGTCACTGATGAGGGCATCCGTTTCTACCACCCCGGTGGGGATCTGAAGTCGATTGTGGTGGAGACCAACGTCCACCCCGGCTTCATGACCGACTGGCAGCAGCCTCTCGTCGTGGCGCTCACCCAGGCCCAGGGCCTGTCCATCGTCCACGAGACCGTCTACGAGAACCGCTTCGGATTCACCGGTGCCCTGTGCAAGATGGGAGCCACCATCCAGGTCTACCGCGAGTGCCTGGGCGGCACCGAATGCCGCTTCGGCCAGCGCAACTTCTACCACTCCGCGGTCATCTCCGGGCCCACGCCACTGACCGGCGCCGACATCGTCGTGCCCGACCTGCGCGGCGGCTTCTCCCACCTCATCGCGGCCCTGACCGCCGAGGGCACCAGCCGGGTCGAGGGAGTCAACCTCATCGACCGTGGCTACGAGCACTTCATGTCCAAGCTCGAGTCCCTCAACGCCGCCGTCACCCGCCTGGCCTGA","MVDGLLQVEGGRPLTGEITVRGAKNLVPKAMVAALLGSSPSVLRNVPLIRDVDVVSGLLSLHGVSIDYDQREGVLQLDPSKVESAHMADIDAHAGSSRIPILFCGPLLHRLGEAFIPDLGGCRIGDRPIDFHLEILRQFGAAVDKQAQGIRLTAPHGLKGTVIELPYPSVGATEQTLLTAVRAHGLTELRNAAVEPEIMDLVDVLQKMGAIISVDTDRTIHVEGVDELCGYTHSALPDRIEAASWASAALATRGDVFVRGAHQSHMTTFLNTFRKVGGAFDVTDEGIRFYHPGGDLKSIVVETNVHPGFMTDWQQPLVVALTQAQGLSIVHETVYENRFGFTGALCKMGATIQVYRECLGGTECRFGQRNFYHSAVISGPTPLTGADIVVPDLRGGFSHLIAALTAEGTSRVEGVNLIDRGYEHFMSKLESLNAAVTRLA$","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","Cytoplasm","UDP-N-acetylglucosamine1-carboxyvinyltransferase","UDP-N-acetylglucosamine 1-carboxyvinyltransferase ","UDP-N-acetylglucosamine 1-carboxyvinyltransferase","","Stallings W.C., Abdel-Meguid S.S., Lim L.W., Shieh H.S., Dayringer H.E., Leimgruber N.K., Stegeman R.A., Anderson K.S., Sikorski J.A., Padgette S.R., Kishore G.M. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(11):5046-5050. PMID: 11607190Padgette S.R., Re D.B., Gasser C.S., Eichholtz D.A., Frazier R.B., Hironaka C.M., Levine E.B., Shah D.M., Fraley R.T., Kishore G.M. Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site. J. Biol. Chem. 1991. 266(33):22364-22369. PMID: 1939260","","","

InterPro
IPR001986
Domain

3-phosphoshikimate 1-carboxyvinyltransferase
PD001867	$\"[14-434]T$	Q6AFK5_BBBBB_Q6AFK5;
G3DSA:3.65.10.10	$\"[23-235]T$	no description
PF00275	$\"[8-429]T$	EPSP_synthase

InterPro
IPR005750
Family

UDP-N-acetylglucosamine 1-carboxyvinyltransferase
PTHR21090:SF4	$\"[98-439]T$	UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE
TIGR01072	$\"[3-438]T$	murA: UDP-N-acetylglucosamine 1-carboxyviny

noIPR
unintegrated

unintegrated
PTHR21090	$\"[98-439]T$	AROM/DEHYDROQUINATE SYNTHASE

","BeTs to 17 clades of COG0766COG name: UDP-N-acetylglucosamine enolpyruvyl transferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0766 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001986 (EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)) with a combined E-value of 1.5e-16. IPB001986A 16-47 IPB001986C 117-143 IPB001986E 239-289","Residues 8-117 are 82% similar to a (TRANSFERASE UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL CELL DIVISION EPT WALL SYNTHESIS 1-CARBOXYVINYLTRANSFERASE PEPTIDOGLYCAN) protein domain (PD850705) which is seen in Q82D56_STRAW.Residues 14-434 are similar to a (TRANSFERASE 1-CARBOXYVINYLTRANSFERASE UDP-N-ACETYLGLUCOSAMINE SYNTHASE BIOSYNTHESIS CELL 3-PHOSPHOSHIKIMATE AMINO AROMATIC ACID) protein domain (PD001867) which is seen in Q6AFK5_BBBBB.Residues 340-432 are 69% similar to a (TRANSFERASE UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL 1-CARBOXYVINYLTRANSFERASE CELL DIVISION EPT WALL SYNTHESIS 1-CARBOXYVINYL) protein domain (PD847751) which is seen in Q6MEP6_PARUW.","","-48% similar to PDB:1UAE STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE (E_value = 4.5E_57);-48% similar to PDB:1A2N STRUCTURE OF THE C115A MUTANT OF MURA COMPLEXED WITH THE FLUORINATED ANALOG OF THE REACTION TETRAHEDRAL INTERMEDIATE (E_value = 5.0E_56);-49% similar to PDB:1EJC CRYSTAL STRUCTURE OF UNLIGANDED MURA (TYPE2) (E_value = 6.5E_56);-49% similar to PDB:1EJD CRYSTAL STRUCTURE OF UNLIGANDED MURA (TYPE1) (E_value = 6.5E_56);-49% similar to PDB:1EYN STRUCTURE OF MURA LIGANDED WITH THE EXTRINSIC FLUORESCENCE PROBE ANS (E_value = 6.5E_56);","Residues 8 to 429 (E_value = 1.6e-67) place ANA_0434 in the EPSP_synthase family which is described as EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase).","","1-carboxyvinyltransferase (murA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0435","455492","456259","768","8.15","1.90","27629","ATGACCCCGTTCTACCGCTTCGCCGCGCGCGGGGCGATCATCCCGTTCCTCAAGATGGTCTCCCGGCAGAAGGTGACCGGCCTGGAGAACATCCCCCGCGAGGGCGGCTTCATCGCCGTGGCCAACCACCTGACCGACCTCGACTCGCTCACGGCCATGCGAGCCCTGGTCGATGCCGATGTCCCCGTCTACTCCCTGGCCAAGTCCACCCTGTTCAAGGTGCCGGTGCTCGGCTCCATCCTGCGGGCCGGCGGCCAGATTCCGGTCCAGCGGGGCACGCAGAACGCGGCCACCGCCCTCAAGGCGGCCAGTGAGGTCCTGGCCGACGGCGGCGCCATCATGATCTTCCCCGAGGGCACGCTCTCCCGCGACCCCCTCAAGTGGCCGATGGTGGCCAAGACTGGGGCGGCCCGGCTGGCCATGACCAGTGGTGCCCCCGTCCTGCCCATGGGGCAGTGGGGGGCCCACGAGATCCTGGACACCTACGGGCGTTCCTTCCATCCCTTCCCCCGCAAGGACGTGCGCGTCACCATCGGTGAGCTCATGGACCTGTCCCGATTCGGCTCGGACACCCAGGACCGTGAGGCCGTGCGCGCCTGCACCACCGAGATCATGCGGGCCATCACCTCCCTGGTGGAGGAACTGCGCGGGGAGAAGGCCCCCCGCCCCTTCGACATGCACTACGACGGCGACCCCGGCAAGGGAAAGATCGGCGTGCGTCGCCCCGACCCGCTGCCCGAGGCGGACACTCAGGAGGAGGGCCAGTGA","MTPFYRFAARGAIIPFLKMVSRQKVTGLENIPREGGFIAVANHLTDLDSLTAMRALVDADVPVYSLAKSTLFKVPVLGSILRAGGQIPVQRGTQNAATALKAASEVLADGGAIMIFPEGTLSRDPLKWPMVAKTGAARLAMTSGAPVLPMGQWGAHEILDTYGRSFHPFPRKDVRVTIGELMDLSRFGSDTQDREAVRACTTEIMRAITSLVEELRGEKAPRPFDMHYDGDPGKGKIGVRRPDPLPEADTQEEGQ$","Phospholipid/glycerol acyltransferase","Cytoplasm, Extracellular","1-acylglycerol-3-phosphate O-acyltransferasehomolog","phospholipid/glycerol acyltransferase","phospholipid/glycerol acyltransferase","","","","","

InterPro
IPR002123
Domain

Phospholipid/glycerol acyltransferase
PF01553	$\"[22-153]T$	Acyltransferase
SM00563	$\"[37-155]T$	PlsC

noIPR
unintegrated

unintegrated
PTHR10434	$\"[4-250]T$	1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE

","BeTs to 18 clades of COG0204COG name: 1-acyl-sn-glycerol-3-phosphate acyltransferaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0204 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 27-182 are 48% similar to a (ACYLTRANSFERASE HEMOLYSIN TRANSFERASE DOMAIN FAMILY MLL0913 MRNA SMC02490 VCA0646 HEMOLYSIN) protein domain (PD107347) which is seen in Q7M7Z9_WOLSU.Residues 29-110 are 60% similar to a (ACYLTRANSFERASE TRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE FAMILY O-ACYLTRANSFERASE 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 2.3.1.- PHOSPHOLIPID LYSOPHOSPHATIDIC) protein domain (PD000989) which is seen in Q7V4F4_PROMM.Residues 113-221 are 49% similar to a () protein domain (PD808323) which is seen in Q8G7C2_BIFLO.Residues 116-212 are 63% similar to a (ACYLTRANSFERASE TRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE FAMILY 2-ACYLGLYCEROPHOSPHOETHANOLAMINE ACYLTRANSFERASE PROBABLE PHOSPHOLIPID) protein domain (PD462158) which is seen in Q9ZBS1_STRCO.","","-42% similar to PDB:1CVL CRYSTAL STRUCTURE OF BACTERIAL LIPASE FROM CHROMOBACTERIUM VISCOSUM ATCC 6918 (E_value = );-42% similar to PDB:1TAH THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE (E_value = );-47% similar to PDB:1Z41 Crystal structure of oxidized YqjM from Bacillus subtilis (E_value = );-47% similar to PDB:1Z42 Crystal structure of oxidized YqjM from Bacillus subtilis complexed with p-hydroxybenzaldehyde (E_value = );-47% similar to PDB:1Z44 Crystal structure of oxidized YqjM from Bacillus subtilis complexed with p-nitrophenol (E_value = );","Residues 22 to 153 (E_value = 8.3e-30) place ANA_0435 in the Acyltransferase family which is described as Acyltransferase.","","O-acyltransferase homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0436","456256","457311","1056","6.70","-0.91","35454","GTGAGCAGCGACGAGCACGCAACGAGTGCGCCGCTGCGCCCGGCCGCGGCCGTCATCGGCTCAGGCGCCTGGGGAACCACCTTCGCCAGCCTCCTGGCCCAGGCCGGCACTCCCACAACGATCTGGGCCCGGCGCCGGGAGGTGGCCGAGGAGATCAACGCCGGCACCAACGAGCGCTACGTCCCCGGTCACCGCCTGCCTCAGGGCCTGAAGGCGACCACCGACCTGGCCCAGGCAGCCGCGGGGGCGAGTGTCGTCGTCGTGGCCGTGCCCTCCCAGGAGGCCCGGAGGGTCCTGGAGCCCCTCCGGGGCGTACTGGCCGACGACGCCGTGGCCGTCTCCCTCATGAAGGGCATCGAGCTGGGTACCGGGCTGCGGATGAGCGAGGTCCTGGCCAGGGCCCTGGGCATCGACACCTCCCGTGTCGTGGTCGTCTCCGGCCCCAATCTCGCCGACGAGATTGCTGCGGGCCAGCCCACGGCCACCGTCGTGGCAGCCGACGACGAGCAGGTCGCCGCCCGGATCGCCTCGCTGTGCGCCACCGGCACCTTCCGCCCCTACACCAACACCGACGTCCTGGGCGTCGAGCTGTGCGGGGCGGTCAAGAACGTCATCGCCCTGGCCGTCGGCGCGGCCGCGGGCCGGGGCCTGGGGGACAACTCCAAGGCCACGATCATCACCCGGGGCCTGGTGGAGATCACCCGGCTGGGCCTTAAGCTCGGGGCTCGCCCGGAGACCTTCTCCGGGCTGGCAGGCATGGGGGACCTGGTGGCCACCTGCTCCTCGCCCCTGAGCCGCAACCAGACCTTCGGCCGCCACCTCGGCGAGGGGATGAGCGTGGCCGAGGCCGCTGCGGCCTCCCGGGGCGTGGCCGAGGGGGCCAAGTCGGCCCGCGCCGTCCTGGACCTGGCCCGGGCCCACGGCGTGGACATGCCAATCACCGCCGGGGTCGTCAGCGTCGTCGAGGGCGCCGCCAGCGTCGCGCAGGTCACTGACGCGCTGCTGGCTCGCCCCCGCAAGGCCGAGGGCGTGCACGCGGAGCCGTCTCAGGCGTAG","VSSDEHATSAPLRPAAAVIGSGAWGTTFASLLAQAGTPTTIWARRREVAEEINAGTNERYVPGHRLPQGLKATTDLAQAAAGASVVVVAVPSQEARRVLEPLRGVLADDAVAVSLMKGIELGTGLRMSEVLARALGIDTSRVVVVSGPNLADEIAAGQPTATVVAADDEQVAARIASLCATGTFRPYTNTDVLGVELCGAVKNVIALAVGAAAGRGLGDNSKATIITRGLVEITRLGLKLGARPETFSGLAGMGDLVATCSSPLSRNQTFGRHLGEGMSVAEAAAASRGVAEGAKSARAVLDLARAHGVDMPITAGVVSVVEGAASVAQVTDALLARPRKAEGVHAEPSQA$","Glycerol-3-phosphate dehydrogenase (NAD(P)(+))","Cytoplasm","Glycerol-3-phosphate dehydrogenase [NAD(P)+](NAD(P)H-dependent glycerol-3-phosphate dehydrogenase)","glycerol-3-phosphate dehydrogenase (NAD(P)(+)) ","Glycerol-3-phosphate dehydrogenase (NAD(P)(+))","","von Kalm L., Weaver J., DeMarco J., MacIntyre R.J., Sullivan D.T. Structural characterization of the alpha-glycerol-3-phosphate dehydrogenase-encoding gene of Drosophila melanogaster. Proc. Natl. Acad. Sci. U.S.A. 1989. 86(13):5020-5024. PMID: 2500660Otto J., Argos P., Rossmann M.G. Prediction of secondary structural elements in glycerol-3-phosphate dehydrogenase by comparison with other dehydrogenases. Eur. J. Biochem. 1980. 109(2):325-330. PMID: 6773774","","","

InterPro
IPR006109
Domain

NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal
PD001278	$\"[219-314]T$	Q8CP64_STAEP_Q8CP64;
PF07479	$\"[190-334]T$	NAD_Gly3P_dh_C

InterPro
IPR006168
Family

NAD-dependent glycerol-3-phosphate dehydrogenase
PR00077	$\"[18-35]T$ $\"[67-94]T$ $\"[144-164]T$ $\"[184-208]T$ $\"[209-233]T$ $\"[249-266]T$	GPDHDRGNASE
PTHR11728	$\"[15-342]T$	GLYCEROL-3-PHOSPHATE DEHYDROGENASE
PS00957	$\"[199-220]T$	NAD_G3PDH

InterPro
IPR011128
Domain

NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01210	$\"[14-173]T$	NAD_Gly3P_dh_N

InterPro
IPR013328
Domain

Dehydrogenase, multihelical
G3DSA:1.10.1040.10	$\"[200-342]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[15-198]T$	no description
PIRSF000114	$\"[14-338]T$	Glycerol-3-phosphate dehydrogenase (NAD)

","BeTs to 21 clades of COG0240COG name: Glycerol 3-phosphate dehydrogenaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0240 is a-m---yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB006168 (NAD-dependent glycerol-3-phosphate dehydrogenase) with a combined E-value of 4.8e-80. IPB006168A 18-29 IPB006168B 51-92 IPB006168C 144-165 IPB006168D 184-232 IPB006168E 246-267","Residues 106-205 are similar to a (DEHYDROGENASE GLYCEROL-3-PHOSPHATE OXIDOREDUCTASE NAD PHOSPHOLIPID BIOSYNTHESIS NADP DEPENDENT NADPH- NAD) protein domain (PD102920) which is seen in GPDA_COREF.Residues 219-314 are similar to a (OXIDOREDUCTASE DEHYDROGENASE NAD GLYCEROL-3-PHOSPHATE G-3-P GPDH-C CYTOPLASMIC NAD GPD-C SEQUENCING) protein domain (PD001278) which is seen in Q8CP64_STAEP.","","-52% similar to PDB:1Z82 Crystal structure of glycerol-3-phosphate dehydrogenase (TM0378) from THERMOTOGA MARITIMA at 2.00 A resolution (E_value = 1.7E_40);-44% similar to PDB:1EVY CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE (E_value = 4.0E_26);-44% similar to PDB:1EVZ CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH NAD (E_value = 4.0E_26);-44% similar to PDB:1JDJ CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH 2-FLUORO-6-CHLOROPURINE (E_value = 4.0E_26);-44% similar to PDB:1M66 Crystal Structure of Leishmania mexicana GPDH Complexed with Inhibitor 2-bromo-6-chloro-purine (E_value = 4.0E_26);","Residues 14 to 173 (E_value = 5.5e-66) place ANA_0436 in the NAD_Gly3P_dh_N family which is described as NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus.Residues 15 to 212 (E_value = 0.00011) place ANA_0436 in the F420_oxidored family which is described as NADP oxidoreductase coenzyme F420-dependent.Residues 16 to 169 (E_value = 2.9e-06) place ANA_0436 in the ApbA family which is described as Ketopantoate reductase PanE/ApbA.Residues 190 to 334 (E_value = 1e-60) place ANA_0436 in the NAD_Gly3P_dh_C family which is described as NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus.","","dehydrogenase [NAD(P)+] (NAD(P)H-dependent glycerol-3-phosphate dehydrogenase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0437","457397","458563","1167","4.70","-20.93","40609","ATGACAGCCCTCCAGGAAGCCGGCCCCTCCGTGCCCAGTTCTGACAAGTCCACCGTGCGTGTCGCCGTCGTCTTCGGTGGGCGCAGTGGTGAGCACACGATCTCCTGCGCCACCGCAGCCGGCGTCCTGTCAGCCATTGACCGCAACCGTTACGAGGTCCTTCCGGTGGGCATCACGCCCGAGGGCCAGTGGCTGCTCGTCGAGGACGATCCGGCCGCCCTCGAGCTCAGCGACAACCGCCCCCCGGTGACCATCACCGCCGAGGGCTTGGGACGCGGGAGGCTCACCGCACCCCTGGGAGGCGGCGAGCTCACGGTCCTCGGTCCCACGGGGCCTGAGGTCCTGGGGCAGGTCGACGTCGTCCTGCCGCTGCTGCACGGGCCCTACGGCGAGGACGGAACCATCCAGGGCATGCTGGAGATGATGGGCATTCCCTACGTCGGCTGCGGGGTGCTGGCCAGCGCCGCGGGCATGGACAAGCAGGTCACTAAGGTGCTCCTGGGGGCCGCGGGCATCGCCACGGCGCCGCACGTCGTCGTCGGTCCCCATGCCTGGAAGCGGGACCCCGAGGCGATCCTGGAGGCCTGTCGGTCCCTGACCTACCCCCTGTTCGTCAAGCCCGCCCGTGCCGGCTCCTCCCTGGGCATCAGCAAGGTCGACCGCCCTGAGGACCTGGCCGGAGCCATCGAGGCGGCCCGCGCGGTCGATCCCAAGGTCCTCGTGGAGAGCGGCATCGTGGGACGAGAGGTCGAGGTCGCCGTCCTTCAGGGCCGCGGCGACGACGCCCCCCGAGTGGCCGAGCCCGGCGAGATCGCCATGGACGCCTCCCAGGGCGCCGGCGAGTTCTACGACTACGAGACTAAGTACCTGGCCCACGACGCTGTGGCCATGGTGTGCCCGGCGCGCATCAGCCCTGAGGCGCGCGCGCTCCTCATGGACACCGCGGCCCGGGCCTTCGAGGCGGTCGGCTGCGAGGGGCTGGCTCGGGTCGACTTCTTCCTCACTGAGGTCGGCGAGGCGGTGGTCAACGAGATCAACACGATGCCCGGTTTCACCCCCTTCTCCATGTACCCCTACATGTGGCAGGTCTCCGGCCTGGGCTACACCGAGCTGGTCTCTGAGCTCATTGAGCTGGCCGTGGCTCGATCCACCGATGTCAACCGCTGA","MTALQEAGPSVPSSDKSTVRVAVVFGGRSGEHTISCATAAGVLSAIDRNRYEVLPVGITPEGQWLLVEDDPAALELSDNRPPVTITAEGLGRGRLTAPLGGGELTVLGPTGPEVLGQVDVVLPLLHGPYGEDGTIQGMLEMMGIPYVGCGVLASAAGMDKQVTKVLLGAAGIATAPHVVVGPHAWKRDPEAILEACRSLTYPLFVKPARAGSSLGISKVDRPEDLAGAIEAARAVDPKVLVESGIVGREVEVAVLQGRGDDAPRVAEPGEIAMDASQGAGEFYDYETKYLAHDAVAMVCPARISPEARALLMDTAARAFEAVGCEGLARVDFFLTEVGEAVVNEINTMPGFTPFSMYPYMWQVSGLGYTELVSELIELAVARSTDVNR$","D-alanine--D-alanine ligase","Cytoplasm","D-ala D-ala ligase","D-alanine--D-alanine ligase ","D-alanine--D-alanine ligase","","Roper D.I., Huyton T., Vagin A., Dodson G. The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA). Proc. Natl. Acad. Sci. U.S.A. 2000. 97(16):8921-8925. PMID: 10908650Fan C., Park I.S., Walsh C.T., Knox J.R. D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant. Biochemistry 1997. 36(9):2531-2538. PMID: 9054558","","","

InterPro
IPR000291
Family

D-alanine--D-alanine ligase/VANA/B/C
PS00843	$\"[126-137]T$	DALA_DALA_LIGASE_1
PS00844	$\"[322-350]T$	DALA_DALA_LIGASE_2

InterPro
IPR005905
Family

D-alanine--D-alanine ligase
TIGR01205	$\"[20-380]T$	D_ala_D_alaTIGR: D-alanine--D-alanine ligas

InterPro
IPR011095
Domain

D-alanine--D-alanine ligase, C-terminal
PF07478	$\"[159-377]T$	Dala_Dala_lig_C

InterPro
IPR011127
Domain

D-alanine--D-alanine ligase, N-terminal
PF01820	$\"[19-158]T$	Dala_Dala_lig_N

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[164-377]T$	ATP_GRASP

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[221-382]T$	no description

InterPro
IPR013817
Domain

Pre-ATP-grasp fold
G3DSA:3.40.50.20	$\"[16-146]T$	no description

noIPR
unintegrated

unintegrated
PTHR23132	$\"[109-383]T$	D-ALANINE--D-ALANINE LIGASE

","BeTs to 17 clades of COG1181COG name: D-alanine-D-alanine ligase and related ATP-grasp enzymesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1181 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB000291 (D-alanine--D-alanine ligase/VANA/B/C) with a combined E-value of 8.7e-91. IPB000291A 21-36 IPB000291B 119-159 IPB000291C 199-242 IPB000291D 279-296 IPB000291E 329-368","Residues 20-71 are 78% similar to a (LIGASE D-ALANINE--D-ALANINE D-ALA-D-ALA D-ALANYLALANINE SYNTHETASE WALL CELL PEPTIDOGLYCAN SYNTHESIS B) protein domain (PD583430) which is seen in DDL_STRCO.Residues 98-180 are similar to a (LIGASE D-ALANINE--D-ALANINE D-ALA-D-ALA WALL CELL D-ALANYLALANINE SYNTHETASE PEPTIDOGLYCAN SYNTHESIS B) protein domain (PD306575) which is seen in Q73VJ4_MYCPA.Residues 199-249 are 84% similar to a (LIGASE SYNTHETASE D-ALANINE--D-ALANINE D-ALA-D-ALA WALL CELL D-ALANYLALANINE PEPTIDOGLYCAN SYNTHESIS B) protein domain (PD000755) which is seen in VANL_STRCO.Residues 303-382 are similar to a (LIGASE D-ALANINE--D-ALANINE D-ALA-D-ALA WALL CELL D-ALANYLALANINE SYNTHETASE PEPTIDOGLYCAN SYNTHESIS B) protein domain (PD522734) which is seen in DDL_STRAW.","","-56% similar to PDB:2I80 Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies (E_value = 1.1E_67);-56% similar to PDB:2I87 Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies (E_value = 1.1E_67);-56% similar to PDB:2I8C Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies (E_value = 1.1E_67);-54% similar to PDB:1E4E D-ALANYL-D-LACATE LIGASE (E_value = 8.6E_57);-54% similar to PDB:2FB9 Crystal structure of the Apo form of D-alanine: D-alanine ligase (Ddl) from Thermus caldophilus: a basis for the substrate-induced conformational changes (E_value = 2.5E_56);","Residues 19 to 158 (E_value = 4.7e-58) place ANA_0437 in the Dala_Dala_lig_N family which is described as D-ala D-ala ligase N-terminus.Residues 159 to 351 (E_value = 5.5e-05) place ANA_0437 in the ATP-grasp family which is described as ATP-grasp domain.Residues 159 to 377 (E_value = 4.8e-93) place ANA_0437 in the Dala_Dala_lig_C family which is described as D-ala D-ala ligase C-terminus.","","D-ala ligase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0438","458589","459659","1071","4.86","-17.25","35871","GTGGGGCAGGACGCGCGGGTCGGTGACCTCAGCGAGGAGGAGCTCCTTGCCGTCATCACCCCCCTCCTGCCCCGCGGCCCGCAGACCCCCGTCGGCACGGGGGACGACTGCGCGGTCCTGTCCTTCCCCGACTCACTTACGGCGGTGAGCACCGACGTCCTGGTCGAAGGGCGCCACTTCCGCACCGACTGGTCCACGGGCCGCGACGTCGGGGCCAGGGCCGCGGCCCAGAACCTCGCCGACGCCGCCGCCATGGGGGCCAGGCCCGTCGCGCTCGTCGTCGGCCTGGTCATGCCTGCGTCCACCCCGGTCGGCTGGGTACGGGACTTCGCCCGAGGGCTGGCCCAGGGCTGCGAGCTCTGCGGGGCGGGCGTCGTGGGCGGTGACCTCAGCTCCGGTGACTCGCTGATCGTGTCCGTCACGGTCCTGGGTGACCTTGAGGGCCGGGCCCCGGTTCTGCGAAGCGGGGCCCGGCCCGGTGACGCCGTCGTGCACGTTGGAACCCTGGGACGTAGCGCAGCGGGACTGGCCCTGCTCAGCGCGGGCACTGACTGCGTACCAGGTTCAAGTGCCGCTGTCCCCTCAGGTCAGGAGCACCCCCAGGCTCAGGCCTGTATCGAGACCTTCCGTGCCCCTGCCCCGCCCCTGGCGGCGGGCCGAGAGCTGGCGCTGATCGGCGCCACCTCCATGTTGGACGTCTCCGACGGTCTGCTGCGCGACGCCGGCCGGATTGCCCGCGCCAGCGGTGTCGTCATCGATCTCGATGATCCCGGTGACCTGCCGGACGCGTCCTTCCTCGAGTCGGTGGCCGTGCTCGTGAGCGGTCACGACGGATCGGCCGCTCGTGACCTGGCCCGCAGCTGGTTGCTCGCCGGGGGAGAGGACCACGGACTGCTCGCCACCGTCCCGGCGGACGGTCTCGATCGGCTACCTGCCGGAGCCCGGGTGATCGGCCGGGTCCTGAGCCCGCAGGAATCGTCGGCCGGGATGCCGGGGTGCAGGCCGAGCGTTCTCCTGGCAGGAGAACCCGCGCAGGAGCACACCGGATGGGACCACTTCTCCCACACCTGA","VGQDARVGDLSEEELLAVITPLLPRGPQTPVGTGDDCAVLSFPDSLTAVSTDVLVEGRHFRTDWSTGRDVGARAAAQNLADAAAMGARPVALVVGLVMPASTPVGWVRDFARGLAQGCELCGAGVVGGDLSSGDSLIVSVTVLGDLEGRAPVLRSGARPGDAVVHVGTLGRSAAGLALLSAGTDCVPGSSAAVPSGQEHPQAQACIETFRAPAPPLAAGRELALIGATSMLDVSDGLLRDAGRIARASGVVIDLDDPGDLPDASFLESVAVLVSGHDGSAARDLARSWLLAGGEDHGLLATVPADGLDRLPAGARVIGRVLSPQESSAGMPGCRPSVLLAGEPAQEHTGWDHFSHT$","Thiamine-monophosphate kinase","Cytoplasm, Membrane","thiamine-monophosphate kinase","thiamine-monophosphate kinase ","thiamine-monophosphate kinase","","","","","

InterPro
IPR006283
Family

Thiamine-monophosphate kinase
PIRSF005303	$\"[10-354]T$	Thiamine monophosphate kinase
TIGR01379	$\"[14-353]T$	thiL: thiamine-monophosphate kinase

InterPro
IPR010918
Domain

AIR synthase related protein, C-terminal
PF02769	$\"[158-331]T$	AIRS_C

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.10	$\"[5-150]T$	no description
G3DSA:3.90.650.10	$\"[153-353]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 7-70 are 57% similar to a (KINASE THIAMINE-MONOPHOSPHATE) protein domain (PDA005T9) which is seen in Q6AFK0_BBBBB.Residues 34-71 are 73% similar to a (KINASE THIAMINE-MONOPHOSPHATE TRANSFERASE THIAMINE THIAMIN-MONOPHOSPHATE MONOPHOSPHATE THIAMINE-PHOSPHATE THIL BIOSYNTHESIS PROBABLE) protein domain (PD825308) which is seen in Q9ZBR7_STRCO.Residues 210-353 are 50% similar to a (KINASE THIAMINE-MONOPHOSPHATE TRANSFERASE THIAMINE MONOPHOSPHATE THIAMIN-MONOPHOSPHATE THIAMINE-PHOSPHATE BIOSYNTHESIS PROBABLE THIL) protein domain (PD553796) which is seen in Q9ZBR7_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 158 to 331 (E_value = 0.0054) place ANA_0438 in the AIRS_C family which is described as AIR synthase related protein, C-terminal domain.","","kinase (thiL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0439","459956","459765","192","11.33","11.26","6837","GTGGCTGCTGTGTGCGACGTTTGCGGCAAGGGCCCCATCTTCGGCAAGAGCGTCTCGCACTCCCACGTGCGGACCAACCGCCGGTGGAACCCCAACATCCAGCGTGTGCGTGCTCTCGTCAATGGCGCCCCCAAGCGCCTCAACGTGTGCACGTCCTGCCTCAAGGCCGGGAAGGTGACGCGCAACATCTGA","VAAVCDVCGKGPIFGKSVSHSHVRTNRRWNPNIQRVRALVNGAPKRLNVCTSCLKAGKVTRNI$","Ribosomal protein L28","Extracellular","ribosomal protein L28","K02902 large subunit ribosomal protein L28","ribosomal protein L28","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001383
Family

Ribosomal protein L28
PF00830	$\"[3-61]T$	Ribosomal_L28
TIGR00009	$\"[2-56]T$	L28: ribosomal protein L28

","BeTs to 17 clades of COG0227COG name: Ribosomal protein L28Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0227 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001383 (Ribosomal protein L28) with a combined E-value of 6.3e-20. IPB001383 1-34","Residues 3-61 are similar to a (RIBOSOMAL L28 50S CHLOROPLAST PEPTIDE SEQUENCING DIRECT TRANSIT PRECURSOR L28) protein domain (PD003595) which is seen in R28A_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 61 (E_value = 9.9e-20) place ANA_0439 in the Ribosomal_L28 family which is described as Ribosomal L28 family.","","protein L28 (rpmB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0440","460236","460325","90","8.25","0.88","3048","ATGTCCTTTCGGCTCTCCGTCGCTCTGGGTGAGGTGCTGGTGTGGTCATCCTGCTCCGGTGGGAGGAATGTGATCGGGCAGGTACTCTGA","MSFRLSVALGEVLVWSSCSGGRNVIGQVL$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide

InterPro
IPR004007
Domain

Dak phosphatase
PF02734	$\"[49-218]T$	Dak2

","BeTs to 6 clades of COG1461COG name: Predicted kinase related to dihydroxyacetone kinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1461 is --------vdrlb------------wNumber of proteins in this genome belonging to this COG is 1","***** IPB004007 (Dak phosphatase domain) with a combined E-value of 5.1e-07. IPB004007A 50-66 IPB004007B 86-106","Residues 97-329 are 43% similar to a (KINASE PREDICTED RELATED DIHYDROXYACETONE DAK2 DOMAIN HYDROXYACETONE ALANINE HYPOTEHTICAL RICH) protein domain (PD025264) which is seen in Q9ZBR4_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 49 to 218 (E_value = 4.7e-16) place ANA_0441 in the Dak2 family which is described as DAK2 domain.","","domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0442","462592","464850","2259","5.94","-12.65","80839","GTGACCCGGCTCGTGGGCAAGCGCACGGCCGCCCAGCTCGCCAAGCAGGGGGTGGAGACCGGGGCGGACCTGCTGCGCCTGCTGCCCCGACGCTACGATACGTGGGGGGAGCTGACCGACATGCGCACCCTCGTCGAGGGTGAGCAGGCCACCATCCAGGCCCAGGTCGTGCGCGCCTCCTCCCGGCGTACCCGCTCCGGCCGGGTCCCGGCCCTTATGGAGGCCACCGTCACTGACGGCGCCTCCACCATGGACCTCGTCCAGTTCGGTGCTGCCGGCCAGATGCGCACCCGGGCTGCCCAGCTGGCCCCCGGAACCACCGTCCTGCTCAGCGGCAAGGTAGGACTCCACCGCGGACGCAAGCAGCTGTCCAACCCGCGCCTGTACGTCCTCGACGAGCTCGATGAGGACGAGCGCGAGGCCCTGCTGGCCCGACCCATGCCCATCTACCCCGGCACGGAGGCCCTCCCGTCCTGGCTGGTGGCCAAGGCGGTGCGCAGCGTCCTGGACCAGCTGGAGCCGGGCGACGTCGCCGACCCCCTCCCCGAGGAGCTGCGGCGCGAGGCGGAGCTGGTCGACGCCTACACCGCCTACCGCTGGGTGCACCGGCCCGAGGACTCCGGGCAGTGGAAGGCCGCCCGGAAACGGCTGTGCCACGAGGAGGCCCTCATCCTGCAGGTCGCCCTGGCCCAGCGTCGAGCCCATCATGAGGCGACATGCACCGCGGTCGCCTGGCCCGTACCGGAGGCGGAGGGCTCCCTGAGAGCGGACCTCGACGCCCGCCTGCCCTACGACCTGACCGCCGGGCAGAAGCGGGTCGGTGAGGAGATCTCCGCCGACCTGGCCCGCACCGTTCCCATGCAGCGCCTTCTTCAGGGCGACGTGGGAAGCGGCAAGACCCTCGTGGCCCTGCGCGCCATGCTCCAGGTGGTTGGAGGCGGCGGGCAGGCCGCCCTCCTGGCCCCCACCGAGGTCCTCGCCGCCCAGCACCACTCCTCACTGGAGGTGGTCCTGGGGCCCATGGCCCGCCTCGGGATGCTCGGCGGCGCCGAACACGCCACCCGCGTCCACCTGCTGACCGGCTCCACCCCCGCCGCTCAGCGCCGTCGGATCCTCACTGAGCTGGCCGCCGGTGAGCCGGCGATTGTCGTGGGTACCCACGCCCTGCTGTCCGACACGGTGCAGATCCCCTTCCTCGGCCTGGTCGTCGTCGACGAGCAGCACCGCTTCGGCGTCGCCCAGCGCGACGCCCTGCGCGAGCGCGGCGGTCTCACCGACCCGGCCACCGGCCAGAGCCACACGCCCCACCTCCTGGTCATGACCGCCACCCCGATCCCGCGCACCATCGCCATGACGGTCTTCGGGGACCTGGCCACCTCCGTCCTGGACGAGCTGCCCGCCGGGCGCAGCACCGTACCCACCCACCTCGTCCCGTGGTCGCGCACCTCCTGGGTGGAGGGGATCTGGCGGCGCGCCGCCAAAGAGGTCGCCTCCGGAGGGCGGGTCTACGTCGTGTGCCCACGGATCGAGGTCGACGACGAGCCCCGGCAGGAGCAGACGGAAGGTGCAGCGGCCGTCGAGACCGATGACAGGCCGGGGGATGAGGCGCTCGCGGAGGAGGGGGACGGCTCGCATCCCGACCGCCCGCTGGCCGCCGTCGAGGAGTGGAGGCGGCGACTGGAGGGGGAACCGGCCCTGGAGGGCGTCGGCGTCGGAGTCCTCACCGGACGCATGAGCAGTGACGACAAGGCTGCCTCCATGGCCGACTTTGCCTCGGGCGCCACCCCGGTCCTGGTGTCCACCACCGTCATCGAGGTGGGGGTGGACGTGCCCGAGGCCTCCATGATGGTCATCCTGGACGCCGAGCGTTTCGGACTGTCCCAGCTCCACCAGCTGCGCGGGCGTGTCGGGCGCGGCAGTAGGCCGTCCCTGTGCGTGGCGGTTACCGGTGCGGAGGTCGGCTCCACCGCCTTCCACCGGCTCAAGGCATTCGCCTCCACCACGGACGGATTCGCGCTGGCCGAGGCGGACCTCGAGCTGCGCAGCGAGGGCGATGTCCTGGGGGCCTCGCAGTCGGGGCGCGCTTCCGGGCTGGACTTGCTGCGCGTCACCCGCGATGCCCGCCTCATCGCCACTGCGAGGCGCCAGGCGGAGCAGATCGTGGCCACCGACCCACAGTTGCGTGAGCACCGGGCCCTGGCCGCGGCGATCGTCGAGCGCCTCGATGAGGAGTCCCAGGCCTTCCTCGAAAGAGCGTGA","VTRLVGKRTAAQLAKQGVETGADLLRLLPRRYDTWGELTDMRTLVEGEQATIQAQVVRASSRRTRSGRVPALMEATVTDGASTMDLVQFGAAGQMRTRAAQLAPGTTVLLSGKVGLHRGRKQLSNPRLYVLDELDEDEREALLARPMPIYPGTEALPSWLVAKAVRSVLDQLEPGDVADPLPEELRREAELVDAYTAYRWVHRPEDSGQWKAARKRLCHEEALILQVALAQRRAHHEATCTAVAWPVPEAEGSLRADLDARLPYDLTAGQKRVGEEISADLARTVPMQRLLQGDVGSGKTLVALRAMLQVVGGGGQAALLAPTEVLAAQHHSSLEVVLGPMARLGMLGGAEHATRVHLLTGSTPAAQRRRILTELAAGEPAIVVGTHALLSDTVQIPFLGLVVVDEQHRFGVAQRDALRERGGLTDPATGQSHTPHLLVMTATPIPRTIAMTVFGDLATSVLDELPAGRSTVPTHLVPWSRTSWVEGIWRRAAKEVASGGRVYVVCPRIEVDDEPRQEQTEGAAAVETDDRPGDEALAEEGDGSHPDRPLAAVEEWRRRLEGEPALEGVGVGVLTGRMSSDDKAASMADFASGATPVLVSTTVIEVGVDVPEASMMVILDAERFGLSQLHQLRGRVGRGSRPSLCVAVTGAEVGSTAFHRLKAFASTTDGFALAEADLELRSEGDVLGASQSGRASGLDLLRVTRDARLIATARRQAEQIVATDPQLREHRALAAAIVERLDEESQAFLERA$","ATP-dependent DNA helicase RecG","Cytoplasm","ATP-dependent DNA helicase recG","ATP-dependent DNA helicase RecG ","DEAD/DEAH box helicase domain protein","","Koonin E.V., Wolf Y.I., Aravind L. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 2000. 54:245-275. PMID: 10829230Keshav K.F., Chen C., Dutta A. Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. Mol. Cell. Biol. 1995. 15(6):3119-3128. PMID: 7760808Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 1997. 385(6612):176-181. PMID: 8990123","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[563-640]T$	Helicase_C
SM00490	$\"[554-640]T$	HELICc
PS51194	$\"[510-679]T$	HELICASE_CTER

InterPro
IPR004365
Domain

Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336	$\"[50-131]T$	tRNA_anti

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[267-452]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[262-480]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[280-462]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[568-680]T$	no description
PTHR14025	$\"[587-620]T$	FAMILY NOT NAMED
PTHR14025:SF10	$\"[587-620]T$	gb def: CG7922-PA

","BeTs to 15 clades of COG1200COG name: RecG-like helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1200 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB003711 (Transcription factor CarD) with a combined E-value of 3.8e-57. IPB003711B 262-286 IPB003711C 287-324 IPB003711D 396-437 IPB003711F 565-608 IPB003711G 609-648 IPB003711H 667-711 IPB003711E 448-476","Residues 98-222 are 48% similar to a (HELICASE DNA HYDROLASE ATP-BINDING ATP-DEPENDENT RECG 3.6.1.- REPAIR RECOMBINATION DNA-BINDING) protein domain (PD233697) which is seen in Q6AFJ8_BBBBB.Residues 213-295 are 62% similar to a (HELICASE ATP-BINDING HYDROLASE DNA COUPLING FACTOR TRANSCRIPTION-REPAIR ATP-DEPENDENT RECG 3.6.1.-) protein domain (PD714286) which is seen in Q73VK4_MYCPA.Residues 296-386 are 78% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT FACTOR DNA BOX RNA-BINDING 3.6.1.-) protein domain (PD410733) which is seen in RECG_MYCTU.Residues 340-394 are 76% similar to a (RECG HELICASE ATP-BINDING HYDROLASE) protein domain (PD960560) which is seen in Q73VK4_MYCPA.Residues 399-478 are 78% similar to a (HELICASE ATP-BINDING HYDROLASE DNA COUPLING FACTOR TRANSCRIPTION-REPAIR ATP-DEPENDENT RECG 3.6.1.-) protein domain (PD398886) which is seen in Q9ZBR3_STRCO.Residues 552-610 are 64% similar to a (HELICASE ATP-BINDING HYDROLASE DNA ATP-DEPENDENT RNA EXCISION FACTOR B REPAIR) protein domain (PD000033) which is seen in Q8G7D8_BIFLO.Residues 613-651 are 87% similar to a (HELICASE ATP-BINDING HYDROLASE DNA COUPLING FACTOR TRANSCRIPTION-REPAIR ATP-DEPENDENT RECG 3.6.1.-) protein domain (PD713801) which is seen in Q6AFJ8_BBBBB.Residues 667-719 are 67% similar to a (HELICASE ATP-BINDING HYDROLASE DNA COUPLING FACTOR TRANSCRIPTION-REPAIR ATP-DEPENDENT RECG 3.6.1.-) protein domain (PD008437) which is seen in Q6AFJ8_BBBBB.","","-50% similar to PDB:1GM5 STRUCTURE OF RECG BOUND TO THREE-WAY DNA JUNCTION (E_value = 2.1E_92);-47% similar to PDB:2EYQ Crystal structure of Escherichia coli transcription-repair coupling factor (E_value = 1.5E_45);","Residues 50 to 131 (E_value = 4.3e-05) place ANA_0442 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.Residues 267 to 452 (E_value = 2.6e-28) place ANA_0442 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 563 to 640 (E_value = 3.9e-21) place ANA_0442 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","DNA helicase recG","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0443","465446","464886","561","6.03","-1.62","19634","ATGACGAGGATCGTGGCCGGAACCGTGGGCGGACGCAGGATCGAGGTGCCCCGGTCCGGGACGCGTCCCACCTCCGAGCGCGTCCGCGAGGCTCTTTTCGCCCGCCTGGACCACTACGGGGTGCTCGACGGCGCTCGGGTGCTGGACCTGTGCGCGGGATCCGGGGCACTGGGCCTGGAAGCCGCGAGCCGAGGAGCCGGCGAGGTCACGCTCGTGGACTCCTCGCGCGGTGCGTCGCAGACCTGCCGACGCAACATCCACTCACTGGGCCTGAGTGGGGTATCGGCGGTGACCGCGAAGGCGGCCGCCTTCCTGGCCGGCCCGGCGGGCGCTCCGGCGGACCTGGTGCTGATCGATCCTCCCTACGAGCTGAGCGAGGAGGAGCTCACGGCGATCCTCACTGCCCTGGTCCGCAGCGAGGATCCGTGGCTGGCGCCGCGCGCCGTCGTCGTCGTCGAGCGCTCGACGCGCTCACCGGAACCGACCTGGCCGGCGGGGCTGGAGCGCTTCGCGGACAAGCGGTACGGCGAGACCACGATCTGGTTCGCCGAGCCGGCCTGA","MTRIVAGTVGGRRIEVPRSGTRPTSERVREALFARLDHYGVLDGARVLDLCAGSGALGLEAASRGAGEVTLVDSSRGASQTCRRNIHSLGLSGVSAVTAKAAAFLAGPAGAPADLVLIDPPYELSEEELTAILTALVRSEDPWLAPRAVVVVERSTRSPEPTWPAGLERFADKRYGETTIWFAEPA$","N6-adenine-specific methylase","Cytoplasm","methyltransferase, putative","hypothetical protein","putative methyltransferase","","Cheng X. Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 1995. 24:293-318. PMID: 7663118Loenen W.A., Daniel A.S., Braymer H.D., Murray N.E. Organization and sequence of the hsd genes of Escherichia coli K-12. J. Mol. Biol. 1987. 198(2):159-170. PMID: 3323532Narva K.E., Van Etten J.L., Slatko B.E., Benner J.S. The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases. Gene 1988. 74(1):253-259. PMID: 3248728Lauster R. Evolution of type II DNA methyltransferases. A gene duplication model. J. Mol. Biol. 1989. 206(2):313-321. PMID: 2541254Timinskas A., Butkus V., Janulaitis A. Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases. Gene 1995. 157(1):3-11. PMID: 7607512Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E., Schildkraut I., Saenger W. Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(23):10957-10961. PMID: 7971991","","","

InterPro
IPR002052
Domain

N-6 Adenine-specific DNA methylase
PS00092	$\"[116-122]?$	N6_MTASE

InterPro
IPR004398
Family

Conserved hypothetical protein 95
PF03602	$\"[2-184]T$	Cons_hypoth95
TIGR00095	$\"[1-186]T$	TIGR00095: putative methyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[22-145]T$	no description

","BeTs to 13 clades of COG0742COG name: N6-adenine-specific methylaseFunctional Class: LThe phylogenetic pattern of COG0742 is ------vcebrhuj--olinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 149-219 are 66% similar to a (METHYLTRANSFERASE METHYLASE) protein domain (PD984453) which is seen in Q6A7Q3_PROAC.Residues 149-217 are 66% similar to a (METHYLTRANSFERASE TRANSFERASE METHYLASE 2.1.1.- METHYLTRANSFERASE N6-ADENINE-SPECIFIC DNA YHHF POSSIBLE PREDICTED) protein domain (PD475370) which is seen in Q6AFJ9_BBBBB.","","-44% similar to PDB:2FPO Putative methyltransferase yhhF from Escherichia coli. (E_value = 8.1E_10);","Residues 37 to 219 (E_value = 1.7e-64) place ANA_0443 in the Cons_hypoth95 family which is described as Conserved hypothetical protein 95.","","putative ","","1","","","Fri Aug 10 16:36:20 2007","","Fri Aug 10 16:36:20 2007","","","Fri Aug 10 16:36:20 2007","Fri Aug 10 16:36:20 2007","Fri Aug 10 16:36:20 2007","","","Fri Aug 10 16:36:20 2007","","","Fri Aug 10 16:36:20 2007","Fri Aug 10 16:36:20 2007","Fri Aug 10 16:36:20 2007","","Fri Aug 10 16:36:20 2007","Fri Aug 10 16:36:20 2007","","","","","yes","","" "ANA_0444","466165","465497","669","4.84","-12.48","23439","ATGCTTCTCAACGACGCTCGACAGCAGATCGCCGATGCCTGCTCCCACCTGTCCGACGACGGCCTGGTCGTCGGCACCGCCGGCAACCTGTCCGTTCGGGAGGGGGACCTGGTCGCCATCACCCCCTCGGGGCTGCCCTACCAGGAGATGCGCCCCGATCTGGTCGCCGTAGTCGAGTACGCCACCGGCAAGCAGGTCGAGGGGCCGCTCAAGCCCGCCAGCGAGCTGGACCTGCACCTGACCGCGCTGCGGGCGACCGGACAGATGGCGGTCGTGCACACCCACTCCTATGCGGCCACTACCGTGGCCAGCCTCGAGGGCGTGAACGCGCTCCCGGCCGTGCACTACTACATCTGCATGTTCGGCGGCAGCGACGTGCGAGTGGCCGACTACGCCATCTACGGCTCGCCGGAGCTGGCTGCCAATGTCGCCAAGGCCCTTGAGGGACGCACCGCGGCCCTCATGAGCAACCACGGCTCCGTGGTGGCCGGCCCGGACCTGGCCTCCACCTATGTCCTGACCCAGGAGCTGGAGTGGGTCTGCGAGCTCTACCTGCGCACACTCGCCGTCGGCAGCCCCAAGATCCTCACCGATGAGCAGATCGAGGCGGTCGCGTGCAAGATCCGGGACACCGGCTACGGTCAGCACGCCCCGGCCGAGGAGAGCTGA","MLLNDARQQIADACSHLSDDGLVVGTAGNLSVREGDLVAITPSGLPYQEMRPDLVAVVEYATGKQVEGPLKPASELDLHLTALRATGQMAVVHTHSYAATTVASLEGVNALPAVHYYICMFGGSDVRVADYAIYGSPELAANVAKALEGRTAALMSNHGSVVAGPDLASTYVLTQELEWVCELYLRTLAVGSPKILTDEQIEAVACKIRDTGYGQHAPAEES$","L-fuculose phosphate aldolase","Cytoplasm","L-fuculose phosphate aldolase","L-fuculose phosphate aldolase ","class II aldolase/adducin family protein","","Dreyer M.K., Schulz G.E. The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli. J. Mol. Biol. 1993. 231(3):549-553. PMID: 8515438Dreyer M.K., Schulz G.E. Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J. Mol. Biol. 1996. 259(3):458-466. PMID: 8676381Rabinovich P.M., Beburov M.I.u., Linevich Z.K., Stepanov A.I. Amplification of the riboflavin operon genes of Bacillus subtilis in Escherichia coli cells. Genetika 1978. 14(10):1696-1705. PMID: 102560","","","

InterPro
IPR001303
Domain

Class II aldolase/adducin, N-terminal
G3DSA:3.40.225.10	$\"[1-202]T$	no description
PF00596	$\"[8-200]T$	Aldolase_II

noIPR
unintegrated

unintegrated
PTHR22789	$\"[77-221]T$	FUCULOSE PHOSPHATE ALDOLASE

","BeTs to 16 clades of COG0235COG name: Ribulose-5-phosphate 4-epimerase and related epimerases and aldolasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0235 is aompkzyqv-rlb-efghs-ujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB001303 (Class II aldolase/adducin, N-terminal) with a combined E-value of 9.2e-08. IPB001303A 38-62 IPB001303B 78-96 IPB001303D 151-166","Residues 20-114 are 66% similar to a (ALDOLASE ISOMERASE 4-EPIMERASE II CLASS PHOSPHATE LYASE ADDUCIN L-FUCULOSE L-RIBULOSE-5-PHOSPHATE) protein domain (PD001906) which is seen in Q829J0_STRAW.Residues 126-190 are 67% similar to a (ALDOLASE LYASE PHOSPHATE L-FUCULOSE ADDUCIN II CLASS ZINC METAL-BINDING RHAMNULOSE-1-PHOSPHATE) protein domain (PD530461) which is seen in Q829J0_STRAW.","","-57% similar to PDB:1DZX L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT R212A (E_value = 5.8E_32);-57% similar to PDB:1DZY L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E214A (E_value = 5.8E_32);-57% similar to PDB:1FUA L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T (E_value = 5.8E_32);-57% similar to PDB:2FUA L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT (E_value = 5.8E_32);-57% similar to PDB:3FUA L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K (E_value = 5.8E_32);","Residues 8 to 200 (E_value = 1.1e-47) place ANA_0444 in the Aldolase_II family which is described as Class II Aldolase and Adducin N-terminal domain.","","phosphate aldolase (fucA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0445","466317","468149","1833","5.11","-23.80","67555","TTGCGCTCACATCGATGTGGGTCCTGGTCATCGTCGCCCAGTGAAAGGAAACTTGCCATGTCCGCTGCGTCCTACCCCGCCATCGGAATCCGTCCCCTCATTGACGGACGTCGTCGTGGCGTGAGGGAGTCCCTCGAGGACAAGACCGCTCAGCTGGCCAAGGACGTCGCCGAGCTCATCTCCTCGCGCCTGACCTACCCCGACGGCAGCCCGGTGCGCTGCGTCGTCTCCGAGACCGCGATCGGGGGCGTGGCCGAGGCCAACCGCTGCAAGGAGCAGTTCCGCACCGAGAACGTGTGTGCCGACCTGACCGTCACCGCCTCCTGGAACTACATCACCGAGGTCCTTGACCTCGACCCCTCCATCCCGCACGCCATCTGGGGCTTCAACGGCACTGAGCGCCCCGGGGCCGTGACCCTGGCCGCCGCGGCCGCCGCCTACAACATGCTGGGCATTCCCTGCTTCGGCATCTACGGCCACGACGTGCAGGACGCCGACGACTCGGGCCTGACCGAGGACGTCGTCGAGAACATCCTGCGCTACGTGCGCGCCGCCCTGGGGGTCGGCCTCATGAAGGGGCGCAGCTACCTCTCGATCGGGACCGTCTCCATGGGGATCGCCGGCTGCCGCGTCCCCGAGCAGTTCTTCGTCGACTACCTGGGCATGCGCGCCGAGTACATCGACATGATCGAGATCGACCGCCGTATCGCCCACGGCATCTACGACCACCAGGAGTACGAGACCGCCCTGGCCTGGGCCCGGGAGCACCTCACCATCGGGGAGAACCGCAACCCGGAGGCCAACCGCTTCACCCAGGAGGAGTACGACGGGCAGTTCGACTACTGCATCAAGATGCTCCTCATCGGACGCGACCTCATGGAGGGCAACCCCGCCCTGGCCGAGCTGGGCTTCGTCGAGGAGGCTGAGGGCCACGACGCCATTGCGGCGGGCTTCCAGGGGCAGCGTCAGTGGACGGACTACAAGCCCAACGGCGACATCCTCGAGACCTTCCTCAACACCACCTTCGACTGGAACGGCAAGCGGCCCGAGAAGGTCTTCGCCACGGAGGGCGACGCCGGCAACGCCGTGGCCATGCTCTTCAACTCCGTCCTGACCCACCGTCCTCAGCTCTTCAGTGACGTGCGCACCTACTGGAGCCCCGAGGCCGTTGAGCGGGTCACCGGTTACAAGCTCGAGGGGCGCGCCGAGAACGGCTTCATCGACCTGCGCAACTCCGGGGCCACCACCCTCAACGCCACCGGCCAGGAGAAGGACGCCGAGGGCAACCCCATCATCAAGCACTGGTGGGAGATCACCGAGGCGGACATCGAGGCGGATCTGAAGGCCTCCACTTTCCATGCCGCCACCCGCGAGTACTTCCCCGGAGGCGGCTTCTCCACGCACTTCACCACCGCCGGCAACATGCCCGTCACTGCGACCCGCCTGAACTTCGTGGCCGGCCAGGGGCCGGTCCTCCAGATCTCCGAGGGCTGGACCGTGGAGCTGCCCGACGACGTGCGCGACCAGATCGTCAACCGTACCGACCCGACGTGGCCGACGACCTTCTTCGTCCCGCGCCTGACCGGCGAGGGCGCCTTCACCTCCGTCTACGACTGGATGGCCAACTGGGGCGCCAACCACACGGCCACCGGCTACGGGCACTTCGGCGCCGACCTCATCACCCTGGCATCGATGCTGCGCATCCCCGTCTACATGCACAACGTCGAGCGCGAGAGGATCCTGCGCCCCAAGGCCTGGGTGCCCTTCGGTACCGCCGAGCCCGAGAGCGCTGACTTCCGGGCCTGCGCCACCTTCGGTCCTCTCTACCGCTGA","LRSHRCGSWSSSPSERKLAMSAASYPAIGIRPLIDGRRRGVRESLEDKTAQLAKDVAELISSRLTYPDGSPVRCVVSETAIGGVAEANRCKEQFRTENVCADLTVTASWNYITEVLDLDPSIPHAIWGFNGTERPGAVTLAAAAAAYNMLGIPCFGIYGHDVQDADDSGLTEDVVENILRYVRAALGVGLMKGRSYLSIGTVSMGIAGCRVPEQFFVDYLGMRAEYIDMIEIDRRIAHGIYDHQEYETALAWAREHLTIGENRNPEANRFTQEEYDGQFDYCIKMLLIGRDLMEGNPALAELGFVEEAEGHDAIAAGFQGQRQWTDYKPNGDILETFLNTTFDWNGKRPEKVFATEGDAGNAVAMLFNSVLTHRPQLFSDVRTYWSPEAVERVTGYKLEGRAENGFIDLRNSGATTLNATGQEKDAEGNPIIKHWWEITEADIEADLKASTFHAATREYFPGGGFSTHFTTAGNMPVTATRLNFVAGQGPVLQISEGWTVELPDDVRDQIVNRTDPTWPTTFFVPRLTGEGAFTSVYDWMANWGANHTATGYGHFGADLITLASMLRIPVYMHNVERERILRPKAWVPFGTAEPESADFRACATFGPLYR$","L-fucose isomerase","Cytoplasm","L-fucose isomerase","L-fucose isomerase ","L-fucose isomerase","","Seemann J.E., Schulz G.E. Structure and mechanism of L-fucose isomerase from Escherichia coli. J. Mol. Biol. 1997. 273(1):256-268. PMID: 9367760","","","

InterPro
IPR001759
Family

Pentaxin
PS00289	$\"[4-11]?$	PENTAXIN

InterPro
IPR004216
Domain

L-fucose isomerase, C-terminal
G3DSA:3.20.14.10	$\"[360-609]T$	no description
PF02952	$\"[375-573]T$	Fucose_iso_C

InterPro
IPR005763
Family

L-fucose isomerase
TIGR01089	$\"[23-610]T$	fucI: L-fucose isomerase

InterPro
IPR012888
Domain

L-fucose isomerase, N-terminal_1
G3DSA:3.40.50.1070	$\"[20-194]T$	no description
PF07881	$\"[23-193]T$	Fucose_iso_N1

InterPro
IPR012889
Domain

L-fucose isomerase, N-terminal_2
G3DSA:3.40.275.10	$\"[195-359]T$	no description
PF07882	$\"[194-374]T$	Fucose_iso_N2

","BeTs to 3 clades of COG2407COG name: L-fucose isomerase and related proteinsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2407 is ----kz--v-----e--h--------Number of proteins in this genome belonging to this COG is 1","***** IPB012889 (L-fucose isomerase, N-terminal_2) with a combined E-value of 1.6e-163. IPB012889A 27-59 IPB012889B 123-171 IPB012889C 201-252 IPB012889D 311-365 IPB012889E 402-436 IPB012889F 457-499 IPB012889G 519-573","Residues 28-368 are similar to a (ISOMERASE L-FUCOSE METABOLISM FUCOSE 3D-STRUCTURE 5.3.1.- MANGANESE L-FUCULOSE) protein domain (PD043614) which is seen in Q8DN24_STRR6.Residues 317-384 are 57% similar to a (L-FUCOSE ISOMERASE ISOMERASE) protein domain (PD677111) which is seen in Q9WYE3_THEMA.Residues 383-610 are 75% similar to a (ISOMERASE L-FUCOSE METABOLISM FUCOSE 3D-STRUCTURE 5.3.1.- MANGANESE L-FUCULOSE) protein domain (PD539624) which is seen in Q8DN24_STRR6.","","-69% similar to PDB:1FUI L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI (E_value = );-57% similar to PDB:1IOF X-RAY CRYSTALLINE STRUCTURES OF PYRROLIDONE CARBOXYL PEPTIDASE FROM A HYPERTHERMOPHILE, PYROCOCCUS FURIOSUS, AND ITS CYS-FREE MUTANT (E_value = );-57% similar to PDB:1IOI x-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, pyrococcus furiosus, and its cys-free mutant (E_value = );-57% similar to PDB:1X10 Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192A) from a Hyperthermophile, Pyrococcus furiosus (E_value = );-57% similar to PDB:1X12 Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192D) from a Hyperthermophile, Pyrococcus furiosus (E_value = );","Residues 23 to 193 (E_value = 2.9e-90) place ANA_0445 in the Fucose_iso_N1 family which is described as L-fucose isomerase, first N-terminal domain.Residues 194 to 374 (E_value = 9.4e-93) place ANA_0445 in the Fucose_iso_N2 family which is described as L-fucose isomerase, second N-terminal domain.Residues 375 to 573 (E_value = 3.7e-91) place ANA_0445 in the Fucose_iso_C family which is described as L-fucose isomerase, C-terminal domain.","","isomerase (fucI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0446","468162","469631","1470","5.05","-20.98","52053","ATGACGAGCACCGACGAGCACCACGTCCTTGCCCTCGACCTCGGCTCCAGCTCTGTGCGAGCGGTCCTGGGGACCTACCGGCAGGGGGTCATCAGCACCGAGGAGGTCTTCCGCCTCCACCACCAGGCGGTGGACGACCACGGCACCCTCACCTGGGACCTCGAGCGCATCATGGATGGTGTTCGTCGGAGCATCGCCATGGCGACGCAGCGCCTGGGGCGGGTCCCCGACTCCATCGGCATCGACACCTGGGGAGTGGACTACGGCCTGCTCGACGCCCACGGAGAGCTGCTGCGCGCCCCGCGCGCCTACCGGGACCAGCGCATGGCCCGCTGGGCCGCAGACCTGGACCGGGCCCTCCCTGTGAAGACGGCTTGGAAAGAGACCGGCATCCTGCCCCAGCAGATCAACACGGTCTATCAGCTCTACGCGGACCTGAGGCAGGAGCCCGACCTCATCGATCGGGTGGATCGCTTCCTGCCCCTGCCCGACCTCGTGGCCTACCTGCTCGGCGCCCCCGCACAGGCGGGGCGGGCGATCGCCTCGACTACCGGGCTCGCCTCACCGGGGGCGCACGACTGGTCGGCTCCTGTGCTCCAGGCCGCCGGGATTCCTCAGGGGTGGATGCCCCCGCTCGTCGATGACGCCACGGTGGCCGGGACGACCCCGGAGGGGATCACCATCGTGCGTCCCGGCGGGCACGACACAGCCGGCGCCGTCCATGCGCTCGGTCTGGCCGCTGACGAGGTGCGCCTGTTCATCTCCTCAGGATCCTGGAGCCTCATCGGAGCCGCGGTTCCCAGCCCCGTCCTGGATGAAGCGGCGCTGCGGGCCGGACTGACCAACGAGGTGCGCACCGACGGAGGCATCCGGCTGCTGCGCAACCTCACCGGCTTCTGGCTGCTCCAGGAGTGCCAGCGAGCCTGGAACGAACCCGACACCGGTGCGCTGGTTGAGGCGGCGGGGGAGTGCGTCTCCCTCGGGGTCGTCATCGACCCCGATGATGAGCTCTTCGCCAGTCCCGGCGACATGCCGGAGAAGATCGCCCAGTGGTGCCGCAGTCACTACAAGGTGGCTCCCGAGGGGCCGGCGCAGACGGTCCGGCTCATCCTCGAGTCGCTCGCCTGCGCCCACGCCGCCTACGCCCAGGGGCTGCAGGGCGTCGTCGGCGACCAGCTGGACCCGGCAGCACCGATCCACCTGGTGGGAGGCGGTGCGCGCAACAGCCTCCTGCCGGCCATGACGGCGGCGGCCTGTCACCGTCAGGTCGTCGTGGGCACACCGGAGGCCAGTGCCCTGGGCAACATCCTCGCCCAGCTCGAGGCCGCCGACGTCCTCGACCCGAGCGCGCGCGGCGAGGTGCTGCGCCGCAGCATCCGCTCCGTGGAGGTCGAGGCCTCTGGGACCATCGCCGATCCCGATACCTTCGACGCCATGCGGGAACGGCTGGGCAATGCCACCGCCGACTGA","MTSTDEHHVLALDLGSSSVRAVLGTYRQGVISTEEVFRLHHQAVDDHGTLTWDLERIMDGVRRSIAMATQRLGRVPDSIGIDTWGVDYGLLDAHGELLRAPRAYRDQRMARWAADLDRALPVKTAWKETGILPQQINTVYQLYADLRQEPDLIDRVDRFLPLPDLVAYLLGAPAQAGRAIASTTGLASPGAHDWSAPVLQAAGIPQGWMPPLVDDATVAGTTPEGITIVRPGGHDTAGAVHALGLAADEVRLFISSGSWSLIGAAVPSPVLDEAALRAGLTNEVRTDGGIRLLRNLTGFWLLQECQRAWNEPDTGALVEAAGECVSLGVVIDPDDELFASPGDMPEKIAQWCRSHYKVAPEGPAQTVRLILESLACAHAAYAQGLQGVVGDQLDPAAPIHLVGGGARNSLLPAMTAAACHRQVVVGTPEASALGNILAQLEAADVLDPSARGEVLRRSIRSVEVEASGTIADPDTFDAMRERLGNATAD$","L-fuculokinase","Cytoplasm","rhamnulokinase","carbohydrate kinase; FGGY","carbohydrate kinase, FGGY","","Reizer A., Deutscher J., Saier Jr M.H., Reizer J. Analysis of the gluconate (gnt) operon of Bacillus subtilis. Mol. Microbiol. 1991. 5(5):1081-1089. PMID: 1659648","","","

InterPro
IPR000577
Family

Carbohydrate kinase, FGGY
PTHR10196	$\"[54-488]T$	XYLULOSE KINASE
PF00370	$\"[8-244]T$	FGGY_N

noIPR
unintegrated

unintegrated
PTHR10196:SF6	$\"[54-488]T$	RHAMNULOSE KINASE

","BeTs to 6 clades of COG1070COG name: Sugar (pentulose and hexulose) kinasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1070 is a----zy-v-rlbcef-h---j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB000577 (Carbohydrate kinase, FGGY) with a combined E-value of 3.2e-12. IPB000577A 8-25 IPB000577F 174-212 IPB000577J 399-447","Residues 9-141 are 61% similar to a (KINASE TRANSFERASE RHAMNULOKINASE L-FUCULOSE METABOLISM FUCOSE L-FUCULOKINASE RHAMNULOSE RHAMNOSE FUCK) protein domain (PD469501) which is seen in Q8XNL6_CLOPE.Residues 268-380 are similar to a (KINASE RHAMNULOKINASE TRANSFERASE RHAMNULOSE RHAMNOSE L-FUCULOSE METABOLISM FUCK CARBOHYDRATE FGGY) protein domain (PD895363) which is seen in Q9XAB1_STRCO.","","-51% similar to PDB:2CGJ CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN COMPLEX WITH L-FRUCTOSE AND ADP. (E_value = 1.2E_61);-51% similar to PDB:2CGK CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN AN OPEN UNCOMPLEXED CONFORMATION. (E_value = 1.2E_61);-51% similar to PDB:2CGL CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN COMPLEX WITH L-FRUCTOSE, ADP AND A MODELED ATP GAMMA PHOSPHATE. (E_value = 1.2E_61);","Residues 8 to 244 (E_value = 4.7e-09) place ANA_0446 in the FGGY_N family which is described as FGGY family of carbohydrate kinases, N-terminal domain.","","(fucK) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0447","469696","470124","429","4.96","-7.09","15799","ATGCTCCGCAACATTCCCGCCAACCTGTCACCCGAACTCGTCAAGATCCTGCTCGAGATGGGCCATGGGGACGAGATTCTCCTGGCCGATGCGAACTTCCCCGGCCACCACCTCCACCCCACTACAGTGCGGGCCGACGGCTTGGGGATTCCCGACCTGCTGCGGTCCATCCTCACTCTCATGCCCCTGGACCGCTACAGCAGCTACCAGGTGGCCCTCATGGAGACGGTGGGCGACGACCCTCGGCCTCCGGTGTGGGACGTCTACGAGCAGATCTGGAACGAGGCCGAGAAGGATGCCGGACCGGTGAACGTCAAGACGATTGAGCGCATGGCCTTCTACGACTACACCCCCAGCGTCTACGCCGTTGTCCTCACCGGGGAGACTGCCCTGTACGGCAATCTCATTCTCAAGAAGGGCGTGCTGTGA","MLRNIPANLSPELVKILLEMGHGDEILLADANFPGHHLHPTTVRADGLGIPDLLRSILTLMPLDRYSSYQVALMETVGDDPRPPVWDVYEQIWNEAEKDAGPVNVKTIERMAFYDYTPSVYAVVLTGETALYGNLILKKGVL$","Fucose transport protein","Cytoplasm","SI:zC217G15.2 (novel protein)","fucose operon protein FucU","RbsD or FucU transport","","Kim M.S., Oh H., Park C., Oh B.H. Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli RbsD, a component of the ribose-transport system with unknown biochemical function. Acta Crystallogr. D 2001. 57:728-730. PMID: 11320319","","","

InterPro
IPR007721
Family

RbsD or FucU transport
PF05025	$\"[5-142]T$	RbsD_FucU

","No hits to the COGs database.","***** IPB007721 (RbsD or FucU transport) with a combined E-value of 2.6e-28. IPB007721A 9-36 IPB007721B 50-61 IPB007721C 113-141","Residues 1-84 are 59% similar to a (PATHWAY ATU2016 FUCU MLR8491 SMB21302 DISSIMILATION AGR_C_3656P PLASMID FUCOSE) protein domain (PD407333) which is seen in Q7MJI4_VIBVY.Residues 1-142 are 62% similar to a (RIBOSE RBSD ABC AFFINITY HIGH PERMEASE TRANSPORTER FUCOSE OPERON FUCU) protein domain (PD021156) which is seen in Q97N90_STRPN.Residues 40-96 are 57% similar to a (ENRICHED PRODUCT:HYPOTHETICAL FULL LIBRARY PROTEIN SEQUENCE INSERT MUS MUSCULUS FULL-LENGTH) protein domain (PD786106) which is seen in Q6ZPD2_HUMAN.","","-53% similar to PDB:2OB5 Crystal structure of protein Atu2016, putative sugar binding protein (E_value = 8.8E_17);","Residues 5 to 142 (E_value = 2.2e-20) place ANA_0447 in the RbsD_FucU family which is described as RbsD / FucU transport protein family.","","(novel protein) (fucU)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0448","470124","471452","1329","9.28","12.19","47094","ATGACTGCGATCCGTGAGTCCGTGGCTGAGGAGGCCCCTGTCCGGGAGGGGACGGCCAAACGGGGGTTCCTGTATCCCGGCATGGTGCTGCCCTTCTGTCTGCTGGTCTCCTGCTTCGCCGCCTGGGGCCTGGCCGGAAACATGACCGATCCTCTGGTCAAGGTCTTCCGCTCCGTGTTCTCCATGAACAACTTCCAGTCCTCCTTGGTGCAGTCCGCCTACTACGGGGCCTACTTCTGCCTGGCGATCCCGGCGGCCTTCATCAACAGCCGCCTGGGCTACAAGGGCGGCGTCCTCATCGGGCTGGTGCTGGCGGGAACCGGCGGGCTCCTGTTCATCCCCGCGGCCTACGTCATGACCTACTCGGTGTTCCTGACCGCCCTGTTCACCCTGGCTGCCGGCCTGTCCATTCTGGAGACCAGCGCCAACCCCTTCGTCATGTCCATGGGGCCGGAGCGCAATGCCACTCGGCGCCTCAACTTCGCGCAGGCCTTCAACCCCATCGGCTCCAATCTGGGGGTGCTGCTGGCGGCCCTACTCATCCTGCCCAAGGTGAACCCGGCCACCGCCGAGCAGCGCAAGGCCATGAGCCACGAGGTGCTGCTGGCCACCCAGAGCGCAGAGCTCAAGGCGGTCATGGGCCCCTATGTCGCCCTCGGGCTCCTCTACATCCTGCTGGCCGTCATGATCGGCCGGGTCAAGGTCGTGGAGAGGCCGGTGGAATCGGCTGCGGGTGACAGCGGCGGGCCGGGCAGGCTCGCGCGCCTGCTGCGCAACAAGCGCTACAGCTTCGGGGTGGTGGCGCAGTACTTCAACGTCTCCGCCCAGACCTGTATCTGGACATACACCCTGCACTACGTCACAGATGCCCTGGGGGTGTCGGACAAGATCGCCGGATACTGGTTGCAGGCGAGTCTCATCGTCTTCCTGGTCTTCCGGTTCCTCATGGTGGGTCTCATGGGGCGGTTTGATGCACGCAAGCTGCTTCTGCTCATGTGCTCCCTCGGGGTCGGCCTGTCCCTGTTCGCCATGGTGAGCGTCAACATTCTGGGGGTGCTGGCCATTGTCTCCCTGTCGGCGTGCATCTCCCTGCTGTTCCCCACTATCTACGGCGAGGCCCTCCTTGGGCTGGGGGAGGACACTAAGTTCGGGGCCGCCGGCCTGGTCATGGCCATCATCGGCGGAGCCACCATGCCACTGGTGCAGAGCTACATCATGGACAAGACGTCTCCTGCGGTGTCCTACATCACGGTAGCCGGGTGCTTCGTGGTGGTGGCCGCCTACGGGGTCTACACGCTGCGCACGCCCAGGCCCGTCAGCGCCTCCTGA","MTAIRESVAEEAPVREGTAKRGFLYPGMVLPFCLLVSCFAAWGLAGNMTDPLVKVFRSVFSMNNFQSSLVQSAYYGAYFCLAIPAAFINSRLGYKGGVLIGLVLAGTGGLLFIPAAYVMTYSVFLTALFTLAAGLSILETSANPFVMSMGPERNATRRLNFAQAFNPIGSNLGVLLAALLILPKVNPATAEQRKAMSHEVLLATQSAELKAVMGPYVALGLLYILLAVMIGRVKVVERPVESAAGDSGGPGRLARLLRNKRYSFGVVAQYFNVSAQTCIWTYTLHYVTDALGVSDKIAGYWLQASLIVFLVFRFLMVGLMGRFDARKLLLLMCSLGVGLSLFAMVSVNILGVLAIVSLSACISLLFPTIYGEALLGLGEDTKFGAAGLVMAIIGGATMPLVQSYIMDKTSPAVSYITVAGCFVVVAAYGVYTLRTPRPVSAS$","L-fucose permease","Membrane, Cytoplasm","L-fucose permease","K02429 MFS transporter; FHS family; L-fucose permease","L-fucose transporter","","Pervaiz S., Brew K. Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science 1985. 228(4697):335-337. PMID: 2580349Flower D.R., North A.C., Attwood T.K. Mouse oncogene protein 24p3 is a member of the lipocalin protein family. Biochem. Biophys. Res. Commun. 1991. 180(1):69-74. PMID: 1834059Flower D.R., North A.C., Attwood T.K. Structure and sequence relationships in the lipocalins and related proteins. Protein Sci. 1993. 2(5):753-761. PMID: 7684291Flower D.R. Multiple molecular recognition properties of the lipocalin protein family. J. Mol. Recognit. 1995. 8(3):185-195. PMID: 8573354","","","

InterPro
IPR002345
Domain

Lipocalin
PS00213	$\"[292-304]?$	LIPOCALIN

InterPro
IPR005275
Family

L-fucose permease
TIGR00885	$\"[28-432]T$	fucP: L-fucose:H+ symporter permease

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[35-181]T$	MFS_1

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[22-42]?$ $\"[72-90]?$ $\"[92-112]?$ $\"[118-138]?$ $\"[159-181]?$ $\"[212-230]?$ $\"[262-280]?$ $\"[299-319]?$ $\"[328-350]?$ $\"[356-378]?$ $\"[383-403]?$ $\"[413-433]?$	transmembrane_regions

","BeTs to 6 clades of COG0738COG name: Fucose permeaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0738 is ------y-----b-e--hsnuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 265-425 are 59% similar to a (TRANSPORTER TRANSMEMBRANE PERMEASE MEMBRANE SUGAR GLUCOSE/GALACTOSE INNER FAMILY FUCOSE FACILITATOR) protein domain (PD381343) which is seen in Q9RQ10_BACTN.Residues 62-123 are 64% similar to a (TRANSMEMBRANE RESISTANCE TRANSPORTER MULTIDRUG MEMBRANE EFFLUX FACILITATOR MAJOR FAMILY PERMEASE) protein domain (PD203898) which is seen in Q8X6R7_ECO57.Residues 62-115 are 64% similar to a (TRANSMEMBRANE TRANSPORTER SUGAR RESISTANCE FAMILY MEMBRANE MULTIDRUG FACILITATOR MAJOR PROBABLE) protein domain (PD000082) which is seen in Q7NVU4_CHRVO.Residues 74-137 are 67% similar to a (PERMEASE L-FUCOSE TRANSPORTER GLUCOSE/GALACTOSE FUCOSE SUGAR INNER MEMBRANE PROBABLE GLUCOSE-GALACTOSE) protein domain (PD187524) which is seen in Q7MJI1_VIBVY.Residues 138-235 are 72% similar to a (PERMEASE TRANSPORTER GLUCOSE/GALACTOSE FUCOSE L-FUCOSE SUGAR TRANSMEMBRANE INNER MEMBRANE GLUCOSE-GALACTOSE) protein domain (PD518938) which is seen in Q7MJI1_VIBVY.Residues 265-425 are 59% similar to a (TRANSPORTER TRANSMEMBRANE PERMEASE MEMBRANE SUGAR GLUCOSE/GALACTOSE INNER FAMILY FUCOSE FACILITATOR) protein domain (PD381343) which is seen in Q9RQ10_BACTN.","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 407 (E_value = 5.8e-07) place ANA_0448 in the MFS_1 family which is described as Major Facilitator Superfamily.","","permease (fucP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0449","472563","471565","999","6.23","-4.70","34542","GTGTCCACACGCGTGACCCTTAGTGACGTGGCCGAGGCAGTCGGAGTCTCAGCGCAGACCGTCTCCCGCGTGCTCAACAACCACCCGTCGGTCCGTCCCGAGACACGTCAGAAGGTTCTGGCGGCCGTTCAGGCACTGGGCTATGAGCCGAATCTCGCCGCCCGTTCGCTGGCCTCGGGATCCTCCGGGGCCGTGGGAATCCTGCTGACGGCCGGGCTGTCGCACGGGATGGCCTCCACCTTCTCCGCGATCGCCAGGGCGGTGCGCGAGCGGGGGGACACCTTCGTCCTGGCCACTGCCGAGGGCGGCGACCCGGAGTCCGTGCGACAGGCACTGGCCCACCTGCACGGTCACCGCGTGGCGACCATCGTGGTCCTGGCCCAGCGCGCCGACGTCCTGGCCATCCTCTCGTCCCAGCGCCACCGCGGTCCGATCGTGGCCATCATCTCGGGGCAGCACGAGTTCTCCGAGCTGGCCACCGTCTCCATCGACCAGGCCCTGGGAGCCAGGCTGGCCACGGAGCATCTTCTGGATCAGGGGCGCAGCCGCCTGCTGCACGTCACCGGGGACCTGTCCTGGCAGGACGCCTCGGAGCGCCTGGCCGCCTACCAGTCGGCGTGCGCACAGGCCGGGGTTCCCGGCCGCTGGGTGGGCACGGACGCCTGGACGGGAGAGGCCGGGGCCAAGGTCGCCAGGCGCCTGCTCGACAGCGGTCTGCCCGACGCCGTCTTCGCCGCCAACGACGACATCGCCCTGGGGCTGTGCCATGAGCTGCTCGCCGCCGGCGTGAGGATCCCCGACGACGTCGCCGTCGTCGGCTTCGATGACATCCCGCTGGCACGTTGGGCGACCCCGTCCCTGTCCAGCGTCACGCAGGACTTCGACGCCCTGGGACGGGCCGCACTGAGCCTGTCCGACGAGATCGTCGAGGGTGCCCCCACCCGCAGTGTCTGCCTGGAGCCAACGCTCGTCGTCAGGGCGTCATCAACCAAGGCCTAG","VSTRVTLSDVAEAVGVSAQTVSRVLNNHPSVRPETRQKVLAAVQALGYEPNLAARSLASGSSGAVGILLTAGLSHGMASTFSAIARAVRERGDTFVLATAEGGDPESVRQALAHLHGHRVATIVVLAQRADVLAILSSQRHRGPIVAIISGQHEFSELATVSIDQALGARLATEHLLDQGRSRLLHVTGDLSWQDASERLAAYQSACAQAGVPGRWVGTDAWTGEAGAKVARRLLDSGLPDAVFAANDDIALGLCHELLAAGVRIPDDVAVVGFDDIPLARWATPSLSSVTQDFDALGRAALSLSDEIVEGAPTRSVCLEPTLVVRASSTKA$","Transcriptional regulator, LacI family","Cytoplasm, Membrane","CEBR protein","K02529 LacI family transcriptional regulator","Alanine racemase","","Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 1992. 267(22):15869-15874. PMID: 1639817Vartak N.B., Reizer J., Reizer A., Gripp J.T., Groisman E.A., Wu L.F., Tomich J.M., Saier Jr M.H. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 1991. 142(9):951-963. PMID: 1805309","","","

InterPro
IPR000843
Domain

Bacterial regulatory protein, LacI
PR00036	$\"[6-16]T$ $\"[16-26]T$	HTHLACI
PF00356	$\"[5-30]T$	LacI
SM00354	$\"[4-74]T$	HTH_LACI
PS50932	$\"[5-59]T$	HTH_LACI_2
PS00356	$\"[7-25]?$	HTH_LACI_1

InterPro
IPR001761
Domain

Periplasmic binding protein/LacI transcriptional regulator
PF00532	$\"[62-328]T$	Peripla_BP_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[5-62]T$	no description
G3DSA:3.40.50.2300	$\"[164-303]T$	no description

","BeTs to 9 clades of COG1609COG name: Transcriptional regulators of the LacI familyFunctional Class: KThe phylogenetic pattern of COG1609 is ------V-EBrH---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 60-244 are 46% similar to a (TRANSCRIPTIONAL REGULATOR LACI FAMILY) protein domain (PD984285) which is seen in Q9AAM4_CAUCR.Residues 65-105 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR OPERON FAMILY LACI REGULATOR) protein domain (PD000947) which is seen in Q6AA58_PROAC.Residues 252-308 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR FAMILY LACI OPERON REGULATOR) protein domain (PD539176) which is seen in Q6AA58_PROAC.Residues 254-386 are 46% similar to a (TRANSCRIPTIONAL REGULATOR LACI FAMILY) protein domain (PDA0X7N9) which is seen in Q6AAK2_PROAC.Residues 317-384 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR FAMILY LACI OPERON REGULATOR) protein domain (PD000591) which is seen in Q6AA58_PROAC.","","-49% similar to PDB:2O20 Crystal structure of transcription regulator CcpA of Lactococcus lactis (E_value = 1.5E_29);-47% similar to PDB:1EFA CRYSTAL STRUCTURE OF THE LAC REPRESSOR DIMER BOUND TO OPERATOR AND THE ANTI-INDUCER ONPF (E_value = 1.7E_28);-47% similar to PDB:1JWL Structure of the Dimeric lac Repressor/Operator O1/ONPF Complex (E_value = 1.7E_28);-47% similar to PDB:1JYE Structure of a Dimeric Lac Repressor with C-terminal Deletion and K84L Substitution (E_value = 1.7E_28);-47% similar to PDB:1JYF Structure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion. (E_value = 1.7E_28);","Residues 60 to 85 (E_value = 9.4e-11) place ANA_0449 in the LacI family which is described as Bacterial regulatory proteins, lacI family.Residues 117 to 383 (E_value = 3.5e-06) place ANA_0449 in the Peripla_BP_1 family which is described as Periplasmic binding proteins and sugar binding domain of the LacI family.","","protein ","","1","","","Fri Aug 10 16:39:51 2007","","Fri Aug 10 16:39:51 2007","","","Fri Aug 10 16:39:51 2007","Fri Aug 10 16:39:51 2007","Fri Aug 10 16:39:51 2007","","","Fri Aug 10 16:39:51 2007","","","Fri Aug 10 16:39:51 2007","Fri Aug 10 16:39:51 2007","Fri Aug 10 16:39:51 2007","","Fri Aug 10 16:39:51 2007","Fri Aug 10 16:39:51 2007","","","","","yes","","" "ANA_0450","472678","473265","588","6.02","-5.70","20240","ATGAGCCTGGCCGTCTACCCCGGAAGCTTCGATCCCCTCACCCTGGGGCATGTCGACATCGTCGCCCGTGCGACCACGCTCTTCGACGTCGTCGTCATCGGGATCGCCCACAACGCCGCCAAGGTCGGGCGCCACCTGCTCGACGTCCACGAACGCCTCCACCTGGCCAGGGAGGCCACCTCCCACCTGTCCGGCGTCGAGGTGGACATCGTCCCCGGGCTCCTGGCCGACTACTGCAGCCGGTGCGGGGCGAGCGCCATCATCAAGGGCCTGCGCAACGGCAGCGACCTGGATGCCGAGCTGCCCATGGCCCTGCTCAACCGCGACCTGGGGGCGCCCGAGACGGTCTTTCTGCCTGCGTCCGCCGCCTACGCGCACATCTCCTCCTCCCTCGTCAAGGACGTCGCGGGCTACGGCCGAGACGTCTCCGCCCTCGTGCCGCCCGCTGTGGCCCACGCCTTGGAGGTTCGGCTGTCCCAGGCCCCCGGGTCTGCAGCCCACGACGGCGTGGACTCAGGACTCATCCCGCCCGGGACCCCGCCAAGCCGCTTCGTCGGCGCCGACCACACTCGAGAGGACCTACCGTGA","MSLAVYPGSFDPLTLGHVDIVARATTLFDVVVIGIAHNAAKVGRHLLDVHERLHLAREATSHLSGVEVDIVPGLLADYCSRCGASAIIKGLRNGSDLDAELPMALLNRDLGAPETVFLPASAAYAHISSSLVKDVAGYGRDVSALVPPAVAHALEVRLSQAPGSAAHDGVDSGLIPPGTPPSRFVGADHTREDLP$","Phosphopantetheine adenylyltransferase","Cytoplasm","Phosphopantetheine adenylyltransferase(Pantetheine-phosphate adenylyltransferase) (PPAT)","phosphopantetheine adenylyltransferase ","pantetheine-phosphate adenylyltransferase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR001980
Family

Coenzyme A biosynthesis protein
PR01020	$\"[2-20]T$ $\"[20-41]T$ $\"[87-103]T$ $\"[113-135]T$	LPSBIOSNTHSS
TIGR01510	$\"[3-158]T$	coaD_prev_kdtB: pantetheine-phosphate adeny

InterPro
IPR004820
Domain

Cytidylyltransferase
PF01467	$\"[5-135]T$	CTP_transf_2

InterPro
IPR004821
Domain

Cytidyltransferase-related
TIGR00125	$\"[3-65]T$	cyt_tran_rel: cytidyltransferase-related do

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[1-159]T$	no description

noIPR
unintegrated

unintegrated
PTHR21342	$\"[1-163]T$	PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE

","BeTs to 15 clades of COG0669COG name: Phosphopantetheine adenylyltransferaseFunctional Class: HThe phylogenetic pattern of COG0669 is -----qvcebrhuj--ol---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 4-138 are similar to a (ADENYLYLTRANSFERASE TRANSFERASE NUCLEOTIDYLTRANSFERASE PHOSPHOPANTETHEINE PPAT BIOSYNTHESIS A PYROPHOSPHORYLASE DEPHOSPHO-COA COENZYME) protein domain (PD004081) which is seen in COAD_DEIRA.","","-68% similar to PDB:1OD6 THE CRYSTAL STRUCTURE OF PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE FROM THERMUS THERMOPHILUS IN COMPLEX WITH 4'-PHOSPHOPANTETHEINE (E_value = 1.9E_38);-64% similar to PDB:1TFU phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis (E_value = 8.5E_34);-66% similar to PDB:1VLH Crystal structure of Phosphopantetheine adenylyltransferase (TM0741) from Thermotoga maritima at 2.20 A resolution (E_value = 1.1E_33);-59% similar to PDB:1O6B Crystal structure of phosphopantetheine adenylyltransferase with ADP (E_value = 6.9E_28);-66% similar to PDB:1B6T PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH 3'-DEPHOSPHO-COA FROM ESCHERICHIA COLI (E_value = 4.5E_27);","Residues 5 to 135 (E_value = 1e-19) place ANA_0450 in the CTP_transf_2 family which is described as Cytidylyltransferase.","","adenylyltransferase (Pantetheine-phosphate adenylyltransferase) (PPAT) (Dephospho-CoApyrophosphorylase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0451","473292","473813","522","5.03","-8.30","18758","CTGCTGCGCATCCTCGATGAGCTCGACGAGCTCATCAGCAACGCCCGATCCATGCCGATGAGCGCCTCGGCGATCGTCAACCGGGAGAACGCCCTGCACCTCATCGATCGGGCTCGCGACGCGGTTCCGACCGCCGTCCGTCGCGCCGAGAAGATCGTCTCCGATGCCGACGCCGTCCTGGCTGAGGGGCGGGCCGAGTCCGAGCGTCTCGTCCAGTACGCCCAGGAGGAGTCCGAGCGTCTCGTGGCTGGGGAGAACATCGTGCGCATGGCCAATGACCGGGCTGACAGTATCGTGGCTGCGGCGGAGGACAAGGCCGCCTCCCTGCGTCACGGGGCCGATGAGTACTCCGACCGCACTCTGGCCTCCCTGGAGGCCGAGGTCGCCAAGGTCGCCGAGCAGATCCGCGCCGGCCGTGAGGTCCTGGCCGGTCGCCTGGGGGACGGCGCGGGGCAGCCGGTGGAGATCCAGGAGCCCGTCCGCCGCCGTTCGGCCTGGTCCGTGGACCCCTCCGCCCACTGA","LLRILDELDELISNARSMPMSASAIVNRENALHLIDRARDAVPTAVRRAEKIVSDADAVLAEGRAESERLVQYAQEESERLVAGENIVRMANDRADSIVAAAEDKAASLRHGADEYSDRTLASLEAEVAKVAEQIRAGREVLAGRLGDGAGQPVEIQEPVRRRSAWSVDPSAH$","ATPase subunit","Cytoplasm","Archaeal/vacuolar-type H+-ATPase subunit H","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG1390COG name: Archaeal/vacuolar type H+-ATPase subunit EFunctional Class: CThe phylogenetic pattern of COG1390 is amtky----------------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","H+-ATPase subunit H (coiled-coil)","","1","","","Fri Aug 10 16:44:17 2007","","Fri Aug 10 16:44:17 2007","","","Fri Aug 10 16:44:17 2007","Fri Aug 10 16:44:17 2007","Fri Aug 10 16:44:17 2007","","","","","","Fri Aug 10 16:44:17 2007","","","","Fri Aug 10 16:44:17 2007","Fri Aug 10 16:44:17 2007","","","","","yes","","" "ANA_0452","473997","474587","591","4.30","-28.73","21018","ATGCCAGGACTCATCGTCGATATCGTCGACCTGCCCCGTGCCACCGGCTCGGTCAAGAACCTGCAGATCCGCACCCCCGCCCCCGCCGACCTGGGCACCGAGGTCATCGGTGTGCCCGAGGGCAGCGACCTCGCCCTCGACGTCACCCTGACCGCCATGGACGACGGCGTCCTGGCACATGCCGACGCCGACCTGCACGTCCACGGCGAGTGCGTGCGCTGCCTGCGCGACCTCGATGAGGACCGCAGCGTGAGGATCGACGAGCTCTACCTCTTCCCCGAGGTCATCGAGGCCCAGCGGGCCGAAGGCGATGAGGAGGCCGAGGGCCTCCTGGCGGTGGGGGAGACCACCCTGGACCTCGAACCGGCGCTGCGCGACGCCCTGGTGCCCACGCTGCCCTTCCAGCCCCTGTGTCGCCCCGACTGCCCCGGACTGTGCCCCGACTGCGGTAAGCGGCTCGAGGACCTACCCGCCGACCACCACCACGAGGTCCTTGACCCGCGCTGGTCCGCCCTGGCCGGCCTGCTGGAGATCGACACCGGTCAGGAGGGCGAGCCGGACGCGCCCACGAGCGGGGAGGAACAGGCCTGA","MPGLIVDIVDLPRATGSVKNLQIRTPAPADLGTEVIGVPEGSDLALDVTLTAMDDGVLAHADADLHVHGECVRCLRDLDEDRSVRIDELYLFPEVIEAQRAEGDEEAEGLLAVGETTLDLEPALRDALVPTLPFQPLCRPDCPGLCPDCGKRLEDLPADHHHEVLDPRWSALAGLLEIDTGQEGEPDAPTSGEEQA$","Metal-binding, possibly nucleic acid-binding protein","Cytoplasm","Uncharacterized ACR, COG1399","hypothetical protein","protein of unknown function DUF177","","","","","

InterPro
IPR003772
Family

Protein of unknown function DUF177
PF02620	$\"[13-177]T$	DUF177

","BeTs to 6 clades of COG1399COG name: Predicted metal-binding, possibly nucleic acid-binding proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1399 is -------qvdr-bcefghsn------Number of proteins in this genome belonging to this COG is 1","***** IPB003772 (Protein of unknown function DUF177) with a combined E-value of 1.2e-11. IPB003772B 69-74 IPB003772C 103-146","Residues 1-59 are 64% similar to a (METAL-BINDING PROTEIN PREDICTED) protein domain (PDA0T0E0) which is seen in Q6A7R4_PROAC.Residues 46-174 are 61% similar to a (PREDICTED YCED NUCLEIC YLBN-LIKE ACID-BINDING G30K POSSIBLY METAL-BINDING PROTEIN METAL-BINDING) protein domain (PD035384) which is seen in Q6AFJ6_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 177 (E_value = 3.6e-19) place ANA_0452 in the DUF177 family which is described as Uncharacterized ACR, COG1399.","","ACR, COG1399","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0454","474587","475381","795","5.64","-6.34","27926","ATGGCCAAGCGCCGCAGCGCTCCGCCCGCGCGCACCGACACCGAGGCCCTCGTCTACCGCTGGGGGCCGAGCATTGATGCCCAGCTGCTCGATCTGGCCCTGACCCACCGTTCCTACGCCCACGAGAACGGCGGCCTGCCCACCAACGAGCGTCTGGAGTTCCTGGGCGACTCCGTCCTGGGCATCATCGTCACCGAGTACCTCTACCGCACCCACCCGGAGGTCCCCGAGGGCCAGCTCGCCAAGATGCGCGCCGCCACCGTCTCCGAGCCGGCCCTGGCCGCCGTCGCCCGCGACCTGGGGCTGGGGGAATTCATCAAGCTCGGCAAGGGCGAGGCGCTCTCGGGCGGGCGGGACAAGGACTCCATCCTGTCCGACACGGTCGAGGCCCTCATCGGCGCCACCTACCTCACCCACGGCCTGGAGGAGACCCGCACGGTCGTCACCCGGCTCGTCTCCCGCTTCCTGGACTCGGCCCGCACCCGCGGCGCGGGCCTGGACTGGAAGACGAGCCTCCAGGAGCTCACCGCCGTCCACCAGCTCGGCAACCCCGCCTACGAGGTCACCGGAACCGGCCCCGACCACCAGCGGGTCTTCACCGCCAGCGCCATCGTTGACGGCGAGGTCCTGGGGCAGGGCACCGGCAGCTCGAAGAAGGTTGCCGAGCATGACGCCGCCGAGGCCGCCTACGCCGCCATCCTGGCCGCCCGGGGCGACGGCGGCCTCAACCTGCCCGGAGTCAATGAGGCCCTACGCGCCGACCTGCTCACCGGGCAGGGCTCCCAGACGAGCTGA","MAKRRSAPPARTDTEALVYRWGPSIDAQLLDLALTHRSYAHENGGLPTNERLEFLGDSVLGIIVTEYLYRTHPEVPEGQLAKMRAATVSEPALAAVARDLGLGEFIKLGKGEALSGGRDKDSILSDTVEALIGATYLTHGLEETRTVVTRLVSRFLDSARTRGAGLDWKTSLQELTAVHQLGNPAYEVTGTGPDHQRVFTASAIVDGEVLGQGTGSSKKVAEHDAAEAAYAAILAARGDGGLNLPGVNEALRADLLTGQGSQTS$","Ribonuclease III","Cytoplasm","Ribonuclease III (RNase III)","ribonuclease III ","Ribonuclease III","","Nashimoto H., Uchida H. DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations. Mol. Gen. Genet. 1985. 201(1):25-29. PMID: 3903434Mian I.S. Comparative sequence analysis of ribonucleases HII, III, II PH and D. Nucleic Acids Res. 1997. 25(16):3187-3195. PMID: 9241229","","","

InterPro
IPR000999
Domain

Ribonuclease III
G3DSA:1.10.1520.10	$\"[26-159]T$	no description
PF00636	$\"[50-140]T$	Ribonuclease_3
SM00535	$\"[28-161]T$	RIBOc
PS50142	$\"[15-140]T$	RNASE_3_2
PS00517	$\"[50-58]T$	RNASE_3_1

InterPro
IPR001159
Domain

Double-stranded RNA binding
PF00035	$\"[168-233]T$	dsrm
SM00358	$\"[168-234]T$	DSRM
PS50137	$\"[167-235]T$	DS_RBD

InterPro
IPR011907
Family

Ribonuclease III, bacterial
TIGR02191	$\"[17-233]T$	RNaseIII: ribonuclease III

InterPro
IPR014720
Domain

Double-stranded RNA-binding-like
G3DSA:3.30.160.20	$\"[167-238]T$	no description

noIPR
unintegrated

unintegrated
PTHR11207	$\"[25-233]T$	RIBONUCLEASE III

","BeTs to 19 clades of COG0571COG name: dsRNA-specific ribonucleaseFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0571 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000999 (Ribonuclease III family) with a combined E-value of 1.1e-48. IPB000999A 29-38 IPB000999B 49-88 IPB000999C 123-140 IPB000999D 167-179 IPB000999E 213-226***** IPB001159 (Double-stranded RNA binding (DsRBD) domain) with a combined E-value of 2.9e-19. IPB001159A 28-39 IPB001159B 49-61 IPB001159C 213-226***** IPB005034 (Protein of unknown function DUF283) with a combined E-value of 1.4e-13. IPB005034N 45-97 IPB005034O 117-149 IPB005034M 111-156","Residues 8-219 are 64% similar to a (RIBONUCLEASE III) protein domain (PD730514) which is seen in Q8G7H1_BIFLO.Residues 16-169 are 70% similar to a (RIBONUCLEASE HYDROLASE III) protein domain (PD986004) which is seen in Q6A7R5_PROAC.Residues 20-142 are 82% similar to a (III RIBONUCLEASE HYDROLASE NUCLEASE ENDONUCLEASE RNA-BINDING RNASE HELICASE ATP-BINDING REPEAT) protein domain (PD002508) which is seen in Q82JT9_STRAW.Residues 23-219 are 47% similar to a (A464R HYDROLASE NUCLEASE RNA-BINDING ENDONUCLEASE) protein domain (PD060738) which is seen in A464_CHVP1.Residues 26-148 are 66% similar to a (RIBONUCLEASE HYDROLASE III) protein domain (PDA186C9) which is seen in Q74AX1_GEOSL.Residues 28-157 are 64% similar to a (RIBONUCLEASE DS RNA III HYDROLASE) protein domain (PD986001) which is seen in Q6F9C2_ACIAD.Residues 29-126 are 50% similar to a (P0456E05.12) protein domain (PDA191T6) which is seen in Q8LQJ0_EEEEE.Residues 33-136 are 57% similar to a (RIBONUCLEASE HYDROLASE III) protein domain (PDA1B7H3) which is seen in Q7UZQ5_PROMP.Residues 166-219 are 59% similar to a (III RIBONUCLEASE RNA-BINDING HYDROLASE RNASE NUCLEASE ENDONUCLEASE KINASE RNA BINDING) protein domain (PD515070) which is seen in Q6AFJ4_BBBBB.","","-72% similar to PDB:2A11 Crystal Structure of Nuclease Domain of Ribonuclase III from Mycobacterium Tuberculosis (E_value = 1.0E_60);-58% similar to PDB:1O0W Crystal structure of Ribonuclease III (TM1102) from Thermotoga maritima at 2.0 A resolution (E_value = 4.0E_33);-50% similar to PDB:1YYK Crystal structure of RNase III from Aquifex Aeolicus complexed with double-stranded RNA at 2.5-angstrom resolution (E_value = 1.5E_16);-50% similar to PDB:1YYW Crystal structure of RNase III from Aquifex aeolicus complexed with double stranded RNA at 2.8-Angstrom Resolution (E_value = 1.5E_16);-50% similar to PDB:1YZ9 Crystal structure of RNase III mutant E110Q from Aquifex aeolicus complexed with double stranded RNA at 2.1-Angstrom Resolution (E_value = 3.4E_16);","Residues 50 to 140 (E_value = 2.2e-46) place ANA_0454 in the Ribonuclease_3 family which is described as RNase3 domain.Residues 168 to 233 (E_value = 4.9e-16) place ANA_0454 in the dsrm family which is described as Double-stranded RNA binding motif.","","III (RNase III) (rnc)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0455","475381","476454","1074","7.27","1.23","38051","ATGCCAGAGCTGCCCGAGGTCGAGGTGGTGCGCGCCGGTCTCGCCCGGCACGTGGCCGGATGCACCGTCACCCGCGTCGAGGTCCTCGATCCGCGTCCGCTGCGCCGCCAGGACGGGGGAGCGCAGGCCTTCATCGACCAGCTCACCGGGCGCACCCTGACCGCGGCCGTCCGCCGCGGAAAGTTCCTGTGGCTGCCCCTGGACGACGGACGCGCCCTGTCGGCCCACCTGGGCATGAGCGGCCAGCTGCTCGTGCGCGGCACCACCGCGGACGCTTCTGACACTGCCCCGGAGCCCAACCGTGCCGCGGCCTTCCTGGCCGACCCGGACACTCTGCCCGGCGGGCGCCCAGCGGACCTGAGTGCTACCGAGCAACCCCGCTACGTGCGGGACATCTCCACCTCCGCTCGCCACCTGCGAGTGCGCCTCCACCTCAGCACCGACCGCGACGACGACGGCGACGATAACTGTGACAACGGCGCCGGCGCGGCGGTCCTCGACCTGGTCGACCAGCGCATGCTCGGCGGCCTGCACGTCGTCGACCTGACCCCCACCGCCGACGGCGCTCCCGGCGGGATGGGCGACCCGCGGCCGCTGCTGCCCGCCGACGCCACCCATATCGCCCGTGACCTGCTCGACCCGGCCCTGCAGCTGGCCGGCCCCACCGGCGTCGTCGCCCGGGTACGCGCCTCGAGGCGCGCCATCAAGACCCAGCTGCTCGACCAGGGACTCGTCTCGGGCATCGGCAACATCTACGCCGACGAGGGCCTGTGGGAGGCCGGGGTGCACGGCCTGCGCCCGGGAACCGGTCTCGGCCCGCGGGTGGTGGCCCGGATCCTCGAGTCCACCGCTGAGGTCATGCGCCGGGCCCTTGAGGTCGGTGGCACGAGCTTCGACGCCCTCTACGTCGATGTCGAGGGCGCCGCCGGGTTCTTCGCCCGAGAACTGGGCGCCTACGGGCGCCATGGGCTGGAGTGCCGCCGCTGCGGGGCCACCATGGCGCGTGAGACTCTGGGAGGTCGCTCTCACACCTACTGCCCCCGTTGCCAGACCCGTCCGCGCCGGCACCGGTAG","MPELPEVEVVRAGLARHVAGCTVTRVEVLDPRPLRRQDGGAQAFIDQLTGRTLTAAVRRGKFLWLPLDDGRALSAHLGMSGQLLVRGTTADASDTAPEPNRAAAFLADPDTLPGGRPADLSATEQPRYVRDISTSARHLRVRLHLSTDRDDDGDDNCDNGAGAAVLDLVDQRMLGGLHVVDLTPTADGAPGGMGDPRPLLPADATHIARDLLDPALQLAGPTGVVARVRASRRAIKTQLLDQGLVSGIGNIYADEGLWEAGVHGLRPGTGLGPRVVARILESTAEVMRRALEVGGTSFDALYVDVEGAAGFFARELGAYGRHGLECRRCGATMARETLGGRSHTYCPRCQTRPRRHR$","Formamidopyrimidine-DNA glycosylase","Cytoplasm, Extracellular","formamidopyrimidine-DNA glycosylase","formamidopyrimidine-DNA glycosylase ","formamidopyrimidine-DNA glycosylase","","O. Connor T.R., Graves R.J., de Murcia G., Castaing B., Laval J. Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role. J. Biol. Chem. 1993. 268(12):9063-9070. PMID: 8473347Duwat P., de Oliveira R., Ehrlich S.D., Boiteux S. Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein. Microbiology 1995. 141:411-417. PMID: 7704272","","","

InterPro
IPR000191
Family

Formamidopyrimidine-DNA glycolase
PD003680	$\"[235-296]T$	Q73VL9_MYCPA_Q73VL9;
PF01149	$\"[2-178]T$	Fapy_DNA_glyco
PF06831	$\"[207-302]T$	H2TH
TIGR00577	$\"[1-350]T$	fpg: formamidopyrimidine-DNA glycosylase

InterPro
IPR000214
Binding_site

Formamidopyrimidine-DNA glycolase, zinc-binding site
PS51066	$\"[317-351]T$	ZF_FPG_2
PS01242	$\"[326-350]T$	ZF_FPG_1

InterPro
IPR010663
Domain

Zinc finger, Fpg-type
PF06827	$\"[323-352]T$	zf-FPG_IleRS

InterPro
IPR012319
Domain

Formamidopyrimidine-DNA glycosylase, catalytic
PS51068	$\"[2-175]T$	FPG_CAT

noIPR
unintegrated

unintegrated
PTHR22993	$\"[226-357]T$	FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE
PTHR22993:SF4	$\"[226-357]T$	FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE (FAPY-DNA GLYCOSYLASE)

","BeTs to 11 clades of COG0266COG name: Formamidopyrimidine-DNA glycosylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0266 is ---------drlbcefghsn-j---wNumber of proteins in this genome belonging to this COG is 2","***** IPB000191 (Formamidopyrimidine-DNA glycolase) with a combined E-value of 1e-53. IPB000191A 1-16 IPB000191B 58-67 IPB000191C 73-85 IPB000191F 235-264 IPB000191G 318-350***** IPB010663 (FPG and IleRS zinc finger) with a combined E-value of 1e-40. IPB010663A 2-18 IPB010663B 73-85 IPB010663E 239-258 IPB010663F 318-350","Residues 1-68 are 56% similar to a (GLYCOSYLASE FORMAMIDOPYRIMIDINE-DNA HYDROLASE GLYCOSIDASE ZINC ZINC-FINGER F6D8.28 ATMMH-2 FAPY-DNA ATMMH-1) protein domain (PD868651) which is seen in Q6Z4R1_EEEEE.Residues 10-86 are 67% similar to a (GLYCOSYLASE GLYCOSIDASE HYDROLASE ZINC ZINC-FINGER FORMAMIDOPYRIMIDINE-DNA DNA REPAIR FAPY-DNA ENDONUCLEASE) protein domain (PD844922) which is seen in Q6AFJ3_BBBBB.Residues 235-296 are 69% similar to a (GLYCOSYLASE GLYCOSIDASE HYDROLASE ZINC ZINC-FINGER FORMAMIDOPYRIMIDINE-DNA DNA REPAIR FAPY-DNA ENDONUCLEASE) protein domain (PD003680) which is seen in Q73VL9_MYCPA.","","-41% similar to PDB:1L1T MutM (Fpg) Bound to Abasic-Site Containing DNA (E_value = 2.2E_27);-41% similar to PDB:1L1Z MutM (Fpg) Covalent-DNA Intermediate (E_value = 2.2E_27);-41% similar to PDB:1L2B MutM (Fpg) DNA End-Product Structure (E_value = 2.2E_27);-41% similar to PDB:1L2C MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex (E_value = 2.2E_27);-41% similar to PDB:1L2D MutM (Fpg)-DNA Estranged Guanine Mismatch Recognition Complex (E_value = 2.2E_27);","Residues 2 to 178 (E_value = 8.6e-40) place ANA_0455 in the Fapy_DNA_glyco family which is described as Formamidopyrimidine-DNA glycosylase N-terminal domain.Residues 207 to 302 (E_value = 8.1e-30) place ANA_0455 in the H2TH family which is described as Formamidopyrimidine-DNA glycosylase H2TH domain.Residues 323 to 352 (E_value = 3.7e-05) place ANA_0455 in the zf-FPG_IleRS family which is described as Zinc finger found in FPG and IleRS.","","glycosylase (mutM)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0456","476562","477215","654","5.39","-6.81","23575","ATGGCACACACCCCATCGTCGGAGATCGTCCGCGTCATGATCGTGGACGACCACGAGATCGTCCGTCGCGGCATCGCCGAGATCATTGACCGCGCTGATGGGCTCGACGTCGTCGCTGAGGCGGGTTCTCGGGCTGAGGCGGTGCGTCGGGCCGAGCTGGTCCGCCCCGACGTCATCCTCGTGGACCTCCAGCTGCCCGATGGCACCGGCATCGAGCTCATGCAGGAGCTGAGGGACTCCGTGCCCCAGGCCCTGCCGATCGTGCTGACCTCCTTCGACGACGACGAGGCCCTGGCCGAGGCCCTGGCGGCAGGTGCCCGGGCCTACCTGCTCAAGACGGTCCACGGTGCCGAGATCAGCGACGTCGTGCGGGCCGTCGCCTCCGGGCGCGTCCTGCTCGATGAGCGCACCGTGACGCGCCGCCGGGCGGACCACGACGACCCTACCGCCGACCTGACCAACGCCGAGCGCAAGGTCCTCGACCTCATCGGTGACGGCCTGTCCAACCGGGAGATCGGTGAGCGGCTCGGAGTCGCAGAGAAGACGGTTAAGAACCACATCACCTCCCTGCTGGCCAAGATGGGCTTGCAGCGACGCACGCAGGTCGCCGCCTGGGTCGCCGGTCAGCGGGCCTCAGGCTGGCGCAACAGCTGA","MAHTPSSEIVRVMIVDDHEIVRRGIAEIIDRADGLDVVAEAGSRAEAVRRAELVRPDVILVDLQLPDGTGIELMQELRDSVPQALPIVLTSFDDDEALAEALAAGARAYLLKTVHGAEISDVVRAVASGRVLLDERTVTRRRADHDDPTADLTNAERKVLDLIGDGLSNREIGERLGVAEKTVKNHITSLLAKMGLQRRTQVAAWVAGQRASGWRNS$","Two component transcriptional regulator, LuxR family","Cytoplasm","CprR","regulatory protein; LuxR:response regulator receiver","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[152-207]T$	Q82F87_STRAW_Q82F87;
PR00038	$\"[152-166]T$ $\"[166-182]T$ $\"[182-194]T$	HTHLUXR
PF00196	$\"[149-206]T$	GerE
SM00421	$\"[149-206]T$	HTH_LUXR
PS50043	$\"[145-210]T$	HTH_LUXR_2
PS00622	$\"[166-193]T$	HTH_LUXR_1

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[10-127]T$	Q9XA59_STRCO_Q9XA59;
PF00072	$\"[10-124]T$	Response_reg
SM00448	$\"[10-123]T$	REC
PS50110	$\"[11-127]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[147-212]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[10-131]T$	no description
PTHR23283	$\"[11-131]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF40	$\"[11-131]T$	TWO-COMPONENT SENSOR HISTIDINE KINASE BACTERIA

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 5.6e-20. IPB000792 152-198***** IPB000673 (CheB methylesterase) with a combined E-value of 2.1e-12. IPB000673A 13-22 IPB000673B 29-82***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 9.8e-12. IPB001867A 57-70 IPB001867B 85-129***** IPB005143 (Autoinducer binding domain) with a combined E-value of 1.8e-10. IPB005143B 152-195","Residues 10-127 are similar to a (SENSORY TRANSDUCTION PHOSPHORYLATION REGULATOR DNA-BINDING TRANSCRIPTION REGULATION RESPONSE TWO-COMPONENT KINASE) protein domain (PD000039) which is seen in Q9XA59_STRCO.Residues 152-207 are similar to a (DNA-BINDING TRANSCRIPTION REGULATION REGULATOR SENSORY PHOSPHORYLATION TRANSDUCTION RESPONSE TRANSCRIPTIONAL TWO-COMPONENT) protein domain (PD000307) which is seen in Q82F87_STRAW.","","-47% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 4.0E_22);-47% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 4.0E_22);-72% similar to PDB:1ZLK Crystal Structure of the Mycobacterium tuberculosis Hypoxic Response Regulator DosR C-terminal Domain-DNA Complex (E_value = 9.9E_13);-76% similar to PDB:1ZLJ Crystal Structure of the Mycobacterium tuberculosis Hypoxic Response Regulator DosR C-terminal Domain (E_value = 1.3E_12);","Residues 10 to 124 (E_value = 9.7e-24) place ANA_0456 in the Response_reg family which is described as Response regulator receiver domain.Residues 142 to 194 (E_value = 0.0049) place ANA_0456 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 149 to 206 (E_value = 2.5e-16) place ANA_0456 in the GerE family which is described as Bacterial regulatory proteins, luxR family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0457","479239","477263","1977","4.89","-35.29","69157","ATGGCGACCTCTTCGGAGGAGGATGCCGGAGCGGCGGGGCGCCTGGCCTACGCCGTCCACGCCGACCAGCTGGTCTCCACCCGTGGCCGCCGGGTGTCGGCCCTTCAGCCGAGCCTGGACGAGGCGACTGTCGCCCTCATCCAGGCGGCCCTGAGCCTCACCAGTTCCCTGCGGGTCCCCGACGCGCTGCGCCGTCTGGTGGAGTCGGCCTGCTCCATCACGGGTGCCTCGTGGGGAACCATCGCCGTGCTCAACCACGCGGACATGGATGTTGACCCGGCCGGCCCCCTCTCGCCCGATTCCTCCGGCGCGAGCTCGGGCACCGGTCTGTGCAGCGGGGTGCCCACGGCGACCCTCGATGAGCTCGCCCAGATGGCCGGCGCCCCCGATACCGCCGGCACTTCGCACGCCTCCTCTGAGTCCCTGCTCAACGGGCTCGAGGGAACCGGGATGGTCATCGACAACGACCTGGGCAGGGCCTCGGCCTTCACCGGTGCCATCGAGGGTGAGGAGACCGGCAGTCTGCTCTCGGCCCCGCTGCGCCTTCACGGCCAGGTCTACGGACATCTCTACCTGTGTGACAAGCCGGGGGGCTTCACCCGCTCGGACGCCGACGCCATCCTGACCCTGGCCCAGGCCGCAGCCGTCGCCGTGGAGAACGCCCGCCTGTACCGCGAGGCCCGTGACCGCGAGCAGTGGATGGTGGTCTCCCAGGAGCTGACGACGCTGCTGCTCTCGGGCGCCGAGGAGGATGACGCGCTGACGCTCATCGCCCACCGTGTCCGCCAGGTCGCTCACGCCGACACCGCCGCCCTCATCCTGCCCAGCATCGGGGAGCGCTGGATCTGCGAGATCGCCGACGGCGAGCACGCCCGGGAGCTGATCGGCACCTTCTTCCCGCCCGAGGGTCGGGCCCTGACCACCCTGGCCCATCAGACCGGCCTGGTCGTGGACTCCCTGGAGGACGCCTGGGGCGACGGCGACCTGATGGTCCCCCAGCTGGCCCAGTTCGGGCCGGCCCTCTACGCCCCCATGATCCACCGGGGGCGGGGCGTGGGGGTGATGCTGCTGCTGCGCTCCCCGGGTGCGGCGCCCTTCACCGCCCAGGACCTGGAGATCGCCGAGCTGGTGGCGGGGCAGGCCACGATGGCCTTCGAGCTGGCCGACGCCCAGCACGCCGAGGAGATGGCCACACTGCTCGATGAGCGGGCCCGGATCGGCCGGGACCTGCACGACCTGGCCATTCAGCAGCTCTTCGCCACCGGCATGCAGATCTCCGCGGCCCGGGAACGGCTGGCCTCCAGCACACAGGCGGACCTGGATGCGGTGTGCTCCGTGCTGAGCACCGCCCTGGAGGCGGTGGACGACTCCGTGGGCCAGATCCGCTCCATCGTGCGCTCCTTGCGTGATCGCGATGAGGAGGTCGGCGTGATCGAGCGGCTGCGGCGCGAGGCCTCCCTGGCCCGCAACGCCCTGGGCTACGCCCCCTCCCTGCTGCTGAGCGTCGACGGCCGGGGCCTGGCCCAGGTGGACCGCGACGAGGAGGACCGGCTCATCTCCTCGGTCGATGCCGCCGTCGCACCGGACATCGCCGACGACATGGTCGCTGTCGTACGTGAGGGACTGAGCAACGTGGCCCGTCATGCCCACGCCTCCTCGGTGACGGTGGACGTCAAGATCGAGGGGGTACAGCCGGGCTCGGAGCAGTGCTGCGGCCCCGGCGACGACGAGGGTCACGCCTCAGGCGACGCCGAGCCCTTCCGGGGCAGCCCGGTGGTGGAGATCGTCTGCCGTGACGACGGCGTCGGGGTGAATCCCTCCGTGACGCGCCGTTCGGGGACGGCCAACATGGCCGAGCGGGCCCGCCGTCACGGCGGCAGCTTCGTCATCGGTCCACGGGCCCGCTCCGACGGCGAGCGGCGCGGCACCTGCTTCACCTGGCGAGTGCCCTTGGACGGGGGCGGCCGGGTGCGCTGA","MATSSEEDAGAAGRLAYAVHADQLVSTRGRRVSALQPSLDEATVALIQAALSLTSSLRVPDALRRLVESACSITGASWGTIAVLNHADMDVDPAGPLSPDSSGASSGTGLCSGVPTATLDELAQMAGAPDTAGTSHASSESLLNGLEGTGMVIDNDLGRASAFTGAIEGEETGSLLSAPLRLHGQVYGHLYLCDKPGGFTRSDADAILTLAQAAAVAVENARLYREARDREQWMVVSQELTTLLLSGAEEDDALTLIAHRVRQVAHADTAALILPSIGERWICEIADGEHARELIGTFFPPEGRALTTLAHQTGLVVDSLEDAWGDGDLMVPQLAQFGPALYAPMIHRGRGVGVMLLLRSPGAAPFTAQDLEIAELVAGQATMAFELADAQHAEEMATLLDERARIGRDLHDLAIQQLFATGMQISAARERLASSTQADLDAVCSVLSTALEAVDDSVGQIRSIVRSLRDRDEEVGVIERLRREASLARNALGYAPSLLLSVDGRGLAQVDRDEEDRLISSVDAAVAPDIADDMVAVVREGLSNVARHAHASSVTVDVKIEGVQPGSEQCCGPGDDEGHASGDAEPFRGSPVVEIVCRDDGVGVNPSVTRRSGTANMAERARRHGGSFVIGPRARSDGERRGTCFTWRVPLDGGGRVR$","Two-component system sensor kinase","Cytoplasm","probable two-component sensor","putative signal transduction histidine kinase","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003018
Domain

GAF
PF01590	$\"[58-218]T$ $\"[249-385]T$	GAF
SM00065	$\"[58-228]T$ $\"[249-395]T$	GAF

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[529-652]T$	HATPase_c
SM00387	$\"[529-653]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[402-473]T$	HisKA_3

noIPR
unintegrated

unintegrated
G3DSA:3.30.450.40	$\"[39-233]T$ $\"[238-395]T$	no description

","BeTs to 3 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 3.1e-15. IPB011712A 401-418 IPB011712B 534-554","Residues 401-474 are 63% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM TRANSFERASE 2.7.3.- SENSORY TRANSDUCTION NITRATE/NITRITE) protein domain (PD288674) which is seen in Q9RI43_STRCO.Residues 539-650 are 41% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM SENSORY TRANSFERASE TRANSDUCTION 2.7.3.- TWO) protein domain (PD005700) which is seen in Q82FJ5_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 218 (E_value = 7.5e-08) place ANA_0457 in the GAF family which is described as GAF domain.Residues 249 to 385 (E_value = 0.00039) place ANA_0457 in the GAF family which is described as GAF domain.Residues 402 to 473 (E_value = 1.3e-13) place ANA_0457 in the HisKA_3 family which is described as Histidine kinase.Residues 529 to 652 (E_value = 1.1e-12) place ANA_0457 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","two-component sensor","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0458","481200","479374","1827","6.42","-3.67","63006","CTGTCCGCCGATGAGCGACGCTCCCTGCGCCGGGCAGTGGGCCTGCTGAACCTGGATCGCTCACGCTTCGCCCTGGCCGTAGTCGCCGGGACGGCGGGTATGGCCTCAGCCGTGGCCCTGTCCGGGGTGGCGGCCTGGCTCATTGCCAGGGCCTCACAGATGCCCGACGTCGTCGCGCTGGGGGTGGCGCCAGTGGCGGTGCGGCTCTTCGGCATCTCACGCTCCGTCCTGCGCTACTGCGAGAGGCTCGTCTCCCATGACACAGCCCTGCGAGGCATGGGCGCGCTGCGCACCCGCCTCTATGAGTCCCTGGCCTCAGCACGCACGGACACGGTTGCGGGCCTGCGCCGCGGCGACGTCCTGGCGCGAGTGGGCAGCGACATCGACGCGGTCGGGGACCTCGTCGTGCGCGCCTATCTGCCGGCGGCTGTCGCCGCCGTCCTGGGCGCGGCCACCAGCCTTGGTATCGCCCTGGTCTACTGGCCGGCAGGCCTCATCCTGCTGGCCTGTCTGCTGCTGTCAGGACTGGTGGGGCCGTTGGCCACCATCCGTTCGGCGAGAATCGCCGAGCAGGCCCGTCAGAGGCAGGCCACTGAGCTGTCCGCGGAGGTGCTGGCGGTCCTGGAGGGTGCTCCTGAGCTGACCGTCTCCGGACGTCTGGCCGGCTCGATGCGCCAGGTCGCCTCCCGGGAGGAGAGCCTGACCCGTCTGCGGGACCGGGCCGCGGTACCGGCCGCGATCGCAGCAGCCGTGGACGTGGCCGCCATGGGCCTGGCGGTCCTGGGCAACCTGGTAGTGGGGGTGAGCGCCGTCTCCGCCGGGCAGCTGGCCCCGGTCTGGCTGGCAGTGATCGTCCTGGTTCCACTGGCCGCCTTCGAAGCCACCTCCGCGCTCGGCCCGGCCAGCGTGCAGCTGGTGAGGTCGGCCGGCGCCGCCTGCCGCATCGTGGAGCTCATCGAGGCCGCTGAAGCCAGTGCCGCCAGCGGCTCCGCGATGTCCTCCGCGCCTCGGGAGCTGCCCGAGCCCTCCGCCCAGGGCCCGTACCTCAAGGCACGGGGCCTGGCGGTGGGCTGGCCGGGCGGCCCGGTGGTGGCCGAGGGCATCGACCTGGATCTGCGGGTCGGTCGCCGAGTGGCGATCGTGGGGCCGTCGGGGATCGGCAAGTCGACACTGCTGGCCACGCTGGCGGGGCTGCTGGAGCCTCGGGGCGGCACGCTGACACTCGACGGCGTCCCCCCGTGGCAGGCGGCCCACTCAGAGGTGGCGGCCCGGGTGTGCCTGACCGCGGAGGACGCGCACGTCTTCCACACCAGCGTCCTGGAGAACCTGCGCGTGGCGCGCGGGGACGTCACCCCCGCCGAGGCCGGCGAGCTGCTGAGCCGGACCGGCCTGGGGAGGTGGCTCGAGGCTCTTCCCGAGGGAGTTGAGACCATCATCGGCACCGATGCCACAACGCTGTCCGGTGGGGAGCGGCGTCGGCTCCTGCTCGCCCGCGCCCTGGCGGCTCCGGCTCCCCTGATGCTGCTGGACGAGCCCGGTGAGCATCTCGATGCCCTCACCGCGGACCGGCTCGTGACCGACCTGCTGACAGCGGGCGACCAGGGCCGCGGCACTCTCCTGGTCACCCATCGTCTCAGCGCCCTGGAGCACGCAGACGAGGTCCTTGTCATGGGGCACCGGTCGTATGCCACCGGTGAGCAGGCCCCGGCGACTATCCTAAATCGAGGCAGCCACCGCGAGCTCCAGGACGTCTCCGAGATCTACCGGTGGTCGCTTTCCCAGGAGGATCAGGACAGGCAGCAGGACCACGTTTCCGGTACGAGCTGA","LSADERRSLRRAVGLLNLDRSRFALAVVAGTAGMASAVALSGVAAWLIARASQMPDVVALGVAPVAVRLFGISRSVLRYCERLVSHDTALRGMGALRTRLYESLASARTDTVAGLRRGDVLARVGSDIDAVGDLVVRAYLPAAVAAVLGAATSLGIALVYWPAGLILLACLLLSGLVGPLATIRSARIAEQARQRQATELSAEVLAVLEGAPELTVSGRLAGSMRQVASREESLTRLRDRAAVPAAIAAAVDVAAMGLAVLGNLVVGVSAVSAGQLAPVWLAVIVLVPLAAFEATSALGPASVQLVRSAGAACRIVELIEAAEASAASGSAMSSAPRELPEPSAQGPYLKARGLAVGWPGGPVVAEGIDLDLRVGRRVAIVGPSGIGKSTLLATLAGLLEPRGGTLTLDGVPPWQAAHSEVAARVCLTAEDAHVFHTSVLENLRVARGDVTPAEAGELLSRTGLGRWLEALPEGVETIIGTDATTLSGGERRRLLLARALAAPAPLMLLDEPGEHLDALTADRLVTDLLTAGDQGRGTLLVTHRLSALEHADEVLVMGHRSYATGEQAPATILNRGSHRELQDVSEIYRWSLSQEDQDRQQDHVSGTS$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","CydC","K06148 ATP-binding cassette; subfamily C; bacterial","ABC transporter, transmembrane region, type 1","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[375-558]T$	ABC_tran
PS50893	$\"[349-584]T$	ABC_TRANSPORTER_2
PS00211	$\"[486-500]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[374-561]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[24-307]T$	ABC_TM1F

InterPro
IPR014223
Family

ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC
TIGR02868	$\"[9-545]T$	CydC: ABC transporter, CydDC cysteine expor

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[312-592]T$	no description
PTHR19242	$\"[20-557]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF55	$\"[20-557]T$	ABC TRANSPORTER (CYDD)
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[25-47]?$ $\"[57-77]?$ $\"[139-157]?$ $\"[163-183]?$ $\"[242-262]?$	transmembrane_regions

","BeTs to 19 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: RThe phylogenetic pattern of COG1132 is ---KYQVCEBRHUJGP--inXNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 31-162 are similar to a (ATP-BINDING ABC TRANSPORTER CYDC COMPONENT TRANSPORTER TRANSMEMBRANE PROBABLE PERMEASE ATPASE) protein domain (PD008283) which is seen in Q740N7_MYCPA.Residues 39-133 are 56% similar to a (ATP-BINDING ABC TRANSPORTER CYDD COMPONENT TRANSPORTER CYTOCHROME-RELATED INNER MEMBRANE PROBABLE) protein domain (PD860030) which is seen in Q6AEW5_BBBBB.Residues 378-574 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 380-586 are 45% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 390-618 are 41% similar to a (LANTIBIOTIC SYSTEM MERSACIDIN TRANSPORTER) protein domain (PDA0G5T2) which is seen in Q7UG09_RHOBA.Residues 396-444 are 67% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q889G0_PSESM.Residues 398-584 are 49% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 401-584 are 51% similar to a (ATP-BINDING SECRETION PROBABLE ABC TOXIN TRANSPORTER) protein domain (PDA0C7R3) which is seen in Q7UXT8_RHOBA.","","-44% similar to PDB:1JJ7 Crystal Structure of the C-terminal ATPase domain of human TAP1 (E_value = 1.7E_18);-45% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 4.1E_17);-45% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 4.1E_17);-43% similar to PDB:2IXF CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT) (E_value = 1.2E_16);-45% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 7.7E_16);","Residues 404 to 587 (E_value = 6.7e-42) place ANA_0458 in the ABC_tran family which is described as ABC transporter.",""," ","","1","","","Fri Aug 10 16:50:05 2007","","Fri Aug 10 16:50:05 2007","","","Fri Aug 10 16:50:05 2007","Fri Aug 10 16:50:05 2007","Fri Aug 10 16:50:05 2007","","","Fri Aug 10 16:50:05 2007","","","Fri Aug 10 16:50:05 2007","Fri Aug 10 16:50:05 2007","Fri Aug 10 16:50:05 2007","","Fri Aug 10 16:50:05 2007","Fri Aug 10 16:50:05 2007","","","","","yes","","" "ANA_0459","483023","481284","1740","6.29","-5.15","60949","ATGCGTTACGCACGCTCCGCCCGCCGATACATTGCCGCCACTGCCGTCACTGGGATGGTGACCGCCGTGCTGGTGGTGGCTCAGGCCTTCCTCATCTCCGGTGCGGTCTCCTCGGTCATCTCCGAGGGGGCTGCACCGTCGGCTGTCAGGGCACTGGCGGTGGCGCTGGGTGGGGTCCTGGCGGCTAGGGCCCTGGTGGTCCTGCTTCAGGAGGTTCATGCCCACCGGTCCGCCACGGAGACCATCGTCGAGCTGCGCCGGCAGGTTCTGGAGCACGCAGCCCGGCTGGGCCCCCGCTGGCAGGCGATTCATGGGACGCAGACGGCCACGTTGCTGACTCGCGCGTTGGACGACCTCGAGCCCTATTTCACCCGCTACCTTCCCCAGCTGGTGTTGGCCTCGACGGTGACACCGGCTACGGTGCTGGTGCTTCTCACCCAGGACTGGTCTGCCGCGGTGGCCGTGGTGTGCACCTTGCCCCTCATTCCGATCTTCATGATTCTCATCGGCAGGATGACCCAGTCCGTCTCCCAGGAGCGCCTCAAGACCATGCAGGTCCTGGGCGATCAGGTACTCGATCTCATCTCGGGCCTGCCCACGCTCAAGGCCCTCGGGCGCGAGCAGGAACCGGCCGAGCAGGTGCGCTCCCTGGGCCGCTCCTACCGGCGCACCACCATGTCGACCTTGCGGGTCGCCTTCCTGTCGGGGGCGGTCTTGGAGTTCATCACGACGCTGTCGGTGGCGATCATCGCCGTCCAGATCGGTTTCCGGCTCGTGGCCGGACGGATGGATCTGTTCACCGGCCTGCTCGTCCTCATGGTGGCCCCTGAGGTCTATCAGCCGCTGCGGCAGGTGGGTTTCCAGTTCCACGCCTCGGCCAACGGGGTGGCGGCGGCGAACGCCGTCTTCGAGGTTCTTCAGACCCCGGTGCCCGAGCACGGCGACCTGCCGGCTCCCGACCTGCGCTCATCGACGATTGAGATCGATGGGGTGTCCGTCGCCTCCCGGGGCGCGTGGGCCCCCGCCGGGCTCAGTGCCTCGATCCGGCCGGGCAGCCTGGTGGCGCTGACCGGCCCGTCAGGTGCGGGCAAGACGACGACGACGCAGGTCCTCCTCGGCCTGCTGCCCCCCGACCGGGGGCGGGTGCGTCTCATGCCCGACGGCGGCGATCCCGGCACCGCGGTCGACCTCGCCCAGATCGATCCGGTTACCTGGTGGGAGCAGATCGCCTGGGTACCCCAGCGCCCCACCATCACCCCGGGCACGGTGCTGGACAACGTCCTGGATCATGCCGAGCCGGGCGCCTCCACAGCAGAGGGCATCCCCGACGTACTGGTCGAGGCGGCCCGTGCCACGGGCTTCGATGAGGTCGTGAACGGCCTGCCGCAGGGCTGGCAGACCCCGGTGGGCAGCGCAGGAGTGGGTTTGTCCGTGGGGCAGCGCCAGCGTCTGGCCCTGACCAGAGCCCTGTGCTCGACGGCGCCCTTGGTGGTCATGGACGAGCCGACCGCGCACCTGGACGCGGCCAGTGAGGCCCACGTCCTGGACGCCGTCCGTGCGCTGCACGCCTCGGGGCGCACAGTGGTGGTCATTGCGCACCGTCCCGCACTCATGGCCCTGGCCGAGCAGACCATCGCCGTGACGAGCCAACCGGTGCCGCCGGCGGACCTCGCACCTGACCGGGTACCTGACCAGGTATCTGCCCATGAGGCGGCGACGGTGCAGGAGGATGCCCTGTGA","MRYARSARRYIAATAVTGMVTAVLVVAQAFLISGAVSSVISEGAAPSAVRALAVALGGVLAARALVVLLQEVHAHRSATETIVELRRQVLEHAARLGPRWQAIHGTQTATLLTRALDDLEPYFTRYLPQLVLASTVTPATVLVLLTQDWSAAVAVVCTLPLIPIFMILIGRMTQSVSQERLKTMQVLGDQVLDLISGLPTLKALGREQEPAEQVRSLGRSYRRTTMSTLRVAFLSGAVLEFITTLSVAIIAVQIGFRLVAGRMDLFTGLLVLMVAPEVYQPLRQVGFQFHASANGVAAANAVFEVLQTPVPEHGDLPAPDLRSSTIEIDGVSVASRGAWAPAGLSASIRPGSLVALTGPSGAGKTTTTQVLLGLLPPDRGRVRLMPDGGDPGTAVDLAQIDPVTWWEQIAWVPQRPTITPGTVLDNVLDHAEPGASTAEGIPDVLVEAARATGFDEVVNGLPQGWQTPVGSAGVGLSVGQRQRLALTRALCSTAPLVVMDEPTAHLDAASEAHVLDAVRALHASGRTVVVIAHRPALMALAEQTIAVTSQPVPPADLAPDRVPDQVSAHEAATVQEDAL$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","CydD","ABC transporter; ATP-binding protein CydD","ABC transporter, transmembrane region, type 1","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[10-252]T$	ABC_membrane

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[476-515]T$	Q9HWG7_PSEAE_Q9HWG7;
PF00005	$\"[351-550]T$	ABC_tran
PS50893	$\"[326-575]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[350-552]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[12-294]T$	ABC_TM1F

InterPro
IPR014216
Family

ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD
TIGR02857	$\"[7-547]T$	CydD: ABC transporter, CydDC cysteine expor

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[288-552]T$	no description
PTHR19242	$\"[1-545]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF55	$\"[1-545]T$	ABC TRANSPORTER (CYDD)
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[149-169]?$ $\"[231-251]?$	transmembrane_regions

","BeTs to 19 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 13","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 5e-35. IPB005074C 340-387 IPB005074D 464-507 IPB005074E 527-547***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.6e-17. IPB010509B 351-376 IPB010509D 471-515 IPB010509E 525-555***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 6.2e-14. IPB013563A 340-374 IPB013563C 473-500***** IPB005116 (TOBE domain) with a combined E-value of 7.6e-14. IPB005116A 358-374 IPB005116C 476-489 IPB005116D 496-515***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.6e-08. IPB010929K 338-382 IPB010929M 473-519 IPB010929D 492-520","Residues 162-290 are similar to a (ATP-BINDING ABC TRANSPORTER CYDD TRANSPORTER COMPONENT TRANSMEMBRANE PERMEASE MEMBRANE PROBABLE) protein domain (PD688989) which is seen in Q8NRA4_CORGL.Residues 306-459 are 48% similar to a (ATP-BINDING/PERMEASE FUSION ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I2L4) which is seen in Q7NX92_CHRVO.Residues 306-533 are 42% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 309-427 are 50% similar to a (ATP-BINDING PROTEIN CYDCD) protein domain (PDA1B3E1) which is seen in Q6ABD5_PROAC.Residues 310-547 are 43% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 311-554 are 43% similar to a (ATP-BINDING) protein domain (PD727310) which is seen in Q8FQ82_COREF.Residues 320-507 are 47% similar to a (ATP-BINDING/PERMEASE ABC TOXIN TRANSPORTER ATP-BINDING PLASMID) protein domain (PD416779) which is seen in Q82YJ4_ENTFA.Residues 321-550 are 48% similar to a (HLYB SECRETION ABC PROTEIN TOXIN FAMILY ATP-BINDING TRANSPORTER) protein domain (PD727846) which is seen in Q8E9W6_SHEON.Residues 326-547 are 44% similar to a (COMPONENT ATPASE ABC- TYPE ABC-TYPE PERMEASE MULTIDRUG/PROTEIN/LIPID TRANSPORTER ATP-BINDING SYSTEM) protein domain (PDA185P6) which is seen in Q8NRA4_CORGL.Residues 337-534 are 46% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 343-384 are 78% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9YD57_AERPE.Residues 344-534 are 44% similar to a (LANTIBIOTIC SYSTEM MERSACIDIN TRANSPORTER) protein domain (PDA0G5T2) which is seen in Q7UG09_RHOBA.Residues 344-535 are 41% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 347-533 are 43% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 347-545 are 48% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 407-549 are 52% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I0J1) which is seen in Q83A70_COXBU.Residues 461-534 are 64% similar to a (ATP-BINDING TRANSPORTER ABC RESISTANCE TRANSMEMBRANE SIMILAR MULTIGENE POLYMORPHISM FAMILY GLYCOPROTEIN) protein domain (PD250423) which is seen in Y742_STRCO.Residues 461-534 are 71% similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PDA0I0J5) which is seen in Q7P0D6_CHRVO.Residues 461-543 are 56% similar to a (APRD ATP-BINDING) protein domain (PDA0I303) which is seen in Q89EV0_BRAJA.Residues 476-515 are 82% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9HWG7_PSEAE.","","-57% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 4.5E_23);-57% similar to PDB:2FF7 The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state (E_value = 4.5E_23);-45% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 5.9E_23);-45% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 5.9E_23);-57% similar to PDB:2FFB The crystal structure of the HlyB-NBD E631Q mutant in complex with ADP (E_value = 1.0E_22);","Residues 10 to 282 (E_value = 3.6e-12) place ANA_0459 in the ABC_membrane family which is described as ABC transporter transmembrane region.Residues 351 to 550 (E_value = 1.1e-43) place ANA_0459 in the ABC_tran family which is described as ABC transporter.","","(ATP-) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0460","484247","483114","1134","7.22","0.78","40609","ATGACACTGAGCATCCTCTGGTTCATCCTCATCGCCGTCCTGTGGATCGGTTACCTCACGCTGGAGGGCTTCGACTTCGGCGTCGGCATGATCCTGAAGATCCTGGGCCGCGACGAGCGCGAGCGGCGCGCGACGCTGTCCACCATCGGCCCCCACTGGGACGGTAACGAGGTGTGGCTGCTGACCGCCGGCGGGGCGACCTTCGCCGCCTTCCCCGAGTGGTACTCCACCCTGTTCTCCGGGGCCTACGTCGTCCTGTTCATCATTCTGCTGTGCCTCATCGTGCGCGTATGCGCCATCGAGTGGCGTCCCAAGGTCAACTCCCAGACCTGGCGCGACCGCTGGGACTGGGTCCACACGATCAGCGCCTGGCTGCCTTCCATCCTGTGGGGCGTGGCCTTCGCGAACCTGGTTCAGGGCATGCACATCGAGGTCGTCCAGACCTCCAACGGCGCCGTCGTCCCGGCCTCCCAGGTGCCGGCCGACTCCCTGGTGCCCGGTGCCGCCCACCAGATCACCGGGGGCCTGCTCACGATGGTGACCCCCTTCACCCTGCTGGGCGGCGTCGTCACCTGCCTGCTCTTCCTCAACCACGGTGCGCTCTTCGTGGCGCTCAAGACCACTGGGGATCTGTCGCAGCGCGCGCTGGGGATGTCACGCCGGCTCGCCCCGGCGGCCACCGCGGTCACCGCCGCCTGGGCCCTGTGGGCGCAGCTGGCCTACTCGGGCAGCGCTCTGTCCTGGATTCCGCTGGTCGTCGCCGCTGCTGGACTCATTGGCTCCCTGCTCATGGGACGCACTGGGAAGGAGGGACGGGCCTTCGCCCTGCACTTTGTGGGGATTGCCTTCGCCGTCGTCTTCATCTTCGCCGCGATGGCCCCCAACGTCATGCGCTCCTCGGTGGACCCGGCCTACTCGCTGACGATCCAGCAGGCCGCGAGCGCCGACACGACCCTGCTCATCATGAGCGTCGCCGCGGCGGTGTTCGTCCCCGGGGTCCTGGCCTACACGATCTGGAGCTACAAGGTCTTCGCCTCGCGCATCAGCGTCGAGAGCATCGACCCCGACCAGGGCGGTCTGCACCCCACGCTGGTGCGTGACTCGGCTCAGCCCGAGGCGCACTTCGGGTACTGA","MTLSILWFILIAVLWIGYLTLEGFDFGVGMILKILGRDERERRATLSTIGPHWDGNEVWLLTAGGATFAAFPEWYSTLFSGAYVVLFIILLCLIVRVCAIEWRPKVNSQTWRDRWDWVHTISAWLPSILWGVAFANLVQGMHIEVVQTSNGAVVPASQVPADSLVPGAAHQITGGLLTMVTPFTLLGGVVTCLLFLNHGALFVALKTTGDLSQRALGMSRRLAPAATAVTAAWALWAQLAYSGSALSWIPLVVAAAGLIGSLLMGRTGKEGRAFALHFVGIAFAVVFIFAAMAPNVMRSSVDPAYSLTIQQAASADTTLLIMSVAAAVFVPGVLAYTIWSYKVFASRISVESIDPDQGGLHPTLVRDSAQPEAHFGY$","Cytochrome bd ubiquinol oxidase subunit II","Membrane, Cytoplasm","cytochrome d ubiquinol oxidase, subunit II","putative cytochrome D ubiquinol oxidase subunit II ","cytochrome d ubiquinol oxidase, subunit II","","Sturr M.G., Krulwich T.A., Hicks D.B. Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a delta cyo delta cyd strain complemented by genes from Bacillus firmus OF4. J. Bacteriol. 1996. 178(6):1742-1749. PMID: 8626304Juty N.S., Moshiri F., Merrick M., Anthony C., Hill S. The Klebsiella pneumoniae cytochrome bd' terminal oxidase complex and its role in microaerobic nitrogen fixation. Microbiology 1997. 143:2673-2683. PMID: 9274021","","","

InterPro
IPR003317
Family

Cytochrome bd ubiquinol oxidase, subunit II
PF02322	$\"[1-349]T$	Cyto_ox_2
TIGR00203	$\"[1-361]T$	cydB: cytochrome d ubiquinol oxidase, subun

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[74-94]?$ $\"[115-135]?$ $\"[176-196]?$ $\"[217-237]?$ $\"[243-263]?$ $\"[273-293]?$ $\"[319-339]?$	transmembrane_regions

","BeTs to 12 clades of COG1294COG name: Cytochrome bd-type quinol oxidase, subunit 2Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1294 is -o-----q--rlbcefgh--ujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB003317 (Cytochrome bd ubiquinol oxidase, subunit II) with a combined E-value of 1.4e-85. IPB003317B 39-56 IPB003317C 68-102 IPB003317D 108-139 IPB003317E 173-189 IPB003317F 306-348","Residues 2-221 are 66% similar to a (SUBUNIT CYTOCHROME II OXIDASE D UBIQUINOL OXIDOREDUCTASE OXIDASE 1.10.3.- TERMINAL) protein domain (PD005057) which is seen in Q8KBG8_CHLTE.","","-43% similar to PDB:1SKY CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3 (E_value = );","Residues 1 to 349 (E_value = 1.5e-109) place ANA_0460 in the Cyto_ox_2 family which is described as Cytochrome oxidase subunit II.","","d ubiquinol oxidase, subunit II (cydB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0461","485825","484269","1557","7.46","1.30","56655","ATGGCCATCTCTCCCATGGCGCTGGACTCTCTGGATCTGGCGCGCTGGCAGTTCGGTATCACCACCGTCTACCACTTCATCCTGGTTCCGCTGACCATCGGACTGTCGCCGCTGGTGGCTCTCATGGAGACGCTCTGGCGCAGGACCGGCAACAAGCAGTGGCTCGTGGCCACCAAGTTCTTCGGCAAGATCCTACTCATCAACTTCGCGCTCGGTGTGGCCACCGGCATCGTTCAGGAGTTCCAGTTCGGCATGAACTGGTCGGAGTACTCCAGGTTCGTCGGCAACATCTTTGGCGCCCCCCTCGCCTTCGAGGCCCTGCTGGCCTTCTTCATGGAGTCCGTCTTCCTGGGCCTGTGGATCTTCGGATGGGACCGCCTGTCCCCCAGGTTGCACAACCTGTGCATGTGGGCCGTGGCCGCCGGCACGAACTTCTCCGCCTTCTTCATCCTTACCGCCAACTCCTGGATGCAGCACCCGGTGGGCGCCGTCGTCAACCCCAAGACGGGCCGCGCCGAGCTCGATGGCGTGAGCGGCTTCCTCAAGCTCCTGTCCAACGAGCTGGTGTGGGCCACCGTGCTGCATGTCATCTCCTCGGCTCTGCTGGTGGCCGCAGCCGTCGTCATGGGCGTGTCCGTGTGGTGGATGGTCAAGGCCGCCCAGGCCAAGCAGGACTTCGAGGCGCGTGAGCTGTGGCGGCGGGTCGCCCGTTTCGGGGCCGTCACCATGGTGGCCGCGGGTCTGGTCACCGCCGGCACCGGCCACATGCAGGGTCAGCTGGTCGCCGAGTACCAGCCGGGCAAGATGGCCGCTGCCGAGGGGCTGTGCCACACCGAGGCCGGAGCCCCCTTCACCGTGGCCGCCTTCGGGGACTGCAAGAACGAGGACGGCATGGTCCGGTTCATCTCGGTTCCCGGTGTCTACTCCTTCATGGCCACCAATGACTTCAACGCCGAGGTCACCGGACTCAAGGAGACCGGTGACATCTACAAGCAGTACGGCACCACCGACGCGCGCGGTAACGCCGTCGACTACAGCCCCAACGTCATGGTCAACTTCTGGTCCTTCCGCCTCATGATCGGGCTGGGCATGGCCTCGATGGCCCTGGGGGCTCTGGCCCTGTGGCTGACCCGCTCCGATCGGCTCATCTCCCGCCCGCTGCTGGGCAAGGCGGCGCTGGCCACCATGTGGCTGCCCTTCATCGCCTGCTCCTTCGGCTGGATCTTCCGTGAGATGGGCCGTCAGCCCTGGGTCATCGTCCCCAACCTGTCCGATCCGGTCTCGCAGGTCTACATGCTCACCGCCGACGGCGTCTCCTCCGTGGTCTCCTCGGGCACGGTGCTGGCCTCCATGGTCATTTTCACCCTGCTGTACGCCGCGCTCGGCGTGGTCTGGTTCGTGCTGCTGCGCCGCTACATCCGTGAAGGGGTGCGCACCCCGGTGCCGGACAAGACTGAGAAGTCCAAGCAGACGGACCGGGATGGCAAGGGCACGGACTCCAGCGACGATTCCGTTGACTCCTCCGAGGCCGCCCCGGCCCTGTCCTTCGCCTACTGA","MAISPMALDSLDLARWQFGITTVYHFILVPLTIGLSPLVALMETLWRRTGNKQWLVATKFFGKILLINFALGVATGIVQEFQFGMNWSEYSRFVGNIFGAPLAFEALLAFFMESVFLGLWIFGWDRLSPRLHNLCMWAVAAGTNFSAFFILTANSWMQHPVGAVVNPKTGRAELDGVSGFLKLLSNELVWATVLHVISSALLVAAAVVMGVSVWWMVKAAQAKQDFEARELWRRVARFGAVTMVAAGLVTAGTGHMQGQLVAEYQPGKMAAAEGLCHTEAGAPFTVAAFGDCKNEDGMVRFISVPGVYSFMATNDFNAEVTGLKETGDIYKQYGTTDARGNAVDYSPNVMVNFWSFRLMIGLGMASMALGALALWLTRSDRLISRPLLGKAALATMWLPFIACSFGWIFREMGRQPWVIVPNLSDPVSQVYMLTADGVSSVVSSGTVLASMVIFTLLYAALGVVWFVLLRRYIREGVRTPVPDKTEKSKQTDRDGKGTDSSDDSVDSSEAAPALSFAY$","Cytochrome bd ubiquinol oxidase, subunit I","Membrane, Cytoplasm, Extracellular","CydA","cytochrome bd-I oxidase subunit I ","cytochrome bd ubiquinol oxidase, subunit I","","Sturr M.G., Krulwich T.A., Hicks D.B. Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a delta cyo delta cyd strain complemented by genes from Bacillus firmus OF4. J. Bacteriol. 1996. 178(6):1742-1749. PMID: 8626304Juty N.S., Moshiri F., Merrick M., Anthony C., Hill S. The Klebsiella pneumoniae cytochrome bd' terminal oxidase complex and its role in microaerobic nitrogen fixation. Microbiology 1997. 143:2673-2683. PMID: 9274021","","","

InterPro
IPR002585
Family

Cytochrome bd ubiquinol oxidase, subunit I
PF01654	$\"[13-484]T$	Bac_Ubq_Cox

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[19-39]?$ $\"[60-78]?$ $\"[97-119]?$ $\"[134-152]?$ $\"[188-217]?$ $\"[238-258]?$ $\"[354-376]?$ $\"[391-409]?$ $\"[447-469]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB002585 (Cytochrome bd ubiquinol oxidase, subunit I) with a combined E-value of 6.2e-157. IPB002585A 11-47 IPB002585B 48-72 IPB002585C 76-105 IPB002585D 106-151 IPB002585E 155-193 IPB002585F 202-243 IPB002585G 253-302 IPB002585H 303-333 IPB002585I 341-363 IPB002585J 387-425","Residues 31-150 are similar to a (CYTOCHROME SUBUNIT I OXIDASE D UBIQUINOL OXIDOREDUCTASE OXIDASE 1.10.3.- TRANSMEMBRANE) protein domain (PD003558) which is seen in Q740N4_MYCPA.Residues 151-279 are 61% similar to a (CYTOCHROME SUBUNIT I OXIDASE D UBIQUINOL OXIDOREDUCTASE OXIDASE 1.10.3.- TRANSMEMBRANE) protein domain (PD491701) which is seen in Q6NFJ0_CORDI.Residues 392-476 are 65% similar to a (SUBUNIT CYTOCHROME I OXIDASE D UBIQUINOL OXIDOREDUCTASE OXIDASE 1.10.3.- TERMINAL) protein domain (PD344108) which is seen in Q7TZV4_MYCBO.","","-47% similar to PDB:1M56 Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type) (E_value = );-47% similar to PDB:1M57 Structure of cytochrome c oxidase from Rhodobacter sphaeroides (EQ(I-286) mutant)) (E_value = );-47% similar to PDB:2GSM Catalytic Core (Subunits I and II) of Cytochrome c oxidase from Rhodobacter sphaeroides (E_value = );","Residues 13 to 484 (E_value = 6.8e-145) place ANA_0461 in the Bac_Ubq_Cox family which is described as Bacterial Cytochrome Ubiquinol Oxidase.","","(AF284438) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0462","486446","489697","3252","5.74","-17.16","115788","ATGGCACGTCGCACCACATCAGAATCAACAGAATCGTACGAGCAGGAGCACGCCGACGGTGACGCCGTGAACGCGCCGACTCCGCGCCGTCGCCGCAGGGTCACCGCGGCAGCGGCCGCCCCCGAGAAGGCTCCTGCTGCCGAGCAGCCCGGTTCGGTAGGGGCCGCCGATGCCGTCACCGCCTTTGGGGCTGAGGAGCCCGGCGTGCAGCAGGCCCCACAGGCCGCGGCTGTTGAGTCGGCCCCGCCTCGTCGTCGTCGGAAGGTCGTCGCGGCCTCTGCCGCCCCCGAGAAGGCTCCTGCTGCCGAGCCCCACGTCACTGCCGGGGCGGACGAGCCAGATGACACGCACGTGACCGAGGATGCATCGAGCGCCGATGCTGCGCAGGAGGATGCCGAGCAGCAGGTCGACACCGAGGGGACCGACGGCGAGGGGCCCGAGATGCCTCAGGAGGATGACGAGGTCACCGGGGCGGACTCGGGTGAGGAGGAGGACCTCCAGGCCCCCCGTCTTCCTGCCGCCTCGCTCCTGTTCCAGGCCCCCGACCCAAGTCGGGCCCGCCGGCGCCGTCGGGTCACCGCGGCCACCGCCGCCCCCCAGGCGGCGCCGAGCGCCTCGCGCCACCAGGGCGCCAAGGACTGGGCGGACGAGGAGGACGCCGACGCGCGGACCGGTGCCCAGGGACATGACGAGGATGCTGAGTCCGAGTCCTCCCGTGCCGACCGCAGTGGCGGTCGCGGCCGTCGGCGTCGGCGGGCCGCCGCCGGTACCGGGGCCCCGCAGGAGTCCCGCGAGGACTCTGCCCTTGACAAGACCGACGCCGAGGTCTCTGAGGCCGACGGCCCTGACGGGGCCGATGAGGCCCAGGCCGAGTCCTCGGAGGACGGCCGTGAGGGCGGGGTCCGCCGCAAGCGTCGCCGCGGTGGTCGCGGTCGGCGCTCGCGCTCGCGGGGTGAAGACTCGACGCGCACTGACGCCGATGACGAGTCGCCGGCCGTGGAGGATGACGGAGCCGATGAGGCTCCATCGCGCGAATCCTCCTCCGATGCCGCCACGGAGATCGCCACGAGCGCCGTGTCCGGATCGCGCCGCCGGCGACGTCGCTCCCGTACCCGCTCGGAGGGTGGCGACCTGCGTGACGAGGTGACTGCCCTCAAGGGCTCCACCCGCCTGGAGGCCAAGCGTCAGCGCCGCCGCGAGGGCAGGGCGGCCGGGCGTCGTCGTCCCATCGTCACCGAGGCCGAGTTCCTGGCCCGTCGCGAGTCCGTGGACCGACAGATGATCGTGCGCGAGTCCGACGGCCTCAACCAGATCGCCGTCCTGGAGGACGGGCTCCTCGTGGAGCACTACGTCTCCCGGCACACCCAAACCTCCATGGTCGGCAACGTCTACGTCGGTCGGGTTCAGAACGTCCTGCCCTCCATGGAGGCCGCCTTCGTGGACCTGGGCAAGGGGCGCAACGCCGTCCTCTACGCCGGCGAGGTCAACTGGGACGCCGCCGGCCTGGAGGGACGGCCCCGCCGCATCGAGGACGCTCTCTCCAGTGGCGACACCGTCCTGGTCCAGGTCACCAAGGACCCCATCGGCCACAAGGGCGCTCGCCTCACCAGCCAGATCACTCTGGCGGGCCGATACCTGGTCCTGGTCCCCGGAGGAACCATGACGGGGATCTCGCGCAAGCTGCCGGACACCGAGCGCAGCCGCCTGAAGAAGATCCTCAAGCGGATCGTGCCCGACTCGGCAGGAGTCATCGTGCGCACCGCCGCGGAGGGGGCCACTCAGGAGCAGCTGACCGCCGACGTCGAACGCCTCGTGGCCCAGTGGGAGGCCATCGACAAGAAGGCGTCCTCCGTCATGAAGGGCAGCGGCAAGGCCCCCGTCCTGCTCAAGGGGGAGCCCGAGCTCGCCGTGAGAGTCATCCGCGACGTCTTCAACGAGGACTTCCGCAAGCTCATCGTCTCCGGCGACAACACCTGGTCCACGATCTCCCAGTACATCGACGAGGTCAGCCCGGATCTGTCCGAGCGCCTCGAGCACTGGGTCGGGCCCGAGGACGTCTTCGCCGCCCACCGTGTCGACGAGCAGCTCGCCAAGGGCTTCGACCGCAAGGTCTGGCTTCCCAGCGGCGGCACCCTGGTCATCGACCGCACCGAGGCGATGACCGTCATCGACGTCAACACCGGGCGCTTCACCGGAGCGGGAGGCACGCTGGAGGAGACCGTCACCCGCAACAACCTGGAGGCCGCCGAGGAGATCGTCCGCCAGCTGCGCCTGCGCGACATCGGTGGCATGGTCGTCATCGACTTCGTCGACATGGTCCTGGAGTCCAACCGGGACCTCGTGCTGCGCCGGCTCGTGGAGTGCCTGGGGCGCGACCGCACCCGCCACCAGGTCACTGAGGTCACCTCTTTGGGGCTGGTCCAGATGACCCGTAAACGGGTCGGCCAGGGCCTGGTCGAGGCATTCTCCACCACCTGCGAGCACTGCAAGGGCCGGGGCTTCATCGTCCACGACGAGCCCGTGGAGAACCAGCAGATCGACATGTCGGCCTCCGCCTCACGCGGCGGCGGACGCTCGCGCGGACGCAAGAACCGTGAGGAGCAGGCCACCGGCGGGGGCAAGAAGGAGACCAAGAAGGACTCCCAGGAGACCAAGGGCTCCAAGGGCTCCAAGGGCTCCGGTCGCGGCAAGGCATCGGCAGGGCGCGACGTTGCCGCATCGCCCGAGTCCGGAGTAGACGACGAGGCCCGGGCGGCAGTGCGAGGCGCTCTGGCCCAGATCGCGGCCGCCGCCGAGCAGGCTCACAAGGACAGCCAGCAGGAGGGACAGGACCCTCATGAGGGTCAGGGGGCCGTTGAGGCCCCGGAGGCCGGCGTGAGTGACACCGCCGACGCTGCGACGCAGACCGCGGAGAACGGGCAGTCCTCCGATGGTCAGGAAGTTTCGGACTCCCCGGCCGAGGACAAGCCGGTCAAGACCCGGTCGAGGAAGGCGGCTGACAAGAAGTCGGTGAAGAAGACCGGTGAGAAGAAGGGCGACAAGGCGGATAAGAAGTCGGGGCGGAAGACCGGCAAGAAGGCCGAGAAGAAGGCCGCCACGACCTCCGAGGACCCCGCTGAGCCGCAGCCTGGCGAGGCGTCGGCGGAGCCGGTGGAGGAGAAGCCGGTGAGGAGAACGCGACGGCGGGCCACGGCCAAGAGCGCCGCGCCCGCGCCGGAGAATTCTTCAGACGCCCCGGAGGCATCGGCCTGA","MARRTTSESTESYEQEHADGDAVNAPTPRRRRRVTAAAAAPEKAPAAEQPGSVGAADAVTAFGAEEPGVQQAPQAAAVESAPPRRRRKVVAASAAPEKAPAAEPHVTAGADEPDDTHVTEDASSADAAQEDAEQQVDTEGTDGEGPEMPQEDDEVTGADSGEEEDLQAPRLPAASLLFQAPDPSRARRRRRVTAATAAPQAAPSASRHQGAKDWADEEDADARTGAQGHDEDAESESSRADRSGGRGRRRRRAAAGTGAPQESREDSALDKTDAEVSEADGPDGADEAQAESSEDGREGGVRRKRRRGGRGRRSRSRGEDSTRTDADDESPAVEDDGADEAPSRESSSDAATEIATSAVSGSRRRRRRSRTRSEGGDLRDEVTALKGSTRLEAKRQRRREGRAAGRRRPIVTEAEFLARRESVDRQMIVRESDGLNQIAVLEDGLLVEHYVSRHTQTSMVGNVYVGRVQNVLPSMEAAFVDLGKGRNAVLYAGEVNWDAAGLEGRPRRIEDALSSGDTVLVQVTKDPIGHKGARLTSQITLAGRYLVLVPGGTMTGISRKLPDTERSRLKKILKRIVPDSAGVIVRTAAEGATQEQLTADVERLVAQWEAIDKKASSVMKGSGKAPVLLKGEPELAVRVIRDVFNEDFRKLIVSGDNTWSTISQYIDEVSPDLSERLEHWVGPEDVFAAHRVDEQLAKGFDRKVWLPSGGTLVIDRTEAMTVIDVNTGRFTGAGGTLEETVTRNNLEAAEEIVRQLRLRDIGGMVVIDFVDMVLESNRDLVLRRLVECLGRDRTRHQVTEVTSLGLVQMTRKRVGQGLVEAFSTTCEHCKGRGFIVHDEPVENQQIDMSASASRGGGRSRGRKNREEQATGGGKKETKKDSQETKGSKGSKGSGRGKASAGRDVAASPESGVDDEARAAVRGALAQIAAAAEQAHKDSQQEGQDPHEGQGAVEAPEAGVSDTADAATQTAENGQSSDGQEVSDSPAEDKPVKTRSRKAADKKSVKKTGEKKGDKADKKSGRKTGKKAEKKAATTSEDPAEPQPGEASAEPVEEKPVRRTRRRATAKSAAPAPENSSDAPEASA$","Ribonuclease, Rne/Rng family","Cytoplasm, Extracellular","ribonuclease, Rne/Rng family domain protein","ribonuclease; Rne/Rng family","ribonuclease, Rne/Rng family","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Bycroft M., Hubbard T.J., Proctor M., Freund S.M., Murzin A.G. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 1997. 88(2):235-242. PMID: 9008164","","","

InterPro
IPR003029
Domain

RNA binding S1
PF00575	$\"[457-538]T$	S1
SM00316	$\"[459-538]T$	S1
PS50126	$\"[461-544]T$	S1

InterPro
IPR004659
Domain

Ribonuclease E and G
TIGR00757	$\"[437-847]T$	RNaseEG: ribonuclease, Rne/Rng family

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[452-544]T$	no description

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[302-405]T$	no description

","BeTs to 13 clades of COG1530COG name: Ribonucleases G and EFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1530 is -o--kz-qv-r-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 380-451 are 91% similar to a (RIBONUCLEASE G SCO2599 PROTEIN) protein domain (PD141897) which is seen in Q6A9I4_PROAC.Residues 460-539 are 91% similar to a (RIBONUCLEASE E G HYDROLASE 3.1.4.- AXIAL RNE/RNG FILAMENT RIBONUCLEASE FAMILY) protein domain (PD383053) which is seen in Q82C89_STRAW.Residues 460-531 are 90% similar to a (RIBOSOMAL S1 30S NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE RNA-BINDING RIBONUCLEASE R NUCLEASE) protein domain (PD594032) which is seen in Q8G4U3_BIFLO.Residues 540-818 are 86% similar to a (RIBONUCLEASE E HYDROLASE 3.1.4.- G RNASE FILAMENT AXIAL CYTOPLASMIC FAMILY) protein domain (PD007819) which is seen in Q9L1H8_STRCO.","","-59% similar to PDB:2BX2 CATALYTIC DOMAIN OF E. COLI RNASE E (E_value = 5.7E_70);-59% similar to PDB:2C0B CATALYTIC DOMAIN OF E. COLI RNASE E IN COMPLEX WITH 13-MER RNA (E_value = 5.7E_70);-59% similar to PDB:2C4R CATALYTIC DOMAIN OF E. COLI RNASE E (E_value = 5.7E_70);-56% similar to PDB:1SLJ Solution structure of the S1 domain of RNase E from E. coli (E_value = 6.6E_10);-56% similar to PDB:1SMX Crystal structure of the S1 domain of RNase E from E. coli (native) (E_value = 6.6E_10);","Residues 457 to 538 (E_value = 3.2e-05) place ANA_0462 in the S1 family which is described as S1 RNA binding domain.","","Rne-Rng family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0463","489874","490194","321","9.60","5.17","11201","ATGAGCATTCAAGTGGTCTACGCGATCGTCAAGGCCGGCGGCCGTCAGGAGAAGGTCTCCGTCGGCGACGTCGTGGTTGTCGACAAGCTTGCTGGTGAGATCGGCGACGAGGTCACCCTCGCCCCCGTCATGCTGGTGGACGGCGACAAGGTGACCACCTCTGCCGCCGATCTGGCCAAGTCCTCCGTCACCGCCGAGATCATCGGCGACGAGAAGGGCCCCAAGATCAACATCCTCAAGTTCAAGAACAAGACCGGCTTCCGCAAGCGCCAGGGCCACCGCGCTCAGCTGACGGCCGTCAAGGTCACCGCCATCAAGTGA","MSIQVVYAIVKAGGRQEKVSVGDVVVVDKLAGEIGDEVTLAPVMLVDGDKVTTSAADLAKSSVTAEIIGDEKGPKINILKFKNKTGFRKRQGHRAQLTAVKVTAIK$","Ribosomal protein L21","Cytoplasm","ribosomal protein L21","ribosomal protein L21","ribosomal protein L21","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001787
Family

Ribosomal protein L21
PD003604	$\"[6-105]T$	Q6NFV5_CORDI_Q6NFV5;
PTHR21349	$\"[3-106]T$	50S RIBOSOMAL PROTEIN L21
PF00829	$\"[6-100]T$	Ribosomal_L21p
TIGR00061	$\"[7-106]T$	L21: ribosomal protein L21

","No hits to the COGs database.","***** IPB001787 (Ribosomal protein L21) with a combined E-value of 3.2e-27. IPB001787A 7-22 IPB001787B 63-105","Residues 6-105 are similar to a (RIBOSOMAL L21 RRNA-BINDING RNA-BINDING RIBONUCLEOPROTEIN 50S CHLOROPLAST LSU L21P L21) protein domain (PD003604) which is seen in Q6NFV5_CORDI.","","-55% similar to PDB:1VSA Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. This file, 1VSA, contains the 50S ribosome subunit. 30S ribosome subunit is in the file 2OW8 (E_value = 8.4E_12);-55% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 8.4E_12);-55% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 8.4E_12);-55% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 8.4E_12);-55% similar to PDB:2J01 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 2 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE I. (E_value = 8.4E_12);","Residues 6 to 100 (E_value = 7.9e-37) place ANA_0463 in the Ribosomal_L21p family which is described as Ribosomal prokaryotic L21 protein.","","protein L21 (rplU)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0464","490264","490521","258","11.77","9.64","9186","ATGGCACACAAGAAGGGTCTTGGTTCCTCCCGTAACGGCCGCGACTCCAACGCGCAGCGCCTCGGCGTCAAGCGCTTCGGCGGCCAGTTCGTCAAGGCCGGCGAGATCATCGTCCGCCAGCGCGGCACCCACTTCCACCCGGGCCGTAACGTCGGCCGCGGCAACGACGACACCCTGTTCGCCACCGCCGCCGGTAACGTCGAGTTCGGCACCTTCCGCGGTCGCCGGGTCGTCAACGTCGTGCTCCCCGAGGCCTGA","MAHKKGLGSSRNGRDSNAQRLGVKRFGGQFVKAGEIIVRQRGTHFHPGRNVGRGNDDTLFATAAGNVEFGTFRGRRVVNVVLPEA$","Ribosomal protein L27","Cytoplasm, Extracellular","ribosomal protein L27","50S ribosomal protein L27","ribosomal protein L27","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001684
Family

Ribosomal protein L27
PD003114	$\"[1-80]T$	Q6AFY2_BBBBB_Q6AFY2;
PR00063	$\"[4-28]T$ $\"[29-53]T$ $\"[54-78]T$	RIBOSOMALL27
PTHR15893	$\"[8-81]T$	RIBOSOMAL PROTEIN L27
PF01016	$\"[2-81]T$	Ribosomal_L27
TIGR00062	$\"[1-81]T$	L27: ribosomal protein L27
PS00831	$\"[34-48]T$	RIBOSOMAL_L27

","BeTs to 19 clades of COG0211COG name: Ribosomal protein L27Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0211 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001684 (Ribosomal protein L27) with a combined E-value of 2.4e-48. IPB001684A 2-34 IPB001684B 35-72","Residues 1-80 are similar to a (RIBOSOMAL L27 50S CHLOROPLAST 60S MITOCHONDRIAL PEPTIDE MITOCHONDRION PRECURSOR L27) protein domain (PD003114) which is seen in Q6AFY2_BBBBB.","","-79% similar to PDB:1V8Q Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8 (E_value = 2.7E_23);-79% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 2.7E_23);-79% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 2.7E_23);-79% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 2.7E_23);-79% similar to PDB:2J01 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 2 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE I. (E_value = 2.7E_23);","Residues 2 to 81 (E_value = 1.1e-51) place ANA_0464 in the Ribosomal_L27 family which is described as Ribosomal L27 protein.","","protein L27 (rpmA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0465","490608","492230","1623","5.47","-15.65","57204","ATGCCCAGCTTCATTGACCGAGTGGTCCTCCACGTGGCCGGCGGCGACGGCGGCAGCGGCTGCACCTCCGTGCACCGTGAGAAGTTCAAGCCCCTGGCCGGGCCCGACGGCGGCGATGGCGGTCATGGCGGCGACGTCGTCCTGACCGTCGACCCCCGGGTGACGACCCTGCTGAGCTACCACCGCTCCCCGCACCAGCGGGCCGGCAACGGCACCCCCGGCATGGGGGACTGGCGCCGCGGTACCGACGGCAAGAACCTCGTCCTGCCCGTTCCCGAGGGCACCGTCGTCAAGGATTCGCGAGGCCAGGTCATCGCCGACCTCGTGGGAGAGGGTGCCAGCGTCGTCGTCGCCCAGGGCGGTACCGGCGGACGCGGCAACTTCTCCCTGGCCTCCTCCAAGCGCAAGGCCCCCGGCTTCCACCTCCTGGGAGAGCCCGGTCAGGCCCAGGACATCACCTTGGAGCTCAAGACCATCGCCGACGTCGCCCTCGTGGGCTACCCCAGCGCCGGCAAGTCCTCCCTCATCGCCGCCATGAGCGCCGCCCGTCCCAAGATCGCCGACTACCCCTTCACGACCCTCGTCCCCAACCTCGGGGTCGTCGAGGCCGGCGACGTGCGCTACACCATCGCCGATGTCCCCGGCCTCATCCCCGGAGCCTCCCAGGGCAAGGGACTGGGGCTGGACTTCCTGCGGCACATCGAGCGCTGCGCCGTCATCGTCCACGTCCTGGACTGCGCCACCCTCGAGCCGGGGCGCGACCCCCTCTCCGACCTGGACACCATTGAGGCAGAGCTCGCAGCCTACTCCGAGCGCCTCGGCGAGCAGGAGGACGACCCCTCCCTCACCGGCCGGGTCCCCCTCATGGAGCGCCCCCGCATCGTGGTGCTCAACAAGGTCGATGTCCCCGACGCCGCCGAGCTCGCCGAGTTCGTGCGCGCCGACATCGAGGCCCGGGGACTGCCCGTCCACATCATCTCCGCGGTCGCGCACACGGGGCTGCGCCCCCTGTCCTTCGCCCTGGCCGGGGAGGTCGAGCGGGCCCGGAAGGCCGCTCCGGCCACGTCCCAGCGCGATGGCGAGCCCGGTGCGACTGACGGTTCGGGTGAGCCGCGCCCCGTCATCCGGCCCGCGGCGGTCGGGCGGCGGGAGAAGGAGAGCGTCGCCCAGGTGCGTCTGCTGGCCCATCCCAGCGAGGGGCAGGTCTACCAGGTCCGCGGGCAGCGCCCCGAGCGCTGGGTGCGTCAGACCGACTTCACCAATGACGAGGCCGTCGGCTACCTCGCCGACCGCCTGGCCGCGGCCGGGGTCGAGGACGAGCTCGTCAAGGCCGGCGCCCACGCCGGCGACACCGTCCTCATCGGCGAGGTCGATGGGGGAGTGCTCTTCACCTGGGAGCCCACAATGACCACCGGGCCCGAGCTGCTGGGCGCCAGAGGCACCGACCTGCGCCTGGAGACCAGTCGGCGTCGGACCAACGTGGAGCGGCGCAGCCAATACCACGAGATGATGGATGCCAAGGAGGCCGCGCGCCAGCAGCTGCGCGACGAGGCCGCCGAGGGCCTGTGGACCGATGCCGCCTCCTGGCACGGGGACGACGAGGAATCAGGCGCGAACCCATGA","MPSFIDRVVLHVAGGDGGSGCTSVHREKFKPLAGPDGGDGGHGGDVVLTVDPRVTTLLSYHRSPHQRAGNGTPGMGDWRRGTDGKNLVLPVPEGTVVKDSRGQVIADLVGEGASVVVAQGGTGGRGNFSLASSKRKAPGFHLLGEPGQAQDITLELKTIADVALVGYPSAGKSSLIAAMSAARPKIADYPFTTLVPNLGVVEAGDVRYTIADVPGLIPGASQGKGLGLDFLRHIERCAVIVHVLDCATLEPGRDPLSDLDTIEAELAAYSERLGEQEDDPSLTGRVPLMERPRIVVLNKVDVPDAAELAEFVRADIEARGLPVHIISAVAHTGLRPLSFALAGEVERARKAAPATSQRDGEPGATDGSGEPRPVIRPAAVGRREKESVAQVRLLAHPSEGQVYQVRGQRPERWVRQTDFTNDEAVGYLADRLAAAGVEDELVKAGAHAGDTVLIGEVDGGVLFTWEPTMTTGPELLGARGTDLRLETSRRRTNVERRSQYHEMMDAKEAARQQLRDEAAEGLWTDAASWHGDDEESGANP$","GTP-binding protein","Cytoplasm","obg protein","K03979 GTP-binding protein","GTP1/OBG sub domain protein","","Vernet C., Ribouchon M.T., Chimini G., Pontarotti P. Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm. Genome 1994. 5(2):100-105. PMID: 8180467","","","

InterPro
IPR002917
Domain

GTP-binding protein, HSR1-related
PF01926	$\"[160-301]T$	MMR_HSR1

InterPro
IPR006073
Domain

GTP1/OBG
PR00326	$\"[162-182]T$ $\"[183-201]T$ $\"[210-225]T$ $\"[227-245]T$	GTP1OBG

InterPro
IPR006074
Domain

GTP1/OBG domain
PS00905	$\"[212-225]T$	GTP1_OBG

InterPro
IPR006169
Domain

GTP1/OBG subdomain
PF01018	$\"[4-158]T$	GTP1_OBG

InterPro
IPR014100
Family

GTP-binding protein Obg/CgtA
TIGR02729	$\"[4-304]T$	Obg_CgtA: GTP-binding protein Obg/CgtA

InterPro
IPR015349
Domain

GTP1/OBG, C-terminal
PF09269	$\"[393-465]T$	DUF1967

noIPR
unintegrated

unintegrated
G3DSA:2.70.210.12	$\"[3-158]T$	no description
G3DSA:3.40.50.300	$\"[158-311]T$	no description
PTHR11702	$\"[3-273]T$ $\"[289-335]T$	DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED
PTHR11702:SF3	$\"[3-273]T$ $\"[289-335]T$	MITOCHONDRIAL GTPASE 2(YEAST)/OBG-RELATED

","BeTs to 19 clades of COG0536COG name: Predicted GTPaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0536 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB006073 (GTP1/OBG GTP-binding protein family signature) with a combined E-value of 1.1e-33. IPB006073A 162-182 IPB006073B 183-201 IPB006073C 210-225 IPB006073D 227-245***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 1e-10. IPB002917 164-196***** IPB013029 (Protein of unknown function DUF933) with a combined E-value of 1.4e-06. IPB013029B 209-261 IPB013029A 168-221","Residues 2-99 are 57% similar to a () protein domain (PDA1C5Z3) which is seen in Q7S8Z8_NEUCR.Residues 3-99 are 57% similar to a (GTP-BINDING SIMILAR HELIOBACILLUS MOBILIS. SPO0B-ASSOCIATED) protein domain (PD740436) which is seen in Q86KT3_DICDI.Residues 11-147 are similar to a (GTP-BINDING GTP1/OBG FAMILY OBG PROBABLE SPO0B-ASSOCIATED PROTEIN FACTOR BINDING GTPASE) protein domain (PD004315) which is seen in P95722_STRCO.Residues 80-265 are 49% similar to a (PROTEIN GTP-BINDING) protein domain (PD839666) which is seen in Q8IB77_PLAF7.Residues 152-185 are 97% similar to a (GTP-BINDING GTP1/OBG FAMILY OBG PROBABLE SPO0B-ASSOCIATED PROTEIN FACTOR BINDING GTPASE) protein domain (PD926571) which is seen in Q6AFY1_BBBBB.Residues 162-245 are 57% similar to a (YHBZ) protein domain (PD801545) which is seen in Q8D279_WIGBR.Residues 242-301 are 73% similar to a (GTP-BINDING GTP1/OBG FAMILY SPO0B-ASSOCIATED OBG PROBABLE PROTEIN FACTOR GTPASE GTP1/OBG-FAMILY) protein domain (PD046517) which is seen in Q6AFY1_BBBBB.Residues 402-465 are 79% similar to a (GTP-BINDING SPO0B-ASSOCIATED OBG PROBABLE FAMILY GTP1/OBG-FAMILY GTP1/OBG PROTEIN GTPASE MG384) protein domain (PD015821) which is seen in P95758_STRGR.Residues 466-537 are 53% similar to a (GTP-BINDING) protein domain (PD773226) which is seen in Q8G4U0_BIFLO.Residues 466-537 are 59% similar to a (GTP-BINDING) protein domain (PD968737) which is seen in Q6AFY1_BBBBB.","","-60% similar to PDB:1LNZ Structure of the Obg GTP-binding protein (E_value = 2.6E_73);-54% similar to PDB:1UDX Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8 (E_value = 4.9E_72);-41% similar to PDB:2DBY Crystal structure of the GTP-binding protein YchF in complexed with GDP (E_value = 3.2E_15);-41% similar to PDB:2DWQ Thermus thermophilus YchF GTP-binding protein (E_value = 3.2E_15);-52% similar to PDB:1JAL YCHF PROTEIN (HI0393) (E_value = 3.5E_14);","Residues 4 to 158 (E_value = 3.5e-69) place ANA_0465 in the GTP1_OBG family which is described as GTP1/OBG.Residues 160 to 301 (E_value = 8e-41) place ANA_0465 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 393 to 465 (E_value = 3.4e-26) place ANA_0465 in the DUF1967 family which is described as Domain of unknown function (DUF1967).","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0466","492284","493396","1113","6.46","-2.90","38068","CTGCCTGAGGGGGCCCGCGTCGTGGTCAAGGTCGGCTCCTCCTCCCTGACACGCGCCGACGGCGGGCTCGATCTCAACCGCATCGATATCCTCGCCGGCCTCATCGCCGGTATGCGCAGTCGCGGCCACGACGTCGTCCTGGTCTCCTCCGGAGCCGTCGCCTCAGGGCTGGTGCCCCTGGGGCTGAGCCGGCGCCCCGACGAGCTCAGCCTCCTGCAGGCGGCCGCCTCCGTGGGACAGGGGCGGCTCGCCGCCCGCTGGGAGACCGCGATGAGCGCCTACGGACTGGTGACCGCCCAGGTCCTCCTGACCGCCCACGACGTCGCCATCCGCAGCCACTACCGCACGGTGCGCGCCACCTTCGACTCCCTGCTCTCACTGGGAGCCGTCCCCATCATCAACGAGAACGACGCGGTGGCCACCAGCGAGTTCAGCCTCGGCGACAACGACCGCCTCGCCGCCCTCGTGGCCCACCTGGTGACCGCCGACGTCCTGGTGCTGCTCACCGACGTCGACGGCCTGTGGACCGCGCGCCCCGGAACCCCCGGCGCCACGCCCATCCGCCACGTGCGCTCCTCAGCGGACCTGGCGGGGGTCAGCGTCTCAGGACGCGGCTCCTTCGTGGGAACCGGCGGCATGACCACCAAGCTCCAGGCCGCCACCATCGCCTGCGCCTCAGGCACCACCACCCTCATCGCCCGGGCCGACGACGCCGCAGCGCTCCTGGGCCAGGAACAGGTTCCCACCGACCTGGGCACCTGGTTCGAGCCCACTGGTCCCCACCGCCCCAGCCGCCGGCTGTGGATGGCCCACGCCTCCCAGCCCGACGGGCGCGTTCTCATCGACGCCGGGGCGGCCCGGGCCCTGACCGTGGGGAAGAAGTCGCTCCTGCTGCCGGGCCTGACCGGCCTCGACGGCGACTTCGAGTCGGGCTCCGTCGTCGACGTCGTCGGCCCTGAGGGCGTCCTGGCCCGGGGGATATGCCGCTACGCCGCCGCCGAGCTGCGCGAGGTCCTGGGGGCCCGGTCCGAGGGCGCCCCCGCCCCCGACCACGTGGCACCCGTGATCCACCGCGACGATCTGGCCGAGCTGCCCCGCATCGCCGGAGTCTGA","LPEGARVVVKVGSSSLTRADGGLDLNRIDILAGLIAGMRSRGHDVVLVSSGAVASGLVPLGLSRRPDELSLLQAAASVGQGRLAARWETAMSAYGLVTAQVLLTAHDVAIRSHYRTVRATFDSLLSLGAVPIINENDAVATSEFSLGDNDRLAALVAHLVTADVLVLLTDVDGLWTARPGTPGATPIRHVRSSADLAGVSVSGRGSFVGTGGMTTKLQAATIACASGTTTLIARADDAAALLGQEQVPTDLGTWFEPTGPHRPSRRLWMAHASQPDGRVLIDAGAARALTVGKKSLLLPGLTGLDGDFESGSVVDVVGPEGVLARGICRYAAAELREVLGARSEGAPAPDHVAPVIHRDDLAELPRIAGV$","Glutamate 5-kinase","Cytoplasm, Membrane","glutamate 5-kinase","glutamate 5-kinase ","glutamate 5-kinase","","Li W., Brandriss M.C. Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase. J. Bacteriol. 1992. 174(12):4148-4156. PMID: 1350780Ogura M., Kawata-Mukai M., Itaya M., Takio K., Tanaka T. Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis. J. Bacteriol. 1994. 176(18):5673-5680. PMID: 8083159","","","

InterPro
IPR001048
Domain

Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10	$\"[6-255]T$	no description
PF00696	$\"[5-234]T$	AA_kinase

InterPro
IPR001057
Domain

Glutamate 5-kinase
PR00474	$\"[42-56]T$ $\"[76-104]T$ $\"[116-137]T$ $\"[148-175]T$ $\"[208-228]T$	GLU5KINASE
PS00902	$\"[206-223]T$	GLUTAMATE_5_KINASE

InterPro
IPR002478
Domain

PUA
PF01472	$\"[277-343]T$	PUA
SM00359	$\"[277-356]T$	PUA
PS50890	$\"[276-353]T$	PUA

InterPro
IPR005715
Domain

Glutamate 5-kinase, ProB-related
TIGR01027	$\"[5-363]T$	proB: glutamate 5-kinase

InterPro
IPR011529
Family

Glutamate 5-kinase, pro-B
PIRSF000729	$\"[3-365]T$	Glutamate 5-kinase

noIPR
unintegrated

unintegrated
PTHR11063	$\"[10-233]T$	GLUTAMATE SEMIALDEHYDE DEHYDROGENASE
PTHR11063:SF2	$\"[10-233]T$	DELTA 1-PYRROLINE-5-CARBOXYLATE SYNTHETASE
tmhmm	$\"[45-63]?$	transmembrane_regions

","BeTs to 15 clades of COG0263COG name: Glutamate 5-kinaseFunctional Class: EThe phylogenetic pattern of COG0263 is ----YqvceBrh-----l---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 27-92 are 75% similar to a (KINASE TRANSFERASE GAMMA-GLUTAMYL 5-KINASE GLUTAMATE GK BIOSYNTHESIS PROLINE SYNTHETASE DELTA) protein domain (PD711348) which is seen in PROB_STRCO.Residues 276-380 are 56% similar to a (KINASE TRANSFERASE 5-KINASE GLUTAMATE GAMMA-GLUTAMYL BIOSYNTHESIS PROLINE GK PRO1 YDR300C) protein domain (PD005319) which is seen in PROB_STRAW.","","-40% similar to PDB:2J5T GLUTAMATE 5-KINASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTAMATE (E_value = 1.6E_31);-40% similar to PDB:2J5V GLUTAMATE 5-KINASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTAMYL-5-PHOSPHATE AND PYROGLUTAMIC ACID (E_value = 1.6E_31);-48% similar to PDB:2AKO Crystal structure of Glutamate 5-kinase from Campylobacter jejuni (E_value = 4.6E_10);-50% similar to PDB:1VR4 Crystal Structure of MCSG TArget APC22750 from Bacillus cereus (E_value = 4.6E_10);-50% similar to PDB:2GTC Crystal structure of the hypthetical protein from Bacillus cereus (ATCC 14579). Northeast structural genomics Target BcR11 (E_value = 4.6E_10);","Residues 24 to 253 (E_value = 5.5e-52) place ANA_0466 in the AA_kinase family which is described as Amino acid kinase family.Residues 296 to 366 (E_value = 1.6e-14) place ANA_0466 in the PUA family which is described as PUA domain.","","5-kinase (proB)","","1","","","Fri Aug 10 16:55:02 2007","","Fri Aug 10 16:55:02 2007","","","Fri Aug 10 16:55:02 2007","Fri Aug 10 16:55:02 2007","Fri Aug 10 16:55:02 2007","","","Fri Aug 10 16:55:02 2007","","","Fri Aug 10 16:55:02 2007","Fri Aug 10 16:55:02 2007","Fri Aug 10 16:55:02 2007","","Fri Aug 10 16:55:02 2007","Fri Aug 10 16:55:02 2007","","","","","yes","","" "ANA_0467","493431","494726","1296","5.40","-13.90","44694","ATGAACGACGTTGAGGCCCACGAGCTCGTCACCACCACCGCCCGCTCAGCCCGCGTGGCGCAACGGAGCCTGGCCAGGGCCCCACGCGCCGTCAAGGACGCCGCCCTGGAGGCCATGGCCCACAGCCTCACCGAGCACGGCGAAGCGATCCTCGCGGCCAACGCCGCCGACCTGGAGCGCGGACGCCAAGGCGGGATGAAGCCCGGCCTCCTCGACCGCCTGGACCTGGACTCCGGCCGACTGGCGGCCATCGCCGACTCCCTGCGTGAGGTGGCCGCCCTGCCCGACCCCGTGGGTCAGGTCGTGGACGGCTCGGTCATGCCCAACGGACTGCGAGTGCGTCGGGTTCGGGTGCCACTGGGCGTCGTCGGCATGATCTACGAGGCCCGCCCCAATGTCACCGTCGACACCGCTGCCCTGGCCGTCAAGTCCGGCAACGCCATCATCCTGCGCGGAGGTAGTGCCGCCCAGGACTCCAACGCCGCCATCGTCGCGGCCCTGCGCAGCGCCCTGGAGGCGCAGGGACTGCCCGCAGACCTCGTCACCAGCGTCGATGCCGCCGGTCGGGATGGGGCCCGCGCCCTCATGCGCGCTCACGGCCTCGTCGACGCCCTGGTGCCGCGGGGAGGGGCCGGGCTCATCCGCACCGTCGTCGAGCAGTCCACCGTCCCCGTCATCGAGACCGGATCGGGCAACTGCCACGTCTACGTCGACGCCAGCGCCGACCTGGAGGCCGCGGTGGACATTATCGTCAACGCCAAGACCCAGCGCGTCGGCGTGTGCAACGCCGCCGAGACGCTCCTGGTCCACACCGATGTCGCCGCCACCTACCTGCCAGCAGCCGCCCGCGCCCTGTGGGACAAGGACACCGTCCTGCACGCCGACCCCACCGCCCACCGGCTCCTGACCGAGGCGGCGACGGCCGGTGGGCGTGATGGACTTCTGACCGAAGCCACTGAGGCCGACTGGGACACCGAGTACGGCTCGCTGGACCTGGCTGTGCGCGTCGTGAAGGGCCTGGAAGAGGCCATCGACCACATCCGTGCCCACACCACCGGGCACACCGAGGCGGTTCTCGCCCAGGACGTGAGCGTCATCAACGACTTCATCGCCGGTATGGATTCGGCGGCCGTCATGGTCAATGCCTCGACCCGGTTCACCGATGGCGGACAGCTGGGGCTGGGGGCCGAGCTGGGCATCTCCACCCAGAAGCTCCATGCCCGTGGCCCCATGGGATTGAGCGAGCTGACGACGACGACCTGGATCGTCGAGGGAGACGGCCACATCCGTCCCTGA","MNDVEAHELVTTTARSARVAQRSLARAPRAVKDAALEAMAHSLTEHGEAILAANAADLERGRQGGMKPGLLDRLDLDSGRLAAIADSLREVAALPDPVGQVVDGSVMPNGLRVRRVRVPLGVVGMIYEARPNVTVDTAALAVKSGNAIILRGGSAAQDSNAAIVAALRSALEAQGLPADLVTSVDAAGRDGARALMRAHGLVDALVPRGGAGLIRTVVEQSTVPVIETGSGNCHVYVDASADLEAAVDIIVNAKTQRVGVCNAAETLLVHTDVAATYLPAAARALWDKDTVLHADPTAHRLLTEAATAGGRDGLLTEATEADWDTEYGSLDLAVRVVKGLEEAIDHIRAHTTGHTEAVLAQDVSVINDFIAGMDSAAVMVNASTRFTDGGQLGLGAELGISTQKLHARGPMGLSELTTTTWIVEGDGHIRP$","Gamma-glutamyl phosphate reductase","Cytoplasm","gamma-glutamyl phosphate reductase","gamma-glutamyl phosphate reductase ","gamma-glutamyl phosphate reductase","","Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M. Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII. Yeast 1996. 12(10):1021-1031. PMID: 8896266Hu C.A., Delauney A.J., Verma D.P. A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9354-9358. PMID: 1384052","","","

InterPro
IPR000965
Domain

Gamma-glutamyl phosphate reductase GPR
TIGR00407	$\"[17-420]T$	proA: gamma-glutamyl phosphate reductase

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PF00171	$\"[9-422]T$	Aldedh

InterPro
IPR003833
Domain

Allophanate hydrolase subunit 1
SM00796	$\"[224-414]T$	no description

InterPro
IPR012134
Family

Glutamate-5-semialdehyde dehydrogenase
PIRSF000151	$\"[7-431]T$	Gamma-glutamyl phosphate reductase
PTHR11063:SF1	$\"[8-431]T$	GLUTAMATE SEMIALDEHYDE DEHYDROGENASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.309.10	$\"[226-411]T$	no description
G3DSA:3.40.605.10	$\"[8-225]T$	no description
PTHR11063	$\"[8-431]T$	GLUTAMATE SEMIALDEHYDE DEHYDROGENASE

","BeTs to 15 clades of COG0014COG name: Gamma-glutamyl phosphate reductaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0014 is ------yqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB000965 (Gamma-glutamyl phosphate reductase GPR) with a combined E-value of 3.1e-146. IPB000965A 39-92 IPB000965B 117-160 IPB000965C 223-270 IPB000965D 332-376 IPB000965E 377-416 IPB000965C 224-271***** IPB002086 (Aldehyde dehydrogenase) with a combined E-value of 4.4e-21. IPB002086A 116-157 IPB002086C 232-280 IPB002086D 307-360 IPB002086E 375-399","Residues 10-417 are 70% similar to a (DEHYDROGENASE OXIDOREDUCTASE ALDEHYDE SEMIALDEHYDE PROLINE NADP REDUCTASE GAMMA-GLUTAMYL PHOSPHATE GPR) protein domain (PD250846) which is seen in PROA_STRAW.Residues 15-306 are 62% similar to a (DEHYDROGENASE SEMIALDEHYDE GSA PHOSPHATE GPR REDUCTASE PROLINE GLUTAMYL-GAMMA-SEMIALDEHYDE GLUTAMATE-5- OXIDOREDUCTASE) protein domain (PDA182K2) which is seen in PROA_DESVH.Residues 125-273 are 60% similar to a (SYNTHETASE GAMMA-GLUTAMYL TRANSFERASE DELTA DEHYDROGENASE PHOSPHATE REDUCTASE 1-PYRROLINE-5-CARBOXYLATE GPR KINASE) protein domain (PD813400) which is seen in PROA_CAMJE.Residues 350-397 are 75% similar to a (DEHYDROGENASE GAMMA-GLUTAMYL PHOSPHATE REDUCTASE GPR SEMIALDEHYDE GLUTAMATE-5- OXIDOREDUCTASE GSA PROLINE) protein domain (PD403271) which is seen in PROA_SERMA.Residues 398-429 are 90% similar to a (DEHYDROGENASE GAMMA-GLUTAMYL PHOSPHATE REDUCTASE GPR OXIDOREDUCTASE SEMIALDEHYDE GLUTAMATE-5- GSA PROLINE) protein domain (PDA1E739) which is seen in PROA_STRCO.","","-59% similar to PDB:1O20 Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolution (E_value = 1.5E_86);-51% similar to PDB:2H5G Crystal structure of human pyrroline-5-carboxylate synthetase (E_value = 3.5E_54);-47% similar to PDB:1VLU Crystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces cerevisiae at 2.40 A resolution (E_value = 2.6E_49);","Residues 9 to 422 (E_value = 4.5e-08) place ANA_0467 in the Aldedh family which is described as Aldehyde dehydrogenase family.","","phosphate reductase (proA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0469","494907","495410","504","5.09","-9.35","16879","ATGGCGAGTCTGCTGCATCGTTTTGGTCGTGGCCGCGTCGTTGCCTCCACGGTCGTCGTCGTGACAGCGGGCCTCCTGCTCGCGGTCAGCCGCATGGTCTTCTCCCACCCCACCGAGTCCGCGAAGGAACCGGGAATCGTCCTGACGGAGAGCCCGCGGGTCACGTCGTCCCAGTCCTCGACCACGGCGACGCCGAGCCGGAGTGCCGGCGGTGCCAGCTCCACCCAGCACGAGTCCGGCGGCTCCGAAGCCGGCTCCTCGCACTCCTCGGACTCCTCGGACTCCTCGGCGCAGGGTCACGCGCCTCAGGCGGTGGAACCCGACCCGCCTGTCGCCGTCGATCACGGCCATCGCCAGCCGGCCCCCGCCGCACCGGCTGCCCCGGCTGGGACTGCCGCACCGGCCGCCCCCGGACGCACCGAGGTGGACGATGACGACGACGATAAGAAGCCGGTCAGGAACGGTGTGAAAGAAGCCGATGACGACGACCGGGACGATGACTGA","MASLLHRFGRGRVVASTVVVVTAGLLLAVSRMVFSHPTESAKEPGIVLTESPRVTSSQSSTTATPSRSAGGASSTQHESGGSEAGSSHSSDSSDSSAQGHAPQAVEPDPPVAVDHGHRQPAPAAPAAPAGTAAPAAPGRTEVDDDDDDKKPVRNGVKEADDDDRDDD$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[3-118]T$	Q9X802_STRCO_Q9X802;
PF00072	$\"[2-114]T$	Response_reg
SM00448	$\"[2-113]T$	REC
PS50110	$\"[3-117]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[129-218]T$	Q8NTN4_CORGL_Q8NTN4;
PF00486	$\"[147-218]T$	Trans_reg_C

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00217	$\"[89-114]?$	SUGAR_TRANSPORT_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[121-218]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[3-118]T$	no description
PTHR23283	$\"[3-118]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[3-118]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 1.1e-41. IPB001867A 47-60 IPB001867B 75-119 IPB001867C 208-218***** IPB001789 (Response regulator receiver) with a combined E-value of 1.5e-12. IPB001789A 47-60 IPB001789B 95-105***** IPB000673 (CheB methylesterase) with a combined E-value of 3.7e-08. IPB000673B 19-72 IPB000673C 73-103","Residues 3-118 are similar to a (SENSORY TRANSDUCTION PHOSPHORYLATION REGULATOR DNA-BINDING TRANSCRIPTION REGULATION RESPONSE TWO-COMPONENT KINASE) protein domain (PD000039) which is seen in Q9X802_STRCO.Residues 5-216 are 40% similar to a (PSBAI-STIMULATING TRANSDUCTION PHOSPHORYLATION SENSORY FACTOR) protein domain (PD792868) which is seen in Q83ZP4_SYNP7.Residues 129-218 are 73% similar to a (DNA-BINDING TRANSCRIPTION SENSORY TRANSDUCTION PHOSPHORYLATION REGULATION REGULATOR RESPONSE TWO-COMPONENT TRANSCRIPTIONAL) protein domain (PD000329) which is seen in Q8NTN4_CORGL.","","-59% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 6.0E_42);-59% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 6.0E_42);-60% similar to PDB:1KGS Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima (E_value = 3.4E_37);-58% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 6.5E_36);-66% similar to PDB:1MVO Crystal structure of the PhoP receiver domain from Bacillus subtilis (E_value = 1.6E_23);","Residues 2 to 114 (E_value = 2.3e-38) place ANA_0470 in the Response_reg family which is described as Response regulator receiver domain.Residues 147 to 218 (E_value = 9.8e-25) place ANA_0470 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","response regulator alr5188","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0471","497629","496100","1530","5.79","-7.84","54869","GTGACCTCACTGCTGCCCACTCGTACCGTCACCATTCGCACCCGTGTCATGTGGGCCATCGTGCTGGTGGCCGGCATCGCGCTGGTCATGTGCGGGACGATTGTGTGGGCATTGGGGCAATCCAGCGTGTCGGCCGATGCCACCAACCGGCTCGAGCACAGCCGCGACCGGATCCGCCAGCTGGCCGCCGACAGGCAGGATCCCTCCAGCGGTCAGCCCCTGGAGGACGTCTCCGCGGTTCTTCGCACGCACATTCAACGCACCGCCGAGGGGCGCGGTGAGGCCGAGCTCGGCTTCGTGGGCACCGATGCCGGCACCGAGCTGACCTGGGTCTCCGCGGACAGCGTCTCCTTCCGCCCCGAGGAGGACAAGGAGCTGCTCACTCGGGTGACCGCCCAGGCCGCCGCCTCGGAGTCCGTCATCGAGACAGTGCGCACCCCCGCCTCGAGCTACCGGGTCCTCGTCGTCCCGCTGCAAGGAGGTTCCCAGCGCGGCGCGCTCGTGCACGTCATCGACCTCAAGATCGCCGAGTCCCAGCTCCGGCGCACCATGGCCTTCTACGCGGCGGCGGCCGTGTTCACTGTCGCCCTGGTGACGGGTCTGGCCTGGTTCGCCGTCGAACGGCTTCTTCGACCCATTGAGCAGCTGCGCCGAGCCACCGAGTCCATCGGTGAGGAGGATCTGACCACCCGGGTGCCGGTCAAGGGCCGGGACGACCTGACGGCCCTGGCCGCGGCCGTCAATCGGATGCTCGACCGGGTCCAGACCTCGGTGGAGGCCCAACGCAACCTGCTCGACGACGTCGGCCACGAGCTGCGCACCCCGATCGCCGTGGTCCGCGGCCACCTCGAGCTCACCGACCCTGTGGACCCCGAGGACGTGCGCCAGACCCAGCTGTTGGCCATTGACGAGCTCGACCGGATGGGGATGCTCGTGAACGACCTGATCCTGCTGGCCAAGAGCGTCCAGAGCGACTTCGTCACCCCGGCGGACACGGATGTCGCCGAGCTGACCGAGCTGGTCTTCGACAAGTCCCTCGCCCTGGGCGAGCGACGCTGGAAGATGGAGTCGGCGGCCTTCACCCGAGCGATGATCGACCCCACCCGGATCACCCAGGCATGGCTCCAGCTGGTGGCCAACGCGGTGAAGTACTCCGAGCACTGCTCCACCGTGTCCCTGGGCTCGGCCGTTCGCGACGGCCACCTGCAGATGTGGGTGGCCGACGAGGGCATCGGGATCGCGCCTGAGGACATCGACCTGGTGCGCCAGCGCTTCAAGCGCACCGCCGGCGCTCAGGAGCTAGCCTCCGGAACGGGACTGGGGCTCAGTATCGTCGAGACGATCGTCGCAGCGCACGGCGGGAGGCTGGACATACGCTCTGAGGTGGGCCGAGGATCGGTGTTCACCATGGTGGTCCCTCTGAAGACCTCCACTGCCTCGTCCTCCTCCCGAGGCGGCGTCCTCGCACCCGCCGGGAACTCAGGCCCCGCTCAGCCCCCGACAGCCTCCCAAAGGAGTCACTCACCATGA","VTSLLPTRTVTIRTRVMWAIVLVAGIALVMCGTIVWALGQSSVSADATNRLEHSRDRIRQLAADRQDPSSGQPLEDVSAVLRTHIQRTAEGRGEAELGFVGTDAGTELTWVSADSVSFRPEEDKELLTRVTAQAAASESVIETVRTPASSYRVLVVPLQGGSQRGALVHVIDLKIAESQLRRTMAFYAAAAVFTVALVTGLAWFAVERLLRPIEQLRRATESIGEEDLTTRVPVKGRDDLTALAAAVNRMLDRVQTSVEAQRNLLDDVGHELRTPIAVVRGHLELTDPVDPEDVRQTQLLAIDELDRMGMLVNDLILLAKSVQSDFVTPADTDVAELTELVFDKSLALGERRWKMESAAFTRAMIDPTRITQAWLQLVANAVKYSEHCSTVSLGSAVRDGHLQMWVADEGIGIAPEDIDLVRQRFKRTAGAQELASGTGLGLSIVETIVAAHGGRLDIRSEVGRGSVFTMVVPLKTSTASSSSRGGVLAPAGNSGPAQPPTASQRSHSP$","Two-component system sensor kinase","Membrane, Cytoplasm","two-component sensor histidine kinase alr5189","two-component sensor histidine kinase","ATP-binding region, ATPase domain protein domain protein","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[332-486]T$	no description
PF02518	$\"[365-475]T$	HATPase_c
SM00387	$\"[365-476]T$	HATPase_c

InterPro
IPR003660
Domain

Histidine kinase, HAMP region
PF00672	$\"[187-256]T$	HAMP
SM00304	$\"[207-259]T$	HAMP
PS50885	$\"[207-259]T$	HAMP

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[260-324]T$	HisKA
SM00388	$\"[260-324]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[402-416]T$ $\"[436-454]T$ $\"[460-473]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[267-476]T$	HIS_KIN

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.240	$\"[250-320]T$	no description
PTHR23283	$\"[7-474]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23	$\"[7-474]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[19-39]?$ $\"[186-206]?$	transmembrane_regions

","BeTs to 17 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB004358 (Bacterial sensor protein C-terminal signature) with a combined E-value of 2e-16. IPB004358A 402-416 IPB004358C 436-454 IPB004358D 460-473***** IPB003661 (Histidine kinase A, N-terminal) with a combined E-value of 2.9e-08. IPB003661A 264-276 IPB003661B 406-425***** IPB003122 (Ligand binding Tar) with a combined E-value of 7.2e-07. IPB003122A 212-263***** IPB003660 (Histidine kinase, HAMP region) with a combined E-value of 7e-06. IPB003660C 439-457","Residues 239-468 are 45% similar to a (ASGA KINASE TRANSFERASE PHOSPHORYLATION TRANSDUCTION SENSORY) protein domain (PDA0J762) which is seen in Q6MI65_BDEBA.Residues 270-481 are 45% similar to a (KINASE TWO-COMPONENT TRANSFERASE HYBRID REGULATOR PHOSPHORYLATION TRANSDUCTION SENSORY SENSOR) protein domain (PD153316) which is seen in Q8YSG4_ANASP.Residues 300-369 are similar to a (KINASE TRANSDUCTION SENSORY SENSOR TRANSMEMBRANE PHOSPHORYLATION TRANSFERASE TWO-COMPONENT HISTIDINE KINASES) protein domain (PD782812) which is seen in Q9X801_STRCO.Residues 366-473 are 53% similar to a (KINASE SYSTEM TWO-COMPONENT TRANSFERASE PHOSPHORYLATION TRANSDUCTION SENSORY SENSOR TRANSMEMBRANE HISTIDINE) protein domain (PD752339) which is seen in Q8G5K8_BIFLO.Residues 437-473 are 86% similar to a (KINASE SENSORY TRANSDUCTION PHOSPHORYLATION TRANSFERASE SENSOR HISTIDINE TWO-COMPONENT TRANSMEMBRANE 2.7.3.-) protein domain (PD000064) which is seen in Q84FB2_MYXXA.","","-49% similar to PDB:2C2A STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN (E_value = 7.6E_19);","Residues 187 to 256 (E_value = 3.1e-18) place ANA_0471 in the HAMP family which is described as HAMP domain.Residues 260 to 324 (E_value = 1.2e-11) place ANA_0471 in the HisKA family which is described as His Kinase A (phosphoacceptor) domain.Residues 365 to 475 (E_value = 1.3e-29) place ANA_0471 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","sensor histidine kinase alr5189","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0472","499029","497704","1326","5.27","-18.24","46606","ATGAACCCTCTCAAGCTCACCGTCATCGGCTGCGGATACCTCGGTGCCGTCCACGCTGCCGCCATGGCCCACCTGGGACACCATGTCCTGGGGATCGACACCCGCCCCGAGCAGGTCGAGGCCCTCTCCCAGGGCCGCGCCCCCTTCTATGAGCCGGGGCTGCCCGAGCTCCTGGTCACGGGGGCCCGGCAGGGAGACCTGCGCTTCACCTCAACGCCGACGCCGGCCGAGCTGGCCGAGGCCGACGTCCACTTCATCGCCGTGGGGACCCCGCAGTCCGCCACCGGTGGGGAGGCCGACCTGAGCCAGCTGTGGAGCGTGGTCGACATGCTTCACGACGCCCTGCCCGAGGGCGGGCGCAGCCTGGTGGTGGGCAAGTCCACCGTTCCGGTGGGCACCGCTCAGCAGGTGGCCGAGCGCCTGGCCGGACGCGCCCTGGTGCTGTGGAACCCCGAGTTCCTGCGCGAGGGCTTCGCTGTGGCCGACACTCTCCATCCCGACCGCATCGTCTACGGGGTCCCCTCCGACCCCCATGACGCCCACGAGGCCCAGGCCGCGCTCGACGCCGTCTACCGGGACCTGCTGGAGGAGGGCATCCCCCGGATCGTCACCGACTACCCCACCGCAGAGCTGGTCAAGACCGCGGCGAACTCCTTCCTGGCCACCAAGATCAGCTTCATCAACGCCATGGCCCACCTGTGCGACACCGCAGGGGCCGACGTCACCGTCCTGGCCGACGCCATCGGCCACGACCCGCGCATCGGTCGGCGCTTCCTCCAGGCCGGCGTCGGCTTCGGCGGAGGCTGCCTTCCCAAGGACATCCGGGCACTGCAGGCCAGCGCCGACCTTCACGGCGCCGTGCACCTGGCGGACCTGCTGGGCCGGGTCGACTCCATCAACCGTGAGCAGCGCGACCGGATCGTCGAGCTGGCCCGCACCCACGTGGGCGGCGACCTGTCCGGCCGGGCCATCACCATCCTGGGGGCGGCCTTCAAGCCCCTGAGCGACGACGTGCGCGACTCCCCCGCCCTGGACGTCGCCTCCCGTCTGGCCGGCCTCGGGGCTGAGGTCACTGTCTGTGACCCGCAGGCCCTGCCCGTGGTGGCTCGCTCCCACCCTCACCTCACCTTGGAGGACGATCCCCGCGCCGCGCTCAAGGGAGCCGAGCTCGTCCTGCTGCTGACCGAGTGGGACCAGTTCGTGGCCCTCGACCCCGCTGAGGCCGCCACTGGCGTCGCCGAGCGCGTCATCATTGACGGACGCAACGCCCTGGACCCGGTGGCCTGGCGTGAGGCCGGGTGGACCTACGCGGGAGTGGGACGCTGA","MNPLKLTVIGCGYLGAVHAAAMAHLGHHVLGIDTRPEQVEALSQGRAPFYEPGLPELLVTGARQGDLRFTSTPTPAELAEADVHFIAVGTPQSATGGEADLSQLWSVVDMLHDALPEGGRSLVVGKSTVPVGTAQQVAERLAGRALVLWNPEFLREGFAVADTLHPDRIVYGVPSDPHDAHEAQAALDAVYRDLLEEGIPRIVTDYPTAELVKTAANSFLATKISFINAMAHLCDTAGADVTVLADAIGHDPRIGRRFLQAGVGFGGGCLPKDIRALQASADLHGAVHLADLLGRVDSINREQRDRIVELARTHVGGDLSGRAITILGAAFKPLSDDVRDSPALDVASRLAGLGAEVTVCDPQALPVVARSHPHLTLEDDPRAALKGAELVLLLTEWDQFVALDPAEAATGVAERVIIDGRNALDPVAWREAGWTYAGVGR$","UDP-glucose 6-dehydrogenase","Cytoplasm","Predicted UDP-glucose 6-dehydrogenase","UDP-glucose 6-dehydrogenase ","UDP-glucose 6-dehydrogenase","","Roychoudhury S., May T.B., Gill J.F., Singh S.K., Feingold D.S., Chakrabarty A.M. Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa. J. Biol. Chem. 1989. 264(16):9380-9385. PMID: 2470755Campbell R.E., Sala R.F., van de Rijn I., Tanner M.E. Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol. J. Biol. Chem. 1997. 272(6):3416-3422. PMID: 9013585","","","

InterPro
IPR001732
Domain

UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03721	$\"[4-196]T$	UDPG_MGDP_dh_N

InterPro
IPR013328
Domain

Dehydrogenase, multihelical
G3DSA:1.10.1040.10	$\"[214-307]T$	no description

InterPro
IPR014026
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation
PF00984	$\"[206-303]T$	UDPG_MGDP_dh

InterPro
IPR014027
Domain

UDP-glucose/GDP-mannose dehydrogenase, C-terminal
PF03720	$\"[325-426]T$	UDPG_MGDP_dh_C

InterPro
IPR014028
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding
PTHR11374	$\"[158-441]T$	UDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC DEHYDROGENASE

InterPro
IPR014360
Family

UDP-glucose/GDP-mannose dehydrogenase
PIRSF000124	$\"[4-441]T$	UDP-glucose/GDP-mannose dehydrogenase

InterPro
IPR014685
Family

UDP-glucose 6-dehydrogenase, bacterial
PIRSF500134	$\"[4-441]T$	UDP-glucose 6-dehydrogenase, bacterial type

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1870	$\"[317-437]T$	no description
G3DSA:3.40.50.720	$\"[4-213]T$	no description
PTHR11374:SF3	$\"[158-441]T$	UDP-GLUCOSE 6-DEHYDROGENASE
signalp	$\"[1-19]?$	signal-peptide

","BeTs to 14 clades of COG1004COG name: Predicted UDP-glucose 6-dehydrogenaseFunctional Class: MThe phylogenetic pattern of COG1004 is AM---qvceBr---------xNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 32-88 are 84% similar to a (DEHYDROGENASE UDP-GLUCOSE OXIDOREDUCTASE 6-DEHYDROGENASE NAD 3-HYDROXYISOBUTYRATE BIOSYNTHESIS UDP-GLUCOSE/GDP-MANNOSE UDP-GLCDH UDPGDH) protein domain (PD398280) which is seen in Q6AGX8_BBBBB.Residues 33-305 are 43% similar to a (LMBL) protein domain (PD824343) which is seen in Q54365_STRLN.Residues 83-462 are 45% similar to a (DEHYDROGENASE UDP-GLUCOSE/GDP-MANNOSE FAMILY UDP-GLUCOSE-6-DEHYDROGENASE) protein domain (PD102173) which is seen in Q93N63_COXBU.Residues 244-332 are similar to a (UDP-GLUCOSE DEHYDROGENASE 6-DEHYDROGENASE OXIDOREDUCTASE NAD UDP-GLCDH UDPGDH UDP-GLC SUGAR NUCLEOTIDE) protein domain (PD001282) which is seen in Q82DF7_STRAW.Residues 314-464 are 45% similar to a (UDP-GLUCOSE 6-DEHYDROGENASE) protein domain (PDA131E5) which is seen in Q6NEW8_CORDI.Residues 345-390 are 76% similar to a (UDP-GLUCOSE DEHYDROGENASE 6-DEHYDROGENASE OXIDOREDUCTASE UDP-GLUCOSE/GDP-MANNOSE POLYSACCHARIDE BIOSYNTHESIS NAD PROBABLE FAMILY) protein domain (PD102170) which is seen in Q8NLU0_CORGL.Residues 350-449 are 56% similar to a (UDP-GLUCOSE DEHYDROGENASE 6-DEHYDROGENASE OXIDOREDUCTASE NAD NUCLEOTIDE SUGAR UDP-GLCDH UDPGDH UDP-GLC) protein domain (PD005757) which is seen in Q8U172_PYRFU.","","-52% similar to PDB:2O3J Structure of Caenorhabditis Elegans UDP-Glucose Dehydrogenase (E_value = 2.8E_60);-50% similar to PDB:1MFZ Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa (E_value = 2.0E_42);-50% similar to PDB:1MUU 2.0 A crystal structure of GDP-mannose dehydrogenase (E_value = 2.0E_42);-50% similar to PDB:1MV8 1.55 A crystal structure of a ternary complex of GDP-mannose dehydrogenase from Psuedomonas aeruginosa (E_value = 2.0E_42);-47% similar to PDB:1DLI THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION (E_value = 5.1E_22);","Residues 32 to 224 (E_value = 2.6e-59) place ANA_0472 in the UDPG_MGDP_dh_N family which is described as UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain.Residues 234 to 331 (E_value = 3.7e-44) place ANA_0472 in the UDPG_MGDP_dh family which is described as UDP-glucose/GDP-mannose dehydrogenase family, central domain.Residues 353 to 454 (E_value = 2.6e-32) place ANA_0472 in the UDPG_MGDP_dh_C family which is described as UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain.","","UDP-glucose 6-dehydrogenase (UDPGDH)","","1","","","Fri Aug 10 17:00:32 2007","","Fri Aug 10 17:00:32 2007","","","Fri Aug 10 17:00:32 2007","Fri Aug 10 17:00:32 2007","Fri Aug 10 17:00:32 2007","","","Fri Aug 10 17:00:32 2007","","","Fri Aug 10 17:00:32 2007","Fri Aug 10 17:00:32 2007","Fri Aug 10 17:00:32 2007","","Fri Aug 10 17:00:32 2007","Fri Aug 10 17:00:32 2007","","","","","yes","","" "ANA_0473","500060","499026","1035","7.27","1.72","37959","ATGCTCAGCACGCTGCGCGCCATCCCCGGACTGCGCCGGGCCTGGCCCGCCACACGAGACTCGGGCCCCGCGAGCGTGAGCATCGAGTGCGTCGATGGCCAGGGCCGTCTGCGCGCCGGACACGTCACCATGGGGGGCGCCCCCGATCTGCTGCCCTACGCCAGTGACCCGGCCCTGCCGACCCTGTCCACGCAGCTGACCGGGAGACTCGTCGTCCACCGCGCCGGCCGCCGCGCCGTCGTGATGGAGGCCTCCCGGGTCCGCAAGATGGTGCGGCCCCACAAGGCCGCCTCCCTGGTGCGGGCCCACACGACCGCCGCCTCGGTGCTACAGGTCACCGGCCTACGAATGCCCAGGATCCTGGGCAACGGGGACGACGTCGTCGATCTCGAGCTGCTGCCGGGCCACAGTCTCGACGAGCTCGGTGATGCCGGCCTGCCCGGATGGCAGCGGTTCACGGAGGCCTGGTCGCGCCTGGGTGAGCGTGAGGCGGATCTGCCTGTTCACGGGCCGCGTCAGGAGGCCGAGGTGCTGCGGCGCTGGCTGGCCTCGGCCCGCCGCTACGGCGTCATCGACCAGCAGGACCTTCTGCACGAGCAGGTGGTGGACACCTGCCTGAGCCTGAGGGAGGGAAGCGAGACACACGTCATCACCCACCGCGACCTCCACGACGGACAGCTCCTGTGGGACGGAACCGACCTGTCCCTGCTCGACCTGGATACCGCGGCCATGGCCGAGGCGGCCCTCGATCTGGGCAACCTCTGGGCCCACGCGGATCTCATGGCGGTTCGTGGCCGGCTCGGCCCCGAGGCCCACTGCCGGGTCCGCGGACTGCTCGACGACCTGGCTCGCACGCTGCCCGTGACGGCGCAGCGCCTGGAGACCTACTACCGCTCCTCAGCACTGCGGCTGGTCTTCGTCCACGCCTTCCGTCCCTCCTCCCACCAGTGGCTGCCCGTCTGGGTGCGCCACTGCCTGGGACACGCCTCCCCCTTCATGCCCCTGGACCTCACCAACGATTGGAACAACTCATGA","MLSTLRAIPGLRRAWPATRDSGPASVSIECVDGQGRLRAGHVTMGGAPDLLPYASDPALPTLSTQLTGRLVVHRAGRRAVVMEASRVRKMVRPHKAASLVRAHTTAASVLQVTGLRMPRILGNGDDVVDLELLPGHSLDELGDAGLPGWQRFTEAWSRLGEREADLPVHGPRQEAEVLRRWLASARRYGVIDQQDLLHEQVVDTCLSLREGSETHVITHRDLHDGQLLWDGTDLSLLDLDTAAMAEAALDLGNLWAHADLMAVRGRLGPEAHCRVRGLLDDLARTLPVTAQRLETYYRSSALRLVFVHAFRPSSHQWLPVWVRHCLGHASPFMPLDLTNDWNNS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","Fri Aug 10 17:03:35 2007","","Fri Aug 10 17:03:35 2007","","","Fri Aug 10 17:03:35 2007","Fri Aug 10 17:03:35 2007","Fri Aug 10 17:03:35 2007","","","","","","Fri Aug 10 17:03:35 2007","","","","Fri Aug 10 17:03:35 2007","Fri Aug 10 17:03:35 2007","","","","","yes","","" "ANA_0474","500081","500932","852","7.74","3.13","29376","GTGTCATCTCAGTCCTTGGTGTTGTCCTCGTCGTGTCCGTCATGCCCAGGTGGTCTCCTCTCCAGGCGACTGGGCGATGCGCTCGATGGCGGTCAGGTCCGCGCCGATGCGCTCGCGCCAGGACGGGTGTGCCCGTCGCAGGGGGTCGGCCAGCCGCGCCAGCCGGGACAGTGCGATCGCCCACCCCAGCTCCTCGGCGCCCGGCACCGGCCGGTGCGTGGCGTAACCCTCCAGCAGTGCATGCCGCTGAGAGGGCGGAGCCTCCGCCAGGTAGGAGCCCAGGTCCATGGCCGCCGGAGCCAGGCGCACCCGGTCGAAGTCGGTCAGCCAGATCCGCCCGGTGGAGTACTCGTAGAGCACCTGGTCGGGGGAGACGTCGCCGTGGGCGAGAACCGGTGTCCCGGTGAGAAGGGAGGGCAGCATGTCACCCACCGCCCGCACCCGGCGTGCCAGCTCAGGGGCCAGGACATCGAGCTGCCGGGCGTGGACCTCGGCCAGGTCCCGGAAGCCGGGAGGCTGATGCGGCAGCCGGTCGATGAGGCCGGCCGACAGCTGCCCGACGCAGGAGTGCAGCTCGGCCAGCAGAGCCCCCACACGCCTGCTGGCCTCCTTGAGGCTCTGTGCAGTGGCCGGACCATCAGCGTTGTCCGCATAGAAGTCAGCCAGGTTCGTGTCCCCGCACCACTGCTGCACGCTGACGCGGCCCTCGCACCGGGCCACGGCCTGCGAGTCGAGCAGGCCGGGGACCGGGAGGAGCCCGGACAGGGCGCGGTGGACGTCGTCAGCCGGCCCGCCGGCTCCAGCTCGCAGTCGCAGGACCGTGGAGCCGTCACGCAGGACCAGGCGCCGTGA","VSSQSLVLSSSCPSCPGGLLSRRLGDALDGGQVRADALAPGRVCPSQGVGQPRQPGQCDRPPQLLGARHRPVRGVTLQQCMPLRGRSLRQVGAQVHGRRSQAHPVEVGQPDPPGGVLVEHLVGGDVAVGENRCPGEKGGQHVTHRPHPACQLRGQDIELPGVDLGQVPEAGRLMRQPVDEAGRQLPDAGVQLGQQSPHTPAGLLEALCSGRTISVVRIEVSQVRVPAPLLHADAALAPGHGLRVEQAGDREEPGQGAVDVVSRPAGSSSQSQDRGAVTQDQAP$","Hypothetical protein","Cytoplasm, Extracellular","Similar to proline-rich protein BstNI subfamily2, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","to proline-rich protein BstNI subfamily 2, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0475","503163","501337","1827","10.00","13.08","64636","ATGGGCTCGCTTCCTCGTCGTCACGGACGCAGTCGGGTACGTCAGTCCCCCATGCGGCAGACCCTGAGGCTGGTGGGCCCTGATGCAGCGCCGCAGTGGCGTCTCATGGCCGGCGGCACGGTGGTACTCCTGGCGGAGGTGATCTTCCGGGTGCTGGAGCCCTGGCCGCTGAAGGTCGCCATCGACTCACTGGTGGCGGCTCTGGGCCGCCACACGGGCAGCGCCCCCGCCACAGTCTCCTCACTGGTGGGGCTCGGTATCGCCCTGCTGGTGATCGTGGCCGGCCGGGCGGTGTGCAACTACCTGGCCACCGTGGCCTTCGCCCTGGTGGGCTCGCGCACCGCGGCCTCCCTGCGCAGCCGGGCCTTCCACCACGTCCAGGGCCTGTCCCAGCAGTTCCACGCCCGCAACCGCAGCGCGGACACGGTTCAGCGACTCATCGCCGACGTCAACCGCATGCAGGAGGTGGCTGTCACCGCCGGCCTGCCGATGGCCGCCAACACCTTGACCCTGCTGGTCATGGTCGTCGTCATGGTGTTCCTGGACCCGCTGCTGGCCATGATCGTGCTCCTGGCGGTGGTGGCCTTCATGCTCGCCTCCTCGGGCAACTCGCGGCGGATCTCCGCGGCCTCCCTGCGCAGCCGCAAGTCGGAGGGGAACCTGGCCAACACCGCCCAGGAGGCGCTCGGGGCCATCAAGGTCGTCCAGGCCTACGGTCTGGAGCCGCTGCTCCATGAACGTTTCACGGGCGCCAATACGGTGTCACTCAGTGAGGGGGTGCGCTCACGCCGGATCGCCGCGCGCCTGGAGCGCTCCACGGACGTCATCGTCGGCGTGGCGACCGCCGTGGTGATGGTCGGTGGGGGCATCCGGGTCCTGAACGGCGCCATGTCCCCGGGGGACCTGGTGCTGTTCACGACCTACCTGCGCACCACCATGAAGCCGCTTCGGGACATGGCCAAGTACACCGGCCGCATCGCCCGGGCGACGGCCTCGGGTGAGCGGGTGGCCGACCTCATGGCGGTCAAGCCAGACATCGTCTCCCCTGCTGACGCCATCGTGCTGGACCGGGTCCGCGGCATGATCCACTTCGACCACGTGCACGCCGCCTACGAGGGTCGCCCGGTGCTGCACGGTGTGAACCTGACGGTGGTTCCCGGCGAGCACGTGGCCCTCGTGGGACCGTCGGGCTCGGGCAAGTCCACCCTGGTGTCCCTGGTGGTGCGAGCCCTGGATCCGACGTCCGGCACGGTGAGCCTGGACGGGCACAGCCTGGACGATCTGGATCTTCGCTTCCTGCGCTCGCAGGCCTCGGTCCTGCACCAGGAGGCGGTTCTGCTGACCGGCACGATCCGGGAGAACATCCGGCTGGGGCGGCCAGATGCCTCCGACGAGGAGGTGGAGGCGGCCGCGCGTGCTGCCCACGCCCACGACTTCATCACCCAGATGCCCGGCGGCTACGACACTGCCGTGGGCGAGCGGGGCGGCACTCTGTCCGGCGGTCAGCGCCAGCGCATCGCCATCGCGCGGGCGCTTCTGCGCAACTCGCCGATCGTCATCCTGGATGAGGCGACCACCGGGCTGGATCCGGCCTCGACGTCGGCGGTGCTGGAGGCGATCGATGAGCTGGTTGCCGGGCGCACGACCTTGACCGTCACTCACGACCCGCAGGCCGCCATGCGCGCCGACCGGGTGGTGTGGATCCAGGACGGGCGGATCCGCCTGGAGGGCAGCCCTCAGGACCTCATGGAGTCCTCGGCCGAGTTCCGTCGGTGGGCGAACAGTCACCTGGCCGAGTCCTTCGCGCTGGTGGGGAGCGGATCATGA","MGSLPRRHGRSRVRQSPMRQTLRLVGPDAAPQWRLMAGGTVVLLAEVIFRVLEPWPLKVAIDSLVAALGRHTGSAPATVSSLVGLGIALLVIVAGRAVCNYLATVAFALVGSRTAASLRSRAFHHVQGLSQQFHARNRSADTVQRLIADVNRMQEVAVTAGLPMAANTLTLLVMVVVMVFLDPLLAMIVLLAVVAFMLASSGNSRRISAASLRSRKSEGNLANTAQEALGAIKVVQAYGLEPLLHERFTGANTVSLSEGVRSRRIAARLERSTDVIVGVATAVVMVGGGIRVLNGAMSPGDLVLFTTYLRTTMKPLRDMAKYTGRIARATASGERVADLMAVKPDIVSPADAIVLDRVRGMIHFDHVHAAYEGRPVLHGVNLTVVPGEHVALVGPSGSGKSTLVSLVVRALDPTSGTVSLDGHSLDDLDLRFLRSQASVLHQEAVLLTGTIRENIRLGRPDASDEEVEAAARAAHAHDFITQMPGGYDTAVGERGGTLSGGQRQRIAIARALLRNSPIVILDEATTGLDPASTSAVLEAIDELVAGRTTLTVTHDPQAAMRADRVVWIQDGRIRLEGSPQDLMESSAEFRRWANSHLAESFALVGSGS$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","ATP-binding protein of ABC transporter all5193","ABC transporter related","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[36-316]T$	ABC_membrane

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[387-571]T$	ABC_tran
PS50893	$\"[362-595]T$	ABC_TRANSPORTER_2
PS00211	$\"[498-512]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[386-572]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[37-328]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[327-593]T$	no description
PTHR19242	$\"[10-586]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91	$\"[10-586]T$	LIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA
tmhmm	$\"[79-99]?$ $\"[179-199]?$ $\"[275-295]?$	transmembrane_regions

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[190-363]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-380]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF44	$\"[2-380]T$	GLYCOSYLTRANSFERASE

","BeTs to 18 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","Residues 1-193 are 60% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE ICSA LPS) protein domain (PD107679) which is seen in Q8YLV2_ANASP.Residues 181-313 are 45% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL TRANSFERASE GROUP FAMILY REPEAT POSSIBLE PLASMID TRANSFERASE-LIKE) protein domain (PD024797) which is seen in TUAH_BACSU.Residues 196-373 are 42% similar to a (WBMJ BBLPS1.12) protein domain (PD185747) which is seen in Q7W256_BORPA.Residues 208-267 are 61% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS GROUP TRANSFERASE SYNTHASE FAMILY STARCH LIPOPOLYSACCHARIDE) protein domain (PD000427) which is seen in Q8YLV2_ANASP.","","No significant hits to the PDB database (E-value < E-10).","Residues 190 to 363 (E_value = 5.7e-22) place ANA_0476 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","all5194 ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0477","505627","504332","1296","5.98","-6.69","46463","ATGAATCCCCCACTCGACACCCACCAGCCCCACCAGGGCGCCCCCCGTATCGGATACGTCCTCAAGGTCTACCCCCGCTTCTCGGAAACCTTCATCGTCACCGAGATCCTGGCCCGCGAGGCCCAGGGCGAGGACCTGAGCATCTATGCACTGCGCCCCACCACGGATGCGCGCTTCCACCCCGAGATCGCCCGGGTCGCCGCCCGCGTCAACTGGGTGGGCCGACCGAACCGGGCCATCGACCTGTGGAGCCAGCTCACCGAGGGCCTGACCCGCCAGGAGGACCGCGAGCGCTTCGCCGCCATCATGCCGGTCCTGGCCGAGCTGCCCGGTGACGTGGTGGCCCAGGGCGTGGAGCTGGCGCGTCAGGCACGCCGGGACTCCATCACCCACCTGCACGCGCACTTCGCGTCCCTGGCGGGGCGGGTGGCGTGGATCGCCTCGGCCCTCACCGGCATCCCCTACACCGTGACCACCCATGCCAAGGACATCTTCCACGAGTCGGTGGACCCGGTGTGGCTGCGCCGGATCTGCTCCGATGCCCAGCGGGTCATCGCCATCAGCCGTTACAACGAGGACTACCTGGGAACTGTGCTGGCGGGCACGGGGGCCACGGTGTCGCTGCGTTACAACGCCCTGGAGCTGGATCGCTTCTCCTACCGTGCCCCGCAGCCGGTGTCCGCCACGAGGGCAGAGCCGCTGCGGGTGTGCGCCGTGGGTCGTCTGGTGCCCAAGAAGGGCTTCGCCGATCTGGTCGAGGCGGTGAGGATCCTGGTGAGCTCGGGGATCGATGTCGAGGTGGAGCTGGCCGGTGACGGCGATGAGCGCGAGCGCCTGACCGAGCAGATCGAGCGCCTGGGACTGGCCGACAGGATCCGTCTGCTGGGTCCGCTCACGCAGGCAGAGGTGCGCGAGCTGCTGGCGCGCTCGCACGTGTTCGCGGCGCCGTGCATCGAGGCGGCCGACGGCAATATCGACGGTCTGCCCACGGTGGTCCTGGAGGCGATGGCCTGCGGGACGCCGGTGGTGGCCACGGCGGTGTCGGGACTTCCGGAGGTGGTTCACGACGGCGTCACCGGGATTCTTCTTCCCCCGGGTGACCCGGCCTCGCTGGCCGTGGCCCTGCGCGGGATCGCACAGGGCAAGGTGGACATCGTCGCGCTGTCGCGCGGTGCGCGGGCACTGATTGAAGAGCAGTTCGACTCTCGGGCCCAGGCCGCGGTGCTGGCCGCCTGGCAGTCGGGTCCCGTCCCGGCTTCCGGCGTGCGCCTGGCCGATCAGGAAGGAGCCGCCTGA","MNPPLDTHQPHQGAPRIGYVLKVYPRFSETFIVTEILAREAQGEDLSIYALRPTTDARFHPEIARVAARVNWVGRPNRAIDLWSQLTEGLTRQEDRERFAAIMPVLAELPGDVVAQGVELARQARRDSITHLHAHFASLAGRVAWIASALTGIPYTVTTHAKDIFHESVDPVWLRRICSDAQRVIAISRYNEDYLGTVLAGTGATVSLRYNALELDRFSYRAPQPVSATRAEPLRVCAVGRLVPKKGFADLVEAVRILVSSGIDVEVELAGDGDERERLTEQIERLGLADRIRLLGPLTQAEVRELLARSHVFAAPCIEAADGNIDGLPTVVLEAMACGTPVVATAVSGLPEVVHDGVTGILLPPGDPASLAVALRGIAQGKVDIVALSRGARALIEEQFDSRAQAAVLAAWQSGPVPASGVRLADQEGAA$","Glycosyl transferase, group 1","Cytoplasm","glycosyltransferase all5195","glycosyl transferase; group 1","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[220-372]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[142-167]T$ $\"[199-403]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF41	$\"[142-167]T$ $\"[199-403]T$	GLYCOSYLTRANSFERASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2000	$\"[212-385]T$	no description

","BeTs to 3 clades of COG1819COG name: Glycosyl transferases, related to UDP-glucuronosyltransferaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1819 is --m---y--dr-bcefg----j----Number of proteins in this genome belonging to this COG is 2","***** IPB004276 (Glycosyl transferase, family 28) with a combined E-value of 1.2e-06. IPB004276E 302-329 IPB004276F 333-354","Residues 7-203 are 57% similar to a (PLASMID TRANSFERASE REDA SLIGHTLY AGR_C_4697P SLL1722 MLR3252 SIMILAR ATU2590 UNDECAPRENOL) protein domain (PD140854) which is seen in Q8YLV0_ANASP.Residues 231-328 are 53% similar to a (ALR5197 GLR1063 REDA AGR_C_4697P) protein domain (PD875994) which is seen in Q8YLU9_ANASP.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0479","507805","507029","777","5.47","-7.43","27191","ATGTCTCGGCATGATCGGCATTCGGCCATCCTCGACATCATCATGGACGAGGGCAGCGTCCATATCGACGACATCATCACGCGGTTGGGGGTCTCGGCAGCGACCGCACGACGCGACCTCGACCATCTGGCGGACCAGCAGCTGATCAGCCGTACCCGCGGCGGCGCCATTGCCAACCCCACCTCCACCGAGCCTCCTCTGCGCTACCGCACCTCCAAGATGGCCGATGAGAAGACCCGTATCGCCAAGGCAGCGGCTGCTCTGGTGCACCCGGGCGACTCCGTCGGCCTCAACGGCGGCACCACGACCACCGAGGTGGCTCGCGAGATCGCGCTCCTACCGGAGCTGACCGATCCAGAGGTGCCGGTCACCCTCGTCACCAATGCCGTCAACATCGCCAACGAGATGGCCGTGCGCCAGTGCGTGCGCGTCGTCGTCACCGGCGGGATCGCGCGAGCCCGTTCCTTCGAGCTCACCGGCCCCCTGGCCTCTCTCATCCTTCCCTCGATCAGCGTGGGCACGCTCTTCCTGGGAGTCGAGGGCCTCGATGAGCGAGGCGCCTACGCCCAGCACGACGGGGAGGCGGCCGTCAACGCCGCCCTGGTTGAGGCCGCCGAGCACGTCGTCATCGTGTGCGACAGCTCCAAGCTGGGCAGGACGGCCTTCGCCCTCATCTGCCCCAGCACCAAGATCGACACGATCATCACCGACGATGCCGCCCCCGCCGACCAGGTTGAGGCCCTGCGGCAAGCCGGAGTCCAGGTGCGACTGGTCTAG","MSRHDRHSAILDIIMDEGSVHIDDIITRLGVSAATARRDLDHLADQQLISRTRGGAIANPTSTEPPLRYRTSKMADEKTRIAKAAAALVHPGDSVGLNGGTTTTEVAREIALLPELTDPEVPVTLVTNAVNIANEMAVRQCVRVVVTGGIARARSFELTGPLASLILPSISVGTLFLGVEGLDERGAYAQHDGEAAVNAALVEAAEHVVIVCDSSKLGRTAFALICPSTKIDTIITDDAAPADQVEALRQAGVQVRLV$","Transcriptional regulator, DeoR family","Cytoplasm","Transcriptional regulator of sugar metabolism","K02081 DeoR family transcriptional regulator; aga operon transcriptional repressor","regulatory protein, DeoR","","Beck von Bodman S., Hayman G.T., Farrand S.K. Opine catabolism and conjugal transfer of the nopaline Ti plasmid pTiC58 are coordinately regulated by a single repressor. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(2):643-647. PMID: 1731335Ray W.K., Larson T.J. Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12. Mol. Microbiol. 2004. 51(3):813-826. PMID: 14731281","","","

InterPro
IPR001034
Domain

Bacterial regulatory protein, DeoR N-terminal
PR00037	$\"[24-38]T$ $\"[38-56]T$	HTHLACR
PF08220	$\"[6-62]T$	HTH_DeoR
SM00420	$\"[6-58]T$	HTH_DEOR
PS51000	$\"[3-58]T$	HTH_DEOR_2
PS00894	$\"[6-40]T$	HTH_DEOR_1

InterPro
IPR014036
Domain

Bacterial regulatory protein, DeoR
PF00455	$\"[75-237]T$	DeoR

","BeTs to 8 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K [Information storage and processing--Transcription] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is 4","***** IPB001034 (Bacterial regulatory protein, DeoR family) with a combined E-value of 8.9e-55. IPB001034A 18-56 IPB001034B 77-110 IPB001034D 144-161 IPB001034E 197-237","Residues 6-86 are 72% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR DEOR FAMILY REGULATOR OPERON) protein domain (PD469489) which is seen in Q9K3L7_STRCO.Residues 88-183 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR DEOR FAMILY OPERON REGULATOR) protein domain (PD002430) which is seen in Q82N56_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 62 (E_value = 1.2e-16) place ANA_0479 in the HTH_DeoR family which is described as DeoR-like helix-turn-helix domain.Residues 75 to 237 (E_value = 4.8e-35) place ANA_0479 in the DeoR family which is described as Bacterial regulatory proteins, deoR family.","","regulator of sugar metabolism (srl)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0480","508147","509181","1035","4.51","-22.98","35025","ATGGGGGTCGATGTCAGTGCCGACGCCGTCACCGCGGTTGTCGCTGACGGCCGGGGGGACGTCGTCTCCTCTGTGGAGAAGCCGGTTCCCAATGAGTGTCGCTCGGACGCCGACCGGCTGGCCCAGGAGGTCGGGAGCGCGATCCGATCCTTGTACGCGAGCCTCACCGACGACCTCGACCTCAGTGGCGGGGCGCCGGGTGTGACGGCCCTTGTCGTCGGGATCAGCGTGCCCGGCGTCGTCGACGAGGATGAGGGGTGCGTGCGCCGCAGTGAGGCTCTCGGGTTGCAGGACACCCCGTTGGCAAGCCTGGTGAGGCAGTCGCTGTCGTCTTGGGCCGCTGAGGTGCCCGGGCTATCCGGAGGCCTTGAGGTGAGGCTCTATCAGGATGCCGGTTGCGGCGCCTGGGCCGAGAGTCAGTGGGGTGCGGCCGGGAGGGACTGCCTCTATCTGGCGGTCGGTGAGCGAATCTCCTCCGCCGTCCTGCTGGGTGGCGTCCCAGTGCTCGGTGAGGGCTGGGCTGGTCAGGTCGGTCGGATTCTGGTACCCGATCCGGACTGGAGCGGGGAGAGGGCCCGTCTGGAGGATGTCGCCTCGATGTGCGCCATGGTGAAGCGGCACACTGCCGGCAAGCTCGATGACTCCGCAGTCTCTTTCGGCTCTGGTGGCGCAGCGCCCGAGCCTGGCGGCTGCGATGACGCTTCCGATGAGTCGTTCCCCCAGTGCGCCTCGGGCCTGGAGTCCCTCCTGGGTGCGATAGCTGCTGGGGACCGGGAGGCGCGCCGGGTCTGGGATACCGGCCTGGACTGCCTGGCTGAGCTCGTCGCTCAGGGGGTGGGTCTGCTCGGCCCCCTCGACGTCGTCGTCAACTCCGAGCTGATGCCGGCTGACGAGGGCGCATTCCTGGAGCCCCTGCGACGCCGGGTGGCTGATCTCGTGGGCGACCTGCCGGCGCCGCGGCTGGTGGCGGCCCGGCTCGGGGCGACCGCCGCAGTGCAGGGAGCAGCGGGGCGCGCACTGGCTGGCTGGAAGTAG","MGVDVSADAVTAVVADGRGDVVSSVEKPVPNECRSDADRLAQEVGSAIRSLYASLTDDLDLSGGAPGVTALVVGISVPGVVDEDEGCVRRSEALGLQDTPLASLVRQSLSSWAAEVPGLSGGLEVRLYQDAGCGAWAESQWGAAGRDCLYLAVGERISSAVLLGGVPVLGEGWAGQVGRILVPDPDWSGERARLEDVASMCAMVKRHTAGKLDDSAVSFGSGGAAPEPGGCDDASDESFPQCASGLESLLGAIAAGDREARRVWDTGLDCLAELVAQGVGLLGPLDVVVNSELMPADEGAFLEPLRRRVADLVGDLPAPRLVAARLGATAAVQGAAGRALAGWK$","ROK family protein","Cytoplasm","putative sugar kinase","ROK family protein","ROK family protein","","Titgemeyer F., Reizer J., Reizer A., Saier Jr M.H. Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 1994. 140:2349-2354. PMID: 7952186","","","

InterPro
IPR000600
Family

ROK
PF00480	$\"[2-203]T$	ROK

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 203 (E_value = 4.5e-06) place ANA_0480 in the ROK family which is described as ROK family.","","sugar kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0482","509261","510043","783","8.78","5.07","28808","ATGGGTGCAGGCCATGGCAGTATGTTCGCCAACTGCAGTCGTCCAAGCCGGTTGAGGAGAATCAAACGTGTCCCCCAGGAGAGAAGCGAGGCGCAGCGCGTGACCCCGTCTGCTCGTCCGCTTCGCATCGGCATCATGGGCGGAACCTTTGATCCGATCCACCATGGGCACCTGGTTGCAGCCAGTGAGGTGCAGAACGTCTTCGCTCTCGACGAGGTCATCTTCGTGCCCACCTGGGCCCAGCCCTTCAAGAAGGAGCGCAAGGTCTCACCGGCCGAGCACCGGTACCTCATGACGGTCATCGCCACGGCCTCCAACCCGAGGTTCACGGTCTCCCGGGTCGATATCGACCGGGGTGGGACGACCTACACGATCGATACCCTTCATGACATCGCGGCCGAGTATCCGGGCGCGGAGCTGTACTTCATCACTGGAGCCGACGCCCTGGCACAGATTCTCACCTGGAAGGACAGTGAGGAGATCTTCGACCTGGCTCATCTGGTGGGGGTGACGCGTCCCGGGCACGTCCTCAGTGACTCCGGGGTTCCCCGTGACCGGATCTCGCTGGTGGAGGTGCCGGCCATGGCGATCTCGTCGACCGACTGCCGTCAGCGGGTCGGGGAGGGGGCACCGGTGTGGTACCTGGTTCCTGACGGTGTCGTGCAGTACATACGCAAGTACGGGCTCTATCGTATGGCCTTGCGGCCGGCGTCGGCGACGTCGATGACGGCGAGAGTGGCCCGCGAGCAGTCCCTGAGGAAGGAGAACGACGGTGAGCACTGA","MGAGHGSMFANCSRPSRLRRIKRVPQERSEAQRVTPSARPLRIGIMGGTFDPIHHGHLVAASEVQNVFALDEVIFVPTWAQPFKKERKVSPAEHRYLMTVIATASNPRFTVSRVDIDRGGTTYTIDTLHDIAAEYPGAELYFITGADALAQILTWKDSEEIFDLAHLVGVTRPGHVLSDSGVPRDRISLVEVPAMAISSTDCRQRVGEGAPVWYLVPDGVVQYIRKYGLYRMALRPASATSMTARVAREQSLRKENDGEH$","Nicotinic acid mononucleotide adenylyltransferase","Cytoplasm","Nicotinic acid mononucleotideadenylyltransferase","putative nicotinate-nucleotide adenylyltransferase ","nicotinate (nicotinamide) nucleotide adenylyltransferase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR004820
Domain

Cytidylyltransferase
PF01467	$\"[45-205]T$	CTP_transf_2

InterPro
IPR004821
Domain

Cytidyltransferase-related
TIGR00125	$\"[43-108]T$	cyt_tran_rel: cytidyltransferase-related do

InterPro
IPR005248
Family

Probable nicotinate-nucleotide adenylyltransferase
PTHR12039	$\"[27-242]T$	NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE
TIGR00482	$\"[45-230]T$	TIGR00482: nicotinate (nicotinamide) nucleo

InterPro
IPR013166
Domain

Citrate lyase ligase, C-terminal
SM00764	$\"[94-224]T$	no description

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[36-230]T$	no description

","BeTs to 15 clades of COG1057COG name: Nicotinic acid mononucleotide adenylyltransferaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1057 is ------yqv-rlbcefg-snuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB004820 (Cytidylyltransferase) with a combined E-value of 4.8e-06. IPB004820 48-57","Residues 46-97 are 88% similar to a (ADENYLYLTRANSFERASE DEAMIDO-NAD NICOTINATE-NUCLEOTIDE NICOTINATE PYROPHOSPHORYLASE NAMN DIPHOSPHORYLASE MONONUCLEOTIDE PROBABLE NAD) protein domain (PD416729) which is seen in Q7TYM1_MYCBO.Residues 98-230 are 84% similar to a (ADENYLYLTRANSFERASE DEAMIDO-NAD NICOTINATE-NUCLEOTIDE NICOTINATE MONONUCLEOTIDE PYROPHOSPHORYLASE DIPHOSPHORYLASE PROBABLE NAD NAMN) protein domain (PD009578) which is seen in NADD_COREF.","","-57% similar to PDB:1KAM Structure of Bacillus subtilis Nicotinic Acid Mononucleotide Adenylyl Transferase (E_value = 5.1E_33);-57% similar to PDB:1KAQ Structure of Bacillus subtilis Nicotinic Acid Mononucleotide Adenylyl Transferase (E_value = 5.1E_33);-51% similar to PDB:1YUL Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa (E_value = 1.0E_25);-51% similar to PDB:1YUM Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa (E_value = 1.0E_25);-51% similar to PDB:1YUN Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa (E_value = 1.0E_25);","Residues 45 to 205 (E_value = 4.3e-46) place ANA_0482 in the CTP_transf_2 family which is described as Cytidylyltransferase.","","acid mononucleotide adenylyltransferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0483","510033","511721","1689","4.23","-54.93","57430","GTGAGCACTGAGCAGACCGGCGTCAATGCCCCCACGTCCGAGGAGCCGACGCCAGATGAGCACGCTCCACGCGGTAGTCGTCGTGCGATCCGGCAGGCGGAGCGCGCCGCGGAGCGCGAGGCGATCCTGACCGGTCAGCAGCCGCTCCTGACCCGGCGTGAGATGAGGCGTCTGCGTGAGGAGGCCAAGGCGCTCAGGGCTGCCGTCGAGGCGGGCGAGATCACCCCTGAGCAGGCTCAGGCGCTCCAAGACCCTCTTGCTGATCCCACGTCGGTCACCTCCCGTTCCTCCGCCACCTCCGGTGACGAGGGCGAGTCCGGGCCGGGGGAGCCGGACGAGCCAGTTGCTGTGGACGGGGGGGACTATCTCGAGCAGGGAGGGCAGAACCCACCCCTGAGCATGTCCGCCCCCGAGGGGTCGGCTGCCTCCGCCCCGAGCTGGCGCTCGCTGTCGGCGGCCGAGGCCGTGGCGATCTCCGAGATCGAGACGGGCCTGATGGAGGCGGTGGACCTGCCGGTGGCCACTCTTGACTACGACGCTCACTGGGCCGCGAACGCCAGCTCCGAGCCGGCGCCGGTCCCCACTCGCTTCTCACTCAAGGACCGCCTTGAGGGAGGCTCCGTCCCCGAGGTGGAGGAGCCGGAGAGCCCGCAGGACAACGAGTCTCAGGGCGCCGTTGAGACGAGCGACGACGCTGAGGCTGAGGAGCCCGCCACCAGCCCTTACGACTACCGGGAGGGTCTGGAGTCGGCGGCCCAGGACGACGGGGATGCCTCCTCGCAGTCCTCCTCAGCGACCGACGCCGTGAGTGCCGCCTCCGCTGTTCCTGCTGTTTCGGCGACGGCCTCCGGTGCCGCTGACTTCGCCGCCTACGGGCAGGCCGGGGCCGCGCGGTCCACTGAATCCGCCCGCAGCGGTGTCAGTGCCGGGTCAGCGTCCTCAGCAGGCTCGGTGCGCCGACCCATCGTGCGGATTCCGGCCGCTGCGCAGGGGGTACGCACCGTGAACGCCTCCACGGGAGAACTCAGCTCGGTCCAGCCCGTGGACAGCTCGCCGTCGGCCCAGGAGGCCGCCGACGCGCAGGATGTCTACGGAGCCCCCTCCATCGAGGAGCCGATGGTGCAGGGTGGCGCTGAGGTCGAGATCGACGTCGAGGCGCAGACCATGGTGGTTCCGGCATCGGAACCCTCGACTCAGGGTGCGCAGGACTCCGAGTTCGGTGCGCCCGGGGCCCCACAGTGGAGGTCGCTGCATCAGGCCCCGCAGGCGGGCAGCTTCCAGGAGGCGATCGTGGACGGGACGGCTGAGACCGCAGCCGTCTCCGGTGAGGCCGTCAGCCCCTACGCCTTCTACAGCGACGAGGTCGAGAACGGCAACGGTCCAATGGGGGCCTCCGAATGGGACTCTGTGGCGGTCCCGGCTGCCGAGGTGCCCGAGGAGCCCTACCTGGCTCCGGTCAACGAGGTCACCGGAAGGGTGCCCACCCCGGATCACGTCCTGCCGATGGAGCAGCCCGGTTCCTCCTCGCGCATCGGTAAGATCCTCATGGCCGCACTTATCATCGTCCTCCTGCTGCTCATTATCGGTGTTGTCCTGGCGCTGCTGATCTCCAACGGCAAGCTCGGCGGCAGCTCGAGCGCCATGGCGGCCAGCATCGGTGCGGGGGAGTGGATCCGTCAGCTCGTCTGA","VSTEQTGVNAPTSEEPTPDEHAPRGSRRAIRQAERAAEREAILTGQQPLLTRREMRRLREEAKALRAAVEAGEITPEQAQALQDPLADPTSVTSRSSATSGDEGESGPGEPDEPVAVDGGDYLEQGGQNPPLSMSAPEGSAASAPSWRSLSAAEAVAISEIETGLMEAVDLPVATLDYDAHWAANASSEPAPVPTRFSLKDRLEGGSVPEVEEPESPQDNESQGAVETSDDAEAEEPATSPYDYREGLESAAQDDGDASSQSSSATDAVSAASAVPAVSATASGAADFAAYGQAGAARSTESARSGVSAGSASSAGSVRRPIVRIPAAAQGVRTVNASTGELSSVQPVDSSPSAQEAADAQDVYGAPSIEEPMVQGGAEVEIDVEAQTMVVPASEPSTQGAQDSEFGAPGAPQWRSLHQAPQAGSFQEAIVDGTAETAAVSGEAVSPYAFYSDEVENGNGPMGASEWDSVAVPAAEVPEEPYLAPVNEVTGRVPTPDHVLPMEQPGSSSRIGKILMAALIIVLLLLIIGVVLALLISNGKLGGSSSAMAASIGAGEWIRQLV$","Hypothetical protein","Extracellular, Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[516-536]?$	transmembrane_regions

InterPro
IPR004394
Family

Iojap-related protein
PTHR21043	$\"[15-134]T$	IOJAP SUPERFAMILY ORTHOLOG
PF02410	$\"[8-109]T$	DUF143
TIGR00090	$\"[15-108]T$	TIGR00090: iojap homolog

","BeTs to 13 clades of COG0799COG name: Uncharacterized ACR (homolog of plant Iojap proteins)Functional Class: S [Function unknown]The phylogenetic pattern of COG0799 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB004394 (Iojap-related protein) with a combined E-value of 4.1e-27. IPB004394A 25-52 IPB004394B 81-108","Residues 42-108 are similar to a (IOJAP-RELATED IOJAP YBEB FAMILY PLANT SIMILAR UNCHARACTERIZED DOMAIN HOMOLOG DUF143) protein domain (PD008103) which is seen in Q6A9H4_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 109 (E_value = 9.7e-36) place ANA_0484 in the DUF143 family which is described as Domain of unknown function DUF143.","","ACR (homolog of plant Iojap proteins)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0485","512203","512844","642","6.80","-0.38","23093","ATGACGGACCTCATTCTGTGGCGCCACGGCCAAACCGACTACAACAGCCAAGGACGTATTCAGGGCCAGGTCGACATCCCTCTCAATGAGACCGGACGCGACCAGGCTCGGCGTGCCGCCGAGGACATCGCGGCCCTGGGGCCCACTCGCATCGTCTCCTCCCCGCTGATTCGGGCGAGGGACACGGCCGAGGCGCTGGCGTCGCTGACCGGACTGAGCGTCGAGATCGATGAGGGTCTGGCGGAGAAGTCCTTCGGAGACTGGGAGGGCCTCAAGGCCGCTGACATCAAGAAGCAGTGGCCGGAGCACTACGCCACCTGGCGGGCCGGGGGAGACCTCCCCCAGTTCCGGATCGAGGGGCGCCGCCAAACCGCCGAGAGAGTGGGGGAGGCGCTCAAGGCCACCGTTGCAGGTTCCCAGAAGGACGACATCATCGTGGCCGTCTCCCACGGTGCGGCCACTAACCTGGGGGCCACGTACCTCCTGGGGATGGACGCTCAGCAGTGGTTCGGTCTGCGTGGGATGAGCAACTGCTGCTATGCACTTCTGCGGACCACCAAACGGCCTCCGGGCTGGGCGGTGGTGACGTGGAACGCCGGACCACCGGTGGACTCCAGTCCGCTGGGCAGGATCCTGGGCTGA","MTDLILWRHGQTDYNSQGRIQGQVDIPLNETGRDQARRAAEDIAALGPTRIVSSPLIRARDTAEALASLTGLSVEIDEGLAEKSFGDWEGLKAADIKKQWPEHYATWRAGGDLPQFRIEGRRQTAERVGEALKATVAGSQKDDIIVAVSHGAATNLGATYLLGMDAQQWFGLRGMSNCCYALLRTTKRPPGWAVVTWNAGPPVDSSPLGRILG$","Phosphoglycerate mutase","Cytoplasm, Periplasm","phosphoglycerate mutase","phosphoglycerate mutase ","Phosphoglycerate mutase","","Le Boulch P., Joulin V., Garel M.C., Rosa J., Cohen-Solal M. Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA. Biochem. Biophys. Res. Commun. 1988. 156(2):874-881. PMID: 2847721White M.F., Fothergill-Gilmore L.A. Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae. FEBS Lett. 1988. 229(2):383-387. PMID: 2831102","","","

InterPro
IPR001345
Active_site

Phosphoglycerate/bisphosphoglycerate mutase
PS00175	$\"[6-15]T$	PG_MUTASE

InterPro
IPR013078
Domain

Phosphoglycerate mutase
PF00300	$\"[3-157]T$	PGAM

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1240	$\"[1-187]T$	no description
PIRSF001490	$\"[2-208]T$	Cofactor-dependent phosphoglycerate mutase
PTHR23029	$\"[2-170]T$	PHOSPHOGLYCERATE MUTASE

","BeTs to 12 clades of COG0406COG name: Fructose-2,6-bisphosphataseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0406 is ---p--yqvdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 3","***** IPB001345 (Phosphoglycerate/bisphosphoglycerate mutase) with a combined E-value of 4.1e-38. IPB001345A 4-32 IPB001345B 48-60 IPB001345C 71-111 IPB001345E 142-185","Residues 1-165 are 47% similar to a (ALPHA-RIBAZOLE-5`-PHOSPHATE COBC PHOSPHATASE) protein domain (PDA1D4N8) which is seen in Q9KSL6_VIBCH.Residues 3-103 are 53% similar to a (MANNITOL-1-PHOSPHATASE) protein domain (PD128634) which is seen in O43980_EIMTE.Residues 4-108 are 59% similar to a (MUTASE PHOSPHOGLYCERATE) protein domain (PD581854) which is seen in P72649_SYNY3.Residues 6-151 are similar to a (PHOSPHOGLYCERATE MUTASE PGAM ISOMERASE GLYCOLYSIS PHOSPHOGLYCEROMUTASE BPG-DEPENDENT 23-BISPHOSPHOGLYCERATE-DEPENDENT DPGM FAMILY) protein domain (PD002638) which is seen in Q9RDL0_STRCO.Residues 9-152 are 49% similar to a (KINASE HYDROLASE FRUCTOSE-26-BISPHOSPHATASE INCLUDES: 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-26-BIPHOSPHATASE MUTASE PHOSPHOGLYCERATE ATP-BINDING 6-PHOSPHOFRUCTO-2-KINASE ISOZYME) protein domain (PD858890) which is seen in Q8RFA7_FUSNN.Residues 51-203 are 48% similar to a () protein domain (PD818356) which is seen in Q8G5N9_BIFLO.","","-51% similar to PDB:1EBB BACILLUS STEAROTHERMOPHILUS YHFR (E_value = 1.2E_12);-51% similar to PDB:1H2E BACILLUS STEAROTHERMOPHILUS PHOE (PREVIOUSLY KNOWN AS YHFR) IN COMPLEX WITH PHOSPHATE (E_value = 1.2E_12);-51% similar to PDB:1H2F BACILLUS STEAROTHERMOPHILUS PHOE (PREVIOUSLY KNOWN AS YHFR) IN COMPLEX WITH TRIVANADATE (E_value = 1.2E_12);-47% similar to PDB:1FZT SOLUTION STRUCTURE AND DYNAMICS OF AN OPEN B-SHEET, GLYCOLYTIC ENZYME-MONOMERIC 23.7 KDA PHOSPHOGLYCERATE MUTASE FROM SCHIZOSACCHAROMYCES POMBE (E_value = 5.2E_11);-49% similar to PDB:2A6P Structure Solution to 2.2 Angstrom and Functional Characterisation of the Open Reading Frame Rv3214 from Mycobacterium tuberculosis (E_value = 7.6E_10);","Residues 3 to 157 (E_value = 8e-44) place ANA_0485 in the PGAM family which is described as Phosphoglycerate mutase family.","","mutase (glycolysis)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0488","513151","513858","708","11.40","12.06","24868","ATGAGGCGAGGGCCATTTTATTTTGCCGCCCGCCGTTGCCGCGTGCGGCACAATGTGGGGATGGCTACTGCTGTGCTCATCAAGGCGCTAGGCGCCTTCTTCGCGATCATGAACCCCTTTGTCAACCTGCCCCTGTTCCTGAGCCTCACCCAGGAACAGGATGCTGCGACCCAGCGGCGCACAGCAGTTCGTACAACGATCTCTTCCACCGTCATGTGCACTGTCGTGCTGCTCCTGGGTGCGACGATCCTGAGATTCTTCGGCATTGGCGTCGACGATTTCCGGATTGCAGGCGGAATCGTCCTGCTCATCATCTCCTTGTCCATGCTCAATGGCAGCGGCTCCAGCGCTCACGAGGGCAGTAGGCAGGAGAAGACGCAGCACAACGTCGTTGCCGGTGGTGGGAGTGACGTCTCCTTCTACCCCATGACCTTCCCGATCCTCGTGGGGCCCGGAACGATCACAACGATCATCGTCATCCAGTCCCAGGCCCAGGGACTGGGCGGGCATGCGGCGGTTGCAGCTGCCCTGGCGGCTGTCCTGACGGCGCTCGGGATCGTTCTCTACTTCTCAGCCAGCATCGGTGCTCGCCTGTCCATGACGATGCGCACCATCATGACCCGCCTCATGGGCATGATCCTGGCCTCGATCGCGGTGCAGATGATCGTCGTCGGGATCCAGCACCTCTTCCCCGGGCTGGCTCGCTGA","MRRGPFYFAARRCRVRHNVGMATAVLIKALGAFFAIMNPFVNLPLFLSLTQEQDAATQRRTAVRTTISSTVMCTVVLLLGATILRFFGIGVDDFRIAGGIVLLIISLSMLNGSGSSAHEGSRQEKTQHNVVAGGGSDVSFYPMTFPILVGPGTITTIIVIQSQAQGLGGHAAVAAALAAVLTALGIVLYFSASIGARLSMTMRTIMTRLMGMILASIAVQMIVVGIQHLFPGLAR$","Multiple antibiotic resistance (MarC)-related protein","Membrane, Cytoplasm","membrane protein, putative","multiple antibiotic resistance (MarC)-related proteins","multiple antibiotic resistance (MarC)-related protein","","","","","

InterPro
IPR002771
Family

Multiple antibiotic resistance (MarC)-related proteins
PF01914	$\"[23-230]T$	MarC
TIGR00427	$\"[21-226]T$	TIGR00427: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[94-114]?$ $\"[148-170]?$ $\"[176-196]?$ $\"[211-231]?$	transmembrane_regions

","BeTs to 15 clades of COG2095COG name: Integral membrane proteins of the MarC familyFunctional Class: S [Function unknown]The phylogenetic pattern of COG2095 is a-mpkz-q-d--b-efghsnuj-it-Number of proteins in this genome belonging to this COG is 2","***** IPB002771 (Multiple antibiotic resistance (MarC)-related proteins) with a combined E-value of 3e-30. IPB002771A 91-111 IPB002771B 142-155 IPB002771C 194-226","Residues 26-111 are similar to a (MEMBRANE TRANSMEMBRANE ANTIBIOTIC MULTIPLE MARC RESISTANCE UPF0056 TRANSPORTER PROTEIN FAMILY) protein domain (PD006289) which is seen in Q8J305_THEK1.","","No significant hits to the PDB database (E-value < E-10).","Residues 23 to 230 (E_value = 1.7e-47) place ANA_0488 in the MarC family which is described as MarC family integral membrane protein.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0491","513985","514872","888","5.07","-12.36","30651","GTGACGTCCGTTCAGGTTCCCGACATCATGCAGCGTGCCCGGCGCACGGCCCGGCGTCTTCTGGCCGGCAGTGGGAGCGCGGCGGTAACGGCCTACCGCATCGACCCCTCCGCGCCGGCCGCGTTCGTCGCTCATGCCTTGCGGGCCGATGGCCGGATCCTCGTTGCCGCATGTCCTCCCCAGGGCACCCCGTTGGCCATCGCGCCCGACGACGTCGCCGTCGACATCCGACTCGATGTCACTCTCGACGCCGCCGAGCCCGGTGTGCGCATCACGGCTGCCACCGCTCACCTGCTGGGGAGCCTGACCTGGGTCGAGGGCGAGGATCGCGCCCTGCTGCTGGCCTCCTCTCGTGCTTCTGCCTGCCACTGCGCCATCGTCGGGGAGGATCCGTTCGAGCGGGTCCGGGAGATCGCCGCGGGTCCCGGCGGCCGGCTGGGCGTCATCACCTGTGAACGGGTCATGCTTCACTGCGTCTCCGGGGTCTCCAGCCACGACATCGAGGAGATCCTCGACATCGATTCGGCCGATGCCGCTGCGGCGCCCTCAGCCTCCTGGAGCCCCCAGGAGATCATGGACGCCCACGAGGCGGTCAGCGCCGTCGGTCAGCTCGGTCTGCGGGCTGTGTGTGAGGCCGTGCGCGAGGGTCAGATGCCCGGATGGATCTGCTCCTCCCGCCCTGCCGTCGGGGTGTGCCCGACGCTGTGGGACAGGACCCTGTGCGTCGACGTCGATGCGCACGGGGTCACCCTTATGTCCATCACCGGTGAGGAGGTCACGACACTCGTGGTCTCCTTCGGGCAGGCACTGGCCGACGCCGGCGAGGTGGGGCCGGCCCTGGAGCAGCTGGCCTCTCACGCTCTGCCGCAGCGCCTGACTCGGCCCTGA","VTSVQVPDIMQRARRTARRLLAGSGSAAVTAYRIDPSAPAAFVAHALRADGRILVAACPPQGTPLAIAPDDVAVDIRLDVTLDAAEPGVRITAATAHLLGSLTWVEGEDRALLLASSRASACHCAIVGEDPFERVREIAAGPGGRLGVITCERVMLHCVSGVSSHDIEEILDIDSADAAAAPSASWSPQEIMDAHEAVSAVGQLGLRAVCEAVREGQMPGWICSSRPAVGVCPTLWDRTLCVDVDAHGVTLMSITGEEVTTLVVSFGQALADAGEVGPALEQLASHALPQRLTRP$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 44-294 are 44% similar to a () protein domain (PDA0R8L3) which is seen in Q6A6T1_PROAC.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0492","514954","515400","447","5.06","-7.70","14585","TTGGCCCCCAGCCGCTCGAGCTGGAGAGCCTTCCGGTCAGCGGACCTCGTAGGTCGTGCAGGCGGCGGTGTCGCCCCCGACGGTCACGGCCTCGGCCGTGCACATGAGATCCTTGTTGTGGACGCACTCGAGACGCTGGCAGGCACCCACGTGGCCCTCTGCCACCGGCAGGCCGCCGCGGGCGTCGAGGCTGATGAAGGTGTCGCAGGCCGGTGCGCCGTTGTCGCCACCAACGGTGATGGCGAAGGCGGTGCAGCCGCCGTTGTTGAAGGCGCAGGAGGTGGTGGTGCAGGAGGAGATCTTGGTGACGGACATGATGCTTTTCCTTTCGAGCGGATGTGCGCTGCGGACATGAGTAACGTAAATCCGCATCCGCTCCCCGGCAACGAAGGACAGCCTGCCCTGCCTCCCGGCATGTCAAAGAACGTTGAAATGACGCCGTTTTAG","LAPSRSSWRAFRSADLVGRAGGGVAPDGHGLGRAHEILVVDALETLAGTHVALCHRQAAAGVEADEGVAGRCAVVATNGDGEGGAAAVVEGAGGGGAGGDLGDGHDAFPFERMCAADMSNVNPHPLPGNEGQPALPPGMSKNVEMTPF$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0493","516364","515642","723","5.98","-4.36","25309","ATGGCCACCCCTCACATCGCTGCAGAGCCCGGAGACTTCGCCCCCGCCGTCCTCATGCCCGGCGACCCCAAACGGGCCCAGCGCATCGCCGAGCTCCTCATGGATGACGCTCGTCTCGTCACTGACGTGCGCGGGATGCTGGGCTTCACCGGGACAGTGAACGGCAGGCCACTGAGCGTCATGGGCTCAGGGATGGGGCAGCCCTCCTTCACGATCTACGCCACCGAGCTGTTCAGCCAGTTCGGCGTGAAGCGGATCATTCGGGTGGGCACTGCCGGCGCCCTGTCCCCGAAGGTCAAGGTCGGCGACGTCATCGTGGCCACCGGCGCCCACACGGACTCCTCCATGAACCAGCTGCGCATCCCGGGCGTCAACTTCAGCGCCGTGGCGGACTTCCGGCTGGCCGCGGCCGCGTACCAGGCCGCGCAGCCCGAGGGTGCTCAGGCTGAAGGAGCAGTCCACCTGGGCACTGTCATGTCGCGGGACCACTTCTACTTCACCCCCCAGGGACAGACCGAGGCGCTGGCGAGGTACGGGGTCCTGGGAGTGGAGATGGAGGCCGCCGCCCTCTACGGGGTCGCCGCCGAGTACGACAAACAGGCACTGGCGATCCTGACCGTCTCCGACCACCTGCTGGACCACTCCAGCGACATGAGCGCCACCGAGCGCGAGACACGTTTCACGGACTCTCTGCGCCTGGCCGTGGCCGCCGCGCACAGCTGA","MATPHIAAEPGDFAPAVLMPGDPKRAQRIAELLMDDARLVTDVRGMLGFTGTVNGRPLSVMGSGMGQPSFTIYATELFSQFGVKRIIRVGTAGALSPKVKVGDVIVATGAHTDSSMNQLRIPGVNFSAVADFRLAAAAYQAAQPEGAQAEGAVHLGTVMSRDHFYFTPQGQTEALARYGVLGVEMEAAALYGVAAEYDKQALAILTVSDHLLDHSSDMSATERETRFTDSLRLAVAAAHS$","Purine nucleoside phosphorylase","Cytoplasm","purine nucleoside phosphorylase","purine nucleoside phosphorylase ","purine nucleoside phosphorylase","","Takehara M., Ling F., Izawa S., Inoue Y., Kimura A. Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp. Biosci. Biotechnol. Biochem. 1995. 59(10):1987-1990. PMID: 8534998Watanabe S., Hino A., Wada K., Eliason J.F., Uchida T. Purification, cloning, and expression of murine uridine phosphorylase. J. Biol. Chem. 1995. 270(20):12191-12196. PMID: 7744869Cacciapuoti G., Porcelli M., Bertoldo C., De Rosa M., Zappia V. Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds. J. Biol. Chem. 1994. 269(40):24762-24769. PMID: 7929153","","","

InterPro
IPR000845
Family

Nucleoside phosphorylase
PF01048	$\"[15-238]T$	PNP_UDP_1
PS01232	$\"[62-77]?$	PNP_UDP_1

InterPro
IPR004402
Family

Purine nucleoside phosphorylase
TIGR00107	$\"[5-238]T$	deoD: purine nucleoside phosphorylase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1580	$\"[3-238]T$	no description
PTHR21234	$\"[5-238]T$	PURINE NUCLEOSIDE PHOSPHORYLASE
PTHR21234:SF7	$\"[5-238]T$	PURINE NUCLEOSIDE PHOSPHORYLASE

","BeTs to 9 clades of COG0813COG name: Purine-nucleoside phosphorylaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0813 is -----z---d-lb-e-gh--uj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB000845 (Purine and other phosphorylases, family 1) with a combined E-value of 6.4e-31. IPB000845A 18-30 IPB000845B 49-78 IPB000845C 81-106","Residues 31-106 are similar to a (PHOSPHORYLASE NUCLEOSIDASE NUCLEOSIDE PURINE TRANSFERASE GLYCOSYLTRANSFERASE URIDINE HYDROLASE MTA/SAH GLYCOSIDASE) protein domain (PD472790) which is seen in Q8EHK0_SHEON.Residues 177-235 are 76% similar to a (PHOSPHORYLASE NUCLEOSIDE PURINE TRANSFERASE GLYCOSYLTRANSFERASE PNP INOSINE PURINE-NUCLEOSIDE II DEOD) protein domain (PD782644) which is seen in DEOD_KLEPN.","","-65% similar to PDB:1PR0 Escherichia coli Purine Nucleoside Phosphorylase Complexed with Inosine and Phosphate/Sulfate (E_value = 9.3E_55);-65% similar to PDB:1PR1 Escherichia coli Purine Nucleoside Phosphorylase Complexed with Formycin B and Phosphate/Sulfate (E_value = 9.3E_55);-65% similar to PDB:1PR2 Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-[2-deoxyribofuranosyl]-6-methylpurine and Phosphate/Sulfate (E_value = 9.3E_55);-65% similar to PDB:1PR4 Escherichia coli Purine Nucleoside Phosphorylase Complexed with 9-beta-D-ribofuranosyl-6-methylthiopurine and Phosphate/Sulfate (E_value = 9.3E_55);-65% similar to PDB:1PR5 Escherichia coli Purine Nucleoside Phosphorylase Complexed with 7-deazaadenosine and Phosphate/Sulfate (E_value = 9.3E_55);","Residues 15 to 238 (E_value = 8.9e-78) place ANA_0493 in the PNP_UDP_1 family which is described as Phosphorylase family.","","nucleoside phosphorylase (deoD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0494","518454","518137","318","7.63","1.35","10665","TTGTGTCCCACCCGCCTGGAAACCGGCCGAACCGGGCCCCAGACGGGTGGTGGAGTCAGTCTCTCTTCTCGAGCGGTCACGTCCGCGTTTCTCAGCGGACCGCACCGGTCAGTCGGTCTCCTCGGGGTGAAGCATGTGCTCGCGGGCCCGCGCCGAGGCCTCGGCCCGGGCGTCGCGGTCCTCGCGGCGTCCGCGCGAGATGAGCGCGGTGATGGACACCGCCAGACCGCCCCAGATGATGACGATGGCGAGCAGCATGATGAGCACGGCGATTCCGGTCATCTCAGTCCTCCTCCTGGGAAGCGGCCTCCAGCGTGA","LCPTRLETGRTGPQTGGGVSLSSRAVTSAFLSGPHRSVGLLGVKHVLAGPRRGLGPGVAVLAASARDERGDGHRQTAPDDDDGEQHDEHGDSGHLSPPPGKRPPA$","Hypothetical protein","Membrane, Extracellular","Trans-acting transcriptional protein ICP0(Immediate-early proteinIE110) (VMW110) (Alpha-0 protein)","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","transcriptional protein ICP0 (Immediate-early proteinIE110) (VMW110) (Alpha-0 protein)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0495","516591","518171","1581","5.94","-3.14","56729","ATGTCCTCCAAGACAGGGGAGAGCGAGTCTCTTCAGGCTCCCCCGCGCGAGCAGTGGAGCGGGCAGCTCGGCTTCCTCATCGCCGCCATCGGCTCGGCGATCGGCCTGGGAAACATCTGGCGCTTCCCAGGGGTGGCCTACACCAACGGCGGCGGTGCCTTCATCGTCCCCTACGTCATCGCGCTGCTGGCTGCCGGGCTGCCGATCCTTTTCCTCGACTACGCCCTGGGGCACCGCTTCCGCGGCTCCCCGCCGGCGGTCTTCAGGCGACTGTCCACCAGGCTCGAGTGGCTGGGATGGTTCCAGGTCTTCATCTGCTTCGTCATCATGACCTACTACGCGGTGGTCGTGGCCTGGTCCTTGCGCTACATGTTCTTCTCCGTCAACGTCGCCTGGGGCGACGACGCGGCAGGCTTCTTTCAGAGCTACATCGGGATGGACCGGCTCGGTTCTGAGGTTGCCTACTCGCCGACCGTCATCATGGGCGTGGCCCTGCCGCTGCTGTTCGTATGGGGCTTCGGTCTGGTGGTGACCGCCCTGGGAGTCAGCGGAGGCCTGGAGAAGGCCAACAAGATCTTCCTGCCGCTGCTGGTCATCATGTTTGCCGGCCTCGTGGTGCGCGCCCTCCTGCTCCCGGGCGCGGGGGAGGGGCTCAATGCCCTGTTCACGCCCAAGTGGTCCGCCCTGCTGGACTACCAGGTGTGGATGGCGGCCTTCGGGCAGATCTTCTTCTCCCTGTCCGTGGGCTTCGGCATCATGCTCACCTACGCCTCCTACCTCCAGCGGCGCCGCTCCAACCTGGTGGGAACCGGCCTCGTGGCGGGCTTCGCCAACTCCTCCTTCGAGCTGTTCGCAGGGATCGGCGTCTTCGCGACCCTCGGCTTCATGGCGCACACGCAGCACGTCGGGATCAGCGAGATGAAGATCACCGGGCCCTCCCTGTCCTTCATCACCTTCCCCACCGTCATCGCCCAGATGCCCGGAGGCGCGCTCTTCGGGGTGCTCTTCTTCGCCTCCTTCTCCATGGCGGGGCTGACCTCCTTCATCTCTATCATCCAGGTGGTCGCCGCCGGCGTGGGGGAGAAGCTCGACCTGACGCCGAAGAAGGCCTCTCTCGTCGTCGGCGTCCCGGCCGCCGTCCTGTCCTTCGTCCTGTTCGCCACCAGCTCGGGCCTGCCGGACCTCGACGTGGTGGACGCCTTCATCAACAACATCGGCGTGGTCGTCTCGGCCATCATCATGTGCGTGGTGGTCGCCTGGCTGCTGCGGCGCACGAAGCTGCTTCAGGACCACCTCAACGCCGTCTCCGAGTCCCGGATGATCGGCCTGTGGTGGAGGGTCCTCGTCGGTGCCGTCGTCCCCGTCCTGCTGGGGTACATGTTCATTCAGACCCTGTGGACGTACCTGTCCGAAGGATATGAGTCGGAGGCCTACTCCAGCGGCTTCGTCATGGTCTTCGGATGGGGGATGCTGCTGGTGGTTGCCTTGGGCACCGCCGTCATGAGCCTCATCCCCTGGAGGACCCCGGTGGACGAGTTCGAGGCCCTCACGCTGGAGGCCGCTTCCCAGGAGGAGGACTGA","MSSKTGESESLQAPPREQWSGQLGFLIAAIGSAIGLGNIWRFPGVAYTNGGGAFIVPYVIALLAAGLPILFLDYALGHRFRGSPPAVFRRLSTRLEWLGWFQVFICFVIMTYYAVVVAWSLRYMFFSVNVAWGDDAAGFFQSYIGMDRLGSEVAYSPTVIMGVALPLLFVWGFGLVVTALGVSGGLEKANKIFLPLLVIMFAGLVVRALLLPGAGEGLNALFTPKWSALLDYQVWMAAFGQIFFSLSVGFGIMLTYASYLQRRRSNLVGTGLVAGFANSSFELFAGIGVFATLGFMAHTQHVGISEMKITGPSLSFITFPTVIAQMPGGALFGVLFFASFSMAGLTSFISIIQVVAAGVGEKLDLTPKKASLVVGVPAAVLSFVLFATSSGLPDLDVVDAFINNIGVVVSAIIMCVVVAWLLRRTKLLQDHLNAVSESRMIGLWWRVLVGAVVPVLLGYMFIQTLWTYLSEGYESEAYSSGFVMVFGWGMLLVVALGTAVMSLIPWRTPVDEFEALTLEAASQEED$","Sodium-dependent transporter of the SNF family","Membrane, Cytoplasm, Extracellular","Na+-dependent transporters of the SNF family","K03308 neurotransmitter:Na+ symporter; NSS family","sodium:neurotransmitter symporter","","van Kuppeveld F.J., Hoenderop J.G., Smeets R.L., Willems P.H., Dijkman H.B., Galama J.M., Melchers W.J. Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. EMBO J. 1997. 16(12):3519-3532. PMID: 9218794Aldabe R., Barco A., Carrasco L. Membrane permeabilization by poliovirus proteins 2B and 2BC. J. Biol. Chem. 1996. 271(38):23134-23137. PMID: 8798506","","","

InterPro
IPR000175
Family

Sodium:neurotransmitter symporter
PD000448	$\"[16-43]T$	Q6M052_METMP_Q6M052;
PR00176	$\"[24-45]T$ $\"[53-72]T$ $\"[97-123]T$ $\"[272-292]T$ $\"[326-345]T$ $\"[404-424]T$	NANEUSMPORT
PTHR11616	$\"[16-479]T$	SODIUM/CHLORIDE DEPENDENT TRANSPORTER
PF00209	$\"[16-524]T$	SNF
PS50267	$\"[15-511]T$	NA_NEUROTRAN_SYMP_3

InterPro
IPR002519
Family

Hepatitis C virus envelope glycoprotein E1
PF01539	$\"[320-360]T$	HCV_env

noIPR
unintegrated

unintegrated
PTHR11616:SF14	$\"[16-479]T$	SODIUM/CHLORIDE-DEPENDENT NORADRENALINE TRANSPORTER
tmhmm	$\"[20-40]?$ $\"[54-76]?$ $\"[97-117]?$ $\"[163-183]?$ $\"[193-215]?$ $\"[234-254]?$ $\"[275-297]?$ $\"[335-355]?$ $\"[370-390]?$ $\"[400-422]?$ $\"[443-463]?$ $\"[477-497]?$	transmembrane_regions

","BeTs to 14 clades of COG0733COG name: Na+-dependent transporters of the SNF familyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0733 is aom-k--q----b---gh-nu--it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 16-43 are 96% similar to a (TRANSMEMBRANE SYMPORT TRANSPORTER SODIUM-DEPENDENT NEUROTRANSMITTER GLYCOPROTEIN CHLORIDE-DEPENDENT FAMILY SODIUM- SOLUTE) protein domain (PD000448) which is seen in Q6M052_METMP.Residues 17-60 are 79% similar to a (SODIUM-DEPENDENT SYMPORT TRANSMEMBRANE TRANSPORTER TRANSPORTER TRYPTOPHAN) protein domain (PDA1E7Y0) which is seen in Q73B68_BACC1.Residues 62-123 are similar to a (TRANSMEMBRANE SYMPORT TRANSPORTER SODIUM-DEPENDENT NEUROTRANSMITTER GLYCOPROTEIN CHLORIDE-DEPENDENT FAMILY SODIUM- SOLUTE) protein domain (PD347035) which is seen in Q6AAA4_PROAC.Residues 211-270 are 86% similar to a (TRANSMEMBRANE SYMPORT TRANSPORTER SODIUM-DEPENDENT NEUROTRANSMITTER GLYCOPROTEIN CHLORIDE-DEPENDENT FAMILY SODIUM- SOLUTE) protein domain (PD256884) which is seen in Q6F6P5_ACIAD.Residues 286-376 are similar to a (TRANSMEMBRANE SYMPORT TRANSPORTER SODIUM-DEPENDENT NEUROTRANSMITTER GLYCOPROTEIN CHLORIDE-DEPENDENT FAMILY SODIUM- TRANSPORTER) protein domain (PD523506) which is seen in Q6NI32_CORDI.","","-52% similar to PDB:2A65 Crystal structure of LEUTAA, a bacterial homolog of Na+/Cl--dependent neurotransmitter transporters (E_value = 6.8E_55);-36% similar to PDB:1YMG The Channel Architecture of Aquaporin O at 2.2 Angstrom Resolution (E_value = 6.8E_55);-36% similar to PDB:2B6P X-ray structure of lens Aquaporin-0 (AQP0) (lens MIP) in an open pore state (E_value = 6.8E_55);-36% similar to PDB:2C32 CO-AXIAL ASSOCIATION OF RECOMBINANT EYE LENS AQUAPORIN-0 OBSERVED IN LOOSELY PACKED 3D-CRYSTALS (E_value = 6.8E_55);","Residues 16 to 524 (E_value = 1.5e-69) place ANA_0495 in the SNF family which is described as Sodium:neurotransmitter symporter family.Residues 320 to 360 (E_value = 0.0063) place ANA_0495 in the HCV_env family which is described as Hepatitis C virus envelope glycoprotein E1.","","transporters of the SNF family (SNF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0496","518462","519319","858","4.75","-15.37","30992","ATGACTCAGACTGATGTGAGCCCCCGGGCGCTGCCCCGCCTGGTGGCCTTCGACCTCGACGACACGCTGGCGCCCTCCAAGTCGGCCATGCCACCGGCCATGGCTACAGCGCTCAGGCGGCTGCTCGACGTCGTCCCCGTCTGCATCATCTCCGGGGGGCAGATGGGGCAGTTCCGCGACCAGGTCCTGGCCCACCTCGACGCCGACGCCGATGAGCTCTCCCGGCTTCACCTCATGCCCACCTGCGGAACGCGCTACTACACCTACGACCCCTCCCGTGCCCAGAGCGATGAGGACGCCTGGACGCTGGTCTACGCCAACGACCTCACCCCTGAGCAGATCCGCATCGGTTTTGAGATCGTCGAGGCCCAGGCCCGTCGCCTCGGTCTGTGGGAGGAGCAGACCTGGGGGGCGATCCTGGAGGACCGCGGCAGCCAGATCACCTTCTCTGCGCTGGGGCAGGAGGCCCCCCTGGACGCCAAGCGTGCGTGGGACCCCACAGGTGAGAAGAAAGCCTCCCTGCGTGACGCCGTCGCCCCGCTCCTACCGGACCTGGAGGTTCGCTCAGGCGGCTCCACGAGCGTCGACATCACCCTCAAGGGGGTGGACAAGGCCTACGGCATGAAGCGCCTGGCGCAGATGACCGGTATCTCGCTGGAAGAGATGATCTTTGTCGGCGACCGCCTGGACCCGGAGGGAAACGACTACCCCGTCAAGGCTCTAGGCGTTCCTTGTCAGGCCGTGGACGGCTGGCAGGACACCGTCACCTACGTCACCTCCCTGGCGAGTCTCATCGCCTCTCAGACGCACGACGGTGAGGACCCGAGCGCCCAGGTCTCACTGGGCGCTCGTCTCTGA","MTQTDVSPRALPRLVAFDLDDTLAPSKSAMPPAMATALRRLLDVVPVCIISGGQMGQFRDQVLAHLDADADELSRLHLMPTCGTRYYTYDPSRAQSDEDAWTLVYANDLTPEQIRIGFEIVEAQARRLGLWEEQTWGAILEDRGSQITFSALGQEAPLDAKRAWDPTGEKKASLRDAVAPLLPDLEVRSGGSTSVDITLKGVDKAYGMKRLAQMTGISLEEMIFVGDRLDPEGNDYPVKALGVPCQAVDGWQDTVTYVTSLASLIASQTHDGEDPSAQVSLGARL$","Predicted hydrolase of the HAD superfamily","Cytoplasm, Periplasm","conserved hypothetical protein","hypothetical protein","Haloacid dehalogenase domain protein hydrolase, type 3","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317","","","

InterPro
IPR013200
Domain

HAD superfamily hydrolase-like, type 3
PF08282	$\"[165-227]T$	Hydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[12-229]T$	no description

","No hits to the COGs database.","***** IPB005833 (Haloacid dehalogenase/epoxide hydrolase family signature) with a combined E-value of 3.2e-07. IPB005833A 12-23 IPB005833F 207-227***** IPB000150 (Cof protein) with a combined E-value of 5.8e-06. IPB000150A 15-24 IPB000150D 190-208","Residues 41-263 are 70% similar to a (YFGH) protein domain (PD400991) which is seen in Q6A676_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 15 to 265 (E_value = 0.00088) place ANA_0496 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0497","519412","521328","1917","6.19","-6.32","65583","GTGCGACGCTGCTGCGCCCTGGTCGTCACGGTGCTGTTGGCGCCGCGCCTGTGGTGGCGTCGCCGTCGCCGCGGGACCCGCACAGCGATCAGTACGGCGGCCATGATCCTGGCCTCCAGCCTCGTCTCCCTCCTGCTGGGGGTGTCCACGGCGACGGCCTCGACGCCGGTCGGTCCGCATGAGGCGACCTGGTCGACCACCCTGGACTCCACCGTCACGCTGGACCTCGGGCCGCTGGGAACCGCTGCAATGGAGTCCCCTGCGGGGATTCTCGGCGTCACGGTGGTCCTAGGGGAGATCCCAGGCGATCCAGCACCTGATACAGCCAACGCGGCCAGCGTGGGGCAGTCCCTGTCATCCGATGCGACCTCCTACCTCTCACTGGTCTCCCATCCCGATCTGACGATCCGGCAGGGCCTCTACGGACTGGCCGGCGACGCCCTGCGCCGGGCCGGGGTCGTCGAAGCGATCTTCCTGTGCTGTGTGGCCGCCTGGCGCCTGGCACCGACCAAGCCATGGCGTGAGACCGTCCGAGCCGGCGTCTCGCACCGCTGGGCCACCACCGTGGCGTTCTCCGCGGCCGTGGCCACCGTGGCATCCCTCCTGGTGCCGGCCATGCGCACAGCCACCTCGCCCGGCTCCACCCTGTCCGTCCTTGAGGGGACCCCGCTGGCCCAGGCCCGTTTCTCAGGACGCATCGCCGACGTCGTCACCGCCTACGGCCCCAAGGCGCGTACCTTCGTGGAGACGAGCAAGGACTTCTACGCCAAGGCGGACACCAACCTACGGGCTGCCTGGAAGGCGGCCGAGCAGACTGAGGGCCTGGTGGACGTCACCGCCGTCGACGGAAAGGTGGACGCCGAGGACCTGCAGGCCCGGGTCAGGGCTTCCTCCGCGAAGACCCTGGTGAAGGCCGCCGATCCTGAGTCCGACGCCGCCCCGCAGGCCTCTGAGAGCCCGCGGGCCACCGCGACGCCCTCGATCTCGGTGACCGGGGCCCGATCAGTGCCCGAGCGCGGACGCAAGACCGCCGTGCTCACCACGGACCTGCACTGCAACCTCGATGTCATCGCCTTCTCCGGGATCCTTGACCAGCTCTCGGGTGCCGATATCCACATGGACGACGGCGACCTGACCATGACCGGCTCGGATCCAGAGCGGGTGTGCGTCGACGCGCTGACCCAGGCGGTCCCGAGCTCGACGAAGAAGGTCGCCACGATCGGCAACCATGACTCCGACGCCACGGCCGCCCGCCTGCGCTCCCAGGGGTGGACCGTCACCAACGGCTCGGTCCAGACGGTCGCCGGGATCACTGTCCTGGGGCACGACGACGCCGAGCGCACAACAGCTGCGGGCACCAAGCCCCGCAACGGGGAGACCACCGAGCAGATTGCCTCCCGCCTGGCCACGACCAGCTGCGGGAGCACACCGGTGGACGTCGTCCTCATCCATCAGCCCGCCACCTTCGACACGCTCACGAAGGAGGGCTGTGCGCCATTGCTCCTGGCTGGGCACGTCCATGCCGAGCGGGGAATGACCACAGCGATCAGCCCCCAAACCGGCCGGCCCGTCACCGGGATCATCTCGGGCGCGGGTAAGGGTGGTACGTCACTAGGATCGGTCACCGAGGACGCATTCCTCCACGTCATGTCCTTCGACTCCGCCGGAGCGCTGGTGGCCTGGCGTGCGGTCATCCTCCACTCCGACGCCTCGGTAACGGTGGGGGCCTGGCGGCCCGTGCCCGGTATCGCCTCGGGGCAGACAGCGGCCACCATGGCGTCGACCTCGAGCCCGACGGCCTCGGCCTCCCCGGTGCAGACGCAGACCCAGGCTCCGCAGAGCACGAGGCCCGAGGATGGCTCTGCGCCACAGGAGGGGGCAGAGCCCCAGGGGGAGAGCGATTCCTCGGACGGGTAG","VRRCCALVVTVLLAPRLWWRRRRRGTRTAISTAAMILASSLVSLLLGVSTATASTPVGPHEATWSTTLDSTVTLDLGPLGTAAMESPAGILGVTVVLGEIPGDPAPDTANAASVGQSLSSDATSYLSLVSHPDLTIRQGLYGLAGDALRRAGVVEAIFLCCVAAWRLAPTKPWRETVRAGVSHRWATTVAFSAAVATVASLLVPAMRTATSPGSTLSVLEGTPLAQARFSGRIADVVTAYGPKARTFVETSKDFYAKADTNLRAAWKAAEQTEGLVDVTAVDGKVDAEDLQARVRASSAKTLVKAADPESDAAPQASESPRATATPSISVTGARSVPERGRKTAVLTTDLHCNLDVIAFSGILDQLSGADIHMDDGDLTMTGSDPERVCVDALTQAVPSSTKKVATIGNHDSDATAARLRSQGWTVTNGSVQTVAGITVLGHDDAERTTAAGTKPRNGETTEQIASRLATTSCGSTPVDVVLIHQPATFDTLTKEGCAPLLLAGHVHAERGMTTAISPQTGRPVTGIISGAGKGGTSLGSVTEDAFLHVMSFDSAGALVAWRAVILHSDASVTVGAWRPVPGIASGQTAATMASTSSPTASASPVQTQTQAPQSTRPEDGSAPQEGAEPQGESDSSDG$","Metallophosphoesterase","Extracellular, Periplasm","Ser/Thr protein phosphatase family","hypothetical protein predicted by Glimmer/Critica","metallophosphoesterase","","Stone S.R., Hofsteenge J., Hemmings B.A. Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A. Biochemistry 1987. 26(23):7215-7220. PMID: 2827745MacKintosh R.W., Haycox G., Hardie D.G., Cohen P.T. Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A. FEBS Lett. 1990. 276(1):156-160. PMID: 2176161","","","

InterPro
IPR004843
Domain

Metallophosphoesterase
PF00149	$\"[342-509]T$	Metallophos

noIPR
unintegrated

unintegrated
signalp	$\"[1-53]?$	signal-peptide
tmhmm	$\"[28-48]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 348-581 are 40% similar to a (MEMBRANE INTEGRAL) protein domain (PD325020) which is seen in Q9RKJ3_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 342 to 509 (E_value = 0.00048) place ANA_0497 in the Metallophos family which is described as Calcineurin-like phosphoesterase.","","protein phosphatase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0498","521423","522157","735","5.19","-4.74","26438","ATGTCGCGCATGCCCACAGATGCCGAGATCGATGAGATGAGTGAGGAAGAGCTCGAGGCCTACCTGGGCGCTGGCCCCACTCAAGAGCTTGACCGACGCACCCGTCGTGATTCCGGCGAGGACTTAGCCGCGCGTCCGGCCTGGCTGCGGCGCTCCGGGGCCGAGCGGGGATTCGGCTGGTTGCTCACCGTGTGCGCACTGATCGGGATCCTCGCCTGCTGGGAGCTCATTACCGCCCAGCTCGACCTGCTGCGCAACCCGGATGCAGAGCTCGTTTGCGACGTTAGCCCCCTGGTGTCCTGCGGGGACTCCCTCAACGTGTGGCAGGGCAACCTGCTGGGGGTGCCCAACTCCTTCGTCGGGGCCATCGCCTTCGGGGCCCTGGCCGCGATCGGCATGGTGCTGCTCAGCGGCGCGCGCCTGCCGCGCTGGATGTGGTGGGGGCTGAGCGCCGGCAGCCTCGGTGGGATCGCCTTCGTCATCTGGTTCCTGTCCGTGTCCATCATGACCTTCGGCAAGCTCTGTCCCTTCTGCATGGTCATCTGGTCCGTCACCATCCCGGTGGCGGCCCACTCCTGGGCCTGGGCCGCGGCCGGTGGGCACCTGGGGCTGCGTGACAACCTGGCGCTGGACGTGCTCAAGGCCCGGTGGTGGATCATGGCGGCGATGTACCTGGCGGTGGTTCTCACCATCGTCATCGCCTTCGGCGGCCAGCTGGCCAGGCTCTTCGGGTGA","MSRMPTDAEIDEMSEEELEAYLGAGPTQELDRRTRRDSGEDLAARPAWLRRSGAERGFGWLLTVCALIGILACWELITAQLDLLRNPDAELVCDVSPLVSCGDSLNVWQGNLLGVPNSFVGAIAFGALAAIGMVLLSGARLPRWMWWGLSAGSLGGIAFVIWFLSVSIMTFGKLCPFCMVIWSVTIPVAAHSWAWAAAGGHLGLRDNLALDVLKARWWIMAAMYLAVVLTIVIAFGGQLARLFG$","Vitamin K epoxide reductase","Membrane, Cytoplasm","hypothetical integral membrane protein","vitamin K epoxide reductase","Vitamin K epoxide reductase","","Goodstadt L., Ponting C.P. Vitamin K epoxide reductase: homology, active site and catalytic mechanism. Trends Biochem. Sci. 2004. 29(6):289-292. PMID: 15276181","","","

InterPro
IPR012932
Domain

Vitamin K epoxide reductase
PF07884	$\"[58-196]T$	VKOR
SM00756	$\"[55-196]T$	VKc

noIPR
unintegrated

unintegrated
tmhmm	$\"[58-78]?$ $\"[119-139]?$ $\"[144-164]?$ $\"[174-196]?$ $\"[217-237]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB012932 (Vitamin K epoxide reductase) with a combined E-value of 1.3e-13. IPB012932A 93-121 IPB012932B 162-184","Residues 67-188 are similar to a (MEMBRANE INTEGRAL PLASMID AT4G35760 PROBABLE CENTER TRANSMEMBRANE REDOX-ACTIVE FOR SIMILAR) protein domain (PD037327) which is seen in Q6SKB1_ARTAU.","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 196 (E_value = 7.5e-33) place ANA_0498 in the VKOR family which is described as Vitamin K epoxide reductase family.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0499","522208","522918","711","5.29","-8.59","25339","GTGGCGGGGGACTCGACCGTCACGCAGGACTACCTCAAGGTCGTGTGGGCCGCCTGCGAGTGGGGCGGTGCGGGTGCCTCCGTCACCGGCCTGGCCAAACGCATGGAGGTGGCCCCCTCGACCGCCTCAGAGAACGTGGCTCGCCTCGTGGAGGAGGGACTGCTCGTCCACGAGCCCTACAAGGCCGTCACCCTCTCCGAGGAGGGACGACGCCGGGCCATGGGCATGATCCGCCGTCACCGCATCCTGGAGACCTACCTGGTCACTCGGCTCGGCTTCGGCTGGGATGAGGTGCATGCTGAGGCCGAGGAGCTCGAGCACGCCGTCTCTGAGCGGCTGCTGGAGAGGCTCGACGCGGTCCTGGGGCACCCCACCCGTGATCCGCATGGGGACCCGATCCCCACGGCCGACGGCCGCCTCATCGTGCCCGACCTGGTGGGCCTGGAGACGTTGCCGGTGGGCTCCGACGGCGTCGTCGGACGGATTCAGGACGACACCGAGACACTGCGCCGTCTGGAGCGGGCTGGCATCGGGCTGGACAGCCGGGTGCGGATCCGTGATCGGGGCACCGTGGCGCCGGCCGTGGAGGGCGGTGGCCGCAGGCGGGCGACCGTCATCGCCCTGCTGGACGAGGACGCCTCACGCGGCGCAGTGCCCGCGGGCGCCCCGGAGGCCGTCATCCCCGACGGCTCCCTGTGGCTGCTGGCCTGA","VAGDSTVTQDYLKVVWAACEWGGAGASVTGLAKRMEVAPSTASENVARLVEEGLLVHEPYKAVTLSEEGRRRAMGMIRRHRILETYLVTRLGFGWDEVHAEAEELEHAVSERLLERLDAVLGHPTRDPHGDPIPTADGRLIVPDLVGLETLPVGSDGVVGRIQDDTETLRRLERAGIGLDSRVRIRDRGTVAPAVEGGGRRRATVIALLDEDASRGAVPAGAPEAVIPDGSLWLLA$","Mn-dependent transcriptional regulator","Cytoplasm","Mn-dependent transcriptional regulator","K03709 Mn-dependent transcriptional regulator","iron dependent repressor","","Schiering N., Tao X., Zeng H., Murphy J.R., Petsko G.A., Ringe D. Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(21):9843-9850. PMID: 7568230Qiu X., Verlinde C.L., Zhang S., Schmitt M.P., Holmes R.K., Hol W.G. Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors. Structure 1995. 3(1):87-100. PMID: 7743135","","","

InterPro
IPR001367
Family

Iron dependent repressor
PF01325	$\"[5-64]T$	Fe_dep_repress
PF02742	$\"[66-136]T$	Fe_dep_repr_C
SM00529	$\"[27-126]T$	HTH_DTXR
PS50944	$\"[1-66]T$	HTH_DTXR

InterPro
IPR007167
Family

FeoA
PF04023	$\"[146-220]T$	FeoA

noIPR
unintegrated

unintegrated
G3DSA:1.10.60.10	$\"[75-144]T$	no description

","BeTs to 13 clades of COG1321COG name: Predicted iron-dependent transcription repressorFunctional Class: RThe phylogenetic pattern of COG1321 is AmTk--v-ebR------lin-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 171-250 are 52% similar to a (REPRESSOR IRON TRANSCRIPTIONAL REGULATORY IRON-DEPENDENT DEPENDENT TRANSCRIPTION REPRESSOR TOXIN REGULATOR) protein domain (PD004881) which is seen in Q73VW6_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 50 to 109 (E_value = 6e-19) place ANA_0499 in the Fe_dep_repress family which is described as Iron dependent repressor, N-terminal DNA binding domain.Residues 52 to 117 (E_value = 0.0013) place ANA_0499 in the MarR family which is described as MarR family.Residues 111 to 181 (E_value = 5e-27) place ANA_0499 in the Fe_dep_repr_C family which is described as Iron dependent repressor, metal binding and dimerisation domain.Residues 191 to 265 (E_value = 0.011) place ANA_0499 in the FeoA family which is described as FeoA domain.","","transcriptional regulator","","1","","","Fri Aug 10 17:11:10 2007","","Fri Aug 10 17:11:10 2007","","","Fri Aug 10 17:11:10 2007","Fri Aug 10 17:11:10 2007","Fri Aug 10 17:11:10 2007","","","Fri Aug 10 17:11:10 2007","","","Fri Aug 10 17:11:10 2007","Fri Aug 10 17:11:10 2007","Fri Aug 10 17:11:10 2007","","Fri Aug 10 17:11:10 2007","Fri Aug 10 17:11:10 2007","","","","","yes","","" "ANA_0501","522970","523416","447","5.28","-8.18","15939","ATGAGCACGATTTTCACCAAGATCATTGCCGGCGAGATCCCCGGCCGTTTCGTGTGGGCGGACGAGGTCTGCGTCGCCTTCGCCACCATTGAGCCGCACACCGACGGGCACGTCCTCGTGGTCCCACGGCTCGAGGTCGACTCCTACGTGGACGCGCCCGATGACGTGGTGGCGCACCTGGCCGTGGTCGCCAAGCGCATTGGAGCTGCACAGGTGCGCGTCTTCGGGGCGCCCCGCGCCGGGCTCATCGTGGCCGGCTACGGCGTCGACCACCTGCACCTGCACGTGCTGCCGATCCGCTGCGAGGAGGACCTGTCCTTCTCATCGGCCCGCCACCCCGAGGCCCCCGAGCTCGACGCCACCATGGAGCGCCTGCGGGCCGGCCTCGTCGAGCACGGCTGGGGCGAGTTCGTACCCGCGCAGATGGACAGCGCGGCGCTCGCGTAG","MSTIFTKIIAGEIPGRFVWADEVCVAFATIEPHTDGHVLVVPRLEVDSYVDAPDDVVAHLAVVAKRIGAAQVRVFGAPRAGLIVAGYGVDHLHLHVLPIRCEEDLSFSSARHPEAPELDATMERLRAGLVEHGWGEFVPAQMDSAALA$","Histidine triad (HIT) protein","Cytoplasm","HIT-like protein","HIT family protein","histidine triad (HIT) protein","","Seraphin B. The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals. DNA Seq. 1992. 3(3):177-179. PMID: 1472710Brenner C., Garrison P., Gilmour J., Peisach D., Ringe D., Petsko G.A., Lowenstein J.M. Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nat. Struct. Biol. 1997. 4(3):231-238. PMID: 9164465Bieganowski P., Garrison P.N., Hodawadekar S.C., Faye G., Barnes L.D., Brenner C. Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. J. Biol. Chem. 2002. 277(13):10852-10860. PMID: 11805111Barnes L.D., Garrison P.N., Siprashvili Z., Guranowski A., Robinson A.K., Ingram S.W., Croce C.M., Ohta M., Huebner K. Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5\"'-P1,P3-triphosphate hydrolase. Biochemistry 1996. 35(36):11529-11535. PMID: 8794732Fong L.Y., Fidanza V., Zanesi N., Lock L.F., Siracusa L.D., Mancini R., Siprashvili Z., Ottey M., Martin S.E., Druck T., Mccue P.A., Croce C.M., Huebner K. Muir-Torre-like syndrome in Fhit-deficient mice. Proc. Natl. Acad. Sci. U.S.A. 2000. 97(9):4742-4747. PMID: 10758156Pace H.C., Garrison P.N., Robinson A.K., Barnes L.D., Draganescu A., Rosler A., Blackburn G.M., Siprashvili Z., Croce C.M., Huebner K., Brenner C. Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(10):5484-5489. PMID: 9576908Brenner C. Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry 2002. 41(29):9003-9014. PMID: 12119013","","","

InterPro
IPR001310
Family

Histidine triad (HIT) protein
PR00332	$\"[4-20]T$ $\"[25-43]T$ $\"[87-97]T$	HISTRIAD
PIRSF000714	$\"[1-136]T$	Histidine triad hydrolase
PTHR23089	$\"[18-127]T$	HISTIDINE TRIAD (HIT) PROTEIN
PF01230	$\"[10-102]T$	HIT
PS51084	$\"[4-107]T$	HIT_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.428.10	$\"[2-98]T$	no description

","No hits to the COGs database.","***** IPB001310 (Histidine triad (HIT) protein) with a combined E-value of 3.4e-21. IPB001310A 4-43 IPB001310B 74-98","Residues 1-43 are similar to a (HIT FAMILY HYDROLASE HISTIDINE HIT-LIKE TRIAD KINASE REGULATION C CELL-CYCLE) protein domain (PD001840) which is seen in Q9L4T6_BBBBB.Residues 45-131 are 56% similar to a (HYDROLASE FAMILY HIT-LIKE HIT ML2237 AP4A RV0759C/MT0784/MB0782C OTHER DIADENOSINE TETRAPHOSPHATE) protein domain (PD240941) which is seen in YHI1_MYCLE.Residues 51-111 are 62% similar to a (HIT FAMILY HYDROLASE HISTIDINE TRIAD HIT-LIKE KINASE REGULATION DIADENOSINE CELL-CYCLE) protein domain (PD406635) which is seen in Q6MQA8_BDEBA.","","-52% similar to PDB:1RZY Crystal structure of rabbit Hint complexed with N-ethylsulfamoyladenosine (E_value = 2.3E_10);-52% similar to PDB:3RHN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH GMP (E_value = 2.3E_10);-52% similar to PDB:4RHN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH ADENOSINE (E_value = 2.3E_10);-52% similar to PDB:5RHN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP (E_value = 2.3E_10);-52% similar to PDB:6RHN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT WITHOUT NUCLEOTIDE (E_value = 2.3E_10);","Residues 10 to 102 (E_value = 4.2e-18) place ANA_0501 in the HIT family which is described as HIT domain.","","protein (Ap4A)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0502","526274","523443","2832","6.17","-10.77","97198","GTGCGGTTCTCTCTGACATCGCAGCAGCGCTCTTTTCCTACTCGTGCTTCCTGGTGCTGGGGCACAGCCTATCGCCCGCCAGCAGTGGGGCCCGGCGGCGTCCGCCCCACGGGCGGGCGAGACCGGTCACGTCGGTGGAGCCCAGCAAGGTTCGAGCGGTCTCGGCGGGCCGTCACACCGGCTCCGAGAGGAGAAGGCGCCGTCGATAAAGGCGCCAGATATGCGGCTAATCGTTGCTGTTCCAGTGATTCTGGAGCCTGCTTCAGCGTGCGGGGAACGGGCACCACTTGCTATACTGTACATATGTTCGAAGGTGTCGTGCTTCCTCGCGTCCCGACCGGTGGCGCAGTCGGGACGCTGGGTGCGCCTGGCGGGGCCCCCACGTCGGTACCGCAGGTCTCGGCAGAGGAGACGGCAGGCCTGTTGGCCTCCCTGGGTGCGGGCCAGGCGCTGGCCGGTGTGGTGGAGGGGCTGCTGGCCCACCTGCTGGTGACTGCCCAGGACGCCGACGACGAGTGCTCCACCGCTGACGGGGATGCAGTGCCGCCTCTCTTCACCAATGAGTCGGGTACTGACGTGGCGCTGGTGGCCGCCTCCGAGCAGCGCCGGACGATGGGCGTGGAGGAGGTCGGCACGTCGGGACTGATCGGCCTGGGGGCCTCGGGTTTGGGGGAACTGGCCGCGGCCTGCCGCCGTCTGGCGGCCTGGGCCACCTGGGGCGAGGCTCTGGCGGCGGCCTGCCTGACAGGGTGCCCTGAGTTGTCGAGTCACCCGGGCCAGTGGGGCCCGCATGGTGAGGTCTCTCCGGTGGTGGGTTATGAGGAGCGGCGGTTCAATGCCACCTGTCTGCTCTCCACCCGCCTGGGCATCTCTCGGACTCGGGCCGGTCAGATGGTGGATCACGGCCAGGCCCTCATGAGCATGGGCTTCGCCCCGGTCGAGGCCATGGAACGCTGCGGGGTCCTGGACTCGGCGAAGGCGTTCCTGGTGACCCGCCGTCTGGAAGACGTACCTACTCCAGTGGCACTGGCGGTCCAGGACAAGGTTCTGCCTCAGGCGCCCAGGCGGAGCGTATCGCAGGTGGGGCGGGATCTGGATCGTGCCCTGATGGAGATCGACCCTGACGGCCACGCTGAGCGGAGCCAGAACAATACCGAGCAGCGGTGTGTGTCGCGCCCCCGGCCTGCAGGAGAGGGCCTCTGCCAAGTCCGGCTTCTGCTGCCAACCATGGACGCCCTGCTGCTGGACGCCACCCTGGACGCAATCGCCGCTTCGGCGCGGGCCTGCGGCGAGAAGCGCACCCTGGGGCAGCTGCGAGCCGATGCCATCACCGCGATGACCCTCTCAACACTGCGTACCAGCCAGCAGGCCGCCTACCATATGCCCGCACAAGCCCCCACCACCCCCGCAAGCACAAATCACGACGGCAGCAGCGGTGGCGACGACGGCACCGACAACGACAATCACGGAGGGTACAGCCTCGGCGGCGGCGGCGTCTGCGGCAGCGGCATCAGTGCCAGCGGTGATGACGGTATCTGTGGTGGTGGTTTGAGTGAGCCGGGTTCAGTGCTCTCGTCCTCGGTTCCTCTTGAGCCCCCTTCCCCGGGGCGGCTGCTGCCTGACGGGGTACCTCTGGAAGGGCTCCTGGGCGCTTTGAGCGGCCTGGTGGGATCGAACAGCCCGTGGTGGACCCCTTCGGCCACCGGTCACCTTCCTCTGCCAGAAGGCATCCACATCAACGTCAACGTCACCGTTCCTCTGAGCAGCCTGGTTGGTCTGGCTCTGCCAGAAAATGGCCCCACCGGCGCCGTCGATCCCGGAGGCGGCGGCCCCGGCACCACATCCGAAGACAACCGGCTCCGGGACGGCATTTCTGGGGGCTGTGGTCCTGGGGACAGCGAGAGCCCCGACGACCCCGACTGTCTTGTTCCAGGTGGTGCCGGCCCTGGCGAATGCTCCACCACCGCGTCCGAGCCTCTCAACAGCGCAGACTCCCCGAGCGGCGGGAGTAATCTGCCCACCCCCGGTGGGAGAAGTCTGCCCGGGTCTCGAGGGAGGAGTCTGCCTGAACTCGCCCCGGTTGCTCCCACCATCCAGCCCACCGCCCAGGTCATCTCCCCGTTTTCCGCCACACCAGTAGAGGTCGCTGAGGTGAGGATCGGGGCGCGCAGCGCAGCGGTACCGGCCATGACTGCCTGGGCCCTGGCCGCCGGCGGGACCTGGAGGCGCCTGGTGACCGACCCCGCCAGCGGCACCGTTCTGGACGTCGGCCGCACCAGGTACCGGCCTCCGGTAGGACTTGCGGATCTCGTACGAGCCCGCGACAAAACATGTGTTTTCCCCACCTGCCAGACTCCGGCCTCCCGCTGCGATATCGACCACCTCACCGCCTGGAGTCAGGGCGGGACCACCAGCCTGGACAACCTCGTGGTGCTCTGTCAGGCCCATCACCGACTCAAGCACACTCCCGGATGGGCACTCACCAGGGACCGTGACAGCGGGGTCTTGTCTTGGCACACTCCGGACAAGACCGTCTATCGGCGCCACCCAGACGGCACCATCGACCGCCTGCCCCACAAGGTCGGCCCCCACCAGTACCTTGTTCCCAGCACCGTCGTCCCGGCCGACCTGAGCCAGCAGATCGGCCCCGAGCTCATCGACCGACTCAACACCGCCCTCGACCGTACCCAGCCCAGCAGCGGCAGTGCCCGCCTCGTGACCCGAGGTCCCCTACCCGGCGAAAAGGCGGGAGACTACGAGACCACCCCTCTTCCGAGGGCCGCCCACTCCTTGGGACTAGCGCCCCTCATCGACCAAGCCCCACCCTTCTGA","VRFSLTSQQRSFPTRASWCWGTAYRPPAVGPGGVRPTGGRDRSRRWSPARFERSRRAVTPAPRGEGAVDKGARYAANRCCSSDSGACFSVRGTGTTCYTVHMFEGVVLPRVPTGGAVGTLGAPGGAPTSVPQVSAEETAGLLASLGAGQALAGVVEGLLAHLLVTAQDADDECSTADGDAVPPLFTNESGTDVALVAASEQRRTMGVEEVGTSGLIGLGASGLGELAAACRRLAAWATWGEALAAACLTGCPELSSHPGQWGPHGEVSPVVGYEERRFNATCLLSTRLGISRTRAGQMVDHGQALMSMGFAPVEAMERCGVLDSAKAFLVTRRLEDVPTPVALAVQDKVLPQAPRRSVSQVGRDLDRALMEIDPDGHAERSQNNTEQRCVSRPRPAGEGLCQVRLLLPTMDALLLDATLDAIAASARACGEKRTLGQLRADAITAMTLSTLRTSQQAAYHMPAQAPTTPASTNHDGSSGGDDGTDNDNHGGYSLGGGGVCGSGISASGDDGICGGGLSEPGSVLSSSVPLEPPSPGRLLPDGVPLEGLLGALSGLVGSNSPWWTPSATGHLPLPEGIHINVNVTVPLSSLVGLALPENGPTGAVDPGGGGPGTTSEDNRLRDGISGGCGPGDSESPDDPDCLVPGGAGPGECSTTASEPLNSADSPSGGSNLPTPGGRSLPGSRGRSLPELAPVAPTIQPTAQVISPFSATPVEVAEVRIGARSAAVPAMTAWALAAGGTWRRLVTDPASGTVLDVGRTRYRPPVGLADLVRARDKTCVFPTCQTPASRCDIDHLTAWSQGGTTSLDNLVVLCQAHHRLKHTPGWALTRDRDSGVLSWHTPDKTVYRRHPDGTIDRLPHKVGPHQYLVPSTVVPADLSQQIGPELIDRLNTALDRTQPSSGSARLVTRGPLPGEKAGDYETTPLPRAAHSLGLAPLIDQAPPF$","HNH endonuclease","Periplasm, Membrane, Extracellular","HNH endonuclease domain protein","HNH nuclease","HNH endonuclease","","Dalgaard J.Z., Klar A.J., Moser M.J., Holley W.R., Chatterjee A., Mian I.S. Statistical modeling and analysis of the LAGLIDADG family of site-specific endonucleases and identification of an intein that encodes a site-specific endonuclease of the HNH family. Nucleic Acids Res. 1997. 25(22):4626-4638. PMID: 9358175Gorbalenya A.E. Self-splicing group I and group II introns encode homologous (putative) DNA endonucleases of a new family. Protein Sci. 1994. 3(7):1117-1120. PMID: 7920259Shub D.A., Goodrich-Blair H., Eddy S.R. Amino acid sequence motif of group I intron endonucleases is conserved in open reading frames of group II introns. Trends Biochem. Sci. 1994. 19(10):402-404. PMID: 7817395","","","

InterPro
IPR002711
Domain

HNH endonuclease
PF01844	$\"[778-824]T$	HNH

InterPro
IPR003615
Domain

HNH nuclease
SM00507	$\"[766-818]T$	HNHc

","No hits to the COGs database.","***** IPB003870 (Protein of unknown function DUF222) with a combined E-value of 7.2e-18. IPB003870F 758-798","Residues 705-840 are 46% similar to a (MB3101 MB1413C) protein domain (PD031496) which is seen in Q73V65_MYCPA.Residues 750-825 are similar to a (REPEAT 13E12 FAMILY ENDONUCLEASE HNH REP13E12 RV1945/MT1995 RESTRICTION MB1980 RV1148C/MT1183/MB1179C) protein domain (PD010625) which is seen in Q9ZB93_RHOER.","","No significant hits to the PDB database (E-value < E-10).","Residues 778 to 824 (E_value = 2.3e-08) place ANA_0502 in the HNH family which is described as HNH endonuclease.","","endonuclease domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0504","526256","529237","2982","4.94","-46.56","109714","ATGTCAGAGAGAACCGCACCGGTCGAGTCCGACACCCCCTTCCGCTACACGGCGGAGCTGGCGGACTCCATCGAGACCGCCTGGCAGGACCGCTGGGAGGCCGAGGGCACCTTCAACGCCGACAACCCCGTCGGCGCTCTGGCCGGCCCCGGGGCGGACAAGGAGAAGTTCTTCCTGCTGGACATGTTTCCCTACCCCTCCGGCAAGGGCCTGCACGTGGGCCACCCGCTGGGCTACATCGCCACCGACGTCGTCGCCCGTTTCACCCGGATGACTGGCAGGAACGTCCTGTACACGATGGGCTACGACGCCTTCGGTCTGCCCGCCGAGCAGTACGCCGTCACCACTGGCCAGCACCCGCGCATCTCCACCGAGGCCAACATCGCCAACATGCGCCGCCAGCTGCGCCGCCTGGGCCTGTCCCACGACCCGCGCCGCTCCCTGGCCACGATCGACGTCGACTACGTGCGCTGGACCCAGTGGATCTTCCTGCAGGTCTTCAACTCCTGGTTCGACCCCGAGGCCCCGCGCCGCGACGGCCGCGGCAAGGGTGCGGCCCGGCCTGTGACCGAGCTGCGCGACAAGCTCGCCTCCGGCCAGGTCCCCGTCCCCGACGGCCGCGACTGGGACGCTCTGAGCGCCGCCGAGCAGGCCGAGGTCATCGACTCCTTCCGCCTGGCCTACGTCTCCAGCGCCCCTGTCAACTGGTGCCCCGGCCTGGGCACGGTGCTGGCCAACGAGGAGGTCACCTCAGAGGGTCGCTCCGAGCGGGGCAACTACCCGGTCTTCAAGCGCAACCTGCGCCAGTGGATGATGCGCATCACCGCCTACGGCGACCGCCTCGCCGAAGACCTGGACACCGTGGACTGGCCCGAGAAGGTCAAGCTCATGCAGCGCAACTGGATCGGACGCTCCGAGGGCGCCGAGGTGACCTTCACCGTCCCCGGGGCCGGTCAGGGCGACCAGCAGGACGCGTCGCTGAGCGTCTACACCACCCGCCCCGACACCCTCTTCGGCGCCACCTTCATGGTGGTGGCCCCCGAGCACCCCATGCTGGGTGGCCTGCAGGCCTCCGGCTCGGTGCGCACCGAGGCCCAGATCGCCGACGACGCCGCGGCCCTGACTGTCCCGGCCGCCTGGCCCGAGGGCACCAAGGAGGCCTGGACCGGCGGCTACGCGACCCCCGCCGAGGCCGTGGCCGCCTACCGCGCCCAGGCCGCGGCGACGTCGGACGCCGACCGCACCGACGAGGGCCGGGTCAAGACCGGCGTCTTCACCGGCTTCTTCGGCATCAACCCCGTCAACGGGGCGAAGGTGCCGGTCTTCGTGGCCGACTACGTCCTCATGGGCTACGGGACTGGCGCCATCATGGCCGTGCCCGCCCACGACGAGCGCGACTACGCCTTCGCCACCAAGTACGACATCGACATCGTCCAGACCATCGGCCCGGCTGACGACCCCCACGGCGTCGACCTGAGCGCCCAGGCCTACACCGGTGACGGTGTGGTCGTGAACTCCGCCCAGGGCGACCTGGACATCAACGGCATGGGCAAGGACGAGGCCAAGGCCACCATGATCGGCTGGCTGGAGGCCAAGGGGGCCGGCCGCGGCGCGGTCACCTACCGCCTGCGCGACTGGCTCTTCTCCCGCCAGCGCTACTGGGGTGAGCCCTTCCCGATCGTGTGGGACGAGGACGGCGGCGTCCACGCCCTGCCTGAGTCGATGCTGCCGGTCGAGCTGCCCGAGGTCACCGACTACTCTCCGCGCTCCTACGACCCCGACGACGCAGACTCCTCCCCGGAGCCGCCGCTGGGCAAGGCCACCGAGTGGGTCGAGGTCGAGCTCGACCTGGGCGATGGCCCCCGGACCTACTACCGCGAGACCAACACGATGCCGCAGTGGGCCGGCTCGTGCTGGTACGAGATGCGCTACATCGACCCCACCGATGACAAGGCGCTCGTCGACCCGGCCAACGAGGCCTACTGGATGGGGCCGCGCCCTCAGGCCGGCAACATCTCCGGCGGCACCGACCTGTACGTCGGCGGTGTCGAGCACGCCGTCCTGCACCTGCTTTACGCGCGCTTCTGGCACAAGGTCCTGTTCGACCTGGGCCACGTCTCCTCCTCCGAGCCCTACCACCGCCTCTTCAACCAGGGCTACGTCCAGGCCTACGCCTACACCGACTCCCGCGGCCAGTACGTGCCCGCTGACGAGGTCGAGGAGGTCACCGCCGAGGACGGCTCCACCAGCTACCTGTGGCAGGGGCAGCCCGTGCGTCGCGAGTACGGCAAGATGGGCAAGTCCCTGAAGAACATCGTCACCCCCGACGACATGTACGAGGCCTACGGCGCCGACACCTTCCGCGTCTACGAGATGAGCATGGGGCCGCTGGACGCCGACCGCCCGTGGGACACCCGCGCCGTCGCCGGCAGCCAGCGCTTCCTGCAGCGCCTGTGGCGCAACGTCATCGACGAGACCACCGGCGAGCTGACGGTGACCGAGCAGAGCGCCGACGAGGAGACCCGCCGGCTCGTGGCCAAGACGATCGTGGGCGTGCGCGAGGACTACGAGGGGATGCGCCTGAACACGGCCATCGCCAAGCTCATCGTCCTCAACAACCACCTCACCGGGCTCGGGGAGGTCCCGCGCGAGGCCGTCGAGGCCCTCGTCCTCATGACGGCGCCTGTGGCTCCGCACATCGCCGAGGAGATCTGGAAGCGCCTGGGCCACGAGCACTCCCTGGCCCACGAGGACTTCCCGGTCGTGACCGACGAGGCGCTGCTGGCCGCCGAGAAGGTCACCTGCGTCATCCAGGTCAAGGGCAAGGTCCGCGACCGCCTCGAGGTCGACCCCGACATCTCCGAGGCCGAGCTCGAGAAGCTGGCCCTGGAGGCCCCCGGCGTCATCCGCACCCTGGACGGGCGCGGCGTGCGCAAGGTGATCGTGCGCGCCCCTAAGTTGGTGAGCATCGTCCCCGAGTGA","MSERTAPVESDTPFRYTAELADSIETAWQDRWEAEGTFNADNPVGALAGPGADKEKFFLLDMFPYPSGKGLHVGHPLGYIATDVVARFTRMTGRNVLYTMGYDAFGLPAEQYAVTTGQHPRISTEANIANMRRQLRRLGLSHDPRRSLATIDVDYVRWTQWIFLQVFNSWFDPEAPRRDGRGKGAARPVTELRDKLASGQVPVPDGRDWDALSAAEQAEVIDSFRLAYVSSAPVNWCPGLGTVLANEEVTSEGRSERGNYPVFKRNLRQWMMRITAYGDRLAEDLDTVDWPEKVKLMQRNWIGRSEGAEVTFTVPGAGQGDQQDASLSVYTTRPDTLFGATFMVVAPEHPMLGGLQASGSVRTEAQIADDAAALTVPAAWPEGTKEAWTGGYATPAEAVAAYRAQAAATSDADRTDEGRVKTGVFTGFFGINPVNGAKVPVFVADYVLMGYGTGAIMAVPAHDERDYAFATKYDIDIVQTIGPADDPHGVDLSAQAYTGDGVVVNSAQGDLDINGMGKDEAKATMIGWLEAKGAGRGAVTYRLRDWLFSRQRYWGEPFPIVWDEDGGVHALPESMLPVELPEVTDYSPRSYDPDDADSSPEPPLGKATEWVEVELDLGDGPRTYYRETNTMPQWAGSCWYEMRYIDPTDDKALVDPANEAYWMGPRPQAGNISGGTDLYVGGVEHAVLHLLYARFWHKVLFDLGHVSSSEPYHRLFNQGYVQAYAYTDSRGQYVPADEVEEVTAEDGSTSYLWQGQPVRREYGKMGKSLKNIVTPDDMYEAYGADTFRVYEMSMGPLDADRPWDTRAVAGSQRFLQRLWRNVIDETTGELTVTEQSADEETRRLVAKTIVGVREDYEGMRLNTAIAKLIVLNNHLTGLGEVPREAVEALVLMTAPVAPHIAEEIWKRLGHEHSLAHEDFPVVTDEALLAAEKVTCVIQVKGKVRDRLEVDPDISEAELEKLALEAPGVIRTLDGRGVRKVIVRAPKLVSIVPE$","Leucyl-tRNA synthetase","Cytoplasm","leucyl-tRNA synthetase","leucyl-tRNA synthetase ","leucyl-tRNA synthetase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[66-76]T$	AA_TRNA_LIGASE_I

InterPro
IPR002300
Domain

Aminoacyl-tRNA synthetase, class Ia
PF00133	$\"[27-111]T$ $\"[431-478]T$	tRNA-synt_1

InterPro
IPR002302
Family

Leucyl-tRNA synthetase bacterial/mitochondrial, class Ia
PR00985	$\"[150-167]T$ $\"[626-644]T$ $\"[676-698]T$ $\"[709-719]T$	TRNASYNTHLEU
PTHR11946:SF7	$\"[24-163]T$ $\"[225-284]T$ $\"[318-367]T$ $\"[400-719]T$ $\"[762-991]T$	LEUCYL-TRNA SYNTHETASE
TIGR00396	$\"[21-993]T$	leuS_bact: leucyl-tRNA synthetase

InterPro
IPR013155
Domain

tRNA synthetase, valyl/leucyl, anticodon-binding
PF08264	$\"[883-961]T$	Anticodon_1

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[53-773]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.730.10	$\"[782-927]T$	no description
PTHR11946	$\"[24-163]T$ $\"[225-284]T$ $\"[318-367]T$ $\"[400-719]T$ $\"[762-991]T$	ISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES

","BeTs to 23 clades of COG0495COG name: Leucyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0495 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB013155 (tRNA synthetase, valyl/leucyl, anticodon-binding) with a combined E-value of 1.7e-99. IPB013155A 25-38 IPB013155B 64-106 IPB013155C 134-152 IPB013155D 225-249 IPB013155E 329-348 IPB013155F 440-476 IPB013155G 545-559 IPB013155H 762-788***** IPB002302 (Leucyl-tRNA synthetase signature) with a combined E-value of 2.5e-84. IPB002302A 150-167 IPB002302B 231-247 IPB002302C 264-277 IPB002302D 293-312 IPB002302E 626-644 IPB002302F 676-698 IPB002302G 709-719***** IPB002300 (Aminoacyl-tRNA synthetase, class Ia) with a combined E-value of 3.5e-22. IPB002300A 71-101 IPB002300B 546-559","Residues 5-49 are 69% similar to a (SYNTHETASE LIGASE BIOSYNTHESIS LEUCYL-TRNA AMINOACYL-TRNA LEURS ATP-BINDING LEUCINE--TRNA LEUS) protein domain (PD684730) which is seen in SYL_STRCO.Residues 28-112 are 78% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS LEUCYL-TRNA METHIONYL-TRNA ISOLEUCYL-TRNA VALYL-TRNA LEURS) protein domain (PD000389) which is seen in Q6NEF5_CORDI.Residues 134-165 are 84% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS LEUCYL-TRNA VALYL-TRNA LEUCINE--TRNA LEURS VALINE--TRNA) protein domain (PD211021) which is seen in SYL_STRAW.Residues 170-239 are 63% similar to a (SYNTHETASE LIGASE LEUCYL-TRNA AMINOACYL-TRNA BIOSYNTHESIS LEURS ATP-BINDING LEUCINE--TRNA LEUS) protein domain (PD336958) which is seen in SYL_STRCO.Residues 226-307 are 60% similar to a (LIGASE LEUCINE-TRNA) protein domain (PDA135S8) which is seen in Q8IBB3_PLAF7.Residues 240-316 are 84% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING LEUCINE--TRNA BIOSYNTHESIS LEUCYL-TRNA LEURS) protein domain (PD747596) which is seen in SYL_STRAW.Residues 240-298 are 91% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA LEUCYL-TRNA ATP-BINDING BIOSYNTHESIS LEUCINE--TRNA LEURS ISOLEUCYL-TRNA VALYL-TRNA) protein domain (PD386284) which is seen in SYL_COREF.Residues 297-343 are 65% similar to a (SYNTHETASE AMINOACYL-TRNA LEUCYL-TRNA LIGASE ATP-BINDING LEUCINE--TRNA SIGNAL BIOSYNTHESIS PRECURSOR LEURS) protein domain (PD512086) which is seen in Q6ND22_RHOPA.Residues 329-541 are 61% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA LEUCYL-TRNA VALYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD000939) which is seen in SYL_CORGL.Residues 495-544 are 66% similar to a (SYNTHETASE AMINOACYL-TRNA PROBABLE LEUCYL-TRNA) protein domain (PDA19220) which is seen in Q6MCC8_PARUW.Residues 545-582 are 94% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA VALYL-TRNA LEUCYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD000647) which is seen in SYL_CORGL.Residues 604-712 are 80% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA LEUCYL-TRNA LEUCINE--TRNA BIOSYNTHESIS LEURS ATP-BINDING MITOCHONDRIAL PRECURSOR) protein domain (PD211055) which is seen in SYL_CORGL.Residues 713-785 are 78% similar to a (SYNTHETASE LIGASE LEUCYL-TRNA AMINOACYL-TRNA BIOSYNTHESIS LEURS ATP-BINDING LEUCINE--TRNA LEUS) protein domain (PDA0G8P2) which is seen in SYL_BIFLO.Residues 786-882 are 78% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA LEUCYL-TRNA LEUCINE--TRNA BIOSYNTHESIS LEURS ATP-BINDING PRECURSOR MITOCHONDRIAL) protein domain (PD685300) which is seen in SYL_BIFLO.Residues 843-991 are 45% similar to a (LIGASE PEPTIDE TRANSIT BIOSYNTHESIS MITOCHONDRION SYNTHETASE LEUCYL-TRNA SYNTHETASE AMINOACYL-TRNA PRECURSOR) protein domain (PD283354) which is seen in SYLM_NEUCR.Residues 900-991 are 76% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA LEUCYL-TRNA LEUCINE--TRNA BIOSYNTHESIS LEURS ATP-BINDING PROBABLE PRECURSOR) protein domain (PD118334) which is seen in SYL_STRCO.","","-47% similar to PDB:1H3N LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A SULPHAMOYL ANALOGUE OF LEUCYL-ADENYLATE (E_value = 7.1E_144);-47% similar to PDB:1OBC LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A POST-TRANSFER EDITING SUBSTRATE ANALOGUE (E_value = 7.1E_144);-47% similar to PDB:1OBH LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A PRE-TRANSFER EDITING SUBSTRATE ANALOGUE IN BOTH SYNTHETIC ACTIVE SITE AND EDITING SITE (E_value = 7.1E_144);-47% similar to PDB:2BTE THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION AND A POST-TRANSFER EDITING SUBSTRATE ANALOGUE (E_value = 7.1E_144);-47% similar to PDB:2BYT THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION (E_value = 7.1E_144);","Residues 27 to 111 (E_value = 2.6e-05) place ANA_0504 in the tRNA-synt_1 family which is described as tRNA synthetases class I (I, L, M and V).Residues 63 to 827 (E_value = 0.00044) place ANA_0504 in the tRNA-synt_1g family which is described as tRNA synthetases class I (M).Residues 431 to 478 (E_value = 0.00033) place ANA_0504 in the tRNA-synt_1 family which is described as tRNA synthetases class I (I, L, M and V).Residues 838 to 961 (E_value = 7e-07) place ANA_0504 in the Anticodon_1 family which is described as Anticodon-binding domain.","","synthetase (leuS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0505","531674","529359","2316","5.64","-10.82","80273","GTGCACCAGCAGCCGGCCCATCAGGGGCGGTTCTTTCGGAAACGACGACGCAGGGGGCAGCATGGGGCGTGTAAACCTCGCGGCACTGGGGCGGGCAGGTGCGGGATCAGACGTACTATCTCAACGCCATTGAGGCCCGAGGGTACCTTGTTCGCCGGGCTCCTGCCTCTCTCACGGTCAGAAACGGCGCCGGCTCCACTGGCATGCCCGGGTCAGCGCACTGGCAGGTTCGGCGTTTACGATGGCGCCATGACCGATTCCGCTGAGATCGCACGCCTCAAGGCCGAGGCCGCACAGGCCGCCGCCGAAGCCGCCGCAGCCAAGGCAGCCGCCGCCCAAGCGGCCCTTGACGCCGCCCTCGCCTCCACCCCGGCCTCGGCCGTGGAGCAGGCCGGCGAGCCCCGCACTACTGACGCACCGGGCGAGCCCGCCGCTCAGGCAGCCGACGCCGCCCCCGTCGCCGAACCTGCTGCCGCCCCGGTTGCACAGCCGGCAGAACAGCCTGCGGCTGAGCCGGCGGCGGCCGCCGAACCGGTACCGACTGCCGAGCAGCCCCAGGAGCCAGTTCAGGATCCGGCACCCGCGCAGGCCGAGACCGCCGCTGCGGCCGAGCATGCCTCGGGCAGTCAGGAGGCCGAGGAGGCCGGCTACACCGCCCAGGTGCGTTCCGGCTACAGCTTCTCCTCCCCCACCCTGCCGGTGGGCACCTACCTCGACACGCTCTCGGGGGGCGAGCCCGCGGCGGTCAAGGACCTGTCGGTGGGCATCCCGCTGGGACTGCTCAACCGGCACGCGCTGGTGGCCGGGGCGACCGGAACCGGTAAGACCCGCACGCTCCAGCTCCTGGCCGAGGGGCTGTCCGCCGCCGGCGTCCCGGTGTTCCTGGCCGACGTCAAGGGGGACCTGACCGGACTGGCCGAGGCCGGAGCCTCCAATGACAAGATCGCCTCCCGCATCGCCTCCACCGGCCAGGACTGGACGGGCCAGTCCTTCCCCATCGAGCTGTTCAACCTCGGCGGGTCGGACTCCGGCGCCGGCATCAGCGGCACCCCGATCCGCACGACGGTCACCGAGTTCGGGCCGATCCTGCTCTCGCGGGTCCTGGGCCTGAACGACACGCAGGCCTCCGCCCTCCAGCTGGTGTTCCACTGGGCGGACAGCCAGGGGCTGGCCCTGCTGGACCTGAAGGACCTGCGCGCCGTCGTCGACTATCTGACGAACACGGAGGCCGGTAAGGAGGAGCTCAAGACCATCGGCGGGGTCTCCGCGGCCACGGCCGGGGTCATCCTGCGGGAGATCGCCGCCCTGGAGGCGGCCGGCGGTGAGGCCTTCTTCGGTGAGCCGGCGCTCGACGTGCGTGACCTCATGCGGGTCTCCCCCGATGGGCGCGGCATCATCTCCGCCCTGGAGCTGGCCGACATCCAGTCCCAGGGCACGCTGTTCTCCACCTTCCTCATGTGGCTGCTCGCCGAGCTCTTCGAGACCCTGCCGGAGGTCGGCGACCCGGACAAGCCCACCATGGTGTTCTTCTTCGACGAGGCGCACCTGCTGTTCTCCGGTGCCTCGAAGGCCTTCCTGGAGGCCGTGGTGCGCACGGTGCGGCTCATTCGCTCCAAGGGCGTGGGCATCGTCTTCATCACCCAGTCGCCCACGGACGTCCCCGACGAGGTCCTGGCCCAGCTCGGCAGCCGGGTGCAGCACGCGCTGCGCGCCCACACCCCGGCCGACGCCGCCAACCTCAAGAAGGCGGTCTCCACCTTCCCGGTCAGCCCGGTGGACCTCAGCCGGGTGCTCACGTCGCTGGGCACCGGCCAGGCCGTCGTCAGCGTGCTGGACGAGAAGGGGCGCCCGGCGCCGGTGGCCCCGGTGGTCATCAACGTGCCCGCCGCCGTCATGGGGCCGGCCCAGGACGGCACCGTCAGCCAGGTGCTGGCCTCCTCACCGCTGAAACCCAAGTACGCCACGAGTGTGGACAACGAGTCCGCCTACGAGCTGCTGGCCCAGCGGGTCCAGGCCGACGCCGAGGCCGCCGAGGCCGCTCGCGCCGCCGAGCAGGCCGCCAAGGAGCAGGCCAAGGCCGACGCCGCCGCGCAGAAGGCCCTGGAGAAGGAGGCCGCCCGCCAGGCGGCTCAGCGTCAGAAGGAGGCCGAGCGCCTGGAGCGCGAGGCCGTCAAGGAGGCCCAGCGTCGCCAGCGCGAGGAGGAGAAGGCTGCCGAGCGCCGCAAGCGGGAGGTCGAGAAGACCATTGGCTCGGTGGGCCGCCAGATCACCCGCGAGATCACGCGCTCCATCTTCGGCACCCTCAGGCGCCGCTGA","VHQQPAHQGRFFRKRRRRGQHGACKPRGTGAGRCGIRRTISTPLRPEGTLFAGLLPLSRSETAPAPLACPGQRTGRFGVYDGAMTDSAEIARLKAEAAQAAAEAAAAKAAAAQAALDAALASTPASAVEQAGEPRTTDAPGEPAAQAADAAPVAEPAAAPVAQPAEQPAAEPAAAAEPVPTAEQPQEPVQDPAPAQAETAAAAEHASGSQEAEEAGYTAQVRSGYSFSSPTLPVGTYLDTLSGGEPAAVKDLSVGIPLGLLNRHALVAGATGTGKTRTLQLLAEGLSAAGVPVFLADVKGDLTGLAEAGASNDKIASRIASTGQDWTGQSFPIELFNLGGSDSGAGISGTPIRTTVTEFGPILLSRVLGLNDTQASALQLVFHWADSQGLALLDLKDLRAVVDYLTNTEAGKEELKTIGGVSAATAGVILREIAALEAAGGEAFFGEPALDVRDLMRVSPDGRGIISALELADIQSQGTLFSTFLMWLLAELFETLPEVGDPDKPTMVFFFDEAHLLFSGASKAFLEAVVRTVRLIRSKGVGIVFITQSPTDVPDEVLAQLGSRVQHALRAHTPADAANLKKAVSTFPVSPVDLSRVLTSLGTGQAVVSVLDEKGRPAPVAPVVINVPAAVMGPAQDGTVSQVLASSPLKPKYATSVDNESAYELLAQRVQADAEAAEAARAAEQAAKEQAKADAAAQKALEKEAARQAAQRQKEAERLEREAVKEAQRRQREEEKAAERRKREVEKTIGSVGRQITREITRSIFGTLRRR$","ATP-binding protein","Cytoplasm, Periplasm","conserved ATP-binding protein","hypothetical protein","protein of unknown function DUF853, NPT hydrolase putative","","Novoseler M., Hershkovits G., Katcoff D.J. Functional domains of the yeast chromatin protein Sin1p/Spt2p can bind four-way junction and crossing DNA structures. J. Biol. Chem. 2005. 280(7):5169-5177. PMID: 15563464","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[261-575]T$	AAA

InterPro
IPR008571
Family

Protein of unknown function DUF853, NPT hydrolase putative
PF05872	$\"[242-771]T$	DUF853

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[475-716]T$	no description

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[641-733]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[257-555]T$	no description

","BeTs to 11 clades of COG0433COG name: Predicted ATPaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0433 is aompkz-qvdrlbcef-h---j----Number of proteins in this genome belonging to this COG is 1","***** IPB009435 (Acid shock) with a combined E-value of 2.7e-08. IPB009435A 97-123 IPB009435B 681-710 IPB009435A 101-127 IPB009435B 676-705 IPB009435B 96-125 IPB009435B 671-700 IPB009435B 87-116 IPB009435B 667-696 IPB009435B 92-121 IPB009435B 686-715 IPB009435B 85-114 IPB009435B 682-711 IPB009435B 101-130***** IPB010528 (TolA) with a combined E-value of 2.6e-06. IPB010528A 696-744 IPB010528A 667-715 IPB010528A 698-746 IPB010528A 669-717 IPB010528A 659-707 IPB010528A 699-747 IPB010528A 690-738 IPB010528A 668-716 IPB010528A 680-728 IPB010528A 676-724 IPB010528A 682-730 IPB010528A 678-726 IPB010528A 666-714 IPB010528A 662-710 IPB010528A 663-711 IPB010528A 684-732 IPB010528A 693-741 IPB010528A 672-720 IPB010528A 679-727 IPB010528A 695-743 IPB010528A 674-722 IPB010528A 687-735 IPB010528A 685-733 IPB010528A 681-729 IPB010528A 689-737 IPB010528A 656-704 IPB010528A 675-723 IPB010528A 692-740 IPB010528A 671-719 IPB010528A 670-718 IPB010528A 688-736 IPB010528A 654-702 IPB010528A 653-701 IPB010528A 655-703 IPB010528A 708-756 IPB010528A 664-712 IPB010528A 657-705 IPB010528A 697-745 IPB010528A 83-131 IPB010528A 673-721 IPB010528A 677-725 IPB010528A 702-750 IPB010528A 704-752 IPB010528A 650-698 IPB010528B 675-705 IPB010528B 86-116 IPB010528B 679-709 IPB010528B 683-713 IPB010528B 680-710 IPB010528B 99-129 IPB010528B 674-704 IPB010528B 101-131 IPB010528B 670-700 IPB010528B 92-122 IPB010528B 669-699 IPB010528B 88-118 IPB010528B 95-125 IPB010528B 87-117 IPB010528B 676-706 IPB010528B 89-119 IPB010528B 678-708 IPB010528B 687-717 IPB010528B 673-703 IPB010528B 661-691 IPB010528B 667-697 IPB010528B 685-715 IPB010528B 100-130 IPB010528B 103-133 IPB010528B 672-702 IPB010528B 692-722 IPB010528B 686-716","Residues 262-382 are 74% similar to a (ATP-BINDING YJGR HYDROLASE ATPASE CONTAINS SPY0500 ECS5240 CC0090 Y3952 ENZYME) protein domain (PD038851) which is seen in Q7TYF0_MYCBO.Residues 411-488 are 70% similar to a (ATP-BINDING YJGR HYDROLASE ATPASE CONTAINS SPY0500 ECS5240 CC0090 Y3952 ENZYME) protein domain (PD607005) which is seen in Q82FS7_STRAW.Residues 491-555 are 83% similar to a (ATP-BINDING PLASMID TRAC ATPASE TRANSFER YJGR ASSEMBLY TRANSPOSON TRAE PILUS) protein domain (PD005306) which is seen in Q92RC7_RHIME.Residues 561-657 are 64% similar to a (ATP-BINDING YJGR HYDROLASE ATPASE CONTAINS SPY0500 ECS5240 CC0090 Y3952 ENZYME) protein domain (PD469526) which is seen in Q82FS7_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 242 to 771 (E_value = 3.3e-228) place ANA_0505 in the DUF853 family which is described as Bacterial protein of unknown function (DUF853).","","ATP-binding protein (f500)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0506","531701","532948","1248","5.93","-8.31","46063","GTGCGGATCGCCTTCTTCATTGACGACTACCTGCCCTCCGTCCACGGCGTGGCCACCTCCACAGCCACCTTCCGTGCCGCCCTGGAGCGCATGGGACACGAGGTCTACGTGGTGGCCCCCAAGGCCGAGGGCTATGAGGAGACCGACGACCACGTCATCCGCCTGTCCTCCTCGCGCTACTACGTCTTCGACAGCCGCGAGGTCGCCACCATCTATCCGGGCCTGGCCCGGCGCTTCGACGCTTACGACTTCGACATCGTCCACAGCCAGACCCAGTTCAGCCTGGGGGTCCTGGCGCACTGGGTGGCCAAGCGCCAGAACATCCCCCACGTCACCACCATCCACACCCTCTACACCGAGCTCATCGACGACTACCCGCTGGCCGTGCTCTCGGGCCTGCTTGCTCTGTCCGTCGCCTTCCCCGTGGCGCTCAAGTCGCAGCCTGTCCTGCCGCGCGTTCACCGGGAGACCATCAAGCACCTCAACAAGCGTGACATGAAGACGGCCCTGTCCCGTCAGGGGTGGCGCCTGACGGCGGCCTTCGCCAACAAGTGCGACGCCTGCCTGTCGCCCTCCCAGCACCTGGCCCGGATTCTCATCGACGACGGCGGACTGACCACCCCCTGCATGGTGCTGCCCAACGGGCTGGACTCCACCCGCTACCGTAGTGCCCGCGCCGCCGACTCACCGATCCCCAAGGCCCCCGGCGAGAAGATCATCATCTGCGTGGCCCGCCTCAGCCCGGAGAAGCGGCAGATGACGCTCGTTGAGGCCATGCCCCACCTGTCCGACCTGTCGGTCAAACTGGTGCTCGTGGGCCCGGGCCCCTCCCAGGAGGAGCTGGGGCGGCGCGCCGAGGAGCTCGGGGTGGCGGATCGGGTGATCCTGACCGGTCAGCGCTCGCCGGAGGAGGTCGCCGTCCTGCTCAAGCAGGCCGATGTCTTCTCCCTGGCCTCCTACCACTTCGACAACCAGCCCATGGTGTTCCTGGAGGCAGCCGCCTGCGGGCTGCCGATCGTCTACTGCGATGAGCGGATGACCGAGTGCCTCACCGAGCGCAACGCGATTCTCACCGACGGCATCGAGGGGGAGGACTTCGCCCGGGTCTTCGCCTCCCTGCTGTCCGACGACGCCCGGCTCGCCGCGCTGTCCGAGGGCGCCCTGGAGGTGGCTCAGCAGTTCGACTCCGAGACGATGACCAGGCGGCTCATCAACCTCTACGAGGACCTCCTGGTCTCCTATCGCTGA","VRIAFFIDDYLPSVHGVATSTATFRAALERMGHEVYVVAPKAEGYEETDDHVIRLSSSRYYVFDSREVATIYPGLARRFDAYDFDIVHSQTQFSLGVLAHWVAKRQNIPHVTTIHTLYTELIDDYPLAVLSGLLALSVAFPVALKSQPVLPRVHRETIKHLNKRDMKTALSRQGWRLTAAFANKCDACLSPSQHLARILIDDGGLTTPCMVLPNGLDSTRYRSARAADSPIPKAPGEKIIICVARLSPEKRQMTLVEAMPHLSDLSVKLVLVGPGPSQEELGRRAEELGVADRVILTGQRSPEEVAVLLKQADVFSLASYHFDNQPMVFLEAAACGLPIVYCDERMTECLTERNAILTDGIEGEDFARVFASLLSDDARLAALSEGALEVAQQFDSETMTRRLINLYEDLLVSYR$","Glycosyl transferase, group 1","Cytoplasm","putative hexosyltransferase","glycosyl transferase; group 1","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[225-390]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-134]T$ $\"[168-412]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF38	$\"[2-134]T$ $\"[168-412]T$	GLYCOSYLTRANSFERASE

","BeTs to 24 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","Residues 1-96 are 56% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS TRANSFERASE GROUP FAMILY 2.4.1.- LIPOPOLYSACCHARIDE PHOSPHATIDYLINOSITOL) protein domain (PD007341) which is seen in Q8DT10_STRMU.Residues 182-367 are 41% similar to a (LPS BIOSYNTHESIS) protein domain (PD271666) which is seen in Q9HS45_HALN1.","","No significant hits to the PDB database (E-value < E-10).","Residues 225 to 390 (E_value = 2.4e-28) place ANA_0506 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","hexosyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0507","533017","533892","876","8.10","2.61","30395","ATGTCGCTCGCCGTCGTCACCGACTCCGCCGCCTGCCTGACGGAGCCCCTGCTGCGTGAGCGCGCGATCGAGGTGGTGCCGCTGCACGCCATCCCCGCTGACAACGGCGAAGCCGCCACCACCTCCCGGCCCAGTGTCCAGGAACTGGTGGACGCCTACCGGCGCGCAGCCAGCAGGGCCGAAGAGGTCCTGGCCATCCACATCTCCTCGGCCCTGTCCGGCACCATGGACAACGCCCGCATCGCCGCGGCCCAGCTCGAGGCCGAGTACCGGGACCAGCCCAACGGCCCGGGCCCGAGCGCGGGGCGCCGACGCCCGCAGTGGCTGCGCGTCGTCGACTCCGGCACCAGCTCCGGCGCCCTGGGGCTCGCGGTGCTGGCAGCCTCCGGCGCCCACGACGCCCGTCGCGGTGCCGCCCTGGCTCAGGCCAGCACCGCTCGGTCCTGCCAGCTCTTTGTCGTCGACGACCTGGGGCGCCTGGCCCGCTCGGGAAGGATCGACCGCACCACGGCCCGCCTGGACGGTGTCCTGGGAATCCGCCCGGTCCTGGCCCTGACCCGCGACGGGATCCGGACGCTGGAGACCGTGCGCGGGGCGGCCCGATCCAGGCGCCACCTCATCGCGCAGGCCGTCCGCGTCGCCGGCGGGACCGCCCTGTCCGGCCCCAGGCACCCCGCAGACCCGGTGCGCCTGGTCATTCAAGGCGACGACGCCGACAAGCTGGCGCTGCTCGAGACCGATCTGCGCCAGGCCATGGAGGAGGCAGGAGCCAAGGTCTCCGAGGTCCTCACCCTCCCGGTCGACGAGGCGACGAGCACCCACGTGGGCCCCGGCGCCCTCGGTATCGCCGTCGCCCCGAACCTGAGGACCCACTGA","MSLAVVTDSAACLTEPLLRERAIEVVPLHAIPADNGEAATTSRPSVQELVDAYRRAASRAEEVLAIHISSALSGTMDNARIAAAQLEAEYRDQPNGPGPSAGRRRPQWLRVVDSGTSSGALGLAVLAASGAHDARRGAALAQASTARSCQLFVVDDLGRLARSGRIDRTTARLDGVLGIRPVLALTRDGIRTLETVRGAARSRRHLIAQAVRVAGGTALSGPRHPADPVRLVIQGDDADKLALLETDLRQAMEEAGAKVSEVLTLPVDEATSTHVGPGALGIAVAPNLRTH$","DegV family protein","Cytoplasm","DegV family protein","hypothetical protein","DegV family protein","","","","","

InterPro
IPR003797
Family

DegV
PF02645	$\"[51-287]T$	DegV

InterPro
IPR007449
Domain

ZipA, C-terminal FtsZ-binding region
SM00771	$\"[60-173]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.1180.10	$\"[150-291]T$	no description
G3DSA:3.40.50.10170	$\"[3-128]T$	no description

","BeTs to 6 clades of COG1307COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1307 is --------vdrlb--f---------wNumber of proteins in this genome belonging to this COG is 1","***** IPB003797 (DegV) with a combined E-value of 2.2e-17. IPB003797A 1-14 IPB003797B 68-79 IPB003797C 157-182 IPB003797D 268-281","Residues 5-91 are 55% similar to a (UPF0230 DEGV FAMILY HOMOLOG PLASMID KINASE MG450 UNCHARACTERIZED 3D-STRUCTURE BCR) protein domain (PD007382) which is seen in Q73XR9_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 51 to 287 (E_value = 1.4e-20) place ANA_0507 in the DegV family which is described as Uncharacterised protein, DegV family COG1307.","","family protein (DegV)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0508","533969","534823","855","7.52","0.90","28312","ATGCGTCCCATGGGTCCGGTCCCTACCGTCGAGGACATGGGAGCCAGACGGAGCGACGCGCACAGGTCCCTGGACGACCTTGTGCGTCTGGCCTGCTCAACCGACCCCGAGGAGCCGGTGCGCCGGCCACGTCGCCTCGCGATCGCGCCCCGGGCGGCGATCATCGCCGGCTCCGCCCTTCTCATCCTGGCTCTCGCCCTGGCCCTGAGAGCCGTGCTGGTCTCCACCGGCGCCGGCAGCCACGAGGCTCCGGCCGCAGTGGAAGGGGCATCGGCTCCAATGCGGCCCCCACCCACAGGGGCGGCCGCGAGTCCAGCCATGAAACCGGCCACGGTGCCGACCACGGGACCGGCAGCAGGACCAGGCGGCTTGAGCACGACATCGGGCAGCGTCGTCGTCCACGTCACCGGGGCGGTGAGCCGGCCGGGGGTGGTGACCCTGCCCCCGGGAAGCCGTGTCACCGACGCCATCAACGCCGTTGGAGGAGCCAGCGCCGAGGCCGACACCCAGCAGCTCAACCTCGCCCGGGTCCTGACCGACGGTGAGCAGATACGGGTCCCGCGCATCGGCGAGGTCCTGCCCGACCCCGCACCGCAACCCGGTGGGGCCACCACCCCCGGTGCACGGACCGCCCCGGGGAAGTCCGGCGACGGCGGCGCATCCGGGACGGTCAATATCAACACGGCCTCGGCCTCTGAGTTGGAGAAGCTGCCCGGAATCGGCCCGGCCCTGGCCCAACGGATCGTCGAGTACCGAGACTCCCACGGGCCCTTCGCCAGCGTGGACTCCCTCACCGACGTCCCCGGCATCGGCAAGGCCAAGCTCGAGGGCCTGCGAGAGCAGGCCACCGTATGA","MRPMGPVPTVEDMGARRSDAHRSLDDLVRLACSTDPEEPVRRPRRLAIAPRAAIIAGSALLILALALALRAVLVSTGAGSHEAPAAVEGASAPMRPPPTGAAASPAMKPATVPTTGPAAGPGGLSTTSGSVVVHVTGAVSRPGVVTLPPGSRVTDAINAVGGASAEADTQQLNLARVLTDGEQIRVPRIGEVLPDPAPQPGGATTPGARTAPGKSGDGGASGTVNINTASASELEKLPGIGPALAQRIVEYRDSHGPFASVDSLTDVPGIGKAKLEGLREQATV$","Competence protein ComEA","Membrane, Extracellular","late competence protein ComEA","K02237 competence protein ComEA","competence protein ComEA helix-hairpin-helix repeat protein","","Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Aravind L., Walker D.R., Koonin E.V. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res. 1999. 27(5):1223-1242. PMID: 9973609Provvedi R., Dubnau D. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol. Microbiol. 1999. 31(1):271-280. PMID: 9987128Doherty A.J., Serpell L.C., Ponting C.P. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 1996. 24(13):2488-2497. PMID: 8692686","","","

InterPro
IPR000445
Domain

Helix-hairpin-helix motif
PF00633	$\"[222-251]T$	HHH

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[232-251]T$ $\"[262-281]T$	HhH1

InterPro
IPR004509
Domain

Competence protein ComEA helix-hairpin-helix region
TIGR00426	$\"[216-284]T$	TIGR00426: competence protein ComEA helix-h

noIPR
unintegrated

unintegrated
PTHR21180	$\"[131-282]T$	FAMILY NOT NAMED
PTHR21180:SF6	$\"[131-282]T$	gb def: Putative DNA-binding protein
signalp	$\"[1-68]?$	signal-peptide
tmhmm	$\"[52-72]?$	transmembrane_regions

","BeTs to 12 clades of COG1555COG name: DNA uptake protein and related DNA-binding proteinsFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1555 is --------vdrlbcefghsnu-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 142-183 are 73% similar to a (COMPETENCE OPERON DNA-BINDING COME COMEA DNA UPTAKE LATE MEMBRANE RELATED) protein domain (PD189516) which is seen in Q73XT3_MYCPA.Residues 224-279 are similar to a (COMPETENCE BINDING ACCESSORY RNA S1 DOMAIN DNA DNA-BINDING TRANSCRIPTION COME) protein domain (PD011817) which is seen in Q8VQ77_BACLI.Residues 233-284 are similar to a (COMPETENCE COMEA COME COMEA-RELATED DNA DNA-BINDING OPERON 1-RELATED FAMILY TRANSMEMBRANE) protein domain (PD997215) which is seen in Q9JS02_NEIMA.","","No significant hits to the PDB database (E-value < E-10).","Residues 222 to 251 (E_value = 9.6e-06) place ANA_0508 in the HHH family which is described as Helix-hairpin-helix motif.","","competence protein ComEA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0509","534976","536712","1737","11.56","29.86","59389","CTGCGCCTACTCGCCCCGGCGCTGGCCTGCTGGGCCGGCGCCGGGTGGGCCGTTGGACGTGAGGCGGCAGACGCCTGGAGGTACGTCCTACTCCTGGCCTCCGGGTGCACCGCCCTGGCAGCGATACTCGTGGTTCTTGTCCTGCGCTTCCGGCCACCACGGCACCGGGCCGACCCGCGTCCCGGAGCCCCCGAGCACGACCCCGGGGCGATGGGTACCCTCAGCGCCAGCCTGCTCGTGTGCGCCCTGTGCGCCGCGACAGTCCTGGCCATCAGCGCCGCCCACCTGTGGGCCCGCCAGCGCGACCCGTTGACCGCGGCAGTGGCCACTGGGCAGCCGGTCACACTCATCGGCACCGTCTCCCAGCAGCCGCGAGTCTCAGCCACCAGCCGCTCCACCCTGGTCATCACAGCCCTCGACGTCGAGCAGGTGGACACGCGGGCCTCCACCCTGAGCGCCACCGTCCTGGGCGACACGCAGTGGCTGAGCCTGCCCATGGGGACCCGCGTCCGTGTGCGCACGCGCCTGCGCCCCACCGAAGCGGGACGTGCGGAGGCGGCCATCATCCCCAAGCGCGCCGGTCTGACCGTCCTTGGCCCGCCGAGCGGGACACTCGGGGCCGTCACCAGCATTCGCGCCGGTCTCGCCCAGGCCGTCGGGGCACCGGGCATGGGGGTCCCGGGCGCCGCAGGAACGGGGGAGGAGACGGGGCTGTGGCCACCGGGAGCCCGCAGCCTCGTATCCGGTGTCGCCCTAGGCGACGACCACTCCCTACCGGCCCCGCTGCGCGAGGACATGCGCACCGTCTCCATGACGCACCTGACCGCCGTCTCCGGGCAGCACGTCGCCATCATCCTGGGACTGGGCCTGGAAGCCCTCGGGGCGCTGCCCCGGCGGTGGCGGGCACTGCTCGGCGCAGTCATGCTCACCCTCCTCGTCATCCTGGTGCGTCCCTCAGGCTCCGTGCTGCGCGCCGCCACCATGGGGGCCGTCATGCTGCTGGGCGTCGTCGCCGGCAGACGCGCCGCCTCCGTGCCCGCCCTGTGCGCTGGAGCCATCGTCCTGCTGCTCATCGACCCCTGGCAGTCCCGCGACTACGGCTTCGCACTGTCCGTGGTGGCCACCGCCGGGATCGTCATCGGCTCCAAGCCGGTCGCCGCCCACCTCTCTCGCCGCCTGCCCAGGTGGCTGGCCGCCGCCGTGGCCCTGCCGCTGGTGGCCCAGGCCGCCTGCGGGCCGATCCTCATCCTCCTTCAGCCCTCGGTGGGGGCCTGGTCGGTGCCCGCCAACCTGCTCAGTGAACCGGCCGCCGTCATCGCCACCATCAGCGGGCTCCTGGCGGCGCTGATCGCACCGGCCTGGCCCGCGGCCGCCGCCGTCACCGCCTGGCCGGCGCTCGCGGCCTGCTCCTGGATGGTGTGGGTTGCTGGCTTCTTCGCCCACCTACCCGGTGCCACGCTGCCCTGGCCGGAGGGCCTGACGGGTGCCCTGGCACTGGGGGCCTGCGAGATCGGGGTCCTGCTCGCAGTGTCTCCCCGAGCGCGCCGCGCCCTGGCGGACGGCGCCGGGCGGTTGAGGCGGCCCGCTCGTGGCAGGCTTGCCCCATGGCAGCGACCCGCACCCCCCGCTCCCGGGGCCCGCGCAAGGCACCGGCTGGACTGCGCTGGGACCAGGCCCAGCTGGCGCCGATCGTCCTCATCCGCGCCGGCGAGGAGGTCCTCGCCGACCGAGCGGTGA","LRLLAPALACWAGAGWAVGREAADAWRYVLLLASGCTALAAILVVLVLRFRPPRHRADPRPGAPEHDPGAMGTLSASLLVCALCAATVLAISAAHLWARQRDPLTAAVATGQPVTLIGTVSQQPRVSATSRSTLVITALDVEQVDTRASTLSATVLGDTQWLSLPMGTRVRVRTRLRPTEAGRAEAAIIPKRAGLTVLGPPSGTLGAVTSIRAGLAQAVGAPGMGVPGAAGTGEETGLWPPGARSLVSGVALGDDHSLPAPLREDMRTVSMTHLTAVSGQHVAIILGLGLEALGALPRRWRALLGAVMLTLLVILVRPSGSVLRAATMGAVMLLGVVAGRRAASVPALCAGAIVLLLIDPWQSRDYGFALSVVATAGIVIGSKPVAAHLSRRLPRWLAAAVALPLVAQAACGPILILLQPSVGAWSVPANLLSEPAAVIATISGLLAALIAPAWPAAAAVTAWPALAACSWMVWVAGFFAHLPGATLPWPEGLTGALALGACEIGVLLAVSPRARRALADGAGRLRRPARGRLAPWQRPAPPAPGARARHRLDCAGTRPSWRRSSSSAPARRSSPTER$","Competence protein ComEC","Membrane, Cytoplasm","putative integral membrane protein","ComEC/Rec2-related protein","ComEC/Rec2-related protein","","","","","

InterPro
IPR004477
Domain

ComEC/Rec2-related protein
PF03772	$\"[250-515]T$	Competence
TIGR00360	$\"[271-444]T$	ComEC_N-term: ComEC/Rec2-related protein

noIPR
unintegrated

unintegrated
signalp	$\"[1-17]?$	signal-peptide
tmhmm	$\"[2-20]?$ $\"[26-48]?$ $\"[78-98]?$ $\"[302-322]?$ $\"[343-361]?$ $\"[367-387]?$ $\"[397-417]?$ $\"[436-456]?$ $\"[461-481]?$ $\"[487-509]?$	transmembrane_regions

","BeTs to 10 clades of COG0658COG name: Uncharacterized BCR, ComEC familyFunctional Class: SThe phylogenetic pattern of COG0658 is -----qvcebrhujgpolin-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 292-556 are 53% similar to a (MB2437C) protein domain (PD070517) which is seen in Q7TYM6_MYCBO.Residues 397-496 are 57% similar to a (COMPETENCE DNA COMEC/REC2 TRANSMEMBRANE MEMBRANE COME INTERNALIZATION-RELATED UPTAKE OPERON COMEC) protein domain (PD128132) which is seen in Q83NL0_TROW8.","","No significant hits to the PDB database (E-value < E-10).","Residues 302 to 567 (E_value = 1.5e-41) place ANA_0509 in the Competence family which is described as Competence protein.","","integral membrane protein","","1","","","Fri Aug 10 17:24:13 2007","","Fri Aug 10 17:24:13 2007","","","Fri Aug 10 17:24:13 2007","Fri Aug 10 17:24:13 2007","Fri Aug 10 17:24:13 2007","","","","","","Fri Aug 10 17:24:13 2007","","Fri Aug 10 17:24:13 2007","","Fri Aug 10 17:24:13 2007","Fri Aug 10 17:24:13 2007","","","","","yes","","" "ANA_0510","536580","537611","1032","9.51","8.86","36373","ATGGCAGCGACCCGCACCCCCCGCTCCCGGGGCCCGCGCAAGGCACCGGCTGGACTGCGCTGGGACCAGGCCCAGCTGGCGCCGATCGTCCTCATCCGCGCCGGCGAGGAGGTCCTCGCCGACCGAGCGGTGAGGAGCCTCCTGGCGCAGGCCAAGGCCAAGGACCCCACCACCGAGATCACGCGCCTGGAGGCCGCCACCTACGAGCCCCACCAGCTCGACACCCTCGTGTCGCCCTCCCTGTTCGGCGAGCCCCGACTCGTCTACGTCCCCGCCCTGGAGCAGATGACTGACGCCCTGCTGAGCGACCTCATCGCCTACGTGGGCGCCGCCGACCCCGAGGTCAGCGTCATCCTGCGCCACAACGGGGGCCAGCGGGGCAAGCGCCTGCTGGACGCCATCAAGGCCTCGCCCTACCCGACCATCCAGTGCGAGGCCGTCAAGAGCGCCAAGGACAAGTCCTCGCTGGTCGTGGCCGACGTGCGCCGCGCCGGACGACGCATCGCCCCCGAGGCCGTCGGTGCCCTCGTCGACGCCCTGGGCAGCGACCTGCGCGAGCTGTGCTCCGCCGTCGACCAGCTCCTCGCTGACACCCAGGGCACCATCAGCGTCGACCACGTGCGCACCTACTACGCCGGGCGCATCGAGGCCACCGGCTTCACCGTGGCCGACGCCGCCGCGGCCGGCAACACCCCGGCCGCCATCACGGCCCTGCGCCACGCCGTGGCCACCGGCACCGACCCGGTGGCCATCGTCGCGGCTCTGGCCATGAAGGTGCGCCAGCTCGCCCGGGTCGCGGCCGCCGGGGGCAGGCGCATGAGCCCCGCCGAGCTGGGCATGGCCCCCTGGCAGGTGGACCGGGCCCGCCGCGAGCTCCAGGGCTGGTCCGACGATGCCCTGGCCACCTCGATCCTGGCCGTGGCCCGGGCCGACGCCGAGGCCAAGGGGGCCAGCCGCGACCCCGTTTACGCCGTCGAGCGGGCGGTCCTGACCATCTGCAACGCCCGCCGCGCAGGCAGTCGCCGGCGCTGA","MAATRTPRSRGPRKAPAGLRWDQAQLAPIVLIRAGEEVLADRAVRSLLAQAKAKDPTTEITRLEAATYEPHQLDTLVSPSLFGEPRLVYVPALEQMTDALLSDLIAYVGAADPEVSVILRHNGGQRGKRLLDAIKASPYPTIQCEAVKSAKDKSSLVVADVRRAGRRIAPEAVGALVDALGSDLRELCSAVDQLLADTQGTISVDHVRTYYAGRIEATGFTVADAAAAGNTPAAITALRHAVATGTDPVAIVAALAMKVRQLARVAAAGGRRMSPAELGMAPWQVDRARRELQGWSDDALATSILAVARADAEAKGASRDPVYAVERAVLTICNARRAGSRRR$","DNA polymerase III, delta subunit","Cytoplasm, Extracellular","DNA polymerase III delta subunit","DNA polymerase III; delta subunit ","DNA polymerase III, delta subunit","","Song M.S., Pham P.T., Olson M., Carter J.R., Franden M.A., Schaaper R.M., Mchenry C.S. The delta and delta ' subunits of the DNA polymerase III holoenzyme are essential for initiation complex formation and processive elongation. J. Biol. Chem. 2001. 276(37):35165-35175. PMID: 11432857","","","

InterPro
IPR005790
Family

DNA polymerase III, delta subunit
TIGR01128	$\"[26-333]T$	holA: DNA polymerase III, delta subunit

InterPro
IPR010372
Family

DNA polymerase III, delta
PF06144	$\"[30-330]T$	DNA_pol3_delta

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 28-124 are 64% similar to a (DELTA DNA POLYMERASE SUBUNIT DNA-BINDING III LIPOPROTEIN III MLCL536.07C MB2436C) protein domain (PD696875) which is seen in Q6AEB2_BBBBB.Residues 126-216 are 60% similar to a (DNA-BINDING DELTA DNA POLYMERASE SUBUNIT LIPOPROTEIN III MLCL536.07C III MB2436C) protein domain (PD836067) which is seen in Q9RDM2_STRCO.Residues 157-208 are 73% similar to a (DNA POLYMERASE DELTA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED SUBUNIT) protein domain (PD465138) which is seen in Q8FN98_COREF.Residues 238-329 are 69% similar to a (DNA POLYMERASE DELTA SUBUNIT III III DNA-BINDING TRANSFERASE NUCLEOTIDYLTRANSFERASE YQEN) protein domain (PD710018) which is seen in Q6AEB2_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 30 to 330 (E_value = 9.9e-06) place ANA_0510 in the DNA_pol3_delta family which is described as DNA polymerase III, delta subunit.","","polymerase III delta subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0511","538093","537620","474","5.47","-3.46","15634","ATGAGCGGATCCGGGGCACCTGAGCAGAGCGCACCTCACGCACGGGGCATGAGGGTGACAGTCGTGGCCGCCCAGTGGCACGAACGCATCATGGGGGGCCTGGTCGCCGGGGCGCTGCGCGCCGTCGAGGAGGCCGGAGCCCAGGCGAGCGTCGTCAGGGCGGTGGGCTCCTTCGAGCTTCCGGTCCTCGCCACGGCCGCCGCGCGAGGCGGTGCCGAGGCGGTCGTCGCGCTGGGCGTCGTCATCCGCGGCGGCACCCCGCACTTCGACTACGTGTGCCGGGCCGCGACCGACGGGCTGAGCCGGGTGGCGCTGGACACCGGGGTGCCGGTGGGCTTCGGCGTGCTCACCTGCGACGACGAGGCCCAGGCGCTGGCCCGCTGCGGCGGGCCGGGCGCGGAGGAGGACAAGGGCTACGAGGCGGCGTGCGCGGCGATGTCCACGGCGCTCACGCTGGCCGCCATGCGGGGCTGA","MSGSGAPEQSAPHARGMRVTVVAAQWHERIMGGLVAGALRAVEEAGAQASVVRAVGSFELPVLATAAARGGAEAVVALGVVIRGGTPHFDYVCRAATDGLSRVALDTGVPVGFGVLTCDDEAQALARCGGPGAEEDKGYEAACAAMSTALTLAAMRG$","6,7-dimethyl-8-ribityllumazine synthase","Cytoplasm","6,7-dimethyl-8-ribityllumazine synthase","K00794 riboflavin synthase beta chain","6,7-dimethyl-8-ribityllumazine synthase","","","","","

InterPro
IPR002180
Family

6,7-dimethyl-8-ribityllumazine synthase
PD003664	$\"[18-140]T$	Q6A6Y6_PROAC_Q6A6Y6;
G3DSA:3.40.50.960	$\"[2-156]T$	no description
PF00885	$\"[14-155]T$	DMRL_synthase
TIGR00114	$\"[17-152]T$	lumazine-synth: 6,7-dimethyl-8-ribityllumaz

noIPR
unintegrated

unintegrated
PTHR21058	$\"[6-156]T$	6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE (DMRL SYNTHASE) (LUMAZINE SYNTHASE)

","BeTs to 18 clades of COG0054COG name: Riboflavin synthase beta-chainFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0054 is aom--zyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB002180 (6,7-dimethyl-8-ribityllumazine synthase) with a combined E-value of 5.4e-33. IPB002180A 18-46 IPB002180B 54-85 IPB002180C 92-136","Residues 18-140 are 68% similar to a (SYNTHASE RIBOFLAVIN TRANSFERASE BIOSYNTHESIS 67-DIMETHYL-8-RIBITYLLUMAZINE LUMAZINE CHAIN BETA DMRL 3D-STRUCTURE) protein domain (PD003664) which is seen in Q6A6Y6_PROAC.","","-55% similar to PDB:1W19 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-TRIHYDRO-9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) PROPANE 1-PHOSPHATE (E_value = 2.2E_22);-55% similar to PDB:1W29 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-TRIHYDRO-9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) BUTANE 1-PHOSPHATE (E_value = 2.2E_22);-55% similar to PDB:2C92 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-TRIHYDRO-9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) PENTANE 1 PHOSPHATE (E_value = 2.2E_22);-55% similar to PDB:2C94 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-TRIHYDRO-9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) 1,1 DIFLUOROPENTANE-1-PHOSPHATE (E_value = 2.2E_22);-55% similar to PDB:2C97 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 4-(6-CHLORO-2,4-DIOXO-1,2,3,4-TETRAHYDROPYRIMIDIN-5-YL) BUTYL PHOSPHATE (E_value = 2.2E_22);","Residues 14 to 155 (E_value = 2e-45) place ANA_0511 in the DMRL_synthase family which is described as 6,7-dimethyl-8-ribityllumazine synthase.","","synthase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0512","539421","538090","1332","5.34","-17.48","47728","ATGCTGAGCACCACGAGCGCATCCCCGGGCACGCCCATGGACCGCGTCGAGGACGCTCTCGCCGCCCTGCGCGAGGGCCGGACGGTCATCGTCGTCGACGATGAGAGCCGAGAGAACGAGGGGGACCTCATCCTGCCCGCGCAGAGCGCCACGACCGAGCAGCTGGCCTTCGCGATCCGGCACTCGACCGGCATCATCTGCGCCCCCATGGCGGGCCAGGAGCTCAACCGCCTGGGCATCCCCATGATGACCGAGCACAACACCGATCCCAAGAGGACGGCCTTCACCCTGAGCGCCGACGCCCGCACCGGCATCACCACGGGTGTGAGCGCCGCCGACCGGGCTCGCACCGTCCGCGTCCTGGCGGATCCGGGCTCAGCTCCCGACGACCTCGTCCGCCCCGGCCACGTCTTCCCCCTGCGGGCGCGCGAGGGCGGGATCCTCACGCGCCGCGGTCACACGGAGGCCGCCGTCGACCTCATGCGCCTGTCGGGCAACCGGCCCGTGGGGGTCCTGGTGGAGGTCATCAACGACGACGGCACGATGGCGCGGCGGCACCAGCTGCGTGAGCTCGCCGACGCCCACGCCATGCCCATGATCTCGATCAGTGACCTGGAGCGCTACCGGTGGCTGCACGAGGAACTCGTCGAGGAGGTCGTCTCGGCGCACCTGCCAACCGCGCACGGGGAGTTCACCGCCCACGCCTTGCGCAGCAGGGTCGACGGCACCGAGTACCTCGCACTGGTGTGCGGCAGCATCGCTGACGGTGAGGACGTCCTGGCCCGAGTCCACTCCGCCTGCCTGACCGGCGACGTCCTGTCCTCCCTCCGCTGTGACTGCGGGCCGCAGCTGCGCGCCGCCATGGAGGCGATCAGTGCCCGCGGCCGCGGGGTCCTCGTCTATGCCTCCGACCATGAGGGGCGCGGCATCGGGCTCATCGACAAGCTCCGCGCCTACGCGCTGCAGGAGGAGGGACTGGACACCCTCGACGCCAACGTCGCGCTGGGGCTGCCGGCCGACGCCCGCAGCTACGCCACCGCCGCCCAGGTGCTGCGCCACCTGGGCGTGCGCTCAGTCGAGCTCATGACGAACAACCCGGACAAGGTGGCCGGCCTGGAGCGCTACGGCGTCAGTGTCCGCTCCATGACGCCGACACCGACCTTCGCCAACGGGGAGAACCTCGACTACCTGCGCACCAAGCGCGACCGCATGGGCCATCTGCTCACCGGGCTCGACCCCACCGGGGCCGACGCGGACTCACCGCCCGGCGAGACGAGGGCCGACGACGACACCTGGCACACGAGCAACGAGAACGAAGGAGAGGAACGATGA","MLSTTSASPGTPMDRVEDALAALREGRTVIVVDDESRENEGDLILPAQSATTEQLAFAIRHSTGIICAPMAGQELNRLGIPMMTEHNTDPKRTAFTLSADARTGITTGVSAADRARTVRVLADPGSAPDDLVRPGHVFPLRAREGGILTRRGHTEAAVDLMRLSGNRPVGVLVEVINDDGTMARRHQLRELADAHAMPMISISDLERYRWLHEELVEEVVSAHLPTAHGEFTAHALRSRVDGTEYLALVCGSIADGEDVLARVHSACLTGDVLSSLRCDCGPQLRAAMEAISARGRGVLVYASDHEGRGIGLIDKLRAYALQEEGLDTLDANVALGLPADARSYATAAQVLRHLGVRSVELMTNNPDKVAGLERYGVSVRSMTPTPTFANGENLDYLRTKRDRMGHLLTGLDPTGADADSPPGETRADDDTWHTSNENEGEER$","GTP cyclohydrolase II","Cytoplasm","3,4-dihydroxy-2-butanone 4-phosphate synthase","GTP cyclohydrolase II ","GTP cyclohydrolase II","","Richter G., Krieger C., Volk R., Kis K., Ritz H., Gotze E., Bacher A. Biosynthesis of riboflavin: 3,4-dihydroxy-2-butanone-4-phosphate synthase. Meth. Enzymol. 1997. 280:374-382. PMID: 9211332","","","

InterPro
IPR000422
Domain

3,4-Dihydroxy-2-butanone 4-phosphate synthase
PD003034	$\"[10-213]T$	RIBB_ECOL6_Q8FDH9;
PF00926	$\"[16-212]T$	DHBP_synthase
TIGR00506	$\"[12-209]T$	ribB: 3,4-dihydroxy-2-butanone 4-phosphate

InterPro
IPR000926
Domain

GTP cyclohydrolase II
PF00925	$\"[216-385]T$	GTP_cyclohydro2
TIGR00505	$\"[217-408]T$	ribA: GTP cyclohydrolase II

noIPR
unintegrated

unintegrated
G3DSA:3.90.870.10	$\"[2-222]T$	no description
PTHR21327	$\"[43-375]T$	GTP CYCLOHYDROLASE II-RELATED
PTHR21327:SF1	$\"[43-375]T$	GTP CYCLOHYDROLASE II

","BeTs to 13 clades of COG0108COG name: 3,4-dihydroxy-2-butanone 4-phosphate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0108 is aom--zyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB000422 (3,4-Dihydroxy-2-butanone 4-phosphate synthase) with a combined E-value of 1.6e-73. IPB000422A 19-67 IPB000422B 93-111 IPB000422C 130-180***** IPB000926 (GTP cyclohydrolase II) with a combined E-value of 4e-59. IPB000926A 216-231 IPB000926B 241-253 IPB000926C 262-280 IPB000926D 299-351 IPB000926E 396-406","Residues 10-213 are similar to a (SYNTHASE 4-PHOSPHATE RIBOFLAVIN 34-DIHYDROXY-2-BUTANONE BIOSYNTHESIS HYDROLASE CYCLOHYDROLASE II DHBP GTP) protein domain (PD003034) which is seen in RIBB_ECOL6.Residues 224-351 are 77% similar to a (HYDROLASE CYCLOHYDROLASE II GTP RIBOFLAVIN BIOSYNTHESIS SYNTHASE 4-PHOSPHATE 34-DIHYDROXY-2-BUTANONE RIBA) protein domain (PD003336) which is seen in Q9EWJ8_STRCO.Residues 354-408 are 74% similar to a (HYDROLASE CYCLOHYDROLASE II GTP RIBOFLAVIN BIOSYNTHESIS SYNTHASE 4-PHOSPHATE 34-DIHYDROXY-2-BUTANONE RIBA) protein domain (PD861668) which is seen in Q8FT57_COREF.","","-70% similar to PDB:1G57 CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE (E_value = 3.2E_63);-70% similar to PDB:1G58 CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE GOLD DERIVATIVE (E_value = 3.2E_63);-70% similar to PDB:1IEZ Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis (E_value = 5.5E_63);-68% similar to PDB:1K49 Crystal Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase (cation free form) (E_value = 6.6E_48);-68% similar to PDB:1K4I Crystal Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase in complex with two Magnesium ions (E_value = 6.6E_48);","Residues 16 to 212 (E_value = 3.7e-103) place ANA_0512 in the DHBP_synthase family which is described as 3,4-dihydroxy-2-butanone 4-phosphate synthase.Residues 216 to 385 (E_value = 3e-89) place ANA_0512 in the GTP_cyclohydro2 family which is described as GTP cyclohydrolase II.","","4-phosphate synthase (DHBP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0513","540074","539415","660","5.06","-8.91","23197","ATGTTCACCGGAATCGTCGAGGAGCTCGGACGCGTCGTCCGGCTCGAGACCGTCGAGGACAGCGCCCGGCTGACGGTCGAGGCGCCCACCGTCACCCAGGACGTGAATCTGGGCGACTCCGTCAGCGTCAACGGGTGCTGCCTGACGGTCACCGCCGTGCAAGGAAGCACCTTCACCGCCGACCTCATGGCCGAGACTCTCACGCGCACCACCCTGGGCTCCCAGGCGCCAGGAGACCCGGTCAACCTCGAGCGCGCCCTGCGCGCCAGCGACCGGCTCGGCGGACACATCGTCCAGGGGCACGTCGATGCCACCGCCGAGGTCCTCGACCACCACCGCGGTGAGCACTGGGACCTCCTACGCATCGGCCTGCCGCAGGAGATCACCCGTTACGTGGCCGTCAAGGGATCGGTCGCCCTCGACGGGGTGTCGCTCACGGTCGTCGACGTCGTCGACGCCTCCAACACCCTCGACGTCGCCCCTGTGCCGAGTGCGGGGGCGTCGCTCAGCGTCGGGCTCATTCCCGAGACGCTGCGACGCACAACCCTGGGCACGAGGCGACCCGGAGAACGGGTCAACCTCGAGGTCGACGTCCTGGCCAAGTACGCCGAGCGTCTTCTGGGCGCCCGCCCGAGCCAGGAGGGGCAGCAGGCATGCTGA","MFTGIVEELGRVVRLETVEDSARLTVEAPTVTQDVNLGDSVSVNGCCLTVTAVQGSTFTADLMAETLTRTTLGSQAPGDPVNLERALRASDRLGGHIVQGHVDATAEVLDHHRGEHWDLLRIGLPQEITRYVAVKGSVALDGVSLTVVDVVDASNTLDVAPVPSAGASLSVGLIPETLRRTTLGTRRPGERVNLEVDVLAKYAERLLGARPSQEGQQAC$","Riboflavin synthase, alpha subunit","Cytoplasm, Periplasm","riboflavin synthase, alpha subunit","putative riboflavin synthase ","riboflavin synthase, alpha subunit","","O. Kane D.J., Woodward B., Lee J., Prasher D.C. Borrowed proteins in bacterial bioluminescence. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(4):1100-1104. PMID: 1996310O. Kane D.J., Prasher D.C. Evolutionary origins of bacterial bioluminescence. Mol. Microbiol. 1992. 6(4):443-449. PMID: 1560772","","","

InterPro
IPR001783
Family

Lumazine-binding protein
PD004110	$\"[4-85]T$ $\"[100-204]T$	Q9EWJ6_STRCO_Q9EWJ6;
PIRSF000498	$\"[1-218]T$	Riboflavin synthase, alpha subunit
PTHR21098	$\"[1-207]T$	RIBOFLAVIN SYNTHASE ALPHA CHAIN
PF00677	$\"[3-86]T$ $\"[99-197]T$	Lum_binding
TIGR00187	$\"[1-218]T$	ribE: riboflavin synthase, alpha subunit
PS51177	$\"[1-96]T$ $\"[97-207]T$	LUMAZINE_BIND

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.20	$\"[1-96]T$ $\"[101-208]T$	no description

","BeTs to 17 clades of COG0307COG name: Riboflavin synthase alpha chainFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0307 is -o----yqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB001783 (Lumazine-binding protein) with a combined E-value of 1.7e-73. IPB001783A 1-10 IPB001783B 38-50 IPB001783C 65-108 IPB001783D 131-147 IPB001783E 169-197 IPB001783B 135-147 IPB001783D 34-50","Residues 1-48 are 72% similar to a (ALPHA RIBOFLAVIN TRANSFERASE SUBUNIT SYNTHASE SYNTHASE CHAIN) protein domain (PD875386) which is seen in Q818X7_BACCR.Residues 100-204 are 60% similar to a (RIBOFLAVIN ALPHA SYNTHASE CHAIN TRANSFERASE SYNTHASE SUBUNIT REPEAT BIOSYNTHESIS CEREVISIAE) protein domain (PD004110) which is seen in Q9EWJ6_STRCO.Residues 38-98 are similar to a (RIBOFLAVIN ALPHA SYNTHASE CHAIN TRANSFERASE SUBUNIT SYNTHASE REPEAT BIOSYNTHESIS PROBABLE) protein domain (PD858488) which is seen in Q74CI4_GEOSL.Residues 43-158 are 49% similar to a (LUMAZINE REPEAT FLAVOPROTEIN LUMP LUMINESCENCE SEQUENCING DIRECT) protein domain (PD705619) which is seen in LUXP_PHOLE.Residues 100-204 are 60% similar to a (RIBOFLAVIN ALPHA SYNTHASE CHAIN TRANSFERASE SYNTHASE SUBUNIT REPEAT BIOSYNTHESIS CEREVISIAE) protein domain (PD004110) which is seen in Q9EWJ6_STRCO.","","-55% similar to PDB:1KZL Riboflavin Synthase from S.pombe bound to Carboxyethyllumazine (E_value = 1.9E_32);-56% similar to PDB:1I8D CRYSTAL STRUCTURE OF RIBOFLAVIN SYNTHASE (E_value = 7.4E_24);-60% similar to PDB:1HZE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI (E_value = 2.2E_15);-60% similar to PDB:1I18 SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI (E_value = 2.2E_15);-60% similar to PDB:1PKV The N-terminal domain of riboflavin synthase in complex with riboflavin (E_value = 2.2E_15);","Residues 3 to 86 (E_value = 6.5e-27) place ANA_0513 in the Lum_binding family which is described as Lumazine binding domain.Residues 99 to 197 (E_value = 1.3e-20) place ANA_0513 in the Lum_binding family which is described as Lumazine binding domain.","","synthase, alpha subunit (ribE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0514","541162","540074","1089","6.52","-3.82","37567","ATGACCTCGTTCACCACCGTGCAGACGGCCGCGATGCAGCGCGCCCTACGGGCCGCGGCCTCCCCCGACGCCCCGCCCGGCCCCAACCCCCGGGTCGGTTGCGTCATCCTCTCCCCCGACGGCGACGTCCTCGCCGAGGGCCATCACCGTGGCGCCGGCACCGCCCACGCCGAGGTCGACGCACTGGCGAACCTCGCCGCGGCGGGCGCCTCCGCCCGAGGAACGACCGCCGTCGTCACCCTCGAGCCGTGCAACCACCAGGGCCGCACCGGCCCGTGCGTCAAGGCGCTCCTCGACGCCGGCGTGGCCGAGGTCATCTACGCCCAGGACGACCCGACCGAGCAGGCCGGAGGCGGCGCGGCGGCGCTGGAGGCCGCCGGCGTGCGGGTACGGCGTGGGCTGTGCGCCCAGGAGGCCGCGCGCCTCAACCGCCCGTGGCTCCTGGCCGTCACCCGCGGGCGCCCCATGGTGACGTGGAAGCTCGCCGCCACCCTCGACGGCCGTATCGCCGCCGCTGACGGCACCAGCCAGTGGATCACCCCGGTGGCGGCCCGCCACGACGCCCACCGCCTACGCCGCCAGTGCGACGCCATCATGGTGGGCACCGGCACCGCCCTCGCCGACGACCCCGCCCTCACCGTCCGCGACGAGGCAGGTCAGCCCGCACCGGCCCACCTCCAGCCGCTGCGCGTCGTCGTCGGCTCCAGGAGCCTGCCTCCCACCTCCAGGGTGCTCGCCGACGACCACTACCTCCTCCTGCCCGACCACGACCCGCGCGCCGTCCTGGCCGTGCTCGCTAAGCGCAAGATCCGCCATGTCCTGCTCGAAGGAGGCCCGACCCTCGCGACCGCATTCCTGCGCGCCGGCCTCGTCGATCAGGTCGTCGCCTACACGGCCCCCGTGCTTCTGGGCGCGGGAGCGGCCGCTCTCGCCGACTTCGGGGCGGAGACGATCAGCGATGCCCTGAGGCTGATTCACCCCCGCGTCGAGGTCCTCGGCGCGGGTGACGAGCTCGCCGTCCGCTTCTGCGGTGACCTGGAGGCCGACGACGTTCCCACTGCCCACTTCCACACCGAGGAGAGTCACTGA","MTSFTTVQTAAMQRALRAAASPDAPPGPNPRVGCVILSPDGDVLAEGHHRGAGTAHAEVDALANLAAAGASARGTTAVVTLEPCNHQGRTGPCVKALLDAGVAEVIYAQDDPTEQAGGGAAALEAAGVRVRRGLCAQEAARLNRPWLLAVTRGRPMVTWKLAATLDGRIAAADGTSQWITPVAARHDAHRLRRQCDAIMVGTGTALADDPALTVRDEAGQPAPAHLQPLRVVVGSRSLPPTSRVLADDHYLLLPDHDPRAVLAVLAKRKIRHVLLEGGPTLATAFLRAGLVDQVVAYTAPVLLGAGAAALADFGAETISDALRLIHPRVEVLGAGDELAVRFCGDLEADDVPTAHFHTEESH$","Riboflavin biosynthesis protein RibD","Cytoplasm, Extracellular","riboflavin biosynthesis protein RibD","riboflavin biosynthesis protein RibD ","riboflavin biosynthesis protein RibD","","Yang C., Carlow D., Wolfenden R., Short S.A. Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene. Biochemistry 1992. 31(17):4168-4174. PMID: 1567863Moore J.T., Silversmith R.E., Maley G.F., Maley F. T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit. J. Biol. Chem. 1993. 268(4):2288-2291. PMID: 8428902Reizer J., Buskirk S., Bairoch A., Reizer A., Saier Jr M.H. A novel zinc-binding motif found in two ubiquitous deaminase families. Protein Sci. 1994. 3(5):853-856. PMID: 8061614Bhattacharya S., Navaratnam N., Morrison J.R., Scott J., Taylor W.R. Cytosine nucleoside/nucleotide deaminases and apolipoprotein B mRNA editing. Trends Biochem. Sci. 1994. 19(3):105-106. PMID: 8203015","","","

InterPro
IPR002125
Domain

CMP/dCMP deaminase, zinc-binding
PF00383	$\"[5-109]T$	dCMP_cyt_deam_1
PS00903	$\"[56-97]?$	CYT_DCMP_DEAMINASES

InterPro
IPR002734
Domain

Bacterial bifunctional deaminase-reductase, C-terminal
PF01872	$\"[155-338]T$	RibD_C

InterPro
IPR004794
Family

Riboflavin biosynthesis protein RibD
PTHR11079:SF10	$\"[12-328]T$	RIBOFLAVIN-SPECIFIC DEAMINASE
TIGR00326	$\"[12-340]T$	eubact_ribD: riboflavin biosynthesis protei

noIPR
unintegrated

unintegrated
G3DSA:3.40.140.10	$\"[6-131]T$	no description
G3DSA:3.40.430.10	$\"[157-311]T$	no description
PTHR11079	$\"[12-328]T$	CYTOSINE DEAMINASE

","BeTs to 19 clades of COG1985COG name: Pyrimidine reductase, riboflavin biosynthesisFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1985 is aom--zyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB002734 (Bacterial bifunctional deaminase-reductase, C-terminal) with a combined E-value of 3.1e-87. IPB002734A 28-38 IPB002734B 59-93 IPB002734C 117-127 IPB002734D 155-170 IPB002734E 174-215 IPB002734F 227-236 IPB002734G 273-305***** IPB011549 (Riboflavin-specific deaminase, C-terminal) with a combined E-value of 2.6e-23. IPB011549 176-215","Residues 33-146 are 61% similar to a (DEAMINASE RIBOFLAVIN BIOSYNTHESIS HYDROLASE CYTOSINE REDUCTASE RIBD RIBOFLAVIN-SPECIFIC PYRIMIDINE DIAMINOHYDROXYPHOSPHORIBOSYLAMINOPYRIMIDINE) protein domain (PD404873) which is seen in Q6A6Y3_PROAC.Residues 78-112 are 80% similar to a (BIOSYNTHESIS RIBOFLAVIN DEAMINASE HYDROLASE RIBOFLAVIN-SPECIFIC RIBD OXIDOREDUCTASE RIBG / D) protein domain (PD472429) which is seen in Q83HC2_TROW8.Residues 78-112 are 82% similar to a (DEAMINASE RIBOFLAVIN REDUCTASE BIOSYNTHESIS RIBD RIBOFLAVIN-SPECIFIC DIAMINOHYDROXYPHOSPHORIBOSYLAMINOPYRIMIDINE HYDROLASE PHOSPHORIBOSYLAMINOURACIL OXIDOREDUCTASE) protein domain (PDA1E9D8) which is seen in Q8NQ50_CORGL.Residues 137-295 are 45% similar to a (BIOSYNTHESIS RIBOFLAVIN RIBD) protein domain (PD439466) which is seen in Q9A9S7_CAUCR.Residues 154-198 are 77% similar to a (RIBOFLAVIN DEAMINASE BIOSYNTHESIS REDUCTASE RIBD RIBOFLAVIN-SPECIFIC DIAMINOHYDROXYPHOSPHORIBOSYLAMINOPYRIMIDINE HYDROLASE OXIDOREDUCTASE HTP) protein domain (PD859291) which is seen in Q9KYI4_STRCO.Residues 200-244 are 71% similar to a (RIBOFLAVIN BIOSYNTHESIS DEAMINASE REDUCTASE RIBD RIBOFLAVIN-SPECIFIC DIAMINOHYDROXYPHOSPHORIBOSYLAMINOPYRIMIDINE HYDROLASE OXIDOREDUCTASE HTP) protein domain (PD004302) which is seen in RIBD_MYCTU.Residues 261-301 are 80% similar to a (RIBOFLAVIN DEAMINASE REDUCTASE BIOSYNTHESIS RIBD RIBOFLAVIN-SPECIFIC HYDROLASE DIAMINOHYDROXYPHOSPHORIBOSYLAMINOPYRIMIDINE OXIDOREDUCTASE HTP) protein domain (PD005260) which is seen in Q9KYI4_STRCO.","","-48% similar to PDB:2G6V The crystal structure of ribD from Escherichia coli (E_value = 4.3E_39);-48% similar to PDB:2O7P The crystal structure of RibD from Escherichia coli in complex with the oxidised NADP+ cofactor in the active site of the reductase domain (E_value = 4.3E_39);-48% similar to PDB:2OBC The crystal structure of RibD from Escherichia coli in complex with a substrate analogue, ribose 5-phosphate (beta form), bound to the active site of the reductase domain (E_value = 4.3E_39);-44% similar to PDB:2B3Z Crystal structure of a bifunctional deaminase and reductase involved in riboflavin biosynthesis (E_value = 2.9E_27);-44% similar to PDB:2D5N Crystal structure of a bifunctional deaminase and reductase involved in riboflavin biosynthesis (E_value = 2.9E_27);","Residues 5 to 109 (E_value = 1.4e-29) place ANA_0514 in the dCMP_cyt_deam_1 family which is described as Cytidine and deoxycytidylate deaminase zinc-binding region.Residues 155 to 338 (E_value = 4.5e-49) place ANA_0514 in the RibD_C family which is described as RibD C-terminal domain.","","biosynthesis protein RibD (ribD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0515","542997","541510","1488","6.19","-6.27","54610","TTGCGCATCGGATTCGACCGCGACAAGTACCTGCGGATGCAGTCCAGCCACATCGCGGAGCGCCGCGCCCAGTTCGGCGGCAAGCTCTATCTGGAGTTCGGCGGCAAGCTCATTGACGACATGCACGCCTCGCGCGTGCTGCCGGGCTTCACCCCGGACAACAAGATCGTCATGCTCGCCGAGCTGGCCGACGAGGTCGAGATCGTCATGGCGGTCAACGCCAAGCACCTCTCCCGCAACAAGGTCCGCGCGGACCTGGGCATCCCCTACGAGGACGACCTGCTGCGCCACATCGACGCCTTCCGCAGCTACGGGCTCTACGTGGGCAGCGTCGTCGTGACCCAGTGGACTGATGACAACCGTCAGGCCCAGGACTTCAAGCGCAAGCTCGAGGCGCTGGGCATCACGGTCTACCGTCACTTCCCCATCCCCGGCTACCCCGGTGACGTCGCCCGCATCGTCTCGGCGGAGGGCTACGGGCGCAACGAGTACATTGAGACCAGGCGGGACCTGGTGGTCGTCACCGCCCCCGGCCCGGGCAGCGGCAAGATGGCCACCTGCCTGTCCCAGATCTACCACGACCACCAGCGGGGCATCTCCTCGGGCTACGCGAAGTTCGAGACCTTCCCGATCTGGAACCTGCCTCTGGACCACCCGGTCAACATCGCCTACGAGGCCGCCACCGCCGACCTCGACGACGTCAACATGATCGACCCCTTCCACCTGGCTGCCCACGGCGTCCAGACCGTCAACTACAACCGCGACGTCGAGGTCTTCCCGGTCCTGAGCCGCCTGTTCGAGGAGATCCTGGGCTCCTCGCCCTACGCCTCCCCCACGGACATGGGCGTCAACATGGCCGGCAACTGCATCAGCGACGACGAGGTCTGCCGGCAGGCCGCCTGTCAGGAGATCATCCGCCGCTACTACCGGGCCCTGGTGACCGAGAAGCGCGAGGTCATCGCCCCCGTCCAGTCCCAGCGGATCGCGCTGCTCATGGCCAAGGTGGGGGTGAACAAGGAGGACCGCCCCGTCGTGCCGCCCGCGCTGGAGGTGGCTGAGGCCACCGGCGAGCCGGCCTCGGCGATCGAGCTGCCCGACGGGCGCATCGTGACGGGCAAGACCTCCGCCCTGCTGGGGTGCTCCTCGGCGATGCTGCTCAACGCTCTCAAGCTCCTGGCCGGGATCGATGATGACGTCAACCTGCTGGCCCCGGCCTCCATCGAACCCATCCAGAAGCTCAAGACCCAGAGGCTGGGAAGCCGCAACCCGCGCCTGCACACCGACGAGGTGCTCATCGCCCTGGCCGTGTCCGCCAACGGGGACGACAACGCCCGCAAGGCCCTCGACCAGCTCGAGACGCTGCGGGGCTGCGAGGTTCACACCTCCACGATCCTGGGACCGGTGGACGAGGGCATCTTCCGCGCCCTGGGAGTCCAGGTCACCAACGAGCCCGTCTACGCCACCAAGTCCCTGTACCGCAAGAAGTGA","LRIGFDRDKYLRMQSSHIAERRAQFGGKLYLEFGGKLIDDMHASRVLPGFTPDNKIVMLAELADEVEIVMAVNAKHLSRNKVRADLGIPYEDDLLRHIDAFRSYGLYVGSVVVTQWTDDNRQAQDFKRKLEALGITVYRHFPIPGYPGDVARIVSAEGYGRNEYIETRRDLVVVTAPGPGSGKMATCLSQIYHDHQRGISSGYAKFETFPIWNLPLDHPVNIAYEAATADLDDVNMIDPFHLAAHGVQTVNYNRDVEVFPVLSRLFEEILGSSPYASPTDMGVNMAGNCISDDEVCRQAACQEIIRRYYRALVTEKREVIAPVQSQRIALLMAKVGVNKEDRPVVPPALEVAEATGEPASAIELPDGRIVTGKTSALLGCSSAMLLNALKLLAGIDDDVNLLAPASIEPIQKLKTQRLGSRNPRLHTDEVLIALAVSANGDDNARKALDQLETLRGCEVHTSTILGPVDEGIFRALGVQVTNEPVYATKSLYRKK$","Uncharacterized protein conserved in bacteria","Cytoplasm","ATP-dependent Zn protease","hypothetical protein","Uncharacterized protein-like","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR001547
Family

Glycoside hydrolase, family 5
PS00659	$\"[476-485]?$	GLYCOSYL_HYDROL_F5

InterPro
IPR014999
Family

Domain of unknown function DUF1846
PF08903	$\"[2-493]T$	DUF1846

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues are similar to a () protein domain () which is seen in .","","-44% similar to PDB:2JG1 STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE WITH COFACTOR AND SUBSTRATE (E_value = );-44% similar to PDB:2JGV STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE IN COMPLEX WITH ADP (E_value = );","Residues 2 to 493 (E_value = 0) place ANA_0515 in the DUF1846 family which is described as Domain of unknown function (DUF1846).","","Zn protease","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0516","543524","543105","420","10.90","19.61","15370","ATGGGGATCCTGAATGATACAGTCGCCTACTGGACCTCTGGCCTGGCCGGCTGCGGGGTCCGGCGACCGGGTCAGCCAGGTGCCCCACCACCTCATGTCAACCCGTGGCGCGAACCCTCTCTCCGGCCATTGACCAATCAGACGCGAGAAAGTTTCACCGTGGCGAACATCAAGTCCCAGATCAAGCGCATCAAGACCAACGAGAAGGCCCGCCTGCGCAACAAGTCCGTCAAGTCCGAGCTCAAGACCTACGTGCGCCGCGTGCGCGAGGCCGTCGAGGCCGGCGACAAGGACGCCGCGCTCGAGCACCTCAAGGCCGCCTCCCGCAAGCTGGACAAGGCCGTCTCCAAGGGCGTCATCCACAAGAACCAGGCTGCCAACCGCAAGTCCAAGCTCGCCAAGCGCGTCGCCTCCCTCTGA","MGILNDTVAYWTSGLAGCGVRRPGQPGAPPPHVNPWREPSLRPLTNQTRESFTVANIKSQIKRIKTNEKARLRNKSVKSELKTYVRRVREAVEAGDKDAALEHLKAASRKLDKAVSKGVIHKNQAANRKSKLAKRVASL$","Ribosomal protein S20","Periplasm, Cytoplasm","30S ribosomal protein","ribosomal protein S20","ribosomal protein S20","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR002583
Family

Ribosomal protein S20
PD004231	$\"[67-139]T$	Q82BZ4_STRAW_Q82BZ4;
G3DSA:1.20.58.110	$\"[49-139]T$	no description
PF01649	$\"[55-138]T$	Ribosomal_S20p
TIGR00029	$\"[54-139]T$	S20: ribosomal protein S20

","BeTs to 18 clades of COG0268COG name: Ribosomal protein S20Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0268 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002583 (Ribosomal protein S20) with a combined E-value of 2.4e-44. IPB002583A 54-100 IPB002583B 111-132","Residues 54-133 are similar to a (RIBOSOMAL S20 30S RRNA-BINDING CHLOROPLAST RPST CYANELLE SUBUNIT PROBABLE RPS20) protein domain (PD511630) which is seen in RS20_CORGL.Residues 58-132 are 64% similar to a (RIBOSOMAL S20) protein domain (PD962305) which is seen in Q73M02_TREDE.Residues 67-139 are similar to a (RIBOSOMAL S20 30S RRNA-BINDING 3D-STRUCTURE SEQUENCING DIRECT S20P SSU RNA-BINDING) protein domain (PD004231) which is seen in Q82BZ4_STRAW.","","-64% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.3E_13);-64% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.3E_13);-64% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 4.3E_13);-64% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 4.3E_13);-64% similar to PDB:2AVY Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 30S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 4.3E_13);","Residues 55 to 138 (E_value = 4.5e-42) place ANA_0516 in the Ribosomal_S20p family which is described as Ribosomal protein S20.","","ribosomal protein (BS20)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0518","544259","543606","654","6.90","-0.34","23204","ATGGCCAGCCTTCTCAACCGGATCCTCACCCTGCTCGGACGCGCCGCCTCCGACGCCGTCAGCGACGCCCTTTCCCAAAAGTCCTCGACGCCGTCGGGCACGGCGGACAGCAGGCCATCCGGTTCAGCTGAGACCGCGCAGTCCCGCGCCCCCAAGTCGTCAGCGGCGAAGCCGTCACCGACCCGGCCCCGCGCCCACGACAGCGGCGCCGCGGCGGGCGCAACGGCCCCCTCGGCGCGAGGCGTCAGCGTCTACGACGTCTCTGCCCTGGGGCTGCCGGATTTCGCCTACTCCCCCGACCCCGATGGCGAGGCCGACCCCGGCGAGGTGGTGTGGGCCTGGGTTCCCTTCGAGGAGGATCCCGCCCAGGGCAAGGACCGGCCCGTCCTGGTCCTGGCTCGCCATGAGACCCGTCTGGTCGTGGCCCAGATGACGAGCAAGGACCATGACCGCGACGCCGCCCAGGAGGCGCGCTGGGGCCGCTTCTGGCACGACGTCGGCACCGGTAACTGGGACCGTCAGGGCCGCCCCAGTGAGGTGCGCCTGGACCGACTGCTCCTGGTGGAGCCGGCCTCGGTGCGCCGCGAGGGGGCCACGATGAAGCGCGAGGTCTTCGACGGCGTCGTGGCCGCCCTGCGCCACCACCACTCCTGA","MASLLNRILTLLGRAASDAVSDALSQKSSTPSGTADSRPSGSAETAQSRAPKSSAAKPSPTRPRAHDSGAAAGATAPSARGVSVYDVSALGLPDFAYSPDPDGEADPGEVVWAWVPFEEDPAQGKDRPVLVLARHETRLVVAQMTSKDHDRDAAQEARWGRFWHDVGTGNWDRQGRPSEVRLDRLLLVEPASVRREGATMKREVFDGVVAALRHHHS$","Conserved hypothetical protein","Extracellular, Periplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-17]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 97-208 are 69% similar to a (SCO0908 MB2428 CGL2342) protein domain (PD104591) which is seen in Q73XU1_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0519","545930","544419","1512","5.06","-16.07","52705","ATGCACTTCCCATCCTCCCCACCCGCTCTTCCCTGGCGGCGCCTCCTGCACATCGCCCTGGCTCTTCCCCTGCTCGCCGCCGCAGCCGTCGCAGCCCCGGCCTCCGCTGATACCGACATCACGGTGGAAGGGACCTACCACACGGCCAGTGCCGGCTGCCACAGCTCCAGCAACACCGAGGGCTGTCTGAGCTGGAGGGTTCGCATCCCATCGGCCATCGCCCCGAAGAGCGCCACGGACGTCACCATTGAGGCCGACTCCGTGCCGGGTCAGTGGACCTGGACCTGCCCCTCCCAGAACGGTGACGAGGTGGCCGGGACGAGCTCCTTCTACATCGACAACGGCGACGGCGAGCCCCCGGCCTTGATCGTGGACTCCGAGCTGAGCTCCATCTCTGAGCTGTACAACCCCCTGCTGGGGGAGCCCATCGGCTCGGTCAAAGCCGTGTCCTGCACTCCTGAGCACCTGAAGCTGACCTATGAGATCAACTTCTACACGCAATGGGACAAGACCAGCTACCTCGACCTGGATCTGGGGGCCACGGTCGTGGCTCCTGGCGCTGACGCACGCAGCTACCGTTTCACTCCCACCATCGAGGTCTCCACGCGCAACGCGATTCTTCGGCCCACTGTCACGGCGAACAAGCCCGCTGCCAGCGCTGCTCACGCCACCGTGTCCACCCAGGACGTCAGGGTCGACGGCGCCGCCAAGGACGCCTCCCGCTTCACCATGACGGCGAGGAACGACTCCACCACGCCCCTGTCCAACTTCACCATCTCCGCCGGCCGGACCAAGGGGCAGGTCCAGGTAAGCGCCCTGACCTGCGACCTGACCGCCTTCGGAGGCAAGGTCGTCTCCGCCACGGGACCGGCCGAGAACCTCAGCGTCTCCAGCGGAACGGCCAAGGTCCCCCAGGGCAAGGAGGTCACCTGCCAGGTGGACCTGACCGGCGTCGTGGGACGCAACCGGGTCAAGGCCGCACTGACCACCGGCAAGCAGACCTTCTCCAGCGACTACGTCAACATCCGGCCGGTGATTGAGGTGGAGACTCATCCCACGGATCTCCTGGTCGAGGCCGAGCCCACAGGCACCTATGAAGTCGAGGTCGGCTACACCGTCACCTTCACCAACAACACCGACGCCAACGGCTCCAGCTCCGATATCGTCCTGCGACCCGGGGTTCCGGCCGGCTTCACCCTCAAGAGCGTGACAGGTACCGGTACCCCGTGGTGGGTCGGCCCGGACAGCTATGCCCTTCAGGATGACGGCTCCTTGTTCTTGCGCACCGGTGACTCCCTGGACGCCCACTCATCAACCACGATGACCTTCACCAGCACCTACCAGGTCAACGCCGAGGCGGTCACCGCGGAGACCTGGAAGGCCCTGGGCGCCTGCGACCCCAAGAACCCCTCCCGGGGACTGACCATGCAGATCGACGTCGCCGGCAGTGAAGGCGGCACCGAGGCCGGGACCCACACGATCTGCACCCCTGTGACGCGCACCGGGAACTAG","MHFPSSPPALPWRRLLHIALALPLLAAAAVAAPASADTDITVEGTYHTASAGCHSSSNTEGCLSWRVRIPSAIAPKSATDVTIEADSVPGQWTWTCPSQNGDEVAGTSSFYIDNGDGEPPALIVDSELSSISELYNPLLGEPIGSVKAVSCTPEHLKLTYEINFYTQWDKTSYLDLDLGATVVAPGADARSYRFTPTIEVSTRNAILRPTVTANKPAASAAHATVSTQDVRVDGAAKDASRFTMTARNDSTTPLSNFTISAGRTKGQVQVSALTCDLTAFGGKVVSATGPAENLSVSSGTAKVPQGKEVTCQVDLTGVVGRNRVKAALTTGKQTFSSDYVNIRPVIEVETHPTDLLVEAEPTGTYEVEVGYTVTFTNNTDANGSSSDIVLRPGVPAGFTLKSVTGTGTPWWVGPDSYALQDDGSLFLRTGDSLDAHSSTTMTFTSTYQVNAEAVTAETWKALGACDPKNPSRGLTMQIDVAGSEGGTEAGTHTICTPVTRTGN$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0521","547845","546103","1743","5.23","-17.13","61206","ATGGGCGAGGTCTGGCAGACGAGCCAGGAAGAACAAACGACAAAGGTCGGTTGCACCGAAAGCTGGGTGCAATCGACCTTTGTCTATTCCTTTCATGAAGGCAGGGAAAGCGCGGCAGAAGAAGCACTACGCCATTTCCATGACACCGTGTTCAGAGATATATTAAAGGACTGGTCGGCGTCCCTTCCGATCATTTCAGTGAAAGGCATGCTCATGCACGTCCCATCTCTCCCATCCGCTCGTCCGTGGCGGCGCCTCCTGGGTGTCGCCATGGCTCTTCCCCTGCTCACCGTAGGTGCCGTCGCCGCTCCGGTGAGCGCAGCCGTCCCAACCGCCACCCCGGGCACTGGAATCACCGTGGAGGGGCGCTATCATCCCGCCGGCGCCGGCTGCCACGGCTCCAACAGTGCTGAGGGCTGCCTGAGCTGGGGTGTCCGAGTCCCCTCGACTGTCGCCCCGAACTCAACGACCACCGTCACCATTGAGGCTGACTCCGTGCCGGGTCAGTGGACCTGGACCTGCCCCTCTCCGGACGGCGACAGGGTGGCCGGGACCAGCGCCTTCTACATCGACAGGGGCAAGGACGAGCCCGTATCGAAGCTGGCCGACTCCGGCCTGGGTTTCTTCGACCACCTGTACTACAACCAGCACGGGGACAGCGCCGGCTCGGTCACAGCCGCTTCCTGCACTCCTGAGCACCTGAGCCTGACCTATGAGGTCAACTTCGACGCCGCCTGGGACCAGAGCTCCTATGTCGATCTGGATCTGGGGGCCACAGTCGTGGCTCCCGGCGCGGACGCGCGCAGCTACACCTTCAGCCCGAAGATCACCACCTCCACGGGCAACCTGGTTCTCACGCCCACCGCGACGGCCCACAAGCCCGCTGCCAGCGAGGCTCACGCCACCGTGTCCACCCAGGAGGTCGCGTTCGACGGCGCCGCCAGGGACACGTCCCGCTTCACCATGACGGCGAGGAACGACTCCACCACGCCCCTGTCCGGCTTCACCATCTCCGCCAGCCGGACCAGGGGGCAGGTCCAGGTGGGCACCTTGACCTGCGATCTGACCGCCTTCGGAGGCAAGGTCGTCTCCGCCACCGGACCGGCCGAGAACCTCACCGTCTCCAGCGGAACGGCCAAGGTCCCCCAGGGCAAGGAGATCACCTGCCAGGTCGACCTGACCGGTGTCACGGGACGCAACGCGGTCAAGGCCTCACTGACCACCGGCAAGCAGACCTTCTCCAGCGACTTCATCAAGGACCGCCCTATCAGCGAGGTGAAGGTCGAGCCCACTGATCGCGGAGTTGAGGCCGCCCCCACCGGCACCTACGAGGTCAAGGTCGGCTACTCCGTCACCTTCACCAACAACACCGACGCCGTGGGACAGACCTCCAATGTCGTCCTGCATCCTCCGGTCCCGGCCGGCTTCGCCCTCAAGTACGTGTGGGGCAGTGGCACGCCGTGGTGGATCAGTATGGACGACTACGCGCTCCAGGACGATGGCTCCATGCCCCTGTCCACGAGTGACACCCTGTACGCACACTCCTCGACCATGATGACCTTCACCGCCTTCTACGAGGTCAATGCCGCGGCGGTCACCGAGGACACGTGGAAGTCCCTGGGCACCTGCGACCCCAAGGACCCCTCCAAGGGACTGACCACCCAGATCGACGTCGTCGGCAGCGACGGGGTTGAGCCCGGCACCTACTCGGCCTGCACCGTCGTGACGCGCACGAAGAACTGA","MGEVWQTSQEEQTTKVGCTESWVQSTFVYSFHEGRESAAEEALRHFHDTVFRDILKDWSASLPIISVKGMLMHVPSLPSARPWRRLLGVAMALPLLTVGAVAAPVSAAVPTATPGTGITVEGRYHPAGAGCHGSNSAEGCLSWGVRVPSTVAPNSTTTVTIEADSVPGQWTWTCPSPDGDRVAGTSAFYIDRGKDEPVSKLADSGLGFFDHLYYNQHGDSAGSVTAASCTPEHLSLTYEVNFDAAWDQSSYVDLDLGATVVAPGADARSYTFSPKITTSTGNLVLTPTATAHKPAASEAHATVSTQEVAFDGAARDTSRFTMTARNDSTTPLSGFTISASRTRGQVQVGTLTCDLTAFGGKVVSATGPAENLTVSSGTAKVPQGKEITCQVDLTGVTGRNAVKASLTTGKQTFSSDFIKDRPISEVKVEPTDRGVEAAPTGTYEVKVGYSVTFTNNTDAVGQTSNVVLHPPVPAGFALKYVWGSGTPWWISMDDYALQDDGSMPLSTSDTLYAHSSTMMTFTAFYEVNAAAVTEDTWKSLGTCDPKDPSKGLTTQIDVVGSDGVEPGTYSACTVVTRTKN$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0523","548720","547845","876","5.07","-9.12","30212","ATGAGTCGTTATCCCGCGATGTTCGCCGCCCTCAAGGAGCGCGGTGAGGGCGCTTTCGTCCCCTTCGTCATGGTCGGTGACCCCGACCCGGACACCAGCGAGGCCGTCATCGAGGCGCTCATCGCCGGTGGGGCCGACGCCCTCGAGCTCGGTGTGCCCTTCACCGACCCGGTCGCCGACGGCCCCACAATCCAGAAGGCGCATGTGCGGGCCCTGGCCGCGGGTGTGGGTTTCCAGGACTGCCTGGAGGTGGTTCGGCGGGTGCGCCGGCGCCACCCGTGGCTGCCCATCGGCATGCTCATCTACGGCAACGTGCCCTTCGCCATGGGCCTGGAGCGCTTCTACTCCGAGTGCGCGCAGGCCGGCATCGACTCGGTGTTGCTGCCCGACGTCCCGATCCGCGAGTCGGCCCCCTTCAGTCGGGCCGCCGAGGAGGCCGGTATCGACGCCGTCTACATCGCCCCGCCGTCGGCCGCGGCCGAGACCCTGGACGCGGTAGCGGCGGCCTCACGCGGCTACGTCTACGCCGTCTCCCGGGTGGGGGTGACCGGCACCGAGCGGGCCTCCTCCACCGTGGGGCTCGCCGAGTCGGTGGAGCGCCTGCGCGCCGACGCCGCCGCACCGGTGATGCTGGGCTTCGGGATCTCCACGCCCGAGCAGGTCGCCGAGGCCATCGCAGCCGGCGCTGACGGGGCCATCAGTGGATCGGCCACGGTCAAGATCGTGGAGCGCTACGCCCCCGAGATTGTGGTGGCCGCCAGCGGCAACAACGGCGCAGGCGGTAACGAGGAGCGTCGTCACTACGCGCTCGGAGCGTTGCGCAGTGACCTGGTCACCTTCACCGCCACGATGAAGGGGGCCACGCGCCCGCACTGA","MSRYPAMFAALKERGEGAFVPFVMVGDPDPDTSEAVIEALIAGGADALELGVPFTDPVADGPTIQKAHVRALAAGVGFQDCLEVVRRVRRRHPWLPIGMLIYGNVPFAMGLERFYSECAQAGIDSVLLPDVPIRESAPFSRAAEEAGIDAVYIAPPSAAAETLDAVAAASRGYVYAVSRVGVTGTERASSTVGLAESVERLRADAAAPVMLGFGISTPEQVAEAIAAGADGAISGSATVKIVERYAPEIVVAASGNNGAGGNEERRHYALGALRSDLVTFTATMKGATRPH$","Tryptophan synthase, alpha subunit","Cytoplasm","tryptophan synthase, alpha subunit","tryptophan synthase alpha chain ","tryptophan synthase, alpha subunit","","Crawford I.P. Evolution of a biosynthetic pathway: the tryptophan paradigm. Annu. Rev. Microbiol. 1989. 43:567-600. PMID: 2679363Hyde C.C., Miles E.W. The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis. Biotechnology 1990. 8(1):27-32. PMID: 1366510Burns D.M., Yanofsky C. Nucleotide sequence of the Neurospora crassa trp-3 gene encoding tryptophan synthetase and comparison of the trp-3 polypeptide with its homologs in Saccharomyces cerevisiae and Escherichia coli. J. Biol. Chem. 1989. 264(7):3840-3848. PMID: 2521855Berlyn M.B., Last R.L., Fink G.R. A gene encoding the tryptophan synthase beta subunit of Arabidopsis thaliana. Proc. Natl. Acad. Sci. U.S.A. 1989. 86(12):4604-4608. PMID: 2734310","","","

InterPro
IPR002028
Domain

Tryptophan synthase, alpha chain
PD001535	$\"[1-135]T$	Q8FLJ5_COREF_Q8FLJ5;
PF00290	$\"[8-289]T$	Trp_syntA
TIGR00262	$\"[8-270]T$	trpA: tryptophan synthase, alpha subunit
PS00167	$\"[48-61]T$	TRP_SYNTHASE_ALPHA

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[1-248]T$	no description

noIPR
unintegrated

unintegrated
PTHR10314	$\"[54-239]T$	SER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF4	$\"[54-239]T$	TRYTOPHAN SYNTHASE ALPHA SUBUNIT

","BeTs to 22 clades of COG0159COG name: Tryptophan synthase alpha chainFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0159 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB002028 (Tryptophan synthase, alpha chain) with a combined E-value of 1.1e-54. IPB002028A 44-65 IPB002028B 96-131 IPB002028C 172-184 IPB002028D 208-224 IPB002028E 229-239","Residues 1-135 are similar to a (TRYPTOPHAN LYASE ALPHA BIOSYNTHESIS SYNTHASE CHAIN SUBUNIT SYNTHASE PHOSPHATE CHLOROPLAST) protein domain (PD001535) which is seen in Q8FLJ5_COREF.Residues 142-208 are 74% similar to a (TRYPTOPHAN LYASE ALPHA BIOSYNTHESIS SYNTHASE CHAIN SUBUNIT PHOSPHATE SYNTHASE CHLOROPLAST) protein domain (PD601458) which is seen in Q8FLJ5_COREF.","","-63% similar to PDB:1V7Y Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature (E_value = 4.8E_59);-63% similar to PDB:1WQ5 Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli (E_value = 4.8E_59);-63% similar to PDB:1A50 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE (E_value = 1.1E_58);-63% similar to PDB:1A5S CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE AND L-SER BOUND AS AMINO ACRYLATE TO THE BETA SITE (E_value = 1.1E_58);-63% similar to PDB:1BKS TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) FROM SALMONELLA TYPHIMURIUM (E_value = 1.1E_58);","Residues 8 to 289 (E_value = 3.9e-101) place ANA_0523 in the Trp_syntA family which is described as Tryptophan synthase alpha chain.","","synthase, alpha subunit (trpA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0524","550989","548722","2268","5.04","-31.95","79706","GTGACCACCCCCGACACCGCCCCCGTCCCCACCGCGTCACCCGATGGCGCAGGCCCTGGCGAGCGCACCCACCGTGAGCCGGTCGAGGCGCGTCTCATCGCCACGGGCACCGTCCTGGACTCGATCGTCCAGGCGCGCCGCGAGCGCATTGATGAGCTGCGCGCCCGTTTCGGGCACCTGAGAGCCGAGGACCTGGAGCGCTCGCAGCGCTCCTTCGCGGCCGCCCTGCGCACCCGTAGCGGCCAGGGCCGCAGCCCGCAGCCGGCTCTCATCATGGAGTGCAAGGCGGCCTCACCCTCACGCGGCACCATCCGCTCCGACTACGACCCGGCCTCGCTGGCCGCCCAGTACGCGCCCTACGCGGCCGCGGTCTCGGTGCTCACCGAACCCGATCGTTTCAACGGCTCCTTCGACGACCTGGCCGCTGTGCGCGAGGTGGTGGACGTGCCCGTCCTGTGCAAGGACTTCATCGTTGATGAGGTCCAGGTGCTGGCGGCTCGCAGCCTGGGGGCGGACGCGGTCCTGCTCATGCTCTCGGTGGTGCCCGACGACGTCTACCGCGAGCTGGCCGAGCTGGCCCACAGCCTGGGCATGGAGGTGCTCACGGAGGTCTCCACGCCTCAGGAGATGCATCGTGCCTCGGCCCTGGGGGCGGAGGTCATCGGTATCAACAACCGTGATCTGCGCACCTTGGAGACGGATCTGGCGCGCACCGAGGAGATGGCTCCGCTGGCTCCGGCCGGGGTGGTGCTTGTGGGTGAGTCGGGGGTCGGTGCTGCCGAGGATGTGCGGCGCCTGTCGGGCCTGGTGGACGCGCTCCTGGTGGGTTCGTCCCTGTCCGGGGCCCCGGATCCGGCCGAGGCCGCTCGTCAGCTGGCCACCGCGGTACCGCTGCCTCAGGGTGAGGGTACGTCGTCGTCGGCCCTGGACCGGGGCGGCCAGGAGACGGGTCACCATCCGCGCCTGCCGGCCTTCTTCGGTCCTTACGGGGGCCAGTTCGTGCCCGAGCTGCTCATCCCGGCGCTGGACCAGCTCGAGGACGCCTTCATCGATGCCCAGGCCGATCCGGCCTTCGCCGCCGAGCTGGAGACGCTCATGACCCGCTACCTGGGGCGTCCCACGGCGGTCACCGAGCTGCGCAACCTGCCGCTGGAGGGCAATGCCCGCATCCTGCTCAAGCGCGAGGACCTGGTCCATGGTGGCGCCCACAAGGGCAACCAGGTTCTGGGGCAGGCCCTCCTGGCCAAGCGGATGGGTAAGCGGCGCATCATCGCTGAGACCGGCGCCGGCCAGCACGGGACGGCCACCGCCATGGTCTGCGCCCTGCTGGGCCTGGACTGCACCATCTATATGGGGGCCACCGACGTCGTGCGTCAGGCGCCCAATGTCGAGCGCATGGAGCTCATGGGCGCCACGGTGGTCCCGGTGGACAGTGGTGCGGGCACGCTCAAGGACGCCGTCAACGAGGCGCTGCGCGACTGGACGGCCTCCTTCGCCGACACCCACTACCTGCTGGGCACGGCGGCCGGTCCTCACCCCTTCCCCACGATCGTGCGTGAGTACCACCGGGTCATCTCCCGGGAGGCCCGCGCCCAGGTCCTGGGCCTGACGGGGCGGCTGCCGGACTCGGTCATCGCCTGCGTGGGCGGCGGCTCCAACGCGATCGGCATGTTCGCCGAGTTCATCGACGACTCCGGGGTCGAGCTCATCGGGGTTGAGCCGGCCGGTGAGGGCCTGGACACCTCCCGCCACGGCGCCCCCATCAACAAGGGGCTGGTGGGGATCCTCCACGGGGCGCGCAGCTACCTCATGCGCACCTCGGAGGGGCAGGTCGAGGAGTCCTTCTCGGTCTCGGCGGGCCTGGACTACCCGGGCGTGGGGCCCGAGCACGCCTGGCTGTCGGACACCGGCCGGGCCCGCTACGTGGGCATTAGTGACGACGAGGCGATCGAGGCTTTCCAGCTGCTGTCACGCCACGAGGGGATCATCCCCGCGGTGGAGTCGGCCCACGCCCTGGCTCAGGCCCTGGCCATGGCCCGCCAGGTGCCCGACGGCGAGGAGCCCCCGATCCTGCTGGTGTGCCTGTCGGGCCGTGGGGACAAGGATCTTGACCAGGTGCAGGCGAGGCTGGGCGGCTCCTTCTCCACTGACGGCGCCGTGGCCAGGGCCTCGCGCATGGTGGAGCAGATGGGCAAGCGCACCGAGTACGCGGGTCTGAACGCCGCCAGGGGCACCAGCCCGGACGCCGGCCCGGATGAGGAGTTCTGA","VTTPDTAPVPTASPDGAGPGERTHREPVEARLIATGTVLDSIVQARRERIDELRARFGHLRAEDLERSQRSFAAALRTRSGQGRSPQPALIMECKAASPSRGTIRSDYDPASLAAQYAPYAAAVSVLTEPDRFNGSFDDLAAVREVVDVPVLCKDFIVDEVQVLAARSLGADAVLLMLSVVPDDVYRELAELAHSLGMEVLTEVSTPQEMHRASALGAEVIGINNRDLRTLETDLARTEEMAPLAPAGVVLVGESGVGAAEDVRRLSGLVDALLVGSSLSGAPDPAEAARQLATAVPLPQGEGTSSSALDRGGQETGHHPRLPAFFGPYGGQFVPELLIPALDQLEDAFIDAQADPAFAAELETLMTRYLGRPTAVTELRNLPLEGNARILLKREDLVHGGAHKGNQVLGQALLAKRMGKRRIIAETGAGQHGTATAMVCALLGLDCTIYMGATDVVRQAPNVERMELMGATVVPVDSGAGTLKDAVNEALRDWTASFADTHYLLGTAAGPHPFPTIVREYHRVISREARAQVLGLTGRLPDSVIACVGGGSNAIGMFAEFIDDSGVELIGVEPAGEGLDTSRHGAPINKGLVGILHGARSYLMRTSEGQVEESFSVSAGLDYPGVGPEHAWLSDTGRARYVGISDDEAIEAFQLLSRHEGIIPAVESAHALAQALAMARQVPDGEEPPILLVCLSGRGDKDLDQVQARLGGSFSTDGAVARASRMVEQMGKRTEYAGLNAARGTSPDAGPDEEF$","Tryptophan synthase, beta subunit","Cytoplasm","Tryptophan synthase beta chain","tryptophan synthase beta chain ","tryptophan synthase, beta subunit","","Goldman A. How to make my blood boil. Structure 1995. 3(12):1277-1279. PMID: 8747452","","","

InterPro
IPR001468
Domain

Indole-3-glycerol phosphate synthase, central region
PD001511	$\"[70-234]T$	TRPC_HAEIN_P46451;

InterPro
IPR001926
Domain

Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291	$\"[367-698]T$	PALP

InterPro
IPR006653
Domain

Tryptophan synthase, beta chain and related
PS00168	$\"[397-411]T$	TRP_SYNTHASE_BETA

InterPro
IPR006654
Family

Tryptophan synthase, beta chain
TIGR00263	$\"[324-710]T$	trpB: tryptophan synthase, beta subunit

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[35-301]T$	no description

InterPro
IPR013798
Domain

Indole-3-glycerol phosphate synthase
PF00218	$\"[38-292]T$	IGPS

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1100	$\"[490-716]T$	no description
PTHR10314	$\"[333-724]T$	SER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF3	$\"[333-724]T$	TRYPTOPHAN SYNTHASE BETA CHAIN

","BeTs to 21 clades of COG0133COG name: Tryptophan synthase beta chainFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0133 is aom-k-yqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB006653 (Tryptophan synthase, beta chain and related) with a combined E-value of 3.8e-160. IPB006653A 390-437 IPB006653B 447-494 IPB006653C 518-559 IPB006653D 584-638 IPB006653E 646-673 IPB006653F 691-703***** IPB001926 (Pyridoxal-5'-phosphate-dependent enzyme, beta family) with a combined E-value of 2.4e-10. IPB001926B 426-451","Residues 70-234 are 69% similar to a (SYNTHASE PHOSPHATE INDOLE-3-GLYCEROL LYASE IGPS DECARBOXYLASE TRYPTOPHAN BIOSYNTHESIS ISOMERASE INCLUDES:) protein domain (PD001511) which is seen in TRPC_HAEIN.Residues 320-372 are 66% similar to a (TRYPTOPHAN PHOSPHATE SYNTHASE LYASE BIOSYNTHESIS PYRIDOXAL CHAIN BETA) protein domain (PD900104) which is seen in TRPB_PROMM.Residues 325-373 are 79% similar to a (TRYPTOPHAN PHOSPHATE PYRIDOXAL LYASE SYNTHASE BIOSYNTHESIS BETA CHAIN SUBUNIT SYNTHASE) protein domain (PD001697) which is seen in TRPB_VIBME.Residues 385-459 are 89% similar to a (PYRIDOXAL PHOSPHATE SYNTHASE CYSTEINE BIOSYNTHESIS LYASE TRYPTOPHAN THREONINE TRANSFERASE BETA) protein domain (PD000323) which is seen in Q6NEB6_CORDI.Residues 466-617 are similar to a (TRYPTOPHAN PHOSPHATE PYRIDOXAL LYASE SYNTHASE BETA BIOSYNTHESIS CHAIN SUBUNIT SYNTHASE) protein domain (PD001443) which is seen in Q6NEB6_CORDI.Residues 618-719 are 65% similar to a (PYRIDOXAL PHOSPHATE SYNTHASE CYSTEINE BIOSYNTHESIS TRYPTOPHAN LYASE TRANSFERASE BETA CHAIN) protein domain (PD001075) which is seen in TRB2_COREF.","","-76% similar to PDB:1K3U CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID (E_value = 3.4E_135);-76% similar to PDB:1K7E CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID (E_value = 3.4E_135);-76% similar to PDB:1K7F CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]VALINE ACID (E_value = 3.4E_135);-76% similar to PDB:1K8X Crystal Structure Of AlphaT183V Mutant Of Tryptophan Synthase From Salmonella Typhimurium (E_value = 3.4E_135);-76% similar to PDB:1KFB CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate (E_value = 3.4E_135);","Residues 38 to 292 (E_value = 1e-119) place ANA_0524 in the IGPS family which is described as Indole-3-glycerol phosphate synthase.Residues 111 to 298 (E_value = 0.0038) place ANA_0524 in the NanE family which is described as Putative N-acetylmannosamine-6-phosphate epimerase.Residues 367 to 698 (E_value = 6.3e-107) place ANA_0524 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme.","","synthase beta chain (trpB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0525","552111","550999","1113","5.14","-14.35","37855","ATGAGTCAGACCAACAGCGCGGCCCCGGCCGCTGCGCAGGCCGCGCCTGCCGCCACGGCGCAGGCCGCGCCTGCCGCCACGGCGCAGGAGGCGCACGAGCTGCTGCGAGAGGTGGTGCAGGGACGGCGCCTGAGCCGCGAGCAGGCCTCTGCGGTCTTCGCGGCCCTGGGCGCCGGCGAGCTGTCCGAGGTGGAGACGGCGGCGCTGCTGGCGGCGCTGCACGCCCGTGGTGAGGAGCCCCAGGAGGTCGCGGGGGCCGCGAGCGCCTTCCGTCAGGCGGCCCGGGACTTCCCGTCGGTGTCCTTCCCGCTGGTGGACGTCGTGGGCACCGGGGGCGACGGCGTGGGCACAATCAACATCTCCACGGGGGCGGGCCTGGTGGCCGCCTCAATGGGGGTCGCGGTGGCCAAGCACGGCAACCGGGCCGTGTCCTCCAAGACGGGGGCAGCCGATGTCATCGCCGAGCTGGGGCTGCCGCTGGACATGGAGCCGGCCACGGCGGTCGAGCTGCTGGCCCGTGACCACTTCACCTTCCTGTTCGCCCAGGCCTACCACCCGGCGATGCGGCATGTGGCGCCGGTGCGCAAGGCGCTGGCGACGCCCACGATCTTCAATGTCCTGGGGCCGCTGGTGAACCCGGCCCACCTGACCTTCCAGCTCATGGGCGTGTGGGACCCGGGCATGCTGGACATGATCGCTGAGGCCATGGTCCAGCTGGGACGCGAGCGCGCGCTCGTGGTCCACGGCTCGGGCCTGGACGAGATCGCCGTCCACGGGCCGACCCTCATGCGTGAGGCGACACCCGACGGGGTGCGGGCCTACGAGGTCACGCCTGCGGACCTGGGCGTGCCCGCCTACGAGCTGGCCGACCTGCTGGGCGGGGAGCCGGCCGACAACGCCCGCCTGCTGCGCGAGGCCGTCTCGGGTGAGGGACGGCCCGCCCACCGCGACGCGATCGCCGTCAATGCCGGTGCCCTGCTGTACCTCACCGGCCGGGCCGACAGCCTCGCCGACGGCTCTGCGTCGGCCCTGGAGCAGATCCTTTCCGGTGGCGTGGCCCGCCACCTGGAGTCCATGACCAAAGCCAGTGACCTCGCCACTGAGACGGCCTGA","MSQTNSAAPAAAQAAPAATAQAAPAATAQEAHELLREVVQGRRLSREQASAVFAALGAGELSEVETAALLAALHARGEEPQEVAGAASAFRQAARDFPSVSFPLVDVVGTGGDGVGTINISTGAGLVAASMGVAVAKHGNRAVSSKTGAADVIAELGLPLDMEPATAVELLARDHFTFLFAQAYHPAMRHVAPVRKALATPTIFNVLGPLVNPAHLTFQLMGVWDPGMLDMIAEAMVQLGRERALVVHGSGLDEIAVHGPTLMREATPDGVRAYEVTPADLGVPAYELADLLGGEPADNARLLREAVSGEGRPAHRDAIAVNAGALLYLTGRADSLADGSASALEQILSGGVARHLESMTKASDLATETA$","Anthranilate phosphoribosyltransferase","Cytoplasm","anthranilate phosphoribosyltransferase","anthranilate phosphoribosyltransferase ","anthranilate phosphoribosyltransferase","","","","","

InterPro
IPR000312
Domain

Glycosyl transferase, family 3
PD001864	$\"[118-332]T$	Q6LPA6_PHOPR_Q6LPA6;
G3DSA:3.40.1030.10	$\"[99-365]T$	no description
PF00591	$\"[101-353]T$	Glycos_transf_3
PF02885	$\"[30-95]T$	Glycos_trans_3N

InterPro
IPR005940
Domain

Anthranilate phosphoribosyl transferase
TIGR01245	$\"[35-362]T$	trpD: anthranilate phosphoribosyltransferas

noIPR
unintegrated

unintegrated
PTHR11922	$\"[33-291]T$	GMP SYNTHASE-RELATED

","BeTs to 22 clades of COG0547COG name: Anthranilate phosphoribosyltransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0547 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000053 (Thymidine/pyrimidine-nucleoside phosphorylase) with a combined E-value of 7.6e-23. IPB000053A 34-48 IPB000053B 62-95 IPB000053C 105-116 IPB000053D 126-152","Residues 118-332 are similar to a (TRANSFERASE GLYCOSYLTRANSFERASE ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE TRYPTOPHAN BIOSYNTHESIS PHOSPHORYLASE THYMIDINE PYRIMIDINE-NUCLEOSIDE TDRPASE) protein domain (PD001864) which is seen in Q6LPA6_PHOPR.Residues 228-356 are 53% similar to a (PHOSPHORIBOSYLTRANSFERASE TRANSFERASE BIOSYNTHESIS GLYCOSYLTRANSFERASE TRYPTOPHAN ANTHRANILATE) protein domain (PD762500) which is seen in TRPD_CHLCV.","","-56% similar to PDB:1KGZ Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase from Erwinia carotovora (current name, Pectobacterium carotovorum) (E_value = 8.4E_54);-56% similar to PDB:1KHD Crystal Structure Analysis of the anthranilate phosphoribosyltransferase from Erwinia carotovora at 1.9 resolution (current name, Pectobacterium carotovorum) (E_value = 8.4E_54);-54% similar to PDB:1V8G Crystal structure of anthranilate phosphoribosyltransferase (TrpD) from Thermus thermophilus HB8 (E_value = 8.4E_54);-52% similar to PDB:1VQU Crystal structure of Anthranilate phosphoribosyltransferase 2 (17130499) from Nostoc sp. at 1.85 A resolution (E_value = 4.3E_42);-53% similar to PDB:1GXB ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH PYROPHOSPHATE AND MAGNESIUM (E_value = 5.9E_39);","Residues 30 to 95 (E_value = 8.8e-17) place ANA_0525 in the Glycos_trans_3N family which is described as Glycosyl transferase family, helical bundle domain.Residues 101 to 353 (E_value = 1.3e-109) place ANA_0525 in the Glycos_transf_3 family which is described as Glycosyl transferase family, a/b domain.","","phosphoribosyltransferase (trpD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0526","552932","552225","708","5.38","-5.95","24531","ATGCCCCTCACCAGCAGCCAGAGCACCGCACAGGCCACCAGGAGTCGTGCCGAGGCATCGGCACCGGCTCGAGTGGTTCTGCTCGACAACCGCGACTCCTTCGTCTACAACCTCGTCGACCAGTTCGCGACCCTCGGCTCCCAGATCGAGGTCTACCGCAACAACGTGCCGGCCTCCCGGGTGCTCGCCGCCCTGGAGCCCACCGAGGCCGAGCGCCAGGCAGGGCGGCGCCCGGTCCTGTGCCTGTCCCCCGGGCCGGGCTACCCGGCGACGTCGGGCTGCCTCATGGAGCTCATCGCCACCGCCCTGGACGAGGCGATTCCGACGCTGGGCATCTGCCTGGGGTTCCAGGCCCTGGTCGAGGCCTGCGGCGGGCGGGTCAGCCCGGTCGGCCCGGTCCACGGCCACTCCGACCGCCTCGAGGTCACCGAGGCGGGGCGCGCGGACGAGGCCTTCGCGGTCCTCGACGGCGGTCCGCTGGACGTGGCCCGCTACCACTCCCTGGGCACGCGCTCGCTGCCCGACGCACTCGTCAGCCTGGCCGAGACCACCCAGACGGACGAGGACACAAGCGGAGGCATCGTCATGGCGGCCCGGCACCGGTCGTTGCCCGCGGTCGGGCTGCAGTTCCACCCCGAGTCGATCCTCACCCCGCAGGGCCCGGCCCTGCTCAAGGCCGTCACCGCTGGCCTGGCCCGGACCCCCTGA","MPLTSSQSTAQATRSRAEASAPARVVLLDNRDSFVYNLVDQFATLGSQIEVYRNNVPASRVLAALEPTEAERQAGRRPVLCLSPGPGYPATSGCLMELIATALDEAIPTLGICLGFQALVEACGGRVSPVGPVHGHSDRLEVTEAGRADEAFAVLDGGPLDVARYHSLGTRSLPDALVSLAETTQTDEDTSGGIVMAARHRSLPAVGLQFHPESILTPQGPALLKAVTAGLARTP$","Anthranilate synthase component II","Membrane, Cytoplasm","Anthranilate synthase component II (Glutamineamido-transferase)","anthranilate synthase component II ","glutamine amidotransferase of anthranilate synthase","","Weng M.L., Zalkin H. Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. J. Bacteriol. 1987. 169(7):3023-3028. PMID: 3298209Nyunoya H., Lusty C.J. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. J. Biol. Chem. 1984. 259(15):9790-9798. PMID: 6086650","","","

InterPro
IPR000991
Domain

Glutamine amidotransferase class-I
PF00117	$\"[26-231]T$	GATase

InterPro
IPR006220
Domain

Anthranilate synthase component II/delta crystallin
PR00097	$\"[25-39]T$ $\"[108-119]T$ $\"[157-169]T$ $\"[207-220]T$	ANTSNTHASEII

InterPro
IPR006221
Domain

Glutamine amidotransferase of anthranilate synthase
TIGR00566	$\"[24-230]T$	trpG_papA: glutamine amidotransferase of an

InterPro
IPR011702
Domain

Glutamine amidotransferase superfamily
PR00096	$\"[80-89]T$ $\"[108-119]T$ $\"[207-220]T$	GATASE

InterPro
IPR012998
Active_site

Glutamine amidotransferase, class I, active site
PS00442	$\"[108-119]?$	GATASE_TYPE_I

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[23-228]T$	no description
PIRSF001375	$\"[24-235]T$	GMP synthase/anthranilate synthase component II
PTHR11922	$\"[24-225]T$	GMP SYNTHASE-RELATED

","BeTs to 22 clades of COG0512COG name: Anthranilate/para-aminobenzoate synthases component IIFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0512 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB006220 (Anthranilate synthase component II signature) with a combined E-value of 2.2e-29. IPB006220A 25-39 IPB006220B 80-89 IPB006220C 108-119 IPB006220D 122-130 IPB006220E 157-169 IPB006220F 207-220***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 6.7e-13. IPB000991A 108-125 IPB000991B 204-214***** IPB001317 (Carbamoyl-phosphate synthase protein GATase domain signature) with a combined E-value of 7.5e-12. IPB001317A 40-54 IPB001317B 77-91 IPB001317C 108-124***** IPB002474 (Carbamoyl-phosphate synthase, small chain) with a combined E-value of 1.8e-10. IPB002474D 78-89 IPB002474E 108-141 IPB002474F 187-229***** IPB001674 (GMP synthase, C terminal) with a combined E-value of 4e-10. IPB001674B 102-117 IPB001674D 206-225","Residues 25-119 are 57% similar to a (CANDIDA SYNTHASE CAABZ1 PARA-AMINOBENZOATE ALBICANS) protein domain (PD976090) which is seen in Q6CHS7_EEEEE.Residues 44-125 are 67% similar to a (GLUTAMINE SYNTHASE AMIDOTRANSFERASE BIOSYNTHESIS LIGASE GMP SYNTHETASE CTP CHAIN COMPONENT) protein domain (PD000306) which is seen in Q8D8B5_VIBVU.Residues 127-224 are 53% similar to a (SYNTHASE LYASE COMPONENT II ANTHRANILATE GLUTAMINE AMIDOTRANSFERASE TRANSFERASE BIOSYNTHESIS AMIDO-) protein domain (PD629605) which is seen in TRPG_CORGL.","","-57% similar to PDB:1I1Q STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM (E_value = 1.8E_34);-55% similar to PDB:1I7Q ANTHRANILATE SYNTHASE FROM S. MARCESCENS (E_value = 2.2E_32);-55% similar to PDB:1I7S ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN (E_value = 2.2E_32);-45% similar to PDB:1QDL THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS (E_value = 5.3E_15);-41% similar to PDB:1WL8 Crystal structure of PH1346 protein from Pyrococcus horikoshii (E_value = 2.3E_10);","Residues 26 to 231 (E_value = 1.5e-46) place ANA_0526 in the GATase family which is described as Glutamine amidotransferase class-I.","","synthase component II (Glutamine amido-transferase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0527","554723","552936","1788","4.74","-38.70","62370","ATGCCACCCACCGCGCCAGACTCCGTGCCAGACACTGCCCCCGAGGCCGCACCGTCAGCTGCATCGCCCACCGTCTCACCCACTGTGCTGACGCGCTCAGTGCGTTACCACGCCGACGGCGGCGCCCTGCTGGAGCAGATGACGCACTCCGGTCTGCTGCGCACCACTGCGGGCCCGGCCACGCAGGGAGGCTCCGTGCGGCCGCTGGACTGCGTCCTGCTGGAGAGCGCAGATATCACCACCAAGGCCTCGCGCACCACGGTCGCCATCCTGGAGGCCTCGGCCAGGCTGACGTGCTGGGGCGGGACCGTGACGGCCGAGGCGCTGGACGCCGTCGACGGAGGGGGCCCCGGGGCCGATGGTCTGGCGGCTCTGGCTCGTCTTGAGGAGGGGCTGGCCGAGCACGTCACCGACCGCGCCCCCGGCCGGTTGACTCTCACCCTGCCCACGATCTGCGACGACGACCCGTCCATCGAGGAGCGCGAGCGGCTCACCGCCCTGTCCACGATCGAGCCGCTGCGCCTCCTGGCCCGGGCAGAGGTCGACCACCCCCACCTGCCGCTGGAGGCGGGAGCCTTCGCCTTCGACTACCTGTCCACCTTCGAGTCCCTGCCCGAGGTGGCCCAGGGCGCCAACACCTGCCCCGACTACCTCTTCTACGACGCGCGCATCATCCTGGTCGTCGACCACCCCACGCAGGAGGCGACCCTGGTGGGAGCCTCGGTCGACGCCACCGACCTGGAGCGGCGCATGGAGGCTTTGGCCGCCGCCATCGACGGGATCGAGGACCCGGCCGACAGCACCGACGCAGCCGCCAGCGCAGCTGCCGACACAGCCGTTGAGGAACCGGCACCGGCCGGTGGCCCCGACTCCCCCGTCCTGCACGCGGTGCCCACCGTCTCCGACGCTGACTTCGAGGCGGTCGTGGAGGAGATGCGCGGATACATCGCTGACGGCGACGTCTACCAGGTGGTGCCCTCGCGCGGTTTCACCATTGACTGCACCGATGCGTTGGCCGCCTACCACGTGCTGCGCCATGCCAATCCCAGCCCGTACATGTTCTACCTGGCCGCGCCGGACTTCGAGCTCTTCGGAGCCTCCCCGGAGTCGGCGCTGCTGTACTCGGTGCGCAGTGGCCGGGTCGCCATCCGACCCATCGCCGGGACCCGGCCGCGCGGGCTGCACCCTGACGGCTCGGTGGACCACGAGCGCGACACCCGCCTGGAGCTGGAGCTGCGCACCGACGCCAAGGAGGTCGCCGAGCACGTCATGCTCGTGGACCTGGCCCGTAACGACGTCGCCCGGGTCAGCCGTCCGGGCACCCGCAGTGTGCAGGACCTGCTGCGCGTGGACCGCTACAGCCGGGTGATGCACCTGGTCTCTGAGGTCTCCGGCGAGCTGGCCGAGGACCTGGACGCCCTGGACGCCTTCCGCGCCTCCATGACGATGGGAACCCTCACCGGGGCCCCCAAACTACGTGCCGCCGAGCTCATCCGCCAGGCCGAGGGCGTGCGTCGCGGCTCCTACGGCGGCTCAGTGGGGTACATCCGAGGTGACGGCGAGCTGGACACCTGCATCGTCATCCGCTCCGGTTTCGTCTCCGCCGGTACAGCCCTGATCCAGGCCGGGGCCGGTGTCGTGGCGGCCTCCTCCCCAGCCGCCGAGGCCGCCGAGACCGTCCACAAGGCCCGCGCCGTCCTGGAGGCAGTCGCCGCCGCGCAGGGTGCCACCCTCGTCATCGACCGCACCGACAGCCAGACCGACATCCAGACCAGCAAGGAGGCCTGA","MPPTAPDSVPDTAPEAAPSAASPTVSPTVLTRSVRYHADGGALLEQMTHSGLLRTTAGPATQGGSVRPLDCVLLESADITTKASRTTVAILEASARLTCWGGTVTAEALDAVDGGGPGADGLAALARLEEGLAEHVTDRAPGRLTLTLPTICDDDPSIEERERLTALSTIEPLRLLARAEVDHPHLPLEAGAFAFDYLSTFESLPEVAQGANTCPDYLFYDARIILVVDHPTQEATLVGASVDATDLERRMEALAAAIDGIEDPADSTDAAASAAADTAVEEPAPAGGPDSPVLHAVPTVSDADFEAVVEEMRGYIADGDVYQVVPSRGFTIDCTDALAAYHVLRHANPSPYMFYLAAPDFELFGASPESALLYSVRSGRVAIRPIAGTRPRGLHPDGSVDHERDTRLELELRTDAKEVAEHVMLVDLARNDVARVSRPGTRSVQDLLRVDRYSRVMHLVSEVSGELAEDLDALDAFRASMTMGTLTGAPKLRAAELIRQAEGVRRGSYGGSVGYIRGDGELDTCIVIRSGFVSAGTALIQAGAGVVAASSPAAEAAETVHKARAVLEAVAAAQGATLVIDRTDSQTDIQTSKEA$","Anthranilate synthase component I","Cytoplasm","anthranilate synthase component I","anthranilate synthase component I ","anthranilate synthase component I","","Spraggon G., Kim C., Nguyen-huu X., Yee M.C., Yanofsky C., Mills S.E. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Proc. Natl. Acad. Sci. U.S.A. 2001. 98(11):6021-6026. PMID: 11371633","","","

InterPro
IPR005257
Family

Anthranilate synthase component I, TrpE
TIGR00565	$\"[36-575]T$	trpE_proteo: anthranilate synthase componen

InterPro
IPR005801
Domain

Anthranilate synthase component I and chorismate binding protein
PD000779	$\"[63-562]T$	Q8FLK0_COREF_Q8FLK0;
PR00095	$\"[410-423]T$ $\"[424-437]T$ $\"[504-518]T$ $\"[519-533]T$	ANTSNTHASEI
PF00425	$\"[301-570]T$	Chorismate_bind

InterPro
IPR006805
Domain

Anthranilate synthase component I, N-terminal
PF04715	$\"[191-237]T$	Anth_synt_I_N

noIPR
unintegrated

unintegrated
G3DSA:3.60.120.10	$\"[70-570]T$	no description
PTHR11236	$\"[158-243]T$ $\"[271-574]T$	AMINOBENZOATE/ANTHRANILATE SYNTHASE
PTHR11236:SF9	$\"[158-243]T$ $\"[271-574]T$	ANTHRANILATE SYNTHASE COMPONENT I

","BeTs to 22 clades of COG0147COG name: Anthranilate/para-aminobenzoate synthases component IFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0147 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB006805 (Anthranilate synthase component I, N-terminal) with a combined E-value of 1.1e-98. IPB006805A 305-329 IPB006805B 348-357 IPB006805C 369-396 IPB006805D 405-457 IPB006805E 475-515 IPB006805F 540-570***** IPB005801 (Anthranilate synthase component I signature) with a combined E-value of 4.5e-23. IPB005801A 410-423 IPB005801B 424-437 IPB005801C 504-518 IPB005801D 519-533","Residues 63-562 are 62% similar to a (SYNTHASE COMPONENT I ANTHRANILATE LYASE ISOCHORISMATE BIOSYNTHESIS PARA-AMINOBENZOATE TRYPTOPHAN SYNTHETASE) protein domain (PD000779) which is seen in Q8FLK0_COREF.Residues 72-541 are 57% similar to a (SYNTHASE COMPONENT I ANTHRANILATE) protein domain (PD958621) which is seen in Q8ECV4_SHEON.Residues 215-534 are 49% similar to a (ALPHA SYNTHASE CHAIN ANTHRANILATE) protein domain (PD812465) which is seen in Q9HPG5_HALN1.Residues 216-530 are 46% similar to a (COMPONENT I SYNTHASE ANTHRANILATE) protein domain (PDA18385) which is seen in Q6AEW3_BBBBB.Residues 300-541 are 57% similar to a (LIPOLYTICA YARROWIA E STRAIN CHROMOSOME CLIB99) protein domain (PDA181N6) which is seen in Q6C5V8_EEEEE.Residues 304-530 are 52% similar to a (SYNTHASE COMPONENT I PARA-AMINOBENZOATE 4.1.3.-) protein domain (PD399030) which is seen in Q9CFZ7_LACLA.Residues 309-498 are 51% similar to a (SYNTHASE BENZOATE PARA-AMINO) protein domain (PD958623) which is seen in Q70C36_XANAL.Residues 309-532 are 48% similar to a (SYNTHETASE PARA-AMINOBENZOIC ACID) protein domain (PD272009) which is seen in Q9P4F3_COPCI.","","-56% similar to PDB:1I1Q STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM (E_value = 1.0E_86);-53% similar to PDB:1I7Q ANTHRANILATE SYNTHASE FROM S. MARCESCENS (E_value = 8.6E_78);-53% similar to PDB:1I7S ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN (E_value = 8.6E_78);-57% similar to PDB:1QDL THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS (E_value = 1.3E_41);-44% similar to PDB:1K0E THE CRYSTAL STRUCTURE OF AMINODEOXYCHORISMATE SYNTHASE FROM FORMATE GROWN CRYSTALS (E_value = 9.7E_29);","Residues 87 to 237 (E_value = 5e-06) place ANA_0527 in the Anth_synt_I_N family which is described as Anthranilate synthase component I, N terminal region.Residues 301 to 570 (E_value = 3.5e-144) place ANA_0527 in the Chorismate_bind family which is described as chorismate binding enzyme.","","synthase component I (trpE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0528","555392","554889","504","11.87","15.36","18188","ATGCTGGAACGGATCCACTCCCTGCCCTATCCCGGGGTCTTCCTGTTCTTCTGGTGCCTGGCCATGATGCGTTCGCACACCATGTACTGGATCGGCCGGGGCATTACGGCGGGGACCGCGCGCACCCGGTGGGTCTCGCTGCTCGAGTCCCCCGTGTACGCCCGGGCCCAGGCGTGGTCGGCGCGCTGGGGCGTGCTGGCAGTGCCGGTGTCCTTCCTGACCGTCGGCATCCAGAGCGTCATCCAGCTCTCCGCGGGAGTGGCCCGCATGCCGCTGCGCCGCTACGTGGCGGCCACAGCCGCCGGGGCGATCGCCTGGGCCGCCGTCTACACGACCATCGGCATGGCGATCCTGTCGGCCTGGCTCACCGGCCCAATCGGCCGCATCGTCGTCATCCTGGCCGCCGCGGCGCTGATCGCCTCCATCGTGGTGCGCCGCCGTCGACGAAGGACCGCGATCGCTGAGACAGCTGGAGAGACCGGTTTCGTCTCCCGGGGTCGGTAG","MLERIHSLPYPGVFLFFWCLAMMRSHTMYWIGRGITAGTARTRWVSLLESPVYARAQAWSARWGVLAVPVSFLTVGIQSVIQLSAGVARMPLRRYVAATAAGAIAWAAVYTTIGMAILSAWLTGPIGRIVVILAAAALIASIVVRRRRRRTAIAETAGETGFVSRGR$","Uncharacterized membrane-associated protein","Membrane, Cytoplasm","conserved hypothetical protein","similar to uncharacterized membrane-associated protein","Uncharacterized membrane-associated protein-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[14-32]?$ $\"[98-118]?$ $\"[124-144]?$	transmembrane_regions

","BeTs to 6 clades of COG0586COG name: Uncharacterized membrane-associated proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG0586 is ---p-----drlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 1-127 are 48% similar to a (YSEH) protein domain (PD398783) which is seen in Q9CEP6_LACLA.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0528.1","556057","557307","1251","7.84","3.63","47325","ATGCTTATTCAAAGGAGTATTCTGTTGCTGTGGCTGACTCGGGTTGTTGAATCAATTAGGTGCATATTTCGGGCGGCGCGGAATAGGGTTGGGAGATTTGGGTTCGTTATTTTCGAGCCTCGACGATGGAGATTATTTGAGACTATTGTTGTTTGGGTGATTTTGGCTATCGTCGCTTTCACTGTGTTGGGTTGGATGTGGGGGAGTGGGCCATATTTTTCCTTGCGTCGAATTCTTGTTAACTGGGCTGGCGACGAACTGCGAACTGAGCCTTTTGAGCGTATCAAGGTTTCATTGACCATGATTGGCGGTATCGGTGCTGTAGGATATTTGGTGATCAGATATCGAGAACGTGCGGGTGTGGAACACGATGAGGCCGATTCCAAGCTTTTGTCTGCGGTTCAGCAACTCGGTAGCGACTCGCCTCAGGTTCGGATTGCGGGCGTCTATTCTCTGGCGGATTTGGCTGACACTTACGGTAGTTCTTATCATCAGCGTGTTGTCAACATTCTGTGTGGCTACTTACGTGTTGAACGAGGGTGCTGGAATTCTCCCGACGGTGCTGAGGTGCGTAGTCGTGAGGTCAAAGACACTTCCGAACTTTACTATACAACGAACGATGGTCCGGTGGAGTCTACTATTTTAAATGTGCTAGCGCGCCATCTCCGTAAAGAAAGGATCGATTCATATTCTCGCCGTCAAGTCAAGCAAGATGTCGCTGACGATCAGTTATGGTGCGACTGTGAAGTTGACTTACATGGCGCTCATTTCGTTGAGCGGGTATGTTTTGGGGGAATTACGTGCCGCTGGCTGAATGCTAGTGGGGCGCAATTTCATAATTATCTAAATCTCGGGATGTCTACGTTTGTTGAAAGCGCTTCGTTTCATGGGGCGTTATTTTCTGATGAAGCTTGTTTTAAGGGTGCAAGATTTCGGGCGTTTGCGAATTTTAATAAGGCAACCTTTAGGGGGTGTGCAACTTTTTCGAGAGCGCTATTTGCGGGAGATGCGCGTTTCCGTGGCATTAAGTTCGAAAGAGGTGGGTCCGGGAATTTCGGAGGGGCGCGCTTTAATGTCGAGTATTGGCATACAGATCCCCCAATTTTTTTGGTGGAACCGCCGTCAGAATTTATATTAGAGTTACCTTCCGGTGCTAGTTGGGCAGACTTTTCTAGTGAGCCTGCTCTGGATATTGACGAACCGGAGGTGTGGTGTCGCAAAAATAGGAGTCGAGAAAAGTTGCGGGAATGA","MLIQRSILLLWLTRVVESIRCIFRAARNRVGRFGFVIFEPRRWRLFETIVVWVILAIVAFTVLGWMWGSGPYFSLRRILVNWAGDELRTEPFERIKVSLTMIGGIGAVGYLVIRYRERAGVEHDEADSKLLSAVQQLGSDSPQVRIAGVYSLADLADTYGSSYHQRVVNILCGYLRVERGCWNSPDGAEVRSREVKDTSELYYTTNDGPVESTILNVLARHLRKERIDSYSRRQVKQDVADDQLWCDCEVDLHGAHFVERVCFGGITCRWLNASGAQFHNYLNLGMSTFVESASFHGALFSDEACFKGARFRAFANFNKATFRGCATFSRALFAGDARFRGIKFERGGSGNFGGARFNVEYWHTDPPIFLVEPPSEFILELPSGASWADFSSEPALDIDEPEVWCRKNRSREKLRE$","Hypothetical protein","Membrane, Cytoplasm","","","","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[49-69]?$	transmembrane_regions

InterPro
IPR000640
Domain

Translation elongation factor EFG/EF2, C-terminal
G3DSA:3.30.70.240	$\"[432-522]T$	no description
PF00679	$\"[429-518]T$	EFG_C

InterPro
IPR000795
Domain

Protein synthesis factor, GTP-binding
PR00315	$\"[34-47]T$ $\"[77-85]T$ $\"[106-116]T$ $\"[122-133]T$ $\"[158-167]T$	ELONGATNFCT
PF00009	$\"[30-216]T$	GTP_EFTU
PS00301	$\"[70-85]T$	EFACTOR_GTP

InterPro
IPR004161
Domain

Translation elongation factor EFTu/EF1A, domain 2
PF03144	$\"[237-307]T$	GTP_EFTU_D2

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[30-210]T$	small_GTP: small GTP-binding protein domain

InterPro
IPR006297
Family

GTP-binding protein LepA
TIGR01393	$\"[30-627]T$	lepA: GTP-binding protein LepA

InterPro
IPR013842
Domain

GTP-binding protein LepA, C-terminal
PF06421	$\"[519-627]T$	LepA_C

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.10	$\"[217-312]T$	no description
G3DSA:3.40.50.300	$\"[25-217]T$	no description
PTHR23115	$\"[25-340]T$	TRANSLATION FACTOR
PTHR23115:SF40	$\"[25-340]T$	GTP-BINDING PROTEIN LEPA

","BeTs to 19 clades of COG0481COG name: Membrane GTPase LepAFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0481 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB013842 (GTP-binding protein LepA, C-terminal) with a combined E-value of 5.3e-263. IPB013842A 32-66 IPB013842B 99-139 IPB013842C 198-252 IPB013842D 264-317 IPB013842E 353-402 IPB013842F 421-465 IPB013842G 475-515 IPB013842H 570-624 IPB013842H 524-578***** IPB000640 (Elongation factor G, C-terminal) with a combined E-value of 2e-57. IPB000640A 33-53 IPB000640B 69-91 IPB000640C 105-144 IPB000640E 484-498***** IPB005517 (Elongation factor G, domain IV) with a combined E-value of 1.5e-48. IPB005517A 33-57 IPB005517B 69-91 IPB005517C 105-144 IPB005517E 426-460***** IPB000178 (Initiation factor 2) with a combined E-value of 3.2e-10. IPB000178B 31-69 IPB000178C 105-140 IPB000178D 141-167***** IPB004160 (Elongation factor Tu, C-terminal) with a combined E-value of 4e-07. IPB004160A 32-52 IPB004160B 97-147","Residues 32-116 are 62% similar to a (GTP-BINDING BIOSYNTHESIS NUCLEAR RIBONUCLEOPROTEIN U5 ELONGATION SMALL FACTOR COMPONENT STRAIN) protein domain (PD196535) which is seen in Q23463_CAEEL.Residues 32-65 are 88% similar to a (GTP-BINDING FACTOR ELONGATION BIOSYNTHESIS G EF-G LEPA RESISTANCE PEPTIDE RELEASE) protein domain (PD000122) which is seen in LEPA_PROMA.Residues 34-144 are 51% similar to a (INITIATION FACTOR GTPASE 2 BIOSYNTHESIS TRANSLATION GTP-BINDING) protein domain (PD971532) which is seen in Q8TV36_METKA.Residues 65-117 are 73% similar to a (GTP-BINDING LEPA) protein domain (PD884672) which is seen in LEPA_COREF.Residues 69-117 are 83% similar to a (FACTOR GTP-BINDING ELONGATION BIOSYNTHESIS TU G EF-TU EF-G LEPA TRANSLATION) protein domain (PD012708) which is seen in Q6AEB5_BBBBB.Residues 117-192 are similar to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS G EF-G PEPTIDE RELEASE CHAIN RF-3) protein domain (PD336744) which is seen in Q9VRH6_DROME.Residues 143-191 are 79% similar to a (GTP-BINDING LEPA) protein domain (PD893792) which is seen in LEPA_TROWT.Residues 143-184 are 92% similar to a (GTP-BINDING FACTOR INITIATION BIOSYNTHESIS TRANSLATION IF-2 LEPA ELONGATION TYPA TYPA/BIPA) protein domain (PD103945) which is seen in LEPA_BIFLO.Residues 193-230 are 89% similar to a (GTP-BINDING LEPA BIOSYNTHESIS ELONGATION FACTOR MEMBRANE GUF1 PROTEIN HOMOLOG GTPASE) protein domain (PD946531) which is seen in LEPA_BIFLO.Residues 249-298 are 86% similar to a (GTP-BINDING FACTOR ELONGATION BIOSYNTHESIS G EF-G LEPA PEPTIDE RELEASE CHAIN) protein domain (PD004660) which is seen in Q6AEB5_BBBBB.Residues 282-339 are 74% similar to a (ELONGATION FACTOR GTP-BINDING BIOSYNTHESIS G EF-G TRANSLATION EF-2 MITOCHONDRIAL PHOSPHORYLATION) protein domain (PD000980) which is seen in LEPA_THETN.Residues 299-340 are 90% similar to a (GTP-BINDING LEPA BIOSYNTHESIS MEMBRANE ELONGATION FACTOR GUF1 HOMOLOG GTPASE CAGUF1) protein domain (PD800985) which is seen in Q6AEB5_BBBBB.Residues 360-434 are similar to a (GTP-BINDING LEPA BIOSYNTHESIS ELONGATION FACTOR MEMBRANE GUF1 PROTEIN HOMOLOG GTPASE) protein domain (PD943996) which is seen in Q6AEB5_BBBBB.Residues 436-503 are similar to a (GTP-BINDING ELONGATION FACTOR BIOSYNTHESIS G EF-G LEPA TRANSLATION EF-2 TYPA) protein domain (PD011419) which is seen in LEPA_MYCTU.Residues 512-592 are similar to a (GTP-BINDING LEPA BIOSYNTHESIS ELONGATION FACTOR MEMBRANE GUF1 HOMOLOG PROTEIN GTPASE) protein domain (PD004661) which is seen in LEPA_BIFLO.Residues 595-624 are 96% similar to a (GTP-BINDING LEPA BIOSYNTHESIS ELONGATION FACTOR MEMBRANE GUF1 HOMOLOG GTPASE CAGUF1) protein domain (PD985085) which is seen in LEPA_MYCTU.","","-54% similar to PDB:1N0U Crystal structure of yeast elongation factor 2 in complex with sordarin (E_value = 3.8E_23);-54% similar to PDB:1N0V Crystal structure of elongation factor 2 (E_value = 3.8E_23);-54% similar to PDB:1S1H Structure of the ribosomal 80S-eEF2-sordarin complex from yeast obtained by docking atomic models for RNA and protein components into a 11.7 A cryo-EM map. This file, 1S1H, Contains 40S subunit. The 60S Ribosomal Subunit Is In File 1S1I. (E_value = 3.8E_23);-54% similar to PDB:1U2R Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae (E_value = 3.8E_23);-54% similar to PDB:1ZM2 Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA (E_value = 3.8E_23);","Residues 30 to 216 (E_value = 1e-64) place ANA_0529 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain.Residues 237 to 307 (E_value = 1.5e-06) place ANA_0529 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2.Residues 429 to 518 (E_value = 1.9e-35) place ANA_0529 in the EFG_C family which is described as Elongation factor G C-terminus.Residues 519 to 627 (E_value = 2e-77) place ANA_0529 in the LepA_C family which is described as GTP-binding protein LepA C-terminus.","","protein LepA (lepA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0530","559609","560424","816","6.14","-6.25","28632","ATGAGTGACACAAGCAGGCAGACCACGGTTGACGCTGCCCTGAGCGATGACGGCTCCGGGCTGGTCCTGACCCGGGAGCTGGCCCGGGTCCTGGGGGAGCCCCACGCCGGTGCGGACGGGCGTCACCAGGACGAGCCCTCACCGTTCCACGACGGCGACCTGGTGGGGACCGTCGGCGCGGTGTGCACGGTCAAGGGGCTGCGGCCCGACGCCGGTCCGGCGGGCGTCTCGGCGATCCATAAGGGCGCCGTCGACGGGCCGGTTGAGGTGAGCCGGACCGGGATCGTCACCGACAGGCACGGGGACCGTGCCCACCACGGTGGCAGTGACAAGGCCCTCTACGTCATGAGCGCCGTTGAGCAGCGCCACTGGTCCGAGGTCCTGGGAGGTATCGAGCCGGGGCGGCTGGGGGAGAACCTCCTCATCGAGGGGGACATCGACGACGTGGAGATCGGCGCGATCCTGTCCATCGGTGACCCGAGCAACGCAGGACTGCGGGTCAGGGTGACCGGTGTGCGCAACCCGTGCGCCACCTTCGCCCGCGGTGTGGGCCGCGCGGACTGGGTGGAGGTCTTCTCGGCGCGCAACCGGGTGGGCGTCTACCTGGCGGTGCTCACCGAGGGGGCGGTGCAGGCCGGTGACGAGGTGCGCGTGGTCTCCTCCCCGGGGCACCGGGTCACCTGCCGGCGCTGGTTCGCCCACCACGACCCGCGCGACGCCCAGGGGATGCTTAACTCCGAGATCTTCGGCAACTGCGTCATCGCCGACTTCACCAAGAAGTACGTGCGGGCCGCCGCCCACGAGCAGGTCGGCTGA","MSDTSRQTTVDAALSDDGSGLVLTRELARVLGEPHAGADGRHQDEPSPFHDGDLVGTVGAVCTVKGLRPDAGPAGVSAIHKGAVDGPVEVSRTGIVTDRHGDRAHHGGSDKALYVMSAVEQRHWSEVLGGIEPGRLGENLLIEGDIDDVEIGAILSIGDPSNAGLRVRVTGVRNPCATFARGVGRADWVEVFSARNRVGVYLAVLTEGAVQAGDEVRVVSSPGHRVTCRRWFAHHDPRDAQGMLNSEIFGNCVIADFTKKYVRAAAHEQVG$","MOSC domain protein","Cytoplasm","MOSC domain protein","hypothetical protein","MOSC domain containing protein","","","","","

InterPro
IPR005302
Domain

Molybdenum cofactor sulphurase, C-terminal
PF03473	$\"[93-218]T$	MOSC

InterPro
IPR015808
Domain

Molybdenum cofactor sulphurase, C-terminal-like
G3DSA:2.40.33.20	$\"[62-264]T$	no description

","BeTs to 7 clades of COG2258COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2258 is ---------dr-b-ef-h--u-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 77-129 are 66% similar to a (YIIM MOSC UNCHARACTERIZED DOMAIN CYTOSOLIC BACTERIA IRON IRON-SULFUR YFLK SO4456) protein domain (PD449433) which is seen in Q8UJ44_AGRT5.Residues 137-223 are 51% similar to a (YIIM MOSC DOMAIN UNCHARACTERIZED CYTOSOLIC BACTERIA IRON IRON-SULFUR YFLK SO4456) protein domain (PD338623) which is seen in Q82DI2_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 93 to 218 (E_value = 1.1e-19) place ANA_0530 in the MOSC family which is described as MOSC domain.","","domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0531","560501","561511","1011","9.19","6.33","37172","ATGGCTCAGCACCACCCGCCCCGCTCCCACGCCATCCACTCCCGGGTGCGCTCCTTCTCGCGCGCCGGCGGCAGGCTGCGCCCCGTCCAGGCCGAGGCCCTGGCCCAGCTCGGTCCCCGCTACGTGGTCGACGTGCCGCGGGCCGACGCCGTGCGCACTGTATCCCCGAGCTTCCGCCTCGATCCGGAGAAGGTCTTCGGGCACATGGGGCAGGTGCGGCCGCTGATTGTCGAGGTCGGCTCGGGCAGTGGTGAGGCGCTCCTGGCCCATGCCGCCGCCCACCCGGAGACCGACTACCTGGCGGTGGAGGTCTGGGAGACCGCGATCGCACGGCTGGTGACCTCGATCCACCGTCAGGGCCTGCACAACGTGCGCGTCGTCCCCGCCGACGCCTCCCAGCTACTGGCCACCGCCCTGCCGGTGTCCTGCGCCAGCGAGGTGTGGGTGTTCTTCCCCGACCCCTGGCGCAAGCCCCGCCACCGCAAGCGCCGCCTGGTGACCACGGCCTTCGCCGACTCGGTGGCGCGGGTGCTGCGTCCCGGCGGGGTGTGGCGCCTGGCCACCGACTGGGCGGACTACGCCTGGCAGATGCGCGACGTCATCGAGGCCGTGGCGGCACTGCCCACCGGCCTGCGTCCGGATACCACCCGGCCCTACTTTCGGCATGACGACGCCGGTGCCCGCCCCGACCTGGGGGCCGAGTCCGCCGAGGAGTACAGCCAGGGCAACGGCCTGGACCCGGGATCCCCGGCGGGCGTGCGCGGCGGGTGGTCGCCCCGTTACGAGGGGCGGGTCATGACCCGCTTCGAGCAGCGGGGCCTGGATGCTGGGCGCACGATCCGCGACCTGACTGCAGTGCGCACCGAGACGGCCTGGATCCCCGAGCGCGGCGCCTCCATGCTGGATCACCTCGAGGCCGAGGGGCAGGCCTGGAACCACGTGGAGTCTCAGCCCTGGCGCCTGCGCGAGGGGCGAGGCGACGGCCTGCTGCATCCGGCGGACCGGCCGTGA","MAQHHPPRSHAIHSRVRSFSRAGGRLRPVQAEALAQLGPRYVVDVPRADAVRTVSPSFRLDPEKVFGHMGQVRPLIVEVGSGSGEALLAHAAAHPETDYLAVEVWETAIARLVTSIHRQGLHNVRVVPADASQLLATALPVSCASEVWVFFPDPWRKPRHRKRRLVTTAFADSVARVLRPGGVWRLATDWADYAWQMRDVIEAVAALPTGLRPDTTRPYFRHDDAGARPDLGAESAEEYSQGNGLDPGSPAGVRGGWSPRYEGRVMTRFEQRGLDAGRTIRDLTAVRTETAWIPERGASMLDHLEAEGQAWNHVESQPWRLREGRGDGLLHPADRP$","tRNA (guanine-N(7)-)-methyltransferase","Cytoplasm","tRNA (guanine-N(7)-)-methyltransferase(tRNA(m7G46)-methyltransferase)","tRNA (guanine-N(7)-)-methyltransferase ","tRNA (guanine-N(7)-)-methyltransferase","","De Bie L.G., Roovers M., Oudjama Y., Wattiez R., Tricot C., Stalon V., Droogmans L., Bujnicki J.M. The yggH gene of Escherichia coli encodes a tRNA (m7G46) methyltransferase. J. Bacteriol. 2003. 185(10):3238-3243. PMID: 12730187","","","

InterPro
IPR003358
Family

Putative methyltransferase
PF02390	$\"[55-288]T$	Methyltransf_4

InterPro
IPR004395
Family

Conserved hypothetical protein 91
TIGR00091	$\"[57-289]T$	TIGR00091: tRNA (guanine-N(7)-)-methyltrans

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[76-188]T$	no description
PTHR23417	$\"[40-203]T$	3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE
PTHR23417:SF1	$\"[40-203]T$	TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE

","BeTs to 19 clades of COG0220COG name: Predicted S-adenosylmethionine-dependent methyltransferaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0220 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003358 (Putative methyltransferase) with a combined E-value of 3.8e-30. IPB003358A 74-105 IPB003358B 118-131 IPB003358C 151-164 IPB003358D 267-283","Residues 78-221 are similar to a (METHYLTRANSFERASE TRNA TRANSFERASE GUANINE-N7--METHYLTRANSFERASE PROCESSING TRNAM7G46- TRNAM7G46-METHYLTRANSFERASE PROBABLE HOMOLOG INCLUDES:) protein domain (PD005334) which is seen in TRMB_RALSO.","","-47% similar to PDB:2FCA The structure of BsTrmB (E_value = 2.7E_11);-48% similar to PDB:1YZH Crystal Structure of the Conserved Hypothetical Protein, Methyltransferase from Streptococcus pneumoniae TIGR4 (E_value = 1.3E_10);-50% similar to PDB:1XJ5 X-RAY STRUCTURE OF SPERMIDINE SYNTHASE FROM ARABIDOPSIS THALIANA GENE AT1G23820 (E_value = 1.3E_10);-41% similar to PDB:2CDQ CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA ASPARTATE KINASE COMPLEXED WITH LYSINE AND S-ADENOSYLMETHIONINE (E_value = 1.3E_10);-53% similar to PDB:1M7X The X-ray Crystallographic Structure of Branching Enzyme (E_value = 1.3E_10);","Residues 55 to 288 (E_value = 2.2e-40) place ANA_0531 in the Methyltransf_4 family which is described as Putative methyltransferase.","","(guanine-N(7)-)-methyltransferase (tRNA(m7G46)-methyltransferase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0532","561508","562824","1317","9.71","11.18","45717","GTGAGCGCAGCTGCCAGGCTGCCCCGCCGGGCCTGGCTCATGGTCATTGTCGCCGGCTTCCTCGGGTTCTGCGCGGTGCTGCGGGCACCGGTCGGCGTCATCCCGCCCCTGCTGACGCGCCTGGGGCAGGACCTGGGGATGGGCGAGGTGGCGCGCGGCACACTGACCTCTGTGCCGATCCTGTGCTTCGGGCTGCTCACCCCACTGGCCTCGATGGTGGTGCGTCGCGTCGGCATCAACACCGCGGGCCTGCTCACCCTGGGAATGGCTCTGGCCGGGGCACTGCTGCGCTCGGCCGGCACCACCTGGGCGGCCTTCGCCGGAACCGTCATCATCGGGGCGGGGCTGACGGTGGGCAACCTGGTGGCGCCCATGGTCATCGGCCGCGATTTCTGGCACCGCACCTCACTCATGACGGGCCTGTACTCCTCGACCTGCAACGTCATCGTCACCGCTGCCACCGCCCTGGCCGTGCCGCTGGCCTTTGTCATCGGCTGGCAGGGCTCGGCCGCCGCCTGGACCGCCATCCCGGTGCTGCTGGCCGGGGCACTGTGGCTGTGGGTCTTCCCGCCCGGCAGCCAGGCGCCCCGGCGGAGCCTGCGAGAGCGGTCGGGGATGACCTCATGGGTGACGGAGCGCTCCTTGGCCCGTCCGACGTCGTCGACCGGTACCGCCGTCTGGAGACGCCCCCTGACCTGGGTGATGGCGGTGGCCTTCGCGGCCCAGACCTTCTCCTACTACGCGATCTCGGGGTGGCTGCCCACGGCACTGGTCGACGAGCTCTCCATGAGCGAGTCCGGTGCGGGAGTGGCCGCCTCCGTGTTCTCCATGCTGGGAATCGTGGGACCCCTGCTGGTCCCGGTCATGTTCGAGGCGCTGGGGTGGCCGGCCAGCAGGGTCCTGGGCGTCATTAGCGCCTGCTGGCTCATGCTGCCGGTCTGCCTGACAGTGGCCCCCGGTTACTGGCTGGTGCCCTGCATGCTCTCCGGCATTGCGCAGGGCGCCTTCTTCGCCGCCCTGTTCACCCTGGTCATCCGCCGCTCGTCGTCGGTCGACGAGAACCGCCAAACCACCGCGGTCATCCAGACGACCGGCTACTGCCTGGCCGCCGTCGGCCCGGTGGTCATGGGCTGGGTCCATGAGCGCAGCGGTGGCTGGGTGGCCCCTTTCTCCATGGTGGCGGGGGTACTGGTGCTCATGACCGTGTGCGCCCAGATCACCGCCCGCGCCGGCGACTCCGGCAGACCCAAGCCGACCATCCCCGCCGGCGTCCTGTCCGGCGAGGATGAGCCGGCCAAGCAAGGCGGCGACCAGTGA","VSAAARLPRRAWLMVIVAGFLGFCAVLRAPVGVIPPLLTRLGQDLGMGEVARGTLTSVPILCFGLLTPLASMVVRRVGINTAGLLTLGMALAGALLRSAGTTWAAFAGTVIIGAGLTVGNLVAPMVIGRDFWHRTSLMTGLYSSTCNVIVTAATALAVPLAFVIGWQGSAAAWTAIPVLLAGALWLWVFPPGSQAPRRSLRERSGMTSWVTERSLARPTSSTGTAVWRRPLTWVMAVAFAAQTFSYYAISGWLPTALVDELSMSESGAGVAASVFSMLGIVGPLLVPVMFEALGWPASRVLGVISACWLMLPVCLTVAPGYWLVPCMLSGIAQGAFFAALFTLVIRRSSSVDENRQTTAVIQTTGYCLAAVGPVVMGWVHERSGGWVAPFSMVAGVLVLMTVCAQITARAGDSGRPKPTIPAGVLSGEDEPAKQGGDQ$","Cyanate permease","Membrane, Extracellular","membrane protein, putative","putative MFS family transport protein (amino acid/amine transport)","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[20-381]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[4-409]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF3	$\"[4-409]T$	CYANATE TRANSPORT PROTEIN CYNX
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[12-32]?$ $\"[51-69]?$ $\"[79-97]?$ $\"[103-123]?$ $\"[144-164]?$ $\"[170-188]?$ $\"[230-250]?$ $\"[269-289]?$ $\"[299-319]?$ $\"[325-345]?$ $\"[360-380]?$ $\"[386-406]?$	transmembrane_regions

","BeTs to 5 clades of COG2807COG name: Cyanate permeaseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2807 is ---------d--b-ef----u-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 61-140 are 56% similar to a (TRANSMEMBRANE TRANSPORTER MEMBRANE EFFLUX TRICHOTHECENE PUMP MFS SUGAR INTEGRAL FACILITATOR) protein domain (PD187860) which is seen in Q8PKE1_XANAC.Residues 229-356 are 57% similar to a (ZM12ORF6) protein domain (PD260090) which is seen in Q9RNK7_ZYMMO.","","-38% similar to PDB:1PW4 Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli (E_value = );-54% similar to PDB:1WDJ Crystal structure of TT1808 from Thermus thermophilus HB8 (E_value = );-37% similar to PDB:2CGJ CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN COMPLEX WITH L-FRUCTOSE AND ADP. (E_value = );-37% similar to PDB:2CGK CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN AN OPEN UNCOMPLEXED CONFORMATION. (E_value = );-37% similar to PDB:2CGL CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN COMPLEX WITH L-FRUCTOSE, ADP AND A MODELED ATP GAMMA PHOSPHATE. (E_value = );","Residues 20 to 381 (E_value = 6.3e-16) place ANA_0532 in the MFS_1 family which is described as Major Facilitator Superfamily.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0534","562860","564107","1248","5.07","-18.50","44986","ATGGGGGAGCTGCCAGCGCAGGTGGCCGCGTCCGCACCGGACGGCAGCGAGCGCCCGTTCTCGGTGTACCTGCACGTGCCCTACTGCCGGGTGCGCTGCGGCTACTGCGACTTCAACACCTACACGAACCTGACCATGGGGCAGGGCGCCTCGGCTGAGGACTTTGTGGGAACCCTCGCCGGCGAGCTGCGCGCCGCCCGCCGCGCCATGGACGAGGCGGGCCTACCGGTGCGCGCCGTGCAGACCGTCTTCGTGGGCGGAGGAACTCCCACCATGCTGCCCGCCGCTGACCTGGTGAGCATGCTGGAGCTGGTGCGCGAGTGCTTCGGGCTCGCTGCCGACGCGGAGGTGACCACGGAGGCTAACCCGGACTCCGTGGACGAGGCCGGCCTGGAGGCCCTGGCCGAAGGCGGTTTCACCCGCGTTTCCTTCGGCATGCAGTCGGCCGTGCCCCACGTGCTGAAGGTCCTGGAGCGCACCCATGAGCCTGCCCGGGTACCGCTTGTGGTGGACTGGGCGCGACGGGCGGGCCTCAGGACCTCCCTGGATCTCATCTATGGGGCGCCGGGGGAGTCCGCCGAGGACTGGCAGCGCTCCCTAGACGCGGTGACCCGCATCGGCCCGGACCACGTGAGCGCCTACGCCCTGGTCATCGAGGAGGGCACTCGCATGTGGGGGCAGGTCCGCCGCGGAGAACTGCCCATGCCCGAGGACGACGACGAGGCCACCAAGTACGAGATGGCCGACGCCGCCCTGGGGCAGGCCGGCTACGAGTGGTACGAGATCTCCAACTGGGCGCGGCCCGGCTCCGAGTGCCGCCACAACCAGGCCTACTGGCTCGACTGGGACTGGTGGGGCGCCGGGCCCGGCGCCCACTCCCACCTGGGGGACGTGCGCCTGTGGAACACCAAGCACCCGGTCGCCTGGGCCGGGCAGATCGCCACCGGTCACCTGCCCGTGGCCGGACACGAGGTCATCGACGCCGACTCCCGCGAGCTGGAGCGGATCATGCTGGGTATCCGGCTGCGCGAGGGCATCGAGCTGGCGAGCCTCGGAAACCGGCCGGACTGCGCCTCAGCGGAGCGCCCTGATAGGGACCGTGTCACCCCACCGCACCTGGTACCCGTTGTGGCCGGCCTCGTCGCCGATGGGCTCCTCGACACCGCTGCGGCCCTGCGGGGCCGGGCGGTCCTGACCCTGCGCGGCCGTCTCATGGCCGACACCGTCACCCGCGCCCTGACTCAGTGA","MGELPAQVAASAPDGSERPFSVYLHVPYCRVRCGYCDFNTYTNLTMGQGASAEDFVGTLAGELRAARRAMDEAGLPVRAVQTVFVGGGTPTMLPAADLVSMLELVRECFGLAADAEVTTEANPDSVDEAGLEALAEGGFTRVSFGMQSAVPHVLKVLERTHEPARVPLVVDWARRAGLRTSLDLIYGAPGESAEDWQRSLDAVTRIGPDHVSAYALVIEEGTRMWGQVRRGELPMPEDDDEATKYEMADAALGQAGYEWYEISNWARPGSECRHNQAYWLDWDWWGAGPGAHSHLGDVRLWNTKHPVAWAGQIATGHLPVAGHEVIDADSRELERIMLGIRLREGIELASLGNRPDCASAERPDRDRVTPPHLVPVVAGLVADGLLDTAAALRGRAVLTLRGRLMADTVTRALTQ$","Putative oxygen-independent coproporphyrinogen III oxidase","Cytoplasm","oxygen-independent coproporphyrinogen IIIoxidase, putative","putative oxygen-independent coproporphyrinogen III oxidase ","putative oxygen-independent coproporphyrinogen III oxidase","","Sofia H.J., Chen G., Hetzler B.G., Reyes-spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 2001. 29(5):1097-1106. PMID: 11222759","","","

InterPro
IPR004559
Family

Putative oxygen-independent coproporphyrinogen III oxidase
TIGR00539	$\"[20-405]T$	hemN_rel: putative oxygen-independent copro

InterPro
IPR006638
Domain

Elongator protein 3/MiaB/NifB
SM00729	$\"[19-247]T$	Elp3

InterPro
IPR007197
Domain

Radical SAM
PF04055	$\"[23-203]T$	Radical_SAM

InterPro
IPR010723
Domain

HemN, C-terminal
PF06969	$\"[276-404]T$	HemN_C

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[27-235]T$	no description

noIPR
unintegrated

unintegrated
PTHR13932	$\"[9-413]T$	COPROPORPHYRINIGEN III OXIDASE

","BeTs to 18 clades of COG0635COG name: Coproporphyrinogen III oxidase and related Fe-S oxidoreductasesFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0635 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB010723 (HemN, C-terminal) with a combined E-value of 3.4e-27. IPB010723B 19-32 IPB010723C 82-94 IPB010723D 116-161 IPB010723E 179-214***** IPB005839 (Protein of unknown function UPF0004) with a combined E-value of 3.8e-07. IPB005839E 142-162 IPB005839F 176-217","Residues 25-67 are 63% similar to a (COPROPORPHYRINOGEN III OXIDASE OXYGEN-INDEPENDENT OXIDOREDUCTASE OXIDASE 1.-.-.- PORPHYRIN BIOSYNTHESIS COPROGEN) protein domain (PD800157) which is seen in Q9RDD2_STRCO.Residues 80-166 are 81% similar to a (COPROPORPHYRINOGEN III OXIDASE OXYGEN-INDEPENDENT OXIDOREDUCTASE OXIDASE 1.-.-.- PORPHYRIN BIOSYNTHESIS PROBABLE) protein domain (PD354252) which is seen in Q8G604_BIFLO.Residues 173-295 are 76% similar to a (COPROPORPHYRINOGEN III OXIDASE OXYGEN-INDEPENDENT OXIDOREDUCTASE OXIDASE 1.-.-.- PORPHYRIN BIOSYNTHESIS PROBABLE) protein domain (PD537200) which is seen in Q8NNB2_CORGL.Residues 173-242 are 55% similar to a (III OXYGEN-INDEPENDENT COPROPORPHYRINOGEN OXIDASE OXIDOREDUCTASE OXIDASE AGR_C_568P 1.-.-.-) protein domain (PD651556) which is seen in Q92SK5_RHIME.Residues 296-403 are 57% similar to a (III COPROPORPHYRINOGEN OXIDASE OXYGEN-INDEPENDENT OXIDOREDUCTASE 1.-.-.- OXIDASE BIOSYNTHESIS COPROGEN COPROPORPHYRINOGENASE) protein domain (PD005289) which is seen in Q6AEB7_BBBBB.","","-49% similar to PDB:1OLT COPROPORPHYRINOGEN III OXIDASE (HEMN) FROM ESCHERICHIA COLI IS A RADICAL SAM ENZYME. (E_value = 5.4E_28);-52% similar to PDB:1QK1 CRYSTAL STRUCTURE OF HUMAN UBIQUITOUS MITOCHONDRIAL CREATINE KINASE (E_value = 5.4E_28);-52% similar to PDB:1CRK MITOCHONDRIAL CREATINE KINASE (E_value = 5.4E_28);-45% similar to PDB:2D00 Subunit F of V-type ATPase/synthase (E_value = 5.4E_28);-36% similar to PDB:1DIO DIOL DEHYDRATASE-CYANOCOBALAMIN COMPLEX FROM KLEBSIELLA OXYTOCA (E_value = 5.4E_28);","Residues 23 to 203 (E_value = 4.2e-24) place ANA_0534 in the Radical_SAM family which is described as Radical SAM superfamily.Residues 276 to 404 (E_value = 5.1e-22) place ANA_0534 in the HemN_C family which is described as HemN C-terminal region.","","coproporphyrinogen III oxidase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0535","564601","565470","870","4.87","-5.62","30243","ATGACTACTCCACAGTATCCAGGTTACCCAGACGACGGATCTCAACCCGGTGGCGTCCCGGGCTACGGAGCACAGCCCGGTTATGGGGCCGGCCCCGACGCTCATCAGCAACCCGGCTACGGACCTCAAGCCGGTGCCGTTCCAAACTACGGGCCTCAGGCTGGGGCGGCACAGGGCTACGGCCCCCAGTCCACCATGGGCGGCGGAGCCGATATGCCGTACTACCCTGCAGGTGCGATGGGCGGTGCGCCGATGAGCGTCGGCGACGGCCTGTCCTGGGCGTGGTCCAAGTTCAAGGACAACGCGCTTATTCTCGTTGTCGGCTTCGGCGTGTGGGCCATTCTTTCAAATCTTGGATTTGACTCGCGTGTCGAGCTCAACGGAGAAGAGTACGGATTCAGCTACGGAATCCCCTTCTGGGGGTATGTCGCTCCCGTTGTCCGCCTGTTCTCGGCCATCGTGGCCGCCAACATGTCCCTCAAGGTGGCTTCTGGGCGGCAGCTGGAGTGGAACGACATCTTCTCCTTCCCGAACTTCGGGGCCAGCCTTCTGGCCAGCTTCCTCACTGCGGTTGCCACGGGAGTGGGCCTGCTCCTGTGCTTCATTCCGGGAATCATCATGGCTTTCCTCCTCTACTATTCCGTCTACTTCACCGTGGATAAGGGCGTGGACGGCATTGCGGGAATGAAGGCGTCGTGGGCAACCTTGTCCAGTCACGTCGGAGAGCTCTTCCCCTTCGCTCTGACCGGTGTCGGCCTCTACTTCATCGGTGGGATCACGCTGATCGGCTGGCTTGTGACGGTCCCGCTGGTGGCGCTGCTCTCCGCCTACTCCTACGTGCGCATCCAGGGCTACGACGTCGTCCGCTGA","MTTPQYPGYPDDGSQPGGVPGYGAQPGYGAGPDAHQQPGYGPQAGAVPNYGPQAGAAQGYGPQSTMGGGADMPYYPAGAMGGAPMSVGDGLSWAWSKFKDNALILVVGFGVWAILSNLGFDSRVELNGEEYGFSYGIPFWGYVAPVVRLFSAIVAANMSLKVASGRQLEWNDIFSFPNFGASLLASFLTAVATGVGLLLCFIPGIIMAFLLYYSVYFTVDKGVDGIAGMKASWATLSSHVGELFPFALTGVGLYFIGGITLIGWLVTVPLVALLSAYSYVRIQGYDVVR$","Hypothetical protein","Extracellular, Membrane","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[73-93]?$ $\"[102-120]?$ $\"[139-159]?$ $\"[180-214]?$ $\"[253-273]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 141-284 are 50% similar to a (MEMBRANE TRANSMEMBRANE PHOSPHODIESTERASE UPF0259 DIESTER GLYCEROPHOSPHORYL YCIC INTEGRAL FAMILY PROTEIN) protein domain (PD114897) which is seen in Q741L9_MYCPA.","","-57% similar to PDB:2O8J Human euchromatic histone methyltransferase 2 (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0536","565625","566668","1044","6.88","-0.48","37940","GTGCCCCTGAGCCCCACCGCCCCTGACCCGAGTGGCGCGGACGAGCGCCCCGCCCTCATCCTGGCCAACCTCGGCACGCCAGCGGCCCCCACGGCCAGGGCCGTCCGGCCCTTCCTGCGGGAGTTCCTCTCCGACCGCCGGATCGTTGAGACGCACCCCCTCCTGTGGCGCCCTGTCCTGGAGGCCATCATCCTGCGGGTGCGCCCTCGCGCGTCAGCGGCGAAGTACGCCACCATCTGGCGCCCCGGCGAGGAGACCAGCCGCTCCGGCTCTCCGCTCATGCACTTCAGCGAGCGACAGGGCCAGCTGCTCCAACGCGAGCTCGGCGAATCGGTCCAGGTGCGTGTCGCCATGCGCTACGGGCAGCCGGCCCTGCGCCGCGTCATGGGCGAGCTCATGGAGGCCGGCTGCCGCCGGATCGCCCTCATCCCGCTCTACCCGCAGTACGCCGCCTCCTCGGCCGGCACCGTCGTCGATGAGGCCGCTCGCTTCATCCCGGCCTCCCGCAACCAGCCCGAGCTGCGCACCATCCGCTCCTTCGAGACGGCGCCCGCCTACATCGAGGCCCTCGCCACCGCCCTGGAGCAGCACTGGCAGGTCCACGGCCGCCCCGACCCGGCCGCCGGCGAGCGCCTCCTGCTGTCCTTCCACTCCATCCCCCAGGCCATGCACGACGCCGGAGACCCCTACCGCTCCGAGTGCGAGCGCACCGCCCAGCTCCTCTCCCGGCGACTCGACCTGCCCGATGGCCTCGCCCAGCTCACCTTCCAGTCCGTCTTCGGGCCCGCCGCCTGGATCGGACCGGCCACCATTGACACGGTCGGCGATCTCGGCCGTGCCGGCTGCCCCCGCCTCGACGTCATCTGCCCCGGCTTCGTCTCCGACTGCCTGGAGACTCTCGAGGAGATCAACCAGCTCAACCGCGAGACCTTCACCACTGCCGGGGGTGGCAGCTTCCACTACGTCCCCTGGGGCAACGACTCCGACGGCGCCATCGCCGCCCTGGCTCAGCAGGCCAGAAAGGTGCTGGCCGGCTGGATCTGA","VPLSPTAPDPSGADERPALILANLGTPAAPTARAVRPFLREFLSDRRIVETHPLLWRPVLEAIILRVRPRASAAKYATIWRPGEETSRSGSPLMHFSERQGQLLQRELGESVQVRVAMRYGQPALRRVMGELMEAGCRRIALIPLYPQYAASSAGTVVDEAARFIPASRNQPELRTIRSFETAPAYIEALATALEQHWQVHGRPDPAAGERLLLSFHSIPQAMHDAGDPYRSECERTAQLLSRRLDLPDGLAQLTFQSVFGPAAWIGPATIDTVGDLGRAGCPRLDVICPGFVSDCLETLEEINQLNRETFTTAGGGSFHYVPWGNDSDGAIAALAQQARKVLAGWI$","Ferrochelatase","Cytoplasm","ferrochelatase","ferrochelatase ","Ferrochelatase","","Labbe-Bois R. The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption, and expression of its structural gene HEM15. J. Biol. Chem. 1990. 265(13):7278-7283. PMID: 2185242Brenner D.A., Frasier F. Cloning of murine ferrochelatase. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(3):849-853. PMID: 1704134Al-Karadaghi S., Hansson M., Nikonov S., Jonsson B., Hederstedt L. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure 1997. 5(11):1501-1510. PMID: 9384565Wu C.K., Dailey H.A., Rose J.P., Burden A., Sellers V.M., Wang B.C. The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat. Struct. Biol. 2001. 8(2):156-160. PMID: 11175906","","","

InterPro
IPR001015
Family

Ferrochelatase
PD002792	$\"[21-340]T$	HEMZ_RALSO_Q8XW32;
PTHR11108	$\"[18-336]T$	FERROCHELATASE
PF00762	$\"[16-343]T$	Ferrochelatase
TIGR00109	$\"[12-344]T$	hemH: ferrochelatase
PS00534	$\"[212-230]T$	FERROCHELATASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1400	$\"[13-235]T$	no description

","BeTs to 17 clades of COG0276COG name: Protoheme ferro-lyase (ferrochelatase)Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0276 is ---p--yq-drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB001015 (Ferrochelatase) with a combined E-value of 1.3e-42. IPB001015A 18-28 IPB001015C 117-149 IPB001015D 212-230 IPB001015E 256-272 IPB001015F 291-304","Residues 21-340 are 60% similar to a (BIOSYNTHESIS HEME LYASE IRON PORPHYRIN FERROCHELATASE PROTOHEME SYNTHETASE FERRO-LYASE PRECURSOR) protein domain (PD002792) which is seen in HEMZ_RALSO.","","-47% similar to PDB:1HRK CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE (E_value = 1.7E_16);-47% similar to PDB:2HRC 1.7 angstrom structure of human ferrochelatase variant R115L (E_value = 1.7E_16);-47% similar to PDB:2HRE Structure of human ferrochelatase variant E343K with protoporphyrin IX bound (E_value = 4.9E_16);-46% similar to PDB:1L8X Crystal Structure of Ferrochelatase from the Yeast, Saccharomyces cerevisiae, with Cobalt(II) as the Substrate Ion (E_value = 1.7E_13);-46% similar to PDB:1LBQ The crystal structure of Saccharomyces cerevisiae ferrochelatase (E_value = 1.7E_13);","Residues 16 to 343 (E_value = 1.1e-88) place ANA_0536 in the Ferrochelatase family which is described as Ferrochelatase.","","(hemH) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0538","566804","568225","1422","5.59","-9.51","50963","GTGCATCTTGAGTGGTGGTCCGTCCTGCCCTTCGCGGGCATGCTCGCCTGCATCGCCGTCCTGCCGCTGATCCCGGCCACTGCCCACTGGTGGGAGAAGCACTCCAGCCAGCTGATCGTCGCCGTGGGCCTGGGGGTGCCGGTGGCCGCCTGGATGTGGGTTGCCCTGGGCTGGACGTCCGTCTTCGCTGCCGTGGTGGAGTACGTCCAGTTCATCTGCCTGCTGCTGGCCCTGTTCGTCGTCTCCGGAGGCATCTTCCTCAAGGGCGACATCCGGGCCACGCCCCGCAACAACACGATCTTCCTGGCCATCGGCGGAGTCATCGCCTCCTTCGTGGGCACCACCGGCGCCGCCATGCTCCTCATCCGGCCCCTGCTGGCCACCAACAAGGAGCGCCACTACCGGGTGCACACGGTGCTGTACACGATCTTCATCGTGGCCAACTGCGGCGGCCTCCTCACGCCCCTGGGCGACCCGCCCCTGTTCCTGGGCTTCCTGCGCGGGGTGCCCTTCACCTGGACCTTCAACCTCCTGCGCGAGTACCTCTTCGTCAACGTCATGCTGCTGGTGAGCTACTACGCCCTGGACTCCTACTACTACTCCCAGGAGCCCGCCAAGGCCGTGCACGACGACGACACCGAGATCGAGCCCCTGGGCCTCAAGGGCTCGCTCAACTTCGTCTTCTTCGCCGTCATCATCGCCGCCGTCGCCTTCGCCCCCTCCGTTGACGCTCACGCCATCGAGGAGGGGCACGCCGTCCTGGGCGATTGGATCCCCGTGCGCGAGTTCATCATGCTGGGCTCCGCGGCCGGCTCCTACTTCCTGGGCAGCCGCGAGGTCCGCTTCAAGGACAACCAGTTCACCTGGGGACCCATCGCCGAGGTCGCCATCCTGTTCATCGGCATCTTCCTCACCATGATCCCGGCCCTGCACTACCTCGACGAGGTGGCCGGCTCGCTGCCGCTCAACGAGGTCACCTTCTTCATCTTCACCGGCGGGCTCTCCTCCGTCCTGGACAACGCCCCCACCTACGCGACCTTCTTCGAGATGGCCGGCAAGGTCTCCCACCCCGGCGGCGCCGACGTTGCCGGGATTCCCGAGCTTTACCTCGTGTCCATCTCGCTGGGCGCCGTCCTGTGCGGAGCCATCACCTACATCGGCAACGGCCCGAACTTCATGGTCAAGTCCGTCGCAGAGTCCGACGGCGTTGAGATGCCCAGCTTCGGCGGTTACGTGGGGCGCTCCATGAAGCACCTGGTGCCGATCATCGCCGCCATGGTCCTGCTCTTCATCGCACCGGGCCTCCTGTGGAAGGCCCTGGGCGGAGTGCTCACCGTGGGGCTCCTGGGCCGCGACGCCCTTCTGCTGGCCCAGTCCCGCCGCCTGGCACTGGTCGACCAGGCCGAGGCCGCTGAGGGCTGA","VHLEWWSVLPFAGMLACIAVLPLIPATAHWWEKHSSQLIVAVGLGVPVAAWMWVALGWTSVFAAVVEYVQFICLLLALFVVSGGIFLKGDIRATPRNNTIFLAIGGVIASFVGTTGAAMLLIRPLLATNKERHYRVHTVLYTIFIVANCGGLLTPLGDPPLFLGFLRGVPFTWTFNLLREYLFVNVMLLVSYYALDSYYYSQEPAKAVHDDDTEIEPLGLKGSLNFVFFAVIIAAVAFAPSVDAHAIEEGHAVLGDWIPVREFIMLGSAAGSYFLGSREVRFKDNQFTWGPIAEVAILFIGIFLTMIPALHYLDEVAGSLPLNEVTFFIFTGGLSSVLDNAPTYATFFEMAGKVSHPGGADVAGIPELYLVSISLGAVLCGAITYIGNGPNFMVKSVAESDGVEMPSFGGYVGRSMKHLVPIIAAMVLLFIAPGLLWKALGGVLTVGLLGRDALLLAQSRRLALVDQAEAAEG$","Na+/H+ antiporter","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","Na+/H+ antiporter NhaD and related arsenite permease-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[35-55]?$ $\"[60-80]?$ $\"[99-121]?$ $\"[136-156]?$ $\"[175-195]?$ $\"[227-247]?$ $\"[257-277]?$ $\"[292-312]?$ $\"[368-386]?$ $\"[419-437]?$	transmembrane_regions

","BeTs to 3 clades of COG1055COG name: Na+/H+ antiporter NhaD and related arsenite permeasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1055 is a--pkz--v-r-bcefg--nuj-i--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 3-314 are 66% similar to a (MEMBRANE PROTEIN TRANSMEMBRANE MLR4884 BLL7122 PROBABLE ANTIPORTER CT0294 NMB0570 POSSIBLE) protein domain (PD361055) which is seen in Q8F285_LEPIN.Residues 331-430 are 63% similar to a (TRANSPORTER MEMBRANE TRANSMEMBRANE PUMP ARSENICAL FAMILY ANTIPORTER NA/H COTRANSPORTER C4-DICARBOXYLATE) protein domain (PD000549) which is seen in Q7NXG5_CHRVO.Residues 331-430 are 63% similar to a (MEMBRANE PROTEIN TRANSMEMBRANE BLL7122 PROBABLE ANTIPORTER CT0294 NMB0570 POSSIBLE PRECURSOR) protein domain (PDA074G0) which is seen in Q8F285_LEPIN.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0539","569371","568304","1068","9.36","6.64","37969","GTGAACACGCCCGCCCCGTACCGCTCCCCCGTTCCCGGATCGACCGCCGCCCGCCGAGCCGCCCTGAGGGCTCGCGCCGAGGCCGAGCAGAAGCAGCAGGCACAGGGCGCCCCGGCCGCTTCGCGCTCGCGCGGTGGGGCGGCTGCGAGCAAGTCCGCTGCCCGCAGGCCCTCGTCGAGCGACCGCTACGGCGGGGACGTCCTGTCGGTCAACCCGCACCGCACGGGGCCCGGCGCCATACGCCCGGAGTCGGTGCACGTGCCGGTGACGCCGGGACTGGTGGTTGAGGACCGCCAGACCGGCTTCGTCGGCGCCGCGGTGGCGGTGGAGAAGTCGGGCGGTCAGCACGTCGTGGTCCTGGAGGACCGTCACGGTGTGCGCCGTGGCTTCGCCCTGGGGCCGGGTTTCTGGATCGAGGGCCGCCCGGTGATCCTGGACCCGCCCGTGGCGCGCACACGCAAGCCCACCGGAGCGGTGAGCGCCGCCGGCAGACGGCTGACGGCCTCGGGCTCCTACGCGGTTGAGGGTGAGCGGGCCAAGGTGGCGCGCGCCTCGCGGATCTGGGTGGAGGGCAAGCACGACGCCGAGCTGGTGGAGAAGGTCTGGGGTGACGACCTGCGCCACGAGGGCGTCGTCGTCCTCATGCTCGACGGCGTCGACAACCTCGAGGAGGTCATGGCCGACTTCGGTCCGGCCCCCGAGCGGCGGGCCGGCGTCCTCGTGGACCACCTGGTGGCCGGTTCCAAGGAGTCGCGGATCGCTCAGCGGGTGGCCGAGATGCCCGGTGGGGAGAACGTGCTGGTTCTGGGGCACCCGTATGTGGACGTGTGGCAGGCGGTCAAGCCGGCCCGGGTGGGTTTGGAGCGCTGGCCGGACATCCCGCGGGGCACCGACATCAAGCACGGCACCCTGGAGGCCCTGGGCTGGCCGCATGACACCCAGGCTGACGTCGCCCGGGGCTGGCAGCGCATCCTGTCGACGGTGCACTCCTACAAGGACCTCGAGCCGAGCCTGCTGGGGCGAATGGAGGAGCTCATCGACTTCGTCACCGCCCCGGGCACGCGCTGA","VNTPAPYRSPVPGSTAARRAALRARAEAEQKQQAQGAPAASRSRGGAAASKSAARRPSSSDRYGGDVLSVNPHRTGPGAIRPESVHVPVTPGLVVEDRQTGFVGAAVAVEKSGGQHVVVLEDRHGVRRGFALGPGFWIEGRPVILDPPVARTRKPTGAVSAAGRRLTASGSYAVEGERAKVARASRIWVEGKHDAELVEKVWGDDLRHEGVVVLMLDGVDNLEEVMADFGPAPERRAGVLVDHLVAGSKESRIAQRVAEMPGGENVLVLGHPYVDVWQAVKPARVGLERWPDIPRGTDIKHGTLEALGWPHDTQADVARGWQRILSTVHSYKDLEPSLLGRMEELIDFVTAPGTR$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 61-350 are 69% similar to a (SCO2557 CGL1535 MB2059C) protein domain (PD125864) which is seen in Q73Z40_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0541","569534","570637","1104","6.21","-2.79","39232","ATGAGGGGAGGAGGACCCGTGGCCAACGACCGACGTCTCAAGGTCCTGTCCGCCATCGTCACCGACTACGTGCGCACGCGCGAGCCCGTGGGTTCCAAGGCCCTCGTGGAGCGCTACCGGCTGGGCGTGTCCCCGGCGACCATCCGCAACGACATGGCGGCCCTGGAGGACGAGGGCTACATCCACCAGCCGCACACCTCGGCCGGGCGCGTGCCCACCCAGAAGGGCTACCGGCTCTTCGTCGACGAGGTCGCCCGCATCAAGCCCCTCTCAGCGCCCGAGCGCGCCGCCATCACCGCGCTCCTGTCGGGGGCGGTCGACCTGGAGCAGGTCGTGGCCCGCACCGTGCGGGCCCTGGCTCAGCTGACCGGACAGCTCGCCGTCGTCGAGTACCCGAGCCTGCGGTACGCGGCCCTCCAACACCTCGAGCTCGTGGCCCTGGGGCCCGAGCGCGTCCTGCTGGTCATCATCACCGACACCGGTCGCGTCGACCAGCGCACCGTGACCCTCAGGTCCCGGGGCTCCCTGAGCTCCCGCCATGACGGGGGCTTCGACATCGCCGACGTCGTCGACCCCCTCGTCCTGGAGCGCCTGCGCACCCGGCTCAACGGCGCCCTCGCGGGCCGCCGCGCCGCCGACGTCGCCCCGATCCTGGCGGCCCTGGCCGAGCAGGCGCCCGCCGACGAGCGCTTCCTGCTCGAGGCCGTCTCCGACGAGCTCATCGCCGCCCTACGCCCCGACGCGGAGGAGCGGCTCGTCGTCGCCGGGACCGCGAACCTGGCCCGCGCCACCCCCGACTTCTCCTCCCTGGGGCCCCTCCTGGACGCCGTCGAGGAGCAGGTGGTGCTGCTGCGCCTGTTCACCGCCGCCGACGGCGCCCCGGCCGGCGAGAACCGGATGCGCGTGAGCATCGGATCGGAGAACAAGGACGACGCCCTGGCCGAGGCCTCCGTCGTCACCACCACCTACGGGCCGGGAACCGGTGAGGCCGTCGCCCACCTCGGGGTCATCGGCCCCACCCGCATGGACTACCCGGCCACCATGACCGCCGTCCGGGCCGTGGCCCGCTACCTGTCCCGGTTCCTGTCCCCACCGGAGACCTGA","MRGGGPVANDRRLKVLSAIVTDYVRTREPVGSKALVERYRLGVSPATIRNDMAALEDEGYIHQPHTSAGRVPTQKGYRLFVDEVARIKPLSAPERAAITALLSGAVDLEQVVARTVRALAQLTGQLAVVEYPSLRYAALQHLELVALGPERVLLVIITDTGRVDQRTVTLRSRGSLSSRHDGGFDIADVVDPLVLERLRTRLNGALAGRRAADVAPILAALAEQAPADERFLLEAVSDELIAALRPDAEERLVVAGTANLARATPDFSSLGPLLDAVEEQVVLLRLFTAADGAPAGENRMRVSIGSENKDDALAEASVVTTTYGPGTGEAVAHLGVIGPTRMDYPATMTAVRAVARYLSRFLSPPET$","Heat-inducible transcription repressor HrcA","Cytoplasm","heat-inducible transcription repressor HrcA","K03705 heat-inducible transcriptional repressor","heat-inducible transcription repressor HrcA","","Roberts R.C., Toochinda C., Avedissian M., Baldini R.L., Gomes S.L., Shapiro L. Identification of a Caulobacter crescentus operon encoding hrcA, involved in negatively regulating heat-inducible transcription, and the chaperone gene grpE. J. Bacteriol. 1996. 178(7):1829-1841. PMID: 8606155Schulz A., Schumann W. hrcA, the first gene of the Bacillus subtilis dnaK operon encodes a negative regulator of class I heat shock genes. J. Bacteriol. 1996. 178(4):1088-1093. PMID: 8576042","","","

InterPro
IPR001034
Domain

Bacterial regulatory protein, DeoR N-terminal
PF08220	$\"[18-74]T$	HTH_DeoR

InterPro
IPR002571
Family

Negative regulator of class I heat shock protein
PF01628	$\"[108-348]T$	HrcA
TIGR00331	$\"[9-362]T$	hrcA: heat-inducible transcription represso

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[9-91]T$	no description

","BeTs to 10 clades of COG1420COG name: Transcriptional regulator of heat shock geneFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1420 is --------v-rlbc----s-uj-i-wNumber of proteins in this genome belonging to this COG is 1","***** IPB002571 (Negative regulator of class I heat shock protein) with a combined E-value of 1.1e-56. IPB002571A 29-82 IPB002571C 304-322 IPB002571D 332-351","Residues 9-65 are 89% similar to a (REPRESSOR TRANSCRIPTION HEAT-INDUCIBLE HRCA HEAT SHOCK REGULATION TRANSCRIPTIONAL HOMOLOG INDUCIBLE) protein domain (PD003513) which is seen in HRCA_STRAL.Residues 9-65 are 68% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR DEOR FAMILY REGULATOR OPERON) protein domain (PD469489) which is seen in Q6F147_MESFL.Residues 10-86 are 71% similar to a (TRANSCRIPTIONAL REGULATOR TRANSCRIPTION FAMILY ANTITERMINATOR BGLG DOMAIN REGULATORY OPERON REGULATION) protein domain (PD013909) which is seen in HRCA_LACSN.Residues 66-98 are 87% similar to a (REPRESSOR TRANSCRIPTION HEAT-INDUCIBLE HRCA HEAT SHOCK REGULATION TRANSCRIPTIONAL GENES I) protein domain (PD837597) which is seen in Q6A998_PROAC.Residues 102-353 are 58% similar to a (REPRESSOR TRANSCRIPTION HEAT-INDUCIBLE HRCA HEAT SHOCK REGULATION TRANSCRIPTIONAL INDUCIBLE HOMOLOG) protein domain (PD011240) which is seen in HRCA_STRCO.","","-58% similar to PDB:1STZ Crystal structure of a hypothetical protein at 2.2 A resolution (E_value = 1.3E_22);-62% similar to PDB:2HIM Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I (E_value = 1.3E_22);-62% similar to PDB:2P2D Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I (E_value = 1.3E_22);-62% similar to PDB:2P2N Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I (E_value = 1.3E_22);-48% similar to PDB:2HXU Crystal structure of K220A mutant of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and L-fuconate (E_value = 1.3E_22);","Residues 18 to 74 (E_value = 0.0039) place ANA_0541 in the HTH_DeoR family which is described as DeoR-like helix-turn-helix domain.Residues 108 to 348 (E_value = 4.4e-46) place ANA_0541 in the HrcA family which is described as HrcA protein C terminal domain.","","transcription repressor HrcA (hrcA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0542","570730","571854","1125","5.29","-10.08","39662","GTGAGCAACTACTACGAGGTCCTCGGCGTCAGCCGCGACGCCAGCCCCGAGGAGATCAAGAAGGCCTACCGCAAGAAGGCCCGCCAGCTGCACCCCGACGTCGCCGGCCCCGGCCACGAGGACGAGTTCAAGGAGGTCTCCTCCGCCTACGAGGTCCTCTCCGACGCCGACAAGCGCCAGATGTACGACCTGGGCGGGGAGGACGCCGTGCGAGGCGGCGGCGGATTCGGTGGGGGCTTCGCCGGAGCCGACTTCGGCGACCTGGGCGGCATCTTCCAGTCCTTCTTCGGTGGGGGAGCGGCCAGCCGCGGACCGGCCTCCCGGGCCCGCCGCGGCCAGGACGCCCTCGTGGCCGTGGACGTGGAGCTCTCCGACGTCGCCTTCGGAGCGACCCGGTCGGTCCCCATCGACACCTACGTCACCTGCACCGCCTGCGACGGCTCCTGCTGCGCACCGGGCACCGAGCCGGTCACCTGCTCCCAGTGCAACGGGGTCGGCAACGTCCAGCGCATGACCCGTACCCTGCTGGGGCAGGTGATGACCTCCTCGCCCTGCCCGGGCTGCCAGGGCTACGGCACCGTCATCGTCACCCCCTGCAAGGACTGCTCCGGCGAGGGCCGCATCCGGGTACGCCAGGACCTGGAGGTCTCCATCCCCGCCGGGGTGTCCACCGGGACCCGTATCCGCATGTCGGGGCGCGGCGAGGCCGGCCCGGCCGGCGGCCCCAACGGCGACCTCTACCTGGAGATCCACGAGAAGCCGCACGAGTTCCTCGAGCGCGACGGCGACGACCTCTACACCGAGCTGCGCGTGCCCATGACCGCGGCCGCGCTGGGTGCCGTCTTCCCGCTGCAGACCCTCGACGGCGAGCAGAACGTCACCGTCAAGGCCGGCAGCCAGCCCGGCGACGAGGTCGTCCTCGACGGACTGGGCGTGGGGCGCCTGCGCCGCAAGGGCCGCGGGGACCTGCACGTGTCCATCGTCGTGGAGACCCCCACGCGCCTGGACGACCGTCAGCGTGAGCTGCTGGCCGAGCTGGCCCGCCTGCGCGGGGAGGACGACGTCGAGCCCGTGCGCGACTCGAGTGTCATGGGCAAGCTCAAGGAGCGCTTCTCCGGGCGCTGA","VSNYYEVLGVSRDASPEEIKKAYRKKARQLHPDVAGPGHEDEFKEVSSAYEVLSDADKRQMYDLGGEDAVRGGGGFGGGFAGADFGDLGGIFQSFFGGGAASRGPASRARRGQDALVAVDVELSDVAFGATRSVPIDTYVTCTACDGSCCAPGTEPVTCSQCNGVGNVQRMTRTLLGQVMTSSPCPGCQGYGTVIVTPCKDCSGEGRIRVRQDLEVSIPAGVSTGTRIRMSGRGEAGPAGGPNGDLYLEIHEKPHEFLERDGDDLYTELRVPMTAAALGAVFPLQTLDGEQNVTVKAGSQPGDEVVLDGLGVGRLRRKGRGDLHVSIVVETPTRLDDRQRELLAELARLRGEDDVEPVRDSSVMGKLKERFSGR$","Chaperone protein DnaJ","Cytoplasm, Extracellular","Chaperone protein dnaJ2","chaperone protein DnaJ","chaperone protein DnaJ","","Greene M.K., Maskos K., Landry S.J. Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(11):6108-6113. PMID: 9600925Cyr D.M., Langer T., Douglas M.G. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 1994. 19(4):176-181. PMID: 8016869Han W., Christen P. cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides. FEBS Lett. 2004. 563(1):146-150. PMID: 15063739","","","

InterPro
IPR001305
Domain

DnaJ central region
PF00684	$\"[129-213]T$	DnaJ_CXXCXGXG
PS51188	$\"[129-211]T$	ZF_CR

InterPro
IPR001623
Domain

Heat shock protein DnaJ, N-terminal
PF00226	$\"[3-63]T$	DnaJ
SM00271	$\"[2-58]T$	DnaJ
PS50076	$\"[3-66]T$	DNAJ_2
PS00636	$\"[43-62]T$	DNAJ_1

InterPro
IPR002939
Domain

Chaperone DnaJ, C-terminal
PF01556	$\"[226-347]T$	DnaJ_C

InterPro
IPR003095
Family

Heat shock protein DnaJ
PR00625	$\"[14-33]T$ $\"[43-63]T$ $\"[134-153]T$ $\"[159-169]T$ $\"[177-195]T$ $\"[197-212]T$ $\"[216-232]T$ $\"[262-279]T$	DNAJPROTEIN

InterPro
IPR012724
Family

Chaperone DnaJ
TIGR02349	$\"[3-350]T$	DnaJ_bact: chaperone protein DnaJ

InterPro
IPR015609
Family

Molecular chaperone, heat shock protein, Hsp40, DnaJ
PTHR11821	$\"[3-334]T$	DNAJ/HSP40

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.110	$\"[2-72]T$	no description
G3DSA:2.10.230.10	$\"[129-211]T$	no description
G3DSA:2.60.260.20	$\"[255-344]T$	no description
PTHR11821:SF79	$\"[3-334]T$	CHAPERONE PROTEIN DNAJ

","BeTs to 22 clades of COG0484COG name: Molecular chaperones (contain C-terminal Zn finger domain)Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0484 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001305 (DnaJ central domain (CXXCXGXG)) with a combined E-value of 1.1e-100. IPB001305A 3-30 IPB001305B 42-67 IPB001305C 111-154 IPB001305D 185-230 IPB001305E 244-279 IPB001305F 306-343***** IPB003095 (DnaJ protein family signature) with a combined E-value of 5.4e-62. IPB003095A 14-33 IPB003095B 43-63 IPB003095C 134-153 IPB003095D 159-169 IPB003095E 177-195 IPB003095F 197-212 IPB003095G 216-232 IPB003095H 262-279 IPB003095D 199-209 IPB003095F 183-198 IPB003095G 293-309","Residues 5-53 are similar to a (CHAPERONE DNAJ HEAT SHOCK REPEAT DNA T ZINC METAL-BINDING REPLICATION) protein domain (PD000231) which is seen in Q6A997_PROAC.Residues 113-168 are similar to a (CHAPERONE REPEAT SHOCK HEAT DNAJ ZINC METAL-BINDING DNA REPLICATION HOMOLOG) protein domain (PD033728) which is seen in Q6AEC0_BBBBB.Residues 179-222 are 77% similar to a (CHAPERONE REPEAT SHOCK HEAT DNAJ ZINC METAL-BINDING REPLICATION DNA HOMOLOG) protein domain (PD000802) which is seen in Q6AEC0_BBBBB.Residues 185-289 are 43% similar to a (CHAPERONE DNAJ PROBABLE REPEAT) protein domain (PD311578) which is seen in Q9N8X9_EEEEE.Residues 214-279 are 57% similar to a (CHAPERONE DNAJ FAMILY MOLECULAR) protein domain (PD531283) which is seen in Q89L95_BRAJA.Residues 225-264 are 77% similar to a (CHAPERONE SHOCK HEAT REPEAT DNAJ ZINC METAL-BINDING DNA REPLICATION HOMOLOG) protein domain (PD404783) which is seen in Q6AEC0_BBBBB.","","-47% similar to PDB:1NLT The crystal structure of Hsp40 Ydj1 (E_value = 3.2E_16);-73% similar to PDB:2DMX Solution structure of the J domain of DnaJ homolog subfamily B member 8 (E_value = 5.1E_14);-73% similar to PDB:2OCH J-domain of dnj-12 from Caenorhabditis elegans (E_value = 6.6E_14);-50% similar to PDB:1EXK SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ. (E_value = 3.3E_13);-79% similar to PDB:1HDJ HUMAN HSP40 (HDJ-1), NMR (E_value = 4.3E_13);","Residues 3 to 63 (E_value = 5.2e-33) place ANA_0542 in the DnaJ family which is described as DnaJ domain.Residues 129 to 213 (E_value = 2.4e-16) place ANA_0542 in the DnaJ_CXXCXGXG family which is described as DnaJ central domain (4 repeats).Residues 226 to 347 (E_value = 1e-55) place ANA_0542 in the DnaJ_C family which is described as DnaJ C terminal region.","","protein dnaJ2","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0543","572670","571870","801","5.56","-3.60","28452","ATGACCGAGTCTTCAGCAGCCGCCCAGTCCCCTCAGTCGTCTCCCTCCCCCTCGTACACCACCGCCGTCACGGTGGAGGACTTCCGCCGCAACCTGGATGCCGTCCGCGCCCGCATCGACGCCGCCGCGAAGCGCGCCGGCCGCGACACCGCCGAGATCCGCCTGCTGCCGGTGTCCAAGACCGTCCCCGAGGAGCGCCTGCGCACCGCCTTCGCCGCGGGCATCACCCAGATGGGTGAGAACAAGGTCCAGGAGGCACAGCGCAAGAGCGAGAACCTGGCGGACCTGGGCATCTCCTGGTCAGTCATCGGCCACCTGCAGACCAATAAGGCCAAGAACGTGGCAGCCTTCGCCGACGAGTTCCAGGCCCTGGACTCCCTGCGCCTGGCCGAGGCCCTTGACCGGCGCCTCCAGGCGGCCGGGCGGGGCCTGGACGTCTACGTGCAGGTCAACTCCTCGGGCGAGCCCAGCAAGTTCGGTCTGGAGCCCGACGACGTCGCAGGCTTCCTCACAGCGCTACCGGCCTACTCCTCGCTGCGGGTGCGTGGGCTCATGACCCTGGCCGCCAACACCAGTGACGAGGCACGGGTGCGCGAGTGCTTCAGCATCATGCGCCGGCTGCGCGATGCCGCGCTCGAAGCGGGCACCGTCGGCGACGGGCTGCTGTCGATGGGAATGAGCGGGGACTTCGAGGCCGCCATCGAGGGCGGCTCCACCTGCGTGCGAGTCGGCCAGGCGATCTTCGGGGCCCGGGCCACCCCCGACTCCCACTACTGGCCCGAGACGCCTCAGACCGCTTAG","MTESSAAAQSPQSSPSPSYTTAVTVEDFRRNLDAVRARIDAAAKRAGRDTAEIRLLPVSKTVPEERLRTAFAAGITQMGENKVQEAQRKSENLADLGISWSVIGHLQTNKAKNVAAFADEFQALDSLRLAEALDRRLQAAGRGLDVYVQVNSSGEPSKFGLEPDDVAGFLTALPAYSSLRVRGLMTLAANTSDEARVRECFSIMRRLRDAALEAGTVGDGLLSMGMSGDFEAAIEGGSTCVRVGQAIFGARATPDSHYWPETPQTA$","Alanine racemase","Cytoplasm, Periplasm","conserved hypothetical protein TIGR00044","hypothetical protein","alanine racemase domain protein","","Whitchurch C.B., Hobbs M., Livingston S.P., Krishnapillai V., Mattick J.S. Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria. Gene 1991. 101(1):33-44. PMID: 1676385De Wergifosse P., Jacques B., Jonniaux J.L., Purnelle B., Skala J., Goffeau A. The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein. Yeast 1994. 10(11):1489-1496. PMID: 7871888Shaw J.P., Petsko G.A., Ringe D. Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Biochemistry 1997. 36(6):1329-1342. PMID: 9063881","","","

InterPro
IPR001608
Domain

Alanine racemase, N-terminal
PF01168	$\"[27-253]T$	Ala_racemase_N

InterPro
IPR011078
Family

Predicted pyridoxal 5'-phosphate-dependent enzyme, YBL036C type
PTHR10146	$\"[11-257]T$	PROLINE SYNTHETASE ASSOCIATED PROTEIN
TIGR00044	$\"[25-251]T$	TIGR00044: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.10	$\"[15-260]T$	no description
PIRSF004848	$\"[30-255]T$	Predicted pyridoxal 5'-phosphate-dependent enzyme, YBL036c type

","BeTs to 15 clades of COG0325COG name: Predicted enzyme with a TIM-barrel foldFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0325 is ------yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB011078 (Protein of unknown function UPF0001) with a combined E-value of 1.8e-53. IPB011078A 55-89 IPB011078B 100-110 IPB011078C 148-161 IPB011078D 177-188 IPB011078E 222-249***** IPB001608 (Protein of unknown function UPF0001) with a combined E-value of 1.2e-41. IPB001608A 55-89 IPB001608B 100-110 IPB001608C 148-161 IPB001608D 177-188 IPB001608E 222-249","Residues 36-249 are 78% similar to a (UPF0001 ENZYME SYNTHETASE PROLINE A FOLD PREDICTED TIM-BARREL WITH YLME) protein domain (PD004988) which is seen in Q7WII0_BORBR.","","-54% similar to PDB:1W8G CRYSTAL STRUCTURE OF E. COLI K-12 YGGS (E_value = 4.7E_34);-51% similar to PDB:1B54 CRYSTAL STRUCTURE OF A YEAST HYPOTHETICAL PROTEIN-A STRUCTURE FROM BNL'S HUMAN PROTEOME PROJECT (E_value = 6.7E_20);-51% similar to PDB:1CT5 CRYSTAL STRUCTURE OF YEAST HYPOTHETICAL PROTEIN YBL036C-SELENOMET CRYSTAL (E_value = 6.7E_20);","Residues 27 to 253 (E_value = 2.3e-09) place ANA_0543 in the Ala_racemase_N family which is described as Alanine racemase, N-terminal domain.","","hypothetical protein TIGR00044","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0544","572731","573543","813","5.51","-5.11","28129","GTGACCGCACCCGTCTTCCTCTTCACGCCCGAGACCATCGAGCCTGCCGACGCCGTCGCTTCGGCGGGGACCGGAACCGTCCTCATGCTCACCGGGCCTGAGGCCCGCCACGCCGTAACCGTCAAGCGCCTGCGTGCCCAGGAGCGCGTGGACCTCGTTGACGGCGCTGGTCTGCGCCTGGTCTGCGAGGTGACCGGGGCCGGCGTCGGCGGCGCCAAGGACCGTCTGGCCGTGCGGGTCCTGGATCGCGTTGAGGAGCCCGAGCCGCCGCTCCGGCTGACCCTCGTTCAGGCCCTGGCCAAGGGCGGGCGCGACGAGCAGGCCGTGGAGACGGCCACCGAGGTCGGAGTGGGGCTGGTGCTGCCCTGGCAGTCCGAGCGCTGCGTATCCGTGTGGCAGGGCGCCAAGCAGGCCAAGGGACGCCAGCGCTGGCAGACCACCGCCCTCCAGGCCGCCAAGCAGGCCCGGCGGGCCAGCGTCCCCGAGGTCGAGGAGGTGCGGGACACCCGCAGTCTGGCCGACTGGGTTGGGCAGACGGTTCGCGGCGGGGGAGTGGTGCTGGTCCTGCACGAGGAGGCCAGCACCCCGATCAGCACCGCGGTGGAGGCCGTGCGCCTGCCCGCGCCCGAAGAGGCGCCGCTGGCGCTAGCCGTCGTCGTGGGGCCCGAGGGCGGTATCAGCCCCGAGGAGACGGCGGCCCTGGAGGCCGCCGGGGCGACGACGGTGCGGCTGGGCCCCCACGTCATGCGCACCGCCTCAGCCGGCCCCGTCGCCCTGGCCGTCCTCGCCCACGCCAGCGGCCTGTGGGAGTGA","VTAPVFLFTPETIEPADAVASAGTGTVLMLTGPEARHAVTVKRLRAQERVDLVDGAGLRLVCEVTGAGVGGAKDRLAVRVLDRVEEPEPPLRLTLVQALAKGGRDEQAVETATEVGVGLVLPWQSERCVSVWQGAKQAKGRQRWQTTALQAAKQARRASVPEVEEVRDTRSLADWVGQTVRGGGVVLVLHEEASTPISTAVEAVRLPAPEEAPLALAVVVGPEGGISPEETAALEAAGATTVRLGPHVMRTASAGPVALAVLAHASGLWE$","Conserved hypothetical protein","Cytoplasm","Uncharacterized BCR","hypothetical protein","protein of unknown function DUF558","","","","","

InterPro
IPR006700
Family

Protein of unknown function DUF558, methyltransferase predicted
PF04452	$\"[28-264]T$	DUF558
TIGR00046	$\"[30-263]T$	TIGR00046: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
G3DSA:3.40.1280.10	$\"[87-269]T$	no description
PIRSF015601	$\"[15-269]T$	Predicted methyltransferase, slr0722 type

","BeTs to 14 clades of COG1385COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1385 is -------qvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 1","***** IPB006700 (Protein of unknown function DUF558) with a combined E-value of 2.7e-13. IPB006700A 140-158 IPB006700B 218-230 IPB006700C 244-254","Residues 1-105 are 48% similar to a () protein domain (PD789158) which is seen in Q8G5Y7_BIFLO.Residues 95-262 are 50% similar to a (UPF0088 YGGJ UNCHARACTERIZED CYTOSOLIC SURFACE XCC2885 NMA0528 RC0210 CC3415 CPE2026) protein domain (PD008210) which is seen in Q8ZHG4_YERPE.Residues 106-263 are 59% similar to a (LP_1989) protein domain (PD934249) which is seen in Q8G5Y7_BIFLO.","","-44% similar to PDB:1VHK Crystal structure of an hypothetical protein (E_value = 4.6E_16);-42% similar to PDB:1NXZ Crystal structure of H. influenzae hypothetical protein yggj_haein northeast structural genomics consortium target IR73. (E_value = 5.1E_15);-42% similar to PDB:1VHY Crystal structure of an hypothetical protein (E_value = 5.1E_15);","Residues 28 to 264 (E_value = 1.6e-60) place ANA_0544 in the DUF558 family which is described as Protein of unknown function (DUF558).","","BCR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0544.1","573911","573642","270","5.26","-2.81","9863","ATGAGTACCTATAAGACGAAGAGTGGAGCCGCGCTCACTGACGACGAGATCGAGCGACTTGGTGAGGCAGCAGAACGAGGAGAGTATCCCGGCACTCCAGGAGAGTTCATTGTTTCTCCAGGCAGGCCTCGACTCTCAGACGAGGATCTTGTCACCATTGCTTTCAAAGTGCCACGCTCACATCGAGACGCACTGGACCGTAGGGCTGAGGCGCAGGGCGAAACTCGCAGTCAGTTCATGCGAGAAGCACTCGAAAGAGCACTAGCCTGA","MSTYKTKSGAALTDDEIERLGEAAERGEYPGTPGEFIVSPGRPRLSDEDLVTIAFKVPRSHRDALDRRAEAQGETRSQFMREALERALA$","Hypothetical protein","Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 10:00:55 2007","Wed Aug 15 10:00:55 2007","Wed Aug 15 10:00:55 2007","Wed Aug 15 09:59:47 2007","","","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","Wed Aug 15 09:59:47 2007","","Wed Aug 15 09:59:47 2007","","Wed Aug 15 09:59:47 2007","yes","","" "ANA_0545","574304","574921","618","5.98","-4.38","21924","ATGAGCCCGCGGGGGCGGCGGCCGGCGGGGAGCCCGGACACGCGTGAGGCCATCCTGGCGGCGGCCCGCACCGCCTTCGCCCGCGACGGCTACCAGACCTCCCTGCGCGGCATCGCGCGCGACGCCGGAGTCGACCCGGCCCTGGTCCACCACTACTTCCCGGACCGGGCCACGCTCTTCGCCAAAGCCGTCATCGAGTCGACCGCCGGGATCGACGCCAACCTCATGCACCGGGCAGCCTCCATCACCGAGCTCGAGCCCGAGCACCTGGGGGAGGGGATCGTGCGTGCCTTCATCGGCCTGTGGGACGACGCGGGCGCGGATCGCTTCACCGCAGTCATCCACGCCGCACTCGGACAGGGCAGTGACGTCGAGCCCTTCCGTGACTTCATCGCCACCGGGATCCTCTCGCCGATCGTTACCCACTTCTGCCCCGACCGCCCCCAGCTGCGCGCCCAGCTCATCGCCAGCCAGATCATCGGTCTCGGCCTGGCCCGCTGGGTCGCCCGCATGGACCACATCGCCGGCCTCGACGCCGAGGCGGTTGTCGCGCTCGTCGGTCCCACCATCCAGCGCTACGCCTTCGACGACCTGCCCGGCCTCAACGATCCCGCCTGA","MSPRGRRPAGSPDTREAILAAARTAFARDGYQTSLRGIARDAGVDPALVHHYFPDRATLFAKAVIESTAGIDANLMHRAASITELEPEHLGEGIVRAFIGLWDDAGADRFTAVIHAALGQGSDVEPFRDFIATGILSPIVTHFCPDRPQLRAQLIASQIIGLGLARWVARMDHIAGLDAEAVVALVGPTIQRYAFDDLPGLNDPA$","Transcriptional regulator, TetR family","Cytoplasm","transcriptional regulator, TetR family domainprotein","hypothetical protein","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[18-31]T$ $\"[38-61]T$	HTHTETR
PF00440	$\"[18-63]T$	TetR_N
PS50977	$\"[12-71]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[3-63]T$	no description

","BeTs to 6 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 4.7e-09. IPB001647 17-59","Residues 29-145 are 50% similar to a (TRANSCRIPTIONAL TETR-FAMILY REGULATOR) protein domain (PDA0Z2D7) which is seen in Q6A8J3_PROAC.","","-50% similar to PDB:2NP3 Crystal structure of TetR-family regulator (SCO0857) from Streptomyces coelicolor A3. (E_value = 1.8E_13);","Residues 18 to 63 (E_value = 3.5e-10) place ANA_0545 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator, TetR family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0546","574978","575808","831","5.18","-8.17","29235","ATGAAAAGCGATGAAGGAGACGCGCCCCGGGAGTCGGGGGCCAGCAACCAATCGCACGACTCCAGTCAAGACATCACGTCCTGCTCCGCCTCGGAGCAGCCGGCCGTCACCGCGACGGACCTGCGCGTGACCCGTGGGCGCAAGGAGATCCTCCACGGCCTGGACCTGAACCTGGCGCCCGGCACCATCACCGGCCTGCTCGGCCCCTCAGGCTGCGGCAAGACCACCCTCATGCGCGCGATCGTCGGCGTCCAGCGCTACCGCGGGCGGCTCGAGGTCCTTGGGTATGCCCCCGGAGCCGCCGCCGTGCGCGGGCGGGTCGGCTACGTCACTCAGGACCAGGCCGTCTACAGAGACCTGACCGCCCGCCAGAACCTGCGCTACTTCGCCTCCCTGGCCGGCAGCCGTGCCCGCGATCTGGATGAGGTGCTTGACGTCGTCGGACTGGCCGCCCTGGCGGACCGGCCCGTGTCCACCTACTCCGGCGGCGAGGCGGGGCGCGTGAGCCTGGCCTGCGCGCTCGTGGCCGACCCCGACCTGCTCGTCATGGATGAGCCGACCGTCGGCCTGGACCCGGTCACCCGTGAGGAGCTGTGGAGCACCTTCCACGCCCTGGCTGAGCGCGGCGCCACCCTGCTGGTCTCCAGTCATGTCATGGACGAGGCCTTCCGCTGCGACCAGGTCCTCCTTATGCGCCAGGGACGCATCCTGGCCACCACCACGGCCACGGACCTCCTGGCCAGCACCGGGGCGGACACCGTGGACGCCGCCTTCCTGACCGTCATTGCCGACTCCGAGAACCAGACTGAGCAGAAAGGAGGGCAGCGCTGA","MKSDEGDAPRESGASNQSHDSSQDITSCSASEQPAVTATDLRVTRGRKEILHGLDLNLAPGTITGLLGPSGCGKTTLMRAIVGVQRYRGRLEVLGYAPGAAAVRGRVGYVTQDQAVYRDLTARQNLRYFASLAGSRARDLDEVLDVVGLAALADRPVSTYSGGEAGRVSLACALVADPDLLVMDEPTVGLDPVTREELWSTFHALAERGATLLVSSHVMDEAFRCDQVLLMRQGRILATTTATDLLASTGADTVDAAFLTVIADSENQTEQKGGQR$","ABC-type multidrug transport system, ATPase component","Membrane, Periplasm, Cytoplasm","ABC-type transporter, ATPase component","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[159-199]T$	Q8NQH9_CORGL_Q8NQH9;
PF00005	$\"[61-234]T$	ABC_tran
PS50893	$\"[36-258]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[60-235]T$	AAA

InterPro
IPR013222
Domain

Glycosyl hydrolase family 98, putative carbohydrate-binding module
SM00776	$\"[21-139]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[36-249]T$	no description
PTHR19222	$\"[36-271]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[36-271]T$	ABC TRANSPORTER

","No hits to the COGs database.","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 7.8e-24. IPB013563A 50-84 IPB013563C 157-184 IPB013563D 210-262***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 6.4e-22. IPB005074C 50-97 IPB005074D 148-191 IPB005074E 211-231***** IPB005116 (TOBE domain) with a combined E-value of 1.7e-19. IPB005116A 68-84 IPB005116B 105-122 IPB005116C 160-173 IPB005116D 180-199***** IPB010929 (CDR ABC transporter) with a combined E-value of 8.8e-13. IPB010929K 48-92 IPB010929L 94-146 IPB010929M 157-203 IPB010929A 60-79 IPB010929C 142-175***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.9e-10. IPB010509B 61-86 IPB010509D 155-199","Residues 9-229 are 40% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 29-191 are 52% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD738131) which is seen in Q830L1_ENTFA.Residues 36-217 are 47% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 36-217 are 48% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 40-197 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD962563) which is seen in Q6L0K0_PICTO.Residues 40-230 are 46% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 46-234 are 48% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 50-215 are 50% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 51-93 are 76% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8NQH9_CORGL.Residues 56-217 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 112-236 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K5M4) which is seen in Q897H9_CLOTE.Residues 113-224 are 52% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 113-236 are 54% similar to a (LACF ATP-BINDING) protein domain (PD807654) which is seen in Q9RAV2_LACLA.Residues 120-200 are 57% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA1A2W6) which is seen in Q6A6S1_PROAC.Residues 126-217 are 56% similar to a (MLC1351.18) protein domain (PD057909) which is seen in O05679_MYCLE.Residues 138-235 are 51% similar to a (GLP_170_16420_13880 ATP-BINDING) protein domain (PDA0Z2E6) which is seen in Q7R6S2_EEEEE.Residues 140-236 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 142-236 are 54% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 147-229 are 57% similar to a (ATP-BINDING TRANSPORTER ABC-TYPE ABC) protein domain (PD891090) which is seen in Q73Y59_MYCPA.Residues 147-229 are 57% similar to a (ATP-BINDING RV2326C/MT2388/MB2353C TRANSMEMBRANE ABC TRANSPORTER) protein domain (PD957860) which is seen in YN26_MYCTU.Residues 147-217 are 56% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q6LMC3_PHOPR.Residues 155-221 are 61% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18641) which is seen in Q8EG59_SHEON.Residues 156-236 are 60% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 159-199 are 87% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q8NQH9_CORGL.","","-48% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 1.6E_24);-50% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 1.6E_16);-50% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 1.6E_16);-50% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 1.6E_16);-50% similar to PDB:2AWN Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg) (E_value = 1.6E_16);","Residues 61 to 234 (E_value = 4.1e-55) place ANA_0546 in the ABC_tran family which is described as ABC transporter.","","transporter, ATPase component","","1","","","","","","","","","","","Mon Aug 13 18:33:54 2007","","Mon Aug 13 18:33:54 2007","","","Mon Aug 13 18:33:54 2007","Mon Aug 13 18:33:54 2007","Mon Aug 13 18:33:54 2007","","Mon Aug 13 18:33:54 2007","Mon Aug 13 18:33:54 2007","","","","","yes","","" "ANA_0547","575808","576554","747","7.34","0.57","27276","ATGCACCTGCGCACCTACCTGGCCACCACCCGCCGCATTCTCACCCAGCTGCGTGCCGACCGGCGCACGGTTGGCCTCATTGCGATCGTGCCGGCGGCGCTGCTGACCCTGCTGTACTTCGTCTACCGCGACTATCCCGGAGCGGACCTGCTGTTCAACCACATCGCGGTCTCCATGATGGCGATCCTGCCGACGACGGTCATGTTCCTGGTCACCAGCGTCGCCATGCTGCGTGAGCGCGTGAGCGGCACCCTGGAGCGGTTGTGGACCACTCCGATCCACCGGGCCGACCTCCTGTTCGGCTACGCCACCGCCTTCGCGATGACCGCCGTTATCCAGTCCCTCATCCTGTGCGCGGTGGCCGCCTGGGGGCTGGACGTGGATATCTCCGCCTCTTGGGGGTGGGTGGTGCTCACCGCCCTGGTGGACGCCTTCGTCGGGGTGTCCCTGGGGCTGTTGGTCTCGGCCTTCGCGCGCACCGAGTTTCAGGCCGTCCAGTTCATGCCGGTGGTCATCGCACCCCAGCTGTTCCTGTGCGGGCTCCTGGTCAGTCGCGACCAGCTGCCGCGCGTCCTGGAGGTGGTCGGTGACGCCCTGCCCATGAGCTGGGCGGTCGACGCCGTCACCGAGCTCACCATGGCCAGCGAGCCCTCTGAGGATTTCTTCCGATACCTGACCTATCTGGTCTGCTTCGGCCTGGTGGTCCTGGGAGTGGCAGCCTCCACCGTGCCGCGCAAGACCCGCTGA","MHLRTYLATTRRILTQLRADRRTVGLIAIVPAALLTLLYFVYRDYPGADLLFNHIAVSMMAILPTTVMFLVTSVAMLRERVSGTLERLWTTPIHRADLLFGYATAFAMTAVIQSLILCAVAAWGLDVDISASWGWVVLTALVDAFVGVSLGLLVSAFARTEFQAVQFMPVVIAPQLFLCGLLVSRDQLPRVLEVVGDALPMSWAVDAVTELTMASEPSEDFFRYLTYLVCFGLVVLGVAASTVPRKTR$","ABC-type multidrug transport system, permease component","Membrane, Cytoplasm","ABC-type transporter, permease components","K01992 ABC-2 type transport system permease protein","ABC-2 type transporter","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR000412
Family

ABC-2
PS51012	$\"[22-246]T$	ABC_TM2

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[18-198]T$	no description

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[3-213]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[55-77]?$ $\"[98-127]?$ $\"[133-153]?$ $\"[163-183]?$ $\"[223-243]?$	transmembrane_regions

","BeTs to 14 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","***** IPB000412 (ABC transporter, family 2) with a combined E-value of 9e-10. IPB000412A 17-40 IPB000412C 174-214","Residues 3-240 are 41% similar to a (MEMBRANE INTEGRAL) protein domain (PD315266) which is seen in Q9L1F2_STRCO.Residues 59-158 are similar to a (ABC PERMEASE TRANSPORTER MEMBRANE ATP-BINDING TRANSPORTER TRANSMEMBRANE PROTEIN COMPONENT INTEGRAL) protein domain (PD115342) which is seen in Q7TZS6_MYCBO.Residues 163-211 are similar to a (ABC PERMEASE TRANSPORTER MEMBRANE TRANSMEMBRANE ATP-BINDING TRANSPORTER INTEGRAL COMPONENT MULTIDRUG) protein domain (PD000633) which is seen in Q9X8G2_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 213 (E_value = 5e-28) place ANA_0547 in the ABC2_membrane family which is described as ABC-2 type transporter.","","transporter, permease components (membrane)","","1","","","","","","","","","","","Mon Aug 13 18:33:22 2007","","Mon Aug 13 18:33:22 2007","","","Mon Aug 13 18:33:22 2007","Mon Aug 13 18:33:22 2007","Mon Aug 13 18:33:22 2007","","Mon Aug 13 18:33:22 2007","Mon Aug 13 18:33:22 2007","","","","","yes","","" "ANA_0548","577161","579695","2535","7.11","0.67","95296","ATGTTGACGAGAACGATTAGCTTGCTTTATGGTCAGTGGGACGATCGCGTTGATTCCCTGCAAGCAAGTCGAGTCTCACGAGAGAGCAGACGTTTGTCTAACCCGTTTGATCAAAACAGACACGCTGGAGATGTGGTGAATAATTTCGAGAGTGGAAAGATATTCAGCTGGAACGATAGTTACCCTACTTCTTCAACCATACTGTCGATAACGCCGTCAGTTGTAATAATATGTTGGGCGAAGCACCTATGGTGGGCAAACCCAGCTGAATGGTGGAAGTTCAAAAATGCTGCGATAGTTGCCGCATTTGCGGGTATGATCCTGATTCCTTTGATGAGTAGCCGTTTGAAAAGGAATTATGCGCTATTTCGCGCAATCGTGATCTGGGTAGTTATCGCACTCATCGCATACACGCTACTCAGCGCAGTCTGGGGAGGAAATTTCAGGGCGGGATGGGAGGACGTCGAGTTCTCGAACTCTAGAGACCGGCTATCCAGCGTATTTACTGCAATCGGCGGAATAGGCGCAGTTGGGTATCTCGTCATAAAGTATCGCCAACAGGCGGGCTCCGAACGCGAGTTAAGTCGCTTAATTGTGAGGGAAGCCGATGACAAACTCATGCAAGCAGTTCAGCAATTAAGTTCGCATTCAGCCCAAGCGAGACTTGCTGGAGTTTATGCACTTTCCGAAATCGCAGATGTTTATGGTAGTGAAGAATATGTGACTGACTACAACAAAAGAGTTGTTGATATATTATGCGGATACCTTCGTACCAAACGGCCAAAAGATGACGGTCCTGTGGAGTCAGCGGTGGTCTCCGTGCTCAACGACCATCTATCGGAACAAAACATTGCTTACGATGGCTCAACAAATATGTCTCCAGGCCCTTGGAGTGAGTACTCTATTGACTTGCGTGGCTCGAAGTTTCGTGAGCCCTTCAGGCTCCGTAATGCGATCATCTCAGACCTTAAGGTGCAGCATTCGAAATTCGTTGACCATGTTGAATTGCATGATGTAGTATTTTCTGAGGGTGTTGATTTCGATTCCGTTCAGTTTCGCGATCTAGTTGTATTTCGAGGCGTCAATTTCTGCGGCGAGACTAAGTTTCAGGACAGCATATTTGAGAAGGATGTTACTTTTGAGGCGATTCAGGCAGGAACCCGAACAGTTTTTGCCTTTGTTGATTTTGAAGGTGTGAATTTTAAAGGACGAACAATTTTCAAGGATGTAGTCTTCGATAAAGCGACTAGATTTAAATCTAACGGCAGAGGTGTCCCAACTACCTTCTCACATGTGACGTTCAGATGTGCTACTTTGAAATCGGTAACAGCATTCATTAGCGTGAAATTTTCTGGAGAGACTGAATTCAACCGAACATGTTTTGAAGGGCCAACTAGTTTCGATGTTGATGAAACTTGTTCTCCAGTCGCCTTTATGGATGTTACCTTCCGAGATGTTGCGTTCAAATCGTTCACTACATTTAAAAACACCTTGTTCGCTGGTTCAGTGGAGTTCAATTCCGTCAAGTTCGGAGAAAACTCTAGCTTTCATCGCATTGAACTTCAGAATGTAGCCTTTAATAAGCCTGCTATTTTCAAAGAGACCGTTTTTAACGGTGTAACTACCTTCAGGAACGCAGAATTTCAGGACGTGACTGAATTTTCTTCAGTTCATTTTAAAGGCTCCTTATATGTCGGGTCCTATCAAGATAAAACAACAAAGTTCAATGCATCTAAGTTTCACGACGTAACATTCGATAGAGATGCGACATTTAGTGGAGTATACTTCGAAGGCGAGGTAGAGTTTAAGAAGGGGATATTTAAAGATGCAGTTAACTTCGGTTGTAATCGAATTCAATCTAGTGCAGTAATAAAATTGAGTAGACAGCAAAAGAATAGTGAATCTCAGGTTACCATATTCAAAGAACGAACTCTTTTTCGAGAGATTGACTTTAAGGGTCTGGCGTATTTCAACGGAGTTCAGTTTCGCGGGGATACGGAATTCTGTGAGGTAGAATTTGAGAAAGACGCCGATTTTTCCTCCTACTTGAATGTTGATAGAACCATATTCTCGGAAGTGCGCTTCGTTGATACGTCCTTCAGAAGTGAGTCGAGTTTCCGGTATGCGACGATGAGGGACGCCCATTTTATGGGGGTGGAATTTTCTGTTGTTAACTTCAATAACTGCAGTATTGAGAGAGCTTCCTTCTATAGGTCGATCCTACGAAATACTTCATTTTCAAGATTGTTCATGAAAGGGGCTAGACTAGGTGATATTACATTCTTCAGTGGAACGGAGTGCGCTGGAGTTGCCGACTTTAGTTATGCGAAGTTCGAAATCGAAGCAGACTTCTCCGGCGGCACTTTCGGTGAAGCGGCCCTATTTCGAGGCGCCATCTTCAACGCTCAATATGATGGGGACAATCCTTTTGTTTTTGGATTAGGAATTCAGGTAACTAGTCGCGGCATTCCCAAAGGGGCAAGGTGGATGAATTTTAGCGATTTAGGACTAGGTGGACGTGGTAAGTCCAAATAA","MLTRTISLLYGQWDDRVDSLQASRVSRESRRLSNPFDQNRHAGDVVNNFESGKIFSWNDSYPTSSTILSITPSVVIICWAKHLWWANPAEWWKFKNAAIVAAFAGMILIPLMSSRLKRNYALFRAIVIWVVIALIAYTLLSAVWGGNFRAGWEDVEFSNSRDRLSSVFTAIGGIGAVGYLVIKYRQQAGSERELSRLIVREADDKLMQAVQQLSSHSAQARLAGVYALSEIADVYGSEEYVTDYNKRVVDILCGYLRTKRPKDDGPVESAVVSVLNDHLSEQNIAYDGSTNMSPGPWSEYSIDLRGSKFREPFRLRNAIISDLKVQHSKFVDHVELHDVVFSEGVDFDSVQFRDLVVFRGVNFCGETKFQDSIFEKDVTFEAIQAGTRTVFAFVDFEGVNFKGRTIFKDVVFDKATRFKSNGRGVPTTFSHVTFRCATLKSVTAFISVKFSGETEFNRTCFEGPTSFDVDETCSPVAFMDVTFRDVAFKSFTTFKNTLFAGSVEFNSVKFGENSSFHRIELQNVAFNKPAIFKETVFNGVTTFRNAEFQDVTEFSSVHFKGSLYVGSYQDKTTKFNASKFHDVTFDRDATFSGVYFEGEVEFKKGIFKDAVNFGCNRIQSSAVIKLSRQQKNSESQVTIFKERTLFREIDFKGLAYFNGVQFRGDTEFCEVEFEKDADFSSYLNVDRTIFSEVRFVDTSFRSESSFRYATMRDAHFMGVEFSVVNFNNCSIERASFYRSILRNTSFSRLFMKGARLGDITFFSGTECAGVADFSYAKFEIEADFSGGTFGEAALFRGAIFNAQYDGDNPFVFGLGIQVTSRGIPKGARWMNFSDLGLGGRGKSK$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[60-80]?$ $\"[95-115]?$ $\"[121-143]?$ $\"[164-182]?$	transmembrane_regions

","BeTs to 6 clades of COG1357COG name: Uncharacterized low-complexity proteinsFunctional Class: S [Function unknown]The phylogenetic pattern of COG1357 is -o-------drlbcef-h---jx-t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 534-726 are 38% similar to a (MJ1147 TRANSMEMBRANE PLASMID VNG1732C) protein domain (PD316250) which is seen in Q82RY0_STRAW.Residues 534-726 are 38% similar to a (MJ1147 TRANSMEMBRANE PLASMID VNG1732C) protein domain (PD316250) which is seen in Q82RY0_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0549","580428","581300","873","9.24","6.06","30134","ATGTGGATCGTATTCGCTTGCGGCTCAGCGCTTTTTGCAGGCATCACCGCTGTCCTGGCTAAGGAGGGGATCCGTACCACGGACTCGACCGTGGCGACGGCGCTGCGCACTATCGTGGTGCTGGCGGGCGCCTGGGGCATGGTGTTCATCGTCGGCTCACAGGCCGAGCTGACTCACCTCGATACCCGCAGCACTGGGCTGCTGGTGTTCTCGGGGCTGGCTACCGGAGTCTCGTGGTTGTGCTACTTCAAGGCGCTCCAGCTCGGCAGCGTCAGCAAGGTCGTGCCGATCGACAAGCTGAGCACAGTGCTGACGGTGCTGCTGGCCCTCATGTTCCTGGGGGAGAGGGTGAGCCTCATCGGTGCGCTCGGAGTGGCTCTGATCGCTGTCGGAACGTTGTTGATGCTCGACGCCGACGACCTGCGCGGCCTGCCTCGGGCTGTGCGCGACGGCGGGGGCTGGCTGCTCTATGCGCTCGGCTCAGCCTTCTTCGCCGCGCTCACAGCGATTCTCGGTAAGGCCGGCATCACTGGGGTGGAGTCCAACCTCGGTACCGCGATCCGCACCGGGGTGGTCCTGGTGATGGCCTGGGTGATGGTGGCCGTCACCGGCAGGCTCCGAGAGGTCCGTAGTGTTCCGCGTGGTGAGCTCGGCTTCGTTCTGGCCTCCGGGGCAGCCACCTGTGCCTCCTGGCTCTGTTACTACCGGGCACTTCAGGACGGCCCGGCTAGCGTGGTGGTCCCCATCGACAAGCTGAGCGTCCTGGTCACCGTCCTCTTCTCCGCCCTCGTCCTGCGCGAGGCCGTCGGTAGGCGGTACCTCGCTGGGCTGGCGCTGTTCGTTGGTGGGACGCTGGCCATGCTGGTCTCCTGA","MWIVFACGSALFAGITAVLAKEGIRTTDSTVATALRTIVVLAGAWGMVFIVGSQAELTHLDTRSTGLLVFSGLATGVSWLCYFKALQLGSVSKVVPIDKLSTVLTVLLALMFLGERVSLIGALGVALIAVGTLLMLDADDLRGLPRAVRDGGGWLLYALGSAFFAALTAILGKAGITGVESNLGTAIRTGVVLVMAWVMVAVTGRLREVRSVPRGELGFVLASGAATCASWLCYYRALQDGPASVVVPIDKLSVLVTVLFSALVLREAVGRRYLAGLALFVGGTLAMLVS$","Membrane protein","Membrane, Cytoplasm","transporter, dme family BMEI0697","K08978 putative membrane protein","protein of unknown function DUF6, transmembrane","","","","","

InterPro
IPR000620
Domain

Protein of unknown function DUF6, transmembrane
PF00892	$\"[11-137]T$ $\"[163-289]T$	DUF6

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[31-51]?$ $\"[66-86]?$ $\"[117-137]?$ $\"[152-172]?$ $\"[182-202]?$ $\"[217-235]?$ $\"[269-289]?$	transmembrane_regions

","BeTs to 5 clades of COG2510COG name: Predicted membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2510 is --m-k--q-------f---n------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 1-72 are similar to a (MEMBRANE FAMILY TRANSPORTER TRANSMEMBRANE TRANSPORTER SUPERFAMILY BACTERIAL/ARCHAEAL PROTEIN EAMA SMU.1560) protein domain (PD726240) which is seen in Q8DT35_STRMU.Residues 226-285 are similar to a (MEMBRANE TRANSMEMBRANE PROTEIN INTEGRAL FAMILY TRANSPORTER DRUG/METABOLITE TRANSPORTER PERMEASE EXPORTER) protein domain (PD058316) which is seen in Q8DT35_STRMU.Residues 226-285 are similar to a (MEMBRANE TRANSMEMBRANE PROTEIN INTEGRAL FAMILY TRANSPORTER DRUG/METABOLITE TRANSPORTER PERMEASE EXPORTER) protein domain (PD058316) which is seen in Q8DT35_STRMU.","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 137 (E_value = 1.3e-17) place ANA_0549 in the DUF6 family which is described as Integral membrane protein DUF6.Residues 163 to 289 (E_value = 3e-16) place ANA_0549 in the DUF6 family which is described as Integral membrane protein DUF6.","","dme family BMEI0697 (orf6)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0549.1","583269","581902","1368","6.26","-6.01","51213","ATGGCAAAAAATACCCTCCCCTTCAAAAATAGAGTGAAGCAACTAGAGTATACATTCAAGTTAATGCTGGCTCAAAAAATTGAAGCAACTCACAACAGATTTACGTCATGGCGCCACGAGAACGACCTATTCTTCTCGATCATCAAATGGATTCTTATGGCAACAGCAGCATACACCCTACTGAACTGGATCTGGGGAGATCGAGGGATCTTCTCAGGATGGTCATTAGAGGAAAATACATCCACTCCACTAGAGAGAATCAAAGTTTCACTAACCATTCTTGGCGGGACTGGAGGTATCGGATACCTTGTCATCAAATTCCGGGAACGCTCAGCGCTCGAACGCGAAGAGGCGAACGAAAAACTTGTACGCGCAGTCCAACAACTAGGCGACGCCTCACCACAGGTTCGCATCGCAGGCGTTTATTCTTTGGCCGACGTCGCCGACACCTACGAAGGCCTATACCATCAGCGTGTTGTTGACATCCTCTGCGGCTACCTGCGTACCGACCGACTCCTCAAAGATGCGAACGGTGAAACACGTTACGCCACCCACGAAGATGGAACACCCAACCACGACCAACCACTTAGCACTGACGGGGCTGTCGAATCGACCATACTTTCCATCCTAGCAAGCCACCTCAAAGCACATTCTCGAACGAACAATGGAAAACAGTTCAGTCTCGGATCATGGAGCTCATGCAACCTCGACTTACACGGGGCCTACATTACAGAACAGGTTGATTTTACTGACACGCAGATAAGCGAAATCAACGCACAAGACACCAAGTTCTCACGCGACGTTTGTTTTTCAAGATCAACATTCACAAGAAAGGTTAACTTTCTGAATGCAAAATTTTCACAACATGCGACATTCACAGGATCGCAAATTGTATGTCTCGCGAACTTCGGAGGGGTTACATTTACTCAACTCGCCAATTTCAACAGGGCTGCATTTGTTAGCGATGCCCAGTTTACAGGCACCACCTTTGGTGGTGGCGTCCTATTTATTGAAACTCTCTTTCAGGAGTGGGCCGATTTTCAAAGCACAAAATTCATTAAGGGATGCGCATTCTTCGATACAAAGCACATTCAGGAACCCATCTTTCATGAGTCTCTATTTAACATAAAACTAAAGAATACAAAATGGTTTGCATTCTCCGAATCTATCGAACTCAACGAAGAGGGACTACCCAAAGGCGCTAAGTGGAGCGAGTTTGATGACCATGGACGCCCCATAACACCAGAGAACCGGAACAGAACGAACTTCACCGATTCCAAAGATCAGGCAGAGAAGACATCACCTACAAACAGCCCCTTGCATGGCGGGGACGAAGACAGCGGTGAGGTCACTAGCGAGATGTCCTGA","MAKNTLPFKNRVKQLEYTFKLMLAQKIEATHNRFTSWRHENDLFFSIIKWILMATAAYTLLNWIWGDRGIFSGWSLEENTSTPLERIKVSLTILGGTGGIGYLVIKFRERSALEREEANEKLVRAVQQLGDASPQVRIAGVYSLADVADTYEGLYHQRVVDILCGYLRTDRLLKDANGETRYATHEDGTPNHDQPLSTDGAVESTILSILASHLKAHSRTNNGKQFSLGSWSSCNLDLHGAYITEQVDFTDTQISEINAQDTKFSRDVCFSRSTFTRKVNFLNAKFSQHATFTGSQIVCLANFGGVTFTQLANFNRAAFVSDAQFTGTTFGGGVLFIETLFQEWADFQSTKFIKGCAFFDTKHIQEPIFHESLFNIKLKNTKWFAFSESIELNEEGLPKGAKWSEFDDHGRPITPENRNRTNFTDSKDQAEKTSPTNSPLHGGDEDSGEVTSEMS$","Hypothetical protein","Cytoplasm, Membrane","","","","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[43-65]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[45-65]?$	transmembrane_regions

InterPro
IPR003714
Family

PhoH-like protein
PF02562	$\"[199-403]T$	PhoH

InterPro
IPR004087
Domain

KH
SM00322	$\"[93-158]T$	KH

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[21-36]?$	transmembrane_regions

","BeTs to 12 clades of COG1702COG name: Phosphate starvation-inducible protein PhoH, predicted ATPaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1702 is -----z-qvdrlbcefghsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB003714 (PhoH-like protein) with a combined E-value of 2.2e-111. IPB003714A 210-251 IPB003714B 252-283 IPB003714C 303-343 IPB003714D 344-379 IPB003714E 388-402","Residues 96-218 are 46% similar to a (PHOH-LIKE) protein domain (PD820193) which is seen in Q8G5Y9_BIFLO.Residues 141-216 are 61% similar to a (PHOSPHATE PHOH PHOH-LIKE STARVATION-INDUCED STARVATION-INDUCIBLE FAMILY ATP-BINDING INDUCIBLE STARVATION PHOH) protein domain (PD191206) which is seen in Q82BX1_STRAW.Residues 219-402 are similar to a (PHOH PHOSPHATE PHOH-LIKE ATP-BINDING STARVATION-INDUCIBLE FAMILY STARVATION-INDUCED ATPASE PHOH-RELATED PREDICTED) protein domain (PD007750) which is seen in Q9L2L5_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 199 to 403 (E_value = 4.2e-137) place ANA_0550 in the PhoH family which is described as PhoH-like protein.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0551","584641","585099","459","4.64","-14.38","16593","ATGACCACTGAGGTCATCAACGAGACCACCACCGTCATCGACGCCGCCGAGTTCGCGGCCCTCGCCGACCACGTTCTGACCGCCATGCACGTCAGCCCCGCCGCCGAGCTCAACATCATGTTCATCGACCCCGAGCCCATGGAAGAGCTCCACGTGCGCTGGCTTGACCTGCCCGGCCCCACCGACGTCATGAGCTTCCCCATGGACGAGCTGCGCCCCGGCTCAGCCGACTCACCCACCCCCGCCGGGACCCTGGGCGACATCGTCCTGTGCCCGCAGGTCGCCGCCAAGCAGGCCCTGGCCGCCGGACACTCCGCCGTCGAGGAGATGCTCCTGCTCACCGTTCACGGCATCCTCCACCTCCTGGGCTACGACCACGCCGAGCCCGAGGAGAAGAAGGAGATGTTCGACCTCCAGCGCCGCCTCCTGCTGACCTTCCTGGCCGAGCGCGGCAAGTGA","MTTEVINETTTVIDAAEFAALADHVLTAMHVSPAAELNIMFIDPEPMEELHVRWLDLPGPTDVMSFPMDELRPGSADSPTPAGTLGDIVLCPQVAAKQALAAGHSAVEEMLLLTVHGILHLLGYDHAEPEEKKEMFDLQRRLLLTFLAERGK$","Metal-dependent hydrolase","Cytoplasm","conserved hypothetical protein TIGR00043","hypothetical protein","protein of unknown function UPF0054","","","","","

InterPro
IPR002036
Family

Protein of unknown function UPF0054
PD005688	$\"[47-140]T$	Q6AEC4_BBBBB_Q6AEC4;
PF02130	$\"[42-144]T$	UPF0054
TIGR00043	$\"[35-147]T$	TIGR00043: conserved hypothetical protein T
PS01306	$\"[116-126]T$	UPF0054

noIPR
unintegrated

unintegrated
G3DSA:3.40.390.30	$\"[33-151]T$	no description

","BeTs to 17 clades of COG0319COG name: Predicted metal-dependent hydrolaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0319 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002036 (Protein of unknown function UPF0054) with a combined E-value of 4.2e-37. IPB002036A 36-67 IPB002036B 84-91 IPB002036C 109-147","Residues 47-140 are similar to a (UPF0054 HYDROLASE YBEY HOMOLOG METAL METALLOENZYME MG388 AT2G25860 METAL-BINDING METAL-DEPENDENT) protein domain (PD005688) which is seen in Q6AEC4_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 42 to 144 (E_value = 2.1e-37) place ANA_0551 in the UPF0054 family which is described as Uncharacterized protein family UPF0054.","","hypothetical protein TIGR00043","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0552","585107","586393","1287","4.81","-25.27","46249","GTGACCGGCATCCCCACCGCTGCGCTCATCGCCTGCGCGGTGATCGTCCTGGCCCTGGGTGCCCTCCTGTCAGCCGGCGAGTCCGCCCTACTGCGCTTCACCCGGGCCGCCGCCGACGACCTCATCGAGGAGGGGCGCCGCGGAGCCGCCCGGGTCCGCCGCCTGGCCGAGCACCGTACCCGGGTCCTGGGTGCCCTCAGCGTCGCCCGCGTCGCCGTCGACATGCTCGCCGCCGTCCTCATCACCCTGGCCGCCTCCGGGCTCGTGCGCGCCTGGTGGCAGGTCCTCGCCCTGGCCCTGCTGGCCAACATCATCCTGCTGGGCGTCGTCGTCGGCTTCTCCCCACGCACCTACGGCCGGCGCAACCCCGCCGCCACCCTGCTCGCCCTGGGCGGCCTGCTCACCTGGGTCGACGTCCTGGCAGCCTCCCAGCGCCGCCTCGTCTCCCGCACCCGCCGCCCCGAGTCCGCCCCCACCGACGCCGAGACCCGTGAGGCCGTCAACGAGGACCTGCGCGAGATGATCGACGAGATCGGCGAGACCGACACCATCGAGGACGAGGACCGCGAGATGATGCGCTCGGTCGTCGAGCTCGGCCAGACCCTCGTGCGCGAGGTCATGGTCCCACGCACCGACATGGTCACCATCGACGCCCACAAGCCCGCCTCCGCCGCCATGCGCCTGTTCATCCGCTCCGGCTACTCGCGCGTCCCCGTCATCGGGGAGGACGCCGACGACGTGCGCGGCATCCTCTACCTCAAGGACGTCCTGCGACGCCTGGCCGCCCACCCCGAGCACGAGTCCCTCGCCGTGGCCGGATTCGCCCGGGACGCCGAGTACGTCCCCGAGATGAAACCCGCCGACGACCTCCTGCGCGAGATGCAGACCGGCCGCTTCCACATGGCCCTGGCCGTCGACGAGTACGGTGGCACCGCCGGCCTGGTCACCATGGAGGACCTCCTGGAGGAGGTCGTCGGCGAGCTCACCGACGAGCACGACCCCGAGCTGCCCGAGGTCGTCGAAGTCGCCCCCGGCACCTACCGCGTCCCCGCCCGACTCGCCCTGGACGAGCTCGGCGAGCTCTTCGACCTCGAGATCGACGACGACGACGTCGACACCGTCGGCGGCCTGCTCACCAAGGCCATCGGCCGCGTCCCCCTGCCCGGCGCCGCCGGAGACACCCAGGGCGTCCACCTCCAGGCCGAGGAGGCCACCGGCCGCCGCCGCCAGGTCTCCACTATTCTCGCCTCGCGCACCCCCGCCCCCGAAGAGGACACCGATGACTGA","VTGIPTAALIACAVIVLALGALLSAGESALLRFTRAAADDLIEEGRRGAARVRRLAEHRTRVLGALSVARVAVDMLAAVLITLAASGLVRAWWQVLALALLANIILLGVVVGFSPRTYGRRNPAATLLALGGLLTWVDVLAASQRRLVSRTRRPESAPTDAETREAVNEDLREMIDEIGETDTIEDEDREMMRSVVELGQTLVREVMVPRTDMVTIDAHKPASAAMRLFIRSGYSRVPVIGEDADDVRGILYLKDVLRRLAAHPEHESLAVAGFARDAEYVPEMKPADDLLREMQTGRFHMALAVDEYGGTAGLVTMEDLLEEVVGELTDEHDPELPEVVEVAPGTYRVPARLALDELGELFDLEIDDDDVDTVGGLLTKAIGRVPLPGAAGDTQGVHLQAEEATGRRRQVSTILASRTPAPEEDTDD$","CBS domain containing protein","Membrane, Cytoplasm","CBS domain protein","CBS domain containing protein","CBS domain containing protein","","Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 2004. 113(2):274-284. PMID: 14722619Carr G., Simmons N., Sayer J. A role for CBS domain 2 in trafficking of chloride channel CLC-5. Biochem. Biophys. Res. Commun. 2003. 310(2):600-605. PMID: 14521953Hebeisen S., Biela A., Giese B., Muller-Newen G., Hidalgo P., Fahlke C. The role of the carboxyl terminus in ClC chloride channel function. J. Biol. Chem. 2004. 279(13):13140-13147. PMID: 14718533","","","

InterPro
IPR000644
Domain

Cystathionine-beta-synthase
PF00571	$\"[207-325]T$	CBS
SM00116	$\"[212-261]T$ $\"[277-325]T$	CBS

InterPro
IPR002550
Domain

Protein of unknown function DUF21
PF01595	$\"[8-188]T$	DUF21

InterPro
IPR005170
Domain

Transporter-associated region
PF03471	$\"[340-420]T$	CorC_HlyC

noIPR
unintegrated

unintegrated
PTHR22777	$\"[42-408]T$	HEMOLYSIN-RELATED
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[4-26]?$ $\"[68-90]?$ $\"[96-114]?$ $\"[124-142]?$	transmembrane_regions

","BeTs to 20 clades of COG1253COG name: Hemolysins and related proteins containing CBS domainsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1253 is -o----yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB005170 (Transporter associated domain) with a combined E-value of 1.2e-49. IPB005170A 191-213 IPB005170B 245-257 IPB005170C 294-333 IPB005170D 368-386***** IPB002550 (CBS) with a combined E-value of 8.8e-19. IPB002550 300-331","Residues 204-254 are similar to a (CBS DOMAIN HEMOLYSIN MAGNESIUM COBALT EFFLUX CORC MEMBRANE REPEAT CONTAINING) protein domain (PD268634) which is seen in Q8G5Z1_BIFLO.Residues 271-322 are similar to a (DOMAIN CBS HEMOLYSIN MAGNESIUM COBALT CORC MEMBRANE EFFLUX PROBABLE REPEAT) protein domain (PD882202) which is seen in Q73Y12_MYCPA.Residues 276-327 are similar to a (CBS DOMAIN MEMBRANE HEMOLYSIN TRANSMEMBRANE COBALT MAGNESIUM REPEAT EFFLUX UPF0053) protein domain (PD002327) which is seen in Q8CJZ2_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 188 (E_value = 3.5e-08) place ANA_0552 in the DUF21 family which is described as Domain of unknown function DUF21.Residues 207 to 325 (E_value = 3.7e-29) place ANA_0552 in the CBS family which is described as CBS domain pair.Residues 340 to 420 (E_value = 8e-18) place ANA_0552 in the CorC_HlyC family which is described as Transporter associated domain.","","domain protein (tlyC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0553","586485","587669","1185","4.71","-29.54","42749","ATGCCCGCGCCCGGCCCCGCCCCGGCCGGCTTCCGCTTCCCCACCGACGCCGAGCTCATGGACGGCCCCAACCCGCTCACCGACCCCGACGACGAGGAAGACGGCGAGGACGAGCCCGGCGATGACTCTGACGGCGAGGACGACGACTCCGATGCCGCCATCCGGCTGGACGCGGACGGCTTCCCGATCCTGGACGAGGACGACGACACGGAAGAGAGCGCCGATATCACGGATTCGGCCCGCGTCGAGATCGTCGTCCCCGACTTCCCCGAGGACTTCCGCGCCGGCTTCGCCTGCATCGTGGGCCGCCCCAACGCCGGCAAGTCCACCCTCACCAACGCCATGGTCGGCGCCAAGATCGCCATCACCTCCGGGCGCCCCCAGACCACCCGCCACAACGTGCGCGGCGTCATCCACAAGGACAACGCGCAGATCGTCCTGGTCGACACCCCCGGTCTCCACCGCCCCCGCACCCTGCTGGGCAAGCGCCTCAACGACCTGGTGCGCGAGACCCTCGTCGACGTCGACGTCGTCGTCTTCTGCATCCCCGCCAACGAGAAGATCGGCCCCGGCGACCGCTTCATCACCCGCGACCTCGCCGAACTGCGCACCCCCGTGGTCGCCGTAGTCACGAAGGCCGACACCGTCACCCGAGAGGCCCTGGCCGCCCAGCTCCTGGCCGTCAGCGAGCTGGGGGAGTGGGCCGACATCGTCCCGGTCTCAGCCCAGCGCAACGAGCAGATCGACGTCCTGGAGGAGGTCCTTCTCAAGTACATGCCCCTGTCCCCGCCGCTGTACCCCACCGGCGAGATCACCGACGAGCCCCAGCAGGTCATGATCGCCGAGCTCGTGCGCGAGGCCGCCCTGGAGGGCGTGCGCGACGAGCTGCCCCACTCCCTGGCCGTCGTCGTCGACGAGATCGCCGACCCCGACGACGAGCGCGAGGTCGGACACATCAAGGGCGCCGGGGGCCGCCTCCAGGTGCGCGTGAGCCTCGTCGTCGAACGCGACTCCCAGAAGGCCATCATCATCGGCAAGGGCGGACGGCGCCTCAAGGAAGTGGGCGTCACCGCCCGCAAGGGCATCGAGAAGCTGCTGGGGCGCAAGGTCTACCTCGACCTGCACGTGCGCACCGCCAAGGACTGGCAGTCCGACCCCAAGGCCCTGGCCCGCCTCGGCTTCTGA","MPAPGPAPAGFRFPTDAELMDGPNPLTDPDDEEDGEDEPGDDSDGEDDDSDAAIRLDADGFPILDEDDDTEESADITDSARVEIVVPDFPEDFRAGFACIVGRPNAGKSTLTNAMVGAKIAITSGRPQTTRHNVRGVIHKDNAQIVLVDTPGLHRPRTLLGKRLNDLVRETLVDVDVVVFCIPANEKIGPGDRFITRDLAELRTPVVAVVTKADTVTREALAAQLLAVSELGEWADIVPVSAQRNEQIDVLEEVLLKYMPLSPPLYPTGEITDEPQQVMIAELVREAALEGVRDELPHSLAVVVDEIADPDDEREVGHIKGAGGRLQVRVSLVVERDSQKAIIIGKGGRRLKEVGVTARKGIEKLLGRKVYLDLHVRTAKDWQSDPKALARLGF$","GTP-binding protein Era","Cytoplasm","Era-like GTP-binding protein.","GTP-binding protein Era","GTP-binding protein Era","","Wimberly B.T., Brodersen D.E., Clemons W.M., Morgan-warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V. Structure of the 30S ribosomal subunit. Nature 2000. 407(6802):327-339. PMID: 11014182Chen X., Court D.L., Ji X. Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(15):8396-8401. PMID: 10411886Worbs M., Bourenkov G.P., Bartunik H.D., Huber R., Wahl M.C. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol. Cell 2001. 7(6):1177-1189. PMID: 11430821","","","

InterPro
IPR002917
Domain

GTP-binding protein, HSR1-related
PF01926	$\"[96-214]T$	MMR_HSR1

InterPro
IPR004044
Domain

KH, type 2
PF07650	$\"[330-394]T$	KH_2
PS50823	$\"[292-380]T$	KH_TYPE_2

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[93-257]T$	small_GTP: small GTP-binding protein domain

InterPro
IPR005662
Family

GTP-binding protein Era
TIGR00436	$\"[96-377]T$	era: GTP-binding protein Era

InterPro
IPR009019
Domain

KH, prokaryotic type
G3DSA:3.30.300.20	$\"[275-394]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[88-270]T$	no description
PTHR11649	$\"[90-387]T$	MSS1/TRME-RELATED GTP-BINDING PROTEIN
PTHR11649:SF3	$\"[90-387]T$	GTP-BINDING PROTEIN ERA

","BeTs to 17 clades of COG1159COG name: GTPasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1159 is -------qvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 2","***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 3.5e-15. IPB002917 100-132***** IPB006073 (GTP1/OBG GTP-binding protein family signature) with a combined E-value of 1.1e-12. IPB006073A 98-118 IPB006073B 120-138","Residues 100-145 are 69% similar to a (RNA-BINDING GTP-BINDING GTPASE ERG ERA-LIKE G-PROTEIN-LIKE ERAL1 ENRICHED RAS-LIKE SEQUENCE) protein domain (PDA0A038) which is seen in ERG_ARATH.Residues 100-195 are 50% similar to a (GTP-BINDING ERA RNA-BINDING HOMOLOG CHROMOSOME II E02H1.2) protein domain (PD035950) which is seen in Q7NB86_MYCGA.Residues 100-131 are 93% similar to a (GTP-BINDING TRNA ENGA REPEAT GTPASE RNA-BINDING MODIFICATION TRME PROBABLE ERA) protein domain (PD000414) which is seen in ERA_MYCTU.Residues 141-171 are 96% similar to a (GTP-BINDING RNA-BINDING ERA HOMOLOG MEMBRANE PHOSPHORYLATION BEX SYNTHETASE FAMILY BINDING) protein domain (PD522451) which is seen in ERA_MYCTU.Residues 182-255 are 73% similar to a (GTP-BINDING RNA-BINDING HOMOLOG ERA WIDELY GTP ERA/THDF FAMILY BEX ERA-LIKE) protein domain (PD582763) which is seen in ERA_STRCO.Residues 259-377 are 73% similar to a (GTP-BINDING RNA-BINDING ERA HOMOLOG MEMBRANE GTPASE PHOSPHORYLATION ERA-LIKE ERG FAMILY) protein domain (PD004541) which is seen in Q73Y13_MYCPA.","","-55% similar to PDB:1WF3 Crystal structure of GTP-binding protein TT1341 from Thermus thermophilus HB8 (E_value = 1.1E_48);-50% similar to PDB:1EGA CRYSTAL STRUCTURE OF A WIDELY CONSERVED GTPASE ERA (E_value = 7.0E_38);-50% similar to PDB:1X1L Interaction of ERA,a GTPase protein, with the 3'minor domain of the 16S rRNA within the THERMUS THERMOPHILUS 30S subunit. (E_value = 7.0E_38);-50% similar to PDB:1X18 Contact sites of ERA GTPase on the THERMUS THERMOPHILUS 30S SUBUNIT (E_value = 7.7E_37);","Residues 96 to 214 (E_value = 5.2e-35) place ANA_0553 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 330 to 394 (E_value = 1.3e-22) place ANA_0553 in the KH_2 family which is described as KH domain.","","GTP-binding protein. (GTPase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0554","587826","591398","3573","5.45","-26.91","127304","ATGACGAACACCGCCGTTCCCAGTCATCCCCGCACCGACTCAGGTAACGCAGAACGCCGCTGCCCCGACGACCTGTGGGCGCTGGGCGAGAAAGCCGTCGCCCGAGCACGCCGGTGGGCTGACGAGTCGGCATCCGAGCCGGTACCGCGCTCAGCCAAGCTCCTTTCCCGCATCCTCTCCGACCCCGAGGGCCTGACCTTCACCACCCGCTTCGTCGACGACGTCGTGCGTCCCACCGACCTCGACGTCGCCAGCACCGCCCTCAAGCGCCTGTCGGCAGGGCGCACAGACTTCCTGCCGCCCGCCCTGGCCGGGGCCATGGGGCTGGGCTCGGCCGCCTCCCGCCTCGCCCCGCGCACCGTCACCGCGGTCGCCCGGCGAGTCTTCCGCGAGATCGTCGGGGACCTCGTCGTCGACGCCACCGACAAGGGACTCGGGCCCGCCCTCGCCCGCCTGCGCAAGGGCGGCAACCGCCTCAACGTCAACCTCCTGGGCGAGGCCGTCCTGGGGGAGAAGGAGGCCTCCCGCCGCCTGGCTGAGGTCTCCCGCCTGGTCACCCGCGAGGACGTCGACTACGTCTCGGTCAAGGTCTCCGCCGTCACCGGTCCCCACAACCCCTGGGGTTTCGAGGAGGTCGTCACCCACGGCGTCCAGGCCCTCCTGCCCCTCTACCGCCTGGCCCGCGACCACGGCACCTTCCTCAACCTGGACATGGAGGACTACAAGGACCTGGACCTGACCATCGCGGTCTTCACCGCGATCCTCGACCAGGAGGACATGCGCGGCTACGAGGCCGGCATCGTCCTGCAGGCCTACCTGCCCGACTCCCTGGGCGCCATGCAGCGCCTCCAGGAGTGGGCCGCCAAGCGTGTCGCCTCCGGTGGATCACGCGTCAAGGTCCGCATCGTCAAGGGCGCCAACCTGTCCATGGAGAAGGTCGACGCCGAGATCCACGGCTGGGAGCTGACCACCTGGCCCTCCAAGCAGGCCACCGACACCAACTACAAGCGCATGCTCTCCTGGGCGATGACGCCCGAGCGCACCCGCAACATCCGCCTGGGCGTGGCCGGCCAGAACCTCTTCGACATCGCCTTCGCCTTCGAGCTGCGCGCCGCACGCGGTGTCGAGGACAGCGTCGAGTTCGAGATGCTCTCCGGCATGGCCACCGGCATCCAGGAGGTCGTGCGCCGCGACACCGGACACCTCCTGCTGTACGTGCCCGTCGTCGACCCCCACGAGTTCGACGTCGCCATCTCCTACCTGGTGCGCCGTCTGGAGGAGAACGCGGCGCCGGAGAACTTCATGTCCGGCGTCTTCGACCTGGCCAGCAACGAGCAGATCTTCGCCCGCGAGCGCGACCGCTTCCTGGCGGCCCTGTCCGACCTCGACCCGGACGCCCCGGTGCCGGTGCCCAACCGCACCCAGAACCGGCTCGCCGAGCGGGAGGCGGGCATCCCTGAGGAGACCGGCACGGTCGCCGAGCGCGCCAGGAGGTCCTTCGTCTCCGAGGCCGACTCCGACCCGGCCCTGGCCGCCAACCGCCAGTGGGCTCGGGACATCGCTGCCGCCATCCCGGGATCCACGCGGGGCGTGGCCGAGGTGGAGGCCGGCGCCGCCCGCCTGGCCACGAACGCCGACGTCGACTCCCTGGTGGCCTCCACGGCCGAGGCGGCCGGCGTCTGGCAGTCCCTGGACCCAGCCGAGCGGGCCGCCGCCCTGCACCGGGTCGGCGATGTCCTGGCCGCCCGGCGCGCCGAGCTCATCGAGGTCGCCGGCTCCGAGGCCGGCAAGACCATCGACCAGTCCGACCCCGAGGTCAGTGAGGCCATCGACTTCTGCCACCACTACGCGGAGTCCTCGCTGCTCCTGCACGACCCGGAGTACATGGTCGGGGCCCGCTTCGCCCCGGTGGACGTCACCGTGGTCGCCTCGCCCTGGAACTTCCCGGTGGCCATCCCCACCGGGGGAGTGGCCGCGGCCCTGGCGGCCGGCAGCGCCGTCATCCTCAAGCCCGCCCCGCCGGCCCGACGCTGCGCGGCCGAGCTCGTGCGCGCCTTCCACGACGCCGGGATCCCCGAGGACCTCGTGGCGCTCGCCCCGCTGGAGGACGGAGAGGTCTCACGCCACCTGGTGACCCACAAGGACGTCGACCGCGTGGTCCTCACCGGCTCCTACGACACGGCCCGCCTCTTCCGCTCCTGGAAGCCGGACATGCACCTGCTGGGGGAGACCAGCGGCAAGAACGCCATCATCGTCACCCCCTCGGCCGACCCCGACATCGCCGTGCGCGACGCGGTCTACTCGGCCTTCGCCCACGCCGGCCAGAAGTGCTCGGCCTCCTCCCTGCTGGTCCTGGTCTCCTCGGCCGGCAAGTCCGAGCGCATCGCCCGCCAGCTCGTGGACGCCACCGCCTCCCTGCGGGTGCGCCTGCCGCTGTCGCTGGACTCCCAGATGGGGCCCGTCGTCGTGCCCGACGACGAGAAGGCCGTGCGCGGCCTGACCACCCTGGGGGTTGGTGAGCACTGGGTCCTCAAGCCCCGCTACCTCGGCGACGGTCTGTGGACCCCGGGTATTCGCGCCGGGGTCGTGCCCGGTAGCGAGTTCCACCTCACCGAGTACTTCGCGCCGGTCATCGGCGTCATGCGGGTCGACACGCTCGAGGAGGCCATCGAGGCGGTCAACGCCGTCGACTACGGGCTCACCTCCGGGCTCCAGACCCTCGACGCGGCCGAGCTGGCCGTCTGGCTCGACTCCATCCAGGCCGGCAACATCTACGTCAACCGCGGTATCACCGGGGCCATCGTGCGCCGCCAGCCCTTCGGCGGCTGGAAGCGCTCGGCCATCGGCTCGACGACGAAGGCCGGCGGCCCCTCCTACCTGCTGGGACTGGGGGACATCGAGCCCGCAGACGGCCAGGACGTGAAGGAACTGGAGGGCCAGGGCACTGCGGCGCTCGACCCGCGCGTGGCGAGCCTGTGCGACGCCGTCAGCGGCCAGCTGGGCGAGGCCGACCTGGCCGGGCTGCGTCGCGCCCTGGTGGCCGACGCCTCCGCCTGGAGGAGCGCCTACGGCGTCAACCGTGACGTCACGGCACTGGCCTGCGAGCGCAACGTCCTGCGCTACCGGCCCACTGACGTGCTCGTGCGCGCCGGGGTGGGAACCGAGCTGGCCGACGTCGTGCGCGTCATGGCGGCCGGTGTGCGGGCCGGTGGGTTCGTCAGCCTGTCCGTGGCCGACCGTCTGCCCCAGCCGTTGCAGAACGCGCTGCAGGCCGCCGGCGTCCAGGTGGCGGTCGAGGACCAGGGAGCCTGGGACGCCCGTCTGGCTGAGCTCTCCGCCTCCGGCGGGCTGGGAACGCGCGTGCGCATCCTCGGCCCGCGTGAGGAGACTTCCGCCGCACGCTGGAGCCACGCCAGTCGGGTGACTGGCGGAAGCCCCGACATCGCCCTGTACACGGGGTCGGTGACGGCCTGCCCGCACTCCGAGCTGCTGCCCTTCCTGCGCGAGCAGGCGGTGGCCATCACCAACCACCGCTTCGGCACCCCGCTGGACCTGGCCGAGGGCCTCCTGTAG","MTNTAVPSHPRTDSGNAERRCPDDLWALGEKAVARARRWADESASEPVPRSAKLLSRILSDPEGLTFTTRFVDDVVRPTDLDVASTALKRLSAGRTDFLPPALAGAMGLGSAASRLAPRTVTAVARRVFREIVGDLVVDATDKGLGPALARLRKGGNRLNVNLLGEAVLGEKEASRRLAEVSRLVTREDVDYVSVKVSAVTGPHNPWGFEEVVTHGVQALLPLYRLARDHGTFLNLDMEDYKDLDLTIAVFTAILDQEDMRGYEAGIVLQAYLPDSLGAMQRLQEWAAKRVASGGSRVKVRIVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMTPERTRNIRLGVAGQNLFDIAFAFELRAARGVEDSVEFEMLSGMATGIQEVVRRDTGHLLLYVPVVDPHEFDVAISYLVRRLEENAAPENFMSGVFDLASNEQIFARERDRFLAALSDLDPDAPVPVPNRTQNRLAEREAGIPEETGTVAERARRSFVSEADSDPALAANRQWARDIAAAIPGSTRGVAEVEAGAARLATNADVDSLVASTAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLHDPEYMVGARFAPVDVTVVASPWNFPVAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVALAPLEDGEVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAGKSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGVGEHWVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLEEAIEAVNAVDYGLTSGLQTLDAAELAVWLDSIQAGNIYVNRGITGAIVRRQPFGGWKRSAIGSTTKAGGPSYLLGLGDIEPADGQDVKELEGQGTAALDPRVASLCDAVSGQLGEADLAGLRRALVADASAWRSAYGVNRDVTALACERNVLRYRPTDVLVRAGVGTELADVVRVMAAGVRAGGFVSLSVADRLPQPLQNALQAAGVQVAVEDQGAWDARLAELSASGGLGTRVRILGPREETSAARWSHASRVTGGSPDIALYTGSVTACPHSELLPFLREQAVAITNHRFGTPLDLAEGLL$","Bifunctional proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase (PutA)","Cytoplasm","NAD-dependent aldehyde dehydrogenases","proline dehydrogenase ","aldehyde dehydrogenase","","Ling M., Allen S.W., Wood J.M. Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein. J. Mol. Biol. 1994. 243(5):950-956. PMID: 7966312","","","

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PF00171	$\"[516-955]T$	Aldedh
PS00070	$\"[770-781]?$	ALDEHYDE_DEHYDR_CYS
PS00687	$\"[742-749]?$	ALDEHYDE_DEHYDR_GLU

InterPro
IPR002872
Domain

Proline dehydrogenase
PF01619	$\"[105-442]T$	Pro_dh

InterPro
IPR003833
Domain

Allophanate hydrolase subunit 1
SM00796	$\"[740-960]T$	no description

InterPro
IPR011350
Family

Bifunctional proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase (PutA)
PIRSF000197	$\"[6-1188]T$	Bifunctional proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase (PutA)

InterPro
IPR015590
Domain

Aldehyde Dehydrogenase_
PTHR11699	$\"[553-967]T$	ALDEHYDE DEHYDROGENASE-RELATED

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.220	$\"[138-475]T$	no description
G3DSA:3.40.605.10	$\"[509-779]T$	no description
PTHR11699:SF16	$\"[553-967]T$	BIFUNCTIONAL PUTA PROTEIN

","BeTs to 18 clades of COG1012COG name: NAD-dependent aldehyde dehydrogenasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1012 is -omp-zyq-drlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 3","***** IPB002086 (Aldehyde dehydrogenase) with a combined E-value of 5.9e-44. IPB002086A 635-676 IPB002086C 748-796 IPB002086D 853-906 IPB002086E 929-953***** IPB011264 (Betaine aldehyde dehydrogenase) with a combined E-value of 5.6e-24. IPB011264A 536-575 IPB011264C 633-671 IPB011264E 740-793 IPB011264G 865-903***** IPB002872 (Proline dehydrogenase) with a combined E-value of 1.6e-14. IPB002872A 274-311 IPB002872B 353-372 IPB002872C 408-428","Residues 58-200 are 64% similar to a (DEHYDROGENASE PROLINE OXIDOREDUCTASE DEHYDROGENASE/DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASES ALDEHYDE NAD-DEPENDENT DELTA-1-PYRROLINE-5-CARBOXYLATE / 1-PYRROLINE-5-CARBOXYLATE) protein domain (PD575778) which is seen in Q6AH48_BBBBB.Residues 207-268 are 68% similar to a (DEHYDROGENASE PROLINE OXIDOREDUCTASE DEHYDROGENASES / ALDEHYDE NAD-DEPENDENT 1-PYRROLINE-5-CARBOXYLATE PYRROLINE-5-CARBOXYLATE BIFUNCTIONAL) protein domain (PD871030) which is seen in Q6AH48_BBBBB.Residues 234-388 are 73% similar to a (PROLINE DEHYDROGENASE OXIDOREDUCTASE OXIDASE BIFUNCTIONAL PUTA DEHYDROGENASE/DELTA-1-PYRROLINE-5-CARBOXYLATE DELTA-1-PYRROLINE-5-CARBOXYLATE P5C PEPTIDE) protein domain (PD008672) which is seen in Q8NU48_CORGL.Residues 398-517 are 63% similar to a (DEHYDROGENASE PROLINE OXIDOREDUCTASE DEHYDROGENASE/DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASES ALDEHYDE NAD-DEPENDENT DELTA-1-PYRROLINE-5-CARBOXYLATE / 1-PYRROLINE-5-CARBOXYLATE) protein domain (PD129147) which is seen in Q8NU48_CORGL.Residues 499-992 are 43% similar to a (ALDEHYDE DEHYDROGENASE) protein domain (PD449341) which is seen in Q98DB0_RHILO.Residues 506-960 are 41% similar to a (BENZALDEHYDE DEHYDROGENASE) protein domain (PD722867) which is seen in Q9A5Q0_CAUCR.Residues 506-960 are 46% similar to a (DEHYDROGENASE PROLINE) protein domain (PD575773) which is seen in Q52711_RHOCA.Residues 510-956 are 40% similar to a (OXIDOREDUCTASE SUCCINATE-SEMIALDEHYDE DEHYDROGENASES ALDEHYDE DEHYDROGENASE PROBABLE NAD-DEPENDENT) protein domain (PDA188E8) which is seen in Q8NM66_CORGL.Residues 525-777 are 45% similar to a () protein domain (PD948750) which is seen in Q73V72_MYCPA.Residues 525-927 are 41% similar to a (MMCL) protein domain (PDA0J2C7) which is seen in Q9X5T0_STRLA.Residues 526-960 are 43% similar to a (OXIDOREDUCTASE DEHYDROGENASE ALDEHYDE PLASMID) protein domain (PDA0J2D0) which is seen in Q6W1I3_RHISN.Residues 535-642 are 53% similar to a (DEHYDROGENASES ALDEHYDE OXIDOREDUCTASE NAD-DEPENDENT) protein domain (PDA1B3Y1) which is seen in Q6AA40_PROAC.Residues 537-949 are 40% similar to a (DEHYDROGENASE VANILLIN) protein domain (PD723371) which is seen in Q84IP9_PSEPA.Residues 537-960 are 44% similar to a (MEIOTIC OXIDOREDUCTASE UP-REGULATED DEHYDROGENASE PROBABLE BADH MEIOSIS ALDEHYDE EXPRESSION NAD) protein domain (PDA0J2D1) which is seen in DHAB_SCHPO.Residues 539-949 are 42% similar to a (ALDEHYDE ALDY DEHYDROGENASE) protein domain (PDA193O6) which is seen in P94358_BACSU.Residues 542-960 are 46% similar to a (1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE) protein domain (PD243617) which is seen in Q9RZC4_DEIRA.Residues 542-961 are 49% similar to a (PREDICTED PROLINE DEHYDROGENASE) protein domain (PD297252) which is seen in Q9F7Q7_PRB01.Residues 542-962 are 42% similar to a (PHENYLACETALDEHYDE OXIDOREDUCTASE DEHYDROGENASE SEQUENCING DIRECT NAD PAD) protein domain (PDA0J2C9) which is seen in FEAB_ECOLI.Residues 542-949 are 42% similar to a (ALDEHYDE DEHYDROGENASE PROBABLE) protein domain (PD723136) which is seen in Q9I5I2_PSEAE.Residues 543-956 are 42% similar to a (F45H10.1) protein domain (PDA181A7) which is seen in O02266_CAEEL.Residues 545-949 are 42% similar to a (DEHYDROGENASE ALDEHYDE) protein domain (PD728494) which is seen in Q9RYT8_DEIRA.Residues 546-959 are 69% similar to a (DEHYDROGENASE OXIDOREDUCTASE ALDEHYDE SEMIALDEHYDE PROLINE NADP REDUCTASE GAMMA-GLUTAMYL PHOSPHATE GPR) protein domain (PD250846) which is seen in Q8FUB9_COREF.Residues 547-942 are 42% similar to a (DEHYDROGENASE NAD METABOLISM PROLINE P5C OXIDOREDUCTASE DELTA-1-PYRROLINE-5-CARBOXYLATE) protein domain (PDA185E9) which is seen in PUT2_AGABI.Residues 828-881 are 75% similar to a (DEHYDROGENASES ALDEHYDE PROLINE OXIDOREDUCTASE DEHYDROGENASE NAD-DEPENDENT) protein domain (PD931127) which is seen in Q6AH48_BBBBB.Residues 886-942 are 89% similar to a (PROLINE DEHYDROGENASE/DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASES ALDEHYDE OXIDOREDUCTASE DEHYDROGENASE ORFV NAD-DEPENDENT DEHYDRAOGENASE) protein domain (PD824973) which is seen in Q6AH48_BBBBB.Residues 943-1018 are 59% similar to a (DEHYDROGENASE PROLINE) protein domain (PDA020W7) which is seen in Q6AH48_BBBBB.Residues 944-1180 are 48% similar to a (DEHYDROGENASE PROLINE OXIDOREDUCTASE DEHYDROGENASE/DELTA-1-PYRROLINE-5-CARBOXYLATE DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASES / ALDEHYDE NAD-DEPENDENT 1-PYRROLINE-5-CARBOXYLATE) protein domain (PD116251) which is seen in Q6AA40_PROAC.","","-45% similar to PDB:1UZB 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE (E_value = 2.6E_44);-45% similar to PDB:2BHP CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND NAD. (E_value = 1.0E_43);-45% similar to PDB:2BHQ CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND PRODUCT GLUTAMATE. (E_value = 1.0E_43);-45% similar to PDB:2BJA CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND NADH (E_value = 1.0E_43);-45% similar to PDB:2BJK CRYSTAL ANALYSIS OF 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FROM THERMUS WITH BOUND NAD AND CITRATE. (E_value = 1.0E_43);","Residues 105 to 442 (E_value = 1e-33) place ANA_0554 in the Pro_dh family which is described as Proline dehydrogenase.Residues 516 to 955 (E_value = 1.3e-88) place ANA_0554 in the Aldedh family which is described as Aldehyde dehydrogenase family.","","aldehyde dehydrogenases (U39263)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0554.1","591563","591802","240","4.30","-9.08","8442","ATGAAGCTAAGCGTGAGTTTGTCGGAGAGTGACCTCATTCTGCTGGACCGATGCGTGGAGCGTGACGGTTTGGCGTCGAGGTCCGCTGGTATTCAGAACGCCATCCGCCTGCTCGGAAAAGCTGATCTTCAGGATGCTTACGCTGAGGCCTGGTCCTCCTGGGATACCTCTGAGGATGCAACCGTCTGGGATAGTGCGGTCGCCGACGGGATCGATGGAGGTGAGGATGCTACGAGGTGA","MKLSVSLSESDLILLDRCVERDGLASRSAGIQNAIRLLGKADLQDAYAEAWSSWDTSEDATVWDSAVADGIDGGEDATR$","Transcriptional regulator, CopG family","Periplasm, Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Thu Aug 16 09:53:42 2007","Thu Aug 16 09:53:42 2007","Thu Aug 16 09:53:42 2007","Fri Aug 10 19:05:33 2007","","","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","Fri Aug 10 19:05:33 2007","","Fri Aug 10 19:05:33 2007","","Fri Aug 10 19:05:33 2007","yes","","" "ANA_0554.2","591789","592136","348","9.53","2.41","12310","ATGCTACGAGGTGAAATCCGCCTTGTCGATTTTGATCCTTCTGTTGGCAGTGAGGCAAACAAGCGTCGACCTGCGCTCATAGTAAGTAATGACCATGCCAATGCGGCGGCTGCGCGTCTTGGTCGCGGCGTGGTGACGGTGATCCCATTGACCAGCTCAACCTCGCGAGTTCTTCCCTTTCAGGTTTTCCTCCCCTCGGAGGCAACTGGCTTGCCCAAGGACTCCAAGGCTCAGGCGGAGCAAGTTCGATCGATTGCCGTGGAGAGAGTCGGCGAGGTTGTCGGCTGGTTACCCAGTGGCCTGATGAAGATGGTCAATGAGGCTCTGATCCTGCATCTCTCCTTGTGA","MLRGEIRLVDFDPSVGSEANKRRPALIVSNDHANAAAARLGRGVVTVIPLTSSTSRVLPFQVFLPSEATGLPKDSKAQAEQVRSIAVERVGEVVGWLPSGLMKMVNEALILHLSL$","PemK protein","Cytoplasm, Membrane","","","","","Zhang J, Zhang Y, Zhu L, Suzuki M, Inouye M.Interference of mRNA function by sequence-specific endoribonuclease PemK.J Biol Chem. 2004 May;279(20):20678-84.PMID: 15024022Hargreaves D, Santos-Sierra S, Giraldo R, Sabariegos-Jareño R, de la Cueva-Méndez G, Boelens R, Díaz-Orejas R, Rafferty JB.Structural and functional analysis of the kid toxin protein from E. coli plasmid R1.Structure. 2002 Oct;10(10):1425-33.PMID: 12377128Kamada K, Hanaoka F, Burley SK.Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition.Mol Cell. 2003 Apr;11(4):875-84.PMID: 12718874","","","

InterPro
IPR003477
Family

PemK-like protein
PF02452	$\"[2-114]T$	PemK

InterPro
IPR011067
Family

Plasmid maintenance toxin/Cell growth inhibitor
G3DSA:2.30.30.110	$\"[1-114]T$	no description

","BeTs to 6 clades of COG2337COG name: Growth inhibitorFunctional Class: TThe phylogenetic pattern of COG2337 is -----q--eB-h----o-IN-Number of proteins in this genome belonging to this COG is","***** IPB003477 (PemK-like protein) with a combined E-value of 1.2e-10. IPB003477A 23-41 IPB003477B 70-98","Residues 4-95 are similar to a (PEMK PLASMID FAMILY GROWTH PEMK-LIKE DNA-BINDING TRANSCRIPTIONAL REGULATOR INHIBITOR PPGPP-REGULATED) protein domain (PD290566) which is seen in Q7TXU4_MYCBO.","","","Residues 2 to 114 (E_value = 3.2e-37) place ANA_0554.2 in the PemK family which is described as PemK-like protein.","","","","1","","Fri Aug 10 19:09:11 2007","Fri Aug 10 19:09:11 2007","Fri Aug 10 19:09:11 2007","Fri Aug 10 19:09:11 2007","Fri Aug 10 19:09:11 2007","Fri Aug 10 19:09:11 2007","Thu Aug 16 09:54:52 2007","Thu Aug 16 09:54:52 2007","Thu Aug 16 09:54:52 2007","Fri Aug 10 19:09:11 2007","","Mon Aug 20 18:05:52 2007","Fri Aug 10 19:09:11 2007","Fri Aug 10 19:09:11 2007","Mon Aug 20 18:05:52 2007","Fri Aug 10 19:09:11 2007","Mon Aug 20 18:05:52 2007","Fri Aug 10 19:09:11 2007","Fri Aug 10 19:09:11 2007","Mon Aug 20 18:05:52 2007","","Fri Aug 10 19:09:11 2007","","Fri Aug 10 19:09:11 2007","yes","","" "ANA_0555","592374","592144","231","6.79","-0.35","8741","GTGACCATGTCCGACGATGTCGTCCACAACCGGATCGCTGTCCTGCGCGCCGACCGCCGGGTGAGTCGCCGAGAGCTCGCTGAGGCACTCGGCGTCCACTACCAGACGGTGGGCTACCTCGAGCGCGGGGAGTACGCCCCCTCGCTGCACCTGGCCCTGCGTATCGCCCGCTACTTCGACGTGCCCGTGGAGTCGGTCTTCTCCCTGGAGGAGTTCCCCCGCCTGACGTGA","VTMSDDVVHNRIAVLRADRRVSRRELAEALGVHYQTVGYLERGEYAPSLHLALRIARYFDVPVESVFSLEEFPRLT$","Transcriptional regulator, XRE family","Cytoplasm","transcription regulator, HTH_3 family","DNA-binding protein","helix-turn-helix domain protein","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[12-66]T$	HTH_3
SM00530	$\"[11-66]T$	HTH_XRE
PS50943	$\"[12-66]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[7-72]T$	no description

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[7-218]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[55-77]?$ $\"[111-133]?$ $\"[139-159]?$ $\"[168-188]?$ $\"[233-253]?$	transmembrane_regions

","BeTs to 12 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","***** IPB000412 (ABC transporter, family 2) with a combined E-value of 1.8e-07. IPB000412C 179-219","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 7 to 218 (E_value = 0.00084) place ANA_0556 in the ABC2_membrane family which is described as ABC-2 type transporter.","","membrane protein","","1","","","","","","","","","","","Mon Aug 13 18:34:38 2007","","Mon Aug 13 18:34:38 2007","","","Mon Aug 13 18:34:38 2007","Mon Aug 13 18:34:38 2007","","","Mon Aug 13 18:34:38 2007","Mon Aug 13 18:34:38 2007","","","","","yes","","" "ANA_0557","594058","593204","855","5.32","-10.13","31099","ATGACTCCAGTCATCACCACGGAGAACCTCGAGTTCTCCTACGGGGACACCCCGGTGCTGCGTGGCATCGACCTGTCGGTCGAGGCCGGCGAGGTCGTCTGCCTGCTCGGCCCCAACGGCGTGGGCAAGACGACCCTCGTGGAGAACCTGCTGGGCTCTCTGACCCCGACCAGCGGCAGGGTGCGCGTGCTCGACACCGATCCGCGTCGGGCGGGCGCCGACTTCTGGGCGAGGGTCGGGCTGGTGCAGCAGAGCTGGACCGACCACGCCAAGTGGAGGGTGAGGGACCAGCTGGAGTGGATCCGCTCGGTCCAGCTGACGGCGGCGAGGCGGGTGAGCAGCGTCGTCGAAGTACTCGACGCCGTCGGCCTCAGCGAGAAGGCCGACTCCCGGCTGTCGAGGCTCTCCGGCGGGCAGCGACGCACCATTGACTTCGCGGCCGCCCTCATGGCCGCGCCCGAGCTCCTCGTCCTGGACGAGCCGACGACCGGACTGGACCCGGTCTCCAAGGCGCGCCTGCACGATCTCATTCTGGCCCGGGTCGACGACGACGCCACCATCGTCATGACCACCCACGACCTGGCTGAGGCCGAGCATCTGGCCTCTCGGGTGCTCATCATGAACGAGGGACGGATTCTCGCCGACGGCACGGTCACGGCGCTGCGCGAGCGCCTCGATCGTGGCGCCGAGATCACCTGGGTTCAGGACGGGACCCACCACGTCCACTCCACCCACTGCCCCGAGCGCTTCGTCAAGGAGCTCGACCTCGACGCCATCTCCGGGCTCACCATCACCCGCCCCACCCTGGAGGAGACCTACCTCTCCCTCGTCAGCAGCAAGGAGCCCCAGTCATGA","MTPVITTENLEFSYGDTPVLRGIDLSVEAGEVVCLLGPNGVGKTTLVENLLGSLTPTSGRVRVLDTDPRRAGADFWARVGLVQQSWTDHAKWRVRDQLEWIRSVQLTAARRVSSVVEVLDAVGLSEKADSRLSRLSGGQRRTIDFAAALMAAPELLVLDEPTTGLDPVSKARLHDLILARVDDDATIVMTTHDLAEAEHLASRVLIMNEGRILADGTVTALRERLDRGAEITWVQDGTHHVHSTHCPERFVKELDLDAISGLTITRPTLEETYLSLVSSKEPQS$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Membrane","ABC-transporter","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[143-177]T$	Q8KNE7_MICEC_Q8KNE7;
PF00005	$\"[30-210]T$	ABC_tran
PS50893	$\"[5-234]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[29-211]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[3-224]T$	no description
PTHR19222	$\"[5-224]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 15 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 3.8e-25. IPB005074C 19-66 IPB005074D 123-166***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 7.8e-20. IPB013563A 19-53 IPB013563C 132-159 IPB013563D 186-238***** IPB005116 (TOBE domain) with a combined E-value of 1.1e-13. IPB005116A 37-53 IPB005116C 135-148 IPB005116D 155-174 IPB005116E 188-201***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 6.7e-11. IPB010509B 30-55 IPB010509D 130-174***** IPB010929 (CDR ABC transporter) with a combined E-value of 6.2e-08. IPB010929K 17-61 IPB010929M 132-178 IPB010929A 29-48","Residues 1-219 are 43% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 1-63 are 62% similar to a (COBALT ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PDA0I1O9) which is seen in Q7NNW9_GLOVI.Residues 3-70 are 54% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 5-63 are 59% similar to a (ATP-BINDING) protein domain (PD743594) which is seen in Q842F1_STRGC.Residues 5-216 are 47% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 5-228 are 43% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 13-223 are 49% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 18-72 are 63% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 19-169 are 53% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 20-214 are 50% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 20-61 are 85% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q7V3W3_PROMM.Residues 20-194 are 47% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 20-231 are 48% similar to a (C24F3.5 ATP-BINDING) protein domain (PD574736) which is seen in Q21213_CAEEL.Residues 114-215 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 143-216 are 64% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 148-225 are 69% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 155-226 are 63% similar to a (GLP_38_64512_71054 ATP-BINDING) protein domain (PDA0H565) which is seen in Q7R1F8_EEEEE.","","-48% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 7.8E_22);-46% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 5.8E_17);-49% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 3.7E_16);-49% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 3.7E_16);-49% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 3.7E_16);","Residues 30 to 210 (E_value = 1.2e-44) place ANA_0557 in the ABC_tran family which is described as ABC transporter.","","(drrA) ","","1","","","","","","","","","","","Mon Aug 13 18:35:08 2007","","Mon Aug 13 18:35:08 2007","","","Mon Aug 13 18:35:08 2007","Mon Aug 13 18:35:08 2007","Mon Aug 13 18:35:08 2007","","Mon Aug 13 18:35:08 2007","Mon Aug 13 18:35:08 2007","","","","","yes","","" "ANA_0559","594433","596214","1782","4.87","-30.64","65323","ATGCGCAACGCCCGCCCCGCCCCCCAGCAGCCCTCCGGTATGCCGTTCGCCAAGTACCGGCCCTTCCTCGACGTCGTCTCCATTGACCTGCCCGACCGCACCTGGCCGGACAAGCGCATCACCGCCGCCCCCCGCTGGCTGAGCACCGACCTGCGCGACGGCAACCAGTCCCTCATCGAGCCCATGGGCCCCCAGGCCAAGCGCGCCATCTTCGACCTGCTCGTGAGCATGGGTTTCAAGGAGATTGAGATCGGCTTCCCGGCCGCCTCCCAGACCGACTTCGACTTCGTGCGCTCCCTGGTGGACGACGGCGCGATCCCCGAGGACGTCACCATCTCCGTGCTCACCCAGTCACGCGGCGAGCTCATCGACCGCACCCTGGACGCCTGCGTCGGCATCCCGCGGGCCACTGTCCACCTCTACAACGCCCTGTCGCCCCTGTTCCGCAACGTCGTCTTCCGCATGGACCGCGACCAGATCCGCGAGCTCGCCGTCGACGGCACCCGCCAGATCATGGCCCGCGCCGAGAAGGTCCTCGACGAGGACACGATCTTCGGCTATGAGTACTCCCCGGAGATCTTCGTGGACACCGAGCTCGACTACAGCATCGAGGTCTGCCAGGCCGTCATGGACGTGTGGGAGCCCGAGGAGGACCGCGAGATCATCCTCAACCTGCCCGCCACCGTCGAGCGCGCCACCCCCAACGTCTACGCCGACCAGATTGAGTGGATGAGCCGCCACCTGCCCCGGCGTGAGTCCGTGTGCCTGTCCCTGCACAACCACAACGACCGCGGCTCAGGCGTGGCCGCCGCCGAGCTCGGCCTCATGGCCGGCGCCGACCGCGTCGAGGGCTGCCTATTCGGCCACGGCGAGCGCACCGGCAACGTGGACTTGGTGACCCTGGCCCTCAACCTCTTCAGCCAGGGCGTGGACCCCATGCTCGACCTGTCCGACATTGACGAGGTCCGCCGCACCGTCGAGCGGGCCACCGGCATGGACGTGCCCCCGCGCACCCCCTACGCCGGCGAGCTCGTCTACACCTCATTCTCCGGCTCTCACCAGGACGCCATCAAGAAGGGCTTCGCGGCGCGCAACACTCAGGTCAGCGCCAAGCAGGCCGAGGGGCTGACCGACGCCGAGGCGCAGATCGCCGTCCCCTGGGCCATGCCCTACCTGCCCATCGACCCCCACGACGTGGGCCGCTCCTACGAGGCCGTCGTGCGCGTCAACTCCCAGTCCGGCAAGGGCGGGGTCGCCTACCTGCTGGGCACCACCCGCAAGCTCGAGCTGCCCCGCCGCCTCCAGATCGAGTTCTCCCGCATCGTCCAGCGCCACACCGACACCTACGGCGGCGAGGTCGACGGCGACCGCCTGTGGTCGATCTTCGCCGACGAGTACCTGCCCGCCGCGGCCGCCCCCGAGGCCGAGCTCAGCCGCTGGGGCCGCTTCGAGCTGCGTGGTGCCACCCTGACCTCCACCGGTGACGACGAGGACTCCACCCTCACCGTCACCCTGGTCGACGGCGGGGAGGAGAAGCACCTGACCGCCTCCGGCAACGGCCCCCTGGACGCCTTCGTCACCGCCCTGGAGAGCACGGGCCTGAGCGTGCGGATCCTCGACTACGTCGAGCACGCCCTGAGCGAGGGACGCGACGCGAAGGCCGCCAGCTACGTCGAGTGCGAGGTCGACGGCCAGGTCCTGTGGGGCGTGGGCATCGACCCCTCCATCACCACCTCCTCCTTCAAGGCCGTCATCTCCGCCATCAATCGCGCCCTGCGCTGA","MRNARPAPQQPSGMPFAKYRPFLDVVSIDLPDRTWPDKRITAAPRWLSTDLRDGNQSLIEPMGPQAKRAIFDLLVSMGFKEIEIGFPAASQTDFDFVRSLVDDGAIPEDVTISVLTQSRGELIDRTLDACVGIPRATVHLYNALSPLFRNVVFRMDRDQIRELAVDGTRQIMARAEKVLDEDTIFGYEYSPEIFVDTELDYSIEVCQAVMDVWEPEEDREIILNLPATVERATPNVYADQIEWMSRHLPRRESVCLSLHNHNDRGSGVAAAELGLMAGADRVEGCLFGHGERTGNVDLVTLALNLFSQGVDPMLDLSDIDEVRRTVERATGMDVPPRTPYAGELVYTSFSGSHQDAIKKGFAARNTQVSAKQAEGLTDAEAQIAVPWAMPYLPIDPHDVGRSYEAVVRVNSQSGKGGVAYLLGTTRKLELPRRLQIEFSRIVQRHTDTYGGEVDGDRLWSIFADEYLPAAAAPEAELSRWGRFELRGATLTSTGDDEDSTLTVTLVDGGEEKHLTASGNGPLDAFVTALESTGLSVRILDYVEHALSEGRDAKAASYVECEVDGQVLWGVGIDPSITTSSFKAVISAINRALR$","2-isopropylmalate synthase","Cytoplasm","2-isopropylmalate synthase","2-isopropylmalate synthase ","2-isopropylmalate synthase","","Wang S.Z., Dean D.R., Chen J.S., Johnson J.L. The N-terminal and C-terminal portions of NifV are encoded by two different genes in Clostridium pasteurianum. J. Bacteriol. 1991. 173(10):3041-3046. PMID: 2022611Stricker O., Masepohl B., Klipp W., Bohme H. Identification and characterization of the nifV-nifZ-nifT gene region from the filamentous cyanobacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 1997. 179(9):2930-2937. PMID: 9139910","","","

InterPro
IPR000891
Domain

Pyruvate carboxyltransferase
PF00682	$\"[52-332]T$	HMGL-like
PS50991	$\"[44-320]T$	PYR_CT

InterPro
IPR002034
Domain

Alpha-isopropylmalate/homocitrate synthase
PS00815	$\"[51-67]?$	AIPM_HOMOCIT_SYNTH_1
PS00816	$\"[256-269]T$	AIPM_HOMOCIT_SYNTH_2

InterPro
IPR005668
Family

Yeast 2-isopropylmalate synthase
PTHR10277:SF2	$\"[146-571]T$	ISOPROPYLMALATE SYNTHASE
TIGR00970	$\"[15-593]T$	leuA_yeast: 2-isopropylmalate synthase

InterPro
IPR013709
Domain

LeuA allosteric (dimerisation) domain
PF08502	$\"[452-592]T$	LeuA_dimer

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[51-330]T$	no description

noIPR
unintegrated

unintegrated
PTHR10277	$\"[146-571]T$	ISOPROPYLMALATE SYNTHASE RELATED

","BeTs to 18 clades of COG0119COG name: Isopropylmalate/homocitrate/citramalate synthasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0119 is a-mpk-yqvdr-bcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB013709 (LeuA allosteric (dimerisation) domain) with a combined E-value of 5.3e-82. IPB013709A 47-82 IPB013709B 117-161 IPB013709C 218-234 IPB013709D 256-295 IPB013709E 325-373***** IPB002034 (Alpha-isopropylmalate/homocitrate synthase) with a combined E-value of 9.4e-70. IPB002034A 46-95 IPB002034B 123-148 IPB002034C 219-234 IPB002034D 256-295 IPB002034E 337-365","Residues 14-201 are 83% similar to a (SYNTHASE TRANSFERASE 2-ISOPROPYLMALATE ALPHA-ISOPROPYLMALATE ALPHA-IPM SYNTHETASE BIOSYNTHESIS LEUCINE ACYLTRANSFERASE STRAIN) protein domain (PD009735) which is seen in LEU1_STRAW.Residues 49-303 are 43% similar to a (SYNTHASE TRANSFERASE 2-ISOPROPYLMALATE ALDOLASE ALPHA-ISOPROPYLMALATE ALPHA-IPM SYNTHETASE BIOSYNTHESIS LEUCINE 4-HYDROXY-2-OXOVALERATE) protein domain (PD004984) which is seen in Q71Y35_LISMF.Residues 202-255 are 83% similar to a (SYNTHASE ALPHA-ISOPROPYLMALATE TRANSFERASE BIOSYNTHESIS LEUCINE ALPHA-IPM SYNTHETASE 2-ISOPROPYLMALATE) protein domain (PDA01420) which is seen in LEU1_STRCO.Residues 224-254 are 90% similar to a (SYNTHASE TRANSFERASE 2-ISOPROPYLMALATE ALPHA-ISOPROPYLMALATE ALPHA-IPM SYNTHETASE BIOSYNTHESIS LEUCINE ACYLTRANSFERASE STRAIN) protein domain (PD876171) which is seen in LE12_RALSO.Residues 256-305 are 98% similar to a (SYNTHASE TRANSFERASE 2-ISOPROPYLMALATE BIOSYNTHESIS ALPHA-ISOPROPYLMALATE SYNTHETASE ALPHA-IPM LEUCINE HOMOCITRATE PRECURSOR) protein domain (PD327958) which is seen in Q6N0U6_RHOPA.Residues 337-447 are 77% similar to a (SYNTHASE TRANSFERASE 2-ISOPROPYLMALATE BIOSYNTHESIS ALPHA-ISOPROPYLMALATE ALPHA-IPM SYNTHETASE LEUCINE HOMOCITRATE LYASE) protein domain (PD411944) which is seen in LEU1_STRAW.Residues 452-580 are 63% similar to a (SYNTHASE TRANSFERASE 2-ISOPROPYLMALATE ALPHA-ISOPROPYLMALATE ALPHA-IPM SYNTHETASE BIOSYNTHESIS LEUCINE ACYLTRANSFERASE LYASE) protein domain (PD002462) which is seen in LEU1_STRAW.Residues 518-590 are 60% similar to a (SYNTHASE ALPHA-ISOPROPYLMALATE TRANSFERASE BIOSYNTHESIS LEUCINE ALPHA-IPM SYNTHETASE 2-ISOPROPYLMALATE PLASMID) protein domain (PD796141) which is seen in LE12_RALSO.","","-65% similar to PDB:1SR9 Crystal Structure of LeuA from Mycobacterium tuberculosis (E_value = 2.0E_175);","Residues 52 to 332 (E_value = 3.4e-87) place ANA_0559 in the HMGL-like family which is described as HMGL-like.Residues 452 to 592 (E_value = 3.2e-42) place ANA_0559 in the LeuA_dimer family which is described as LeuA allosteric (dimerisation) domain.","","synthase (leuA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0560","596237","596986","750","7.45","1.46","26822","GTGACGAGCAGGCTGTACCGGGATGAGGCGATCATCCTGCGCACCTACAAGCTGGGCGAGGCCGACCGCATCATCGTGATGCTCACCCGCCATCACGGCCAGGTGCGCGCCGTGGCCAAGGGGGTGCGCCGCACCACCTCCCGCTTCGGGGCCCGTCTGGAGCCCTTCTCCATGACCGACGTCCAGCTCCATGCCGGACGCACCCTCGACGTCGTCACCCAGGCCGAGATCATCGACCCCTTCGGCCGGGTCGTCAGCGCCGACTACGCCATGTTCACCTGCGCATCGACCATGGTGGAGACCGCTGAGCGCCTCAGTGCCGACGACGGTGACCTGGGCACCGAGGCCAGCCCCCAGCAGTACCTGCTACTGGCCGGGGCCCTGGCCGCCATGTCCCACCGGCGCCACGCCCCCGGACTCATCCTGGACTCCTACCTGCTGCGGGCCCTGGCCCTGGGGGGCTGGGCGCCATCGTGCTACGACTGCGCCCTGTGCGGCGCCCCCGGACCCCACCGGGCCTTCCACATCCAGGCCGGTGGGGCGGTGTGCGAGTCCTGCCGCTCGGCAGGCGCCGTCGAGGTCGAGCCGTCTACGATGGCGCTCCTGGGCGCCCTGCTCTCCGGGGACTGGGCCGTGGCCGACGCCTCCGGCCAGCGCGAGCGCTCGCAGGCCTCCGGGCTCGTCTCGGCCTACACGACCTGGTACCTGGAGCGGCGCCTGCGCTCCCTCGCACTGGTGGAAAGGGCATAA","VTSRLYRDEAIILRTYKLGEADRIIVMLTRHHGQVRAVAKGVRRTTSRFGARLEPFSMTDVQLHAGRTLDVVTQAEIIDPFGRVVSADYAMFTCASTMVETAERLSADDGDLGTEASPQQYLLLAGALAAMSHRRHAPGLILDSYLLRALALGGWAPSCYDCALCGAPGPHRAFHIQAGGAVCESCRSAGAVEVEPSTMALLGALLSGDWAVADASGQRERSQASGLVSAYTTWYLERRLRSLALVERA$","DNA repair protein RecO","Cytoplasm","DNA repair protein RecO","DNA repair protein RecO","DNA repair protein RecO","","Ziegelin G., Scherzinger E., Lurz R., Lanka E. Phage P4 alpha protein is multifunctional with origin recognition, helicase and primase activities. EMBO J. 1993. 12(9):3703-3708. PMID: 8253092","","","

InterPro
IPR003717
Family

Recombination protein O, RecO
PF02565	$\"[4-246]T$	RecO
TIGR00613	$\"[6-249]T$	reco: DNA repair protein RecO

InterPro
IPR013237
Domain

Phage P4 alpha, zinc-binding
SM00778	$\"[162-193]T$	no description

InterPro
IPR013991
Domain

PhnA protein N-terminal, proteobacterial
SM00782	$\"[162-191]T$	no description

","BeTs to 9 clades of COG1381COG name: Recombinational DNA repair protein (RecF pathway)Functional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1381 is ---------drlbcefghsn-jxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003717 (Recombination protein O, RecO) with a combined E-value of 8.1e-13. IPB003717A 10-43","Residues 6-67 are 90% similar to a (DNA REPAIR RECOMBINATION RECO O RECOMBINATIONAL POSSIBLE TLR2234 REPAIR/RECOMBINATION RECO) protein domain (PD008539) which is seen in Q6AED5_BBBBB.Residues 69-243 are 69% similar to a (DNA REPAIR RECOMBINATION RECO O DR0819 PATHWAY RECOMBINATIONAL RECF SINGLE-STRANDED) protein domain (PD334674) which is seen in Q6AED5_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 246 (E_value = 2.8e-43) place ANA_0560 in the RecO family which is described as Recombination protein O.Residues 4 to 248 (E_value = 1.5e-49) place ANA_0560 in the RecO family which is described as Recombination protein O.","","repair protein RecO (recO)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0561","597061","597858","798","6.45","-2.39","29821","GTGCTGCCGGCCGCCGCCCTGCCCCAGCATGTCGCCGTCGTCATGGACGGCAACGGGCGCTGGGCCAACGCCCGCGGCCTGCCCCGCACCGAGGGCCACCGGGTGGGGGAGGCCAATATGCTCGACGTCGCCGCCGGCGCTATCGAGATCGGCGTCAAAGAGCTGAGCGTCTACGCCTTCTCCACCGAGAACTGGCGGCGCTCACCGGGCGAGGTCCGTTTCATCATGGGCTTCGCCCGCAAGGTCCTGCGCGTCCAGCGCGATGTCCTCAACTCCTGGAACGTCAGGTTGCGCTGGATCGGACGCACTCCGCGCCTGTGGAAGTCCGTCCTGCATGAGCTGCGTGAGGCCGAGCGCGTCACCGCGCACAACACGGGCCTCACCCTCAACCTGTGCATCAACTACGGCGGGCGGGCCGAGATCGCCGACGCCACCCGAGCCATCGCCGAGGACGTCGCCGCCGGCCGCCTCAAGGCCTCCTCCATCAACGAGAAGACCATCCAGCGTTACCTCTACTCACCCACCATGCGGGACGTGGACCTGTTCATCCGCACCGGCGACGAGCAGCGCACCTCCAACTTCCTCATGTGGTCCTCCTCCTACGCCGAGCTCTACTTCTCGCCCCTGGCCTGGCCCGACTTCAACCGCACCGAGCTGTGGAAGGCCTGCGAGGCCTACGCCGGGCGCGAGCGCCGCTACGGCGGGGCCGTGGACAAGGTGCTGCACGAGGAACCCGCCGGCGCCGAGGATCCGGAGGACGACGAGGCCGACGAGTCACCGCACCACGACGGGCAGTAG","VLPAAALPQHVAVVMDGNGRWANARGLPRTEGHRVGEANMLDVAAGAIEIGVKELSVYAFSTENWRRSPGEVRFIMGFARKVLRVQRDVLNSWNVRLRWIGRTPRLWKSVLHELREAERVTAHNTGLTLNLCINYGGRAEIADATRAIAEDVAAGRLKASSINEKTIQRYLYSPTMRDVDLFIRTGDEQRTSNFLMWSSSYAELYFSPLAWPDFNRTELWKACEAYAGRERRYGGAVDKVLHEEPAGAEDPEDDEADESPHHDGQ$","Undecaprenyl diphosphate synthase","Cytoplasm, Extracellular","undecaprenyl diphosphate synthase","undecaprenyl diphosphate synthase ","undecaprenyl diphosphate synthase","","Apfel C.M., Takacs B., Fountoulakis M., Stieger M., Keck W. Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene. J. Bacteriol. 1999. 181(2):483-492. PMID: 9882662","","","

InterPro
IPR001441
Family

Di-trans-poly-cis-decaprenylcistransferase
PD003461	$\"[9-229]T$	UPS2_COREF_Q8FNG2;
G3DSA:3.40.1180.10	$\"[1-243]T$	no description
PTHR10291	$\"[1-245]T$	DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE
PF01255	$\"[14-235]T$	Prenyltransf
TIGR00055	$\"[7-234]T$	uppS: undecaprenyl diphosphate synthase

","BeTs to 25 clades of COG0020COG name: Undecaprenyl pyrophosphate synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0020 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001441 (Di-trans-poly-cis-decaprenylcistransferase) with a combined E-value of 2.6e-56. IPB001441A 10-22 IPB001441B 51-78 IPB001441C 131-148 IPB001441D 180-214","Residues 1-220 are 46% similar to a (NRRL STRAIN LACTIS KLUYVEROMYCES CHROMOSOME Y- Y-1140 B) protein domain (PD980637) which is seen in Q6CVD6_EEEEE.Residues 1-214 are 54% similar to a (DEHYDRODOLICHYL P35196 DIPHOSPHATE SYNTHETASE CEREVISIAE SACCHAROMYCES) protein domain (PD980635) which is seen in Q6CBH1_EEEEE.Residues 1-234 are 49% similar to a (IPF3375 CANDIDA ALBICANS) protein domain (PD985463) which is seen in Q6BRU3_EEEEE.Residues 2-215 are 49% similar to a (DEDOL-PP DEHYDRODOLICHYL SYNTHASE TRANSFERASE 2.5.1.- DIPHOSPHATE SYNTHETASE) protein domain (PD079003) which is seen in SRT1_YEAST.Residues 2-220 are 46% similar to a (Q03175 YMR101C TRANSFERASE CEREVISIAE SACCHAROMYCES) protein domain (PD980636) which is seen in Q6FN24_EEEEE.Residues 6-240 are 56% similar to a (SYNTHETASE UNDECAPRENYL CELL DIVISION TRANSFE WALL UPP SYNTHESIS PYROPHOSPHATE SYNTHASE) protein domain (PD723743) which is seen in UPPS_NITEU.Residues 7-214 are 53% similar to a (DEDOL-PP MEMBRANE ENDOPLASMIC DEHYDRODOLICHYL SYNTHASE TRANSFERASE 2.5.1.- DIPHOSPHATE RETICULUM SYNTHETASE) protein domain (PD498059) which is seen in RER2_YEAST.Residues 7-235 are 60% similar to a (SYNTHETASE UNDECAPRENYL SYNTHASE INCLUDES: CRTB/UPPS UPP BIFUNCTIONAL PYROPHOSPHATE 2.5.1.- DIPHOSPHATE) protein domain (PDA181M0) which is seen in CRUP_STRCO.Residues 7-215 are 55% similar to a (TRANSFERASE SEQUENCE ZZZ226 MRNA) protein domain (PD745609) which is seen in Q86E48_SCHJA.Residues 8-229 are 58% similar to a (SYNTHETASE UNDECAPRENYL PYROPHOSPHATE SYNTHASE TRANSFERASE DIPHOSPHATE UDS DI-TRANS-POLY-CIS-DECAPRENYLCISTRANSFERASE UPP) protein domain (PD250413) which is seen in UPPS_HALN1.Residues 9-229 are similar to a (UNDECAPRENYL SYNTHETASE CELL PYROPHOSPHATE SYNTHASE DIPHOSPHATE UPP UDS DI-TRANS-POLY-CIS-DECAPRENYLCISTRANSFERASE DIVISION) protein domain (PD003461) which is seen in UPS2_COREF.Residues 11-142 are 52% similar to a (DEHYDRODOLICHYL TRANSFERASE 2.5.1.- DIPHOSPHATE SYNTHETASE) protein domain (PD756896) which is seen in Q8IB97_PLAF7.","","-61% similar to PDB:1JP3 Structure of E.coli undecaprenyl pyrophosphate synthase (E_value = 3.6E_50);-61% similar to PDB:1UEH E. coli undecaprenyl pyrophosphate synthase in complex with Triton X-100, magnesium and sulfate (E_value = 3.6E_50);-61% similar to PDB:1V7U Crystal structure of Undecaprenyl Pyrophosphate Synthase with farnesyl pyrophosphate (E_value = 3.6E_50);-61% similar to PDB:1X06 Crystal structure of undecaprenyl pyrophosphate synthase in complex with Mg, IPP and Fspp (E_value = 3.6E_50);-61% similar to PDB:1X07 Crystal structure of undecaprenyl pyrophosphate synthase in complex with Mg and IPP (E_value = 3.6E_50);","Residues 14 to 235 (E_value = 1.6e-111) place ANA_0561 in the Prenyltransf family which is described as Putative undecaprenyl diphosphate synthase.","","diphosphate synthase (uppS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0563","598333","597908","426","6.00","-3.76","15542","ATGAGCGCAAGCAGCACGGCGCAGCGCCCCCGCACCACACGCCAACGCGCCGCCGTCGCCGACATCCTCGCCCGCACCGACGAGTTCCGCTCGGCCCAGCAGATCCATGCCGCCCTGGAGGCCGAAGGCACCAAGGTGGGACTGGCCACCGTCTACCGCAACCTGCAGACCCTGGCGGAGTCCGGCGCGGTGGACCAGGTGCGCAGCGCCGAGGGCGAGGTCCTCTACCGGGCCTGTGAGGAGCAGGAGCACCACCACCACATCGTGTGCCGCCGCTGCGGCTACACCGTGGAGGTGTCCGGCGGCGGGCTGGAGGAGTGGATTCAGCGGGTCTCGACCCGGCAGGGCTTCACCCAGATGGAGCACACGGCGGAGTTCTTCGGCCTGTGCGCCACGTGCTCGACCCAGGACGCCTCACAGGACTGA","MSASSTAQRPRTTRQRAAVADILARTDEFRSAQQIHAALEAEGTKVGLATVYRNLQTLAESGAVDQVRSAEGEVLYRACEEQEHHHHIVCRRCGYTVEVSGGGLEEWIQRVSTRQGFTQMEHTAEFFGLCATCSTQDASQD$","Ferric-uptake regulator","Cytoplasm","Fe2+/Zn2+ uptake regulation proteins","K03711 Fur family transcriptional regulator; ferric uptake regulator","ferric-uptake regulator","","","","","

InterPro
IPR002481
Family

Ferric-uptake regulator
PD002003	$\"[31-133]T$	Q7TYR6_MYCBO_Q7TYR6;
PF01475	$\"[7-127]T$	FUR

","BeTs to 17 clades of COG0735COG name: Fe2+/Zn2+ uptake regulation proteinsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0735 is a--p-z-qvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002481 (Ferric-uptake regulator) with a combined E-value of 3.7e-19. IPB002481A 5-23 IPB002481B 46-55 IPB002481C 84-94 IPB002481D 121-130","Residues 31-133 are 65% similar to a (UPTAKE FERRIC REGULATOR REGULATION FUR FAMILY TRANSCRIPTIONAL IRON TRANSCRIPTION ZINC) protein domain (PD002003) which is seen in Q7TYR6_MYCBO.","","-64% similar to PDB:2O03 Crystal structure of FurB from M. tuberculosis- a Zinc uptake regulator (E_value = 4.4E_29);-48% similar to PDB:2FE3 The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch (E_value = 1.9E_11);","Residues 7 to 127 (E_value = 2.4e-31) place ANA_0563 in the FUR family which is described as Ferric uptake regulator family.","","uptake regulation proteins","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0564","599220","598330","891","8.73","4.52","30081","ATGATCGAGTTCGTCTCCGACATGCTTGCCAGTCCCCTCATCCAGCGGGCCTTCATCGTGGCGGTCCTGGTGGGGCTGGCCGCCCCGGTGGTGGGCACCTACCTGGTTCAGCGGGGCCTGGCGCTGCTGGGCGACGGGATCGGGCACATCGCCCTGACCGGCATCGCCCTGGGCTGGCTGGCCGGGGCCGCCGCCAACGTCACTCCTCACGACGCCTGGGCCGTGCCCGGGGCGATCCTCATCAGCGTGCTGGGAGCCGTGATGATCGAGATCATCCGTGCCAACGGCCGAACTCGGGGAGACGTGGCCCTGGCGATCCTGTTCTACGGGGGCATCGCCGGGGGCGTCATCCTCATTCGTGTCGCCGGCGGGACGACGACGAATCTCAACTCCTACCTGTTCGGCTCGATCTCCACGGTCTCGGTCTCCGACGCCTGGTTCACCATCGCCCTGGCCACCCTGGTGCTCCTGGTGGGGCTGGGGCTGCGCGGCCCACTGTTCGCGTTGTGCCACGACGAGGAGTTCGCCCACGCCTGCGGCCTGCCAACCGGTGCCCTCAACGTGCTGGTAGCGGTGGTGGCGGCGCTGACGGTCTCGGTGTCCATGCGGGTGGTGGGGGCGCTGCTGGTCTCGGCGGTCATGATCGTGCCGGTGGCCATCGCCCAGCTCGTGTCGCACTCCTTCGCCCGCACCATGTACCTGGCGATGGGGCTGGGCGTGGTGGCCTGTGTGTCAGGTCTGACGATCACCTACCTGGTGGCGGCCTCTCCCGGCGCCATGATCGTGGTACTCCTAGTGGGGGGCTACGCCGTCGTCGCCCTCCTGTCCGGACTGCTGCAGCTCGTCAGCCGCTCGCGACGGCACCACATCACCTCAGGAGGCAGATCATGA","MIEFVSDMLASPLIQRAFIVAVLVGLAAPVVGTYLVQRGLALLGDGIGHIALTGIALGWLAGAAANVTPHDAWAVPGAILISVLGAVMIEIIRANGRTRGDVALAILFYGGIAGGVILIRVAGGTTTNLNSYLFGSISTVSVSDAWFTIALATLVLLVGLGLRGPLFALCHDEEFAHACGLPTGALNVLVAVVAALTVSVSMRVVGALLVSAVMIVPVAIAQLVSHSFARTMYLAMGLGVVACVSGLTITYLVAASPGAMIVVLLVGGYAVVALLSGLLQLVSRSRRHHITSGGRS$","Zinc/manganese transport system permease protein","Membrane, Cytoplasm","ABC transporter MreB","K02075 zinc/manganese transport system permease protein","ABC-3 protein","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR001626
Family

ABC-3
PF00950	$\"[10-276]T$	ABC-3

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[14-36]?$ $\"[41-63]?$ $\"[69-89]?$ $\"[104-123]?$ $\"[142-162]?$ $\"[183-203]?$ $\"[209-229]?$ $\"[234-256]?$ $\"[262-282]?$	transmembrane_regions

","BeTs to 18 clades of COG1108COG name: ABC-type Mn2+/Zn2+ transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1108 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB001626 (ABC transporter, family 3) with a combined E-value of 6.2e-31. IPB001626A 28-55 IPB001626B 134-144 IPB001626C 171-181 IPB001626D 190-221","Residues 79-261 are 60% similar to a (PERMEASE ABC TRANSPORTER IRON SYSTEM TRANSPORTER FERRICHROME MEMBRANE COMPOUND IRONIII) protein domain (PD247701) which is seen in Q839U3_ENTFA.","","No significant hits to the PDB database (E-value < E-10).","Residues 10 to 276 (E_value = 1e-49) place ANA_0564 in the ABC-3 family which is described as ABC 3 transport family.","","transporter MreB (zinc)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0565","600152","599217","936","9.58","6.34","32087","ATGACCTCATCATCTCCACCTTCACCAGCGTCTGTGACGACGCCGTCCGGTTCCCCCCGGGCGGCGTCGTCCGCGCTCGCCATCAAGGTCCGTGAGCTCAGCGTCGTCCTGGGCTCCTCCCTCATCCTGGACGACGTGAGCCTGGCCGTGGGCGGCGGCGAGTCCGTGGCGATCCTGGGCGCCAACGGCTCGGGCAAGTCCACCCTCGTCAAGGCCATTCTGGGCCTGGTGCCCCTGTCCGGCGGCAGCATCGAGCTCCTGGGCACCCCTACTTCGCATCGGCACAGGGTCCCCTGGGAGCGGGTCGGCTACGTCCCCCAGCGGATCGGTGCTGGCTCCGGCGTCCCGGCCACCGCCCTGGAGGTGGTGCGCTCCGGGCTCCTGGGGCCGCGCCGGCCTTGGGCCGATCGGGGGCGGGCCGCCAAACGCAAGGCCATGGCCGCCTTGGACGCCGTCGGGCTGGCCCACCGGGCCGCGGACCATGTCCAGGTCTTCTCCGGCGGGCAGGCCCAGCGGGTCCTCATCGCCCGGGCCCTGGTCCGCTCCCCCGAGCTGCTCATCCTCGATGAGCCTCTGGCCGGCATCGACCGCGCCAGCCGCGAGTCCCTGGCCGAGATCCTTCAGGGGCTGCGCGCGCAGGGGCTGACCCTGGTGACGGTTCTGCACGAGATGGGCGAGCTCGCCGACGTCGTCCAGCGGGCGATCCTCCTGCAGGACGGCCGGCTCGTCGCCGATGGCCCGGCCGGCGAGGTCGCTCATCTGCGCGACAGCGGGACCGGCGCGCCCCAGGGCGACCTGCACCGCGCGCACTCCAACTACGGCGCCGACGGCGACCACCACCCGGACGCCAGCGGCCCTCCGGCCCACCACGCCCCCGTCCTCGACCATCGGCTGCCTGACACGCGCCCTCATTCCGGTAGGAGCACCCGCCCATGA","MTSSSPPSPASVTTPSGSPRAASSALAIKVRELSVVLGSSLILDDVSLAVGGGESVAILGANGSGKSTLVKAILGLVPLSGGSIELLGTPTSHRHRVPWERVGYVPQRIGAGSGVPATALEVVRSGLLGPRRPWADRGRAAKRKAMAALDAVGLAHRAADHVQVFSGGQAQRVLIARALVRSPELLILDEPLAGIDRASRESLAEILQGLRAQGLTLVTVLHEMGELADVVQRAILLQDGRLVADGPAGEVAHLRDSGTGAPQGDLHRAHSNYGADGDHHPDASGPPAHHAPVLDHRLPDTRPHSGRSTRP$","Zinc/manganese transport system ATP-binding protein","Membrane, Cytoplasm","manganese transport system ATP-binding protein","K02074 zinc/manganese transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[166-207]T$	Q9L2H7_STRCO_Q9L2H7;
PF00005	$\"[53-240]T$	ABC_tran
PS50893	$\"[28-264]T$	ABC_TRANSPORTER_2
PS00211	$\"[165-179]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[52-241]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[21-253]T$	no description
PTHR19222	$\"[28-251]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 12 clades of COG1121COG name: ABC-type Mn/Zn transport systems, ATPase componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1121 is aom-kz-qvd-lbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 8e-34. IPB005074C 42-89 IPB005074D 153-196***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3e-28. IPB013563A 42-76 IPB013563C 162-189 IPB013563D 216-268***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 2.5e-16. IPB010509B 53-78 IPB010509D 160-204***** IPB005116 (TOBE domain) with a combined E-value of 8.5e-16. IPB005116A 60-76 IPB005116C 165-178 IPB005116D 185-204***** IPB007517 (Rad50 zinc hook motif) with a combined E-value of 6.3e-07. IPB007517A 40-69 IPB007517C 186-203***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.3e-06. IPB010929K 40-84 IPB010929M 162-208","Residues 28-125 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD616033) which is seen in Q8PV90_METMA.Residues 32-131 are 56% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD735025) which is seen in Q8G5L4_BIFLO.Residues 39-207 are 46% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 41-167 are 55% similar to a (ATP-BINDING) protein domain (PDA1B1R2) which is seen in Q7M969_WOLSU.Residues 42-242 are 48% similar to a (ATP-BINDING CG1494-PA) protein domain (PD310846) which is seen in Q9VRG3_DROME.Residues 43-247 are 50% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 43-90 are 79% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q82BS1_STRAW.Residues 43-245 are 45% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 152-222 are 61% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 152-245 are 59% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 152-247 are 57% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 152-246 are 52% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 153-250 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 153-251 are 51% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 153-245 are 52% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 153-261 are 49% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 154-253 are 56% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 154-243 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z9) which is seen in Q8DM53_SYNEL.Residues 157-243 are 57% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 160-242 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA106Q1) which is seen in Q73R37_TREDE.Residues 161-245 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 165-250 are 52% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z3) which is seen in Q72D80_DESVH.Residues 165-251 are 57% similar to a (APRD ATP-BINDING) protein domain (PDA0I303) which is seen in Q89EV0_BRAJA.Residues 166-245 are 61% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD957735) which is seen in Q73JF3_TREDE.Residues 166-243 are 57% similar to a (COMPONENT METHYL M-REDUCTASE COENZYME ATP-BINDING) protein domain (PD462863) which is seen in Q93RF2_TREMD.Residues 166-207 are 83% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9L2H7_STRCO.Residues 168-251 are 63% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 169-256 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD476601) which is seen in Q89GD9_BRAJA.","","-46% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 8.2E_20);-45% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 2.5E_16);-43% similar to PDB:1G6H CRYSTAL STRUCTURE OF THE ADP CONFORMATION OF MJ1267, AN ATP-BINDING CASSETTE OF AN ABC TRANSPORTER (E_value = 3.6E_15);-43% similar to PDB:1G9X CHARACTERIZATION OF THE TWINNING STRUCTURE OF MJ1267, AN ATP-BINDING CASSETTE OF AN ABC TRANSPORTER (E_value = 3.6E_15);-43% similar to PDB:1GAJ CRYSTAL STRUCTURE OF A NUCLEOTIDE-FREE ATP-BINDING CASSETTE FROM AN ABC TRANSPORTER (E_value = 3.6E_15);","Residues 53 to 240 (E_value = 5.5e-48) place ANA_0565 in the ABC_tran family which is described as ABC transporter.","","transport system ATP-binding protein (troB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0566","601428","600226","1203","5.55","-17.26","42775","ATGCTCCACCGGGAAGGCCCTCACGACCACCGTTCAAACCGGCTCTCAGCAGCGCACACGCGGACTCGCCCGAGTTTGACGCAGGACCGGCAGAGTATGAGAATGATTCGCATGAATGTTTCACAGGCTCGTTCCCGTCGTCTCCACCGCGTCGTGGCGCTCGGAGCCACCCTGATGCTGGCTGCCGGCATGAGCGCATGCGGCGCCCTGAAGGGCGAGAGCTCATCAGACGCATCGGCACCGCACACGATCGCCCCGGGCAAGACCCTGACGGTCTCCACGTCCTTCTACCCGATCCAGTACCTGGCCGAGGCCATTGGCGGCAAGCTCGTCAAGGTCTCCACCGTGACCCCCTCCAACGTCGAGCCGCACGACTTCGAGCTCTCCGGCAAGGAGACCGCCGAGCTGGGCAAGGCCGATCTCATCGCCTACGTCCCCGGCTTCCAGCCCTCCCTGGACAAGGCCGTCAAGGAGGTCGGCTCCGGCCCCACCGTGGTGGACCTGAGCAAGCCGGCCAACCTCGTCCACCACGAGGGGGTTGAGGAGGAGCATGAGCACGAGCACGGCGAGGAGGCCTCCGACGGCGCCTCGGCCACGGCCAGTAGCGCCGCCACCGCGCAGGCCAGCGAGGCCGAGCACGACGAGCACGGCCACGATGAGCACGCCGAGGGCGGTGAGGGGCACGACGGCGACCTCGACCCGCACTTCTGGCTCGACCCGGACCGCATGATCAAGGTGGCCGAGGCCCTTGAGGCCTCCTTCGCCAAGATCGACCCGGCCAACGCCAACGACTACAAGGCGGGCCTGGACAAGCTCAAGACGGCGCTGACCGGAGTGGACAACCAGTACAAGCAGGGCTTTACCAGCTGCCAGCACAAGACCTTCATCACCTCCCACGCCGCCTTCGGCTACATGGCCGAGCGCTACGGCCTGACCCAGCCCTCCATCTCCGGCATCGACCCGGAGACCGAGCCCAGCCCCGCCGAGATGGCCAACATCAAGTCGGTGGTCGAGAAGACGGGGGAGAAGACGATCTTCACCGAGGAGCTGGTCTCCGACGCCCCCGCCAAGGCGATCGCCGCGGAGACCGGGGCGGAGACGAGCGTCCTCAGCCCCCTGGAGTCCAAGCCCGAGCAAGGCGACTACACCGACGCCATGACCACCAACCTGGAGCGACTCAAGTCCGCCATGGTGTGCAAGTAG","MLHREGPHDHRSNRLSAAHTRTRPSLTQDRQSMRMIRMNVSQARSRRLHRVVALGATLMLAAGMSACGALKGESSSDASAPHTIAPGKTLTVSTSFYPIQYLAEAIGGKLVKVSTVTPSNVEPHDFELSGKETAELGKADLIAYVPGFQPSLDKAVKEVGSGPTVVDLSKPANLVHHEGVEEEHEHEHGEEASDGASATASSAATAQASEAEHDEHGHDEHAEGGEGHDGDLDPHFWLDPDRMIKVAEALEASFAKIDPANANDYKAGLDKLKTALTGVDNQYKQGFTSCQHKTFITSHAAFGYMAERYGLTQPSISGIDPETEPSPAEMANIKSVVEKTGEKTIFTEELVSDAPAKAIAAETGAETSVLSPLESKPEQGDYTDAMTTNLERLKSAMVCK$","Zinc/manganese transport system substrate-binding protein","Periplasm, Cytoplasm","Zinc-binding protein adcA precursor","K02077 zinc/manganese transport system substrate-binding protein","periplasmic solute binding protein","","","","","

InterPro
IPR006127
Family

Periplasmic solute binding protein
PF01297	$\"[59-398]T$	SBP_bac_9

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1980	$\"[88-288]T$ $\"[289-375]T$	no description
tmhmm	$\"[51-69]?$	transmembrane_regions

","BeTs to 18 clades of COG0803COG name: ABC-type Mn/Zn transport system, periplasmic Mn/Zn-binding (lipo)protein (surface adhesin A)Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0803 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 4","***** IPB006129 (Adhesin B signature) with a combined E-value of 4.4e-33. IPB006129A 89-110 IPB006129B 114-132 IPB006129D 232-251 IPB006129E 288-305 IPB006129F 314-332 IPB006129G 337-354 IPB006129H 359-377***** IPB006127 (Periplasmic solute binding protein) with a combined E-value of 2.5e-32. IPB006127A 116-150 IPB006127B 233-268 IPB006127C 293-310***** IPB006128 (Adhesin family signature) with a combined E-value of 4.6e-21. IPB006128A 89-107 IPB006128B 120-133 IPB006128D 288-309 IPB006128E 341-359 IPB006128F 363-382","Residues 75-144 are 63% similar to a (LIPOPROTEIN ABC PERIPLASMIC ZINC BINDING PRECURSOR SIGNAL TRANSPORTER TRANSPORTER METAL-BINDING) protein domain (PD002751) which is seen in Q9L2H8_STRCO.Residues 276-394 are 63% similar to a (LIPOPROTEIN ABC PERIPLASMIC ZINC PRECURSOR SIGNAL TRANSPORTER BINDING TRANSPORTER METAL-BINDING) protein domain (PD002761) which is seen in Q9L2H8_STRCO.","","-54% similar to PDB:2O1E Crystal Structure of the Metal-dependent Lipoprotein YcdH from Bacillus subtilis, Northeast Structural Genomics Target SR583 (E_value = 5.6E_27);-44% similar to PDB:1PSZ PNEUMOCOCCAL SURFACE ANTIGEN PSAA (E_value = 1.3E_12);-47% similar to PDB:1PQ4 Crystal structure of ZnuA (E_value = 2.3E_12);-44% similar to PDB:1XVL The three-dimensional structure of MntC from Synechocystis 6803 (E_value = 2.5E_11);","Residues 59 to 398 (E_value = 3e-56) place ANA_0566 in the SBP_bac_9 family which is described as Periplasmic solute binding protein family.","","protein adcA precursor (lipo)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0567","601544","602935","1392","5.35","-13.90","52811","TTGGCATCCACCCCTTCACGCCTCGACGCCGTCATCAACCTCGCCAAGCGGCGCGGCTTCGTCTTCCCCTGCGGCGAGATCTACGGCGGAACCCGCTCGGCCTGGGACTACGGGCCGCTGGGCGTCGAGCTCAAGGAGAACATCAAGCGCCAGTGGTGGCAGTACATGGTCCGCTCGCGCGACGACGTCGTCGGGCTGGACTCCTCCGTCATCCTGCCGCGTGAGACCTGGGTCGCCTCCGGTCACGTCGGCGCCTTCACCGACCCGCTCGTGGAGTCCCTGCACACCCACAAGCGCTACCGCGCCGACCAACTCATCGAGGACTACGCCGCCCGCAAGGGCCTCGACCCTGAGAATGTCACCCTCGACATGGTTCCCGACCCGGTCACCGGCCAGCCGGGCTCCTGGACCGAGCCGCGCGAGTTCTCCGGCCTGCTCAAGACCTACCTGGGGCCGGTCGACGACGAGTCCGGCCTGCACTACCTGCGCCCCGAGACCGCCCAGGGCATCTTCATCAACTTCGCCAACGTCATGAGCGCGGCCCGCAAGAAGCCGCCCTTCGGCATCGGCCAGGTGGGCAAGTCCTTCCGCAACGAGATTACGCCGGGAAACTTCATCTTCCGCACCCGCGAGTTCGAGCAGATGGAGCTGGAGTTCTTCTGCGAGCCGGGCACCGACGAGGAGTGGCACCAGTACTGGATCGACTACCGCAAGGCCTGGTACACCGACCTGGGCATCAGCGAGGACAACCTGCGCCTGTATGAGCACCCCGCCGAGAAGCTCTCCCACTACTCCAAGCGCACCGTGGACCTGGAGTACCGCTTCGGCTTCGCCGGCTCGGAGTGGGGCGAGCTCGAGGGCATTGCCAACCGCACCGACTTCGACCTGTCCACCCACGCCGAGCACTCCGGCAAGGACATGTCCTACTTCGACCAGACCCGCTCCGAGCGCTGGACCCCCTACGTCATCGAGCCCTCCGCCGGCCTGACCCGCTCGCTCATGGCCTTCCTCGTGGAGGCCTACACCGAGGACGAGGCCCCCAACACCAAGGGAGGGGTGGACAAGCGCATCGTGCTCAAGCTCGACGCGCGCATCGCCCCGGTCAAGGCGGCCGTCCTGCCGCTGAGCCGCAAGGAGGAGCTGACCGGGCCGGCCAAGGAACTGGCCGCCCGCCTGCGCCGCTCCTGGAACGTGGAGTACGACGACGCCGGCGCGGTCGGCCGTCGCTACCGCCGCCAGGACGAGGTCGGCACGCCCTTCTGCCTGACCTACGACTTCGACTCGCCCGAGGACGGGGCCGTCACCGTGCGCGAGCGCGACACGATGACCCAGGAGCGCATCCCGCTCGAGGGCGTCGAGCGCTACCTGGCTGAGCGCCTCATCGGCTGCTGA","LASTPSRLDAVINLAKRRGFVFPCGEIYGGTRSAWDYGPLGVELKENIKRQWWQYMVRSRDDVVGLDSSVILPRETWVASGHVGAFTDPLVESLHTHKRYRADQLIEDYAARKGLDPENVTLDMVPDPVTGQPGSWTEPREFSGLLKTYLGPVDDESGLHYLRPETAQGIFINFANVMSAARKKPPFGIGQVGKSFRNEITPGNFIFRTREFEQMELEFFCEPGTDEEWHQYWIDYRKAWYTDLGISEDNLRLYEHPAEKLSHYSKRTVDLEYRFGFAGSEWGELEGIANRTDFDLSTHAEHSGKDMSYFDQTRSERWTPYVIEPSAGLTRSLMAFLVEAYTEDEAPNTKGGVDKRIVLKLDARIAPVKAAVLPLSRKEELTGPAKELAARLRRSWNVEYDDAGAVGRRYRRQDEVGTPFCLTYDFDSPEDGAVTVRERDTMTQERIPLEGVERYLAERLIGC$","Glycyl-tRNA synthetase","Cytoplasm","glycyl-tRNA synthetase","glycyl-tRNA synthetase ","glycyl-tRNA synthetase","","Wolf Y.I., Aravind L., Grishin N.V., Koonin E.V. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999. 9(8):689-710. PMID: 10447505Aberg A., Yaremchuk A., Tukalo M., Rasmussen B., Cusack S. Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase. Biochemistry 1997. 36(11):3084-3094. PMID: 9115984","","","

InterPro
IPR002314
Domain

tRNA synthetase, class II (G, H, P and S)
PF00587	$\"[44-278]T$	tRNA-synt_2b

InterPro
IPR002315
Family

Glycyl-tRNA synthetase, alpha2 dimer
PR01043	$\"[27-41]T$ $\"[140-152]T$ $\"[161-178]T$ $\"[193-210]T$ $\"[210-220]T$ $\"[320-332]T$ $\"[406-425]T$	TRNASYNTHGLY
PTHR10745	$\"[164-462]T$	GLYCYL-TRNA SYNTHETASE
TIGR00389	$\"[6-460]T$	glyS_dimeric: glycyl-tRNA synthetase

InterPro
IPR004154
Domain

Anticodon-binding
G3DSA:3.40.50.800	$\"[340-460]T$	no description
PF03129	$\"[369-459]T$	HGTP_anticodon

InterPro
IPR006195
Domain

Aminoacyl-transfer RNA synthetase, class II
PS50862	$\"[9-374]T$	AA_TRNA_LIGASE_II

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[4-339]T$	no description

","BeTs to 13 clades of COG0423COG name: Glycyl-tRNA synthetase, class IIFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0423 is aompkzy--dr-------------twNumber of proteins in this genome belonging to this COG is 1","***** IPB002315 (Glycyl-tRNA synthetase signature) with a combined E-value of 6e-76. IPB002315A 27-41 IPB002315B 140-152 IPB002315C 161-178 IPB002315D 193-210 IPB002315E 210-220 IPB002315F 320-332 IPB002315G 406-425","Residues 8-88 are 88% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA GLYCYL-TRNA GLYCINE--TRNA GLYRS BIOSYNTHESIS ATP-BINDING TRNA SYNTHETASE) protein domain (PD328901) which is seen in Q6A964_PROAC.Residues 89-155 are 82% similar to a (SYNTHETASE LIGASE GLYCYL-TRNA AMINOACYL-TRNA GLYCINE--TRNA GLYRS BIOSYNTHESIS ATP-BINDING 3D-STRUCTURE SYNTHASE) protein domain (PD684200) which is seen in Q6NG25_CORDI.Residues 92-255 are 84% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA GLYCYL-TRNA GLYCINE--TRNA GLYRS BIOSYNTHESIS ATP-BINDING TRNA SYNTHETASE) protein domain (PD004145) which is seen in Q6A964_PROAC.Residues 153-456 are 44% similar to a (DNA POLYMERASE SUBUNIT MITOCHONDRIAL ACCESSORY GAMMA MTPOLB 2 PRECURSOR POLG-BETA) protein domain (PD135923) which is seen in DPG2_XENLA.Residues 156-225 are 94% similar to a (SYNTHETASE LIGASE GLYCYL-TRNA AMINOACYL-TRNA GLYCINE--TRNA GLYRS BIOSYNTHESIS ATP-BINDING SYNTHETASE II) protein domain (PD974837) which is seen in SYG_MYCTU.Residues 256-310 are 94% similar to a (SYNTHETASE GLYCYL-TRNA AMINOACYL-TRNA LIGASE GLYCINE--TRNA GLYRS BIOSYNTHESIS ATP-BINDING SYNTHETASE II) protein domain (PDA06949) which is seen in Q8G7W9_BIFLO.Residues 311-382 are 88% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA GLYCYL-TRNA GLYCINE--TRNA GLYRS BIOSYNTHESIS ATP-BINDING TRNA SYNTHETASE) protein domain (PD003725) which is seen in Q6A964_PROAC.Residues 385-453 are 86% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS THREONYL-TRNA HISTIDYL-TRNA PROLYL-TRNA HISTIDINE--TRNA HISRS) protein domain (PD000606) which is seen in Q6A964_PROAC.","","-61% similar to PDB:1ATI CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (E_value = 1.7E_118);-59% similar to PDB:1B76 GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH ATP (E_value = 5.4E_109);-59% similar to PDB:1GGM GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH GLYCYL-ADENYLATE (E_value = 5.4E_109);-46% similar to PDB:2PME The Apo crystal Structure of the glycyl-tRNA synthetase (E_value = 6.1E_36);-46% similar to PDB:2PMF The crystal structure of a human glycyl-tRNA synthetase mutant (E_value = 6.1E_36);","Residues 44 to 278 (E_value = 2.3e-60) place ANA_0567 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T).Residues 369 to 459 (E_value = 4.8e-23) place ANA_0567 in the HGTP_anticodon family which is described as Anticodon binding domain.","","synthetase (glyS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0569","603234","604382","1149","6.94","-0.24","39372","ATGCTCGGTGCCATTGTCGGCGCCCTGGTCCTGGCCACCGTCGTCGGGCTGTTCGTGCTCTGGCCGGGCAAGAGCTCACTCATCGGCTCGCGCTCCTTCACCGCCGAGGGCGGCTCGGTGGGCAAGGCCACCATCACATCCACGGACCTGTCGGGCTGTCAGAGCTCGGTGAGCGCCCTGACGGAGGTCAACGGCGTCAAGCCCGAGGAGTTCGCCAAGGGCCACGTGTGCGCCCGCATCACCGAGGGGGAGGGAAAGGGCCTGGTCATGCCGGTCCAGCTGGTGGGTGAGCCCCGCAAGCTCGCCCACGCCGGTGACCGGCTCGTCGTCCTCTACTCGCCTCAGGCCATCCTGTCCGGCTCCCCCTACTCCTTCATCGACTACCAGCGCCAGCTCCCGGTCGGCGCCCTGGCGGTCGTCTACCTGGTGCTCGTCGTCGCCGTGGCCGGGCGCAAGGGCGTCCTCAGCGTCCTGGGCCTGCTGGTGGCCACCGGCGTACTCGCCTTCTTCATGATCCCGGCGCTCCTGTCCGGCTCCCACCCGCTGGCGGTGACCCTGGTCGGATCGATGGCGATGATGCTGGCGGCCGTCTACGTTGCCCACGGCGTGTCCATCCGCACCACGACCGCCCTACTGGGAACGGTGGCCGGCATCGTGCTGACCGTGCTGCTGGCCCTGTGGGGGACCGACGCCGCCCACCTGACCGGCGACGTCGATGAGACCGCCCGTCTGCTGGCCTCACGCACACACATCGATCTGCAGACGCTGCTGACCTGCGGCATGGTCATCGCCGGGCTCGGTGTCCTCAACGACGTCACCATCACCCAGGCCTCCTCGGTGTGGGAGCTGCACGCCGCCAACCCGCTGCTGTCTCGCACGCGCCTGTTCACCGGCGGGATGAGGATCGGGCGGGACCACATCGCCTCAACCGTCTACACCCTGGCCTTCGCCTACGCCGGCACGGCGCTGCCCCTCATCCTGGCCGCCGCCCTCATGGACCGGGCCGTGCTGGACACCATGCTCTCGGGTGAGATTGCCGAGGAGATCGTGCGCACCCTCATCTCCTCCATCGGCCTGGTCCTGGCGATCCCGGCGACCACGGCGATCGCGGCGGCCCTGTGCCGCGTCACCCCGGTCCTCGACGAGTAG","MLGAIVGALVLATVVGLFVLWPGKSSLIGSRSFTAEGGSVGKATITSTDLSGCQSSVSALTEVNGVKPEEFAKGHVCARITEGEGKGLVMPVQLVGEPRKLAHAGDRLVVLYSPQAILSGSPYSFIDYQRQLPVGALAVVYLVLVVAVAGRKGVLSVLGLLVATGVLAFFMIPALLSGSHPLAVTLVGSMAMMLAAVYVAHGVSIRTTTALLGTVAGIVLTVLLALWGTDAAHLTGDVDETARLLASRTHIDLQTLLTCGMVIAGLGVLNDVTITQASSVWELHAANPLLSRTRLFTGGMRIGRDHIASTVYTLAFAYAGTALPLILAAALMDRAVLDTMLSGEIAEEIVRTLISSIGLVLAIPATTAIAAALCRVTPVLDE$","YibE/F family protein","Membrane, Cytoplasm","putative membrane protein","hypothetical protein","YibE/F family protein","","","","","

InterPro
IPR012507
Family

YibE/F-like
PF07907	$\"[132-373]T$	YibE_F

noIPR
unintegrated

unintegrated
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[5-23]?$ $\"[128-148]?$ $\"[153-173]?$ $\"[179-199]?$ $\"[209-229]?$ $\"[312-332]?$ $\"[353-373]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB012507 (YibE/F-like) with a combined E-value of 1e-31. IPB012507A 261-283 IPB012507B 298-329 IPB012507C 348-366","Residues 169-240 are 70% similar to a (MEMBRANE UNCHARACTERIZED PROTEIN CPE1367 MW0423 EF0069 SA0427 YIBF INTEGRAL SE2315) protein domain (PD921278) which is seen in Q9X9U1_STRCO.Residues 169-245 are 57% similar to a (MEMBRANE SPANNING) protein domain (PDA0Z0G3) which is seen in Q72J55_THET2.Residues 170-240 are 69% similar to a (MEMBRANE INTEGRAL) protein domain (PD669118) which is seen in Q73T89_MYCPA.Residues 251-360 are similar to a (MEMBRANE UNCHARACTERIZED PROTEIN INTEGRAL SA0428 CPE1367 YIBE MW0423 EF0069 EF0070) protein domain (PD407841) which is seen in Q82FI6_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 132 to 373 (E_value = 1.4e-70) place ANA_0569 in the YibE_F family which is described as YibE/F-like protein.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0570","605726","604428","1299","6.28","-4.71","46430","ATGAGTGAGACCTCCCCCCGCCTCCCCGACGCCTGCGCCTCGGGCCGCGCGCCCGCGCCGCTGCGCATCGGGCCGCTGGTGGTGCCCACCCCGGTCGAGCTCGCCCCCATGGCCGGAGTCACCAACGCCTCCTTCCGCCGCCTGTGCCGTGAGATGGCTGAGGCAGCCCTGCCGGAGTCGCTGAGGCCCTCCCATCCCGGTCCGCTGCCCACGCCTGACGGCGGCCTGCTGGCCCCGGCGGGCCTGTACGTCACGGAGATGGTCACCACCCGCGCCCTGGTGGAGCGCAACGAGCGCACTCTGGCGATGGTGCGCACCGACCCGGCCGAGAGGGTGCGTTCCATCCAGCTCTACGGGGTCGATCCGGCCACGGTGGGGGCCGCGGTGCGGATCCTGGTGGAGGAGGATCTGGCCGACCACATCGACTTGAACTTCGGCTGCCCGGTCCCCAAGGTGACCCGCAAGGGCGGCGGGGCGGCACTGCCGTGGAAGCGAGACCTGCTGGCGGCGATCCTCACCGAGGCGGTGCGTGCCAGTGAGGCCGCCGTCCACACCGTCGGGCGGGCGCGGCAGGTGCCGGTGACCATGAAGATGCGTCTGGGCATCGACGAGGAGCACGAGACCTTCCTCGACGCCGCCCGAGCCGCCGACAACGCCGGGATCGCGGCCGTGGCCCTGCACGCCCGCAGCGCGCGCCAGCACTACTCGGGCCAGGCCCGCTGGGAGGAGATCGCCCGGCTCAAGGAGGCCACTGACCTGCCAGTGCTCGGCAACGGTGACATCTGGCTGGGCGACGACGCGGTGCGCATGATGGAGGCCACCGGCTGCGACGGCGTCGTCGTGGGCCGCGGCTGCCAGGGCCGGCCCTGGCTGTTCGCTGACATCGTCTCGGCCATGCACGGCTCGCCTGCGCGCACCCGCCCGGACCTGGACTCCGTCATCGAGGTCATCCGTCGCCACGGGCGGATGCTGGCCGAGGAGATGGGCGAGGACCGGGGGGTGCGTGACCTGCGCAAGCACGTGGGCTGGTACCTCAAGGGCTACCCGGTCGGCGGCGCGGCGCGCGCCGACCTCATGGGGATCCGGAGCCTGGACGAGCTCGACGCCGGCCTGGAGCGGATGCGCGCGCGCCTGCCCGAGGTCGTGGACTACCCCGGCGACATCGTCGAGGGCCCCCGAGGGCGGGCCGGCAGCCCCAAGACTCCCCGTCTGCCCGACGGCTGGCTGGACTCCCCCACCCTGGATGCGGCCCACCGCGAGATGCTCAGCCAGGCCGAGTCCGACGTCTCCGGCGGCTGA","MSETSPRLPDACASGRAPAPLRIGPLVVPTPVELAPMAGVTNASFRRLCREMAEAALPESLRPSHPGPLPTPDGGLLAPAGLYVTEMVTTRALVERNERTLAMVRTDPAERVRSIQLYGVDPATVGAAVRILVEEDLADHIDLNFGCPVPKVTRKGGGAALPWKRDLLAAILTEAVRASEAAVHTVGRARQVPVTMKMRLGIDEEHETFLDAARAADNAGIAAVALHARSARQHYSGQARWEEIARLKEATDLPVLGNGDIWLGDDAVRMMEATGCDGVVVGRGCQGRPWLFADIVSAMHGSPARTRPDLDSVIEVIRRHGRMLAEEMGEDRGVRDLRKHVGWYLKGYPVGGAARADLMGIRSLDELDAGLERMRARLPEVVDYPGDIVEGPRGRAGSPKTPRLPDGWLDSPTLDAAHREMLSQAESDVSGG$","Transcriptional regulator, NifR3 family","Cytoplasm","POSSIBLE TRANSCRIPTIONAL REGULATORY PROTEIN","possible transcriptional regulatory protein","putative TIM-barrel protein, nifR3 family","","Xing F., Martzen M.R., Phizicky E.M. A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA. RNA 2002. 8(3):370-381. PMID: 12003496","","","

InterPro
IPR001269
Family

Dihydrouridine synthase, DuS
PF01207	$\"[33-382]T$	Dus
PS01136	$\"[141-159]T$	UPF0034

InterPro
IPR004652
Family

Dihydrouridine synthase TIM-barrel protein nifR3
TIGR00737	$\"[23-379]T$	nifR3_yhdG: putative TIM-barrel protein, ni

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[26-307]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.1200.80	$\"[309-388]T$	no description
PTHR11082	$\"[85-382]T$	TRNA-DIHYDROURIDINE SYNTHASE
PTHR11082:SF9	$\"[85-382]T$	TRNA-DIHYDROURIDINE SYNTHASE-RELATED

","BeTs to 18 clades of COG0042COG name: Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 familyFunctional Class: RThe phylogenetic pattern of COG0042 is amt-YqvCEBrHuj--OlinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 277-351 are similar to a (SYNTHASE OXIDOREDUCTASE TRNA-DIHYDROURIDINE TRNA FLAVOPROTEIN FAD PROCESSING 1.-.-.- FAMILY NIFR3) protein domain (PD468831) which is seen in Q82BQ5_STRAW.Residues 382-485 are 53% similar to a (DIHYDROURIDINE NIFR3 FAMILY TIM-BARREL ENZYME TRANSCRIPTIONAL WITH DOMAIN PROBABLE SYNTHASE) protein domain (PD486897) which is seen in Q73RG6_TREDE.Residues 443-480 are similar to a (SYNTHASE OXIDOREDUCTASE TRNA TRNA-DIHYDROURIDINE FLAVOPROTEIN PROCESSING FAD 1.-.-.- NIFR3 FAMILY) protein domain (PD000434) which is seen in Q82BQ5_STRAW.Residues 491-545 are similar to a (SYNTHASE OXIDOREDUCTASE TRNA-DIHYDROURIDINE TRNA 1.-.-.- FAD FLAVOPROTEIN PROCESSING NIFR3 FAMILY) protein domain (PD004944) which is seen in Q7U170_MYCBO.Residues 559-622 are 60% similar to a (TRANSCRIPTIONAL NIFR3/SMM1 FAMILY REGULATOR) protein domain (PD959874) which is seen in Q6AFU9_BBBBB.","","-47% similar to PDB:1VHN Crystal structure of a putative flavin oxidoreductase with flavin (E_value = 5.0E_28);-46% similar to PDB:1GQT ACTIVATION OF RIBOKINASE BY MONOVALENT CATIONS (E_value = 5.0E_28);-46% similar to PDB:1RK2 E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP, SOLVED IN SPACE GROUP P212121 (E_value = 5.0E_28);-46% similar to PDB:1RKA THE APO FORM OF E. COLI RIBOKINASE (E_value = 5.0E_28);-46% similar to PDB:1RKD E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP (E_value = 5.0E_28);","Residues 223 to 572 (E_value = 2e-105) place ANA_0570 in the Dus family which is described as Dihydrouridine synthase (Dus).","","TRANSCRIPTIONAL REGULATORY PROTEIN","","1","","","Wed Aug 1 17:16:00 2007","","Wed Aug 1 17:16:00 2007","","","Wed Aug 1 17:16:00 2007","Wed Aug 1 17:16:00 2007","Wed Aug 1 17:16:00 2007","","","Wed Aug 1 17:16:00 2007","","","Wed Aug 1 17:16:00 2007","Wed Aug 1 17:16:00 2007","Wed Aug 1 17:16:00 2007","","Wed Aug 1 17:16:00 2007","Wed Aug 1 17:16:00 2007","","","","","yes","","" "ANA_0571","605908","606636","729","5.64","-2.56","24353","ATGAACGAAGAGACCGAGCCGTCGATATCACGTTCCGTCGTCGTGACCGGAGCCTCCCGGGGAATCGGGGAGGCGGTTACGAAGGCGTTCCTGGCACAGGGCGACCGGGTGGCGGGCATCTCCCGCTCCGGTGAGGCCCCCGACGGCGCCCTGGCCCTGGCCGCCGACGTCACCGACCCCGACGCCCTGGCCGCCGCCCTGGCCACCGCCACCGAGGCGCACGGCCCCATCGAGGTCCTCGTGGCCTCGGCCGGCATCAACCGGGAGTCACTGGCGGCCCGCACCTCCTCCCAGATGTGGGACGAGGTCATCTCCGCGGACCTGACCGGCACCTTCAACACCGTGCGCGCCGTGACACCAGCCATGATGCGGGCCCGCAAGGGGCGCATCGTCCTGGTCTCCTCGGCCATCGCCGCACGCGGAGGCGTCGGCCTGTCGGCCTACGGCGCCGCCAAGGGCGGTGTGGAGGGACTGACCCGCTCCCTGGCCCGCGAGCTCGCACCGCGCGGCATCACCGTCAACGCCGTCGCCCCCGGCTTCGTCACCACGGCGATGACCGCCTCTCTGCCCGACCACATCCGCACCGCCTACCTCGAGCAGATCCCCCTGGGGCGCTTCGCCGACGTCACCGACATCGCCGGCCCCGTCCTCTTCCTGGCCTCACCCGCGGCCGCCTACGTCACTGGCGCGATCCTCGGCGTCGACGGCGGCCTGGGCATGGGGCGCTAG","MNEETEPSISRSVVVTGASRGIGEAVTKAFLAQGDRVAGISRSGEAPDGALALAADVTDPDALAAALATATEAHGPIEVLVASAGINRESLAARTSSQMWDEVISADLTGTFNTVRAVTPAMMRARKGRIVLVSSAIAARGGVGLSAYGAAKGGVEGLTRSLARELAPRGITVNAVAPGFVTTAMTASLPDHIRTAYLEQIPLGRFADVTDIAGPVLFLASPAAAYVTGAILGVDGGLGMGR$","3-oxoacyl-(acyl-carrier-protein) reductase","Cytoplasm, Extracellular","3-oxoacyl-[ACP] reductase (aka MabA)","3-oxoacyl-","short-chain dehydrogenase/reductase SDR","","Jornvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 1995. 34(18):6003-6013. PMID: 7742302Villarroya A., Juan E., Egestad B., Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 1989. 180(1):191-197. PMID: 2707261Persson B., Krook M., Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 1991. 200(2):537-543. PMID: 1889416Neidle E., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 1992. 204(1):113-120. PMID: 1740120Benyajati C., Place A.R., Powers D.A., Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 1981. 78(5):2717-2721. PMID: 6789320","","","

InterPro
IPR002198
Family

Short-chain dehydrogenase/reductase SDR
PR00080	$\"[75-86]T$ $\"[128-136]T$ $\"[148-167]T$	SDRFAMILY
PTHR19410	$\"[11-236]T$	SHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106	$\"[11-167]T$	adh_short
PS00061	$\"[135-163]?$	ADH_SHORT

InterPro
IPR002347
Family

Glucose/ribitol dehydrogenase
PR00081	$\"[12-29]T$ $\"[75-86]T$ $\"[122-138]T$ $\"[148-167]T$ $\"[169-186]T$ $\"[202-222]T$	GDHRDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[11-238]T$	no description
PTHR19410:SF87	$\"[11-236]T$	3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE

","BeTs to 22 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 4","***** IPB002347 (Glucose/ribitol dehydrogenase family signature) with a combined E-value of 4.1e-46. IPB002347A 12-29 IPB002347B 75-86 IPB002347C 122-138 IPB002347D 148-167 IPB002347E 169-186 IPB002347F 202-222***** IPB002198 (Short-chain dehydrogenase/reductase SDR) with a combined E-value of 2.1e-27. IPB002198B 128-176***** IPB003560 (2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature) with a combined E-value of 4.2e-26. IPB003560A 17-34 IPB003560C 98-118 IPB003560D 163-186 IPB003560E 192-211 IPB003560F 218-237***** IPB002424 (Insect alcohol dehydrogenase family signature) with a combined E-value of 9.6e-09. IPB002424D 110-128 IPB002424F 147-165 IPB002424G 170-183","Residues 13-232 are 45% similar to a (SLR5088 GLL3943 OXIDOREDUCTASE FAMILY PLASMID SHORT-CHAIN DEHYDROGENASE/REDUCTASE) protein domain (PD833341) which is seen in Q6ZEP2_SYNY3.Residues 75-179 are 51% similar to a (OXIDOREDUCTASE OXIDOREDUCTASE CHAIN FAMILY DEHYDROGENASE/REDUCTASE SHORT) protein domain (PD993862) which is seen in Q88LI1_PSEPK.Residues 75-196 are 48% similar to a (ALCOHOL DEHYDROGENASE-LIKE CHAIN SHORT) protein domain (PDA0I3Z5) which is seen in Q7UQH4_RHOBA.Residues 97-183 are similar to a (OXIDOREDUCTASE RUBJ) protein domain (PDA14164) which is seen in Q8KY44_STRCU.Residues 100-237 are 50% similar to a (FABG 3-KETOACYL-ACYL REDUCTASE CARRIER) protein domain (PD999098) which is seen in Q6MC19_PARUW.Residues 108-234 are 46% similar to a (OXIDOREDUCTASE SIMK SIMD3 3-KETO-ACYL-REDUCTASE) protein domain (PD636264) which is seen in Q9F5J6_STRAT.Residues 116-191 are 57% similar to a (OXIDOREDUCTASE ALCOHOL DEHYDROGENASE AGR_L_3035P SHORT-CHAIN) protein domain (PD894446) which is seen in Q8UAR9_AGRT5.Residues 118-168 are 68% similar to a (OXIDOREDUCTASE DEHYDROGENASE REDUCTASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY CHAIN SHORT PROBABLE OXIDOREDUCTASE) protein domain (PD003795) which is seen in Q88J66_PSEPK.Residues 121-185 are 58% similar to a (OXIDOREDUCTASE GLL4203) protein domain (PD963550) which is seen in Q7NDN2_GLOVI.Residues 200-237 are 76% similar to a (OXIDOREDUCTASE REDUCTASE DEHYDROGENASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE CHAIN SHORT PROBABLE FAMILY OXIDOREDUCTASE) protein domain (PD000197) which is seen in Q7WPN5_BORBR.","","-62% similar to PDB:2NM0 Crystal Structure of SCO1815: a Beta-Ketoacyl-Acyl Carrier Protein Reductase from Streptomyces coelicolor A3(2) (E_value = 1.6E_54);-59% similar to PDB:1UZL MABA FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 5.4E_42);-59% similar to PDB:2NTN Crystal structure of MabA-C60V/G139A/S144L (E_value = 5.4E_42);-59% similar to PDB:1UZM MABA FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 7.0E_42);-59% similar to PDB:1UZN MABA FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 7.0E_42);","Residues 11 to 167 (E_value = 5.3e-32) place ANA_0571 in the adh_short family which is described as short chain dehydrogenase.Residues 12 to 184 (E_value = 3.8e-06) place ANA_0571 in the KR family which is described as KR domain.Residues 13 to 229 (E_value = 0.0021) place ANA_0571 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.","","reductase (aka MabA) (SDR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0572","606722","607222","501","7.07","0.16","18203","ATGCGCCGGCTCGTGCTCGTCCGACACTCCAAGGCCTCTCACGACGCCGTCACCGACCTGGAACGTCCTCTGACCCCCAAGGGCACCGCCCTGGCCGGCCTGCTGGCCAAAGAGCTGCGCAAGCGCCTGGAGACCACCGACCTGCTCCTGGTCTCCCCGGCGGCCCGAGCCCGCGAGACCGCCCGCCCCATCCGCGACCGCCTAGAGCCCACCGACACCCTCGTGCGCGAGGAGATCTACAACCTGGGCCCCAATGGCATCCTCAAGGTCCTGGCCGAGGACGGTGCTGACGCCAGGACGGTCGTCGTCGTCGGCCACGAGCCCACGATCTCCGTGCTCGCCCACATCCTCCACGACACCGACGACGACCTTGCCTCCCAGATCTCCTTCGGGGTGCCCACGGCCACCGCCGTCATCATCGATGTCCCCGGCACCTGGGCGGACCTGGAGCCCAAGAGCGCCCGCATCCGGGAGATCTTCACCGCCCGCAAGCGCGACTGA","MRRLVLVRHSKASHDAVTDLERPLTPKGTALAGLLAKELRKRLETTDLLLVSPAARARETARPIRDRLEPTDTLVREEIYNLGPNGILKVLAEDGADARTVVVVGHEPTISVLAHILHDTDDDLASQISFGVPTATAVIIDVPGTWADLEPKSARIREIFTARKRD$","Phosphohistidine phosphatase SixA","Cytoplasm","phosphohistidine phosphatase SixA","hypothetical protein","Phosphoglycerate mutase","","Ogino T., Matsubara M., Kato N., Nakamura Y., Mizuno T. An Escherichia coli protein that exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay. Mol. Microbiol. 1998. 27(3):573-585. PMID: 9489669","","","

InterPro
IPR013078
Domain

Phosphoglycerate mutase
PF00300	$\"[3-113]T$	PGAM

InterPro
IPR014595
Family

Phosphohistidine phosphatase SixA
PIRSF035806	$\"[2-163]T$	Phosphohistidine phosphatase, SixA type

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1240	$\"[2-143]T$	no description
PTHR23029	$\"[2-79]T$	PHOSPHOGLYCERATE MUTASE

","BeTs to 10 clades of COG2062COG name: Phosphohistidine phosphatase SixAFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG2062 is a----z-q--r--cefghs-uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 79-156 are 56% similar to a (HYDROLASE SIXA 3.1.3.- PHOSPHOHISTIDINE PHOSPHATASE CC0526 SMC00468 RV1276C/MT1313 ATU1358 MLR0774) protein domain (PD093694) which is seen in YC76_MYCTU.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 113 (E_value = 1.1e-13) place ANA_0572 in the PGAM family which is described as Phosphoglycerate mutase family.","","phosphatase SixA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0573","607889","607251","639","4.95","-10.14","22424","GTGACTGAGGGCCCCGGCCTGCTGGTCATGGACGTGGACTCTACCCTCATCGAGCAGGAGGTCATCGAGCTCATCGCCGAGCGCGCCGGAACCCACGAGCTGGTCGCCGAGGTCACGGCACGGGCGATGCGCGGGGAGCTGGACTTCGCGGCCTCCCTGCGCGAGCGGGTGGCGACGCTGGCCGGTGTCCCCCAGGGGGTCTTCGCGGAGGTTTTGGCCGAGGTGCGCCCCACTCAGGGGGCGGCCGAGCTCATTGAGGCGCTGCACGCACGCGGTTGCCGGGTGGGGGTCGTCTCGGGAGGTTTCGAGGAGGTCGTGGTGCCTCTGGCCGAGCGGCTGGGCATCGACCACGTGGCGGCCAACCGCCTGGAGGTGGTCGAGGGCCGTCTCACCGGCCGGGTGATGGGGCGGATCGTGGACCGTCAGGAGAAGGTCCGCTGCCTGATCGCCTGGGCCCGGCAGGACGGTGTGCCCATGGAGCGCACCATCGCGGTCGGTGACGGGGCCAACGACCTGGGCATGCTGGAGGCCGCGGGGCTGGGGGTGGCGTTCTGCGCCAAGCCGGTGGTCGTTGAGCAGGCCGACGCGGCCATCCACGTGCGTGACCTGCGTGCCGTCCTGCAGCTGATCGGGGGTTGA","VTEGPGLLVMDVDSTLIEQEVIELIAERAGTHELVAEVTARAMRGELDFAASLRERVATLAGVPQGVFAEVLAEVRPTQGAAELIEALHARGCRVGVVSGGFEEVVVPLAERLGIDHVAANRLEVVEGRLTGRVMGRIVDRQEKVRCLIAWARQDGVPMERTIAVGDGANDLGMLEAAGLGVAFCAKPVVVEQADAAIHVRDLRAVLQLIGG$","Phosphoserine phosphatase SerB","Cytoplasm","phosphoserine phosphatase SerB","phosphoserine phosphatase ","phosphoserine phosphatase SerB","","","","","

InterPro
IPR004469
Domain

Phosphoserine phosphatase SerB
TIGR00338	$\"[1-210]T$	serB: phosphoserine phosphatase SerB

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[5-188]T$	Hydrolase

InterPro
IPR006383
Domain

HAD-superfamily hydrolase, subfamily IB, PSPase-like
TIGR01488	$\"[7-178]T$	HAD-SF-IB: HAD-superfamily hydrolase, subfa

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[62-211]T$	no description
PTHR10000	$\"[7-211]T$	PHOSPHOSERINE PHOSPHATASE

","BeTs to 15 clades of COG0560COG name: Phosphoserine phosphataseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0560 is aompkzy---rl--efghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB000150 (Cof protein) with a combined E-value of 3.5e-12. IPB000150A 8-17 IPB000150E 156-187***** IPB008250 (E1-E2 ATPase-associated region) with a combined E-value of 1.2e-11. IPB008250B 75-115 IPB008250C 162-185","Residues 6-208 are similar to a (PHOSPHATASE PHOSPHOSERINE HYDROLASE PHOSPHOHYDROLASE O-PHOSPHOSERINE PSP SERB PSPASE TRANSMEMBRANE ATP-BINDING) protein domain (PD186741) which is seen in Q9CHW3_LACLA.Residues 7-210 are 48% similar to a (PHOSPHOSERINE PHOSPHATASE) protein domain (PD829884) which is seen in Q8NKM9_AAAAA.Residues 7-211 are 57% similar to a (NRRL STRAIN LACTIS KLUYVEROMYCES E CHROMOSOME Y- Y-1140) protein domain (PD984032) which is seen in Q6CN02_EEEEE.Residues 108-183 are 57% similar to a (HYDROLASE PHOSPHATASE PHOSPHOSERINE FAMILY ACYLTRANSFERASE TRANSFERASE HYDROLASE HAD-SUPERFAMILY HALOACID ENZYME) protein domain (PD013822) which is seen in Q7NGF8_GLOVI.","","-60% similar to PDB:1F5S CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII (E_value = 2.6E_39);-60% similar to PDB:1J97 Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase (E_value = 2.6E_39);-60% similar to PDB:1L7M HIGH RESOLUTION LIGANDED STRUCTURE OF PHOSPHOSERINE PHOSPHATASE (PI COMPLEX) (E_value = 2.6E_39);-60% similar to PDB:1L7N TRANSITION STATE ANALOGUE OF PHOSPHOSERINE PHOSPHATASE (ALUMINUM FLUORIDE COMPLEX) (E_value = 2.6E_39);-60% similar to PDB:1L7O CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE IN APO FORM (E_value = 1.0E_38);","Residues 5 to 188 (E_value = 1.9e-23) place ANA_0573 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.Residues 8 to 210 (E_value = 0.00094) place ANA_0573 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.","","phosphatase SerB (serB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0574","609303","608059","1245","5.59","-10.37","45396","ATGGCTCAACCTCGTGTTCTCGCAATCGTCCTCGCCGGTGGCGAGGGCAAGCGCCTCATGCCCCTGACCGTCGATCGCGCCAAGCCCGCCGTGCCCTTCGGCGGCATCTACCGCCTCATCGACTTCTCCCTGTCCAACATGATCAACTCCGGCTTCCTCAAGGTCGTGGTGCTCACCCAGTACAAGTCCCACTCGCTGGACCGTCACATCTCCAAGACGTGGCGCATGTCCGACATGCTGGGCAACTACATCGCGCCGGTGCCGGCCCAGCAGCGCGTGGGCAAGCACTGGTTCCTGGGGAGCGCCGACGCGATCTACCAGTCCCTCAACCTGCTCGACGACGAGCGGCCGGACTATGTGGTCATCACCGGTGCGGACAACATCTACCGCATGGACTTCTCCCAGATGCTGGACCACCACATCGCCTCTGGTCTGCCCTGCACTGTCGCGGGCATCCGTCAGCCGCGGTCCCTGGCGGACCAGTTCGGCGTCATCGAGACCGACCCGTCCGACCGCGGCAGGATCAAGGCCTTCGTGGAGAAGCCCAAGGAGACCCCCGGCCTGCCGGACTCCCCCGACGAGGTCCTGGCCTCGATGGGCAACTACATCATGAACTCCGATGCGCTCCTGGAGGCCGTGACGGTCGACGCCGCCGACGAGACCTCCAAGCACGACATGGGCGGCAGCATCGTGCCCTGGTTCGTCAACCAGGGGGCGGCCGGCGTCTACGACTTCAAGGACAACGACGTCCCGGGCTCCTCCGAGCGCGACCGCGACTACTGGCGCGACGTGGGTACTGTGGACGCCTTCTTCGAGGCGCACCAGGACCTCATCTCGGTGACCCCCGTGTTCAACCTGTACAACGACCGCTGGCCGCTGTTCGCCGGCTACCAGGCCGCGATGCCTCCGGCCAAGTTCGTCTACGGCCACCACGAGCGCCTGGGGCACGCGGTCGACTCGATCGTCTCGCCGGGCGTCATCGTCTCCGGTGGTGAGGTGATCTCCTCGGTCCTGTCGCCCGGTGTGCGCGTCAACTCCTGGTCCTCGGTGCGCGAGTCCGTCATCATGGACGGGGCCGAGGTGGGCCGTAACACCGTGGTCAACCGCGCGATCCTGGACAAGTACGTCAAGGTCGAGGAGGGCGCCATGGTGGGGATCGACCCCGAGCACGACCGTGAGCGGGGCTTCACCGTGACCGAGTCCGGCATCACGGTGGTGGCCAAGGGTCAGCTCGTCACCCGCTGA","MAQPRVLAIVLAGGEGKRLMPLTVDRAKPAVPFGGIYRLIDFSLSNMINSGFLKVVVLTQYKSHSLDRHISKTWRMSDMLGNYIAPVPAQQRVGKHWFLGSADAIYQSLNLLDDERPDYVVITGADNIYRMDFSQMLDHHIASGLPCTVAGIRQPRSLADQFGVIETDPSDRGRIKAFVEKPKETPGLPDSPDEVLASMGNYIMNSDALLEAVTVDAADETSKHDMGGSIVPWFVNQGAAGVYDFKDNDVPGSSERDRDYWRDVGTVDAFFEAHQDLISVTPVFNLYNDRWPLFAGYQAAMPPAKFVYGHHERLGHAVDSIVSPGVIVSGGEVISSVLSPGVRVNSWSSVRESVIMDGAEVGRNTVVNRAILDKYVKVEEGAMVGIDPEHDRERGFTVTESGITVVAKGQLVTR$","Glucose-1-phosphate adenylyltransferase","Cytoplasm","glucose-1-phosphate adenylyltransferase","glucose-1-phosphate adenylyltransferase ","glucose-1-phosphate adenylyltransferase","","Nakata P.A., Greene T.W., Anderson J.M., Smith-White B.J., Okita T.W., Preiss J. Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits. Plant Mol. Biol. 1991. 17(5):1089-1093. PMID: 1657244","","","

InterPro
IPR005835
Domain

Nucleotidyl transferase
PF00483	$\"[7-280]T$	NTP_transferase

InterPro
IPR005836
Family

ADP-glucose pyrophosphorylase
PS00808	$\"[12-31]T$	ADP_GLC_PYROPHOSPH_1
PS00809	$\"[97-105]T$	ADP_GLC_PYROPHOSPH_2
PS00810	$\"[197-207]?$	ADP_GLC_PYROPHOSPH_3

InterPro
IPR011831
Family

Glucose-1-phosphate adenylyltransferase
TIGR02091	$\"[6-386]T$	glgC: glucose-1-phosphate adenylyltransfera

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[7-331]T$	no description
PTHR22572	$\"[14-412]T$	SUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF10	$\"[14-412]T$	GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE
signalp	$\"[1-16]?$	signal-peptide

","BeTs to 9 clades of COG0448COG name: ADP-glucose pyrophosphorylaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0448 is --------vdrlbce-gh---j-i--Number of proteins in this genome belonging to this COG is 1","***** IPB005836 (ADP-glucose pyrophosphorylase) with a combined E-value of 5.3e-40. IPB005836A 9-31 IPB005836B 32-65 IPB005836D 97-114 IPB005836E 121-150 IPB005836I 252-281 IPB005836G 194-214***** IPB005835 (Nucleotidyl transferase) with a combined E-value of 2.7e-13. IPB005835A 9-23 IPB005835B 170-182 IPB005835C 257-266","Residues 9-40 are 90% similar to a (ADP-GLUCOSE TRANSFERASE PYROPHOSPHORYLASE NUCLEOTIDYLTRANSFERASE GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE SUBUNIT LARGE SYNTHASE GLYCOGEN) protein domain (PDA1F3E7) which is seen in Q826D9_STRAW.Residues 9-40 are 96% similar to a (ADP-GLUCOSE TRANSFERASE PYROPHOSPHORYLASE NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE GLUCOSE-1-PHOSPHATE SUBUNIT SYNTHASE SMALL GLYCOGEN) protein domain (PDA1B1F4) which is seen in Q6AA20_PROAC.Residues 11-212 are 65% similar to a (TRANSFERASE NUCLEOTIDYLTRANSFERASE KINASE GLUCOSE-1-PHOSPHATE PYROPHOSPHORYLASE THYMIDYLYLTRANSFERASE URIDYLYLTRANSFERASE UTP-GLUCOSE-1-PHOSPHATE UTP--GLUCOSE-1-PHOSPHATE MANNOSE-1-PHOSPHATE) protein domain (PD001252) which is seen in GLC2_VIBPA.Residues 41-76 are 88% similar to a (ADP-GLUCOSE TRANSFERASE PYROPHOSPHORYLASE NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE GLUCOSE-1-PHOSPHATE GLYCOGEN BIOSYNTHESIS SUBUNIT SYNTHASE) protein domain (PD766559) which is seen in Q73WU6_MYCPA.Residues 61-114 are 94% similar to a (ADP-GLUCOSE TRANSFERASE PYROPHOSPHORYLASE NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE GLUCOSE-1-PHOSPHATE SUBUNIT GLYCOGEN BIOSYNTHESIS SYNTHASE) protein domain (PD451498) which is seen in Q8G5Y5_BIFLO.Residues 103-274 are 44% similar to a (AGPLU1) protein domain (PDA0V219) which is seen in Q6PYZ8_EEEEE.Residues 118-153 are 80% similar to a (ADP-GLUCOSE TRANSFERASE NUCLEOTIDYLTRANSFERASE PYROPHOSPHORYLASE ADENYLYLTRANSFERASE GLUCOSE-1-PHOSPHATE GLYCOGEN BIOSYNTHESIS SUBUNIT SYNTHASE) protein domain (PD415406) which is seen in Q6AA20_PROAC.Residues 159-213 are 74% similar to a (ADP-GLUCOSE TRANSFERASE NUCLEOTIDYLTRANSFERASE GLYCOGEN BIOSYNTHESIS ADENYLYLTRANSFERASE GLUCOSE-1-PHOSPHATE PYROPHOSPHORYLASE ADPGLC PPASE) protein domain (PDA1E6B8) which is seen in Q6AF21_BBBBB.Residues 216-279 are 82% similar to a (TRANSFERASE NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE GLUCOSE-1-PHOSPHATE GLYCOGEN ADP-GLUCOSE BIOSYNTHESIS PYROPHOSPHORYLASE ADPGLC PPASE) protein domain (PD768080) which is seen in Q6AF21_BBBBB.","","-45% similar to PDB:1YP2 Crystal structure of potato tuber ADP-glucose pyrophosphorylase (E_value = 4.4E_38);-45% similar to PDB:1YP3 Crystal structure of potato tuber ADP-glucose pyrophosphorylase in complex with ATP (E_value = 4.4E_38);-45% similar to PDB:1YP4 Crystal structure of potato tuber ADP-glucose pyrophosphorylase in complex with ADP-glucose (E_value = 4.4E_38);","Residues 7 to 280 (E_value = 1.7e-85) place ANA_0574 in the NTP_transferase family which is described as Nucleotidyl transferase.","","adenylyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0575","609653","610882","1230","5.09","-18.97","43848","ATGAGGGTCGACCTGCTGACCAAGGAGTACCCACCCTTCATCTACGGCGGCGCCGGAGTCCACGTCAACGAGCTCGCCAAGGTCCTGCGCCCCCTGGCGGACGTGCGCGTCCACGCCTTCGGCGGCCCCCGTGAGCCCGGCACCGAGGGCGCCGACGACGGCGTCACCGGCTACCCCGAGATCGCCGAGCTCGACGGCGCCAACGCCGCCCTGCGCACCTTCGGCGTCGACCTGGAGATGGCCCAGGGCACCGAGGGAACCGACCTCGTCCACTCCCACACCTGGTACGCCAACCTCGCCGGCCACCTGGCCGGCCTGCTCCACGGCGTCCCCCACGTCATCAGCGCCCACTCCCTAGAACCCCTGCGCCCCTGGAAGGCCGAGCAGCTCGGCGGCGGCTACGCCCTGTCCTCCTGGGCGGAGAAGACCGCCTACGAGGCCGCCTCCGGGATCATCGCGGTCTCCAACGGCATGCGCGAGGACATCCTGCGCTGCTACCCCGCCATCGACCCCGAGCGCGTCAAGGTCGTCCACAACGGCATCGACCTTGAGGCATGGAAGCACCCCCAGGGCCAGGAGGCCGACGCCGCGGCCGCCACCACCCTCAAGCGCCTGGGCATCGACCCCGACCGCCCCACCATCGTCTTCGTCGGACGCATCACCCGACAGAAGGGCCTGCCGCACCTGCTGCGCGCCTGCGAGCAGCTGCCCGCGGACGTCCAGGTCATCCTGTGCGCCGGCGCCCCCGACACCCCCGAGATCAAGGCCGAGGTCGAGGGCCTCGTGGCCCACCTGCGCGACAAGCGCACCGGCGTGGTCTGGATCGAGGAGATGCTGCCGCGCCCCGAGCTCATCGCCGTACTGGCCGCCTCCGACGTCTTCGTGTGCCCCTCCGTCTACGAGCCCCTGGGCATCGTCAACCTCGAGGCCATGGCCGTGGGCCTGCCCGTCGTCGGCTCAGCCACCGGCGGCATCCCAGACGTCATCGTCGACGGCGAGACCGGCCTGCTGGTGCCCATCGAGCAGGTCCAGGACGGCACCGGCACCCCCATCGACCCGGCCCGCTTCGAGGCCGATCTGGCCGAGCGCCTCACCACCCTGGTCACCGACACCGAGGCAGCCAAGGCCATGGGGCAGGCCGCCCGACGCCGCGTCGAGGAGCACTTTGCTTGGCAGGCCATCGCCCAGCGCACCATGGACGTCTACAACTGGGTCCTGGCCCAGGGCTGA","MRVDLLTKEYPPFIYGGAGVHVNELAKVLRPLADVRVHAFGGPREPGTEGADDGVTGYPEIAELDGANAALRTFGVDLEMAQGTEGTDLVHSHTWYANLAGHLAGLLHGVPHVISAHSLEPLRPWKAEQLGGGYALSSWAEKTAYEAASGIIAVSNGMREDILRCYPAIDPERVKVVHNGIDLEAWKHPQGQEADAAAATTLKRLGIDPDRPTIVFVGRITRQKGLPHLLRACEQLPADVQVILCAGAPDTPEIKAEVEGLVAHLRDKRTGVVWIEEMLPRPELIAVLAASDVFVCPSVYEPLGIVNLEAMAVGLPVVGSATGGIPDVIVDGETGLLVPIEQVQDGTGTPIDPARFEADLAERLTTLVTDTEAAKAMGQAARRRVEEHFAWQAIAQRTMDVYNWVLAQG$","Glycogen synthase","Cytoplasm","possible glycosyltransferase","glycogen synthase","glycogen synthase","","Tzvetkov M., Klopprogge C., Zelder O., Liebl W. Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition. Microbiology 2003. 149:1659-1673. PMID: 12855718","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[198-384]T$	Glycos_transf_1

InterPro
IPR011875
Family

Glycogen synthase, corynebacterial
TIGR02149	$\"[1-406]T$	glgA_Coryne: glycogen synthase, Corynebacte

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-406]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF44	$\"[2-406]T$	GLYCOSYLTRANSFERASE

","BeTs to 23 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","***** IPB013534 (Starch synthase catalytic region) with a combined E-value of 1.6e-16. IPB013534B 87-101 IPB013534D 139-162 IPB013534F 289-329***** IPB001296 (Glycosyl transferase, group 1) with a combined E-value of 9.5e-15. IPB001296B 297-329","Residues 1-81 are 62% similar to a (TRANSFERASE GLYCOSYL GLYCOSYLTRANSFERASE 2.-.-.- GLYCOSYLTRANSFERASES PREDICTED SYNTHASE GLYCOGEN POSSIBLE) protein domain (PD079772) which is seen in Q8G624_BIFLO.Residues 88-136 are 93% similar to a (TRANSFERASE GLYCOSYL GLYCOSYLTRANSFERASE 2.-.-.- GLYCOSYLTRANSFERASES SYNTHASE GLYCOGEN POSSIBLE PREDICTED) protein domain (PD985694) which is seen in Q9X9U5_STRCO.Residues 137-232 are 70% similar to a (TRANSFERASE GLYCOSYL GLYCOSYLTRANSFERASE 2.-.-.- GLYCOSYLTRANSFERASES SYNTHASE GLYCOGEN U1756O POSSIBLE PREDICTED) protein domain (PD970597) which is seen in Q826E0_STRAW.Residues 138-187 are 74% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL MANNOSYLTRANSFERASE 2.4.1.- BIOSYNTHESIS GROUP FAMILY B PROBABLE) protein domain (PD013465) which is seen in Q8RCY0_THETN.Residues 214-285 are 72% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS GROUP TRANSFERASE SYNTHASE FAMILY STARCH LIPOPOLYSACCHARIDE) protein domain (PD000427) which is seen in Q8RCY0_THETN.Residues 241-296 are 73% similar to a (TRANSFERASE GLYCOSYL GLYCOSYLTRANSFERASE 2.-.-.- GLYCOSYLTRANSFERASES SYNTHASE GLYCOGEN POSSIBLE PREDICTED) protein domain (PD481515) which is seen in Q8G624_BIFLO.Residues 298-339 are 92% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE SYNTHASE GLYCOSYL GLYCOGEN BIOSYNTHESIS STARCH GROUP FAMILY TRANSFERASE) protein domain (PD064079) which is seen in Q8G624_BIFLO.Residues 340-406 are 65% similar to a (GLYCOSYLTRANSFERASE TRANSFERASE POSSIBLE) protein domain (PD743678) which is seen in Q8G624_BIFLO.","","-43% similar to PDB:2BIS STRUCTURE OF GLYCOGEN SYNTHASE FROM PYROCOCCUS ABYSSI (E_value = 1.4E_17);-51% similar to PDB:2BFW STRUCTURE OF THE C DOMAIN OF GLYCOGEN SYNTHASE FROM PYROCOCCUS ABYSSI (E_value = 4.6E_16);-39% similar to PDB:2GEJ Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man (E_value = 2.2E_10);-39% similar to PDB:2GEK Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP (E_value = 2.2E_10);","Residues 198 to 384 (E_value = 3.9e-33) place ANA_0575 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","glycosyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0576","611733","610939","795","5.14","-11.87","27847","ATGGTGACCGCTCCCCCTCGAGGCTCGCCTCACCACCATTCACTATGGTTGGCCCCCATGGATCCCCTCAACCCGCCTGTCAGCATCGTGCTGGCCCTGTGGGCGCCATCGCCCTCCTCCCACGGCATGTCGCTCGTTGAAGGCCCCGACGGCGCCCATGACGTCATCGGCAGCGTCGTCACCGGGGGCTCGGACACACCGACTGCCGCCGACGACGGTCCAGGACGCGTCAGCCTGGAACGGTGGCTCGCCTCCGCCCGCCCCCTGAGTCGGGTGAGCGCGGTACTGCCCTCACCGGCCGGAGGCACCGGCACCTGGGGGCTCCTTCCCGACATCGAGGAGGGCGTCGTGCTGGAGGGGGCAGCCGGCCGGGTGCTGCTGGTTCCTGAGGACTCCGGCACCTCGGTGTCCTGGCACGCCGAGCCACTCAGCTCCCCGCTGCCTCCACTGGATGCGGCACACGCCCGTCGGCAGGTGCACGCCGCCACCGAGGAGGCCATCGAGGCGCTCATCGAGCTCGACCTGGCCCGCGAGCGCCCGGACATGGCCGACACCCTCAATGACCTGCTCACCGCGGTAGTGGATCCGCGGCTCGTCCCGCCGTGGCTGGCGCGCCGTGATCGGGAGCTGTTGGAGCGCTCCTTGCGCCTGGCGGGGATGTGCGAGCTGGCCCTGGACGACGATGGTGCGGCCACGACCGCCCTGCAGGCGCAGCGACGGGCCGACGTCCTGCGCCCGCTGCTGGCGGTGGCGCGTCACGGTGCCGCTGCGGCCACCGAGTGGTGGGCCCGGTAG","MVTAPPRGSPHHHSLWLAPMDPLNPPVSIVLALWAPSPSSHGMSLVEGPDGAHDVIGSVVTGGSDTPTAADDGPGRVSLERWLASARPLSRVSAVLPSPAGGTGTWGLLPDIEEGVVLEGAAGRVLLVPEDSGTSVSWHAEPLSSPLPPLDAAHARRQVHAATEEAIEALIELDLARERPDMADTLNDLLTAVVDPRLVPPWLARRDRELLERSLRLAGMCELALDDDGAATTALQAQRRADVLRPLLAVARHGAAAATEWWAR$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0579","611798","612619","822","6.00","-7.13","29387","ATGACCAGTGTCCTGCATCTCGACGACGTCTCACTGCACCGCGGCAGCCACCAGATCCTCAGTCACGTCAGCTGGACCGTGGACGAGGGGCAGCACTGGGTGCTGCTGGGGTCCAACGGCGCGGGCAAGACCACGATCGCCAGGATCGCCTCGGCCAGGCTCTTCCCCTCCTCCGGCACGGTCGACATCCTCTCCGAGCGGCTCGGGCGCGTGGACGTCTCCGAGCTCCACCCCCGTATCGGCCTGTTGTCCTCGGCCCTGGCCGCCGATGTCCAGAACGGCGAGAAGGTGCTCGGCGTGGTCCTGTCGGCCTCCTACGGGCGCATCGGGCGCTGGCGCGAGGAGTACGACGACTTCGACCTCGAGCGCGCTCACGCCCTGCTGGGCGCCCTGGGGGCCGCTCACCTGGTCGACCGGTCGTGGGGAACGCTGTCATCGGGGGAGCGCAAGCGCGTCGAGCTGGCTCGCGCTCTGATGCCGGACCCGGAGATGCTCTTCCTGGATGAGCCCGCCTCGGGGCTGGACCTGGCCGGCCGCGAGCAGCTCCTGGCGGCGCTCACCGAGATCATCTCCTCGCCCGACTCGCCCTCCATGGTCCTGGTGACCCACCACCTGGAGGAGATCCCGGAGGGCTTCACCCACGCGCTCACGCTGCGTGAGGGGAAGATCGTGGGCTCCGGCCCGCTTCAGGAGGTCCTCACCGCGGACACGATCAGCACGACCTTCGGTATGCCGCTGGAGGTCACCTACGACCGCGGTCGCTACGCGGCCAGGGGGCTCCCTGCCGGCCACGGCAGGCGCGTCGCCGAGGCCAAGGGCTGA","MTSVLHLDDVSLHRGSHQILSHVSWTVDEGQHWVLLGSNGAGKTTIARIASARLFPSSGTVDILSERLGRVDVSELHPRIGLLSSALAADVQNGEKVLGVVLSASYGRIGRWREEYDDFDLERAHALLGALGAAHLVDRSWGTLSSGERKRVELARALMPDPEMLFLDEPASGLDLAGREQLLAALTEIISSPDSPSMVLVTHHLEEIPEGFTHALTLREGKIVGSGPLQEVLTADTISTTFGMPLEVTYDRGRYAARGLPAGHGRRVAEAKG$","ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA","Cytoplasm, Membrane","ABC-type transporter, ATPase component","ABC-type molybdenum transport system; ATPase component","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[143-186]T$	Q6A7I8_PROAC_Q6A7I8;
PF00005	$\"[30-221]T$	ABC_tran
PS50893	$\"[5-245]T$	ABC_TRANSPORTER_2
PS00211	$\"[144-158]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[29-229]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[5-243]T$	no description
PTHR19222	$\"[5-252]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31	$\"[5-252]T$	METAL ABC TRANSPORTER

","BeTs to 4 clades of COG1119COG name: ABC-type molybdenum transport system, ATPase component/photorepair protein PhrAFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1119 is ------y--drlb-e--h--------Number of proteins in this genome belonging to this COG is 1","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.1e-21. IPB005074C 19-66 IPB005074D 132-175***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 5.3e-16. IPB013563A 19-53 IPB013563C 141-168 IPB013563D 197-249***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.1e-12. IPB010509B 30-55 IPB010509D 139-183***** IPB005116 (TOBE domain) with a combined E-value of 7.3e-10. IPB005116A 37-53 IPB005116C 144-157 IPB005116D 164-183***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.4e-09. IPB010929K 17-61 IPB010929M 141-187","Residues 3-87 are 65% similar to a (ATP-BINDING) protein domain (PDA0K5Q4) which is seen in P97112_LEUMC.Residues 3-94 are 55% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD276706) which is seen in Q9RSH9_DEIRA.Residues 4-110 are 58% similar to a (YLMA ATP-BINDING) protein domain (PDA0J3Q6) which is seen in O31723_BACSU.Residues 12-228 are 41% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 20-68 are 75% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q829D1_STRAW.Residues 31-81 are 76% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER ABC-TYPE ATPASE TRANSPORTER PROBABLE MOLYBDENUM PROTEIN) protein domain (PDA1D8Z6) which is seen in Q7TXD9_MYCBO.Residues 70-204 are 55% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 138-248 are 52% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.Residues 143-186 are 88% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6A7I8_PROAC.Residues 144-224 are 58% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 144-233 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 144-257 are 57% similar to a (PROBABLE ATP-BINDING ABC TRANSPORTER ATP BINDING) protein domain (PD763654) which is seen in Q8G625_BIFLO.Residues 187-254 are 64% similar to a (YLMA ATP-BINDING) protein domain (PDA0I9A8) which is seen in O31723_BACSU.Residues 189-255 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I992) which is seen in Q9KAL7_BACHD.Residues 209-254 are 71% similar to a (ATP-BINDING ABC TRANSPORTER COMPONENT TRANSPORTER PROBABLE ABC-TYPE PROTEIN SYSTEM ATPASE) protein domain (PD012247) which is seen in Q6A7I8_PROAC.","","-47% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 3.3E_14);-46% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 1.3E_13);-44% similar to PDB:2ONK ABC transporter ModBC in complex with its binding protein ModA (E_value = 2.2E_13);-46% similar to PDB:2IXF CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645Q, Q678H MUTANT) (E_value = 2.8E_13);-48% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 4.8E_13);","Residues 30 to 221 (E_value = 1.5e-41) place ANA_0579 in the ABC_tran family which is described as ABC transporter.","","transporter, ATPase component (AJ275980)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0580","612726","613193","468","8.22","0.90","15987","ATGGAATGGCTGTTCTGGGTCGCAGGGGCGCTGCTCCTCGTCGTCATCGAGACGATGACAGCGGATCTCACCTTCCTCATGATCGCCGGAGGTGCGCTGGGAGGAGGGCTGACATCCTTCCTCGGCGGGCCCGTGTGGGCGCAGGTCGTGGTCTTCGCCTGCGTCTCCACCCTGCTTCTCTTCGCCGTGCGCCCCTGGGCCAAGCGTCGCCTTGCGGCCGCCACCCCGCAGATGAAGACCAACGTCGAGGCCCTCATCGGTCGGTCTGCCGTCACCATTACTCCTGTCGACCGTGAAGGTGGGCGGGTGCGCCTGGGCGGCGAGGAGTGGAGCGCCCGCCTGGCTCCCGCCGTCCAGGGAGGCGTCACCCGTCTGGAGGCCGGGGTGAGTGTGACCGTGGCCCAGATCGACGGGGCCGTGGCCGTGGTCGCCCCGGTGACGACCTCCACCACCGCTCCCGCGTCCTGA","MEWLFWVAGALLLVVIETMTADLTFLMIAGGALGGGLTSFLGGPVWAQVVVFACVSTLLLFAVRPWAKRRLAAATPQMKTNVEALIGRSAVTITPVDREGGRVRLGGEEWSARLAPAVQGGVTRLEAGVSVTVAQIDGAVAVVAPVTTSTTAPAS$","Membrane protein implicated in regulation of membrane protease activity","Membrane, Cytoplasm","MAV145","hypothetical protein","protein of unknown function DUF107","","Garcia-rodriguez F.M., Toro N. Sinorhizobium meliloti nfe (nodulation formation efficiency) genes exhibit temporal and spatial expression patterns similar to those of genes involved in symbiotic nitrogen fixation. Mol. Plant Microbe Interact. 2000. 13(6):583-591. PMID: 10830257","","","

InterPro
IPR002810
Family

Nodulation efficiency, NfeD
PF01957	$\"[5-147]T$	NfeD

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[44-62]?$	transmembrane_regions

","BeTs to 5 clades of COG1585COG name: Membrane protein implicated in regulation of membrane protease activityFunctional Class: N [Cellular processes--Cell motility and secretion] Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1585 is --m-k---vdr--cefghs--j----Number of proteins in this genome belonging to this COG is 1","***** IPB002810 (Protein of unknown function DUF107) with a combined E-value of 5.8e-14. IPB002810A 10-38 IPB002810B 94-111 IPB002810C 131-146","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 147 (E_value = 1.3e-15) place ANA_0580 in the NfeD family which is described as NfeD-like.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0582","613255","614553","1299","4.91","-15.78","45367","GTGCCCTTCGTCTCCATCATTTTGCTTCTCGTGGCCGTCCTGGTCATCGTCGCCATCTTCCGGGCGGTGCGGATCGTCAAGCAGAGCACTGCGATCATCGTTGAGCGCCTGGGGCGCTTCCAGGCGGCCTACGGCGCTGGAATGCACTTCCTGGTGCCCTTCATCGACCGGGTGCGCAACATCATGGACCTGCGTGAGCAGGTCGTCTCCTTCCCGCCTCAGCCCGTCATCACCTCCGACAACCTCGTGGTGAGCATCGACTCGGTGGTCTACTACCAGATCACCGACCCCATGCGCGCCACCTACGAGATCTCCAACTACCTGCAGGCCATTGAGCAGTTGACGGTCACCACGCTGCGCAACGTCGTCGGATCCATGGACCTGGAGCAGACGCTGACCAGCCGCGACCAGATCAACGGCCAGCTGCGAGGCGTCCTGGACCAGGCCACCGGCCGCTGGGGAATCCGCGTCAACAGCGTGGAGCTGAAGTCCATCGACCCGCCGGCCTCCATCCAGGGCTCCATGGAGCAGCAGATGCGCGCCGAGCGTGACCGCCGCGCCGCGATCCTGACCGCCGAGGGTGTCAAGCAGTCCCAGATTCTTACGGCAGAGGGTGACAAGCAGTCCGCGATCCTGCGCGCCGAGGGGCAGGCGCAGTCCGCGATCCTCAAGGCCCAGGGTGAGTCGCGCGCCATCCTTCAGGTCTTCGACGCCATCCACCGCGGTAACGCCGACTCCAAGCTGCTGGCCTACCAGTACCTCCAGACCCTGCCCAAGATCGCCAACGGCTCCTCCTCCAAGATGTGGATCGTGCCCACGGAGTTCACGGCGGCGCTCGACGGCATCGCCGGCGCCCTGGGCGGTGGCAAGGACGGTGGCCCCGGCGGCTCGGACGACTCCGACGACGACGCCGCCCGTCCCGGTGTCGACCTCTCCGGCAGTGAGCTCGACCTGGGGATCGCCTCGGATCTGGCCAGCACCAGTCTCCAGGCCCCCGAGGAGGCCCTCGCCCAGGCCCGTGGTGAGGTCGAGTCGGCCTCCCAGGAGGCCAGTGAGGAGCCCGCACCCAAGGCAGGCGTCTCCCCGAAGGCTCCCACGGATGAGGCCGATGGCGGGGCCACCGTGAGCGTTCCGACCTCCGACGGCCTTGAAGGGCCTCATGCCGCGCACGGCAGCCACGTGGCCGCCCCCGAGGAGGCCCAGCCCGGTTCCGTGCCCCCTCGCGGCGGATACGGCATCCAGGCCCAGCCCGGCTACGGCACGCCTCCCGGCGCGCCCCAGGGTCCCTACGGGGCCTGA","VPFVSIILLLVAVLVIVAIFRAVRIVKQSTAIIVERLGRFQAAYGAGMHFLVPFIDRVRNIMDLREQVVSFPPQPVITSDNLVVSIDSVVYYQITDPMRATYEISNYLQAIEQLTVTTLRNVVGSMDLEQTLTSRDQINGQLRGVLDQATGRWGIRVNSVELKSIDPPASIQGSMEQQMRAERDRRAAILTAEGVKQSQILTAEGDKQSAILRAEGQAQSAILKAQGESRAILQVFDAIHRGNADSKLLAYQYLQTLPKIANGSSSKMWIVPTEFTAALDGIAGALGGGKDGGPGGSDDSDDDAARPGVDLSGSELDLGIASDLASTSLQAPEEALAQARGEVESASQEASEEPAPKAGVSPKAPTDEADGGATVSVPTSDGLEGPHAAHGSHVAAPEEAQPGSVPPRGGYGIQAQPGYGTPPGAPQGPYGA$","Band 7 protein","Membrane, Cytoplasm","Membrane protease subunits, stomatin/prohibitinhomologs","band 7 protein","band 7 protein","","Stewart G.W. Stomatin. Int. J. Biochem. Cell Biol. 1997. 29(2):271-274. PMID: 9147127Foley M., Tilley L. Quinoline antimalarials: mechanisms of action and resistance. Int. J. Parasitol. 1997. 27(2):231-240. PMID: 9088993","","","

InterPro
IPR001107
Family

Band 7 protein
PF01145	$\"[22-196]T$	Band_7
SM00244	$\"[21-179]T$	PHB

InterPro
IPR001972
Family

Stomatin
PR00721	$\"[28-50]T$ $\"[76-97]T$ $\"[111-128]T$ $\"[131-154]T$ $\"[155-173]T$ $\"[174-195]T$	STOMATIN

noIPR
unintegrated

unintegrated
PTHR10264	$\"[3-308]T$	STOMATIN-RELATED
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-23]?$	transmembrane_regions

","BeTs to 24 clades of COG0330COG name: Membrane protease subunits, stomatin/prohibitin homologsFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0330 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB001972 (Stomatin) with a combined E-value of 2.4e-81. IPB001972A 22-38 IPB001972B 46-88 IPB001972C 89-127 IPB001972D 128-162 IPB001972E 165-195 IPB001972F 252-261 IPB001972E 198-228 IPB001972E 187-217","Residues 33-94 are similar to a (TRANSMEMBRANE PROTEASE MEMBRANE HFLC HFLK FAMILY STOMATIN BAND HYDROLASE STOMATIN-LIKE) protein domain (PD300956) which is seen in Q9X9Z6_STRCO.Residues 76-274 are 44% similar to a (BAND DOMAIN / FAMILY SPFH) protein domain (PD320696) which is seen in Q87TY4_PSESM.Residues 96-168 are similar to a (TRANSMEMBRANE PROTEASE MEMBRANE HFLK STOMATIN FAMILY BAND STOMATIN-LIKE SPFH DOMAIN/BAND) protein domain (PD186090) which is seen in Q9K458_STRCO.Residues 169-208 are 82% similar to a (TRANSMEMBRANE MEMBRANE PROTEASE FAMILY STOMATIN-LIKE BAND SPFH DOMAIN/BAND STOMATIN GNA1220) protein domain (PD001059) which is seen in Q97K67_CLOAB.Residues 170-231 are similar to a (TRANSMEMBRANE PROTEASE HFLC HYDROLASE MEMBRANE SUBUNIT 3.4.-.- LARGE ATP E) protein domain (PD034740) which is seen in Q9K458_STRCO.Residues 170-266 are 55% similar to a (TRANSMEMBRANE) protein domain (PD808038) which is seen in Q86IY7_DICDI.Residues 235-274 are 87% similar to a (TRANSMEMBRANE SECRETED PROTEASE STOMATIN/PROHIBITIN HOMOLOG HOMOLOGS SUBUNIT MEMBRANE SUBUNITS RV1488/MT1533.2/MB1524) protein domain (PDA001B7) which is seen in Q829C9_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 22 to 196 (E_value = 1.7e-84) place ANA_0582 in the Band_7 family which is described as SPFH domain / Band 7 family.","","protease subunits, stomatin-prohibitin homologs","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0583","614807","615562","756","5.78","-5.43","25995","ATGGCCGAGTCCTCCAAGGTCATCACGCGCGCCGTGGCCGCCGGGCACGCCCCGCGCTCCTTCCTCATGGCCCCGCGTCACCTGGAGGAGATGCGCCCGGTCATCGCCTCCGCGGCCGGATGCGCAGGCAGCGACGACGGCGGTGAGGTCCCCGTGTTCGTCGCCCCCGAGGAGGTCCTGGAGTCCATCACGGGATTCCACCTGCACCGCGGGGCCCTGGCCGCTATGAACCGGCCCGAGCTCGCCGGTGTTCCCGAGCTGCTTGCGGCCGCCCGTGGGGGAGCGGGGGCCAGGCGGGTCGCGATCCTGGAGGACCTGGTGGACCACACGAACGTGGGGGCCGCCTTCCGCAGCGCAGCCGCCCTGGGGATCGACGCCGTCCTGGTCACTCCGCGCTGTGCGGACCCCCTCTACCGGCGCAGCGTGCGCGTCTCCATGGGCACCGTCTTCCAGGTCCCCTGGACCCGGATCGAGCGCTGGCCCGCCATGGACGAGCTCCACGCACAGGGCTTCACCGTGGCCGCCCTGGCACTGTCGGACACCTCCGTGGCACTGGATGAGTTCGCGGCCTCCACGGCGTGCACCGGCGCGGACTCCAGGGTCGCCGTCGTCCTGGGCACGGAGGGCGACGGACTGTCCCACCGGACCGTCACCGCGGCCGACGAGGTGGTGCGCATCCCCATGGCCGGGGGAGTGGACTCCCTCAACGTGGCGGCAGCGGCCGCCGTGGCCTTCTGGGCGCTGCGTCTGCCCTGA","MAESSKVITRAVAAGHAPRSFLMAPRHLEEMRPVIASAAGCAGSDDGGEVPVFVAPEEVLESITGFHLHRGALAAMNRPELAGVPELLAAARGGAGARRVAILEDLVDHTNVGAAFRSAAALGIDAVLVTPRCADPLYRRSVRVSMGTVFQVPWTRIERWPAMDELHAQGFTVAALALSDTSVALDEFAASTACTGADSRVAVVLGTEGDGLSHRTVTAADEVVRIPMAGGVDSLNVAAAAAVAFWALRLP$","tRNA/rRNA methyltransferase (SpoU)","Cytoplasm","possible tRNA/rRNA methyltransferase","putative rRNA methylase ","tRNA/rRNA methyltransferase (SpoU)","","Persson B.C., Jager G., Gustafsson C. The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity. Nucleic Acids Res. 1997. 25(20):4093-4097. PMID: 9321663Koonin E.V., Rudd K.E. SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases. Nucleic Acids Res. 1993. 21(23):5519-5519. PMID: 8265370Sirum-Connolly K., Mason T.L. Functional requirement of a site-specific ribose methylation in ribosomal RNA. Science 1993. 262(5141):1886-1889. PMID: 8266080","","","

InterPro
IPR001537
Domain

tRNA/rRNA methyltransferase, SpoU
PD001243	$\"[100-236]T$	Q6AF11_BBBBB_Q6AF11;
PF00588	$\"[98-246]T$	SpoU_methylase

noIPR
unintegrated

unintegrated
G3DSA:3.40.1280.10	$\"[93-246]T$	no description
PTHR12029	$\"[51-246]T$	RNA METHYLTRANSFERASE
PTHR12029:SF7	$\"[51-246]T$	RRNA METHYLASE

","BeTs to 20 clades of COG0566COG name: rRNA methylasesFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0566 is a-----yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB001537 (tRNA/rRNA methyltransferase (SpoU)) with a combined E-value of 1e-23. IPB001537A 101-125 IPB001537B 203-243","Residues 14-78 are 61% similar to a (METHYLTRANSFERASE TRANSFERASE RRNA METHYLASE RNA TRNA/RRNA 2.1.1.- FAMILY RIBOSOMAL 23S) protein domain (PD091740) which is seen in Q6A7J2_PROAC.Residues 100-236 are 75% similar to a (METHYLTRANSFERASE TRANSFERASE RRNA METHYLASE TRNA/RRNA 2.1.1.- RNA FAMILY SPOU METHYLTRANSFERASE) protein domain (PD001243) which is seen in Q6AF11_BBBBB.Residues 103-236 are 48% similar to a (RRNA METHYLASE METHYLTRANSFERASE) protein domain (PD949438) which is seen in Q7VCJ2_PROMA.","","-49% similar to PDB:1GZ0 23S RIBOSOMAL RNA G2251 2'O-METHYLTRANSFERASE RLMB (E_value = 1.5E_10);","Residues 98 to 246 (E_value = 8.7e-44) place ANA_0583 in the SpoU_methylase family which is described as SpoU rRNA Methylase family.","","tRNA-rRNA methyltransferase (AL157953)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0584","617817","615709","2109","5.38","-11.97","72715","ATGGCAACCACGACCTCAACCCCTGAGGCAATCCTCGACGCCGTGGGCGGCGCCGAGAACATCATCCATTTCACCCACTGCGCTACCCGACTGCGTTTCGAGCTCAAGGACGCCTCCGGCATCGACAAGGCGGCCGTCGAGGCCATCCCGGGCGTCATGGGCGCCGTTCCCCAGTCCGGGGACCGCTACCAGATCGTCATCGGTGGTGCGGTGCAGAGCGTGTACGACGAGATCAACAGCCTGCCGGCCATGAAGAGCCAGGGCGGCTCCTCCGGCTCGGGCCAGTCCGACGCCGACGTCAAGGCCGCCGCCCGGGCCAAGGCCCGCGGCAAGAACGCCTACGTCGATGCCTTCTTCGAGTACCTGTCCGACTCCTTCCGCCCCCTGCTACCGGTGCTGCTCGGCGCCTCGCTCATCATCGCGGGCCTCGCGGTACTGGATTCGTTCGGCGTCATCAATGCCAGTGACCCAACCCTGACGGCCGCGGACAAGCCTGCCGCACAGGTCTTCGCGGAAGCCATGTTCAAGTCGGTGTTCCACTTTCTGCCCATCATGGTGGCCTACAACGCTGCCAAAAAGCTCAACATCGACCCTTGGGTCGGCGCTGCGGTCATGGCCGCACTTATGACGCCTCAGTTCCTCGACCTCAGCAAGGCAATGGGAACGACCTGCACCCACAACGCCACGTTGAACAAGGATCTGTGCGTCGCGCATGTCGCGGGCCTTCCCATGCAGCTCAACGACTACAGCGGCCAGGTCTTCGTGCCCCTCATGATGGTCGCCGTCCTGGCCCTGGTCTACAAGGGTCTGGCCAAGCTCATTCCCTCCAACGTGCAGATGGTGTTTGTTCCATTCTTCTCATTCATCATCATGATGCCGGTGACGGCCTTCATCATCGGTCCAGTAGGTGTCTGGGTCGGTACAGGCCTGGGATCCGGACTGGCGTGGCTCAACACGAGCGCCCCGATCGTCTTCGCGATCGTCATCCCGCTGCTCTACCCGTTCCTGGTGCCGCTGGGTCTGCACTGGCCTCTCAACGCCATCATGCTGGCCAACATCAGTACGCTGGGCTACGACTTCATCCAGGGCCCCATGGGCTCGTGGAACTTCGCCTGCTTCGGCGCCACCGCCGGTGTGCTGGTCCTGGCCATTCGTGACAAGGACAAGGTCATGCGTCAGACAGCCTCTGGCGCCCTGGCCGCAGGCCTCTTCGGTGGCATCTCCGAGCCGAGCCTCTACGGTATCCACCTCCGCTTCAAGCGCATCTACCCGCGTCTGCTGGCCGGCTGCCTCGTGGGTGGTCTCATCACCGGTATCGGCGGCGGCATCAAGGCCTCCACCTTCGTGTTCAGCTCGCTGCTGAGCATCCCGGTCTTCTCCCCGATGCCTCTGTACGGCATCGCCATCACCGCGGCCTTCGCCACGTCCATGACTCTCATCATTCTCACGGACTACCGCACCAAGGAGGAGCGCGCCGAGGCTCGTGCGGCGGCGGCTGCCGCTGGCGAGGCCATCGCCTCCACTGAGGCGAAGCCTGCTGAGAAGAAGGAGACCGACGGCGCCGCTGCGGCTGCCGCTCCCGTGGAGGAGGGCGACCGGACTGCGAAGGCGCCCACGCCCAAGCCGGCCCTCGTTCCCGGTGCGGTCACTGAGATCGCCTCGCCTCTCAAGGCCACGACCATGGACCTGGACAAGGTCCCCGACCCGGTGTTCTCCTCGGGCGCCGTCGGTCAGGGCGTGGGCCTGGAGCCCCAGGGCGACATCGTCGTCACGGCTCCGGCGGACGGCACCGTCGTCGTGGCCCCGTCCTCGGGGCACGCCTTCGGCATCACCCTGGACAGCGGCGTGGAGATCCTCATCCACGTGGGTCTGGACACCGTCAACCTGGAGGGCCAGGGCTTCGACGTCAAGGTCTCCCAGGGCGACCGCGTCAGCGCGGGACAGGAGCTCGTCCGCGTGGACCGCTCCGTCATCGAGCAGGCCGGTTACCCGCTGACCACGCCGGTGCTCGTCACCAACACCGCCTCCTTCGCCTCGGTCGAGGTCGTCGGCGGCGACTCGGTGGAGCCCGGCGAGGCCCTCATCAAGGTCACCGCGCCTGAGGCCTGA","MATTTSTPEAILDAVGGAENIIHFTHCATRLRFELKDASGIDKAAVEAIPGVMGAVPQSGDRYQIVIGGAVQSVYDEINSLPAMKSQGGSSGSGQSDADVKAAARAKARGKNAYVDAFFEYLSDSFRPLLPVLLGASLIIAGLAVLDSFGVINASDPTLTAADKPAAQVFAEAMFKSVFHFLPIMVAYNAAKKLNIDPWVGAAVMAALMTPQFLDLSKAMGTTCTHNATLNKDLCVAHVAGLPMQLNDYSGQVFVPLMMVAVLALVYKGLAKLIPSNVQMVFVPFFSFIIMMPVTAFIIGPVGVWVGTGLGSGLAWLNTSAPIVFAIVIPLLYPFLVPLGLHWPLNAIMLANISTLGYDFIQGPMGSWNFACFGATAGVLVLAIRDKDKVMRQTASGALAAGLFGGISEPSLYGIHLRFKRIYPRLLAGCLVGGLITGIGGGIKASTFVFSSLLSIPVFSPMPLYGIAITAAFATSMTLIILTDYRTKEERAEARAAAAAAGEAIASTEAKPAEKKETDGAAAAAAPVEEGDRTAKAPTPKPALVPGAVTEIASPLKATTMDLDKVPDPVFSSGAVGQGVGLEPQGDIVVTAPADGTVVVAPSSGHAFGITLDSGVEILIHVGLDTVNLEGQGFDVKVSQGDRVSAGQELVRVDRSVIEQAGYPLTTPVLVTNTASFASVEVVGGDSVEPGEALIKVTAPEA$","PTS system, glucose-specific IIABC component","Membrane, Cytoplasm","glucose permease","phosphotransferase system IIC component; glucose/maltose/N-acetylglucosamine-specific ","PTS system, glucose subfamily, IIA subunit","","Saier Jr M.H., Reizer J. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 1992. 174(5):1433-1438. PMID: 1537788","","","

InterPro
IPR001127
Domain

Phosphotransferase system, sugar-specific permease EIIA 1 domain
PD002243	$\"[552-673]T$	Q6A8Q9_PROAC_Q6A8Q9;
PF00358	$\"[547-680]T$	PTS_EIIA_1
TIGR00830	$\"[552-673]T$	PTBA: PTS system, glucose subfamily, IIA co
PS51093	$\"[568-673]T$	PTS_EIIA_TYPE_1
PS00371	$\"[615-627]T$	PTS_EIIA_TYPE_1_HIS

InterPro
IPR001996
Domain

Phosphotransferase system, EIIB
PD001476	$\"[35-74]T$	Q6A8Q9_PROAC_Q6A8Q9;
PF00367	$\"[8-42]T$	PTS_EIIB
PS51098	$\"[5-88]T$	PTS_EIIB_TYPE_1
PS01035	$\"[20-37]T$	PTS_EIIB_TYPE_1_CYS

InterPro
IPR003352
Domain

Phosphotransferase system, EIIC
PF02378	$\"[123-433]T$	PTS_EIIC

InterPro
IPR013013
Domain

Phosphotransferase system, EIIC component, type 1
PS51103	$\"[120-501]T$	PTS_EIIC_TYPE_1

noIPR
unintegrated

unintegrated
G3DSA:2.70.70.10	$\"[538-700]T$	no description
G3DSA:3.30.1360.60	$\"[2-95]T$	no description
tmhmm	$\"[129-149]?$ $\"[194-214]?$ $\"[253-271]?$ $\"[285-305]?$ $\"[314-336]?$ $\"[366-384]?$ $\"[423-443]?$ $\"[462-482]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB001996 (Phosphotransferase system PTS, EIIB domain) with a combined E-value of 5.6e-25. IPB001996A 11-54 IPB001996B 59-68***** IPB001127 (Sugar-specific permease, EIIA 1 domain) with a combined E-value of 7.9e-25. IPB001127 590-634***** IPB011535 (Phosphotransferase system, glucose-like IIB component) with a combined E-value of 2e-15. IPB011535A 8-41","Residues 1-83 are 56% similar to a (ENZYME TRANSFERASE II SUCROSE PHOSPHOTRANSFERASE) protein domain (PD763360) which is seen in Q82GH2_STRAW.Residues 10-81 are 62% similar to a (TRANSFERASE PHOSPHOTRANSFERASE SUGAR) protein domain (PD235644) which is seen in Q9RL52_STRCO.Residues 35-74 are 90% similar to a (PTS COMPONENT SYSTEM IIBC ENZYME TRANSFERASE IIABC SYSTEM PHOSPHOTRANSFERASE SUCROSE-SPECIFIC) protein domain (PD001476) which is seen in Q6A8Q9_PROAC.Residues 178-220 are 81% similar to a (COMPONENT PTS SYSTEM ENZYME IIBC IIABC TRANSFERASE PHOSPHOTRANSFERASE SYSTEM SUCROSE-SPECIFIC) protein domain (PD943782) which is seen in Q8G3X0_BIFLO.Residues 239-285 are 72% similar to a (PTS COMPONENT SYSTEM IIBC ENZYME TRANSFERASE SYSTEM IIABC PHOSPHOTRANSFERASE SUCROSE-SPECIFIC) protein domain (PD003077) which is seen in PTNA_CORGL.Residues 287-360 are 85% similar to a (PTS COMPONENT SYSTEM IIBC ENZYME TRANSFERASE SYSTEM PHOSPHOTRANSFERASE IIABC SUCROSE-SPECIFIC) protein domain (PD914218) which is seen in Q6NHI6_CORDI.Residues 361-417 are 85% similar to a (COMPONENT GLUCOSE-SPECIFIC SYSTEM PTS IIABC) protein domain (PDA0Z2M5) which is seen in Q8G3X0_BIFLO.Residues 361-419 are 91% similar to a (COMPONENT PHOSPHOTRANSFERASE IIABC TRANSFERASE PTS ENZYME GLUCOSE-SPECIFIC PERMEASE SYSTEM PYRUVATE) protein domain (PDA133S3) which is seen in Q6NHI6_CORDI.Residues 420-487 are 66% similar to a (COMPONENT PHOSPHOTRANSFERASE IIABC ENZYME PTS SYSTEM TRANSFERASE GLUCOSE-SPECIFIC PERMEASE II) protein domain (PD337461) which is seen in PTGA_CORGL.Residues 420-487 are 65% similar to a (COMPONENT TRANSFERASE GLUCOSE-SPECIFIC SYSTEM PTS IIABC SUGAR PYRUVATE GLUCOSE PERMEASE) protein domain (PD873603) which is seen in O68468_CORAM.Residues 527-702 are 52% similar to a (ENZYME ACETYLGLUCOSAMINE-SPECIFIC SYSTEM TRANSFERASE GLUCOSE/MALTOSE/N- SUCROSE PHOSPHOTRANSFERASE COMPONENTS II IIC) protein domain (PDA18773) which is seen in Q8NMD6_CORGL.Residues 534-682 are 66% similar to a (TRANSFERASE PTS BETA-GLUCOSIDES EIIBCA) protein domain (PDA18449) which is seen in Q88SA6_LACPL.Residues 546-697 are 60% similar to a (ENZYME COMPONENT II ABC SYSTEM PTS BETA-GLUCOSIDE-SPECIFIC) protein domain (PDA183N3) which is seen in Q9KG19_BACHD.Residues 552-673 are 76% similar to a (COMPONENT PTS SYSTEM PHOSPHOTRANSFERASE IIABC IIA ENZYME SYSTEM TRANSFERASE GLUCOSE-SPECIFIC) protein domain (PD002243) which is seen in Q6A8Q9_PROAC.Residues 552-698 are 61% similar to a (SYSTEM SUGAR PHOSPHOENOLPYRUVATE-DEPENDENT PYRUVATE TRANSFERASE SUCROSE SPECIFIC PHOSPHOTRANSFERASE EIIABC) protein domain (PD947125) which is seen in Q74HI8_LACJO.","","-58% similar to PDB:1F3G THREE-DIMENSIONAL STRUCTURE OF THE ESCHERICHIA COLI PHOSPHOCARRIER PROTEIN III GLC (E_value = 1.0E_21);-58% similar to PDB:1F3Z IIAGLC-ZN COMPLEX (E_value = 1.0E_21);-58% similar to PDB:1GGR COMPLEX OF ENZYME IIAGLC AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE (E_value = 1.0E_21);-58% similar to PDB:1GLA STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE (E_value = 1.0E_21);-58% similar to PDB:1GLB STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE (E_value = 1.0E_21);","Residues 8 to 42 (E_value = 2.4e-16) place ANA_0584 in the PTS_EIIB family which is described as phosphotransferase system, EIIB.Residues 123 to 433 (E_value = 5.3e-22) place ANA_0584 in the PTS_EIIC family which is described as Phosphotransferase system, EIIC.Residues 547 to 680 (E_value = 3.2e-53) place ANA_0584 in the PTS_EIIA_1 family which is described as phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1.","","permease (PTS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0586","618195","618851","657","4.96","-7.00","23891","ATGAGCGCGCAGACCTCCCTGGCCGCACAGCCGGCATCGCCGGTCCTACCGAACATCCCGGTTCGCCCGCCCACCACGACTCCGCCTCCCGTCCTTGCCCCGACCGCCGCGTCTGATGTGCCGCGGCTCTACGGTCCACCGGGATGGACGGTGCGCATCGGCCTGTGGCGCCTGCTGGAGCCCTGGCTCGACACCCCGCGCTGCCTGCCGGGGGAGAACCCGCTGCGACTGGATGCCCGGGGCGCCCCGGAGAGCGACTACGTGCCCTTCCGCGGCTTGGACGCCGCCACCGCGGCCGACCTGCTGAGCCGGCTGCCGGCTGCGGCACTGAGAGACCGTCAGAACCTCGCCCCGAGCCTCAAGACGATGCTGACCGCCTGCGCCGGGGCGGATGGGCAGGTACGCCTGTGCGGCTACGGCATCGGTCCCCAGCGGGAGGACGAGCGTCTGAGCGCTGAGGCCCTGTGGGTCGCCGACGCGGACCTGCAGGGCTACGAGGTCCTCGTCGAGCACAGCCGGGACTGCCAGTGCTCCGCGCTGTGGGAGCGGGTCAGAGACCGGTACGAGCTCGACGCCTGCTGCATTCCCGACGACATCGTGCGCACCCGGCCCGAGTGGGCCGGCGGCGGAGTCGGCTGGTGGATGTGGTGGGACTGA","MSAQTSLAAQPASPVLPNIPVRPPTTTPPPVLAPTAASDVPRLYGPPGWTVRIGLWRLLEPWLDTPRCLPGENPLRLDARGAPESDYVPFRGLDAATAADLLSRLPAAALRDRQNLAPSLKTMLTACAGADGQVRLCGYGIGPQREDERLSAEALWVADADLQGYEVLVEHSRDCQCSALWERVRDRYELDACCIPDDIVRTRPEWAGGGVGWWMWWD$","Hypothetical protein","Cytoplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-37% similar to PDB:1UEK Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase (E_value = );-64% similar to PDB:2CS4 Solution structure of N-terminal domain of chromosome 12 open reading frame 2 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0587","618900","620558","1659","5.96","-9.62","59416","GTGATCAATGTCCAGGACCTCACCATGCGCATCGGTGCCCGCCAGCTCGTCGCTCACGCCGGCTTCCGGGTCGATAAGGGGATGCGCATTGGCCTCGTGGGTCGTAACGGCGCAGGCAAGACCACGATGACCAAGCTGCTCGCCGCCGCCTCCGTGGCCCAGGGCGCCGGCCGCGCCGTCAACGACGCCGACGAGCGCCACGGGCTGGAGGCCGTCGAGCACGAGGGCACCATCACCTGCACGAGCTCGGTGGGCTACCTGCCTCAGGACACCAAGGTCGGCGACCTCAGCGAGATCGCCCGGGACCGGATCCTCTCGGCCCGCGGTATCGATGCGCTCCTGGCCCGCATCCGCAAGGCCGAGGAGCGCATCGCCGTCACCGAGGGGGAGGCCCAGGCCAAGGCCCTGGACCGCTACACGCGCCTGGACCACGAGTTCACCATGGCCGGCGGCTACGCCGCCGCCTCCGAGGCCGCCCGCATCAGCGCCGCGCTGGGCCTGCCCGACCGCGTCCTGGACCAGCCCATCGGCACGCTCTCAGGTGGCCAGCGCCGTCGGGTCGAGCTTTCCCGGGTCCTGTTCCAGCAGCCCGACACGCTCCTGCTCGACGAGCCCACCAACCACCTCGACCACGACTCGATCCTGTGGCTGCGCGACCACCTGCGCACCTACGCCGGCGGCTTCATCGTCATCAGCCACGACGTCGAGCTCCTGCGCGACACCGTCAACCAGGTCATGTACCTCGACGCAGGCCGCGGGGTCCTCGACGTCTACCACCTGGGCTGGGACGCCTACCTCAAGCAGCGCGCCGACGACGAGCACCGGCGCCGTCGGGAGCGCGCCAACGCGGAGAAGAAGGCCGCCGCCCTGCGCGCCCAGGGAGAGAAGATGCGGGCCAAGGCCACCAAGGCCGTGGCCGCCCAGCAGATGCTCAAGCGGGCCGAGCGCCTCATGGCCGACCTGGAGGACGAGGCGGCTGTGGAGAAGGTCGCCCACCTGCGTTTCCCCGACCCCGCCCCCTGCGGCAAGACCCCGCTGCGCGCCTCCGGGCTGTCCAAGGCCTACGGCTCCCTGGAGGTCTTCGCCGGCGTGGACCTGGCCATCGACCGCGGCAGCCGGGTCGTGGTCCTGGGCCTCAACGGCGCCGGCAAGACCACGCTCCTGCGTCTGCTCGGCGGGGTGGAGGAGCCCGACTCCGGTGAGGTCATCCCCGGCCACGGCCTCAAGATCGGCTACTACGCCCAGGAGCACGAGACCATCGACACCGCGGCGAGCGTCGTGGAGAACCTGCGCCGCGCCGCCCCCGGCATGGACGACACCCAGGTGCGCAGTGTCCTGGGCTCCTTCCTCTTCTCGGGCGCGGACGCCGACAAGCCCGCCCGGGTCCTCTCCGGCGGTGAGAAGACCCGCCTGGCCCTGGCCATGCTCGTGGTCTCCAGCGCCAACGTCCTCCTGCTCGACGAGCCGACGAACAACCTCGACCCCGCCAGCCGCGAGGAGATCCTCGGGGCGCTGGGCACCTTCGCCGGCGCCGTCGTCCTGGTCACCCACGACGAGGGCGCCGTCGAGGCCCTCAACCCCGACCGGGTCCTCCTGCTGCCCGACGGCGACGAGGACCTGTGGGGGCCGGAGTACCTTGAGCTGGTGGCCCTGGCCTGA","VINVQDLTMRIGARQLVAHAGFRVDKGMRIGLVGRNGAGKTTMTKLLAAASVAQGAGRAVNDADERHGLEAVEHEGTITCTSSVGYLPQDTKVGDLSEIARDRILSARGIDALLARIRKAEERIAVTEGEAQAKALDRYTRLDHEFTMAGGYAAASEAARISAALGLPDRVLDQPIGTLSGGQRRRVELSRVLFQQPDTLLLDEPTNHLDHDSILWLRDHLRTYAGGFIVISHDVELLRDTVNQVMYLDAGRGVLDVYHLGWDAYLKQRADDEHRRRRERANAEKKAAALRAQGEKMRAKATKAVAAQQMLKRAERLMADLEDEAAVEKVAHLRFPDPAPCGKTPLRASGLSKAYGSLEVFAGVDLAIDRGSRVVVLGLNGAGKTTLLRLLGGVEEPDSGEVIPGHGLKIGYYAQEHETIDTAASVVENLRRAAPGMDDTQVRSVLGSFLFSGADADKPARVLSGGEKTRLALAMLVVSSANVLLLDEPTNNLDPASREEILGALGTFAGAVVLVTHDEGAVEALNPDRVLLLPDGDEDLWGPEYLELVALA$","ABC transporter, ATP-binding protein","Cytoplasm, Membrane","ATP binding protein of ABC transporter","ABC transporter ATP binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[178-221]T$ $\"[463-505]T$	Q9RJ28_STRCO_Q9RJ28;
PF00005	$\"[27-251]T$ $\"[371-536]T$	ABC_tran
PS50893	$\"[2-275]T$ $\"[346-551]T$	ABC_TRANSPORTER_2
PS00211	$\"[179-193]T$ $\"[463-477]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[26-252]T$ $\"[370-537]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[2-254]T$ $\"[308-536]T$	no description
PTHR19211	$\"[149-547]T$	ATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19211:SF8	$\"[149-547]T$	ABC TRANSPORTER EF-3 FAMILY (ATP-BINDING PROTEIN)

","BeTs to 16 clades of COG0488COG name: ATPase components of ABC transporters with duplicated ATPase domainsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0488 is ------y--drlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 4","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 3.1e-20. IPB005074C 16-63 IPB005074D 167-210***** IPB005116 (TOBE domain) with a combined E-value of 1.4e-17. IPB005116A 378-394 IPB005116C 463-476 IPB005116D 483-502 IPB005116A 34-50***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3.4e-11. IPB013563A 360-394 IPB013563C 460-487***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4e-11. IPB010509B 27-52 IPB010509D 174-218","Residues 91-177 are 65% similar to a (ATP-BINDING TRANSPORTER ABC ATP BINDING) protein domain (PDA184P4) which is seen in Q8G6F3_BIFLO.Residues 99-176 are 70% similar to a (TRANSPORTER ABC ATP BINDING) protein domain (PDA184C0) which is seen in Q6A7I0_PROAC.Residues 165-252 are 49% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 166-252 are 58% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 172-233 are 62% similar to a (ZINC COMPONENT ABC-TYPE MANGANESE ATPASE ATP-BINDING UPTAKE SYSTEM) protein domain (PDA186P7) which is seen in Q6MI08_BDEBA.Residues 172-433 are 42% similar to a (ARD1 ATP-BINDING) protein domain (PD071350) which is seen in Q53912_STRCP.Residues 405-540 are 60% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD951113) which is seen in Q73MV4_TREDE.Residues 176-233 are 65% similar to a (ATP-BINDING SYSTEM ABC) protein domain (PDA18612) which is seen in Q7MAH4_WOLSU.Residues 463-505 are 90% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9RJ28_STRCO.Residues 179-233 are 69% similar to a (ATP-BINDING RESISTANCE MSRC PROTEIN ERYTHROMYCIN) protein domain (PD896383) which is seen in Q8ESE1_OCEIH.Residues 463-518 are 57% similar to a (ATP-BINDING TRANSPORTER COBALT ABC PROTEIN) protein domain (PD944400) which is seen in Q72D73_DESVH.Residues 234-345 are similar to a (ATP-BINDING ABC TRANSPORTER ATP ATPASE TRANSPORTER BINDING PROBABLE COMPONENT MACROLIDE-TRANSPORT) protein domain (PD086203) which is seen in Q6A7I0_PROAC.Residues 293-416 are 47% similar to a (ATP-BINDING) protein domain (PDA1A6P8) which is seen in Q6MDW1_PARUW.Residues 320-485 are 48% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD859686) which is seen in Q88UG4_LACPL.Residues 327-453 are 48% similar to a (ATP-BINDING F42A10.1) protein domain (PD732595) which is seen in Q20306_CAEEL.Residues 346-548 are 46% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 346-406 are 61% similar to a (ATP-BINDING NATA ABC TRANSPORTER) protein domain (PD742287) which is seen in O83851_TREPA.Residues 350-430 are 63% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I7U7) which is seen in Q6MNC7_BDEBA.Residues 351-459 are 51% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD731029) which is seen in Q8EW48_MYCPE.Residues 356-543 are 45% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 359-533 are 44% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 360-529 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 360-494 are 48% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 364-518 are 45% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 364-406 are 97% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9RJ28_STRCO.Residues 366-518 are 50% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 373-536 are 48% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD962563) which is seen in Q6L0K0_PICTO.Residues 405-540 are 60% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD951113) which is seen in Q73MV4_TREDE.Residues 414-460 are 82% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER ATPASE COMPONENT PROBABLE DUPLICATED DOMAINS SYSTEM) protein domain (PD348029) which is seen in Q8G6F3_BIFLO.Residues 457-532 are 57% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 463-536 are 59% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 463-505 are 90% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9RJ28_STRCO.Residues 463-518 are 57% similar to a (ATP-BINDING TRANSPORTER COBALT ABC PROTEIN) protein domain (PD944400) which is seen in Q72D73_DESVH.","","-47% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 6.6E_16);-42% similar to PDB:2IW3 ELONGATION FACTOR 3 IN COMPLEX WITH ADP (E_value = 2.5E_15);-42% similar to PDB:2IWH STRUCTURE OF YEAST ELONGATION FACTOR 3 IN COMPLEX WITH ADPNP (E_value = 2.5E_15);-42% similar to PDB:2IX3 STRUCTURE OF YEAST ELONGATION FACTOR 3 (E_value = 2.5E_15);-45% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 6.1E_14);","Residues 27 to 251 (E_value = 1.2e-32) place ANA_0587 in the ABC_tran family which is described as ABC transporter.Residues 371 to 536 (E_value = 3.8e-46) place ANA_0587 in the ABC_tran family which is described as ABC transporter.","","binding protein of ABC transporter (974)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0588","620791","621183","393","4.32","-13.65","13904","ATGGCAGAGACCACCCTGACCGAGACCACTGACACCCAGACCCCCGAGCACGAGGTCATCCTCACCGAGACCGCCGCCGCGAAGGTCGCCAGCCTCCTGGCCCAGGAGGGGCGCGACGACCTGCGCCTGCGCGTGGCCGTCCAGCCCGGCGGCTGCTCCGGACTGGTCTACCAGCTCTACTTCGACGAGCGTCTCCTGGACGGCGACGCCGTGCGCGCCTTCCCCACCGGCAGCGACGAGATGACTAGCGTCGAGGTGGTTGTCGACCGCATGAGCGTGCCCTACCTGTCGGGCGCCACCATCGACTTCGCCGACACCATCGAGAAGCAGGGCTTCACCATCGACAACCCCAACGCCGCCGGAAGCTGCGCCTGCGGCGAGTCCTTCCACTGA","MAETTLTETTDTQTPEHEVILTETAAAKVASLLAQEGRDDLRLRVAVQPGGCSGLVYQLYFDERLLDGDAVRAFPTGSDEMTSVEVVVDRMSVPYLSGATIDFADTIEKQGFTIDNPNAAGSCACGESFH$","Iron-sulfur cluster assembly accessory protein","Cytoplasm","Protein Rv2204c/MT2260/Mb2227c","hypothetical protein","iron-sulfur cluster assembly accessory protein","","Huang T.C., Lin R.F., Chu M.K., Chen H.M. Organization and expression of nitrogen-fixation genes in the aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus sp. strain RF-1. Microbiology 1999. 145:743-753. PMID: 10217509Hwang D.M., Dempsey A., Tan K.T., Liew C.C. A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution. J. Mol. Evol. 1996. 43(5):536-540. PMID: 8875867","","","

InterPro
IPR000361
Family

HesB/YadR/YfhF
PD002183	$\"[43-112]T$	Q6AE82_BBBBB_Q6AE82;
PTHR10072	$\"[10-129]T$	HES-B
PF01521	$\"[19-117]T$	Fe-S_biosyn
TIGR00049	$\"[19-130]T$	TIGR00049: iron-sulfur cluster assembly acc
PS01152	$\"[112-129]T$	HESB

noIPR
unintegrated

unintegrated
G3DSA:2.60.300.12	$\"[10-117]T$	no description
PTHR10072:SF26	$\"[10-129]T$	HES-B

","BeTs to 13 clades of COG0316COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0316 is ------yq-dr-bcefghsn-jx---Number of proteins in this genome belonging to this COG is 1","***** IPB000361 (Protein of unknown function, HesB/YadR/YfhF) with a combined E-value of 3.9e-33. IPB000361A 43-57 IPB000361B 86-130","Residues 19-129 are 49% similar to a (HESB) protein domain (PD985684) which is seen in Q7X1K9_BBBBB.Residues 43-112 are 80% similar to a (HESB FAMILY HESB/YADR/YFHF HESB-LIKE DOMAIN STRAIN CLUSTER CHROMOSOME ASSEMBLY ISCA) protein domain (PD002183) which is seen in Q6AE82_BBBBB.","","-64% similar to PDB:2APN hi1723 solution structure (E_value = 5.6E_22);-58% similar to PDB:1NWB Solution structure of the Hypothetical protein AQ_1857 from Aquifex aeolicus: Northeast Structural Genomics Consortium Target QR6 (E_value = 1.1E_17);-53% similar to PDB:1S98 E.coli IscA crystal structure to 2.3 A (E_value = 1.9E_14);-52% similar to PDB:1R94 Crystal Structure of IscA (MERCURY DERIVATIVE) (E_value = 1.6E_13);-52% similar to PDB:1R95 Crystal Structure of IscA (native) (E_value = 1.6E_13);","Residues 19 to 117 (E_value = 7.1e-27) place ANA_0588 in the Fe-S_biosyn family which is described as Iron-sulphur cluster biosynthesis.","","Rv2204c-MT2260-Mb2227c ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0589","621223","622215","993","5.36","-4.67","33569","GTGCGCCGCACATCCCTGACCCTGACCGCCCTGGCCGCGGCCGCCTGCCTCGCGCTGGCCGGCTGCTCGGGGTCGTCCAAGAACGCCTCCGCCACGCCCTCGGCCCAGGCGTCCCCGACCCTGACCCCCTCGATCATCAACTGTGCTCAGGAGGCCGGAACGATCGAGACCGACTCAGAGGCGCTTCCAGCGATCGCCGGTGACGCGGGAGCCGAGCCGACCGTCACCTGGAGTGAGGGTAAGCAGGCCCCTGCCAACCTCGTCTCCAAGACACTCACCTCCGCGGAAGGCCCGGCGGTGTCCTCGGGCGACATCATCACCGTCAACTACGTGGGCTGGAAGTGGGGGTCAACGGAGGCTTTCGACTCCTCCTTCAAGAAGGGCGCCCCGATCACCTTTGGCCTGACCGGGGTCATCCCGGGGTGGACCTGTGGTCTGGCCGGGCACAAGGTCGGCGAGCGCGTCCAGCTGTCGATCCCGGGCAAGCTCGCCTACGGAGAGACCGCCGATCCGGCTCGCCCGAACTCGCCGACCGGCCCGCTCGTCTTCGTCGTCGACATCACCGCTCGCATCACGGGCGATGAGCTGACTCCGTCCACGAAGGACGCCACGGTCGACTCCGCGGAGGTCAAGAAGCTCACTGATCGCGGCGTGACGATCTCCGGCGACCTGGGCGCCCCCGCAGCCGGACTTGCGGGCCCCAAGGCCGAGGAGCCTCTGCAGCCGGAGGTCTTCGTCGTCGCCCGCGGAAAGGGCGCGGCCATCAAGGAGACCGACACCGTGGCCGTGCAGATGTCGCGCACCTCGTGGGACGGCACGACGAGGAGCTCGACCTGGGAGGATCACGCCCCCAGCGCCATGCCGGCCGGACAGATCCGTGCGGCCGGGCTGCCAGTGGGATCCAGGATCGTGCTGCTGGCCCCCGGTAACTCCAACGGGGGGCAGCGTCAGTCGGCGTACATCTTCGTGATGGACCTCGAGAAGGTCATCTGA","VRRTSLTLTALAAAACLALAGCSGSSKNASATPSAQASPTLTPSIINCAQEAGTIETDSEALPAIAGDAGAEPTVTWSEGKQAPANLVSKTLTSAEGPAVSSGDIITVNYVGWKWGSTEAFDSSFKKGAPITFGLTGVIPGWTCGLAGHKVGERVQLSIPGKLAYGETADPARPNSPTGPLVFVVDITARITGDELTPSTKDATVDSAEVKKLTDRGVTISGDLGAPAAGLAGPKAEEPLQPEVFVVARGKGAAIKETDTVAVQMSRTSWDGTTRSSTWEDHAPSAMPAGQIRAAGLPVGSRIVLLAPGNSNGGQRQSAYIFVMDLEKVI$","Peptidylprolyl isomerase, FKBP-type","Extracellular, Periplasm","FKBP-33, putative","peptidylprolyl isomerase; FKBP-type","peptidylprolyl isomerase, FKBP-type","","","","","

InterPro
IPR001179
Domain

Peptidyl-prolyl cis-trans isomerase, FKBP-type
PTHR10516	$\"[90-190]T$	FK506 BINDING PROTEIN
PF00254	$\"[95-188]T$	FKBP_C
PS50059	$\"[103-191]T$	FKBP_PPIASE

noIPR
unintegrated

unintegrated
G3DSA:3.10.50.40	$\"[49-216]T$	no description
PTHR10516:SF17	$\"[90-190]T$	FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
signalp	$\"[1-20]?$	signal-peptide

","BeTs to 11 clades of COG0545COG name: FKBP-type peptidyl-prolyl cis-trans isomerases 1Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0545 is ------y--d---cefghsn-j-it-Number of proteins in this genome belonging to this COG is 2","***** IPB000774 (Domain amino terminal to FKBP-type peptidyl-prolyl isomerase) with a combined E-value of 2.9e-08. IPB000774D 139-166","No significant hits to the ProDom database.","","-57% similar to PDB:1Q6H Crystal structure of a truncated form of FkpA from Escherichia coli (E_value = 1.1E_14);-57% similar to PDB:1Q6I Crystal structure of a truncated form of FkpA from Escherichia coli, in complex with immunosuppressant FK506 (E_value = 1.1E_14);-57% similar to PDB:1Q6U Crystal structure of FkpA from Escherichia coli (E_value = 1.1E_14);","Residues 95 to 188 (E_value = 3.9e-23) place ANA_0589 in the FKBP_C family which is described as FKBP-type peptidyl-prolyl cis-trans isomerase.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0590","622945","622322","624","5.32","-8.13","22696","ATGGCCGTGTACACCCTTCCCGAGCTCCCCTACGACTACGCCGCCCTGGAGCCCCACATCTCCGGCAAGATCATGGAGCTCCACCACGACAAGCACCACGCCGCCTACGTCGCCGGCGCCAACGCCGCCCTGGAGGCCCTGTCCGCCGCCCGTGAGGCCGGCGACCTGGCCGCCATCAACCTGTGGGAGAAGAACCTCGCCTTCAACCTGGGCGGCCACACCAACCACTCCATCTTCTGGAAGAACCTCTCCCCCAACGGCGGGGGCCAGCCCGAGGGCGAGCTCGCCGAGGCCATCAAGGACTCCTTCGGCTCCTTCGAGAAGTTCCAGGCGCAGTTCACCGCCACCGCCATGGGCATCCAGGGCTCGGGCTGGGCCGTGCTCGCCTACGACTCCCTCTCCGGAAAGCTCGTCACCTTCCAGCTCTTCGACCAGCAGGGCAACGTGCCCGTGGGCACCATCCCGCTGTTCATGGTGGACATGTGGGAGCACGCCTTCTACCTCGACTACCTCAACGTCAAGGCCGACTACGTCAAGGCCGTCTGGAACATCGCCAACTGGCAGGACGTCTCCGAGCGCCTGGCCAACGCCGTCGCCAAGGCCCAGGACCTCATCGTCCGCTGA","MAVYTLPELPYDYAALEPHISGKIMELHHDKHHAAYVAGANAALEALSAAREAGDLAAINLWEKNLAFNLGGHTNHSIFWKNLSPNGGGQPEGELAEAIKDSFGSFEKFQAQFTATAMGIQGSGWAVLAYDSLSGKLVTFQLFDQQGNVPVGTIPLFMVDMWEHAFYLDYLNVKADYVKAVWNIANWQDVSERLANAVAKAQDLIVR$","Superoxide dismutase","Extracellular, Cytoplasm","superoxide dismutase (Fe/Mn)","superoxide dismutase ","Superoxide dismutase","","Bannister J.V., Bannister W.H., Rotilio G. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit. Rev. Biochem. 1987. 22(2):111-154. PMID: 3315461Parker M.W., Blake C.C. Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett. 1988. 229(2):377-382. PMID: 3345848Smith M.W., Doolittle R.F. A comparison of evolutionary rates of the two major kinds of superoxide dismutase. J. Mol. Evol. 1992. 34(2):175-184. PMID: 1556751Guan Y., Hickey M.J., Borgstahl G.E., Hallewell R.A., Lepock J.R., O'connor D., Hsieh Y., Nick H.S., Silverman D.N., Tainer J.A. Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Biochemistry 1998. 37(14):4722-4730. PMID: 9537987Ursby T., Adinolfi B.S., Al-Karadaghi S., De vendittis E., Bocchini V. Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: analysis of structure and thermostability. J. Mol. Biol. 1999. 286(1):189-205. PMID: 9931259","","","

InterPro
IPR001189
Family

Manganese and iron superoxide dismutase
PD000475	$\"[90-204]T$	SODM_MYCSM_P53649;
PR01703	$\"[7-18]T$ $\"[28-41]T$ $\"[67-80]T$ $\"[120-128]T$ $\"[158-170]T$	MNSODISMTASE
PTHR11404	$\"[1-199]T$	SUPEROXIDE DISMUTASE 2
PF00081	$\"[3-84]T$	Sod_Fe_N
PF02777	$\"[88-194]T$	Sod_Fe_C
PS00088	$\"[160-167]T$	SOD_MN

","BeTs to 21 clades of COG0605COG name: Superoxide dismutaseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0605 is -omp-zyq-drlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001189 (Manganese and iron superoxide dismutase) with a combined E-value of 2.7e-79. IPB001189A 9-41 IPB001189B 69-85 IPB001189C 98-148 IPB001189D 155-187","Residues 2-82 are 81% similar to a (OXIDOREDUCTASE SUPEROXIDE DISMUTASE METAL-BINDING MANGANESE IRON MN FE SEQUENCING DIRECT) protein domain (PD583305) which is seen in Q6A6R9_PROAC.Residues 83-137 are 67% similar to a (METAL-BINDING DISMUTASE MANGANESE OXIDOREDUCTASE SUPEROXIDE MN) protein domain (PD700585) which is seen in SOD2_HALVO.Residues 90-204 are similar to a (OXIDOREDUCTASE DISMUTASE SUPEROXIDE MANGANESE METAL-BINDING MN IRON PRECURSOR FE MITOCHONDRION) protein domain (PD000475) which is seen in SODM_MYCSM.","","-70% similar to PDB:1GN3 H145Q MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE. (E_value = 5.0E_67);-70% similar to PDB:1GN4 H145E MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE. (E_value = 1.1E_66);-69% similar to PDB:1IDS X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS AT 2.0 ANGSTROMS RESOLUTIONS REVEALS NOVEL DIMER-DIMER INTERACTIONS (E_value = 1.9E_66);-69% similar to PDB:1GN2 S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS. (E_value = 7.2E_66);-69% similar to PDB:1GN6 G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE. (E_value = 9.4E_66);","Residues 3 to 84 (E_value = 1e-43) place ANA_0590 in the Sod_Fe_N family which is described as Iron/manganese superoxide dismutases, alpha-hairpin domain.Residues 88 to 194 (E_value = 2.3e-60) place ANA_0590 in the Sod_Fe_C family which is described as Iron/manganese superoxide dismutases, C-terminal domain.","","dismutase (Fe-Mn)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0591","623021","623569","549","5.43","-4.34","19464","ATGGTTCATGCTAGACGTGGCTCCGGAAGAGGGATAGTGAGCCTGTGTGTGATTACACTGACCGCGGAAACACTGCCGTCCGTACCCGTCCACGAAGGATTCGCTATGACCGACCAGGCTGCTTCCGCCCGTCTCGAGCTTCTCGTCTTCTCCGACGACGCCACCGTGCGTCAGGAGGTCATCGACGGTGTCGGACGCCGACCGGCCAAGGGCCTGCCACTGGTGACCTGGACCGAGGCGGCCACCGCCGAGGGCGTGCGCATGGCCATCAAGGACCGCGAGAAGGAGGACCAGCCGCCCTTCGACGCACTGGTCCTGGACGCCGAGGCCAAGAAGCTCGGCGGCATGGGGCTGGCTCACGAGCTGTTCACCGAGCTCGACGAGCGCCCCGCCGTCGTCCTGCTGACCGCCCGTCCCCAGGATGACTGGCTGGCGGCCTGGGCCAAGGCGGAGGTCGTCGTGCCCCGCCCCCTGGACCCGCTGAGCCTCCAGGAGGGCGTCGCCAAGGCCCTCACCGCCCGCCGCGGCACCGTCACCCCCGCCGGCTGA","MVHARRGSGRGIVSLCVITLTAETLPSVPVHEGFAMTDQAASARLELLVFSDDATVRQEVIDGVGRRPAKGLPLVTWTEAATAEGVRMAIKDREKEDQPPFDALVLDAEAKKLGGMGLAHELFTELDERPAVVLLTARPQDDWLAAWAKAEVVVPRPLDPLSLQEGVAKALTARRGTVTPAG$","Two-component system response regulator","Cytoplasm","probable response regulator","hypothetical protein","hypothetical protein","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[96-171]T$	Q8DJE3_SYNEL_Q8DJE3;

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide

","BeTs to 4 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","No significant hits to the Blocks database.","Residues 43-175 are 57% similar to a (REGULATOR RESPONSE PHOSPHORYLATION TRANSDUCTION SENSORY PROBABLE SYSTEM TWO-COMPONENT) protein domain (PD082442) which is seen in Q9X810_STRCO.","","-41% similar to PDB:1W25 RESPONSE REGULATOR PLED IN COMPLEX WITH C-DIGMP (E_value = );-43% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = );-43% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = );-45% similar to PDB:1DZ3 DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A (E_value = );-45% similar to PDB:1QMP PHOSPHORYLATED ASPARTATE IN THE CRYSTAL STRUCTURE OF THE SPORULATION RESPONSE REGULATOR, SPO0A (E_value = );","No significant hits to the Pfam 21.0 database.","","response regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0592","625254","623632","1623","9.23","8.82","58222","ATGGGCACGCCCCTGGAGCGGGCGACCTTCGTCGTGGTGGACCTGGAGACCACCGGCGGGGCGCCGGGTGCTCGCTCTCTGACCGAGATCGGGGCCGTCAAGGTGCGCGGCGGACAGGTGCTGGCGGAGTTCTCCACCCTGGTCAACCCCGGCGTCGCCATCCCCGCCCAGATCACCATGCTCACCGGCATCACGAACGCCATGGTGGCCGGTGCCCCCGGCGTGCGCACCTGTGTGGAGGCCTTCCTGGACTGGGCGGACCTGCTGGCCGACGACGTCGTCCTCGTCGCGCACAATGCCCGCTTCGACGTCGGTCACCTGCGTGGCGCCGCAGCGGCCCTGGGCCTGGGGTGGCCCGAGCCCCGCGTGCTGGACACCCTGGCGCTGGCCCGCAAGGCCTGGACCCGCAGCGAGGTGCCCAACCACAAGCTGGGGACGCTGGCCGCCTTCGTGGGCTCCCAGATCCGTCCCACGCACCGGGCCCTGGATGACGCGCGCGCCACCGTGGACGTGCTGCACGCCGCCCTGGAGGTCATGGCGCCGCTCGGCGTCACGCACCTGGAGGATCTGGCCACCGCCTCCGACCCGGTTCCGGCCGGGCGCCGGGCCAAGAGCCGCCTGGCTGACGCCCTGCCCAGTGGCCCCGGCGTTTACCAGTTCCGCTCGGCGGCCGACCAAGTGCTCTACGTGGGCAGCGCCGTGGACCTCAAGCGCCGGGTGCGCTCCTACTTCACCGCCGCGGAGAAACGCCGCCAGGTGGCGCAGATGCTGGACACCACCGTGAGCGTGCGGCACATCACCACACCCACGCTCATTGAGGCGCGGGTGCGCGAGCTGCGGATGATCGCCGAGCTCGACCCGCCGGTCAACCGCCGCTCCCGGGCCCCGCGGCGCCGGCCCTGGCTTCACCTGACCCAGGGCTCAGGCTCGGGGGCCGAGCCGCGGTTGGCGCTGACCACCGCGCTGCCCACGGAGGAGGTCGGCCATGCGGTGGGCCCCTTCGCCTCACGCGGCAGGGGCCAGGAGGCCCTGCGCGCCGCCGAGTCGGTGCTGCGTCTGCGCCGCTGGGACGGGCGCGAACTGCGGCGGGTGCGCCACGACGACGTCCCGGCTGAGCCGGCCGAGGTGCTGGCCTGCCTGTCGGGCGAGGTCGACCTGGTGGCCTCTCCCCTGCTGGAGCGCATCGCGGCACTGTCCCGGGCCGAGCGTTACGAGGAGGCCGGGACCTGGACGGGCCGCCTGCGCTGCCTGCTGCGCGCGGTGGATCGGGCCGAGCGGGTGCGGCCCCTGCTGGCCTGCCCGCATCTCATGGCGGCCCGCCGCCGCGAGGTCGGGGGCTGGGAGCTGGTGGTGGTGCGCTGGGGCGTGCTGGCCGGCTCCATGACAACCGCGCCGGGGGCCGACCCGCGTCCCGCCGTCGAGCTGCTACGTGCCAGCGCCCGGGTCGTTGAGCGGCCCGGCCGCGTCGGTGAGGTGGCGAGCATTGAGGAGACGAGCCTGCTGGCCGACTGGGTCCTGGACGAGGGCTCCCGCATCGTGGAGGTCGACGGCGACCCCACGGTGCTCACATGGCCGATCGGTGCGGCTGCCCGCCACCGCAAGGTCCTGGCCTCGCAGGAATGA","MGTPLERATFVVVDLETTGGAPGARSLTEIGAVKVRGGQVLAEFSTLVNPGVAIPAQITMLTGITNAMVAGAPGVRTCVEAFLDWADLLADDVVLVAHNARFDVGHLRGAAAALGLGWPEPRVLDTLALARKAWTRSEVPNHKLGTLAAFVGSQIRPTHRALDDARATVDVLHAALEVMAPLGVTHLEDLATASDPVPAGRRAKSRLADALPSGPGVYQFRSAADQVLYVGSAVDLKRRVRSYFTAAEKRRQVAQMLDTTVSVRHITTPTLIEARVRELRMIAELDPPVNRRSRAPRRRPWLHLTQGSGSGAEPRLALTTALPTEEVGHAVGPFASRGRGQEALRAAESVLRLRRWDGRELRRVRHDDVPAEPAEVLACLSGEVDLVASPLLERIAALSRAERYEEAGTWTGRLRCLLRAVDRAERVRPLLACPHLMAARRREVGGWELVVVRWGVLAGSMTTAPGADPRPAVELLRASARVVERPGRVGEVASIEETSLLADWVLDEGSRIVEVDGDPTVLTWPIGAAARHRKVLASQE$","DNA polymerase III, epsilon subunit","Cytoplasm","exonuclease family","DNA polymerase III; epsilon subunit ","DNA polymerase III, epsilon subunit","","Verhoeven E.E., Van kesteren M., Turner J.J., Van der marel G.A., Van boom J.H., Moolenaar G.F., Goosen N. The C-terminal region of Escherichia coli UvrC contributes to the flexibility of the UvrABC nucleotide excision repair system. Nucleic Acids Res 2002. 30(11):2492-2500. PMID: 12034838","","","

InterPro
IPR000305
Domain

Excinuclease ABC, C subunit, N-terminal
PF01541	$\"[214-296]T$	GIY-YIG
SM00465	$\"[214-295]T$	GIYc
PS50164	$\"[215-290]T$	UVRC_1

InterPro
IPR006054
Domain

DNA polymerase III, epsilon subunit
TIGR00573	$\"[2-204]T$	dnaq: exonuclease, DNA polymerase III, epsi

InterPro
IPR006055
Domain

Exonuclease
SM00479	$\"[9-181]T$	EXOIII

InterPro
IPR013520
Domain

Exonuclease, RNase T and DNA polymerase III
PF00929	$\"[10-172]T$	Exonuc_X-T

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[3-183]T$	no description

","BeTs to 9 clades of COG0847COG name: DNA polymerase III epsilon subunit and related 3'-5' exonucleasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0847 is a--p--yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB006055 (Exonuclease) with a combined E-value of 3.7e-08. IPB006055A 11-21 IPB006055B 158-172***** IPB000305 (Excinuclease ABC, C subunit, N-terminal) with a combined E-value of 9.1e-07. IPB000305A 229-243","Residues 9-65 are 72% similar to a (DNA POLYMERASE EXONUCLEASE EPSILON III TRANSFERASE III SUBUNIT CHAIN HYDROLASE) protein domain (PD002851) which is seen in Q73YM5_MYCPA.Residues 68-168 are 62% similar to a (DNA POLYMERASE EXONUCLEASE EPSILON III III SUBUNIT TRANSFERASE T HYDROLASE) protein domain (PD369841) which is seen in Q73YM5_MYCPA.Residues 380-517 are 56% similar to a (EXONUCLEASE 3_apos;-5_apos; MB2214 DNA POLYMERASE III RV2191/MT2247 EPSILON SUBUNIT) protein domain (PD869761) which is seen in Q6A9T9_PROAC.","","-49% similar to PDB:2P1J Crystal structure of a polC-type DNA polymerase III exonuclease domain from Thermotoga maritima (E_value = 3.4E_17);","Residues 10 to 172 (E_value = 9e-37) place ANA_0592 in the Exonuc_X-T family which is described as Exonuclease.Residues 214 to 296 (E_value = 3.5e-14) place ANA_0592 in the GIY-YIG family which is described as GIY-YIG catalytic domain.","","family ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0594","625425","626357","933","8.20","1.70","33103","ATGGTGCAGGACCGTGTGGTGGCCGCCCAGCCAGCAGTTCACAGGAGGCCCCGCGTGGGATACGGACCCATCAAGGCAACAGTCGGCCCGGCCCTGGAGATGCTCTACCAGCCCTGGATCCGCGGCGAGGAGAACATTCCCGCCGAGGGCGCGGCGATCCTGGCCTCCAACCACCTGGCGGTCATCGACTCCTTCTTCCTTCCGCTGCTGGTGGACCGCGAGGTCGCCTTCATCGGCAAGGCCGACTACTTCACCGGCAAGGGCGTCAAGGGCTGGGCGGTGAAGAACTTCATGAAGACCGTGGGTACGATCCCCGTGGACCGCTCCGGCGGCAAGGCCTCCCAGGCGGCGCTCCAGGCCGGCATCGACCGGCTGCTCTCGGGGCAGCTCTTCGGCATCTATCCCGAGGGCACGCGCAGCCCCGACGGACGCCTCTACCGCGGAAAAACCGGCGTGGCCCGCATCGCCCTGGCCACCGGCGCCCCTGTGGTTCCTGTGGCGATGATCGGCTCCAACCTGGCCCAGCCGATCGGCAAGTCCATCCCCTCCACCCGCCACCGCGTGGGCATCGTCATCGGCGAGCCGCTGGACTTCTCCCGCTACAAGGGTCTGGAGAACGACCGCTTCGTGCTGCGCTCCATCACCGACGAGATCATGTACGCCCTCATGGCGCTCTCCGGACAGGAGTACGTGGACCTCTACGCTGCCGACGTCAAGAAGGCCATGGACTCGGAGAAGAAGACCGCTGACGAGGTCGTCACCGAGATGCTCGCCGCTCAGGCGCAGGCCCGTCCCTCGGCCGCCCCCGTGGCCGCGCCCGGTGGCCGCCCCGCCCCCGAGGTCTCCGTGCCCGAGCCGCCCGAGGACAAGAGCGGCAAGGACAAGAAGAAGGACAAGACTACCGACGACGAGCCCGAGCCCGGCGCCGAGTAG","MVQDRVVAAQPAVHRRPRVGYGPIKATVGPALEMLYQPWIRGEENIPAEGAAILASNHLAVIDSFFLPLLVDREVAFIGKADYFTGKGVKGWAVKNFMKTVGTIPVDRSGGKASQAALQAGIDRLLSGQLFGIYPEGTRSPDGRLYRGKTGVARIALATGAPVVPVAMIGSNLAQPIGKSIPSTRHRVGIVIGEPLDFSRYKGLENDRFVLRSITDEIMYALMALSGQEYVDLYAADVKKAMDSEKKTADEVVTEMLAAQAQARPSAAPVAAPGGRPAPEVSVPEPPEDKSGKDKKKDKTTDDEPEPGAE$","Phospholipid/glycerol acyltransferase","Cytoplasm, Membrane, Extracellular","1-acylglycerol-3-phosphate O-acyltransferasehomolog SC6E10.16c","phospholipid/glycerol acyltransferase","phospholipid/glycerol acyltransferase","","","","","

InterPro
IPR002123
Domain

Phospholipid/glycerol acyltransferase
PF01553	$\"[37-169]T$	Acyltransferase
SM00563	$\"[52-171]T$	PlsC

noIPR
unintegrated

unintegrated
PTHR10434	$\"[5-263]T$	1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE

","BeTs to 18 clades of COG0204COG name: 1-acyl-sn-glycerol-3-phosphate acyltransferaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0204 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB002123 (Phospholipid/glycerol acyltransferase) with a combined E-value of 2.1e-08. IPB002123A 53-71 IPB002123B 133-146","Residues 44-128 are 77% similar to a (ACYLTRANSFERASE TRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE FAMILY O-ACYLTRANSFERASE 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 2.3.1.- PHOSPHOLIPID LYSOPHOSPHATIDIC) protein domain (PD000989) which is seen in Q6AE48_BBBBB.Residues 131-223 are 84% similar to a (ACYLTRANSFERASE TRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE FAMILY 2-ACYLGLYCEROPHOSPHOETHANOLAMINE ACYLTRANSFERASE PROBABLE PHOSPHOLIPID) protein domain (PD462158) which is seen in Q9S2M2_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 37 to 169 (E_value = 7.8e-34) place ANA_0594 in the Acyltransferase family which is described as Acyltransferase.","","O-acyltransferase homolog SC6E10.16c","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0596","626518","627747","1230","4.96","-20.72","44559","ATGTCGATTCGTCGCGTCGCCCTGCTCACCGCTGGCGGTTTCGCCCCCTGTCTGTCCGCCGCCGTCGGCGACCTCATCGAGCGCTACACGCAGGTCGCTCCCGAGGTCGAGATCATCGCCTACCAGTACGGCTACCACGGCCTGCTCACCGGCAACTACATCGTCATCGACGACGAGGGCCGCAAGAACGCCGGCATCCTGCGTGACTTCGGCGGGTCCCCGATCGGCAACTCCCGCGTCAAGCTCACCAACGCCAAGAACCTCGTCGAGCGCGGCCTGGTGAAGGAGGGCGTCAACCCCCTGGAGTTCGCCGCCGAGCAGCTGCGCAAGGACGGCGTCGACGTCTTGCACACCATCGGTGGCGACGACACCAACACCACCGCCGCCGACCTGGCCGCCTACCTCCACGAGAACGACTACGAGCTCACCGTCGTCGGCCTGCCCAAGACCATCGACAACGACGTGGTTCCGATCCGCCAGTCCCTGGGCGCCTGGACCGCGGCCGACGAGGGCGCCGGCTTCGCCTTCAACGTCATCGGCGAGCACCGCTCCAACCCCCGCATGCTCATCGTCCACGAGTGCATGGGCCGCAACTGCGGCTACCTCACCGCCGAGACCGCCCGCCGCTACCACGACCTGCTCCAGACCAAGCAGTGGGCCCCCTCCCTCGGCCTGACCAAGGAGCGCTGGGACGTCCACGCCGTCTTCCTCCCCGAGGTAAAGCTCGACATCGCCGCCGAGGCCGAGCGCCTCAAGGCCATCATGGACGAGCAGGGCAACGTCAACATCTTCCTGTCCGAGGGCGCCGGCGTCCCCGAGATCATCGCGGAGATGGAGGCCGCCGGCCAGGAGGTCCAGCGCGACCCCTTCGGCCACGTCAAGCTCGACACCATCAACCCCGGCCAGTGGTTCGCCAAGCAGTTCGCCGAGCTCATCGGCGCTGAGAAGGTCATGGTCCAGAAGTCCGGCTACTACTCGCGGGCCGCCCACGCCAACGCCGAGGACCTCGCCCTCATCAAGAAGATGTGCGACCTGGCCGTCGACTGCGCCCTGCGCGGCGAGTCCGGCGTCATCGGCCAGGACGAGGAGAACAACGACGAGCTCACCGCGATCGCCTTCCCGCGCATCGCCGGCGCCAAGCCCTTCGACATCACTCAGGCCTGGTTCACCGACCTCATGGCCGAGCTGGGCCAGAAGGTCGAGCCCGCCGAGGCCGCTCCCGAGCACTGA","MSIRRVALLTAGGFAPCLSAAVGDLIERYTQVAPEVEIIAYQYGYHGLLTGNYIVIDDEGRKNAGILRDFGGSPIGNSRVKLTNAKNLVERGLVKEGVNPLEFAAEQLRKDGVDVLHTIGGDDTNTTAADLAAYLHENDYELTVVGLPKTIDNDVVPIRQSLGAWTAADEGAGFAFNVIGEHRSNPRMLIVHECMGRNCGYLTAETARRYHDLLQTKQWAPSLGLTKERWDVHAVFLPEVKLDIAAEAERLKAIMDEQGNVNIFLSEGAGVPEIIAEMEAAGQEVQRDPFGHVKLDTINPGQWFAKQFAELIGAEKVMVQKSGYYSRAAHANAEDLALIKKMCDLAVDCALRGESGVIGQDEENNDELTAIAFPRIAGAKPFDITQAWFTDLMAELGQKVEPAEAAPEH$","6-phosphofructokinase","Cytoplasm","pyrophosphate-frustose 6-phosphate1-phosphotransferase","diphosphate--fructose-6-phosphate 1-phosphotransferase ","phosphofructokinase","","Hellinga H.W., Evans P.R. Mutations in the active site of Escherichia coli phosphofructokinase. Nature 1987. 327(6121):437-439. PMID: 2953977Wegener G., Krause U. Different modes of activating phosphofructokinase, a key regulatory enzyme of glycolysis, in working vertebrate muscle. Biochem. Soc. Trans. 2002. 30(2):264-270. PMID: 12023862Raben N., Exelbert R., Spiegel R., Sherman J.B., Nakajima H., Plotz P., Heinisch J. Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am. J. Hum. Genet. 1995. 56(1):131-141. PMID: 7825568Shirakihara Y., Evans P.R. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. J. Mol. Biol. 1988. 204(4):973-994. PMID: 2975709","","","

InterPro
IPR000023
Family

Phosphofructokinase
PD000707	$\"[135-202]T$	PFP_PROFR_P29495;
PR00476	$\"[8-27]T$ $\"[112-128]T$ $\"[145-162]T$ $\"[184-200]T$	PHFRCTKINASE
PTHR13697	$\"[142-203]T$ $\"[223-318]T$	PHOSPHOFRUCTOKINASE
PF00365	$\"[4-313]T$	PFK

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.450	$\"[1-207]T$	no description
signalp	$\"[1-23]?$	signal-peptide

","BeTs to 14 clades of COG0205COG name: 6-phosphofructokinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0205 is ------yqvdrlbce-ghs--j-itwNumber of proteins in this genome belonging to this COG is 3","***** IPB000023 (Phosphofructokinase) with a combined E-value of 3.6e-18. IPB000023A 6-27 IPB000023B 166-219 IPB000023C 316-347","Residues 5-121 are similar to a (KINASE TRANSFERASE GLYCOLYSIS PHOSPHOFRUCTOKINASE 6-PHOSPHOFRUCTOKINASE ALLOSTERIC ENZYME PHOSPHOHEXOKINASE ATP-BINDING MAGNESIUM) protein domain (PD024538) which is seen in Q6A8S9_PROAC.Residues 135-202 are similar to a (KINASE TRANSFERASE GLYCOLYSIS PHOSPHOFRUCTOKINASE 6-PHOSPHOFRUCTOKINASE ALLOSTERIC ENZYME PHOSPHOHEXOKINASE ATP-BINDING MAGNESIUM) protein domain (PD000707) which is seen in PFP_PROFR.Residues 204-398 are similar to a (TRANSFERASE 1-PHOSPHOTRANSFERASE PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE KINASE PPI-PHOSPHOFRUCTOKINASE DEPENDENT PYROPHOSPHATE--FRUCTOSE-6-PHOSPHATE PYROPHOSPHATE PROBABLE) protein domain (PD131586) which is seen in Q6A8S9_PROAC.","","-46% similar to PDB:1PFK CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS (E_value = 1.0E_10);-44% similar to PDB:1ZXX The crystal structure of phosphofructokinase from Lactobacillus delbrueckii (E_value = 1.0E_10);-46% similar to PDB:2PFK THE CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI (E_value = 1.0E_10);","Residues 4 to 313 (E_value = 1.7e-07) place ANA_0596 in the PFK family which is described as Phosphofructokinase.","","6-phosphate 1-phosphotransferase (AF246209)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0598","628066","629415","1350","5.23","-18.61","49337","ATGAACGAGCTCTCCGCCGCCCGCACGGACGCCCAGGCCCCCGCATGGCGCCACCTGCCCGCCCTCCAGCAGCCCGCCTACCCCGATGAGGCCGCGCTTGCCGACGTGGTGGCGGATCTGCGCCGCCGGCCCCCGCTCGTCTTCGCCGGAGAGGTCGACTCCCTGCGCGAGCTCATCGCCCAGGCCAGCGCCGGGGACGCCTTTGTCCTCATGGGCGGGGACTGCGCCGAGTCCTTCACCCACAACACGGCCGACAACATCCGCCTCAAGGTCCAGACCATCCTCCAAATGGCCGCGGTCCTCACCTACGGCGCCTCCACGCCCGTGGTCAAGATCGGCCGCATGGCCGGCCAGTACGCCAAGCCCCGCAGCTCGGACACCGAGACCCGCGGAGAGGTCACCCTGCCCGCCTTCCGCGGCGACTCCGTCAACGGCCACGAGTTCACCCCCGAGGCCCGCATCCCCGACCCCACCCGCATGCTCGACGCCTACCTGCGCTCGGGCACCACTCTCAACCTCATCCGCGCCTTCACGATGGGCGGTTACGCGGACCTGCGCGAGGTCCACTCCTGGAACCGCGGCTTCACCGCCAACCCCGCCTACAAGCGCTTCGAGTCCTTCGCCGAGGAGCTCGACCGGGCCATGCGCTTCATGGAGGCCGCCGGCGTTGACTTCGAGGCCCTGCGCCAGGTCGACTTCTACGCCGCCCACGAGGCCCTGCTCCTGGAGTACGAGGACGCCATGATCCGTGAGGACTCCCGCTCCGGGCGCCTCTACGACACCTCCGCCCACATGCTCTGGGTGGGGGAGCGCACCCGCGAGGCCGACGGCGCCCACGTCGCCATCCTCGCCGGCGTCCACAACCCCGTGGGCGTCAAGGTCGGCCCCACCACGTCCCCCGACGACGTCGCCCGGCTTATGGACCGCCTCAACCCCGAGGGTCTGCCCGGACGCCTGTCCCTCATCACCCGCATGGGCGCCGACCGCATCCGTGAGGCCCTGCCGCAGCTGGTGGAGGCGGTGCGCGCCGACGGGCGTCCCGTCACCTGGATCGCCGACCCCATGCACGGCAACACCATCACCTCGGACAACGGCTACAAGACCCGCCGCTTCGAGACGATCCTCGACGAGATCCGCGGCTTCTTCGAGGTGCACCGCTCCCTGGGCTCCGCCCCGGGCGGTATCCACGTCGAGCTCACTGGCGACGACGTCACCGAGGTCCTCGGCGGCGGTGAGCACATCGACGAGGCCGGCCTGGCCGAGCACTACGAGACCCTCGTCGACCCGCGCCTCAATCACCAGCAGTCCCTCGAGGTCGCCTTCGAGATCGCCGAGATGCTCAAGGGCTGA","MNELSAARTDAQAPAWRHLPALQQPAYPDEAALADVVADLRRRPPLVFAGEVDSLRELIAQASAGDAFVLMGGDCAESFTHNTADNIRLKVQTILQMAAVLTYGASTPVVKIGRMAGQYAKPRSSDTETRGEVTLPAFRGDSVNGHEFTPEARIPDPTRMLDAYLRSGTTLNLIRAFTMGGYADLREVHSWNRGFTANPAYKRFESFAEELDRAMRFMEAAGVDFEALRQVDFYAAHEALLLEYEDAMIREDSRSGRLYDTSAHMLWVGERTREADGAHVAILAGVHNPVGVKVGPTTSPDDVARLMDRLNPEGLPGRLSLITRMGADRIREALPQLVEAVRADGRPVTWIADPMHGNTITSDNGYKTRRFETILDEIRGFFEVHRSLGSAPGGIHVELTGDDVTEVLGGGEHIDEAGLAEHYETLVDPRLNHQQSLEVAFEIAEMLKG$","Phospho-2-dehydro-3-deoxyheptonate aldolase","Cytoplasm","3-deoxy-7-phosphoheptulonate synthase","phospho-2-dehydro-3-deoxyheptonate aldolase ","phospho-2-dehydro-3-deoxyheptonate aldolase","","Walker G.E., Dunbar B., Hunter I.S., Nimmo H.G., Coggins J.R. Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa. Microbiology 1996. 142:1973-1982. PMID: 8760910","","","

InterPro
IPR002480
Family

DAHP synthetase, class II
PTHR21337	$\"[16-449]T$	PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2
PF01474	$\"[10-444]T$	DAHP_synth_2
TIGR01358	$\"[11-448]T$	DAHP_synth_II: 3-deoxy-7-phosphoheptulonate

","BeTs to 5 clades of COG3200COG name: 3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG3200 is ----------r----f----uj----Number of proteins in this genome belonging to this COG is 1","***** IPB002480 (DAHP synthetase, classII) with a combined E-value of 7.5e-171. IPB002480A 48-95 IPB002480B 96-145 IPB002480C 193-243 IPB002480D 244-293 IPB002480E 308-355 IPB002480F 356-403","Residues 23-171 are similar to a (ALDOLASE SYNTHASE 7-PHOSPHATE PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE 3-DEOXY-D-ARABINO-HEPTULOSONATE DAHP SYNTHETASE LYASE TRANSFERASE PRECURSOR) protein domain (PD001974) which is seen in Q6AE49_BBBBB.Residues 198-248 are 84% similar to a (ALDOLASE PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE SYNTHASE 7-PHOSPHATE TRANSFERASE DAHP 3-DEOXY-D-ARABINO-HEPTULOSONATE PROBABLE LYASE ALDOLASE) protein domain (PD234721) which is seen in Q6AE49_BBBBB.Residues 250-326 are 83% similar to a (ALDOLASE SYNTHASE 7-PHOSPHATE PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE 3-DEOXY-D-ARABINO-HEPTULOSONATE DAHP SYNTHETASE LYASE TRANSFERASE PRECURSOR) protein domain (PD860219) which is seen in Q6AE49_BBBBB.Residues 328-374 are 76% similar to a (ALDOLASE SYNTHASE 7-PHOSPHATE PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE 3-DEOXY-D-ARABINO-HEPTULOSONATE DAHP SYNTHETASE PRECURSOR PHOSPHO-2-KETO-3-DEOXYHEPTONATE AROMATIC) protein domain (PD856765) which is seen in Q6N8C0_RHOPA.Residues 377-432 are 83% similar to a (ALDOLASE SYNTHASE 7-PHOSPHATE PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE 3-DEOXY-D-ARABINO-HEPTULOSONATE DAHP SYNTHETASE LYASE TRANSFERASE PRECURSOR) protein domain (PD860216) which is seen in Q6AE49_BBBBB.","","-67% similar to PDB:2B7O The Structure of 3-Deoxy-D-Arabino-Heptulosonate 7-Phosphate Synthase from Mycobacterium tuberculosis (E_value = 5.3E_122);","Residues 10 to 444 (E_value = 4.5e-238) place ANA_0598 in the DAHP_synth_2 family which is described as Class-II DAHP synthetase family.","","synthase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0599","631520","629493","2028","6.60","-2.07","70622","GTGGTCACAGATCCTCTCATTGGTCGGTTGGTCGACTCTCGCTACGAGATCGTCGACCGCCTAGCGCGTGGCGGGATGGCCACCGTCTACCGCGCCCATGACCGTCGCCTGGACCGGACCGTGGCGCTCAAGCTCATGCACGCCCACCTGGCCGACTCCCCCGACTTCGTCTCGCGCTTCCGCCGTGAGGCACGGGCCGCGGCACGCCTGTCCAACCCGGGCGTGGTGGCCGTCTTCGACCAGGGCAGCCTCGACGGGGTCGCCTACCTCGTCATGGAGTACGTCGAGGGGCCCACGCTGCGGGACCTCATTGCGGCGGGACCGCTGTCGGTCAAGGAGGCCCTGGGGCTGGTGGCCCAGCTGCTGCGCCCGCTCGGCGCGGCCCACCGGGCCGGCCTGGTCCACCGCGACATCAAGCCGGAGAACGTACTGCTGCCCTCCGACGGCTCGGTGGCCAAGGTCGCCGACTTCGGCCTGGCCCGGGCAGTCACGGAGGTGACGCAGACGACGACGGGCAACGTGCTGGGCACGGTCGCCTACCTGGCGCCAGAGCTCATCACCTCCGGGGACTCCACCTCTCGTGCCGATGTCTTCTCCGCCGGGGTGGTCCTCTACGAGCTCCTCACCGGCCAGCAGCCCTTCACCGCGGACTCCCCCATTCAGATCGCCTTCCGCAATGTCCACGAGGACGTGCCCCTGCCCTCCAAGCTGGTGCCCGACATGCCTGCCGACGTCGACGAGCTCGTGGCCACCATGACGCGTCGTGAGCCGCAGGAGCGCCCGGCCGATGCCGACGAGGCGCTGGCGCTGCTGCGCAACGTCGTTGACGAGCTCACCGACTCCGAGCTCTCCGTGCGCCGCGGGGGCGGGACCGGCTCCATCCGGACCCAGCAGGTCATGACGGCCAATGCGCAGGCTGCCCGCTCCGCCATCGATAACGCGCCCCAGGACGACGCCGACGACTCCTCCGCCGAGGAGGCCTCGCCGCACGCCGGGATGCGCACCGTCTCCCTTCCCATTGGTTCGATCGGCCCGGACTCCAAGGGGAGAACACGTGCGCTCTCCCGCAAGGCCCTGGCGGCCGACGCTCAGGAAACCACTGCCGTCCCCACCCGGAAGAAGAGCACTGGCGGCTTCAGTCGCCGTCGTGCGCTCGTCATCGGGCTGCTGGCCGTGGCTGGAACCGGTGCGAGCGCCACCTGGTACCTGACGGCCGGTCCCGGCAGGCGAGTTTCCGTGCCGAACATCATTGGCATGTCTGAGGACCAGGCGCAGCTCGCCCTGGAGAAGCAGGGGCTCGACTGGGGCACGCCCGAGCGCGTCTACTCCGACACGGTCCCGGCCGGCAGCATCGTCTCCTGCCAGCCGAAGGCGGGCCAGAAGGTGGGACTCGGCCAGGCCGTCACCGCCACCGTCTCCCGAGGCGTGGAGACCAAGACCGTTCCCGACGTCGTCGGGAAGACCAAGGACCAGGCCACGGCCGCAATCACGGCGGCCGGCCTGACCCCGGGGGACGTCACCGAGGAGTACTCCGCCAGCGTGGAGTCGGGCAAGGTCATCTCCTGCGACCCCACGGCCGGAAAGGTCATCAAGCACACTGAGAAGGTCTCGCTCGTGGTCTCCAAGGGCAAGGAGCCGGCTACGATCCCCGACGTGACCGGTATGAGCGAGGACGAGGCCAAGAAGGTCCTGGAGGATGCCGGGCTGAAGAAGGGCAAGGTCAGCAAGGGCTACTCCGACTCCGTGGCGAAGGGGAATGTCATCTCCTCCTCCCCCATCGCCGGGGCCTCGGGCTACTACAAGGGCGACTCGGTGGACCTGACGGTCTCCAAGGGGCCGGAGAAAGTGACGGTCCCGGATGTGACCGGCAAGAGCCAGGACGAGGCCAAGAAGGCGCTGGAGGACGCCGGGCTCAAGGTGGAGGTCAACAAGCGCCTGGGCGGCCCCTTCGGAACGGTGCGCTCCACTGATCCTGCGCCGGGCTCCAGCGTCAAGCCGGACTCCAAGGTCACCATCAACATCTTCTGA","VVTDPLIGRLVDSRYEIVDRLARGGMATVYRAHDRRLDRTVALKLMHAHLADSPDFVSRFRREARAAARLSNPGVVAVFDQGSLDGVAYLVMEYVEGPTLRDLIAAGPLSVKEALGLVAQLLRPLGAAHRAGLVHRDIKPENVLLPSDGSVAKVADFGLARAVTEVTQTTTGNVLGTVAYLAPELITSGDSTSRADVFSAGVVLYELLTGQQPFTADSPIQIAFRNVHEDVPLPSKLVPDMPADVDELVATMTRREPQERPADADEALALLRNVVDELTDSELSVRRGGGTGSIRTQQVMTANAQAARSAIDNAPQDDADDSSAEEASPHAGMRTVSLPIGSIGPDSKGRTRALSRKALAADAQETTAVPTRKKSTGGFSRRRALVIGLLAVAGTGASATWYLTAGPGRRVSVPNIIGMSEDQAQLALEKQGLDWGTPERVYSDTVPAGSIVSCQPKAGQKVGLGQAVTATVSRGVETKTVPDVVGKTKDQATAAITAAGLTPGDVTEEYSASVESGKVISCDPTAGKVIKHTEKVSLVVSKGKEPATIPDVTGMSEDEAKKVLEDAGLKKGKVSKGYSDSVAKGNVISSSPIAGASGYYKGDSVDLTVSKGPEKVTVPDVTGKSQDEAKKALEDAGLKVEVNKRLGGPFGTVRSTDPAPGSSVKPDSKVTINIF$","Eukaryotic-type serine/threonine protein kinase","Membrane, Periplasm","Serine/threonine-protein kinase PK-1 (stoPK-1)","putative eukaryotic-type serine/threonine protein kinase ","protein kinase","","Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995. 9(8):576-596. PMID: 7768349Hunter T. Protein kinase classification. Meth. Enzymol. 1991. 200:3-37. PMID: 1835513Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth. Enzymol. 1991. 200:38-62. PMID: 1956325Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988. 241(4861):42-51. PMID: 3291115Knighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991. 253(5018):407-414. PMID: 1862342","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[15-260]T$	Q73YP1_MYCPA_Q73YP1;
PF00069	$\"[15-271]T$	Pkinase
PS50011	$\"[15-271]T$	PROTEIN_KINASE_DOM

InterPro
IPR005543
Domain

PASTA
PF03793	$\"[411-474]T$ $\"[479-542]T$ $\"[547-611]T$ $\"[616-674]T$	PASTA
SM00740	$\"[407-474]T$ $\"[475-542]T$ $\"[543-611]T$ $\"[612-674]T$	PASTA
PS51178	$\"[406-474]T$ $\"[475-542]T$ $\"[543-611]T$ $\"[612-675]T$	PASTA

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[133-145]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[67-268]T$	no description
PTHR22986	$\"[12-261]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES

","BeTs to 10 clades of COG0515COG name: Serine/threonine protein kinasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0515 is -o-p-zyq-drlbcefghs--j-i-wNumber of proteins in this genome belonging to this COG is 10","***** IPB000961 (Protein kinase C-terminal domain) with a combined E-value of 5.3e-20. IPB000961A 14-48 IPB000961C 116-158 IPB000961D 173-214***** IPB008266 (Tyrosine protein kinase, active site) with a combined E-value of 4.9e-18. IPB008266A 120-160 IPB008266B 179-215***** IPB003527 (MAP kinase) with a combined E-value of 1.8e-14. IPB003527C 109-159 IPB003527D 191-233***** IPB000861 (PKN/rhophilin/rhotekin rho-binding repeat) with a combined E-value of 3.2e-11. IPB000861D 92-145 IPB000861E 179-228***** IPB013695 (Wall-associated kinase) with a combined E-value of 5.9e-10. IPB013695J 164-213***** IPB010513 (Ribonuclease 2-5A) with a combined E-value of 1.4e-07. IPB010513D 124-145 IPB010513E 196-216***** IPB013896 (Ubiquitin-associated region 2) with a combined E-value of 3.9e-07. IPB013896D 115-147 IPB013896E 181-234***** IPB001772 (Kinase-associated, C-terminal) with a combined E-value of 4.8e-07. IPB001772A 12-43 IPB001772D 184-223***** IPB013543 (Calcium/calmodulin dependent protein kinase II, association-domain) with a combined E-value of 3.2e-06. IPB013543A 5-50 IPB013543D 112-148 IPB013543F 186-221***** IPB000472 (Domain in TGF-beta receptor/activin receptor, type I/II) with a combined E-value of 4.1e-06. IPB000472D 130-160 IPB000472E 174-185***** IPB000959 (POLO box duplicated region) with a combined E-value of 8e-06. IPB000959D 177-231","Residues 1-271 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756057) which is seen in Q81ZV7_STRAW.Residues 1-289 are 53% similar to a (KINASE PKN9 SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD268676) which is seen in Q9XBP3_MYXXA.Residues 2-278 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA0K9H0) which is seen in Q7NMV0_GLOVI.Residues 2-265 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE TRANSCRIPTION ATP-BINDING DNA-BINDING SERINE-THREONINE REGULATION) protein domain (PDA1B2W7) which is seen in Q6PV87_BBBBB.Residues 3-279 are 66% similar to a (KINASE SERINE-THREONINE) protein domain (PDA1D4F7) which is seen in Q6A9T0_PROAC.Residues 3-214 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING PPKA) protein domain (PDA1D587) which is seen in Q7UMX3_RHOBA.Residues 3-414 are 50% similar to a (SERINE/THREONINE-PROTEIN KINASE PKN3 TRANSFERASE ATP-BINDING) protein domain (PD316927) which is seen in PKN3_MYXXA.Residues 3-307 are 70% similar to a (KINASE SERINE/THREONINE) protein domain (PDA1A7D8) which is seen in Q6AE50_BBBBB.Residues 4-284 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA191E0) which is seen in Q8DLN7_SYNEL.Residues 4-275 are 54% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE TPR PHOSPHORYLATION REPEAT PKN1 ATP-BINDING) protein domain (PD052299) which is seen in PKN1_MYXXA.Residues 5-261 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN ACR142WP TRANSFERASE ATP-BINDING) protein domain (PDA0A7Q6) which is seen in Q75CE9_ASHGO.Residues 5-257 are 60% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA TRANSFERASE ATP-BINDING PROBABLE) protein domain (PDA188K3) which is seen in PKNA_MYCLE.Residues 5-271 are 50% similar to a (KINASE REPEAT TPR SERINE/THREONINE ATP-BINDING PKN8) protein domain (PD280760) which is seen in Q9XBP6_MYXXA.Residues 6-286 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING PLASMID) protein domain (PD756391) which is seen in Q820A7_STRAW.Residues 6-261 are 47% similar to a (KINASE TRANSFERASE TYROSINE-PROTEIN ATP-BINDING F11E6.8) protein domain (PD247428) which is seen in Q9XVQ7_CAEEL.Residues 6-266 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN PPKA TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA025J8) which is seen in Q7UT84_RHOBA.Residues 6-258 are 45% similar to a () protein domain (PD454795) which is seen in Q9AQ02_BBBBB.Residues 6-272 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756060) which is seen in Q81ZY9_STRAW.Residues 6-274 are 62% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD810446) which is seen in Q895P6_CLOTE.Residues 7-266 are 53% similar to a (KINASE SERINE/THREONINE) protein domain (PD456344) which is seen in Q98IK2_RHILO.Residues 7-261 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD975784) which is seen in Q7NPK1_GLOVI.Residues 7-282 are 54% similar to a (KINASE PKNB SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5H6) which is seen in Q7UFU9_RHOBA.Residues 7-226 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD498679) which is seen in Q8Z111_SALTI.Residues 8-293 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796751) which is seen in Q81ZW2_STRAW.Residues 8-224 are 52% similar to a (KINASE STE20-LIKE ATP-BINDING DON3) protein domain (PD609771) which is seen in Q8NJX3_USTMA.Residues 8-282 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING PROBABLE SERINE-THREONINE) protein domain (PD736072) which is seen in Q8G6Q0_BIFLO.Residues 8-262 are 53% similar to a (BLR3604 KINASE TRANSFERASE ATP-BINDING) protein domain (PD828726) which is seen in Q89P79_BRAJA.Residues 8-261 are 55% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE KINASE ATP-BINDING) protein domain (PD828286) which is seen in Q9RRH3_DEIRA.Residues 9-331 are 53% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD724652) which is seen in Q81ZW8_STRAW.Residues 9-540 are 48% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA2 PROBABLE TRANSFERASE REPEAT ATP-BINDING) protein domain (PD848557) which is seen in PKNA_BIFLO.Residues 9-271 are 57% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796289) which is seen in Q9S2A6_STRCO.Residues 9-276 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD842227) which is seen in Q81ZZ0_STRAW.Residues 10-268 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D464) which is seen in Q7UW31_RHOBA.Residues 11-277 are 55% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA1A878) which is seen in Q72IA2_THET2.Residues 11-262 are 52% similar to a (SIMILAR DEBARYOMYCES HANSENII DEHA0C16181G) protein domain (PD991318) which is seen in Q6C3K8_EEEEE.Residues 12-245 are 45% similar to a (KINASE CELL DIVISION SERINE/THREONINE-PROTEIN 3D-STRUCTURE CYCLE TRANSFERASE PHOSPHORYLATION PLSTIRE ATP-BINDING) protein domain (PD470147) which is seen in CDK6_HUMAN.Residues 12-225 are 46% similar to a (KINASE REPEAT DICTYOSTELIUM SIMILAR SERINE/THREONINE-PROTEIN SLIME MEK-LIKE CONTAINING MOLD. ANK) protein domain (PD747196) which is seen in Q86AT8_DICDI.Residues 12-276 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN PROBABLE SERINE/THREONINE) protein domain (PD721958) which is seen in Q83H75_TROW8.Residues 12-247 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD727335) which is seen in Q86JX3_DICDI.Residues 12-224 are 45% similar to a (ATP-BINDING AGCP10418) protein domain (PDA0J0F6) which is seen in Q7QGN6_EEEEE.Residues 13-285 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN REPEAT TRANSFERASE TPR 2.7.1.- ATP-BINDING) protein domain (PDA0F980) which is seen in Q7URL4_RHOBA.Residues 13-265 are 47% similar to a (AFR724CP ATP-BINDING) protein domain (PDA101P3) which is seen in Q751V1_ASHGO.Residues 13-274 are 59% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA0H1H6) which is seen in Q7UJD9_RHOBA.Residues 13-214 are 44% similar to a (KINASE R11E3.1 TRANSFERASE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD278557) which is seen in Q9TYX4_CAEEL.Residues 14-293 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796214) which is seen in Q81ZX4_STRAW.Residues 14-214 are 52% similar to a (KINASE P27636 SERINE/THREONINE-PROTEIN TRANSFERASE CDC15 CEREVISIAE ATP-BINDING SACCHAROMYCES YAR019C) protein domain (PDA0F8T8) which is seen in Q6FWK3_EEEEE.Residues 14-260 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA19096) which is seen in Q7UJC1_RHOBA.Residues 14-262 are 49% similar to a (KINASE LIKE NEUROSPORA RELATED STE20- B16M17.090 Q871H9 DON3 CRASSA) protein domain (PDA064R7) which is seen in Q6C8H9_EEEEE.Residues 14-226 are 51% similar to a (CELL DIVISION SERINE/THREONINE-PROTEIN CONTROL KINASE CYCLE TRANSFERASE 2.7.1.- MITOSIS ATP-BINDING) protein domain (PDA0F8T7) which is seen in CC15_YEAST.Residues 14-260 are 42% similar to a (SERINE/THREONINE-PROTEIN KINASE MEK1 MEIOSIS TRANSFERASE ATP-BINDING MEIOSIS-SPECIFIC) protein domain (PDA0I4P9) which is seen in MEK1_SCHPO.Residues 14-271 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA08789) which is seen in Q7UL45_RHOBA.Residues 14-274 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING SERINE/THREONINE-SPECIFIC PROBABLE) protein domain (PDA1D2S2) which is seen in Q7UFH1_RHOBA.Residues 15-276 are 55% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA10203) which is seen in Q7UIJ7_RHOBA.Residues 15-268 are 47% similar to a (KINASE 1-LIKE RESPONSIVE ATP-BINDING STRESS) protein domain (PD099489) which is seen in O61125_DICDI.Residues 15-288 are 58% similar to a (KINASE SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA010X1) which is seen in Q7UKY9_RHOBA.Residues 15-265 are 46% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE WD SERINE/THREONINE ATP-BINDING) protein domain (PD288091) which is seen in Q9RDS3_STRCO.Residues 15-270 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D5J2) which is seen in Q7UZ75_RHOBA.Residues 15-265 are 50% similar to a (SERINE/THREONINE-PROTEIN KINASE REPEAT PROBABLE TRANSFERASE WD PKWA ATP-BINDING) protein domain (PD110150) which is seen in PKWA_THECU.Residues 15-314 are 44% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE APOPTOSIS HIPPO ATP-BINDING) protein domain (PD727337) which is seen in HPO_DROME.Residues 15-264 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D3Y0) which is seen in Q7UVF2_RHOBA.Residues 15-265 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE-THREONINE ATP-BINDING) protein domain (PD319602) which is seen in Q9K3W7_STRCO.Residues 15-104 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN REPEAT TRANSFERASE 2.7.1.- WD ATP-BINDING PROBABLE) protein domain (PDA19784) which is seen in Q7UWP5_RHOBA.Residues 15-274 are 53% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD298418) which is seen in Q9X8G8_STRCO.Residues 15-273 are 46% similar to a (KINASE STRESS-RESPONSIVE PRKSD ATP-BINDING) protein domain (PD087289) which is seen in O62571_SUBDO.Residues 15-165 are 59% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA18944) which is seen in Q7UPN1_RHOBA.Residues 15-101 are 55% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE ATP-BINDING PHOSPHORYLATION PKN5) protein domain (PD076500) which is seen in PKN5_MYXXA.Residues 15-248 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD500022) which is seen in Q8YMH9_ANASP.Residues 15-311 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNA TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5E6) which is seen in Q7UX63_RHOBA.Residues 15-278 are 55% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA10189) which is seen in Q7UKJ3_RHOBA.Residues 15-276 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PDA0G6B9) which is seen in Q6MAN0_PARUW.Residues 15-276 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA0Z806) which is seen in Q7NLM6_GLOVI.Residues 15-261 are 47% similar to a (KINASE SER/THR TRANSFERASE ATP-BINDING) protein domain (PD126531) which is seen in O54229_STRGT.Residues 15-261 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD820279) which is seen in Q81ZY2_STRAW.Residues 15-305 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD239091) which is seen in Q9KJN8_MYXXA.Residues 15-261 are 47% similar to a (ORYZA SIMILAR 36I5.3 RICE. SATIVA ATP-BINDING) protein domain (PD808911) which is seen in Q86IX1_DICDI.Residues 15-269 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD141352) which is seen in O54230_STRGT.Residues 15-286 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA1D4Q5) which is seen in Q7ULK7_RHOBA.Residues 15-260 are 66% similar to a (KINASE ATP-BINDING TRANSFERASE SERINE/THREONINE-PROTEIN RECEPTOR PHOSPHORYLATION SERINE/THREONINE TYROSINE-PROTEIN REPEAT CELL) protein domain (PD000001) which is seen in Q73YP1_MYCPA.Residues 15-295 are 50% similar to a () protein domain (PDA046H8) which is seen in Q73YC5_MYCPA.Residues 15-282 are 56% similar to a (PKND) protein domain (PDA18730) which is seen in Q73UI1_MYCPA.Residues 15-266 are 58% similar to a (SERINE/THREONINE-PROTEIN KINASE PROBABLE TRANSFERASE PKNJ TRANSMEMBRANE ATP-BINDING) protein domain (PD063660) which is seen in PKNJ_MYCTU.Residues 16-260 are 57% similar to a (KINASE SERINE/THREONINE-PROTEIN PKN10 TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA043E6) which is seen in Q7UGA2_RHOBA.Residues 16-261 are 47% similar to a (KINASE TRANSFERASE TYROSINE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD289861) which is seen in Q9Y1Y3_EEEEE.Residues 16-260 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING MAP) protein domain (PDA18314) which is seen in Q93WR7_MEDVA.Residues 18-225 are 49% similar to a (CELL DIVISION KINASE SERINE/THREONINE-PROTEIN TRANSFERASE MITOSIS ATP-BINDING HOMOLOG CONTROL CYCLE) protein domain (PDA1A0C7) which is seen in CDC2_CAEEL.Residues 19-262 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN GLP_28_16955_18661 TRANSFERASE ATP-BINDING) protein domain (PDA08641) which is seen in Q7R1Q1_EEEEE.Residues 20-222 are 44% similar to a (KINASE DJFGFR1 TRANSFERASE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD611563) which is seen in Q8MY86_DUGJA.Residues 21-260 are 43% similar to a (YARROWIA LIPOLYTICA STRAIN CHROMOSOME CLIB99 B) protein domain (PDA12896) which is seen in Q6CFM7_EEEEE.Residues 21-229 are 45% similar to a (T20L15_160 AT5G01890/T20L15_160 ATP-BINDING) protein domain (PD280913) which is seen in Q9LZV7_ARATH.Residues 21-221 are 49% similar to a (KINASE SER/THR P08458 SPS1 CEREVISIAE YDR523C SACCHAROMYCES) protein domain (PDA0B8H6) which is seen in Q6C9X8_EEEEE.Residues 24-261 are 48% similar to a (KINASE RELATED ATP-BINDING SEVERIN) protein domain (PDA0F7C6) which is seen in Q7SFV7_NEUCR.Residues 32-151 are 53% similar to a (KINASE SERINE/THREONINE-PROTEIN REGULATOR SERINE/THREONINE) protein domain (PD843536) which is seen in Q9L096_STRCO.Residues 41-234 are 49% similar to a (KINASE CAMP-DEPENDENT SERINE/THREONINE-PROTEIN CATALYTIC TRANSFERASE ATP-BINDING SUBUNIT) protein domain (PD750451) which is seen in Q9BMY6_TOXGO.Residues 50-283 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN SERINE/THREONINE KINASE) protein domain (PD745593) which is seen in Q9RUY7_DEIRA.Residues 70-265 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN MAP TRANSFERASE ATP-BINDING) protein domain (PD324666) which is seen in Q9N9B1_LEIMA.Residues 70-214 are 49% similar to a (KINASE TRANSFERASE ATP-BINDING) protein domain (PD325465) which is seen in Q9LRY7_ARATH.Residues 70-260 are 52% similar to a (SERINE/THREONINE-PROTEIN KINASE YKL101W PROBABLE ATP-BINDING TRANSFERASE) protein domain (PD095148) which is seen in KKK1_YEAST.Residues 70-213 are 47% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN ANK ATP-BINDING TRANSFERASE GLP_39_28978_30531) protein domain (PD959207) which is seen in Q7R3P5_EEEEE.Residues 70-189 are 48% similar to a (CG17698-PA) protein domain (PD980872) which is seen in Q7PLK3_DROME.Residues 70-260 are 51% similar to a (KINASE CBS138 CANDIDA SEQUENCE K SERINE/THREONINE-PROTEIN GLABRATA STRAIN ATP-BINDING TRANSFERASE) protein domain (PD957660) which is seen in Q6FMF3_EEEEE.Residues 72-271 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE BRASSINOSTEROID ATP-BINDING INSENSITIVE) protein domain (PD595107) which is seen in Q84ZJ8_EEEEE.Residues 75-217 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN AGR334WP TRANSFERASE ATP-BINDING) protein domain (PDA1D2X0) which is seen in Q74Z72_ASHGO.Residues 75-291 are 50% similar to a (KINASE TRANSFERASE ATP-BINDING MOS) protein domain (PD267193) which is seen in Q9GRC0_ASTPE.Residues 82-227 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING PENTATRICOPEPTIDE REPEAT-CONTAINING PPR) protein domain (PDA18435) which is seen in Q7XB71_EEEEE.Residues 82-211 are 51% similar to a (RECEPTOR KINASE KINASE) protein domain (PD398305) which is seen in Q9C8I5_ARATH.Residues 83-213 are 53% similar to a (P0418B08.10 OJ1740_D06.39) protein domain (PDA10665) which is seen in Q69P46_EEEEE.Residues 86-208 are 49% similar to a (KINASE CDC2-LIKE ATP-BINDING) protein domain (PDA189G6) which is seen in Q6ZAG3_EEEEE.Residues 87-218 are 46% similar to a (KINASE PROBABLE TRANSMEMBRANE SERINE-THREONINE MEMBRANE POSSIBLE SCO3893 L222-ORF10) protein domain (PD147778) which is seen in Q9X8S9_STRCO.Residues 89-276 are 47% similar to a (KINASE RECEPTOR TRANSFERASE TYROSINE-PROTEIN ATP-BINDING TYROSINE) protein domain (PD566768) which is seen in Q8WSM2_SCHMA.Residues 89-214 are 54% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE CAMP ATP-BINDING CAMP-DEPENDENT NUCLEAR) protein domain (PD061517) which is seen in O00843_PARPR.Residues 89-236 are 53% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE ATP-BINDING SHK2) protein domain (PD078766) which is seen in SHK2_SCHPO.Residues 89-214 are 46% similar to a (KINASE CG6297-PB SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING JIL-1 CG6297-PA) protein domain (PD272901) which is seen in Q9V3I5_DROME.Residues 89-282 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE FLR-4 F09B12.6 ATP-BINDING) protein domain (PD291044) which is seen in Q9NLA1_CAEEL.Residues 90-261 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING MAP) protein domain (PD290024) which is seen in Q9P8J0_PNECA.Residues 90-266 are 50% similar to a () protein domain (PD743406) which is seen in Q8G5T5_BIFLO.Residues 91-260 are 47% similar to a (DOMAIN KINASE TRANSFERASE PHOSPHORYLATION TRANSDUCTION SENSORY SENSOR KINASE/GAF HISTIDINE) protein domain (PD781329) which is seen in Q88CD9_PSEPK.Residues 98-239 are 48% similar to a (GLP_80_8296_7247) protein domain (PDA0V6P5) which is seen in Q7QYK4_EEEEE.Residues 103-214 are 53% similar to a (KINASE TYROSINE-PROTEIN TRANSFERASE C03B1.5 ATP-BINDING X CHROMOSOME) protein domain (PD092556) which is seen in YX05_CAEEL.Residues 109-215 are 54% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD667099) which is seen in Q9FDV6_FAGSY.Residues 109-281 are 47% similar to a (KINASE RECEPTOR TRANSFERASE GROWTH PLATELET-DERIVED TYROSINE-PROTEIN BETA ATP-BINDING FACTOR) protein domain (PD064314) which is seen in P79749_FUGRU.Residues 109-271 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE F24O1.13 ATP-BINDING) protein domain (PD235013) which is seen in Q9MAV2_ARATH.Residues 114-261 are 50% similar to a (REPEAT GLP_59_8273_5847 ANK) protein domain (PDA1D0J5) which is seen in Q7QUF5_EEEEE.Residues 117-236 are 51% similar to a (KINASE DIVISION CELL SERINE/THREONINE-PROTEIN TRANSFERASE RELATED ATP-BINDING CYCLE 2-RELATED) protein domain (PD849176) which is seen in Q86ZH1_NEUCR.Residues 120-220 are 49% similar to a (GLP_154_37233_36121 ATP-BINDING) protein domain (PDA190Q2) which is seen in Q7R0L1_EEEEE.Residues 130-212 are 67% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING KINASE-LIKE) protein domain (PDA183S2) which is seen in O65480_ARATH.Residues 133-282 are 46% similar to a (ANK REPEAT GLP_170_100413_102890) protein domain (PD980353) which is seen in Q7R6M2_EEEEE.Residues 133-212 are 66% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING KINASE-LIKE) protein domain (PDA198D0) which is seen in Q8S1B9_EEEEE.Residues 179-279 are 50% similar to a (SCO6626 ATP-BINDING) protein domain (PDA0H7N8) which is seen in O86560_STRCO.Residues 385-471 are 54% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING SERINE/THREONINE PROBABLE REPEAT EUKARYOTIC-TYPE PKNB 2.7.1.-) protein domain (PD868469) which is seen in Q9ZNB3_STRCO.Residues 397-559 are 47% similar to a (KINASE DOMAIN TP0307 BB0063 OUTERMEMBRANE PASTA SERINE/THREONINE TRANSMEMBRANE) protein domain (PD360505) which is seen in Q73M66_TREDE.Residues 540-609 are 64% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING SERINE/THREONINE PROBABLE REPEAT 2.7.1.- PKNB EUKARYOTIC-TYPE) protein domain (PD186733) which is seen in PK1_STRTO.Residues 480-674 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PD837718) which is seen in Q88WL0_LACPL.Residues 540-609 are 64% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING SERINE/THREONINE PROBABLE REPEAT 2.7.1.- PKNB EUKARYOTIC-TYPE) protein domain (PD186733) which is seen in PK1_STRTO.Residues 541-641 are 58% similar to a (KINASE SERINE/THREONINE) protein domain (PDA0V9C9) which is seen in Q6AHM0_BBBBB.","","-59% similar to PDB:1MRU Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB. (E_value = 2.2E_48);-59% similar to PDB:1O6Y CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 2.2E_48);-59% similar to PDB:2FUM Catalytic domain of protein kinase PknB from Mycobacterium tuberculosis in complex with mitoxantrone (E_value = 2.2E_48);-55% similar to PDB:2H34 Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE (E_value = 8.2E_40);-46% similar to PDB:2BDW Crystal Structure of the Auto-Inhibited Kinase Domain of Calcium/Calmodulin Activated Kinase II (E_value = 8.5E_21);","Residues 15 to 271 (E_value = 3.6e-55) place ANA_0599 in the Pkinase family which is described as Protein kinase domain.Residues 142 to 222 (E_value = 1e-12) place ANA_0599 in the Pkinase_Tyr family which is described as Protein tyrosine kinase.Residues 411 to 474 (E_value = 3e-08) place ANA_0599 in the PASTA family which is described as PASTA domain.Residues 479 to 542 (E_value = 1.1e-14) place ANA_0599 in the PASTA family which is described as PASTA domain.Residues 547 to 611 (E_value = 1.2e-10) place ANA_0599 in the PASTA family which is described as PASTA domain.Residues 616 to 674 (E_value = 7.1e-10) place ANA_0599 in the PASTA family which is described as PASTA domain.","","kinase PK-1 (stoPK-1) (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0600","632793","631633","1161","5.80","-9.21","40962","ATGAGTGCGCTGCCTGCGGCCCTGGGCCGTGTCCGTCCCGCCGTCGAGCACCGCCTGACCCAGGTCCTGGAGGACTGCCACCTGCGCTGGGAGGACCTGGGGCAGGCCGCCCCGGAGCTGCTCGAGGCCGCCGGGAGCGTCCTGAGTGGCGGCAAGCGCATGCGGGCCGTCCTGGGGGCTGTCGGCTGCGCGATCCTGAGCGCCCCGAAGCAGCGGGCCGAGCGCCTGACCGGTTCCGACGCCGTCCACCTGGGTACGGCGCTGGAGCTCTACCAGGCCAGTGCCCTGGTGCACGACGACCTCATGGATAGCGCCGACACGCGCCGGGGCCTACCCGCAGCACACCGCGTCTTCGCCCGAAACCACGAGGCCCGGGGCTGGCTGGGGCGCCCGCAGACCTTTGGGGCCAATGGCGCCATCCTGCTCGGCGATCTCCTGCTGTCCCTGGCCGGCGAGGAGATGAGCGCGCTGGCGCCGTCGCGAGCCTCAAGCCAGACCCGAAGCAGTGCGGTGCGGTACGCCAGGTCCGCTTTCGACGCCATGACCACCGAGGTGGCCCTGGGCCAGTTCCTCGACGTGCGCAGCGAGAACCTGCCCCTGCCTTGGGACCAGGAGCCGGGTGCCGCAGCCAGGCGCATGCAGAACGAGGCCCTGTCGGTCGTACGGCACAAGTCAGCTCGCTACTCGGTGCGCCACCCACTGCTCATCGGCGCCCTCCTGGCCGGACTGGACCCGAGCGGGACCACTGCCGAGCACCTGGCCGCCTTCGGCGAGGACGTCGGCATCGCCTTCCAGCTGCGCGACGACGATCTGGGAGTCTTCGGCTCGCCACAGGCCACCGGCAAGCCGGCCGGGGACGATCTGCGCGAGGGCAAGCGCACAGTGCTGCTGGCCCTGACCTGGGGGCGCTGCGACGAGGCCGGCCGCCGGATGCTCGGTAGCGTCCTGGCCAATCCCGAGGCCACGGAGGAGCAGATCGGCGAGGTCGCCGCTCTCATCGAGGACTGCGGCGCGCGCGCCGCCCACGAGGAGATCATCGCCGCGCACCGCGAGGCCGGGAACCGGGCGCTGGAGCGCCTCGGGGACGAGGGCGTGGTGAGCACCGCATCCCTGGAGGACCTGGCGGTGCTGGCGGACCTGCTGACGCACCGGGTCTCCTGA","MSALPAALGRVRPAVEHRLTQVLEDCHLRWEDLGQAAPELLEAAGSVLSGGKRMRAVLGAVGCAILSAPKQRAERLTGSDAVHLGTALELYQASALVHDDLMDSADTRRGLPAAHRVFARNHEARGWLGRPQTFGANGAILLGDLLLSLAGEEMSALAPSRASSQTRSSAVRYARSAFDAMTTEVALGQFLDVRSENLPLPWDQEPGAAARRMQNEALSVVRHKSARYSVRHPLLIGALLAGLDPSGTTAEHLAAFGEDVGIAFQLRDDDLGVFGSPQATGKPAGDDLREGKRTVLLALTWGRCDEAGRRMLGSVLANPEATEEQIGEVAALIEDCGARAAHEEIIAAHREAGNRALERLGDEGVVSTASLEDLAVLADLLTHRVS$","Geranylgeranyl pyrophosphate synthase","Cytoplasm","Geranylgeranyl pyrophosphate synthase","geranylgeranyl pyrophosphate synthase ","Polyprenyl synthetase","","Ashby M.N., Edwards P.A. Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase. J. Biol. Chem. 1990. 265(22):13157-13164. PMID: 2198286Fujisaki S., Hara H., Nishimura Y., Horiuchi K., Nishino T. Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli. J. Biochem. 1990. 108(6):995-1000. PMID: 2089044Carattoli A., Romano N., Ballario P., Morelli G., Macino G. The Neurospora crassa carotenoid biosynthetic gene (albino 3) reveals highly conserved regions among prenyltransferases. J. Biol. Chem. 1991. 266(9):5854-5859. PMID: 1826006Kuntz M., Romer S., Suire C., Hugueney P., Weil J.H., Schantz R., Camara B. Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: correlative increase in enzyme activity and transcript level during fruit ripening. Plant J. 1992. 2(1):25-34. PMID: 1303794Math S.K., Hearst J.E., Poulter C.D. The crtE gene in Erwinia herbicola encodes geranylgeranyl diphosphate synthase. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(15):6761-6764. PMID: 1495965","","","

InterPro
IPR000092
Family

Polyprenyl synthetase
PTHR12001	$\"[50-115]T$ $\"[132-384]T$	GERANYLGERANYL PYROPHOSPHATE SYNTHASE
PF00348	$\"[40-343]T$	polyprenyl_synt
PS00723	$\"[96-110]T$	POLYPRENYL_SYNTHET_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.600.10	$\"[15-384]T$	no description
PTHR12001:SF7	$\"[50-115]T$ $\"[132-384]T$	GERANYLGERANYL DIPHOSPHATE SYNTHASE

","BeTs to 25 clades of COG0142COG name: Geranylgeranyl pyrophosphate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0142 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB000092 (Polyprenyl synthetase) with a combined E-value of 8.4e-13. IPB000092B 100-113 IPB000092D 260-282","Residues 18-335 are 40% similar to a (FARNESYL SYNTHETASE PYROPHOSPHATE DIPHOSPHATE SYNTHASE BIOSYNTHESIS FPP INCLUDES: GERANYLTRANSTRANSFERASE DIMETHYLALLYLTRANSTRANSFERASE) protein domain (PD614874) which is seen in Q8WMY2_BOVIN.Residues 92-193 are 55% similar to a (SYNTHASE TRANSFERASE GERANYLGERANYL DIPHOSPHATE PYROPHOSPHATE GERANYLTRANSTRANSFERASE SYNTHETASE POLYPRENYL OCTAPRENYL-DIPHOSPHATE 2.5.1.-) protein domain (PD000572) which is seen in Q8NNM1_CORGL.Residues 181-337 are 50% similar to a (SYNTHASE PYROPHOSPHATE POLYPRENYL DIPHOSPHATE GERANYLGERANYL) protein domain (PD717068) which is seen in Q83NG2_TROW8.Residues 218-337 are 50% similar to a (TRANSFERASE CHAIN DIPHOSPHATE BIFUNCTIONAL ISOPRENYL SHORT) protein domain (PD987135) which is seen in Q7NR31_CHRVO.Residues 224-274 are 68% similar to a (SYNTHETASE GERANYLGERANYL SYNTHASE DIPHOSPHATE PYROPHOSPHATE GGPP TRANSFERASE POLYPRENYL IDSA2 PROBABLE) protein domain (PD957486) which is seen in Q6AE53_BBBBB.Residues 275-337 are 55% similar to a (SYNTHASE OCTAPRENYL-DIPHOSPHATE TRANSFERASE SYNTHETASE PYROPHOSPHATE DIPHOSPHATE GERANYLGERANYL 2.5.1.- POLYPRENYL GGPP) protein domain (PD582049) which is seen in Q6A9S7_PROAC.","","-38% similar to PDB:1WMW Crystal structure of geranulgeranyl diphosphate synthase from Thermus thermophilus (E_value = 1.2E_15);-40% similar to PDB:2H8O The 1.6A crystal structure of the geranyltransferase from Agrobacterium tumefaciens (E_value = 9.9E_13);-42% similar to PDB:1UBX STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE (E_value = 1.6E_10);-41% similar to PDB:1FPS CRYSTAL STRUCTURE OF RECOMBINANT FARNESYL DIPHOSPHATE SYNTHASE AT 2.6 ANGSTROMS RESOLUTION (E_value = 7.8E_10);-39% similar to PDB:1RQI Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate (E_value = 7.8E_10);","Residues 40 to 343 (E_value = 3.1e-23) place ANA_0600 in the polyprenyl_synt family which is described as Polyprenyl synthetase.","","pyrophosphate synthase (GGPPSASE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0602","632947","634662","1716","4.79","-40.44","63528","TTGTCTACTGCGCCGGATCGGGTTCCCATACCCCGTCACCGGCTGTCCGCCCGCCCACGCGAAAGGAACTCCGTGGCTTCTTCCACAGTGAAGCGCTCCAGCACCGAGCTCACTGACGACGTCGACGAGACCCCGCTCGACGACGAGGACTTCGACCTCGACGACGAAGGAGACGACGACGCCGACTACGACGACGAGGACTACGACGACTCTGACGAGGACGACGAGGACTCCTCTGATGGGGACGAGGACCAGGATGACGACTCCGAGGCGCAGGCTGTCCAGGAGGATGACGGCCCAGCCGCCGAGCTGCGCGACTACTACCTGGATGTGAGCCTGGAGGAGAACGGCGACGGCTCCAAGCGCAGCCCCTTCAACGACCCCGCCTCCCTCAAGGGGGTTCGTCTGGCACCGGGGGCGACTCTCTTCGTGCGATCGCGCACGGTTGTGGAGAACCTGGAGATCGCCGGCCACGGCACCCTGGAGGAGCCCATCACGCTGGCCCCCTACGGCCACGGACCGGTGCCTCGCTTCGTCATCGGCGACTCCGCCCCCATGGTGGCGCGCGACTACCTCGCTCAGAACGGCTACATCTTCCGTGGCTGGGTCATCAAGGGCATCAAGATGCAGCCCTCCATCGCGGCCCTGACCGGTGAGCTCGAGCGCATGCGTCGGGAGGAGGCGGAGAAGGCCGCCTCCAAGAAGTCCGGCAAGCGCGGCAAGTCCCAGGACAAGGACGGCTCCTTCACCGTCTCCGACTCCGACGAGGGTGACGAGCCGGCCCAGCGGGTCGTCACCGCCGGCGCCACCGCGGACCCGGTCAAGGACTACCTCAAGCAGATCGGTAAGGTCGCGCTGCTGAACGCCGAGCAGGAGGTCGAGCTCGCCAAGCGCATCGAGGCCGGTCTTTACGCCGAGCACCGCCTGGCCGAGGAGGGCAACGACCTGCCGGCCAAGCTGCGTCGCGAGCTGCACTGGGTGGCCCAGGACGGCCAGGGGGCCAAGAACCACCTGCTGGAGGCCAACCTGCGACTGGTGGTCTCCCTGGCCAAGCGCTACACGGGCCGCGGCATGCTCTTCCTGGACCTCATCCAGGAGGGCAACCTGGGCCTCATCCGCGCCGTGGAGAAGTTCGACTACACCAAGGGCTTCAAGTTCTCCACCTACGCCACCTGGTGGATTCGCCAGGCCATTACCCGCGCGATGGCGGACCAGGCCCGTACCATCCGCATTCCGGTGCACATGGTCGAGGTCATCAACAAGCTCGCCCGCGTACAGCGCCAGATGCTTCAGGACCTGGGACGTGAGCCCACCCCGGAGGAGCTGGCCGTCGAGCTGGACATGACCCCGGAAAAGGTGGTCGAGGTCCAGAAGTACGGGCGCGAGCCGATCTCCCTGCACACGCCGCTGGGTGAGGACGGGGACTCGGAGTTCGGTGACCTCATTGAGGACTCCGAGGCCGTGGTCCCGGCCGACGCGGTGAGTTTCACCCTCCTGCAGGAGCAGCTCCACGCCGTGCTGGACACCCTCTCGGAGCGTGAGGCCGGCGTGGTCTCCATGCGTTTCGGTCTGACCGATGGCCAGCCCAAGACCCTCGATGAGATCGGCAAGGTCTACGGGGTTACCCGGGAGCGTATCCGCCAGATCGAGTCCAAGACCATGTCCAAGCTGCGCCACCCCTCGCGCAGCCAGGTCCTGCGCGACTACCTGGACTGA","LSTAPDRVPIPRHRLSARPRERNSVASSTVKRSSTELTDDVDETPLDDEDFDLDDEGDDDADYDDEDYDDSDEDDEDSSDGDEDQDDDSEAQAVQEDDGPAAELRDYYLDVSLEENGDGSKRSPFNDPASLKGVRLAPGATLFVRSRTVVENLEIAGHGTLEEPITLAPYGHGPVPRFVIGDSAPMVARDYLAQNGYIFRGWVIKGIKMQPSIAALTGELERMRREEAEKAASKKSGKRGKSQDKDGSFTVSDSDEGDEPAQRVVTAGATADPVKDYLKQIGKVALLNAEQEVELAKRIEAGLYAEHRLAEEGNDLPAKLRRELHWVAQDGQGAKNHLLEANLRLVVSLAKRYTGRGMLFLDLIQEGNLGLIRAVEKFDYTKGFKFSTYATWWIRQAITRAMADQARTIRIPVHMVEVINKLARVQRQMLQDLGREPTPEELAVELDMTPEKVVEVQKYGREPISLHTPLGEDGDSEFGDLIEDSEAVVPADAVSFTLLQEQLHAVLDTLSEREAGVVSMRFGLTDGQPKTLDEIGKVYGVTRERIRQIESKTMSKLRHPSRSQVLRDYLD$","RNA polymerase sigma factor RpoD","Cytoplasm","RNA polymerase principal sigma factor hrdB","K03086 RNA polymerase primary sigma factor","RNA polymerase sigma factor RpoD","","Simmer J.P., Kelly R.E., Rinker Jr A.G., Scully J.L., Evans D.R. Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD. J. Biol. Chem. 1990. 265(18):10395-10402. PMID: 1972379","","","

InterPro
IPR000943
Domain

RNA polymerase, Sigma-70 factor
PR00046	$\"[362-375]T$ $\"[386-394]T$ $\"[510-522]T$ $\"[531-546]T$ $\"[546-557]T$	SIGMA70FCT
PS00715	$\"[362-375]T$	SIGMA70_1
PS00716	$\"[531-557]T$	SIGMA70_2

InterPro
IPR005479
Domain

Carbamoyl-phosphate synthase L chain, ATP-binding
PS00867	$\"[338-345]?$	CPSASE_2

InterPro
IPR007624
Domain

RNA polymerase sigma-70 region 3
PF04539	$\"[412-494]T$	Sigma70_r3

InterPro
IPR007627
Domain

RNA polymerase sigma-70 region 2
PF04542	$\"[338-408]T$	Sigma70_r2

InterPro
IPR007630
Domain

RNA polymerase sigma-70 region 4
PF04545	$\"[506-559]T$	Sigma70_r4

InterPro
IPR009042
Domain

RNA polymerase, Sigma-70 region 1.2
PF00140	$\"[271-307]T$	Sigma70_r1_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[411-462]T$ $\"[492-570]T$	no description

InterPro
IPR012760
Domain

RNA polymerase sigma factor RpoD, C-terminal
TIGR02393	$\"[334-571]T$	RpoD_Cterm: RNA polymerase sigma factor Rpo

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[14-117]T$	no description

InterPro
IPR014284
Domain

RNA polymerase sigma-70
TIGR02937	$\"[333-561]T$	sigma70-ECF: RNA polymerase sigma factor, s

noIPR
unintegrated

unintegrated
G3DSA:1.10.601.10	$\"[286-407]T$	no description

","BeTs to 18 clades of COG0568COG name: DNA-directed RNA polymerase sigma subunits (sigma70/sigma32)Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0568 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB007631 (Sigma-70, non-essential region) with a combined E-value of 1.1e-131. IPB007631B 268-314 IPB007631C 327-367 IPB007631D 368-389 IPB007631E 390-412 IPB007631F 413-447 IPB007631G 448-484 IPB007631H 502-530 IPB007631I 533-571***** IPB000943 (Sigma-70 factor family) with a combined E-value of 5.2e-58. IPB000943A 351-402 IPB000943B 531-558***** IPB007630 (Sigma-70 region 4) with a combined E-value of 1.1e-39. IPB007630A 362-395 IPB007630B 531-558***** IPB007759 (DNA-directed RNA polymerase delta subunit) with a combined E-value of 1.3e-12. IPB007759B 55-91 IPB007759B 40-76 IPB007759B 38-74 IPB007759B 50-86 IPB007759B 48-84 IPB007759B 46-82 IPB007759B 36-72 IPB007759B 42-78 IPB007759B 47-83 IPB007759B 39-75 IPB007759B 52-88 IPB007759B 49-85 IPB007759B 54-90 IPB007759B 53-89 IPB007759B 43-79 IPB007759B 56-92 IPB007759B 41-77 IPB007759B 45-81 IPB007759B 60-96 IPB007759B 37-73 IPB007759B 62-98 IPB007759B 34-70 IPB007759B 30-66 IPB007759B 57-93 IPB007759B 59-95 IPB007759B 64-100 IPB007759B 51-87 IPB007759B 44-80 IPB007759B 58-94 IPB007759B 65-101 IPB007759B 35-71 IPB007759B 29-65 IPB007759B 31-67 IPB007759B 67-103 IPB007759B 33-69 IPB007759B 66-102 IPB007759B 68-104 IPB007759B 61-97 IPB007759B 70-106 IPB007759B 26-62 IPB007759B 32-68***** IPB007984 (Poxvirus DNA-directed RNA polymerase, 19 kDa subunit) with a combined E-value of 8.2e-09. IPB007984A 56-84 IPB007984A 55-83 IPB007984A 64-92 IPB007984A 50-78 IPB007984A 48-76 IPB007984A 53-81 IPB007984A 62-90 IPB007984A 47-75 IPB007984A 60-88 IPB007984A 52-80 IPB007984A 70-98 IPB007984A 65-93 IPB007984A 51-79 IPB007984A 58-86 IPB007984A 63-91 IPB007984A 66-94 IPB007984A 46-74 IPB007984A 54-82 IPB007984A 61-89 IPB007984A 45-73","Residues 260-303 are 95% similar to a (SIGMA FACTOR RNA POLYMERASE DNA-DIRECTED TRANSCRIPTION REGULATION DNA-BINDING TRANSFERASE RPOD) protein domain (PD003138) which is seen in P95644_RENSA.Residues 322-358 are 91% similar to a (FACTOR RNA SIGMA POLYMERASE DNA-DIRECTED TRANSCRIPTION REGULATION DNA-BINDING TRANSFERASE RPOD) protein domain (PD000245) which is seen in Q6AFF9_BBBBB.Residues 361-391 are identical to a (FACTOR SIGMA RNA POLYMERASE DNA-DIRECTED TRANSCRIPTION DNA-BINDING REGULATION TRANSFERASE RPOD) protein domain (PDA00051) which is seen in Q6AFF9_BBBBB.Residues 362-568 are 45% similar to a (RNA FACTOR POLYMERASE SIGMA-F LAMBDABA02 PROPHAGE) protein domain (PD842007) which is seen in Q81W67_BACAN.Residues 392-463 are 62% similar to a (POLYMERASE RNA SIGMA FACTOR DNA-DIRECTED RPOS TRANSFERASE REGULATION DNA-BINDING TRANSCRIPTION) protein domain (PD766475) which is seen in O67437_AQUAE.Residues 392-416 are identical to a (SIGMA FACTOR RNA POLYMERASE DNA-DIRECTED TRANSCRIPTION REGULATION DNA-BINDING TRANSFERASE RPOD) protein domain (PD000270) which is seen in Q9ANT7_BBBBB.Residues 392-443 are 76% similar to a (FACTOR SIGMA RNA POLYMERASE DNA-DIRECTED TRANSFERASE TRANSCRIPTION PLASTID DNA-BINDING REGULATION) protein domain (PD968495) which is seen in Q7UTR4_RHOBA.Residues 392-570 are 56% similar to a (POLYMERASE DNA-DIRECTED RNA SIGMA SUBUNITS REGULATION DNA-BINDING SIGMA70/SIGMA32 TRANSFERASE FACTOR) protein domain (PD751493) which is seen in Q8R8A7_THETN.Residues 417-513 are 50% similar to a (POLYMERASE RNA DNA-DIRECTED SIGC SIGMA TRANSFERASE REGULATION DNA-BINDING FACTOR TRANSCRIPTION) protein domain (PD751505) which is seen in P77841_CHLAU.Residues 417-455 are 89% similar to a (RNA POLYMERASE SIGMA FACTOR DNA-DIRECTED TRANSCRIPTION DNA-BINDING REGULATION TRANSFERASE RPOD) protein domain (PD996759) which is seen in RPOD_BACSU.Residues 417-456 are identical to a (SIGMA FACTOR RNA POLYMERASE DNA-DIRECTED TRANSCRIPTION REGULATION DNA-BINDING TRANSFERASE RPOD) protein domain (PD871459) which is seen in P95644_RENSA.Residues 462-571 are 56% similar to a (SIGB SIGC) protein domain (PD711741) which is seen in O64420_CYACA.Residues 463-511 are similar to a (SIGMA FACTOR RNA POLYMERASE DNA-DIRECTED TRANSCRIPTION REGULATION DNA-BINDING TRANSFERASE RPOD) protein domain (PD637792) which is seen in Q82KF9_STRAW.Residues 512-547 are identical to a (SIGMA FACTOR RNA POLYMERASE DNA-DIRECTED TRANSCRIPTION REGULATION DNA-BINDING TRANSFERASE RPOD) protein domain (PD867700) which is seen in Q82KF9_STRAW.","","-66% similar to PDB:1IW7 Crystal structure of the RNA polymerase holoenzyme from Thermus thermophilus at 2.6A resolution (E_value = 2.1E_89);-70% similar to PDB:1L9U THERMUS AQUATICUS RNA POLYMERASE HOLOENZYME AT 4 A RESOLUTION (E_value = 2.1E_89);-66% similar to PDB:1SMY Structural basis for transcription regulation by alarmone ppGpp (E_value = 2.1E_89);-66% similar to PDB:1ZYR Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin (E_value = 2.1E_89);-66% similar to PDB:2A68 Crystal structure of the T. thermophilus RNA polymerase holoenzyme in complex with antibiotic rifabutin (E_value = 2.1E_89);","Residues 271 to 307 (E_value = 6.3e-18) place ANA_0602 in the Sigma70_r1_2 family which is described as Sigma-70 factor, region 1.2.Residues 338 to 408 (E_value = 2.6e-29) place ANA_0602 in the Sigma70_r2 family which is described as Sigma-70 region 2.Residues 412 to 494 (E_value = 1.2e-41) place ANA_0602 in the Sigma70_r3 family which is described as Sigma-70 region 3.Residues 506 to 559 (E_value = 3.4e-25) place ANA_0602 in the Sigma70_r4 family which is described as Sigma-70, region 4.","","polymerase principal sigma factor hrdB (SigA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0603","635219","634812","408","8.47","2.34","13563","GTGAAACGTCCTCTCCGCGTCATAACCGCCTCTGCTCTGCTCGTCGTTTGCAGCGCGATCGCACTTTCAGGATGCTCCGGTTCCGCCGGCTCCAGCGCCTCCTCCTCTGCCAACACCGCCTCGGCGGGCGCGAAGGCATCCGGTCCCGTCATCATCGACCTGCGTTCGGCTGAGGAGTTCAAGAAGGGGCACCTCGAGGGGGCAGTTAACTACGACTTCTCCTCAGGTGATTTCTCCAGCCAGATCTCGAGCCTGGACCACAGCTCCCAGTACCAGCTTTACGGCTCCGCCGACCAGCCCAAGATGGCCAGCGCCGTCATGCGCAACGCCGGCTTCTCCAGCGTCACCGAACTGGGGACCCTCGACGCCGCCAAGAAGACCACCGGGGCCAAGGTCGTCACCGGCTGA","VKRPLRVITASALLVVCSAIALSGCSGSAGSSASSSANTASAGAKASGPVIIDLRSAEEFKKGHLEGAVNYDFSSGDFSSQISSLDHSSQYQLYGSADQPKMASAVMRNAGFSSVTELGTLDAAKKTTGAKVVTG$","Phage shock protein","Extracellular, Periplasm","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Hofmann K., Bucher P., Kajava A.V. A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. J. Mol. Biol. 1998. 282(1):195-208. PMID: 9733650Gliubich F., Gazerro M., Zanotti G., Delbono S., Bombieri G., Berni R. Active site structural features for chemically modified forms of rhodanese. J. Biol. Chem. 1996. 271(35):21054-21061. PMID: 8702871","","","

InterPro
IPR001763
Domain

Rhodanese-like
SM00450	$\"[35-130]T$	RHOD
PS50206	$\"[45-133]T$	RHODANESE_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.250.10	$\"[46-118]T$	no description
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[10-30]?$	transmembrane_regions

","BeTs to 9 clades of COG0607COG name: Rhodanese-related sulfurtransferasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0607 is aomp--yq-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 3","***** IPB001763 (Rhodanese-like) with a combined E-value of 3.2e-06. IPB001763A 51-68","No significant hits to the ProDom database.","","-76% similar to PDB:1C25 HUMAN CDC25A CATALYTIC DOMAIN (E_value = );-79% similar to PDB:1TQ1 Solution structure of At5g66040, a putative protein from Arabidosis Thaliana (E_value = );","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0604","635727","635464","264","5.07","-4.44","9275","ATGAGCACAACCGGAACCTCAACCGCCGCGCAGGCGGTGACCACCCTGGACGAGCAGGCCACTCCTGCCGCCGACTCCACCGAGCGCCCGCTGACCACAGCCGACCGCTGCGACGTCTGCGACGCGCAGGCCTACGTCCGAGTCGTCATGCTGACCGGCGAGCTCTTCTTCTGCGGCCACCATGCCCGCAAGCACGCAGACAAGCTCAAAGAGGTCGCCCTGCTGTTCCAGGACGAGACCTCGACCCTGACCTCCGGCAGCTGA","MSTTGTSTAAQAVTTLDEQATPAADSTERPLTTADRCDVCDAQAYVRVVMLTGELFFCGHHARKHADKLKEVALLFQDETSTLTSGS$","Hypothetical protein","Periplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 31-69 are similar to a (GP52) protein domain (PD926331) which is seen in Q6AFE7_BBBBB.","","-67% similar to PDB:1B89 CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE) (E_value = );-67% similar to PDB:1XI4 Clathrin D6 Coat (E_value = );-67% similar to PDB:1XI5 Clathrin D6 coat with auxilin J-domain (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0605","635920","636693","774","5.12","-8.37","27473","ATGTCAGTGGTGCAGGAGTTCCGCGACCGTGAGATCGCGCGCCTGGAGCGCTCGGGCTGGGCGACCAACGTGGCCCTTCGACAGAGGCTGGAGGCCGTAGGGCTGCGGCCGCCCGCCGAGGTCGTTGCCGAGTGCCTGGACGAGGGCGCGGGAGACGGAGGCGGTGCCGGTGCCCGCTGGGCGCGGGCCGAGTGCGCGGTGGCCCACTTAAGGGAGCACTTCGCCTCATTCCGCTTCTCCGACGACGTCGACTACGGGCTCCTGGCGGTCCCGGCCAGTAACCGACTCGACACCCGCGGGGCCATGGACCTGAACATCCGCCGCGGTCAGCAGCCCGATCTGACCGAGGACTTCGTCGATCCGGCCCTGGGGGAGGGGGCCGACCTCGCCGACTCCACCGATGCTGCTGGGGCCACGCTGGGAAAGGACGGCTGGATGGTGGTGGCCGGCGTCGTCGGCCAGTACGGGATCTCGGCGGGAAGCCATGAGGACGTCACCGCCGCCGCGGAGCTCTTCGAGGTCGACGGCGTCGACACCCGCACCCTCATGACCCGTCAGATCTGGGGAGCCCGCCTCCTGCAGTGCCCACCAGGGCTCGTTCCCGACTCGGACTACGCCGAGCGATGGACCTTCACGCTCCTGCCCGGCGAGGGGCTAGTGGATGGGCGGGCCGTCTCCGGCACCGTGCTCAAGAGGCGGGTGCGCTTCCGACTGGGCAAGGCCGACCGTGGGATCGGCAGTGCGCGGGTGAGCCCCGCCCTGCCGCTGACGTAG","MSVVQEFRDREIARLERSGWATNVALRQRLEAVGLRPPAEVVAECLDEGAGDGGGAGARWARAECAVAHLREHFASFRFSDDVDYGLLAVPASNRLDTRGAMDLNIRRGQQPDLTEDFVDPALGEGADLADSTDAAGATLGKDGWMVVAGVVGQYGISAGSHEDVTAAAELFEVDGVDTRTLMTRQIWGARLLQCPPGLVPDSDYAERWTFTLLPGEGLVDGRAVSGTVLKRRVRFRLGKADRGIGSARVSPALPLT$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0606","636796","639048","2253","5.94","-11.37","81812","GTGCCCTCATCTGAGAACAAGACCAGCCGGGGCGACTACTCCGCCCGCCACCTCTCCGTCCTGGAGGGGCTCGAGGCCGTGCGCAAGCGGCCGGGAATGTACATCGGCTCCACCGACCAGCGCGGTCTCATGCACTGCGTGTGGGAGATCGTGGACAACGCCGTCGATGAGGCCCTCGAGGGGCACGGCGACGACATCTCAGTGACCGTCCACGACGACGGCTCCATCGAGGTGCGTGACAACGGGCGCGGCGTGCCCGTGGACATCGAGCCCTCATCCGGCCTGACCGGCGTCGAGCTCGTCTACACCAAGCTGCACGCCGGCGGGAAGTTCGGCGGCGGCTCCTACGGCGCCGCCGGCGGTCTGCACGGCGTGGGGGCGTCCGTCGTCAACGCCCTGGCCGAGCGCATGGACGTCGAGGTCGACCGCGGCGGCAAGACCTACGCCATGAGCTTCCACCGCGGCGAGCCCGGCATCTTCGACGACTCCGCCGGGCGCGGCCCCTCCTCGCCCTTCACCGGATTCACGAAGTCCTCCGAGCTGCGCGTCATCGGCAAGGTGCGCCGCGGCGTGACCGGAACCCGGGTCCGCTACTGGGCCGACCCCCAGATCTTCCCCAAACCCACCGAGTACGACGCCGCCGCCCTGCGCGCCCGCCTGCGCCAGACCAGTTTCCTCGTCCCGGGCCTCACCCTGCGCCTGGAGGACAAGCGCCCCGAGGCCGAGGCCATCGCGGCCTCCACCACGCCGGCTGCCGACGCCGGCGAGACCGACGACGCCGTCCACGAGGTCACCCTGCGCGCGGCTGCCAAGAACGCCACCGAGAATCGCGGCGACCTGTTCGACACCGGTGATGACGACGGCGTCGAGGTCTTCCAGGCCCTGGGCGGCACCGCCGACTTCGTCGACTTCCTGGCCTCCGACGGCTCAGTCACCGACACCTTCCGCCTCACCGGCGAAGGCACCTACACCGAGACCGTCCAGCAGCTCGACCGCGCCAGCGGGCACCTGCGCCCCGTGGAGGTCGAGCGCACCTGCATGGTTGACGTCGCCCTGCGCTGGGGGATCGGCTACGACACCACGGAACGCTCCTTCGTCAACATTATCGCCACCCCCATGGGCGGCACCCACCTGACCGGATTCGAGCAGGCCCTCACCAAGGTGCTGCGCAAGCGCATCGAGGCCGACTCCCGGGCCTTGAAGCTCAGCGCCAAGGACGGCCGCGTCGAGAAGGACGACATCATGGCGGGCCTGACCGCCGTCATCACCGTGCGCGTCCCCGAGCCCCAGTTCGAGGGCCAGACCAAGGAGGTCCTGGGCACCGGGCCCGTGCGCCAGATCGTCTCCAAGGTGGTCGAGCGCGAGCTCACCGCCCTGCTGACCTCCTCCAAACGGGACCTCAAGACCCAGGCGCGCGCCCTGGAGGAGAAGATCGTCGGTGAGATGCGTGCCCGCGTCTCAGCGCGCCTGCACAAGGAGATCACTCGCCGCAAAACCGCTCTGGAGACCTCCTCCCTGCCGGCCAAGCTCGCCGACTGCCGCAGCGACGACGTTGCCGCCTCCGAGCTGTTCATCGTCGAGGGCGACTCCGCCCTGGGGACCGCCAAGAATGCCCGCGACTCCGAGTTCCAGGCGCTCCTGCCGATCCGCGGCAAGATCCTCAACGTGCAGAAGGCCTCCCAGGCCGACATGCTGCGCAACGTCGAGTGCTCGGCCATTATCCAGGTGGTCGGCGCCGGCAGCGGACGCACCTTCGACCTGGAGGCCGCCCGCTACGGCAAGGTCATCCTCATGACCGACGCCGACGTCGACGGCGCTCACATCCGTACCCTCCTGCTGACTCTCTTCTTCCGCTACATGCGCCCCATGATCGAGGCGGGCCGGGTTTTCGCCGCCGTCCCGCCCCTGCACCGCATCGAGGTCTCCGGCTCTGGGCGGCGCAAGAAGGAGATCATCTACACCTACTCCGATGAGGAGCTCGTCACCACCCTGCGCCGCCTGGAGCGCGCGGGCCGCAGCTTCAAGGAGCCGCAGCGCTACAAGGGCCTGGGGGAGATGGACGCCCACCAGCTCGCCGAGACCACCATGGAGCCCCAGCACCGGACCCTGCGGCGCATCACCCTGGGGGACGAGGCCCAGATCATGGAGGCCGAGTCCGTCTTCGAGCTCCTCATGGGCTCATCGGTCGAGCCCCGCCGGGACTTCATCGTCGAAGGCGCCCGTGACGTTGATCGCGAGCGCATCGACGCCTGA","VPSSENKTSRGDYSARHLSVLEGLEAVRKRPGMYIGSTDQRGLMHCVWEIVDNAVDEALEGHGDDISVTVHDDGSIEVRDNGRGVPVDIEPSSGLTGVELVYTKLHAGGKFGGGSYGAAGGLHGVGASVVNALAERMDVEVDRGGKTYAMSFHRGEPGIFDDSAGRGPSSPFTGFTKSSELRVIGKVRRGVTGTRVRYWADPQIFPKPTEYDAAALRARLRQTSFLVPGLTLRLEDKRPEAEAIAASTTPAADAGETDDAVHEVTLRAAAKNATENRGDLFDTGDDDGVEVFQALGGTADFVDFLASDGSVTDTFRLTGEGTYTETVQQLDRASGHLRPVEVERTCMVDVALRWGIGYDTTERSFVNIIATPMGGTHLTGFEQALTKVLRKRIEADSRALKLSAKDGRVEKDDIMAGLTAVITVRVPEPQFEGQTKEVLGTGPVRQIVSKVVERELTALLTSSKRDLKTQARALEEKIVGEMRARVSARLHKEITRRKTALETSSLPAKLADCRSDDVAASELFIVEGDSALGTAKNARDSEFQALLPIRGKILNVQKASQADMLRNVECSAIIQVVGAGSGRTFDLEAARYGKVILMTDADVDGAHIRTLLLTLFFRYMRPMIEAGRVFAAVPPLHRIEVSGSGRRKKEIIYTYSDEELVTTLRRLERAGRSFKEPQRYKGLGEMDAHQLAETTMEPQHRTLRRITLGDEAQIMEAESVFELLMGSSVEPRRDFIVEGARDVDRERIDA$","DNA gyrase subunit B","Cytoplasm","DNA gyrase subunit B","DNA gyrase subunit B ","DNA topoisomerase (ATP-hydrolyzing)","","Bergerat A., de Massy B., Gadelle D., Varoutas P.C., Nicolas A., Forterre P. An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 1997. 386(6623):414-417. PMID: 9121560Versalovic J., Lupski J.R. The Haemophilus influenzae dnaG sequence and conserved bacterial primase motifs. Gene 1993. 136(1):281-286. PMID: 8294018Aravind L., Leipe D.D., Koonin E.V. Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Nucleic Acids Res. 1998. 26(18):4205-4213. PMID: 9722641","","","

InterPro
IPR000565
Family

DNA topoisomerase, type IIA, subunit B
PR01159	$\"[13-23]T$ $\"[225-238]T$ $\"[457-477]T$ $\"[573-582]T$ $\"[717-733]T$	DNAGYRASEB

InterPro
IPR001241
Domain

DNA topoisomerase, type IIA, subunit B or N-terminal
PR00418	$\"[42-57]T$ $\"[77-90]T$ $\"[120-134]T$ $\"[589-605]T$ $\"[607-624]T$ $\"[627-639]T$ $\"[677-693]T$	TPI2FAMILY
SM00433	$\"[42-741]T$	TOP2c
PS00177	$\"[525-533]?$	TOPOISOMERASE_II

InterPro
IPR002288
Domain

DNA topoisomerase, type IIA, subunit B, C-terminal
PF00986	$\"[668-737]T$	DNA_gyraseB_C

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[10-249]T$	no description
PF02518	$\"[38-203]T$	HATPase_c
SM00387	$\"[38-204]T$	HATPase_c

InterPro
IPR006171
Domain

TOPRIM
PF01751	$\"[521-632]T$	Toprim

InterPro
IPR011558
Domain

DNA topoisomerase, type IIA, subunit B, conserved region
PD149633	$\"[528-640]T$	O69998_STRCO_O69998;

InterPro
IPR013506
Domain

DNA topoisomerase, type IIA, subunit B, region 2
PF00204	$\"[297-494]T$	DNA_gyraseB

InterPro
IPR013759
Domain

DNA topoisomerase, type IIA, subunit B or N-terminal, alpha-beta
G3DSA:3.40.50.670	$\"[487-720]T$	no description

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[345-468]T$	no description

noIPR
unintegrated

unintegrated
PTHR10169	$\"[32-152]T$ $\"[172-242]T$ $\"[289-317]T$ $\"[344-746]T$	DNA TOPOISOMERASE/GYRASE
PTHR10169:SF3	$\"[32-152]T$ $\"[172-242]T$ $\"[289-317]T$ $\"[344-746]T$	DNA GYRASE SUBUNIT B

","BeTs to 22 clades of COG0187COG name: DNA gyrase (topoisomerase II) B subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0187 is ao-p--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB002288 (DNA gyrase, subunit B, C-terminal) with a combined E-value of 7.5e-200. IPB002288A 13-53 IPB002288B 66-91 IPB002288C 99-134 IPB002288D 192-205 IPB002288E 349-392 IPB002288F 410-449 IPB002288G 522-558 IPB002288H 584-631 IPB002288I 677-710***** IPB011557 (DNA gyrase, subunit B) with a combined E-value of 9.3e-170. IPB011557A 13-56 IPB011557B 99-134 IPB011557C 187-206 IPB011557D 350-392 IPB011557E 411-445 IPB011557F 463-508 IPB011557G 515-547 IPB011557H 584-633 IPB011557I 677-721***** IPB005737 (DNA topoisomerase IV, subunit B, Gram-negative) with a combined E-value of 8.5e-146. IPB005737A 33-85 IPB005737B 106-145 IPB005737C 189-232 IPB005737E 363-398 IPB005737F 407-461 IPB005737G 522-571 IPB005737H 586-631 IPB005737I 677-704***** IPB011558 (DNA topoisomerase, type IIA, subunit B, conserved region) with a combined E-value of 5.5e-112. IPB011558A 20-38 IPB011558B 42-61 IPB011558C 116-134 IPB011558D 193-205 IPB011558E 365-377 IPB011558F 506-541 IPB011558G 590-618 IPB011558H 678-701***** IPB000565 (DNA gyrase subunit B signature) with a combined E-value of 4.4e-36. IPB000565A 13-23 IPB000565B 210-225 IPB000565C 225-238 IPB000565F 411-427 IPB000565H 477-497 IPB000565I 573-582 IPB000565J 698-710 IPB000565K 717-733","Residues 2-233 are 57% similar to a (TOPOISOMERASE 5.99.1.- IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PD382459) which is seen in PARE_CAUCR.Residues 2-238 are 57% similar to a (TOPOISOMERASE B:DNA DNA II ATP-BINDING SUBUNIT GYRASE GYRB ISOMERASE) protein domain (PDA0U8U0) which is seen in Q82Y82_NITEU.Residues 3-238 are 58% similar to a (GYRASE DNA TOPOISOMERASE NUCLEOMORPH ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PD815511) which is seen in Q98RQ4_GUITH.Residues 5-234 are 56% similar to a (GYRASE SIMILAR DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8T8) which is seen in Q9SDC3_EEEEE.Residues 5-157 are 63% similar to a (GYRASE DNA BETA ATP-BINDING SUBUNIT TOPOISOMERASE ISOMERASE) protein domain (PDA19992) which is seen in Q8KY64_BBBBB.Residues 7-156 are 68% similar to a (TOPOISOMERASE IV DNA ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA19633) which is seen in Q83F84_COXBU.Residues 7-238 are 60% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8V1) which is seen in Q8EX47_MYCPE.Residues 8-238 are 62% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8W0) which is seen in Q6NKL3_CORDI.Residues 8-238 are 60% similar to a (TOPOISOMERASE 5.99.1.- DNA IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8T2) which is seen in Q8EQK5_OCEIH.Residues 9-156 are 68% similar to a (TOPOISOMERASE IV PREDICTED ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA19632) which is seen in Q9F7P0_PRB01.Residues 10-155 are 73% similar to a (TOPOISOMERASE 5.99.1.- IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA19989) which is seen in PARE_MYCGE.Residues 10-155 are 69% similar to a (TOPOISOMERASE 5.99.1.- IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA19991) which is seen in PARE_MYCPN.Residues 11-168 are 68% similar to a (GYRASE DNA SUBUNIT B ISOMERASE) protein domain (PDA1A187) which is seen in Q6ABQ6_PROAC.Residues 12-238 are 58% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8T0) which is seen in GYRB_HALSQ.Residues 12-238 are 58% similar to a (DNA TOPOISOMERASE ATP-BINDING SUBUNIT B GYRASE ISOMERASE) protein domain (PDA0U8U9) which is seen in Q74H89_GEOSL.Residues 12-237 are 58% similar to a (TOPOISOMERASE 5.99.1.- TOPIIB IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PD663017) which is seen in PARE_MYCGA.Residues 12-238 are 61% similar to a (TOPOISOMERASE 5.99.1.- IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8U3) which is seen in Q9CGW3_LACLA.Residues 12-237 are 58% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8U5) which is seen in Q7UU72_RHOBA.Residues 12-155 are 70% similar to a (TOPOISOMERASE 5.99.1.- ATP-BINDING SUBUNIT B IB ISOMERASE) protein domain (PDA19990) which is seen in Q6KHQ6_MYCMO.Residues 12-238 are 61% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PD695569) which is seen in Q8DL50_SYNEL.Residues 12-157 are 71% similar to a (TOPOISOMERASE GYRASE DNA II ATP-BINDING ISOMERASE) protein domain (PDA0U8T9) which is seen in Q7VH40_HELHP.Residues 12-238 are 56% similar to a (DNA TOPOISOMERASE ATP-BINDING SUBUNIT B GYRASE ISOMERASE) protein domain (PDA0U8U4) which is seen in Q72G57_DESVH.Residues 12-238 are 58% similar to a (DNA TOPOISOMERASE ATP-BINDING SUBUNIT B GYRASE ISOMERASE) protein domain (PDA0U8T7) which is seen in Q9RVW5_DEIRA.Residues 12-238 are 61% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8U2) which is seen in GYRB_BORBU.Residues 12-238 are 54% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PD815506) which is seen in Q9RH27_ZYMMO.Residues 12-238 are 61% similar to a (GYRASE DNA SUBUNIT B) protein domain (PDA1B3E4) which is seen in Q6AHN1_BBBBB.Residues 13-155 are 69% similar to a (GYRASE DNA ATP-BINDING SUBUNIT B TOPOISOMERASE ISOMERASE) protein domain (PDA184V6) which is seen in GYRB_MYCHO.Residues 13-238 are 59% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PD815508) which is seen in GYRB_BUCAI.Residues 13-237 are 57% similar to a (TOPOISOMERASE IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8T5) which is seen in Q9PQ24_UREPA.Residues 13-237 are 57% similar to a (TOPOISOMERASE IV DNA ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8U7) which is seen in Q8EAK3_SHEON.Residues 13-238 are 56% similar to a (GYRASE PROBABLE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8T1) which is seen in Q8XTV6_RALSO.Residues 13-238 are 62% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8U6) which is seen in Q9F6Z0_TREHY.Residues 13-238 are 58% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8T6) which is seen in Q899S8_CLOTE.Residues 13-238 are 57% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8T3) which is seen in GYRB_BUCAP.Residues 13-238 are 61% similar to a (GYRASE DNA TOPOISOMERASE ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PDA0U8U8) which is seen in GYRB_BACHD.Residues 13-157 are 71% similar to a (GYRASE DNA ATP-BINDING SUBUNIT B TOPOISOMERASE ISOMERASE) protein domain (PDA19988) which is seen in Q7MAV1_WOLSU.Residues 13-237 are 58% similar to a (TOPOISOMERASE DNA IV ATP-BINDING SUBUNIT B ISOMERASE) protein domain (PD815515) which is seen in Q8EVB8_MYCPE.Residues 13-305 are 55% similar to a (GYRASE B DNA TOPOISOMERASE ATP-BINDING SUBUNIT NOVOBIOCIN-SENSITIVE ISOMERASE) protein domain (PD727958) which is seen in Q8G6K5_BIFLO.Residues 13-156 are 71% similar to a (DNA TOPOISOMERASE ATP-BINDING SUBUNIT B GYRASE ISOMERASE) protein domain (PDA0U8U1) which is seen in Q73IP4_WOLPM.Residues 18-237 are 63% similar to a (DNA REPAIR MISMATCH TOPOISOMERASE MUTL ISOMERASE SUBUNIT ATP-BINDING B II) protein domain (PD000740) which is seen in GYRB_THEMA.Residues 87-149 are 77% similar to a (GYRASE DNA ATP-BINDING SUBUNIT B TOPOISOMERASE ISOMERASE) protein domain (PD815514) which is seen in Q83WB8_BBBBB.Residues 150-237 are 73% similar to a (SUBUNIT TOPOISOMERASE B ISOMERASE GYRASE DNA ATP-BINDING A IV II) protein domain (PDA135H2) which is seen in Q6AFE6_BBBBB.Residues 348-441 are 82% similar to a (TOPOISOMERASE ISOMERASE ATP-BINDING DNA SUBUNIT B GYRASE DNA-BINDING IV II) protein domain (PD001260) which is seen in Q6AFE6_BBBBB.Residues 445-521 are 75% similar to a (TOPOISOMERASE ISOMERASE ATP-BINDING SUBUNIT B DNA GYRASE IV GYRASE 5.99.1.-) protein domain (PD881119) which is seen in Q83WB8_BBBBB.Residues 528-640 are similar to a (TOPOISOMERASE ISOMERASE ATP-BINDING DNA SUBUNIT B GYRASE DNA-BINDING IV II) protein domain (PD149633) which is seen in O69998_STRCO.Residues 678-749 are 79% similar to a (TOPOISOMERASE ISOMERASE ATP-BINDING SUBUNIT B DNA GYRASE IV 5.99.1.- GYRASE) protein domain (PD706927) which is seen in Q6A8X3_PROAC.","","-43% similar to PDB:1KIJ Crystal structure of the 43K ATPase domain of Thermus thermophilus gyrase B in complex with novobiocin (E_value = 1.7E_46);-53% similar to PDB:1AJ6 NOVOBIOCIN-RESISTANT MUTANT (R136H) OF THE N-TERMINAL 24 KDA FRAGMENT OF DNA GYRASE B COMPLEXED WITH NOVOBIOCIN AT 2.3 ANGSTROMS RESOLUTION (E_value = 1.2E_34);-54% similar to PDB:1EI1 DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATING THE ATPASE CATALYTIC CENTER (E_value = 1.5E_34);-53% similar to PDB:1KZN Crystal Structure of E. coli 24kDa Domain in Complex with Clorobiocin (E_value = 2.9E_33);-47% similar to PDB:1S16 Crystal Structure of E. coli Topoisomerase IV ParE 43kDa subunit complexed with ADPNP (E_value = 3.1E_27);","Residues 38 to 203 (E_value = 1.3e-25) place ANA_0606 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.Residues 297 to 494 (E_value = 3.7e-28) place ANA_0606 in the DNA_gyraseB family which is described as DNA gyrase B.Residues 521 to 632 (E_value = 4.8e-06) place ANA_0606 in the Toprim family which is described as Toprim domain.Residues 668 to 737 (E_value = 2e-26) place ANA_0606 in the DNA_gyraseB_C family which is described as DNA gyrase B subunit, carboxyl terminus.","","gyrase subunit B","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0608","639178","640230","1053","5.02","-13.78","39051","ATGGCAACCGGTTACGGCATCCGCCGGGCGGGATCCTCACCCTGGCCCATCCTGCGCCCTGGGCCCCGCTCGTCTCTGTCACGGCAGCTGACCTGGCGGCCGCTGGGTCCGGAGGACAACCACGAGTTGGCCGCGCTCATCGCTCGGGCCGAGGATGTCGACAACCCTCCCTACCGCACCAGTGAGCAGGAGACGGCCGAGTACTTCCTCGACCCCACCTACTCCGGCGTCGCCGGGCGTGACACCGATGGCGTCATGCGCGCCTTCGGGCTGGTACGCCTCCGACCGGCCGGGGAGATATACGCCTCCATGACCGGCACCGTGGACCCGTCCGTACGCAACCGCGGCATCGGGCGCACCCTCCTGTACTGGCAGGCCGAGCGGGCCCGCCACCTCGTGGGGGCCGAACGGGCCGGCTCCGTGCCGGGCAAGGGCTCGGCCCAGGTCCCCGCCCACGTGGTCACCACTGTCATGGAGGATGACCAACGCATGCAGGACCACCTCAAGGACATGGGTTTCGAACCCATGCGCTGGTACCGGGAGGTACGCCGATTCCTCGGTGACGAGATCCCCGAGGTGGACCTGGACGGCTTCATCACCATCGACCCGTGGACCCCCGAGATCGACGACGACGTCCGGCGCGCCTACAACCAGGCCATGGCCGAGACCTGGGAGACGGAGAACGTCACCCCCGAGGACTGGACTGCCGGCAGCGCCTACTTCGCCCCGCAGTGGAGCTTCGTGGCCATGGACCGCTCCGGGGACCGGGCCCGCGTCGCCGGGTACCTGCGCTCGGGCCGCTACGAGCAGGACTGGCAGGCCCTGGGCTGGCGGGAGGGCTACACCGACGTGCTCGGGGTCCTCAGCGACTACCGCCACCGGCAGATCGGGCCCGCGCTGCTGGTGGCCGCCATGCGCGCCTACGCCGCCGACGGCATGGAGTACGCCGCCGCCGGCGTCGACACCGACAACCCCAGTGGCGCCGTGGACCTGTATGAGTCCCTGGGCTACGTGCCCACCCGCGGCACCATCCTCTACGCCCTCGACGTCTGA","MATGYGIRRAGSSPWPILRPGPRSSLSRQLTWRPLGPEDNHELAALIARAEDVDNPPYRTSEQETAEYFLDPTYSGVAGRDTDGVMRAFGLVRLRPAGEIYASMTGTVDPSVRNRGIGRTLLYWQAERARHLVGAERAGSVPGKGSAQVPAHVVTTVMEDDQRMQDHLKDMGFEPMRWYREVRRFLGDEIPEVDLDGFITIDPWTPEIDDDVRRAYNQAMAETWETENVTPEDWTAGSAYFAPQWSFVAMDRSGDRARVAGYLRSGRYEQDWQALGWREGYTDVLGVLSDYRHRQIGPALLVAAMRAYAADGMEYAAAGVDTDNPSGAVDLYESLGYVPTRGTILYALDV$","GCN5-related N-acetyltransferase","Cytoplasm","acetyltransferase, GNAT family family","GCN5-related N-acetyltransferase","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[251-338]T$	Acetyltransf_1
PS51186	$\"[30-196]T$ $\"[199-350]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[199-341]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 251 to 338 (E_value = 0.00012) place ANA_0608 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","GNAT family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0609","641818","640256","1563","5.09","-21.69","54480","CTGCGCCGAGGTGACCCGTGCCCCGGCGCCCTGGCCGCACCGCCGCCCCCGGGTGAGACCGTGGATGTACGTATCACGGCGGGCCGGGTCGTCGAGGTGGGACAGGGGCTGAATGCTCCCGGGACACGGGTCCTTGATGCCGAGGGCTCCTTCCTCATTCCCGGCCTGTGGGACGCTCACGCCCACCTGGACATGGAGGCGGCGCGCTCGGCACGCATCGACACGCTGGCCACCCGCAGCGCGGAGGAGGCCCTGGAGCTGGTGGCCCAGGCGCTGCGGGATCATCCGGCCGGTTCGCGGCCGGCCACGATACAGGGCTTCGGGCACCGCCTGTCCAACTGGCCCCGGGTGCCCACGGTGGCCGAGCTCGACGCCGTCACCGGGGAGGTTCCCACGCTGCTCATCTCCGGGGACGTGCACTCCGGGTGGCTGAACTCGGCGGCGCTGCGTGTCTTCGGCCTGCCGGGGGCCAGCGCCCAGGACCCGGGAGCACCGATGAAGGAGGACCCGTGGTTCGCCCTACTCGACCGCCTCGATGAGGTCCCGGGGACACGCGAGCTGCGGGAGTCCGGCTACCGACAGGTCCTGGCCGACATGCTGTCCCGGGGTGTCACCGGCGTGGTGGACATGAGCTGGTCGGAAGATCCCGATGACTGGCCGCGGCGCTTGCGGGCCATGGCGGACGAGGGCGTACTCCCCCAGGTGCTGCCCCGCATCCGCATCGGGGTCTACCGCGACAAGCTGGAACGGTGGATCGCCCGGGGCCTGCGCACCGGGACCGCGCTGGCAGGCTCACCCCGCCTGCCCGACGGTTCCCCGGTGCTGGTGCAGGGGCCGCTCAAGGTGATCGCAGACGGCTCGATGGGCTCGGGCAGCGCACACATGTGCGAGCCCTATCCCGCCGAGCTGGGCCTGGAGCACGCCTGCGGCGTGGTCAACATCGACCGGGCCGAGCTCACCAACCTCATGGCCCACGCCTCCCGGCAGGGTTATGAGATGGCCATCCACGCCATCGGGGACGCGGCGGTCGACGACGTCGCTGCGGCCTTCGCGCACTCGGGTGCCGCCGGGCGCCTGGAACACGCCCAGCTGCTGCCGGCAGACGCCCTCGCTGAGCCTGATGGGGCGCTCAGGCGCCTCGTGGGCTGCGGGATCGAGCTGTCGGTTCAGCCGGCCCACCTCATTGACGACTGGGCGGCCGTGGGGCGGGTGTGGCCGGGACTGGAGGGGCGCACCTACGCCTTCGCAGACATGGTGGCCGCCGGGGCCCTGCTTCAGCTGGGCTCGGATGCGCCGGTGGCGCCCCTGGACCCGTGGTTGGCCATGTCGGCGGCCGTGGGGCGCCGGACGCCGGACGGCTCGGTGTGGTCGCCGGATCAGCGCCTGACGGCCGAGGAGGCGCTGGCGGCCAGTGTCAACGGGGCCGGCTCGGTGGCGGTGGGTTCTCAGGCCGACCTGGTGCTCCTGGCCGAGGACCCCCTGCGCTTGGAGGCCGAGGAGCTGGCGGGCTCTCGCCCAGTGGCCACTGTGGTGGCCGGAGCCGTGGCCCACCTGCACGGGTGA","LRRGDPCPGALAAPPPPGETVDVRITAGRVVEVGQGLNAPGTRVLDAEGSFLIPGLWDAHAHLDMEAARSARIDTLATRSAEEALELVAQALRDHPAGSRPATIQGFGHRLSNWPRVPTVAELDAVTGEVPTLLISGDVHSGWLNSAALRVFGLPGASAQDPGAPMKEDPWFALLDRLDEVPGTRELRESGYRQVLADMLSRGVTGVVDMSWSEDPDDWPRRLRAMADEGVLPQVLPRIRIGVYRDKLERWIARGLRTGTALAGSPRLPDGSPVLVQGPLKVIADGSMGSGSAHMCEPYPAELGLEHACGVVNIDRAELTNLMAHASRQGYEMAIHAIGDAAVDDVAAAFAHSGAAGRLEHAQLLPADALAEPDGALRRLVGCGIELSVQPAHLIDDWAAVGRVWPGLEGRTYAFADMVAAGALLQLGSDAPVAPLDPWLAMSAAVGRRTPDGSVWSPDQRLTAEEALAASVNGAGSVAVGSQADLVLLAEDPLRLEAEELAGSRPVATVVAGAVAHLHG$","Amidohydrolase 3","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","Amidohydrolase 3","","Holm L., Sander C. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 1997. 28(1):72-82. PMID: 9144792","","","

InterPro
IPR013108
Domain

Amidohydrolase 3
PF07969	$\"[51-488]T$	Amidohydro_3

","BeTs to 9 clades of COG1574COG name: Predicted metal-dependent hydrolasesFunctional Class: RThe phylogenetic pattern of COG1574 is ---k-qv--bR----------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 426-517 are 58% similar to a (HYDROLASE METAL-DEPENDENT REGULATORY PLASMID EXOENZYMES AEPA LIPOPROTEIN PREDICTED ISOFORM WITH) protein domain (PD554207) which is seen in Q6A973_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 120 to 557 (E_value = 9.4e-30) place ANA_0609 in the Amidohydro_3 family which is described as Amidohydrolase family.","","hypothetical protein","","1","","","Wed Aug 1 17:29:27 2007","","Wed Aug 1 17:29:27 2007","","","Wed Aug 1 17:29:27 2007","Wed Aug 1 17:29:27 2007","Wed Aug 1 17:29:27 2007","","","Wed Aug 1 17:29:27 2007","","","Wed Aug 1 17:29:27 2007","Wed Aug 1 17:29:27 2007","Wed Aug 1 17:29:27 2007","","Wed Aug 1 17:29:27 2007","Wed Aug 1 17:29:27 2007","","","","","yes","","" "ANA_0610","644510","641967","2544","6.31","-7.07","90315","ATGCCGAAGTCTGCCACCACCAGGACTCCTCCCCCGACCGACGGGGAGATCGTCGATCTCGACCTGTCCACGGAGATGCGCACCAGCTTCCTGGAGTACGCCTACTCCGTCATCTACGCGCGTGCCCTACCTGACGCCCGAGACGGGCTCAAGCCGGTTCAGCGCCGCATCCTTTTCCAGATGGACCGGATGGGGCTGCGCCCGGATCGTCCACACGTGAAGTCCTCCCGGGTCGTGGGTGATGTCATGGGTCGGCTCCACCCTCACGGGGACACCGCGATCTACGAGGCGCTGGTGCGTCTGGCCCAGCCCTTCACGATGCGCCTGCCGCTCATCGACGGCCACGGCAACTTCGGCTCCCTGGATGACGGTCCGGCGGCCCCCCGCTACACCGAGGCGCGTCTGGCCGCCTCGGCCCTGGCACTGACGGCGGACCTGGATGAGGACACGGTCGACTTCTCCCCCAACTACGACTACACACTCACCGAGCCCGAGGTGCTGCCGGCGGCCTTCCCGAACTTGCTGGTCAACGGTGCAGCGGGTATCGCGGTGGGTATGGCCACGAACATGCCGCCGCACAACCTCGTGGAGGTGGTGGCCGCCGCTCGGCACCTGCTGACTCACCCGGAGGCGAGTCTGGAGGACCTCATGGCCTTCGTGCCGGGGCCGGACCTGCCCGCCGGTGGCATGATCGTAGGCCTGGACGGGATCCGGGAGGCCTACCGCACGGGGCGGGGCAAGTTCCTCACGCGGGCCACTGCTCACGTGGAGTCCGTCTCCCCGCGTCGCAAGGGCATCGTGGTCACCGAGCTGCCCTACATGGTGGGACCGGAGAAGGTCATCGCCCGCATCAAGGAGGCGGTGGGCTCCAAGAAGCTCCAGGGCATCACCGACGTCGCCGATCTCACCGACCGCAAGCACGGCACCCGCCTGGTCATCAGCGTCAAGAACGGCTACAACCCCGAGGCGGTCCTGGCCCAGCTCTACAAGCACACGCCGCTGGAGGACTCCTTCGGAATCAACAACGTCTCCCTCGTGGAGGGTCAGCCCCACACCCTGGGGCTGCGCGAGCTGCTGGAGGTGTTCGTGCGCCACCGCCTCACGGTGGTCACGCGGCGCACCCGGTTCCGTCTGGGCAAGCGTCGCGAGCGCGCCCACCTGGTGGACGGCCTGCTCATCGCCATCCTCGACATCGACGAGGTCATCGCCGTCATCCGCTCCTCCGACGACGCCGCCACGGCGCGCACCCGGCTCATGCAGGTCTTCGACCTCACCGAGCCGCAGGCCGGATACATCCTTGAGCTCCAGCTGCGCCGGCTCACGAAGTTCTCGGTGATCGAGCTGGAGAAGGAGCGCGACGAGCTGGCCCGCGAGATCGAGGCCCTCGAGGCGATCCTGGCCGACGACGTGCTGCTGCGGCGCGTGGTCTCCCGTGAACTGGCGGCCGTGGCCGAGCAGTTCGGCACCCCGCGGCGCACGGTGCTGCTGGAGGCCTCCGGTGAGCGCGTGACGTCGTCGGCCGCTGCAGAGACTGCGGACGACGCCTCCGCCTCAGGTCGGGGTGCGAAGCGGGCCGGTGGCGCCGCTCAGCCGATGACGCTCATGCCCAGCGCCTCCCCGGTGCCGCTGACCGTCCCCGACGACCCGTGCCGGGTGCTGCTGTCGGCCACCGGACTGGTGGCGCGCACGGCCGGCACCGAGCCGGTGGCCCGCACCGGTGGGCGCCAGCCCCACGACGCCCTGACCTCCCAGGTGGCCACCACGGCGCGTGGGCGCATCGGCGCGGTCACCGACACCGGGCGGCTGGTGCTGCTCGACGTCGTCTCCACCACGGAGGTGCCCCGCACCGAGGGGGCCCCGGGGCTGGCCGGTGCGACTCAGGTTCGCCAGCTGGTGGACATTGAGCCGGAGGAGAAGGTGGTGGGGCTGGTCCCGGTGGGGTCGGCCGACAACCCGCCCATCGTCCTGGCCACGGCTGAGGGCGTCATCAAGCGGGTCAAGCCCGGTGACGAGCCCAGGAACGCCGAGAGCTGGGAGGTCATCTCCCTGTCCGAGGGCGACCGGGTGGTCTTCGCCGGCACCGCGGCGGACACGGACTTCCTGGCACTGGTGACCTCCGACGCCCAGCTGCTGCGGTTCCAGGCCGCCAAGGTGCGTCCGCAGGGCCGGGGCGCCTGCGGCATGGCGGGGATCTCGCTTCATGAGGGCGCCCGGGTCATCGCCGGCGCGGCGGTTCCTGAGGAGCTCCTGGCCGAGGCCGTGGTGGTGACGGTGGCGGGCTCCGAGGGCTCGCTCCCGGGCACCGGCGGAGGCAGTGTCAAGGTCACCCCCTTGGATCGCTACCCGGCGAAGGGACGGGCCACGGGCGGGGTTCGCTCGCACCGGTTCCTGCGCGGCGAGGACGAGCTGGTGGTCGCCTGGGTGGGGGTGGCCCCGCCTAGGGCGCTGCGCGAGGGCGGCAAGCCGGTCGCGCTGCCGGAGCCCGATGAGCGGCGTGACGGCTCCGGCTCACCGCTACCGGCCCCCATCATCGGAATCGGCTGA","MPKSATTRTPPPTDGEIVDLDLSTEMRTSFLEYAYSVIYARALPDARDGLKPVQRRILFQMDRMGLRPDRPHVKSSRVVGDVMGRLHPHGDTAIYEALVRLAQPFTMRLPLIDGHGNFGSLDDGPAAPRYTEARLAASALALTADLDEDTVDFSPNYDYTLTEPEVLPAAFPNLLVNGAAGIAVGMATNMPPHNLVEVVAAARHLLTHPEASLEDLMAFVPGPDLPAGGMIVGLDGIREAYRTGRGKFLTRATAHVESVSPRRKGIVVTELPYMVGPEKVIARIKEAVGSKKLQGITDVADLTDRKHGTRLVISVKNGYNPEAVLAQLYKHTPLEDSFGINNVSLVEGQPHTLGLRELLEVFVRHRLTVVTRRTRFRLGKRRERAHLVDGLLIAILDIDEVIAVIRSSDDAATARTRLMQVFDLTEPQAGYILELQLRRLTKFSVIELEKERDELAREIEALEAILADDVLLRRVVSRELAAVAEQFGTPRRTVLLEASGERVTSSAAAETADDASASGRGAKRAGGAAQPMTLMPSASPVPLTVPDDPCRVLLSATGLVARTAGTEPVARTGGRQPHDALTSQVATTARGRIGAVTDTGRLVLLDVVSTTEVPRTEGAPGLAGATQVRQLVDIEPEEKVVGLVPVGSADNPPIVLATAEGVIKRVKPGDEPRNAESWEVISLSEGDRVVFAGTAADTDFLALVTSDAQLLRFQAAKVRPQGRGACGMAGISLHEGARVIAGAAVPEELLAEAVVVTVAGSEGSLPGTGGGSVKVTPLDRYPAKGRATGGVRSHRFLRGEDELVVAWVGVAPPRALREGGKPVALPEPDERRDGSGSPLPAPIIGIG$","DNA gyrase subunit A","Cytoplasm","DNA gyrase-like protein","DNA gyrase subunit A ","DNA topoisomerase (ATP-hydrolyzing)","","","","","

InterPro
IPR002205
Domain

DNA topoisomerase, type IIA, subunit A or C-terminal
PD000742	$\"[56-130]T$	Q8G4F2_BIFLO_Q8G4F2;
PF00521	$\"[41-488]T$	DNA_topoisoIV
SM00434	$\"[20-473]T$	TOP4c

InterPro
IPR006691
Repeat

DNA gyrase/topoisomerase IV, subunit A, C-terminal beta-pinwheel
PF03989	$\"[698-747]T$	DNA_gyraseA_C

InterPro
IPR013757
Domain

DNA topoisomerase, type IIA, subunit A, alpha-helical
G3DSA:1.10.268.10	$\"[378-467]T$	no description

InterPro
IPR013758
Domain

DNA topoisomerase, type IIA, subunit A or C-terminal, alpha-beta
G3DSA:3.90.199.10	$\"[39-304]T$	no description

noIPR
unintegrated

unintegrated
PTHR10169	$\"[48-206]T$	DNA TOPOISOMERASE/GYRASE
PTHR10169:SF2	$\"[48-206]T$	DNA TOPOISOMERASE II

","BeTs to 22 clades of COG0188COG name: DNA gyrase (topoisomerase II) A subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0188 is ao-p--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB002205 (DNA gyrase/topoisomerase IV, subunit A) with a combined E-value of 6.6e-71. IPB002205A 41-59 IPB002205B 74-109 IPB002205C 121-135 IPB002205D 177-198 IPB002205E 220-229 IPB002205F 239-248***** IPB012542 (DTHCT) with a combined E-value of 1.7e-09. IPB012542C 143-197 IPB012542F 425-463","Residues 17-55 are 92% similar to a (SUBUNIT A DNA ISOMERASE TOPOISOMERASE GYRASE IV DNA-BINDING 5.99.1.- GYRASE) protein domain (PD699864) which is seen in Q6A8X0_PROAC.Residues 56-130 are similar to a (TOPOISOMERASE SUBUNIT DNA ISOMERASE A GYRASE DNA-BINDING IV ATP-BINDING II) protein domain (PD000742) which is seen in Q8G4F2_BIFLO.Residues 151-229 are similar to a (TOPOISOMERASE SUBUNIT DNA ISOMERASE A GYRASE DNA-BINDING IV ATP-BINDING II) protein domain (PD491907) which is seen in Q6AFE5_BBBBB.Residues 231-288 are 82% similar to a (SUBUNIT A DNA ISOMERASE TOPOISOMERASE GYRASE IV DNA-BINDING 5.99.1.- GYRASE) protein domain (PD874064) which is seen in Q6A8X0_PROAC.Residues 296-360 are 86% similar to a (SUBUNIT A DNA ISOMERASE TOPOISOMERASE GYRASE IV DNA-BINDING 5.99.1.- GYRASE) protein domain (PD701689) which is seen in Q82KI0_STRAW.Residues 386-496 are 80% similar to a (SUBUNIT A DNA ISOMERASE GYRASE TOPOISOMERASE IV DNA-BINDING 5.99.1.- GYRASE) protein domain (PD488062) which is seen in Q6A8X0_PROAC.Residues 541-679 are 60% similar to a (DNA SUBUNIT GYRASE A ISOMERASE GYRASE-LIKE A-LIKE TOPOISOMERASE IV) protein domain (PD491828) which is seen in O50510_STRCO.Residues 676-731 are 59% similar to a (GYRASE A DNA SUBUNIT ISOMERASE) protein domain (PDA0Z6W6) which is seen in Q6A8X0_PROAC.Residues 680-740 are 68% similar to a (SUBUNIT A DNA GYRASE ISOMERASE TOPOISOMERASE DNA-BINDING IV GYRASE 5.99.1.-) protein domain (PD254467) which is seen in Q6AFE5_BBBBB.Residues 701-740 are 82% similar to a (DNA SUBUNIT A GYRASE ISOMERASE TOPOISOMERASE DNA-BINDING GYRASE GYRA IV) protein domain (PD102302) which is seen in Q82KI0_STRAW.Residues 774-843 are 75% similar to a (A DNA SUBUNIT GYRASE ISOMERASE GYRASE-LIKE TOPOISOMERASE IV) protein domain (PD102336) which is seen in Q8G4F2_BIFLO.","","-57% similar to PDB:2NOV Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target (E_value = 1.6E_88);-53% similar to PDB:1AB4 59KDA FRAGMENT OF GYRASE A FROM E. COLI (E_value = 1.1E_86);-46% similar to PDB:1ZVU Structure of the full-length E. coli ParC subunit (E_value = 6.3E_77);-47% similar to PDB:1BGW TOPOISOMERASE RESIDUES 410-1202, (E_value = 6.0E_11);-47% similar to PDB:1BJT TOPOISOMERASE II RESIDUES 409-1201 (E_value = 6.0E_11);","Residues 41 to 488 (E_value = 1.4e-257) place ANA_0610 in the DNA_topoisoIV family which is described as DNA gyrase/topoisomerase IV, subunit A.Residues 698 to 747 (E_value = 4e-07) place ANA_0610 in the DNA_gyraseA_C family which is described as DNA gyrase C-terminal domain, beta-propeller.","","gyrase-like protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0611","644509","645282","774","5.00","-12.38","26792","ATGGGCGCATTCTCCGAGGAATCGGGCCGAAAACAAACCACGACACCCGGGCGTGACAGGTCAGACGCACCCACTCGGCACGATCGGCCCTCCTCAAGCAAGCGGATACCGGTGCTCGACGGCGAAGGGGCGGACGATGGCACAATGGCGACCATGACGACCCACTCAGGCCGCAGCTCGGCTGCAGGCCCCGCCTCGCACGAGGCGTCCCAGGAGGCCTTCGCAGACCTGGTGCAGCAGGTGGAGCTCGCCGGCTACTACCCCGAGCTGGTGCTCGACACCCTCCGCCTGGCCACGGGCGAGGAGGAGATCCTCTCCGGCATGGTCCAAGCCGAGACCACCTTCGCCGAGGCGGTCCACCGCCACCTGACCGTCCTGGCCCTGACCCCCAGCCGTCTCATCATCGTCCACGTTGACGACACCCCTCGCGACGACGGCAGCCCCGGCGCCCTGGCCACCAGCGAGGCCGTGCCGCTCAGCCGTATCCGCTCCATGGCCCTGACCCGCGGCGTGACCGACCCCGCCCAGGGCGGAGGAACCCTCACCGAGATGACGATCGCGGTCTCCTGGGGCTCGGTGCGCCGTATCGACATGGAGCCGGCCACCTGCGGCGACCCCGACTGCCAGGCCGACCACGGCATGACCGGTGTGTCTGTGCCCGACGACGTCGTCATCCGCGTGGCCGCGGGCGTGGAGGGCGCCGCCGCCCTGGCCCGTGCCGAGACCTTCGCCGGCCGGCTCTCACAGATGGCGGCCCGCGCCGCCGCCCTGTGA","MGAFSEESGRKQTTTPGRDRSDAPTRHDRPSSSKRIPVLDGEGADDGTMATMTTHSGRSSAAGPASHEASQEAFADLVQQVELAGYYPELVLDTLRLATGEEEILSGMVQAETTFAEAVHRHLTVLALTPSRLIIVHVDDTPRDDGSPGALATSEAVPLSRIRSMALTRGVTDPAQGGGTLTEMTIAVSWGSVRRIDMEPATCGDPDCQADHGMTGVSVPDDVVIRVAAGVEGAAALARAETFAGRLSQMAARAAAL$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 81-255 are 63% similar to a (SCO5843) protein domain (PD106212) which is seen in O50517_STRCO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0612","645294","646649","1356","5.58","-11.87","47009","ATGGGGCCCCTGACCGCCGGCGGACAGCCCGCACCGGCTCCCGCCCCGGACTCCCCACAGGATCCGGCGCTCCGCTACGTCCTGGCGGTCGGCGCCGTCAGTGCCGGACTGAGCCTGGCTGACACCAAGCACGACGGCGATACCGACCGTGATGCCGACCGAGATGCCGTCCTCAGCCCCACCGGCGATCCCGCTGAACCAGTCGTCTCCGACGCCCGTGCCCGGGCGGTCGCCCGCAGCTGGGGCATCGAGCCGGCTGGTGAGCCGGGGGAGGCCGGTGGCGGCCCGGGAACCGTCGTCGTCCTCGTGGACGGTCTGGGTCTGGAGATGCTCCGTCAGCGTCGCGGGCATACCCCCACCCTGCGCCAGTGGCTGGTACAGCGCGAGGCCGCCACTGCCGCCGCCGGTGCGGGAATCCTCACCTGCCGGCCCTCGACGACGGCTGCGGCCCTGACCATGCTGGGCACCTCCGCACTGCCCGGCACCACCGGCATGGTCGGCTACTCGGTGCTCAACCCCCGCCTGGGGCCCTCTCTCGACGCCTCCGTCCTCCCCGGTCCCGACCAGGTCCTCAGCCTCATCACCTGGAAGGGGGACAACGTCCCCAGCCCCGCCTCCTGGCAGGACGTGCCCACGATCTTCGAGCGGCTCCCGGCCGGGAGCGCGGTGAGCATCGGACCGAGCCGGTTTGCCGGCTCCGGTCTGACCGAGGCCGCCCTACGAGGCGCTTCGCACCTGGGGGCCGACCGGCTGGAGGACCGGCCCGGCCTGGCTGCCGGAGCCCTGCGCCGCGGCACCCCGCTGGTCTACCTCTACGTCGGCGAGCTGGACAAGACCGGTCACAAGCACGGGTGGCTCAGTGAGCAGTGGCTGACCCAGCTCGAGCGCCTCGACGCCGCCATGGCCGAGCTGGCCCGCCGTGTTCCCGCCGGAACCAGGATTCTCCTCAGCGCCGACCACGGCATGGTCGATACCGATCCCGATCACCGTGTCGACTTGAGCGCCCACCGAGATCTCGTTCGCGACGTCGTCGCCGTGGCCGGTGAGCCCAGGCTGACGCACCTGCACGTGGCCGACGGCGACGTGGACCTGGCCGCCGAGGTGGCCCAGCGCTACCGCCGCGTCCTGGGGGATCGGGCGATGTGGATCGGGACCAGGGAGCAGGCCGGCGAGCACCTCGGACCCCTCGGAGTGCGAGCACGAGGGGTTGTCGGGGACGTCGTCGTGGCCATGGCCGAGAACTGGGTCCTCGTGGACCCCCGGGTCCACTCCGAGTCCGCCATCGCCATGCCCGGCGTCCACGGCTCCTTCACCCCGGCCGAGACCGAGGTGCCGCTGCTCATCACCGAGGCCTGA","MGPLTAGGQPAPAPAPDSPQDPALRYVLAVGAVSAGLSLADTKHDGDTDRDADRDAVLSPTGDPAEPVVSDARARAVARSWGIEPAGEPGEAGGGPGTVVVLVDGLGLEMLRQRRGHTPTLRQWLVQREAATAAAGAGILTCRPSTTAAALTMLGTSALPGTTGMVGYSVLNPRLGPSLDASVLPGPDQVLSLITWKGDNVPSPASWQDVPTIFERLPAGSAVSIGPSRFAGSGLTEAALRGASHLGADRLEDRPGLAAGALRRGTPLVYLYVGELDKTGHKHGWLSEQWLTQLERLDAAMAELARRVPAGTRILLSADHGMVDTDPDHRVDLSAHRDLVRDVVAVAGEPRLTHLHVADGDVDLAAEVAQRYRRVLGDRAMWIGTREQAGEHLGPLGVRARGVVGDVVVAMAENWVLVDPRVHSESAIAMPGVHGSFTPAETEVPLLITEA$","Type I phosphodiesterase/nucleotide pyrophosphatase","Cytoplasm","Type I phosphodiesterase / nucleotidepyrophosphatase family","type I phosphodiesterase/nucleotide pyrophosphatase","type I phosphodiesterase/nucleotide pyrophosphatase","","Trowsdale J., Martin D., Bicknell D., Campbell I. Alkaline phosphatases. Biochem. Soc. Trans. 1990. 18(2):178-180. PMID: 2379681Mansouri K., Piepersberg W. Genetics of streptomycin production in Streptomyces griseus: nucleotide sequence of five genes, strFGHIK, including a phosphatase gene. Mol. Gen. Genet. 1991. 228(3):459-469. PMID: 1654502Manes T., Glade K., Ziomek C.A., Millan J.L. Genomic structure and comparison of mouse tissue-specific alkaline phosphatase genes. Genomics 1990. 8(3):541-554. PMID: 2286375Hulett F.M., Kim E.E., Bookstein C., Kapp N.V., Edwards C.W., Wyckoff H.W. Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure. J. Biol. Chem. 1991. 266(2):1077-1084. PMID: 1898729","","","

InterPro
IPR001952
Family

Alkaline phosphatase
G3DSA:3.40.720.10	$\"[98-329]T$	no description

InterPro
IPR002591
Family

Type I phosphodiesterase/nucleotide pyrophosphatase
PF01663	$\"[96-437]T$	Phosphodiest

noIPR
unintegrated

unintegrated
PTHR10151	$\"[268-349]T$	ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE

","BeTs to 7 clades of COG1524COG name: Uncharacterized proteins of the AP superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1524 is a--pk-y-v---b--f--s-uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 144-234 are 56% similar to a (PHOSPHODIESTERASE TYPE SCO5844 PYROPHOSPHATASE HYPOTETHICAL / I NUCLEOTIDE) protein domain (PD138822) which is seen in Q73VT6_MYCPA.Residues 235-339 are 59% similar to a (PHOSPHODIESTERASE TYPE SCO5844 I NUCLEOTIDE PYROPHOSPHATASE HYPOTETHICAL / ML1572) protein domain (PDA0R005) which is seen in Q8G4F1_BIFLO.Residues 343-447 are 54% similar to a (PHOSPHODIESTERASE TYPE SCO5844 PYROPHOSPHATASE HYPOTETHICAL / I NUCLEOTIDE) protein domain (PD395794) which is seen in Q6A8W7_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 96 to 437 (E_value = 1.3e-21) place ANA_0612 in the Phosphodiest family which is described as Type I phosphodiesterase / nucleotide pyrophosphatase.","","I phosphodiesterase - nucleotide pyrophosphatase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0613","648118","646658","1461","5.01","-18.51","51082","ATGGTCGAACTCGAGCTGCTGGGTGCCAACGGTGACACGATTGTCATGACCGACGAGGACGGCGAGCGTTACAGCATCGTCGTCGACGACGCCCTCAGGGCCGCGGTACGCCGTGACCGCGGAGCGATCCTGCCCCCGTCGGGGACGGTCGCCGAGGCGCCGGCGCCCCTGCGCCCCCGGCAGCTCCAGGCCTACATGCGCGCCGGTGCGACCGCCGCCGAGGTCGCCATCAGCACGGGCATGGACGTGGAGCACGTGCGCCGTTTCGAGGGGCCGGTGCTCGCCGAGCGCCAGTGGGCCGTCTCGCAGGCCCAGTCCTGCCGGATCGGCTGGGAGAAGGACTCCCCCCTGCTCGGCGAGCTGGTGGTGGACCGCCTGGCCACACGCGGCGTCGATCCTTCCAGCCTCGAGTGGGACGCGCTGCGCGAGGGCCGCGACCCCTGGCTCATCATGGTGACCTTCGTGCAGTCCGCCGAGGAGAAGCAGGCGCGCTGGTCACTGGACCTGACCGCCCGCGCGGTTCACGCCCTGGACGATGAGGCTCGCTGGCTCACCGAGGCCGGAGCCGGATCCAAGCGCCCTGCCGTCTTCGACCAGGACTCCAAGGCCCCCGGGGCCTCAGCCTCTGCGCCGTCGGCCCAGTCGGGGCACTCCCCCGCGGCCGCGGGCTCAGCGGCCGGCAGTGCGGTCTCGGCGGCCTCCGCCCCGGCTGCGGCCTCCGGCGAGTCCACCGGGCTGGCCGTCGAGATGCCCGCCGGGATGCTGCCGGTTCGGGAGTACGGTCGCCCCACCAGTGGCGCCATGTCGGCCGATGACACCGACGCGCTGCTGGCCGACCTGGCCTCCAGCCGGGGCCGGCGCGTCGACGTGGAGATGCCCCAGGACGACGACCTGAGCGGCTTCGCCGGTGAGGGTAACGCGGATGAGGACGCCTTCACCGATCCCCACGGCATCGACTACACCAGCAGCCCTGAGAGCCCCGAGGTCCCCTCACCCCCGGCCCGGGGCATGGAGGAGCGCCGCACCGAGGCCGGTTCCAGGGCCGACGATGAGTCCTTGGAGCAGACCGCGGGCCTGAATGCGCAGGTCTACTCGATGTCGGAGCGCAGACGTCTGCACACCGGCAACCACCCGGCCGGAACCCGGCTGGTGACGGCCTCCAGCGCCCCCTCGGCGGCGCCGTCTGCCCCGAGCCCAGCGGTGGAGCGCATCCCCGTGGGACGTCGGGCACCGCTGGGGGCGGACAGCCCCACCGAACCGGTGCCGGAGATCCCCATGCCCTCGCGCTCCGAGGTCCTGGCCAAGGCCTCCCCCGGCCCGTCTGCCGCCTCGGCGGCGGGTACGCAGGAGCCCCTGCCCGACATGCCCAGGACGCCTCCGGCCAAGAAGAAGTCCCGCCGTCGCTCGCGGCGCTCCGTGCCCTCTTGGGACGAGATCGTCTTCGGTGCCAGGCCCGAGTAG","MVELELLGANGDTIVMTDEDGERYSIVVDDALRAAVRRDRGAILPPSGTVAEAPAPLRPRQLQAYMRAGATAAEVAISTGMDVEHVRRFEGPVLAERQWAVSQAQSCRIGWEKDSPLLGELVVDRLATRGVDPSSLEWDALREGRDPWLIMVTFVQSAEEKQARWSLDLTARAVHALDDEARWLTEAGAGSKRPAVFDQDSKAPGASASAPSAQSGHSPAAAGSAAGSAVSAASAPAAASGESTGLAVEMPAGMLPVREYGRPTSGAMSADDTDALLADLASSRGRRVDVEMPQDDDLSGFAGEGNADEDAFTDPHGIDYTSSPESPEVPSPPARGMEERRTEAGSRADDESLEQTAGLNAQVYSMSERRRLHTGNHPAGTRLVTASSAPSAAPSAPSPAVERIPVGRRAPLGADSPTEPVPEIPMPSRSEVLAKASPGPSAASAAGTQEPLPDMPRTPPAKKKSRRRSRRSVPSWDEIVFGARPE$","DNA-binding protein","Periplasm, Cytoplasm, Extracellular","hypothetical protein","DNA-binding protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 52-184 are 60% similar to a (DNA-BINDING RV0883C/MT0906/MB0907C MLCB57.36C CGL0827 ML2137) protein domain (PD023795) which is seen in Q82KJ2_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0617","648457","648762","306","4.10","-20.43","11056","ATGGCGACCGACTACGACGCCCCGCGCAAGAATGATGACGAGCCCGAGGCCGATTCCATCGAAGAGCTGACCTCGCGGCAGAAGGACCAGTCGTCCGCCGCGATCGAGGAGGACGAGAACGAGGCCGCCGAGGGCTTTGAGCTTCCCGGGGCGGACCTGTCCCGTGAGGAGCTGAGCGTTCATGTCGTTCCGCAGCTCGAGGACGAGTTCACCTGCTCGGAGTGCTTCCTCGTCCATCACCGCAGCCAGCTGGCCTTCGTCGACGAGGCGACCGGTCTTCCGGTGTGCGCCGACTGCGCCGGCTGA","MATDYDAPRKNDDEPEADSIEELTSRQKDQSSAAIEEDENEAAEGFELPGADLSREELSVHVVPQLEDEFTCSECFLVHHRSQLAFVDEATGLPVCADCAG$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-99 are 79% similar to a (U1764J CGL1908 MB2718C ML1026 SCO5864 PLASMID) protein domain (PD020208) which is seen in Q82KK0_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0618","648790","649494","705","4.52","-21.03","24691","ATGGGACTGTTCTCGCGCCGTCGTGACGACGCAACCACCGATTCTGACGAGTCCATTCTCGGACGCGACCCCGGCGACGACGACCTCGACGAGGCCGCCCCCGGCCCCTGGGACCTCAGTGAGCTGCCCGAGGACCAGGAGGAGGTGCCCCGTATCGACCTGGGGGCGCTGCAGGTCCCGGCCGTTGACGGGATGCAGCTGCGTCTGGAGCAGGCGCCCGACGGCACCGTCACCGCCGTCGTCCTGGCGCTGGGCGGCTCGGCGCTCGAGCTGCGAGCCTTCGCCGCACCGCGCACCGCGGGCATCTGGGACGAGCTGCGCGGCGACATCGCCAACGAGCTCGCCGGGAACGGCGCCCGCTACGAGGAGAGCGACGGGGAGCACGGCACCGAGCTGATCGCGCACCTGCCCATGCGCGGTCCCGACGGCACGATGGCGACCGGCACGATCCGGTTCCTGGGGATCGACGGCCCCCGCTGGTTCCTGCGCGGCGTCCTTCAGGGGCCCGCCGCCTCCTCCGAGCACTCCGCCCAGGCGCTGCGGGAGGTGCTGCGCGGAATCGTCGTCGTGCGCGACGGCCAGGCCCGTCCGCCCCGTGAGATCCTGCCCCTGCATGCGCCCGGAGCCGCAGCCGGCCCTGAGGCCGAGGACCTGCCAGGCATCGACCCGCTGGCACCCGGCCCGACTATCGCCGAAGTGCGTTAA","MGLFSRRRDDATTDSDESILGRDPGDDDLDEAAPGPWDLSELPEDQEEVPRIDLGALQVPAVDGMQLRLEQAPDGTVTAVVLALGGSALELRAFAAPRTAGIWDELRGDIANELAGNGARYEESDGEHGTELIAHLPMRGPDGTMATGTIRFLGIDGPRWFLRGVLQGPAASSEHSAQALREVLRGIVVVRDGQARPPREILPLHAPGAAAGPEAEDLPGIDPLAPGPTIAEVR$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 65-204 are 60% similar to a (ALANINE GLYCINE VALINE RICH ML1029 U1764K SCO5869 CGL1904) protein domain (PD023743) which is seen in Q6AFD9_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0619","649516","649872","357","9.86","5.87","13142","GTGAAGCGGCTCTACGAATCACTGCGCACCAGCCGCGAGCACTTGGAGGCCGAGGATGAGGAGCGCTCCGCCAGCCGACGGGGCACCGATCCGATCGGCTCACTGACCTCGCGCCAGCGGACCTGCGTCTCCGGTGTGCTTCAGGCGGTCACCTACCGCTCGAGCCAGGACAAGCCCATCCTCGTCGGGCAGCTCTATGACGGTACTGGCAGCATCGACCTGGTGTGGTGGGGTCGGCGACGCATCCCCGGCATCAAGCCGGGGGCCCACCTCCTCGCTGAGGGGCGGGTCGCCGACGGCACCCACCGCCAGCAGATCCACAACCCCGCCTATCGCCTGCTGGGGCCGGGGCAGTAG","VKRLYESLRTSREHLEAEDEERSASRRGTDPIGSLTSRQRTCVSGVLQAVTYRSSQDKPILVGQLYDGTGSIDLVWWGRRRIPGIKPGAHLLAEGRVADGTHRQQIHNPAYRLLGPGQ$","RecG-like helicase","Cytoplasm, Extracellular","OB-fold nucleic acid binding domain protein","hypothetical protein","nucleic acid binding, OB-fold, tRNA/helicase-type","","Koonin E.V., Wolf Y.I., Aravind L. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 2000. 54:245-275. PMID: 10829230Keshav K.F., Chen C., Dutta A. Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. Mol. Cell. Biol. 1995. 15(6):3119-3128. PMID: 7760808Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 1997. 385(6612):176-181. PMID: 8990123","","","

InterPro
IPR004365
Domain

Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336	$\"[41-114]T$	tRNA_anti

","BeTs to 3 clades of COG1200COG name: RecG-like helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1200 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 2-113 are similar to a (MB2713C SCO5873) protein domain (PD031537) which is seen in O54139_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 41 to 114 (E_value = 7.7e-07) place ANA_0619 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.","","nucleic acid binding domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0620","649906","650682","777","9.40","4.61","27669","ATGAGCAGCCGTTCCACTGGAACCACCCGTACGGGCCTGGGGGCCATCGACTCCGAGCGCTTCGACGCCATGGCCGCCGTGGGCGGGTGGCGCGGCATCCTCGAGTCAGTGGTGCCCACCCTCATGTTCGTCCTGGTCATGGCGGTGCGGCCCGTCGCACTGGTGGCCGCTCTGCTCGCCTCCCTGGCCATCAGCGCCATCTGCTTCGTGGCCCGCCTGGTACAGCGCCAGTCCCCGGCTCAGGTCGTCGGTGGGATTGCGCTGGTCCTGGTCTCGGCCCTGTGGGCCTGGCGCAGCGGCGACGCCTCCAACTTCTACGCCACCGGCCTCATGATTAACGCGGCCTGGCTGGTCGCCTGCCTGGTCTCCCTGCTCATCGGGTGGCCGATCGTGGGCGCCCTCATGACTCTGTGGCATCGCGTCACCGACGAGTCGGAGCGTCGTGAGGGTGGTGGTGCGAGTAAGGACCCGGAAGGCACCCAGGCGCCGCAGGCCGACGACGACCCCGCTGCACTGCCCTCGGCCTGGCGCACCGAGCCGGCCCTGCGCCATGTTCGGCGCCGCTACCACGCGGGCACCTGGGTCCTGACGCTCATGTTCGCCCTGCGGCTCGTCGTCGAGGTGCCCCTCTACCTGGCCGGAGCCCAGGCCGTGTCCTACCTCGGAGCGGCCCGCCTCATCCTGGGCGTGCCGCTGTACGCCGTGACCCTGTGGTTCATCTGGCTGCTCGTGGCCCCCAGCCGGATCGCCCAGGCCCAGGCTCCCGTCGAGCGGTAG","MSSRSTGTTRTGLGAIDSERFDAMAAVGGWRGILESVVPTLMFVLVMAVRPVALVAALLASLAISAICFVARLVQRQSPAQVVGGIALVLVSALWAWRSGDASNFYATGLMINAAWLVACLVSLLIGWPIVGALMTLWHRVTDESERREGGGASKDPEGTQAPQADDDPAALPSAWRTEPALRHVRRRYHAGTWVLTLMFALRLVVEVPLYLAGAQAVSYLGAARLILGVPLYAVTLWFIWLLVAPSRIAQAQAPVER$","Integral membrane protein","Membrane, Cytoplasm","narrowly conserved hypothetical transmembraneprotein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-54]?$	signal-peptide
tmhmm	$\"[27-47]?$ $\"[53-73]?$ $\"[78-98]?$ $\"[104-138]?$ $\"[193-213]?$ $\"[223-245]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 28-244 are 50% similar to a (MEMBRANE INTEGRAL ALANINE PROBABLE LEUCINE RICH TRANSMEMBRANE NARROWLY) protein domain (PD111007) which is seen in Q8G4I9_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","conserved hypothetical transmembrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0621","651357","650695","663","4.61","-18.62","23961","ATGCAGATCGTCATCGCCGGAGCCGGATCCGTGGGCCGTTCCATCGCCCGCGAGCTCATCAGCCACGGCCACGAGGTCACCCTCGTCGACCGTTCCACCGAGGCCATGCGCATCGCCTCGGTCCCGCAGGCCGACTGGCAGCTGGCCGACGCCTGCGACATCGACGCCCTGGAGCGCGCCGGGGCTGAGACCTGCGACGTTATCGTGGCCGCCACCGGGGATGACAAGGCCAACCTGGTGATCTCCCTGCTGGCCAAGACCGAGTACGGGGTGCCGCGCACGGTCGCGCGCGTCAACAACCCCAAGAGCGAGTGGCTCTTCGATGAGACCTGGGGCGTGGACGTGGCCGTGTCCACCCCGCGCTTCATGACGGCCCTGGTGGAGGAGGCCGTCAGTGTCGGCAGCCTGGTGAGCATCTTCCACTTCCACCAGTCGGGCGCCTCCATGCACGAGCTGACCCTGCCGGAGGACTCACCGGTCATTGGCGAGCTCGTCACCGACATCGAGCTGCCGCCACACACGGTGCTGGCCGCGATCCTGCGCGACTACCGCCCCATCACACCGGACCGCGACGAGCGCTTCGAGCGCGGCGACGAGCTCATCTTCCTCACGGCGCGGGAGGGAGAGTCCAGCTTGGAGGAGCTGCCCCTCATCTTCACGTAA","MQIVIAGAGSVGRSIARELISHGHEVTLVDRSTEAMRIASVPQADWQLADACDIDALERAGAETCDVIVAATGDDKANLVISLLAKTEYGVPRTVARVNNPKSEWLFDETWGVDVAVSTPRFMTALVEEAVSVGSLVSIFHFHQSGASMHELTLPEDSPVIGELVTDIELPPHTVLAAILRDYRPITPDRDERFERGDELIFLTAREGESSLEELPLIFT$","Trk system potassium uptake protein TrkA, NAD-binding component","Cytoplasm","TRK SYSTEM POTASSIUM UPTAKE PROTEIN CEOC","K03499 trk system potassium uptake protein TrkA","TrkA-N domain protein","","Schlosser A., Hamann A., Bossemeyer D., Schneider E., Bakker E.P. NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport. Mol. Microbiol. 1993. 9(3):533-543. PMID: 8412700Parra-Lopez C., Lin R., Aspedon A., Groisman E.A. A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium. EMBO J. 1994. 13(17):3964-3972. PMID: 8076592Munro A.W., Ritchie G.Y., Lamb A.J., Douglas R.M., Booth I.R. The cloning and DNA sequence of the gene for the glutathione-regulated potassium-efflux system KefC of Escherichia coli. Mol. Microbiol. 1991. 5(3):607-616. PMID: 2046548","","","

InterPro
IPR003148
Domain

TrkA-N
PF02254	$\"[3-119]T$	TrkA_N
PS51201	$\"[2-124]T$	RCK_N

InterPro
IPR006036
Family

TrkA potassium uptake protein
PR00335	$\"[2-16]T$ $\"[19-33]T$ $\"[59-69]T$ $\"[72-86]T$	KUPTAKETRKA

InterPro
IPR006037
Domain

TrkA-C
PF02080	$\"[149-217]T$	TrkA_C
PS51202	$\"[137-218]T$	RCK_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[1-137]T$	no description
PTHR10366	$\"[7-69]T$	NAD DEPENDENT EPIMERASE/DEHYDRATASE

","BeTs to 18 clades of COG0569COG name: K+ transport systems, NAD-binding componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0569 is aom-kz-qvdrlbcefgh-nu---twNumber of proteins in this genome belonging to this COG is 3","***** IPB006036 (TrkA potassium uptake protein signature) with a combined E-value of 5e-22. IPB006036A 2-16 IPB006036B 19-33 IPB006036C 48-58 IPB006036D 59-69 IPB006036E 72-86***** IPB003148 (TrkA-N) with a combined E-value of 1.4e-08. IPB003148 57-78","Residues 43-154 are similar to a (TRKB SYSTEM UPTAKE POTASSIUM) protein domain (PDA146Q9) which is seen in Q8DT34_STRMU.Residues 49-123 are similar to a (POTASSIUM UPTAKE SYSTEM TRKA TRANSMEMBRANE CHANNEL TRK POTASSIUM-EFFLUX GLUTATHIONE-REGULATED IONIC) protein domain (PD288767) which is seen in O54141_STRCO.Residues 147-215 are similar to a (POTASSIUM UPTAKE TRKA SYSTEM TRANSMEMBRANE TRK CHANNEL HOMOLOG IONIC MEMBRANE) protein domain (PD013953) which is seen in O54141_STRCO.","","-57% similar to PDB:1LSS KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+ (E_value = 3.7E_15);-53% similar to PDB:2G1U Crystal structure of (tm1088a) from THERMOTOGA MARITIMA at 1.50 A resolution (E_value = 3.3E_11);","Residues 2 to 31 (E_value = 5.8e-07) place ANA_0621 in the DAO family which is described as FAD dependent oxidoreductase.Residues 2 to 34 (E_value = 1.3e-05) place ANA_0621 in the F420_oxidored family which is described as NADP oxidoreductase coenzyme F420-dependent.Residues 3 to 119 (E_value = 4.3e-35) place ANA_0621 in the TrkA_N family which is described as TrkA-N domain.Residues 3 to 32 (E_value = 6e-07) place ANA_0621 in the ApbA family which is described as Ketopantoate reductase PanE/ApbA.Residues 3 to 60 (E_value = 0.00057) place ANA_0621 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 3 to 60 (E_value = 2.6e-05) place ANA_0621 in the Saccharop_dh family which is described as Saccharopine dehydrogenase.Residues 5 to 35 (E_value = 6e-06) place ANA_0621 in the PDH family which is described as Prephenate dehydrogenase.Residues 149 to 217 (E_value = 9.4e-09) place ANA_0621 in the TrkA_C family which is described as TrkA-C domain.","","SYSTEM POTASSIUM UPTAKE PROTEIN CEOC (trkA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0622","652026","651361","666","7.58","1.14","24091","GTGCACTTCGTCATCATGGGTTGTGGGCGCGTGGGAGCGTCCATGGCTGTTCAGCTCGACCGTATGGGGCACTCGGTGTCCGTCATCGACCGTTCCTCGGACTCTTTCCGCCGCCTGCCCTCGGACTTCAACGGCCGCAAGGTCAAGGGTGTCGGTTACGACCGCGACGCCTTGGAGCAGGCGGGCATTGATGAGGCCTACGCCTTCGTGGCCGTGTCCAACGGGGACAACTCCAACATCGTGGCTGCGCGCGTGGCCAGGGAGAGCTTCGGCGTGGACAACGTCGTCGCCCGGATCTATGACTCGCGGCGGGCCGATGTCTACGAGCGTCTGGGCATCCCCACGGTGGCCACCGTGCGTCAGACGGCCGACCAGATGATGCGCCGCATCCTGCCGGGCTCCAGTGCCCGCGAGCTCGAGGACCCCTCGGGCACGGTGGCTCTCATCCAGCCCAATGCCTCCCCGCAGTGGGTCGGTACGACGATCGGGGTGTTGGAGGACCGCCTCAGAGTGCGGGTGGCCTGGATCTCACGCGATGCCACGGCGCTGCTGCCTGAGGCCGCCACCGTCATCCAGGAGCACGACCGACTGCACCTGGCGGTGAGCACCGACCGTATCGGCCAGGTCCGCCGCGCCCTGTCACACGCCCCGACCCAGGAGGCCTGA","VHFVIMGCGRVGASMAVQLDRMGHSVSVIDRSSDSFRRLPSDFNGRKVKGVGYDRDALEQAGIDEAYAFVAVSNGDNSNIVAARVARESFGVDNVVARIYDSRRADVYERLGIPTVATVRQTADQMMRRILPGSSARELEDPSGTVALIQPNASPQWVGTTIGVLEDRLRVRVAWISRDATALLPEAATVIQEHDRLHLAVSTDRIGQVRRALSHAPTQEA$","Trk system potassium uptake protein TrkA, NAD-binding component","Cytoplasm","Trk system potassium uptake protein trkA(K(+)-uptake protein trkA)","K03499 trk system potassium uptake protein TrkA","TrkA-N domain protein","","Anantharaman V., Koonin E.V., Aravind L. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J. Mol. Biol. 2001. 307(5):1271-1292. PMID: 11292341","","","

InterPro
IPR003148
Domain

TrkA-N
PF02254	$\"[3-119]T$	TrkA_N
PS51201	$\"[2-123]T$	RCK_N

InterPro
IPR006037
Domain

TrkA-C
PF02080	$\"[146-214]T$	TrkA_C
PS51202	$\"[133-215]T$	RCK_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[1-137]T$	no description

","BeTs to 20 clades of COG0569COG name: K+ transport systems, NAD-binding componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0569 is aom-kz-qvdrlbcefgh-nu---twNumber of proteins in this genome belonging to this COG is 3","***** IPB006036 (TrkA potassium uptake protein signature) with a combined E-value of 1.5e-14. IPB006036A 2-16 IPB006036B 19-33 IPB006036D 60-70 IPB006036E 73-87","Residues 48-112 are similar to a (POTASSIUM UPTAKE SYSTEM TRKA TRANSMEMBRANE CHANNEL TRK POTASSIUM-EFFLUX GLUTATHIONE-REGULATED IONIC) protein domain (PD288767) which is seen in Q73W52_MYCPA.Residues 114-205 are similar to a (CEOB SYSTEM TRK UPTAKE POTASSIUM TRKA) protein domain (PDA1F5S3) which is seen in Q7TY36_MYCBO.Residues 144-212 are similar to a (POTASSIUM UPTAKE TRKA SYSTEM TRANSMEMBRANE TRK CHANNEL HOMOLOG IONIC MEMBRANE) protein domain (PD013953) which is seen in Q82KL2_STRAW.","","-62% similar to PDB:2G1U Crystal structure of (tm1088a) from THERMOTOGA MARITIMA at 1.50 A resolution (E_value = 2.1E_18);-56% similar to PDB:1LSS KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+ (E_value = 7.1E_14);","Residues 3 to 119 (E_value = 1.9e-26) place ANA_0622 in the TrkA_N family which is described as TrkA-N domain.Residues 146 to 214 (E_value = 5.7e-06) place ANA_0622 in the TrkA_C family which is described as TrkA-C domain.","","system potassium uptake protein trkA (K(+)-uptake protein trkA) (PA0016)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0623","652076","654184","2109","9.19","11.23","75193","GTGCGTGACTTCGCAGACCGCATCAAGCGGCTTCTCGTCGGCCGTCCTGTTCCCAGCGGAGCTCTGGGGGAGACGCTCCTGCCCAAGAGGATCGCCCTTCCGGTATTCGCCTCCGACGCCCTGTCCTCCGTGGGCTACGCCCCCGATGAGGTGCTCATCACGTTGGCCGTGGCCGGTGTGGTGGCCACCTCCCTGTCGCCGTGGGTGGCCCTGGCCGTCGTCGGCGTCCTGGCCGTCGTCGTGGCCTCCTACCGTCAAACCGTTCACGCCTACCCCTCGGGCGGCGGCGACTACGAGGTGGTCTCGGCCAACCTCGGCTCCCACGCCGGGCTCCTGGTGGCCTCGGCCCTGCTGAGCGACTATGTCCTGACCGTTGCGGTCTCAGTGTCCTCGGGCACCTCCTACCTCGCGGCCGCCCTGCCCGCCCTGGTCCCCTACAAGGTGGAGATCGCCGTCGCGGTCGTCACCGTCCTGGCCGTGCTCAACATGCGCGGCTCGCGCGAGTCGGGCCGGGCCTTCGCCATCCCCACCTACCTGTACATGGGTGTCATCGGCATCATGGCCGTCGCCGGCCTCGTCCAGGAGCTGACCGGGACCCTGGGGCGGGCCGAGTCCGCCGGCTTCGACGTCGTCACTCACGCCGGCTGGGAGCATGGCCTGACCGGCCTGGCCGGAGGCTTCCTGGTCCTGCGGGCCTTCTCCTCGGGGTGCGCGGCCCTGACCGGCGTGGAGGCGATCTCCAACGGCGTGCCCAGCTTCCAGCGCCCCAAGTCCCGCAACGCCGCTACCACGCTGCTGCTCCTGGGAGGAATCGCCGCACTGATGCTCATGAGCGTCATCCACCTGGCCGGCGCCGTCGGCGTGCGCATGGTGGAGGACCCGGCCCACCAGCTCCTGCACAACGGCGTCCCGGTCGGGGACAGCTACCACCAGGACCCCGCGATCGGACAGATCGCCGCCACCGTCTTCTCCGGCTTCCGCCCGATGTTCTACCTGGTCGCCACCGTCACCGGGCTGATCCTGGTCCTGGCCGCCAACACCGCCTTCAACGGGTTCCCGGTCCTGGCCAGTGTCCTGGCCCGTGACGAGTTCCTGCCCCGCCAGCTCTCCCAGCGCGGCGACCGCCTGGCCTTCTCCAACGGCATCATCGTCCTGTGGCTGGGGGCCGTGGCCTTCCTCATCGGCTTCGAGGCCAACACGACCCGCCTCATCCAGCTCTACATCGTGGGCGTGTTCATCTCCTTCACGCTCTCCCAGGTGGGCATGGTGCGCCACTGGACACGCGAGCTGACCATCGCCACTGAGCCGCGGGCCCGCTCACGCATGCACCGCGCCCGCATCATCAACTCCATCGGCGTGCTGGGCACCGGGACGGTCCTGGTCATCGTTCTGCTCACCAAGCTCACCCGGGGAGCCTGGATCACCCTGACGATCATGGCGCTGCTCTACCTGGTGATGAACCGGATCCGCCGCCACTACCGCCGAGTCAGCGAGGAGGTGGCCATCTCCGACCTCCACGACGCCCGCGTCCTGCCGGCCCACGTCCACGCCATCGTCCTGGCCTCCCGCCTCCACCAGCCCACGCTGCGGGCCCTGACCTACGCCCAGTCGACGCACCCCACCGTCCTGGAGGCCCTGACGGTGGACACCGGTGACGGTGGCGCCGAGCATCTCCTGGATGCCTGGGAGGAGGCCGACATCGCCGTGCCCCTGACGGTCCTGGACTCCCCCTACCGGGACATCACCCGCCCGGTCATCAACTACGTCCGCTCGGTGCGCCGGGAGTCCCCCCGAGACCTCGTCGTCGTCTTCCTGCCCGAGTACATCGTGCGTCACTGGTGGGAGCAGATCCTCCACAACCAGACCGCCCTGCGCCTCAAGACCGTCCTGCTGTTCACCCCCGGGGTCGTCGTGGCCTCCGTGCCCTGGCAGCTGGGACTGCCCGGTCAGCGGCACATCCACCACGGCGTGCGGGCCCGCACCGCCGAGGGGATCATCGACGCCGACGTCGCCATGCGCCGTCACGTCGATAGCCATCTCAGTCACCTCGACCAGCACAGCCCCGCCGGTACCGGCGGCGTCGGTGCCGACCCCCAGGAGAATCGATGA","VRDFADRIKRLLVGRPVPSGALGETLLPKRIALPVFASDALSSVGYAPDEVLITLAVAGVVATSLSPWVALAVVGVLAVVVASYRQTVHAYPSGGGDYEVVSANLGSHAGLLVASALLSDYVLTVAVSVSSGTSYLAAALPALVPYKVEIAVAVVTVLAVLNMRGSRESGRAFAIPTYLYMGVIGIMAVAGLVQELTGTLGRAESAGFDVVTHAGWEHGLTGLAGGFLVLRAFSSGCAALTGVEAISNGVPSFQRPKSRNAATTLLLLGGIAALMLMSVIHLAGAVGVRMVEDPAHQLLHNGVPVGDSYHQDPAIGQIAATVFSGFRPMFYLVATVTGLILVLAANTAFNGFPVLASVLARDEFLPRQLSQRGDRLAFSNGIIVLWLGAVAFLIGFEANTTRLIQLYIVGVFISFTLSQVGMVRHWTRELTIATEPRARSRMHRARIINSIGVLGTGTVLVIVLLTKLTRGAWITLTIMALLYLVMNRIRRHYRRVSEEVAISDLHDARVLPAHVHAIVLASRLHQPTLRALTYAQSTHPTVLEALTVDTGDGGAEHLLDAWEEADIAVPLTVLDSPYRDITRPVINYVRSVRRESPRDLVVVFLPEYIVRHWWEQILHNQTALRLKTVLLFTPGVVVASVPWQLGLPGQRHIHHGVRARTAEGIIDADVAMRRHVDSHLSHLDQHSPAGTGGVGADPQENR$","Amino acid transporter","Membrane, Cytoplasm","Amino acid permease","probable conserved integral membrane alanine and valine and leucine rich protein","Amino acid transporter-like","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[68-88]?$ $\"[142-162]?$ $\"[172-192]?$ $\"[223-243]?$ $\"[264-284]?$ $\"[333-355]?$ $\"[376-396]?$ $\"[406-426]?$ $\"[447-465]?$ $\"[469-487]?$	transmembrane_regions

","BeTs to 4 clades of COG0531COG name: Amino acid transportersFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0531 is aomp-zy---rlbcefghs--jxi-wNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 9-95 are 81% similar to a (TRANSMEMBRANE MEMBRANE ACID AMINO PERMEASE PROBABLE PROTEIN INTEGRAL ALANINE VALINE) protein domain (PD538621) which is seen in Q73W53_MYCPA.Residues 104-248 are 70% similar to a (TRANSMEMBRANE MEMBRANE ACID AMINO PERMEASE PROBABLE PROTEIN INTEGRAL ALANINE VALINE) protein domain (PD017696) which is seen in Q82E42_STRAW.Residues 250-367 are 71% similar to a (TRANSMEMBRANE MEMBRANE ACID AMINO PERMEASE PROBABLE PROTEIN INTEGRAL ALANINE VALINE) protein domain (PD520192) which is seen in Q93HB5_STRAW.Residues 372-421 are 86% similar to a (TRANSMEMBRANE MEMBRANE ACID AMINO PERMEASE PROBABLE PROTEIN INTEGRAL ALANINE VALINE) protein domain (PD888750) which is seen in O54098_STRCO.Residues 372-429 are 64% similar to a () protein domain (PDA0Z5N9) which is seen in Q82PI2_STRAW.Residues 422-548 are 71% similar to a (TRANSMEMBRANE MEMBRANE ACID AMINO PERMEASE PROBABLE PROTEIN INTEGRAL ALANINE VALINE) protein domain (PD724215) which is seen in Q73W53_MYCPA.Residues 552-645 are similar to a (TRANSMEMBRANE MEMBRANE ACID AMINO PERMEASE PROBABLE PROTEIN INTEGRAL ALANINE VALINE) protein domain (PD395688) which is seen in Q73W53_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","acid permease","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0624","654181","655578","1398","7.71","3.07","49296","ATGACCCCCCAGCCCAGCCGGAGCGCAGACCAGCCTGCCCCCAGCCGTGGCGAGCCGCGCGAGCTGACCCTGGCGGTGGGGGCCCCTGCGCACGGCGGGCACTGCGTGGCCCGCCCCGTGGACGACCCGGGCGGCCGCGTCATCTTCGTGCGCCATGCCCTGCCCGGTGAGACCGTGCGGGCCCGCCTGACCGAGATGACCTCGCGGACCTGGCGTGCCGACGCCGTTGAGATCCTCCAGGCCTCCCCGGACCGCGACGAGTCCGTCTGGCCCGAGGCCGGCCCGGGGGGAGTGGGTGGGGGAGAGCTCGCCCACGTGGCCCTGGATGCCCAGCGCACCTGGAAGCGCTGGGTCCTGGCCGACTGCCTGCGCCGGATCGGCGGGCAGGAGGTGGCCGACGCCGTCGCCGTCCTGCCCGAGGCCTCCGCCGCTGCCGCCGTGCCGATCGAGCCCATGCCCACCGACGCCGCGGCCCAGGCCTCCAACAGCGCCCGGCGGCGTGCCCTGGCCGGAACCGCCACCCGCACCCGCGTGAGCCTGACGGTCGGTGAGGACGGCAGGCCCGGCATGCATGCCTTCCGCTCCGGGACGGTCCTGCCCCTGCGCCGCCTGCCTCTGGCGGTTGAGGCCATCACCGAGATCGGGCTGCTGGAGCGCTCCCGCTGGCGCGCCCACTACCGACCCGGCATGCGCATCGAGGCCATCGCACCCAGCGGCGGTGAGCCCGTCGTCCTGCTCGACGAGCGGCTCCTGACCGCTCAGGCCCGCAGCACCGGGCGGCGCCGGGTCCGGGAGGTTGTGGACGCCTCGGCCCTGGGGCTGGGGGAGCTGACTTACTCCGTCCACGCCGAGGGCTTCTGGCAGGTCCACGTCGACGCCCCTCGGGTGCTCGTCGAGCGCGTTGTACGCGGCGCCCTGGGGGCGGACCTCGATGGTGCCGCGGGCAGCCGCGTCCTGGAGCTCTATTCGGGGGCCGGCCTGTTCACCCTGCCGCTGGCCGCCCTGGTGGGGGACCGCGGTCAGGTCCTGTCCCTGGAGGGCAATGAGCAGGCCGTTCGCGACGCCCGCCGCACCCTGCATGACCACCCCGCTGCACGCCTGGCCTCGGGTCGCGTGAGCGCCCGCTCGGTGCGCGAGCTCGCCGGCTCCTTCACCGGCGGCCGCCCCGACGTCGTCGTCCTCGACCCGCCGAGGCAAGGAGCTGGGCGCGAGGTCATCGAGGCCGTCGGCGCCCTGGGAGCCGAGCGGATCGTCCTAGTGGCCTGCGACCCGGCGGCGCTGGCCCGGGACCTGGGAACCCTCCTGCGCTCGGGCTACACGCTGGGCTCCATGAGCGCGCTGGACATGTTCCCGCACACCCACCACTTCGAGACGATCGCGGTACTCGAGCGCTCCTGA","MTPQPSRSADQPAPSRGEPRELTLAVGAPAHGGHCVARPVDDPGGRVIFVRHALPGETVRARLTEMTSRTWRADAVEILQASPDRDESVWPEAGPGGVGGGELAHVALDAQRTWKRWVLADCLRRIGGQEVADAVAVLPEASAAAAVPIEPMPTDAAAQASNSARRRALAGTATRTRVSLTVGEDGRPGMHAFRSGTVLPLRRLPLAVEAITEIGLLERSRWRAHYRPGMRIEAIAPSGGEPVVLLDERLLTAQARSTGRRRVREVVDASALGLGELTYSVHAEGFWQVHVDAPRVLVERVVRGALGADLDGAAGSRVLELYSGAGLFTLPLAALVGDRGQVLSLEGNEQAVRDARRTLHDHPAARLASGRVSARSVRELAGSFTGGRPDVVVLDPPRQGAGREVIEAVGALGAERIVLVACDPAALARDLGTLLRSGYTLGSMSALDMFPHTHHFETIAVLERS$","RNA methyltransferase","Cytoplasm","RNA methyltransferase","putative RNA methyltransferase ","(Uracil-5)-methyltransferase","","Johansson M.J., Bystrom A.S. Dual function of the tRNA(m(5)U54)methyltransferase in tRNA maturation. RNA 2002. 8(3):324-335. PMID: 12003492Agarwalla S., Kealey J.T., Santi D.V., Stroud R.M. Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli. J. Biol. Chem. 2002. 277(11):8835-8840. PMID: 11779873","","","

InterPro
IPR002792
Domain

Deoxyribonuclease/rho motif-related TRAM
PF01938	$\"[15-77]T$	TRAM
PS50926	$\"[13-77]T$	TRAM

InterPro
IPR010280
Family

(Uracil-5)-methyltransferase
PF05958	$\"[155-465]T$	tRNA_U5-meth_tr
PS01231	$\"[447-457]T$	TRMA_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[287-395]T$	no description
PTHR11061	$\"[274-464]T$	RNA M5U METHYLTRANSFERASE FAMILY
PTHR11061:SF2	$\"[274-464]T$	RNA M5U METHYLTRANSFERASE

","BeTs to 14 clades of COG2265COG name: SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG2265 is ----k-yqv-rlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 2","***** IPB001566 (tRNA (uracil-5-)-methyltransferase/TrmA) with a combined E-value of 5.7e-26. IPB001566B 318-333 IPB001566C 392-401 IPB001566D 417-427 IPB001566E 439-464***** IPB010280 ((Uracil-5)-methyltransferase) with a combined E-value of 2.3e-23. IPB010280A 98-115 IPB010280B 318-330 IPB010280C 417-434 IPB010280D 438-457","Residues 11-78 are 64% similar to a (METHYLTRANSFERASE TRANSFERASE 2.1.1.- RNA 23S RRNA URACIL-5--METHYLTRANSFERASE PROCESSING 5-U1939-METHYLTRANSFERASE METAL-BINDING) protein domain (PD007943) which is seen in YNA1_STRCO.Residues 279-359 are 61% similar to a (METHYLTRANSFERASE RNA TRANSFERASE 2.1.1.- ALANINE GLYCINE VALINE RICH CGL1903/CG2084 DIP1398) protein domain (PD599333) which is seen in YD94_BIFLO.Residues 317-464 are 52% similar to a (METHYLTRANSFERASE BD2056 RNA TRANSFERASE 2.1.1.-) protein domain (PDA0D540) which is seen in YK56_BDEBA.Residues 390-430 are 80% similar to a (METHYLTRANSFERASE TRANSFERASE 2.1.1.- RNA 23S RRNA URACIL-5--METHYLTRANSFERASE PROCESSING TRNA RRNAM-) protein domain (PD004091) which is seen in YNA1_STRCO.","","-53% similar to PDB:1UWV CRYSTAL STRUCTURE OF RUMA, THE IRON-SULFUR CLUSTER CONTAINING E. COLI 23S RIBOSOMAL RNA 5-METHYLURIDINE METHYLTRANSFERASE (E_value = 9.2E_16);-53% similar to PDB:2BH2 CRYSTAL STRUCTURE OF E. COLI 5-METHYLURIDINE METHYLTRANSFERASE RUMA IN COMPLEX WITH RIBOSOMAL RNA SUBSTRATE AND S-ADENOSYLHOMOCYSTEINE. (E_value = 9.2E_16);","Residues 15 to 77 (E_value = 0.00024) place ANA_0624 in the TRAM family which is described as TRAM domain.Residues 155 to 465 (E_value = 0.00019) place ANA_0624 in the tRNA_U5-meth_tr family which is described as tRNA (Uracil-5-)-methyltransferase.","","methyltransferase (uracyl-5-)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0625","655817","658489","2673","4.83","-41.64","95660","GTGACCAGCCTCAACACCTTCGCCTCCCGCAGCACCCTCGACGTCGATGGCCGCGACTACGAGATCTACCGCCTCGACGCCGTCCCCGGCCTGGAGCGCCTGCCCTACAGCCTCAAGGTGCTGGCCGAGAACCTGCTGCGCACCGAGGACGGCGCCAACATCACCGCCGACCACGTGCGCGCCCTGGCCGCCTGGGACCCGGCTGCCGAGCCCGACACGGAGATTCAGTTCACCCCAGCCCGCGTCGTCATGCAGGACTTCACCGGCGTGCCCTGCATCGTGGACCTGGCCACCATGCGCGAGGCGGTCGCTGACCTCGGAGGCGACCCCGAGGTCATCAACCCCCTCAACCCCGCTGAGATGGTCATCGACCACTCCGTGCAGATCGACTCCTTCGGCCTGCCCGGATCCCTGGAGCGCAACAAGGAGCGCGAGTACGAGCGCAACTCCGAGCGCTACCAGTTCCTGCGCTGGGGACAGGGGGCGCTGTCCAACTTCCGCGTCGTCCCCCCGGGTACGGGCATCGTCCACCAGGTCAACATCGAGTACCTGGCCCGCATCGTCTTCACCCACGAAGCCGACGGCGTCACCCAGGCCTACCCCGACACCTGCGTGGGCACCGACTCCCACACCACCATGGTCAACGGCCTGGGCGTCCTGGGCTGGGGCGTGGGCGGCATCGAGGCCGAGGCCGCCATGCTGGGCCAGCCCGTCTCCATGCTCATCCCCAAGGTGGTGGGCTTCAAGCTCTCCGGCGCCATCCCCGCCGGCGCCACCGCCACCGACGTGGTCCTGACCATCACCGAGATGCTGCGCGCCCACGGCGTGGTGGGCAAGTTCGTCGAGTTCTACGGCGAGGGCGTTGCCGAGGTGCCGCTGGCCAACCGCGCCACCATCGGCAACATGAGCCCCGAGTTCGGCTCCACCGCCGCAATCTTCCCGATCGACGAGGTCACCCTGGACTACCTGCGCCTGACCGGCCGCTCCGAGGAACGCGTGCGCCTGGTCGAGGCCTACACCAAGGCCCAGGGAATGTGGCACGACCCGGCCCGCGAGCCCGTCTACTCCGAGTACCTCGAGCTGGACCTGTCCACCGTGGTGCCCTCCATCGCTGGCCCCAAGCGCCCCCAGGACCGTATCGTCCTGTCACGGGCCAAGGAGTCCTTCCAGGAGGTCCTGCCCACCTACGCCTCCCAGCCATCCAAGCCGACGCCGGTGACCCTGGCCGACGGCACCGCCACCGAGCTCGACAACGGGCACGTCGCCATCGCCTCGATCACCTCGTGCACCAACACCTCCAACCCCTCGGTGATGATGGCAGCTGGCCTGCTGGCCCGTAACGCCGTCGCCCGGGGCCTGCGCTCCAAGCCCTGGGTGAAGACCTCCACCGCCCCGGGCAGCCAGGTCGTCACCGACTACTACGAGAAGGCCGGGTTGTGGCCCGCCCTCAACGAGCTGGGCTTCAACGTCGTCGGCTACGGCTGCGCCACCTGCATCGGCAACTCCGGGCCCCTGCCGGCCGAGGTCTCCCAGGCGGTCAACGACGCCGACCTCGCCGTGGTCTCGGTGCTCTCGGGCAACCGCAACTTCGAGGGGCGCATCAACCCCGACGTCAAGATGAACTACCTGGCCTCCCCGCCCCTGGTCATCGCCTACGCCCTGGCCGGGACCATGGACATCGACTTCGCCACCGAGCCGCTGGGCCAGGACCCCGAGGGCCACGACGTCTTCCTGTCCGACATCTGGCCCGATCCCACCGAGGTCCAGGCCGTCATCGACGCCACCATCGACCGCGAGATGTACACGCGCGACTACGCCGATGTCTTCGCCGGCGACGAGCGCTGGCAGGGCCTGGACACCCCCGAGGGGGACACCTTCGCCTGGGACGAGGAGTCCACCTACGTGCGCAAGGCCCCCTTCTTCGAGGGCCTGTCCATGGAGCTCACCCCGGTCACCGACATCAAGGACGCCCGAGTGCTCGCCCTGCTGGGGGACTCGGTGACCACCGACCACATCTCCCCGGCCGGCGCCATCAAGGCCGACTCCCCGGCCGGGCGCTACCTGGCCGAGCACGGCGTGGCCCGCGCGGACTTCAACTCCTACGGCTCGCGCCGCGGCAACCACGAGGTCATGATCCGCGGCACCTTCGCCAACATCCGCCTGCGCAACCGGCTGCTCGACGGCGTCGAGGGCGGCTACACCCGCAACTTCCTCACCGGCGAGCAGGAGTCGATCTTCGACGCCTCCCAGGCCTACCAGGCCGCAGGCATCCCGCTGGTGGTCCTGGGCGGCAAGGAGTACGGCTCGGGCTCCTCACGCGACTGGGCGGCCAAGGGCACGGCACTGCTGGGCGTCAAGGCCGTCATCGCCGAGTCCTTCGAGCGCATCCACCGCTCCAACCTCATCGGCATGGGCGTGGTTCCCCTCCAGTTCCCGGCCGGACAGAGCGCCGAGTCGCTCGGCCTGGACGGCACCGAGACCTTCTCCATCACGGGCCTGACCGCGCTTAACGAGGGCACCACCCCGCGCACCGTCGCGGTCACGGCGCAGAAGGCTGACGGCTCGGCGGTCTCCTTCGACGCCGTCGTACGCATCGACACCCCCGGCGAGGCTGACTACTTCCGCCACGGCGGCATCCTGCAGTACGTGCTGCGCCAGCTCGCCAGCTCCTGA","VTSLNTFASRSTLDVDGRDYEIYRLDAVPGLERLPYSLKVLAENLLRTEDGANITADHVRALAAWDPAAEPDTEIQFTPARVVMQDFTGVPCIVDLATMREAVADLGGDPEVINPLNPAEMVIDHSVQIDSFGLPGSLERNKEREYERNSERYQFLRWGQGALSNFRVVPPGTGIVHQVNIEYLARIVFTHEADGVTQAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPKVVGFKLSGAIPAGATATDVVLTITEMLRAHGVVGKFVEFYGEGVAEVPLANRATIGNMSPEFGSTAAIFPIDEVTLDYLRLTGRSEERVRLVEAYTKAQGMWHDPAREPVYSEYLELDLSTVVPSIAGPKRPQDRIVLSRAKESFQEVLPTYASQPSKPTPVTLADGTATELDNGHVAIASITSCTNTSNPSVMMAAGLLARNAVARGLRSKPWVKTSTAPGSQVVTDYYEKAGLWPALNELGFNVVGYGCATCIGNSGPLPAEVSQAVNDADLAVVSVLSGNRNFEGRINPDVKMNYLASPPLVIAYALAGTMDIDFATEPLGQDPEGHDVFLSDIWPDPTEVQAVIDATIDREMYTRDYADVFAGDERWQGLDTPEGDTFAWDEESTYVRKAPFFEGLSMELTPVTDIKDARVLALLGDSVTTDHISPAGAIKADSPAGRYLAEHGVARADFNSYGSRRGNHEVMIRGTFANIRLRNRLLDGVEGGYTRNFLTGEQESIFDASQAYQAAGIPLVVLGGKEYGSGSSRDWAAKGTALLGVKAVIAESFERIHRSNLIGMGVVPLQFPAGQSAESLGLDGTETFSITGLTALNEGTTPRTVAVTAQKADGSAVSFDAVVRIDTPGEADYFRHGGILQYVLRQLASS$","Aconitate hydratase 1","Cytoplasm","aconitate hydratase 1","aconitate hydratase 1 ","aconitate hydratase 1","","Weidner G., Steffan B., Brakhage A.A. The Aspergillus nidulans lysF gene encodes homoaconitase, an enzyme involved in the fungus-specific lysine biosynthesis pathway. Mol. Gen. Genet. 1997. 255(3):237-247. PMID: 9268014","","","

InterPro
IPR000573
Domain

Aconitate hydratase, C-terminal
PF00694	$\"[684-814]T$	Aconitase_C

InterPro
IPR000585
Domain

Hemopexin
PS00024	$\"[578-592]?$	HEMOPEXIN

InterPro
IPR001030
Domain

Aconitate hydratase, N-terminal
PD000511	$\"[171-573]T$	Q6A8V4_PROAC_Q6A8V4;
PR00415	$\"[142-155]T$ $\"[166-174]T$ $\"[199-212]T$ $\"[213-228]T$ $\"[275-288]T$ $\"[289-302]T$ $\"[368-382]T$ $\"[425-436]T$ $\"[487-500]T$	ACONITASE
PF00330	$\"[53-556]T$	Aconitase
PS00450	$\"[421-437]T$	ACONITASE_1
PS01244	$\"[487-500]T$	ACONITASE_2

InterPro
IPR006249
Family

Aconitate hydratase 1
TIGR01341	$\"[18-888]T$	aconitase_1: aconitate hydratase

InterPro
IPR012084
Family

Aconitase/homoaconitase
PIRSF001417	$\"[9-890]T$	Aconitase A/homoaconitase (aconitate hydratase 1)

noIPR
unintegrated

unintegrated
G3DSA:3.20.19.10	$\"[645-889]T$	no description
G3DSA:3.30.499.10	$\"[15-245]T$ $\"[364-570]T$	no description
G3DSA:3.40.1060.10	$\"[246-363]T$	no description
PTHR11670	$\"[8-888]T$	ACONITASE
PTHR11670:SF1	$\"[8-888]T$	ACONITASE

","BeTs to 14 clades of COG1048COG name: Aconitase AFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1048 is -o-p-zyq-drlb-efg-sn-jx---Number of proteins in this genome belonging to this COG is 1","***** IPB001030 (Aconitate hydratase, N-terminal) with a combined E-value of 5.3e-80. IPB001030B 196-230 IPB001030C 252-262 IPB001030D 275-324 IPB001030E 424-438 IPB001030F 467-520***** IPB000573 (Aconitate hydratase, C-terminal) with a combined E-value of 2.4e-35. IPB000573A 664-679 IPB000573B 760-800","Residues 33-77 are 84% similar to a (ACONITATE HYDRATASE LYASE ACONITASE CITRATE HYDRO-LYASE IRON-SULFUR 4FE-4S IRON REGULATORY) protein domain (PD421200) which is seen in Q82KV4_STRAW.Residues 74-98 are identical to a (ACONITASE LYASE HYDRATASE ACONITATE HYDRO-LYASE ACN CITRATE PROBABLE A ACNA) protein domain (PD926628) which is seen in Q6AFD6_BBBBB.Residues 99-170 are 83% similar to a (ACONITATE HYDRATASE LYASE ACONITASE CITRATE HYDRO-LYASE IRON-SULFUR IRON REGULATORY 4FE-4S) protein domain (PD537715) which is seen in Q6A8V4_PROAC.Residues 171-573 are similar to a (LYASE ISOMERASE ACONITATE 3-ISOPROPYLMALATE HYDRATASE IRON-SULFUR DEHYDRATASE 4FE-4S LARGE SUBUNIT) protein domain (PD000511) which is seen in Q6A8V4_PROAC.Residues 183-393 are 73% similar to a (LYASE HYDRATASE ACONITATE) protein domain (PD690511) which is seen in Q8EQL5_OCEIH.Residues 183-393 are 76% similar to a (ACONITATE LYASE HYDRATASE) protein domain (PD995517) which is seen in Q6MIH9_BDEBA.Residues 315-420 are 66% similar to a (ACONITATE LYASE HYDRATASE) protein domain (PD995518) which is seen in Q6F827_ACIAD.Residues 410-557 are 83% similar to a (HYDRATASE LYASE ACONITATE METHYL-CIS-ACONITIC PROBABLE ACID) protein domain (PD664512) which is seen in Q8YEM3_BRUME.Residues 558-608 are 64% similar to a (ACONITATE LONG HYDRATASE 870AA) protein domain (PD995512) which is seen in Q9YBI0_AERPE.Residues 561-608 are 66% similar to a (ACONITATE HYDRATASE) protein domain (PD995510) which is seen in Q98EA3_RHILO.Residues 609-673 are 86% similar to a (ACONITATE HYDRATASE LYASE ACONITASE CITRATE HYDRO-LYASE IRON-SULFUR IRON REGULATORY 4FE-4S) protein domain (PD977780) which is seen in Q6NH63_CORDI.Residues 609-673 are 69% similar to a (LYASE ACONITATE HYDRATASE TRICARBOXYLIC IRP-LIKE ACONITASE CYCLE ACID CITRATE 4FE-4S) protein domain (PDA1D9E4) which is seen in Q72KN3_THET2.Residues 674-742 are 86% similar to a (ACONITATE HYDRATASE LYASE ACONITASE CITRATE HYDRO-LYASE IRON-SULFUR IRON REGULATORY 4FE-4S) protein domain (PD004178) which is seen in Q83B05_COXBU.Residues 740-839 are 86% similar to a (ACONITATE HYDRATASE LYASE ACONITASE ISOMERASE HYDRO-LYASE CITRATE B ACID 4FE-4S) protein domain (PD489052) which is seen in Q6NH63_CORDI.Residues 745-793 are 93% similar to a (LYASE ISOMERASE 3-ISOPROPYLMALATE SMALL SUBUNIT DEHYDRATASE ACONITATE HYDRATASE BIOSYNTHESIS IPMI) protein domain (PD001077) which is seen in Q6AFD6_BBBBB.Residues 794-851 are 91% similar to a (ACONITATE HYDRATASE LYASE ACONITASE CITRATE HYDRO-LYASE IRON-SULFUR IRON REGULATORY 4FE-4S) protein domain (PD094652) which is seen in Q8FTA8_COREF.Residues 834-889 are 66% similar to a (ACONITASE LYASE) protein domain (PDA1F1X2) which is seen in Q8PLC0_XANAC.Residues 840-890 are 68% similar to a (ISOMERASE PHOSPHINOMETHYLMALATE) protein domain (PDA1A4T4) which is seen in Q9RIL3_STRVR.Residues 864-887 are identical to a (ACONITATE HYDRATASE LYASE ACONITASE CITRATE HYDRO-LYASE IRON REGULATORY IRON-SULFUR 4FE-4S) protein domain (PD838720) which is seen in Q8FTA8_COREF.","","-42% similar to PDB:5ACN STRUCTURE OF ACTIVATED ACONITASE. FORMATION OF THE (4FE-4S) CLUSTER IN THE CRYSTAL (E_value = 1.3E_48);-42% similar to PDB:6ACN STRUCTURE OF ACTIVATED ACONITASE. FORMATION OF THE (4FE-4S) CLUSTER IN THE CRYSTAL (E_value = 1.3E_48);-42% similar to PDB:7ACN CRYSTAL STRUCTURES OF ACONITASE WITH ISOCITRATE AND NITROISOCITRATE BOUND (E_value = 1.3E_48);-42% similar to PDB:1B0J CRYSTAL STRUCTURE OF ACONITASE WITH ISOCITRATE (E_value = 2.9E_48);-42% similar to PDB:1B0K S642A:FLUOROCITRATE COMPLEX OF ACONITASE (E_value = 2.9E_48);","Residues 53 to 556 (E_value = 1.1e-198) place ANA_0625 in the Aconitase family which is described as Aconitase family (aconitate hydratase).Residues 684 to 814 (E_value = 4.1e-59) place ANA_0625 in the Aconitase_C family which is described as Aconitase C-terminal domain.","","hydratase 1 (acnA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0626","659802","658834","969","8.20","3.76","35490","ATGCCCGATCCATCCTCATATGCTCAAGGCAGCGCGCCCATCACTCCTGGCCCCTTCAAGCAAGCCACCGGCGCCCGAAGCTGGATCCTGTGCTTGGCGGCCTCAGTTATCGGCTGGCTCCTGGTACAGCTGTTCAATCTCCTGAACCAGTCCAGCTCGCAGACCTCGAATTCGTGGAACGTGGGAACGCGGCTAGCCGTCGTCGCCCTGAGCTCGCTCAACTCCATCCTCCTCATCGCCGCTATAGTTCTGTTCATCAACCATATGCACCGGGTCTATGTGGCCCATCGGAGGCGTGCAGGCCACTTCACCTTGGAAGAACGCCGTGAAATCGCACGACGCGATGATCTGTACAAGTCCTGGGATCACGCCCGCGCACTGGCGATCAGCCTCCTGTCCGATGACCCTGGTGGCAGGTTCCGGCCCTGGGACGTCGTGCTGGATCCCGGCGAGGCTGCGGTTGTGGACTGCCCGGCCGGCTACGCGCGCTTCTACGGAACCACCGTGTCCTACACGCAGTCCAGCGGTATGTTCTTTGGATCGCCAGCCTTCGTCCTGGCAGGTATGGGCGCCACCGCGATCAGCAACAGCGCCAGACGTCGAGCCGCCGAACGACTCGCGGCGGATCAGTGGCGCGAGCACCAGCAGGTGCGTTGTCTGGTCACCGAGCAGCGCATCCTGCTGCAGCGTGCGGACTACCAGTGGCTCAGTTTCTACTTCTCCGCCATAGTATCTATGCATCCTTTCCCCGCCGAGGGCCTGTTCTTCGCCGAGTTTGAGGACACGTCCCCCTTGCGCCTCGAGGGCGCGGCCGCAGTGATCGCCTCCGTGGTGACGGTGTGGTACCGCTTCGGAGCCACAGGACTGCGCGATCATCCCGGATTGCAGTGCTTGCGACTACCTCAGCAAGTCCTGACAGCAACCGAGCCAGTTGAAGGTGCCCCGCCCCCGGAGGTGACGAAACCCTAG","MPDPSSYAQGSAPITPGPFKQATGARSWILCLAASVIGWLLVQLFNLLNQSSSQTSNSWNVGTRLAVVALSSLNSILLIAAIVLFINHMHRVYVAHRRRAGHFTLEERREIARRDDLYKSWDHARALAISLLSDDPGGRFRPWDVVLDPGEAAVVDCPAGYARFYGTTVSYTQSSGMFFGSPAFVLAGMGATAISNSARRRAAERLAADQWREHQQVRCLVTEQRILLQRADYQWLSFYFSAIVSMHPFPAEGLFFAEFEDTSPLRLEGAAAVIASVVTVWYRFGATGLRDHPGLQCLRLPQQVLTATEPVEGAPPPEVTKP$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[25-45]?$ $\"[66-86]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide

","BeTs to 6 clades of COG1309COG name: Transcriptional regulators, AcrR familyFunctional Class: KThe phylogenetic pattern of COG1309 is a-T--QVCEBRH---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:35:38 2007","Wed Aug 15 10:35:38 2007","Wed Aug 15 10:35:38 2007","Wed Aug 15 10:34:36 2007","","","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","Wed Aug 15 10:34:36 2007","","Wed Aug 15 10:34:36 2007","","Wed Aug 15 10:34:36 2007","yes","","" "ANA_0628","660242","660553","312","5.39","-3.34","10773","ATGACCCAGGTCCCTGCCGAGGCCTCGGACGGGAGCCTGAGTCCGCTACGGTCATCCGCTGCGCAACGCACGGTTGCCATCGTCACCGCGGCGCTGGCCGGCTACCGCATCCCCGAGGATCGGATCATCGACGCTGTGCGAATGACCCGGGCGTCACTCCATGGCTTCGTGGATATCGAGGTCCACGGTGGCTTCGCCATGAATGCCCCCATTGACGTGAGTTTCGACACGCTCGTCGACTCGCGGGACGCCGCCCTGGTCGCTCTCGGCGAGCATGAGGGCGGACAGGTATCAGTGAGGACGAAAGGATAA","MTQVPAEASDGSLSPLRSSAAQRTVAIVTAALAGYRIPEDRIIDAVRMTRASLHGFVDIEVHGGFAMNAPIDVSFDTLVDSRDAALVALGEHEGGQVSVRTKG$","Transcriptional regulator, TetR family fragment","Cytoplasm","putative tetR family transcriptional regulator","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","tetR family transcriptional regulator","","1","","","","","","","","","","","Wed Aug 15 10:36:29 2007","","","","","Wed Aug 15 10:36:29 2007","","","","Wed Aug 15 10:36:29 2007","Wed Aug 15 10:36:29 2007","","","","","yes","","" "ANA_0629","660724","662175","1452","5.12","-15.89","50176","ATGTCACAGTCCACCGTCAACAGCGACGCGACCAACCAGACAGACGCTCCGGTCGAGGAGGTCGACCTTCTCGTCGTCGGAGGCGGCAAGGCCGGCAAGTCCCTGGCGATGCTGCGCGCCAAGGCCGGCGACAAGGTCGTCATGGTGGAGCGGGACAAGGTGGGCGGCACCTGCATCAACGTCGCCTGCATCCCCACCAAGACCCTCATCTCCGCCGCCCGCGTCCTCCGTGAGGTCCAGGGCTCGCAGGCCTACGGCGTCACCCTGCCCGAGCAGGACGGCGGCGCTGACGCCCTGGCCCAGGCCCGTATCGAGCTGGCCTCCTTCCGCGCCCGCAAGGAGGCCGTCGTGGGCGGCATGGTGGCTGCTCACGAGAAGATGTTCCCCGCCTCCGGCATGGACTTCGTCAAGGGCACCGCCCGCTTCGTGGGGGAGCGCACCGTCGAGATCGCCCTCAACGACGGCGGCCTGCGGCGCGTGCGCGGCGCCAAGGTCCTCATCAACACCGGCACCACGCCGTCGGTCCCCCCGATCGAGGGCCTGTCCGACGTGCGCTACTGGACCAGCGAGGACCTGCTCACCCTGCCCGAGCTGCCCAGTAGCCTCATCGTCCTGGGCGGCGGCGTCATCGGCGTCGAGATGGCCTCCCTCATGGGGCTCCTCGGTGTCCCGGTCACCATCGTCCACGCCGGGCCGCACATCCTGGACCGCGAGGACGAGGACGTCGCCGCTGAGGTGACCGCCGGCCTGGAGGCCCTGGGGGTCACGGTCCTGACTGGCGCACTCGCCTCGAAGGTCGCCGCCGCGGCCGACGGGAACGGCGTCGTCGTCACCACCGCCGACGGGCACGAGGTGAGCGGATCCCACCTGCTCGTCGCCCTGGGGCGCACCCCCGTCACCGCCGGCCTCGGCCTGGAGGCCGCGGGCGTGGAGCTGACCGAGCGCGGCTTCGTGCGCGTCGACGACCACCTGTGCACCACCGCCGAGAACGTCTACGCCGCCGGTGACGTGGCCGGAACGCCCCAGTTCACCCACGCCTCCTGGAACGACTTCCGCGTCCTGCGCGACCTCTTCGCCGGCAAGGAGGCCTCCACCACCGGACGTCTCATCCCCTGGGCCGTCTTCACCACGCCCGAGCTCGGGCACGTGGGCATGAGCGAGGCCGAGGCCCGCGAGGCCGGCTATGAGGTGCGCGTCGCCAAGACCCCGACGGCGGCCGTCCCGCGCGCCAAGACCCTGGGCCGTACCGAGGGCTTCTTCAAGGTCATCATCGACGCCCGCACCGACCTGATCCTGGGTGCCGCCATCATCGGCGCCGAGGCCAGTGAGGTCGTCACCAGCATCCAGATGGCGATGCTGGGCGACCTGACGTGGCAGCAGGTGCGCGACGCCGTCATCACCCACCCCACCATGAGCGAGGGACTCAACATCGTCCTGGACTCCCTCGGCTGA","MSQSTVNSDATNQTDAPVEEVDLLVVGGGKAGKSLAMLRAKAGDKVVMVERDKVGGTCINVACIPTKTLISAARVLREVQGSQAYGVTLPEQDGGADALAQARIELASFRARKEAVVGGMVAAHEKMFPASGMDFVKGTARFVGERTVEIALNDGGLRRVRGAKVLINTGTTPSVPPIEGLSDVRYWTSEDLLTLPELPSSLIVLGGGVIGVEMASLMGLLGVPVTIVHAGPHILDREDEDVAAEVTAGLEALGVTVLTGALASKVAAAADGNGVVVTTADGHEVSGSHLLVALGRTPVTAGLGLEAAGVELTERGFVRVDDHLCTTAENVYAAGDVAGTPQFTHASWNDFRVLRDLFAGKEASTTGRLIPWAVFTTPELGHVGMSEAEAREAGYEVRVAKTPTAAVPRAKTLGRTEGFFKVIIDARTDLILGAAIIGAEASEVVTSIQMAMLGDLTWQQVRDAVITHPTMSEGLNIVLDSLG$","Dihydrolipoamide dehydrogenase/glutathione oxidoreductase","Cytoplasm","possible class I pyridinenucleotide-disulfideoxidoreductase","pyridine nucleotide-disulphide oxidoreductase dimerisation region","pyridine nucleotide-disulphide oxidoreductase dimerisation region","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Kunert K.J., Cresswell C.F., Schmidt A., Mullineaux P.M., Foyer C.H. Variations in the activity of glutathione reductase and the cellular glutathione content in relation to sensitivity to methylviologen in Escherichia coli. Arch. Biochem. Biophys. 1990. 282(2):233-238. PMID: 2241146Shames S.L., Fairlamb A.H., Cerami A., Walsh C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 1986. 25(12):3519-3526. PMID: 3718941Carothers D.J., Pons G., Patel M.S. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 1989. 268(2):409-425. PMID: 2643922Misra T.K. Bacterial resistances to inorganic mercury salts and organomercurials. Plasmid 1992. 27(1):4-16. PMID: 1311113","","","

InterPro
IPR000815
Family

Mercuric reductase
PR00945	$\"[32-50]T$ $\"[166-183]T$ $\"[201-218]T$ $\"[221-236]T$ $\"[402-422]T$ $\"[467-483]T$	HGRDTASE

InterPro
IPR001100
Family

Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411	$\"[22-44]T$ $\"[54-69]T$ $\"[165-174]T$ $\"[201-226]T$ $\"[288-302]T$ $\"[331-338]T$ $\"[366-387]T$ $\"[431-446]T$ $\"[453-473]T$	PNDRDTASEI

InterPro
IPR001327
Domain

Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139	$\"[169-241]T$	Q72D92_DESVH_Q72D92;
PF00070	$\"[201-295]T$	Pyr_redox

InterPro
IPR004099
Domain

Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30	$\"[370-477]T$	no description
PF02852	$\"[370-479]T$	Pyr_redox_dim

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368	$\"[22-44]T$ $\"[165-174]T$ $\"[201-226]T$ $\"[288-302]T$ $\"[331-338]T$	FADPNR
PF07992	$\"[22-341]T$	Pyr_redox_2

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[20-363]T$	no description
PTHR22912	$\"[24-482]T$	DISULFIDE OXIDOREDUCTASE
PTHR22912:SF29	$\"[24-482]T$	MERCURIC REDUCTASE

InterPro
IPR007214
Domain

YbaK/prolyl-tRNA synthetase associated region
PF04073	$\"[52-189]T$	YbaK

noIPR
unintegrated

unintegrated
G3DSA:3.90.960.10	$\"[31-190]T$	no description

","BeTs to 6 clades of COG2606COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2606 is -----z----rlb-efgh-n-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 98-172 are similar to a (SYNTHETASE AMINOACYL-TRNA PROLYL-TRNA LIGASE PROLINE--TRNA DNA-BINDING PRORS BIOSYNTHESIS ATP-BINDING TRNA) protein domain (PD006954) which is seen in Q6A5S1_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 52 to 189 (E_value = 1.9e-07) place ANA_0630 in the YbaK family which is described as YbaK / prolyl-tRNA synthetases associated domain.","","- prolyl-tRNA synthetases associated domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0631","663472","662819","654","6.55","-1.11","23139","ATGAGCACCACTGAGTCGCATACCACCTCCCCCATTCTGACCTGCGGCGCGCTGGCCGGCAACATCGTGCGTCTGGAGCCGCTGTCGCCTGAGCACGTACCGGGGCTGCAGATGGCCGCAGAGGGGGCCGCGACCAGCCCCTTCGCCACGGTGCCGGCACCGGAGACGGTCGAGGACTACGTGGCCCATAGCCTGGCCCGCCGGGACACGGGTGCCTACGCGCCCTTCGCCCAGGTGGAGGTCGCTACCGGCCGCGTCGTCGGGCACACCGCCTACCTGACGCCCCGGTGGATGCCCGATGGGCGGCTCTTCGCCGTCGAGGTCGGTTCCTCCTGGCTCTCCCCCACTGTTCGTGGCACCGCCGTCAACCCGGCTGCCAAGCTCCTGCTGCTGGCGCAGGCCCTCGAGGACTGGGGCGTGGACCGTGTGGACATCAAGACCGATGCACGCAATGAGGTGGCTCGCGGTGCGATCGCGGCCCTGGGGGCGACCTTCGAGGGGGTCCTGCGCGCCTGGCAGCCCTCGCTGGCTCCCGGTGAGGAGGGGCGCACGCGCGACACGGCCATGTTCGCCATCACCCCGCAGCAGTGGCCCGGGGTCAGGACCCGTCTGGTGGAGCGCATCGAGAGGCGCTCGACGTCGTCGAAAGGATGA","MSTTESHTTSPILTCGALAGNIVRLEPLSPEHVPGLQMAAEGAATSPFATVPAPETVEDYVAHSLARRDTGAYAPFAQVEVATGRVVGHTAYLTPRWMPDGRLFAVEVGSSWLSPTVRGTAVNPAAKLLLLAQALEDWGVDRVDIKTDARNEVARGAIAALGATFEGVLRAWQPSLAPGEEGRTRDTAMFAITPQQWPGVRTRLVERIERRSTSSKG$","Acetyltransferase, GNAT family","Cytoplasm","Acetyltransferases, including N-acetylases ofribosomal proteins","acetyltransferase; GNAT family","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[78-164]T$	Acetyltransf_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[18-201]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 18-114 are 60% similar to a (TRANSFERASE ACETYLTRANSFERASE GNAT FAMILY AMINO-ACID ACETYLTRANSFERASE SIMILAR PROBABLE RIBOSOMAL N-ACETYLASES) protein domain (PD949701) which is seen in Q9RDH2_STRCO.Residues 116-191 are 71% similar to a (TRANSFERASE ACETYLTRANSFERASE ACETYLTRANSFERASE FAMILY GNAT ACYLTRANSFERASE RIBOSOMAL-PROTEIN-ALANINE RIBOSOMAL 2.3.1.- N-ACETYLTRANSFERASE) protein domain (PD338839) which is seen in Q9RDH2_STRCO.","","-46% similar to PDB:1YRE Hypothetical protein PA3270 from Pseudomonas aeruginosa in complex with CoA (E_value = 4.1E_11);-38% similar to PDB:1H3N LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A SULPHAMOYL ANALOGUE OF LEUCYL-ADENYLATE (E_value = 4.1E_11);-38% similar to PDB:1OBC LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A POST-TRANSFER EDITING SUBSTRATE ANALOGUE (E_value = 4.1E_11);-38% similar to PDB:1OBH LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A PRE-TRANSFER EDITING SUBSTRATE ANALOGUE IN BOTH SYNTHETIC ACTIVE SITE AND EDITING SITE (E_value = 4.1E_11);-38% similar to PDB:2BTE THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION AND A POST-TRANSFER EDITING SUBSTRATE ANALOGUE (E_value = 4.1E_11);","Residues 78 to 164 (E_value = 0.016) place ANA_0631 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","including N-acetylases of ribosomal proteins","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0632","663892","664887","996","7.21","0.65","35030","ATGGTATTGCTTAATGAGGATTCGCTGCTGCGTGCCTCCCACCTGGTTCGCTCCTTCGGGAAAAAGGACAAAACCTTCGTCGCCGTGGAGGATGTGTCCCTGGACGTCGGGGCGGGGCAGGTCCATGGTCTGCTGGGGCCCAACGGTGCCGGTAAGACGACGACGGTGCGGATGTGCGCCACGCTGCTGGCTCCGACGTCGGGTGAGGTCTGGGTCGACGGCATCGATGCGGTGCGCCATCCGGAGCGGGCCAGGTCCCGGCTGGGCCTGGTCCTGGGCGGTGAGCTGGGGTTCTACCCGCGGGCTACGGCACGCGACAACCTGCTGTTCTTCGCCGACATTCAGGGTCTCGACGCCCGGCGGCGACACAGCGCGGTCATGGACGCCCTGGAGCGTGTGGGGCTGGTCGAGGCGGCGTCCCGGAAGACGGGCGAGCTGTCTCGAGGGATGCGGCAGCGTCTGCACCTGGCCCGGGCGCTGCTCGGGTCGCCGGCTCTTCTGCTGCTGGATGAGCCCACCACCGGCTTGGACCCGGACGTGGCGCTGCAGGTACGCGATCTGGTGCGTGAGCTGGCGCAGCGGGGAACGGGGGTGCTATTGACCTCGCACTCGATGCCGGAGGTCGAGGAGCTGGCCGACATCATCTCGGTGATCGGGGCGGGCCGGATCGTCGTGCGCGGCGGCGTGGGTGACGTGTCCGCCTTGGCCGGGGTGAGTGCCACCACGACTTTCACGTTACCGGCCCGCCACGGGGGCGCCGTCGAGGCGCTTCGCAGCGGTCTGGGGTCGCGGGCGACGGTGAAGCAGCGCGCCTCCTCGGCCCGGTGGGCCGTGACGGTCTACTGGGCTATCGAGGCGACCGGCACTACCGACGCCGACGAGCAGGTTCGCCAGGTCCTGGCCGAAGCCGGCGTGGGAGCGCCGTCTGACCTGCTGACGCGGCCGGTCTCCCTGGAGGAGGCCTACCTGGCCCTGGCCGACAGGCTCGCCCGATGA","MVLLNEDSLLRASHLVRSFGKKDKTFVAVEDVSLDVGAGQVHGLLGPNGAGKTTTVRMCATLLAPTSGEVWVDGIDAVRHPERARSRLGLVLGGELGFYPRATARDNLLFFADIQGLDARRRHSAVMDALERVGLVEAASRKTGELSRGMRQRLHLARALLGSPALLLLDEPTTGLDPDVALQVRDLVRELAQRGTGVLLTSHSMPEVEELADIISVIGAGRIVVRGGVGDVSALAGVSATTTFTLPARHGGAVEALRSGLGSRATVKQRASSARWAVTVYWAIEATGTTDADEQVRQVLAEAGVGAPSDLLTRPVSLEEAYLALADRLAR$","ABC-type multidrug transport system, ATPase component","Membrane, Cytoplasm","ATP-binding transport protein natA (Na(+) ABCtransporter)","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Tougu K., Peng H., Marians K.J. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 1994. 269(6):4675-4682. PMID: 8308039","","","

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[39-221]T$	ABC_tran
PS50893	$\"[10-245]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[38-230]T$	AAA

InterPro
IPR013173
Domain

DNA primase DnaG, DnaB-binding
SM00766	$\"[151-285]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[3-232]T$	no description
PTHR19222	$\"[10-224]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[10-224]T$	ABC TRANSPORTER

","BeTs to 18 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 6.8e-27. IPB005074C 28-75 IPB005074D 134-177***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 6.8e-23. IPB013563A 28-62 IPB013563C 143-170 IPB013563D 197-249***** IPB005116 (TOBE domain) with a combined E-value of 1.8e-14. IPB005116A 46-62 IPB005116C 146-159 IPB005116D 166-185 IPB005116E 199-212***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 5.1e-14. IPB010509B 39-64 IPB010509D 141-185***** IPB010929 (CDR ABC transporter) with a combined E-value of 4.1e-06. IPB010929K 26-70 IPB010929M 143-189 IPB010929A 38-57","Residues 7-142 are 53% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA188U2) which is seen in Q9RXA9_DEIRA.Residues 9-114 are 53% similar to a (ATP-BINDING NATA ABC TRANSPORTER) protein domain (PD742287) which is seen in O83851_TREPA.Residues 17-209 are 47% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 27-213 are 47% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 28-213 are 48% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 28-88 are 59% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 29-76 are 77% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9UZZ5_PYRAB.Residues 32-112 are 58% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 34-205 are 49% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 34-213 are 49% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 81-142 are 67% similar to a (COMPONENT ATPASE ATP-BINDING TRANSPORTER ABC) protein domain (PDA1B189) which is seen in Q74HR9_LACJO.","","-52% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 1.8E_23);-50% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 7.6E_19);-49% similar to PDB:1G29 MALK (E_value = 1.1E_17);-48% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 4.6E_16);-45% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 5.6E_14);","Residues 39 to 221 (E_value = 3.1e-51) place ANA_0632 in the ABC_tran family which is described as ABC transporter.","","transport protein natA (Na(+) ABC transporter) (extrusion)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0633","664884","665642","759","10.36","10.21","26804","ATGAGGCGTCAGGTGAGGATGACGGTCTTTCACGTCCGTCAGTTCGTGTCGGTTCCCTACTTCATCCAGCTCATGGTCATGACCACGACATCCACCACGCTGGTGCAGTTCCTGGCGGCCTCGGCATGGGGTGGGATCACCCCGACGCAGGGCTGGGTGCGCGGGGGCGTCGTGGGAATGTGGACGACGACGACCTGCGCGGCGGGGATCATTGGATTCGAGCGGTACAAGGGCACGCTGGTCCATCTGGTCATGGCTCCGGTGGGGGCGCTCAGGTCGTTGGCGGCCGTGGTGTGCGCGGCGGCGTCCTTCGGTCTGGTCGCCTTCCCGGTGGCGTGGTGCACGTGGGCGCTGCTGTCGACGTCAGTCTCCTTCACGGGGCCGGGGTGGGAGGTCTGGGCGCGCCTGACCGCAGGGGCCCTCATGCTGCTGGTCGGCTGCCTTGCCCTGAGTCTGGTCATCGCGGCGCTGTTCGTGCTCACCCCCAACGCGATCCAGTACGAGGGGCTGCTGCTGGTGCCGGTGCTCGTGGTCTCAGGCATCGTGTTCACCTCGACGACGCCGCCTGCCTGGCTGGCTGTGGTGAGTCGGTTCCTGCCGTTGTCGGTACCCTTCGAGCTGCTGCTGGGCCGGGCGACGTCGGCAGTGGCGCTGTGCGCTTGGCTGGTGTGCACGGCCGCGTGGCTGGGGCTTGCTGCCTTCCTCGGCCGGCGGGCGCTGCGTCTGGCGACACGGACCGGCACCTTGGAGGTGGTCTGA","MRRQVRMTVFHVRQFVSVPYFIQLMVMTTTSTTLVQFLAASAWGGITPTQGWVRGGVVGMWTTTTCAAGIIGFERYKGTLVHLVMAPVGALRSLAAVVCAAASFGLVAFPVAWCTWALLSTSVSFTGPGWEVWARLTAGALMLLVGCLALSLVIAALFVLTPNAIQYEGLLLVPVLVVSGIVFTSTTPPAWLAVVSRFLPLSVPFELLLGRATSAVALCAWLVCTAAWLGLAAFLGRRALRLATRTGTLEVV$","ABC-type multidrug transport system, permease component","Membrane, Extracellular","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[21-43]?$ $\"[53-73]?$ $\"[94-114]?$ $\"[140-160]?$ $\"[170-192]?$ $\"[215-235]?$	transmembrane_regions

","BeTs to 3 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","No significant hits to the Blocks database.","Residues 57-158 are 53% similar to a (ABC PERMEASE TRANSPORTER MEMBRANE ATP-BINDING TRANSPORTER TRANSMEMBRANE PROTEIN COMPONENT INTEGRAL) protein domain (PD115342) which is seen in Q74HS0_LACJO.","","-52% similar to PDB:1ZTM Structure of the Uncleaved Paramyxovirus (hPIV3) Fusion Protein (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0634","665642","666424","783","9.11","3.60","26763","ATGCGCGCCCGGGCTCTGGCCTTCGCCTACCGGTTCTCCTCAGGGGTGCGTGTCTCGTGGGCCTCGTCGACGGCCTTCGCGACTTTGGGTACGGCCGTGGTCACGCTGCTGGTGCTGCCGCTACTGGACGTGCTCTTCGATGTCCTCATGGGCTCGGACCTCTCCGCGCCTGACCTGGTGCGCACCGGATACGCAGCGGCCCTGGTGGCACTGGCCGTCTCGGTGGCCTCCGGAGTGGTGGGTACCGTGGCCACGGACCGGATGCTGGGCGTCTTCCAGGAGGTCCATACCCGCAGGCGCCTCGACGTCGCCTACTGGCTGTCCGTCGCCGTCGTGCCGGCGCTCCTGGCTGCCTCGACCGCCATCGTCGCGATCGGCGTCGTCTTCGCGCTCTCACCGCTGCACGACGTTGGAGCGCTGGGGCGTGTCATCACACTGGCAGCACCGACCATCGTGTGCGGGCTGCTCATGGGGATCATGGCCGCCGGTGTCGGAGTCAACCTGCCCGATCCCTATCTGGGTGCCACGATCATCGCCACGTTCCTGCCGCTGCTGACCGGCGTCATCGTACCGCTCGAGCAATGCCCTACCTGGTTGCAGGCTCTGGCCCACCTGGTTCCGCTCAGCGGCACCGTGACGGTCCTGGACGCACCGGCAGCCGCCGTTCCGGCCCTGCTGGGCCGCGACCTCGCGGTCGCCGCCGTATGGGCCGGGATCGGGCTGGCCGTCACCCGTCGTGCCGTCACCCGACTCCGTCAGGGCCAACGCACCGACATCATCTGA","MRARALAFAYRFSSGVRVSWASSTAFATLGTAVVTLLVLPLLDVLFDVLMGSDLSAPDLVRTGYAAALVALAVSVASGVVGTVATDRMLGVFQEVHTRRRLDVAYWLSVAVVPALLAASTAIVAIGVVFALSPLHDVGALGRVITLAAPTIVCGLLMGIMAAGVGVNLPDPYLGATIIATFLPLLTGVIVPLEQCPTWLQALAHLVPLSGTVTVLDAPAAAVPALLGRDLAVAAVWAGIGLAVTRRAVTRLRQGQRTDII$","ABC-type multidrug transport system, permease component","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","ABC-2 type transporter","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[10-220]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
signalp	$\"[1-51]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[60-82]?$ $\"[103-132]?$ $\"[146-166]?$ $\"[171-191]?$ $\"[225-243]?$	transmembrane_regions

","BeTs to 8 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 10 to 220 (E_value = 0.00045) place ANA_0634 in the ABC2_membrane family which is described as ABC-2 type transporter.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0635","666469","666927","459","5.94","-4.40","16901","GTGCTGCACGTCATCTTCTTTGAGCCGCGCATCCCGGGCAACACCGGGGCGGCGATCCGCCTGAGCGCCAACACCGGCTCCATGCTCCACCTGGTGGACCCCCTGTTCGACATGGACGACGCCAAGCTGCGCCGCGCCGGCCTGGACTACCACGACCTGGCCAACACGCGCGTCCACGCCACCTGGCAGGAGTGCCTCGAGCAGATCCCCGGGCGCATCTACGCCTTCACCTCCCACACCGACCGTCTCTACACCCAGGTCGACTGGCGCGACGACGACGCCCTCCTGTTCGGCCCCGAGCCCACCGGCTTGCCCCAGGAGATCCTCGACCACCCGCGAGTGAGCGCCCACCTGCGCATCCCCATGGTGGAGGGCAACCGCTCCCTCAACCTCGCCAACTCCGCCGCCATCGGCCTGTACGAGGCATGGCGGTCCCTGGGCTTCGCCGGAGGGGCCTGA","VLHVIFFEPRIPGNTGAAIRLSANTGSMLHLVDPLFDMDDAKLRRAGLDYHDLANTRVHATWQECLEQIPGRIYAFTSHTDRLYTQVDWRDDDALLFGPEPTGLPQEILDHPRVSAHLRIPMVEGNRSLNLANSAAIGLYEAWRSLGFAGGA$","tRNA/rRNA methyltransferase (SpoU)","Cytoplasm, Membrane","Predicted rRNA methylase (SpoU class)","tRNA/rRNA methyltransferase (SpoU)","tRNA/rRNA methyltransferase (SpoU)","","Persson B.C., Jager G., Gustafsson C. The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity. Nucleic Acids Res. 1997. 25(20):4093-4097. PMID: 9321663Koonin E.V., Rudd K.E. SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases. Nucleic Acids Res. 1993. 21(23):5519-5519. PMID: 8265370Sirum-Connolly K., Mason T.L. Functional requirement of a site-specific ribose methylation in ribosomal RNA. Science 1993. 262(5141):1886-1889. PMID: 8266080","","","

InterPro
IPR000568
Family

ATPase, F0 complex, subunit A
PS00449	$\"[16-25]?$	ATPASE_A

InterPro
IPR001537
Domain

tRNA/rRNA methyltransferase, SpoU
PD001243	$\"[2-147]T$	Q8FRV0_COREF_Q8FRV0;
PF00588	$\"[1-140]T$	SpoU_methylase

noIPR
unintegrated

unintegrated
G3DSA:3.40.1280.10	$\"[1-150]T$	no description
PTHR12029	$\"[2-144]T$	RNA METHYLTRANSFERASE
PTHR12029:SF11	$\"[2-144]T$	23S RRNA METHYLTRANSFERASE

","BeTs to 13 clades of COG0219COG name: Predicted rRNA methylase (SpoU class)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0219 is ---------drlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is 1","***** IPB001537 (tRNA/rRNA methyltransferase (SpoU)) with a combined E-value of 3.3e-16. IPB001537A 4-28 IPB001537B 95-135","Residues 2-147 are 74% similar to a (METHYLTRANSFERASE TRANSFERASE RRNA METHYLASE TRNA/RRNA 2.1.1.- RNA FAMILY SPOU METHYLTRANSFERASE) protein domain (PD001243) which is seen in Q8FRV0_COREF.","","-67% similar to PDB:1J85 Structure of YibK from Haemophilus influenzae (HI0766), a truncated sequence homolog of tRNA (guanosine-2'-O-) methyltransferase (SpoU) (E_value = 3.7E_35);-67% similar to PDB:1MXI Structure of YibK from Haemophilus influenzae (HI0766): a Methyltransferase with a Cofactor Bound at a Site Formed by a Knot (E_value = 3.7E_35);","Residues 1 to 140 (E_value = 9e-41) place ANA_0635 in the SpoU_methylase family which is described as SpoU rRNA Methylase family.","","rRNA methylase (SpoU class)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0636","667812","666949","864","8.78","3.39","30492","GTGAGCCCACAGATCGCCCAGGTCGACGCCTCGTCCTCCAAGGCGGGCCGGCGTCGCCGTCAGGGGGAGTCCGTCCCCTTCACCCCCGCTCACGGTTTCACACGCGCCGGCTCCGGCCGCCACCAGCGCCGCCCCATCGCCCTGATCACCGGGGCGACCTCCGGGATCGGCCTGGCCGTGGCCAGGGACCTGGCCCGGGACCACGACCTCATCCTGCTGGCCCGTTCCGTCAACGACCTGGAGGAGCTGGCGCTCGCGCTGGAGGAGGAGTCCCAGACGGCGGTCCTCATCTGCCCGGTCGACCTGACCGACGACACGGCCCTGACCAGGCTGGTCAGCCGGATCGACATTGAGAGCCTCGACGTGCTGGTGCACAGCGCCGGCATGGAGGCGCCCGGTGCCGTTGACAAGATCACCCCCACGCGTTGGCGGGCGGTTCTCAACCTCAACCTGGTGGCGACGGCGTATCTGACGAGCCTGCTGCTGCCGGCGCTGCGGGAGGCGCGCGGACTGACGGTGTTCATCAACTCCGGCGCCGGGGTGAGCCCACGGTCGGGCAACGCCCTCTACTCCGCCTCCAAGGCGGGGCTGAAGTCCCTGGCCGACACGCTGCGCCAGGAGGAGGCGGGCAAGGTGCGGGTCACCTCGATCTACCCGGGCCGGGTGGACACCCCTATGCAGGAGCGTCTGCACGCCTTCAATGCGGCACGCCTGCGCACCGAGGGGATCATGGCCACCCCCGCATACAGGGCTGCGGACCATATGGCGCCGCAGTCGGTGGCCGCGGCCGTGCGCCTGGCCGTCAACACCCCGATGGACGCGGTCGTGGAGGACCTGGCGATCCGCCCCGCCGGCATGCTCTGA","VSPQIAQVDASSSKAGRRRRQGESVPFTPAHGFTRAGSGRHQRRPIALITGATSGIGLAVARDLARDHDLILLARSVNDLEELALALEEESQTAVLICPVDLTDDTALTRLVSRIDIESLDVLVHSAGMEAPGAVDKITPTRWRAVLNLNLVATAYLTSLLLPALREARGLTVFINSGAGVSPRSGNALYSASKAGLKSLADTLRQEEAGKVRVTSIYPGRVDTPMQERLHAFNAARLRTEGIMATPAYRAADHMAPQSVAAAVRLAVNTPMDAVVEDLAIRPAGML$","Short-chain dehydrogenase/reductase SDR","Cytoplasm, Membrane","oxidoreductase, short-chaindehydrogenase/reductase family","short chain dehydrogenase","short-chain dehydrogenase/reductase SDR","","Jornvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 1995. 34(18):6003-6013. PMID: 7742302Villarroya A., Juan E., Egestad B., Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 1989. 180(1):191-197. PMID: 2707261Persson B., Krook M., Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 1991. 200(2):537-543. PMID: 1889416Neidle E., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 1992. 204(1):113-120. PMID: 1740120Benyajati C., Place A.R., Powers D.A., Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 1981. 78(5):2717-2721. PMID: 6789320","","","

InterPro
IPR000568
Family

ATPase, F0 complex, subunit A
PS00449	$\"[261-270]?$	ATPASE_A

InterPro
IPR002198
Family

Short-chain dehydrogenase/reductase SDR
PR00080	$\"[118-129]T$ $\"[190-209]T$	SDRFAMILY
PTHR19410	$\"[41-285]T$	SHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106	$\"[45-209]T$	adh_short
PS00061	$\"[177-205]T$	ADH_SHORT

InterPro
IPR002347
Family

Glucose/ribitol dehydrogenase
PR00081	$\"[46-63]T$ $\"[118-129]T$ $\"[164-180]T$ $\"[190-209]T$ $\"[210-227]T$	GDHRDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[43-271]T$	no description
PTHR19410:SF16	$\"[41-285]T$	3-OXOACYL-[ACYL-CARRIER PROTEIN] REDUCTASE-RELATED

","BeTs to 17 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 4","***** IPB002347 (Glucose/ribitol dehydrogenase family signature) with a combined E-value of 4.6e-23. IPB002347A 46-63 IPB002347B 118-129 IPB002347D 190-209 IPB002347E 210-227***** IPB002198 (Short-chain dehydrogenase/reductase SDR) with a combined E-value of 2.6e-12. IPB002198A 120-129 IPB002198B 170-218***** IPB003560 (2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature) with a combined E-value of 1.8e-08. IPB003560A 51-68 IPB003560B 121-138 IPB003560D 204-227","Residues 157-207 are 76% similar to a (OXIDOREDUCTASE DEHYDROGENASE REDUCTASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY CHAIN SHORT PROBABLE OXIDOREDUCTASE) protein domain (PD003795) which is seen in Q9Z587_STRCO.Residues 208-283 are 60% similar to a (DEHYDROGENASE CHAIN SHORT) protein domain (PDA118R2) which is seen in Q6A722_PROAC.","","-49% similar to PDB:2JAH BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE CLAVULANIC ACID DEHYDEOGENASE (CAD) FROM STREPTOMYCES CLAVULIGERUS (E_value = 9.3E_23);-49% similar to PDB:2JAP CLAVULANIC ACID DEHYDROGENASE: STRUCTURAL AND BIOCHEMICAL ANALYSIS OF THE FINAL STEP IN THE BIOSYNTHESIS OF THE BETA-LACTAMASE INHIBITOR CLAVULANIC ACID (E_value = 9.3E_23);-46% similar to PDB:1XG5 Structure of human putative dehydrogenase MGC4172 in complex with NADP (E_value = 2.0E_17);-45% similar to PDB:2BD0 Chlorobium tepidum Sepiapterin Reductase complexed with NADP and Sepiapterin (E_value = 2.5E_15);-48% similar to PDB:2D1Y Crystal structure of TT0321 from Thermus thermophilus HB8 (E_value = 1.3E_13);","Residues 45 to 209 (E_value = 1.2e-35) place ANA_0636 in the adh_short family which is described as short chain dehydrogenase.Residues 48 to 209 (E_value = 2.2e-06) place ANA_0636 in the KR family which is described as KR domain.","","short-chain dehydrogenase-reductase family (AE005204)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0637","668384","667809","576","4.47","-15.68","19992","ATGACAGCCGACCTCACTCGCCCCCGCCCGCCGGCCCCTACCGGCCTCCTGCCCTCAGTCCCCTCCTTCACCCTGACCTCTGCGGATCTGACCGAGCAGGGGCGGATTCCGGACATCTTCACTGGCATCCATGACAACGTCTCCCCCGCCCTGAGCTGGTCGGGCTTCCCCGAGCAGACGCAGTCCTTCGTCGTATCCTGCTTCGACCCGGACGCTCCGACCATGTCGGGCTGGTGGCACTGGACCATCGTGGACCTGGACGCCTCGGTCACCTCGCTGGAGCGGGGCGCGGGGGCCAGCGACCTTCAGCTCGACGGTGCCGCCTTCCACCTGGCCGGGGACTCGGGCGATCACGCCTGGCTCGGTCCCTGCCCGCCTGCGGGCGACGGCGACCACCGCTATGTCTTCACCGTCTCCGCTCTGGACGTGGACACGCTGGGGCTGGACGACGAGGCCAGTCCCGCCATGGCGGCCTTCACCCTGGCACCGCACTGCATCGCCCGGGCCACGCTCACCGCCACCTACTCCGTGCCCGGGGAGCCCGGGGCCGCCGCCTTCCTCAGGGACGGCCAGTGA","MTADLTRPRPPAPTGLLPSVPSFTLTSADLTEQGRIPDIFTGIHDNVSPALSWSGFPEQTQSFVVSCFDPDAPTMSGWWHWTIVDLDASVTSLERGAGASDLQLDGAAFHLAGDSGDHAWLGPCPPAGDGDHRYVFTVSALDVDTLGLDDEASPAMAAFTLAPHCIARATLTATYSVPGEPGAAAFLRDGQ$","Phosphatidylethanolamine-binding protein","Cytoplasm, Extracellular","Ybhb","hypothetical protein","PEBP family protein","","Vallee B.S., Coadou G., Labbe H., Sy D., Vovelle F., Schoentgen F. Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo. J. Pept. Res. 2003. 61(2):47-57. PMID: 12492898Hengst U., Albrecht H., Hess D., Monard D. The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. J. Biol. Chem. 2001. 276(1):535-540. PMID: 11034991Banfield M.J., Brady R.L. The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator. J. Mol. Biol. 2000. 297(5):1159-1170. PMID: 10764580Corbit K.C., Trakul N., Eves E.M., Diaz B., Marshall M., Rosner M.R. Activation of Raf-1 Signaling by Protein Kinase C through a Mechanism Involving Raf Kinase Inhibitory Protein. J. Biol. Chem. 2003. 278(15):13061-13068. PMID: 12551925Yeung K.C., Rose D.W., Dhillon A.S., Yaros D., Gustafsson M., Chatterjee D., Mcferran B., Wyche J., Kolch W., Sedivy J.M. Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation. Mol. Cell. Biol. 2001. 21(21):7207-7217. PMID: 11585904","","","

InterPro
IPR005247
Family

YbhB and YbcL
TIGR00481	$\"[27-175]T$	TIGR00481: conserved hypothetical protein T

InterPro
IPR008914
Family

PEBP
PD004330	$\"[49-136]T$	Q9VD02_DROME_Q9VD02;
PF01161	$\"[28-178]T$	PBP

noIPR
unintegrated

unintegrated
G3DSA:3.90.280.10	$\"[23-175]T$	no description

","BeTs to 15 clades of COG1881COG name: Phospholipid-binding proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1881 is aompk-yq--r-b-e-ghsnuj-i-wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 46-164 are 64% similar to a (UPF0098 YBHB PHOSPHOLIPID-BINDING PLASMID YBCL MEMBRANE COLD OUTER REGULATED SMB20703) protein domain (PD006154) which is seen in Q829C7_STRAW.","","-59% similar to PDB:1VI3 Crystal structure of an hypothetical protein (E_value = 3.8E_31);-60% similar to PDB:1FJJ CRYSTAL STRUCTURE OF E.COLI YBHB PROTEIN, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY (E_value = 1.5E_30);-57% similar to PDB:1FUX CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY (E_value = 1.2E_27);","Residues 28 to 178 (E_value = 1.9e-10) place ANA_0637 in the PBP family which is described as Phosphatidylethanolamine-binding protein.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0639","668615","669529","915","6.11","-1.63","31408","ATGAGAGCCTCGATCACGCGCGCGCCAGCGGAGGCTCAGAACCGCCTCGATCGGGCCCGCCTCGCCCTGAGGCTGGCCGAGGAGCGCACCGGACTGCGCGACTCAGCAGCCCTGACGGTGCAGCGCGCCCTGTCCTCGGCATCAACCAGCGCCCTGCTGAGCACATCAGCCGACTCGCCTCAGGCCGGCTCCTCCGCATCCCCCGCACCCCCTGCGGCGCTCTCGGCATGTCAGGACTCCGGCGTCCTCACCCTCCGCGGATCCACCACCCTCCTCCTGGCCGCCCTCGCCCTGCGCCAGGGCGCCACCGGCTGGTGCGGCGTCATCGGGGGAGACGAGCTGGGGTGGTGCGCAGCCATCGAGGTCGGCCTCGACCTCAACCGGGTCCTCGCCGTTCCAGCCCCCCTCCTCGATGACGCCTCGACCCTGACAGTCACCTCCACGCTGCTCGACGGCGTCGACACCCTCCTCATCGGTGCCCCCGTCGCCGAAGGCCTGCGCCCCCAGTACCGCAGACGCCTGCTGTCCCGAGCACGCGAACGCGGCCACCTCATTCTGACCCCCGCTCGTTGGGAAGGCGCCCGCATCCTCCGAGCCGATGCCCTGGCCCCCGACACTGGAACCAGCAACACGCCTCCCGCCCAGGCCCCGGCGGAGGCCCCCGCAGAGCCCTCCGCCGACGGCGTCGTCATCCCCATCGGGCGAGGAGCCTCACCCGCCCCGGTGCGAGCCATCGAGATGCCGGCTGGATACCTGCAACGCCTCACCTGGACCCTGGCCGACCCGCAGCGCCCACGGCTCGCCCCCACCGAAGAGCTCACGCTCTCACTGTCCGCCGAAGGGCTGCGCACAGGCTCCCGCAACGCCGCCGACACCGCCGACCCGACCTCCCACCCGCAGGAGGTGGCCGGATGA","MRASITRAPAEAQNRLDRARLALRLAEERTGLRDSAALTVQRALSSASTSALLSTSADSPQAGSSASPAPPAALSACQDSGVLTLRGSTTLLLAALALRQGATGWCGVIGGDELGWCAAIEVGLDLNRVLAVPAPLLDDASTLTVTSTLLDGVDTLLIGAPVAEGLRPQYRRRLLSRARERGHLILTPARWEGARILRADALAPDTGTSNTPPAQAPAEAPAEPSADGVVIPIGRGASPAPVRAIEMPAGYLQRLTWTLADPQRPRLAPTEELTLSLSAEGLRTGSRNAADTADPTSHPQEVAG$","Hypothetical protein","Periplasm, Membrane","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0640","671934","671191","744","9.83","6.31","26085","ATGCTCTCACTCGACCACCTGCCTCACACCTGGCGCACCAGGCAAGCCGGCACGCTGGCCGCAACCGCCGTCATCACGCTGTCGCTGTTCTCCTGGCTGGCCCTGACCACGAACTCCGGAACGGGGCTGGCGCCTCACGACCAGAGCGTCACCACCTGGGCCGTGGACGAGCGCATCCCGGCCCTGACCGTCATCATGCAGGTGTTCACCGCCCTGGGCTCCACCGTGGGGCTGACGATCCTGACCGCGATCTGTGCTGTCCTCCTCTTCATGAGGGGCCACCGCGTGCGAGCACTAGTCCTGAGCCTCACGATGATCGGCTCCAGCCTGTTGACGGTGGCGCTCAAAGAGTTCTTCAGGCGTGCACGCCCCTCAACCGACACCCTTCTAGGCGAGCCCGCCTCAACCACCTCTTTCCCCTCGGGGCACTCCTTCAACACGGCTGTCTTCGCCGGCCTGCTAGCGGGGATGGTCCTGGCATCCACGGCGTCGATCCTGTACCGGGCCTTAGCGATCATGGCGGCGGCGGGGGCGACCCTGCTGGTGGGGGCATCCCGCGTCTACCTGGGCTACCACTGGATGACCGATGTTCTAGCCGGCTGGTCCCTGGGGCTGGCCTGGCTGTGCCTGGTGACGCTGGCGCTCCTGTGGCTGAAGGGACGACGGCGCCCGACCCCACCTCTTGCGACCGCATCATCGGACAGCTCCTCAGGAGTAGAGGGCATCGAGCCACCACCGGCCTGA","MLSLDHLPHTWRTRQAGTLAATAVITLSLFSWLALTTNSGTGLAPHDQSVTTWAVDERIPALTVIMQVFTALGSTVGLTILTAICAVLLFMRGHRVRALVLSLTMIGSSLLTVALKEFFRRARPSTDTLLGEPASTTSFPSGHSFNTAVFAGLLAGMVLASTASILYRALAIMAAAGATLLVGASRVYLGYHWMTDVLAGWSLGLAWLCLVTLALLWLKGRRRPTPPLATASSDSSSGVEGIEPPPA$","Membrane-associated phospholipid phosphatase","Membrane, Extracellular","membrane-associated phospholipid phosphatase","phosphoesterase; PA-phosphatase related","phosphoesterase, PA-phosphatase related","","","","","

InterPro
IPR000326
Family

Phosphoesterase, PA-phosphatase related
PF01569	$\"[97-220]T$	PAP2
SM00014	$\"[98-212]T$	acidPPc

noIPR
unintegrated

unintegrated
G3DSA:1.20.144.10	$\"[98-210]T$	no description
PTHR14969	$\"[86-215]T$	SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE
PTHR14969:SF3	$\"[86-215]T$	SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE (PAP2 FAMILY PROTEIN)
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[70-90]?$ $\"[99-119]?$ $\"[147-167]?$ $\"[172-192]?$ $\"[198-218]?$	transmembrane_regions

","BeTs to 15 clades of COG0671COG name: Membrane-associated phospholipid phosphataseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0671 is -om-k-yq-drlbcefghs-ujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB000326 (PA-phosphatase related phosphoesterase) with a combined E-value of 1.2e-15. IPB000326A 138-145 IPB000326B 185-204","Residues 47-155 are 46% similar to a (PHOSPHATIDYLGLYCEROPHOSPHATASE B-RELATED) protein domain (PD258164) which is seen in Q9RUM9_DEIRA.","","No significant hits to the PDB database (E-value < E-10).","Residues 97 to 220 (E_value = 2.9e-26) place ANA_0640 in the PAP2 family which is described as PAP2 superfamily.","","phospholipid phosphatase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0641","669526","671226","1701","6.27","-5.97","60472","ATGAACCCGCCACAACCGCCCTCGCCGGCCGGCCCACCCGCCTCCAGATTCGTGGCCATCTGGGTCCCCGACTGGCCCGTCGTTGCCCTCACCATGGAGACCCGCCAGCAGCATCGACACCCCCGAGCGCGCCAAGGAACCCCCCACCTGCCGGACCCGGCCACCGAACCTGTCGCCGTCGTCGGCGCTCGCGGAGTCCTCGCCGCCTCGGCCCCGGCCCGCCGTGCCGGCATCACCACCGGCATGCGACTGCGTACCGCCCGCTCCCTGTGCCCCGAGCTCACCGTCCTGCCTCCCCAGGAGGAACGCCAGGCCCGCGCCTTCGAAACCGTCATGGAGGCCCTCACCTCCCTCCTGGCGGACCCCATGGTGGCCCGCCCCGGACTGGCCCTGTCCCACGTCAGAGGTCCCGCAGCCTGGATCGGCGGGGAAGAACCCCTCGCCTCAGCCCTCGTGGAGACCGTCACCCAGGAGGCCGACGTCGAGTGCCAGGTCGGCATCGCCGACTCCCTGCCCGGAGCCGTCCTGGCCGCCCGCCAAGGAATCATCGTCGAACCGGGACGGACCCCGGAGTTCCTCGCCCCCTGGCCCCTGGACGCACTCCTGACCTGCCTGCCCCTCAGCCGCCTGCGGCGCGACGCCCGCCCCATGCTGGAGAGCTTCTCCCGACTCGGCCTGCGCACCTTGGCGGACCTGGCGGCCCTGCCCAGAAAAGACGTCACCGCCCGCTTCGGCCCCCTGGGGAACAGGCTCCACCACCTGGCCGCCGGCACCCACCACGAGGTCCCCGCCATACCCCGGCCGGCCCAGGACATCACCGTCACCTCCGACCTCGACCCTCCCGTCGAACGCGCCGACACCGCAGCCTTCGCCGCCCGCCACCTCGCCGAGAACCTGGCGGCGCACCTGTTGTCCGCAGGCCTTTCCGTCGGACGCCTCTGCGTTGCCGCCCGCTGCGAGGACGGCACCGACCTGGCCCGAAGCTGGATGCTGGAGGACACCCCCACCCCCGCCGAGCTCACCGACCGCGTGCGCTGGCAGCTCGAGGGATGGCTCTCCGGACGATCCGGGCGCCCACCCTCCTCCGGCCTGACCCACCTGAGCCTGACAGCCCTCGAGCTGAGCCCCGCCACGACCTCCCAGGCAGGACTGTGGCAAGCGCCGGGCCACCAGGCCCAGTCGCGCGCCCGCCGCGCCGCCGAGCGCGTGGAGTCACTCCTGGGGGCCGGAAGCGTCCAGGTTCCCAGGATCGTTCCCGGGCGCGACCCGCGCTCGCGGGTTCGCCTCATCCCCTGGGGTGAGAGCGAAGGCGTAGGGGAGTCCACGGGTGATGAGACAGCGCCCTGGAGCGGCGCTCTGCCCGAGCCCTCACCCTCCATCGTCCTGCCCCGACCGGTTCCTGCGCGTCTCACCGACATTGAGGGGAGAGAGCTCGGCGTCGACATCCATGGTCAGCTCGACGGTGTCCCCGGCTTCCTCAGTGTCGACGACGGCGTGGTTGGCGTTGATGAGGGTGCTGTGGGGACTGGGCCCCAGATGGAGGCCGTGCTCCTGTGGGCCGGGCCCTGGCCGGTCGACGAGGGGTGGTGGACCTCCCAGGGGCCGTCGCGACGCGCCTACCTCCAGGTGGTCACCGACGTCGGGCCGCCCCGCCTGCTGGTGCGATCAGGCCGGTGGTGGCTCGATGCCCTCTACTCCTGA","MNPPQPPSPAGPPASRFVAIWVPDWPVVALTMETRQQHRHPRARQGTPHLPDPATEPVAVVGARGVLAASAPARRAGITTGMRLRTARSLCPELTVLPPQEERQARAFETVMEALTSLLADPMVARPGLALSHVRGPAAWIGGEEPLASALVETVTQEADVECQVGIADSLPGAVLAARQGIIVEPGRTPEFLAPWPLDALLTCLPLSRLRRDARPMLESFSRLGLRTLADLAALPRKDVTARFGPLGNRLHHLAAGTHHEVPAIPRPAQDITVTSDLDPPVERADTAAFAARHLAENLAAHLLSAGLSVGRLCVAARCEDGTDLARSWMLEDTPTPAELTDRVRWQLEGWLSGRSGRPPSSGLTHLSLTALELSPATTSQAGLWQAPGHQAQSRARRAAERVESLLGAGSVQVPRIVPGRDPRSRVRLIPWGESEGVGESTGDETAPWSGALPEPSPSIVLPRPVPARLTDIEGRELGVDIHGQLDGVPGFLSVDDGVVGVDEGAVGTGPQMEAVLLWAGPWPVDEGWWTSQGPSRRAYLQVVTDVGPPRLLVRSGRWWLDALYS$","Nucleotidyltransferase/DNA polymerase involved in DNA repair","Cytoplasm, Membrane","conserved hypothetical protein","hypothetical protein","Nucleotidyltransferase/DNA polymerase involved in DNA repair-like","","Smith B.T., Walker G.C. Mutagenesis and more: umuDC and the Escherichia coli SOS response. Genetics 1998. 148(4):1599-1610. PMID: 9560379","","","

InterPro
IPR001126
Domain

UMUC-like DNA-repair protein
PF00817	$\"[51-103]T$	IMS
PS50173	$\"[44-180]T$	UMUC

noIPR
unintegrated

unintegrated
PTHR11076	$\"[49-257]T$	DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER

","BeTs to 5 clades of COG0389COG name: Nucleotidyltransferase/DNA polymerase involved in DNA repairFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0389 is -o----y---rlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 73-194 are 59% similar to a (PLASMID INVOLVED DNA POLYMERASE REPAIR TRANSFERASE NUCLEOTIDYLTRANSFERASE/DNA BLR3025 AGR_L_3171P XAC1198) protein domain (PD416429) which is seen in Q7TWK0_MYCBO.Residues 224-565 are 50% similar to a (INVOLVED DNA POLYMERASE REPAIR CGL0617 MB3426C TRANSFERASE UMUC NUCLEOTIDYLTRANSFERASE/DNA) protein domain (PD607750) which is seen in Q73U81_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 51 to 103 (E_value = 8.2e-10) place ANA_0641 in the IMS family which is described as impB/mucB/samB family.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0642","672082","672729","648","5.54","-3.70","23754","GTGGCCAAGCTCTACTTCCGCTACGGCGCCATGAACTCCGGTAAGTCCACGGGGCTGCTCCAGACCGCCTACAACTACGAGGAGCGCGATCAGCGCGTCCTGCTCCTCAAGGCGGTGGTCGACACCAAGGGTGAGGACTCAGTGGTCTCCCGGCTCGGGGTGTCGCGCCGCGTTGACCTCCTCGTCGACGCCGACGACGACCTGCGCGCCCTGGTGCACCGGCGGGCCCTGAGCGGTGCGCGGCCCGTCCGCGACGAGGACGGCGTCCCGCGAGAGGCGGCGACATTGCGTGAGGTTCTTGACTGCGTGCTCATCGACGAGGCTCAGTTCCTCACGGCCCTTCAGGTGGACCAGCTCATGGAGATCGCGCTGATCGACGACGTGCCCGTCCTGGCCTACGGGATCCGCACCGACTTCCGCACAGTCAGCTTTCCCGGGTCGCGCAGGCTACTGGAGATCGCCCACTCCCTGGAGGAGCTCAAGACCATCTGCCGCTGCGGGCGCAAGGCCATCTTCAACGCCCGCAAGGTGGGGGAGTCCTTCGTCTTCGACGGCGATCAGGTGGCCATCGACTCCGGGGACGTCACGTATGAGTCATTGTGCGGCCAGTGCTACCTCGCCGCCGGTGGGAGGCTTCCTGGCAGGTAG","VAKLYFRYGAMNSGKSTGLLQTAYNYEERDQRVLLLKAVVDTKGEDSVVSRLGVSRRVDLLVDADDDLRALVHRRALSGARPVRDEDGVPREAATLREVLDCVLIDEAQFLTALQVDQLMEIALIDDVPVLAYGIRTDFRTVSFPGSRRLLEIAHSLEELKTICRCGRKAIFNARKVGESFVFDGDQVAIDSGDVTYESLCGQCYLAAGGRLPGR$","Thymidine kinase","Cytoplasm","thymidine kinase","thymidine kinase ","Thymidine kinase","","Boyle D.B., Coupar B.E., Gibbs A.J., Seigman L.J., Both G.W. Fowlpox virus thymidine kinase: nucleotide sequence and relationships to other thymidine kinases. Virology 1987. 156(2):355-365. PMID: 3027984Blasco R., Lopez-Otin C., Munoz M., Bockamp E.O., Simon-Mateo C., Vinuela E. Sequence and evolutionary relationships of African swine fever virus thymidine kinase. Virology 1990. 178(1):301-304. PMID: 2389555","","","

InterPro
IPR001267
Family

Thymidine kinase
PTHR11441	$\"[2-83]T$ $\"[101-212]T$	THYMIDINE KINASE
PF00265	$\"[2-205]T$	TK

","BeTs to 7 clades of COG1435COG name: Thymidine kinaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG1435 is -o-p----vd-lb-e-gh---j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB001267 (Thymidine kinase) with a combined E-value of 8.1e-35. IPB001267A 9-21 IPB001267C 99-111 IPB001267D 115-164 IPB001267E 191-205","Residues 100-175 are similar to a (KINASE TRANSFERASE DNA ATP-BINDING SYNTHESIS THYMIDINE CYTOSOLIC KINASE PHOSPHORYLATION KINASE-THYMIDYLATE) protein domain (PD002207) which is seen in Q6AGX9_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 205 (E_value = 1.6e-33) place ANA_0642 in the TK family which is described as Thymidine kinase.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0643","672827","673555","729","6.66","-1.34","26309","TTGGGTCATTACAAGCACTATCGTGAAGCCGTGAATGCTTCCTACGCACTCATCGCAGACATCATCCGCTCGCGTGAGCTCCCTGATCGCAGGCGTGCTCAGCGCGTCATCCACGAGACTCTGGATCGGGCCGCTGAAGGGCTGAAGCTGACGCAGCGCCCGTACGCCACGGTTGGTGACGAGCTGCAGGCAGTCTCGGCGACCCTTGCCGACGCTCTCGCTCTCACCATGCGTACACACCTTCTTCTGCCTGATGGCTTAGGCCTGCGCTTCGGAATCGGAGTCGGAGCGATCTCCGAGGTGGAGGGGGCGGCGGGAAGCGGTGCAGACGGTGCGCCAGGACGTCCGATCCAGGACGGCTCGGCATGGTGGGCCGCACGCGAAGCCATCGAGAAGGCTCATCATCTCCAGGATGAGGGGAGGTCCTTCATTCGCACCTGGCTGCGCATCCACCCGGATGCGGTCGGCGGATCCGGAGGGGAGTGGAGTGAACGTGAGGAGTTCGTCAACTCCGTCCTCATCCTGCGAGACCAGGCGGTATTCCGCTTTCAGCCCCGTCAGCGCCGCATTATGGCCGGACTCCTCATGGGGGTGACCCAGGTTGAGATCGCCCGCCAGGAGAAGGTGAGTCAGCAAGCCGTCTCAGAATTCGCTCGCGGTGCCGGTTCCTCCTTGCTGGAGGTTCAAAAGCTTCTCGACGGGTTGAGTGGGGGAGGTGAAGGAGAATGA","LGHYKHYREAVNASYALIADIIRSRELPDRRRAQRVIHETLDRAAEGLKLTQRPYATVGDELQAVSATLADALALTMRTHLLLPDGLGLRFGIGVGAISEVEGAAGSGADGAPGRPIQDGSAWWAAREAIEKAHHLQDEGRSFIRTWLRIHPDAVGGSGGEWSEREEFVNSVLILRDQAVFRFQPRQRRIMAGLLMGVTQVEIARQEKVSQQAVSEFARGAGSSLLEVQKLLDGLSGGGEGE$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 17-226 are 47% similar to a () protein domain (PDA043A1) which is seen in Q743S9_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0644","673552","674358","807","9.54","7.78","27950","ATGATTTCCCTGTTCCTCCTTCTGTTTGCTGCCGCCTCCGTGGTTGTCGACTCCGACCGGGTGAGTGGGGGATTGTCCAGGAGGTCCGCCGGGGCGAGACTTCTGGTGGGAGTGCCTGCAGTCGTTGCTCTTGGCGTCCTGGTCGGGTGGCCCGTTCTTCATCTCGGGGCGGGAGGTGTTGTCGTCAGCGTTCTGGTAGCCACTGCATGGTTGTGCTGCGGCCTGGTTTCGCAGGTCTGGTGGGACAAATCGTTGAGGGCCTATCAGCGGAAGCGGCTGGGGTGGAGTGTCTCTGAGGGCGGTGAGGGGCGGCTGGGGCCGTTCATCCGGCTTGTCCATGCGGGTCTGTTGCTCCTCGCCGTGGGGCTCTGTGTCGTCGCGTCGCAGCCGCTTGGATCTCGGGCTGCCAAGATGAGCGCTGTCGTCGGAGTGGTCGTCCTTCTGACTGTTCCTGCCAATCGAGTCGTCGCCGACATTCTTGCTGTTGCGCGCCACTCCTCGCAGCGTGACGTAAAAGCTGTTGCGGTTGGTTGTGAGCTCTCGCAGGAGAGCGGGAAGCAGGATGAGATGGAGGGCTCGATGCGCGGCGGTCGCTGGATCGGTCCGCTTGAGCGAATCCTCATTCTCCTGCTCGCCTCTGTTGAGGCGCCCGCCGCTATTGCCGCAATTGTTGCCGCCAAGGGTGTGATCCGATTTCCCGAGATCAGTCAGGATAAGGCGGGGCAGAAGGCTGAGGAGTTCCTCATCGGCTCCTTCGTCTCCTGGATCCTGGCGGTCTTGGGTGCTGTGATCATTCACTTCGCCTGA","MISLFLLLFAAASVVVDSDRVSGGLSRRSAGARLLVGVPAVVALGVLVGWPVLHLGAGGVVVSVLVATAWLCCGLVSQVWWDKSLRAYQRKRLGWSVSEGGEGRLGPFIRLVHAGLLLLAVGLCVVASQPLGSRAAKMSAVVGVVVLLTVPANRVVADILAVARHSSQRDVKAVAVGCELSQESGKQDEMEGSMRGGRWIGPLERILILLLASVEAPAAIAAIVAAKGVIRFPEISQDKAGQKAEEFLIGSFVSWILAVLGAVIIHFA$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[34-54]?$ $\"[60-80]?$ $\"[111-131]?$ $\"[206-226]?$ $\"[247-267]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0645","674804","677425","2622","6.07","-16.37","89375","ATGTTCGAAGGCGGTGTGCTTCCTCGTGTCCCGGCCGGTGGTGCGGCCGGGACACTGAGTGCGCCTGCCCAGGACGCGTCGGCGGGGGCTGTGACCTGCACTGAGGACGTGGTGGGTCTGCTGGGGTCCTTGGCCGGCGGTGGAGCGCTGGCCGGTGTGGTCGAGGGGCTGCTGTCCCGGCTGCTGGTCACCGCCCAGAACCACCACCACGACGACGGCGATGGCGATGGCGGCGGCGTCGGTGGTGAGGGCTCTGATGCTGAGAGCGCCGGCAGTGCTGATGGTGAGGGCTTGTTCGCAGGCGATTCGGACGCTGACGCGACGCTGGTGGCCGCTGCTGATGGACACAGGGTCGTGTCTCTGGAGGAGGTCGGTGCTACTGGGCTGCTTGGCCTGGGAGCACGGGGTCTGGGGGAGCTGGCCGCGGCCTGCCACCGCCTGGCGGCCTGGGCCGCGTGGGGTGAGTCCCTGGCGGCGGCGTGCCTGACCGGGTGCGCCGAGCTGTCGACGCATCCGGATCAGTGGGGCCCGGGCGGTCGGGTCTCACCGGTGGTGGGGTTTGAGGAGCGGCGGTTCAACACCACCTGCCTGCTATCGGCCCGCCTGGGGGTATCCCGGAGTCGGGCCGGGCAGATCGTGGACCACGGCAGCGCCCTGATGGACATGGGGTTCGGGCCCACCGAGGCCATGGAGCGGTGCGGGGTACTGGATGCAGCCAAGGCGTCCTTAGTGACTCGCCGCCTGGGAGACGTACCGGCTCCGGTGGCACTGGCCGTTCAGGAGCAGGTCCTGCCTCAGGCGCCTAGGCGCAGCGTGTCCCAGGTAGGACGCGACATCGAGCGGGCCCTAATGGAGACAGACCCCGACGGACACGCTGAGCGGGTGCGAGTCAATGTCTCCCGGCGGTGCGTGACGCGTCCCAGGCCCGCTGGCGAGGGCATGTCACAGGTCCGCCTGGTGCTGCCCACGATGGACGCGCTGCTGCTGGACGCCACCTTGGACGCGATCGCCGCCAGCGCCAGGGCCTGCGGCGAGCAGCGCACCCCAGCCCAGCTGCGCGCCGACGCCATCACCGCGATGACCCTGTCCACACTACGCACCAGCCAGCAGACCGCCTACCAGGCGACCACGCAAGCCCCCGACGACGACACCAGTGGCGCCACTGGCGGTAGTGACGGTCTCGGCAGCAGCACTGGAGACTTTGGCGGTGTGAGTGAGCTGGGTTCAGTGCCTGCCTCGTTCTCTCCTCCCAGGCGTTCTGCCTCCCTGGGTCGTCTGCTGCCTGACGGGGTGCCTCTGGAAGGCCTCCTGGGGGCCTTGAGCTCCTTGGTGGGGTCCGCCAGCCCGTGGTGGACTCCCTCAGGCACCGGCCACCTCCCCCTGCCAGCGGGCATCCACATCGACGTCCAGGTCACCGTCCCCCTGACCAGCCTGGCTGGTCTGGCTCCGCCAGAAGACACCACCGACCACACCCCAGCTGCTCACGGTCCCGGCGGCCGCGAACCCGCCACCAGCATCGGAGGCAACCGGCTCCAGGACAGCGATCACGGGGGCTATGTGCCCGAGGGCTGTGCTCCTAAGCGTGGTGTTCCCGAGAGCGCTGGGCGCCCCGAAGGTCCCTGCCATCCGAAGTCCGGCAGAGCCAGCCCAGACAAGAGCCCCACCATTGTCACGCCCGACCCTCTCAATGACGCAGCATCCCCGCATGACCGGAGAGGCCTGCCCACCACTGGTGGGAGGAGTCTGCCCGGCTCCAGTGGGAGGAGTCTGCCTGTACCCGACCCGGCTACTCCCGCCTTCTCGTGCTCGGCTGCTCACGACTCCTCGCCTGCCGCGTCGTTGTCCACTGCTCTCATCGCCCAGCTGGCCGCCTCGCCGGCTGAGGTCGCGGAGGTGCGCATTGGGGCGCGCAGTGTGGCGGTGCCGGCTATGACTGCCTGGGCCCTGGCCGCCGGCGGGACCTGGAGGCGCCTGGTCACCGACCCGGCAAGCGGAGTCGTGATCGACGTGGGTCGCACCAGGTACCGTCCCCCGGCCGGTCTGGCCGACCTGGTGCGCGCCCGCGACCGAGCCTGCGTCTTCCCCACCTGCCAGACCCCCGCCGAGCGGTGCGACATCGACCACCTCACCGCCTGGAGCCAGGGCGGAACCACCAGCCTGGACAACCTCGCCACCCTGTGCGAGGCCCACCACCGCCTCAAGCACACCCCCGGATGGGCCCTCACCCGAGACGAAGCCAGCGGAACCCTGTCCTGGCACACCCCCGACAAGACCATCTACCAACGCCACCCCAACGGCACCATCACCCGCCTACCCCACAAGACCGGCCCCCACCAGCACCACACCCCCGGCGCCGTCGTCCCAGCCGACCTGAGCCAGCAGATCGGCCCCGACATCCTCAACCGCCTCAACCGGGCCGTTGACAGAGCACTCGACGACCAGGCCCACGACCACACCGGCCTCGGCACCACCACCAACACCAACGGCAGCACCAGCCCCCGCCTCGAGACCCGCGGCCCCCAACCCGGCCAGAAACCCGGAGACTACGAGACCACCCCCTACCCCAAAGCCGCCCACACCCTCCAACTCGCACCCCTCATCGACCAAGCCCCACCCTTCTAA","MFEGGVLPRVPAGGAAGTLSAPAQDASAGAVTCTEDVVGLLGSLAGGGALAGVVEGLLSRLLVTAQNHHHDDGDGDGGGVGGEGSDAESAGSADGEGLFAGDSDADATLVAAADGHRVVSLEEVGATGLLGLGARGLGELAAACHRLAAWAAWGESLAAACLTGCAELSTHPDQWGPGGRVSPVVGFEERRFNTTCLLSARLGVSRSRAGQIVDHGSALMDMGFGPTEAMERCGVLDAAKASLVTRRLGDVPAPVALAVQEQVLPQAPRRSVSQVGRDIERALMETDPDGHAERVRVNVSRRCVTRPRPAGEGMSQVRLVLPTMDALLLDATLDAIAASARACGEQRTPAQLRADAITAMTLSTLRTSQQTAYQATTQAPDDDTSGATGGSDGLGSSTGDFGGVSELGSVPASFSPPRRSASLGRLLPDGVPLEGLLGALSSLVGSASPWWTPSGTGHLPLPAGIHIDVQVTVPLTSLAGLAPPEDTTDHTPAAHGPGGREPATSIGGNRLQDSDHGGYVPEGCAPKRGVPESAGRPEGPCHPKSGRASPDKSPTIVTPDPLNDAASPHDRRGLPTTGGRSLPGSSGRSLPVPDPATPAFSCSAAHDSSPAASLSTALIAQLAASPAEVAEVRIGARSVAVPAMTAWALAAGGTWRRLVTDPASGVVIDVGRTRYRPPAGLADLVRARDRACVFPTCQTPAERCDIDHLTAWSQGGTTSLDNLATLCEAHHRLKHTPGWALTRDEASGTLSWHTPDKTIYQRHPNGTITRLPHKTGPHQHHTPGAVVPADLSQQIGPDILNRLNRAVDRALDDQAHDHTGLGTTTNTNGSTSPRLETRGPQPGQKPGDYETTPYPKAAHTLQLAPLIDQAPPF$","HNH endonuclease","Periplasm, Membrane, Cytoplasm, Extracellular","HNH endonuclease domain protein","HNH nuclease","HNH endonuclease","","Smith D.K., Xue H. Sequence profiles of immunoglobulin and immunoglobulin-like domains. J. Mol. Biol. 1997. 274(4):530-545. PMID: 9417933Potapov V., Sobolev V., Edelman M., Kister A., Gelfand I. Protein-Protein Recognition: Juxtaposition of Domain and Interface Cores in Immunoglobulins and Other Sandwich-like Proteins. J. Mol. Biol. 2004. 342(2):665-679. PMID: 15327963Fowler S.B., Clarke J. Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state. Structure 2001. 9(5):355-366. PMID: 11377196","","","

InterPro
IPR002711
Domain

HNH endonuclease
PF01844	$\"[692-738]T$	HNH

InterPro
IPR003006
Family

Immunoglobulin/major histocompatibility complex
PS00290	$\"[600-606]?$	IG_MHC

InterPro
IPR003615
Domain

HNH nuclease
SM00507	$\"[680-732]T$	HNHc

","No hits to the COGs database.","***** IPB003870 (Protein of unknown function DUF222) with a combined E-value of 3.2e-18. IPB003870F 672-712","Residues 626-742 are 46% similar to a (MB3101 MB1413C) protein domain (PD031496) which is seen in Q73V65_MYCPA.Residues 664-739 are similar to a (REPEAT 13E12 FAMILY ENDONUCLEASE HNH REP13E12 RV1945/MT1995 RESTRICTION MB1980 RV1148C/MT1183/MB1179C) protein domain (PD010625) which is seen in Q9ZB93_RHOER.","","No significant hits to the PDB database (E-value < E-10).","Residues 692 to 738 (E_value = 1.9e-06) place ANA_0645 in the HNH family which is described as HNH endonuclease.","","endonuclease domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0646","677449","680856","3408","6.86","-2.81","122763","ATGACCGGCCGACACCGCTATGCCGAGCTCCACGCCCACTCCGCCTACTCCTTCCTCGACGGGGCCAACGAGCCCGATGAGCTGGCCTCGGCTGCCGTCGAGCTCGGCCTGGAGGCCCTCGCCCTGACCGATCACGACGGCGTCCCCGGCATCGTCAAGCATGCCCAAGCAGGCCGCGCCCACGGCCTGCCCACCATTCACGGCACCGAGCTCACCCTGGCCGACGGCTCCCACCTGCCCGTCCTGGCTCGCAACCCCGTCGGCTACCGCCGCCTGGTGTCCGCCATCTCCCAGCACAACCTGGACGCAGGGCACCGTCAAGAACCAGCCCACGACCCGACCGCGCTAGCCTCGGCTCTCCGCTCCGACCCCACCGACCAGACCGAGGCAGCGTCGGGAAGCTGCCTCGTCCTCACCGGAACCGCCAACGGCCCCCTGCGTCGGGCGCTGGGCGATCCACGTCGCCCTGATACTTGGGACCTGAAGGCGGCAGACGCCTGCCTGGGACACCTGACCGAGCTCTTCGCCGCGCCTGACCGAGGCCGTCCCCTCGGCACCGGCCCCACGACCACCGCTCACCGGCAGGTTGAAGGAGATGCCGCAATCGGCCTGGCCGTTGAGCTCACCCTGGACGGAGGCCCCACCGATGCCGCCCTCACCGATGCCCTGACCCGGCTGGCCCACACCCACCGGCTGCCCCTCGTAGCCACCGGTGCAGTGCGCTGCGCCCGCCCCACCGACGCCCGCCTCGCCGACGTACTCACCTCCACCCGCCTGGCCACCGACCTGGAAGGCGCCCGCGGTCACCTGCCCGCCATCGGCCGCTGGCTGCGAGGGGCCCAGGACATGGCGCTGCTCCACCGACGCTGCCCCGACGCCGTCGACCTGGCCGCCGAGTTCGCCTCAGACCTCGCCTTCGACCTGTCCCTCATCGCCCCCGACCTCCCCGACGCCGATGTCCCGGAAGGACACACACCTGCCAGCTGGTTGCGCGAGCTCACCCGCCAAGGCGCCACCCGCCGCTACGGCACCCCGCAGGAGCACCCCCGAGCCTGGGAGGTGCTCAACCACGAGCTCGAGGTCATCGAGTCCCTGGGATTCCCCGGCTACTTCCTCATCGTGCACGCCATCGTCGAGTTCTGCGCACAGTCGGGAATCCTGTGCCAGGGGAGAGGCTCGGCGGCCAACTCTGCAGTCTGCTACGCCCTGGGCATCACAGCCGTCGACGCCGTCAGGCACCAGATGCTCTTCGAGCGCTTCCTGTCCCCGGGGCGAGCCGGCTACCCGGACATCGACCTCGATATCGAGGCCTGCCGCCGCGAGGAGGTCATCCAACACGTCTACTCCCGATACGGCAGAGAACGTGCCGCCCAGGTCGCCAACGTCATCTCCTACCGCCCCCGATCCGCAGTCCGTGACGCCGCCCGAGCCCTCGGCCACCCCTCCGGCGTGCAGGACGCATGGGCCAAGCAGATGGATCGATGGGCCTCAGTGCGCCCCGGAGGACTGACCGGGCAGAGCGACGAGGTCCCTGAGCCGGTCCTCGACATCGCGGAGAAGCTGCTGCGGCTGCCCCGCCACCTGGGGGTTCACCCCGGAGGTATGGTCCTGTGCGGCCGCCCCGTCACCGAGGTCTGCCCGGTGCGCTGGGCCGCCATGGACGACCGCTCGGTCCTCCAATGGGACAAGGATGACTGCGCCGAGGCCGGCCTGGTCAAGTTCGACCTCCTGGGCCTGGGAGCGCTCACCGCCCTGCGTCTGGCCTTCACCACATTGGCACAGCGGGGACAGACCGTTCCCGACGCCGTGAAGGAAGGGGAGCTGCGCACCTCCCAGTCCGGTCGTCCCTGGGGGCTGCACACCCTGCCCGAGGAGGACCCCGCCGTCTACCGGCTGCTCACGGCCGCGGACACGGTTGGGGTCTTCCAGGTCGAGTCGCGTGCCCAGATGGCCACTCTGCCCCGACTGCGCCCCCAGGAGTTCTACGACATCGTCGTCGAGGTCGCCCTCATCCGCCCCGGCCCCATCCAGGGCGACGCCGTCAACCCCTACATCCGCCGCAGGCTGGGGCGCGAGGAGGTCACCTATCTGCATGACTCCCTCAAACCCGCCCTGACTAAGACCCTGGGAGTGCCGCTCTTCCAGGAGCAGCTCATGCAGATCGCCGTCGACGCCGCGGGGTTCAGCCCCGCCGAGGCAGACAGCCTGCGTCAGGCCATGGGGGCCAAACGATCCATCGAGCGTATGGACGCCCTCCGTGACAAACTCATAGCCGGAATGAGGTCCCGGGGCATCGACGCGCCCACTGCGGAGACGATCTACAGCAAGCTGAGGTCGTTCGCCGAGTTCGGCTTCCCCGAGTCCCACGCCTTCTCCTTCGCCTACCTGGTCTACGCCTCGGCCTGGCTCAAGGCGCGCAAGCCCGAGGACTTCTACGCCGGGGTCCTGGCCGCCCAGCCCATGGGCTTCTGGTCCCCGCAGTCCCTGGTCGCCGACGCTCGCCGCCATGGTGTGCGCGTCCTACCCGCAGACATCAACCGCTCACTGGCGCAGGCCACCGTCGAGCAGCGGGAGGACCACCAGGAGGCAGGCCACTCAGACCAGTGGGAGCCGCTGAGGCCCCATCCCGCTGCCCCGTCCTCCCTGGACGTCCACGACGACCTCGCAGTACGCCTGGGCCTGGCCCCGATCAAGGGGCTGGGGGAGCGGTCCGCGCAGGCCATCGTCACCGAGCGCCGTGCTCACGGCCCCTACCAGGACCTGGCGGATCTTGCGCGACGCGTGAGTCTGAGCCGCTCCCGCCTTGAGTCGCTGGCCGTCTCAGGAGCCCTGGACAGCCTAGGGGTGGAACGCCGTCAGGCCCTGTGGGCTGCCGGAGTCCTCTCCGATGAGCACGGCCGACGTCGTGGCGCCTCTCGCCGGGGGCAGGGCGCGTGGTATCAGCCCACGCTACCGGGAACCGCTGTCGGCGCCCAGGCCCCGACCCTGCCGATCATGACCGACCGTGAGCGCCAGGCAGCCGACCTGAGCCTGACCGGAGTGTCCACGCAGGGCTCGCCCTTGAAGCTGCTGCGCCCCATATTGGCCGACGACGGCGTGCTCAGTGCAGCCGACCTGGCGGATCAGGAGCATGGGAGCCGGGTGCGCGTCGCCGGCGTCGTCACCCACCGACAGCGCCCCCACACGGCTTCCGGCATGATCTTCCTCAACCTGGAGGATGAGACCGGTCTGCTCAACGTCGCCTGCAGAGCCGGAATGTGGCGCCGCTACCGCAGCATCGGCAGACGCGCCGTCGCTCTTATCGTGCGCGGCACCGTGGAGAAGGGTGACGGAGTCGTTGCACTCATGGCTGATCGCCTCCAGGTCCTTCCAGGTGTTCCGGGTACCGGCAGCCGGGACTGGTGCTGA","MTGRHRYAELHAHSAYSFLDGANEPDELASAAVELGLEALALTDHDGVPGIVKHAQAGRAHGLPTIHGTELTLADGSHLPVLARNPVGYRRLVSAISQHNLDAGHRQEPAHDPTALASALRSDPTDQTEAASGSCLVLTGTANGPLRRALGDPRRPDTWDLKAADACLGHLTELFAAPDRGRPLGTGPTTTAHRQVEGDAAIGLAVELTLDGGPTDAALTDALTRLAHTHRLPLVATGAVRCARPTDARLADVLTSTRLATDLEGARGHLPAIGRWLRGAQDMALLHRRCPDAVDLAAEFASDLAFDLSLIAPDLPDADVPEGHTPASWLRELTRQGATRRYGTPQEHPRAWEVLNHELEVIESLGFPGYFLIVHAIVEFCAQSGILCQGRGSAANSAVCYALGITAVDAVRHQMLFERFLSPGRAGYPDIDLDIEACRREEVIQHVYSRYGRERAAQVANVISYRPRSAVRDAARALGHPSGVQDAWAKQMDRWASVRPGGLTGQSDEVPEPVLDIAEKLLRLPRHLGVHPGGMVLCGRPVTEVCPVRWAAMDDRSVLQWDKDDCAEAGLVKFDLLGLGALTALRLAFTTLAQRGQTVPDAVKEGELRTSQSGRPWGLHTLPEEDPAVYRLLTAADTVGVFQVESRAQMATLPRLRPQEFYDIVVEVALIRPGPIQGDAVNPYIRRRLGREEVTYLHDSLKPALTKTLGVPLFQEQLMQIAVDAAGFSPAEADSLRQAMGAKRSIERMDALRDKLIAGMRSRGIDAPTAETIYSKLRSFAEFGFPESHAFSFAYLVYASAWLKARKPEDFYAGVLAAQPMGFWSPQSLVADARRHGVRVLPADINRSLAQATVEQREDHQEAGHSDQWEPLRPHPAAPSSLDVHDDLAVRLGLAPIKGLGERSAQAIVTERRAHGPYQDLADLARRVSLSRSRLESLAVSGALDSLGVERRQALWAAGVLSDEHGRRRGASRRGQGAWYQPTLPGTAVGAQAPTLPIMTDRERQAADLSLTGVSTQGSPLKLLRPILADDGVLSAADLADQEHGSRVRVAGVVTHRQRPHTASGMIFLNLEDETGLLNVACRAGMWRRYRSIGRRAVALIVRGTVEKGDGVVALMADRLQVLPGVPGTGSRDWC$","DNA polymerase III, alpha subunit","Cytoplasm","DNA polymerase III alpha subunit","DNA polymerase III; alpha subunit ","DNA polymerase III, alpha subunit","","Koonin E.V., Wolf Y.I., Aravind L. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 2000. 54:245-275. PMID: 10829230Keshav K.F., Chen C., Dutta A. Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. Mol. Cell. Biol. 1995. 15(6):3119-3128. PMID: 7760808Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 1997. 385(6612):176-181. PMID: 8990123","","","

InterPro
IPR003141
Domain

Polymerase and histidinol phosphatase, N-terminal
SM00481	$\"[8-75]T$	POLIIIAc

InterPro
IPR004013
Domain

PHP, C-terminal
PF02811	$\"[8-101]T$	PHP

InterPro
IPR004365
Domain

Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336	$\"[1048-1123]T$	tRNA_anti

InterPro
IPR004805
Family

DNA polymerase III, alpha subunit
TIGR00594	$\"[7-1083]T$	polc: DNA polymerase III, alpha subunit

InterPro
IPR011708
Domain

Bacterial DNA polymerase III, alpha subunit
PF07733	$\"[275-764]T$	DNA_pol3_alpha

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.140	$\"[5-45]T$	no description

","BeTs to 18 clades of COG0587COG name: DNA polymerase III alpha subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0587 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB011708 (Bacterial DNA polymerase III, alpha subunit) with a combined E-value of 4.3e-132. IPB011708A 36-68 IPB011708B 394-435 IPB011708C 440-477 IPB011708D 518-537 IPB011708E 567-583 IPB011708F 642-672 IPB011708G 704-748 IPB011708H 783-817***** IPB003141 (Phosphoesterase PHP, N-terminal) with a combined E-value of 2.8e-66. IPB003141A 8-45 IPB003141B 364-373 IPB003141C 387-430 IPB003141D 526-535 IPB003141E 783-811","Residues 234-323 are 53% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED REPLICATION) protein domain (PD126687) which is seen in Q7TWL9_MYCBO.Residues 249-342 are 48% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE CHAIN NUCLEOTIDYLTRANSFERASE) protein domain (PD669552) which is seen in Q8FRX6_COREF.Residues 325-386 are 69% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD216927) which is seen in Q73U92_MYCPA.Residues 390-460 are 64% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD005473) which is seen in Q6FAL5_ACIAD.Residues 419-454 are 86% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD921859) which is seen in Q8NSN0_CORGL.Residues 456-496 are 80% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE DNAE2 CHAIN NUCLEOTIDYLTRANSFERASE) protein domain (PDA1E558) which is seen in Q73U92_MYCPA.Residues 459-667 are 66% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE DNA-DIRECTED III NUCLEOTIDYLTRANSFERASE REPLICATION) protein domain (PD004180) which is seen in Q7TWL9_MYCBO.Residues 668-703 are 77% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD949751) which is seen in Q6A780_PROAC.Residues 704-785 are 71% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD847062) which is seen in Q73U92_MYCPA.Residues 788-951 are 59% similar to a (DNA POLYMERASE ALPHA III TRANSFERASE SUBUNIT DNA-DIRECTED REPLICATION NUCLEOTIDYLTRANSFERASE III) protein domain (PD352075) which is seen in Q6NJ04_CORDI.Residues 1012-1121 are 67% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE CHAIN DNA-DIRECTED) protein domain (PD679201) which is seen in Q6A780_PROAC.","","-41% similar to PDB:2HPI Eubacterial and Eukaryotic Replicative DNA Polymerases are not Homologous: X-ray Structure of DNA Polymerase III (E_value = 3.8E_93);-41% similar to PDB:2HPM Eubacterial and Eukaryotic Replicative DNA Polymerases are not Homologous: X-ray Structure of DNA Polymerase III (E_value = 3.8E_93);-43% similar to PDB:2HNH Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III (E_value = 1.8E_90);-43% similar to PDB:2HQA Crystal structure of the catalytic alpha subunit of E. Coli replicative DNA polymerase III (E_value = 1.8E_90);-52% similar to PDB:2BW3 THREE-DIMENSIONAL STRUCTURE OF THE HERMES DNA TRANSPOSASE (E_value = 1.8E_90);","Residues 8 to 244 (E_value = 6.1e-20) place ANA_0646 in the PHP family which is described as PHP domain.Residues 275 to 764 (E_value = 1.4e-207) place ANA_0646 in the DNA_pol3_alpha family which is described as Bacterial DNA polymerase III alpha subunit.Residues 1048 to 1123 (E_value = 4.6e-09) place ANA_0646 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.","","polymerase III alpha subunit (dnaE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0647","682322","680868","1455","6.93","-0.38","51945","ATGGCAACACACAGCTCTCCGTCACAGAAGCCGACTCAGGACACGTCGGCCGAGGTTCCCGAGTCCTCCGAGAGCCCCGACTCCCACCAGGCGGCGCAGGAACGCGAATCGGAGAAGAGGTCCACCCGAGAGATGCTCAGCAGCAGTGGCCTGCTGAGTCGGCTCAAGAGCGCACGTACGGCGCTGGACCGGGGGATCGACTGGGCGGAGAGGCGCCGGCAGGCGGACCGTGACTACCAGCTGCACTGGGAGTCGGCCCCGGAGGAGGAGGCCAGGCCGGTCTCTCCCCCGGTGTCCACCACACATGTGCGCGTGGCCCCCTCGGTCTCCTTCCCCGAGACGGTCACGACCCGTTCCTCGGTCATGGACTCCCTACCCTCCTGGCTGGTGCGGGGCGGGATGGGGGCCTGGCTGGGACTGGGCATCATCATCGTCATCGGCCTTGTCTTCTATGCCACTTCGCAGGTGATCCCAGTCTTCATCGGCCTGTTCATGGCACTGGTGTTCACCTCGATCCTCCAGCCGATGGTCAACCTCTTCGCCAGGATCATGCCCCGATACCCGGCGACCTTCCTGGCACTGCTCACCACCATCGGTGCGATCGCCGGACTGGTCACGTACGTGGTCGCCTCGGTCACCAGCCAGTGGAGCTCCTTGGCATCCCAATTCGGCGATGGTCTCAACACGATCATGGACTTCCTGGAGAAGGGGCCGCTGCACCTGACGCAGCAGCAGATCTATCACCAGCTCCAGCTCTGGCTGCGCCAGGGGCAGCACTATCTGCAGTCCAACGCCCCGTCCCTGGCCTCGGAGGTGCTCTCCAACGCCAGTGCGGTCGTCGATGTGCTCACGGTCCTGGCCCTGGCGCTGTTCGTCACGATCTTCTTCCTGGCCTCCGGGGGCCGGATGTGGCGCTGGTTCCTCAACGAGCTGCCCGCCACGATGCGGGAGTCGACCCACCGGGCCGCGGGTGCCGGCTGGTACACCTTCGCCGGGTACGCCCGTGGCACTGTGCTGGTGGCGCTCACCGACGCCATCATGGCCGGGATATTCCTCCAGCTGGCGGGGATCCCGTTGGCGGCTCCCCTGGCGGTGCTCGTGTTCATCGGCGCCTTCATTCCGATCATCGGCGCACCTCTGGCGATGCTCGTGGCCATGGTGGTGGCCCTGGCCTCCGGCGGCTTCGTCACCATGATCGTTGTCGGCGTGGGAGTAGCCGGGATCGGCCAGATCGAGGGTCACATACTCCAGCCCCTCATCATGGGTCGCCAGGTCTCTTTGCACCCTGTGGTGGTCATTATCGGTGTCGCCCTGGGGACCTACGCCGCCGGCCTGCTCGGTGCGATCGTCGCAGTCCCGCTGATCAGTGTGCTCTGGTCCGTCTACTCCGAGCTGCACACCAAGGACGCCCCGGTCACGGGCGAGCTGCCCGCCTACTCCTCGCGCAAGGAGTGA","MATHSSPSQKPTQDTSAEVPESSESPDSHQAAQERESEKRSTREMLSSSGLLSRLKSARTALDRGIDWAERRRQADRDYQLHWESAPEEEARPVSPPVSTTHVRVAPSVSFPETVTTRSSVMDSLPSWLVRGGMGAWLGLGIIIVIGLVFYATSQVIPVFIGLFMALVFTSILQPMVNLFARIMPRYPATFLALLTTIGAIAGLVTYVVASVTSQWSSLASQFGDGLNTIMDFLEKGPLHLTQQQIYHQLQLWLRQGQHYLQSNAPSLASEVLSNASAVVDVLTVLALALFVTIFFLASGGRMWRWFLNELPATMRESTHRAAGAGWYTFAGYARGTVLVALTDAIMAGIFLQLAGIPLAAPLAVLVFIGAFIPIIGAPLAMLVAMVVALASGGFVTMIVVGVGVAGIGQIEGHILQPLIMGRQVSLHPVVVIIGVALGTYAAGLLGAIVAVPLISVLWSVYSELHTKDAPVTGELPAYSSRKE$","Integral membrane protein","Membrane, Cytoplasm","putative integral membrane protein","hypothetical protein","protein of unknown function UPF0118","","","","","

InterPro
IPR002549
Family

Protein of unknown function UPF0118
PTHR21716	$\"[213-462]T$	TRANSMEMBRANE PROTEIN
PF01594	$\"[136-466]T$	UPF0118

noIPR
unintegrated

unintegrated
tmhmm	$\"[128-150]?$ $\"[156-176]?$ $\"[191-211]?$ $\"[278-298]?$ $\"[331-351]?$ $\"[357-377]?$ $\"[386-406]?$ $\"[425-459]?$	transmembrane_regions

","BeTs to 15 clades of COG0628COG name: Predicted permeaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0628 is aom-k--qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB002549 (Protein of unknown function UPF0118) with a combined E-value of 6.8e-19. IPB002549A 357-381 IPB002549B 418-455","Residues 136-227 are 54% similar to a (MEMBRANE INTEGRAL) protein domain (PD210203) which is seen in Q82MQ3_STRAW.Residues 260-341 are similar to a (MEMBRANE PERMEASE PROTEIN TRANSMEMBRANE PERM INTEGRAL PREDICTED UPF0118 SPANNING PROBABLE) protein domain (PD132771) which is seen in Q82MQ3_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 136 to 466 (E_value = 3.1e-53) place ANA_0647 in the UPF0118 family which is described as Domain of unknown function DUF20.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0648","682392","683303","912","6.28","-3.92","32118","ATGACCGCCCCGAATGTCGGCAATCCGATGCACCCCGCCGTGACGAGCCAGCTGCGTCTGCCCCGCGCCGCCGCGTTAGGGCCAGGGCGGGGAGGGCAACAGAGGCTTCTCATCGACGCCCCGGCCGGAGCGGCAGAGATCTACCTCCACGGCGCCACCGTGACCTCCTGGGTGCCGCGCGGAGGCTCGGAGGTCATCTTCACTTCCCGGCAGGCGGTCTTCGACGGCGCTACCGCCATTCGTGGAGGAATCCCCCTGTGCCTGCCGGAATTCGGCGTCGGCATCAACGGCGACGCCGTACCGAAGCACGGATGGGCGCGCATCGCTCCCTGGAGACTGCGAACGGTCACCACCACCGACGGCGGCGGGGTCCGCGCTCTTCTCAGCGTCAGTCGCGATCGACTGACAGCGCTCTATGAGGTTGAGGTTGGTGAGACGCTGCGCCTGGGACTCAGCCTGCGCAACGAGGGGACCGAGCCCCGCACGGTGGAGGCGGCCGCACACACCTATCTCTCAGTCCACGACGTCACCGCCAGCCGCATCAGCGGGCTCGCAGGCGCCCGTTACAGTGACAACCTGGCTCGCAGCCCCCAGGAGGCCTACCACGTCCAGGAAGGCGATGTGACGATCAGTGGCCCCGTGGACCGCATCTATGACTCTGCCGAGCCGATCACGGTCACTGATCCTGGACACCAACGCACCATCGGCATCGATAAGCGCAACGCGCCCTCGACGATCGTGTGGAACCCCTGGTCCACTCACAGTGCCCCACTGCCGGACATGGCTAACGACGAGTTCCCTGCCATGGTGTGCGTCGAAAGTGGGGCGGTGCGAGAGCACGCACCCACCATCGAGCCCGGGGCGAGCTGGTCCATGCAGGTGACCTTGAGTGTCGAGAGTACCGCAGTGTGA","MTAPNVGNPMHPAVTSQLRLPRAAALGPGRGGQQRLLIDAPAGAAEIYLHGATVTSWVPRGGSEVIFTSRQAVFDGATAIRGGIPLCLPEFGVGINGDAVPKHGWARIAPWRLRTVTTTDGGGVRALLSVSRDRLTALYEVEVGETLRLGLSLRNEGTEPRTVEAAAHTYLSVHDVTASRISGLAGARYSDNLARSPQEAYHVQEGDVTISGPVDRIYDSAEPITVTDPGHQRTIGIDKRNAPSTIVWNPWSTHSAPLPDMANDEFPAMVCVESGAVREHAPTIEPGASWSMQVTLSVESTAV$","Aldose 1-epimerase","Cytoplasm, Extracellular","Possible apospory-associated protein C","aldose 1-epimerase","Aldose 1-epimerase","","Volpi N., Maccari F. Purification and characterization of hyaluronic acid from the mollusc bivalve Mytilus galloprovincialis. Biochimie 2003. 85(6):619-625. PMID: 12829379Ducki A., Grundmann O., Konermann L., Mayer F., Hoppert M. Glucoamylase from Thermoanaerobacterium thermosaccharolyticum: Sequence studies and analysis of the macromolecular architecture of the enzyme. J. Gen. Appl. Microbiol. 1998. 44(5):327-335. PMID: 12501412","","","

InterPro
IPR003778
Domain

Allophanate hydrolase subunit 2
SM00797	$\"[25-177]T$	no description

InterPro
IPR008183
Family

Aldose 1-epimerase
PF01263	$\"[34-297]T$	Aldose_epim

InterPro
IPR014718
Domain

Glycoside hydrolase-type carbohydrate-binding, subgroup
G3DSA:2.70.98.10	$\"[31-296]T$	no description

noIPR
unintegrated

unintegrated
PTHR11122	$\"[1-301]T$	APOSPORY-ASSOCIATED PROTEIN C-RELATED

","BeTs to 7 clades of COG0676COG name: Uncharacterized enzymes related to aldose 1-epimeraseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0676 is ------y----l-cefghs--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 140-217 are 57% similar to a (APOSPORY-ASSOCIATED ALDOSE 1-EPIMERASE C YEAD RELATED POSSIBLE YMR099C C-LIKE LIKE) protein domain (PD715965) which is seen in Q82VR2_NITEU.Residues 141-300 are 49% similar to a (ALDOSE 1-EPIMERASE FAMILY) protein domain (PDA000N6) which is seen in Q6A648_PROAC.","","-44% similar to PDB:2HTA Crystal Structure of a putative mutarotase (YeaD) from Salmonella typhimurium in orthorhombic form (E_value = 5.0E_22);-44% similar to PDB:2HTB Crystal Structure of a putative mutarotase (YeaD) from Salmonella typhimurium in monoclinic form (E_value = 5.0E_22);-45% similar to PDB:2CIQ STRUCTURE-BASED FUNCTIONAL ANNOTATION: YEAST YMR099C CODES FOR A D-HEXOSE-6-PHOSPHATE MUTAROTASE. (E_value = 4.7E_20);-45% similar to PDB:2CIR STRUCTURE-BASED FUNCTIONAL ANNOTATION: YEAST YMR099C CODES FOR A D-HEXOSE-6-PHOSPHATE MUTAROTASE. COMPLEX WITH GLUCOSE-6-PHOSPHATE (E_value = 4.7E_20);-45% similar to PDB:2CIS STRUCTURE-BASED FUNCTIONAL ANNOTATION: YEAST YMR099C CODES FOR A D-HEXOSE-6-PHOSPHATE MUTAROTASE. COMPLEX WITH TAGATOSE-6-PHOSPHATE (E_value = 4.7E_20);","Residues 34 to 297 (E_value = 1.7e-18) place ANA_0648 in the Aldose_epim family which is described as Aldose 1-epimerase.","","apospory-associated protein C (E60620)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0650","684436","683720","717","5.03","-4.71","25254","GTGCTCCCCACTGCAGAGGGGAGGAACCGAGATGACGAGCCCTCCCCTCTGCCCTTAGGCTGTGACTCGTACGCCGACCTGACACCAGAAAGCGCATCAGCCCGGGTGCTCTCAGCCATGGCGGCACCCGTCACTCCCTGCCCCGTCTTACATGGAGGATTCATGTCCTACGGAACCGGCCCCGCACCCTACGGCGGCCAGGCACCATACAGCGACCAACCGGCCTACGGCGGCCAGGCTCCCTACCCGGGCGGCCCTGCCCCCTACGGCGCACCCAACCAGTTCGGGGCTATGTCATTAGCCCCCGACGTCGCCCCGCTGCCTGGTGCAAGCTTCGGCGAGGCCGTCAAGCGCTACTTCCAGCGCTACGCCCAGTTCCGAGGCTATGCATCTCAGTCCGAGTTCTGGTGGCCATTCCTCATATTCCAGATGCTCATCCCCATTGGCCTCTATATTCTGGCAGTGGCAATCGGCGCTTCGGCAGCGATTTCGGGCGCCGACGAGTTGCCTTCTGCGGTGGTCGCGATCTTTGGCCTGCTCATGCTCTACGTTGCCGCGATCCTTATTCCGTCGCTCGCAGTGATGGTCCGTCGCCTCCATGACACCGGACAGTCAGGACTGTTCCTGCTTTTCTACTTCGTCGGACTGGGGATCGTGCCGCTCATCATGTGCTGCATGCCTCCCCGCCCCGACCTCTACCGTCCTGAGTGGAGCTGA","VLPTAEGRNRDDEPSPLPLGCDSYADLTPESASARVLSAMAAPVTPCPVLHGGFMSYGTGPAPYGGQAPYSDQPAYGGQAPYPGGPAPYGAPNQFGAMSLAPDVAPLPGASFGEAVKRYFQRYAQFRGYASQSEFWWPFLIFQMLIPIGLYILAVAIGASAAISGADELPSAVVAIFGLLMLYVAAILIPSLAVMVRRLHDTGQSGLFLLFYFVGLGIVPLIMCCMPPRPDLYRPEWS$","Uncharacterized membrane protein","Membrane, Cytoplasm","Protein of unknown function (DUF805) family","hypothetical protein","protein of unknown function DUF805","","","","","

InterPro
IPR008523
Family

Protein of unknown function DUF805
PF05656	$\"[122-232]T$	DUF805

noIPR
unintegrated

unintegrated
tmhmm	$\"[146-166]?$ $\"[172-192]?$ $\"[207-227]?$	transmembrane_regions

","BeTs to 3 clades of COG3152COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG3152 is --------------efg----j----Number of proteins in this genome belonging to this COG is 1","***** IPB008523 (Protein of unknown function DUF805) with a combined E-value of 7.1e-14. IPB008523A 125-136 IPB008523C 190-217","No significant hits to the ProDom database.","","-53% similar to PDB:1AJ8 CITRATE SYNTHASE FROM PYROCOCCUS FURIOSUS (E_value = );","Residues 122 to 232 (E_value = 5.5e-14) place ANA_0650 in the DUF805 family which is described as Protein of unknown function (DUF805).","","of unknown function (DUF805) family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0651","684493","685755","1263","8.89","5.52","42766","ATGCACTCCGTCACCTCACCGAGCAGTCCTTCTGATGTGAGGCGCAGTCCTGATCTGCTCCGTGCGCGCGCCGGGGTCAGCCTGGTGTTCCTGGCCAATGGCCTGGGATTCGCCAATCTGGTGCCGCGTTTCCCGGAGATCGTGGAGGGGCTGGGGCTGAGCAGGAGCGCCTTCGGGCAGGCGGTGGCCGCAGCCAGCGTTGGTGCTCTCGTGGCGGGACTGGCCGCGTCTTGGCTCATCTCCCGCCTGACCTCGGCCAAGGTGGCCAGCCTGGGCATGCTCGTGGTGGCCCTGGCTCTCCTGGGAGCTGGGTTGGCCCGTTCGTGGCTCGTCCTGGCGGTCTGCCTGCTGGTTGTGGGCGGGACGGACTCCATTGTCGATGTCGCGCAGAACGCACACGGGCTGCGGGTCCAGCGCCGTTGGGGTGCCTCCATCGTGACGAGCTTCCATGCCTCATGGTCACTGGGGGCGGTCCTGGGGGCAGCCATGGGGCAGGCTTTGGCTGGAGCCGGAGTGGGGGTGGGAACCCACATGGTCCTGACGGCGGTGGTGTTGCTCGTCCTCTCGACAGGCCCCCTGCTCGCAGGCTGGTTCCTACCCGGCCATGACCGCGCTGATCGCGAGCCCGATGAGATCAAGGAGTTCGACAACGCCCCCCAGGTGAGGCCGGCGACATCGTCTCGTCGAGTCGGACCGGTCACGATCCTCGTGCTCCTCGTCGTCGGGCTACTATGCGCGGCCTCGATGTTCCCCGAGGACGTGGCCATGAACTGGTCCTCCCTGCTCCTGTCCGAACAGGGCGCCGGTGCCGGTCACGTCGGGCTGGGGCTGGTGGCCCTCCAAGGAACGATGATCGTGGGGCGCCTGGTGGGTGACCGCATCATTGATGCTGTCGGTCAACGAGCCGTGATCGCCTGGGGTGGAGCACTGGTTACCCTCGGAATGAGCATCGCCCTCCTGCTCTCCTCCGTTCCCGGGACGCTGCTGGGGATGGCGATCTCCGGGGCTGGGTGCGCCGTCGCCGTTCCCGTGACCTACTCCGCCGCTGACGATGTTGAAGGGCTTCCTCCCGGGCTGGGACTGACCATCGTGTCCTGGCTGGCCCGCCTGGCGGGTCTCCTGTCGCCACCCGTTGTCGGCCGGCTCGCTGACGATCACGGGCTGTGGGTGGCTCTGGCCTACGGCCTACTGGGAGGCCTCATCATGGTCTTCTGCTGGCCGGTCCTGCGCCGTAGGTCTGCGGGGACTCAGAGGCCAGGCTGA","MHSVTSPSSPSDVRRSPDLLRARAGVSLVFLANGLGFANLVPRFPEIVEGLGLSRSAFGQAVAAASVGALVAGLAASWLISRLTSAKVASLGMLVVALALLGAGLARSWLVLAVCLLVVGGTDSIVDVAQNAHGLRVQRRWGASIVTSFHASWSLGAVLGAAMGQALAGAGVGVGTHMVLTAVVLLVLSTGPLLAGWFLPGHDRADREPDEIKEFDNAPQVRPATSSRRVGPVTILVLLVVGLLCAASMFPEDVAMNWSSLLLSEQGAGAGHVGLGLVALQGTMIVGRLVGDRIIDAVGQRAVIAWGGALVTLGMSIALLLSSVPGTLLGMAISGAGCAVAVPVTYSAADDVEGLPPGLGLTIVSWLARLAGLLSPPVVGRLADDHGLWVALAYGLLGGLIMVFCWPVLRRRSAGTQRPG$","Permease of the major facilitator superfamily MFS_1","Membrane, Extracellular","putative integral membrane protein","major facilitator superfamily MFS_1","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[22-410]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[26-384]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[9-417]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF5	$\"[9-417]T$	FOSMIDOMYCIN RESISTANCE-RELATED
tmhmm	$\"[24-42]?$ $\"[61-81]?$ $\"[83-103]?$ $\"[109-129]?$ $\"[149-169]?$ $\"[179-199]?$ $\"[230-250]?$ $\"[269-287]?$ $\"[302-322]?$ $\"[328-348]?$ $\"[358-378]?$ $\"[388-408]?$	transmembrane_regions

","BeTs to 9 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","Residues 127-265 are 56% similar to a (MEMBRANE TRANSMEMBRANE REGULATOR TRANSCRIPTIONAL DEOR-TYPE INTEGRAL PROTEIN MOSC YBJJ PERMEASE) protein domain (PD314007) which is seen in Q93J00_STRCO.Residues 286-335 are 72% similar to a (MEMBRANE TRANSMEMBRANE TRANSCRIPTIONAL DEOR-TYPE REGULATOR MOSC PROTEIN PERMEASE INTEGRAL TRANSPORTER) protein domain (PD582590) which is seen in Q93J00_STRCO.Residues 337-409 are similar to a (MEMBRANE TRANSMEMBRANE REGULATOR INTEGRAL DEOR-TYPE TRANSCRIPTIONAL PROTEIN MOSC YBJJ TRANSPORTER) protein domain (PD017122) which is seen in Q93J00_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 384 (E_value = 1.2e-21) place ANA_0651 in the MFS_1 family which is described as Major Facilitator Superfamily.","","integral membrane protein","","1","","","","","","","","","","","Tue Aug 14 10:29:36 2007","","Tue Aug 14 10:29:36 2007","","","Tue Aug 14 10:29:36 2007","","Tue Aug 14 10:29:36 2007","","Tue Aug 14 10:29:36 2007","Tue Aug 14 10:29:36 2007","","","","","yes","","" "ANA_0652","687098","685764","1335","10.54","18.32","47895","ATGAGTATGCCCGGCCCTGTACCTGCACGTCGTCACCATGGCCCCGCGATCGCACGCTGGAAGCTCCCAGCGGTGCGAGTACGCCAGGAAGGCGGGGTCGTCACGGTCGAGCAGAGGGTCCCGGCCCGCATCAGCAACATCACGGCCAGCACCACGTCCAACGCCAGTGGGAACGTTCAGACCGTGCGCACCTACTACTACGAGTCCGGGCTCGGCTCCAACTCCAGGCTCCCCCTGGTTCGTGAACGACTCACGGTGCCGGCGTCCATCGCCGGTCGAGATCAGGTTGAGCAAGCGGTCAAGGCCGCCGTCTCCACCTACGATCCGGGCACTGCGGCGCCAGGTAGGCAGTGGGGCCCGGGAATGTGGAGCAGGTTGGCCATGGTCGGCTTCGGAGTCTTCTTCTCCTTCATCTCGTTCTCCTTCCTCATAGTTGGCACTCGCGTGATGAGGTTCGACGAGGAGGTTTACGGACGTTCCTTCGATTATGGTTCTCTCTTCCTGCTCCTGCCTACTGGGTTCACCCTCCTGGGCGTGCTCATCACGGTCATTGGGCTCCGGAGTGCCTGGATCCTGCGCACACCGGACTTCGTCGCTGAGGAACAGTGGCAGCTCCTGCGCTCAATCCTCACCCGGATGACCGGGCAGCAGCCGGGATCGTCGCGCCCGCTCGACGTCGAAGCAGGACTACGACCGGATCTCATCACCCACCCTCACGGTGAGACACGCAGACGGGGAGTCACACTTGACGGCCGCATGGGGCCGGCCTGGCCCGACGCCTACAGTGTTGCCAAGGCCATCAAAAGAGGCAGGCTCAAGGTCCTCCTCACCTTATCCCTCATCATCATCATTGCCGGCCTCATGTACGTCTTCAGCAGAGGTGGGGCAAGCCTGGGTGCCGGTCAGGCGATCACCGCCATTCTGGTCGGCACGGGAATGGTTGGAGCAGCTCTGATGCCACCATTACAGGCCTGCGACCGACTCCTGGCCGCCTACCCGACTCAGGTCCCCGGTGAGGACGCTCCTCGCCGCATAGGTCTCCGAGATGTTGATGTTGACAATCTGCCCGGCTGGTGTGCTGCGCGCCTTCGACAGGACTACTGGAACGCAGCATCGGCCGGCTTCTGGGTCCTGTGTGCAGCCGGAGGCGTTCTGCTCTTCATTCAACGCCATTCAGAACACTCAACCGATGCTTCAACGGGCTCAGCACTGTTCTTGAGCGCCCCTGTGCTCATCGGAGTCACCGTGATCGCCGTGGTCGCGACCGTTGTAGTCAGCGTCATCTGGGCCCGCAACCGGGACGCCGGACGACGACGCCTCGTGGGACTGCCCTGA","MSMPGPVPARRHHGPAIARWKLPAVRVRQEGGVVTVEQRVPARISNITASTTSNASGNVQTVRTYYYESGLGSNSRLPLVRERLTVPASIAGRDQVEQAVKAAVSTYDPGTAAPGRQWGPGMWSRLAMVGFGVFFSFISFSFLIVGTRVMRFDEEVYGRSFDYGSLFLLLPTGFTLLGVLITVIGLRSAWILRTPDFVAEEQWQLLRSILTRMTGQQPGSSRPLDVEAGLRPDLITHPHGETRRRGVTLDGRMGPAWPDAYSVAKAIKRGRLKVLLTLSLIIIIAGLMYVFSRGGASLGAGQAITAILVGTGMVGAALMPPLQACDRLLAAYPTQVPGEDAPRRIGLRDVDVDNLPGWCAARLRQDYWNAASAGFWVLCAAGGVLLFIQRHSEHSTDASTGSALFLSAPVLIGVTVIAVVATVVVSVIWARNRDAGRRRLVGLP$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[126-146]?$ $\"[165-185]?$ $\"[274-292]?$ $\"[302-322]?$ $\"[368-388]?$ $\"[407-429]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[131-151]?$ $\"[167-187]?$ $\"[274-296]?$ $\"[302-322]?$ $\"[370-390]?$ $\"[409-431]?$	transmembrane_regions

InterPro
IPR002110
Repeat

Ankyrin
PR01415	$\"[55-67]T$ $\"[189-201]T$	ANKYRIN

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[66-83]T$	SUGAR_TRANSPORT_1

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[12-497]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[16-416]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[2-202]T$ $\"[251-418]T$ $\"[466-491]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57	$\"[2-202]T$ $\"[251-418]T$ $\"[466-491]T$	DRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[49-69]?$ $\"[78-96]?$ $\"[102-122]?$ $\"[137-157]?$ $\"[163-185]?$ $\"[200-220]?$ $\"[226-244]?$ $\"[265-287]?$ $\"[303-323]?$ $\"[332-352]?$ $\"[358-380]?$ $\"[470-490]?$	transmembrane_regions

","BeTs to 17 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","Residues 48-219 are similar to a (TRANSLOCASE MEMBRANE ANTIPORTER INTEGRAL ANTIBIOTIC TRANSPORTER) protein domain (PD653719) which is seen in Q8KHB7_NOCAE.Residues 148-200 are similar to a (TRANSMEMBRANE RESISTANCE TRANSPORTER MULTIDRUG EFFLUX MEMBRANE DRUG PROBABLE FAMILY FACILITATOR) protein domain (PD409625) which is seen in Q936C7_STRCL.Residues 246-295 are 72% similar to a (TRANSMEMBRANE RESISTANCE MULTIDRUG EFFLUX TRANSPORTER MEMBRANE DRUG FAMILY TRANSPORTER PROBABLE) protein domain (PD687914) which is seen in Q9L1B4_STRCO.Residues 373-420 are 77% similar to a (TRANSMEMBRANE RESISTANCE EFFLUX MULTIDRUG MEMBRANE TRANSPORTER DRUG PROBABLE FACILITATOR TRANSPORTER) protein domain (PD349131) which is seen in Q936C7_STRCL.","","No significant hits to the PDB database (E-value < E-10).","Residues 16 to 416 (E_value = 1.6e-52) place ANA_0655 in the MFS_1 family which is described as Major Facilitator Superfamily.Residues 64 to 112 (E_value = 4.3e-05) place ANA_0655 in the Sugar_tr family which is described as Sugar (and other) transporter.","","multidrug transporter","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0656","691308","691877","570","4.84","-11.29","20979","ATGAGAACCTCGAAACGGGACCGCATCATCACCGCGGCGCTCGAGCTCGCCCACCGAGACGGCTTCGATGCCCTCACCTTCGATGCCTTGGCCGAGCACGTCGGACTGACCCGAGGCGGTGTCATCTACCACTTCCGCACCAAGACCGAGCTCTTGGAGGGGATCGCTGCGGCCTTCCAGGAACGATGGCAGGCCGAGGCGCTGGAGGCACTGGGCAAGCCCCTGGAGGAGGCGAGCCGCACCGAGCGCATCGAGGCCCTGACGCGCTCCGTCCTCGACGGCGAGATCCTCCCCGGAGAGGTCAGCTTCATACTCTCGTCCACGCCGCAGGCCGAGACGATCAAGAACGCCTGGGACATGCTGCGTGACGAGTGGATCGGCGAGGTGGACGAACTCAGCGCGATGCAGCGCGTGGCGCTGCTGGCCGTGGACGGATGGTGGGCGAACCGCGCTGTCGACAGCCGTAGCCGCAATCCCGATGAGCCCGCCATCGCCGAGCTCATTGTGTCTTTAGCGGCGGGAAACCCGCCCGATGAGAAGCTCTTCAAGCCCTCCGATAAGGACCAATGA","MRTSKRDRIITAALELAHRDGFDALTFDALAEHVGLTRGGVIYHFRTKTELLEGIAAAFQERWQAEALEALGKPLEEASRTERIEALTRSVLDGEILPGEVSFILSSTPQAETIKNAWDMLRDEWIGEVDELSAMQRVALLAVDGWWANRAVDSRSRNPDEPAIAELIVSLAAGNPPDEKLFKPSDKDQ$","Transcriptional regulator, TetR family","Cytoplasm, Extracellular","transcriptional regulator","bacterial regulatory protein; TetR family","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[9-22]T$ $\"[30-53]T$	HTHTETR
PF00440	$\"[9-55]T$	TetR_N
PS50977	$\"[3-63]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[2-66]T$	no description

","BeTs to 15 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 1.3e-13. IPB001647 9-51***** IPB013572 (Tetracycline transcriptional repressor MAATS-type, C-terminal) with a combined E-value of 7.7e-06. IPB013572B 30-52","Residues 1-171 are 46% similar to a (REGULATORY TRANSCRIPTIONAL DNA-BINDING TETR-FAMILY PROTEIN TRANSCRIPTION REGULATOR BACTERIAL REGULATION FAMILY) protein domain (PD633629) which is seen in Q8NMG3_CORGL.","","-47% similar to PDB:1V7B TetR-family transcription factor CGL2612 from C.glutamicum (E_value = 1.8E_12);-47% similar to PDB:2DH0 Crystal structure of the TetR-family protein CGL2612 from C.glutamicum bound to ethidium (E_value = 1.8E_12);","Residues 9 to 55 (E_value = 6.3e-13) place ANA_0656 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0657","691936","693987","2052","4.77","-44.92","74501","ATGAGCGAGACCACCGACGGCACCGACCTCCCGGAGTCGAACGTCTTCGCCAAGCCATGGCCGCTCGATCTCGGCCTGCCCGGCTTCACAGCCGTGGACCACGCCGACATCGAACCGGCCATCCGCGCCGGGATGGCTGTCGAGCGCCAGGAGTGGGAGGCGATCGCCACCAACGAGGACGCACCCACGATCGCCAACACCGTCGAGGCGTTGGAGCGATCCGGCGAGCTGCTGGAGCGGGCGCTGACGGTGCTGGACGCTCTGACCTCCGCCACCGACTGCCCGGACCTCGACGAGCTCGAGGAGGCCCTGGCCCCCGAGCTGGCGGCCCACTCCGACGCCTATCACCTCGACTCCCGTCTCTACCGCCGTTTCAAGGCGCTCGACGAGCTCGTGTCCCAAGCCCCTGAGGGGCAGGCCGCGCGCGACGCCGACGGCACCGTCATCGATGCTGAGGCCGCCCGCCTCATCCGCCTGACCGTCGAGGAGTTCGAACGCAACGGCGTCGGCCTGGACGAAGCGGACACGCAGGCGCTCAAGGAGATCAACGCCCGCGTCAACGCGCTCAAGATGCGTTTCTCCGTCCTGGTCACCGAGGCCATGCACGCGGCCGGTGTCACCAACGTCACGGTGCCGCCGGCCCTGGCCACCACCCGGCCCCACGGCGCCAGGCTCGCCCTGCTGGAGACCTCCATGAGCCGAGGGCTGGGGGAGCAGGGCGCCTTCGGCGACACCCGCGGCATCGTTCTGGAACTCGCCCGGCTGCGCGCCGAGCGGGCCGTCCTCCTGGGCTTCCCGCACCACGCCGCCCTCGTGGCCGCGGAGTCGGCCGCCCGCACCACCGAGGCGGTCTCAGAGCTGCTCGCCCGGCTCACTACGCCGGCCATGGACAACGCCCGCGCTGACGCTCAGGTCTACGCCGCCCGCATGGACCTGGATCCGCAGACCCAGGCCGGTGAGACCTTCGGGCCCGCCGACTGGCCCCTCTACGAGGCCGCTGAGCGCAAGGAGCGCTTCGGCGTCGACGACGAGGTGCTGGCCCCCTACCTGGAGCTGTGGAGCGTGGTCACCAAGGGGGTCTTCTACGCCGCCAACCGCCTCTACGGCATCACCTTCCACGAGCGCGAGGACCTGGCCGAGCACATGTACGCCCCGGGCGTGAAGGTCTGGGAGGTGCGCGACGGTGAGGACGCCCAGGCGCCGGTCATGGGTCTGTTCGTCGGCGACTACTACGCCCGGGCGGGCAAGTCCGGCGGCGCCTGGATGGACAGCCTCGTCACCGGCTCAACGCTCACCGGCCGCAAGCCGGTCGTCATCAACTGTTGCAATATCGAGCAGCCCACCTCCGGCCGGGTCCTGCTGACCTGGGATGAGGTCGTTACGTGCTTCCACGAGTTCGGGCACGCTCTGCATGCCCTGTTCTCCCAGGCCCGCTACCCCTCGGCCTCCGGAACGGCCGTGCCCCGCGACGTCGTCGAGTTCCCCAGCCAGGTCAACGAGAAGTGGGCGCTTCACCCCGAGGTGCTGTCCTCCTACGCGCGCCACGTGGACACCGGCGAGCCCATGCCCTCCGACCTCGCCGAGCAGCTGCGCGGCCAGGGCACCTTCGGCCAGGGCTACGCCACCACCGAGTACCTGGGAGCCGCCCTGCTCGACCAGGCCTGGCACACCCTGGCCCCCGACGAGGTTCCCGGAGACGTTGCCGAGGTGGAGGACTTCGAGCACCGGGCCCTGGCCCAGGCCGGAGTCGATGACGCGCTCGTGCCTCCCCGCTACCGCTCCACCTACTTCTCCCACGTCTTCGCCGGGGGCTACAGCGCCGCCTACTACGCCTACATCTGGAGCGAGGTCATGGACGCCGATGCCGTCGAGTGGTTCACCACTGACGGCGCGATCGACGGCGATCTCGGCCTGAATCGTCGGGCCGGAGAGATCTTCCGTCGCGAGTTCCTCTCCCGCGGCGACTGTCGAGACCCCCTGGTCTCCTATCGGGCCTTCACTGGGCGTGAACCCGGCATCCTGCCTCTTCTTCAACGTCGCGGACTTGCCTGA","MSETTDGTDLPESNVFAKPWPLDLGLPGFTAVDHADIEPAIRAGMAVERQEWEAIATNEDAPTIANTVEALERSGELLERALTVLDALTSATDCPDLDELEEALAPELAAHSDAYHLDSRLYRRFKALDELVSQAPEGQAARDADGTVIDAEAARLIRLTVEEFERNGVGLDEADTQALKEINARVNALKMRFSVLVTEAMHAAGVTNVTVPPALATTRPHGARLALLETSMSRGLGEQGAFGDTRGIVLELARLRAERAVLLGFPHHAALVAAESAARTTEAVSELLARLTTPAMDNARADAQVYAARMDLDPQTQAGETFGPADWPLYEAAERKERFGVDDEVLAPYLELWSVVTKGVFYAANRLYGITFHEREDLAEHMYAPGVKVWEVRDGEDAQAPVMGLFVGDYYARAGKSGGAWMDSLVTGSTLTGRKPVVINCCNIEQPTSGRVLLTWDEVVTCFHEFGHALHALFSQARYPSASGTAVPRDVVEFPSQVNEKWALHPEVLSSYARHVDTGEPMPSDLAEQLRGQGTFGQGYATTEYLGAALLDQAWHTLAPDEVPGDVAEVEDFEHRALAQAGVDDALVPPRYRSTYFSHVFAGGYSAAYYAYIWSEVMDADAVEWFTTDGAIDGDLGLNRRAGEIFRREFLSRGDCRDPLVSYRAFTGREPGILPLLQRRGLA$","Peptidyl-dipeptidase","Cytoplasm, Extracellular","Zn-dependent oligopeptidases","peptidyl-dipeptidase ","Peptidyl-dipeptidase Dcp","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR001567
Domain

Peptidase M3A and M3B, thimet/oligopeptidase F
PF01432	$\"[214-682]T$	Peptidase_M3

noIPR
unintegrated

unintegrated
G3DSA:1.10.1370.10	$\"[167-682]T$	no description
PTHR11804	$\"[346-683]T$	PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED
PTHR11804:SF8	$\"[346-683]T$	PEPTIDYL-DIPEPTIDASE DCP

","BeTs to 9 clades of COG0339COG name: Zn-dependent oligopeptidasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0339 is ------y--d---cefghsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB001567 (Peptidase M3) with a combined E-value of 1.4e-21. IPB001567A 409-420 IPB001567B 457-484 IPB001567D 604-614","Residues 18-80 are 58% similar to a (HYDROLASE ZINC METALLOPROTEASE OLIGOPEPTIDASE A PEPTIDYL-DIPEPTIDASE CARBOXYPEPTIDASE DCP DIPEPTIDYL II) protein domain (PDA0Y0C2) which is seen in Q8NNA3_CORGL.Residues 283-426 are 54% similar to a (HYDROLASE METALLOPROTEASE ZINC OLIGOPEPTIDASE A PEPTIDYL-DIPEPTIDASE MITOCHONDRIAL CARBOXYPEPTIDASE ENDOPEPTIDASE INTERMEDIATE) protein domain (PD430743) which is seen in Q8NNA3_CORGL.Residues 409-592 are 66% similar to a (HYDROLASE METALLOPROTEASE ZINC OLIGOPEPTIDASE A PEPTIDYL-DIPEPTIDASE MITOCHONDRIAL CARBOXYPEPTIDASE ENDOPEPTIDASE DCP) protein domain (PD607536) which is seen in Q87D30_XYLFT.Residues 597-682 are 63% similar to a (HYDROLASE METALLOPROTEASE ZINC OLIGOPEPTIDASE A PEPTIDYL-DIPEPTIDASE MITOCHONDRIAL CARBOXYPEPTIDASE ENDOPEPTIDASE DCP) protein domain (PD002945) which is seen in Q8PQS3_XANAC.","","-49% similar to PDB:1Y79 Crystal Structure of the E.coli Dipeptidyl Carboxypeptidase Dcp in Complex with a Peptidic Inhibitor (E_value = 7.1E_108);-41% similar to PDB:1S4B Crystal structure of human thimet oligopeptidase. (E_value = 7.8E_30);-41% similar to PDB:2O36 Crystal structure of engineered thimet oligopeptidase with neurolysin specificity in neurotensin cleavage site (E_value = 5.1E_29);-41% similar to PDB:2O3E Crystal structure of engineered neurolysin with thimet oligopeptidase specificity for neurotensin cleavage site. (E_value = 1.5E_28);-41% similar to PDB:1I1I NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE (E_value = 9.6E_28);","Residues 214 to 682 (E_value = 3.6e-95) place ANA_0657 in the Peptidase_M3 family which is described as Peptidase family M3.","","oligopeptidases ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0658","694036","695136","1101","5.25","-12.06","39306","ATGGCTCGCGTCACCATCGTCGGCGGTGGATACGGTGGCATCACCGCCGCCAAGGCCCTCGACGACGTCGCCGAGGTCACCCTCGTGGAGCAGAAGGACACCTTCGTCAGCCACGCCGCGGCGCTGCGCGCTGCGGTCGACCGTGACTGGGCGGAGAAGATCTTCCTGCCCTACGACAAGCTCCTCACCAACGGGCGCGTCGTTCACGGAACGGCGCTGACCGTGCGAGGCACCACCGTCGAGGTCTCCGGTCACGGGCAGATCGAGGCTGACTACCTGGTGCTGGCCACCGGGACCGCCTACCCCTTCCCCGCCAAGCACATGGAGTCCTCCTCCGTCATCGCCAAGGCCCGTATCGAGCGCGTCCACTCCAACCTCGAGCAGTCCTCGCGAGTGCTCATCTTGGGCGCCGGCGCCGTCGGCATCGAGCTGGCCGGTGAGATCACCTCGGCCTTCCCGCAGGTCAAGGTGACCATGCTGGAGGCCGCCGACAGGATTCTGCCCGCCGGTGACTACAAGCCGGAGATTCGTGAGGCCATCGCCGACCAGCTCGCTCAGCGCAGGGTGGAGATCCTCACCGGTGACTCCCTCAGCTTCCTGCCCCCGGTCGACGTCGGCGTGCTCTCGCCCTTCCGGGTCACCACCCAGGGCGGGCGCCAGCTCGAGGCCGACATGTGGTTCCGTGCCTACGGCTCGGCGGCCGCCACCGGATTCCTCAGCGAGGACTATGACGAGGTGCGCCACTACGACGGCACGATCCGCGTCGACGAGTACCTGCGCGTGGTGGACCACCCCGGTGTCTGGGCCATCGGAGACATCACCGACGTGCGCGAGTCCAAGCGCGCCGACGCCGCCCGCGCCCATGCCCGAGTGGTCGCCAGCAACATCGCCGACATGATCGCGGGCCGCGAGCCCTCCGCGACCTACACGCCCGGAACCGAGCGGATCATCCTGCCCCTGGGGCCCGACGGCGGTGCCTCCCAGATCCTGCGCGACGGTGTGCGCGTCGTCGTCGGCCCCGAGGAGACCAGCAAGATCAAGGGAGAGGACCTCTTCCTGGGCTTCATCCGTCAGGAGCTGGGAGTCGAGTCGGAGGCCTGA","MARVTIVGGGYGGITAAKALDDVAEVTLVEQKDTFVSHAAALRAAVDRDWAEKIFLPYDKLLTNGRVVHGTALTVRGTTVEVSGHGQIEADYLVLATGTAYPFPAKHMESSSVIAKARIERVHSNLEQSSRVLILGAGAVGIELAGEITSAFPQVKVTMLEAADRILPAGDYKPEIREAIADQLAQRRVEILTGDSLSFLPPVDVGVLSPFRVTTQGGRQLEADMWFRAYGSAAATGFLSEDYDEVRHYDGTIRVDEYLRVVDHPGVWAIGDITDVRESKRADAARAHARVVASNIADMIAGREPSATYTPGTERIILPLGPDGGASQILRDGVRVVVGPEETSKIKGEDLFLGFIRQELGVESEA$","FAD-dependent pyridine nucleotide-disulphide oxidoreductase","Cytoplasm","putative protein","apoptosis-inducing factor (AIF)-like mitochondrion-associated inducer of death","FAD-dependent pyridine nucleotide-disulphide oxidoreductase","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Russel M., Model P. Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 1988. 263(18):9015-9019. PMID: 3288628Cohen G., Argaman A., Schreiber R., Mislovati M., Aharonowitz Y. The thioredoxin system of Penicillium chrysogenum and its possible role in penicillin biosynthesis. J. Bacteriol. 1994. 176(4):973-984. PMID: 8106340Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N. Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 1990. 265(18):10535-10540. PMID: 2191951Xu X.M., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T. Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1. J. Biochem. 1991. 109(5):678-683. PMID: 1917890Mathieu I., Meyer J., Moulis J.M. Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum. Biochem. J. 1992. 285:255-262. PMID: 1637309Waksman G., Krishna T.S., Williams Jr C.H., Kuriyan J. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. J. Mol. Biol. 1994. 236(3):800-816. PMID: 8114095McKie J.H., Douglas K.T. Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett. 1991. 279(1):5-8. PMID: 1995341","","","

InterPro
IPR000103
Domain

Pyridine nucleotide-disulphide oxidoreductase, class-II
PR00469	$\"[3-25]T$ $\"[91-99]T$ $\"[127-151]T$ $\"[262-280]T$	PNDRDTASEII

InterPro
IPR001327
Domain

Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139	$\"[102-168]T$	Q6AQU4_BBBBB_Q6AQU4;
PF00070	$\"[3-98]T$ $\"[131-194]T$	Pyr_redox

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368	$\"[3-25]T$ $\"[93-102]T$ $\"[131-156]T$ $\"[267-274]T$	FADPNR
PF07992	$\"[250-278]T$	Pyr_redox_2

InterPro
IPR013166
Domain

Citrate lyase ligase, C-terminal
SM00764	$\"[109-200]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[2-105]T$ $\"[122-312]T$	no description
PTHR22915	$\"[3-342]T$	NADH DEHYDROGENASE-RELATED
PTHR22915:SF5	$\"[3-342]T$	APOPTOSIS-INDUCING FACTOR (AIF)-LIKE MITCHONDRION-ASSOCIATED INDUCER OF DEATH (P53-RESPONSIVE GENE 3) (AMID PROTEIN)

","BeTs to 10 clades of COG0446COG name: Uncharacterized NAD(FAD)-dependent dehydrogenasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0446 is aompkzyqvdrlbcefgh---j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 1.9e-12. IPB013027A 3-25 IPB013027C 131-156 IPB013027E 267-274 IPB013027A 131-153***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase, class-II) with a combined E-value of 1.3e-07. IPB000103A 4-22 IPB000103E 262-299 IPB000103A 132-150","Residues 25-306 are 43% similar to a (SIMILAR HOMO SAPIENS APOPTOSIS-INDUCING FACTOR) protein domain (PD850396) which is seen in Q875G2_PODAN.Residues 40-185 are 50% similar to a (HXT17-COS10) protein domain (PD462525) which is seen in YN9B_YEAST.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 98 (E_value = 0.0034) place ANA_0658 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 3 to 278 (E_value = 9.4e-06) place ANA_0658 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 131 to 231 (E_value = 2.5e-07) place ANA_0658 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0659","695597","695403","195","6.44","-0.08","6753","GTGGGCCCCACCGCCGAGAGATGGGCTGAGGAACGTCGTCCGTCCAGCCAGGGACCTCAGTCAGTCCTCGTCGTCGTAGTCCTCATCATCCTCATCATCGTCATCATCGCTGTCGTCGTAGTCGTCGTCATCCTCGTCGTACTCGCCGTCGTCGTAGTCCTCATCATCATCGTCGTCCTCATCGTCGCCATCTGA","VGPTAERWAEERRPSSQGPQSVLVVVVLIILIIVIIAVVVVVVILVVLAVVVVLIIIVVLIVAI$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-49]?$	signal-peptide
tmhmm	$\"[15-37]?$ $\"[43-63]?$	transmembrane_regions

InterPro
IPR002491
Family

Periplasmic binding protein
PF01497	$\"[100-369]T$	Peripla_BP_2
PS50983	$\"[102-394]T$	FE_B12_PBP

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[36-66]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1980	$\"[96-189]T$	no description

","BeTs to 14 clades of COG0614COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, periplasmic componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0614 is aompkz--vdrlbcefgh-nuj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","Residues 100-154 are 76% similar to a (ABC TRANSPORTER BINDING PERIPLASMIC LIPOPROTEIN FERRIC IRON TRANSPORTER ANGUIBACTIN-BINDING SOLUTE-BINDING) protein domain (PD786250) which is seen in P94421_BACSU.Residues 300-357 are similar to a (ABC TRANSPORTER IRON PERIPLASMIC LIPOPROTEIN FERRIC BINDING COMPOUND ANGUIBACTIN-BINDING COMPOUND-BINDING) protein domain (PD121590) which is seen in Q8YCC5_BRUME.Residues 306-377 are 56% similar to a (SIMILAR PERIPLASMIC UPTAKE SIDEROPHORE BINDING) protein domain (PDA1C9H7) which is seen in Q7N7H5_PHOLL.","","-47% similar to PDB:2CHU CEUE IN COMPLEX WITH MECAM (E_value = 4.0E_33);","Residues 100 to 369 (E_value = 1e-31) place ANA_0661 in the Peripla_BP_2 family which is described as Periplasmic binding protein.","","anguibactin-binding protein (III)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0662","696814","697836","1023","10.88","12.57","35545","ATGAGCCCCAGGAACCCCGTTGCGGCCTGGGAACACAGGCCACGACGGTCGGGCCTGTCGCTCCTGGTCGGTGGCCTTCTGCTTCTGCTCGTCCTGGGACTCGTGTCGGTGTGTATCGGAGTGGCAGACTTCGATCCGGTGGATCTGGTTCGCACCGGTTCGCAGGGCCGCTCCATGCGCCTCTTCATGGTCTCGAGAGTGCCGCGCACCCTGGCGGCCGTCCTCGCCGGTTCGGGCATCGCTGTGGCGGGCGCCGTCATGCAGATGAGTGTGCGCAACCGTTTCGTGTCCCCGACCACGGCAGGCACGACTCAGTTCGCCGTCGTCGGGCTGCTGCTTGTGGCTCTCTTCGCACCGGGCACCAGTGTTCTGGCGAAGATGCTGGTGGCCTCGGCATGCGCGGTAGCGGGCTCGGCAGTCTTCCTGTGGCTCCTGCGACTGCTGCCCCACCGGCGCACGTCCGATGACGTCACGGTCCCCCTGATCGGCCTCATGCTCGGTGGCGTGGTCGGAGCGGGTACCACCTTCGTGGCCTGGCGCTACGACTTGCTGCAGTCACTAGGTTCCTGGACGGCCGGCGACCTGTCCCGGGTGCTGGCCGGCCGCTATGAGCTGCTCTGGCTGGTGGCGCTCATCGTCCTGCTGCTCTATCTCGCCGCCGACCGCCTCACTGTGGCGAGCCTTGGGGCGGAGACGGCCACCGGGCTCGGGCTGAGCTATCACCGCACCATCAACCTCACGATCATGGCCGCAGCCGTCATGACGGCGGTCAGCGTCGTCGTGGTCGGGAGCCTGCCGTTCCTCGGGCTCGTGGTACCCAACATCGTCTCCCGGCTCATAGGGGACAATCTGCGCCGGAGTCTTCCGATCATTGCCGTCGGTGGTGCTGTTCTGACGCTGGGGTGCGACGTCGTCGGACGTGTGGTCCGCTACCCCTACGAGGTTCCGCTGTCCGTCATCATGGGGGTCGTCGGCGCCGGCGTCTTCACCGTGCTCATCCTGCGAGGTGTGGAACGTGGCTGA","MSPRNPVAAWEHRPRRSGLSLLVGGLLLLLVLGLVSVCIGVADFDPVDLVRTGSQGRSMRLFMVSRVPRTLAAVLAGSGIAVAGAVMQMSVRNRFVSPTTAGTTQFAVVGLLLVALFAPGTSVLAKMLVASACAVAGSAVFLWLLRLLPHRRTSDDVTVPLIGLMLGGVVGAGTTFVAWRYDLLQSLGSWTAGDLSRVLAGRYELLWLVALIVLLLYLAADRLTVASLGAETATGLGLSYHRTINLTIMAAAVMTAVSVVVVGSLPFLGLVVPNIVSRLIGDNLRRSLPIIAVGGAVLTLGCDVVGRVVRYPYEVPLSVIMGVVGAGVFTVLILRGVERG$","ABC-type cobalamin/Fe3+-siderophores transport system, permease component","Membrane, Cytoplasm","ferrichrome ABC transporter (AP001510)","K02015 iron complex transport system permease protein","transport system permease protein","","","","","

InterPro
IPR000522
Family

Bacterial transport system permease protein
PF01032	$\"[28-335]T$	FecCD

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[67-87]?$ $\"[99-119]?$ $\"[125-145]?$ $\"[160-180]?$ $\"[199-219]?$ $\"[248-268]?$ $\"[287-305]?$ $\"[315-335]?$	transmembrane_regions

","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 7","***** IPB000522 (FecCD transport family) with a combined E-value of 4.5e-34. IPB000522A 66-107 IPB000522C 259-277 IPB000522D 312-335","Residues 69-335 are 75% similar to a (PERMEASE ABC TRANSPORTER IRON SYSTEM TRANSPORTER FERRICHROME MEMBRANE COMPOUND IRONIII) protein domain (PD247701) which is seen in Q8YCC6_BRUME.Residues 199-335 are 72% similar to a (AGR_C_4489P TRANSPORTER MEMBRANE ABC SPANNING) protein domain (PD797327) which is seen in Q8UCK9_AGRT5.","","No significant hits to the PDB database (E-value < E-10).","Residues 28 to 335 (E_value = 3.1e-45) place ANA_0662 in the FecCD family which is described as FecCD transport family.","","ABC transporter (AP001510) (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0663","697829","698812","984","11.18","8.88","34708","GTGGCTGACGCGCTGTCCGGACGTCGTCGCCGGGAGAACCGGCGTTCCATCCTCCGCCTGGTGGTCGTCCTGCTCCTGGTGCTGGTGGCCAGCGGCGTCTTCCTGGTCATCAACGCCTTCGACCCGCTTCTGGTCCTGCCCTACCGGTTGCCCTCCCTCGGGGCGATGCTGTGTGTGGGATGGGCCAGTGGCGTGTCCACCGTCATGTTCCAGACGGTCACCGGCAACCGGATCCTCACGCCCTCCGTGCTCGGTCTGGATGCGCTCTACGCCCTGCTGCAGGTGGTTCTTCTTCTCGTGCTGGGGGCGGCGGGACTCTCCTCGCTGCCGGACCTGGGTGCTTTCGTCCTGACGCTTCTGGTAATGATCGGTGTGTCCGCGGCGCTCATGGGTGCCGTGCTCAGTGCCAGGCGCTCGGTGACCACTCTGGTGCTGCTGGGCATCGTGCTGGGAACCTTCCTGCGCTCTGGGACCACCTTCATCCAGCGGCTCCTGGATCCCAATGACTTCCTCATCCTTCAGGACCGGCTCTTCGCCTCCTTCGGCTCGATCAACCCCGATCTGCTGGTACTCTCGCTGATCCTGACCGTCGCGGTGTCAATTCTGGCGATCCGGGAGCTGCGGGCGCTCGATGTCGTGGCTCTCGGGCCCGATATCGCCACCGCACTCGGAGTCGATCACCGTCGTATCAGCCGGCGCGTGATGTTCATGGTGGCCGTGCTGGTATCCGTGTCCACGGCCCTGGTCGGGCCGATCATGTTCCTGGGCCTCCTCGTTGCCCACCTGGCCTACTGGGCCGCCGGTACCAACCGCCACGTGGTCACCGTGCCCATGGCGGCACTCGTCGCCATGCTCGTCCTGGTGACCGGACAGACAGTGCTGGCTCATGTCCTGGATGCCGACAACGTCCTGTCCGTCATCATCGAGTTCCTCGGCGGGCTCACCCTCATCGCCCTCCTCATCAGCTCCAGGAGACGTTCATGA","VADALSGRRRRENRRSILRLVVVLLLVLVASGVFLVINAFDPLLVLPYRLPSLGAMLCVGWASGVSTVMFQTVTGNRILTPSVLGLDALYALLQVVLLLVLGAAGLSSLPDLGAFVLTLLVMIGVSAALMGAVLSARRSVTTLVLLGIVLGTFLRSGTTFIQRLLDPNDFLILQDRLFASFGSINPDLLVLSLILTVAVSILAIRELRALDVVALGPDIATALGVDHRRISRRVMFMVAVLVSVSTALVGPIMFLGLLVAHLAYWAAGTNRHVVTVPMAALVAMLVLVTGQTVLAHVLDADNVLSVIIEFLGGLTLIALLISSRRRS$","ABC-type cobalamin/Fe3+-siderophores transport system, permease component","Membrane, Cytoplasm","ferric anguibactin transport system permeaseprotein fatC","K02015 iron complex transport system permease protein","transport system permease protein","","","","","

InterPro
IPR000522
Family

Bacterial transport system permease protein
PF01032	$\"[18-282]T$	FecCD

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[21-39]?$ $\"[53-73]?$ $\"[88-108]?$ $\"[114-134]?$ $\"[143-165]?$ $\"[184-204]?$ $\"[238-260]?$ $\"[303-323]?$	transmembrane_regions

","BeTs to 17 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 7","***** IPB000522 (FecCD transport family) with a combined E-value of 1.1e-28. IPB000522A 49-90 IPB000522C 246-264 IPB000522D 299-322","Residues 45-321 are 69% similar to a (PERMEASE ABC TRANSPORTER IRON SYSTEM TRANSPORTER FERRICHROME MEMBRANE COMPOUND IRONIII) protein domain (PD247701) which is seen in Q8YCC7_BRUME.Residues 158-235 are 73% similar to a (PERMEASE ABC TRANSPORTER TRANSPORTER FERRIC SYSTEM FERRICHROME MW0696 IRON-COMPOUND IRON) protein domain (PD173656) which is seen in Q46004_CAMCO.Residues 250-324 are 61% similar to a (PERMEASE ABC FERRIC SYSTEM TRANSPORTER IRON ANGUIBACTIN TRANSPORTER MEMBRANE MW0696) protein domain (PD754066) which is seen in Q6FYY2_BARQU.","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 322 (E_value = 1.9e-14) place ANA_0663 in the FecCD family which is described as FecCD transport family.","","anguibactin transport system permease protein fatC (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0664","698809","699567","759","5.48","-7.36","27605","ATGATCGCAGTTCGTAGCCTTGCCAAGTCCTACGGTGAGCGTCAGGTGCTCTCCGACGTCGACCTCGACCTGCCGGCCGGCGGAGTCATCGGGCTGGTTGGTGCCAACGGGGCCGGTAAGTCCACGCTGTTGTCCGTGATGGCCAGACTCCTGGGAGCCGACGCCGGCACGGTGGAAGTCGGTGGTCTGAACGTCGCCACCGCCCCGGGGCGCCAGCTCGCCACCGTTCTGTCCGTCCTCAAGCAGGACAACCATCTCGCCGTGCGACTGACTGTGCGTGACCTCGTGGGATTTGGCCGCTATCCGCACAATCGGGGACGCCCCACCGAGCACGATGAGACGATCGTCGACCAGGCCCTGGAGTGGATGGACCTGACAGAGTTGGCCGACCGCTACCTCGACGAGATGTCCGGTGGGCAGCGTCAGCGGGCCTTCGTCGCCATGGTGCTGGCCCAGGAGACTCCCTACATGCTCCTGGACGAGCCCCTCAACAACCTGGACATGGTCCACTCGGTGGCCATGATGCGTCGTCTACGCGCTGCCGCCCACGAGCTCGAGCGCACGGTCGTGGTTGTCATGCATGACATCAATATGGCTGCCGCATGGTTGGACCGGATCGTCGCCATGCGTGAGGGCCGAGTCGTCCTTCAAGGAACCCCCGAGGAGACCATGACCCGGGAGTGTCTGAGTGAGGTCTTCGGTATGGATGTACCGGTCCATGAGATCGACGGCAGGCGCATCGCCCTCGTCTGGGGCTGA","MIAVRSLAKSYGERQVLSDVDLDLPAGGVIGLVGANGAGKSTLLSVMARLLGADAGTVEVGGLNVATAPGRQLATVLSVLKQDNHLAVRLTVRDLVGFGRYPHNRGRPTEHDETIVDQALEWMDLTELADRYLDEMSGGQRQRAFVAMVLAQETPYMLLDEPLNNLDMVHSVAMMRRLRAAAHELERTVVVVMHDINMAAAWLDRIVAMREGRVVLQGTPEETMTRECLSEVFGMDVPVHEIDGRRIALVWG$","ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component","Cytoplasm, Membrane","ferrichrome ABC transporter (ATP-bindingprotein)","putative iron ABC transporter; ATP-binding protein ","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[135-172]T$	Q6FYY1_BARQU_Q6FYY1;
PF00005	$\"[27-212]T$	ABC_tran
PS50893	$\"[2-236]T$	ABC_TRANSPORTER_2
PS00211	$\"[136-150]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[26-213]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[2-234]T$	no description
PTHR19222	$\"[2-243]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31	$\"[2-243]T$	METAL ABC TRANSPORTER

","BeTs to 16 clades of COG1120COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1120 is aompk---vdrlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 4","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 4.2e-24. IPB005074C 16-63 IPB005074D 124-167***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.7e-22. IPB013563A 16-50 IPB013563C 133-160 IPB013563D 188-240***** IPB005116 (TOBE domain) with a combined E-value of 2e-13. IPB005116A 34-50 IPB005116C 136-149 IPB005116D 156-175***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 5.7e-09. IPB010509B 27-52 IPB010509D 131-175***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.3e-08. IPB010929K 14-58 IPB010929M 133-179 IPB010929C 118-151","Residues 1-212 are 49% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD756741) which is seen in Q8A5R4_BACTN.Residues 1-167 are 49% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD738131) which is seen in Q830L1_ENTFA.Residues 1-120 are 52% similar to a (PM1309 ATP-BINDING) protein domain (PD390268) which is seen in Q9CLC9_PASMU.Residues 2-234 are 43% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 4-218 are 48% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 8-215 are 45% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 16-152 are similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 20-65 are 78% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8UCK7_AGRT5.Residues 22-172 are 47% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 79-121 are 88% similar to a (ATP-BINDING ABC TRANSPORTER IRON TRANSPORTER COMPONENT FERRICHROME IRONIII SYSTEM COMPOUND) protein domain (PD001985) which is seen in Q8UCK7_AGRT5.Residues 120-249 are 55% similar to a (IRONIII ABC-TYPE SYSTEM ATP ATP-BINDING BINDING) protein domain (PDA106C0) which is seen in Q6M0S1_METMP.Residues 123-240 are 54% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 123-250 are 53% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.Residues 125-226 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 135-172 are 92% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6FYY1_BARQU.Residues 139-194 are 75% similar to a (CEUD ATP-BINDING) protein domain (PD055560) which is seen in Q46005_CAMCO.Residues 195-249 are 70% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER IRON FERRICHROME COMPOUND IRONIII ABC-TYPE ATPASE) protein domain (PD799794) which is seen in Q8FVY9_BRUSU.","","-47% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 7.3E_21);-47% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 7.3E_21);-47% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 7.3E_21);-47% similar to PDB:2AWN Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg) (E_value = 7.3E_21);-47% similar to PDB:2AWO Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ADP-Mg) (E_value = 7.3E_21);","Residues 27 to 212 (E_value = 8.3e-48) place ANA_0664 in the ABC_tran family which is described as ABC transporter.","","ABC transporter (ATP-binding protein) (AP001510)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0665","700586","699606","981","5.94","-6.62","34717","ATGGAGCACAGGAGACTCGGCCGGACCGGCCTGCGTGTGTCCTCCGTGGGCCTGGGCACGATGACCTGGGGCCGGGACACCGATGAGCTCGAGGCCAAGGAACAGCTCGACATCTTCCTCGATGCCGGGGGCACGCTCGTGGACACCGCCGCCTCCTACGGCGAGGGCGTCAGCGAGGAGGTGATCGGCATGCTCCTGCGCGAGCACGTGGATCGCCAGGACCTCGTCCTGGTCTCCAAGGCCGGTGTGCGCACCTGGCGAACCGGGGAGCGGTCCTCGGTGGCTGACGCCTCCCGCGGCTCGCTGCTGGACACGCTCGACACCAGCCTGGCCCGCCTGGGCACCGATCACCTGGACCTCCTGCTGGTCCAGGTGCCCGATTCCAGCACCTCCCTGGAGGAGACGGCCCACGCACTGAGCCTGGCCGTCTCCTCCGGGCGCACCCGGTACGTGGGCATCGCCAACCACCCCGCGTGGGCTTCGGTGCGCATACATGATCTGCTCAGCGAGTGCGGCCGGGGTCCGGGGCTGGCGGCCGTCGAGGTGGAGCACTCACTGCTCTCCCGAGGTATCGAGCGCGAGCTGCGGCCCGCCTCGCAGGCCCTGGGCTTCGGCATCCTCGGCTACGCCCCCCTGGGTCGGGGCGTGCTCACCGGCAAGTACCGGGCGACGATTCCACCGGACTCACGGGCCGCCTCCCCGCACCTGCGCTCCTACGTGTCCCCCTACCTGGGCGAGGCGCACCGGGGTGTGGTTGAGGCCGTGGCCACTGCCGCCTCGGGCCTGGACCGTAAGCCGGCCGAGGTCGCACTCGCTTGGGCCCGCGATGCCCCCGGGATCGCCTCAACCATTGTGGGTGCCCGCACTCCGGCTCAGCTCCAGGGCGTGCTGTCGGCAGACGACCTGGAGCTTCCGGTCCAGATCCGACACGCCCTGGACGAGGTCACCTCCGTCCAGCTCGGCTACCCCGAGCGCTTCTAA","MEHRRLGRTGLRVSSVGLGTMTWGRDTDELEAKEQLDIFLDAGGTLVDTAASYGEGVSEEVIGMLLREHVDRQDLVLVSKAGVRTWRTGERSSVADASRGSLLDTLDTSLARLGTDHLDLLLVQVPDSSTSLEETAHALSLAVSSGRTRYVGIANHPAWASVRIHDLLSECGRGPGLAAVEVEHSLLSRGIERELRPASQALGFGILGYAPLGRGVLTGKYRATIPPDSRAASPHLRSYVSPYLGEAHRGVVEAVATAASGLDRKPAEVALAWARDAPGIASTIVGARTPAQLQGVLSADDLELPVQIRHALDEVTSVQLGYPERF$","Aldo/keto reductase","Cytoplasm","rhizopine catabolism protein mocA","putative oxidoreductase","aldo/keto reductase","","Bohren K.M., Bullock B., Wermuth B., Gabbay K.H. The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 1989. 264(16):9547-9551. PMID: 2498333Schade S.Z., Early S.L., Williams T.R., Kezdy F.J., Heinrikson R.L., Grimshaw C.E., Doughty C.C. Sequence analysis of bovine lens aldose reductase. J. Biol. Chem. 1990. 265(7):3628-3635. PMID: 2105951Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A. An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 1992. 257(5066):81-84. PMID: 1621098Borhani D.W., Harter T.M., Petrash J.M. The crystal structure of the aldose reductase.NADPH binary complex. J. Biol. Chem. 1992. 267(34):24841-24847. PMID: 1447221Gulbis J.M., Zhou M., Mann S., MacKinnon R. Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. Science 2000. 289(5476):123-127. PMID: 10884227","","","

InterPro
IPR001395
Family

Aldo/keto reductase
PD000288	$\"[6-293]T$	Q828M9_STRAW_Q828M9;
PR00069	$\"[108-126]T$ $\"[139-156]T$	ALDKETRDTASE
G3DSA:3.20.20.100	$\"[1-315]T$	no description
PTHR11732	$\"[1-222]T$ $\"[245-288]T$	ALDO/KETO REDUCTASE
PF00248	$\"[7-317]T$	Aldo_ket_red

noIPR
unintegrated

unintegrated
PTHR11732:SF15	$\"[1-222]T$ $\"[245-288]T$	ALDO/KETO REDUCTASE

","BeTs to 16 clades of COG0667COG name: Predicted oxidoreductases (related to aryl-alcohol dehydrogenases)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0667 is -o-p-zyqvdrlbcefg-s-uj--t-Number of proteins in this genome belonging to this COG is 3","***** IPB001395 (Aldo/keto reductase) with a combined E-value of 9.4e-46. IPB001395A 13-25 IPB001395B 39-63 IPB001395C 70-82 IPB001395D 109-126 IPB001395E 135-170 IPB001395F 178-213 IPB001395G 253-307","Residues 1-220 are 43% similar to a (OXIDOREDUCTASE) protein domain (PDA0J6Q5) which is seen in Q9F3N3_STRCO.Residues 1-219 are 48% similar to a (OXIDOREDUCTASE ALDO/KETO REDUCTASE FAMILY) protein domain (PDA0J6Q8) which is seen in Q98CQ3_RHILO.Residues 1-155 are 49% similar to a (TRANSMEMBRANE OXIDOREDUCTASE) protein domain (PDA18313) which is seen in Q92SS1_RHIME.Residues 1-302 are 47% similar to a (OXIDOREDUCTASE) protein domain (PD521436) which is seen in Q92SD9_RHIME.Residues 1-221 are 48% similar to a (ALDO-KETO REDUCTASE) protein domain (PDA0J6R1) which is seen in O25804_HELPY.Residues 1-222 are 55% similar to a (OXIDOREDUCTASE ALDO/KETO REDUCTASE FAMILY) protein domain (PDA1A4R5) which is seen in Q881G1_PSESM.Residues 1-299 are 46% similar to a (ALDO/KETO REDUCTASE FAMILY) protein domain (PDA181S1) which is seen in Q75H72_EEEEE.Residues 1-235 are 44% similar to a (OXIDOREDUCTASE) protein domain (PDA0J6Q4) which is seen in Q82P83_STRAW.Residues 1-325 are 49% similar to a (CHANNELS IONIC K CHANNEL BETA-SUBUNIT) protein domain (PDA189C4) which is seen in O82064_SOLTU.Residues 1-273 are 48% similar to a (ALDO/KETO REDUCTASE) protein domain (PDA192L0) which is seen in Q6F1L4_MESFL.Residues 2-238 are 51% similar to a (CHANNEL IONIC O59826 POTASSIUM SUBUNIT POMBE SCHIZOSACCHAROMYCES) protein domain (PDA1B370) which is seen in Q6CI80_EEEEE.Residues 2-217 are 51% similar to a () protein domain (PDA0K0A3) which is seen in Q7S2E8_NEUCR.Residues 4-273 are 47% similar to a (ALDO-KETO REDUCTASE) protein domain (PDA1C8N6) which is seen in Q7VG62_HELHP.Residues 4-213 are 44% similar to a (GLL1894) protein domain (PDA0T5N9) which is seen in Q7NJD8_GLOVI.Residues 6-293 are 66% similar to a (REDUCTASE OXIDOREDUCTASE ALDO/KETO FAMILY DEHYDROGENASE OXIDOREDUCTASE NADP ALDO-KETO 1.1.1.- ACID) protein domain (PD000288) which is seen in Q828M9_STRAW.Residues 9-206 are 45% similar to a (OXIDOREDUCTASE DEHYDROGENASES OXIDOREDUCTASES RELATED PREDICTED ARYL-ALCOHOL) protein domain (PD611486) which is seen in Q8NU47_CORGL.Residues 9-304 are 45% similar to a () protein domain (PD756934) which is seen in Q8FUB8_COREF.Residues 10-304 are 38% similar to a (ALDO-KETO REDUCTASE POSSIBLE FAMILY OXIDOREDUCTASE) protein domain (PD520489) which is seen in Q8G5I8_BIFLO.Residues 11-326 are 43% similar to a (DEHYDROGENASE) protein domain (PDA0J2I3) which is seen in Q6UEH5_ASPPA.Residues 11-224 are 50% similar to a (ENZYME ALDO/KETO REDUCTASE FAMILY) protein domain (PDA0J6R0) which is seen in Q9X5G7_STRCL.Residues 11-317 are 41% similar to a (ALDO-KETO REDUCTASE FAMILY) protein domain (PD765756) which is seen in Q8ZXA1_PYRAE.Residues 11-231 are 50% similar to a (ALDO/KETO REDUCTASE) protein domain (PDA0J6Q9) which is seen in Q9RS66_DEIRA.Residues 14-218 are 44% similar to a (REDUCTASE ALDOSE) protein domain (PD290704) which is seen in O51478_BORBU.Residues 15-217 are 47% similar to a (ALDO/KETO REDUCTASE) protein domain (PDA1B2B2) which is seen in Q6L0N6_PICTO.Residues 17-215 are 47% similar to a () protein domain (PDA192E4) which is seen in Q74HC5_LACJO.Residues 17-305 are 41% similar to a (D-THREO-ALDOSE 1-DEHYDROGENASE) protein domain (PD756940) which is seen in Q8ETF4_OCEIH.Residues 169-315 are 53% similar to a (OXIDOREDUCTASE) protein domain (PD737981) which is seen in Q82PN0_STRAW.Residues 213-293 are 65% similar to a (OXIDOREDUCTASE) protein domain (PD700282) which is seen in Q9AD97_STRCO.","","-48% similar to PDB:1LQA TAS PROTEIN FROM ESCHERICHIA COLI IN COMPLEX WITH NADPH (E_value = 6.3E_34);-48% similar to PDB:1PZ1 Structure of NADPH-dependent family 11 aldo-keto reductase AKR11B(holo) (E_value = 5.5E_30);-50% similar to PDB:1ZSX Crystal Structure Of Human Potassium Channel Kv Beta-subunit (KCNAB2) (E_value = 3.0E_28);-49% similar to PDB:1EXB STRUCTURE OF THE CYTOPLASMIC BETA SUBUNIT-T1 ASSEMBLY OF VOLTAGE-DEPENDENT K CHANNELS (E_value = 6.7E_28);-49% similar to PDB:1QRQ STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT (E_value = 6.7E_28);","Residues 7 to 317 (E_value = 7.7e-41) place ANA_0665 in the Aldo_ket_red family which is described as Aldo/keto reductase family.","","catabolism protein mocA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0666","700831","700610","222","4.06","-9.12","7981","ATGCGCACTGTTCTGGAGACCACCGGTCAGGTCTGCCCCTTCCCCGTCATCGAGGCCGAAGAGGCCATGGAGGAGCTCAGCGTCGGCGACGAGCTCGTCATCGGCTTCGACTGCACCCAGGGGACTCAGACACTGCCGGCTTGGGCCGCCGACAACGGCTACACCGTCACCGAGTTCGAGCGCACCGGCGACGCGGCCTGGACCATCACCGTACGCAAGTAG","MRTVLETTGQVCPFPVIEAEEAMEELSVGDELVIGFDCTQGTQTLPAWAADNGYTVTEFERTGDAAWTITVRK$","Redox protein, regulator of disulfide bond formation","Cytoplasm","Uncharacterized protein family UPF0033superfamily","hypothetical protein","SirA family protein","","Teplitski M., Goodier R.I., Ahmer B.M. Pathways Leading from BarA/SirA to Motility and Virulence Gene Expression in Salmonella. J. Bacteriol. 2003. 185(24):7257-7265. PMID: 14645287Heeb S., Haas D. Regulatory roles of the GacS/GacA two-component system in plant-associated and other gram-negative bacteria. Mol. Plant Microbe Interact. 2001. 14(12):1351-1363. PMID: 11768529Katoh E., Hatta T., Shindo H., Ishii Y., Yamada H., Mizuno T., Yamazaki T. High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division. J. Mol. Biol. 2000. 304(2):219-229. PMID: 11080457","","","

InterPro
IPR001455
Family

SirA-like
PF01206	$\"[1-73]T$	SirA
PS01148	$\"[5-29]T$	UPF0033

noIPR
unintegrated

unintegrated
G3DSA:3.30.110.40	$\"[1-72]T$	no description

","BeTs to 13 clades of COG0425COG name: Predicted redox protein, regulator of disulfide bond formationFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0425 is aomp---qv---bcefgh-nuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001455 (Protein of unknown function UPF0033) with a combined E-value of 2.7e-10. IPB001455 5-46","Residues 5-73 are similar to a (YEED ECS2814 SA1849 UPF0033 YEDF SE1645 MW1968) protein domain (PD708130) which is seen in Q8CRR0_STAEP.Residues 5-73 are 63% similar to a (SIRA HOMOLOG UPF0033 3D-STRUCTURE PREDICTED AMINOTRANSFERASE OXIDOREDUCTASE REGULATOR BOND TRANSCRIPTIONAL) protein domain (PD004783) which is seen in Y990_METJA.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 73 (E_value = 3.3e-27) place ANA_0666 in the SirA family which is described as SirA-like protein.","","protein family UPF0033 superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0667","701997","700912","1086","11.37","16.32","37894","GTGCCGTCACCCACCATCCTCACTGGGCTCATCGTTGGAGCCATCCTCGGTTTCATCCTCCAACGAGGCCGTTTCTGCATCACCGGAGCCTTCCGGGACCTGTGGGTCTCCCGCTCCTGGCGCTGGTTCACAGCCTTCCTGCTGGCCATCGCCGTTCAGGCGGTCGGAGTCGCCGTCCTGACCTCAGCAGGCTCCATTACCCCTGAGATCCCCAAGCTGTCAGTGGTTGCCACCGTTGTCGGCTCCTTCCTGTTCGGAGTCGGGATCGTCCTGGCCGGCGGCTGCGCCACCGGGACCTACTACCGCGCCGGAGAGGGCCTGGTCGGCTCCTGGTTCGCGCTCGTGGCCTATGCCACCACGGCGGCCGCGTCGAAGACGGGACTCCTGTCGGGGGTGACGAGCTGGGTCAAAGGACTGTGGGTCACCGACCTGACCACCATCCCGGCCACCATCGGCCTGCCGAACTGGGGCGGCGTCGTCATCCTGGCCAGCGTCACCGGGCTCATTGTGCACCGCTTCATCGTCCTGGAGCGCAACCGTCCCGCTCAGATCCAGCTGCCCGCCCGGCGCACGGGCCTGGCTCACCTGCTGCTGGAGAAGCAGTGGAATCCTCTGGCCACCGGATTCCTCGTGGGCGTCGTCGCCGTCATCGCCTGGCCCACGTCCTGGGCCTCGGGGCGCCCGGACGGGCTGGGGATCACGACACCGTCGTCGAACCTGGTGAACCTCATCGTCACTGGGGAGGCCGAGCGGCTCGACTGGGGCGTGCTCCTGGTCCTGGGCATCCTGCTCGGCTCCTTCCTCGCGGCCAAGGCCTCTGGCGAGTTCCGTGTCCGCGTGCCCAGCGCCCAGGTCATCCAGCGCTCCATCGCCGGCGGTGTCCTCATGGGGATCGGCGCCGCCTGGGCGGGTGGCTGCTCCATCGGCAACGCCCTGGTACAGACCTCGCTCCTGTCATGGCAGGGCTGGATCGCACTGGTCTTCCAGGTGCTGGGGGTCGGGGTGGCCGCCTGGTTCCTCCTCATCCGGCCCCGGCAGCGTCGTCGCGCCGAGCGAGCGGCCTCACGCGTGCCCGCCACCGTCTGA","VPSPTILTGLIVGAILGFILQRGRFCITGAFRDLWVSRSWRWFTAFLLAIAVQAVGVAVLTSAGSITPEIPKLSVVATVVGSFLFGVGIVLAGGCATGTYYRAGEGLVGSWFALVAYATTAAASKTGLLSGVTSWVKGLWVTDLTTIPATIGLPNWGGVVILASVTGLIVHRFIVLERNRPAQIQLPARRTGLAHLLLEKQWNPLATGFLVGVVAVIAWPTSWASGRPDGLGITTPSSNLVNLIVTGEAERLDWGVLLVLGILLGSFLAAKASGEFRVRVPSAQVIQRSIAGGVLMGIGAAWAGGCSIGNALVQTSLLSWQGWIALVFQVLGVGVAAWFLLIRPRQRRRAERAASRVPATV$","Transport system permease protein","Membrane, Cytoplasm","predicted transporter components","putative transport system permease protein","protein of unknown function DUF395, YeeE/YedE","","Kisker C., Schindelin H., Rees D.C. Molybdenum-cofactor-containing enzymes: structure and mechanism. Annu. Rev. Biochem. 1997. 66:233-267. PMID: 9242907Kletzin A., Adams M.W. Tungsten in biological systems. FEMS Microbiol. Rev. 1996. 18(1):5-63. PMID: 8672295White H., Strobl G., Feicht R., Simon H. Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes. Eur. J. Biochem. 1989. 184(1):89-96. PMID: 2550230Trautwein T., Krauss F., Lottspeich F., Simon H. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. Eur. J. Biochem. 1994. 222(3):1025-1032. PMID: 8026480Mukund S., Adams M.W. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 1995. 270(15):8389-8392. PMID: 7721730Ma K., Hutchins A., Sung S.J., Adams M.W. Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(18):9608-9613. PMID: 9275170Chan M.K., Mukund S., Kletzin A., Adams M.W., Rees D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 1995. 267(5203):1463-1469. PMID: 7878465","","","

InterPro
IPR007272
Domain

Protein of unknown function DUF395, YeeE/YedE
PF04143	$\"[69-132]T$ $\"[280-344]T$	DUF395

InterPro
IPR013983
Domain

Aldehyde ferredoxin oxidoreductase, N-terminal
SM00790	$\"[165-305]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-17]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[43-63]?$ $\"[73-93]?$ $\"[114-136]?$ $\"[155-175]?$ $\"[202-222]?$ $\"[252-270]?$ $\"[290-312]?$ $\"[322-342]?$	transmembrane_regions

","BeTs to 7 clades of COG2391COG name: Predicted transporter componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2391 is -o-p----vd----efg-s-uj----Number of proteins in this genome belonging to this COG is 1","***** IPB007272 (YeeE/YedE) with a combined E-value of 7.2e-54. IPB007272A 10-41 IPB007272B 42-74 IPB007272C 79-109 IPB007272D 255-305 IPB007272C 290-320 IPB007272D 44-94 IPB007272D 256-306","Residues 7-111 are similar to a (MEMBRANE PERMEASE SYSTEM TRANSPORTER TRANSMEMBRANE INTEGRAL PROTEIN PREDICTED YEDE PROBABLE) protein domain (PD590925) which is seen in Q8X8T6_ECO57.Residues 142-284 are 67% similar to a (SYSTEM PERMEASE MEMBRANE MW1969 PROBABLE YEEE SE1646 TRANSMEMBRANE SA1850) protein domain (PD812695) which is seen in YEEE_ECOLI.Residues 292-340 are 81% similar to a (MEMBRANE SYSTEM PERMEASE TRANSMEMBRANE TRANSPORTER YARROWIA PROBABLE INTEGRAL YEEE/YEDE FAMILY) protein domain (PD041565) which is seen in YEEE_ECOLI.","","No significant hits to the PDB database (E-value < E-10).","Residues 69 to 132 (E_value = 1.8e-14) place ANA_0667 in the DUF395 family which is described as YeeE/YedE family (DUF395).Residues 280 to 344 (E_value = 1.6e-15) place ANA_0667 in the DUF395 family which is described as YeeE/YedE family (DUF395).","","transporter components","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0668","703405","702383","1023","8.29","4.74","37500","ATGTCTCTCCCCGCGGGTGCGGCCTGTGGAGGAAGGCCGCGCCCTCCGGCCAGATCCGACGCCGCGTCACCTCCTCGCGGTAGCGTCGTCCCCATGCCCCACGAGCCGCTCACCGCATCCAGCTCATCGCCTCAGACCGGCGTCAGGCCCACCGGTCCGGGTGCCAGTGGCCGTCCGGGAGCGGGCGCGGGCGGCGGACGCCGCGCGGCCCTGTCCCCCTCTCGGGCCAAGGACTTCATGCAGTGCCCGCTCATGTTCCGTCTGCGCACGGTCGACCGCCTTCCCGAGCCCGGTTCGCTGGCGACGCACAAGGGCACCGTGGTCCACGGCGTACTGGAGCGTCTCTACGATCTTCCGGCCTCGGAACGCCTCCCACAGGCGGCCCTCGAGCTCCTGCCCGGCCAGTGGGCATCCCACCGCGAGAAGAACCCGGAGGTCATGGACCTGTTCGAGGACGCCGACCACGTGGAGACCTGGCTGGAGGAGGCCCGCGGACTCATTCGCACCTACTTCACCCTGGAGAACCCCCAGCGCCTGGAGCCGGCCGAGCGCGAGCTCTTCGTCCAGACTGAGACCGGAGACGGCCTGCTCCTGCGAGGCTTCGTGGACCGTCTGGACGTGGCACCCGACGGCGCTATGAGAGTGGTCGACTACAAGACCGGGCGCAGCCCCGGCACGCGTTTCATGGAGGAGGCGCTGTTCCAGATGCGCTTCTACGCGCTGGTGCTGTGGCGCCTGCGCGGGCGGGCGCCGGCCCGTCTCCAGCTGGTCTATCTCAAGGACGGACGGGTCCTGACTCACGATCCTCGCCTGGCCGAGCTGGAACGCACCGAGACGCGCCTGGCGCACCTGTGGGACGAGGTCGAGGACTGCGCTCGCAACGGCTCCTTCCATCCCCGCCGCTCCCGGCTGTGCGACTGGTGCGCCTTCCAGGCCCAGTGCCCGCTCTTCGGCGGCACCACACCGCAGGTGCCCGATGACGGGATCGCCCGCCTCCTGACCGCACGCCGCACCGCTGCCTGA","MSLPAGAACGGRPRPPARSDAASPPRGSVVPMPHEPLTASSSSPQTGVRPTGPGASGRPGAGAGGGRRAALSPSRAKDFMQCPLMFRLRTVDRLPEPGSLATHKGTVVHGVLERLYDLPASERLPQAALELLPGQWASHREKNPEVMDLFEDADHVETWLEEARGLIRTYFTLENPQRLEPAERELFVQTETGDGLLLRGFVDRLDVAPDGAMRVVDYKTGRSPGTRFMEEALFQMRFYALVLWRLRGRAPARLQLVYLKDGRVLTHDPRLAELERTETRLAHLWDEVEDCARNGSFHPRRSRLCDWCAFQAQCPLFGGTTPQVPDDGIARLLTARRTAA$","RecB family exonuclease","Cytoplasm, Periplasm","RecB family exonuclease","K07465 putative RecB family exonuclease","RecB family exonuclease-like","","","","","No hits reported.","BeTs to 7 clades of COG2887COG name: RecB family exonucleaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2887 is --m--z----r---------ujx-t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 78-128 are 74% similar to a (EXONUCLEASE ML1312 MB2143 RECB FAMILY SCO1653 MLCB2533.08C) protein domain (PD111356) which is seen in Q9RJ55_STRCO.Residues 152-325 are similar to a (HELICASE ATP-DEPENDENT DNA FAMILY SUBUNIT 3.6.1.- HYDROLASE EXONUCLEASE HELICASE UVRD/REP) protein domain (PD356768) which is seen in Q828J7_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","family exonuclease","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0669","703429","704589","1161","8.77","2.65","39963","ATGCGGCTCCCGGCTGCCGACGGCGTTAGGCTCGCGCCCATGCCTGCCTCCACATCGACCGGCGAGTGGGTGATCGCCCGCGTCGGCGGTGCCCCCGTCGTCATCTCACCGACCTCTCTCCTGCTCGGCCTGCTCATCGCGGGCAGCTGGTACCCGCTGGTCTCCTCGGCCCTGGGTGGTTTCGGGACCACTACGGTGCTGCTGGTGGTGGTCTCCACGGTTCTGGGCGTTGCGGTCTCGGTGCTGCTGCACGAGCTGGCCCACGGGCTGTCTGGAACTCTCATGGGCAGGCGACCCACCCGTTACGAGCTCTACCTGTGGGGCGGGCGCACCTCCTTCGGGCCGGCACGCGAGTGGACCGCGTGGAAGGACCTGGTCACCTCCCTGTCAGGACCTGCCACCAACCTGCTCATCTGGGGCATCGGAACGTGGGCACAGAACTCCGTCAGTCTGCCGGTTCCCGTCGCCTTCACCATATGGGCCGTGACCCTGGTCAACCTGGCCCTGGCCATCTTCAACGCCCTGCCGGGTCTTCCCCTCGACGGCGGCTACGCCCTAGCCGCGCTCGTGGTCCAGGTGACCGGCAACCGCAGACTCGGTCTCAAAGTGGCCGGCTGGGGCGGGCTGGCGGTGGTCGGCGGTGTCGTGTGGTGGTGGATCCTGCGCCCACTCGTGCTTGACGGTCGCCAGCCCGACGCCTTCAACCTCATCCTGGTTCTCATGGTGGGTTGGTCGATCGTGGCCTCCAGCTGGCAGGTCCTCGAGCTCGGGGGAGGAGCCAGGGCCGCCTCGAAGCTGGACCTGCGCGAGCTGGCCAGGCCTCTGCACGTCGTCGGACCCGAAACGCCTGTGTCCCAGGTGCGTGGAGCGCTGGCGCAAGGAGCCGCACTCGTCCTCGTCACTGACGGGCCCGAGCTGGTGGGCACGATCGACGAGGCCTCCCTCAAGGAGCTCGGGCTGTCGGACGCCGCAGGCTCAACCCCTACGCTCGGGGTGAGCGCCAGGCAGGTCTGCACGGTGCTGCCGGCAGCTGCGGTGACGACTGATCTGACCGGTCAGGAGGCCGCCGACGCCATGAAACGAGCCCGGGAGGTCTCACGCTGGCTGGTGCTCGTGGAGGCGGGGAGCCTGGCCGGTGCGGTCCCCACCGGCGCGCGCTGA","MRLPAADGVRLAPMPASTSTGEWVIARVGGAPVVISPTSLLLGLLIAGSWYPLVSSALGGFGTTTVLLVVVSTVLGVAVSVLLHELAHGLSGTLMGRRPTRYELYLWGGRTSFGPAREWTAWKDLVTSLSGPATNLLIWGIGTWAQNSVSLPVPVAFTIWAVTLVNLALAIFNALPGLPLDGGYALAALVVQVTGNRRLGLKVAGWGGLAVVGGVVWWWILRPLVLDGRQPDAFNLILVLMVGWSIVASSWQVLELGGGARAASKLDLRELARPLHVVGPETPVSQVRGALAQGAALVLVTDGPELVGTIDEASLKELGLSDAAGSTPTLGVSARQVCTVLPAAAVTTDLTGQEAADAMKRAREVSRWLVLVEAGSLAGAVPTGAR$","Zn-dependent protease","Membrane, Extracellular","Sterol-regulatory element binding protein(SREBP) site 2 protease family","hypothetical protein","peptidase M50","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 1989. 242(2):211-214. PMID: 2914602Murphy G.J., Murphy G., Reynolds J.J. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett. 1991. 289(1):4-7. PMID: 1894005","","","

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[81-90]?$	ZINC_PROTEASE

InterPro
IPR008915
Family

Peptidase M50
PF02163	$\"[72-220]T$	Peptidase_M50

noIPR
unintegrated

unintegrated
tmhmm	$\"[29-51]?$ $\"[57-79]?$ $\"[125-145]?$ $\"[151-173]?$ $\"[175-197]?$ $\"[203-221]?$ $\"[236-254]?$	transmembrane_regions

","BeTs to 14 clades of COG1994COG name: Zn-dependent proteasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1994 is aompkz-qvdr-bc--g--nuj----Number of proteins in this genome belonging to this COG is 1","***** IPB008915 (Peptidase M50) with a combined E-value of 2.2e-06. IPB008915E 163-191 IPB008915A 79-108","Residues 128-190 are similar to a (METALLOPROTEASE ZINC PROTEASE MEMBRANE TRANSMEMBRANE 3.4.24.- HYDROLASE INNER MEMBRANE-ASSOCIATED ZN-DEPENDENT) protein domain (PD005718) which is seen in Q7NKH6_GLOVI.","","No significant hits to the PDB database (E-value < E-10).","Residues 72 to 220 (E_value = 6.1e-15) place ANA_0669 in the Peptidase_M50 family which is described as Peptidase family M50.","","element binding protein (SREBP) site 2 protease family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0670","704749","705888","1140","4.65","-25.38","41002","ATGAGCGACGTCAGCCCCCAGGACCTCTCTCAAGAGATTCTGGCCTCGCCGGCCAAGGCATCGATCTTCCTCACGGTGACAGTACGCAGCGGGGGCGAGTCCGTCGTCATCGATCTGCTGACTGCTGTGTCCGGGCTGACCCGGGCCGTTGGTTTCCGTTACCCCGAGACGATGCTCAGCTGCGTCGTCGGTATTGGGGCAGGCATGTGGGATCGTCTCTTCGACGTACCTCGTCCCGAGTACCTGCACGATTTTGAGGCACTTCAGGGAGGAAAGCACAGTGCCCCCTCGACGCCGGGAGACCTGTTCTTCCACCTGCGCGCCTCAACTCTCGACATGTGCTTCGAGTTGGCGCGCCAGATCATGCGCCGACTGGGCACTGCGGTCAGTACCTACGATGAGGTTCACGCCTTCCGCTACCTCGATAATCGGGACCCTCTGGGCTTCGTCGACGGCACTGAGAGTCCGCGGGGGCAGGCGGCCGTTGCCGCGGCGCTCATCAACGAGGGCGCGTGGGCGGGCGGCAGCTACATCATTGAGCAGAAGTACGTCCACAACCTCACCGCTTGGGACTCATTGAGTGTCGAGGAGCAGGAACGCGTCATCGGTCGCACCAAGCTCGATGACACCCAGCTCCCCGATGATGAGCAGCCCACCAACAGCCACGTCACCATGAACACCATTGAGGACGCTGACGGTAACGAGCTCCAGATCGTGCGTGACAATCTGGCCTTCGGTGAGGCCTCTGGGGAGCAGGGCACGTTCTTCATGAGCTACGCAGCAGACCCACGCGTCACTGAGCTCATGCTCCGGCGTATGTTCCTGGGGGAGCCCGAGGGCAACTACGACCGCATCCTTGATTTCTCCACGCCTCTGACAGGATGTCTCTTCTTCGCTCCGCCGGCCGCCTTCCTCGACGACGCCGACCAGTACGCGAGGCCTTCTGTCCGACCTGAGGCGGGACCGCAGGACCCGACCCAGCCCGCCACTGAGCTGAGCGCCGCCAAGGACCTAGGGTTCAACGCATCGTCTGAGGCGCCGCGTGACCAGACACCAGATGACCACAGCAATGGTGCGGGTTCCACTGCCGCACCGTCCGATGGATCCCTCGGGATCGGAAACCTGAAAGGTCGAGTATGA","MSDVSPQDLSQEILASPAKASIFLTVTVRSGGESVVIDLLTAVSGLTRAVGFRYPETMLSCVVGIGAGMWDRLFDVPRPEYLHDFEALQGGKHSAPSTPGDLFFHLRASTLDMCFELARQIMRRLGTAVSTYDEVHAFRYLDNRDPLGFVDGTESPRGQAAVAAALINEGAWAGGSYIIEQKYVHNLTAWDSLSVEEQERVIGRTKLDDTQLPDDEQPTNSHVTMNTIEDADGNELQIVRDNLAFGEASGEQGTFFMSYAADPRVTELMLRRMFLGEPEGNYDRILDFSTPLTGCLFFAPPAAFLDDADQYARPSVRPEAGPQDPTQPATELSAAKDLGFNASSEAPRDQTPDDHSNGAGSTAAPSDGSLGIGNLKGRV$","Iron-dependent peroxidase","Cytoplasm, Extracellular","tyrA protein VC2145","K07223 putative iron-dependent peroxidase","Dyp-type peroxidase family","","Sugano Y., Nakano R., Sasaki K., Shoda M. Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1. Appl. Environ. Microbiol. 2000. 66(4):1754-1758. PMID: 10742277","","","

InterPro
IPR006314
Family

Dyp-type peroxidase
PF04261	$\"[10-305]T$	Dyp_perox
TIGR01413	$\"[10-305]T$	Dyp_perox_fam: Dyp-type peroxidase family

","BeTs to 6 clades of COG2837COG name: Predicted iron-dependent peroxidaseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2837 is ---------dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is 2","***** IPB006314 (Dyp-type peroxidase) with a combined E-value of 1.1e-28. IPB006314B 102-112 IPB006314C 145-155 IPB006314D 174-211 IPB006314E 280-288","Residues 59-294 are 72% similar to a (PEROXIDASE TYRA YCDB IRON-DEPENDENT PREDICTED YFEX EXPORTED MEMBRANE SECRETED SEC-INDEPENDENT) protein domain (PD040640) which is seen in Q7U189_MYCBO.","","-62% similar to PDB:2GVK Crystal structure of a dye-decolorizing peroxidase (DyP) from Bacteroides thetaiotaomicron VPI-5482 at 1.6 A resolution (E_value = 5.6E_61);-55% similar to PDB:2HAG Crystal structure of putative melanin biosynthesis protein TyrA (np_716371.1) from Shewanella oneidensis at 2.75 A resolution (E_value = 3.0E_46);-55% similar to PDB:2IIZ Crystal structure of putative melanin biosynthesis protein TyrA with bound heme (NP_716371.1) from Shewanella Oneidensis at 2.30 A resolution (E_value = 3.0E_46);-42% similar to PDB:1BOL THE CRYSTAL STRUCTURE OF RIBONUCLEASE RH FROM RHIZOPUS NIVEUS AT 2.0 A RESOLUTION (E_value = 3.0E_46);-50% similar to PDB:1F32 CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 (E_value = 3.0E_46);","Residues 10 to 305 (E_value = 2.9e-117) place ANA_0670 in the Dyp_perox family which is described as Dyp-type peroxidase family.","","protein VC2145 (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0671","705885","706679","795","4.81","-16.35","28726","ATGAACAATCTGCATCGTCAGCTGGCCCCCATCTCCGAGGCTGCGTGGGGTGAGATCGACCAAGAGGCGCGGCGCACCTTCATCCGCTGGATCGCTGGACGACGCGTCGTCGACGTCGTTGGACCCGACGGAGAGGAACTCGCGGCAGTACGCACCGGTCACCAGGTATGTGTGGACACCCCCTTCGAAGGCGTCCAGGCCCACCAGCGTCAGGTCCGCCAGATCGTCGAGCTGAGGGTTCCCTTCCGGGTCAGCCGCGAGGCCGTCGACGCCGTCGACCGCGGAGCCCAGGACTCCGACTGGCAGCCTGTGAAGGACGCCGTTGCTCAGATCGCCAGGGCCGAGGACGGCATTGTCTTCGACGGGCTGGCGAGCGCAGGCATCGAGGGACTGGTTCCCTCAAGCTCCAACCCTGCCGTATCGCTCCCACAGCCGAAGGATCTTCCTGACGCCGTTGCCGCTGCCCTCAAGGAGCTCCGCCTCGCCGGAGTTGAAGGCCCCTACGCCCTCCTGCTCTCCGCCGAGCTGTGGACCGCCGTTGCGGAGACCACTGATGACGGTTACCCCATTCGCAAGCACATCGATCGTCTCTTGGAAGGTGAGGTCCTGTGGGCTCCCGCCATCCAGGGAGCTGTCCTGCTGAGCACGCGGGGCGGCGACTACGAGCTGCACCTCGGCCAGGACCTCTCCATCGGATATCTCTCACACGATGCCGAGTCGATTGAGCTCTATCTCCAAGAGACGCTCACATTCCTCCCGTACACCTCTGAGGCGAGTGTCGTGCTGACGCACTGA","MNNLHRQLAPISEAAWGEIDQEARRTFIRWIAGRRVVDVVGPDGEELAAVRTGHQVCVDTPFEGVQAHQRQVRQIVELRVPFRVSREAVDAVDRGAQDSDWQPVKDAVAQIARAEDGIVFDGLASAGIEGLVPSSSNPAVSLPQPKDLPDAVAAALKELRLAGVEGPYALLLSAELWTAVAETTDDGYPIRKHIDRLLEGEVLWAPAIQGAVLLSTRGGDYELHLGQDLSIGYLSHDAESIELYLQETLTFLPYTSEASVVLTH$","Linocin_M18 bacteriocin protein","Cytoplasm","29 kDa antigen","Linocin_M18 bacteriocin protein","Linocin_M18 bacteriocin protein","","Valdes-stauber N., Scherer S. Nucleotide sequence and taxonomical distribution of the bacteriocin gene lin cloned from Brevibacterium linens M18. Appl. Environ. Microbiol. 1996. 62(4):1283-1286. PMID: 8919789Valdes-stauber N., Scherer S. Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens. Appl. Environ. Microbiol. 1994. 60(10):3809-3814. PMID: 7986050","","","

InterPro
IPR007544
Family

Linocin_M18 bacteriocin protein
PF04454	$\"[1-258]T$	Linocin_M18

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-130 are 71% similar to a (BACTERIOCIN ANTIGEN CFP29 M18 LINOCIN AQ_1760) protein domain (PD023974) which is seen in Q7WJL4_BORBR.Residues 145-250 are similar to a (BACTERIOCIN ANTIGEN CFP29 M18 LINOCIN) protein domain (PD686406) which is seen in Q743F5_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 258 (E_value = 2.1e-109) place ANA_0671 in the Linocin_M18 family which is described as Linocin_M18 bacteriocin protein.","","kDa antigen","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0672","706733","707800","1068","6.34","-4.37","38841","GTGAACTCACCCACGGAGTCCTCCCAGCGCCCCGCCCCCCAGGAGAACCTGGGGCAGGCCGGTCGCCGGGGCCCCTTCCGCTACGGCGAACGCATCCAGGTCACCGACACCAAGGGCCGCAAGAACACCTTCCTGCTCGACCCTCACGGCTACTTCCAGTCCGTGCGCGGCTCCTTCCACCACCGAGACGTCGTCGGCATGGACGAGGGCAGCGTCATCGAGACCGACACCGGCCACGAGCTGCTCCTGCTGCGCCCGCTCCTGGCCGACTACGTCCTGTCCATGCCCCGCGGCGCCCAGGTGGTCTACCCCAAGGACTCCGGACAGGTCATCGCCATGGGGGACATCTTCCCCGGCGCCCGCGTTCTGGAGGCCGGCGTCGGTTCCGGCGCGCTGACCATGAACCTGCTCTCCGCCATCGGGGAGGGCGGCCACCTGCTGTCCATTGAGCGCCGTGAGGACTTCGCCCAGATTGCCGCCTCCAACGTCGACGCCTGGTTCGGCCGCCACCATCCCGCCTGGGAGCTGCGCACCGGGGACTTCGCCGACGTCGTTGCCGCCCGGGTGGAACCCGGCAGCATCGACCGGGTAGTCCTGGACATGCTCGCCCCCTGGGAGAACGTCGAGGCCGCCTCCTCGGCTCTGGCCCCGGGCGGGCTCTTCCTGGCCTACGTGGCCACCGTCACCCAGCTCTCCCGCACCGTGGAGTCTCTGCGTCACAGCGACCTGTTCACCGAGCCCGAGTCCTGGGAGTCCATGGTGCGCACCTGGAACGTCGACGGGCTCGCCGTGCGCCCCGACCACCGCATGGTGGCCCACACCGGCTTCCTGCTGACCGCCCGTCGCCTGGCCGCCGGCTCCAGGCCCCTGACCCGCAAGCGCCCGCCCGCCCGCGGCGCCTACGACGAAGGCGGCTACTGGCTGCCCGACGACGTCAAGGAGCGCACCAGCACCGACAAGAAGGTCCGCCGCGTTCTGCGAGACTGCCGGGCCAAGCAGCCCACCGACGCCACACCCGTTCTCAGCGGGAGCGCGGACGACGACCAGGACGGCGCTGACCATGTCTGA","VNSPTESSQRPAPQENLGQAGRRGPFRYGERIQVTDTKGRKNTFLLDPHGYFQSVRGSFHHRDVVGMDEGSVIETDTGHELLLLRPLLADYVLSMPRGAQVVYPKDSGQVIAMGDIFPGARVLEAGVGSGALTMNLLSAIGEGGHLLSIERREDFAQIAASNVDAWFGRHHPAWELRTGDFADVVAARVEPGSIDRVVLDMLAPWENVEAASSALAPGGLFLAYVATVTQLSRTVESLRHSDLFTEPESWESMVRTWNVDGLAVRPDHRMVAHTGFLLTARRLAAGSRPLTRKRPPARGAYDEGGYWLPDDVKERTSTDKKVRRVLRDCRAKQPTDATPVLSGSADDDQDGADHV$","SAM-dependent methyltransferase involved in tRNA-Met maturation","Cytoplasm","Predicted SAM-dependent methyltransferaseinvolved in tRNA-Met maturation","tRNA (adenine-N(1)-)-methyltransferase ","tRNA(1-methyladenosine) methyltransferase and related methyltransferase-like","","Anderson J., Phan L., Cuesta R., Carlson B.A., Pak M., Asano K., Bjork G.R., Tamame M., Hinnebusch A.G. The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev. 1998. 12(23):3650-3662. PMID: 9851972","","","

InterPro
IPR014816
Family

tRNA methyltransferase complex GCD14 subunit
PF08704	$\"[26-282]T$	GCD14

noIPR
unintegrated

unintegrated
G3DSA:3.10.330.20	$\"[20-86]T$	no description
G3DSA:3.40.50.150	$\"[87-286]T$	no description
PTHR12133	$\"[28-309]T$	UNCHARACTERIZED METHYLTRANSFERASE

","BeTs to 12 clades of COG2519COG name: Predicted SAM-dependent methyltransferase involved in tRNA-Met maturationFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG2519 is aompkzyqv-r---------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 34-106 are 73% similar to a (METHYLTRANSFERASE TRANSFERASE FLJ20628 SAM-DEPENDENT BETA-ASPARTATE RNA CARBOXYL PIMT L-ISOASPARTYL POSSIBLE) protein domain (PD007319) which is seen in Q49777_MYCLE.Residues 107-166 are 63% similar to a () protein domain (PD990117) which is seen in Q9WZK7_THEMA.Residues 107-162 are 80% similar to a (METHYLTRANSFERASE TRANSFERASE SAM-DEPENDENT FLJ20628 TRNA-MET MATURATION PROTEIN-L-ISOASPARTATE RNA POSSIBLE PREDICTED) protein domain (PD901492) which is seen in Q6AFW5_BBBBB.Residues 110-162 are 79% similar to a (METHYLTRANSFERASE TRANSFERASE STRAIN REPRESSOR RIKEN CANDIDA ENRICHED NRRL PRODUCT:HYPOTHETICAL GCN4) protein domain (PD452595) which is seen in Q9RJ57_STRCO.Residues 174-283 are similar to a (METHYLTRANSFERASE TRANSFERASE SAM-DEPENDENT PROTEIN-L-ISOASPARTATE STRAIN TRNA-MET INVOLVED MATURATION OTHER CHROMOSOME) protein domain (PD010865) which is seen in Q6AFW5_BBBBB.","","-69% similar to PDB:1I9G CRYSTAL STRUCTURE OF AN ADOMET DEPENDENT METHYLTRANSFERASE (E_value = 3.2E_79);-52% similar to PDB:1O54 Crystal structure of SAM-dependent O-methyltransferase (TM0748) from Thermotoga maritima at 1.65 A resolution (E_value = 4.0E_29);-48% similar to PDB:2B25 Human putative tRNA(1-methyladenosine)methyltransferase (E_value = 2.8E_27);-46% similar to PDB:1YB2 Structure of a putative methyltransferase from Thermoplasma acidophilum. (E_value = 1.0E_13);","Residues 26 to 282 (E_value = 4.5e-08) place ANA_0672 in the GCD14 family which is described as tRNA methyltransferase complex GCD14 subunit.","","SAM-dependent methyltransferase involved in tRNA-Met maturation (pimT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0673","707793","709514","1722","5.34","-14.55","60063","ATGTCTGAGACGTCTGCCGCCGACGCCGGCACGCCCCAGCCGCTGGGGATGCCCGCCACGGACTTCACCAGCCACCAGCTGCGTGAGGCCCGCGCTCAGGCCGTCAGCCTGGCGGCCAAGAACGAGCGCCTGGTGACCGCTCTGGGCACCGCCCGCGAGCGCATCGCCGAGCTCGGCCAACAGCTCGATGCCGTCACTCACCCCCCGGTCACCCTGGGACTGCTCACTGGCCCGCCCCGCACGAGGGGCGCCGCAGGTGACACCGTCGATGCCGTCGATGCTGTCGATGCCGCCGACGCCACCCAGCCCCGCGAGGTCGCCGTGAGCCTTTCTGGCCGACAGATGCTCCTGCACGTCCACCCCGGCGTCGATGACACCGAGTTGCAGGTCGGGCGGCTCGTGGCTGTCAATGACCAGATGCTCGTCGTCGCCACCCTCCCTGAGCCCCGCACCGGTGAGGCCGTCACCCTCGAGGAGAGGCTCGATGACGCCCGCGTCCTGGTGACCACCGGCGGGGGAAGCGCCCGAATCCTCACCCTGTCCTCGGCTCTTGGCCGCATCGCCGGGACCGGTGAGGGGCTCAAACCCGGTGACACCCTAGCCGCCGACCTGCGCGCCGACGTCGCCACGGCTCTCATTGAGCGCACCAGCGTCGAGCAGCTGGTCGTGGCCGAGACACCCGATGTCTCCTGGGCGGACATCGGCGGCCTGGGCCCGCAGATCGAGCAGATCCGCGATGCCCTCGAGCTGCCCTTCACCCACCCCGAGCTGTTCCACGCCTACGGCCTGCGCGCCCCCAAGGGACTGCTGCTCTACGGCCCGCCCGGCTGCGGCAAGACCCTCATCGCCAAGGCCGTGGCCACCTCCCTGGCTGATTCGCCCAGCGCCTCGGGCATCACAGGACGCCCGCCCGCGTTCCTCAACATCAAGGGTCCTGAGCTGCTGAGCAAGTTCGTCGGCGAGACCGAGCGCCAGATCCGTGCCATCTTCGACCAGGCCCGTAAGGCCGCCGCCGAGGACCGGCCGGTGGTCATCTTCTTCGATGAGATGGAGGCCCTCTTCCGCACCCGTGGCACCGGCGTGTCCTCCGACGTCGAGACCATGATCGTGCCCCAGGTCCTGGCGGAGATCGACGGCGTGGAGTCCCTGCGCAACGTCGTCATCATCGGGGCCTCCAATCGTGAGGACATGATCGACCCCGCCATCCTGCGCCCCGGGCGCCTGGACGTGAAGATCCGCATCAACCGGCCCGATGCGGCCGCTGCCGAGGAGATCCTCGCCCGGCACCTCATCGCCGACCTGCCCCTGGCCCCGGGCGAGCTCGCGGCCCATGGGGGAGACCGTGAGGCCACTGCCGCCTCCTTGCGACGGGTCGTCATCGATGCCCTTTACGCCCGCAACGAGGCCACCGCCGTCCTGGAGATCACCGAGGCCCACGCGGCCGGTGGCACCTCCACCCGCGTCCTTCACCTGGCCGACCTCACCAGCGGCGCCATGCTGGCCGCCATCGTCTCGCGCGCCAAGACCGCCTCCATCAAGGACGAGCTCGCCGGGGGACAGGGCGGTCTGAGCGCAGCCAGGCTCCGCTCGGCCGTCGCGACCGAGGCACGGCAGAACGAGGAGATCACCGGCGCCACCACCCCCGAGGGCTGGGCCCGGCTCATCGGCACCCGCACCTCGCAGATCCTCAGCGTGCGCAGACTCGGCAAGGAGAGCACATGA","MSETSAADAGTPQPLGMPATDFTSHQLREARAQAVSLAAKNERLVTALGTARERIAELGQQLDAVTHPPVTLGLLTGPPRTRGAAGDTVDAVDAVDAADATQPREVAVSLSGRQMLLHVHPGVDDTELQVGRLVAVNDQMLVVATLPEPRTGEAVTLEERLDDARVLVTTGGGSARILTLSSALGRIAGTGEGLKPGDTLAADLRADVATALIERTSVEQLVVAETPDVSWADIGGLGPQIEQIRDALELPFTHPELFHAYGLRAPKGLLLYGPPGCGKTLIAKAVATSLADSPSASGITGRPPAFLNIKGPELLSKFVGETERQIRAIFDQARKAAAEDRPVVIFFDEMEALFRTRGTGVSSDVETMIVPQVLAEIDGVESLRNVVIIGASNREDMIDPAILRPGRLDVKIRINRPDAAAAEEILARHLIADLPLAPGELAAHGGDREATAASLRRVVIDALYARNEATAVLEITEAHAAGGTSTRVLHLADLTSGAMLAAIVSRAKTASIKDELAGGQGGLSAARLRSAVATEARQNEEITGATTPEGWARLIGTRTSQILSVRRLGKEST$","Vesicle-fusing ATPase","Cytoplasm, Membrane","ARC","vesicle-fusing ATPase ","AAA ATPase, central domain protein","","","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[265-418]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[268-430]T$	AAA

InterPro
IPR003960
Domain

AAA ATPase, subdomain
PS00674	$\"[386-404]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[217-414]T$	no description
PTHR23073	$\"[212-496]T$	26S PROTEASE REGULATORY SUBUNIT
PTHR23073:SF4	$\"[212-496]T$	AAA-FAMILY ATPASE

","BeTs to 10 clades of COG0464COG name: ATPases of the AAA+ classFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0464 is aompkzy--dr-bc-f----uj----Number of proteins in this genome belonging to this COG is 3","***** IPB003960 (AAA-protein subdomain) with a combined E-value of 1.2e-49. IPB003960A 231-246 IPB003960B 266-287 IPB003960C 322-357 IPB003960D 372-422 IPB003960B 274-295***** IPB003338 (AAA ATPase VAT, N-terminal) with a combined E-value of 2.5e-47. IPB003338A 252-305 IPB003338B 331-358 IPB003338C 364-418***** IPB000642 (Peptidase M41) with a combined E-value of 1.5e-38. IPB000642A 249-298 IPB000642B 316-358 IPB000642C 385-429***** IPB004201 (Cell division protein 48, CDC48, domain 2) with a combined E-value of 2.6e-24. IPB004201B 309-361 IPB004201C 384-431","Residues 26-237 are 44% similar to a (ATP-BINDING ATPASE AAA-FAMILY AAA ARC ATPASES AAA ML1316 H-TRANSPORTING PROBABLE) protein domain (PD023538) which is seen in O50202_RHOER.Residues 218-288 are 66% similar to a (GLP_139_21831_19885) protein domain (PDA086D5) which is seen in Q7QQ47_EEEEE.Residues 231-357 are 47% similar to a (ATPASE ATP-BINDING) protein domain (PDA043P0) which is seen in Q7WSR6_BBBBB.Residues 240-315 are 75% similar to a (ATP-BINDING PROTEASE CELL DIVISION DNA SUBUNIT HELICASE PROTEASOME HYDROLASE ATPASE) protein domain (PD337570) which is seen in Q6NH92_CORDI.Residues 262-333 are 65% similar to a (ATP-BINDING PEROXISOME ATPASE FACTOR-2 PEROXIN PEROXIN-6 MEMBRANE BIOGENESIS ASSEMBLY REPEAT) protein domain (PD010151) which is seen in Q9VK63_DROME.Residues 311-366 are 92% similar to a (ATP-BINDING CELL DIVISION PROTEASOME SUBUNIT ATPASE 26S PROTEASE REGULATORY FTSH) protein domain (PD000092) which is seen in Q8NQD8_CORGL.Residues 369-399 are 96% similar to a (ATP-BINDING CELL DIVISION PROTEASOME FTSH ATPASE PROTEASE HYDROLASE 3.4.24.- HOMOLOG) protein domain (PD186075) which is seen in Q828J2_STRAW.Residues 400-442 are 81% similar to a (ATP-BINDING CELL DIVISION PROTEASOME SUBUNIT 26S ATPASE PROTEASE FTSH REGULATORY) protein domain (PD240561) which is seen in O50202_RHOER.Residues 454-568 are 54% similar to a (ATP-BINDING ATPASE AAA-FAMILY AAA ARC ATPASES AAA ML1316 H-TRANSPORTING PROBABLE) protein domain (PD022222) which is seen in Q9RJ58_STRCO.","","-63% similar to PDB:1OZ4 VCP/p97 (E_value = 2.7E_44);-63% similar to PDB:1R7R The crystal structure of murine p97/VCP at 3.6A (E_value = 2.7E_44);-63% similar to PDB:1YPW Structure of p97/VCP in Complex in ADP/AMP-PNP (E_value = 2.7E_44);-63% similar to PDB:1YQ0 Structure of p97/VCP in complex with ADP/ADP.AlFx (E_value = 2.7E_44);-63% similar to PDB:1YQI VCP/p97 complexed with ADP (E_value = 2.7E_44);","Residues 268 to 465 (E_value = 1.1e-56) place ANA_0673 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).","","(cdc48) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0674","709511","711190","1680","5.68","-13.43","60863","ATGAACGATGTCGGCTTTCAGCCCGGTCCGGTGACGCGACCCGTCGGCCTGGAGACCGAGTTCGGGGTCCTGCGCCCGGGCGACGCCTACGCCAACCCCGTGGTCCTGTCCACCCGCGTGGTGGAGGCCTACTGCGCAGGCTCCGGCGTGCCCACCGTGCGGTGGGACTACGAGGGAGAGGATCCCCTGGCCGACCTGCGAGGCGGCAGGCTCCGGCGCTCCGCCGCCCACCCCAGCCAGCTCACCGACGACCCCGCCCGCCCTGCGCCCTCGGGCGATGCACCGTCGGCCGATGCGGGGGAGACGGCAGACCCTCCGCCGGCCCCCTGGGGGTCGCGCGCTCGCCCCAGTGCCGCCGAGGCAGCCCTGCCCCGGGCCACGACTGCGGTCCTGGTCAACGGCGCCCGCTTCTACGTCGACCACGCCCACCCCGAGTACTCCTCACCCGAGGTCCTCACACCCCGCGACGCCCTGATCTGGGACCGCGCCGGTGAGGTGGTCGCCCGGCGCGCCATGACGGCCCTGGGTGACGAGGGCGATCGGGATGGGACACCGGTGGAGATCGTCCTGTACAAGAACAACGTGGATGGCAAGGGTGCGGCCTACGGCTCCCACGAGAACTACCTCGTGCGGCGCGATGTGCCCTTCGAGGAGCTGGCCGCGGTCCTGACCCCCTTCCTCGTCACCAGGCCCGTCATCGCCGGTGCCGGCCGGGTCGGGATCGGGCAGCGCAGTGAGCACCCCGGATTCCAGGTCAGCCAGCGCGCCGACTACGTCGAGTCCGAGATCGGCCTGCAGACCACGTTCAACCGCCCCATCATCAACACCCGCGACGAACCGCACGCCGACAATGCCCGCTGGCGCAGGCTTCACGTCATCAACGGTGACGCCAACCGCTTCGACGTTCCCATCTACCTCAAGGTCGCCACCACCGACCTGCTTGTCTGGTTCCTGGAGCAGGCGTGCACCGAGGGCTCCGGCCCGTTCAAGGAGGCTCTGGCCCGCGTCAAGGACCTGGCCATCATCGGCGATCCTGTCGAGGAGCACTGGGCCCTCTCCCACGACCCCACCCTGTCTCACGAGCTGCGAACCCAGGCCGGGGCCTTGACCGCCCTGGCGATTCAACGCGCCTTCCTCGATGCCGTCAGCCCCACTGTCACCCGTGTCGAGGACGCCCGGGCTCATCGCGCCCTGGCTCTGTGGAGGCAGGTCCTCGACGCCCTGGAGCAGTGGCGCCATGACGGATCCGGCCCTGCTGCTCAGATGGTGGAATGGGTTGCCAAGTACGAGCTCTGCGAGGGACTGCGCCGCAGGTCGGGAACCGGCTGGGATGACCCCCGTCTGGCCGCTCTCGACATCCAGTGGGCCGACCTGCGACCGGGACGATCCGTCGTCGACAAGCTCGACGCCGCCGGCAGGATCCACCGGCTGGTCACCGACGCGGAGATCCAAAACGCGGTCGACACGCCCCCCGAGGGCACGCGCGCCGCTATCCGGGGAACCGCCATCCGCCGTCACCGGCAGGTCGTGGGAGCCTCCTGGACCTGCCTGCTCCTCGACGTGCCGGGTGCCCCCGCTCTGGCGCGTCTGCGCCTGCCAGACGACGTGGTCGTCGGCTCTGATGAGACGGCGACCATCCTGGAGGAAATTGGTCGCCGGGCAGATCCTGAGAGACACTGA","MNDVGFQPGPVTRPVGLETEFGVLRPGDAYANPVVLSTRVVEAYCAGSGVPTVRWDYEGEDPLADLRGGRLRRSAAHPSQLTDDPARPAPSGDAPSADAGETADPPPAPWGSRARPSAAEAALPRATTAVLVNGARFYVDHAHPEYSSPEVLTPRDALIWDRAGEVVARRAMTALGDEGDRDGTPVEIVLYKNNVDGKGAAYGSHENYLVRRDVPFEELAAVLTPFLVTRPVIAGAGRVGIGQRSEHPGFQVSQRADYVESEIGLQTTFNRPIINTRDEPHADNARWRRLHVINGDANRFDVPIYLKVATTDLLVWFLEQACTEGSGPFKEALARVKDLAIIGDPVEEHWALSHDPTLSHELRTQAGALTALAIQRAFLDAVSPTVTRVEDARAHRALALWRQVLDALEQWRHDGSGPAAQMVEWVAKYELCEGLRRRSGTGWDDPRLAALDIQWADLRPGRSVVDKLDAAGRIHRLVTDAEIQNAVDTPPEGTRAAIRGTAIRRHRQVVGASWTCLLLDVPGAPALARLRLPDDVVVGSDETATILEEIGRRADPERH$","Proteasome component","Cytoplasm","Putative proteasome component family","hypothetical protein","protein of unknown function DUF245 domain protein","","Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R. The 20S proteasome of Streptomyces coelicolor. J. Bacteriol. 1998. 180(20):5448-5453. PMID: 9765579Pouch M.N., Cournoyer B., Baumeister W. Characterization of the 20S proteasome from the actinomycete Frankia. Mol. Microbiol. 2000. 35(2):368-377. PMID: 10652097Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., Tanaka K., De Mot R., Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr. Biol. 1995. 5(7):766-774. PMID: 7583123","","","

InterPro
IPR004347
Domain

Protein of unknown function DUF245, C-terminal
PF03136	$\"[210-550]T$	DUF245

InterPro
IPR004989
Domain

Protein of unknown function DUF275, N-terminal
PF03316	$\"[15-209]T$	DUF275

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 15-78 are 61% similar to a (PROTEASOME COMPONENT MLCB2533.17 SIMILAR CGL1496 ORF61 RHODOCOCCUS NI86/21 SCO1647 B2126_C1_172) protein domain (PD022888) which is seen in Q49779_MYCLE.Residues 130-209 are 68% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD009688) which is seen in Q53081_RHOER.Residues 212-410 are 60% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD008464) which is seen in Q73YW6_MYCPA.Residues 423-530 are 62% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 B2126_C3_265 SCO1640 ORF61 RHODOCOCCUS) protein domain (PD008229) which is seen in Q7AKQ3_STRCO.","","-47% similar to PDB:1UPI MYCOBACTERIUM TUBERCULOSIS RMLC EPIMERASE (RV3465) (E_value = );-42% similar to PDB:1Z01 2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction (E_value = );-42% similar to PDB:1Z02 2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction (E_value = );-42% similar to PDB:1Z03 2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction (E_value = );","Residues 15 to 209 (E_value = 1.4e-42) place ANA_0674 in the DUF275 family which is described as Actinomycetales protein of unknown function, DUF275.Residues 210 to 550 (E_value = 5.7e-91) place ANA_0674 in the DUF245 family which is described as Putative proteasome component.","","proteasome component family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0675","711199","711465","267","5.03","-4.34","9164","GTGCGCTCACCAGCGGTGAGCAGCTGGGCAGGACGAGTGAAGGAGCAACACATGACGCCGCAGCACGCCAGTCAGACCCATGGGCAGGTCCGTCGCACCGGCGTCGAGACCACTGCAGCCGACGCCGACCAGGCCATCAGCACCGGTACATCCGCGTCGGCCGAGCAGGCCAGTGACGTTGACAGCATCCTCGACGAGATCGACTCGGTCATCGAGACCAATGCCGCGGCCTTCGTCCAGGGCTTCGTTCAGAAGGGCGGCCAGTGA","VRSPAVSSWAGRVKEQHMTPQHASQTHGQVRRTGVETTAADADQAISTGTSASAEQASDVDSILDEIDSVIETNAAAFVQGFVQKGGQ$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

InterPro
IPR008515
Family

Protein of unknown function DUF797
PF05639	$\"[28-88]T$	DUF797

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 28 to 88 (E_value = 3.9e-12) place ANA_0675 in the DUF797 family which is described as Protein of unknown function (DUF797).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0676","711486","712907","1422","5.56","-16.83","52336","TTGGCGCGGCGCATCATCGGGGTGGAGACCGAGTACGGCATCACCTGCGCCCCCACCACCGACGGCCCTCCTCCCATGGACGCCGACCACGCTGCTCGTGAGCTCTTCGAACCCGTGGTCCAGCGCTCTCGCTCCTCGAACGTCTTCACTCGCGGGGGCGCTCGTCTCTACCTGGACGTGGGCTCCCACCCCGAGTTCGCCACCGCCGAGTGCGACCGCCTCGAGGACGTGCTCGCTCAGGACCGCGCCGGTGAGCTCGTCATGGCCGATCTCGTCGAGCAGGCCAATGCGCACCTGGTAGCCTCGGGTGTCCCCGGGCGGATCCACCTGCTGAAGAACAACCGCGACGCTGAGGACAACGGCTTCGGGTGCCACGAGAACTACCTCGTGCGGCGTCGTGGAGACTTCTGGAACGACGCCCGCACTCTCGTACCCCACCTGGTGACCCGGCAGATCCTCGTCGGCGCCGGCCATATCACCGCAGGCGGGGACGCTCGGCCCGCCGCCGACGGGCTCCGGGGCTATGTCTTCTCCCAGCGGGCCGACCAGATGTGGGACGCCGTCTCCTCAGCCACGACCCGGGCCAGGCCGCTGATCAACACCCGGGACGAACCGCATGCCGATGCCGAGCGTTACCGGCGCATGCACGTCATCGTCGGGGACTCCAACATCGCTCAGGGATCCACCCTGCTCAAAGTGGCGGCCATGGACCTGCTCCTGGACTACCTGGAGCACGGGGGAGACCTCGGCGACCTGGCCCTGGCCGACCCCATGAGGGCCATTCGCGACACCTGCCATGACATGACTGGAGGGGTGCTCCTGGAACGGTCTGACGGGCGGACCATCACGCCGTTGGAGATGCAGGCCGAGCACCTCGGGCGTCTCCGTGACCACGTTGCGCAGGGCATCGAGGTCACTGCTCTGCACGAAGCCGCACTGGAACTGTGGGAACGAGGACTCCAGGCCCTGCGCCTGCAGCAGCCCGAGATCGTGGACACGGAGCTGGACTGGGCGGTCAAGCAGCGGCTGCTGACCCGTTACTGCCAGCGGCACGACACCGATCTGACCGATCCCCGGGTGAACCGCCTGGCCCTGGCCTACCACGACGTCTCTCCCGGTGAGGGACTGCGACAGCGTCTGGAGGACGCTGGTCTCCTGCACCGATTCGTTGACGAGGCGACCTGCCGCCGGGCGGTGGATACCCCACCTGCGACCACGCGTGCGCGCCTGCGCGGCGCCGTCGTCGGCCGGGCCGAGGACCTGCGCCGTGACGTGAGTGTTGACTGGGTGCGGGTTCGACTCGACGACGGCGTCTGCTCACCTGTTACGCTGAATGATCCCTTCTGTGCCGTAGACGAGCGCATCGATGCACTCCTGGAGAGCATGGAGCACTCGGCAACCGACCTTCCCAACGGGGTGTGA","LARRIIGVETEYGITCAPTTDGPPPMDADHAARELFEPVVQRSRSSNVFTRGGARLYLDVGSHPEFATAECDRLEDVLAQDRAGELVMADLVEQANAHLVASGVPGRIHLLKNNRDAEDNGFGCHENYLVRRRGDFWNDARTLVPHLVTRQILVGAGHITAGGDARPAADGLRGYVFSQRADQMWDAVSSATTRARPLINTRDEPHADAERYRRMHVIVGDSNIAQGSTLLKVAAMDLLLDYLEHGGDLGDLALADPMRAIRDTCHDMTGGVLLERSDGRTITPLEMQAEHLGRLRDHVAQGIEVTALHEAALELWERGLQALRLQQPEIVDTELDWAVKQRLLTRYCQRHDTDLTDPRVNRLALAYHDVSPGEGLRQRLEDAGLLHRFVDEATCRRAVDTPPATTRARLRGAVVGRAEDLRRDVSVDWVRVRLDDGVCSPVTLNDPFCAVDERIDALLESMEHSATDLPNGV$","Proteasome component","Cytoplasm","Putative proteasome component superfamily","hypothetical protein","protein of unknown function DUF245 domain protein","","Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R. The 20S proteasome of Streptomyces coelicolor. J. Bacteriol. 1998. 180(20):5448-5453. PMID: 9765579Pouch M.N., Cournoyer B., Baumeister W. Characterization of the 20S proteasome from the actinomycete Frankia. Mol. Microbiol. 2000. 35(2):368-377. PMID: 10652097Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., Tanaka K., De Mot R., Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr. Biol. 1995. 5(7):766-774. PMID: 7583123","","","

InterPro
IPR004347
Domain

Protein of unknown function DUF245, C-terminal
PF03136	$\"[130-462]T$	DUF245

InterPro
IPR004989
Domain

Protein of unknown function DUF275, N-terminal
PF03316	$\"[47-129]T$	DUF275

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 6-129 are 66% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD009688) which is seen in YK97_MYCLE.Residues 130-323 are 68% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD008464) which is seen in Q7WZ91_BBBBB.Residues 331-462 are 65% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 B2126_C3_265 SCO1640 ORF61 RHODOCOCCUS) protein domain (PD008229) which is seen in P72263_RHOER.","","No significant hits to the PDB database (E-value < E-10).","Residues 47 to 129 (E_value = 3e-15) place ANA_0676 in the DUF275 family which is described as Actinomycetales protein of unknown function, DUF275.Residues 130 to 462 (E_value = 1.2e-111) place ANA_0676 in the DUF245 family which is described as Putative proteasome component.","","proteasome component superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0677","712955","714409","1455","6.58","-1.55","50182","ATGAGTACTACCTCCCCTCTGGACCCCGAAGCGGGCATGCCCCTGACACGGCGTCAGCGCCGTGCGCTCGAACGTGCTCAGCAGGCCCAGCAGGAGGCAGCGACCCAGGACCTGCCGGCACTGTCTCAACCTACTGTGCAGACACGCCCTGCCGGTACTGTGTCCCCCGGCACTCGAACCACAACCGGCACACCGGCGCCGCGCACTGAGCTGCAACCGCAGCCGCAGCGTCAGCCACGGACTCTGCCACAGCCTCAGGAGCTGGGTAGCAGCCATGATCGTCGCAACGCGCACAGACCGTCCGCACGAACTGATCGACGCGATCACCCTCATGAGCCCGGGTACCGACAGGACGAGGTGGTCGCCGAGACCCAGGAGCCCGAACCGACGCAGCGGCAACATACTCTGGGCGGTCCGCTGGGGCGTATGCCGCGGGGGCCCCTGGCGGTCGCCCTCATCGGTGTCGTCGTCCTTGCCATGATCCTGGTGCCGCTGGCTGTCAACAAGCTCGTCTCCGGAAGGAACGGAGCGGGCACCAGCACCGCGGCTCAGTCAACCGTGTTGGATGGCAACGCACCTCTCAGTCAGCTGCTGACGGTCAGCGGACGGGTCGGATCAGGGGTGGCCCCCTCCGTCGAGCTGAACGGCGACGCCTCTCTGTCAGCCCCCAGCTCGGTACTGACCGACGTCGTCCAGACCGGGCAGGGGCGCGCTGTCTCCGCGGGGACGCCTGTGATCCTGCAGGTCTCACAGTTCTCCGGTCTCAACGGGAGCAACACGACGGGTAACGAGGCAGGGTATAAGCTCTGGCAGGGCCTGCTCGGGCCCGAGGTGGGCGACTACATCAACGCGGCGGTCTCCGGCCAGCGCGAAGGCGCACGCGTCGTTCTGCGCGAACCGGCCCAGGAGGAAGACGGCTCCCGGACGACGAAGATCACCGTTGTCGACCTCTTACCCACCACTGCGACAGGGGAGACGAAGCAACCGGCGGCAGGGGCCCCCACCGTGACCGAAGGACCGGACGGCTCCATCACCGTCAGCAGCGCTGGACTTCCTGCACCGACTCGAGTGTCCACAGAGATCCTCATCAAGGGCACCGGTCCGCAGATCGGTTCCCAGGACCGTCTGATCGCTCGGACCACGATGGTCAGCTGGGCCACGGGACAGCCCCTTGAGAAGTCAACCTTCGGGCACCAGGAGCCGCCCAAGCAGCTCGACATGAGCAACGCGCTGGTGGGAGTCTCGCAGAACCTGGTTGATATCACTGTCGGCTCCCGGGTGGTCCTCTCGCTGCCCGCTGAGCAGGCGCAGGGCAAGGAACCAGTCGTCGTCGTGATCGATGTCCTGGCCAAGGATCCTGTCCAGGCTTCCGGAGCCTCTGGGGCGCGTGCAGGCAGTGAGTCGAGCCCCACTCCTGACATCTCCGCCGGCCCAACATCCAAGGACCAGTCATGA","MSTTSPLDPEAGMPLTRRQRRALERAQQAQQEAATQDLPALSQPTVQTRPAGTVSPGTRTTTGTPAPRTELQPQPQRQPRTLPQPQELGSSHDRRNAHRPSARTDRRDHPHEPGYRQDEVVAETQEPEPTQRQHTLGGPLGRMPRGPLAVALIGVVVLAMILVPLAVNKLVSGRNGAGTSTAAQSTVLDGNAPLSQLLTVSGRVGSGVAPSVELNGDASLSAPSSVLTDVVQTGQGRAVSAGTPVILQVSQFSGLNGSNTTGNEAGYKLWQGLLGPEVGDYINAAVSGQREGARVVLREPAQEEDGSRTTKITVVDLLPTTATGETKQPAAGAPTVTEGPDGSITVSSAGLPAPTRVSTEILIKGTGPQIGSQDRLIARTTMVSWATGQPLEKSTFGHQEPPKQLDMSNALVGVSQNLVDITVGSRVVLSLPAEQAQGKEPVVVVIDVLAKDPVQASGASGARAGSESSPTPDISAGPTSKDQS$","Peptidylprolyl isomerase, FKBP-type","Membrane, Periplasm","peptidyl-prolyl cis-trans isomerase, FKBP-typedomain protein","peptidylprolyl isomerase; FKBP-type","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[148-168]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 201-370 are 44% similar to a (ISOMERASE PEPTIDYLPROLYL LIPOPROTEIN ROTAMASE CIS-TRANS PEPTIDYL-PROLYL DRUG-BINDING FKBP-TYPE) protein domain (PD716843) which is seen in Q6AFW4_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","cis-trans isomerase, FKBP-type domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0678","714406","715176","771","5.83","-4.64","26600","ATGAGCGTTGCCATCCGCATCATTCCCTGTCTGGACGTCAAGGACGGTCGTGTCGTCAAAGGCGTCAACTTCCAGGGTCTCAAGGATGCCGGAGACCCCGTGGAGCTCGCCTCCCGCTACGGCGCCCAAGGGGCCGACGAGATCACATTCCTCGATGTCTCGGCCTCGCACGAGGGCCGTTCCACCATGTTGGACGTGGTCCGCCGTACTGCCGAGCAGGTCTTCGTTCCGCTGACCGTCGGCGGGGGAGTGCGCTCAGTCGATGACGTGGACCAGCTGCTGCGTGCCGGGGCGGACAAAGTCGGTATCAACACTGCGGCCATTAACCGTCCCGAACTGTTGACAGAGGTGGCGCAGCGTTTTGGCAATCAGGTGATCGTCCTGTCGGTGGATGCGCGTCGGTGCCCTTCCGGCGTCTCAACGGCCTCCGGCTTCGAGGTCACCACGCACGGAGGGCGGACCTCCACCGGCATTGATGCAGTCGCCTGGGCGGTTCAAGGAGCCGAGCTCGGCGCCGGTGAGATTCTCCTGAACTCCATGGATGCCGACGGTGTCACCAAAGGATTCGACACTGAGATGATCGACGCCGTTCGTCGGCGGGTCCGGGTGCCACTCATCGCCTCCGGCGGTGCCGGATCCCCGCAGGACTTCGTCACGGCGGCCAACCACGGTGCCGACGCCGTTCTGGCAGCCTCAGTGTTCCACTACGGAGTGATGACCATCGCTGCGGCCAAGAATGCGCTGCACGACGCAGGCCATCCGGTCCGTTGA","MSVAIRIIPCLDVKDGRVVKGVNFQGLKDAGDPVELASRYGAQGADEITFLDVSASHEGRSTMLDVVRRTAEQVFVPLTVGGGVRSVDDVDQLLRAGADKVGINTAAINRPELLTEVAQRFGNQVIVLSVDARRCPSGVSTASGFEVTTHGGRTSTGIDAVAWAVQGAELGAGEILLNSMDADGVTKGFDTEMIDAVRRRVRVPLIASGGAGSPQDFVTAANHGADAVLAASVFHYGVMTIAAAKNALHDAGHPVR$","Imidazoleglycerol phosphate synthase, cyclase subunit","Cytoplasm","imidazoleglycerol phosphate synthase, cyclasesubunit","imidazole glycerol phosphate synthase subunit ","imidazoleglycerol phosphate synthase, cyclase subunit","","","","","

InterPro
IPR004651
Domain

Histidine biosynthesis, HisF
TIGR00735	$\"[2-256]T$	hisF: imidazoleglycerol phosphate synthase,

InterPro
IPR006062
Domain

Histidine biosynthesis
PF00977	$\"[6-240]T$	His_biosynth

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[2-256]T$	no description

noIPR
unintegrated

unintegrated
PTHR21235	$\"[101-256]T$	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H (IGP SYNTHASE SUBUNIT HISF/H)
PTHR21235:SF2	$\"[101-256]T$	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF (IGP SYNTHASE SUBUNIT HISF)

","BeTs to 18 clades of COG0107COG name: Imidazoleglycerol-phosphate synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0107 is aom---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB006062 (Histidine biosynthesis protein) with a combined E-value of 7.1e-72. IPB006062A 7-20 IPB006062B 31-56 IPB006062C 76-124 IPB006062D 171-191 IPB006062E 201-217 IPB006062E 74-90","Residues 1-48 are 95% similar to a (SUBUNIT SYNTHASE HISF IGP HISTIDINE BIOSYNTHESIS IMIDAZOLE PHOSPHATE GLYCEROL 4.1.3.-) protein domain (PD581226) which is seen in HIS6_CORDI.Residues 67-118 are 94% similar to a (SUBUNIT SYNTHASE HISF IGP HISTIDINE BIOSYNTHESIS PHOSPHATE GLYCEROL IMIDAZOLE 4.1.3.-) protein domain (PD697329) which is seen in HIS6_STRAW.Residues 71-121 are 84% similar to a (ISOMERASE HISTIDINE BIOSYNTHESIS SUBUNIT SYNTHASE CARBOXAMIDE PHOSPHORIBOSYLFORMIMINO-5-AMINOIMIDAZOLE RIBOTIDE IMIDAZOLE-4-CARBOXAMIDE 1-5-PHOSPHORIBOSYL-5-5-PHOSPHORIBOSYLAMINOMETHYLIDENEAMINO) protein domain (PD555676) which is seen in Q6A7Y8_PROAC.Residues 117-236 are 48% similar to a (SUBUNIT HISF2 SYNTHASE PHOSPHATE IGP BIOSYNTHESIS IMIDAZOLE GLYCEROL HISTIDINE IMGP) protein domain (PD922168) which is seen in Q7WYR2_BBBBB.Residues 122-193 are 78% similar to a (SUBUNIT SYNTHASE HISF ISOMERASE HISTIDINE IGP BIOSYNTHESIS IMIDAZOLE PHOSPHATE GLYCEROL) protein domain (PD625483) which is seen in HIS6_MYCPA.Residues 194-256 are 69% similar to a (SUBUNIT SYNTHASE HISF IGP HISTIDINE BIOSYNTHESIS IMIDAZOLE PHOSPHATE GLYCEROL 4.1.3.-) protein domain (PD223608) which is seen in Q6A7Y8_PROAC.Residues 196-256 are 63% similar to a (SUBUNIT HISF SYNTHASE IGP BIOSYNTHESIS IMGP IGPS IMIDAZOLE PHOSPHATE CYCLASE) protein domain (PD244923) which is seen in HIS6_HALN1.","","-66% similar to PDB:1KA9 Imidazole Glycerol Phosphate Synthase (E_value = 5.2E_67);-66% similar to PDB:1H5Y HISF PROTEIN FROM PYROBACULUM AEROPHILUM (E_value = 1.2E_63);-63% similar to PDB:1VH7 Crystal structure of a cyclase subunit of imidazolglycerolphosphate synthase (E_value = 3.6E_60);-63% similar to PDB:2A0N Crystal structure of Imidazole glycerol phosphate synthase subunit hisF (EC 4.1.3.-) (tm1036) from Thermotoga maritima at 1.64 A resolution (E_value = 3.6E_60);-63% similar to PDB:1THF CYCLASE SUBUNIT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA (E_value = 6.2E_60);","Residues 6 to 240 (E_value = 6.7e-124) place ANA_0678 in the His_biosynth family which is described as Histidine biosynthesis protein.","","phosphate synthase, cyclase subunit (hisF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0679","716254","716667","414","10.61","6.31","14367","ATGCGGGTCGGACTGGGGCTTCTGATGGTTCTGTCCGCCCTGCCGGGTGGCCTCATCGTGCTGCGCGCTCTGACTCTGCCCCGCAGCTCTCCGGGGCTTCCCGACCTCTGCCCGCTTCACCGCACCACCGGGCTGTGGTGCCCGCTGTGCGGAGGTACCCGGGCGACTCGGGAGCTCATACACGGCGACCTGTGGGCCGCCATGGGTTACAACCCCTTTGCGCTTGCGCTGGAGGCGGTGGCCGTTGTCCTGGTGGCGCGCTGGTTGCTCGCATCCGCCCGAGGCCTGCGACGACCGCTCGTCACCGGTGGGGAGGGCATCCTTTTCGGGGTCGCGCTGGCCGTCTTCGCGGTGGTACGCAACCTGCCAGGCATGTGGGTCTACCTCGGTCCTCTGCTTGGCCCTCCGGGCTGA","MRVGLGLLMVLSALPGGLIVLRALTLPRSSPGLPDLCPLHRTTGLWCPLCGGTRATRELIHGDLWAAMGYNPFALALEAVAVVLVARWLLASARGLRRPLVTGGEGILFGVALAVFAVVRNLPGMWVYLGPLLGPPG$","Conserved membrane protein","Membrane, Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[70-90]?$ $\"[100-120]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-50% similar to PDB:1H3N LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A SULPHAMOYL ANALOGUE OF LEUCYL-ADENYLATE (E_value = );-50% similar to PDB:1OBC LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A POST-TRANSFER EDITING SUBSTRATE ANALOGUE (E_value = );-50% similar to PDB:1OBH LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A PRE-TRANSFER EDITING SUBSTRATE ANALOGUE IN BOTH SYNTHETIC ACTIVE SITE AND EDITING SITE (E_value = );-50% similar to PDB:2BTE THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION AND A POST-TRANSFER EDITING SUBSTRATE ANALOGUE (E_value = );-50% similar to PDB:2BYT THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0680","716680","717057","378","6.27","-2.73","13855","GTGCATAATGCGGATGTGACTCTCGATTCCCAGATCTCTGCGCGCCTGAAGCGCAACACCGACGGCCTGGTCTGCGCCGTCGTCCAGCAGTACGACTCACATGAGGTCCTCATGGTGGGGTGGATGGACGATGAAGCGCTCCGGCGCACCCTGGAAGAGGGACGAGTGACCTTCTGGTCGCGGTCGCGGCGCGAGTACTGGCGCAAGGGGGACACGTCCGGACACGCGCAGTACGTCAAGTCCGTCCATCTGGACTGCGACGGCGACGCCCTCCTGATCAAGGTCGATCAGGTCGGAGCCGCCTGCCACACCGGCGAGCGCAGCTGCTTCCTGGCCGGCGGTGATCTGGGGGCGCACGTGGGAGACCGTCCCAGCTGA","VHNADVTLDSQISARLKRNTDGLVCAVVQQYDSHEVLMVGWMDDEALRRTLEEGRVTFWSRSRREYWRKGDTSGHAQYVKSVHLDCDGDALLIKVDQVGAACHTGERSCFLAGGDLGAHVGDRPS$","Phosphoribosyl-AMP cyclohydrolase","Cytoplasm","Phosphoribosyl-AMP cyclohydrolase (PRA-CH)","phosphoribosyl-AMP cyclohydrolase ","Phosphoribosyl-AMP cyclohydrolase","","D. Ordine R.L., Klem T.J., Davisson V.J. N1-(5'-phosphoribosyl)adenosine-5'-monophosphate cyclohydrolase: purification and characterization of a unique metalloenzyme. Biochemistry 1999. 38(5):1537-1546. PMID: 9931020","","","

InterPro
IPR002496
Family

Phosphoribosyl-AMP cyclohydrolase
PD002610	$\"[61-110]T$	HIS3_BIFLO_Q8G6F6;
PF01502	$\"[38-112]T$	PRA-CH

noIPR
unintegrated

unintegrated
PTHR21256	$\"[27-110]T$	HISTIDINOL DEHYDROGENASE (HDH)

","BeTs to 18 clades of COG0139COG name: Phosphoribosyl-AMP cyclohydrolaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0139 is aom---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002496 (Phosphoribosyl-AMP cyclohydrolase) with a combined E-value of 1.1e-42. IPB002496A 42-95 IPB002496B 101-112","Residues 15-60 are 86% similar to a (HISTIDINE BIOSYNTHESIS HYDROLASE PHOSPHORIBOSYL-AMP CYCLOHYDROLASE PRA-CH BIFUNCTIONAL INCLUDES: PHOSPHORIBOSYL-ATP PYROPHOSPHATASE) protein domain (PD431341) which is seen in HIS3_BIFLO.Residues 61-110 are similar to a (HISTIDINE BIOSYNTHESIS PHOSPHORIBOSYL-AMP CYCLOHYDROLASE HYDROLASE PRA-CH PHOSPHORIBOSYL-ATP INCLUDES: BIFUNCTIONAL PYROPHOSPHATASE) protein domain (PD002610) which is seen in HIS3_BIFLO.","","-70% similar to PDB:1ZPS Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI (E_value = 4.0E_27);-47% similar to PDB:1ZY8 The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex. (E_value = 4.0E_27);-47% similar to PDB:2DNC Solution Structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid dehydrogenase (E_value = 4.0E_27);-59% similar to PDB:1YZ8 Solution structure of the k50 class homeodomain pitx2 bound to dna and implications for mutations that cause rieger syndrome (E_value = 4.0E_27);-57% similar to PDB:2DMU Solution structure of the homeobox domain of Homeobox protein goosecoid (E_value = 4.0E_27);","Residues 38 to 112 (E_value = 3.4e-45) place ANA_0680 in the PRA-CH family which is described as Phosphoribosyl-AMP cyclohydrolase.","","cyclohydrolase (PRA-CH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0681","717172","717996","825","5.24","-8.72","28437","ATGACCTCGTTCGAGGCGATGGTGGCCGAGGCCAAGATGGCTGCCGAAGGTCGCGCTTCGCTGGTACCCCTGGCCCGCCTGAGAGAGGCCTCCCGCCTGGTTCCCGGCGCCATCAGCGCCCTGTCCAGCCTGCGCACCGATGATCGGGCGGTCACAGTGATCGCCGAGGTCAAGCGCTCCACGGCCACGTTCGCCGACCTCAGTGGCGTTGGGGATCCGGGGATGCTGGCCTGCTTCTACGCCGCCGGCGGCGCCGCCTGCGTCTCAGTGGTCACCGGGCCGAGTGCCACGCGAGGCTCCCTCAAGGACCTGGATGCAGTCAGGGCCTCCGTGGATCTTCCCGTCCTCGCCAACGACCTGGTGGTCACGCCCTACCAGGTGCACGAGGCCCGGGCTCACGGCGCCGATCTGCTCATGCTCGACGCCCGCCTTGAGCCCCTCGTGCTCGAAGGGCTCATCGAGAGGGTGCACTCCCTGGGGATGGGCGCCGTTGTCGAGGTCCGTACCCGCCGTGAGGCGCTGACCGCAGTCGATGCGGGGGCCTGCATCGTGGCCATCGACACCCGTGATCCCGACACCCTGGCCGTCGACTGCAGCCTGTTCGACCAGGTCACTGACGTTCTGCCGGCGCAGGTCGTGCGGATCGCCGCCGGAGGAGTCAGAGGCCCGCACGATGTCATGAGCTTCGCGCGCTGCGGCGCCGATGTCGTCCTCGTCGGTGAGGCCATCATCCGCTCCACCGACCCCCAGCAGTTCGTTGCCGAGCTGGTCGCCGCCGGCGCCCACCCGGCACTGATCCCCTCCGCCCATCGAGAGGTTCTCTGA","MTSFEAMVAEAKMAAEGRASLVPLARLREASRLVPGAISALSSLRTDDRAVTVIAEVKRSTATFADLSGVGDPGMLACFYAAGGAACVSVVTGPSATRGSLKDLDAVRASVDLPVLANDLVVTPYQVHEARAHGADLLMLDARLEPLVLEGLIERVHSLGMGAVVEVRTRREALTAVDAGACIVAIDTRDPDTLAVDCSLFDQVTDVLPAQVVRIAAGGVRGPHDVMSFARCGADVVLVGEAIIRSTDPQQFVAELVAAGAHPALIPSAHREVL$","Indole-3-glycerol-phosphate synthase","Cytoplasm","indole-3-glycerol phosphate synthase","indole-3-glycerol-phosphate synthase ","Indole-3-glycerol-phosphate synthase","","Lolis E., Alber T., Davenport R.C., Rose D., Hartman F.C., Petsko G.A. Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 1990. 29(28):6609-6618. PMID: 2204417Knowles J.R. Enzyme catalysis: not different, just better. Nature 1991. 350(6314):121-124. PMID: 2005961Olah J., Orosz F., Keseru G.M., Kovari Z., Kovacs J., Hollan S., Ovadi J. Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease. Biochem. Soc. Trans. 2002. 30(2):30-38. PMID: 12023819","","","

InterPro
IPR000652
Family

Triosephosphate isomerase
PD001005	$\"[241-256]T$	O74067_CERSY_O74067;

InterPro
IPR001468
Domain

Indole-3-glycerol phosphate synthase, central region
PD001511	$\"[53-197]T$	TRPC_MYCTU_O06129;

InterPro
IPR002638
Family

Quinolinate phosphoribosyl transferase
PD003988	$\"[198-240]T$	Q9HNY9_HALN1_Q9HNY9;

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[4-258]T$	no description

InterPro
IPR013798
Domain

Indole-3-glycerol phosphate synthase
PF00218	$\"[5-256]T$	IGPS

noIPR
unintegrated

unintegrated
PTHR22854	$\"[27-266]T$	TRYPTOPHAN BIOSYNTHESIS PROTEIN
PTHR22854:SF2	$\"[27-266]T$	INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE

","BeTs to 21 clades of COG0134COG name: Indole-3-glycerol phosphate synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0134 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 53-197 are 68% similar to a (SYNTHASE PHOSPHATE INDOLE-3-GLYCEROL LYASE IGPS DECARBOXYLASE TRYPTOPHAN BIOSYNTHESIS ISOMERASE INCLUDES:) protein domain (PD001511) which is seen in TRPC_MYCTU.Residues 201-257 are 73% similar to a (SYNTHASE PHOSPHATE INDOLE-3-GLYCEROL LYASE IGPS DECARBOXYLASE TRYPTOPHAN BIOSYNTHESIS ISOMERASE INCLUDES:) protein domain (PD551789) which is seen in Q82A84_STRAW.","","-54% similar to PDB:1VC4 Crystal Structure of Indole-3-Glycerol Phosphate Synthase (TrpC) from Thermus Thermophilus At 1.8 A Resolution (E_value = 6.1E_24);-52% similar to PDB:1A53 COMPLEX OF INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS WITH INDOLE-3-GLYCEROLPHOSPHATE AT 2.0 A RESOLUTION (E_value = 3.2E_17);-52% similar to PDB:1IGS INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS AT 2.0 A RESOLUTION (E_value = 3.2E_17);-52% similar to PDB:1JUK INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS IN A TRIGONAL CRYSTAL FORM (E_value = 3.2E_17);-52% similar to PDB:1JUL INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS IN A SECOND ORTHORHOMBIC CRYSTAL FORM (E_value = 3.2E_17);","Residues 5 to 256 (E_value = 2.3e-25) place ANA_0681 in the IGPS family which is described as Indole-3-glycerol phosphate synthase.Residues 86 to 258 (E_value = 0.00015) place ANA_0681 in the NanE family which is described as Putative N-acetylmannosamine-6-phosphate epimerase.","","phosphate synthase (trpC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0682","717997","719055","1059","6.81","-0.62","37552","GTGCCTGTCGCCGCCCTTTCCGCCATGATGCCAACGATGCCAACGATGCCAACACTGCTGACGATGCCGTTCACGGCCGCGCTGACCGCAGGCATACCGAGCCCGTCCTCGCCCGTGTGGTACCTCGGCCCCATCCCGGTGAGGGCCTACGCGTTGTGCATCCTCACCGGGGTCTTCGTGGCCGTGTGGTGGTCGGACCGGCGCTACCGGGCCCGGGGAGGCCGACCGGAGCTGGTCCTCGACGTCGCCATCGTGGCCGTGCCGGCTGGAATCGTGGGTGCCCGTCTCTACCACGTGATCTCCTCGCCCGACGACTACTTCGGCCCGAACGGCGACCTGGCCCGTATCCCACAGACATGGCAAGGGGGCCTGGGAATCTGGGGAGGCATCGCCGGCGGGGTCCTGGCTGGGGTGCTCCTACTGCGCCATCGCGGCCTGCGCGTAGCCCCGTTGGCCGACGCCGTCGCCCCGACCCTGCTGGTCGCTCAGGCGATCGGCCGACTGGGCAACTGGTTCAACCAGGAGCTCTACGGCTCCCCGACGACGCTGCCCTGGGGACTACGGATCGACGAGGCCCACCTGCCGGCGGGATCCACCTACCCACCCGGCACCCTGTTTCATCCGACCTTCCTCTATGAGGCCCTGTGGAACCTTGCTGGGGCGGCTCTTCTGGTGTGGATCGGCAGGCGGATGCTCGCCCGCAGCGGCGTCACGGGCGGCAGGCTGCTGTGGGTGTACCTCATGGTCTACACCGCCGGCCGGGTGTGGATCGAGATGCTGCGCATCGACGAGGCCGAGACGGTCCTCGGCCTGAGACTGAACGTGTGGACCTCCATCGTCATCTTCCTCGTCGGCGCTCTTGGACTGGCCCTCACCTCTCGGCGCCCCCTGAGCGACGCCATCGACAGGCCGGGGCGCGGGACGAGGAAGGACCGCTCGGCTGCCGAGGAGGATGACTCCGTCGAGGACGCCGCCGCTGAGCATGACTCGCCTGAGGGCGCCTCACCGGCAGAACCCGCCGCTACGGCGTCGGCCCACCCAGGTCAGACGGATTCGTAA","VPVAALSAMMPTMPTMPTLLTMPFTAALTAGIPSPSSPVWYLGPIPVRAYALCILTGVFVAVWWSDRRYRARGGRPELVLDVAIVAVPAGIVGARLYHVISSPDDYFGPNGDLARIPQTWQGGLGIWGGIAGGVLAGVLLLRHRGLRVAPLADAVAPTLLVAQAIGRLGNWFNQELYGSPTTLPWGLRIDEAHLPAGSTYPPGTLFHPTFLYEALWNLAGAALLVWIGRRMLARSGVTGGRLLWVYLMVYTAGRVWIEMLRIDEAETVLGLRLNVWTSIVIFLVGALGLALTSRRPLSDAIDRPGRGTRKDRSAAEEDDSVEDAAAEHDSPEGASPAEPAATASAHPGQTDS$","Prolipoprotein diacylglyceryl transferase","Membrane, Cytoplasm","Prolipoprotein diacylglyceryltransferase","prolipoprotein diacylglyceryl transferase ","prolipoprotein diacylglyceryl transferase","","Sankaran K., Wu H.C. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 1994. 269(31):19701-19706. PMID: 8051048","","","

InterPro
IPR001640
Family

Prolipoprotein diacylglyceryl transferase
PF01790	$\"[35-295]T$	LGT
TIGR00544	$\"[28-305]T$	lgt: prolipoprotein diacylglyceryl transfer
PS01311	$\"[166-178]?$	LGT

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[41-63]?$ $\"[78-100]?$ $\"[119-141]?$ $\"[151-171]?$ $\"[209-227]?$ $\"[242-257]?$ $\"[271-291]?$	transmembrane_regions

","BeTs to 17 clades of COG0682COG name: Prolipoprotein diacylglyceryltransferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0682 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001640 (Prolipoprotein diacylglyceryl transferase) with a combined E-value of 3.6e-37. IPB001640A 119-132 IPB001640B 153-179 IPB001640C 205-219 IPB001640D 240-264","Residues 95-170 are 68% similar to a (TRANSFERASE PROLIPOPROTEIN DIACYLGLYCERYL 2.4.99.- TRANSMEMBRANE INNER MEMBRANE LIPOPROTEIN GLYCOSYLTRANSFERASE CENTER) protein domain (PD285051) which is seen in LGT_BIFLO.Residues 175-277 are 65% similar to a (TRANSFERASE PROLIPOPROTEIN DIACYLGLYCERYL 2.4.99.- TRANSMEMBRANE INNER MEMBRANE LIPOPROTEIN GLYCOSYLTRANSFERASE FAMILY) protein domain (PD005412) which is seen in LGT2_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 295 (E_value = 7.2e-81) place ANA_0682 in the LGT family which is described as Prolipoprotein diacylglyceryl transferase.","","diacylglyceryltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0683","719178","720608","1431","5.20","-15.14","51230","ATGCGTAGAGCCAAGATCGTATGTACCCTCGGACCCGCTACTGACTCTCCCGAGCAGGTGCAAGCGCTCGTGGACGCCGGCATGAACGTCGCGCGCATCAACCGCTCCCACGGTCGCGCCGAGGACCAGGAAGAGGTCATCGGCCGCATCCGTGAGGCCGCAGCCGCTTCCGGCCGAGCCGTCGCCATCCTCGTCGACCTCCAGGGCCCCAAGATCCGACTGGGACGTTTCGTAGACGACCAGAAGGTCATGCTCAACAAGGGTGATGAGTTCACCATCACCATTGATGACGTTCTGGGCACCGTCAAGCGTGCCTCCACCACCTTCAAGGGACTTCCCGGCGACTGCCGCCCCGGCGACCGGCTCCTCATCGACGACGGCAACGTCGCGGTACGTGTCGTGGCCGTCACCGACACCGATGTCGTCACCAAGGTCGAGGTGCCCGGCTACGTCTCCAACAACAAGGGCATCAACCTGCCCGGTGTCGCCGTCTCCGTTCCGGCCCTGAGCGAGAAGGACCGCGAGGACCTGCGCTGGGCCCTCAAGATCGGTGCTGACCTCATCGCCCTGTCCTTCGTGCGCGACGCAGACGACATCAAGGACGTCCACGAGATCATGGACGAGGTCGGCGTGCGTATCCCGGTCATCGCCAAGATCGAGAAGCCCCAGGCGGTGGAGAACCTCTTCGACATCGTCTCCACCTTCGACGGCATCATGGTCGCCCGTGGTGACCTCGGTGTGGAAATGCCCCTGGAGGCCGTCCCGCTGGTGCAGAAACGCGCCATCGAGCTGGCCCGCCGCCAGGCCAAGCCGGTCATCGTGGCCACCCAGGTCCTGGAGTCCATGATCCAGAACCCGCGGCCCACACGGGCTGAGGCCTCCGACTGCGCCAACGCCATTCTCGACGGCGCCGACGCCGTCATGCTCTCCGGTGAGACCTCCGTGGGTGCCTACCCCATCGAGGCCGTGCGCACCATGGCCAGTATCATCGAGAACGTTGAGGAGCACGGAGGGGAGCGCATCCCCGGCCTGGGCTCCTACCCGCAGACGCGCGGCGGTGCCCTGACCCGCGCCGCCGCGGAGATGGGCGAGCACCTCGACGTCACCTACCTGGTGACCTTCACCCAGTCAGGTGACACCGCCCGGCGCCTGTCGCGTCTGCGCTCGCCGCTTCCGCTGCTTGCCTTCACCCCGCTGCACGAGACTCGCAACCAGCTCGCCGTCTCCTGGGGTGTGCAGTGCTACGAGGTGCCCGAGGTCCAGCACACTGACGAGATGGTGGCCCAGGTCGATGAGATCCTTCAGGACAAGCATCTGGCCCAGCCTGGGGACACCGTCGTCATCGTGGCCGGAATGCCTCCGGGCACGCCCGGCTCGACCAACTCGATCCGTGTCCACACCGTCGGTGAGACGGGCGACTACAAGGTCTGA","MRRAKIVCTLGPATDSPEQVQALVDAGMNVARINRSHGRAEDQEEVIGRIREAAAASGRAVAILVDLQGPKIRLGRFVDDQKVMLNKGDEFTITIDDVLGTVKRASTTFKGLPGDCRPGDRLLIDDGNVAVRVVAVTDTDVVTKVEVPGYVSNNKGINLPGVAVSVPALSEKDREDLRWALKIGADLIALSFVRDADDIKDVHEIMDEVGVRIPVIAKIEKPQAVENLFDIVSTFDGIMVARGDLGVEMPLEAVPLVQKRAIELARRQAKPVIVATQVLESMIQNPRPTRAEASDCANAILDGADAVMLSGETSVGAYPIEAVRTMASIIENVEEHGGERIPGLGSYPQTRGGALTRAAAEMGEHLDVTYLVTFTQSGDTARRLSRLRSPLPLLAFTPLHETRNQLAVSWGVQCYEVPEVQHTDEMVAQVDEILQDKHLAQPGDTVVIVAGMPPGTPGSTNSIRVHTVGETGDYKV$","Pyruvate kinase","Cytoplasm","pyruvate kinase","pyruvate kinase ","Pyruvate kinase","","Muirhead H. Isoenzymes of pyruvate kinase. Biochem. Soc. Trans. 1990. 18(2):193-196. PMID: 2379684Munoz M.E., Ponce E. Pyruvate kinase: current status of regulatory and functional properties. Comp Biochem Physiol B Biochem Mol Biol 2003. 135(2):197-218. PMID: 12798932Valentini G., Chiarelli L.R., Fortin R., Dolzan M., Galizzi A., Abraham D.J., Wang C., Bianchi P., Zanella A., Mattevi A. Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J. Biol. Chem. 2002. 277(26):23807-23814. PMID: 11960989","","","

InterPro
IPR001697
Family

Pyruvate kinase
PTHR11817	$\"[3-468]T$	PYRUVATE KINASE
TIGR01064	$\"[2-468]T$	pyruv_kin: pyruvate kinase

InterPro
IPR015793
Domain

Pyruvate kinase, barrel
PD001009	$\"[2-160]T$ $\"[164-334]T$	Q82A42_STRAW_Q82A42;
PR01050	$\"[59-75]T$ $\"[185-199]T$ $\"[215-241]T$ $\"[242-266]T$ $\"[267-291]T$ $\"[292-310]T$ $\"[311-327]T$	PYRUVTKNASE
PF00224	$\"[1-329]T$	PK
PS00110	$\"[213-225]T$	PYRUVATE_KINASE

InterPro
IPR015794
Domain

Pyruvate kinase, alpha/beta
G3DSA:3.40.1380.20	$\"[333-468]T$	no description
PF02887	$\"[354-467]T$	PK_C

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.60	$\"[1-333]T$	no description

","BeTs to 21 clades of COG0469COG name: Pyruvate kinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0469 is -ompkzy-vdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB001697 (Pyruvate kinase) with a combined E-value of 5.2e-154. IPB001697A 7-51 IPB001697B 61-75 IPB001697C 107-129 IPB001697D 151-199 IPB001697E 224-268 IPB001697F 274-323 IPB001697G 370-397","Residues 1-45 are 84% similar to a (KINASE PYRUVATE TRANSFERASE GLYCOLYSIS MAGNESIUM PK II KINASE I FAMILY) protein domain (PD005456) which is seen in Q82A42_STRAW.Residues 2-95 are 58% similar to a (PYRUVATE KINASE CHLOROPLAST G PEPTIDE ISOZYME TRANSFERASE GLYCOLYSIS TRANSIT PRECURSOR) protein domain (PD135156) which is seen in KPYG_TOBAC.Residues 2-73 are 66% similar to a (PYRUVATE KINASE TRANSFERASE GLYCOLYSIS MAGNESIUM) protein domain (PD611321) which is seen in Q8S7N6_EEEEE.Residues 3-77 are 68% similar to a (GLP_178_2333_672 KINASE TRANSFERASE GLYCOLYSIS MAGNESIUM) protein domain (PDA181T6) which is seen in Q7QVW2_EEEEE.Residues 3-96 are 58% similar to a (PYRUVATE KINASE CYTOSOLIC TRANSFERASE GLYCOLYSIS MAGNESIUM) protein domain (PD983049) which is seen in Q9M511_LILLO.Residues 5-74 are 75% similar to a (PYRUVATE KINASE TRANSFERASE GLYCOLYSIS MAGNESIUM) protein domain (PD624795) which is seen in Q8SQP0_EEEEE.Residues 9-77 are 65% similar to a (KINASE PYRUVATE TRANSFERASE GLYCOLYSIS MAGNESIUM II TYPE AGR_L_2146P LONG 458AA) protein domain (PD607716) which is seen in Q9PF54_XYLFA.Residues 66-160 are 51% similar to a (PYRUVATE KINASE TRANSFERASE GLYCOLYSIS MAGNESIUM) protein domain (PD772251) which is seen in Q8L200_BARHE.Residues 80-163 are 67% similar to a (KINASE PYRUVATE TRANSFERASE GLYCOLYSIS MAGNESIUM PK II I KINASE FAMILY) protein domain (PD326214) which is seen in Q8G5M1_BIFLO.Residues 164-334 are similar to a (KINASE PYRUVATE TRANSFERASE GLYCOLYSIS MAGNESIUM PK II KINASE I ISOZYME) protein domain (PD001009) which is seen in Q82A42_STRAW.Residues 348-468 are 73% similar to a (KINASE PYRUVATE TRANSFERASE GLYCOLYSIS MAGNESIUM PK II KINASE ISOZYME I) protein domain (PD498268) which is seen in Q6AF62_BBBBB.","","-54% similar to PDB:1E0U STRUCTURE R271L MUTANT OF E. COLI PYRUVATE KINASE (E_value = 1.5E_82);-54% similar to PDB:1PKY PYRUVATE KINASE FROM E. COLI IN THE T-STATE (E_value = 1.5E_82);-54% similar to PDB:1E0T R292D MUTANT OF E. COLI PYRUVATE KINASE (E_value = 9.9E_82);-50% similar to PDB:1F3W RECOMBINANT RABBIT MUSCLE PYRUVATE KINASE (E_value = 1.2E_66);-50% similar to PDB:1A49 BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE (E_value = 1.5E_66);","Residues 1 to 347 (E_value = 3.7e-147) place ANA_0683 in the PK family which is described as Pyruvate kinase, barrel domain.Residues 354 to 467 (E_value = 7.8e-17) place ANA_0683 in the PK_C family which is described as Pyruvate kinase, alpha/beta domain.","","kinase (pyk)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0684","721246","720761","486","7.02","0.03","17583","GTGTTGTGGGTTCGAGTCCCACCGGAGGTACCAACAAGTCCCTACCCAGCCCCACCTCAGGACAGACCGGGCCAGATGGAGAACACCTTGAGCACGACGTGGGTCTCGCTGTACGAAGCGGCCAAGGCGGTTCAGCGTCCTCGCCACGTGTCTTCATACATCGAGGCGGGCGGAGTCGCAGCTGCGGTGGAGTCGGCCTCGGGAAGAATCTATACGGGCGTCTGCGTGGATACGGCCTGCACACTGGGAATCTGTGCCGAGCGCAACGCGATCCTCAACATGGTCACCAACGGCGAGGATGCAATCCGGCGTGTTCTGACGATCATGCGCGACGGCCGTACCGGTCCACCTTGCGGAGCATGTCGAGAAATGATGACGCAGCTGATGCCGAGCCGGTTCGGCGCTGTCGAGGTAATGATCGACTACGAAGCTGGGAAGACGACGACTCTTGCCGATCTGACTCCACAGTGGTGGCTACGGCGATGA","VLWVRVPPEVPTSPYPAPPQDRPGQMENTLSTTWVSLYEAAKAVQRPRHVSSYIEAGGVAAAVESASGRIYTGVCVDTACTLGICAERNAILNMVTNGEDAIRRVLTIMRDGRTGPPCGACREMMTQLMPSRFGAVEVMIDYEAGKTTTLADLTPQWWLRR$","Cytidine deaminase","Periplasm, Membrane, Cytoplasm","cytidine deaminase","cytidine/deoxycytidylate deaminase family protein; putative","CMP/dCMP deaminase, zinc-binding","","Yang C., Carlow D., Wolfenden R., Short S.A. Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene. Biochemistry 1992. 31(17):4168-4174. PMID: 1567863Moore J.T., Silversmith R.E., Maley G.F., Maley F. T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit. J. Biol. Chem. 1993. 268(4):2288-2291. PMID: 8428902Reizer J., Buskirk S., Bairoch A., Reizer A., Saier Jr M.H. A novel zinc-binding motif found in two ubiquitous deaminase families. Protein Sci. 1994. 3(5):853-856. PMID: 8061614Bhattacharya S., Navaratnam N., Morrison J.R., Scott J., Taylor W.R. Cytosine nucleoside/nucleotide deaminases and apolipoprotein B mRNA editing. Trends Biochem. Sci. 1994. 19(3):105-106. PMID: 8203015","","","

InterPro
IPR002125
Domain

CMP/dCMP deaminase, zinc-binding
PF00383	$\"[31-137]T$	dCMP_cyt_deam_1
PS00903	$\"[85-125]?$	CYT_DCMP_DEAMINASES

InterPro
IPR006262
Family

Cytidine deaminase, homotetrameric
PIRSF001250	$\"[30-160]T$	Cytidine deaminase

noIPR
unintegrated

unintegrated
G3DSA:3.40.140.10	$\"[35-158]T$	no description
PTHR11644	$\"[59-125]T$	CYTIDINE DEAMINASE

","BeTs to 10 clades of COG0295COG name: Cytidine deaminaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0295 is -o---zy-vdrlb-e-gh---j--twNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 34-158 are 56% similar to a (DEAMINASE CYTIDINE CYTIDINE/DEOXYCYTIDYLATE FAMILY SPR1880) protein domain (PD711940) which is seen in Q97NG2_STRPN.","","No significant hits to the PDB database (E-value < E-10).","Residues 31 to 137 (E_value = 0.00013) place ANA_0684 in the dCMP_cyt_deam_1 family which is described as Cytidine and deoxycytidylate deaminase zinc-binding region.","","deaminase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0686","721345","721953","609","4.80","-13.34","22433","GTGAGCAATGAGTCCAGCACCACCAAGTCCCGCCGGGTGCTCGTCGCTGAGGACGAGACCCTCATCCGCCTTGACATCGTCGAGACTCTCACCGACGCCGGCTACGAGATCGTCGCGGAGGCCGTAGATGGTGAGGAGGCCGTCCGCCTGGCTGATGAGCATGACCCTGACCTGTGCGTTCTTGACGTCAAGATGCCGGTGACTGACGGCATCACCGCGGCGGAGAGGATTCTCGAGAAGCATAACTGCGCCGTCGTCATGCTGACCGCCTTCTCCCAGACCGAGCTCGTCGAACGAGCCAGCGCCGCCGGCGCCATGGCCTACGTCGTCAAGCCCTTCACCCCGGCGGATCTCATCCCGGCACTTGAGATCGCCATGTCACGGCATGAGGAGATTCTCTCCCTGGAGAGTGAGATTTCTGACCTCACCGAGCGCTTCGAGACCCGCAAGCGCGTCGACCGGGCCAAGGGGCTGCTCATGGAGCGCATGGGGCTGAGCGAGCCGGAGGCCTTCCGCTGGCTGCAGAAGACCTCCATGAACCGGCGTCTGACCATGCGCGAGGTGGCCGATGCCGTCATCGAGCAGGTCGGTTCGGCCAAGAAGGACTAA","VSNESSTTKSRRVLVAEDETLIRLDIVETLTDAGYEIVAEAVDGEEAVRLADEHDPDLCVLDVKMPVTDGITAAERILEKHNCAVVMLTAFSQTELVERASAAGAMAYVVKPFTPADLIPALEIAMSRHEEILSLESEISDLTERFETRKRVDRAKGLLMERMGLSEPEAFRWLQKTSMNRRLTMREVADAVIEQVGSAKKD$","Response regulator antiterminator","Cytoplasm","response regulator","K07183 response regulator NasT","response regulator receiver","","Wilson S.A., Wachira S.J., Drew R.E., Jones D., Pearl L.H. Antitermination of amidase expression in Pseudomonas aeruginosa is controlled by a novel cytoplasmic amide-binding protein. EMBO J. 1993. 12(9):3637-3642. PMID: 8253087Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457Grebe T.W., Stock J.B. The histidine protein kinase superfamily. Adv. Microb. Physiol. 1999. 41:139-227. PMID: 10500846West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Kern D., Volkman B.F., Luginbuhl P., Nohaile M.J., Kustu S., Wemmer D.E. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 1999. 402(6764):894-898. PMID: 10622255O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E., Pearl L.H. Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex. EMBO J. 1999. 18(19):5175-5186. PMID: 10508151Norman R.A., Poh C.L., Pearl L.H., O'Hara B.P., Drew R.E. Steric hindrance regulation of the Pseudomonas aeruginosa amidase operon. J. Biol. Chem. 2000. 275(39):30660-30667. PMID: 10893220Shu C.J., Zhulin I.B. ANTAR: an RNA-binding domain in transcription antitermination regulatory proteins. Trends Biochem. Sci. 2002. 27(1):3-5. PMID: 11796212Wilson S.A., Wachira S.J., Norman R.A., Pearl L.H., Drew R.E. Transcription antitermination regulation of the Pseudomonas aeruginosa amidase operon. EMBO J. 1996. 15(21):5907-5916. PMID: 8918468","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[12-123]T$	Q6A9N8_PROAC_Q6A9N8;
PF00072	$\"[11-123]T$	Response_reg
SM00448	$\"[11-122]T$	REC
PS50110	$\"[12-126]T$	RESPONSE_REGULATORY

InterPro
IPR005561
Domain

ANTAR
PF03861	$\"[138-193]T$	ANTAR
PS50921	$\"[132-193]T$	ANTAR

InterPro
IPR008327
Family

Response regulator antiterminator
PIRSF036382	$\"[9-200]T$	Response regulator antiterminator

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[140-202]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[12-139]T$	no description
PTHR23283	$\"[1-130]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF31	$\"[1-130]T$	SENSOR HISTIDINE KINASE

","BeTs to 3 clades of COG3707COG name: Response regulator with putative antiterminator output domainFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG3707 is ----------r----f-----j----Number of proteins in this genome belonging to this COG is 1","***** IPB000673 (CheB methylesterase) with a combined E-value of 5.2e-19. IPB000673B 29-82 IPB000673C 82-112***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 2.5e-11. IPB001867A 57-70 IPB001867B 84-128***** IPB001789 (Response regulator receiver) with a combined E-value of 5.9e-08. IPB001789A 57-70 IPB001789B 104-114","Residues 12-123 are similar to a (SENSORY TRANSDUCTION PHOSPHORYLATION REGULATOR DNA-BINDING TRANSCRIPTION REGULATION RESPONSE TWO-COMPONENT KINASE) protein domain (PD000039) which is seen in Q6A9N8_PROAC.Residues 141-192 are 88% similar to a (TRANSDUCTION PHOSPHORYLATION SENSORY REGULATOR RESPONSE TWO-COMPONENT NAST SYSTEM TRANSCRIPTION REGULATORY) protein domain (PD027901) which is seen in Q6AF58_BBBBB.","","-72% similar to PDB:1S8N Crystal structure of Rv1626 from Mycobacterium tuberculosis (E_value = 6.4E_56);-72% similar to PDB:1SD5 Crystal structure of Rv1626 (E_value = 6.4E_56);-60% similar to PDB:1TMY CHEY FROM THERMOTOGA MARITIMA (APO-I) (E_value = 7.7E_17);-60% similar to PDB:1U0S Chemotaxis kinase CheA P2 domain in complex with response regulator CheY from the thermophile thermotoga maritima (E_value = 7.7E_17);-60% similar to PDB:2TMY CHEY FROM THERMOTOGA MARITIMA (APO-II) (E_value = 7.7E_17);","Residues 11 to 123 (E_value = 7.3e-32) place ANA_0686 in the Response_reg family which is described as Response regulator receiver domain.Residues 138 to 193 (E_value = 9.1e-26) place ANA_0686 in the ANTAR family which is described as ANTAR domain.","","regulator (cheY)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0687","722373","721987","387","6.38","-1.85","13505","CTGCACGCGGTGCTGGAGGACAGTGAGGAGGGCACGCTCATGGAGACCCTCGGGATGGAGGTGGTGACTCGCGACGCTCATCGGACCGAGGTCCGGATGCCGGTCGATGGAGCCCGACAGGTCGTCGGAATCCTGCACGGCGGTGCCACCGCCGCCATCATCGAGACGGCCGCTTCCGTGGCCGCGCGCGCGGCGGCGCCCGACGGTGCCGTCCCGGTGGGTGCGGAACTGACGGTCAGCCACTTGCGCTCCGTGTCCCGGGGCTGGGTGAAGGCCACCGCCGTTCCTCTCCACCGAGGCCGTCGTACCGTGGTCTACCAGGTGACGGTCACGGATGACGATGAGCGGACCATCGCCGTCGGGACACTGCGCAGCCTGTTCACCTGA","LHAVLEDSEEGTLMETLGMEVVTRDAHRTEVRMPVDGARQVVGILHGGATAAIIETAASVAARAAAPDGAVPVGAELTVSHLRSVSRGWVKATAVPLHRGRRTVVYQVTVTDDDERTIAVGTLRSLFT$","Phenylacetic acid degradation-related protein","Cytoplasm","function unknown","hypothetical protein predicted by Glimmer/Critica","thioesterase superfamily protein","","Weinrauch Y., Guillen N., Dubnau D.A. Sequence and transcription mapping of Bacillus subtilis competence genes comB and comA, one of which is related to a family of bacterial regulatory determinants. J. Bacteriol. 1989. 171(10):5362-5375. PMID: 2507523","","","

InterPro
IPR003736
Domain

Phenylacetic acid degradation-related protein
TIGR00369	$\"[12-127]T$	unchar_dom_1: uncharacterized domain

InterPro
IPR006683
Domain

Thioesterase superfamily
PF03061	$\"[42-119]T$	4HBT

noIPR
unintegrated

unintegrated
G3DSA:3.10.129.10	$\"[10-127]T$	no description

","BeTs to 6 clades of COG2050COG name: Uncharacterized protein PaaI, possibly involved in aromatic compounds catabolismFunctional Class: RThe phylogenetic pattern of COG2050 is A--k-q--Ebrhuj-------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 145 to 222 (E_value = 4e-19) place ANA_0687 in the 4HBT family which is described as Thioesterase superfamily.","","unknown ","","1","","","Wed Aug 1 17:47:07 2007","","Wed Aug 1 17:47:07 2007","","","Wed Aug 1 17:47:07 2007","Wed Aug 1 17:47:07 2007","Wed Aug 1 17:47:07 2007","","","Wed Aug 1 17:47:07 2007","","","Wed Aug 1 17:47:07 2007","","","","Wed Aug 1 17:47:07 2007","Wed Aug 1 17:47:07 2007","","","","","yes","","" "ANA_0688","722643","725480","2838","5.05","-43.90","102305","GTGAGCACCACCGCGACCAGCCCTGCGACGAGTCCAACACCTCAGTCCCCCTCGGACCCGGTTCCCGAGCGGCTTCTTCTCATCGACGGACACTCGATGGCCTTTCGCGCCTTTTACGCGCTGCCCGTCGACAACTTCACGACGTCGACCGGCCAGTCCACCAATGCCGTCCACGGCTTCGTGTCCATGTTCCTGTCGCTGCTGGACAACGAGCGACCCACCCACGTGGCGGTCGCCTTCGACCTGCCCGGAGGCACCTTCCGCACCGAGGAGTACGCCGAGTACAAGGGAACCCGCGATGAGACACCGCAGCCCTTCCTCGGGCAGGTCGAGCTCATCCGGCAGGTCCTGGAGGCCATGGGCGTCACCGCGCTCACCGCGCCGGGCTACGAGGCCGACGACATTCTGGCGACCTTGGCGACCTCGGCACAGGCCGAGGGCATGGAGGTCCTCATCTGCTCCGGAGACCGTGACTCCTTCCAGACGGTCACCGAGCGGTGCACCGTGCTCTACCCGGTCAAGGGCGTGTCAACACTGCGCCGCATGACGCCTCAGGAGGTGGAGGAGCGCTACGGGGTGACGCCCGAACGCTACCCGCACCTCGCCGCCCTGGTCGGCGAGACCAGCGACAACCTCCCCGGAGTGCCGGGGGTGGGCCCCAAGACCGCCGCCAAGTGGCTCAACCTCTACGACGGGCTCGACGGCGTCATCGCTCACGCGGACCAGATCAAGGGTAAGGCCGGACAGTCGCTGCGCGACCATCTCGACGACGTCGTGCGCAACCGCCGCCTCAACCACCTGCTCACCGACCTGGATCTCGGAGTCCTCCCGCGCACCGACCTGCGCCTCGCCGGTGCCGACCGATCCGCCCTGGCGCGCGTGTTCGAGGCCCTGGAGTTCCGCACCCTGCACCAACGGGCGCTACGCATTCTGAGCTTCACCGACACCTCCGATCACGTCGAGCCGGGCGAGGCGGAGGAAGCCGGCGCCTTGAACGCACTGAGCGATCTGGAGATCGTCTCGCTGGGACACGATCTTGCCGCGGGGCAGCTGGCTGAATGGTTGGAGACAAGTCTGCCGGCGGATGGTGATAACGGCACCCGCCCCCTGGGGGTCGATGTTGTCGGCGTCCTCAGACCCGTCGAGGGCGATGCCGCACTCGTGTCGCTGTCCGACGGCTCTCGGGCGGTGGTCGTCGACCTCACCGAGATCCTGCCTGAGGATGAAGCCGCCCTGGCCCGGCTCCTGGCCGACGTGGAGCGCCCCAAGCTCGTCGCCGACGCCAAGGGCAGCTGGCACGCGCTGAGCGCCCGGGGGCTCACGCTCGACGGCGTCGTCGCAGATCCCTCCCTGGCCGGCTACCTGTGTCGCCCGGAACAGCGCAGCTACGACGTCGACACCCTCACCCAGCGCTGGCTCGGCATCGATCTGGCCGCCGTCAACGAGGGGCGAGCCCCGGCTGGCGACAGTTCCCGTGAGTCCCAGAGCGCCTTCGACCTCGAGGCCCTCACCTCCGAGGCCGTTCCCGCATCCCACCTGGCCAGTGCGGGTCGGGCCGCCGCCCTGCTCCCGCTCCAGGTCGTGCTCGATGAGCAGATGGTGGCTCGTGATGCCTTGGGGCTCTTCACCGACCTGGAGATGCCCGTGGCAGCGACCTTGACCGTCATGGAGGACGCCGGCATCGCCGTCGATGACGCCGTGCTCCAAACCCGCCAGACCGAGCTCGACGCCCGCGTGACCCACGCCGCTGAGGGTGCCTACGCCGCCGCCGGGCGAGAGCTCAACCTCTCCAGTCCCAAGCAGCTCCAGGCCGTCCTATTCGACGAGCTGAAGATGCCCAAGACCCGTAAGACCAAGACCGGCTACACCACGGATGCCGACGCCTTGGCCGGGCTGTATGCCAAGACCTCCCACCCCTTCCTGGAGCACCTTCTCGAGCACCGCGACGCCATCAAGCTGCGGCAGACGGTGGAGGGGCTGCGCAAGGCGATCCAGCCCGATGGCCGCATCCACACCACCTTCCAGCAGACCATCGCCGCCACAGGGCGCCTGTCCTCCACGGACCCCAACCTGCAGAACATTCCGGCCCGGCACGAGGAGGGGATGCGCATCCGCGAGGCCTTCACCGTCGGAGAGGGCTACGAGTGCCTCATGACCGCCGACTACTCCCAGATCGAGATGCGCATCATGGCACATCTGTCCGCAGACCAGGCGCTGATCGATGCCTTCCGCAGCGGGGAGGACCTGCACCGCTACGTAGCCGCCCTGGTCCACGGCATCGACGTTGAGGACGTCACCGCCCAGCAGCGCAGCCACGTCAAGGCCATGAGCTATGGACTGGCCTACGGGCTGTCGACCTTCGGGCTGGCCCGTCAGCTCGGTATCGACAACGCCGACGCAGCAGATCTGAGGAACGCCTACTTCGCCAGGTTCGGGAAGGTTCACGACTACCTGGAGTCCGTGGTGGAGCAGGCGCGCCGCGACGGATACACCGAGACGATGTTCGGGCGGCGCCGTTACCTTCCCGACCTGACCAGCGACAACCGGCAGCGCCGTGAGATGGCTGAGCGGGCCGCCCTCAACGCTCCCATCCAGGGCAGCGCCGCCGATATCGTCAAGAAAGCCATGATCGACGTCGACAGCGCCCTGACCGAGCGGGCACTAGCAAGCCGCATTCTTCTGCAGATTCACGACGAGCTTCTCATCGAGGTCGCGCCCGGAGAGGCCGAGGCGGTCGAGAACCTCCTCAAGGAGCAGATGGGCGGGGCGGCAGAGCTCTCGGTCCCCCTGGACGTCGCCGTCGGACGAGGGCGCACCTGGCGTGAGGCCGCCCACTAG","VSTTATSPATSPTPQSPSDPVPERLLLIDGHSMAFRAFYALPVDNFTTSTGQSTNAVHGFVSMFLSLLDNERPTHVAVAFDLPGGTFRTEEYAEYKGTRDETPQPFLGQVELIRQVLEAMGVTALTAPGYEADDILATLATSAQAEGMEVLICSGDRDSFQTVTERCTVLYPVKGVSTLRRMTPQEVEERYGVTPERYPHLAALVGETSDNLPGVPGVGPKTAAKWLNLYDGLDGVIAHADQIKGKAGQSLRDHLDDVVRNRRLNHLLTDLDLGVLPRTDLRLAGADRSALARVFEALEFRTLHQRALRILSFTDTSDHVEPGEAEEAGALNALSDLEIVSLGHDLAAGQLAEWLETSLPADGDNGTRPLGVDVVGVLRPVEGDAALVSLSDGSRAVVVDLTEILPEDEAALARLLADVERPKLVADAKGSWHALSARGLTLDGVVADPSLAGYLCRPEQRSYDVDTLTQRWLGIDLAAVNEGRAPAGDSSRESQSAFDLEALTSEAVPASHLASAGRAAALLPLQVVLDEQMVARDALGLFTDLEMPVAATLTVMEDAGIAVDDAVLQTRQTELDARVTHAAEGAYAAAGRELNLSSPKQLQAVLFDELKMPKTRKTKTGYTTDADALAGLYAKTSHPFLEHLLEHRDAIKLRQTVEGLRKAIQPDGRIHTTFQQTIAATGRLSSTDPNLQNIPARHEEGMRIREAFTVGEGYECLMTADYSQIEMRIMAHLSADQALIDAFRSGEDLHRYVAALVHGIDVEDVTAQQRSHVKAMSYGLAYGLSTFGLARQLGIDNADAADLRNAYFARFGKVHDYLESVVEQARRDGYTETMFGRRRYLPDLTSDNRQRREMAERAALNAPIQGSAADIVKKAMIDVDSALTERALASRILLQIHDELLIEVAPGEAEAVENLLKEQMGGAAELSVPLDVAVGRGRTWREAAH$","DNA polymerase I","Cytoplasm, Extracellular","DNA polymerase I (POL I)","DNA polymerase I ","DNA polymerase I","","Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Aravind L., Walker D.R., Koonin E.V. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res. 1999. 27(5):1223-1242. PMID: 9973609Provvedi R., Dubnau D. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol. Microbiol. 1999. 31(1):271-280. PMID: 9987128Doherty A.J., Serpell L.C., Ponting C.P. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 1996. 24(13):2488-2497. PMID: 8692686","","","

InterPro
IPR001098
Family

DNA-directed DNA polymerase
PF00476	$\"[563-943]T$	DNA_pol_A
SM00482	$\"[701-908]T$	POLAc
PS00447	$\"[770-789]?$	DNA_POLYMERASE_A

InterPro
IPR002298
Family

DNA polymerase A
PR00868	$\"[670-692]T$ $\"[693-708]T$ $\"[716-739]T$ $\"[746-759]T$ $\"[770-795]T$ $\"[807-818]T$ $\"[829-840]T$ $\"[861-877]T$ $\"[891-904]T$	DNAPOLI
TIGR00593	$\"[25-944]T$	pola: DNA polymerase I

InterPro
IPR002421
Domain

5'-3' exonuclease
PF01367	$\"[193-293]T$	5_3_exonuc
PF02739	$\"[23-191]T$	5_3_exonuc_N
SM00475	$\"[23-284]T$	53EXOc

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[210-229]T$	HhH1

InterPro
IPR008918
Domain

Helix-hairpin-helix motif, class 2
SM00279	$\"[195-230]T$	HhH2

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.20	$\"[725-868]T$	no description
G3DSA:1.20.1060.10	$\"[559-673]T$	no description
G3DSA:3.30.420.10	$\"[382-557]T$	no description
G3DSA:3.40.50.1010	$\"[12-227]T$	no description
PTHR10133	$\"[27-304]T$ $\"[338-466]T$ $\"[501-944]T$	DNA POLYMERASE I

","BeTs to 16 clades of COG0749COG name: DNA polymerase I - 3'-5' exonuclease and polymerase domainsFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0749 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB002421 (5'-3' exonuclease) with a combined E-value of 2e-197. IPB002421A 25-40 IPB002421B 76-113 IPB002421C 120-162 IPB002421D 189-241 IPB002421F 548-561 IPB002421G 590-609 IPB002421H 647-657 IPB002421I 669-709 IPB002421J 721-750 IPB002421K 770-783 IPB002421L 829-838 IPB002421M 856-877 IPB002421N 890-905 IPB002421O 926-940***** IPB002298 (DNA-polymerase family A (pol I) signature) with a combined E-value of 1.1e-87. IPB002298A 670-692 IPB002298B 693-708 IPB002298C 716-739 IPB002298D 746-759 IPB002298E 770-795 IPB002298F 807-818 IPB002298G 829-840 IPB002298H 861-877 IPB002298I 891-904***** IPB001098 (DNA-directed DNA polymerase) with a combined E-value of 2e-43. IPB001098B 724-755 IPB001098C 770-783 IPB001098D 859-877 IPB001098E 888-908***** IPB002562 (3'-5' exonuclease) with a combined E-value of 1e-22. IPB002562A 72-81 IPB002562B 748-759 IPB002562C 770-782 IPB002562D 857-870 IPB002562E 891-901***** IPB008918 (Helix-hairpin-helix motif, class 2) with a combined E-value of 2.2e-16. IPB008918A 74-88 IPB008918C 209-232","Residues 25-59 are 97% similar to a (DNA POLYMERASE I TRANSFERASE EXONUCLEASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED DNA-BINDING HYDROLASE REPAIR) protein domain (PD684184) which is seen in Q6A9N6_PROAC.Residues 63-106 are 75% similar to a (DNA POLYMERASE I EXONUCLEASE TRANSFERASE NUCLEOTIDYLTRANSFERASE HYDROLASE DNA-DIRECTED DNA-BINDING 5_apos;-3_apos;) protein domain (PD002066) which is seen in Q6AF56_BBBBB.Residues 115-198 are 59% similar to a (EXONUCLEASE HYDROLASE NUCLEASE 5_apos;-3_apos; 3.1.11.- DNA-BINDING PROBABLE) protein domain (PDA184A2) which is seen in EX53_BUCAI.Residues 152-197 are 78% similar to a (DNA POLYMERASE I TRANSFERASE EXONUCLEASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED DNA-BINDING HYDROLASE REPAIR) protein domain (PD937735) which is seen in Q8NQS1_CORGL.Residues 201-243 are 79% similar to a (EXONUCLEASE POLYMERASE DNA 5_apos;-3_apos; IX I HYDROLASE 3.1.11.- EXODEOXYRIBONUCLEASE TRANSFERASE) protein domain (PD717826) which is seen in Q8G5M4_BIFLO.Residues 204-302 are 67% similar to a (DNA POLYMERASE I TRANSFERASE EXONUCLEASE ENDONUCLEASE HYDROLASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED DNA-BINDING) protein domain (PD522726) which is seen in Q83AT5_COXBU.Residues 244-273 are 90% similar to a (DNA POLYMERASE I TRANSFERASE EXONUCLEASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED HYDROLASE REPAIR POL) protein domain (PD410673) which is seen in Q6A9N6_PROAC.Residues 385-473 are 64% similar to a (DNA POLYMERASE I TRANSFERASE DNA-DIRECTED NUCLEOTIDYLTRANSFERASE EXONUCLEASE POL DNA-BINDING HYDROLASE) protein domain (PD463009) which is seen in Q9F192_BBBBB.Residues 541-639 are 74% similar to a (DNA POLYMERASE I TRANSFERASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED EXONUCLEASE DNA-BINDING HYDROLASE REPAIR) protein domain (PD520406) which is seen in Q740M8_MYCPA.Residues 644-708 are 60% similar to a (TRANSFERASE I DNA POLYMERASE NUCLEOTIDYLTRANSFERASE) protein domain (PDA0A7E9) which is seen in Q6MST6_MYCMS.Residues 645-877 are similar to a (DNA POLYMERASE I TRANSFERASE DNA-DIRECTED NUCLEOTIDYLTRANSFERASE EXONUCLEASE DNA-BINDING REPLICATION HYDROLASE) protein domain (PD001497) which is seen in Q6A9N6_PROAC.Residues 728-818 are 75% similar to a (DNA POLYMERASE I TRANSFERASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED EXONUCLEASE POL DNA-BINDING HYDROLASE) protein domain (PD868954) which is seen in Q6AF56_BBBBB.Residues 821-942 are 50% similar to a (ORF86/ORF88/ORF90) protein domain (PDA0A7G6) which is seen in Q6Y7N1_VVVVV.Residues 830-883 are 75% similar to a (DNA POLYMERASE I TRANSFERASE NUCLEOTIDYLTRANSFERASE EXONUCLEASE DNA-DIRECTED POL DNA-BINDING HYDROLASE) protein domain (PD843020) which is seen in Q9F176_RHOER.Residues 888-940 are 84% similar to a (DNA POLYMERASE I TRANSFERASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED EXONUCLEASE DNA-BINDING HYDROLASE REPAIR) protein domain (PD335608) which is seen in DPO1_MYCTU.","","-57% similar to PDB:1D8Y CRYSTAL STRUCTURE OF THE COMPLEX OF DNA POLYMERASE I KLENOW FRAGMENT WITH DNA (E_value = 3.2E_93);-57% similar to PDB:1D9D CRYSTALL STRUCTURE OF THE COMPLEX OF DNA POLYMERASE I KLENOW FRAGMENT WITH SHORT DNA FRAGMENT CARRYING 2'-0-AMINOPROPYL-RNA MODIFICATIONS 5'-D(TCG)-AP(AUC)-3' (E_value = 3.2E_93);-57% similar to PDB:1D9F CRYSTAL STRUCTURE OF THE COMPLEX OF DNA POLYMERASE I KLENOW FRAGMENT WITH DNA TETRAMER CARRYING 2'-O-(3-AMINOPROPYL)-RNA MODIFICATION 5'-D(TT)-AP(U)-D(T)-3' (E_value = 3.2E_93);-57% similar to PDB:1DPI STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE I COMPLEXED WITH D/TMP (E_value = 3.2E_93);-57% similar to PDB:1KFD CRYSTAL STRUCTURES OF THE KLENOW FRAGMENT OF DNA POLYMERASE I COMPLEXED WITH DEOXYNUCLEOSIDE TRIPHOSPHATE AND PYROPHOSPHATE (E_value = 3.2E_93);","Residues 23 to 191 (E_value = 4.9e-79) place ANA_0688 in the 5_3_exonuc_N family which is described as 5'-3' exonuclease, N-terminal resolvase-like domain.Residues 193 to 293 (E_value = 2e-27) place ANA_0688 in the 5_3_exonuc family which is described as 5'-3' exonuclease, C-terminal SAM fold.Residues 563 to 943 (E_value = 1.3e-171) place ANA_0688 in the DNA_pol_A family which is described as DNA polymerase family A.","","polymerase I (POL I)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0689","725792","727246","1455","4.68","-37.74","53227","ATGACAACCACCACGCCCAGCCCCGCCCCGGTCGCCGTCAACGACATCGGTTCGACCGAGGAGATCCTCGCCGCCGTTGACGAGACCATCAAGTACTTCGATGACGGCGACATCGTCGAGGGCACTGTCGTCAAGGTCGACCGTGATGAGGTCCTCCTCGACATCGGCTACAAGACCGAAGGCGTCATCCTCGCTCGTGAGCTGTCCATCAAGCACGACGTCGACCCCGATGAGATCGTCTCCGTCGGCGATGAGATCGAAGCCCTCGTCCTGCAGAAGGAGGACAAGGAAGGGCGTCTGCTCCTGAGCAAGAAGCGCGCGCAGTACGAGCGCGCCTGGGGCACCATCGAGCGCATCAAGGAGGAGGACGGCGTCGTCACCGGCTCCGTCATCGAGGTCGTCAAGGGTGGTCTCATCCTGGACATCGGCCTGCGTGGCTTCCTGCCTGCCTCCCTGGTGGAGATGCGTCGCGTTCGCGACCTCCAGCCCTACGTGGGCCGCGAGCTCGAGGCGAAGATCATTGAGCTGGACAAGAACCGCAACAACGTGGTCCTCTCCCGCCGCGCCTGGCTCGAGCAGACCCAGTCCGAGGTCCGCACCAACTTCCTGCAGACCCTGCAGAAGGGGCAGGTCCGCTCCGGTGTCGTGTCCTCCATCGTCAACTTCGGTGCCTTCGTGGACCTGGGTGGCGTCGATGGTCTGGTCCACGTCTCCGAGCTGTCCTGGAAGCACATCGACCACCCCTCCGAGGTCGTCGAGGTCGGCAACGAGGTCACGGTCGAGGTCCTGGACGTCGACTTCGACCGCGAGCGCGTCTCCCTGTCGCTCAAGGCGACCCAGGAGGACCCGTGGCAGGCCTTCGCCCGCACCCACGCCATCGGCCAGGTCGTTCCCGGCAAGGTCACCAAGCTGGTCCCCTTCGGTGCATTCGTGCGTGTCGAGGACGGCATCGAGGGCCTGGTCCACATCTCCGAGCTGGCGCAGCGGCACGTCGAGGTCCCCGAGCAGGTGGCCAAGGTCGGCGACGAGGTCTTCGTCAAGGTCATCGACATCGACCTGGAGCGCCGTCGCATCTCCCTGTCGCTGAAGCAGGCCAACGAGGGTGTCGACCCCGCCTCCGAGGACTTCGACCCCAGCCTCTACGGGATGGCGGCCGAGTACGACGAGCAGGGCAACTACAAGTACCCCGAGGGCTTCGACCCGGAGACCAACGAGTGGCTCGAGGGCTACGACGCCCAGCGCGAGGCGTGGGAGGCCGAGTACGCAGCTGCTCACGCCCGCTGGGAGGCCCACAAGGCCCAGGTCGCCAAGGCCCTGGAGGAGGAGCAGGAGTCCGGTGCTCCGGCAGCCCCCTCCGGCGGCACCTCGTACTCCTCGGCGCCGTCTGAGGCCTCCGGCACGCTGGCCTCCGATGAGGCCCTGGCCGCTCTGCGCGAGAAGCTCACTGGTAACTGA","MTTTTPSPAPVAVNDIGSTEEILAAVDETIKYFDDGDIVEGTVVKVDRDEVLLDIGYKTEGVILARELSIKHDVDPDEIVSVGDEIEALVLQKEDKEGRLLLSKKRAQYERAWGTIERIKEEDGVVTGSVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYVGRELEAKIIELDKNRNNVVLSRRAWLEQTQSEVRTNFLQTLQKGQVRSGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVGNEVTVEVLDVDFDRERVSLSLKATQEDPWQAFARTHAIGQVVPGKVTKLVPFGAFVRVEDGIEGLVHISELAQRHVEVPEQVAKVGDEVFVKVIDIDLERRRISLSLKQANEGVDPASEDFDPSLYGMAAEYDEQGNYKYPEGFDPETNEWLEGYDAQREAWEAEYAAAHARWEAHKAQVAKALEEEQESGAPAAPSGGTSYSSAPSEASGTLASDEALAALREKLTGN$","30S ribosomal protein S1","Cytoplasm","ribosomal protein","30S ribosomal protein S1","RNA binding S1 domain protein","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Subramanian A.R. Structure and functions of ribosomal protein S1. Prog. Nucleic Acid Res. Mol. Biol. 1983. 28:101-142. PMID: 6348874Sorensen M.A., Fricke J., Pedersen S. Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo. J. Mol. Biol. 1998. 280(4):561-569. PMID: 9677288Danchin A. Comparison between the Escherichia coli and Bacillus subtilis genomes suggests that a major function of polynucleotide phosphorylase is to synthesize CDP. DNA Res. 1997. 4(1):9-18. PMID: 9179491","","","

InterPro
IPR000110
Family

Ribosomal protein S1
PR00681	$\"[36-54]T$ $\"[54-68]T$ $\"[102-121]T$ $\"[126-142]T$ $\"[143-160]T$ $\"[172-192]T$ $\"[229-250]T$ $\"[307-326]T$ $\"[346-364]T$	RIBOSOMALS1

InterPro
IPR003029
Domain

RNA binding S1
PF00575	$\"[32-105]T$ $\"[119-188]T$ $\"[205-277]T$ $\"[290-363]T$	S1
SM00316	$\"[34-105]T$ $\"[121-188]T$ $\"[207-277]T$ $\"[292-363]T$	S1
PS50126	$\"[36-105]T$ $\"[123-188]T$ $\"[209-277]T$ $\"[294-363]T$	S1

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[33-107]T$ $\"[108-190]T$ $\"[209-285]T$ $\"[289-365]T$	no description

noIPR
unintegrated

unintegrated
PTHR10724	$\"[203-329]T$	TEX PROTEIN-RELATEDTRANSCRIPTION ACCESSORY PROTEIN (S1 RNA BINDING DOMAIN)

","BeTs to 18 clades of COG0539COG name: Ribosomal protein S1Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0539 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000110 (Ribosomal protein S1 signature) with a combined E-value of 1.5e-106. IPB000110A 36-54 IPB000110B 54-68 IPB000110C 102-121 IPB000110D 126-142 IPB000110E 143-160 IPB000110F 172-192 IPB000110G 229-250 IPB000110H 307-326 IPB000110I 346-364 IPB000110F 347-367 IPB000110F 261-281***** IPB003029 (RNA binding S1) with a combined E-value of 2e-07. IPB003029A 299-310 IPB003029B 341-352 IPB003029A 214-225 IPB003029B 255-266 IPB003029B 36-47","Residues 293-366 are similar to a (RIBOSOMAL S1 30S NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE RNA-BINDING RIBONUCLEASE R NUCLEASE) protein domain (PD594032) which is seen in Q9S2K5_STRCO.Residues 36-106 are similar to a (RIBOSOMAL S1 30S REPEAT RNA-BINDING DNA-BINDING HOMOLOG CHLOROPLAST A S1) protein domain (PD599421) which is seen in Q83HP3_TROW8.Residues 109-198 are similar to a (RIBOSOMAL S1 30S REPEAT RNA-BINDING HOMOLOG DNA-BINDING S1 MITOCHONDRION A) protein domain (PD002626) which is seen in Q9S2K5_STRCO.Residues 293-366 are similar to a (RIBOSOMAL S1 30S NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE RNA-BINDING RIBONUCLEASE R NUCLEASE) protein domain (PD594032) which is seen in Q9S2K5_STRCO.Residues 293-366 are similar to a (RIBOSOMAL S1 30S NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE RNA-BINDING RIBONUCLEASE R NUCLEASE) protein domain (PD594032) which is seen in Q9S2K5_STRCO.Residues 293-366 are similar to a (RIBOSOMAL S1 30S NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE RNA-BINDING RIBONUCLEASE R NUCLEASE) protein domain (PD594032) which is seen in Q9S2K5_STRCO.Residues 373-411 are 92% similar to a (RIBOSOMAL S1 30S RPSA REPEAT RNA-BINDING PROBABLE) protein domain (PD032981) which is seen in Q8G5L7_BIFLO.","","-71% similar to PDB:1SRO S1 RNA BINDING DOMAIN, NMR, 20 STRUCTURES (E_value = 2.9E_12);-68% similar to PDB:2OCE Crystal structure of hypothetical protein PA5201 from Pseudomonas aeruginosa (E_value = 4.2E_11);","Residues 32 to 105 (E_value = 3.5e-19) place ANA_0689 in the S1 family which is described as S1 RNA binding domain.Residues 119 to 188 (E_value = 1.7e-15) place ANA_0689 in the S1 family which is described as S1 RNA binding domain.Residues 205 to 277 (E_value = 7.7e-31) place ANA_0689 in the S1 family which is described as S1 RNA binding domain.Residues 290 to 363 (E_value = 1.5e-29) place ANA_0689 in the S1 family which is described as S1 RNA binding domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0690","727448","729193","1746","5.72","-9.76","62513","ATGAGCTATTGGGGCGACATTGCCCGCGCTCTGGAGGATGTCGACCCCGTCTGCCCCAGTCGCGACGCTGCTGCGGCCCTGTGGAAGGCGGTCGCCACCGACGACGTCGAGGACACGGCTGCGGGGAACGCGCCCGACCAGGTGGTGGAGGCGGTCTGCGCCGTCGACCGGGCGTGGCTGGTTCAGCTGGGCCAGGACCCGGACACGAGCAGGAGGAGCCTTGAGCGGGCGATCGCCTTCTGTCAGGGACTTCGGGCCGCCCACGGCCGCTCAACGCTCCCACTGCGCTACGCCCAGGTGGAGCTCTCCGCCGTTCTTGGCCTCAGGGACGAGGCCCTGGAGCAGCTCCGTGAGGCCAGACTCTTCTCCTTCGGCAAGGCCGACACCGGAGCCGTGCTGGCCACTGCTCGCATGCACGATGACTACTCCGGCGTCATCAGCACAGCCACGGCCACACCGAGGCGTGCCGAGGCTGATCCCGTGGAGTCCGCGAGGGGGTTGGGGGCGGTGCTGGTTCCTTACCTGGCCCACCAACGCATCGTCGAGGCCGAGGACGCTTTCGCCTCCTTGAGCCTGCTCAATCTTCCAGATGCTGTGTCACTTCAGTGCCTGGCGGACAGGCTCGAGTACCTGGGACTGTCCTCCCAGTGGCAACGGGCCATCGCGTTCATCCGTCACAGCCCCATGAAGGCTGTCTCCGAGGCGTCGGCCTGGCAGTTGATGAACACTGCTGTCGGACTGGCTCTCGTCATGCGGGAGGCTAACCGAGCTGATTACGGAAACCATGCACTGGGCGTCTCGTTGAGCTGGTCAACGCCGTGGGGGAACGTGGAGCTCACGGCTTGGGATACCGTCGTCCACGCCTATGACGTCATGACCGGTTTTGTGCGCGGCATCGCCCACCGCTTCGATGTCCGTAACGGCAACAATGGCGTGTCGTACCGGGTTGAGATGCGCATGGCCGCTGAGGCCGCAGGTTTGGCCAGCCGGTCCTATGGGACGGTAACGAGCGGCCTGCCGGCTGACCGTGCCCGGTTACGCAACCAGGGCGCCCTGCTCAAGGAGGTCCGTGAGCTGCTTACGCTGTCTCGGGGTTATGGCATGGAGTCAGTGCGACAGCGCGCCATGTCAACTGCGGAGACGGTCAGCGCCTCGCTGTCCGAGGTGGTGGACGACTCCGCCTTGGAGCTGGTCGTCGACCTCCGTCTGGCCTTCGGCCGGCTGCTGGCGGCACTGGGTGCCAATGAACGTGCGGAGAAGGAACATCTCGACACGGCGGAGTTGAGTCTGAGCCAGGGGTGGACGGAAACTGCTTGCGCCGCTCTGGCTCTGGCCTCGCACGCCGCTCAGGCTCGCGGGGACCGCGCTTCCAGCGGCCGGGCATGGCGCAAGTGCCGTGAGGCGATGGGGGCCTGGCCGATGAACCGGCCCGGAGAACGCTGCGGGACACTCGTCGACGCCGTCGGTGACCCTCTGGTTGCCTTGCAGGTCCTTTCCGCGCTGGCGGAGGTCCTGGTTGACGGGGTGGAGGAGGATCACTCTCGTGCGCCGATCATCCGCGAGATCATCTCGCGGGCCTCGGAGCAGGCCTCCCGGTGCGTGAGTCCCCCGCAGGGCGCGGTGGAGTCGTTGGCCCGGGTCGAGGAGCGTATCGCGCCCTACGGTCGGGGCCGGGGAGGAAGAAGGCGACCCGGTTCGACCACAACGATCAGGACTGAGGGTCGGGCGGCCTCGGAGGACGAGTGA","MSYWGDIARALEDVDPVCPSRDAAAALWKAVATDDVEDTAAGNAPDQVVEAVCAVDRAWLVQLGQDPDTSRRSLERAIAFCQGLRAAHGRSTLPLRYAQVELSAVLGLRDEALEQLREARLFSFGKADTGAVLATARMHDDYSGVISTATATPRRAEADPVESARGLGAVLVPYLAHQRIVEAEDAFASLSLLNLPDAVSLQCLADRLEYLGLSSQWQRAIAFIRHSPMKAVSEASAWQLMNTAVGLALVMREANRADYGNHALGVSLSWSTPWGNVELTAWDTVVHAYDVMTGFVRGIAHRFDVRNGNNGVSYRVEMRMAAEAAGLASRSYGTVTSGLPADRARLRNQGALLKEVRELLTLSRGYGMESVRQRAMSTAETVSASLSEVVDDSALELVVDLRLAFGRLLAALGANERAEKEHLDTAELSLSQGWTETACAALALASHAAQARGDRASSGRAWRKCREAMGAWPMNRPGERCGTLVDAVGDPLVALQVLSALAEVLVDGVEEDHSRAPIIREIISRASEQASRCVSPPQGAVESLARVEERIAPYGRGRGGRRRPGSTTTIRTEGRAASEDE$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0691","729351","729944","594","4.74","-10.05","20772","GTGGGGCTCACCGGTGGTATCGGCTCAGGCAAGTCCACAGTGGCCTGTCTGCTCAAGGAGCGCGGCGCGGTCGTGACCAGTGCCGACGAGGTCGCTCGCGATGTCGTCAGCCCGGGCAGTGACGGTCTTGCGGCAGTGGTGGCCGAGTTCGGGGAAGGGATCCTGGCTGCGGACGGCTCCCTGGACCGCGGTGCCCTGGGGCGGCTGGTCTTCTCCGACGACCTGCGTCGTGCGCGCCTGGAAGAGCTCCTCCTGCCCCTCATCGCAGCAGAGGCATGGGCTCGGATGGACACGGTTCCGGCTGGGCAGGTGGCGGTCTACGACGTTCCTCTCCTCGTTGAGGGACAGATGCAGGACCTGTTCGATCTTGTCATCGTCGTCGAGGCCGAGCTCGAACTGCGTCTGAAGCGGCTCGCTGCACGAGGGATGACCCGTGACGAGGCGCTGGCCCGTATCGCCGTGCAGGCCACTGACAAGGAGCGGCGGGCCGTTGCCGACGTCGTCGTGTCCAACTCCGGGGCGCTGGAGGACCTGAGCGCCGAGGTCGACAGACTATGGAGAACCCGGATCCTGGAGCCGGGAGCCACTGCCTGA","VGLTGGIGSGKSTVACLLKERGAVVTSADEVARDVVSPGSDGLAAVVAEFGEGILAADGSLDRGALGRLVFSDDLRRARLEELLLPLIAAEAWARMDTVPAGQVAVYDVPLLVEGQMQDLFDLVIVVEAELELRLKRLAARGMTRDEALARIAVQATDKERRAVADVVVSNSGALEDLSAEVDRLWRTRILEPGATA$","Dephospho-CoA kinase","Cytoplasm","Dephospho-CoA kinase (Dephosphocoenzyme Akinase)","dephospho-CoA kinase ","dephospho-CoA kinase","","","","","

InterPro
IPR001977
Family

Dephospho-CoA kinase
PD003329	$\"[1-73]T$	COAE_STRCO_Q9S2K7;
PTHR10695	$\"[73-191]T$	DEPHOSPHO-COA RELATED KINASES
PF01121	$\"[1-177]T$	CoaE
TIGR00152	$\"[1-184]T$	TIGR00152: dephospho-CoA kinase
PS51219	$\"[1-197]T$	DPCK

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-187]T$	no description
PS01294	$\"[59-88]?$	COAE

","BeTs to 18 clades of COG0237COG name: Dephospho-CoA kinaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0237 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001977 (Dephospho-CoA kinase) with a combined E-value of 5.3e-37. IPB001977A 1-26 IPB001977B 58-87 IPB001977C 133-171","Residues 1-73 are similar to a (KINASE A DEPHOSPHO-COA TRANSFERASE ATP-BINDING COENZYME DEPHOSPHOCOENZYME BIOSYNTHESIS SYNTHASE ADENYLYLTRANSFERASE) protein domain (PD003329) which is seen in COAE_STRCO.Residues 104-174 are 75% similar to a (KINASE A DEPHOSPHO-COA TRANSFERASE ATP-BINDING COENZYME DEPHOSPHOCOENZYME BIOSYNTHESIS SYNTHASE ADENYLYLTRANSFERASE) protein domain (PD582583) which is seen in COAE_MYCTU.","","-51% similar to PDB:1N3B Crystal Structure of Dephosphocoenzyme A kinase from Escherichia coli (E_value = 7.1E_20);-51% similar to PDB:1T3H X-ray Structure of Dephospho-CoA Kinase from E. coli Norteast Structural Genomics Consortium Target ER57 (E_value = 7.1E_20);-51% similar to PDB:1VHL Crystal structure of dephospho-CoA kinase with adenosine-5'-diphosphate (E_value = 7.1E_20);-51% similar to PDB:1VHT Crystal structure of dephospho-coA kinase with bis(adenosine)-5'-triphosphate (E_value = 7.1E_20);-51% similar to PDB:1VIY Crystal structure of dephospho-CoA kinase (E_value = 7.1E_20);","Residues 1 to 177 (E_value = 6.4e-65) place ANA_0691 in the CoaE family which is described as Dephospho-CoA kinase.","","kinase (Dephosphocoenzyme A kinase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0692","730367","732463","2097","5.01","-34.29","78711","ATGCGTCCCGTCACCGAGCTCCAGCGCGCAGCCAAGCCCTTCGAGGTCATCAGCCCTTACTCGCCCAGCGGGGACCAGCCCACGGCGATCGCCGAGCTGACTGAGCGTCTGCGGGCGGGGGAGAAGGACATCGTCCTGCTCGGTGCCACGGGAACCGGCAAGTCCGCGACGACCGCCTGGCTCGTCGAGCAGGTCCAGCGCCCCACCCTCATCCTGGAGCCGAACAAGACCCTGGCCGCCCAGATGGCCGCCGAGTTCCGTGAGCTTCTCCCGAATAACGCGGTGGAGTACTTCGTCTCCTACTACGACTACTACCAGCCTGAGGCCTACGTCCCGCAGACGGACACCTTCATCGAGAAGGACTCCTCCATCAATGACGAGGTCGAGCGCCTGCGCCACAGCGCCACCAACTCCCTGCTCACCCGCCGGGACGTCGTCGTGGTCTCCTCGGTCTCCTGCATCTACGGCCTGGGCACCCCCCAGGAGTACGTGGACCGGATGACGCCCCTGGAGGTGGGCCAGCAGATCGACCGGGACGATCTCCTGCGGCGGTTCGTGACGATGCAGTACACCCGCAACGACATCGACTTCACCCGGGGCACCTTCCGCGTGCGCGGCGACACGGTGGAGATCATCCCGATGTACGAGGAGCTCGCCATCCGCATTGAGTTCTTCGGAGACGAGATCGAGGCCCTGGCCACGCTGCACCCCGTGACCGGGGACGTCATCGACACCGTCGAGCAGGTCTTCGTCTTCCCCGCCTCCCACTACGTGGCCGGCCCCGAACGCATGCAGAAGGCCATTGAGGGTATTGAGGCCGAGCTCGCCGAGCGTCTGGCCCAGCTCGAGCACGACGGCCGTCTCTTGGAGGCCCAGCGCCTGCGCATGCGCACCACCTACGACCTGGAGATGCTTCAGCAGATCGGCATGTGCTCGGGGATCGAGAACTACTCGCTGCACATCGACGGGCGCGAGACCGGCACCCCGCCCAACACGCTCCTGGACTACTTCCCCGAGGACTTCCTCCTCGTCATCGATGAGTCCCACGTGACCGTTCCCCAGATCGGCGCCATGCACGAGGGGGACGCCTCCCGCAAGCGCACCCTGGTTGAGCATGGATTCCGTCTGCCCTCCGCACTGGACAACCGTCCCCTGACCTTCGCCGAGTTCGAGGACCGCGTCGGTCAGACCGTCTACCTGTCGGCCACCCCGGGCGACTACGAGACCCAGCGCTCCGACGGCGTCGTCGAGCAGATCATCCGCCCCACTGGACTGGTGGACCCCAAGGTCGTCGTCAAGCCCACGCAGGGACAGATCGACGACCTGCTCGAGGAGGTGCGCACCCGCGTCGAGCGCCAGGAGCGGATCCTGGTGACCACCCTGACCAAGCGCATGGCCGAGGACCTGACCACCTACCTCGCCGAGAGGGGCGTGCGCGTGGAGTACCTCCACTCCGACGTCGACACGCTGCGGCGCGTCGAGCTCCTGCGCGAGCTGCGGCTGGGGCGCTTCGATGTCCTGGTGGGCATCAACCTGCTGCGTGAGGGCCTGGACCTGCCGGAGGTCTCGCTCGTGTCCATCCTGGACGCGGACAAGGAGGGCTTCCTGCGCTCGACCCGCTCCCTGGTGCAGACCATCGGACGTGCCGCCCGCAACGTCTCCGGCGAGGTCCACATGTACGCCGACACCATCACCCCGGCCATGGCTGAGGCCATCGAGGAGACTGAGCGCCGCCGCACCAAGCAGTTGGCCTACAACGCCGAGCACGGCATCGACCCGCAACCGCTGCGCAAGAAGATCGCTGACGTCACCGACATGCTCGCCCGCGAGGACGTCGACACCGCCGACCTTCTGGCCGGAGGCTACCGGGGCCACGAGGACTCCTCGGTGCGGGCCAGGCGCAAGCACGCCGCCGAGGCCACGGTGCGTGAGAAGCTCGCCGGCGCGGCGCAGGGCGACCTCGCCGAGCTCATTAACGAGCTCACCCAGCAGATGCACGCCGCCGCCGAGGACCTCCACTTCGAGCTCGCCGCCCGGCTGCGCGACGAGATCCAGGACCTCAAGAAGGAGCTGCGCGCCATGCGGGCCGCCGACTGA","MRPVTELQRAAKPFEVISPYSPSGDQPTAIAELTERLRAGEKDIVLLGATGTGKSATTAWLVEQVQRPTLILEPNKTLAAQMAAEFRELLPNNAVEYFVSYYDYYQPEAYVPQTDTFIEKDSSINDEVERLRHSATNSLLTRRDVVVVSSVSCIYGLGTPQEYVDRMTPLEVGQQIDRDDLLRRFVTMQYTRNDIDFTRGTFRVRGDTVEIIPMYEELAIRIEFFGDEIEALATLHPVTGDVIDTVEQVFVFPASHYVAGPERMQKAIEGIEAELAERLAQLEHDGRLLEAQRLRMRTTYDLEMLQQIGMCSGIENYSLHIDGRETGTPPNTLLDYFPEDFLLVIDESHVTVPQIGAMHEGDASRKRTLVEHGFRLPSALDNRPLTFAEFEDRVGQTVYLSATPGDYETQRSDGVVEQIIRPTGLVDPKVVVKPTQGQIDDLLEEVRTRVERQERILVTTLTKRMAEDLTTYLAERGVRVEYLHSDVDTLRRVELLRELRLGRFDVLVGINLLREGLDLPEVSLVSILDADKEGFLRSTRSLVQTIGRAARNVSGEVHMYADTITPAMAEAIEETERRRTKQLAYNAEHGIDPQPLRKKIADVTDMLAREDVDTADLLAGGYRGHEDSSVRARRKHAAEATVREKLAGAAQGDLAELINELTQQMHAAAEDLHFELAARLRDEIQDLKKELRAMRAAD$","Excinuclease ABC, B subunit","Cytoplasm","excinuclease ABC, B subunit","excinuclease ABC subunit B","excinuclease ABC, B subunit","","Van Houten B., Snowden A. Mechanism of action of the Escherichia coli UvrABC nuclease: clues to the damage recognition problem. Bioessays 1993. 15(1):51-59. PMID: 8466476Moolenaar G.F., Franken K.L., Dijkstra D.M., Thomas-Oates J.E., Visse R., van de Putte P., Goosen N. The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3'-incision. J. Biol. Chem. 1995. 270(51):30508-30515. PMID: 8530482","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[472-553]T$	Helicase_C
SM00490	$\"[467-553]T$	HELICc
PS51194	$\"[438-604]T$	HELICASE_CTER

InterPro
IPR001943
Domain

UvrB/UvrC protein
PF02151	$\"[655-690]T$	UVR
PS50151	$\"[655-690]T$	UVR

InterPro
IPR004807
Family

Excinuclease ABC, B subunit
TIGR00631	$\"[13-688]T$	uvrb: excinuclease ABC, B subunit

InterPro
IPR006935
Family

Type III restriction enzyme, res subunit
PF04851	$\"[19-131]T$	ResIII

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[18-433]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[35-210]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[14-183]T$ $\"[297-418]T$ $\"[419-586]T$	no description
G3DSA:4.10.860.10	$\"[633-695]T$	no description
PTHR10967	$\"[440-525]T$	DEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF8	$\"[440-525]T$	ATP-DEPENDENT HELICASE DDX7

","BeTs to 20 clades of COG0556COG name: Helicase subunit of the DNA excision repair complexFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0556 is -om----qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001943 (UvrB/UvrC protein) with a combined E-value of 1.3e-56. IPB001943A 46-55 IPB001943B 85-112 IPB001943C 199-210 IPB001943D 389-405 IPB001943E 508-549","Residues 26-97 are 94% similar to a (DNA EXCISION B ATP-BINDING SUBUNIT REPAIR NUCLEASE SOS RECOMBINATION RESPONSE) protein domain (PD035493) which is seen in Q8CK11_STRCO.Residues 104-144 are identical to a (DNA EXCISION B REPAIR SUBUNIT NUCLEASE SOS ATP-BINDING RECOMBINATION RESPONSE) protein domain (PD579515) which is seen in UVRB_MICLU.Residues 153-239 are 91% similar to a (DNA EXCISION ATP-BINDING B REPAIR SUBUNIT NUCLEASE HELICASE SOS RECOMBINATION) protein domain (PD002798) which is seen in Q829Y6_STRAW.Residues 250-443 are similar to a (DNA EXCISION B REPAIR SUBUNIT NUCLEASE SOS ATP-BINDING RECOMBINATION RESPONSE) protein domain (PD186159) which is seen in Q8CK11_STRCO.Residues 456-520 are 92% similar to a (HELICASE ATP-BINDING HYDROLASE DNA ATP-DEPENDENT RNA EXCISION FACTOR B REPAIR) protein domain (PD000033) which is seen in Q7WK66_BORBR.Residues 509-594 are 89% similar to a (DNA EXCISION ATP-BINDING B REPAIR SUBUNIT NUCLEASE SOS RECOMBINATION RESPONSE) protein domain (PD099792) which is seen in UVRB_MICLU.Residues 657-695 are 84% similar to a (DNA EXCISION B REPAIR SUBUNIT NUCLEASE SOS RECOMBINATION RESPONSE ATP-BINDING) protein domain (PD878087) which is seen in UVRB_MICLU.","","No significant hits to the PDB database (E-value < E-10).","Residues 19 to 131 (E_value = 1.1e-06) place ANA_0692 in the ResIII family which is described as Type III restriction enzyme, res subunit.Residues 472 to 553 (E_value = 1.6e-16) place ANA_0692 in the Helicase_C family which is described as Helicase conserved C-terminal domain.Residues 655 to 690 (E_value = 6.1e-13) place ANA_0692 in the UVR family which is described as UvrB/uvrC motif.","","ABC, B subunit (uvrB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0693","732702","733706","1005","6.09","-4.91","36719","GTGGACGTCCACATCCTGGGGTGGATCGGCCTGGCGGCCATCATCCTGACCCTCATCGTGATCGACATCGTCGGTCACGTGCGCACCCCCCACGAGCCCACCATGAAGGAGGCCGCCGTCTGGTCAGTGGCCTATATCGGCATGGCCCTGGTCTTCGGCGGCATCGTCTGGTTCGTGTGGGGCGGGGGCTTCGCCCAGGAGTACCTGGCCGGCTACATCACCGAGAAGGCGCTGAGCATCGACAACCTCTTCGTCTTCGTCATCATGATGTCCTCCTTCAAGGTGCCTCGGAAGTACCAGCAGGAGGTGCTGCTCGCCGGCATCGTCATCGCCCTTGTTCTCCGGCTCATCTTCATCCTCGCCGGCGCCGCGCTCATCGAGAACTTCTCCTGGGTGTTCTACTTCTTCGGGGCCTGGCTCCTGTGGACCGCCTTCTCCCAGGCCCGGGAGGGCGTCCAGGAGCCCGACGACGATGACGAGGAGTACAGGCCCAGCGGCTTCGTCAAGCTCGTCGCCCGCGTCATCCCCATGACCGACGGCTTCGTGGGCGGCAAGGTCATTCACCGCCACGCCGGGCGCACCATGATTACTCCCATGATGCTGTGCATCATCGCCATCGGTACCGCCGATGTCATGTTCGCCGTCGACTCCATCCCCGCGATCTACTCCCTGACCAGTGAGCCCTTCCTGGTCTTCTCAGCGAACGCCTTCTCCCTGCTGGGCCTGCGCCAGCTCTACTTCCTCATCGACGGGCTGCTCGACCGACTCGTCTACCTCCACTACGGCCTGGCGGTCATTCTCGGCTTCATCGGCTTCAAGCTCATCGTTCACGCCCTGCACACCAATGAGGTCCCCTTCATCAACGGGGGCCAGGAGTGGCACGCCATCCCCGAGGCGTCGATCGGAGTGTCCCTGAGCGTCATCATCAGCACCGTCCTGGTCACGGTCATCGCATCGGTCCTCAAGTCGCGGGCAGATGCCCGGCGCTTGGAGGCGGCATCCTGA","VDVHILGWIGLAAIILTLIVIDIVGHVRTPHEPTMKEAAVWSVAYIGMALVFGGIVWFVWGGGFAQEYLAGYITEKALSIDNLFVFVIMMSSFKVPRKYQQEVLLAGIVIALVLRLIFILAGAALIENFSWVFYFFGAWLLWTAFSQAREGVQEPDDDDEEYRPSGFVKLVARVIPMTDGFVGGKVIHRHAGRTMITPMMLCIIAIGTADVMFAVDSIPAIYSLTSEPFLVFSANAFSLLGLRQLYFLIDGLLDRLVYLHYGLAVILGFIGFKLIVHALHTNEVPFINGGQEWHAIPEASIGVSLSVIISTVLVTVIASVLKSRADARRLEAAS$","Integral membrane protein TerC","Membrane, Cytoplasm","Membrane protein TerC, possibly involved intellurium resistance","integral membrane protein TerC","Integral membrane protein TerC","","Burian J., Tu N., Kl'ucar L., Guller L., Lloyd-jones G., Stuchlik S., Fejdi P., Siekel P., Turna J. In vivo and in vitro cloning and phenotype characterization of tellurite resistance determinant conferred by plasmid pTE53 of a clinical isolate of Escherichia coli. Folia Microbiol. 1998. 43(6):589-599. PMID: 10069007","","","

InterPro
IPR005496
Family

Integral membrane protein TerC
PF03741	$\"[67-184]T$	TerC

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[39-59]?$ $\"[69-89]?$ $\"[104-124]?$ $\"[130-148]?$ $\"[195-215]?$ $\"[229-249]?$ $\"[259-279]?$ $\"[301-321]?$	transmembrane_regions

","BeTs to 8 clades of COG0861COG name: Membrane protein TerC, possibly involved in tellurium resistanceFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0861 is ---------dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB005496 (Integral membrane protein TerC family) with a combined E-value of 1.3e-16. IPB005496A 70-89 IPB005496B 131-141 IPB005496C 210-224","Residues 67-102 are 91% similar to a (TRANSMEMBRANE TERC RESISTANCE MEMBRANE TELLURIUM ALX FAMILY EXPORT PROTEIN INTEGRAL) protein domain (PD328364) which is seen in Q8FPC3_COREF.Residues 118-186 are 65% similar to a (TRANSMEMBRANE TERC RESISTANCE MEMBRANE TELLURIUM ALX FAMILY EXPORT PROTEIN INTEGRAL) protein domain (PD863049) which is seen in Q8G5M0_BIFLO.Residues 197-235 are 89% similar to a (TRANSMEMBRANE TERC RESISTANCE MEMBRANE TELLURIUM ALX FAMILY EXPORT PROTEIN INTEGRAL) protein domain (PD358719) which is seen in Q829Y3_STRAW.Residues 237-291 are similar to a (TRANSMEMBRANE RESISTANCE TERC MEMBRANE TELLURIUM ALX FAMILY EXPORT PROTEIN INTEGRAL) protein domain (PD011587) which is seen in YR23_MYCTU.","","No significant hits to the PDB database (E-value < E-10).","Residues 67 to 184 (E_value = 6.9e-32) place ANA_0693 in the TerC family which is described as Integral membrane protein TerC family.","","protein TerC, possibly involved in tellurium resistance (terC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0694","733763","736252","2490","7.54","1.87","86777","GTGAGCACCACGCATCCCCCTGAGTCCTCGATCAGCGGGCTCAGCGCCGCCCAGGTCGCCGAGCGCGTCAGCACCGGACGGACCAACGAGTACCGCGAGCGGACCTCCCGCAGCGCCGCGCAGATTCTGCGAGCCAATGTCTTCACGATCTTCAACGGCATCCTTGGCGCCGCACTGGTGCTCGTCCTGGCGCTGGGGCACTGGGCGGATGCACTGTTCGGTTTCGTCCTTGTGCTCAACACCGCCACCGGAACCCTGGCGGAGATCCGCGCCAAGCGTGCCCTGGACCGTCTGTCCGTGCTGGAAACCCCCCGCGCCATCGTCGTCAGGGACGGGGCCGAGACCGAGGTGGCCGTCGGCCAGGTCGTCCTCGACGACGTCGTACGCCTCGCAGCCGGCCAGCAGGTGCCGGCCGACGGGGAGGTTCTGACCAGCGACGGCCTGGAGATCGATGAGTCGATCCTCACCGGCGAGTCCCGGCCGGTGCGCCCCGTGAGCGGAGCGAAGGTCATGTCCGGGACCACGGTGACGGCCGGGACCGGGCTGTTCCGCACCACCGCGGTCGGCGGGGACGCCTACGCCCACCGGCTGGCCCGGGAGGCCCGCAAGTACTCACTCGTCGTCAGCGAGCTGCAGGCCGGGACCAACCGGGTGCTGCACTGGATCAGCTGGGTCATCGTGCCCGTGGCCCTGGTCCTGGTGTGGTCCCAGCTGCGGTTGAGCGGAAGCGTCGGCGAGGCCTGGAGCAGCGGCGCCTGGCGCCACGCGGTCGTCGCCGGCATCGCGGGCGTGGTCAGCATGGTGCCCCAGGGTCTGGTGCTCCTGACCTCGGTCAACTTCGCCACCGCTTCCCTGGCCCTGGCCAGGCGCAACGTCCTGGTTCAGGAGCTGCCCGCCGTCGAGGTCCTGGCCCGGGTCGACACCCTGTGCCTGGACAAGACCGGCACCATCACCACCGGACGCATCCGCCTCGGTGAGATCCAGGGGCCCGACGGCGGTGAGGCTCCTCCCGAGGTGCTCTCGGCGCTCGCACTTCTCAGTACGGTGGGGGAGGCCAACGCCACCGCCGATGCCATCAGGGACGGGCTCGCTGATTCCGAGTGGCTCGGTGCACAAGGACTTCAAGAGGCGCTGTCGTCGGCCGGCGCTGGCAGCAGGGCCGGTGTGGAGTCAGTGCCCTTCTCCTCGCGCCGCAAGTGGTCCGCGGTTCGCGACAGCTTCGGCACCACCTGGGTGCTCGGCGCCCCCGAGATCGTCCTGGCCGGATACAACGGGTCAGTGCTGGATCGTGCCCGTCAGATCGCCGCGCAGGGGATGCGCGTCGTGGCCCTGGCCTGCTCGCGCTCGCCCTGGAGCTTGGCTCCGGGGGAGGAGGACCCGCGGCTTCCCGATGCTCTTGAGGCCGCAGGGGTCGTGATCCTCACCGAGGAGATCCGCCCCGACGCCGCGGAGACCCTGGCCTACTTCCGCCAGCAGGGGGTCGACGTCAAGGTCATCTCCGGGGACAGCCCCGAGACGGTGGCCGCGGTCGCCCGTCAGGCCGGAGTCACCGCACCCGACGGCGGCGAGCTCGTCGTCCTGGACGCACGTACCCTGCCTGCCGGAGCGGGTAGCGGGCAGGAGACGGAGGAGGACCTGGAGCGCCTGGCCGACGCGGTTGAGCGCGCCAGTGTCCTAGGACGCGTCACGCCCGAGCAGAAACGGGCACTGGTGCGGGCGCTGAAGTCCCGAGGGCACGTCGTCGCGATGACCGGGGACGGCGTCAACGACGCCCTGGCGCTCAAGGACGCCGACCTCGGCATCGCCATGGGCAACGGAGCGCCGGCGACCAAGGCGGTGGCGCGCCTGGTGCTGCTCAAGGGAGAGTTCTCGGCCCTTCCCGGGGTCGTGGCTCAGGGGCGCCGCGTCATGGCCAACACCGAGCGCATCGCCTCGCTGTTCCTGGCCAAGACCATCTACGCCTCGCTTATCGCCGTCGTCGTGTCGGCCATGGCGGTCGCTTACCCGTTCCTGCCCCGCCAGTTCACGGTCGTCTCCTCACTGACGATCGGGATCCCCGCCTTCGTCCTGGCCCTGGCCCCCAGCAACCAGCGCTACCGGGAGGGCTTTCTCGGGCGGGTGCTCAGCCTGTGCGTACCGGCCGGGCTCATGGCGGGCACCGTCACGCTGTCCACCTACCTCTGGTTGACGCTCACCCACGCCCCGCGCGCCCAGGTGACCACGGCGACGACCCTGGTCCTCATCACCTGCGGGCTGTGGCTGCTCACGCTCACTGCCAGACCATTGACGAGCTGGCGGCTGGGGCTGGTCGCTCTCATGGGGACGATCGCGGTCCTCGGCGTCGTCGCCCCACCGGTGCGCGCCTTCTTCCTGCTGGCCTGGCCCACCCCTGGGGTGTGGTGGGTCATCGCGCTCATGGCGGGCCTGGCCGTTGGCGGCATTGAGCTGGTCCACCTGGTGCGACGCCGGATCGTGGGCGACCGCGGCTAA","VSTTHPPESSISGLSAAQVAERVSTGRTNEYRERTSRSAAQILRANVFTIFNGILGAALVLVLALGHWADALFGFVLVLNTATGTLAEIRAKRALDRLSVLETPRAIVVRDGAETEVAVGQVVLDDVVRLAAGQQVPADGEVLTSDGLEIDESILTGESRPVRPVSGAKVMSGTTVTAGTGLFRTTAVGGDAYAHRLAREARKYSLVVSELQAGTNRVLHWISWVIVPVALVLVWSQLRLSGSVGEAWSSGAWRHAVVAGIAGVVSMVPQGLVLLTSVNFATASLALARRNVLVQELPAVEVLARVDTLCLDKTGTITTGRIRLGEIQGPDGGEAPPEVLSALALLSTVGEANATADAIRDGLADSEWLGAQGLQEALSSAGAGSRAGVESVPFSSRRKWSAVRDSFGTTWVLGAPEIVLAGYNGSVLDRARQIAAQGMRVVALACSRSPWSLAPGEEDPRLPDALEAAGVVILTEEIRPDAAETLAYFRQQGVDVKVISGDSPETVAAVARQAGVTAPDGGELVVLDARTLPAGAGSGQETEEDLERLADAVERASVLGRVTPEQKRALVRALKSRGHVVAMTGDGVNDALALKDADLGIAMGNGAPATKAVARLVLLKGEFSALPGVVAQGRRVMANTERIASLFLAKTIYASLIAVVVSAMAVAYPFLPRQFTVVSSLTIGIPAFVLALAPSNQRYREGFLGRVLSLCVPAGLMAGTVTLSTYLWLTLTHAPRAQVTTATTLVLITCGLWLLTLTARPLTSWRLGLVALMGTIAVLGVVAPPVRAFFLLAWPTPGVWWVIALMAGLAVGGIELVHLVRRRIVGDRG$","ATPase, P-type (transporting), HAD superfamily, subfamily IC","Membrane, Cytoplasm","cation-transporting ATPase, E1-E2 family","ATPase; P-type (transporting); HAD superfamily; subfamily IC","ATPase, P-type (transporting), HAD superfamily, subfamily IC","","Smith D.L., Tao T., Maguire M.E. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 1993. 268(30):22469-22479. PMID: 8226755Fagan M.J., Saier Jr M.H. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 1994. 38(1):57-99. PMID: 8151716","","","

InterPro
IPR001757
Family

ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
PR00119	$\"[151-165]T$ $\"[310-324]T$ $\"[470-481]T$ $\"[492-502]T$ $\"[584-603]T$ $\"[607-619]T$	CATATPASE
PTHR11939	$\"[9-336]T$ $\"[380-694]T$	CATION-TRANSPORTING ATPASE
TIGR01494	$\"[561-672]T$	ATPase_P-type: ATPase, P-type (transporting
PS00154	$\"[312-318]?$	ATPASE_E1_E2

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[306-607]T$	Hydrolase

InterPro
IPR008250
Domain

E1-E2 ATPase-associated region
PF00122	$\"[71-302]T$	E1-E2_ATPase

InterPro
IPR013982
Domain

AICARFT/IMPCHase bienzyme, formylation region
SM00798	$\"[339-612]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.20.1110.10	$\"[558-827]T$	no description
G3DSA:2.70.150.10	$\"[12-182]T$	no description
PTHR11939:SF60	$\"[9-336]T$ $\"[380-694]T$	CATION-TRANSPORTING ATPASE
tmhmm	$\"[45-65]?$ $\"[71-86]?$ $\"[218-238]?$ $\"[651-671]?$ $\"[707-727]?$ $\"[737-757]?$ $\"[767-789]?$ $\"[799-819]?$	transmembrane_regions

","BeTs to 11 clades of COG0474COG name: Cation transport ATPasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0474 is --mp--yq--rlbcef-----j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB006068 (Cation transporting ATPase, C-terminal) with a combined E-value of 1.2e-66. IPB006068A 87-110 IPB006068B 117-157 IPB006068C 165-197 IPB006068E 289-315 IPB006068H 476-517 IPB006068I 559-591 IPB006068J 601-652***** IPB008250 (E1-E2 ATPase-associated region) with a combined E-value of 7.1e-36. IPB008250A 310-320 IPB008250B 476-516 IPB008250C 581-604***** IPB000695 (H+-transporting ATPase (proton pump) signature) with a combined E-value of 1e-24. IPB000695A 427-445 IPB000695B 556-572 IPB000695C 584-600 IPB000695D 615-640***** IPB001757 (ATPase, E1-E2 type) with a combined E-value of 2.5e-18. IPB001757A 310-320 IPB001757B 581-603","Residues 13-54 are 76% similar to a (PHOSPHORYLATION TRANSMEMBRANE ATP-BINDING HYDROLASE ATPASE CATION-TRANSPORTING E1-E2 INTEGRAL CATION FAMILY) protein domain (PD683641) which is seen in Q6AFD7_BBBBB.Residues 129-189 are 60% similar to a (HYDROLASE ATP-BINDING PHOSPHORYLATION TRANSMEMBRANE ATPASE MAGNESIUM PUMP CALCIUM ALPHA FAMILY) protein domain (PD861420) which is seen in Q72JJ6_THET2.Residues 170-223 are 74% similar to a (HYDROLASE PHOSPHORYLATION TRANSMEMBRANE ATP-BINDING ATPASE CATION-TRANSPORTING E1-E2 MEMBRANE PROBABLE INTEGRAL) protein domain (PD026885) which is seen in Q742J2_MYCPA.Residues 224-281 are 77% similar to a (HYDROLASE PHOSPHORYLATION TRANSMEMBRANE ATP-BINDING ATPASE CATION-TRANSPORTING MEMBRANE INTEGRAL E1-E2 ATPASE) protein domain (PD970604) which is seen in Q8G4I6_BIFLO.Residues 393-447 are 65% similar to a (HYDROLASE PHOSPHORYLATION TRANSMEMBRANE ATP-BINDING ATPASE CATION-TRANSPORTING E1-E2 MEMBRANE PROBABLE INTEGRAL) protein domain (PD940435) which is seen in Q8G4I6_BIFLO.Residues 468-683 are 43% similar to a (P-TYPE PROBABLE HYDROLASE PHOSPHORYLATION TRANSMEMBRANE ATPASE ATP-BINDING CATION-TRANSPORTING) protein domain (PDA0Z2J6) which is seen in Q7UQF3_RHOBA.Residues 469-637 are 43% similar to a (COPPER MULTIGENE POTENTIAL HYDROLASE METAL-BINDING COPPER-TRANSPORTING PHOSPHORYLATION ION FAMILY TRANSMEMBRANE) protein domain (PD626429) which is seen in AHM6_ARATH.Residues 471-622 are 46% similar to a (P-TYPE TRANSPORTING HYDROLASE HEAVY-METAL TRANSMEMBRANE ATPASE ATP-BINDING PHOSPHORYLATION) protein domain (PD795816) which is seen in Q8EUP9_MYCPE.Residues 479-633 are 69% similar to a (ATP-BINDING HYDROLASE PHOSPHORYLATION TRANSMEMBRANE ATPASE P-TYPE MAGNESIUM B CHAIN CATION-TRANSPORTING) protein domain (PD000121) which is seen in Q9KXM5_STRCO.Residues 541-620 are 61% similar to a (P-TYPE HYDROLASE TRANSMEMBRANE ATPASE ATP-BINDING COPPER ATKB PHOSPHORYLATION) protein domain (PD626416) which is seen in Q9JP67_LACSK.Residues 557-630 are 64% similar to a (TRAX) protein domain (PD162139) which is seen in Q50124_MYCLE.Residues 557-648 are 53% similar to a (PROBABLE HYDROLASE PHOSPHORYLATION 3.6.3.- TRANSMEMBRANE ATPASE ATP-BINDING MAGNESIUM CATION-TRANSPORTING) protein domain (PD072472) which is seen in ATX9_TETTH.Residues 566-637 are 57% similar to a (P-TYPE D PROBABLE HYDROLASE PHOSPHORYLATION 3.6.3.- TRANSMEMBRANE ATPASE ATP-BINDING MAGNESIUM) protein domain (PD964162) which is seen in CTPD_MYCTU.Residues 627-792 are 61% similar to a (HYDROLASE PHOSPHORYLATION TRANSMEMBRANE ATP-BINDING ATPASE CATION-TRANSPORTING CATION E1-E2 P-TYPE ATPASE) protein domain (PD189829) which is seen in Q9Z4W5_STRCO.","","-41% similar to PDB:1MHS Model of Neurospora crassa proton ATPase (E_value = 2.4E_36);-48% similar to PDB:1IWO Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+ (E_value = 3.5E_24);-48% similar to PDB:1KJU Ca2+-ATPase in the E2 State (E_value = 3.5E_24);-48% similar to PDB:1SU4 Crystal structure of calcium ATPase with two bound calcium ions (E_value = 3.5E_24);-48% similar to PDB:1T5S Structure of the (SR)Ca2+-ATPase Ca2-E1-AMPPCP form (E_value = 3.5E_24);","Residues 71 to 302 (E_value = 1.8e-45) place ANA_0694 in the E1-E2_ATPase family which is described as E1-E2 ATPase.Residues 306 to 607 (E_value = 2.5e-24) place ANA_0694 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","ATPase, E1-E2 family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0695","736718","736350","369","5.94","-4.37","13462","GTGTCTCATGGTCGGGACACCGGAAGAATGACCGTGCTCCCGGGTTCTCACCACGGTCGGAGCCAGCACCCCTATGCTGAGGCCATGAGCAAGATCTACGCCGTCGAGTACCACTACGTCACTGACAAGGACGAGGAGATGGCCGCTGTCCGTCCCTCGCACCGCGCTTTCAACGGCCGCTGGGCCGACGAGGGCCGGCTGCTGGCCGCCGGCCCCTATGTGGGCACCCACGATGCCCTCATCGTCGTGCGGGCCGAGGACGAGGCCGGTGCACTGGCCCTCCTCGAGGACGATCCTTTCCAGCAGGCCGGCTTCATCTCTGAGCGCATTCCACGCGAGTGGAACCCCGTCATCGGGGTCCTGGCCTGA","VSHGRDTGRMTVLPGSHHGRSQHPYAEAMSKIYAVEYHYVTDKDEEMAAVRPSHRAFNGRWADEGRLLAAGPYVGTHDALIVVRAEDEAGALALLEDDPFQQAGFISERIPREWNPVIGVLA$","YCII-related protein","Cytoplasm","YCII-related domain family","hypothetical protein predicted by Glimmer/Critica","YCII-related","","","","","

InterPro
IPR005545
Domain

YCII-related
PF03795	$\"[39-118]T$	YCII

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.1060	$\"[28-118]T$	no description

","BeTs to 4 clades of COG2350COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2350 is ---------d--bcefgh-n-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 39 to 118 (E_value = 6e-10) place ANA_0695 in the YCII family which is described as YCII-related domain.","","domain family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0697","736744","739620","2877","6.24","-9.66","105209","ATGTGCGCTCACCCCTTAGACTCGAATCCCGTGAACGACTCTCTCATCATCCGTGGGGCCCGCGAGCACAATCTCAAGGGCGTAGACCTGGACCTGCCGCGCGACACGATGATCGTCTTCACCGGACTGTCGGGCTCGGGCAAGTCCTCCCTCGCCTTCGACACGATCTTCGCCGAGGGGCAGCGCCGCTACGTGGAGTCCCTGTCCTCCTACGCCCGTCAGTTCCTCGGGCAGATGGACAAACCCGACGTCGAGCTCATCGAGGGCCTGAGCCCGGCGGTGTCCATCGATCAGAAGTCCACCTCGCGCAACCCCCGGTCCACGGTGGGCACCGTGACAGAGATCTACGACTACCTGCGTCTGCTCTACGCGCGGGCCGGCATCCAGCACTGCCCGGTCTGTGACGCCGTCATCTCCTCCCAGACCCCGCAGCAGATCGTGGACCAGGTCCGCGCCCTGCCCGAGGGCACTCGCTTCCAGGTTCTCGCCCCGGTGGTGCGGGGCCGCAAGGGTGAGTACTCCGAGCTCTTCGGCGAGCTGCGCGGACGCGGCTTCAACCGGGTGCGCGTCGACGGCGCCGCCGAGCGCCTCGACAACCCCCCGACCCTCAACAAGCGCCTCAAGCACGACATCGAGGTCATCGTCGACCGGCTGGTTGTCCGCGAGGGCATCCGCCAGCGCCTCACCGACTCCGTCGAGACAGCACTGGGGCTGGCGGAGGGGCTGGTCATCATCGAGCTGGTCGATCTACCCGAGGACGACCCCCACCGGGAGCGGCGCTACTCTGAGAAGCGCGCCTGCCCCAACGAGCACCCCTTGGCCCTGGACGAGATGGAGCCCCGCACCTTCTCATTCAACGCCCCCTACGGCGCCTGCCCCGCCTGCACCGGAATCGGCACCCGGCTCGAGGTGGACCCCGAGCTCGTCGTCCCCGACGAGGAGCTCACCCTGGCCGAGGGCGCCGTCGCCCCCTGGTCGAGCCACCAGAAGTACTTCACCCGCCAGCTTGAGGCCCTGGGCAAGGAGCTCTCCTTCGACGTCGACACCCCCTGGCGCGCCCTGCCTGCGCGGGCTCGTGAGGCGATCCTGCGAGGTAAGGACTACGAGGTCAAGGTCACCTACCGCAACCGGTGGGGACGCGAACGCATCTACTCCAGCGGCTTCGAAGGAGTGCTCGACTACGTCATGCGCAAGCACGACGAGACCGAGTCCGACTGGTCCCGGGAGCGCTACCAGGCCTACATGCGTGAGATCCCCTGCCCCGTCTGCGACGGAGCCCGCCTCAAGCCCGAGGTGCTGGCCGTGCGCGTGGGCGAGCTGTCCATCGCTCAGCTGTGCGAGCTTCCGATCAACGAGGCCCGCGACTTCCTGGCCGACCTCAACCTCACCGGCCAGGCCGCCCAGATCGCCGGAAGCGTCCTGACCGAGATCAACGCGCGCCTCGGCTTCCTTGTGGACGTGGGGCTGGACTACCTCAGCCTGGCCCGTGGTGCGGCCACGCTCTCCGGGGGCGAGGCCCAGCGCATCCGCCTGGCCACCCAGATCGGCTCAGGCCTGGTGGGCGTCCTCTACGTCCTGGACGAGCCCAGTATCGGCCTGCACCAGCGCGACAACACCCGACTCATCGAGACCCTCCAGCGGCTGCGGGACCTGGGCAACACGCTCATCGTCGTCGAGCATGACGAGGACACCATCCGCTCGGCCGACTGGATCGTCGACATCGGGCCCGGAGCCGGTGAGCTGGGCGGTGAGGTCGTCTACTCCGGCGACGTCGCGGGCCTGACCGGAGCCGAGGGTTCCATCACCGGTGACTACCTGGCACGGCGGCGTGAGATCGAGATTCCCGCTACTCGGCGCAAGCGGGATAAGAACCGTGAGGTCACCGTCGTCGGAGCCCGGGAGAACAACCTCAAGGACGTCACCGTCTCCTTCCCGCTTGGCGTGCTCACCGCCGTCACGGGTGTATCCGGGTCGGGGAAGTCCTCCCTGGTCAACTCCATCCTCTACCAGGTGCTTGCCAACCGCCTCAACCGCGCCCGCGGCGTACCCGGCAGGCACAAGACGGTGCGAGGCGTGGAGCACCTGGACAAGGTGGTCCACGTGGACCAGTCGCCGATCGGACGTACCCCTCGGTCCAATCCCGCCACCTACACCGGCGTGTGGGACCACATCCGCAAGATCTTCGCGGCCGTGCCCGAGTCGAAGGTGCGCGGCTACGGACCCGGGCGTTTCTCCTTCAACGTCAAGGGCGGACGCTGCGAGTCCTGCAAGGGCGACGGCACGCTCAAGATCGAGATGAACTTCCTGCCCGACGTCTACGTCCCCTGCGAGGTCTGCCACGGCGCCCGCTACAACCGGGAGACCCTGGAGATCCGTTACAAGGACAAGACGGTCGCCGACGTCCTGGACATGACCATCCACCAGGCGGCCGAGTTCTTCTCCGCCTCCTCCGTCATCTCCCGCCACCTCAACACCCTGGTCGAGGTGGGACTGGGGTACGTGCGCCTGGGGCAGTCGGCCACCACGCTCTCCGGCGGTGAGGCCCAGCGCGTCAAGCTCGCCACCGAGCTGCAGCGCCGCTCCACCGGTCGCACCATCTACGTCCTGGATGAACCGACCACCGGGCTGCACTTCGAGGACATCCGTAAGCTGCTCGGGGTGCTTCAGGGACTGGTGGACAAGGGCAACTCCGTGGTCGTCATCGAGCACAACCTCGACGTCATCGCCAACGCCGACTGGGTCATCGACATGGGCCCAGAGGGCGGCAAGGGTGGGGGAACCGTCGTCGTGGCCGGAACCCCGGAGAAGGTCGCGGCCACCGAGGCGTCCTACACCGGTCAGTTCTTGGCCCCGGTGCTGGAGGCCGGCCGCGGCTGA","MCAHPLDSNPVNDSLIIRGAREHNLKGVDLDLPRDTMIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSSYARQFLGQMDKPDVELIEGLSPAVSIDQKSTSRNPRSTVGTVTEIYDYLRLLYARAGIQHCPVCDAVISSQTPQQIVDQVRALPEGTRFQVLAPVVRGRKGEYSELFGELRGRGFNRVRVDGAAERLDNPPTLNKRLKHDIEVIVDRLVVREGIRQRLTDSVETALGLAEGLVIIELVDLPEDDPHRERRYSEKRACPNEHPLALDEMEPRTFSFNAPYGACPACTGIGTRLEVDPELVVPDEELTLAEGAVAPWSSHQKYFTRQLEALGKELSFDVDTPWRALPARAREAILRGKDYEVKVTYRNRWGRERIYSSGFEGVLDYVMRKHDETESDWSRERYQAYMREIPCPVCDGARLKPEVLAVRVGELSIAQLCELPINEARDFLADLNLTGQAAQIAGSVLTEINARLGFLVDVGLDYLSLARGAATLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNTRLIETLQRLRDLGNTLIVVEHDEDTIRSADWIVDIGPGAGELGGEVVYSGDVAGLTGAEGSITGDYLARRREIEIPATRRKRDKNREVTVVGARENNLKDVTVSFPLGVLTAVTGVSGSGKSSLVNSILYQVLANRLNRARGVPGRHKTVRGVEHLDKVVHVDQSPIGRTPRSNPATYTGVWDHIRKIFAAVPESKVRGYGPGRFSFNVKGGRCESCKGDGTLKIEMNFLPDVYVPCEVCHGARYNRETLEIRYKDKTVADVLDMTIHQAAEFFSASSVISRHLNTLVEVGLGYVRLGQSATTLSGGEAQRVKLATELQRRSTGRTIYVLDEPTTGLHFEDIRKLLGVLQGLVDKGNSVVVIEHNLDVIANADWVIDMGPEGGKGGGTVVVAGTPEKVAATEASYTGQFLAPVLEAGRG$","Excinuclease ABC, A subunit","Cytoplasm","excinuclease ABC, A subunit","excinuclease ABC; A subunit","excinuclease ABC, A subunit","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[843-888]T$	Q8CQ28_STAEP_Q8CQ28;
PF00005	$\"[647-921]T$	ABC_tran
PS50893	$\"[622-950]T$	ABC_TRANSPORTER_2
PS00211	$\"[501-515]T$ $\"[843-857]T$	ABC_TRANSPORTER_1

InterPro
IPR004602
Family

Excinuclease ABC, A subunit
TIGR00630	$\"[14-938]T$	uvra: excinuclease ABC, A subunit

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[494-634]T$ $\"[835-945]T$	no description
PTHR19222	$\"[828-917]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 20 clades of COG0178COG name: Excinuclease ATPase subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0178 is -om----qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 594-717 are 44% similar to a (A EXCINUCLEASE ATP-BINDING SUBUNIT ABC) protein domain (PD953261) which is seen in Q7URK7_RHOBA.Residues 25-51 are identical to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD002065) which is seen in Q8NQQ0_CORGL.Residues 59-156 are similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR UVRABC) protein domain (PD363446) which is seen in Q8TKS1_METAC.Residues 161-268 are similar to a (A DNA ATP-BINDING SUBUNIT EXCINUCLEASE EXCISION ABC UVRA REPAIR UVRABC) protein domain (PD003919) which is seen in Q8FTQ6_COREF.Residues 722-801 are 84% similar to a (A DNA ATP-BINDING SUBUNIT EXCINUCLEASE EXCISION ABC UVRA REPAIR UVRABC) protein domain (PD001646) which is seen in Q6A9K3_PROAC.Residues 316-378 are 78% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT EXCISION ABC UVRA REPAIR UVRABC) protein domain (PD661928) which is seen in Q740K9_MYCPA.Residues 382-457 are 74% similar to a (A DNA ATP-BINDING SUBUNIT EXCINUCLEASE ABC EXCISION UVRA REPAIR UVRABC) protein domain (PD697224) which is seen in Q740K9_MYCPA.Residues 802-902 are 52% similar to a (UVRA-LIKE TRANSPORTER ABC) protein domain (PDA1A825) which is seen in Q6A9D4_PROAC.Residues 823-901 are 64% similar to a (LIN1813) protein domain (PD661935) which is seen in Q92AV6_LISIN.Residues 821-854 are 96% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD565575) which is seen in UVRA_MYCTU.Residues 802-902 are 65% similar to a (RESISTANCE ATP-BINDING DAUNORUBICIN) protein domain (PDA1A571) which is seen in Q836S6_ENTFA.Residues 519-717 are 47% similar to a (DNA A EXCISION EXCINUCLEASE ATP-BINDING SUBUNIT SOS UVRA DNA-BINDING SYSTEM) protein domain (PD190842) which is seen in UVRA_CHLPN.Residues 869-902 are 97% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD001034) which is seen in Q8FTQ6_COREF.Residues 560-589 are 93% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR UVRABC) protein domain (PD508139) which is seen in Q8G6E1_BIFLO.Residues 594-717 are 44% similar to a (A EXCINUCLEASE ATP-BINDING SUBUNIT ABC) protein domain (PD953261) which is seen in Q7URK7_RHOBA.Residues 594-636 are 74% similar to a (A EXCINUCLEASE ATP-BINDING SUBUNIT ABC DNA EXCISION SOS UVRA ZINC) protein domain (PDA0P5A2) which is seen in Q8G6E1_BIFLO.Residues 635-806 are 46% similar to a (A EXCINUCLEASE ATP-BINDING ABC SUBUNIT-RELATED ABC SUBUNIT) protein domain (PD708955) which is seen in Q81Q62_BACAN.Residues 637-687 are 62% similar to a (A EXCINUCLEASE ATP-BINDING SUBUNIT ABC) protein domain (PD953259) which is seen in Q7UK42_RHOBA.Residues 691-721 are identical to a (A DNA ATP-BINDING SUBUNIT EXCINUCLEASE EXCISION ABC UVRA REPAIR UVRABC) protein domain (PD782864) which is seen in UVRA_MICLU.Residues 722-801 are 84% similar to a (A DNA ATP-BINDING SUBUNIT EXCINUCLEASE EXCISION ABC UVRA REPAIR UVRABC) protein domain (PD001646) which is seen in Q6A9K3_PROAC.Residues 801-902 are 54% similar to a (DNA A EXCISION EXCINUCLEASE ATP-BINDING SUBUNIT SOS UVRA DNA-BINDING SYSTEM) protein domain (PD174439) which is seen in UVRA_CHLTR.Residues 802-902 are 65% similar to a (RESISTANCE ATP-BINDING DAUNORUBICIN) protein domain (PDA1A571) which is seen in Q836S6_ENTFA.Residues 802-864 are 65% similar to a (UV-REPAIR ATP-BINDING) protein domain (PDA18726) which is seen in Q70J73_BBBBB.Residues 802-902 are 52% similar to a (UVRA-LIKE TRANSPORTER ABC) protein domain (PDA1A825) which is seen in Q6A9D4_PROAC.Residues 821-854 are 96% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD565575) which is seen in UVRA_MYCTU.Residues 823-901 are 64% similar to a (LIN1813) protein domain (PD661935) which is seen in Q92AV6_LISIN.Residues 869-902 are 97% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD001034) which is seen in Q8FTQ6_COREF.","","No significant hits to the PDB database (E-value < E-10).","Residues 647 to 921 (E_value = 6.3e-31) place ANA_0697 in the ABC_tran family which is described as ABC transporter.","","ABC, A subunit (uvrA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0698","741682","739670","2013","9.75","17.28","70041","GTGCTCGTCCTGTCGGCCGGGGTCAGTCTGCTGGCTCTCGTCTGGGACTACATTCCCAACCCGGTCAAGATCCTGGGACTGGCACTCATCGCGGTCACAATGACAGCCTCCGGGGCACGCCTGGGGGTCAGTCATCCCCGTCATCGTGTTGCCGCGGCGACGATCACGGGAACCGGTGGGGGACTCGGTTTCGTCGCCATCGTGGGAGCCGTTCTTCTCGGTGGAATGCTCAGCCCAGAGCCCGCCCTGGCCCTGATGGCTTGCTGGGGCCTCGTGCTCCTGGCTGTGTCACACATGACGCGGGTGCTGTTCACCGCGGTCGTCTCCACCCTCGGCGCCCTGGTGACCATCGGGTTCGCAGTCAGTCACGTGGCGCGTCAGCCTCAGGCCGCACTCATCACGTGGCTGATGATCGGTATCTACGTCACGGTGCTGGCACTGACCTGCGTGGTCCTGTCCCGTCACACGGAGCGGATGAGGCTGGCCGCCTGGTATCCGGTGACATCGATGGTGGCAACGGCGACAGCCCTCATCGCCGCACCGATCCGGTCGATGCTGCGCGTCTCCACCATCGGCGGCACCAGCGTCATTCTCATCCTATGCGTGCTGCTGGTGTCTCAGACGATGCACGCGAGCACGCGGCTGTGGAGCATCGGGATCAAGACCTCGGGCTGGGACTGGGGTCCGACGGCGGTGGTCCTCATGCTGGAGTTCGGAAACCTGATGACGGAGCAGACGAGTCTCCACCTGGCACACAGCGTCGTCGTCATCACCTTCCTCCTCGAGCTCCTCCTGCTGGCCGCAGCGGCACTTGCGACACTCCCGCCCTACTGCCCCACTGATTGGCGCAGTACCATGGCGCTTGGACACGAAGTTGCGTTCTTCCCCCTCGTGCTGATTGGGATGATGATCATCGGCGACCCCCGAGTCCATCTCTTCGTCGTCGTCGCTGCGCTGCTGTGCCTGCTTCCGGCGATCTTGAACGCGAGAGCAGAACCGGCCCCGATCCTGGCCCTTCTCGGGACTGTGCCGATTCTCATGGCCCCGGGCTCTGTTCACTCCCGCGGCGACGTCTGGTCTCTCATCATCTCCGTGGTGATCTCGGTGCTCATGGTCGTCGTGGCCGAAGGGCTCGGTGACCGAGTCACGCACAGCTCTCCGCCCCCAGCCTCGTATGCCGCGCTGTCGCACGTTCAAGCACGGGCGCTGGCCCTGCGAGCGGCTCTGGCGACAGTGGCCTTCAATATCGCAGTCGTCGTTCCGTTCCTGGGCTCCGGCCTCGTGGAGGGCTTCCGTGGTCCCTGGGCGGGCCTGCGCATGGTTCCGGGTCTGGTGACGATCGCACTCATCGCGCTGGGGGCGGTCTCCAGTGACGCCACGCCTCTGCGAGTGCTCAGTGGACAGTGCCGAGGAGCCCGTTACCGGGTGGGTCCCCACGGCGAGGCTCTGCCCGATCCGACAGGGAGGCAGACGGGAGCACCGGCACCGTCCTGGATCATCTCGGGGATGGTGGCCGTGCTGGCACTGATGACGCTCTCGTGGGCTGAGGCCACCTCCAAGACGATAGGGACGCTGTTGCTGGTCGCCGTCGCTCTGGGGCTGGGAGCCAGCGCCACGTGGCTCCTACTTCCCTGGCGACGGAGTGCTGAGGTGTGCCTGAGCCTTGCGATCGGCAACTCGTTGCTCATGTGGTTCTCAGTCATGGTGGCCACCGAGATCGGTCCGGGCTCAGTCCTCATGTCAGTGCTGGTGCTGCTGACAGGTGGGGCCTGCATCGTCCTCGGCTTCAGGACACGCCTAACGATTCTGCGCCACTACGGACTGACCCTGGTACTCCTGTCCGTGCTCAAGCTCGCTGTTGTGGACGTGGCCTCGCAGAACTCGATCATTCGAGTCATCTCGCTGGCGGCCGCGGGCGTCGTCTGCTTTGTTCTCTCCCTGCTCTACAACCGCTTCGCGCAGGAGCAGCGTCGCGAGAGCAACCAGGCCCCCATGGGGCCCGGAAGCATCTGA","VLVLSAGVSLLALVWDYIPNPVKILGLALIAVTMTASGARLGVSHPRHRVAAATITGTGGGLGFVAIVGAVLLGGMLSPEPALALMACWGLVLLAVSHMTRVLFTAVVSTLGALVTIGFAVSHVARQPQAALITWLMIGIYVTVLALTCVVLSRHTERMRLAAWYPVTSMVATATALIAAPIRSMLRVSTIGGTSVILILCVLLVSQTMHASTRLWSIGIKTSGWDWGPTAVVLMLEFGNLMTEQTSLHLAHSVVVITFLLELLLLAAAALATLPPYCPTDWRSTMALGHEVAFFPLVLIGMMIIGDPRVHLFVVVAALLCLLPAILNARAEPAPILALLGTVPILMAPGSVHSRGDVWSLIISVVISVLMVVVAEGLGDRVTHSSPPPASYAALSHVQARALALRAALATVAFNIAVVVPFLGSGLVEGFRGPWAGLRMVPGLVTIALIALGAVSSDATPLRVLSGQCRGARYRVGPHGEALPDPTGRQTGAPAPSWIISGMVAVLALMTLSWAEATSKTIGTLLLVAVALGLGASATWLLLPWRRSAEVCLSLAIGNSLLMWFSVMVATEIGPGSVLMSVLVLLTGGACIVLGFRTRLTILRHYGLTLVLLSVLKLAVVDVASQNSIIRVISLAAAGVVCFVLSLLYNRFAQEQRRESNQAPMGPGSI$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[24-44]?$ $\"[53-73]?$ $\"[79-97]?$ $\"[102-122]?$ $\"[132-152]?$ $\"[162-180]?$ $\"[186-206]?$ $\"[250-272]?$ $\"[310-328]?$ $\"[333-353]?$ $\"[359-379]?$ $\"[403-425]?$ $\"[435-455]?$ $\"[495-515]?$ $\"[521-543]?$ $\"[552-570]?$ $\"[576-596]?$ $\"[606-624]?$ $\"[628-648]?$	transmembrane_regions

InterPro
IPR002618
Family

UTP--glucose-1-phosphate uridylyltransferase
PTHR11952	$\"[30-444]T$	UDP- GLUCOSE PYROPHOSPHORYLASE
PF01704	$\"[11-426]T$	UDPGP

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[27-354]T$	no description
PIRSF000806	$\"[1-444]T$	UTP--glucose-1-phosphate uridylyltransferase
PTHR11952:SF1	$\"[30-444]T$	UTP-GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE 2 (UDP- GLUCOSE PYROPHOSPHORYLASE 2)

","No hits to the COGs database.","***** IPB002618 (UTP--glucose-1-phosphate uridylyltransferase) with a combined E-value of 1.6e-95. IPB002618A 58-80 IPB002618B 90-130 IPB002618C 141-157 IPB002618D 175-216 IPB002618E 264-290 IPB002618F 323-363 IPB002618G 381-426","Residues 47-432 are 79% similar to a (PYROPHOSPHORYLASE TRANSFERASE NUCLEOTIDYLTRANSFERASE UDP-GLUCOSE URIDYLYLTRANSFERASE UTP--GLUCOSE-1-PHOSPHATE UGPASE UDPGP KINASE MULTIGENE) protein domain (PD004424) which is seen in Q6AAH5_PROAC.","","-57% similar to PDB:2OEF Open and Closed Structures of the UDP-Glucose Pyrophosphorylase from Leishmania major (E_value = 3.4E_92);-57% similar to PDB:2OEG Open and Closed Structures of the UDP-Glucose Pyrophosphorylase from Leishmania major (E_value = 3.4E_92);-55% similar to PDB:1Z90 X-ray structure of gene product from arabidopsis thaliana at3g03250, a putative UDP-glucose pyrophosphorylase (E_value = 8.6E_64);-55% similar to PDB:2ICX Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UTP (E_value = 8.6E_64);-55% similar to PDB:2ICY Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UDP-glucose (E_value = 8.6E_64);","Residues 11 to 426 (E_value = 1.5e-66) place ANA_0701 in the UDPGP family which is described as UTP--glucose-1-phosphate uridylyltransferase.","","uridylyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0707","744718","746874","2157","7.98","5.48","77972","ATGGCCGACCCTTCGACGTACCGTCCTGCCCCGGGCGAGATCCCCACGTCCCCGGGGGTCTACCGGTTCCTGGACGGGCAGGGACGGGTCATCTACGTCGGCAAGGCCAAGAACCTGCGTCAGCGCCTGTCCAACTACTTCCAGGACCTCGCCGCACTGCACCCGCGCACCCAGAAGATGGTCACCACCGCATGCGCGGTGGAATGGACGGTCGTGTCCACCGAGGTGGAGTCCCTGGCCCTGGAGTACTCCTGGATCAAGGAGTTCAACCCCCGTTTCAACGTCATGTACAAGGACGACAAGTCCTACCCCTACCTGGCGGTGACGATGGGGGAGACCTACCCCCGCGTCCAGGTGGTCCGCGGGGCCCGCAAACCGGGAACCCGCTACTTCGGTCCCTTCGTCCAGGCCTGGTCCATCCGCGAGACCGTCGAGCAGCTGCTGCGGGTCTTCCCGGTGCGTTCCTGCTCGGCCGGCGTCTTCCGCCGTGCCCAGGCCTCGGGGCGTCCCTGCCTGCTGGGATACATCGACAAGTGCTCGGCCCCCTGCGTGGGCCGCATCAGCCCGCAGGACCATCGGGCGCTGGCTGAGGACTTCTGCGCCTTCATGGCCGGTCGCACCGGCCCCTACCTGCGCCAGGTCGAGGCTGAGATGAAGGCGGCTGCCGCCGCCCTCGATTTCGAGAAGGCCGCCCGCCTGCGTGACGACGCCGCCGCACTGCGCAAGGTCATCGAGGGCAACGCCGTCGTCCTTCCCGACGCGACCGACGCCGACGTCTTCGCCCTGGTCCGCGACGAGCTCGAGGCCGCCGTCCAGGTCTTCCACGTCCGCGGCGGCCGGGTGCGCGGGCAGCGCGGCTGGGTCGTGGACCTCATCGACGACGCCGGGGACGCCGAGCTCATCGAGCGCCTCCTCGAACAGGTCTACGCCTCCCTCGTTGATCCGGCCGACGCCGGCGCCGTCCACCACAGTGGCGCCCCCACCTCCTCGGGCACCACCACCTCCGTCGGGGTGGGGGACCGTGCCCCCTCCAGCCCTCAGCCCCGCAGCGGCCCCAACGGTTCCAACGGTGACGCCTCCCGGCGTAAGGGAGAGTCGGCGGCCACGAGCGTCGACGACGTCGCCCACACCGCCACCACGGCGGTGCCCAAGGAGATCCTGGTTCCCGAGCTGCCCAGCAATGCCGCCACCGTGCGAACCTGGTTGTCCGGCCTGCGCGGAGCGAAGGTTGACCTGCGCGTCCCGCAGCGCGGCGACAAGGCCGCCCTCATGGATACGGTGCGCAAGAACGCGCATGAGGCTCTGCGGCTGCACAAGACCCGTCGGGCGGGGGATCTCACCCAGCGCGCCCTAGCCCTCGATGAGCTCGCCGAGGCCCTCGATCTGCCCGAGGCGCCCCTGCGCGTCGAGTGCTACGACATCTCCCACACCCAGGGCACCTACCAGGTCGGCTCCATGGTCGTCTTCGAGGACGGTACGCCGCGCAAGTCCGACTACCGGCGCTTCACTGTGCGCGGCCAGGATGGCAGCGGCGCCGCTGACGACACCGCCGCCATGCACGAGGTCCTCACCCGCCGGTTCAAACGCCTCATCGCCGAGCAGGGGCGCGGTGAGGCCGCTGCTCGGGCTGCGCAGGAGATCGAGGATGTCGAGGGCATTGCCGTCGTCTCCGGGCCCATCGATCCTGAGACCGGCAAGGCTCGGCGCTTCTCCTACGCGCCCGGGCTGGTCGTCGTCGACGGCGGGCTGCCGCAGGTCAATGCCGCGCGCACCGTGCTCGATGAGCTCGGCATCGACGTGCCGCTCATCGGCCTGGCCAAGCGTCTGGAGGAGGTGTGGGTGCCGGGGGAGGAGTTCCCCGTTATCCTGCCGCGCACGTCGCCCGCCCTCTACCTGCTTCAGCACCTGCGCGACGAGTCCCACCGCTTCGCCATCACCCACCACCGCAAGAAGCGCTCGGCCGGCATGACCCGCTCCGTCCTGGATGGTATCCCCGGCCTGGGACCGGCGCGTCAGGCGGCCCTCCTGCGGGAGTTCGGCTCAGTCACGCGCATCCGGCAGGCCGACGTTGATGACATCACCCGCGTCAAGGGCATCGGACCGGCTCTGGCAGGTACTATCTTGGCTCACCTCAACAGTCCAGGTACTGAACAATAG","MADPSTYRPAPGEIPTSPGVYRFLDGQGRVIYVGKAKNLRQRLSNYFQDLAALHPRTQKMVTTACAVEWTVVSTEVESLALEYSWIKEFNPRFNVMYKDDKSYPYLAVTMGETYPRVQVVRGARKPGTRYFGPFVQAWSIRETVEQLLRVFPVRSCSAGVFRRAQASGRPCLLGYIDKCSAPCVGRISPQDHRALAEDFCAFMAGRTGPYLRQVEAEMKAAAAALDFEKAARLRDDAAALRKVIEGNAVVLPDATDADVFALVRDELEAAVQVFHVRGGRVRGQRGWVVDLIDDAGDAELIERLLEQVYASLVDPADAGAVHHSGAPTSSGTTTSVGVGDRAPSSPQPRSGPNGSNGDASRRKGESAATSVDDVAHTATTAVPKEILVPELPSNAATVRTWLSGLRGAKVDLRVPQRGDKAALMDTVRKNAHEALRLHKTRRAGDLTQRALALDELAEALDLPEAPLRVECYDISHTQGTYQVGSMVVFEDGTPRKSDYRRFTVRGQDGSGAADDTAAMHEVLTRRFKRLIAEQGRGEAAARAAQEIEDVEGIAVVSGPIDPETGKARRFSYAPGLVVVDGGLPQVNAARTVLDELGIDVPLIGLAKRLEEVWVPGEEFPVILPRTSPALYLLQHLRDESHRFAITHHRKKRSAGMTRSVLDGIPGLGPARQAALLREFGSVTRIRQADVDDITRVKGIGPALAGTILAHLNSPGTEQ$","Excinuclease ABC, C subunit","Cytoplasm","excinuclease ABC, C subunit","K03703 excinuclease ABC subunit C","excinuclease ABC, C subunit","","Verhoeven E.E., Van kesteren M., Turner J.J., Van der marel G.A., Van boom J.H., Moolenaar G.F., Goosen N. The C-terminal region of Escherichia coli UvrC contributes to the flexibility of the UvrABC nucleotide excision repair system. Nucleic Acids Res 2002. 30(11):2492-2500. PMID: 12034838","","","

InterPro
IPR000305
Domain

Excinuclease ABC, C subunit, N-terminal
PF01541	$\"[17-100]T$	GIY-YIG
SM00465	$\"[17-99]T$	GIYc
PS50164	$\"[18-95]T$	UVRC_1

InterPro
IPR000445
Domain

Helix-hairpin-helix motif
PF00633	$\"[681-710]T$	HHH

InterPro
IPR001162
Domain

Excinuclease ABC, C subunit, C-terminal
PD005870	$\"[468-660]T$	Q741E5_MYCPA_Q741E5;
PF08459	$\"[456-645]T$	UvrC_HhH_N
PS50165	$\"[259-593]T$	UVRC_2

InterPro
IPR001943
Domain

UvrB/UvrC protein
PF02151	$\"[208-243]T$	UVR
PS50151	$\"[208-243]T$	UVR

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[659-678]T$ $\"[691-710]T$	HhH1

InterPro
IPR004791
Family

Excinuclease ABC, C subunit
TIGR00194	$\"[7-692]T$	uvrC: excinuclease ABC, C subunit

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.20	$\"[658-713]T$	no description
G3DSA:4.10.860.10	$\"[186-248]T$	no description
PTHR14025	$\"[664-717]T$	FAMILY NOT NAMED
PTHR14025:SF2	$\"[664-717]T$	gb def: Helicase

","BeTs to 20 clades of COG0322COG name: Nuclease subunit of the excinuclease complexFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0322 is -om----qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000305 (Excinuclease ABC, C subunit, N-terminal) with a combined E-value of 7.9e-35. IPB000305A 32-46 IPB000305B 75-94 IPB000305C 169-183 IPB000305D 574-583 IPB000305E 637-646","Residues 25-58 are 88% similar to a (C DNA SUBUNIT EXCINUCLEASE EXCISION ABC UVRC NUCLEASE REPAIR SOS) protein domain (PD482363) which is seen in UVRC_STRCO.Residues 79-186 are 87% similar to a (DNA C EXCINUCLEASE SUBUNIT EXCISION ABC UVRC NUCLEASE REPAIR SOS) protein domain (PD013358) which is seen in UVRC_STRCO.Residues 244-436 are 52% similar to a (C DNA EXCINUCLEASE SUBUNIT EXCISION ABC NUCLEASE UVRC REPAIR SOS) protein domain (PD002762) which is seen in UVRC_MYCLE.Residues 468-660 are 67% similar to a (C DNA EXCINUCLEASE SUBUNIT EXCISION ABC NUCLEASE UVRC REPAIR SOS) protein domain (PD005870) which is seen in Q741E5_MYCPA.Residues 661-704 are 77% similar to a (DNA C EXCINUCLEASE SUBUNIT EXCISION ABC RECOMBINATION REPAIR UVRC NUCLEASE) protein domain (PD686595) which is seen in Q8NQ55_CORGL.","","-54% similar to PDB:2NRT Crystal structure of the C-terminal half of UvrC (E_value = 1.2E_36);-54% similar to PDB:2NRV Crystal structure of the C-terminal half of UvrC (E_value = 1.2E_36);-54% similar to PDB:2NRW Crystal structure of the C terminal half of UvrC (E_value = 1.2E_36);-54% similar to PDB:2NRX Crystal structure of the C-terminal half of UvrC, in the presence of sulfate molecules (E_value = 1.2E_36);-54% similar to PDB:2NRZ Crystal structure of the C-terminal half of UvrC bound to its catalytic divalent cation (E_value = 1.2E_36);","Residues 17 to 100 (E_value = 3.8e-27) place ANA_0707 in the GIY-YIG family which is described as GIY-YIG catalytic domain.Residues 208 to 243 (E_value = 2.2e-09) place ANA_0707 in the UVR family which is described as UvrB/uvrC motif.Residues 456 to 645 (E_value = 2.3e-88) place ANA_0707 in the UvrC_HhH_N family which is described as UvrC Helix-hairpin-helix N-terminal.Residues 681 to 710 (E_value = 0.00012) place ANA_0707 in the HHH family which is described as Helix-hairpin-helix motif.","","ABC, C subunit (uvrC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0708","746925","747137","213","6.64","-0.08","7141","ATGAGGATCTCCGCCCGCAACCAGCTGCCCGGCACCGTCGTCTCCATCGAGAAGGGCGCCGTCAACGGCGTCGTCAAGATCGAGGTCGCCCCCGGCGTCATCATCACCTCCTCCATCACCAACGCGGCCATCGAGGAGCTCGAGCTGGCAGAGGGCAAGAAGGCGGTCGCCGTCGTCAAGGCCTCCTCGGTCATGGTGGGTCTCCAGGACTGA","MRISARNQLPGTVVSIEKGAVNGVVKIEVAPGVIITSSITNAAIEELELAEGKKAVAVVKASSVMVGLQD$","Molybdopterin-binding protein","Cytoplasm","molybdenum transport protein ModE","molybdenum-pterin binding","TOBE domain protein","","Koonin E.V., Wolf Y.I., Aravind L. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 2000. 54:245-275. PMID: 10829230","","","

InterPro
IPR004606
Domain

Molybdenum-pterin binding
TIGR00638	$\"[1-70]T$	Mop: molybdenum-pterin binding domain

InterPro
IPR005116
Domain

TOBE
PF03459	$\"[3-66]T$	TOBE

noIPR
unintegrated

unintegrated
G3DSA:2.40.50.100	$\"[1-70]T$	no description

","BeTs to 3 clades of COG3585COG name: Molybdopterin-binding proteinFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG3585 is ---------------f-h---j----Number of proteins in this genome belonging to this COG is 1","***** IPB003725 (Molybdenum-binding protein, N-terminal) with a combined E-value of 3.4e-12. IPB003725C 35-66","Residues 6-68 are similar to a (MOLYBDENUM MODE BINDING TRANSCRIPTIONAL REPEAT REGULATOR REPRESSOR MOLYBDENUM-BINDING MOLYBDENUM-PTERIN MOLYBDO-PTERIN) protein domain (PD482277) which is seen in Q6N0P3_RHOPA.Residues 11-66 are similar to a (BINDING MOLYBDENUM-PTERIN MULTIGENE FAMILY MOLYBDENUM 3D-STRUCTURE METAL I MOPI PROBABLE) protein domain (PD818188) which is seen in Q9CP44_PASMU.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 66 (E_value = 1.7e-16) place ANA_0708 in the TOBE family which is described as TOBE domain.","","transport protein ModE (mopI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0709","747257","748714","1458","5.20","-17.41","54451","ATGACCACACCATCGCCCGACCCCGACCTGCGCTTCCCCGGCGGCTTCCTGTGGGGCGGGGCCACCGCCGCCAACCAGATCGAGGGCGCTTACAACGAGGACGGCAAGGGCCTGTCCGTTCAGGACGTCATGCCCCGGGGCATCCTGGCCCCGCCCACCCAGGCCCCCACACCGGACAACCTCAAGCTTGAAGCCATCGACTTCTACCACCGTTACGTCGAGGACATCGCCCTGCTGGCGGAGATGGGCTTCAAGGTCTTCCGCTTCTCCATCGCCTGGAGCCGTATCTTCCCGCTCGGTGACGAGACCGAGCCCAACGAGGAGGGGCTGGCCTTCTACGACCGGGTCCTCGACGAGCTCGAGAAGCACGGCATCGAGCCGCTGGTCACCATCAGCCACTACGAGACCCCGCTCCACCTGGCCCGCACCTATGACGGCTGGACCGACCGCCGCCTCATCGGCTTCTTCGAGCGCTACGCCCGCACCCTGTTCGAGCGATACGGCAAGCGGGTCAGGTACTGGCTCACCTTCAACGAGATCAACTCCGTCCTCCACGAGCCCTTCCTGTCCGGCGGCATCGCCACCCCCAAGGACAGGCTCAGCGAGCAGGACCTCTACCAGGCCATCCACCACGAGCTCGTCGCCTCCGCTGCCGCCACGAGGATCGCCCACGAGGTCAACCCCGACATCCAGGTCGGCTGCATGATCCTGGCCGTGCCCACCTACCCGCTGACCCCCGATCCCCGTGACGTCTGGGCCGCCAAGCAGGCCGAGCGCGCCAACTACGCCTTCGGGGACCTCCACGTGCGCGGCGAGTACCCCGGCTACCTGCTGCGTTCCCTGCGAGACAAGGGCATCAAGCTGGAGATCACCGAGGAGGACCGCGCGCTGCTGCGGGAGCACACCGTCGACTTCGTCTCCTTCTCCTACTACATGTCCGTGTGCGAGACCGTTACCCAGCCGGCCGAGGCCGGCCGGGGCAACCTTATGGGCGGCGTTCCCAATCCCACCCTCGAGGCCTCCGAGTGGGGGTGGCAGATCGACCCGGCGGGCCTGCGCACCATCCTCAACGACTACTGGGACCGCTGGGGTAAGCCCCTGTTCATTGTCGAGAACGGTCTGGGAGCCAAGGATGTTCTCGTTGACGGCCCCAACGGCCCCACGGTTGAGGACGACTACCGCATCGCCTACATGAACGACCACCTGGTCCAGGTCGCCCAGGCCATCGCCGACGGCGTCGAGGTCCTGGGCTACACCTCCTGGGGCTGCATCGACCTGGTCTCGGCCTCCACCGCCCAGATGTCCAAGCGCTACGGCTTCATCTACGTGGACCGCGACGACGACGGCAGCGGCACCCTGGCCCGCTACCGTAAGAAGTCCTTCGGCTGGTACCGCGACGTCATCGCCTCCAACGGCGCCCGCCTCGTACCTGCGGCGCAGAAACCGCCACGGGGATAG","MTTPSPDPDLRFPGGFLWGGATAANQIEGAYNEDGKGLSVQDVMPRGILAPPTQAPTPDNLKLEAIDFYHRYVEDIALLAEMGFKVFRFSIAWSRIFPLGDETEPNEEGLAFYDRVLDELEKHGIEPLVTISHYETPLHLARTYDGWTDRRLIGFFERYARTLFERYGKRVRYWLTFNEINSVLHEPFLSGGIATPKDRLSEQDLYQAIHHELVASAAATRIAHEVNPDIQVGCMILAVPTYPLTPDPRDVWAAKQAERANYAFGDLHVRGEYPGYLLRSLRDKGIKLEITEEDRALLREHTVDFVSFSYYMSVCETVTQPAEAGRGNLMGGVPNPTLEASEWGWQIDPAGLRTILNDYWDRWGKPLFIVENGLGAKDVLVDGPNGPTVEDDYRIAYMNDHLVQVAQAIADGVEVLGYTSWGCIDLVSASTAQMSKRYGFIYVDRDDDGSGTLARYRKKSFGWYRDVIASNGARLVPAAQKPPRG$","Glycoside hydrolase, family 1","Cytoplasm, Extracellular","beta-glucosidase","6-phospho-beta-glucosidase ","glycoside hydrolase, family 1","Chen L, Ma L, Park NH, Shi W.Cariogenic actinomyces identified with a beta-glucosidase-dependent green color reaction to Gardenia jasminoides extract.J Clin Microbiol. 2001 Aug;39(8):3009-12.PMID: 11474036","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR001360
Family

Glycoside hydrolase, family 1
PR00131	$\"[302-316]T$ $\"[367-375]T$ $\"[391-402]T$ $\"[412-429]T$ $\"[437-449]T$	GLHYDRLASE1
PTHR10353	$\"[11-477]T$	GLYCOSIDE HYDROLASES
PF00232	$\"[8-473]T$	Glyco_hydro_1
PS00572	$\"[367-375]T$	GLYCOSYL_HYDROL_F1_1
PS00653	$\"[16-30]T$	GLYCOSYL_HYDROL_F1_2

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[11-472]T$	no description

noIPR
unintegrated

unintegrated
PTHR10353:SF3	$\"[11-477]T$	BETA-GLUCOSIDASE

","BeTs to 5 clades of COG2723COG name: Beta-glucosidase/6-phospho-beta-glucosidase/Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2723 is ---pk------lb-e-g----j----Number of proteins in this genome belonging to this COG is 1","***** IPB001360 (Glycoside hydrolase, family 1) with a combined E-value of 6.4e-101. IPB001360A 12-42 IPB001360B 67-100 IPB001360C 106-138 IPB001360D 169-180 IPB001360E 366-375 IPB001360F 391-402 IPB001360G 411-438 IPB001360H 455-464***** IPB011580 (6-phospho-beta-galactosidase, eukaryotic) with a combined E-value of 7.3e-17. IPB011580A 5-40 IPB011580B 146-200","Residues 1-179 are 55% similar to a (GLYCOSIDASE HYDROLASE BETA-GLUCOSIDASE) protein domain (PD118549) which is seen in Q46043_CELFI.Residues 9-447 are 47% similar to a (GLYCOSIDASE MALE-SPECIFIC HYDROLASE BETA-GLYCOSIDASE) protein domain (PDA0I423) which is seen in Q8WQL9_LEUMA.Residues 10-183 are 50% similar to a (HYDROLASE GLYCOSIDASE BETA-GLUCOSIDASE) protein domain (PD649792) which is seen in Q55000_STRRO.Residues 11-444 are 44% similar to a (CG9701-PA LP05116P GLYCOSIDASE HYDROLASE) protein domain (PD612818) which is seen in Q9VV98_DROME.Residues 11-39 are 93% similar to a (HYDROLASE GLYCOSIDASE 6-PHOSPHO-BETA-GLUCOSIDASE BETA-GLUCOSIDASE HYDROLASE FAMILY LMO0917 ASCB GLYCOSYL LIN0918) protein domain (PD785455) which is seen in Q724E7_LISMF.Residues 11-343 are 47% similar to a (A PROBABLE BGLA BETA-GLUCOSIDASE) protein domain (PDA1A2B5) which is seen in Q6AKE8_BBBBB.Residues 11-179 are 56% similar to a (HYDROLASE GLYCOSIDASE BETA-GLUCOSIDASE) protein domain (PD237773) which is seen in Q9UUQ3_ORPSP.Residues 12-311 are 50% similar to a (HYDROLASE GLYCOSIDASE BETA-GLUCOSIDASE) protein domain (PDA190V4) which is seen in O64880_ARATH.Residues 12-469 are 45% similar to a (GLYCOSIDASE HYDROLASE 8_apos;-O-BETA-GLUCOSIDE DALCOCHININ BETA-GLUCOSIDASE) protein domain (PDA0I422) which is seen in Q9SPK3_EEEEE.Residues 12-447 are 44% similar to a (HYDROLASE HYDROXYISOURATE GLYCOSIDASE) protein domain (PD649793) which is seen in Q8S3J3_SOYBN.Residues are similar to a () protein domain () which is seen in .Residues 15-468 are 48% similar to a (HYDROLASE ISOFORM GLYCOSIDASE PRUNASIN PRECURSOR PHA SIGNAL) protein domain (PDA0I411) which is seen in Q9M5X5_PRUSE.Residues 206-468 are 43% similar to a (16-O-GLUCOHYDROLASE GLYCOSIDASE CARDENOLIDE HYDROLASE) protein domain (PD194055) which is seen in Q9ZPB6_DIGLA.Residues 181-234 are 92% similar to a (HYDROLASE GLYCOSIDASE BETA-GLUCOSIDASE) protein domain (PD737273) which is seen in Q9AEN6_ACTNA.Residues 188-295 are 53% similar to a (HYDROLASE PHOSPHO-BETA-GLUCOSIDASE GLYCOSIDASE BGLB) protein domain (PD737277) which is seen in Q9X564_ENTFC.Residues 204-304 are 49% similar to a (BETA-GLUCOSIDASE) protein domain (PD976428) which is seen in Q74LJ1_LACJO.Residues 206-468 are 43% similar to a (16-O-GLUCOHYDROLASE GLYCOSIDASE CARDENOLIDE HYDROLASE) protein domain (PD194055) which is seen in Q9ZPB6_DIGLA.Residues 235-288 are 96% similar to a (HYDROLASE GLYCOSIDASE 6-PHOSPHO-BETA-GLUCOSIDASE BETA-GLUCOSIDASE BETA-GLUCOSIDASE-FRAGMENT GLUCOHYDROLASE DEGRADATION CELLULOSE CELLOBIASE GLUCOSIDE) protein domain (PD669393) which is seen in Q9AEN6_ACTNA.Residues 301-353 are 96% similar to a (HYDROLASE GLYCOSIDASE BETA-GLUCOSIDASE BETA-GLUCOSIDASE-FRAGMENT GLUCOHYDROLASE DEGRADATION CELLULOSE CELLOBIASE GLUCOSIDE PHOSPHO-CELLOBIASE) protein domain (PDA1F1S1) which is seen in Q9AEN6_ACTNA.Residues 355-475 are 52% similar to a (BETA-GLUCOSIDASE-FRAGMENT) protein domain (PD946668) which is seen in Q6M213_CORGL.Residues 356-475 are 98% similar to a (HYDROLASE GLYCOSIDASE BETA-GLUCOSIDASE GLUCOHYDROLASE DEGRADATION CELLULOSE CELLOBIASE GLUCOSIDE PHOSPHO-CELLOBIASE AMYGDALASE) protein domain (PD822444) which is seen in Q9AEN6_ACTNA.","","-53% similar to PDB:1UYQ MUTATED B-GLUCOSIDASE A FROM PAENIBACILLUS POLYMYXA SHOWING INCREASED STABILITY (E_value = 6.6E_65);-53% similar to PDB:1BGA BETA-GLUCOSIDASE A FROM BACILLUS POLYMYXA (E_value = 1.5E_64);-53% similar to PDB:1BGG GLUCOSIDASE A FROM BACILLUS POLYMYXA COMPLEXED WITH GLUCONATE (E_value = 1.5E_64);-53% similar to PDB:1E4I 2-DEOXY-2-FLUORO-BETA-D-GLUCOSYL/ENZYME INTERMEDIATE COMPLEX OF THE BETA-GLUCOSIDASE FROM BACILLUS POLYMYXA (E_value = 4.3E_64);-53% similar to PDB:1TR1 CRYSTAL STRUCTURE OF E96K MUTATED BETA-GLUCOSIDASE A FROM BACILLUS POLYMYXA, AN ENZYME WITH INCREASED THERMORESISTANCE (E_value = 4.3E_64);","Residues 8 to 473 (E_value = 1.1e-163) place ANA_0709 in the Glyco_hydro_1 family which is described as Glycosyl hydrolase family 1.",""," ","","1","","","","","","","","","","","","Thu Jul 26 15:10:01 2007","","","","Thu Jul 26 15:10:01 2007","Thu Jul 26 15:10:01 2007","Thu Jul 26 15:10:01 2007","","Thu Jul 26 15:10:01 2007","Thu Jul 26 15:10:01 2007","","","","","yes","","" "ANA_0710","750028","748742","1287","5.25","-12.17","45239","ATGAGCTCCTCCCCCATGTCCGACCAGGCTCTCTCATGCCAGTTCACGCCTCAGGAGACGCCGATGCGTCGGCCCACCGCCCCAGTGCTGGGTACGCCCTGGACCAGCAGCGCAACGAAGGTGGCGCTGCTGGGCGCCGGTGAGATCGGCAAGGAGGTGGCGATCGCTCTGACCCGCCTGGGGGTGGAGGTCACGGCGATCGACCGCTATGAGGGGGCTCCGGCCCAGCAGGTGGCGCACAACGCCATGACGGTGGACATGAGCGACCCCGAGGCGCTGACGGCCGCCATCCGCGCCAGCGGTGCCGCCGTCGTGATCCCGGAGATCGAGGCGCTGGCCACCGACGCCCTGGCGGCGCTGGAGAGCGCCGGCGAGGTGCAGGTGGTACCGACCGCCCGTGCAGTGCAGCTGACGATGAATCGTGAGGGCATCCGACGCCTGGCGGCTGAGGAGCTGGGGCTGGCGACCAGTCCCTACGCCTTCGCCTCGTCCTTAGACGAGCTGCGCGCAGGTGCTCAGCAAGTGGGCTTTCCGTGTGTGGTCAAACCGGTCATGTCCTCATCCGGGCACGGCCAGTCCGTGGTACGCGGGCCGCAGGACCTGGAGGCGGCCTGGCGCTACGCGGCGGCCGACGGGCGCGTGGACCGAGGCCGGGTCATCGTGGAGGGATTCGTGCGTTTCGACACCGAGATCACGCTGCTCACGGTGCGCTGGCGTCATCCCGGCACCGGGGAGACGGTGACGAGCTTCTGCGAGCCGATCGGGCACCGGCAGGTCGACGGGGACTATGTGGAGTCCTGGCAGCCGCAGCCCCTGAGCCCGGTGGCCCTGGAACGGGCCCAGCAGGTGGCCGAGCGCGTGACCGCGGCGCTGGGCGGCTGGGGCCTGTTCGGGGTGGAGCTGTTCATCTGCGGGGAGGAGGTTCTCTTCTCCGAGGTCTCCCCGCGCCCCCATGACACCGGCCTGGTGACACTGGCGAGCCAGCGCCTGAGCGAGTTCGAGCTGCACGCCCGCGCCCTGCTGGGGCTGCCCGTCGACACCGCGCTGCGCTCCCCCGGCGCCTCGGTGACCATCAAAGCGACGGGAGAGTCCGCGCCGGGTGAGGGCGTGCGTTTCGCGGGTCTTGATGAGGCGCTCGCTCATGAGGGCGCGGATCTGCGACTCTTCGGCAAGCCGGTGGCTCACGAGGGTCGGCGCCTGGGCGTTGTCGTGGCCTACGCCGACGACGTGCAGGTCGCCCGAGATCGGGCGCGGTCCGCCGCCCAGGCGATCCGTCCCAGCGTCTGA","MSSSPMSDQALSCQFTPQETPMRRPTAPVLGTPWTSSATKVALLGAGEIGKEVAIALTRLGVEVTAIDRYEGAPAQQVAHNAMTVDMSDPEALTAAIRASGAAVVIPEIEALATDALAALESAGEVQVVPTARAVQLTMNREGIRRLAAEELGLATSPYAFASSLDELRAGAQQVGFPCVVKPVMSSSGHGQSVVRGPQDLEAAWRYAAADGRVDRGRVIVEGFVRFDTEITLLTVRWRHPGTGETVTSFCEPIGHRQVDGDYVESWQPQPLSPVALERAQQVAERVTAALGGWGLFGVELFICGEEVLFSEVSPRPHDTGLVTLASQRLSEFELHARALLGLPVDTALRSPGASVTIKATGESAPGEGVRFAGLDEALAHEGADLRLFGKPVAHEGRRLGVVVAYADDVQVARDRARSAAQAIRPSV$","Phosphoribosylglycinamide formyltransferase 2","Cytoplasm","phosphoribosylglycinamide formyltransferase 2","phosphoribosylglycinamide formyltransferase 2 ","phosphoribosylglycinamide formyltransferase 2","","Galperin M.Y., Koonin E.V. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 1997. 6(12):2639-2643. PMID: 9416615Fan C., Moews P.C., Walsh C.T., Knox J.R. Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. Science 1994. 266(5184):439-443. PMID: 7939684Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Fan C., Moews P.C., Shi Y., Walsh C.T., Knox J.R. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(4):1172-1176. PMID: 7862655","","","

InterPro
IPR003135
Domain

ATP-grasp fold, ATP-dependent carboxylate-amine ligase-type
PF02222	$\"[140-328]T$	ATP-grasp

InterPro
IPR005097
Family

Saccharopine dehydrogenase
PF03435	$\"[41-106]T$	Saccharop_dh

InterPro
IPR005862
Family

Phosphoribosylglycinamide formyltransferase 2
PTHR23047:SF2	$\"[97-428]T$	PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE 2
TIGR01142	$\"[40-427]T$	purT: phosphoribosylglycinamide formyltrans

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[146-341]T$	ATP_GRASP

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[202-426]T$	no description

InterPro
IPR013817
Domain

Pre-ATP-grasp fold
G3DSA:3.40.50.20	$\"[28-149]T$	no description

noIPR
unintegrated

unintegrated
PTHR23047	$\"[97-428]T$	PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE ATPASE-SUBUNIT

","BeTs to 8 clades of COG0027COG name: Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase)Functional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0027 is --m-k-----r-bcefgh--------Number of proteins in this genome belonging to this COG is 1","***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 2.4e-06. IPB013027C 40-65 IPB013027A 40-62","Residues 41-156 are similar to a (PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE SUBUNIT ATPASE LYASE TRANSFERASE PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE CARBOXYLASE TRANSFORMYLASE) protein domain (PD425067) which is seen in Q7WEY0_BORBR.Residues 140-283 are 51% similar to a (TRANSFERASE FORMYLTRANSFERASE PHOSPHORIBOSYLGLYCINAMIDE) protein domain (PD988322) which is seen in Q6NF44_CORDI.Residues 157-232 are 57% similar to a (TRANSFORMYLASE GAR TRANSFERASE 2.1.2.- FORMYLTRANSFERASE PURT PHOSPHORIBOSYLGLYCINAMIDE FORMATE-DEPENDENT PROBABLE GART) protein domain (PD651253) which is seen in Q73T48_MYCPA.Residues 173-225 are 84% similar to a (LIGASE SYNTHETASE D-ALANINE--D-ALANINE D-ALA-D-ALA WALL CELL D-ALANYLALANINE PEPTIDOGLYCAN SYNTHESIS B) protein domain (PD000755) which is seen in Q9HXP3_PSEAE.Residues 227-276 are 64% similar to a (TRANSFERASE TRANSFORMYLASE PHOSPHORIBOSYLGLYCINAMIDE GAR FORMYLTRANSFERASE LONG FORMYL 2.1.2.- GART 5_apos;-PHOSPHORIBOSYLGLYCINAMIDE) protein domain (PD890285) which is seen in Q9UY67_PYRAB.Residues 233-282 are 84% similar to a (FORMYLTRANSFERASE PHOSPHORIBOSYLGLYCINAMIDE TRANSFERASE TRANSFORMYLASE 2.1.2.- GAR FORMATE-DEPENDENT GART 5_apos;-PHOSPHORIBOSYLGLYCINAMIDE PROBABLE) protein domain (PD899537) which is seen in Q7W006_BORPE.Residues 284-358 are 85% similar to a (PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE SUBUNIT ATPASE LYASE TRANSFERASE PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE CARBOXYLASE TRANSFORMYLASE) protein domain (PD002772) which is seen in Q8FMB3_COREF.","","-64% similar to PDB:1EYZ STRUCTURE OF ESCHERICHIA COLI PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE COMPLEXED WITH MG AND AMPPNP (E_value = 5.5E_100);-64% similar to PDB:1EZ1 STRUCTURE OF ESCHERICHIA COLI PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE COMPLEXED WITH MG, AMPPNP, AND GAR (E_value = 5.5E_100);-64% similar to PDB:1KJ8 Crystal Structure of PurT-Encoded Glycinamide Ribonucleotide Transformylase in Complex with Mg-ATP and GAR (E_value = 5.5E_100);-64% similar to PDB:1KJ9 Crystal structure of purt-encoded glycinamide ribonucleotide transformylase complexed with Mg-ATP (E_value = 5.5E_100);-64% similar to PDB:1KJI Crystal structure of glycinamide ribonucleotide transformylase in complex with Mg-AMPPCP (E_value = 5.5E_100);","Residues 40 to 69 (E_value = 6.3e-05) place ANA_0710 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 41 to 106 (E_value = 2e-05) place ANA_0710 in the Saccharop_dh family which is described as Saccharopine dehydrogenase.Residues 140 to 328 (E_value = 8.5e-83) place ANA_0710 in the ATP-grasp family which is described as ATP-grasp domain.","","formyltransferase 2 (purT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0711","750149","751123","975","6.97","-0.15","35763","ATGCATGACGAGCGCCGCCCTCAGTCCTCCTCCGGCAAGCGCCAGCGGCTTCAGGACACGGTTCCCATTGAGATCCCCGCCCTCGATGAGGCGACTCCTCCGGTTCCCCCGGCGGAACGCCCCGAGATGATTATTGTCACGGGTATGTCCGGGGCGGGGCGCTCGCGCGCGGCCAACGCGCTGGAGGACCTCGACTGGTACGTCGTGGATAACCTGCCGCCCCAGCTGCTGCCGGCTCTGTCGGGAATGATGACGACGGTCGGCGCCGGTGTGCACCGGCTGGCCGCGGTGGTCGATGTGCGCAGTCGCGAGTTCTTCTCCCACTTCATGGACTATCTGCGCAAGGTCCGCAACAACGGCACCGACGTGAGGCTCATCTTCCTGGATGCCTCCGACGCCGTGCTGGTCAGACGCTTTGAGTCCTCTCGCCGACCCCACCCGTTGCAGGGCAGTGGCTCCGTCCTGGACGGGATTGAGCACGAGCGCACTCTCCTGGGGGGTTTGCGGGGCGTGGCCGACAGCGTCATCGACACCTCCAACTACTCCGTCCACGACCTCGCCCGGCGGGTGCGCGAGCTCGTGGCGCACGAGTCCGACCTGGCCCTGCGTATCAACGTCATGTCCTTCGGGTTCAAGTACGGCATTCCCCTGGACGCCGACCACGTTCTGGACGTGCGCTTCATTCCCAACCCCTACTGGGTCTCCGAGCTGCGCCACCTCACCGGACGTGACGCTCCGGTGGCCGACTACGTCTTCGCCCAGAAGGGGGCGGCGGCCTTCGTCGACGGCTACGCCGACCTGCTCATCCCCGCGCTCCCGCAGTACATCGATGAGCTCAAGCCCCACGTCACCCTGGCTGTGGGCTGCACCGGCGGCAAGCACCGTTCCGTGGCCTCGGCGGAGCGGCTCGGGGCCAGGTTGAGGCGCGGGGGCTTCGAGGTCGTTGTCCAGCACCGCGATCTGGGACGGGAGTAG","MHDERRPQSSSGKRQRLQDTVPIEIPALDEATPPVPPAERPEMIIVTGMSGAGRSRAANALEDLDWYVVDNLPPQLLPALSGMMTTVGAGVHRLAAVVDVRSREFFSHFMDYLRKVRNNGTDVRLIFLDASDAVLVRRFESSRRPHPLQGSGSVLDGIEHERTLLGGLRGVADSVIDTSNYSVHDLARRVRELVAHESDLALRINVMSFGFKYGIPLDADHVLDVRFIPNPYWVSELRHLTGRDAPVADYVFAQKGAAAFVDGYADLLIPALPQYIDELKPHVTLAVGCTGGKHRSVASAERLGARLRRGGFEVVVQHRDLGRE$","P-loop-containing kinase","Cytoplasm","nucleotide kinase","hypothetical protein","uncharacterised P-loop ATPase protein UPF0042","","","","","

InterPro
IPR005337
Family

P-loop ATPase protein
PF03668	$\"[42-324]T$	ATP_bind_2

","BeTs to 9 clades of COG1660COG name: Predicted P-loop-containing kinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1660 is ---------drlb-efghsn------Number of proteins in this genome belonging to this COG is 1","***** IPB005337 (Uncharacterised P-loop ATPase protein family UPF0042) with a combined E-value of 1.6e-42. IPB005337A 45-74 IPB005337B 208-242","Residues 44-197 are 73% similar to a (UPF0042 ATP-BINDING PTSN-PTSO P-LOOP YHBJ ORF4 PLU4044 5_apos;REGION PTSO FAMILY) protein domain (PD473567) which is seen in Q6AF48_BBBBB.Residues 204-320 are 70% similar to a (UPF0042 ATP-BINDING PTSN-PTSO P-LOOP YHBJ ORF4 PLU4044 5_apos;REGION PTSO FAMILY) protein domain (PD013996) which is seen in Y705_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 42 to 324 (E_value = 8.5e-119) place ANA_0711 in the ATP_bind_2 family which is described as P-loop ATPase protein family.","","kinase (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0712","751127","752137","1011","5.33","-12.43","35829","GTGGGAACCACGATCGATGCGGCGGGCTGGCCCCGCCGCGGTGAGGAGGGACCCGCCGTCGTCGCCCTGGGAGGCGGGCACGGACTGTCCGCCACGCTGCGGGCGCTGCGCCACGTCACCCACCGGCTCACCGCTGTCGTCACCGTCGCCGACGACGGAGGCTCCTCGGGACGCCTGCGCCGAGAGTTCGACTGTCTGCCGCCAGGAGACCTGAGAATGGCGCTGGCATCGCTCTGCGAGGACTCCGAGTGGGGCCTGACCTGGCGAGACGTGCTCCAGCACCGCTTCGAGGGGCAGGGCGAGCTCGACAATCACGCCCTGGGGAACCTGCTCATCCTGGCGCTGTGGCAGCTGCTGGGGGACGAAGTTGCCGGGCTCGACTGGGTGGGGCGCCTGCTGACGATCCACGGCCGCGTCGTTCCCATGTCCTCCTCACCCCTGGTCATTGAGGCCGACATCGTCTCCGGGGGGAGTCGACGCCGGGTCAGTGGTCAGGTGGCAGTGGCCTCGGCCCGCGGACGTCTGGAGAACGTGGGGATGGTTCCTCAGGACGCCGAGGCCCATCCCGAGGCGCTGCGCGCCATCGATGAGGCCGAATGGGTAGTCCTGGGGCCCGGCTCCTGGTACACCTCGGTGCTCCCGCACCTCATCCTGCCGTCCATGCGCCGCGCGCTGGTGAACACCTCGGCCCGCAAGGTCGTGGTCCTCAACCTCTCCGCTCAGCAGGGCGAGACCGACGGGATGACCAGTGCCGATCATCTTCGGGTCCTGAGCCAGTACGCGCCCGACCTGCGCCTGGACGTGGTGCTGGCCGACCCCTCCACCGTTGAGGACGTCGAGGATCTTGCAGCGGTGGCCGCCGCCATGGGGGCCACCGTCGTCCTGCGCCAGGTGCGCACCGGCGAGGCCCTGTGCCACCACGATCCGCTTCGCCTGGCAGCCGCCTTCCGGGACGCCTTCGAGGGGGCTCTGGGGGACGTCACCGATCTCAGTGGACGTGATGACATGTGA","VGTTIDAAGWPRRGEEGPAVVALGGGHGLSATLRALRHVTHRLTAVVTVADDGGSSGRLRREFDCLPPGDLRMALASLCEDSEWGLTWRDVLQHRFEGQGELDNHALGNLLILALWQLLGDEVAGLDWVGRLLTIHGRVVPMSSSPLVIEADIVSGGSRRRVSGQVAVASARGRLENVGMVPQDAEAHPEALRAIDEAEWVVLGPGSWYTSVLPHLILPSMRRALVNTSARKVVVLNLSAQQGETDGMTSADHLRVLSQYAPDLRLDVVLADPSTVEDVEDLAAVAAAMGATVVLRQVRTGEALCHHDPLRLAAAFRDAFEGALGDVTDLSGRDDM$","Uncharacterized conserved protein","Cytoplasm","Uncharacterized ACR","hypothetical protein","protein of unknown function UPF0052 and CofD","","Graupner M., Xu H., White R.H. Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F(420) biosynthesis in Methanococcus jannaschii. Biochemistry 2002. 41(11):3754-3761. PMID: 11888293","","","

InterPro
IPR002882
Family

Protein of unknown function UPF0052 and CofD
PF01933	$\"[20-316]T$	UPF0052

InterPro
IPR010119
Family

Conserved hypothetical protein, CofD related
TIGR01826	$\"[20-321]T$	CofD_related: conserved hypothetical protei

","BeTs to 11 clades of COG0391COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0391 is aom---yqvdrlbce-gh--------Number of proteins in this genome belonging to this COG is 1","***** IPB002882 (Protein of unknown function UPF0052) with a combined E-value of 6.8e-17. IPB002882 43-75","Residues 20-62 are 86% similar to a (UPF0052 YBHK UNCHARACTERIZED CYTOSOLIC STRUCTURAL PRECURSOR SIGNAL SPR1423 SP1565 ALR2298) protein domain (PD006387) which is seen in Q9Z514_STRCO.Residues 67-272 are 71% similar to a (UPF0052 YBHK UNCHARACTERIZED TRANSFERASE FBIA IPF2223 METHYLTRANSFERASE CYTOSOLIC YNL011C PROBABLE) protein domain (PD414816) which is seen in Q9Z514_STRCO.","","-63% similar to PDB:2HZB X-Ray structure of the hypothetical UPF0052 protein BH3568 from Bacillus halodurans. Northeast Structural Genomics Consortium BhR60. (E_value = 9.4E_49);-63% similar to PDB:2O2Z Crystal structure of hypothetical protein (NP_244435.1) from Bacillus halodurans at 2.60 A resolution (E_value = 1.2E_48);-59% similar to PDB:2PPV Crystal structure of uncharacterized protein (NP_764104.1) from Staphylococcus epidermidis ATCC 12228 at 2.00 A resolution (E_value = 1.8E_39);-57% similar to PDB:2P0Y Crystal structure of Q88YI3_LACPL from Lactobacillus plantarum. Northeast Structural Genomics Consortium target LpR6 (E_value = 2.3E_39);","Residues 20 to 316 (E_value = 9e-101) place ANA_0712 in the UPF0052 family which is described as Uncharacterised protein family UPF0052.","","ACR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0713","752404","753384","981","10.15","10.89","35214","ATGTCGCTGACGGTCACCGTCAAGGATGAGCTCGCGCTCGTCGCTACTGAGAACGCCGCCCAACGACGGGCGGAGGTCTCCGCGATGCTGCGCTTCGCCGGAGGGCTCCATATCGTCTCCGGGCGCATCGTCGTCGAGGCCGAGCTCGATCACGGCGGAGCGGTGCGGCGCCTGCACCAGCACCTCAAGGAGCTCTACGGGATGGAGCCCGAGGTCATGGTGGTTCAGGGCGGTTCCCTGCACCGAGGGTCCCGTTACGTGCTGCGAGTGACCAAGCGCGGCAAGGACCTGGCCCGGCTGTCCGGGCTGGTCGACGACCGGGGCCGGCCGGTGCGGGGCATGCCGGTGTCGGTCATTCAAGGAGGGCGCAACGCCGCCGCTGCCGCCTGGCGTGGAGCCTTCCTGGCCCGCGGATCCCTGACCGAGCCCGGCCGGTCCTCCTCCTTGGAGGTCACCTGTCCCGGCTCCGAGGCCGCACTGGCCCTGGTCGGGGCCGCGCGGCGCTTCGACATCTCCGCCAAGGCCCGAGAGGTGCGCGGGGCCGACCGCGTCGTCGTTCGCGACGGTGAGGCCATCGGTGTTCTCCTGGAGCGGATGGGGGCGCCGGAGGCCTTCAAGGTGTGGGCCGAGCGCCGATCTCGGCGCGAGTCCCGGGGGACCGCCAACCGCCTGGCCAACTTCGACGACGCCAACCTGCGCCGTTCGGCCCGCGCCGCCGTCGCCTCGGGTGCCCGCGTCGAGCGAGCCTTCGAGATCCTGGGGGACGATGTTCCCGCCCACCTGCTTCAGGCCGGTCGCCTGCGCATCGCGCACAAGCAGGCATCCCTGGAGGAGCTTGGGCAGCTCTCCGACCCACAGCTGACCAAGGACGCCGTCGCTGGACGTATCCGCCGCCTCTTGGCCATGGCGGACAAGCAGGCCCACGAGCTGGGCATCCCCGACACGGAGTCGGTTCTCACCCAGGAGATGCTCGAGCCCTGA","MSLTVTVKDELALVATENAAQRRAEVSAMLRFAGGLHIVSGRIVVEAELDHGGAVRRLHQHLKELYGMEPEVMVVQGGSLHRGSRYVLRVTKRGKDLARLSGLVDDRGRPVRGMPVSVIQGGRNAAAAAWRGAFLARGSLTEPGRSSSLEVTCPGSEAALALVGAARRFDISAKAREVRGADRVVVRDGEAIGVLLERMGAPEAFKVWAERRSRRESRGTANRLANFDDANLRRSARAAVASGARVERAFEILGDDVPAHLLQAGRLRIAHKQASLEELGQLSDPQLTKDAVAGRIRRLLAMADKQAHELGIPDTESVLTQEMLEP$","Uncharacterized conserved protein","Cytoplasm","Uncharacterized BCR, COG1481","hypothetical protein","protein of unknown function DUF199","","","","","

InterPro
IPR003802
Family

Protein of unknown function DUF199
PF02650	$\"[3-304]T$	DUF199

","BeTs to 4 clades of COG1481COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1481 is --------v-rlb------------wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 2-299 are similar to a (TRANSCRIPTIONAL WHIA REGULATORY UNCHARACTERIZED PROBABLE HOMOLOG CYTOSOLIC BCR REGULATOR MG103) protein domain (PD024150) which is seen in Q8FT63_COREF.Residues 3-119 are 75% similar to a (TRANSCRIPTIONAL WHIA REGULATORY PROBABLE HOMOLOG SAWC UNCHARACTERIZED BCR SCO1950 REGULATOR) protein domain (PD130018) which is seen in Q6A9J5_PROAC.Residues 139-174 are 91% similar to a (SAWC SCO1950 WHIA) protein domain (PD471386) which is seen in Q829W5_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 304 (E_value = 2.5e-109) place ANA_0713 in the DUF199 family which is described as Uncharacterized BCR, COG1481.","","BCR, COG1481","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0714","753576","754643","1068","6.02","-5.18","37673","ATGTGTGAAAAGAGCCCCAGCAACCGTGCGCCGCCAACCGGCGCACTAGGAGGACACAAAGTGACCACCCGCGTTGGTATTAACGGCTTCGGCCGGATCGGCCGCAACTTCTTCCGTGCCGCCCTCGAGCAGGGCGCCGACATCGAGGTTGTCGCCGTCAACGACCTGACGGACAACAAGACCCTGGCCCACCTGCTCAAGTACGACTCGATCCTCGGTCGTTTCGACGGCGAGGTCTCCTACGACGAGGATGGCATCACCGTCAACGGCAAGCACATCAAGGTGCTCGCTCAGCGCAACCCCGCCGACCTGCCCTGGGGCGACCTGGGCGTCGAGGTCGTCGTGGAGTCCACCGGCTTCTTCACCGATGGCGAGAAGGCCAAGGCCCACCTCGACGGTGGCGCCAAGAAGGTCGTCATCTCCGCTCCCGCCAAGAACGTCGACGGCACCTTCGTCATGGGTGTCAACGAGGGCGACTACGACAACGCCACGATGAACATCGTGTCCAACGCCTCGTGCACCACCAACTGCCTCGCCCCCCTGGCCAAGGTTCTCCACGAGAACTTCGGCATCGAGCGCGGCATCATGACCACCATCCACTCCTACACGGGTGACCAGCGCGTCCTCGACGCCCCGCACAGCGACCTGCGCCGTGCTCGCGCCGCCGCGCTGAACATGATCCCCACCAAGACCGGTGCCGCCCAGGCCGTGGCCCTCGTTCTGCCCGCCCTCAAGGGCAAGTTCGACGGTCTGGCCGTGCGTGTCCCCACCCCGACCGGCTCGCTGACCGACCTGACCTTCATCGCTGAGAAGGAGGTCTCCGTCGAGGCCGTCAAGGCTGCCGTCAAGGCCGCCGCCGAGGGCGAGCTCAAGGGCGTTCTCGAGTACACCGAGGACCCGATCGTCTCCACCGACATCGTGGGCAACCCGCACACCTCGATCTTCGACGCCACCGAGACCAAGGTCATCGGCAACCTCGTCAAGGTCCTCTCCTGGTACGACAACGAGTGGGGCTACTCCAACGCCCTGGTCCGCCTGACCTCCCTGGTCGGCTCCAAGCTCGCCTGA","MCEKSPSNRAPPTGALGGHKVTTRVGINGFGRIGRNFFRAALEQGADIEVVAVNDLTDNKTLAHLLKYDSILGRFDGEVSYDEDGITVNGKHIKVLAQRNPADLPWGDLGVEVVVESTGFFTDGEKAKAHLDGGAKKVVISAPAKNVDGTFVMGVNEGDYDNATMNIVSNASCTTNCLAPLAKVLHENFGIERGIMTTIHSYTGDQRVLDAPHSDLRRARAAALNMIPTKTGAAQAVALVLPALKGKFDGLAVRVPTPTGSLTDLTFIAEKEVSVEAVKAAVKAAAEGELKGVLEYTEDPIVSTDIVGNPHTSIFDATETKVIGNLVKVLSWYDNEWGYSNALVRLTSLVGSKLA$","Glyceraldehyde-3-phosphate dehydrogenase","Cytoplasm","glyceraldehyde-3-phosphate dehydrogenase, typeI","glyceraldehyde-3-phosphate dehydrogenase ","glyceraldehyde-3-phosphate dehydrogenase, type I","","Huang X.Y., Barrios L.A., Vonkhorporn P., Honda S., Albertson D.G., Hecht R.M. Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans. J. Mol. Biol. 1989. 206(3):411-424. PMID: 2716055Dugaiczyk A., Haron J.A., Stone E.M., Dennison O.E., Rothblum K.N., Schwartz R.J. Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle. Biochemistry 1983. 22(7):1605-1613. PMID: 6303388Berry M.D., Boulton A.A. Glyceraldehyde-3-phosphate dehydrogenase and apoptosis. J. Neurosci. Res. 2000. 60(2):150-154. PMID: 10740219Tatton W., Chalmers-redman R., Tatton N. Neuroprotection by deprenyl and other propargylamines: glyceraldehyde-3-phosphate dehydrogenase rather than monoamine oxidase B. J. Neural Transm. 2003. 110(5):509-515. PMID: 12721812","","","

InterPro
IPR000173
Family

Glyceraldehyde 3-phosphate dehydrogenase
PR00078	$\"[130-143]T$ $\"[167-185]T$ $\"[194-210]T$ $\"[250-267]T$ $\"[290-305]T$	G3PDHDRGNASE
PTHR10836	$\"[23-353]T$	GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
PF00044	$\"[23-173]T$	Gp_dh_N
PF02800	$\"[178-333]T$	Gp_dh_C
PS00071	$\"[171-178]T$	GAPDH

InterPro
IPR006424
Family

Glyceraldehyde-3-phosphate dehydrogenase, type I
TIGR01534	$\"[24-345]T$	GAPDH-I: glyceraldehyde-3-phosphate dehydro

noIPR
unintegrated

unintegrated
G3DSA:3.30.360.10	$\"[172-335]T$	no description

","BeTs to 22 clades of COG0057COG name: Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0057 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 3","***** IPB000173 (Glyceraldehyde 3-phosphate dehydrogenase) with a combined E-value of 1.3e-126. IPB000173A 24-35 IPB000173B 110-146 IPB000173C 167-209 IPB000173D 214-266 IPB000173E 311-346","Residues 24-62 are 92% similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GAPDH GLYCERALDEHYDE 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD000269) which is seen in Q6A9J4_PROAC.Residues 63-101 are 92% similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GAPDH GLYCERALDEHYDE 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD859695) which is seen in Q6A9J4_PROAC.Residues 103-154 are similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GAPDH GLYCERALDEHYDE 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD000250) which is seen in Q6A9J4_PROAC.Residues 155-194 are 92% similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GLYCERALDEHYDE GAPDH 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD589901) which is seen in Q6A9J4_PROAC.Residues 196-267 are similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GLYCERALDEHYDE GAPDH 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD000244) which is seen in Q6A9J4_PROAC.Residues 288-344 are similar to a (OXIDOREDUCTASE DEHYDROGENASE GLYCERALDEHYDE-3-PHOSPHATE NAD GLYCOLYSIS GLYCERALDEHYDE GAPDH 3-PHOSPHATE MULTIGENE FAMILY) protein domain (PD444561) which is seen in Q6A9J4_PROAC.","","-71% similar to PDB:1VC2 Crystal structure of Glyceraldehyde 3-Phosphate Dehydrogenase from Thermus thermophilus HB8 (E_value = 4.7E_107);-71% similar to PDB:1CER DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION (E_value = 4.4E_105);-71% similar to PDB:2G82 High Resolution Structures of Thermus aquaticus Glyceraldehyde-3-Phosphate Dehydrogenase: Role of 220's Loop Motion in Catalysis (E_value = 4.4E_105);-70% similar to PDB:1GD1 STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.8 ANGSTROMS RESOLUTION (E_value = 1.0E_101);-70% similar to PDB:2GD1 COENZYME-INDUCED CONFORMATIONAL CHANGES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILLUS (E_value = 1.0E_101);","Residues 23 to 173 (E_value = 3.3e-102) place ANA_0714 in the Gp_dh_N family which is described as Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain.Residues 178 to 333 (E_value = 5.1e-106) place ANA_0714 in the Gp_dh_C family which is described as Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain.","","dehydrogenase, type I (gap)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0715","754744","755949","1206","4.94","-14.26","41580","ATGAGAGGCTTCATGAAGACCATCGAGTCCCTGGGCGACCTCAAGGGCAAGCGAGTCCTGGTCCGCTCCGACTTCAACGTGCCGCTGGACGCCGACAAGAACATCACCGACGACGGCCGCATCCAGGCCGCTCTGCCCACCCTGCGCACCCTGCTCGACGCCGGCGCCAAGGTGATCATCACCGCCCACCTGGGGCGCCCCAAGGGGCAGGTCAACCCCGACTACTCCCTGGCCCCCGTCGCCAAGCGCCTCGCCGAGGTCACCGGTGTCAAGGTGACCCTCGCCGAGGACACCGTGGGCGAGTCCGCCAAGGCCGCCGTCGCAGCAGCCGGTGACGGAGAGATCGTCCTGCTGGAGAACGTGCGCTTCAACGCCGCCGAGACCTCCAAGGACGACGCCGAGCGCGAGGCCTTCGCCGCCGAGCTCGCCGCCCTGGCCGACGTCTTCGTCTCCGACGGCTTCGGCGTCGTGCACCGCAAGCAGGCTTCCGTCTACGACGTCGCCAAGCTGTTGCCCTCCGCCGCCGGCCTGCTCGTCGTCAAGGAGATCGAGTCCCTGGGGCGCGCCGTCAACGACCCCGAGCGCCCCTACACCGTGGTGCTCGGCGGCTCCAAGGTCTCGGACAAGCTCGGCGTCATCTCCAACCTGCTGAGCAAGGCCGACCGTCTCCTCATCGGTGGCGGCATGGCCTACACCTTCCTGGCCGCCCAGGGCTACGAGGTGGGTACCTCCCTGCTGGAGAAGGACCAGATCGACACCGTCAAGGGCTACCTGGAGACCGCCAAGGCCAACGGCGTCGAGCTGCTGCTGCCCGTCGACACCGTCGTGGCCCCGACCTTCGCCGCGGACGCCCCCGCCACCGTGGTGCCGGCTGACGCACTGCCCGCCGACCAGATGGGCCTGGACATCGGCCCTGAGACGCGAAAGCTCTTCGCCGATGCCATCGCCACCTCCAAGACCGTGGTGTGGAACGGCCCCATGGGCGTCTTCGAGTTCCCGGCCTTCGCCGAGGGCACCAAGGCCGTGGCCAAGGCGATCTCCGAGTCCGACGCCTTCTCCGTCATCGGCGGTGGCGACTCCGCCGCGGCCGTGCGCACGCTCGGCTTCGACGAGGCCACGTTCTCCCACATCTCCACCGGCGGCGGCGCCTCCCTCGAGCTCCTCGAGGGCAAGACCCTGCCCGGTATCGCCGTGCTCAACGACTGA","MRGFMKTIESLGDLKGKRVLVRSDFNVPLDADKNITDDGRIQAALPTLRTLLDAGAKVIITAHLGRPKGQVNPDYSLAPVAKRLAEVTGVKVTLAEDTVGESAKAAVAAAGDGEIVLLENVRFNAAETSKDDAEREAFAAELAALADVFVSDGFGVVHRKQASVYDVAKLLPSAAGLLVVKEIESLGRAVNDPERPYTVVLGGSKVSDKLGVISNLLSKADRLLIGGGMAYTFLAAQGYEVGTSLLEKDQIDTVKGYLETAKANGVELLLPVDTVVAPTFAADAPATVVPADALPADQMGLDIGPETRKLFADAIATSKTVVWNGPMGVFEFPAFAEGTKAVAKAISESDAFSVIGGGDSAAAVRTLGFDEATFSHISTGGGASLELLEGKTLPGIAVLND$","Phosphoglycerate kinase","Cytoplasm","phosphoglycerate kinase","phosphoglycerate kinase ","Phosphoglycerate kinase","","Kumar S., Ma B., Tsai C.J., Wolfson H., Nussinov R. Folding funnels and conformational transitions via hinge-bending motions. Cell Biochem. Biophys. 1999. 31(2):141-164. PMID: 10593256","","","

InterPro
IPR001576
Family

Phosphoglycerate kinase
PR00477	$\"[13-29]T$ $\"[35-57]T$ $\"[113-128]T$ $\"[145-167]T$ $\"[175-197]T$ $\"[198-217]T$ $\"[320-345]T$ $\"[353-364]T$ $\"[377-394]T$	PHGLYCKINASE
PIRSF000724	$\"[5-401]T$	Phosphoglycerate kinase
PTHR11406	$\"[5-401]T$	PHOSPHOGLYCERATE KINASE
PF00162	$\"[2-399]T$	PGK
PS00111	$\"[18-28]T$	PGLYCERATE_KINASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1260	$\"[4-179]T$	no description
G3DSA:3.40.50.1270	$\"[185-401]T$	no description

","BeTs to 25 clades of COG0126COG name: 3-phosphoglycerate kinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0126 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB001576 (Phosphoglycerate kinase) with a combined E-value of 2.3e-133. IPB001576A 13-47 IPB001576B 58-67 IPB001576C 113-127 IPB001576D 147-167 IPB001576E 175-221 IPB001576F 260-280 IPB001576G 301-339 IPB001576H 375-396","Residues 6-399 are 79% similar to a (KINASE PHOSPHOGLYCERATE TRANSFERASE GLYCOLYSIS MULTIGENE FAMILY KINASE CYTOSOLIC SEQUENCING DIRECT) protein domain (PD000619) which is seen in PGK_BIFLO.","","-64% similar to PDB:1VPE CRYSTALLOGRAPHIC ANALYSIS OF PHOSPHOGLYCERATE KINASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA (E_value = 3.4E_96);-62% similar to PDB:1PHP STRUCTURE OF THE ADP COMPLEX OF THE 3-PHOSPHOGLYCERATE KINASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.65 ANGSTROMS (E_value = 5.4E_94);-59% similar to PDB:1V6S Crystal Structure of Phosphoglycerate Kinase from Thermus thermophilus HB8 (E_value = 9.2E_86);-59% similar to PDB:2IE8 Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation (E_value = 2.7E_85);-56% similar to PDB:13PK TERNARY COMPLEX OF PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI (E_value = 1.1E_75);","Residues 2 to 399 (E_value = 1e-218) place ANA_0715 in the PGK family which is described as Phosphoglycerate kinase.","","kinase (pgk)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0716","755965","756744","780","4.91","-15.21","27701","ATGAGTAACCGCACCCCGCTCATGGCGGGCAACTGGAAGATGAACCTCGACCACCTCGAGGCCAACCACCTCGTCCAGGGCCTGGCCATGGAGCTCAAGGACCACGACCACGACTACACCAAGTGCGAGGTCCTCGTGATCCCGCCCTTCACGGACATCCGCACCGTGCAGACCGTCGTTGAGGCCGACTCCCTGGACATCAAGTACGGCGCCCAGGACGTCTCCATCCACGACAACGGCGCCTACACCGGCGAGATCTCCACCGAGATGCTCACCAAGCTTGGTGTCAGCTACGTCGTCATGGGCCACTCCGAGCGCCGCGAGTACCACGGTGAGTCCGACGCCCTCGTGGGCGCCAAGGCCCGCAAGGTGCTCGACGCCGGCATGACCCCCATCCTGTGCTGCGGTGAGGCCCTGGAGATCCGCAAGGCCGGTACCCACGTCGACTTCGTCCTAGGGCAGATCCGCGCCGCCCTGGAGGGATGGAGCGGCGAGGACGTCGCCAAGATCGTCATCGCCTACGAGCCCATCTGGGCCATCGGCACCGGCGAGACCGCTACCGCCGAGGACGCCCAGGAGGTGTGCGGAGCGATCCGCGAGGCCCTGCGCGCCGACTACGGTGACGCTACGGCCGATGCCACCCGCATCCTCTACGGCGGCTCCGCCAAGCCCGGCAACATCAAGGAGCTCATGGCCCAGCCCGACGTCGACGGCGCACTCGTCGGTGGAGCCTCCCTCAAGGCGGACTCCTTCGCCGCCATGGCCGGCTTCTACGCCTGA","MSNRTPLMAGNWKMNLDHLEANHLVQGLAMELKDHDHDYTKCEVLVIPPFTDIRTVQTVVEADSLDIKYGAQDVSIHDNGAYTGEISTEMLTKLGVSYVVMGHSERREYHGESDALVGAKARKVLDAGMTPILCCGEALEIRKAGTHVDFVLGQIRAALEGWSGEDVAKIVIAYEPIWAIGTGETATAEDAQEVCGAIREALRADYGDATADATRILYGGSAKPGNIKELMAQPDVDGALVGGASLKADSFAAMAGFYA$","Triosephosphate isomerase","Cytoplasm","triosephosphate isomerase","triosephosphate isomerase ","Triose-phosphate isomerase","","Lolis E., Alber T., Davenport R.C., Rose D., Hartman F.C., Petsko G.A. Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 1990. 29(28):6609-6618. PMID: 2204417Knowles J.R. Enzyme catalysis: not different, just better. Nature 1991. 350(6314):121-124. PMID: 2005961Olah J., Orosz F., Keseru G.M., Kovari Z., Kovacs J., Hollan S., Ovadi J. Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease. Biochem. Soc. Trans. 2002. 30(2):30-38. PMID: 12023819","","","

InterPro
IPR000652
Family

Triosephosphate isomerase
PD001005	$\"[4-242]T$	Q6A9J2_PROAC_Q6A9J2;
PTHR21139	$\"[1-259]T$	TRIOSEPHOSPHATE ISOMERASE
PF00121	$\"[6-255]T$	TIM
TIGR00419	$\"[7-249]T$	tim: triosephosphate isomerase
PS00171	$\"[173-183]T$	TIM

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[4-258]T$	no description

","BeTs to 25 clades of COG0149COG name: Triosephosphate isomeraseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0149 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB000652 (Triosephosphate isomerase) with a combined E-value of 4.7e-92. IPB000652A 7-17 IPB000652B 80-120 IPB000652C 128-154 IPB000652D 171-195 IPB000652E 214-247","Residues 4-242 are similar to a (ISOMERASE GLYCOLYSIS FATTY GLUCONEOGENESIS BIOSYNTHESIS ACID SHUNT PENTOSE TRIOSEPHOSPHATE TIM) protein domain (PD001005) which is seen in Q6A9J2_PROAC.","","-64% similar to PDB:1YYA Crystal structure of TT0473, putative Triosephosphate Isomerase from Thermus thermophilus HB8 (E_value = 5.7E_61);-62% similar to PDB:2BTM DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES? (E_value = 5.0E_57);-61% similar to PDB:1B9B TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA (E_value = 1.5E_56);-61% similar to PDB:1BTM TRIOSEPHOSPHATE ISOMERASE (TIM) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID (E_value = 4.2E_56);-61% similar to PDB:1AW1 TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS COMPLEXED WITH 2-PHOSPHOGLYCOLATE (E_value = 6.5E_49);","Residues 6 to 255 (E_value = 1.4e-125) place ANA_0716 in the TIM family which is described as Triosephosphate isomerase.","","isomerase (tpiA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0717","756920","757219","300","11.18","5.16","10540","ATGCCGGAGCGTGAGGCCCCCGCAGCAAGACGGAACCAACAACGAAGGGAACGTGACGTGAACGTAGTGCGTATCGTCCTTCAGGTGCTGCTCGTCCTCTCGAGCTTCTTCCTCATCATGTCGATCCTCCTGCACAAGGGCAAGGGCGGCGGTCTGTCGGACATGTTCGGCGGCGGTATCTCCTCCTCCGCAGGGTCCTCCGGCGTGGCCGAGCGCAACCTCGACCGCATCACGGTGGCGGTGGCCATCATCTGGACGATCACGATCGTCGGGCTCGGCCTGGTCGCCAAGCTCGGCTGA","MPEREAPAARRNQQRRERDVNVVRIVLQVLLVLSSFFLIMSILLHKGKGGGLSDMFGGGISSSAGSSGVAERNLDRITVAVAIIWTITIVGLGLVAKLG$","Preprotein translocase, SecG subunit","Membrane, Cytoplasm","protein-export membrane protein SecG","hypothetical protein predicted by Glimmer/Critica","preprotein translocase, SecG subunit","","Bieker K.L., Phillips G.J., Silhavy T.J. The sec and prl genes of Escherichia coli. J. Bioenerg. Biomembr. 1990. 22(3):291-310. PMID: 2202721Driessen A.J. SecB, a molecular chaperone with two faces. Trends Microbiol. 2001. 9(5):193-196. PMID: 11336818Muller J.P. Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. FEMS Microbiol. Lett. 1999. 176(1):219-227. PMID: 10418149Douville K., Price A., Eichler J., Economou A., Wickner W. SecYEG and SecA are the stoichiometric components of preprotein translocase. J. Biol. Chem. 1995. 270(34):20106-20111. PMID: 7650029Veenendaal A.K., Van der does C., Driessen A.J. Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis. J. Biol. Chem. 2001. 276(35):32559-32566. PMID: 11445571","","","

InterPro
IPR004692
Family

Preprotein translocase SecG subunit
PR01651	$\"[25-45]T$ $\"[45-59]T$ $\"[76-98]T$	SECGEXPORT
PF03840	$\"[24-97]T$	SecG
TIGR00810	$\"[24-96]T$	secG: preprotein translocase, SecG subunit

noIPR
unintegrated

unintegrated
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[25-45]?$ $\"[76-96]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB004692 (Protein-export SecG membrane protein signature) with a combined E-value of 3e-21. IPB004692A 25-45 IPB004692B 45-59 IPB004692C 60-76 IPB004692D 76-98","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 97 (E_value = 6.7e-19) place ANA_0717 in the SecG family which is described as Preprotein translocase SecG subunit.","","membrane protein SecG","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0718","757311","758234","924","9.86","10.14","33408","TTGAGGGGCTACCTGGCCCACCTGCGCGTTGAGCGCGGGCTGAGTCCTCACACTCTGAGTGCCTACGAGCGCGACCTCGGCCGCTACCTGCGCTACCTGAGGAGCACCGGCATCTCAGCGCCGCAGGACGTCAGCCGCAACGACGTGGCCGGCTTCCTCGAGGTCCTGCGCACCGGATCCGACGGCGCCCGTCCGCTGGCGTCGTCCTCGGCATCCAGAACCGTCACGGCCGTGCGCGGCTGGCACAAGTTCCTCCTGGCCGAGGGCACCACCTCAGAGGATCCCTCGGCCACCGTGCGCCCGCCCCAGCCCGGAAGGCGCCTGCCCAAGGCCTTAGGGGTCGATGAGGTCCGCCGCCTCCTGGAGGCAGCAGGCGTTGACGACTCCCCGGTGAGCCTGCGCGACCGAGCGCTGCTGGAGGTCCTCTACGCCACCGGCGCCCGCATCTCCGAGGCGGTGGGGCTCGTCGTCGACGACCTTGACACCGACTCCAAGCTGCTGAGGCTGTTCGGCAAGGGACGCAAGGAACGCGTGGTCCCCATGGGGGCCTACGCCTGGGAGGCGCTGGACGCCTACCTGGTGCGAGGCCGGCCGGTCCTGGCCGAGAAGGGCAGGGGAGTGCCACAGGTTTTCCTCAACACCCTGGGCAGGCCCTTGAGTCGGCAGAGCGCCTGGGCCGTCCTGCAGCAGGCCGCTGAACGGGCCGGGCTCATCGGGACGGACGGTGCCGACGAGCGGCGCATCTCCCCCCACACCCTGCGCCACTCCTTCGCCACGCATCTGCTGGCGGGAGGGGCGGACGTGCGTGTCGTCCAGGAGATGCTCGGACACGCCTCGGTCACCACCACCCAGATCTACACGAAGGTCACCGTCGACCACCTGCGGGAGGTCTACGCCACCAGTCACCCGCGGGCTCTGGCCTGA","LRGYLAHLRVERGLSPHTLSAYERDLGRYLRYLRSTGISAPQDVSRNDVAGFLEVLRTGSDGARPLASSSASRTVTAVRGWHKFLLAEGTTSEDPSATVRPPQPGRRLPKALGVDEVRRLLEAAGVDDSPVSLRDRALLEVLYATGARISEAVGLVVDDLDTDSKLLRLFGKGRKERVVPMGAYAWEALDAYLVRGRPVLAEKGRGVPQVFLNTLGRPLSRQSAWAVLQQAAERAGLIGTDGADERRISPHTLRHSFATHLLAGGADVRVVQEMLGHASVTTTQIYTKVTVDHLREVYATSHPRALA$","Tyrosine recombinase xerD","Cytoplasm","Tyrosine recombinase xerD","tyrosine recombinase XerD","tyrosine recombinase XerD","","Yates J., Aroyo M., Sherratt D.J., Barre F.X. Species specificity in the activation of Xer recombination at dif by FtsK. Mol. Microbiol. 2003. 49(1):241-249. PMID: 12823825","","","

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[92-250]T$	no description

InterPro
IPR002104
Domain

Integrase, catalytic core, phage
PF00589	$\"[120-296]T$	Phage_integrase

InterPro
IPR004107
Domain

Integrase, N-terminal SAM-like, phage
PF02899	$\"[1-89]T$	Phage_integr_N

InterPro
IPR011932
Family

Tyrosine recombinase XerD
TIGR02225	$\"[2-305]T$	recomb_XerD: tyrosine recombinase XerD

InterPro
IPR013762
Domain

Integrase-like, catalytic core, phage
G3DSA:1.10.443.10	$\"[110-299]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.130	$\"[1-99]T$	no description

","BeTs to 24 clades of COG0582COG name: IntegraseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0582 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB004107 (Phage integrase, N-terminal SAM-like) with a combined E-value of 9.6e-25. IPB004107A 145-155 IPB004107B 171-177 IPB004107C 249-263 IPB004107D 274-284","Residues 1-83 are 64% similar to a (DNA RECOMBINASE TYROSINE INTEGRATION RECOMBINATION DIVISION DNA-BINDING CHROMOSOME PARTITION CELL) protein domain (PD003816) which is seen in XERD_MYCTU.Residues 84-140 are 71% similar to a (DNA DIVISION DNA-BINDING INTEGRATION RECOMBINASE XERD CHROMOSOME TYROSINE PARTITION RECOMBINATION) protein domain (PD878093) which is seen in Q740E3_MYCPA.Residues 88-305 are 43% similar to a (INTEGRASE/RECOMBINASE) protein domain (PDA027R6) which is seen in Q7NNG2_GLOVI.Residues 134-195 are similar to a (DNA INTEGRASE/RECOMBINASE RECOMBINASE INTEGRASE RECOMBINATION INTEGRATION PLASMID TYROSINE DIVISION DNA-BINDING) protein domain (PD000548) which is seen in XERD_COREF.Residues 208-304 are 44% similar to a (SITE-SPECIFIC RECOMBINASE SSRA INTEGRASE/RECOMBINASE PLASMID) protein domain (PD857335) which is seen in Q8TM57_METAC.Residues 210-257 are 72% similar to a (DNA RECOMBINASE TYROSINE INTEGRATION RECOMBINATION DIVISION DNA-BINDING CHROMOSOME PARTITION CELL) protein domain (PD631017) which is seen in XERD_CORGL.Residues 258-298 are 92% similar to a (DNA INTEGRASE RECOMBINASE INTEGRASE/RECOMBINASE INTEGRATION RECOMBINATION TYROSINE DIVISION DNA-BINDING CHROMOSOME) protein domain (PD254221) which is seen in Q6A7X6_PROAC.","","-58% similar to PDB:1A0P SITE-SPECIFIC RECOMBINASE, XERD (E_value = 4.2E_48);-47% similar to PDB:2A3V Structural basis for broad DNA-specificity in integron recombination (E_value = 2.4E_19);","Residues 1 to 89 (E_value = 1.6e-22) place ANA_0718 in the Phage_integr_N family which is described as Phage integrase, N-terminal SAM-like domain.Residues 120 to 296 (E_value = 1e-45) place ANA_0718 in the Phage_integrase family which is described as Phage integrase family.","","recombinase xerD","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0719","758394","759266","873","4.87","-15.61","31336","GTGAATGACTCCATCCAGCCAGGCCTGATCGACAACCCCGGCACCGACGAGAGCGAGGAGAAGGACTTCCCCGTTCCCGCGCCGCTGGAGTCGCACGGACCCGCTCGGGTCATCTCCATGTGCAACCAGAAGGGCGGCGTCGGCAAGACCACGACGACGATCAACCTCGGTGCGGCCCTGGCCGAGCTGGGGCGCAAGGTCCTCATCGTCGACTTCGACCCCCAGGGAGCGGCCTCGGCCGGCCTGGGCATCAACGCCCACGAGCTCGACTCCACCATCTACGACCTGCTCGTCGCCAGCCGTCCGGACATCCGCACGGTCATCCACGAGACCACGGTGGAGGGGCTGGACATCGTCCCGGCCAACATCGACCTGTCCGCCGCCGAGGTCCAGCTCGTCAACGAGGTCGCCCGCGAGCAGGCCCTCAAGCGGGTGCTGCGTCCGGTGCTTGACGAGTACGACGTGATCCTCGTGGACTGCCAGCCCTCGCTCGGACTGCTGACCATCAACGCCCTGACCGCCTCCCACGGCGTCATCATCCCGCTGGAGACCGAGTTCTTCGCCCTGCGCGGGGTGGCGCTCCTGGTGGAGACCGTCGAGCGCGTCAAGGACCGTCTCAACGCGACCCTGGAGATCGACGGCATCCTGGCCACCATGGTGGACTCCCGCACCCTGCACTCCCGGGAGGTGCTTGAGCGCCTGGAGCAGGCTTTCGGCGAGCAGCTCTTCGACACGCGCATCCGGCGCACGATCAAGTTCCCGGACGCCTCCGTGGCCAACGAGCCGATCACCAGCTACGCGCCCTCCCACCCCGGTGCGGACGCCTACCGCCGGCTGGCCCGTGAGGTCATCGCCCGCGGCGATGTCGCCTGA","VNDSIQPGLIDNPGTDESEEKDFPVPAPLESHGPARVISMCNQKGGVGKTTTTINLGAALAELGRKVLIVDFDPQGAASAGLGINAHELDSTIYDLLVASRPDIRTVIHETTVEGLDIVPANIDLSAAEVQLVNEVAREQALKRVLRPVLDEYDVILVDCQPSLGLLTINALTASHGVIIPLETEFFALRGVALLVETVERVKDRLNATLEIDGILATMVDSRTLHSREVLERLEQAFGEQLFDTRIRRTIKFPDASVANEPITSYAPSHPGADAYRRLAREVIARGDVA$","Cobyrinic acid a,c-diamide synthase","Cytoplasm","ATPases involved in chromosome partitioning","cobyrinic acid a;c-diamide synthase","Cobyrinic acid a,c-diamide synthase","","Pollich M., Klug G. Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus. J. Bacteriol. 1995. 177(15):4481-4487. PMID: 7635831Roth J.R., Lawrence J.G., Rubenfield M., Kieffer-Higgins S., Church G.M. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. J. Bacteriol. 1993. 175(11):3303-3316. PMID: 8501034","","","

InterPro
IPR002586
Domain

Cobyrinic acid a,c-diamide synthase
PF01656	$\"[38-255]T$	CbiA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[36-283]T$	no description
PTHR23264	$\"[37-72]T$	NUCLEOTIDE-BINDING PROTEIN NBP35(YEAST)-RELATED
PTHR23264:SF1	$\"[37-72]T$	gb def: Mus musculus 9 days embryo whole body cDNA, RIKEN full-length enriched library,

","BeTs to 19 clades of COG1192COG name: ATPases involved in chromosome partitioningFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG1192 is -ompk--q-dr-bcefg-snujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB002586 (Cobyrinic acid a,c-diamide synthase) with a combined E-value of 1.9e-27. IPB002586A 38-71 IPB002586B 149-171***** IPB003348 (Anion-transporting ATPase) with a combined E-value of 7.7e-12. IPB003348A 39-75 IPB003348B 153-173***** IPB000808 (Mrp family) with a combined E-value of 8.9e-11. IPB000808A 34-73***** IPB000392 (NifH/frxC family) with a combined E-value of 2.2e-07. IPB000392A 40-79","Residues 35-70 are 94% similar to a (ATP-BINDING NITROGENASE PLASMID IRON-SULFUR 4FE-4S IRON PARA OXIDOREDUCTASE ATPASE REDUCTASE) protein domain (PD000159) which is seen in Q6NHF1_CORDI.Residues 37-183 are 48% similar to a (PARA FAMILY) protein domain (PDA0E9I4) which is seen in Q74CA6_GEOSL.Residues 73-123 are 74% similar to a (PARA PARTITIONING CHROMOSOME FAMILY SOJ PLASMID SPORULATION INHIBITOR INITIATION ATPASE) protein domain (PD849386) which is seen in Q6A7X7_PROAC.Residues 112-284 are 46% similar to a (PARTITIONING ATPASE CHROMOSOME PUTATIVE PARA FAMILY PLASMID) protein domain (PD809048) which is seen in Q9RZT2_DEIRA.Residues 136-195 are similar to a (PLASMID PARA PARTITIONING DIVISION CHROMOSOME FAMILY CELL MIND SEPTUM SITE-DETERMINING) protein domain (PD194671) which is seen in Q6NHF1_CORDI.Residues 197-283 are similar to a (PARA PARTITIONING CHROMOSOME FAMILY PLASMID SOJ SPORULATION ATPASE INHIBITOR INITIATION) protein domain (PD342105) which is seen in Q6A7X7_PROAC.","","-65% similar to PDB:1WCV STRUCTURE OF THE BACTERIAL CHROMOSOME SEGREGATION PROTEIN SOJ (E_value = 2.2E_51);-65% similar to PDB:2BEJ STRUCTURE OF THE BACTERIAL CHROMOSOME SEGREGATION PROTEIN SOJ (E_value = 2.2E_51);-64% similar to PDB:2BEK STRUCTURE OF THE BACTERIAL CHROMOSOME SEGREGATION PROTEIN SOJ (E_value = 1.8E_50);-46% similar to PDB:1ION THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3 (E_value = 5.0E_16);-46% similar to PDB:1G3Q CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND (E_value = 3.3E_15);","Residues 38 to 255 (E_value = 1.2e-52) place ANA_0719 in the CbiA family which is described as CobQ/CobB/MinD/ParA nucleotide binding domain.","","involved in chromosome partitioning (probable)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0720","759256","760077","822","4.92","-16.86","30315","ATGTCGCCTGAGCCTGAGGAGCAGGGGCCGCCCAGGCTGCCCGGATTCAGCGTCACGCTACCCCAGTTCGAAGGCCCCTTCGACCTGCTACTGAGCCTCATCGCCCGCAAGCGGCTCGACGTCACCGAGCTGGCGCTGGCCGAGGTGACCGACGACTTCATCGCCCACATGCGCTCGGACTGGGACCTGGGGCGCGCATCTGAGTTCATCGTCGTGGCCTCCACCCTCCTGGCGCTCAAGGCCCACCGCCTTCTGCCCCATGACGAGAACGAGGAGGAGCCCGACCTCGAGCTGCTCGAGGCCCGCGACCTGCTCTTCGCCCGGCTCCTGCAGTACCGGGCCTTCAAGGAGGCCGCAGCTGCCTTCCGACACCGGGCGGAGACCTCCGCACGCAGCTACCCGCGCATCGTCGCCCTGGAACCGCATCTGGCGGCGCTGCTGCCCAAGCTCGTGGCCACCATCACCCCCGAGGAGCTGACGCGGCTGGCGGTGGGAGCCTTCACCCGGCCCACGGATCCGGGCGTCCAGACCGTCCACCTGCATGAGCGGGTACCGGTCGGTGAGCAACTGAGCCTCATCGCCAGCAGGCTGCGCAGTCACGGAACCCTGACCTTCGCCCAACTCATTGAAGACGCCGAGCGCACCGCCGTCGTGGTGGCCCGCTTCCTGGCGCTGCTCATCCTCCACCGGCAGGGCAGCGCCGAGCTGGACCAGACGGAGGCCATGGGCGAGATCACCGTGACCTGGTGCGGCGGTCAGGACGACCTGACCGGCATGATGACCTCTGAGAACCTCACTGAGCTCGAGGAGGAATTCGCATGA","MSPEPEEQGPPRLPGFSVTLPQFEGPFDLLLSLIARKRLDVTELALAEVTDDFIAHMRSDWDLGRASEFIVVASTLLALKAHRLLPHDENEEEPDLELLEARDLLFARLLQYRAFKEAAAAFRHRAETSARSYPRIVALEPHLAALLPKLVATITPEELTRLAVGAFTRPTDPGVQTVHLHERVPVGEQLSLIASRLRSHGTLTFAQLIEDAERTAVVVARFLALLILHRQGSAELDQTEAMGEITVTWCGGQDDLTGMMTSENLTELEEEFA$","Segregation and condensation protein A","Cytoplasm","segregation and condensation protein A","K05896 segregation and condensation protein A","chromosome segregation and condensation protein ScpA","","Mascarenhas J., Soppa J., Strunnikov A.V., Graumann P.L. Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein. EMBO J. 2002. 21(12):3108-3118. PMID: 12065423Volkov A., Mascarenhas J., Andrei-Selmer C., Ulrich H.D., Graumann P.L. A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure. Mol. Cell. Biol. 2003. 23(16):5638-5650. PMID: 12897137Yamazoe M., Onogi T., Sunako Y., Niki H., Yamanaka K., Ichimura T., Hiraga S. Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli. EMBO J. 1999. 18(21):5873-5884. PMID: 10545099Soppa J., Kobayashi K., Noirot-Gros M.F., Oesterhelt D., Ehrlich S.D., Dervyn E., Ogasawara N., Moriya S. Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB. Mol. Microbiol. 2002. 45(1):59-71. PMID: 12100548","","","

InterPro
IPR003768
Family

Prokaryotic chromosome segregation and condensation protein ScpA
PF02616	$\"[33-250]T$	ScpA_ScpB

","BeTs to 10 clades of COG1354COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1354 is aompk--qvdrlbc-f--sn-j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB003768 (Protein of unknown function DUF173) with a combined E-value of 1.2e-18. IPB003768A 43-54 IPB003768B 73-91 IPB003768D 182-201 IPB003768E 219-247","Residues 23-83 are 85% similar to a (A SEGREGATION CONDENSATION DIVISION CHROMOSOME PARTITION CELL CYTOSOLIC PH1797 DUF173) protein domain (PD013752) which is seen in Q9S230_STRCO.Residues 122-198 are 56% similar to a (ML1368 UNCHARACTERIZED A ACR MB1736 SEGREGATION CONDENSATION SCO1770 MLC1351.05C) protein domain (PD242733) which is seen in Q9S230_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 33 to 250 (E_value = 1.3e-36) place ANA_0720 in the ScpA_ScpB family which is described as ScpA/B protein.","","and condensation protein A (scpA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0721","760074","760682","609","4.62","-14.33","21429","ATGAGCGAGGCTGTGGGGTCAGAGGGGTCTGAGCTGCGCAGTGCTGCTGAGGCCATCCTCATCGTCGCCGACGAGCCGGTGACCACCTCTGCGATCGCCGAGGCCCTCGGTATGGAGGAGAGCGTCTGCGAGGAGCTGCTCGAGGGTCTCGCAGCCGAGTACCGTGGAGAGGCGCCCGGCAGCCGTGCTCATGGATTCCTCCTGAGACGTGCGGCAGGTGGGTGGCGTTTCGCCTCCGTGCCCGAGCACGCCGACCTCGTCGAGCAGTTCATCATCGGCGGCGCCACCGCACGCCTGAGTCAGGCCGCCCTGGAGACCCTGGCTGTCGTCGCCTACCGGCAGCCGGTCACCCGGGGGCGCGTCGCGCAGATCCGCGGGGTCAATGTCGACGGCGTCATGCGCACCCTGCACGCCCGCGGCCTCATCGAGGAGGCCGGTGCCGAGACCTCCGGTGCGATTCTGTACCGGACCACGGGAGACTTCCTGGAGTACCTGGGAATCGACTCCCTGGACGAGCTGCCACCCCTGGCTCCCTACCTCCCCCGCGTCGAGGCGCTGGGGGAGATCGTCGAACAGGCCGATGAGATGGCCGGTAGGAGGACCCCATGA","MSEAVGSEGSELRSAAEAILIVADEPVTTSAIAEALGMEESVCEELLEGLAAEYRGEAPGSRAHGFLLRRAAGGWRFASVPEHADLVEQFIIGGATARLSQAALETLAVVAYRQPVTRGRVAQIRGVNVDGVMRTLHARGLIEEAGAETSGAILYRTTGDFLEYLGIDSLDELPPLAPYLPRVEALGEIVEQADEMAGRRTP$","Segregation and condensation protein B","Cytoplasm","segregation and condensation protein B","K06024 segregation and condensation protein B","segregation and condensation protein B","","Mascarenhas J., Soppa J., Strunnikov A.V., Graumann P.L. Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein. EMBO J. 2002. 21(12):3108-3118. PMID: 12065423Volkov A., Mascarenhas J., Andrei-Selmer C., Ulrich H.D., Graumann P.L. A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure. Mol. Cell. Biol. 2003. 23(16):5638-5650. PMID: 12897137Yamazoe M., Onogi T., Sunako Y., Niki H., Yamanaka K., Ichimura T., Hiraga S. Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli. EMBO J. 1999. 18(21):5873-5884. PMID: 10545099Soppa J., Kobayashi K., Noirot-Gros M.F., Oesterhelt D., Ehrlich S.D., Dervyn E., Ogasawara N., Moriya S. Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB. Mol. Microbiol. 2002. 45(1):59-71. PMID: 12100548","","","

InterPro
IPR005234
Family

Prokaryotic chromosome segregation and condensation protein ScpB
PF04079	$\"[14-176]T$	DUF387
TIGR00281	$\"[11-199]T$	TIGR00281: segregation and condensation pro

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[5-93]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.10.590	$\"[94-167]T$	no description

","BeTs to 13 clades of COG1386COG name: Predicted transcriptional regulator containing the HTH domainFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1386 is a--pk---vdrlbc-f--sn-j--twNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 17-134 are 68% similar to a (SEGREGATION CONDENSATION B DIVISION CHROMOSOME PARTITION CELL PLASMID TRANSCRIPTIONAL CYTOSOLIC) protein domain (PD416897) which is seen in Q8G4K8_BIFLO.Residues 135-188 are 65% similar to a (TRANSCRIPTIONAL DOMAIN CONTAINING REGULATOR THE PREDICTED HTH) protein domain (PDA1F087) which is seen in Q7ZAN2_COREF.","","-55% similar to PDB:1T6S Crystal structure of a conserved hypothetical protein from Chlorobium tepidum (E_value = 1.8E_18);-57% similar to PDB:1FHE GLUTATHIONE TRANSFERASE (FH47) FROM FASCIOLA HEPATICA (E_value = 1.8E_18);-39% similar to PDB:1T8T Crystal Structure of human 3-O-Sulfotransferase-3 with bound PAP (E_value = 1.8E_18);-39% similar to PDB:1T8U Crystal Structure of human 3-O-Sulfotransferase-3 with bound PAP and tetrasaccharide substrate (E_value = 1.8E_18);-43% similar to PDB:2GO1 NAD-dependent formate dehydrogenase from Pseudomonas sp.101 (E_value = 1.8E_18);","Residues 14 to 176 (E_value = 1.1e-55) place ANA_0721 in the DUF387 family which is described as Putative transcriptional regulators (Ypuh-like).","","and condensation protein B (scpB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0722","760679","761653","975","5.27","-14.38","35660","ATGACCCCGAGAAACTGCCACACCCGAACCAACTCTGTGCCCCACAGCGATTTTGGGGCGCAGGAGTTCTACGACGAGGACGACCTCGAAGAGCTCGACGAGCAGGCCGACGCCGGCGACCTGGCCGCCTTCGACGCCGAGGCCATCGATGAAGACGAAGAGGCTCGTCTGCTCCAGATGCGTGAGCGTGCCACCAAGGGCGGCCAGGACGACCCGCACGTCGCCTCCGGGCAACGGCTGCAGAAGGTCCTGGCCCACGCAGGGGTTGCCTCGCGCCGCGCCTGCGAGCAGCTCATCGCCGACGGCCGCGTCAGCGTCGACGGTATCTCCGTCACCGAGGCGGGCGTCAGAGTGGACCCGCTGACCCAGGAGATCCGCGTTGACGGCAGCCGAATCCTCACCAACCCCGAGCTCATCACCCTCATGCTCCACAAGCCGGCAGGGATCGTCACCACCATGGAGGACCCTGAGGGCCGACCCACCGTGGCCCAGTACGGACGCGACTACCTGGCCGAGCACCCCGAGCTGCCCGACTCGCTGCGCCTGGTGCATGTCGGCCGCCTCGACACCGAGACCGAGGGGCTGCTCCTGCTGTCCAACGACGGCGAGCTCTCCCACCGGCTCATGCACCCCAGCTTCGAGATCGCCAAGACCTATGTCGCCATCGTCGAGGGACAGGTTGAGCCCTGGGTCCCGCGCAAGCTGCGGCGCGGCATCGAGCTGGAGGACGGTGAGGCCAAGGCGGACCGGGTCACCGTCAAGGACTCCGGGCCGCGCGGTTCCATCGTCGAGATCACCCTCCACTCCGGCAAGAACCGCATCGTGCGACGCATGCTGGACGCCGTCGGCCACCCGGTGACGCGCCTGGCGCGCACCCGGCTCGGACCGCTGCGGCTGGGTAACCTGCGCCCCGGCCAGACCCGCCCACTCAGTGGCGAGGAGATCGCCGCGCTGCAGCAGGAGGTCGGGCTGTGA","MTPRNCHTRTNSVPHSDFGAQEFYDEDDLEELDEQADAGDLAAFDAEAIDEDEEARLLQMRERATKGGQDDPHVASGQRLQKVLAHAGVASRRACEQLIADGRVSVDGISVTEAGVRVDPLTQEIRVDGSRILTNPELITLMLHKPAGIVTTMEDPEGRPTVAQYGRDYLAEHPELPDSLRLVHVGRLDTETEGLLLLSNDGELSHRLMHPSFEIAKTYVAIVEGQVEPWVPRKLRRGIELEDGEAKADRVTVKDSGPRGSIVEITLHSGKNRIVRRMLDAVGHPVTRLARTRLGPLRLGNLRPGQTRPLSGEEIAALQQEVGL$","Pseudouridine synthase","Cytoplasm","ribosomal large subunit pseudouridine synthaseB","pseudouridine synthase; Rsu ","pseudouridine synthase","","Wrzesinski J., Bakin A., Nurse K., Lane B.G., Ofengand J. Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli. Biochemistry 1995. 34(27):8904-8913. PMID: 7612632","","","

InterPro
IPR000748
Domain

Pseudouridine synthase, Rsu
TIGR00093	$\"[144-312]T$	TIGR00093: conserved hypothetical protein
PS01149	$\"[186-200]T$	PSI_RSU

InterPro
IPR002942
Domain

RNA-binding S4
PF01479	$\"[78-125]T$	S4
SM00363	$\"[78-137]T$	S4
PS50889	$\"[78-145]T$	S4

InterPro
IPR006145
Domain

Pseudouridine synthase
PF00849	$\"[139-281]T$	PseudoU_synth_2

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[2-68]T$	no description

noIPR
unintegrated

unintegrated
PTHR21600	$\"[82-324]T$	RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B
PTHR21600:SF2	$\"[82-324]T$	RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B

","BeTs to 17 clades of COG1187COG name: 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthasesFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1187 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000748 (Pseudouridine synthase, Rsu) with a combined E-value of 2.7e-67. IPB000748A 79-104 IPB000748B 142-159 IPB000748C 185-217 IPB000748D 265-299","Residues 62-120 are 66% similar to a (LYASE RIBOSOMAL SUBUNIT B PSEUDOURIDINE SYNTHASE LARGE) protein domain (PDA192R9) which is seen in Q7UUP0_RHOBA.Residues 63-162 are 70% similar to a (LYASE RIBOSOMAL SUBUNIT B PSEUDOURIDINE SYNTHASE LARGE) protein domain (PDA1B6T3) which is seen in Q8G6A9_BIFLO.Residues 75-156 are 58% similar to a (PSEUDOURIDYLATE RNA SYNTHASE) protein domain (PD945399) which is seen in Q9A9V6_CAUCR.Residues 75-162 are 68% similar to a (SYNTHASE HYDROLYASE PSEUDOURIDYLATE LYASE URACIL ML1370 RNA-BINDING PSEUDOURIDINE) protein domain (PD990891) which is seen in YH11_MYCLE.Residues 77-121 are 82% similar to a (RNA PSEUDOURIDINE SYNTHASE) protein domain (PDA192R6) which is seen in Q6AGF9_BBBBB.Residues 78-159 are 57% similar to a (SYNTHASE) protein domain (PD645085) which is seen in Q8T866_DICDI.Residues 79-153 are 60% similar to a (TP0459) protein domain (PD266279) which is seen in O83472_TREPA.Residues 176-228 are 84% similar to a (SYNTHASE LYASE PSEUDOURIDINE PSEUDOURIDYLATE RIBOSOMAL SUBUNIT LARGE HYDROLYASE URACIL RRNA) protein domain (PD753585) which is seen in Q6A7X9_PROAC.Residues 235-289 are 73% similar to a (SYNTHASE LYASE PSEUDOURIDINE PSEUDOURIDYLATE RIBOSOMAL SUBUNIT LARGE HYDROLYASE URACIL RRNA) protein domain (PD033985) which is seen in Q6AGF9_BBBBB.","","-47% similar to PDB:1KSK STRUCTURE OF RSUA (E_value = 1.3E_18);-47% similar to PDB:1KSL STRUCTURE OF RSUA (E_value = 1.3E_18);-47% similar to PDB:1KSV STRUCTURE OF RSUA (E_value = 1.3E_18);-46% similar to PDB:1VIO Crystal structure of pseudouridylate synthase (E_value = 7.9E_13);-48% similar to PDB:2GML Crystal Structure of Catalytic Domain of E.coli RluF (E_value = 5.1E_12);","Residues 78 to 125 (E_value = 2.1e-11) place ANA_0722 in the S4 family which is described as S4 domain.Residues 139 to 281 (E_value = 9e-19) place ANA_0722 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase.","","large subunit pseudouridine synthase B","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0723","761650","762810","1161","5.26","-11.12","39194","GTGAGCGGCCCCGAACCGCGGGCATCAGTGTCCACGCGCGGCCCGGTGCTCATCGTCGGCACGGGGCTGCTGGGAACCTCACTCGCTCTGGCGCTGCGGACGGCGGGTGTCGGGGTTCTGCTCTCCGACACCTCGCCCACCTCCCTGGCCCTGGCTCGAGACATGGGAGCAGGATCGCTTCATGACGAGGACAGCCCTGAGCCGCAGGTTGTTGTCGTGGCCACGCCCCCCGACGTCACCGCCGACGTCGTCGTCGCGCAGTTGAGCGCCCACCCCAGTGCTGTGGTCACTGACGTGGCCTCCGTCAAGGAACGGGTCGTCGCCGAGGTCCGGGCCCGGGCGGGAGCGCAGGCGCGCAGGTACGTCGGCTCCCACCCGATGGCCGGCCGGGAGCGCTCGGGCGCCGGCGCCGCCGACTGCGACCTCTTCGCCGGGCGCCCCTGGGTGGTGGTCGGCCAGGACGCCGATCCACAGGCGGAGCTGGTCATCAGGAACCTGGCGGTCGATGTGGGCGCCACCCCGGTGCGCATGGGTGCGGCGGAGCATGACGCTGCCGTCGCTGCCGTCTCCCACATGCCCCAGCTCGTCTCCTCACTCGTGGCCGCCCGCCTGGAGGAGCTGGGGGAGGGGGCCCTGGCTCTGTCGGGGCAGGGGCTTCGTGACGTCACCAGGATCGCGGCCTCGGATCCCAGGTTGTGGTCGGCCATCATCGTGGGCAACGCCGGGCCCGTGGTCGACCTGCTGCGCCGAATCCGTGATGACCTAGGCGTACTGATCACAGGGATCGAAGCGGCCGCCTGCGATTCGGACAGTCCGGAGCACACAGCTCCGGGAGCGGCACGTGTGGTCGCTCCCGGGGCCGTCGGCGCGGTCACCGATGTCATGACACGGGGAAACCTCGGTCGGGAACGCATCCCCGGAAAGCACGGCGGGGCGCCGCGCCGCTACACCGAGGTCCAGGTCCTGGTACCCGACGCCGCCGGCGAGCTGGGCAGGCTCTTCTCGGACGTCGGAGCCGCCGGCGTCAACATTGAGGACTTCTCCCTGGAGCACTCGGCCGGGCAGAGCGCGGGCATCGCCCTCATCTCCGTCCTTCCTGCGGCCGCCCAACGGCTGGAGGAGGCGCTGGACGCCCAGGGCTGGCGCGTCGTCGCGGGCTGA","VSGPEPRASVSTRGPVLIVGTGLLGTSLALALRTAGVGVLLSDTSPTSLALARDMGAGSLHDEDSPEPQVVVVATPPDVTADVVVAQLSAHPSAVVTDVASVKERVVAEVRARAGAQARRYVGSHPMAGRERSGAGAADCDLFAGRPWVVVGQDADPQAELVIRNLAVDVGATPVRMGAAEHDAAVAAVSHMPQLVSSLVAARLEELGEGALALSGQGLRDVTRIAASDPRLWSAIIVGNAGPVVDLLRRIRDDLGVLITGIEAAACDSDSPEHTAPGAARVVAPGAVGAVTDVMTRGNLGRERIPGKHGGAPRRYTEVQVLVPDAAGELGRLFSDVGAAGVNIEDFSLEHSAGQSAGIALISVLPAAAQRLEEALDAQGWRVVAG$","Prephenate dehydrogenase","Cytoplasm, Membrane","prephenate dehydrogenase homolog","prephenate dehydrogenase ","Prephenate dehydrogenase","","Pohnert G., Zhang S., Husain A., Wilson D.B., Ganem B. Regulation of phenylalanine biosynthesis. Studies on the mechanism of phenylalanine binding and feedback inhibition in the Escherichia coli P-protein. Biochemistry 1999. 38(38):12212-12217. PMID: 10493788Aravind L., Koonin E.V. Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 1999. 287(5):1023-1040. PMID: 10222208Christendat D., Turnbull J.L. Identifying groups involved in the binding of prephenate to prephenate dehydrogenase from Escherichia coli. Biochemistry 1999. 38(15):4782-4793. PMID: 10200166Christendat D., Saridakis V.C., Turnbull J.L. Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli. Biochemistry 1998. 37(45):15703-15712. PMID: 9843375","","","

InterPro
IPR002912
Domain

Amino acid-binding ACT
PF01842	$\"[317-377]T$	ACT

InterPro
IPR003099
Domain

Prephenate dehydrogenase
PF02153	$\"[18-282]T$	PDH
PS51176	$\"[14-292]T$	PDH_ADH

InterPro
IPR008236
Family

Predicted prephenate dehydrogenase, feedback inhibition-sensitive
PIRSF005547	$\"[13-385]T$	Predicted prephenate dehydrogenase, feedback inhibition-sensitive

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[7-85]T$	no description
PTHR21363	$\"[11-370]T$	PREPHENATE DEHYDROGENASE
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

","BeTs to 11 clades of COG0287COG name: Prephenate dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0287 is aomp-zyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003099 (Prephenate dehydrogenase) with a combined E-value of 1.7e-25. IPB003099A 88-103 IPB003099B 125-146 IPB003099C 171-195","Residues 86-149 are 68% similar to a (DEHYDROGENASE PREPHENATE OXIDOREDUCTASE CYCLOHEXADIENYL BIOSYNTHESIS PDH TYRA AROGENATE SYNTHASE TYROSINE) protein domain (PD399755) which is seen in Q6AGF8_BBBBB.Residues 162-272 are 70% similar to a (DEHYDROGENASE PREPHENATE OXIDOREDUCTASE CYCLOHEXADIENYL BIOSYNTHESIS PDH TYRA AROGENATE SYNTHASE TYROSINE) protein domain (PD356257) which is seen in Q6AGF8_BBBBB.Residues 298-383 are similar to a (DEHYDROGENASE PREPHENATE OXIDOREDUCTASE CYCLOHEXADIENYL CLOF NOVF PCZA363.1) protein domain (PD356713) which is seen in Q8CK19_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 282 (E_value = 2.6e-58) place ANA_0723 in the PDH family which is described as Prephenate dehydrogenase.Residues 317 to 377 (E_value = 6.3e-05) place ANA_0723 in the ACT family which is described as ACT domain.","","dehydrogenase homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0724","762929","765100","2172","5.09","-26.99","77841","ATGGAGGGCACCATGGGAATCGTCGTTGCGATCGACGGACCGAGCGGATCGGGCAAGTCCACCGTCTCGCGGCGCGTCGCCGCCGAGCTGGGACTGGCCTACCTGGACACCGGTGCCATGTACCGGGCCGCCGCCTGGTGGTGCGAGCACGAGGGCATCGATCTGGAGGACGGGGCCGCCGTCGCCGAGGCCGTCGCCGTGATGCCCCTGCACATGGGGCTGAATCCCGAGCACCCCACCTTCACCGTGGACGGCACGGACGTATCGACCGCGATTCGCGACCCGCACATCGCCACCGTCGTCTCGAAGGTCGCCACCAACCTCGAGGTGCGTGCCGACCTGGCGCGCCGCCAGCGCGAGATCATCCGCTTCGAGGCGACCGGGCACACCGGCTCCTTCTCCGCCGGTGCCGGCATCGTGGCCGAGGGACGTGACATCACCACCGTCATCGCGCCCGACGCCGACGCCCGCCTACTGGTGACCGCATCGGAGGAGGCCCGCCTGGCCCGCCGCGCCGGGGACCTGGAGGCCGCCGGCAAGCAGGTCGACGCCGACGCCCTGCGCGACCAGGTGGTGCGCCGCGACCGCGACGACGCCACGGTCTCCCAGTTCCTCACCGCGCCCGAGGGCGTCACCCTGGTGGACACCTCGGAGCTGACCCTGGAGCAGTCCGTCGAACGGGTCCTGGACCTGGTGGAGGAGGCCGCCGACGCCGCCGCCCAGCGGGACGCCGAGGAGGATCTGCGGGCCCAGGCCATGCGCGCGGGCCTGGCCGACTACGAGCTCGATGAGGAGGACCTCGCCCTCCTGGAGGCCGACGGCGGCCTGCCCACCGGTGACAGCGTCGAGCCCGGATTGCCGGTCCTGGCCGTCGTCGGCCGCCCCAACGTGGGCAAGTCGACGCTGGTCAACCGGGTCCTGGGCCGTCGCGAGGCCGTCGTCCAGGACACCCCTGGTGTCACGCGCGACCGGGTCTCCTACCCCGCGGAGTGGGCCGGGCGCCGCTTCACCATCGTCGACACCGGCGGATGGGAGGTGGACGTGGCCGGCCTCGACGCCGCCGTGGCCACCCAGGCCGAGATCGCCGTGGAGATGGCCGATGCCGTCCTGCTGGTCGTCGACGCCCAGGTCGGCATCACCGAGACCGACGCCCGCGTGGTGCGGATGCTGCGCCGCAGCGGCAAGCCGGTGGTGCTGGCCGCCAACAAGGTCGACTCCCCGGCCCAGGAGGGGGACGCCGCCACCCTGTGGAACCTGGGGCTGGGCGAGCCCTTCCCGGTCTCGGCCCTGCACGGCCGGGGCAGCGGCGAGGTCCTCGACGCCGTCATGGAGGTCCTTCCGGAGGTCTCCGCCGTGGCCACCGCAGCGCCGGAGGGGGACCTGCACCGCATCGCTCTCGTGGGGCGTCCTAACGTCGGCAAGTCCTCTCTGCTGAACTCCATCGCGGGCCAGGAGCGCGTCGTCGTCAACGAGACCGCGGGCACGACACGTGACCCGGTCGACGAGATCATCGAGCTCGACGGGCGCCAGTGGGTCTTCGTTGACACCGCCGGAATCCGCCGGCGGGTCAAGCAGTCACGGGGCGCCGACTACTATGCGGTGCTGCGCACGCAGGGCGCCATCGACAAGGCCGAGGTCGCCGTCGTCCTGCTGGACGCCTCCGAGCCGATCAGCGAGCAGGACGTGCGCGTGGTCCAGCAGGCCGTCGATGCCGGCCGAGCCCTGGTCCTGGTCAACAACAAGTGGGACCTGGTGGACGAGGAGCGCCAGAAGATGCTCCTGTGGGAGGTCGAGCACGACCTGGCCCACGTCTCCTGGGCCCCCCACATCAACCTGGCAGCCCGGACCGGCTGGCACACCAACCGGCTCGTGCGCGCTCTCGACGCCGCACTGGAGGGTTGGACCACGCGCGTGCCCACAGGCCGGCTCAACGGCTTCCTGGGGCAGCTGCAGTCCGCCACCCCGCACCCGGTGCGAGGCGGTAAGCAGCCCCGCATCCTCTTCGCCACTCAGGTCCAGGTGGCCCCGCCCCGGATCGTCATCTTCACCACCGGTTTCCTCGACGCCGGCTACCGGCGCTTCATCGAGCGGCGCCTGCGTGAGGAGTTCGGCTTCACCGGCACCCCCATCCAGATCGGGGTGCGCGTGCGTGAGAAGCGCCAGCGGCGCTGA","MEGTMGIVVAIDGPSGSGKSTVSRRVAAELGLAYLDTGAMYRAAAWWCEHEGIDLEDGAAVAEAVAVMPLHMGLNPEHPTFTVDGTDVSTAIRDPHIATVVSKVATNLEVRADLARRQREIIRFEATGHTGSFSAGAGIVAEGRDITTVIAPDADARLLVTASEEARLARRAGDLEAAGKQVDADALRDQVVRRDRDDATVSQFLTAPEGVTLVDTSELTLEQSVERVLDLVEEAADAAAQRDAEEDLRAQAMRAGLADYELDEEDLALLEADGGLPTGDSVEPGLPVLAVVGRPNVGKSTLVNRVLGRREAVVQDTPGVTRDRVSYPAEWAGRRFTIVDTGGWEVDVAGLDAAVATQAEIAVEMADAVLLVVDAQVGITETDARVVRMLRRSGKPVVLAANKVDSPAQEGDAATLWNLGLGEPFPVSALHGRGSGEVLDAVMEVLPEVSAVATAAPEGDLHRIALVGRPNVGKSSLLNSIAGQERVVVNETAGTTRDPVDEIIELDGRQWVFVDTAGIRRRVKQSRGADYYAVLRTQGAIDKAEVAVVLLDASEPISEQDVRVVQQAVDAGRALVLVNNKWDLVDEERQKMLLWEVEHDLAHVSWAPHINLAARTGWHTNRLVRALDAALEGWTTRVPTGRLNGFLGQLQSATPHPVRGGKQPRILFATQVQVAPPRIVIFTTGFLDAGYRRFIERRLREEFGFTGTPIQIGVRVREKRQRR$","GTP-binding protein","Cytoplasm, Membrane","GTPase family protein","K03977 GTP-binding protein","cytidylate kinase","","Wieland B., Tomasselli A.G., Noda L.H., Frank R., Schulz G.E. The amino acid sequence of GTP:AMP phosphotransferase from beef-heart mitochondria. Extensive homology with cytosolic adenylate kinase. Eur. J. Biochem. 1984. 143(2):331-339. PMID: 6088234Tomasselli A.G., Noda L.H. Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies. Eur. J. Biochem. 1979. 93(2):263-270. PMID: 218813Cooper A.J., Friedberg E.C. A putative second adenylate kinase-encoding gene from the yeast Saccharomyces cerevisiae. Gene 1992. 114(1):145-148. PMID: 1587477Briozzo P., Golinelli-Pimpaneau B., Gilles A.M., Gaucher J.F., Burlacu-Miron S., Sakamoto H., Janin J., Barzu O. Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity. Structure 1998. 6(12):1517-1527. PMID: 9862805","","","

InterPro
IPR000623
Domain

Shikimate kinase
PF01202	$\"[15-37]T$	SKI

InterPro
IPR002917
Domain

GTP-binding protein, HSR1-related
PF01926	$\"[287-405]T$ $\"[462-583]T$	MMR_HSR1

InterPro
IPR003136
Family

Cytidylate kinase
TIGR00017	$\"[5-232]T$	cmk: cytidylate kinase

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[5-250]T$ $\"[285-423]T$ $\"[460-705]T$	AAA

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[284-444]T$ $\"[459-629]T$	small_GTP: small GTP-binding protein domain

InterPro
IPR005289
Domain

GTP-binding
TIGR00650	$\"[292-322]T$ $\"[467-507]T$	MG442: GTP-binding conserved hypothetical p

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[325-342]?$	SUGAR_TRANSPORT_1

InterPro
IPR006073
Domain

GTP1/OBG
PR00326	$\"[464-484]T$ $\"[513-528]T$	GTP1OBG

InterPro
IPR011769
Domain

Adenylate/cytidine kinase, N-terminal
PD000657	$\"[8-43]T$	Q8YSZ3_ANASP_Q8YSZ3;

InterPro
IPR011994
Domain

Cytidylate kinase region
PF02224	$\"[62-230]T$	Cytidylate_kin

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[2-239]T$ $\"[279-448]T$ $\"[454-642]T$	no description
PTHR11649	$\"[286-718]T$	MSS1/TRME-RELATED GTP-BINDING PROTEIN
PTHR11649:SF5	$\"[286-718]T$	GTP-BINDING PROTEIN ENGA

","BeTs to 18 clades of COG1160COG name: Predicted GTPasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1160 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003136 (Cytidylate kinase) with a combined E-value of 9.9e-61. IPB003136A 9-42 IPB003136B 85-119 IPB003136C 140-174 IPB003136D 186-225***** IPB006073 (GTP1/OBG GTP-binding protein family signature) with a combined E-value of 1.4e-17. IPB006073A 464-484 IPB006073B 486-504 IPB006073C 513-528***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 7.6e-16. IPB002917 466-498 IPB002917 291-323***** IPB000764 (Uridine kinase signature) with a combined E-value of 1.7e-06. IPB000764A 6-23***** IPB003373 (Ferrous iron transport protein B) with a combined E-value of 6.9e-06. IPB003373A 464-494 IPB003373A 289-319","Residues 7-57 are 68% similar to a (KINASE CYTIDYLATE TRANSFERASE GTP-BINDING FUSION KINASE/GTP-BINDING) protein domain (PD709777) which is seen in Q6MTJ7_MYCMS.Residues 8-43 are 94% similar to a (KINASE TRANSFERASE ATP-BINDING ADENYLATE TRANSPHOSPHORYLASE ATP-AMP CYTIDYLATE MONOPHOSPHATE CYTIDINE CMP) protein domain (PD000657) which is seen in Q8YSZ3_ANASP.Residues 92-175 are 61% similar to a (KINASE CYTIDYLATE TRANSFERASE MONOPHOSPHATE CYTIDINE CMP CK ATP-BINDING PANTOTHENATE CMK) protein domain (PD005731) which is seen in Q6AGF7_BBBBB.Residues 289-331 are 79% similar to a (GTP-BINDING ENGA REPEAT) protein domain (PDA0L2E1) which is seen in ENGA_MYCPE.Residues 463-624 are 51% similar to a (GTP-BINDING LIPOPROTEIN PRENYLATION RAS-RELATED GTPASE ADP-RIBOSYLATION SMALL FAMILY FACTOR RAS) protein domain (PD000015) which is seen in ENGA_CLOAB.Residues 466-499 are 94% similar to a (GTP-BINDING TRNA ENGA REPEAT GTPASE RNA-BINDING MODIFICATION TRME PROBABLE ERA) protein domain (PD000414) which is seen in ENGA_STRCO.Residues 335-448 are similar to a (GTP-BINDING ENGA REPEAT GTPASE PROBABLE PROTEIN FAMILY GTP PROTEIN-LIKE BINDING) protein domain (PD084499) which is seen in ENGA_STRCO.Residues 463-624 are 51% similar to a (GTP-BINDING LIPOPROTEIN PRENYLATION RAS-RELATED GTPASE ADP-RIBOSYLATION SMALL FAMILY FACTOR RAS) protein domain (PD000015) which is seen in ENGA_CLOAB.Residues 466-499 are 94% similar to a (GTP-BINDING TRNA ENGA REPEAT GTPASE RNA-BINDING MODIFICATION TRME PROBABLE ERA) protein domain (PD000414) which is seen in ENGA_STRCO.Residues 500-546 are 78% similar to a (GTP-BINDING ENGA REPEAT PROBABLE GTPASE FAMILY ERA-LIKE DOMAIN PROTEIN DOUBLE) protein domain (PDA0C6Z1) which is seen in ENGA_BIFLO.Residues 513-559 are 85% similar to a (GTP-BINDING REPEAT ENGA BINDING GTP GTPASE B2511 KINASE/GTP-BINDING PROTEIN-RELATED KINASE) protein domain (PD884742) which is seen in Q6AGF6_BBBBB.Residues 576-626 are 78% similar to a (GTP-BINDING ENGA REPEAT GTPASE PROBABLE FAMILY PROTEIN ERA-LIKE DOMAIN GTP) protein domain (PD440355) which is seen in Q6AGF6_BBBBB.Residues 650-720 are 83% similar to a (GTP-BINDING ENGA REPEAT PROBABLE GTPASE PROTEIN-LIKE FAMILY PROTEIN ERA-LIKE DOUBLE) protein domain (PD005185) which is seen in ENGA_BIFLO.","","-55% similar to PDB:2HJG The crystal structure of the B. subtilis YphC GTPase in complex with GDP (E_value = 4.8E_78);-55% similar to PDB:1MKY Structural Analysis of the Domain Interactions in Der, a Switch Protein Containing Two GTPase Domains (E_value = 1.2E_60);-56% similar to PDB:2DYK Crystal structure of N-terminal GTP-binding domain of EngA from Thermus thermophilus HB8 (E_value = 2.3E_27);-50% similar to PDB:1Q3T Solution structure and function of an essential CMP kinase of Streptococcus pneumoniae (E_value = 5.0E_19);-53% similar to PDB:2H92 Crystal Structure of Staphylococcus aureus Cytidine Monophosphate Kinase in complex with cytidine-5'-monophosphate (E_value = 3.3E_18);","Residues 15 to 37 (E_value = 3.4e-05) place ANA_0724 in the SKI family which is described as Shikimate kinase.Residues 62 to 230 (E_value = 1.7e-24) place ANA_0724 in the Cytidylate_kin family which is described as Cytidylate kinase.Residues 287 to 405 (E_value = 1.4e-41) place ANA_0724 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 288 to 405 (E_value = 3.4e-05) place ANA_0724 in the Miro family which is described as Miro-like protein.Residues 462 to 583 (E_value = 9.8e-42) place ANA_0724 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 463 to 583 (E_value = 0.00019) place ANA_0724 in the Miro family which is described as Miro-like protein.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0725","765625","765113","513","4.89","-9.13","18192","ATGAGTACACGCAACCTATCCGGGGCCACTGGTCACTACACGACTGATGGGACTCCGCACGGCTTCACCAGCATCACACCGTTTCTGGCGGTTGACGGCGCCGACCGAGCGCTCAGGTTCTACCGTGACGTCTTCGGTGCGCGCATCGTGGACAGTGTGGAGATCGAGGGTGCGGTCGTCCACGCAGAGCTCGACTTCGGTCACGGCAGGATCCAGATCGGTGAGCCCTCAGCCTTGTCCGGTCTGGTTGCGACTCCGTCGGATGAGCCGGTCTGCTACTCGATCCGCCTGTATTGCCCGGATGTCGACGCCGCCGTTGAGCGGGCTACTGCCGCCGGTGCGACCTTGCTGGAACCGCCCGACACCTTCGTGTCCGGGGACAGGTTCGCCTCCATCCGCGATCCCTTCGGCGTGCGGTGGTCGGTCATGACCCGGGTCGAGGACTTGTCCGAGGAGGAGAGTTCCGCACGTGTTGCCGCGTGGGCTAAGAAGCAGGCCGTTTCCGACAGCTGA","MSTRNLSGATGHYTTDGTPHGFTSITPFLAVDGADRALRFYRDVFGARIVDSVEIEGAVVHAELDFGHGRIQIGEPSALSGLVATPSDEPVCYSIRLYCPDVDAAVERATAAGATLLEPPDTFVSGDRFASIRDPFGVRWSVMTRVEDLSEEESSARVAAWAKKQAVSDS$","Glyoxalase/bleomycin resistance protein/dioxygenase","Cytoplasm","glyoxalase family protein","K04750 PhnB protein","Glyoxalase/bleomycin resistance protein/dioxygenase","","Kim N.S., Umezawa Y., Ohmura S., Kato S. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 1993. 268(15):11217-11221. PMID: 7684374","","","

InterPro
IPR004360
Domain

Glyoxalase/bleomycin resistance protein/dioxygenase
PF00903	$\"[21-142]T$	Glyoxalase

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.10	$\"[29-147]T$	no description

","BeTs to 3 clades of COG2764COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2764 is ----------rlb-ef-----j----Number of proteins in this genome belonging to this COG is 1","***** IPB004361 (Glyoxalase I) with a combined E-value of 3.8e-07. IPB004361A 26-59 IPB004361C 90-124 IPB004361D 129-141","No significant hits to the ProDom database.","","-42% similar to PDB:1CQE PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN (E_value = );-42% similar to PDB:1DIY CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE CYCLOOXYGENASE ACTIVE SITE OF PGHS-1 (E_value = );-42% similar to PDB:1EBV OVINE PGHS-1 COMPLEXED WITH SALICYL HYDROXAMIC ACID (E_value = );-42% similar to PDB:1EQG THE 2.6 ANGSTROM MODEL OF OVINE COX-1 COMPLEXED WITH IBUPROFEN (E_value = );-42% similar to PDB:1EQH THE 2.7 ANGSTROM MODEL OF OVINE COX-1 COMPLEXED WITH FLURBIPROFEN (E_value = );","Residues 21 to 142 (E_value = 7.1e-14) place ANA_0725 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0726","765899","766513","615","8.53","3.10","22262","ATGGCTCTGCACGGCCCGACGACGAGCATCTCCTATCGTGAGCTGGAAGGCCGAGGATGGGCCGTCGGAGCCCTTCTCAGGCCTGCGGCAGCGGGTGCGCTGTGCTCCCCGTCCCTGATCCGGAACTCCCATCGGCCGCTCGAGGACCCTGACCTGGGCGCTGCGGTTGCTGACGCCATGGCGGATACCAACACGATGAGGGGTGGACAACGTGCCGCCAGTGCGCTGGCAGACTGGGTGGCGCAACATGCCGGGCCGCCACAAGCGATGGCGCTCATCGCCAACAAGATGGAGGACGTCGTCGCCTCCGACAGAAGCGTCCTGCGCGTCGATCAGCTGGCGCGACGCCTCGATCTTTCTGTCCGCAGTCTCCAACGCCTCTGTGAGAAGTACATCGGCCTGCCCCCACTCGCAGTGATCCGACGCTACCGGCTCCAAGAAGCAGCACAGCGGCTTCGGGAGGATTCGTCCGTCACCGTTGCGCAGGTGGCCGCCGAACTCGACTACGCGGACCACGCCCACCTGACCGCCGACTTCCGACGCGTTCTGGGGCTCTCACCGAGCCAGTACCGACAGCAGACCATGAGCGATCGTCAGGTACTCAGTGACCGGTAG","MALHGPTTSISYRELEGRGWAVGALLRPAAAGALCSPSLIRNSHRPLEDPDLGAAVADAMADTNTMRGGQRAASALADWVAQHAGPPQAMALIANKMEDVVASDRSVLRVDQLARRLDLSVRSLQRLCEKYIGLPPLAVIRRYRLQEAAQRLREDSSVTVAQVAAELDYADHAHLTADFRRVLGLSPSQYRQQTMSDRQVLSDR$","Transcriptional regulator, AraC-family","Cytoplasm, Periplasm","putative AraC-family transcriptional regulator","putative transcriptional regulator","helix-turn-helix- domain containing protein, AraC type","","Postma P.W., Lengeler J.W., Jacobson G.R. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 1993. 57(3):543-594. PMID: 8246840Meadow N.D., Fox D.K., Roseman S. The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Annu. Rev. Biochem. 1990. 59:497-542. PMID: 2197982","","","

InterPro
IPR000005
Domain

Helix-turn-helix, AraC type
PR00032	$\"[160-175]T$ $\"[175-191]T$	HTHARAC
PF00165	$\"[147-192]T$	HTH_AraC
SM00342	$\"[107-191]T$	HTH_ARAC
PS01124	$\"[87-193]T$	HTH_ARAC_FAMILY_2

InterPro
IPR002114
PTM

Phosphotransferase system, HPr serine phosphorylation site
PS00589	$\"[99-114]?$	PTS_HPR_SER

noIPR
unintegrated

unintegrated
PTHR11019	$\"[108-193]T$	THIJ/PFPI
PTHR11019:SF11	$\"[108-193]T$	ARAC FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN
signalp	$\"[1-31]?$	signal-peptide

","BeTs to 9 clades of COG2207COG name: AraC-type DNA-binding domain-containing proteinsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2207 is --------v-rlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000005 (Helix-turn-helix, AraC type) with a combined E-value of 3.2e-10. IPB000005 160-191***** IPB003313 (Arac protein, arabinose-binding/dimerisation) with a combined E-value of 8.4e-06. IPB003313E 108-153 IPB003313F 155-195","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 147 to 192 (E_value = 8.2e-09) place ANA_0726 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, AraC family.","","AraC-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0727","766634","768289","1656","5.01","-23.88","60244","ATGCTGAATCCGGTTGACCCCACCACCACGCCCGCCTGGAAGCGCCTCACCGAGCTCCACGACACCATGACCCCGGACCTGCGCGCCTGGTTCGCCGACGATCCCGAGCGCGCCGAGCGCTTCTCCTACGAGCTGGGAGACCTCTACATCGACCTGTCCAAGAACCTGCTGACCGACGACGTCCGCGCCGCCCTGGTCGAGCTCGCCGAGCAGGTCGACGTCCCGGGCCGCCGCGACGCCATGTACGCCGGCGAGCACATCAACATCACCGAGGACCGTGCCGTCCTCCACACCGCCCTGCGTCGCCCGGCCGCCGACTCCCTGACCGTGGACGGCCAGGACGTCGTCGCCGACGTTCACGAGGTCCTGGAGAAGATCTACGCCTTCGCCCGACGTGTGCGCTCGGGGGAGTGGACCGGCATCACCGGCAAGCCCATCAAGACGGTGGTCAACATCGGCATCGGCGGCTCCGACCTCGGCCCCGTCATGGTCTATGAGGCCCTCAAGCCCTACGTGCAGAAGGGCCTTGAGTGCCGCTTCATCTCCAACATCGACCCCACCGACTGTGCCGAGAAGGTCGCGGACCTCGACCCGGAGACGACCCTGTTCATCATCGCCTCCAAGACCTTCACCACCCTGGAGACCCTCACCAACGCCCGCATGGCCCGCGACTGGTTCCTGGCCGCCCTCCAGGCCAAGGGCATTGAGACCGACGGCGCCATCGCCAAGCACTTCGTGGCCGTCTCCACCGCCCTGGACAAGGTCGCCGAGTTCGGCATCGACCCGGCCAACGCCTTCGGCTTCTGGAACTGGGTGGGTGGACGCTACTCGGTGGACTCCGCCGTCGGTACGGTCCTGGCCGTGGCCATCGGCCCGGAGAACTTCGCCGACTTCCTCTCCGGCTTCCACACCGTTGACGAGCAATTCGCCACCAAGGCCCCGGCCGAGAACGTCCCCATGCTCATGGGCCTGCTCAACGTCTGGTACGTCAACTTCTTCAAGGCCGGCTCCCACGCCATCCTGCCCTACGCCCAGTACCTGCACCGCTTCCCCGCCTACCTCCAGCAGCTCACCATGGAGTCCAACGGCAAGTCCGTGCGCTGGGACGGCAGCCCCGTGACCACCGAGACCGGCGAGGTCTTTTGGGGTGAGCCGGGCACCAACGGCCAGCACGCCTTCTACCAGCTCATCCACCAGGGCACCCAGCTCATCCCCGCGGACTTCATCGCCGTGGCCAATCCTGCGCACCCCACCAAGGACGGGGGAGTGGACGTCCATGAGCTGTTCCTGTCCAACTACCTGGCCCAGACTGCGGCGCTCGCCTTCGGCAAGACCGCCGAAGAGGTGCGTGCCGAGGGCACCGCCGAGGAGATCGTCCCGGCCCGCGTCTTCGCCGGCAACAAGCCGACCACCTCGATCCTCGCCCCGGCGCTGACGCCCGCGGTCGTCGGAGAGCTCATCGCCCTCTACGAGCACATCACCTTCACCCAGGGCATCGTGTGGGGTATCGACTCCTTCGACCAGTGGGGGGTGGAGCTGGGCAAGAAGCTGGCCCTCGAGATCGCCCCCGCCGTCCAGGGCGACGAGGAGGCCCTCGCAGGACAGGACGCCTCCACCCGCGGCCTCATCACCCGCTACCGCAGCCTGCGCCGCTAG","MLNPVDPTTTPAWKRLTELHDTMTPDLRAWFADDPERAERFSYELGDLYIDLSKNLLTDDVRAALVELAEQVDVPGRRDAMYAGEHINITEDRAVLHTALRRPAADSLTVDGQDVVADVHEVLEKIYAFARRVRSGEWTGITGKPIKTVVNIGIGGSDLGPVMVYEALKPYVQKGLECRFISNIDPTDCAEKVADLDPETTLFIIASKTFTTLETLTNARMARDWFLAALQAKGIETDGAIAKHFVAVSTALDKVAEFGIDPANAFGFWNWVGGRYSVDSAVGTVLAVAIGPENFADFLSGFHTVDEQFATKAPAENVPMLMGLLNVWYVNFFKAGSHAILPYAQYLHRFPAYLQQLTMESNGKSVRWDGSPVTTETGEVFWGEPGTNGQHAFYQLIHQGTQLIPADFIAVANPAHPTKDGGVDVHELFLSNYLAQTAALAFGKTAEEVRAEGTAEEIVPARVFAGNKPTTSILAPALTPAVVGELIALYEHITFTQGIVWGIDSFDQWGVELGKKLALEIAPAVQGDEEALAGQDASTRGLITRYRSLRR$","Glucose-6-phosphate isomerase","Cytoplasm","glucose-6-phosphate isomerase","glucose-6-phosphate isomerase ","Glucose-6-phosphate isomerase","","Lundrigan M.D., Kadner R.J. Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli. Homology among outer membrane receptors that interact with TonB. J. Biol. Chem. 1986. 261(23):10797-10801. PMID: 3015941Schramm E., Mende J., Braun V., Kamp R.M. Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors. J. Bacteriol. 1987. 169(7):3350-3357. PMID: 2439491Nau C.D., Konisky J. Evolutionary relationship between the TonB-dependent outer membrane transport proteins: nucleotide and amino acid sequences of the Escherichia coli colicin I receptor gene. J. Bacteriol. 1989. 171(2):1041-1047. PMID: 2644220Gudmundsdottir A., Bell P.E., Lundrigan M.D., Bradbeer C., Kadner R.J. Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport. J. Bacteriol. 1989. 171(12):6526-6533. PMID: 2687240","","","

InterPro
IPR001672
Family

Phosphoglucose isomerase (PGI)
PR00662	$\"[149-168]T$ $\"[266-284]T$ $\"[343-364]T$ $\"[466-484]T$ $\"[484-498]T$ $\"[498-511]T$	G6PISOMERASE
PTHR11469	$\"[1-551]T$	GLUCOSE-6-PHOSPHATE ISOMERASE
PF00342	$\"[51-543]T$	PGI
PS00174	$\"[498-515]T$	P_GLUCOSE_ISOMERASE_2
PS00765	$\"[270-283]T$	P_GLUCOSE_ISOMERASE_1

InterPro
IPR010916
Domain

TonB box, N-terminal
PS00430	$\"[1-113]?$	TONB_DEPENDENT_REC_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.10490	$\"[4-511]T$	no description

","BeTs to 19 clades of COG0166COG name: Glucose-6-phosphate isomeraseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0166 is -omp-zyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB001672 (Phosphoglucose isomerase (PGI)) with a combined E-value of 3.8e-154. IPB001672A 81-101 IPB001672B 152-161 IPB001672C 196-226 IPB001672D 266-284 IPB001672E 295-334 IPB001672F 340-364 IPB001672G 377-401 IPB001672H 425-445 IPB001672I 483-515","Residues are similar to a () protein domain () which is seen in .","","-67% similar to PDB:1GZD CRYSTAL STRUCTURE OF PIG PHOSPHOGLUCOSE ISOMERASE (E_value = 3.9E_154);-67% similar to PDB:1GZV THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE FROM PIG MUSCLE COMPLEXED WITH 5-PHOSPHOARABINONATE (E_value = 3.9E_154);-67% similar to PDB:2CVP Crystal structure of mouse AMF (E_value = 5.1E_154);-67% similar to PDB:2CXN Crystal structure of mouse AMF / phosphate complex (E_value = 5.1E_154);-67% similar to PDB:2CXO Crystal structure of mouse AMF / E4P complex (E_value = 5.1E_154);","Residues 51 to 543 (E_value = 2.3e-250) place ANA_0727 in the PGI family which is described as Phosphoglucose isomerase.","","isomerase (pgi)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0728","768353","768649","297","4.88","-4.09","10356","ATGAAGGAAATCAATGTCGATGAGCTGCGGCGGCGGCTCGAGGTGGGGGAGGACCTGGTGGTTCTCGACGTGCGTGAGCCCGACGAGGTCGAACGCGCGGCGATCCCCGGCTCAGTCAACATCCCGCTGGGCGAGGTGACCGACCGGATGGGCGAGCTCGATGCGGCCCGCCCCACCGCGGTCATCTGCGCCGGCGGAGTGCGCTCCGCCAAGGCGGTCAAGGCCCTGACTGCTGCCGGCTACACCGGTGAGCTGGTCAACGTCAGCGGCGGCATGAAGGCGTGGCTGGGCCAGTAA","MKEINVDELRRRLEVGEDLVVLDVREPDEVERAAIPGSVNIPLGEVTDRMGELDAARPTAVICAGGVRSAKAVKALTAAGYTGELVNVSGGMKAWLGQ$","Molybdopterin biosynthesis protein","Cytoplasm","Molybdopterin biosynthesis MoeB protein","hypothetical protein predicted by Glimmer/Critica","Rhodanese domain protein","","Hofmann K., Bucher P., Kajava A.V. A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. J. Mol. Biol. 1998. 282(1):195-208. PMID: 9733650Gliubich F., Gazerro M., Zanotti G., Delbono S., Bombieri G., Berni R. Active site structural features for chemically modified forms of rhodanese. J. Biol. Chem. 1996. 271(35):21054-21061. PMID: 8702871","","","

InterPro
IPR001763
Domain

Rhodanese-like
PF00581	$\"[5-98]T$	Rhodanese
SM00450	$\"[4-98]T$	RHOD
PS50206	$\"[15-97]T$	RHODANESE_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.250.10	$\"[1-96]T$	no description
PTHR13253	$\"[7-96]T$	FAMILY NOT NAMED

","BeTs to 14 clades of COG0607COG name: Rhodanese-related sulfurtransferasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0607 is aomp--yq-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 3","***** IPB001763 (Rhodanese-like) with a combined E-value of 2.2e-08. IPB001763A 21-38 IPB001763B 81-95","Residues 29-95 are 62% similar to a (TRANSFERASE SULFURTRANSFERASE DOMAIN THIOSULFATE GLPE HYDROLASE METABOLISM GLYCEROL RHODANESE-RELATED RHODANESE-LIKE) protein domain (PD002675) which is seen in Q6SKE4_ARTAU.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 98 (E_value = 9.5e-16) place ANA_0728 in the Rhodanese family which is described as Rhodanese-like domain.","","biosynthesis MoeB protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0729","769541","768711","831","4.71","-19.17","29255","TTGCCTGCGCAGATCGATCTCCGTCTTGTCGTCACCGACATGGATGGGACTCTCCTTGATGGTCAGGGGCGCGTTCCCGCCGGGCTGCTTGAGGCAGTCGAAGACATGCGAGCCGCCGGCATCGTCTTCACCCCCGCCTCGGGCAGGCAGCTGGCGAACCTGCGTGCGGTCCTGGGCTCCGCCGTCGAGGACTCACCACTGATCGCTGAGAACGGTTCCTTCGTCGTCCACGGCGGTGAGGAGGTCCACTCTGACACCATCAGCGCCCAGGATGCCGAGGCCGCCATCACCACGACCCGCAACCTGGCCGACTCCGGGTACGACGTCGGCGCGGTTGTGGCCTGCAAGCACTGCGCCTACATCGAGCGCTCCGATGCGGCCTTCCTGAAACAGGCCGGTTTGTACTACGAGGCGTTGGAGATCGTCGAGGATCTGACCGCCATCGCCCTGGATGAGGCGCTCAAGGTCGCGGTCTTCGACTTCGACGACGTCGAGAATGGGAGCTCTCAGGCACTGACCGCGGCGGTTCCCCACGTGCAGACCGTCGTCTCCGGGTTGCACTGGACGGACATAATGTCGGCGCAGGTCTCGAAGGGACGGGCCCTGGCGGCGCTTCAGGCCAGGCTCGGGGTCCTCCCGGAGCAGACTGCCGTCTTCGGCGACTACCTCAATGACCTGGATCTCTATGACCACGCGGATCTGGGCTTCGCCATGCGCAATGCCCACCCCGGCATCCATGCCGCGGCGACCTACACGGCGCCCGCCAATACCGAGGATGGTGTCCTGCGTACAGTCGAGGAGCTGCTCAGGCGCTGTCGGAGACAAGGCTGA","LPAQIDLRLVVTDMDGTLLDGQGRVPAGLLEAVEDMRAAGIVFTPASGRQLANLRAVLGSAVEDSPLIAENGSFVVHGGEEVHSDTISAQDAEAAITTTRNLADSGYDVGAVVACKHCAYIERSDAAFLKQAGLYYEALEIVEDLTAIALDEALKVAVFDFDDVENGSSQALTAAVPHVQTVVSGLHWTDIMSAQVSKGRALAALQARLGVLPEQTAVFGDYLNDLDLYDHADLGFAMRNAHPGIHAAATYTAPANTEDGVLRTVEELLRRCRRQG$","HAD-superfamily hydrolase, subfamily IIB","Cytoplasm","Predicted hydrolases of the HAD superfamily","hypothetical protein","HAD-superfamily hydrolase, subfamily IIB","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317","","","

InterPro
IPR006379
Family

HAD-superfamily hydrolase, subfamily IIB
TIGR01484	$\"[9-238]T$	HAD-SF-IIB: HAD-superfamily hydrolase, subf

InterPro
IPR013200
Domain

HAD superfamily hydrolase-like, type 3
PF08282	$\"[10-265]T$	Hydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[3-269]T$	no description

","BeTs to 17 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0561 is aompkzy-vdrlbce-gh-n-j-itwNumber of proteins in this genome belonging to this COG is 6","***** IPB000150 (Cof protein) with a combined E-value of 1e-28. IPB000150A 10-19 IPB000150B 40-49 IPB000150C 66-82 IPB000150D 184-202 IPB000150E 210-241","Residues 13-265 are 57% similar to a (HYDROLASE FAMILY HAD HALOACID HYDROLASE DEHALOGENASE-LIKE SUPERFAMILY COF THE PREDICTED) protein domain (PD173303) which is seen in Q8FQY7_COREF.Residues 14-188 are 56% similar to a (HYDROLASE PREDICTED HAD THE SUPERFAMILY) protein domain (PDA1D0Z9) which is seen in Q6A8E9_PROAC.","","-42% similar to PDB:1RLM Crystal Structure of ybiV from Escherichia coli K12 (E_value = 7.5E_14);-42% similar to PDB:1RLO Phospho-aspartyl Intermediate Analogue of ybiV from E. coli K12 (E_value = 7.5E_14);-42% similar to PDB:1RLT Transition State Analogue of ybiV from E. coli K12 (E_value = 7.5E_14);-41% similar to PDB:2HF2 Domain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPH (E_value = 2.2E_13);-39% similar to PDB:1RKQ Crystal structure of NYSGRC target T1436: A Hypothetical protein yidA. (E_value = 7.8E_11);","Residues 6 to 268 (E_value = 0.00015) place ANA_0729 in the S6PP family which is described as Sucrose-6F-phosphate phosphohydrolase.Residues 7 to 242 (E_value = 4.7e-05) place ANA_0729 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.Residues 10 to 265 (E_value = 2.2e-46) place ANA_0729 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.","","hydrolases of the HAD superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0730","770684","769725","960","8.39","1.42","32592","ATGAACATCAAGCGCGTCATCGCCGCAGCTGCGCTCACCGTCGTGCCGCTGACCGCCTCCTCGGCCGCACTGGCCGCTCCGGTCGCCCCTGAGGGTGCACCGGCAGCAGCCGCCGCGGTTCCCGCCCAGGTGACCTCGGAGGGGGCCCAGTACGCCAACACCGTCCTGAACAAGGTCAACGAGCTGCGCAGCAGCATGGGCCTTCAGCCCGTGACCCGGTACCAGGAGCTCGACGCCGTCGCACAGGACTGGTCCGAGCAGCAGGCCGCCGCCAACAACATGAGCCACCGCCCCGACTTTACGTCGGTCTACCCGCAGGGCTGGACCACAGGCTCTGAGAACGTGGCCTGGCGTACCTCGGGTGGCGACACCGGCGCACTGATCTTCGAGCAGTGGCGCAACTCCCCCGGCCACTACAAGAACATGACGGACCCGAACGTCAACTCCATCGGCATCGGATTCGCGCCGACCTCGGACGGCAAGTGGTACGCCACCCAGAACTTCGCCGCCTACAACGTCAGCAACTCGACGCTGACTCCGACGACCACGACGACCACCAACACCACGACGACGAAGAGCAACACCCCGCCGTCGACGACTGACACCCCACCGACGGGCACCACGGTCCCCAGCCCGACGCCGACCCCGGAGACCACTCCGTCGACGCCGACCACCTCGACGACTCCTCCGGCTCCGGTCGCTCCCCCGACCGCGCAGACCACCACCCCTTCGACCACGCCGACGCCGTCCGCTCCGGCCACCACGGTGACCACTGAGACCGTCACGACCACCGGTACCCCGGCCAAGCCGTCCGCGACTCCTGTCGTTGCGGCTCCTCGCACGACCCCGACGAAGCCCGCGCTGGCCACCACCGGTCCGAGCATCGCCGTTGCCGTCGTCGCCGCCGGCCTGCTCGGCTCCGGCGCCTTCCTCGTCATGCGTCGCCGCCAGGCCAGCTAA","MNIKRVIAAAALTVVPLTASSAALAAPVAPEGAPAAAAAVPAQVTSEGAQYANTVLNKVNELRSSMGLQPVTRYQELDAVAQDWSEQQAAANNMSHRPDFTSVYPQGWTTGSENVAWRTSGGDTGALIFEQWRNSPGHYKNMTDPNVNSIGIGFAPTSDGKWYATQNFAAYNVSNSTLTPTTTTTTNTTTTKSNTPPSTTDTPPTGTTVPSPTPTPETTPSTPTTSTTPPAPVAPPTAQTTTPSTTPTPSAPATTVTTETVTTTGTPAKPSATPVVAAPRTTPTKPALATTGPSIAVAVVAAGLLGSGAFLVMRRRQAS$","SCP-like extracellular protein","Extracellular, Periplasm, Cellwall","SCP-like extracellular protein subfamily,putative","allergen V5/TPX-1 family protein","LPXTG-motif cell wall anchor domain","","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
TIGR01167	$\"[287-318]T$	LPXTG_anchor: LPXTG-motif cell wall anchor

InterPro
IPR014044
Domain

SCP-like extracellular
PF00188	$\"[56-168]T$	SCP

noIPR
unintegrated

unintegrated
PR01217	$\"[179-191]T$ $\"[196-212]T$ $\"[218-230]T$ $\"[231-252]T$ $\"[252-268]T$ $\"[269-286]T$	PRICHEXTENSN
G3DSA:3.40.33.10	$\"[49-169]T$	no description
PTHR10334	$\"[60-132]T$	CYSTEINE-RICH SECRETORY PROTEIN (CRISP/SCP/TPX1)-RELATED
PTHR10334:SF8	$\"[60-132]T$	GOLGI-ASSOCIATED PLANT PATHOGENESIS-RELATED PROTEIN 1 (GOLGI- ASSOCIATED PR-1 PROTEIN)
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[292-312]?$	transmembrane_regions

","BeTs to 4 clades of COG2340COG name: Uncharacterized protein with SCP/PR1 domainsFunctional Class: S [Function unknown]The phylogenetic pattern of COG2340 is a-----y--d--b--f-----j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB007758 (Nsp1-like, C-terminal) with a combined E-value of 1.3e-10. IPB007758B 174-211 IPB007758C 226-270 IPB007758B 223-260 IPB007758C 214-258 IPB007758C 210-254 IPB007758C 151-195 IPB007758C 241-285 IPB007758C 229-273 IPB007758C 248-292 IPB007758C 244-288 IPB007758C 202-246 IPB007758C 192-236 IPB007758C 230-274 IPB007758C 242-286 IPB007758C 216-260 IPB007758C 153-197 IPB007758C 180-224 IPB007758C 177-221 IPB007758C 253-297 IPB007758C 213-257 IPB007758C 256-300","Residues 50-168 are 46% similar to a (TRANSMEMBRANE PRECURSOR SIGNAL SIMILAR UNCHARACTERIZED YKWD MEMBRANE MUCIN EXTRACELLULAR SCP-LIKE) protein domain (PD023876) which is seen in Q897P1_CLOTE.","","No significant hits to the PDB database (E-value < E-10).","Residues 56 to 168 (E_value = 6.4e-19) place ANA_0730 in the SCP family which is described as SCP-like extracellular protein.","","extracellular protein subfamily, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0732","771773","771336","438","11.18","12.86","15670","ATGGCAGCTCACCCTCGTTCCGCCCCCAGCGGCAACAGCACCCCAGGTGCTCCGACGTCGGCTCGTATCGACGTCTGGCTGTGGAGCGTGCGGCAGATCAAGTCCCGCTCGGCAGCGACGAGCGCCTGCAAGGCGGGGCACGTGCGCATCAACGGGGAGACCGCCAAGCCCGCCCAGCACGTCTCAGTGGGGGACGAGGTCCGCTACCGTATCGACGGGTTCGACCGCCTGCTGACCGTCACTCGGATCCTCACTAAGCGGGTGGGAGCACCCATCGCCCGGACCGCGTACATCGACTCCTCTCCCCCTCGCCCGTCTCCTCTGGACGCGCCGGCCGCCGTCATCCGAGATCGCGGGGCGGGCCGGCCTACGAAGAAGGAACGACGTCAGCTCGACGCCCTCATGGGAGGCGGGCGCCATCAGGATGACCGCTTCTGA","MAAHPRSAPSGNSTPGAPTSARIDVWLWSVRQIKSRSAATSACKAGHVRINGETAKPAQHVSVGDEVRYRIDGFDRLLTVTRILTKRVGAPIARTAYIDSSPPRPSPLDAPAAVIRDRGAGRPTKKERRQLDALMGGGRHQDDRF$","Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit","Membrane, Cytoplasm, Extracellular","Ribosome-associated heat shock proteinimplicated in the recycling of the 50S subunit (S4","K04762 ribosome-associated heat shock protein Hsp15","RNA-binding S4 domain protein","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Aravind L., Koonin E.V. Novel predicted RNA-binding domains associated with the translation machinery. J. Mol. Evol. 1999. 48(3):291-302. PMID: 10093218","","","

InterPro
IPR002942
Domain

RNA-binding S4
PF01479	$\"[21-67]T$	S4
SM00363	$\"[21-79]T$	S4
PS50889	$\"[21-89]T$	S4

noIPR
unintegrated

unintegrated
G3DSA:3.10.290.10	$\"[13-106]T$	no description

","BeTs to 8 clades of COG1188COG name: Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1188 is --------v--lb-efgh-nuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 15-137 are 53% similar to a (HEAT SHOCK-LIKE SHOCK) protein domain (PD497793) which is seen in Q92L27_RHIME.Residues 24-97 are similar to a (SHOCK HEAT HSP15 RIBOSOME-ASSOCIATED RNA-BINDING THE IMPLICATED MLR3853 RECYCLING 50S) protein domain (PD021159) which is seen in Q6NGE9_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 21 to 67 (E_value = 3.8e-11) place ANA_0732 in the S4 family which is described as S4 domain.","","heat shock protein implicated in the recycling of the 50S subunit (S4 paralog)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0733","772857","771796","1062","7.96","2.74","37429","ATGAACGCTTCCGGTCGGCTCCTGGCGCGCCTGACGGTGCTCGGCGTGCTCGGTGCGTTCGGGATGACAGCAGGTCTTCCCGTTCACGCTGATGACGCCTCGCCGGAGTCCTCCCAGAGGTCAGCGGCCACGGAGCTCGCTGCTCTCCATGAGGCGCCCTGGGACCGCAGAGGCGACTTCATCCTGTCTGTGAGCGCCTCTCTTGAGGCGCTCGCAGAGCTGCCCGACGACGCTCCGGCCGCACGGTCCTGGGCCGAGGGAGGTTCCCGCACCGGCTGGTTCGGTGAAGCGTGGACCGACGTTGACGGCGACGGTTGCGACACTCGCAATGAGATCCTGGCTCGGGACCTGACGGACGCCGACTTCTCGCGTGCCGACGGCGTCCAGTCTCGTGAGGAGGGACGTGGCCGAGGTGCGGGCGTATGCCCGGACGCCACTGTCTGGGCAGGCGTCCTTCAAGATCCCTACACCGGCAGAAGAATCACCTTCACACGTGGTCAGGAGACCTCGGCGACTGTCCAGATCGACCATGTGGTGCCGCTGAACTACCTCTACGCCCACGGAGCCTGGCAGTGGGATGAGCGTACCCGACTGCTGGTGGCCAACGACCCGCTGAATCTCGTCGCCGTTGAAGGCGAGGCCAACCAGACCAAGGGTGCCTGCGGGCCGGCGAGCTGTCCCGTTGGTTCAACCGAGACCGGCAGCTGGCGGCCCACAGGCCCAGGGGGCTGGTGGCCGGCCGACACTTCCTACCGCTGCACCTATGCACGTCGCTTCGTCTCAGTGGCCGCCGCCTACCGGCTTGGCCTGCCCCAGGCCGACAAGGCCGCACTGAGCACCACCTTGAGCAGCTGTCTCACAGGTGGCGACGGGACTGCATCCCTCCCCGAACGAGCCGCTCGTACCGCAAAGGAGGTCGGCTCCGTTGTGTGGCGCAGCCCCGGGTATGCCGCGCTGGCAGCGGTTGGCGCCCTGGTTCTGGGCTGCGGGCTCATCCTTCGGGGCAGACGCCGAGGGCGCGCATCCTCGCGGCGACGTCGCCGTTCTGCGTCCCGCCGCTGA","MNASGRLLARLTVLGVLGAFGMTAGLPVHADDASPESSQRSAATELAALHEAPWDRRGDFILSVSASLEALAELPDDAPAARSWAEGGSRTGWFGEAWTDVDGDGCDTRNEILARDLTDADFSRADGVQSREEGRGRGAGVCPDATVWAGVLQDPYTGRRITFTRGQETSATVQIDHVVPLNYLYAHGAWQWDERTRLLVANDPLNLVAVEGEANQTKGACGPASCPVGSTETGSWRPTGPGGWWPADTSYRCTYARRFVSVAAAYRLGLPQADKAALSTTLSSCLTGGDGTASLPERAARTAKEVGSVVWRSPGYAALAAVGALVLGCGLILRGRRRGRASSRRRRRSASRR$","Hypothetical protein","Extracellular, Membrane","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[315-333]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 94-177 are 54% similar to a (LIPOPROTEIN EXPORTED OR MEMBRANE POSSIBLE CGL1265 MLCB1243.02 EXTRACELLULAR DEOXYRIBONUCLEASE PLASMID) protein domain (PD035773) which is seen in Q8FM54_COREF.Residues 178-279 are 53% similar to a (SECRETED LIPOPROTEIN EXPORTED PLASMID OR MEMBRANE POSSIBLE PRECURSOR SIGNAL CGL1265) protein domain (PD244661) which is seen in Q9F2P3_STRCO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0734","773734","772940","795","5.88","-6.74","27459","ATGACTGACAACCGCACGGCTGACGCCCAGGCGATCACTGAGATCCAGGCGGCGGCCTCCTCGGCTGCCAAGCCAGAGGTCATGGTGCTTCCCACCTTGAGCGACGCCGCACGCAGGGCCTGCCAGGACACCGTGCGGGTCCTGGCCGCGGCGGTGACGAATCGGGGCGTCGCCCACCTGGCGCTGACAGGCGGTTCCGGGGGGATGGCGCTGTCTGAGACCCTTGCGCCGCTCATCGCCGCCCAGCACGAGACGGTGCGCCGTGCCATCCACCTGTGGTTCGGCGACGAGCGCTTCGTGCCCGCCGGGGACCCGGAGCGTAACGATCTGCTGGCCACTCCTCTCATCGCCGCAGGCATCAGGGAGTCTCAGACACACCGGCTGGTCGCTCCGAACGAGGTCGGTGGCCTGGATGAGGCGACCGCCCGCATGGTCCACGAGCTCGAGTCGGCGGGTGTGGCCCACAGCGGCTTCGACGTCGTCCACGTGGGGTTGGGACCTGACGCACACGTCTGCTCCCTCTTCCCCGGGCACCCGGCTGCACTCGCGGTGGGAGTGCCCGCCGTAGCCGTGCGCAACTCACCCAAGCCGCCTCCCGAGCGCTACTCGCTGACCTTCGAGGCCTTGCAGCATGCCGGCCGAGTCATGGTGGTGGCCGGTGGTGAGGGCAAGGCCGAGGCGGTCCGCCTGGGGCTGGGTACTCCCGATGTGCTCAAGGCACCGGCCTCATGCTGCCGGGGAGAGCAGACCACCTGGTACCTGGATGAACCGGCCAACGCTCTGATGACTGATTGA","MTDNRTADAQAITEIQAAASSAAKPEVMVLPTLSDAARRACQDTVRVLAAAVTNRGVAHLALTGGSGGMALSETLAPLIAAQHETVRRAIHLWFGDERFVPAGDPERNDLLATPLIAAGIRESQTHRLVAPNEVGGLDEATARMVHELESAGVAHSGFDVVHVGLGPDAHVCSLFPGHPAALAVGVPAVAVRNSPKPPPERYSLTFEALQHAGRVMVVAGGEGKAEAVRLGLGTPDVLKAPASCCRGEQTTWYLDEPANALMTD$","6-phosphogluconolactonase","Cytoplasm","6-phosphogluconolactonase","6-phosphogluconolactonase ","6-phosphogluconolactonase","","","","","

InterPro
IPR005900
Domain

6-phosphogluconolactonase
TIGR01198	$\"[29-262]T$	pgl: 6-phosphogluconolactonase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1360	$\"[12-256]T$	no description
PTHR11054	$\"[13-258]T$	6-PHOSPHOGLUCONOLACTONASE

","BeTs to 13 clades of COG0363COG name: 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0363 is ------y-v-rlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 27-260 are 41% similar to a (6-PHOSPHOGLUCONOLACTONASE) protein domain (PDA0L6L4) which is seen in Q7NGI9_GLOVI.Residues 37-170 are 47% similar to a (HYDROLASE 6-PHOSPHOGLUCONOLACTONASE) protein domain (PDA1B928) which is seen in Q6A7F7_PROAC.Residues 90-260 are 53% similar to a (ISOMERASE DEAMINASE GLUCOSAMINE-6-PHOSPHATE HYDROLASE METABOLISM CARBOHYDRATE GNPDA GLCN6P PHOSPHATE GLUCOSAMINE-6-) protein domain (PD006132) which is seen in 6PGL_MYCTU.Residues 90-170 are 54% similar to a (6-PHOSPHOGLUCONOLACTONASE) protein domain (PDA1A5D3) which is seen in Q829U8_STRAW.","","-44% similar to PDB:1Y89 Crystal Structure of devB protein (E_value = 1.2E_13);","No significant hits to the Pfam 21.0 database.","","(pgl) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0735","774698","773727","972","5.45","-9.09","35052","ATGATTACCACACTGACCGCGACGACCACGTCCCGGATCGTCTCCCGGCTGGTGGAGCACGAGGGGACCTCCGGCTCCTCCCGGGTGCTGACACTCGTGATCTCCACCGACGAGAAGGGCCTGGAGGATGCGCTGTGCGCCGCGCACGGCGCCAGCCGGGATCACCCCAGCCGCATCATCGCCGTCGTCAAACCGCCTGAGGAGGACGCTGTCGGTCGCGCGACTCCGCGCAGCCGTGACGGACATGTCCCGGCCCAGGCCGGTGGGCACCTGGACGCTGAGATCCGTGTTGGTCACGACGCCGGTGCGGGTGAGACGCTGGTCCTGCGGCCCTGGGACGAGGCGGCTCTGCACACCGACACGCTGGTGGTGCCCTTTCTTCTGCCCGACGCCCCGGTGGTCGTGTGGTGGCCGACGACCGTCCCCGAGATCCCCTCACAGGATCCCTTGGGACGCCTGGGCTCCACACGCATCACCAACACTCCCGCGCAGGACTTCCCGGCCAGGGCGCTGCGGGCGCTGGCACCGGTAAGCGCACGTGGCGACATCGACCTGGCCTGGACTCGCATCACCCTGTGGCGCGCCATGGTGGCCTCCACCCTGGACCCGCTGCTGCGTGCGGGCAGCCTGCGAGAGGTCGTGGTCGCCGGCGAGCCGAGGAACTCCTCGCTCTCCCTCATGATCGCGTGGTTGCGGCTTCGGCTGGACGTACCGGTCACACGAGTCGATGAGGAGGGCTTCAAGGGCATCTCCTCCATCACCGCCAGAACCGACGACGGCGAGGTCATCATCGCCCGCCACGACCTGGAGCGGGTCACCATCACGCGCCCCGGCTCCCCGGAGCCCCAGGTGGTCACGATGGCCCGGCGCGAGCCGATCAGCACCCTCAATGAGGAGCTGCGCCGGCTCACCCCCGACCTCGTCTACCAGGAGGTCCTGGCCACACTGCTCGAGGAGCCCGTCAATGACTGA","MITTLTATTTSRIVSRLVEHEGTSGSSRVLTLVISTDEKGLEDALCAAHGASRDHPSRIIAVVKPPEEDAVGRATPRSRDGHVPAQAGGHLDAEIRVGHDAGAGETLVLRPWDEAALHTDTLVVPFLLPDAPVVVWWPTTVPEIPSQDPLGRLGSTRITNTPAQDFPARALRALAPVSARGDIDLAWTRITLWRAMVASTLDPLLRAGSLREVVVAGEPRNSSLSLMIAWLRLRLDVPVTRVDEEGFKGISSITARTDDGEVIIARHDLERVTITRPGSPEPQVVTMARREPISTLNEELRRLTPDLVYQEVLATLLEEPVND$","Glucose-6-P dehydrogenase subunit;oxpp cycle protein","Cytoplasm","oxppcycle protein OpcA","oxppcycle protein","Glucose-6-P dehydrogenase subunit-like","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 29-242 are 61% similar to a (OPCA OXPPCYCLE GLUCOSE-6-P DEHYDROGENASE OXPP CYCLE B1496_F1_30 ACTIVITY BCR UNCHARACTERIZED) protein domain (PD333012) which is seen in Q82M91_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein OpcA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0737","776278","774695","1584","5.75","-8.07","58721","GTGTCCAGCTCCGATTCTGCGACTCCGTTCCCGTCGTCGAGACCCACGCGGGCGGCCAACCCGCTTCTCGACGCCCGCGATCTTCGCCTTCCGCGTATCGCGGACCCCTGCGTCCTAGTGATGTTCGGCATCACTGGTGATCTGGCTCGTCACAAGCTCCTGCCCGCGATCTACGACCTGGCCAACCGGGGCCTGCTCTCCCCCAGCTTCTCCCTGGTGGGGGTCGGCCGGCGCTCCTGGTCCGACGACGACCTGCGCGCCTACGTGGAGAAGTCGGCTCGGGAGGGCGCCCGCACCCCGTGGCGTCCCGCCATCTGGGAGCAGCTGGCAGCGGGGATGCGCTTCGTGGAGTTCGCCTCCTTCGAGGACGACGCCGCCTACGACCGGCTCACGGCCGTGGTGGATGACCTGGACGCCACCCGGGGCACGCGCGGCAACCGCGCCTTCTACCTGTCGATCCCCCCGGGATGGTTCCCGGCCGTGACTGAGCGGATAGCCCGCTCCGGGCTCGTGGAGGAGTCGCCCGAGGCCTGGCGCCGCGTGGTCATTGAGAAGCCCTTCGGGCACGACCGCGCCAGCGCCCGAGAGCTCGATGACCTTGTGGGACGCATCGTGCGTCCCGACGACGTCTTCAGAGTCGACCACTACCTGGGCAAGGAGACGGTGCAGAACATCCTGGCGCTGCGGTTCGCCAACACGATGTTCGAGCCGCTGTGGAACCAGCGCTACGTCGACCACGTCCAGATCACGATGGCCGAGGACATCGGTATCGGAACCCGGGCCGGCTACTACGACACCATCGGCTCGGCGCGCGACGTCATTCAGAACCACCTGCTCCAGCTCCTGGCGCTGACCGCGATGGAGGAGCCCACCAGCATGGAGGCGGCCGCGGTGCGCCTGGAGAAGGAGAAGGTGCTCAACTGCGTTCGCCTGGAGCGCGATGGGGTGCTGGACCTGGACCTCACCACTGCCCGGGGCCGTTACGACGCAGGCTTCCAGGGAGGGCTGCCGGTGCGGGGCTACCTGGAGGAGGACGGCGTCGCCGCCGACTCCCGCACTGAGACCTTCGCTGCCCTGCGCCTGGAGATCGCCAACCGTCGCTGGGCCGGTGTGCCGTTCTACCTGCGTGCCGGTAAGCGCCTGACCCGCCGGGTCACCGAGGTCGCCGTCGTCTTCAAGCAGCCGCCGTTCCTGCCCTTTGAGTCGGCGGCCACCACGGCCGTGGGTGCCAACACCATCGTGCTGCGCATCCAGCCCGATGAGGGCATCACGCTGCGGCTGGCCTCCAAGGTGCCCGGAACCCAGATGGAGCTGCGTGACGTCTCGATGGACTTCGGCTACGGGGCCACCTTCAACGAGGAGTCCCCGGAGGCCTACGAGCGCCTCATCCTCGACGCGCTTTTGGGTGACGCCCCGTTGTTCCCCCACCAGCGTGAGGTCGACCTGTCCTGGCGCATCCTGGATCCCGTCATCGAGCACTGGGGCGCCGGTGGGAGTCCCGAGGGCTATCGCCCCGGCTCCTGGGGGCCGGCCAGTGCTCACGAACTCCTTGCCCGCGACGGCCGCACCTGGAGGCGCTCATGA","VSSSDSATPFPSSRPTRAANPLLDARDLRLPRIADPCVLVMFGITGDLARHKLLPAIYDLANRGLLSPSFSLVGVGRRSWSDDDLRAYVEKSAREGARTPWRPAIWEQLAAGMRFVEFASFEDDAAYDRLTAVVDDLDATRGTRGNRAFYLSIPPGWFPAVTERIARSGLVEESPEAWRRVVIEKPFGHDRASARELDDLVGRIVRPDDVFRVDHYLGKETVQNILALRFANTMFEPLWNQRYVDHVQITMAEDIGIGTRAGYYDTIGSARDVIQNHLLQLLALTAMEEPTSMEAAAVRLEKEKVLNCVRLERDGVLDLDLTTARGRYDAGFQGGLPVRGYLEEDGVAADSRTETFAALRLEIANRRWAGVPFYLRAGKRLTRRVTEVAVVFKQPPFLPFESAATTAVGANTIVLRIQPDEGITLRLASKVPGTQMELRDVSMDFGYGATFNEESPEAYERLILDALLGDAPLFPHQREVDLSWRILDPVIEHWGAGGSPEGYRPGSWGPASAHELLARDGRTWRRS$","Glucose-6-phosphate 1-dehydrogenase","Cytoplasm","glucose-6-phosphate 1-dehydrogenase","glucose-6-phosphate 1-dehydrogenase ","glucose-6-phosphate 1-dehydrogenase","","Fouts D., Ganguly R., Gutierrez A.G., Lucchesi J.C., Manning J.E. Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene. Gene 1988. 63(2):261-275. PMID: 2838391Vulliamy T.J., D. Urso M., Battistuzzi G., Estrada M., Foulkes N.S., Martini G., Calabro V., Poggi V., Giordano R., Town M. Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia. Proc. Natl. Acad. Sci. U.S.A. 1988. 85(14):5171-5175. PMID: 3393536","","","

InterPro
IPR001282
Family

Glucose-6-phosphate dehydrogenase
PD001129	$\"[323-422]T$	Q70AQ7_BBBBB_Q70AQ7;
PR00079	$\"[180-193]T$ $\"[204-232]T$ $\"[256-273]T$ $\"[274-290]T$ $\"[367-393]T$	G6PDHDRGNASE
PIRSF000110	$\"[37-527]T$	Glucose-6-phosphate dehydrogenase
PTHR23429	$\"[85-525]T$	GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE (G6PD)
PF00479	$\"[40-224]T$	G6PD_N
PF02781	$\"[226-527]T$	G6PD_C
TIGR00871	$\"[35-527]T$	zwf: glucose-6-phosphate 1-dehydrogenase
PS00069	$\"[214-220]T$	G6P_DEHYDROGENASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.360.10	$\"[213-524]T$	no description
G3DSA:3.40.50.720	$\"[32-212]T$	no description

","BeTs to 16 clades of COG0364COG name: Glucose-6-phosphate 1-dehydrogenaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0364 is ------yqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB001282 (Glucose-6-phosphate dehydrogenase) with a combined E-value of 2.2e-152. IPB001282A 39-61 IPB001282B 146-158 IPB001282C 212-239 IPB001282D 247-290 IPB001282E 340-388 IPB001282F 411-433 IPB001282G 456-491 IPB001282H 503-521","Residues 36-84 are 83% similar to a (METABOLISM GLUCOSE OXIDOREDUCTASE NADP GLUCOSE-6-PHOSPHATE CARBOHYDRATE 1-DEHYDROGENASE G6PD DEHYDROGENASE CHLOROPLAST) protein domain (PD731451) which is seen in Q6A7F9_PROAC.Residues 135-195 are 77% similar to a (METABOLISM GLUCOSE OXIDOREDUCTASE NADP GLUCOSE-6-PHOSPHATE CARBOHYDRATE 1-DEHYDROGENASE DEHYDROGENASE G6PD CHLOROPLAST) protein domain (PD724648) which is seen in Q82M92_STRAW.Residues 197-304 are similar to a (METABOLISM GLUCOSE OXIDOREDUCTASE NADP GLUCOSE-6-PHOSPHATE CARBOHYDRATE 1-DEHYDROGENASE DEHYDROGENASE G6PD CHLOROPLAST) protein domain (PD457536) which is seen in Q6AF38_BBBBB.Residues 323-422 are similar to a (METABOLISM GLUCOSE OXIDOREDUCTASE NADP GLUCOSE-6-PHOSPHATE CARBOHYDRATE 1-DEHYDROGENASE DEHYDROGENASE G6PD CHLOROPLAST) protein domain (PD001129) which is seen in Q70AQ7_BBBBB.Residues 423-484 are 85% similar to a (METABOLISM GLUCOSE OXIDOREDUCTASE NADP GLUCOSE-6-PHOSPHATE CARBOHYDRATE 1-DEHYDROGENASE DEHYDROGENASE G6PD CHLOROPLAST) protein domain (PD544210) which is seen in Q70AQ7_BBBBB.Residues 486-526 are 75% similar to a (METABOLISM GLUCOSE OXIDOREDUCTASE NADP GLUCOSE-6-PHOSPHATE CARBOHYDRATE 1-DEHYDROGENASE G6PD DEHYDROGENASE 6-PHOSPHATE) protein domain (PD074201) which is seen in Q6AF38_BBBBB.","","-53% similar to PDB:2BH9 X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP (E_value = 7.5E_78);-53% similar to PDB:2BHL X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE (E_value = 7.5E_78);-53% similar to PDB:1QKI X-RAY STRUCTURE OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE (VARIANT CANTON R459L) COMPLEXED WITH STRUCTURAL NADP+ (E_value = 1.3E_77);-54% similar to PDB:1E77 COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE (E_value = 2.2E_77);-54% similar to PDB:1H9A COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L. MESENTEROIDES WITH COENZYME NADP (E_value = 2.2E_77);","Residues 40 to 224 (E_value = 1.3e-82) place ANA_0737 in the G6PD_N family which is described as Glucose-6-phosphate dehydrogenase, NAD binding domain.Residues 226 to 527 (E_value = 4.9e-130) place ANA_0737 in the G6PD_C family which is described as Glucose-6-phosphate dehydrogenase, C-terminal domain.","","1-dehydrogenase (zwf)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0738","776704","778179","1476","5.19","-17.17","52393","ATGACCAGCTTCACCCCCGCACCGGCCACAGCCGACCTCGGTGTCTTCGGGCTGGGGGTGATGGGGGCGAACCTGGCCCGCAACCTGGCTCGTCATGGCCACGCGGTCGCCGTCTTCAACCGCACGCTGGCCCGCACCGAGAGGCTCATCGAACGCTACGGCTCCGAAGGTGACTTCGTGCCCGCAGCCGACCTGAAGGACTTTGTGGCCTCGCTGCGCACGCCGCGCGTGGCCATCATCATGGTTCAGGCCGGAGCGGCCACCGAGGCGGTCATCGAGGAGCTCGCTGCCCTCATGGAGCCCGGTGACATCATCGTCGATGCCGGCAACACGCTCTACACCGACACCCGGCGCCGCGAGGTCTCCCTGCGTGAGCGCGGGCTGCACTTCGTGGGCATGGGGGTCTCCGGAGGCGAGGAAGGGGCACTCAACGGCCCCTCGATCATGCCCGGCGGCACCGCCGAGTCCTACGACCGCCTGGGGCCGATGCTGGAATCCATCTCCGCCCACGTGGACGGCACGCCGTGCTGCACCCACGTCGGTCCCGACGGCGCCGGCCACTTCGTCAAGATGGTCCACAACGGCATCGAGTACGCCGACATGCAGCTCATCGCCGAGGCGTACGACCTGCTGCGCCACGTCGGCGGGTTCACGGTTCCCGAGATCGCCGAGGTCTTCCGCTCCTGGAAGGACTCCGAGCTCGACTCCTACCTCATCGACATCACCACCGAGGTCCTGTCCCACACCGATGCGGCCACCGGTGAGGCCTTCGTCGATGTCGTCGTCGACGCGGCCGGCCAGAAGGGCACCGGCGTGTGGACCACCCAAACGGCCCTCGAGCTGGGAGTGGCCGTGCCCGCCATCGCCGAGGCCACCTTCGCGCGAGCGGTCTCCTCCTCCAGCGCGGCGCGGGCCGCGGTCCAGGCCGCTGATATTGCTGCAGGAACCACACAGACGGCCCTGACCGAACCCGAGGAGCGACGCGCCTTCGTCGATGCCGTCAAGCAGGCCCTCTACGGCTCCAAGATCGCGGCCTACGCCCAGGGCTTCGATGAGATCGCCACCGCCTCCAAGCAGTTCGACTGGAAAATCGACCTGGGCGCCATGGCCCGTATCTGGCGAGGCGGCTGCATCATCCGAGCCCGCTTCCTGGACGACATCACCCGTGCTTACGCCGAGAACCCCTCTCTGGCCAGTCTGCTCACGGCGCCGGTCTTCGCCTCCTCCCTGGCGACGGTTCTGCCCGCCTGGCGCCAGGTCGTGGCCACCTCCGCCACCACCGGCGTCCCCGCCCCGGCCTTCGCCTCCTCCCTGGCCTACGTCGACCAGCTGCGCTCCCGGCGCCTACCGGCCGCCCTCATCCAGGGGCAGCGAGACTTCTTCGGCTCGCACACCTACCACCGCACCGATGACGTCGAGGGCGTCTACCACACCCTGTGGGCCACGCCCGAGCGCACCGAGGAAAAGTGGGACTGA","MTSFTPAPATADLGVFGLGVMGANLARNLARHGHAVAVFNRTLARTERLIERYGSEGDFVPAADLKDFVASLRTPRVAIIMVQAGAATEAVIEELAALMEPGDIIVDAGNTLYTDTRRREVSLRERGLHFVGMGVSGGEEGALNGPSIMPGGTAESYDRLGPMLESISAHVDGTPCCTHVGPDGAGHFVKMVHNGIEYADMQLIAEAYDLLRHVGGFTVPEIAEVFRSWKDSELDSYLIDITTEVLSHTDAATGEAFVDVVVDAAGQKGTGVWTTQTALELGVAVPAIAEATFARAVSSSSAARAAVQAADIAAGTTQTALTEPEERRAFVDAVKQALYGSKIAAYAQGFDEIATASKQFDWKIDLGAMARIWRGGCIIRARFLDDITRAYAENPSLASLLTAPVFASSLATVLPAWRQVVATSATTGVPAPAFASSLAYVDQLRSRRLPAALIQGQRDFFGSHTYHRTDDVEGVYHTLWATPERTEEKWD$","6-phosphogluconate dehydrogenase, decarboxylating","Cytoplasm","6-phosphogluconate dehydrogenase,decarboxylating","6-phosphogluconate dehydrogenase ","6-phosphogluconate dehydrogenase, decarboxylating","","Broedel Jr S.E., Wolf Jr R.E. Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase. J. Bacteriol. 1990. 172(7):4023-4031. PMID: 2113917Adams M.J., Archibald I.G., Bugg C.E., Carne A., Gover S., Helliwell J.R., Pickersgill R.W., White S.W. The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution. EMBO J. 1983. 2(6):1009-1014. PMID: 6641716Reizer A., Deutscher J., Saier Jr M.H., Reizer J. Analysis of the gluconate (gnt) operon of Bacillus subtilis. Mol. Microbiol. 1991. 5(5):1081-1089. PMID: 1659648Guthe S., Kapinos L., Moglich A., Meier S., Grzesiek S., Kiefhaber T. Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin. J. Mol. Biol. 2004. 337(4):905-915. PMID: 15033360","","","

InterPro
IPR006113
Family

6-phosphogluconate dehydrogenase, decarboxylating
TIGR00873	$\"[12-482]T$	gnd: 6-phosphogluconate dehydrogenase, deca

InterPro
IPR006114
Domain

6-phosphogluconate dehydrogenase, C-terminal
PF00393	$\"[186-481]T$	6PGD

InterPro
IPR006115
Domain

6-phosphogluconate dehydrogenase, NAD-binding
PF03446	$\"[10-182]T$	NAD_binding_2

InterPro
IPR006183
Family

6-phosphogluconate dehydrogenase
PR00076	$\"[11-34]T$ $\"[74-103]T$ $\"[127-152]T$ $\"[175-203]T$ $\"[257-284]T$ $\"[369-391]T$	6PGDHDRGNASE

InterPro
IPR006184
Binding_site

6-phosphogluconate-binding site
PS00461	$\"[261-273]?$	6PGD

InterPro
IPR012284
Domain

Fibritin/6-phosphogluconate dehydrogenase, C-terminal extension
G3DSA:1.20.5.320	$\"[448-480]T$	no description

InterPro
IPR013328
Domain

Dehydrogenase, multihelical
G3DSA:1.10.1040.10	$\"[188-447]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[9-187]T$	no description
PTHR11811	$\"[187-481]T$	6-PHOSPHOGLUCONATE DEHYDROGENASE

","BeTs to 11 clades of COG0362COG name: 6-phosphogluconate dehydrogenase, family 1Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0362 is ------y-v-rlbce-gh-n-j-it-Number of proteins in this genome belonging to this COG is 1","***** IPB006115 (6-phosphogluconate dehydrogenase, NAD binding domain) with a combined E-value of 4.9e-178. IPB006115A 13-41 IPB006115B 78-119 IPB006115C 127-152 IPB006115D 175-208 IPB006115E 229-242 IPB006115F 263-301 IPB006115G 337-350 IPB006115H 360-407 IPB006115I 450-466***** IPB002204 (3-hydroxyisobutyrate dehydrogenase) with a combined E-value of 2.9e-15. IPB002204A 13-32 IPB002204C 181-216***** IPB011548 (3-hydroxyisobutyrate dehydrogenase) with a combined E-value of 8e-06. IPB011548A 13-35","Residues 26-129 are 75% similar to a (OXIDOREDUCTASE NADP DEHYDROGENASE REDUCTOISOMERASE 6-PHOSPHOGLUCONATE PENTOSE SHUNT UTILIZATION GLUCONATE KETOL-ACID) protein domain (PD378363) which is seen in Q826E4_STRAW.Residues 130-171 are 88% similar to a (OXIDOREDUCTASE DEHYDROGENASE 6-PHOSPHOGLUCONATE NADP SHUNT PENTOSE UTILIZATION GLUCONATE DEHYDROGENASE DECARBOXYLATING) protein domain (PD511821) which is seen in Q8VJV7_BBBBB.Residues 192-480 are 69% similar to a (OXIDOREDUCTASE SHUNT PENTOSE NADP 6-PHOSPHOGLUCONATE UTILIZATION GLUCONATE DEHYDROGENASE DEHYDROGENASE DECARBOXYLATING) protein domain (PD001025) which is seen in Q93J68_STRCO.","","-63% similar to PDB:2IYO STRUCTURAL CHARACTERIZATION OF A BACTERIAL 6PDH REVEALS ASPECTS OF SPECIFICITY, MECHANISM AND MODE OF INHIBITION (E_value = 8.0E_119);-63% similar to PDB:2IYP PRODUCT RUP (E_value = 8.0E_119);-63% similar to PDB:2IZ0 PEX INHIBITOR-HOME DATA (E_value = 8.0E_119);-63% similar to PDB:2IZ1 6PDH COMPLEXED WITH PEX INHIBITOR SYNCHROTRON DATA (E_value = 8.0E_119);-60% similar to PDB:1PGN CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM (E_value = 4.6E_106);","Residues 10 to 182 (E_value = 3.8e-89) place ANA_0738 in the NAD_binding_2 family which is described as NAD binding domain of 6-phosphogluconate dehydrogenase.Residues 13 to 165 (E_value = 0.0049) place ANA_0738 in the ApbA family which is described as Ketopantoate reductase PanE/ApbA.Residues 186 to 481 (E_value = 8.2e-175) place ANA_0738 in the 6PGD family which is described as 6-phosphogluconate dehydrogenase, C-terminal domain.","","dehydrogenase, decarboxylating (gnd)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0740","778360","780954","2595","5.25","-33.56","94246","GTGGCTGTCGACGTCACCGGGGCCATCGACCGCCACGAGGCCACCTTCAGCGTGCGTTGCCTGATGAGCCTGGACATCAGGCAACGCGCCGAAGGACTCTGGGTGGACTTCGTGGGGCAGGCGATCGACTCCCTCAGCATCGACGGGCAACCCGCCCCGGTGACCTGGGACGGGGCCCGTATCGAGCTGCCCGTCCTCGACCCGGGCGAGCACACGGTGGAAATCGCGGCGCGCGGCCTCTACTCCAACTCGGGTCAGGGGCTGCACCGCTTCCACGACCCGGTCGATGGCGCCACCTACCTCTACACCCACTTCGAGCCCTCCGACGCGCGCCGGGCCTGGCCGGTCATGGAACAGCCGGACATCAAGACCCGCTTCTCGCTGGAGGTCAAGCACCCCCGCGGCTGGACAGTCATGTCCAACGCGCGACCGACGGCGGGCAGCTCGAGTGTCTCGGTCGGCACCGACTCCGGCTATGAGACGACGTCCTTCGCCGCCTCCAGGCCCCTGCCCAGCTACCTCACCGCACTGGCCGCCGGCCCCTGGCACCGAGTGACCGGGCAATGGACGTCACCGAGCCGACCGGGCCTGACGGTCCCGCTGTCCTGGTCCTGCCGCGCCAGCCTGGCCGAGCACCTCGATGCCGCCGAGCTCCTCGACCTGACCCGCGCCGGCCTGGACCTCTACGACCGGGCCTACGCCTACGGCTTCCCCTGGGACTCCTACGACAGCGTTCTCGTCCCGGAGTACAACCTCGGAGCCATGGAGAACCCGGGCTGCGTCACCTTCAACGAGGAGCTCTACCTCTTCAGAGGACCGGTCACCCGCTCCCAGAGGGCCGGACGCGCCAACACGATCCTCCACGAGATGTGTCACATGTGGTTCGGTGACCTCGTGACCCCCACCTGGTGGGAGGACACCTGGCTCAAAGAGTCCTTCGCCGATCACCAGGGCACCTGGGCCGAGGCCGAAGCCGCCGGCTACACCGAGGCCTGGGTGAGCTTCGCCTCCACCCGTAAGGCCTGGGCCTACCTGGAGGACTCCCGGCCGGCCACCACCCACCCCATTGTCGCGCAGGTCGACGACGTCGAGGCCGCCCGGCAGGCCTTCGACGGCATCACCTACGCCAAGGGCGCCGCCGTCCTCAAGCAGCTCGTCGCCCATGTCGGCCAGGAGGCCTTCTTCAAGGCCGCGGGGCTCCTCTTCGAGCGCAGGGCCTACGGCAACGCATGCCTGGACGACTTCCTGGGCGTGCTCTCCCAGGTCTCGGGCCGAGACATGCACGACTGGGCCCGCGCCTGGCTCCACACCGCAGGCCCCTCGGTCATCACCGACGAGCTGGCCGTTCATGAGGGACGGATCGCCTCCCTGACCCTGCAGCAGGAGGGGATCGACCCGGTGACCGGGCAGAGCGTCCTGCGTCCGCACACGCTCGTCGTCGGCCTGTACTCCTTCGACGGGGATGGGGCGCTGGTACGCACCCACCGGCTGCCGGTGGTCCTGGAGGCCGAGCAGCTCGACATCGTCGAGGCCGTGGGACTGCCCGCTCCCGATCTCGTCATCGTCAACGACGAGGACCTCACCTACGCCGTCGTGCGGCCCGACGACACCTCGCTGTCCTGCCTGGCCGCTTCGCTCGGAGCCCTGCGCGATCCCATGGCGCGGTCCTTGACCTGGTCGATGCTGCACAACCTCGTCCGCGACGCGGTCATCGATGCGGCACTGTTCGTCCAGGCCGTCCTGGCGCACGCCGACGACGACACCGAGCCGAGCACCCTGACCGTCCTGCTGAACCAGGCGCTACGAGTCACGAGCAGGTATGCCGGCCCGCACACGCGGCGCGCGCTCCTGGAACGCCTCGTGGCCGATGACTCGACCGAGCCCTCGAAGATGACGGACCCGGCTTTCCTGCACGGCGGGTGGGGCAGGCTCCGCGCTTCCGCGCCGGGCTCCGACGCCCAGATCGTCCGGGCCCGTGCCTGGCTGGAGGCTGCAGGGCAGGCGCGGCTGCTCGGTGAGGCGGGCAGCGCTCAGGCGGCTGCTCGTGTACGGGAGATACTGGACGGGGCTCTTCCCGGACTGGAGCTGGACGCCGACATGCGATGGCGGGCCCTGACCGCCTTGGCGCAACTGGACGCCGTCAGTGCCGACGAGCTCGAGGCGCAGCGGAAGGCGGACCCGACGGCCAGCGGCATCACCCATCACCTGCAGGCCTCCAGCTCGATGCCCCGCCAGGACCTTAAGGCCGAGGTCTTCGACAGGCTCCTGGGCGACACCGCTTTGAGCAACGACCACATCGACGCCCTCGTGGCGGGTTTCGCCGTCGACGCCCACCGGGAGCTGACCGGGGCATTCACCCGCCGCTACCTCCGGGAGCTCCAAGGGCTGTGGGGTGCGCGCGGCCAGGAGATCGCCACCCGGTTAGTCGTCGGGCTCTTCCCCGCCTGCGGGGACGAGGCGGACGTCCAGGCGGTCGAGGACTGGCTCGCGACGCACCCCGAGGCGCCGTCGGCTCTGCGCCGGCTCGTCCTCAAGAGTCTTGACGACCTGCGGCGTGCTCTGACCGCTCGACGCACTGGTTCAGAGGATCTCTGA","VAVDVTGAIDRHEATFSVRCLMSLDIRQRAEGLWVDFVGQAIDSLSIDGQPAPVTWDGARIELPVLDPGEHTVEIAARGLYSNSGQGLHRFHDPVDGATYLYTHFEPSDARRAWPVMEQPDIKTRFSLEVKHPRGWTVMSNARPTAGSSSVSVGTDSGYETTSFAASRPLPSYLTALAAGPWHRVTGQWTSPSRPGLTVPLSWSCRASLAEHLDAAELLDLTRAGLDLYDRAYAYGFPWDSYDSVLVPEYNLGAMENPGCVTFNEELYLFRGPVTRSQRAGRANTILHEMCHMWFGDLVTPTWWEDTWLKESFADHQGTWAEAEAAGYTEAWVSFASTRKAWAYLEDSRPATTHPIVAQVDDVEAARQAFDGITYAKGAAVLKQLVAHVGQEAFFKAAGLLFERRAYGNACLDDFLGVLSQVSGRDMHDWARAWLHTAGPSVITDELAVHEGRIASLTLQQEGIDPVTGQSVLRPHTLVVGLYSFDGDGALVRTHRLPVVLEAEQLDIVEAVGLPAPDLVIVNDEDLTYAVVRPDDTSLSCLAASLGALRDPMARSLTWSMLHNLVRDAVIDAALFVQAVLAHADDDTEPSTLTVLLNQALRVTSRYAGPHTRRALLERLVADDSTEPSKMTDPAFLHGGWGRLRASAPGSDAQIVRARAWLEAAGQARLLGEAGSAQAAARVREILDGALPGLELDADMRWRALTALAQLDAVSADELEAQRKADPTASGITHHLQASSSMPRQDLKAEVFDRLLGDTALSNDHIDALVAGFAVDAHRELTGAFTRRYLRELQGLWGARGQEIATRLVVGLFPACGDEADVQAVEDWLATHPEAPSALRRLVLKSLDDLRRALTARRTGSEDL$","Aminopeptidase N","Cytoplasm, Extracellular","Aminopeptidase N (Lysyl aminopeptidase)(Lys-AP)(Alanine aminopeptidase)","putative aminopeptidase ","aminopeptidase N","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 1989. 242(2):211-214. PMID: 2914602Murphy G.J., Murphy G., Reynolds J.J. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett. 1991. 289(1):4-7. PMID: 1894005","","","

InterPro
IPR001930
Family

Peptidase M1, membrane alanine aminopeptidase
PTHR11533	$\"[81-806]T$	PROTEASE M1 ZINC METALLOPROTEASE

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[285-294]?$	ZINC_PROTEASE

InterPro
IPR012778
Family

Peptidase M1, aminopeptidase N actinomycete-type
PTHR11533:SF12	$\"[81-806]T$	AMINOPEPTIDASE N
TIGR02412	$\"[1-859]T$	pepN_strep_liv: aminopeptidase N

InterPro
IPR014782
Domain

Peptidase M1, membrane alanine aminopeptidase, N-terminal
PR00756	$\"[111-126]T$ $\"[164-179]T$ $\"[250-260]T$ $\"[285-300]T$ $\"[304-316]T$	ALADIPTASE
PF01433	$\"[1-378]T$	Peptidase_M1

","No hits to the COGs database.","***** IPB001930 (Membrane alanyl dipeptidase (M1) family signature) with a combined E-value of 4.7e-25. IPB001930A 111-126 IPB001930B 164-179 IPB001930C 250-260 IPB001930D 285-300 IPB001930E 304-316","Residues 34-121 are 66% similar to a (AMINOPEPTIDASE N HYDROLASE LYSYL LYS-AP ALANINE PROBABLE PEPN ZINC SEQUENCING) protein domain (PD833360) which is seen in Q6A6B8_PROAC.Residues 237-300 are 79% similar to a (AMINOPEPTIDASE HYDROLASE LEUKOTRIENE METALLOPROTEASE ZINC N MICROSOMAL DIRECT A-4 SEQUENCING) protein domain (PD249058) which is seen in Q6A6B8_PROAC.Residues 247-300 are 85% similar to a (AMINOPEPTIDASE N HYDROLASE METALLOPROTEASE ZINC 3.4.11.- GLYCOPROTEIN PROBABLE DIRECT SEQUENCING) protein domain (PD779462) which is seen in Q9L200_STRCO.Residues 303-344 are 66% similar to a (AMINOPEPTIDASE HYDROLASE N) protein domain (PDA1D923) which is seen in Q6A6B8_PROAC.Residues 351-410 are 78% similar to a (AMINOPEPTIDASE N HYDROLASE METALLOPROTEASE ZINC 3.4.11.- GLYCOPROTEIN MEMBRANE PROBABLE DIRECT) protein domain (PD679435) which is seen in Q6A6B8_PROAC.Residues 412-846 are 52% similar to a (AMINOPEPTIDASE N HYDROLASE LYSYL LYS-AP ALANINE PROBABLE PEPN ZINC SEQUENCING) protein domain (PD043116) which is seen in Q9L200_STRCO.","","-42% similar to PDB:1Z1W Crystal structures of the tricorn interacting facor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations (E_value = 1.5E_36);-42% similar to PDB:1Z5H Crystal structures of the Tricorn interacting Factor F3 from Thermoplasma acidophilum (E_value = 1.5E_36);-39% similar to PDB:2DQ6 Crystal Structure of Aminopeptidase N from Escherichia coli (E_value = 5.7E_17);-39% similar to PDB:2DQM Crystal Structure of Aminopeptidase N complexed with bestatin (E_value = 5.7E_17);-39% similar to PDB:2GTQ Crystal structure of aminopeptidase N from human pathogen N. meningitides (E_value = 5.7E_17);","Residues 1 to 378 (E_value = 7.7e-39) place ANA_0740 in the Peptidase_M1 family which is described as Peptidase family M1.","","N (Lysyl aminopeptidase) (Lys-AP)(Alanine aminopeptidase) (LYS-AP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0741","781212","781664","453","6.06","-2.86","15734","ATGTCGAGCAGTCCGATCGAGCAGGATCCCTCCTCCACACAGACCTTCGGGGTCGTCGACGTCGCCAGCTCAGTGGACTCCCCGGTGGTGGGACTGAGTCAGCAGGACGCCGCTGCAATCGCTGCCCTGCCGTCGGGAACGGCGCTTCTCCTCGTCCACCACGGACCGACCACTGGTGCGCGTTTCCTCCTGGATGCTGAGGAGACCACCGTGGGGCGCCACCCCCGTGCCGACATCTTCCTCGACGACGTCACCGTCTCCAGGAAGCACGCGGTCTTCTCGTCTCTGCCCGATGGCGGGTACGGCGTGCGTGACTCCGGTTCGCTCAACGGGACATACGTCAATCGCACGCGCGTTGAGCAGGTGGCTCTTCGCTCCGGTGATGAGGTCCAGATCGGCAAGTACCGGATGACCTACCACCCCGGCCCCCAGAGCGGAGCCGCGTCTCGGTGA","MSSSPIEQDPSSTQTFGVVDVASSVDSPVVGLSQQDAAAIAALPSGTALLLVHHGPTTGARFLLDAEETTVGRHPRADIFLDDVTVSRKHAVFSSLPDGGYGVRDSGSLNGTYVNRTRVEQVALRSGDEVQIGKYRMTYHPGPQSGAASR$","FHA-domain-containing protein","Extracellular, Cytoplasm","possible signal transduction protein","hypothetical protein","Forkhead-associated protein","","Hofmann K., Bucher P. The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors. Trends Biochem. Sci. 1995. 20(9):347-349. PMID: 7482699Durocher D., Jackson S.P. The FHA domain. FEBS Lett. 2002. 513(1):58-66. PMID: 11911881","","","

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[69-133]T$	FHA
SM00240	$\"[68-119]T$	FHA
PS50006	$\"[69-119]T$	FHA_DOMAIN

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.20	$\"[36-149]T$	no description
PTHR19241	$\"[71-115]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19241:SF6	$\"[71-115]T$	ABC TRANSPORTER

","BeTs to 8 clades of COG1716COG name: FHA-domain-containing proteinsFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1716 is ------y--dr-bc----s----i--Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","Residues 58-133 are similar to a (ATP-BINDING KINASE DOMAIN FHA TRANSCRIPTION ABC ZINC-FINGER NUCLEAR TRANSPORTER TRANSFERASE) protein domain (PD001303) which is seen in Q9KZP8_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 69 to 133 (E_value = 6.2e-18) place ANA_0741 in the FHA family which is described as FHA domain.","","signal transduction protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0742","781775","782425","651","7.59","0.94","23926","ATGAAGATCGGGCAGGTGGTGGATCTCCTCAAGGTGGAGTTCCCTGCCCTGTCGATCTCCAAGGTTCGTTATCTCGAGGGTGAGGGGCTCATCAGTCCTCACCGTGTCGGTAACGGGTACCGTCGCTACTCGCAGGCGGACCTGGAGCGTCTGCGCTATGCCTTGGCGGTGCAGCGCGACGAGTACCTCCCGTTGCACGTCATCCGTGACCGTCTGGCGCGGCTGGATGCTGACGTCGAGGCCCCCGCTCCACAGCCCGTGGCCAGGGTGGTTGCCCGAGACGGACAGATCGTCGACGACGGTCCCATGGATCTGGAGGCACTCCTGGCCCACTCTGGTGCCAGCGAGTCTCAGATTGAGGAGCTCGTCGCCGTCGGACTCATCAGTCCCGATGTTCGTGGGCGCTACAGCCAGCAGAACCTTAGGACCGTGCGCCTGGCCATGGAGATCACCCGCAAGGGAGTGCCTCTGCGCAACCTGCGCGCAGTACGCGCCTCAGCCGAGCGGGAGGCGGATACGATCGACCAGGCAGTGGCTCCGCGTCGGTCGCGGTCGCGCAGCGCTGGTGAGGAGACGGCCCGGGAGCTGGCCGAGCTCGTTGCGGACCTGCACACGATTCTGCTGCGTCGCGCCGTTGAGGCTCTGGGCTGA","MKIGQVVDLLKVEFPALSISKVRYLEGEGLISPHRVGNGYRRYSQADLERLRYALAVQRDEYLPLHVIRDRLARLDADVEAPAPQPVARVVARDGQIVDDGPMDLEALLAHSGASESQIEELVAVGLISPDVRGRYSQQNLRTVRLAMEITRKGVPLRNLRAVRASAEREADTIDQAVAPRRSRSRSAGEETARELAELVADLHTILLRRAVEALG$","Transcriptional regulator, MerR family","Cytoplasm","conserved hypothetical protein","hypothetical protein","regulatory protein, MerR","","Holmes D.J., Caso J.L., Thompson C.J. Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 1993. 12(8):3183-3191. PMID: 7688297Helmann J.D., Wang Y., Mahler I., Walsh C.T. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons. J. Bacteriol. 1989. 171(1):222-229. PMID: 2492496Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 1995. 177(14):3904-3910. PMID: 7608059Nakano Y., Kimura K. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 1991. 109(2):223-228. PMID: 1677938Sadowsky M.J., Cregan P.B., Gottfert M., Sharma A., Gerhold D., Rodriguez-Quinones F., Keyser H.H., Hennecke H., Stacey G. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(2):637-641. PMID: 1988958Helmann J.D., Ballard B.T., Walsh C.T. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. Science 1990. 247(4945):946-948. PMID: 2305262","","","

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PF00376	$\"[2-43]T$	MerR
SM00422	$\"[1-75]T$	HTH_MERR
PS50937	$\"[1-74]T$	HTH_MERR_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[1-78]T$	no description

","BeTs to 11 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","Residues 1-52 are 76% similar to a (DNA-BINDING TRANSCRIPTIONAL SCO1383 HTH-TYPE TRANSCRIPTION RV1828/MT1876/MB1859 REGULATOR REGULATION ML2075 MLCB1788.35C) protein domain (PDA1D7K0) which is seen in YI28_MYCTU.Residues 17-53 are 86% similar to a (DNA-BINDING REGULATORY REGULATORS IS TRANSCRIPTIONAL TYPE 5/10 MERR-FAMILY PREDICTED GENOME) protein domain (PDA12750) which is seen in Q6A8T4_PROAC.Residues 55-212 are 51% similar to a (DNA-BINDING TRANSCRIPTIONAL REGULATORY FINGERPRINT REGULATORS IS SCO1383 TYPE 4-5 HTH-TYPE) protein domain (PD034120) which is seen in Q9KZP9_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 43 (E_value = 3.4e-06) place ANA_0742 in the MerR family which is described as MerR family regulatory protein.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0743","782545","783030","486","4.93","-10.68","17425","GTGCCCTTGATGCAATTGGTGGGTGTCAGATCCACTGATCCTGATGACGGCTTGGTCGCCGTCCTCGTGGAGGACGGCGGGCCGGCGATGCTGGCCATTCCGGTGACGGCGCACGAGGGGCTGGTGCTTCAGGCTCATGGCTCGCACCGCTCACCCTCGTGGCCCAGGCTTCTTGATGACGTCGTCGAGGCGCTGGGCGGTCGCATCGGGTGCACTGAGCTTGACGTCGATGATGACGCACGCATCGTTGCCAGGCTCGTCGTGGAGACTCCTGCCTGCACGAGTCGGTTGACGAGGGTCGCCTGCACTCCCGGAGAGGGACTGCTCCTGAGCGGATACCACCGGTTCCCGGTGCACGCCAGCAGCTCGCTGACGCGCCTGAGGTCCGTGGACCTCAGTGATGACCAGGGAGCGGAGAGGCTGGAGAAGTGGCAGCACATGTTGTCGCAGACCGATCGACTGGATGACGACGACACGCGGGACTGA","VPLMQLVGVRSTDPDDGLVAVLVEDGGPAMLAIPVTAHEGLVLQAHGSHRSPSWPRLLDDVVEALGGRIGCTELDVDDDARIVARLVVETPACTSRLTRVACTPGEGLLLSGYHRFPVHASSSLTRLRSVDLSDDQGAERLEKWQHMLSQTDRLDDDDTRD$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0744","783303","783875","573","6.79","-0.39","20359","ATGAATGAAGCCAGTGCGATAGCAAGGCCTCAGCGTACTCAGGGCATGCTGTTCGGCGACCCGCTGCCCCAGCTCGATGCCGATTCTGGCTACCGCGGGCCGGTGGCCTGCCGAGCCGCCGGCATCACGTATCGCCAGCTCGACTACTGGGCGCGTACCGGGTTGGTTGAGCCGTCGATTCGAAGCGCCAAGGGATCGGGCTCCCAGCGGCTCTACTCCTTCCGCGACATCCTGGTTCTCAAGGTCGTCAAGCGCCTCTTGGACACTGGGGTCTCGCTCCAGCAGATCCGCACGGCGGTCAGCGCCCTGCACTCCCGCGGTGTCGAGGACCTGGCCTCCATCACCCTCATGAGTGACGGCGCCTCGGTCTACGAGTGCACCTCGGCTGACGAGGTCGTCGACCTGGTCGCCGGCGGCCAGGGCGTCTTCGGCATCGCCGTGGGGCGGGTGTGGCACGAGGTTGAGGGAGCGCTGGCGGACCTCCCCGTCGATCACGCTCAGGCCCTCGGTACTCCTCTGGTTGAGGACGAGCTGGCCAAGCGTCGCGCCGCCAAGCGGCAGCAGGCCATCTGA","MNEASAIARPQRTQGMLFGDPLPQLDADSGYRGPVACRAAGITYRQLDYWARTGLVEPSIRSAKGSGSQRLYSFRDILVLKVVKRLLDTGVSLQQIRTAVSALHSRGVEDLASITLMSDGASVYECTSADEVVDLVAGGQGVFGIAVGRVWHEVEGALADLPVDHAQALGTPLVEDELAKRRAAKRQQAI$","Transcriptional regulator, MerR family","Cytoplasm","Introduction of orf1 on a high-copy numberplasmid significantly repressed aerial mycelium formation","transcriptional regulator; MerR family","regulatory protein, MerR","","Holmes D.J., Caso J.L., Thompson C.J. Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 1993. 12(8):3183-3191. PMID: 7688297Helmann J.D., Wang Y., Mahler I., Walsh C.T. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons. J. Bacteriol. 1989. 171(1):222-229. PMID: 2492496Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 1995. 177(14):3904-3910. PMID: 7608059Nakano Y., Kimura K. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 1991. 109(2):223-228. PMID: 1677938Sadowsky M.J., Cregan P.B., Gottfert M., Sharma A., Gerhold D., Rodriguez-Quinones F., Keyser H.H., Hennecke H., Stacey G. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(2):637-641. PMID: 1988958Helmann J.D., Ballard B.T., Walsh C.T. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. Science 1990. 247(4945):946-948. PMID: 2305262","","","

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
SM00422	$\"[31-103]T$	HTH_MERR
PS50937	$\"[30-102]T$	HTH_MERR_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[31-109]T$	no description

InterPro
IPR001395
Family

Aldo/keto reductase
PD000288	$\"[12-212]T$	Q9A528_CAUCR_Q9A528;
PR00069	$\"[109-127]T$ $\"[140-157]T$	ALDKETRDTASE
G3DSA:3.20.20.100	$\"[10-310]T$	no description
PTHR11732	$\"[11-225]T$ $\"[243-286]T$	ALDO/KETO REDUCTASE
PF00248	$\"[9-315]T$	Aldo_ket_red
PS00062	$\"[140-157]?$	ALDOKETO_REDUCTASE_2

noIPR
unintegrated

unintegrated
PTHR11732:SF15	$\"[11-225]T$ $\"[243-286]T$	ALDO/KETO REDUCTASE

","BeTs to 15 clades of COG0667COG name: Predicted oxidoreductases (related to aryl-alcohol dehydrogenases)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0667 is -o-p-zyqvdrlbcefg-s-uj--t-Number of proteins in this genome belonging to this COG is 3","***** IPB001395 (Aldo/keto reductase) with a combined E-value of 7.3e-38. IPB001395B 40-64 IPB001395C 78-90 IPB001395D 110-127 IPB001395E 136-171 IPB001395G 251-305","Residues 1-231 are 53% similar to a (ALDO/KETO REDUCTASE) protein domain (PDA0J6Q9) which is seen in Q9RS66_DEIRA.Residues 4-306 are 40% similar to a (ALDO-KETO REDUCTASE POSSIBLE FAMILY OXIDOREDUCTASE) protein domain (PD520489) which is seen in Q8G5I8_BIFLO.Residues 5-233 are 48% similar to a (ENZYME ALDO/KETO REDUCTASE FAMILY) protein domain (PDA0J6R0) which is seen in Q9X5G7_STRCL.Residues 6-230 are 48% similar to a (OXIDOREDUCTASE ALDO/KETO REDUCTASE FAMILY) protein domain (PDA0J6Q8) which is seen in Q98CQ3_RHILO.Residues 6-164 are 49% similar to a (OXIDOREDUCTASE) protein domain (PDA0J6Q4) which is seen in Q82P83_STRAW.Residues 6-272 are 48% similar to a (ALDO/KETO REDUCTASE) protein domain (PDA192L0) which is seen in Q6F1L4_MESFL.Residues 7-312 are 44% similar to a (ALDO-KETO REDUCTASE) protein domain (PDA1C8N6) which is seen in Q7VG62_HELHP.Residues 8-157 are 47% similar to a (REDUCTASE ALDOSE) protein domain (PD290704) which is seen in O51478_BORBU.Residues 9-314 are 43% similar to a (ALDO-KETO REDUCTASE FAMILY) protein domain (PD765756) which is seen in Q8ZXA1_PYRAE.Residues 10-306 are 45% similar to a (DEHYDROGENASE) protein domain (PDA0J2I3) which is seen in Q6UEH5_ASPPA.Residues 10-299 are 48% similar to a (ALDO/KETO REDUCTASE FAMILY) protein domain (PDA181S1) which is seen in Q75H72_EEEEE.Residues 11-317 are 59% similar to a () protein domain (PD756934) which is seen in Q8FUB8_COREF.Residues 12-212 are 68% similar to a (REDUCTASE OXIDOREDUCTASE ALDO/KETO FAMILY DEHYDROGENASE OXIDOREDUCTASE NADP ALDO-KETO 1.1.1.- ACID) protein domain (PD000288) which is seen in Q9A528_CAUCR.Residues 12-214 are 63% similar to a (TRANSMEMBRANE OXIDOREDUCTASE) protein domain (PDA18313) which is seen in Q92SS1_RHIME.Residues 12-269 are 50% similar to a (OXIDOREDUCTASE ALDO/KETO REDUCTASE FAMILY) protein domain (PDA1A4R5) which is seen in Q881G1_PSESM.Residues 12-229 are 47% similar to a (CHANNEL IONIC O59826 POTASSIUM SUBUNIT POMBE SCHIZOSACCHAROMYCES) protein domain (PDA1B370) which is seen in Q6CI80_EEEEE.Residues 12-300 are 47% similar to a (CHANNELS IONIC K CHANNEL BETA-SUBUNIT) protein domain (PDA189C4) which is seen in O82064_SOLTU.Residues 12-269 are 44% similar to a () protein domain (PDA0K0A3) which is seen in Q7S2E8_NEUCR.Residues 14-307 are 41% similar to a (OXIDOREDUCTASE) protein domain (PD521436) which is seen in Q92SD9_RHIME.Residues 14-193 are 62% similar to a (OXIDOREDUCTASE DEHYDROGENASES OXIDOREDUCTASES RELATED PREDICTED ARYL-ALCOHOL) protein domain (PD611486) which is seen in Q8NU47_CORGL.Residues 130-313 are 42% similar to a () protein domain (PD848664) which is seen in Q8IM05_PLAF7.Residues 173-304 are 49% similar to a (OXIDOREDUCTASE) protein domain (PD737981) which is seen in Q82PN0_STRAW.Residues 191-268 are 59% similar to a (OXIDOREDUCTASE ALDO/KETO REDUCTASE) protein domain (PDA0K293) which is seen in Q6AA72_PROAC.Residues 211-268 are 61% similar to a (OXIDOREDUCTASE DEHYDROGENASES OXIDOREDUCTASES RELATED PREDICTED ARYL-ALCOHOL PROBABLE) protein domain (PD537805) which is seen in Q8NU47_CORGL.Residues 218-291 are 50% similar to a (OXIDOREDUCTASE) protein domain (PD700282) which is seen in Q9AD97_STRCO.","","-48% similar to PDB:1LQA TAS PROTEIN FROM ESCHERICHIA COLI IN COMPLEX WITH NADPH (E_value = 2.7E_34);-46% similar to PDB:1PZ1 Structure of NADPH-dependent family 11 aldo-keto reductase AKR11B(holo) (E_value = 3.6E_26);-44% similar to PDB:1PYF Structure of NADPH-dependent family 11 aldo-keto reductase AKR11A(apo) (E_value = 1.0E_25);-44% similar to PDB:1PZ0 Structure of NADPH-dependent family 11 aldo-keto reductase AKR11A(holo) (E_value = 1.0E_25);-45% similar to PDB:1ZSX Crystal Structure Of Human Potassium Channel Kv Beta-subunit (KCNAB2) (E_value = 1.5E_16);","Residues 9 to 315 (E_value = 5.5e-46) place ANA_0745 in the Aldo_ket_red family which is described as Aldo/keto reductase family.","","(PA3795) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0746","786608","785022","1587","5.29","-20.16","57280","ATGAAGAACCTGGACAGCATCGGCAGCGGCACCCTCCCCGACCAGGGAATCGACCACGAGTCAGCAACAGACATCGATCTGGGAATCGACCTGGGGACGACACGCACCGTCGTGGCACGTGCTGACCGGGGGAACTATCCCGTTATCAGCTTCACCGACGAGCACGGCGACGAGCACGACTTCATCCCCTCGCTGACAGCGCTGCACGAGGGGACGCTCGTTCACGGTTTCGCCGCCAGGAAGGCAGCTCACCAGGGCGCTCCGTTGCTGCGCAGCCTCAAACGGGTCCTGGCCTCCCCCACGCTGACAGCTGCCACACCGGTACCGCTGGGAGACCAGACATTCTCCGTTTTGGAGGTTCTCACCAGCTATCTGCGTCACCTTGAAGGCGAGCTCGCCGATCGGGGCATCGACATCGCACGCGCCCGCGTGGTGGTCGCCGTACCCGCCCACGCCTACGGGGCGCAGCGTCTTCTGACTCTTGAGGCCTTCCAGCAGGCCGGTTTCCGCGTCGCCGCCATGCTCAACGAGCCCAGTGCGGCCGGATTCGAGTACACCCACCGCAAGGCGACCACCGTCTCATCCAGGCGCACCCGGGTGCTGGTCTACGACCTGGGCGGCGGCACCTTCGACACCTCGCTGGTCGACGTCGTCGGCACGTCTCACGAGGTACTGGCCTCTCACGGGCTGGGAGACCTGGGCGGGGACGACGTCGACCTGCTCATGGCCACGATGGCCCTCAGCCGGGCGGGCATCTCCGAGGAGGACCTCTCCCCCACCGAGCTCGACGACTTGTTGGACCAGTGCCGCGACGCCAAGGAGCACCTCACCCCTCAGAGCCGTCGGGTGCTCATCATCCTCAGAGGCCAGGACGTCGTCCTGCCGGTGTCCGACCTGTACACGGCTTGCACACCGCTCATTGAGCGGTCCTTGGCCACGATGGCCCCCCTGGTCGGCAGGCTGGACGATGGCAGCCCGGACCTGACCGAGATCGCCGGAGTCTACCTGGTCGGCGGCGCCTCCGGTCTTCCCCTGGTGCCCAGGCTCTTGCGGGAACGCTTCGGTCGTCGGGTTCACCGCTCCCCCTACCCCGGGGCCTCCACGGCCATCGGCCTGGCAATCGCGGCGGACCGCACCAGTGACTACGACCTGACCGACCGGCTCTCACGGGGTTTCGGTGTCTTCCGGGAGGCCGACGGCGGCCACCGTCTCACCTTCGACGCGATCCTGAGCCCAGAGTCGGTCCAGGCCTCGCCCGGGGGCCGGGAGGGCACGGTGCTGACCCGCGAGTACGACGCGGCGCACAACATCGGCTGGTACCGCTTTGTGGAGTGCGCCGGTGTCGACGAGGGCGGTGAGCCACGCGGCGAGATCGCCCCCTACCAGGACATCGTCTTCCCCTTCGAGTCCTCACTGCGGGACGTCGATGACGAGGAGCTGAGGACCTACTCAGTGGAGCGGCGCGATCAAGGTCCGCGAATTCAGGAGCACTACCGCGTCGATGAGGCCGGCCTGGTTCGTGTCACCATCACCGACCTCTCCGACGGATACAGCCGCCGTTACGTTCTGGGCAGGCGCACCCTGTAG","MKNLDSIGSGTLPDQGIDHESATDIDLGIDLGTTRTVVARADRGNYPVISFTDEHGDEHDFIPSLTALHEGTLVHGFAARKAAHQGAPLLRSLKRVLASPTLTAATPVPLGDQTFSVLEVLTSYLRHLEGELADRGIDIARARVVVAVPAHAYGAQRLLTLEAFQQAGFRVAAMLNEPSAAGFEYTHRKATTVSSRRTRVLVYDLGGGTFDTSLVDVVGTSHEVLASHGLGDLGGDDVDLLMATMALSRAGISEEDLSPTELDDLLDQCRDAKEHLTPQSRRVLIILRGQDVVLPVSDLYTACTPLIERSLATMAPLVGRLDDGSPDLTEIAGVYLVGGASGLPLVPRLLRERFGRRVHRSPYPGASTAIGLAIAADRTSDYDLTDRLSRGFGVFREADGGHRLTFDAILSPESVQASPGGREGTVLTREYDAAHNIGWYRFVECAGVDEGGEPRGEIAPYQDIVFPFESSLRDVDDEELRTYSVERRDQGPRIQEHYRVDEAGLVRVTITDLSDGYSRRYVLGRRTL$","Molecular chaperone, HSP70 family","Cytoplasm","Molecular chaperone","chaperone protein DnaK - heat shock protein 70","Heat shock protein 70","","Craig E.A. Essential roles of 70kDa heat inducible proteins. Bioessays 1989. 11(2):48-52. PMID: 2686623Pelham H.R. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 1986. 46(7):959-961. PMID: 2944601Pelham H. Heat-shock proteins. Coming in from the cold. Nature 1988. 332(6167):776-777. PMID: 3282176Flaherty K.M., DeLuca-Flaherty C., McKay D.B. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 1990. 346(6285):623-628. PMID: 2143562Snutch T.P., Heschl M.F., Baillie D.L. The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization. Gene 1988. 64(2):241-255. PMID: 2841196","","","

InterPro
IPR001023
Family

Heat shock protein Hsp70
PR00301	$\"[25-38]T$ $\"[144-164]T$ $\"[208-218]T$ $\"[331-347]T$ $\"[491-507]T$	HEATSHOCK70
PTHR19375	$\"[13-381]T$	HEAT SHOCK PROTEIN 70KDA

InterPro
IPR013126
Family

Heat shock protein 70
PF00012	$\"[144-242]T$	HSP70
PS00329	$\"[202-215]T$	HSP70_2
PS01036	$\"[334-348]?$	HSP70_3

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.40	$\"[21-220]T$	no description

","BeTs to 22 clades of COG0443COG name: Molecular chaperoneFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0443 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001023 (Heat shock protein Hsp70) with a combined E-value of 6.2e-22. IPB001023C 130-184 IPB001023D 203-257***** IPB002731 (ATPase, BadF/BadG/BcrA/BcrD type) with a combined E-value of 6.2e-07. IPB002731A 28-42 IPB002731D 334-374***** IPB003494 (Cell division protein FtsA) with a combined E-value of 5.4e-06. IPB003494D 330-363 IPB003494E 364-375","Residues 49-168 are 54% similar to a (ATP-BINDING HEAT SHOCK CHAPERONE FAMILY MOLECULAR HSP70) protein domain (PD634768) which is seen in Q8NN35_CORGL.Residues 174-273 are 70% similar to a (HEAT SHOCK ATP-BINDING CHAPERONE HSP70 DNAK PHOSPHORYLATION FAMILY MULTIGENE SHAPE-DETERMINING) protein domain (PD514219) which is seen in Q8NN35_CORGL.Residues 274-454 are 70% similar to a (ATP-BINDING HEAT MOLECULAR SHOCK CHAPERONE CHAPERONE FAMILY HSP70) protein domain (PD670242) which is seen in Q8NN35_CORGL.","","-41% similar to PDB:1QQN D206S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN (E_value = 2.9E_13);-41% similar to PDB:1QQM D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN (E_value = 5.0E_13);-47% similar to PDB:1YUW crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant (E_value = 6.5E_13);-42% similar to PDB:1QQO E175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN (E_value = 1.1E_12);-47% similar to PDB:1BA1 HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL MUTANT WITH CYS 17 REPLACED BY LYS (E_value = 1.4E_12);","Residues 27 to 523 (E_value = 5.2e-08) place ANA_0746 in the HSP70 family which is described as Hsp70 protein.","","chaperone (dnaK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0747","786932","788170","1239","8.22","4.71","42352","ATGAGCACCATTCTCTTCCTCGTGATCGTTGTCGTCGTGACGGCCCTCGTCTTCGACTTCACGAACGGTTTCCACGACTCGTCCAATGCCATGGCGACGTCGGTGGCGACAGGCGCCTTCACACCCAGAAGAGCGGTTCTGGTCGCCGCCGTGCTCAACGTCATCGGTGCCTGCCTGTCGACCGAGGTCTCCAAGACGATCTCGCACGGGATGTTCGACGACACGGTGATCGAGGCGGCGCCGGCCATGATCTTCGCTGGTCTGGCCGGCGCCATCCTGTGGAACCTGGCGACCTGGCTGTTCGGGCTGCCATCGTCCTCGTCCCACGCGCTGTTCGGAGGACTCATCGGAGCGGTCGTGGTGGCGGCCGGGGTCCAAGGAGTCCACTGGGGGACGGTGATCTCCAAGATCATCCTGCCCGCTATCATCGCACCGGTCGTGGCCGGGCTGGCGGCAGCGCTGGCCACAGCCCTGGCCTACCGCATCGCGCACCCGACCAACCCGTACTCCGAGAAGCTCTTCCGCAACAGCCAGCGGGTCACAGCATCGCTGGTGGCGCTGTCTCACGGCACCTCTGATGGGCAGAAGACCATGGGGGTCATCACGTTGGTGCTGGTGGCCGGCGGCTACCAGGAGGCCGGTACCGGGCCTCACTGGTGGGTCATTGCGGCAGCGGGCCTCGCCATCGGCCTGGGCACCTACTCAGGCGGGTGGCGCATCATGCGCACCATGGGGCGTGGGCTGGTGCATGTCGAGGCGCCGCAGGGCTTCGCCTCCGAGACCGCCTCGACGGTGGCGATCCTGGCCTCTTCCCATCTGGGATTTGCCCTGTCCACCACCCACATCTGTACCGGGTCGATCCTGGGCTCCGGGATCGGCCGGGGCACCAAGGTGTCCTGGAGGACTGCGGGCAAGATGGGGATCGCCTGGCTGGTGACGCTTCCGTGCTCAGGCCTGGTGGGGGCCGCCACGTCGTATGTCGCGGTCAAGGGCGGCGTGCTGGGCACAATCGCGGTCATCTGCCTGCTCATCCTGGGGGCCCTGGCCATCATCCGACAGGCGGGGCACAACCGGGTGGACTTCTCCAACGTCAATGACGCCTCCGAGGTCGTTGTCGTCAAGCAGGATCCGGAGCTGGGGCGTGAACCGCGGACGCTGGACGAGGTGCGTTCCGAGATCATCGGCGGTGTGACGGATCAGGACAGCACGCATCGGATGACGACAGGATCCATGGCATGA","MSTILFLVIVVVVTALVFDFTNGFHDSSNAMATSVATGAFTPRRAVLVAAVLNVIGACLSTEVSKTISHGMFDDTVIEAAPAMIFAGLAGAILWNLATWLFGLPSSSSHALFGGLIGAVVVAAGVQGVHWGTVISKIILPAIIAPVVAGLAAALATALAYRIAHPTNPYSEKLFRNSQRVTASLVALSHGTSDGQKTMGVITLVLVAGGYQEAGTGPHWWVIAAAGLAIGLGTYSGGWRIMRTMGRGLVHVEAPQGFASETASTVAILASSHLGFALSTTHICTGSILGSGIGRGTKVSWRTAGKMGIAWLVTLPCSGLVGAATSYVAVKGGVLGTIAVICLLILGALAIIRQAGHNRVDFSNVNDASEVVVVKQDPELGREPRTLDEVRSEIIGGVTDQDSTHRMTTGSMA$","Low-affinity inorganic phosphate transporter","Membrane, Cytoplasm","phosphate transport protein","low-affinity inorganic phosphate transporter","phosphate transporter","","Versaw W.K., Metzenberg R.L. Repressible cation-phosphate symporters in Neurospora crassa. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(9):3884-3887. PMID: 7732001","","","

InterPro
IPR001204
Family

Phosphate transporter
PTHR11101	$\"[12-352]T$	PHOSPHATE TRANSPORTER
PF01384	$\"[22-321]T$	PHO4

noIPR
unintegrated

unintegrated
PTHR11101:SF3	$\"[12-352]T$	LOW-AFFINITY INORGANIC PHOSPHATE TRANSPORTER-RELATED
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[44-64]?$ $\"[79-101]?$ $\"[107-127]?$ $\"[137-159]?$ $\"[218-238]?$ $\"[307-325]?$ $\"[331-351]?$	transmembrane_regions

","BeTs to 19 clades of COG0306COG name: Phosphate/sulphate permeasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0306 is aompk-y-vdr-b-efgh-nuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB001204 (Phosphate transporter) with a combined E-value of 1.5e-36. IPB001204A 23-58 IPB001204B 186-199 IPB001204C 274-291 IPB001204D 306-321 IPB001204C 102-119","Residues 181-322 are 86% similar to a (PHOSPHATE TRANSPORTER PERMEASE TRANSMEMBRANE LOW-AFFINITY FAMILY RECEPTOR INORGANIC PROBABLE LEUKEMIA) protein domain (PD001131) which is seen in Q6A658_PROAC.Residues 181-220 are 92% similar to a (PHOSPHATE TRANSPORTER FAMILY LOW-AFFINITY INORGANIC PITH PITA LMO2249 LIN2351) protein domain (PD331239) which is seen in Q6A658_PROAC.Residues 181-322 are 86% similar to a (PHOSPHATE TRANSPORTER PERMEASE TRANSMEMBRANE LOW-AFFINITY FAMILY RECEPTOR INORGANIC PROBABLE LEUKEMIA) protein domain (PD001131) which is seen in Q6A658_PROAC.","","-45% similar to PDB:2D57 Double layered 2D crystal structure of AQUAPORIN-4 (AQP4M23) at 3.2 a resolution by electron crystallography (E_value = );","Residues 22 to 321 (E_value = 2e-68) place ANA_0747 in the PHO4 family which is described as Phosphate transporter family.","","transport protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0749","788167","788412","246","6.77","-0.39","8494","ATGACCGGTATGGCGATCGACTGGGGCTCGCTGGGACTGGTGGCGTCAGTGACGGTGCTGGGCACCGCCTTCATCCTTACCATCTGCTCGCTGGCGGCTCGCATGCTGGCCACCGTGCACGCCAAGCACGAGGCCGGCGAGGCCGAAGGGGTGCGTCTGGCTCAGGTGCTGGCGGTTGTCTTCATCGCCATCGCCGCCATGATTGCGTTGTTCGGCCTGTGGCTCATCGTCCCCTACTTCCACTGA","MTGMAIDWGSLGLVASVTVLGTAFILTICSLAARMLATVHAKHEAGEAEGVRLAQVLAVVFIAIAAMIALFGLWLIVPYFH$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[53-75]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 4-81 are 64% similar to a (MEMBRANE) protein domain (PD936740) which is seen in Q6A659_PROAC.","","-54% similar to PDB:1OM3 FAB 2G12 unliganded (E_value = );-54% similar to PDB:1OP3 Crystal Structure of Fab 2G12 bound to Man1->2Man (E_value = );-54% similar to PDB:1OP5 Crystal Structure of Fab 2G12 bound to Man9GlcNAc2 (E_value = );-54% similar to PDB:1ZLS FAB 2G12 + Man4 (E_value = );-54% similar to PDB:1ZLU FAB 2G12 + Man5 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0750","788456","789988","1533","4.98","-28.82","56226","GTGACTGAGGACCTCAAGCGCCTGGCCCAGGATGCGATTACAACATCCGCAGCGGTCGACGACCCGGACTATCCCTGCTTTCACGTCGTCCCGCCGGTGGGCCGACTCAACGATCCCAACGGGCTGCTCGTCGACGGCGACACCTACCACGCCTTCTACCAGCTCAGTCCCTTCCATCCCCACCGCAAGCTGGTCTACTGGGGGCATTCCTCCTCGACGGACCTGCTGCACTGGAGCCACCACGCGCCTGCCATCATCCCGGACTCCTCCTACGACCGCAGCGGCGCCTACTCCGGCAACGCGATCGTGCTGGAGGGCCATGAGGTCGATGCCGCCCCTGCGCGGGTTCCGTTCCAGCTGTTCTACACCGGGAACCTCAAGGACCCGGTGACCGACGAGCGCACCGCCAGCCAGTGCCTGGTCACCAGCGGCGACCTGACCGACTTCACCAAGTGGCCCGGCAACCCGCTCATCCCCACCCACGCCGAGGGCTACACGTCCCACTACCGTGACCCGCAGGTCTTCCGAGATCCTGACCGGCCGGGGGAGTACCGCATGCTCATCGGAGTCCAGCGTGCCGATAAGACCGGCGCCGCCGTCCTGTACCGCTCCCTGGACCTGGTCTCTTGGGAGCTGGAGGGCGAGCTGAGCTTCCCTGGAGCGGGAGGCGCCTTCGATGCCTTCGGGTACATGTGGGAGTGCCCCGGCCTGGTGCGGCTGAAGGATGAGGACACCGGTGAGGACTGGGACGTCCTCATCTGGTGCCCGCAGGGCATCGAACCCGACCGGGAGGGCTTTGAGAACATCTTCCCCTGCGTCTACACGGCGGGACACCTGGTGGGCACTGAGCTGCGAGACACCGGCGGGGTCTTCTACGAGGTTGACCGGGGTTTCGAGTTCTACGCCCCTCAGGTCTTCGCCCGGCGGTCCTCCGAGCCGGGGCCGGTGCTGCTGACCGGGTGGGCGGGCAACGCCTCCGAGGACGATCAGCCCTCCATCGAGACTGGGCAGTGGGTCCACGCCCTGACCATGCCTCGGATGCTGAGTCTCAAAGCAGGCCGACTCATCCAGCGCCCCGCCGCCTCACTGCAGTATGACGCCGGGGAACCGGCTCTCGTGGGGGAGAGACTGAAGGCGGGCCTTCACGAGGTCGATGAGCTCAGCGGGCACCGCAGCTGGCAGCTGTGCCTGGAGGCAGACGCCGAGCAGACCACGGGGGCGTGGGGACTGCGGATCGGACCGGATGACTCGCACGTGGACATCACCCTGGATAAGCAGGTGCTGCGAGTGGACCGCACCACCTCCCGCTACGCCCAGCACGGATCGGTGCGCAGCGTGACGCTTCCTGAAGGGTGTGCGCCGGTGCTGGAGGTCATTCACGACCGATCACTGACCGAGGTTTTCGTCGGTGACGGGGAGCTGGTCCTCACGCTGCGCAGCTTCGTCGAGGTCAGCAGCACGGGAGTACGGCTGATGGTGGACAGGGACCTCGCCTTGACGGCCGGCAGCACGAGGACATTCACACCGTCCTGA","VTEDLKRLAQDAITTSAAVDDPDYPCFHVVPPVGRLNDPNGLLVDGDTYHAFYQLSPFHPHRKLVYWGHSSSTDLLHWSHHAPAIIPDSSYDRSGAYSGNAIVLEGHEVDAAPARVPFQLFYTGNLKDPVTDERTASQCLVTSGDLTDFTKWPGNPLIPTHAEGYTSHYRDPQVFRDPDRPGEYRMLIGVQRADKTGAAVLYRSLDLVSWELEGELSFPGAGGAFDAFGYMWECPGLVRLKDEDTGEDWDVLIWCPQGIEPDREGFENIFPCVYTAGHLVGTELRDTGGVFYEVDRGFEFYAPQVFARRSSEPGPVLLTGWAGNASEDDQPSIETGQWVHALTMPRMLSLKAGRLIQRPAASLQYDAGEPALVGERLKAGLHEVDELSGHRSWQLCLEADAEQTTGAWGLRIGPDDSHVDITLDKQVLRVDRTTSRYAQHGSVRSVTLPEGCAPVLEVIHDRSLTEVFVGDGELVLTLRSFVEVSSTGVRLMVDRDLALTAGSTRTFTPS$","Sucrose-6-phosphate hydrolase","Cytoplasm","sucrose-6-phosphate hydrolase","sucrose-6-phosphate hydrolase ","Glycosyl hydrolase family 32, N terminal domain protein","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR001362
Family

Glycoside hydrolase, family 32
SM00640	$\"[28-472]T$	Glyco_32
PS00609	$\"[28-41]T$	GLYCOSYL_HYDROL_F32

InterPro
IPR013148
Domain

Glycosyl hydrolases family 32, N-terminal
PF00251	$\"[28-359]T$	Glyco_hydro_32N

InterPro
IPR013189
Domain

Glycosyl hydrolase family 32, C-terminal
PF08244	$\"[397-472]T$	Glyco_hydro_32C

noIPR
unintegrated

unintegrated
G3DSA:2.60.120.560	$\"[388-495]T$	no description

","BeTs to 5 clades of COG1621COG name: Beta-fructosidases (levanase/invertase)Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1621 is ------y-v--lb-e-gh--------Number of proteins in this genome belonging to this COG is 5","***** IPB001362 (Glycoside hydrolase, family 32) with a combined E-value of 3.5e-11. IPB001362 27-55","Residues 25-488 are 37% similar to a (HYDROLASE GLYCOSIDASE FRUCTOSIDASE LEVANASE/INVERTASE BETA-FRUCTOSIDASES BETA-) protein domain (PD680132) which is seen in Q8NRD6_CORGL.Residues 27-189 are 57% similar to a (HYDROLASE GLYCOSIDASE INVERTASE SUCROSE-6-PHOSPHATE PRECURSOR SIGNAL BETA-FRUCTOFURANOSIDASE ACID TRANSFERASE WALL) protein domain (PD581674) which is seen in P94466_BACST.Residues 201-351 are 55% similar to a (HYDROLASE GLYCOSIDASE INVERTASE SUCROSE-6-PHOSPHATE PRECURSOR SIGNAL ACID BETA-FRUCTOFURANOSIDASE TRANSFERASE WALL) protein domain (PD186064) which is seen in Q8NMD5_CORGL.","","-44% similar to PDB:1UYP THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA (E_value = 3.4E_35);-44% similar to PDB:1W2T BETA-FRUCTOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH RAFFINOSE (E_value = 7.5E_35);-43% similar to PDB:2AC1 Crystal structure of a cell-wall invertase from Arabidopsis thaliana (E_value = 1.7E_23);-36% similar to PDB:1Y4W Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21 (E_value = 1.5E_22);-36% similar to PDB:1Y9G Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose (E_value = 1.5E_22);","Residues 28 to 359 (E_value = 3.7e-101) place ANA_0750 in the Glyco_hydro_32N family which is described as Glycosyl hydrolases family 32 N terminal.Residues 397 to 472 (E_value = 0.0036) place ANA_0750 in the Glyco_hydro_32C family which is described as Glycosyl hydrolases family 32 C terminal.","","hydrolase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0751","790121","792286","2166","5.10","-24.16","75689","GTGTGGCCGCCGGGAGTCAGCGACGTTCCCGACCGTTGGGTTTCCCAGCCCTCCCAGTTCTCGCGGTCCCATCACGAGAAAGGAAACCTCCGGGTGGCAATGGATCACGCCCGCGTGGCGAAGGACGTCCTGACGTACGTCGGTGGCGCCGACAACATCAACGCAGCAGCGCACTGCGCGACCCGCCTGCGTCTTGTCCTCAATGACATGGACAAGGTCGACCAGAAGGCTCTCGACAAGGACCCCGACCTCAAGGGCACCTTCATCGCGGGCGGCATGTTCCAGATCATCGTCGGGCCGGGAGACGTCGACCTCGTCTTCTCCGAGATGATCCACACCGGAGGCGTCAAGGAGGTCTCCAAGGACGAGGCTAAGGAGCAGGCCGCTAAGAGCGGTAACCCGCTCTCCCGTTTCATCAAGGCTATCGCGGATATCTTCGTCCCGCTGCTACCGGCCCTTGTCGCCGGCGGTCTCATGATGGCGATTCATAATGTCCTCACGGCCGATTTCTTCACTGCGTCCTCCTTCGTCACGTCGGACAACCCCACTGGTGCCTACGGACTCGTCGACCGGTTCTCATGGCTTACCGACTACGACGACGTCATCAACCTCGTATCCTCGGCAGCCTTCGCCTTCCTGCCGGTGCTCGTCGGCTTCTCCGCAGTCAAACGCTTCGGTGGCAACGTCTACCTGGGTGCGGCCATGGGGGCCGCCATGGTGTCCACCCAGCTGACCAGTGCCTACGAGATCGAGACGGCTCGACAGGCCGGCACTATTGAGGTCTGGCACCTCTTTGGGCTGACCGTGGACAAGATCGGTTACCAGGCCATGGTCATCCCTGTCCTGTGCGTGTCATGGCTGCTGGCATACATCGAGAAATGGCTCCACAAGCGCCTGTCGGGAACTGCCGACTTCTTGCTGACCCCGCTCATCACGCTGCTGGTGACCGGCTTCCTCACCTTCGTCGTCGTCGGCCCTCTGGCGCGGGAGCTCTCCGACGGTATTACCAACGGCCTGAGCTGGCTGTACACGACCGCCGGACCCCTGGGCGGCTTTCTCTTCGGCATGGTCTACTCGCCGATCGTGGTGACCGGATTGCACCAGTCCTTCCCGGCCGTGGAGCTGCCTCTCATCGCACAGATGAGCAGCGGCGGTCCCGGCTCCTTCATCTTCCCGATCGCCTCCATGGCCAATGTCGCCCAGGGCGCTGTGACCCTGGCGGTCTTCCTCCTGACCAAGGACTCCAAGATGAAGGGTCTGGCTGGTGCTGGTGGTGTCTCCGCGATCGTTGGTATCACCGAGCCCGCCATTTTCGGTGTCAACCTGCGCCTGCGTTGGCCGTTCTTCATTGGGATGGGTGTGGCCTCCCTCGGGGGTGCCGCCGTCGCCCTGCTCGATATCCACAACCAGGCTCTGGGCGCCGCCGGATTCGTTGGTTTCGTCTCGATCGTCCCCGACGACATTGTCAAGTACCTCATCCTCGAGGTTATCGTCTTCTTCGCCGCTTTCGGCGCCGCCTTCGCCTACGGCACTACTCGAGGAAAGGCATCTCTGGCCGGCGATGACGTCGACGCCGATGAGGCCGCCCTGGAGGCCGAGGCCATGGCCGAGCACGCCGAGACCGTCGAGCTGCCCGCTGAGGCCACTGAGGACTTCACCGTCACCGCTCCGATCCAGGGACGTGCGATCCCGCTGTCCGAGGTGGAGGACCAGACCTTCGCCTCAGGCATGCTCGGTCCGGGCATGGCCATTGCACCCGCCGAGGGGCCGGTTGTCTCCCCGGTCGACGGCGAGGTCCTCGTGGCCTTCCCGACCGGTCACGCCTACGGCCTACGATCCGCCAGCGGAGTCGAGCTGCTCATTCACGTCGGCATGGACACCGTCCAGCTCGAGGGCAAGCACTTCAGCCCCAAGGTCAAGGCCGGCGACAAGGTTCTGCGGGGCATGCCGCTGGTGGACGTCGACTGGGCCGCCGTCGGAGCCGCCGGCTACCAGACCGTCACCCCGATCGTCGTTTCCAACGCCCAGGGCTACGAGGGGATCGAGGAGCACGGTGCTGGAACGATTCACCGAGGCGATGCGCTCTTCGACGTCGTGCGCAAGGCCGATGACTCCGGTGCCGACAAGACGGATGTTCGGGCCGACGCCGCTCAGGCCAAAGCCTGA","VWPPGVSDVPDRWVSQPSQFSRSHHEKGNLRVAMDHARVAKDVLTYVGGADNINAAAHCATRLRLVLNDMDKVDQKALDKDPDLKGTFIAGGMFQIIVGPGDVDLVFSEMIHTGGVKEVSKDEAKEQAAKSGNPLSRFIKAIADIFVPLLPALVAGGLMMAIHNVLTADFFTASSFVTSDNPTGAYGLVDRFSWLTDYDDVINLVSSAAFAFLPVLVGFSAVKRFGGNVYLGAAMGAAMVSTQLTSAYEIETARQAGTIEVWHLFGLTVDKIGYQAMVIPVLCVSWLLAYIEKWLHKRLSGTADFLLTPLITLLVTGFLTFVVVGPLARELSDGITNGLSWLYTTAGPLGGFLFGMVYSPIVVTGLHQSFPAVELPLIAQMSSGGPGSFIFPIASMANVAQGAVTLAVFLLTKDSKMKGLAGAGGVSAIVGITEPAIFGVNLRLRWPFFIGMGVASLGGAAVALLDIHNQALGAAGFVGFVSIVPDDIVKYLILEVIVFFAAFGAAFAYGTTRGKASLAGDDVDADEAALEAEAMAEHAETVELPAEATEDFTVTAPIQGRAIPLSEVEDQTFASGMLGPGMAIAPAEGPVVSPVDGEVLVAFPTGHAYGLRSASGVELLIHVGMDTVQLEGKHFSPKVKAGDKVLRGMPLVDVDWAAVGAAGYQTVTPIVVSNAQGYEGIEEHGAGTIHRGDALFDVVRKADDSGADKTDVRADAAQAKA$","Phosphotransferase system IIC component, glucose/maltose/N-acetylglucosamine-specific","Membrane, Cytoplasm","Phosphotransferase system IIC components,glucose/maltose/N-acetylglucosamine-specific","sucrose PTS; EIIBCA","PTS system, glucose subfamily, IIA subunit","","Saier Jr M.H., Reizer J. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 1992. 174(5):1433-1438. PMID: 1537788","","","

InterPro
IPR001127
Domain

Phosphotransferase system, sugar-specific permease EIIA 1 domain
PD002243	$\"[554-674]T$	Q8Y904_LISMO_Q8Y904;
PF00358	$\"[549-681]T$	PTS_EIIA_1
TIGR00830	$\"[554-674]T$	PTBA: PTS system, glucose subfamily, IIA co
PS51093	$\"[570-674]T$	PTS_EIIA_TYPE_1
PS00371	$\"[616-628]?$	PTS_EIIA_TYPE_1_HIS

InterPro
IPR001996
Domain

Phosphotransferase system, EIIB
PD001476	$\"[67-106]T$	Q9S6S6_BBBBB_Q9S6S6;
PF00367	$\"[40-74]T$	PTS_EIIB
PS51098	$\"[37-120]T$	PTS_EIIB_TYPE_1
PS01035	$\"[52-69]T$	PTS_EIIB_TYPE_1_CYS

InterPro
IPR003352
Domain

Phosphotransferase system, EIIC
PF02378	$\"[143-456]T$	PTS_EIIC

InterPro
IPR011535
Domain

Phosphotransferase system, glucose-like IIB component
TIGR00826	$\"[61-144]T$	EIIB_glc: PTS system, glucose-like IIB comp

InterPro
IPR013013
Domain

Phosphotransferase system, EIIC component, type 1
PS51103	$\"[140-525]T$	PTS_EIIC_TYPE_1

noIPR
unintegrated

unintegrated
G3DSA:2.70.70.10	$\"[540-701]T$	no description
G3DSA:3.30.1360.60	$\"[25-127]T$	no description
tmhmm	$\"[146-166]?$ $\"[202-222]?$ $\"[272-291]?$ $\"[305-325]?$ $\"[340-362]?$ $\"[389-411]?$ $\"[421-441]?$ $\"[447-465]?$ $\"[470-485]?$ $\"[491-511]?$	transmembrane_regions

","BeTs to 3 clades of COG1263COG name: Phosphotransferase system IIC components, glucose/maltose/N-acetylglucosamine-specificFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1263 is -----------lb-efgh---j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB001127 (Sugar-specific permease, EIIA 1 domain) with a combined E-value of 4.8e-28. IPB001127 591-635***** IPB011535 (Phosphotransferase system, glucose-like IIB component) with a combined E-value of 1.8e-20. IPB011535A 40-73 IPB011535B 90-102***** IPB001996 (Phosphotransferase system PTS, EIIB domain) with a combined E-value of 2.7e-19. IPB001996A 43-86","Residues 34-297 are 43% similar to a (SYSTEM COMPONENT IIBC SUCROSE PTS) protein domain (PDA1C8J0) which is seen in Q6F0T8_MESFL.Residues 35-123 are 52% similar to a (SYSTEM COMPONENT IIBC PTS SUCROSE) protein domain (PD961401) which is seen in Q6F0U9_MESFL.Residues 36-109 are 58% similar to a (ENZYME TRANSFERASE II SUCROSE PHOSPHOTRANSFERASE) protein domain (PD763360) which is seen in Q82GH2_STRAW.Residues 36-126 are 55% similar to a (SUGAR PHOSPHOENOLPYRUVATE-DEPENDENT PYRUVATE SYSTEM PROBABLE TRANSFERASE PHOSPHOTRANSFERASE EIIABC BETA-GLUCOSIDE-SPECIFIC) protein domain (PD974743) which is seen in Q74J49_LACJO.Residues 38-124 are 57% similar to a (SYSTEM COMPONENT SUCROSE-SPECIFIC IIABC PTS) protein domain (PDA1A6Y2) which is seen in Q8EUF9_MYCPE.Residues 39-110 are 66% similar to a (GLYCOLYSIS TPIA SHUNT FATTY GLUCONEOGENESIS SYNTHESIS BIOSYNTHESIS ACID PENTOSE LIPID) protein domain (PD736489) which is seen in Q9CKH8_PASMU.Residues 41-120 are 59% similar to a (TREHALOSE ENZYME SYSTEM TRANSFERASE IIBC PTS SPECIFIC) protein domain (PDA1A1F1) which is seen in Q6KIM8_MYCMO.Residues 43-175 are 52% similar to a (SYSTEM COMPONENT TREHALOSE/SUCROSE/BETA-GLUCOSIDE IIBC PTS) protein domain (PDA0Z2L2) which is seen in Q6F133_MESFL.Residues 47-253 are 44% similar to a (SYSTEM COMPONENT TREHALOSE/SUCROSE/BETA-GLUCOSIDE IIBC PTS) protein domain (PDA1B873) which is seen in Q6F138_MESFL.Residues 67-106 are 77% similar to a (PTS COMPONENT SYSTEM IIBC ENZYME TRANSFERASE IIABC SYSTEM PHOSPHOTRANSFERASE SUCROSE-SPECIFIC) protein domain (PD001476) which is seen in Q9S6S6_BBBBB.Residues 67-137 are 65% similar to a (ENZYME ACETYLGLUCOSAMINE-SPECIFIC SYSTEM COMPONENTS TRANSFERASE GLUCOSE/MALTOSE/N- II IIC SUCROSE PHOSPHOTRANSFERASE) protein domain (PD961400) which is seen in Q8NMD6_CORGL.Residues 264-310 are 82% similar to a (PTS COMPONENT SYSTEM IIBC ENZYME TRANSFERASE SYSTEM IIABC PHOSPHOTRANSFERASE SUCROSE-SPECIFIC) protein domain (PD003077) which is seen in Q8NMD6_CORGL.Residues 326-379 are 79% similar to a (PTS COMPONENT SYSTEM IIBC ENZYME TRANSFERASE SYSTEM PHOSPHOTRANSFERASE IIABC SUCROSE-SPECIFIC) protein domain (PD914218) which is seen in PTSA_STRMU.Residues 391-442 are 78% similar to a (PTS COMPONENT SYSTEM IIBC ENZYME SYSTEM TRANSFERASE IIABC PHOSPHOTRANSFERASE SUCROSE-SPECIFIC) protein domain (PD024747) which is seen in Q88ZV9_LACPL.Residues 543-701 are 64% similar to a (ENZYME ACETYLGLUCOSAMINE-SPECIFIC SYSTEM TRANSFERASE GLUCOSE/MALTOSE/N- SUCROSE PHOSPHOTRANSFERASE COMPONENTS II IIC) protein domain (PDA18773) which is seen in Q8NMD6_CORGL.Residues 551-701 are 58% similar to a (SYSTEM SUGAR PHOSPHOENOLPYRUVATE-DEPENDENT PYRUVATE TRANSFERASE SUCROSE SPECIFIC PHOSPHOTRANSFERASE EIIABC) protein domain (PD947125) which is seen in Q74HI8_LACJO.Residues 554-700 are 65% similar to a (ENZYME COMPONENT II ABC SYSTEM PTS BETA-GLUCOSIDE-SPECIFIC) protein domain (PDA183N3) which is seen in Q9KG19_BACHD.Residues 554-674 are 73% similar to a (COMPONENT PTS SYSTEM PHOSPHOTRANSFERASE IIABC IIA ENZYME SYSTEM TRANSFERASE GLUCOSE-SPECIFIC) protein domain (PD002243) which is seen in Q8Y904_LISMO.Residues 554-682 are 70% similar to a (TRANSFERASE PTS BETA-GLUCOSIDES EIIBCA) protein domain (PDA18449) which is seen in Q88SA6_LACPL.Residues 554-645 are 60% similar to a (ENZYME SYSTEM COMPONENT IIABC PTS) protein domain (PD809022) which is seen in Q8EVH3_MYCPE.","","-59% similar to PDB:1AX3 SOLUTION NMR STRUCTURE OF B. SUBTILIS IIAGLC, 16 STRUCTURES (E_value = 3.4E_23);-59% similar to PDB:1GPR REFINED CRYSTAL STRUCTURE OF IIA DOMAIN OF THE GLUCOSE PERMEASE OF BACILLUS SUBTILIS AT 1.9 ANGSTROMS RESOLUTION (E_value = 3.4E_23);-53% similar to PDB:2GPR GLUCOSE PERMEASE IIA FROM MYCOPLASMA CAPRICOLUM (E_value = 1.0E_19);-55% similar to PDB:1F3G THREE-DIMENSIONAL STRUCTURE OF THE ESCHERICHIA COLI PHOSPHOCARRIER PROTEIN III GLC (E_value = 4.2E_18);-55% similar to PDB:1F3Z IIAGLC-ZN COMPLEX (E_value = 4.2E_18);","Residues 40 to 74 (E_value = 5.6e-17) place ANA_0751 in the PTS_EIIB family which is described as phosphotransferase system, EIIB.Residues 143 to 456 (E_value = 1.4e-49) place ANA_0751 in the PTS_EIIC family which is described as Phosphotransferase system, EIIC.Residues 549 to 681 (E_value = 9.2e-61) place ANA_0751 in the PTS_EIIA_1 family which is described as phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1.","","system IIC components, glucose-maltose-N-acetylglucosamine-specific (PTS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0753","793401","792370","1032","6.40","-3.65","37518","GTGGAGTCACACCGCGAACCCACACTGGCTGATGTCGCCCAGGCTGCAGGCGTCTCGCTGACGACAGTCTCCCGCGTACTCAACAACCGCGGCTACCTCTCCCAAGAGACACGGGAGCGGGTGGCTGAGGCGATCGCTCAGCTCAACTACCGCCCCAATCAGATCGCCCGAGCACTGCACGGAAAGTCCACGCATTCAATCGGGCTGATCGTCCCCACCGTTGCCCTGCCTTTCTTCGGCGAGCTGACCGAGCATGTCGAGGACTTCCTCGCAGAGCGCGGCTACCGGACCTTCGTCTGCAACTCGATGGGCAAGGCGGATCGGGAGCGCGAGTACCTCGACCTGCTCGTCTCCCACCGGGTCGATGGCATCATCTCCAGTGCCCACAATGACGGTCTTGCCGACTACAGCTCGATTCACCTGCCCCTGGTCAGTGTGGATCGGGACCTCTCCCCCATCGTCCCCAATGTCCGCTGCGACAACGAGGCCGGCGGTCGGCTCGCCGCCGAGCACCTGCTCAAGCGGGGGGCGCGTCGTCCGGCCCTGCTGACGTCTCGCACCGGAATCCACAACCTGAGGGAGAAGGGGTACCGCCAGGTGCTCCAGCAGGCGGGCATCGAGCCGGTGGTCTTGACCGTCGACTTCAACACACCCAACAGTGAGCGCCCCCGTCTCATCCGCGAACGGCTCGACCTCGTGGCCGACGACGTTGACGCGGTCTTCGCGACCGACGATCTGGCTGCCGCGCAAGTGATGGAGTGGGCTGCCGAGCGCGACCTGCGGATTCCGGACGACTTCAAGGTGATCGGCTTCGACGGAACGGTCGCCATGCGGCATGCTCTGCCGGCGCTGACCACGATCCAGCAACCCATCACCAAGCTGGCACGGGCGGCAGTCGACCTGCTCCTGAAGCGGATCGACTCGGCCACCGATGTCTCCGCGCAGAGCACGCAGTCGGGTGGTCCCGGGGTGGAGGACCTGCAGGTCCCCTCCCCCATGCCGGTGAAGTTGCTGCCCGGCCGTACCGCCTAG","VESHREPTLADVAQAAGVSLTTVSRVLNNRGYLSQETRERVAEAIAQLNYRPNQIARALHGKSTHSIGLIVPTVALPFFGELTEHVEDFLAERGYRTFVCNSMGKADREREYLDLLVSHRVDGIISSAHNDGLADYSSIHLPLVSVDRDLSPIVPNVRCDNEAGGRLAAEHLLKRGARRPALLTSRTGIHNLREKGYRQVLQQAGIEPVVLTVDFNTPNSERPRLIRERLDLVADDVDAVFATDDLAAAQVMEWAAERDLRIPDDFKVIGFDGTVAMRHALPALTTIQQPITKLARAAVDLLLKRIDSATDVSAQSTQSGGPGVEDLQVPSPMPVKLLPGRTA$","LacI family transcriptional regulator; sucrose operon repressor","Cytoplasm","repressor FruR","K03484 LacI family transcriptional regulator; sucrose operon repressor","Alanine racemase","","Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 1992. 267(22):15869-15874. PMID: 1639817Vartak N.B., Reizer J., Reizer A., Gripp J.T., Groisman E.A., Wu L.F., Tomich J.M., Saier Jr M.H. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 1991. 142(9):951-963. PMID: 1805309","","","

InterPro
IPR000843
Domain

Bacterial regulatory protein, LacI
PR00036	$\"[8-18]T$ $\"[18-28]T$	HTHLACI
PF00356	$\"[7-32]T$	LacI
SM00354	$\"[6-76]T$	HTH_LACI
PS50932	$\"[7-61]T$	HTH_LACI_2
PS00356	$\"[9-27]T$	HTH_LACI_1

InterPro
IPR001761
Domain

Periplasmic binding protein/LacI transcriptional regulator
PF00532	$\"[64-183]T$	Peripla_BP_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[7-64]T$	no description
G3DSA:3.40.50.2300	$\"[161-306]T$	no description

InterPro
IPR001087
Family

Lipolytic enzyme, G-D-S-L
PF00657	$\"[87-196]T$	Lipase_GDSL

InterPro
IPR008265
Active_site

Lipolytic enzyme, G-D-S-L, active site
PS01098	$\"[13-23]?$	LIPASE_GDSL_SER

InterPro
IPR013831
Domain

Esterase, SGNH hydrolase-type, subgroup
G3DSA:3.40.50.1110	$\"[12-204]T$	no description

","BeTs to 3 clades of COG2755COG name: Lysophospholipase L1 and related esterasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2755 is ------y---rlbcefgh-nuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-41% similar to PDB:2CB1 CRYSTAL STRUCTURE OF O-ACTETYL HOMOSERINE SULFHYDRYLASE FROM THERMUS THERMOPHILUS HB8,OAH2. (E_value = );","Residues 87 to 196 (E_value = 4.6e-05) place ANA_0754 in the Lipase_GDSL family which is described as GDSL-like Lipase/Acylhydrolase.","","Lipase-Acylhydrolase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0755","794930","794181","750","7.69","1.87","26994","ATGACCGCATCAGCAGCAGCAAGTGGAGCGGCAACCCCGGTCATGTCCCTGGAGTCGGTGACCCGCGACTACCGTCAGGGAGATGAGACCGTTCACGCCCTGCGCAGCACGGACCTCAAGCTGCGCGCTGGTGAGCTGGTGGGGATCCTGGGCCCCTCAGGATCAGGGAAGTCCACGCTCCTGACCATCATGGGCGGCCTGCGCACTCCCTCGAGTGGCCGCGTGACGATCTCCGGTCAGCCCTTCTCCAGCCTGCCAGAGAAACAGCGGGCCAGGCTCCGACTTCGGCGCATCGGCTTCGTCCTCCAGGCCTCGGGGCTGGTTCCCTTCCTCAGGCTCAACGACCAGTTCAGCCTGCACGACCGAGCGGCACGAACGCAGGGCGACACCGACCGACGGGACCATCTGCTGGACTCACTCGGCATCACGAAGCGCGCCCACGCCTACCCCTCGGAGCTCTCCGGGGGCGAGCGTCAGCGCGCCGCCATCGCGGTGGCGCTCTACCACGACCCGGACATCATCCTGGCCGATGAGCCCACCGCCTCCCTGGACACCCGACGGGCTCAGGACGTCGCTCGTCTGCTTGCGGACCAGACCCACGAGCTGGGCAAGGCCACGGTGATGGTCACTCATGACGAGCGGCTGCTTCCCGTATGCGACCGGGTCCTGGCGATGCACGACGGTGTCCTGACCGAACAGGACGCACCCAAGGACAGCGAGCGCCAGAGCGGTTCACGCGATGACCGCTGA","MTASAAASGAATPVMSLESVTRDYRQGDETVHALRSTDLKLRAGELVGILGPSGSGKSTLLTIMGGLRTPSSGRVTISGQPFSSLPEKQRARLRLRRIGFVLQASGLVPFLRLNDQFSLHDRAARTQGDTDRRDHLLDSLGITKRAHAYPSELSGGERQRAAIAVALYHDPDIILADEPTASLDTRRAQDVARLLADQTHELGKATVMVTHDERLLPVCDRVLAMHDGVLTEQDAPKDSERQSGSRDDR$","ABC-type transport system, involved in lipoprotein release, ATPase component","Membrane, Periplasm","ABC transporter, ATP-binding protein","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[153-195]T$	Q837P1_ENTFA_Q837P1;
PF00005	$\"[44-228]T$	ABC_tran
PS50893	$\"[15-249]T$	ABC_TRANSPORTER_2
PS00211	$\"[153-167]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[43-239]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[12-242]T$	no description
PTHR19222	$\"[15-238]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 22 clades of COG1136COG name: ABC-type transport systems, involved in lipoprotein release, ATPase componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1136 is aom--z-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 10","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.8e-33. IPB005074C 33-80 IPB005074D 141-184 IPB005074E 205-225***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.1e-24. IPB013563A 33-67 IPB013563C 150-177***** IPB005116 (TOBE domain) with a combined E-value of 2.1e-20. IPB005116A 51-67 IPB005116B 96-113 IPB005116C 153-166 IPB005116D 173-192***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 2.8e-16. IPB010509B 44-69 IPB010509D 148-192***** IPB010929 (CDR ABC transporter) with a combined E-value of 4.6e-06. IPB010929K 31-75 IPB010929M 150-196","Residues 13-234 are 46% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 14-228 are 42% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 14-138 are 48% similar to a (LIPOPROTEIN ATP-BINDING RELEASING SYSTEM LOLD) protein domain (PDA0I1Q0) which is seen in Q7UH39_RHOBA.Residues 14-132 are 47% similar to a (CG1801-PA ATP-BINDING) protein domain (PD324461) which is seen in Q9VRG5_DROME.Residues 14-99 are 59% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0J0E5) which is seen in Q6LV70_PHOPR.Residues 15-228 are 43% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 15-101 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3K8) which is seen in Q9A6K2_CAUCR.Residues 15-209 are 45% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 15-248 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 22-111 are 57% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 26-228 are 48% similar to a (ATP-BINDING ABC PRECURSOR TRANSPORTER SIGNAL) protein domain (PDA0X2Z3) which is seen in Q6MM73_BDEBA.Residues 31-242 are 44% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 32-228 are 43% similar to a (ATP-BINDING) protein domain (PDA101X7) which is seen in Q6LGG0_PHOPR.Residues 33-84 are 65% similar to a (COBALT ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PDA0I1O9) which is seen in Q7NNW9_GLOVI.Residues 34-230 are 46% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 34-203 are 49% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 34-174 are 47% similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 34-85 are 75% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q89X55_BRAJA.Residues 34-212 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 37-225 are 43% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 38-223 are 44% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 47-239 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD738128) which is seen in Q8G833_BIFLO.Residues 107-212 are 50% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA184H5) which is seen in Q6W139_RHISN.Residues 116-236 are 44% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 127-231 are 48% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.Residues 131-239 are 51% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 134-233 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 137-195 are 64% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD436020) which is seen in Q9A7G4_CAUCR.Residues 140-212 are 57% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q87LE8_VIBPA.Residues 141-242 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 144-234 are 54% similar to a (ATP-BINDING BIOM) protein domain (PDA0I300) which is seen in Q6GUB2_RHIET.Residues 149-211 are 60% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 150-232 are 58% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 150-234 are 55% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 153-195 are 88% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q837P1_ENTFA.","","-60% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 5.5E_37);-60% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 1.2E_36);-56% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 4.5E_31);-53% similar to PDB:1G29 MALK (E_value = 1.1E_24);-52% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.5E_23);","Residues 44 to 228 (E_value = 5.1e-55) place ANA_0755 in the ABC_tran family which is described as ABC transporter.","","transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0756","796039","794927","1113","5.52","-5.85","38960","ATGTTCCTCGCGCTGCGCGAGATCCGCCACGAACCCGTGCGCTTCACGCTCATCATCTCCGTCATCACCCTGGTGGCCTACCTCACATTTTTCTTGGCCTCCTTGGCTGTGGGCCTCGCCCATCGCTACCGCGCCGGCATCGACGGCTGGAACACCGCCAGCGTCGCCGTCACGGACGCCTCCAACGAGAACCTCTCCGCCTCCCGTCTGAGCGACAAGCAGCTGGAAGCGGCCACGGCCCTGGCCAAGGACAACGGAACCACAGCCTCTGCCCTGATGAGCACGGCCGCTGTTGCCCAGGCGCCAGACGTCAAGGACGAGGACGGCGAGGCGCTGCGTGAGGATGTCTTCGCCTTCGGAATCGATCTGGACGGACAGCTCAGTCCGCCTGTGGCCGACGGGCGGACGATCTCTGCCCCCGATAGCGAGGTCCTCGTCGACGACTCGCTGAAGGCCAAGGGACTCGCGGTTGGTGACACGATTCGACTGCTGGGCTCTGACCACGACTGGACCGTTGTCGGATTCACCCATGACACCACCTTCCAGGCGGCTCCCGTGGTGACCATGGACAGCCGGGCCTTGCGCCAGCACGGCCCCACCAGCCTGTCCCCAGCCGTCTCCGCCGTCGTCTTCAACTCCGACCTGACCACCGACAGCAAGGCCACGCAGTCCGCCAAGGACGCAGGACTGACGATCCTCACCACCGAGGAACTCGTTCGCACGCTCCCCGGCTACTCGGCCCAGGTACTCACCTTCAGCCTCATGATCGGCTCACTCATCATCATCACCTCCACGGTTCTGGGCATCTTCATCTACGTGCTGACGCTGCAGAAGAGACCGGTCCTGGGCATCCTCAAAGCCCGCGGCGTCCCCACCGGCTACCTCATCCGCTCCGGATGCGCCCAGACCCTCGTGCTGTCGGTAGCCGGCATCGGCATCGGCCTGCTTCTGACGATGGCGACGTCCCTGGTCCTCCCCCGCGCCGTGCCTTTCAGGATTTCCGCTCCCCTGGACCTGCTCATCGTCACGGCATTCATCGCCATCTCCGTCATCGGAGGCTTCATCTCCGTCCGGGTCATCTCCCGCATCGATCCCGTGGAGGCCATCTCATGA","MFLALREIRHEPVRFTLIISVITLVAYLTFFLASLAVGLAHRYRAGIDGWNTASVAVTDASNENLSASRLSDKQLEAATALAKDNGTTASALMSTAAVAQAPDVKDEDGEALREDVFAFGIDLDGQLSPPVADGRTISAPDSEVLVDDSLKAKGLAVGDTIRLLGSDHDWTVVGFTHDTTFQAAPVVTMDSRALRQHGPTSLSPAVSAVVFNSDLTTDSKATQSAKDAGLTILTTEELVRTLPGYSAQVLTFSLMIGSLIIITSTVLGIFIYVLTLQKRPVLGILKARGVPTGYLIRSGCAQTLVLSVAGIGIGLLLTMATSLVLPRAVPFRISAPLDLLIVTAFIAISVIGGFISVRVISRIDPVEAIS$","ABC-type transport system, involved in lipoprotein release, permease component","Membrane, Cytoplasm, Extracellular","ABC transporter permease","K02004","protein of unknown function DUF214","","","","","

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[205-365]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[256-276]?$ $\"[305-325]?$ $\"[335-355]?$	transmembrane_regions

","BeTs to 12 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","Residues 1-278 are 52% similar to a (PERMEASE ABC TRANSMEMBRANE TRANSPORTER TRANSPORTER LIPOPROTEIN ABC-TYPE MEMBRANE SYSTEM COMPONENT) protein domain (PD041504) which is seen in Q6GK08_STAAR.Residues 301-369 are 68% similar to a (PERMEASE ABC TRANSPORTER TRANSPORTER MEMBRANE TRANSMEMBRANE SYSTEM PROTEIN LIN2726 SPYM18_0832) protein domain (PD581331) which is seen in Q9CDG5_LACLA.","","No significant hits to the PDB database (E-value < E-10).","Residues 205 to 365 (E_value = 6.8e-15) place ANA_0756 in the FtsX family which is described as Predicted permease.","","transporter permease (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0757","796257","798749","2493","6.50","-7.26","88469","TTGTTCTCAGGAGCGCTGTGCGCGGCATCGGGACCGGGACATCCGGTCGTCGGCGACGTCTGGCAGTCCGGCACAATGGTGCGTGTGACTGGAAGGGCTGCTGGAGACAACCCCGCCGATGCGCATGACGTCATCCGTGTCGTCGGGGCTCGTGAGAACAACTTGCGCAGTGTCGACGTCGTCATCCCCAAGCGCAGGCTGACGGTCTTCACCGGTGTATCGGGCTCGGGCAAGAGCTCGCTCGTTTTCGCCACGATCGCCGCCGAGTCGCGCCGTCTGGTCAATGAGACCTACCCGGCTTTCGTGCAGGGCTTCATGGAGACTGGCACACGTCCCGACGTCGACCGTCTGGAAGGACTGACGCCGGCGATCGTCGTGGACCAGGAACGCCTGGGATCCAACCCGCGCTCAACCCTCGGCACCGTCAGCGACGTCGGAGCCCTCCTGAGGGTTCTGTACTCGACGCACGGCGTGCCACACATCGGCTCACCTCAAGCCTTCGCCTTCAACGTCCCGTCCGTCACCGGTGGTGGTGCGCTCACCACGCAGCGCGGCAGCCGCAAGATCGTCGAGCGCAAGACATTCACCATCCAGGGCGGGATGTGCCCGGCTTGTGAAGGCATGGGTCAGGTCTCAGACATCGATCTGACGCAAGTGCTCGATGAGACGCTCTCCTTGAATGACGGCGCCATCACCGTCCCAGGATACGCAGCCGGTGGCTGGCAGGTGCGCAGCTTTACTGAATCCGGTCTTTTTCCGGCAGATGTTCCGGTAGCCGCCTTCACGCTCCAGCAGCGAGACGATCTGCTCTACAAGGAGCCCACGAAGATCAAGGTCGGCGGCATCAATGTGACCTACGAGGGGCTCGTTCTGAGAATTCGACGGTCGATCCTGTCCAAGGAACCACAGGCACTGCAGCCTCATATTCGCTCCTTCGTGGAACGGGCCGTCGTGTTCGGAACCTGCCCGCAATGTGATGGAACCCGCCTGTCCGAACCCGCCCGCAGCTGTTTGATCGACGGTAAATCCATTGCTGATGCCTGCGCCATGCAGATCTCGGATCTGGCGCAGTGGATCACTCGTCTTCAAGGGATTCTGACCGGTGCCGTTCCCCTGCTGGATAATCTGAAGGACATGCTGGACGCCTTCGTGCTCATCGGGCTGGGCTATCTGTCACTGGACCGCCCGGCCTCGACCCTCTCGGGCGGTGAGGCCCAGCGCACCAAGCTCGTGCGCCACCTGGGCTCGGCCCTCACCGATGTCACCTACGTCTTCGATGAGCCCAGCATCGGTCTGCACCCGCACGACCTCCACCAGATGAATGAGCTGCTGCTGTCGCTACGGGACAAAGGAAACACCGTGCTCGTCATCGAGCACAAACCCGAGACCATCTCGATAGCCGACCACGTGGTGGACCTGGGGCCGGGAGCGGGAACCCGAGGAGGCCGGATCTGCTTCGAAGGAACGGTCGAGCAGTTGCGCGGCTCCGACACTCTTACCGGACGCCACCTAGCGGACCGGATGCGAATCAAGAACAGCCACCGCTCCCCCACGGGAAGAATCGAGATTCGCGGCGCCAGCACGAACAATCTTCACGACGTCGATGTCGATATTCCCCTGGGAGTTCTCAGCGTCATCACTGGAGTGGCCGGATCTGGCAAGTCGAGCCTCATCCATGGTCACCTCTCCCCCATTGATGGCGTGGTGACGATCGACCAGGCACCGATCAAAGGCTCCAGGCGCTCGAATCCCGCCACCTATACCGGACTGCTCGACCCTGTTCGCAAGGCCTTCGCCACAGCCAATAAGGACCAAGGTGCGAAACCCGCGCATTTCTCGGCGAACTCCGACGGGGCCTGTCCGGTGTGCGGCGGAACGGGTGTCATTGAGACGCAGCTGGGCTTCATGGAGACCGTGGAGTCCCGATGCCAGGCCTGTGACGGTCGGCGTTTCAGGGACGAGGTGCTCGCCTATCGCCTCGCCGGATACAGCATCGCCGATGTCCTGGACATGAGCGTCGAGGCGGCGCTGGCCTTCTTCTCCCAGGGCGAGGCTCGTCTCCCCGCGGCAGCCAGAATCCTGTCACGGCTGAAGGATGTGGGGCTCGGCTACCTCCACCTCGGCCAGGCCCTGACCACCTTGTCCGGTGGTGAGCGTCAGCGGCTCAAGCTCGCCGTCCACCTGAGCCAGGAAGGCCGCATCATCGTGCTCGATGAGCCGACTGTCGGACTGCACCCGGCCGACATCGAGGCCATGCTGACGCTCCTGGATCACCTCGTAGATAGCGGCCGCACCGTCGTCGTCGTTGAGCACCATCAGGCCGTGATGGTGCACGCCGACTGGATCATCGACCTCGGCCCCGGAGCGGGCCACGACGGCGGCCGCGTTGTGTTCACCGGAACACCGGCGCAGATGGTGGCGGAGCGAAGCACACTGACGGGCCAGTACCTCGCCCGGTACGTCGAGGAGGTGAACGACGATGCCCCCGAGTGA","LFSGALCAASGPGHPVVGDVWQSGTMVRVTGRAAGDNPADAHDVIRVVGARENNLRSVDVVIPKRRLTVFTGVSGSGKSSLVFATIAAESRRLVNETYPAFVQGFMETGTRPDVDRLEGLTPAIVVDQERLGSNPRSTLGTVSDVGALLRVLYSTHGVPHIGSPQAFAFNVPSVTGGGALTTQRGSRKIVERKTFTIQGGMCPACEGMGQVSDIDLTQVLDETLSLNDGAITVPGYAAGGWQVRSFTESGLFPADVPVAAFTLQQRDDLLYKEPTKIKVGGINVTYEGLVLRIRRSILSKEPQALQPHIRSFVERAVVFGTCPQCDGTRLSEPARSCLIDGKSIADACAMQISDLAQWITRLQGILTGAVPLLDNLKDMLDAFVLIGLGYLSLDRPASTLSGGEAQRTKLVRHLGSALTDVTYVFDEPSIGLHPHDLHQMNELLLSLRDKGNTVLVIEHKPETISIADHVVDLGPGAGTRGGRICFEGTVEQLRGSDTLTGRHLADRMRIKNSHRSPTGRIEIRGASTNNLHDVDVDIPLGVLSVITGVAGSGKSSLIHGHLSPIDGVVTIDQAPIKGSRRSNPATYTGLLDPVRKAFATANKDQGAKPAHFSANSDGACPVCGGTGVIETQLGFMETVESRCQACDGRRFRDEVLAYRLAGYSIADVLDMSVEAALAFFSQGEARLPAAARILSRLKDVGLGYLHLGQALTTLSGGERQRLKLAVHLSQEGRIIVLDEPTVGLHPADIEAMLTLLDHLVDSGRTVVVVEHHQAVMVHADWIIDLGPGAGHDGGRVVFTGTPAQMVAERSTLTGQYLARYVEEVNDDAPE$","UvrABC system protein A","Cytoplasm","uvrA-like protein","ABC transporter related","ABC transporter related","","Ziegelin G., Scherzinger E., Lurz R., Lanka E. Phage P4 alpha protein is multifunctional with origin recognition, helicase and primase activities. EMBO J. 1993. 12(9):3703-3708. PMID: 8253092","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[713-757]T$	Q92XA4_RHIME_Q92XA4;
PF00005	$\"[65-476]T$ $\"[689-788]T$	ABC_tran
PS50893	$\"[169-500]T$ $\"[508-812]T$	ABC_TRANSPORTER_2

InterPro
IPR013237
Domain

Phage P4 alpha, zinc-binding
SM00778	$\"[615-649]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[393-510]T$ $\"[521-816]T$	no description
PTHR19222	$\"[670-822]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","No hits to the COGs database.","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.1e-12. IPB005074D 702-745 IPB005074E 765-785***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.2e-08. IPB010509D 709-753 IPB010509E 763-793***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.2e-07. IPB013563A 54-88 IPB013563C 711-738","Residues 42-88 are 70% similar to a (A EXCINUCLEASE ABC ATP-BINDING SUBUNIT) protein domain (PDA1A4F6) which is seen in Q88X70_LACPL.Residues 53-215 are 44% similar to a (A EXCINUCLEASE ATP-BINDING ABC SUBUNIT-RELATED ABC SUBUNIT) protein domain (PD708955) which is seen in Q737S0_BACC1.Residues 89-215 are 78% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR UVRABC) protein domain (PD363446) which is seen in Q82LB4_STRAW.Residues 173-223 are 71% similar to a (UVRA-LIKE) protein domain (PD988575) which is seen in Q6AF09_BBBBB.Residues 225-289 are 76% similar to a (ATP-BINDING UVRA-LIKE RESISTANCE DAUNORUBICIN EXCINUCLEASE ABC SUBUNIT A ATPASE TRANSPORTER) protein domain (PD739903) which is seen in Q8FQH9_COREF.Residues 282-320 are 92% similar to a (SNORO ATP-BINDING) protein domain (PD988573) which is seen in Q9RIP8_STRNO.Residues 285-362 are 82% similar to a (A DNA ATP-BINDING SUBUNIT EXCINUCLEASE ABC EXCISION UVRA REPAIR UVRABC) protein domain (PD697224) which is seen in O86699_STRCO.Residues 669-765 are 60% similar to a (RESISTANCE ATP-BINDING DAUNORUBICIN) protein domain (PDA1A571) which is seen in Q836S6_ENTFA.Residues 693-765 are 58% similar to a (UVRA-LIKE TRANSPORTER ABC) protein domain (PDA1A825) which is seen in Q6A9D4_PROAC.Residues 380-457 are 65% similar to a (LIN1813) protein domain (PD661935) which is seen in Q92AV6_LISIN.Residues 694-725 are 90% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD565575) which is seen in Q6AF09_BBBBB.Residues 418-587 are 46% similar to a (DNA A EXCISION EXCINUCLEASE ATP-BINDING SUBUNIT SOS UVRA DNA-BINDING SYSTEM) protein domain (PD190842) which is seen in UVRA_CHLPN.Residues 426-458 are 93% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD001034) which is seen in Q8Y5K9_LISMO.Residues 459-504 are 69% similar to a (A EXCINUCLEASE ABC ATP-BINDING SUBUNIT) protein domain (PDA124P2) which is seen in Q88X70_LACPL.Residues 459-488 are 93% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR UVRABC) protein domain (PD508139) which is seen in Q82LB4_STRAW.Residues 486-590 are 58% similar to a (A EXINUCLEASE ATP-BINDING SUBUNIT ABC) protein domain (PD953256) which is seen in Q8CPR9_STAEP.Residues 493-587 are 49% similar to a (A EXCINUCLEASE ATP-BINDING SUBUNIT ABC) protein domain (PD953261) which is seen in Q7URK7_RHOBA.Residues 591-668 are 67% similar to a (A DNA ATP-BINDING SUBUNIT EXCINUCLEASE EXCISION ABC UVRA REPAIR UVRABC) protein domain (PD001646) which is seen in O86699_STRCO.Residues 669-765 are 60% similar to a (RESISTANCE ATP-BINDING DAUNORUBICIN) protein domain (PDA1A571) which is seen in Q836S6_ENTFA.Residues 693-765 are 58% similar to a (UVRA-LIKE TRANSPORTER ABC) protein domain (PDA1A825) which is seen in Q6A9D4_PROAC.Residues 694-725 are 90% similar to a (A DNA ATP-BINDING EXCINUCLEASE SUBUNIT ABC EXCISION UVRA REPAIR NUCLEASE) protein domain (PD565575) which is seen in Q6AF09_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 65 to 476 (E_value = 1.9e-08) place ANA_0757 in the ABC_tran family which is described as ABC transporter.Residues 541 to 788 (E_value = 6.2e-22) place ANA_0757 in the ABC_tran family which is described as ABC transporter.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0759","798736","800019","1284","5.82","-8.42","45901","ATGCCCCCGAGTGAGGCGCAGGGTGATGGACGTGCCGAGGCGGCATGTACCTATCGGATCCGCCCGGCGACGATGGCTGACTCTCCCGCGATCCGCCGGATCCGTAACGCCGCCGTGCGGGAGTCCCTGGCCATCTGGACCAGCATTGAGCAGGACCACGCCGGGGCCGAGGCCTGGCTGGCGCCCATGGTGCAGCGCGGAACGGCTCTCGTCGCTCACGTCAGCGGTAAGCCGCAGGACGTCGTTGGCTTCGCGGTGGCCGGCCCCTGGCACTCCTACGAGGGCTACGCCCGCACCGTTGAGGACTCGATCTACCTGAGCCCTGCGGCACAAGGCAAAGGTCTTGGTGCCAGGCTCCTCGCCGCCCTCATCGAGGCCTCACGGCGGGCAGGGGACCGCACGATGATCGCTCTCATCGAGGCGGGTCACGCGACATCGGTGCGCCTGCACGAGCGCTATGGTTTCACCACTGTCGGCACTGTCCCGCAGGCCGGCGAGAAACATGGTCAGATCCTCGACCTGACCCTCATGAGCCGTTGCCTGAAAGGACCCACCGTGTGCGACAACCAGAACGAGCCCTCTGACAGCCTCCGACGGGTCAACGCCGACCAGGCCATCCAGCTCCAGCCCGAGGAACCTGCCGTCACCCAGTGGCAGGTCAGTGCCACCGATGAGCTCGTTGCGCACCTGCTTAACCTGGTCGGCACGCCCCAGGGACGGCCGGCGATCATCGCCGTCGACGGGAGGGGCGGATCGGGCAAGACCACACTCACCACGGCGCTGGCCGCAGCCGTCCCCGGCGCGCAAGCCTTTCACCTGGACGACCTCATCTGGAACGAGCCGCTCTACGACTGGGATCAGCTGTACGTCGACACCCTGACCCAGCTGCGGCAGGCCGGCAGCCTCGACCTGGTCCCGGACAAGTGGCGCGAGCACGGCCGCGAGGGCTCCATCCGGATCCCAGCCGGCTCTCCCCTGGTCCTCGTCGAGGGGACCGGGGCGGGTCTGGCCGCAGTGCGCAGCCTCATTGACGCGCACGTGTGGGTTCAGACCGGCGACGACGTGGCCGAGCGCCGCGGCATCAAGCGGGACATCGCTGAGGGAGTCAACGGCGACGCCGAGGAGTCGGTGCGTTTCTGGCACTGGTGGATGGCCGGCGAGCGCCTTTTCTTCGCCAAGGACCGTCCCTGGCGGCGCGCAGACGTCATCGTCTCCGGTGACGCGCCCACCGGTGTAGGCCCAGGAGAGATCGCCTGGACTCCGGGGCCGCTCCTGGCCGGCTGA","MPPSEAQGDGRAEAACTYRIRPATMADSPAIRRIRNAAVRESLAIWTSIEQDHAGAEAWLAPMVQRGTALVAHVSGKPQDVVGFAVAGPWHSYEGYARTVEDSIYLSPAAQGKGLGARLLAALIEASRRAGDRTMIALIEAGHATSVRLHERYGFTTVGTVPQAGEKHGQILDLTLMSRCLKGPTVCDNQNEPSDSLRRVNADQAIQLQPEEPAVTQWQVSATDELVAHLLNLVGTPQGRPAIIAVDGRGGSGKTTLTTALAAAVPGAQAFHLDDLIWNEPLYDWDQLYVDTLTQLRQAGSLDLVPDKWREHGREGSIRIPAGSPLVLVEGTGAGLAAVRSLIDAHVWVQTGDDVAERRGIKRDIAEGVNGDAEESVRFWHWWMAGERLFFAKDRPWRRADVIVSGDAPTGVGPGEIAWTPGPLLAG$","Phosphinothricin N-acetyltransferase","Cytoplasm, Extracellular","phosphinothricin N-acetyltransferase, putative","phosphinothricin N-acetyltransferase; putative ","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[73-156]T$	Acetyltransf_1
PS51186	$\"[18-177]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[240-427]T$	no description
G3DSA:3.40.630.30	$\"[18-192]T$	no description
PTHR10285	$\"[251-367]T$	URIDINE KINASE RELATED

","BeTs to 6 clades of COG1247COG name: Sortase and related acyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1247 is ---------d-lbcefg----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-50% similar to PDB:1YVO hypothetical acetyltransferase from P.aeruginosa PA01 (E_value = 3.0E_21);-50% similar to PDB:2BL1 CRYSTAL STRUCTURE OF A PUTATIVE PHOSPHINOTHRICIN ACETYLTRANSFERASE (PA4866) FROM PSEUDOMONAS AERUGINOSA PAC1 (E_value = 3.0E_21);-50% similar to PDB:2J8M STRUCTURE OF P. AERUGINOSA ACETYLTRANSFERASE PA4866 (E_value = 3.0E_21);-50% similar to PDB:2J8N STRUCTURE OF P. AERUGINOSA ACETYLTRANSFERASE PA4866 SOLVED AT ROOM TEMPERATURE (E_value = 3.0E_21);-50% similar to PDB:2J8R STRUCTURE OF P. AERUGINOSA ACETYLTRANSFERASE PA4866 SOLVED IN COMPLEX WITH L-METHIONINE SULFOXIMINE (E_value = 3.0E_21);","Residues 73 to 156 (E_value = 6e-15) place ANA_0759 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","N-acetyltransferase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0760","801163","800042","1122","7.11","0.75","39232","ATGGCTCAGCGCATCGGCATTCTCACGGCGGGCGGCGACGCCCCGGGACTCAACGCGGCGATCCGAGGTTTCGGAAAGGCGGCGATCCAGCAGCACGGCTGGGAGCTCGTCGGCTTCCGGGACGGCATGCGCGGCCTGGCCGAGAACCGCTTCACTGAGCTCGACCCCGCTGCTCTGTCCGGGATCCTCACTACCGGCGGAACCATGTTGGGAACCAGCCGGGACAAGGTGCATCGGATGATGGTGGACGGCGAGCCCCGGGACATGGTGCCTACCATCGTGGAGAACTGCGAGAAGGACGGGATCGACGCCCTGGTCTGCCTCGGCGGGGGCGGGACCGCGAAGAACGCCAAGCGCCTCATGGATGCTGGCCTGAACGTCATCCATCTGCCCAAGACCATCGACAACGACATCGTCCACACCGACTCCTCCTTCGGCTTCGCCACGGCTCTGGAGATCGCCACCCAGGCCGTGGACCGCCTGCACTCGACGGCGCACTCCCACCACCGCATCATCCTCACCGAGATCATGGGGCACCGAGCCGGCTGGCTGGCCCTGGGCGCCGGCATCGCAGGTGGGGCGGATGTCATTCTGCTGCCGGAGATTCCGTACTCGGTGGACGCGATCGCGGACAAGATTGAGCGGCGCCGCTCCCACGGGTCGTCCTTCTCCGTGGTGGCCGTGGCCGAGGGGGCGCTGTCCGTGACGGATCACGCCGAGCTGGAGCACGCCCGCGCCCTGGTCAAGGACGCTTCCAGTCCCGAGCGCAAGGCCATGGCGAAGCGGGGCGTCAAGCGTCTGGAGGCCTCTCACCGCGCCAACACCTTCACCCTGGCCGAGCAGCTGGAGAGCCTGACCGGGCTGGAGGCGCGCGTGTCCATCCTGGGATACGTCCAGCGCGGCGGCTCGCCCTGCGGAGCGGATCGTCTGTTGGGCACGCGCCTGGGCGTGGCCGGAGCCAACGCGATTGCGGAGGGCCACTTCGGAGTCATGGTCGCCGACCGCGGTCACGGCACGGAGCTGGTGCCGCTCAAGGAGGTGGCCGGACGCACCAAGTTCGTTCCGGCCAACCACGAGTGGATCCAGGCCGCACGTGCCGTGGGGACCGCGCTGGGGGACTGA","MAQRIGILTAGGDAPGLNAAIRGFGKAAIQQHGWELVGFRDGMRGLAENRFTELDPAALSGILTTGGTMLGTSRDKVHRMMVDGEPRDMVPTIVENCEKDGIDALVCLGGGGTAKNAKRLMDAGLNVIHLPKTIDNDIVHTDSSFGFATALEIATQAVDRLHSTAHSHHRIILTEIMGHRAGWLALGAGIAGGADVILLPEIPYSVDAIADKIERRRSHGSSFSVVAVAEGALSVTDHAELEHARALVKDASSPERKAMAKRGVKRLEASHRANTFTLAEQLESLTGLEARVSILGYVQRGGSPCGADRLLGTRLGVAGANAIAEGHFGVMVADRGHGTELVPLKEVAGRTKFVPANHEWIQAARAVGTALGD$","6-phosphofructokinase","Cytoplasm","Phosphofructokinase","6-phosphofructokinase ","6-phosphofructokinase","","Ronimus R.S., Morgan H.W. The biochemical properties and phylogenies of phosphofructokinases from extremophiles. Extremophiles 2001. 5(6):357-373. PMID: 11778837Blangy D., Buc H., Monod J. Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli. J. Mol. Biol. 1968. 31(1):13-35. PMID: 4229913Evans P.R., Hudson P.J. Structure and control of phosphofructokinase from Bacillus stearothermophilus. Nature 1979. 279(5713):500-504. PMID: 156307Bapteste E., Moreira D., Philippe H. Rampant horizontal gene transfer and phospho-donor change in the evolution of the phosphofructokinase. Gene 2003. 318:185-191. PMID: 14585511Hansen T., Musfeldt M., Schonheit P. ATP-dependent 6-phosphofructokinase from the hyperthermophilic bacterium Thermotoga maritima: characterization of an extremely thermophilic, allosterically regulated enzyme. Arch. Microbiol. 2002. 177(5):401-409. PMID: 11976749Hellinga H.W., Evans P.R. Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase. Eur. J. Biochem. 1985. 149(2):363-373. PMID: 3158524","","","

InterPro
IPR000023
Family

Phosphofructokinase
PD000707	$\"[119-180]T$	Q6ABK5_PROAC_Q6ABK5;
PR00476	$\"[7-26]T$ $\"[33-46]T$ $\"[101-117]T$ $\"[128-145]T$ $\"[146-164]T$ $\"[166-182]T$ $\"[184-201]T$ $\"[220-232]T$	PHFRCTKINASE
PTHR13697	$\"[125-240]T$ $\"[283-354]T$	PHOSPHOFRUCTOKINASE
PF00365	$\"[3-325]T$	PFK

InterPro
IPR012003
Family

ATP-dependent phosphofructokinase, prokaryotic
PIRSF000532	$\"[3-373]T$	ATP-dependent phosphofructokinase, prokaryotic type

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.450	$\"[3-204]T$	no description

","BeTs to 14 clades of COG0205COG name: 6-phosphofructokinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0205 is ------yqvdrlbce-ghs--j-itwNumber of proteins in this genome belonging to this COG is 3","***** IPB000023 (Phosphofructokinase) with a combined E-value of 8.9e-51. IPB000023A 5-26 IPB000023B 148-201 IPB000023C 289-320","Residues 4-117 are similar to a (KINASE TRANSFERASE GLYCOLYSIS PHOSPHOFRUCTOKINASE 6-PHOSPHOFRUCTOKINASE ALLOSTERIC ENZYME PHOSPHOHEXOKINASE ATP-BINDING MAGNESIUM) protein domain (PD024538) which is seen in Q6ABK5_PROAC.Residues 119-180 are similar to a (KINASE TRANSFERASE GLYCOLYSIS PHOSPHOFRUCTOKINASE 6-PHOSPHOFRUCTOKINASE ALLOSTERIC ENZYME PHOSPHOHEXOKINASE ATP-BINDING MAGNESIUM) protein domain (PD000707) which is seen in Q6ABK5_PROAC.Residues 195-354 are 45% similar to a (KINASE PHOSPHOFRUCTOKINASE BLL2850) protein domain (PD714571) which is seen in Q8KFS2_CHLTE.Residues 196-355 are 42% similar to a (KINASE 6-PHOSPHOFRUCTOKINASE TRANSFERASE PREDICTED PHOSPHOFRUCTOKINASE PHOSPHOFRUCTOKINASE) protein domain (PD690105) which is seen in Q98CS6_RHILO.Residues 311-364 are 72% similar to a (KINASE TRANSFERASE 6-PHOSPHOFRUCTOKINASE GLYCOLYSIS PHOSPHOFRUCTOKINASE ALLOSTERIC ENZYME PHOSPHOHEXOKINASE ATP-BINDING MAGNESIUM) protein domain (PD603823) which is seen in Q6ABK5_PROAC.","","-49% similar to PDB:1PFK CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS (E_value = 2.0E_42);-49% similar to PDB:2PFK THE CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI (E_value = 2.0E_42);-46% similar to PDB:6PFK PHOSPHOFRUCTOKINASE, INHIBITED T-STATE (E_value = 2.7E_39);-46% similar to PDB:1MTO X-ray Crystal structure of a Phosphofructokinase mutant from Bacillus stearothermophilus bound with frutose-6-phosphate (E_value = 4.5E_39);-46% similar to PDB:1ZXX The crystal structure of phosphofructokinase from Lactobacillus delbrueckii (E_value = 4.5E_39);","Residues 3 to 325 (E_value = 4.1e-67) place ANA_0760 in the PFK family which is described as Phosphofructokinase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0761","801345","801704","360","4.83","-8.64","13601","ATGGCAGACCGCGCACTGCGAGGCATGACCATTGGCGCGAAGTCGATGGAGTCGGAGGACGGCGTCGAGTTCGCCGAGCGGATGATCGTCAGCTACGAGTGCCCGATGGCGCACGTCACCAGGATCCCGATGTCCACCGAGGCCGAGGTGCCTCCCACCTGGGAGTGCCCCGAGTGCGGCCAGCTCGCCGCCCGACGCGGCGAGGACGAGCCCGAGCCCGACGAGCCCAAGAAGACCCCGCGCACCCACTGGGACATGCTCCTGGAGCGCCGCAAGGTCGATGAGCTCGAGGTTCTCCTCAACGAGCGCCTCGAGGCGCTGCGCAGCGGTGAGGTCTACCGCGAGCGGGTCAGCGGCTGA","MADRALRGMTIGAKSMESEDGVEFAERMIVSYECPMAHVTRIPMSTEAEVPPTWECPECGQLAARRGEDEPEPDEPKKTPRTHWDMLLERRKVDELEVLLNERLEALRSGEVYRERVSG$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","Meyer J., Gagnon J., Sieker L.C., Van Dorsselaer A., Moulis J.M. Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data. Biochem. J. 1990. 271(3):839-841. PMID: 2244884Adman E.T., Sieker L.C., Jensen L.H. Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution. J. Mol. Biol. 1991. 217(2):337-352. PMID: 1992166Lee W.Y., Brune D.C., Lobrutto R., Blankenship R.E. Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, Heliobacillus mobilis. Arch. Biochem. Biophys. 1995. 318(1):80-88. PMID: 7726577Day M.W., Hsu B.T., Joshua-Tor L., Park J.B., Zhou Z.H., Adams M.W., Rees D.C. X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. Protein Sci. 1992. 1(11):1494-1507. PMID: 1303768Frey M., Sieker L., Payan F., Haser R., Bruschi M., Pepe G., LeGall J. Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 A resolution. J. Mol. Biol. 1987. 197(3):525-541. PMID: 3441010","","","

InterPro
IPR001052
Domain

Rubredoxin
PS00202	$\"[50-60]T$	RUBREDOXIN

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-104 are 70% similar to a (ELECTRON GTPASE CGL1477 SCO1421 ML1439 MB2076 MLCB2052.03C MEMBRANE-ASSOCIATED) protein domain (PD029236) which is seen in Q8G6A4_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0762","802550","801711","840","7.08","0.19","30390","GTGAAGGCACTCGTCGTCATCCCCACCTACAACGAGATCGAGTCCCTGCCCACGGCACTGGACCGGGTCCGCGAGCACGCTCCTGAGGCCGACATTCTCGTCGTCGACGACGGTTCCCCCGACGGCACCGGCGACTACGCCGACACCCGTGCCGACGAGGACTCCCACATCCATGTCCTGCACCGCTCGGAGAAGAACGGGCTGGGCCCGGCCTACCTCGCCGGGTTCTCCTGGGCACTGGCTGCCGGCTACGAGCTCATCGTGGAGATGGATGCCGACGGCTCCCACCGCGCCGAGGACCTGGCCCTGCTCATTCAGCGCGCTGAGATGGCGGACGAGCCGGACCTCGTCATCGGCTCGCGGTGGGTCTCCGGCGGCGCCACCGAGGGCTGGGACGCCAAGCGCGTGGCCCTGTCCAAGGCCGGGAACCTCTACATCAACGCCATGCTGGGGCTGCGCGTCAAGGACGCCACCGCGGGCTTCCGGGTCTTCCGCGCCTCGATCCTGCGCCGCATGGACCTGGGGAAGGTCGAGGCCCTCGGCTACGGGTTCCAGGTCAACATGACCAAACTGGTTGACGAGATCGGCGGACGCATCGTGGAGATGCCGATCACCTTCTTGGAGCGGGAGGCCGGGCAGTCCAAGCTCTCGGGGGGTATATTCACCGAGGAGCTGTCCCTGGTGACCCGCTGGGGTGTAGCCAAGCGCTCCGGCCAGCTGCTCGATGCGGCCAAGGTCGCCGGAAGCAGGCTGCGCGCCGCCCGCGACAAGCGCCGTCGGGCCGCCGCCGGGTACCAGCAGCAGCGTCCGACGAGCTCATCGCGGCAGAAGCGCTCCTGA","VKALVVIPTYNEIESLPTALDRVREHAPEADILVVDDGSPDGTGDYADTRADEDSHIHVLHRSEKNGLGPAYLAGFSWALAAGYELIVEMDADGSHRAEDLALLIQRAEMADEPDLVIGSRWVSGGATEGWDAKRVALSKAGNLYINAMLGLRVKDATAGFRVFRASILRRMDLGKVEALGYGFQVNMTKLVDEIGGRIVEMPITFLEREAGQSKLSGGIFTEELSLVTRWGVAKRSGQLLDAAKVAGSRLRAARDKRRRAAAGYQQQRPTSSSRQKRS$","Glycosyltransferase involved in cell wall biogenesis","Cytoplasm","Glycosyltransferases involved in cell wallbiogenesis","dolichyl-phosphate beta-D-mannosyltransferase ","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[4-173]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[5-123]T$	no description
PTHR10859	$\"[9-235]T$	GLYCOSYLTRANSFERASE RELATED

","BeTs to 21 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","No significant hits to the Blocks database.","Residues 5-47 are similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL FAMILY TRANSFERASE MANNOSYLTRANSFERASE DOLICHOL-PHOSPHATE TRANSMEMBRANE 2.4.1.- NODULATION) protein domain (PD395383) which is seen in Q8FTG3_COREF.Residues 8-47 are 77% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL FAMILY TRANSFERASE GROUP DOLICHYL-PHOSPHATE BIOSYNTHESIS LIPOPOLYSACCHARIDE 2.4.-.-) protein domain (PD915724) which is seen in Q6AHD9_BBBBB.Residues 9-93 are 59% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL FAMILY TRANSFERASE GROUP SYNTHASE BIOSYNTHESIS 2.4.1.- 2.-.-.-) protein domain (PD000196) which is seen in Q8TX01_METKA.Residues 38-142 are 54% similar to a (DOLICHOL SYNTHASE MANNOSE POSSIBLE MONOPHOSPHATE) protein domain (PD970252) which is seen in Q82U54_NITEU.Residues 62-217 are 45% similar to a (INVOLVED BIOGENESIS TRANSFERASE WALL GLYCOSYLTRANSFERASE CELL) protein domain (PD631606) which is seen in Q8TXU5_METKA.Residues 67-121 are 70% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE MANNOSYLTRANSFERASE DOLICHOL-PHOSPHATE SYNTHASE GLYCOSYL MANNOSE PHOSPHATE DOLICHYL-PHOSPHATE DOLICHOL) protein domain (PD822729) which is seen in Q827K1_STRAW.Residues 145-231 are similar to a (TRANSFERASE SYNTHASE GLYCOSYLTRANSFERASE MANNOSYLTRANSFERASE DOLICHOL-PHOSPHATE MANNOSE GLYCOSYL PHOSPHATE DOLICHYL-PHOSPHATE DOLICHOL) protein domain (PD331550) which is seen in Q83H81_TROW8.","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 173 (E_value = 1.1e-27) place ANA_0762 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","involved in cell wall biogenesis (Ppm1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0763","804296","802617","1680","10.26","18.57","59093","ATGCTTCACCGCGTGACAGTGCCCTCTCGGTTGCCCTCCCGGATGCTCTCTCGTTCCCCCGGCTGGCTTCGTCGATCAGCCCCGGCGGTGGTGGCGCTGCTGGCGGGTCTGGCCACCTACGCCGCCTTCCCCCCGGTGAACCTGTGGTGGTCGGCCCTCATCGGGGTCGGGGTCTTCATGCTCCTCATTCGGGGACGTCGCTTCTGGGCGGGCACCGGTCTGGGACTGCTCTACGGCTTCGGCCTGTTCACTCCTCTGCTGCACTTCACGATGGTGGGCATGGGCAACCCGATCGGCTGGATCGCGCTGACGCTCTTCGAGTCCCTCTACCTGGCCGCACTCGGCGGGGCCTGGTCCCTGGTGAGCCGTCTCCCGCTGCTGCAGGGAGCCGCCCGACGAGGGCGGCTCGCGCGGCGTGTGCCGGCCGGCGCGGCAGACGTGCTCTTCTTCGCCCTGCTGTGGTCCGGGATGGAGGAGCTACGCTCGGTGTGGCCGCTGGGCGGTTTCCCCTTCGGACGCCTGGCCTTCGCCATGGCGGACGCCCCTGTCCTGCCGGCGGCGGCCTATGTCGGCAGCGCCGGGGTGGGGCTGCTGGTGGCACTGGCGGCCGCATGCCTCGCCCATGCAGCTCGCTCCATCTATGAGCGCCGCGCGATGCCGGTCCTCGCCTGCGCAGCAATCGCGGCGGCTGTGCTCGTTGCGCCGCGGACACTGCCCCTGGAGACACGCGCTGAGAACGGTACCGTCCGGGTCGGAGCCGTCCAGGGCAATGTGGCCACCGACTTCGAGGACGCCTTCAACCGGGCCCTGGAGGTGACCGGCAACCACGCCAAGGCGACCAAGCAGCTGGCCGCCGACGTGGGCCCCGGCAGCCTCGACATGGTCATCTGGCCTGAGAACTCTGCGGACCTGGACCCTCGCGACTACCCGGCCTCGGCAACCATTGTCGATGAGGCCGCCCAGGCGGTCCAGGCGCCGGTGCTCGTGGGCGCGGTTCCTGTTGTCGGCGACATCCGCTACAACGATGTCCTCATCTGGAATCCCGGAGACGTCTCGGGCAAGACGGCTCATCCTTACTACCGCAAGCACCGGCCTGTGCCCTTCGCGGAGTACATCCCCTCCCGTTCTCTGGTACGGCGCCTGACCACCCAGGTCGACCGGGTCGGCATCGACATGCTGCCCGGCACCGGCCCCAGCACACTGACGGTTCCGGCCGTCACCCAGGGCCGGGACGTCACCTTCGCCATGGGCATCTGTTTCGAGGTCGCCTACGACGACGCCCTGCGTACCGGTATCAAACAGGGAGGGCAGGCGATCATCATCCCGACGAACAACGCCTCCTTCCTCGACTCCGGCGAGGCGGCCCAGCAGCTCGCCCAGGGCCGTGTCCAGGCGGTGGTCCACGGCCGCAGCGTCATCCAGGCCTCCACCGTCGGCTACACCGCGATCATCAACCCCCGCGGTGAGGTCGAGCAGGTCACCCGGCCCTACACCCAGGCGAGCCTCGTGGCCGACGTTCCGCTGCGCAGCTCGCAAACCGTCGCCGACCGGCTCGGTGCCGCCCCCGGCATCATCCTGCTCGCCGGTGCAGGCCTACTGGTGGGAGCCGGTATCCTGAGCCGGCTGCGCTCAGGGCGGAAGGCAGTGGCTGCGGCCGGGGATCGCCGGCGCCGCCGCTGA","MLHRVTVPSRLPSRMLSRSPGWLRRSAPAVVALLAGLATYAAFPPVNLWWSALIGVGVFMLLIRGRRFWAGTGLGLLYGFGLFTPLLHFTMVGMGNPIGWIALTLFESLYLAALGGAWSLVSRLPLLQGAARRGRLARRVPAGAADVLFFALLWSGMEELRSVWPLGGFPFGRLAFAMADAPVLPAAAYVGSAGVGLLVALAAACLAHAARSIYERRAMPVLACAAIAAAVLVAPRTLPLETRAENGTVRVGAVQGNVATDFEDAFNRALEVTGNHAKATKQLAADVGPGSLDMVIWPENSADLDPRDYPASATIVDEAAQAVQAPVLVGAVPVVGDIRYNDVLIWNPGDVSGKTAHPYYRKHRPVPFAEYIPSRSLVRRLTTQVDRVGIDMLPGTGPSTLTVPAVTQGRDVTFAMGICFEVAYDDALRTGIKQGGQAIIIPTNNASFLDSGEAAQQLAQGRVQAVVHGRSVIQASTVGYTAIINPRGEVEQVTRPYTQASLVADVPLRSSQTVADRLGAAPGIILLAGAGLLVGAGILSRLRSGRKAVAAAGDRRRRR$","Apolipoprotein N-acyltransferase","Membrane, Cytoplasm, Extracellular","apolipoprotein n-acyltransferaseLnt/dolichol-phosphate-mannosyl transferase Dpm1","apolipoprotein N-acyltransferase ","apolipoprotein N-acyltransferase","","Bork P., Koonin E.V. A new family of carbon-nitrogen hydrolases. Protein Sci. 1994. 3(8):1344-1346. PMID: 7987228","","","

InterPro
IPR003010
Domain

Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase
G3DSA:3.60.110.10	$\"[249-523]T$	no description
PF00795	$\"[250-444]T$	CN_hydrolase
PS50263	$\"[249-551]T$	CN_HYDROLASE

InterPro
IPR004563
Domain

Apolipoprotein N-acyltransferase
TIGR00546	$\"[78-490]T$	lnt: apolipoprotein N-acyltransferase

noIPR
unintegrated

unintegrated
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[21-40]?$ $\"[46-64]?$ $\"[74-92]?$ $\"[98-118]?$ $\"[139-157]?$ $\"[186-206]?$ $\"[218-238]?$ $\"[519-539]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 247-318 are 56% similar to a (TRANSFERASE N-ACYLTRANSFERASE ACYLTRANSFERASE APOLIPOPROTEIN LIPOPROTEIN 2.3.1.- MEMBRANE ALP TRANSMEMBRANE INNER) protein domain (PD716586) which is seen in Q84F25_STRVF.Residues 341-490 are 45% similar to a (HYDROLASE NITRILASE CARBON-NITROGEN AMIDOHYDROLASE FAMILY NAD SYNTHETASE LIGASE ATP-BINDING HYDROLASE) protein domain (PD052217) which is seen in Q72LE9_THET2.Residues 367-448 are 51% similar to a (TRANSFERASE SYNTHASE ACYLTRANSFERASE PPM1 LIPOPROTEIN POLYPRENOL-MONOPHOSPHOMANNOSE APOLIPOPROTEIN DPM1 2.3.1.- N-ACYLTRANSFERASE) protein domain (PDA1D9P1) which is seen in Q9F409_MYCSM.","","No significant hits to the PDB database (E-value < E-10).","Residues 250 to 444 (E_value = 0.00013) place ANA_0763 in the CN_hydrolase family which is described as Carbon-nitrogen hydrolase.","","n-acyltransferase Lnt-dolichol-phosphate-mannosyl transferase Dpm1 (CutE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0764","805230","804313","918","6.86","-0.70","32114","ATGTCAGGCTTCTTCGCCCTCCTTGACGACATCGCCACGCTCGCCAAGCTGACGCTGTCCACTGTTGACGACACGGCCTCCATGGCTGTCAAGACCTCGGCGAAGGTCTCGGCGGCCGCCGTCGACGACGTCGCCACCACCCCCCAGTACGTCACCGGCATCACCCCGGACCGGGAGTTGCCGATCATCAAGAAGATCACGCTGGGCTCGCTGCGCAACAAGCTCCTCATCATCCTGCCGATCGGCCTGCTGCTGACGGCCGTGGCGCCATGGCTCCTGCCGGTGGCGCTCGTCATCGGTGGCGCCTACCTGTGCTTCGAGGGCGGGGAGAAGATCCTGGAGCGCTTCGGCGGCGCTGCTCACGCCGAGGAGGAGTCTGGTCCAATCGACGAGGCCCAGATCATCCGTCAGGCCATCACCACGGACTTCGTCCTATCCACCGAGATCATGCTGCTGGCCCTGGCCGAGGTGGAGGGGGAGTCCTCCATGCGGCGCATCATCGTGCTGGTCCTCATCGCCCTGCTCATCACCTTCGCCGTCTACGGCCTGGTGGCGGCCCTCATCAAGCTCGACGACGCCGGCGCGCACCTGGCCGGACAGGGCCGCACCGGCGCCATCCGCTCGCTTGGCCGCGCGATCGTGACGTCTGCGCCGGCCCTCTTCCGCGGCATCGGGATCGTCGGGACCGTGGCGATGCTGTGGGTGGGCGGCCACATCCTGGCGGCCAACCTCGCCAAGGTCGGTTTCCACCCGCTGCACCACGCCATCGAGTGGGCCGAGGAACTCACCCACAACCCAGTCCTGTCCTGGATCACCGGAACAGCCATGTCCTGCCTCATCGGAGCCGTCATCGGCACCCTGCTGGCCCTGGCCTGGCGGCCCGTGCATCACGCTCTGGCCCGCCGTCACAAAGGTTAA","MSGFFALLDDIATLAKLTLSTVDDTASMAVKTSAKVSAAAVDDVATTPQYVTGITPDRELPIIKKITLGSLRNKLLIILPIGLLLTAVAPWLLPVALVIGGAYLCFEGGEKILERFGGAAHAEEESGPIDEAQIIRQAITTDFVLSTEIMLLALAEVEGESSMRRIIVLVLIALLITFAVYGLVAALIKLDDAGAHLAGQGRTGAIRSLGRAIVTSAPALFRGIGIVGTVAMLWVGGHILAANLAKVGFHPLHHAIEWAEELTHNPVLSWITGTAMSCLIGAVIGTLLALAWRPVHHALARRHKG$","Protein of unknown function DUF808","Membrane, Cytoplasm","Uncharacterized BCR","protein of unknown function DUF808","protein of unknown function DUF808","","","","","

InterPro
IPR008526
Family

Protein of unknown function DUF808
PF05661	$\"[1-295]T$	DUF808

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[75-95]?$ $\"[166-188]?$ $\"[220-242]?$ $\"[270-292]?$	transmembrane_regions

","BeTs to 6 clades of COG2354COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2354 is ---------dr---efg--n-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 2-123 are similar to a (MEMBRANE YEDI METHYL-INDEPENDENT UNCHARACTERIZED PROBABLE PROTEIN INTEGRAL REPAIR MISMATCH VPA0406) protein domain (PD040316) which is seen in Q9A8B8_CAUCR.Residues 188-283 are 52% similar to a (MEMBRANE YEDI METHYL-INDEPENDENT UNCHARACTERIZED PROBABLE PROTEIN INTEGRAL REPAIR MISMATCH VPA0406) protein domain (PD188084) which is seen in Q8NRG1_CORGL.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 295 (E_value = 2.2e-111) place ANA_0764 in the DUF808 family which is described as Protein of unknown function (DUF808).","","BCR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0765","809332","806381","2952","8.94","17.36","107217","ATGAGCTCACCAGCCGAGCGCTATGCCGCATCTCGACGTCGACAGGCCGCCTCCAACAGTGAGCTCGCCCGCTTCGCCCAGGGCTACGACTTCCCCCTCGACCCCTTCCAGGAGGAGGCCTGCGGAGCCGTCGAGAGGGGAGAGGGTGTCCTGGTCGCCGCCCCGACAGGCGCCGGCAAGACAGTGGTGGGGGAGTTCGCCGTGTACCTGGGCCTGGTCCGGGGGCTCAAGACCTTCTACACCGCCCCCATCAAGGCGCTGAGCAACCAGAAGTACCTGGACCTCGTGGCCCGGCACGGTCAGGAACGGGTGGGGCTGCTGACCGGTGACACCTCCGTCAACCCCCACGCGGACGTGGTGGTCATGACCACCGAGGTGCTGCGCAACATGCTCTACTCGGGCTCGCGTGACCTGGACCGGCTGGGCTTCGTGGTCATGGACGAGGTCCACTACCTGGCCGACCGCTTCCGCGGGCCGGTGTGGGAGGAGGTCATCATCCACCTGCCCGCCGAGGTCCAGGTGATCTCCCTGTCTGCCACGGTCTCCAACGCCGAGGAATTCGGCGACTGGCTCGGCCAGGTGCGCGGCAGGACCGCCGTCGTCGTCTCCGAGGAACGCCCCGTCCCACTGACTCAGCACATGATGGTCGGACGCCGGCTGCTGCCGCTGTACTCCCACCCCGCAGAGATACCTGAGCAGTCCGAGCAGACCGAGCAGACCGAGCTGGAGCGGCAGCCGTTGCAGACGGGGCAGCCCCCGCTCAACCCCGAACTGCTTAAGGCCGTCAAGCAGGCCAGGCGTGCCGCCGCCTCCGGTGGCGCCTCCAAGAACAGCTACCGTGGCCGCGGTGGCGGTTCGGCCAGGGGACCGCAGCCCTGGAAGCGCTCCGCCCGAGGGGGACGGGCGCCTCGCCGTGGCGAGGGGGGAGCCCGCACGGCAAGGTTGAAGCCGCCCTCACGACTGCAGGTCGTCACGGCCCTGGAGGGGGCGCGCCTGCTGCCCGCGATCGTCTTCGTCTTCTCTCGGGCGGGCTGTGAGCAGGCCGTCCACCAGGTGGTCAGCGCCGGGGTGGACCTGACCACCGAGGCCGAGGCGGCCCGAATCCGGGAGGTCATCGAGCGGCGCACGGCTGACATCCCCGCCGGCGACCTGGGGGTCCTCGGCTTCCACTTCTGGGCCCACGCCCTGGAGCGCGGCGTCGCGGCCCACCACGCGGGACTGCTGCCGGTGTTCAAGGAGACGGTGGAGGAGCTCTTCAGCGCGGGCCTGGTCAAGGTCGTCTACGCCACCGAGACCCTGGCACTGGGCATCAACATGCCCGCCCGCACCGTGGTCCTGGAGTCGCTGCGCAAGTGGAACGGCTCGGCCCACGTCACCCTCAGCCCGGGGGAGTACACCCAGCTGACGGGGCGGGCCGGGCGCCGCGGCATCGACGTGGAGGGCCACGCCGTCGTGCTGGCGGCTGACGACGTCGAGCCGGCCACGGTCTCCTCACTGGCCTCCCGGCGCACCTACCCGCTGGTCTCCGCTTTCCGTCCGACCTACAACATGGCCGTCAACCTGCTTGAGCGCATGCCGCGGATGCGGGTGCGCGAGGTGCTCGAGCAGTCCTTCGCCCAGTTCCAGGCCGACCGCGGGGTCGTGGAGCTGGCCGCTCAGGCTCGCCGCAAGCGCCGCAGCCTGGAGGGCCTGGAGAAGGACATGACGTGCCGTCTGGGCGACTTCCGCGAGTACGCCTCCCTGCGCCAGGCCATTGCCGACGCCGAGGCGGACCTGTCGCGGGACAAGTCCGCGGCGCGCCGCAGCGAGACGGGACGGACCATGAGCTCACTGGGACGCGGTGACGTCATCGTCTTCCGCAAGGGGCGACGCCGCCGCCACGGCATCGTCCTTCAAGTCGGTGCCGACCGGACCGGGACCCCCACCATCACGGTGCTGGGGGAGGATGCGCGAGTCGTCTCCCTGACCCCGGACACGGCACCGGACGGGGTCATGCGCGTGGGCGCGCTGCGGGTGGCGGACTCGGTGGACCCGCACCGGCCCCGGGACCGGGACCGGCTCGTTCAGCGTCTGGTCGACGCACTGCGTGCCGGGGACCTGGAAGGGAGCGGTAAGCGCACGCGCACCCGCTCCAGCCGCGCCCAGGCCCGCCGAGACAGCGCGATCGAGAACCTCGAGCGACTGCGCCACGAGATGCGCTCCCACCCCTGCCATGGCTGCCCCGACCGGGAGGAACACGCCCGGGTGGGCCGCAAGTGGTCCAGGGCCAAGGCCGAGGCCGAGCGCCTCCAGCGGCGCATCGAGACCCGCACCGGCACCATCGCCCGCCTCTTCGACGCCGTCTGCGAGGTCCTGCTCGAACTGGGCTATCTGCACCCTGTGGACCGGGGCCACCCGGAGCGCGAGCTGCGGGTCACCGGTGCCGGCAAGGTCCTGGCCCGGATCTACGCCGAACGGGACCTGCTCATCGCCGAGTGCCTGCGCACGGGAGTCTTCGAGGACCTCAGCGCCGCGGAGCTGGCCGGGGCACTGAGCGCCTGCGTCTACGAGCCCCGACTGAGCGCACAGTCGATCGGGCTGCCCGTGGCGCCCGGCTCCAGGCTCGGCCAGTGCCTGCGCGCACAGCTGGGGGTCTCACACCGAATCCACGACCTGGAGTCCCTGGCCCGCATCGAGGCCTCCTCGGGCGCGGAGCCGGCACTGGCAGGGGCCGTCCAGGCCTGGTGCGACGGCGCGCAGCTGGCGGACATCCTGGACGCCACGGAGCTGACGGCCGGGGACTTCGTGCGCTGGTGCAAGCAGCTGCTCGACGTCGTCGGGCAGATCGCGAGCCTCTCACCGCCACCGGATGCCATCCCCGAGCAGGCCAGGGCGGTCACCGACCTGTCGATGCGCGCCGCCGAGGCCTCCCTGGATCTCAATAGGGGAGTGGTGAGCTGGTCGGCGGTGTAG","MSSPAERYAASRRRQAASNSELARFAQGYDFPLDPFQEEACGAVERGEGVLVAAPTGAGKTVVGEFAVYLGLVRGLKTFYTAPIKALSNQKYLDLVARHGQERVGLLTGDTSVNPHADVVVMTTEVLRNMLYSGSRDLDRLGFVVMDEVHYLADRFRGPVWEEVIIHLPAEVQVISLSATVSNAEEFGDWLGQVRGRTAVVVSEERPVPLTQHMMVGRRLLPLYSHPAEIPEQSEQTEQTELERQPLQTGQPPLNPELLKAVKQARRAAASGGASKNSYRGRGGGSARGPQPWKRSARGGRAPRRGEGGARTARLKPPSRLQVVTALEGARLLPAIVFVFSRAGCEQAVHQVVSAGVDLTTEAEAARIREVIERRTADIPAGDLGVLGFHFWAHALERGVAAHHAGLLPVFKETVEELFSAGLVKVVYATETLALGINMPARTVVLESLRKWNGSAHVTLSPGEYTQLTGRAGRRGIDVEGHAVVLAADDVEPATVSSLASRRTYPLVSAFRPTYNMAVNLLERMPRMRVREVLEQSFAQFQADRGVVELAAQARRKRRSLEGLEKDMTCRLGDFREYASLRQAIADAEADLSRDKSAARRSETGRTMSSLGRGDVIVFRKGRRRRHGIVLQVGADRTGTPTITVLGEDARVVSLTPDTAPDGVMRVGALRVADSVDPHRPRDRDRLVQRLVDALRAGDLEGSGKRTRTRSSRAQARRDSAIENLERLRHEMRSHPCHGCPDREEHARVGRKWSRAKAEAERLQRRIETRTGTIARLFDAVCEVLLELGYLHPVDRGHPERELRVTGAGKVLARIYAERDLLIAECLRTGVFEDLSAAELAGALSACVYEPRLSAQSIGLPVAPGSRLGQCLRAQLGVSHRIHDLESLARIEASSGAEPALAGAVQAWCDGAQLADILDATELTAGDFVRWCKQLLDVVGQIASLSPPPDAIPEQARAVTDLSMRAAEASLDLNRGVVSWSAV$","ATP-dependent RNA helicase","Cytoplasm","Superfamily II DNA and RNA helicases","probable ATP-dependent DNA helicase HelY ","DEAD/DEAH box helicase domain protein","","Staub E., Fiziev P., Rosenthal A., Hinzmann B. Insights into the evolution of the nucleolus by an analysis of its protein domain repertoire. Bioessays 2004. 26(5):567-581. PMID: 15112237","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[392-476]T$	Helicase_C
SM00490	$\"[390-476]T$	HELICc
PS51194	$\"[344-523]T$	HELICASE_CTER

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[34-187]T$	DEAD

InterPro
IPR012961
Domain

DSH, C-terminal
PF08148	$\"[781-979]T$	DSHCT

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[29-213]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[41-199]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[33-183]T$	no description
PTHR11752	$\"[30-261]T$ $\"[315-942]T$	HELICASE SKI2W
PTHR11752:SF2	$\"[30-261]T$ $\"[315-942]T$	HELICASE SKI2W

","BeTs to 8 clades of COG0513COG name: Superfamily II DNA and RNA helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: K [Information storage and processing--Transcription],JThe phylogenetic pattern of COG0513 is a-mp--yq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 4","***** IPB012961 (DSH, C-terminal) with a combined E-value of 3.7e-152. IPB012961A 49-95 IPB012961B 127-181 IPB012961C 200-214 IPB012961D 334-349 IPB012961E 398-439 IPB012961F 463-478 IPB012961G 502-523 IPB012961H 901-942***** IPB013701 (DEAD/H associated) with a combined E-value of 5.3e-19. IPB013701A 24-67 IPB013701D 131-158 IPB013701E 174-191 IPB013701H 418-451***** IPB004179 (Sec63 domain) with a combined E-value of 1.2e-18. IPB004179A 32-72 IPB004179C 141-166 IPB004179E 424-453 IPB004179F 464-481","Residues 44-191 are 44% similar to a (HELICASE DEAH HYDROLASE ATP-DEPENDENT ATP-BINDING) protein domain (PDA0E4K6) which is seen in Q46545_BACNO.Residues 55-123 are 82% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT FACTOR DNA BOX RNA-BINDING 3.6.1.-) protein domain (PD410733) which is seen in Q8NQE6_CORGL.Residues 125-216 are 55% similar to a (HELICASE HYDROLASE ATP-BINDING RNA DNA II SUPERFAMILY DEAD OR BOX-LIKE) protein domain (PD285135) which is seen in Q82MT6_STRAW.Residues 125-223 are 47% similar to a (HELICASE F20P5.20 HYDROLASE ATP-BINDING) protein domain (PD100113) which is seen in O04538_ARATH.Residues 126-181 are 76% similar to a (HELICASE ATP-BINDING HYDROLASE ATP-DEPENDENT 3.6.1.- RNA DNA NUCLEAR PROBABLE CEREVISIAE) protein domain (PD001310) which is seen in Q6NHA1_CORDI.Residues 182-262 are 55% similar to a (HELICASE HYDROLASE ATP-BINDING RNA PROBABLE HELY 3.6.1.- DNA ATP-DEPENDENT II) protein domain (PD484663) which is seen in HELY_MYCLE.Residues 318-419 are 70% similar to a (HELICASE ATP-BINDING HYDROLASE RNA 3.6.1.- CEREVISIAE DNA ATP-DEPENDENT SKI2 STRAIN) protein domain (PD100066) which is seen in Q9RJ70_STRCO.Residues 428-493 are 87% similar to a (HELICASE ATP-BINDING HYDROLASE RNA 3.6.1.- ATP-DEPENDENT NUCLEAR DNA CEREVISIAE PROBABLE) protein domain (PD007814) which is seen in Q7TZ20_MYCBO.Residues 493-582 are 65% similar to a (HELICASE PROBABLE HYDROLASE ATP-BINDING) protein domain (PD997781) which is seen in Q8G6A5_BIFLO.Residues 496-548 are 75% similar to a (HELICASE ATP-BINDING HYDROLASE RNA CEREVISIAE 3.6.1.- ATP-DEPENDENT SKI2 STRAIN DNA) protein domain (PD538560) which is seen in Q7TZ20_MYCBO.Residues 550-617 are 61% similar to a (HELICASE HYDROLASE ATP-BINDING RNA ATP-DEPENDENT) protein domain (PD035628) which is seen in Q828H4_STRAW.Residues 722-978 are 43% similar to a (HELICASE ATP-BINDING HYDROLASE RNA CEREVISIAE SKI2 STRAIN 3.6.1.- SACCHAROMYCES SKI2W) protein domain (PD005482) which is seen in Q6MZZ8_HUMAN.Residues 725-966 are 44% similar to a (HELICASE HYDROLASE ATP-BINDING DNA F20P5.20 RNA ANTIVIRAL ALR0489 TLR0350 II) protein domain (PD217280) which is seen in Q7U8I2_SYNPX.Residues 725-852 are 63% similar to a (HELICASE HYDROLASE ATP-BINDING RNA PROBABLE HELY 3.6.1.- DNA ATP-DEPENDENT II) protein domain (PD719609) which is seen in Q6AFV9_BBBBB.Residues 881-969 are 54% similar to a (HELICASE HYDROLASE ATP-BINDING RNA 3.6.1.- PROBABLE DNA ATP-DEPENDENT HELY II) protein domain (PDA005E0) which is seen in Q9RJ70_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 34 to 187 (E_value = 1.6e-35) place ANA_0765 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 392 to 476 (E_value = 7.2e-09) place ANA_0765 in the Helicase_C family which is described as Helicase conserved C-terminal domain.Residues 781 to 979 (E_value = 2.8e-20) place ANA_0765 in the DSHCT family which is described as DSHCT (NUC185) domain.","","II DNA and RNA helicases (SKI2W)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0766","810325","809354","972","6.76","-1.36","34153","ATGCGTATCGCTCTGCTGTCCAACCCCTCTTCGGGACGAGGACGTCATGCGGCCGCCGATGACGTCGCCCGCCGGATCCTCACCGAGGCCGGCCACGAGGTCCTTCACGTCCGTGGCAGCTCCTACGAGCAGGCGCGTGACGCAGGACGGGCCCTCCTGGGGGATGAACCGCACCATAACGTTGAGGCATTGGTGGTCGTCGGCGGGGACGGTATGGTCCACCTGGGGGTGGACATCGTCGCCACGACGGGCGTGCCCCTGGGCATCGTGGCCACCGGCACCGGTAACGACATCGCCAGGCACTTCGGTCTGCCCAGCCGGGACGCGGAGGCCTCCGCCCGCCTCATCAACCAGGCGCTGTCCGGGAAGGGCGCCATCACGGCGGTGGACGCGATCTATGCCTCCCGCCCCGATGGAACCCTGCTGGCCCCGCAGCGGCGCTGGTCCCTGGCCGTGGTCAGCGCCGGAGTGGACGCAGCCGTCAACGCCCGCGCCAACACCCTCTCCTGGCCGGCCGGCGAGGGACGTTACGTGCGCGCCTTCACCGCCGAGCTCGCGACGCTGGCGCCTTACGGCTACCGGGTCACCACCGACGAGGGCACCTGGGAGGGGCCGGCGCTCCTGCTGGCGGTGGCCAACACCCGTTACGTCGGCGGAGGCATGGACCTGGCGCCCCAGGCCGACCCCACTGACGGCCTGCTGGAGGTGCTGCGCCTGGATCCCGTGGGCCGCACCCACCTGCTCGCCCTCTTCCGCCGGCTCTTCCGCGGCACGCACCTGACCGACCCGGCCGTCCACGTGGAGCGCAGCCGCACCGTCACCATTGAGTCGCTCACTGAGCGAACCGGCCGTGATCGGGGCCTGCGCCCGCCTCCTCACCCCTTCGCCGACGGCGAGCCGCTGGCCGAGCTGCCCCTGCGCCTTGAGGCCGTCCCCGACGCCGTCCGGCTGCTCCTACCAGCTCCGGGCTGA","MRIALLSNPSSGRGRHAAADDVARRILTEAGHEVLHVRGSSYEQARDAGRALLGDEPHHNVEALVVVGGDGMVHLGVDIVATTGVPLGIVATGTGNDIARHFGLPSRDAEASARLINQALSGKGAITAVDAIYASRPDGTLLAPQRRWSLAVVSAGVDAAVNARANTLSWPAGEGRYVRAFTAELATLAPYGYRVTTDEGTWEGPALLLAVANTRYVGGGMDLAPQADPTDGLLEVLRLDPVGRTHLLALFRRLFRGTHLTDPAVHVERSRTVTIESLTERTGRDRGLRPPPHPFADGEPLAELPLRLEAVPDAVRLLLPAPG$","Kinase related to diacylglycerol kinase","Cytoplasm","conserved hypothetical protein","hypothetical protein","diacylglycerol kinase, catalytic region","","Kanoh H., Yamada K., Sakane F. Diacylglycerol kinases: emerging downstream regulators in cell signaling systems. J. Biochem. 2002. 131(5):629-633. PMID: 11983067","","","

InterPro
IPR001206
Domain

Diacylglycerol kinase, catalytic region
PD005043	$\"[3-112]T$	Q8G6X8_BIFLO_Q8G6X8;
PF00781	$\"[2-137]T$	DAGK_cat

noIPR
unintegrated

unintegrated
PTHR12358	$\"[1-279]T$	SPHINGOSINE KINASE
PTHR12358:SF4	$\"[1-279]T$	BMRU PROTEIN

","BeTs to 8 clades of COG1597COG name: Predicted kinase related to diacylglycerol kinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1597 is ---p--y-vdrlbcef-----j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 3-112 are 58% similar to a (KINASE DIACYLGLYCEROL REPEAT TRANSFERASE KINASE DIGLYCERIDE DAG PHORBOL-ESTER BINDING SPHINGOSINE) protein domain (PD005043) which is seen in Q8G6X8_BIFLO.Residues 136-260 are 54% similar to a (KINASE DIACYLGLYCEROL BMRU DOMAIN CATALYTIC REGULATOR MULTIDRUG RESISTANCE TRANSCRIPTIONAL PROTEIN) protein domain (PD604008) which is seen in Q828H5_STRAW.Residues 176-323 are 44% similar to a (DR2234) protein domain (PD276118) which is seen in Q9RS93_DEIRA.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 137 (E_value = 5.7e-15) place ANA_0766 in the DAGK_cat family which is described as Diacylglycerol kinase catalytic domain (presumed).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0767","811196","810375","822","9.44","6.87","30415","GTGCCCAAGCTCCCTCAGATCAAGCGATCGAGGCGCAAGGACAACCCCGAGGCGCGCATGTCCATCGGGGACCACCTGCGCGAGCTGCGCCAGCGTCTCTTCGTCTCCGCCGCGGGCGTCATGGTGATGACGGTTGTCGGTTACCTGGTCTACGAGCGGGCCTTCGCCCTCATCACCCGCCCCATCGAGCAGGCCAATGCCAAGGGCGCGCACCTCACCCTGAACTTCGACACGATCCTGGCCTCCTTCGATATGAAGCTCGAGGTGTCGATCTGGCTGGGAGTTCTGCTGTCCTCACCGTTGTGGATGTACGAGTTCTGGGCCTTCGTGGGACCGGGGATGACCCGCAAGGAGAAGGCATACACCTGGGCCTACGGCACGGCTGGCCTGTTCCTCTTCCTCGCCGGCGCCGGCCTGGGAATCTGGGTCATGCCGCACGCGGTCTCCATCCTCACCAGCTTCATCCCTGACGGCCCCACTGCCGGAGTGATCGGGGCGAATCTCTACCTGTCCTTCGTCATGAGGCTGGTCCTCGTCTTCGGGATCGCCTTCCTCCTGCCCGAGCTCCTCGTCGCCCTCAACATGCTCGGGCTCATGCAGGGAAAGACCATGCTCAAGGGCTGGCGCTGGGCCATCATGGGCATCGTCACCTTTATGGCCATTGCCAACCCGCTGCCGGATCCCTGGTCGATGGTCTTCATGTCCGTTCCCATTGCCGGCCTGTACTTCCTGGCCTGCTTCATCTCCATCAGGCATGACAAACGGGTGGAGAAGAAGCGCGCTGAGCTCGACGCCGAGCTCGAGGCCGCCCTGGCCGAGTAG","VPKLPQIKRSRRKDNPEARMSIGDHLRELRQRLFVSAAGVMVMTVVGYLVYERAFALITRPIEQANAKGAHLTLNFDTILASFDMKLEVSIWLGVLLSSPLWMYEFWAFVGPGMTRKEKAYTWAYGTAGLFLFLAGAGLGIWVMPHAVSILTSFIPDGPTAGVIGANLYLSFVMRLVLVFGIAFLLPELLVALNMLGLMQGKTMLKGWRWAIMGIVTFMAIANPLPDPWSMVFMSVPIAGLYFLACFISIRHDKRVEKKRAELDAELEAALAE$","Sec-independent protein secretion pathway component TatC","Membrane, Cytoplasm","twin arginine translocation complex component","K03118 sec-independent protein translocase protein TatC","Sec-independent protein translocase, TatC subunit","","Weiner J.H., Bilous P.T., Shaw G.M., Lubitz S.P., Frost L., Thomas G.H., Cole J.A., Turner R.J. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 1998. 93(1):93-101. PMID: 9546395Sargent F., Bogsch E.G., Stanley N.R., Wexler M., Robinson C., Berks B.C., Palmer T. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 1998. 17(13):3640-3650. PMID: 9649434","","","

InterPro
IPR002033
Family

Sec-independent periplasmic protein translocase
PR01840	$\"[21-48]T$ $\"[100-118]T$ $\"[118-144]T$ $\"[169-197]T$	TATCFAMILY
PF00902	$\"[31-237]T$	TatC
TIGR00945	$\"[22-242]T$	tatC: twin arginine-targeting protein trans

noIPR
unintegrated

unintegrated
tmhmm	$\"[33-51]?$ $\"[90-110]?$ $\"[125-145]?$ $\"[151-171]?$ $\"[176-198]?$ $\"[228-250]?$	transmembrane_regions

","BeTs to 18 clades of COG0805COG name: Sec-independent protein secretion pathway component TatCFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0805 is ao-p-z-q-dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB002033 (Sec-independent periplasmic protein translocase) with a combined E-value of 8.6e-42. IPB002033A 22-34 IPB002033B 96-146 IPB002033C 169-211 IPB002033D 217-246","Residues 79-157 are similar to a (SEC-INDEPENDENT TRANSLOCASE TATC TRANSMEMBRANE MITOCHONDRION COMPONENT TRANSLOCATION SECRETION MEMBRANE TRANSPORTER) protein domain (PD003525) which is seen in Q6AFW0_BBBBB.Residues 170-255 are similar to a (SEC-INDEPENDENT TRANSLOCASE TATC TRANSMEMBRANE COMPONENT MITOCHONDRION TRANSLOCATION SECRETION MEMBRANE FAMILY) protein domain (PD153713) which is seen in Q9RJ69_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 31 to 237 (E_value = 6.2e-37) place ANA_0767 in the TatC family which is described as Sec-independent protein translocase protein (TatC).","","arginine translocation complex component (519)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0769","811502","811242","261","8.40","1.16","9642","GTGAACCTCTTTAAGCCGTCGCACATCATCTTCCTGCTCATCGTCGTCATCCTGCTGTTCGGCTACAAGAAGCTGCCTGACATCGCCCGCAGCGTGGGCCAGTCCATGAAGGTCTTCAAGAAGGAGGTCAAGGAGCTGCGCGACGACGACTCCAAGGACTCCCAGGCTCAGATTCAGCAGCCGCAGGAGGGCACTTACTACACCGAGCCCACCCAGTCCGGCCAGACCGCTCAGAGCGCCGAGGGCTCATCCCAGAAGTGA","VNLFKPSHIIFLLIVVILLFGYKKLPDIARSVGQSMKVFKKEVKELRDDDSKDSQAQIQQPQEGTYYTEPTQSGQTAQSAEGSSQK$","Twin-arginine translocation protein, TatA/E family subunit","Periplasm, Membrane","Sec-independent protein translocase proteintatA/E homolog","hypothetical protein predicted by Glimmer/Critica","twin-arginine translocation protein, TatA/E family subunit","","Settles A.M., Yonetani A., Baron A., Bush D.R., Cline K., Martienssen R. Sec-independent protein translocation by the maize Hcf106 protein. Science 1997. 278(5342):1467-1470. PMID: 9367960Weiner J.H., Bilous P.T., Shaw G.M., Lubitz S.P., Frost L., Thomas G.H., Cole J.A., Turner R.J. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 1998. 93(1):93-101. PMID: 9546395","","","

InterPro
IPR003369
Family

Bacterial sec-independent translocation protein mttA/Hcf106
PF02416	$\"[6-56]T$	MttA_Hcf106

InterPro
IPR006312
Family

Twin-arginine translocation protein TatA/E
TIGR01411	$\"[2-49]T$	tatAE: twin arginine-targeting protein tran

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[4-22]?$	transmembrane_regions

","BeTs to 14 clades of COG1826COG name: Sec-independent protein secretion pathway componentsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1826 is ao-p-z-q-dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003369 (Bacterial sec-independent translocation protein mttA/Hcf106) with a combined E-value of 2.1e-14. IPB003369 4-41","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 56 (E_value = 2.9e-13) place ANA_0769 in the MttA_Hcf106 family which is described as mttA/Hcf106 family.","","protein translocase protein tatA-E homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0771","812630","811614","1017","6.09","-5.68","35971","ATGGCGCGCGTATCCGCCTCCGACCAGCTCACGCGGCTGCTCGCCCTGCCCGCCTGGGTCGCGGAACACCCCGGCGTGACCGTTGCCGAGGCCGCCAAGCACTTCGGCGTCACCCCGGCCGTCATTGAGCGCGACGTCAACACGCTGTGGATCTCCGGCTTGCCCGGCGGCATGCACGGGGACCTCGTGGACTTCGACGCCGCGGACTTCGAGGCCGGACGCCTGCGCCTGTCCGAACCGCTGGGGCTGGACCGCCCGGTTCGGCTCACCCGGCAGGAGGCGATCTCTCTGCTCATGGCGCTCAGGGTGCTCGCCGACCTCCTGGCCGACGACGATGCCTCCGCACCCGTCATCGCCTCTACCCAGCAGGCGGTGACCGCTTTGCTCAGCTCTGGCGCCTCCACCGAGGACGCCGACGCCCGCGTCGATCCGGGAACCGTCACCTCCACCGGCCCAGGCCCTGCACACGCCGGACGTTCCAGCCATACGTCCCGGATCCTGGCCACAGTGCGCTCCGCCCTGCAGGGCCGACGCCGCCTCCACCTGGCCTATGTCTCCGCCACCGACACCCCTTCGGAGCGAGACGTCGACCCCATCACCCTGGAAAGTGATGGATCACATATGACGCTGGTGGGCTGGTGCCTCAGTGCCCAGGCCGAGCGCAGCTTCCGCCTGGACCGGATCACCTCGGCTGAGGCGCTCGACGCCCCGTCCGTGCGGCACCGCGCCTCACGCAGGACGAAGCAGGCCGCGGCCGATCACTATACGGGCAACAAACCTCGTGCCACGCTGGTTCTCCAACCGACGGGCCGTTGGCTCGCCGAGCAGGTCCCGTGCCTCTCCCAGGAGGAGACCGGGGACGGCAACCTTAGGGTGGTCGTTGAGGGACGCGATCGCTCCTGGCTCATCGGCCTGGTCCTCTCGGCGGGTCGCCATCTCGTGGCGGTGGAGCCCCCGGAGCTCGCCCAAGAGGCGGCAGCAGCAGCCAAACAGGCTCTGACCTCATACGACTGCTGA","MARVSASDQLTRLLALPAWVAEHPGVTVAEAAKHFGVTPAVIERDVNTLWISGLPGGMHGDLVDFDAADFEAGRLRLSEPLGLDRPVRLTRQEAISLLMALRVLADLLADDDASAPVIASTQQAVTALLSSGASTEDADARVDPGTVTSTGPGPAHAGRSSHTSRILATVRSALQGRRRLHLAYVSATDTPSERDVDPITLESDGSHMTLVGWCLSAQAERSFRLDRITSAEALDAPSVRHRASRRTKQAAADHYTGNKPRATLVLQPTGRWLAEQVPCLSQEETGDGNLRVVVEGRDRSWLIGLVLSAGRHLVAVEPPELAQEAAAAAKQALTSYDC$","Transcriptional regulator","Cytoplasm, Membrane","conserved hypothetical protein","hypothetical protein","transcriptional regulator-like","","","","","No hits reported.","BeTs to 7 clades of COG2378COG name: Predicted transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2378 is ---------dr-b-efg-snuj----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 12-96 are 60% similar to a (TRANSCRIPTIONAL PRECURSOR SIGNAL SCO1636 ML1330 REGULATOR REGULATOR REGULATORY ORF111 FAMILY) protein domain (PD020507) which is seen in Q6A7Y3_PROAC.Residues 166-238 are 62% similar to a (REGULATOR TRANSCRIPTIONAL TRANSCRIPTION DNA-BINDING REPRESSOR REGULATION DEOR-FAMILY REGULATOR PLASMID FAMILY) protein domain (PD014122) which is seen in P72265_RHOER.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0772","813790","812633","1158","8.75","4.38","41303","ATGCCGTCCTGGTCCCGGTCACTACGCCATCGCGCCACATCATGGCGGCAGACTATCCGGGCGCGCGCGTCACCAGCCGCAGGCCACCGGACTCTCCTAGGCTGGGGCACCGTGAGCCAGCCGACCCGTAGCACCGAGGAGCGTCTAGTGAGCCTTCTGCTCACCTTGCGCAACACCACCACCGGTCTCAGTGCCGAGGAGCTCGTGGCCAGTGTGCCGGGATACGGCTTGGCGGACCCCTCCACCAATCCGCTCTCGGCTCGCCGCAAGTTCGAGCGGGACAAGGACACGCTGCGCGAGCTCGGTATCGAGGTGACCACCACCGGGCGCCCCGAGGAGCCCCGGTACCGGGTCATCGAGGAAGACTACACTTTGCCCGCGCTGCACCTGAGCGCCGAGCAGGCCGCCTGCCTGAGCCTGGCCGCCTCCGCCTGGCGCGACGGCGATCTTCCCGCCACGGCCCGGCGGGCCCTGACCAAGCTGCGCGCTGTCAGTGAGGGACCGACCGGCAGCAGCTCCGCTGGTCTGCCGGTCCTCACCGCGGACCTGTCCGGCGAGGAGATCCCCGGGGAGCTCCTCACCGCGGTCGACGAGCGCCGCCTGGTCACCTTCGACTACATCTCGGCCCGCTCGGGCAACACCCGGGCCCGCACTGTCGAGCCGCACCACCTGCGCCTGGCCGAGGGCGCCTGGTACCTCGACGCCGTCGAGCCGGCAGGCGCCCACCGCCCAGACGCCAGCAGGCAACCGGAGGAACCGGAAGGAACCGCCGTCGGGCTGCGGACCTTCCGGCTGGCTCGCATCACCGGCTCAGTCACCGTTCACGGAAACCCCAGAGCCTTCACCCGGCTTCCCGCCAAGTCGCCCAGCCGCCGGCGCGCACTGCTCGCCGCCCTGCCGGGGCGTGCTCTGGGACTGCGTCTGGCCGGAGCCCACCTCGATCCGGCTCAGCGCCCGCAGGCAGAACTGCCTGCCCTGCCGGCACACCTCGAAGGCCGTGATCTCATCGCCGTCGAGTACGAGGATCCCTTCTCCTTCGCCGGAACCGTGGCCGCTCTTGGCGACGCAGTCGTCGTCCTCGCCCCCGATTCCTTGCGCCAGGCGGTCCTATCCCACCTGCGAGGCGCGGCTGGGCTCACGGCATCGGAGGGGGAGTGA","MPSWSRSLRHRATSWRQTIRARASPAAGHRTLLGWGTVSQPTRSTEERLVSLLLTLRNTTTGLSAEELVASVPGYGLADPSTNPLSARRKFERDKDTLRELGIEVTTTGRPEEPRYRVIEEDYTLPALHLSAEQAACLSLAASAWRDGDLPATARRALTKLRAVSEGPTGSSSAGLPVLTADLSGEEIPGELLTAVDERRLVTFDYISARSGNTRARTVEPHHLRLAEGAWYLDAVEPAGAHRPDASRQPEEPEGTAVGLRTFRLARITGSVTVHGNPRAFTRLPAKSPSRRRALLAALPGRALGLRLAGAHLDPAQRPQAELPALPAHLEGRDLIAVEYEDPFSFAGTVAALGDAVVVLAPDSLRQAVLSHLRGAAGLTASEGE$","Transcriptional regulator","Cytoplasm","conserved hypothetical protein","hypothetical protein","transcriptional regulator-like","","","","","No hits reported.","BeTs to 3 clades of COG2378COG name: Predicted transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2378 is ---------dr-b-efg-snuj----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 67-150 are 54% similar to a (TRANSCRIPTIONAL REGULATOR PREDICTED RV2096C/MT2157/MB2123C ML1329 DEOR-FAMILY SCO1637 ORF101) protein domain (PD653991) which is seen in Q6AFW3_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0773","813751","814920","1170","6.13","-8.27","40283","ATGTGGCGCGATGGCGTAGTGACCGGGACCAGGACGGCATGGGGACCCGCGGGGCGATCCTGCGCCGAGCTGGACGTGGAGATCGTCGGGGCCCCAAATGGTGCGGACGGCCTGCTGCCAGGCCAGCGGGTCCGTGCGGTCGCCTACGAGGCCCTCACTGGGCTGCCCGACTCTGGGGAGCGGGTGAGGCTGGAGGTCTCGGCCCTCGACCGTGCCCTGGGCACGGGTGGGCACGCCATGGTCAGCTCTCGCCTCGACGTCCTGCCCCCCGATCCTCCGCGCGAGGGGCACCTCGTCAAGGCCCGCTACATGCCGGACCAGGTGATGGTCACCGGCGTTGACGAGCAGGGCACGGCCCACCACGGCCTGCTGTCCCAGCCGATCGGCAGCCTCCATCTGGAGGGGATGCCGGTGGTGGTGGCCGACCTGCACTCGAGTCTGCCGGCGGTGCTCGCCGGGCTGCGCTTCCCCGACGGCCAGGAGCAGCCACGAGTCGCCTACATCATGACCGACGGCGGGGCCCTGCCCCTGGCCTACTCGCGTGTCGTTGCCGCCCTGAGCCTGGCCGGGTGGCTGACCGGGACCATCACGGCCGGGCAGGCCTGGGGCGGCGACCTCGAGGCGGTCAGCATGCACAACGCGCTCCTGGCGGCCCGGCACGTCCTGCACGCCGATGCCGCCGTCGTCATCCAGGGGCCCGGCAATCTGGGCACCGAGACGCCCTGGGGCTTCTCCGGGGTGGCCTGCGGGGACGCAATCAACGCCGTCGCCACGCTGAGCGGACACCCGGTGGCCTGCCTGCGTGTCTCTGACGCCGATGCCCGCGCCCGCCACCGGGGCGTGTCCCACCACTCGATGACGGCTTACGGACGAGTCGCACTGGCGGGGGCCGACATCGTCGTCCCCGACCTGGAGGGGCCACTGGGGGCACAGGTGCGTCAGGAGGCCGAGGCCTTGTGCGCGCCCCGGCCGGGCGCCGGGCAGCACCGACTCGTCGAGGTTCCCACCGACGGGCTCCTGGAGCTGCTGCGGGAGGCGGAGGCGCAGACCGGAGTGAGACTGTCCACCATGCGACGAGGCTTGGATGAGGACGCGGCCGCTTTCATCGCCGCAGCGGCGGCCGGTCGCCACGCACGGCGGGTCCTGGACGAGGGAACAGCGCATGGCTGA","MWRDGVVTGTRTAWGPAGRSCAELDVEIVGAPNGADGLLPGQRVRAVAYEALTGLPDSGERVRLEVSALDRALGTGGHAMVSSRLDVLPPDPPREGHLVKARYMPDQVMVTGVDEQGTAHHGLLSQPIGSLHLEGMPVVVADLHSSLPAVLAGLRFPDGQEQPRVAYIMTDGGALPLAYSRVVAALSLAGWLTGTITAGQAWGGDLEAVSMHNALLAARHVLHADAAVVIQGPGNLGTETPWGFSGVACGDAINAVATLSGHPVACLRVSDADARARHRGVSHHSMTAYGRVALAGADIVVPDLEGPLGAQVRQEAEALCAPRPGAGQHRLVEVPTDGLLELLREAEAQTGVRLSTMRRGLDEDAAAFIAAAAAGRHARRVLDEGTAHG$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 42-287 are 60% similar to a (BH1523) protein domain (PD607790) which is seen in Q8RAB4_THETN.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0774","814835","816301","1467","7.15","0.80","52107","ATGAGGACGCGGCCGCTTTCATCGCCGCAGCGGCGGCCGGTCGCCACGCACGGCGGGTCCTGGACGAGGGAACAGCGCATGGCTGATCGAGACGGCCAACCGGGCGCGACGGCCCGCAGCGCGGTGCTGCCGACGACAGCGAGTCTGTCAGCGGCCTACGACTGGCAGGCCCGTCACCGCATGGTGCCGGGACGAGGAGGTCGCTGGGCACACTACTCGATCCCGGTCGTGGATCTCGCCCTGGGGATCGTCTTCCTCGCCTTCGCACTGGAGTCGGTCACCTTCATCCTGCGCTTCGGCGGCTATGCCATCTATGTTGCGGACTTCGCCCTGTGTCTGGCGCTGGCGCTGACGCAGTTCGGACGGTTGCGTCTCCTGCGTGTCTCCTTCATCGCGACCTACGCCCTGCTGGCGGCCTACGCGATCCTCGTGGTCATCTCCCCCGTCAACCTCGGCCTCAACCCGATCATCGCCACGGCCATCACCAGTCTCTACACCGTCACCCGCTGGGAGCCCGACCGGCGCTGGGGCACGGCGGCACTCCTGCTGGCTCTGGCCGGCGCCCTGGTCAACCCCGTTACCCTCGCCTCCTACACCCCGCCCTACGAATCAGACGCCGACCCGACGACAGGCTCCGGCTGGGACGGAACCATCCTCCTGGTCAGAGCACTCTCCAGCCTGGTCTTCGTCGGTGCCGTGGTGCTCACCTACCTGCTGGCCTCCTCCCGGCGCCGGATCGCCGAGAACCAAGCCCTCGACGTCGGCATCGCCGCGGCCCAGGCGGTTGCGGCCGAGCGCCTCAGCCTGGCCCGAGAGCTCCACGACCTGGTGGGCCACAGCCTCACCACGATCAAGGTGCAGGCCGCCACCGGCCTGGCCCTGGGAGGCGAGGAACGGCTGCGCAGCACCCTGACCACGGTGCGTGACACGGCCGATGCCTCCCTGGCCTCCGTGCGCCAGCTCGTCTCCGTGCTGCGCTCCGACGCCGGCGAGATCACTCCCCTGGCGGACCTGCGGACCATCCCGGCCCTCATCGAGACCACTCGCAGCTCGGGGAGCCGGATCAGCGCCGTGCTTCCCGAACCGGAGGTCCTGGAGCGTTGCAACTCGGCGTGGTCTGCGATACAACGCCTCACCCTCGTGCGTCTGGTAGGAGAGACCCTCACCAACGCCGTCAGGCACGGAACCGGCCAGATCGAGCTGAGCCTGACACTGTCGCAGGACTCCTGCCACCTTCACGTCGCCAACCCGGTGCCCGACGTCGCAGAGCACTCCCCCTTCGGTGGCAGCGGACTCGTCGGCCTCGAGGAGCGGCTCAGGCTCGTGGGCGGAACCATGACCCACGGCATCCACAACAACGGGGACCACAGCTTCTTCACCATTGATGTCGACTTCCCGGTGGCGCCGCTCGACCTGCCCGCGAGCGCCATGACCGCCGGCGAGACAGAATCAGGAGACTACAGATGA","MRTRPLSSPQRRPVATHGGSWTREQRMADRDGQPGATARSAVLPTTASLSAAYDWQARHRMVPGRGGRWAHYSIPVVDLALGIVFLAFALESVTFILRFGGYAIYVADFALCLALALTQFGRLRLLRVSFIATYALLAAYAILVVISPVNLGLNPIIATAITSLYTVTRWEPDRRWGTAALLLALAGALVNPVTLASYTPPYESDADPTTGSGWDGTILLVRALSSLVFVGAVVLTYLLASSRRRIAENQALDVGIAAAQAVAAERLSLARELHDLVGHSLTTIKVQAATGLALGGEERLRSTLTTVRDTADASLASVRQLVSVLRSDAGEITPLADLRTIPALIETTRSSGSRISAVLPEPEVLERCNSAWSAIQRLTLVRLVGETLTNAVRHGTGQIELSLTLSQDSCHLHVANPVPDVAEHSPFGGSGLVGLEERLRLVGGTMTHGIHNNGDHSFFTIDVDFPVAPLDLPASAMTAGETESGDYR$","Two-component system sensor kinase","Membrane, Cytoplasm","putative two-component system sensor kinase","two-component system sensor kinase","histidine kinase, dimerisation and phosphoacceptor region","","Chen C.M., Ye Q.Z., Zhu Z.M., Wanner B.L., Walsh C.T. Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B. J. Biol. Chem. 1990. 265(8):4461-4471. PMID: 2155230Kulakova A.N., Kulakov L.A., Quinn J.P. Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida. Gene 1997. 195(1):49-53. PMID: 9300819","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[375-447]T$	HATPase_c
SM00387	$\"[375-467]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[265-331]T$	HisKA_3

InterPro
IPR013991
Domain

PhnA protein N-terminal, proteobacterial
SM00782	$\"[363-400]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[69-89]?$ $\"[95-115]?$ $\"[125-145]?$ $\"[151-169]?$ $\"[179-199]?$ $\"[218-240]?$	transmembrane_regions

","BeTs to 5 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 1.4e-10. IPB011712A 264-281 IPB011712B 380-400","Residues 271-352 are 57% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM TRANSFERASE 2.7.3.- SENSORY TRANSDUCTION NITRATE/NITRITE) protein domain (PD288674) which is seen in Q9K428_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 265 to 331 (E_value = 7.3e-17) place ANA_0774 in the HisKA_3 family which is described as Histidine kinase.Residues 375 to 447 (E_value = 0.0033) place ANA_0774 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","two-component system sensor kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0775","816298","817053","756","5.24","-7.65","25566","ATGACGACCAGAACGACCGGTGTTATCAGGGTGGCTGTTGTCGACGATCAGCCGCTGCTGGTCAGCGCCTTCAGTGCTCTCGTGGCCGCACAGCCCGACATGGAGGTGGTTCTGGAGGCCGTTAACGGGCGTCAGGCCGTCGAGGGTTTGACCGCTCGAGCCACCGGTCCCCACGGAGGGGCCGACCTTGTGCTCATGGATCTGCGGATGCCGGTCCTGGACGGGGTCAGTGCCATTCGCGAGCTGCGTGCCGCACCGGCCACTGCCTCGTTGCGGGTTCTGGTCCTGACCACCTTCGATGATGAGGAGCTCGTCCTGGCCTCGCTGGGTGCCGGCGCCCACGGCTTCCTCCTCAAGGACGCCGAGCCGACGACGCTGCTGGAGGCGATCCGCGTCGTCGCCGGCGGAGGGTCCTGGCTGGATCCGGCCGTCACCGGAACCGTTCTGGCGCATCTTGATGCAGGTACCGGACCTGGTGCCCCGCCGTCGTCGGCCTCCCCGTCGGCACCGATCGATGGGGCTGTGCCCGTTGTGGGGGCGCCGTCGGGTCCCTACGAGGCTCTTACTGTTCGGGAGGACGCCGTACTCGCGTTGGTGTGCCAGGGGTTGAGTAACGCCAGTATCGGTGAGCGGCTCCATGTCGCCGAGTCGACGGTCAAGTCCCATGTCAAGACGATCCTGGGTAAGACGGGCTGCCACAACCGGGTCGAGCTCGTCATTTACGCCCTGACCACGGGACTCGCCCAGCCGCGGTAG","MTTRTTGVIRVAVVDDQPLLVSAFSALVAAQPDMEVVLEAVNGRQAVEGLTARATGPHGGADLVLMDLRMPVLDGVSAIRELRAAPATASLRVLVLTTFDDEELVLASLGAGAHGFLLKDAEPTTLLEAIRVVAGGGSWLDPAVTGTVLAHLDAGTGPGAPPSSASPSAPIDGAVPVVGAPSGPYEALTVREDAVLALVCQGLSNASIGERLHVAESTVKSHVKTILGKTGCHNRVELVIYALTTGLAQPR$","Two-component system response regulator","Cytoplasm, Membrane","chitinase two-component response regulator","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[188-243]T$	Q8DK22_SYNEL_Q8DK22;
PR00038	$\"[188-202]T$ $\"[202-218]T$ $\"[218-230]T$	HTHLUXR
PF00196	$\"[185-242]T$	GerE
SM00421	$\"[185-242]T$	HTH_LUXR
PS50043	$\"[181-246]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[9-134]T$	Q6ABR9_PROAC_Q6ABR9;
PF00072	$\"[9-131]T$	Response_reg
SM00448	$\"[9-130]T$	REC
PS50110	$\"[10-134]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[179-248]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[9-143]T$	no description
PTHR23283	$\"[10-134]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF47	$\"[10-134]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (DHKB)
signalp	$\"[1-30]?$	signal-peptide

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[147-189]T$	Q6NKE2_CORDI_Q6NKE2;
PF00005	$\"[48-222]T$	ABC_tran
PS50893	$\"[23-246]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[47-230]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[16-237]T$	no description
PTHR19222	$\"[23-255]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 16 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 9.1e-23. IPB005074C 37-84 IPB005074D 135-178***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 8.2e-22. IPB013563A 37-71 IPB013563C 144-171 IPB013563D 198-250***** IPB005116 (TOBE domain) with a combined E-value of 2.6e-09. IPB005116A 55-71 IPB005116D 167-186 IPB005116E 200-213***** IPB013283 (ABC transporter family E signature) with a combined E-value of 8.5e-07. IPB013283D 52-77","Residues 2-228 are 44% similar to a (C24F3.5 ATP-BINDING) protein domain (PD574736) which is seen in Q21213_CAEEL.Residues 23-144 are 52% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA188U2) which is seen in Q9RXA9_DEIRA.Residues 23-225 are 45% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD756741) which is seen in Q8A5R4_BACTN.Residues 23-228 are 45% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 25-119 are 55% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 27-227 are 43% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 28-224 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 33-147 are 46% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 37-193 are 45% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 37-204 are 45% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 38-216 are 44% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 40-85 are 71% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q7V804_PROMM.Residues 43-206 are 49% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 48-219 are 45% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 48-229 are 43% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 54-228 are 46% similar to a (ATP-BINDING BRANCHED-CHAIN ABC PROTEIN ACID AMINO TRANSPORTER) protein domain (PD542092) which is seen in Q8ZXB5_PYRAE.Residues 102-229 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 116-204 are 51% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 126-227 are 59% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 132-228 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J201) which is seen in Q73M59_TREDE.Residues 133-229 are 52% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z3) which is seen in Q72D80_DESVH.Residues 134-227 are 57% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 134-204 are 67% similar to a (ATP-BINDING LONG TRANSPORTER ABC 331AA 298AA) protein domain (PD502979) which is seen in Q96ZV0_SULTO.Residues 142-221 are 65% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18641) which is seen in Q8EG59_SHEON.Residues 142-228 are 59% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 143-224 are 59% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K1H6) which is seen in Q73MA6_TREDE.Residues 145-225 are 60% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 147-189 are 88% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6NKE2_CORDI.","","-50% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 5.9E_21);-46% similar to PDB:1G6H CRYSTAL STRUCTURE OF THE ADP CONFORMATION OF MJ1267, AN ATP-BINDING CASSETTE OF AN ABC TRANSPORTER (E_value = 1.8E_17);-46% similar to PDB:1G9X CHARACTERIZATION OF THE TWINNING STRUCTURE OF MJ1267, AN ATP-BINDING CASSETTE OF AN ABC TRANSPORTER (E_value = 3.0E_17);-46% similar to PDB:1GAJ CRYSTAL STRUCTURE OF A NUCLEOTIDE-FREE ATP-BINDING CASSETTE FROM AN ABC TRANSPORTER (E_value = 6.8E_17);-51% similar to PDB:2ONK ABC transporter ModBC in complex with its binding protein ModA (E_value = 6.8E_17);","Residues 48 to 222 (E_value = 5.1e-43) place ANA_0776 in the ABC_tran family which is described as ABC transporter.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0777","818174","819625","1452","10.83","13.54","50984","ATGCACATGTATGCCGGGGGCTTCGCCGTGCCTCTGGGGCTGCTGACCGGGGCGATGGCCCAGTGGCGTGAGCAGCGGTGGCGTCAGGGTGGGACGGCATGGCGCGCCGTCGCGCCGCGCCGGGTGGCGGGTGCCCGCCTCGTGGTCCTGAGCCTGTCCGCGTTGGCCTGCCAGGTGGCGCTGGTCGCCCCGGTGGTGGGGCACGCCCTGATCGTCGGCAACGGCTGGGGTCCTTGGGACCGGTACCTGCTGTTTGCCACCTACATGTGGATCGTCGTTACCGGCGCCTGCGCCTGGGGCATGGCAGCCTTCCACGTGCTGCGAGTTGTTTCCGTAGGGGTCGCCCCTGTCCTCGGCTTCGTCTGGTCCGTGGCGGGCGTGGTCCAGGCCGAGCGGAGCGACTGGTGGATGCTCCCGTGGGCCTGGACGGCGAGGGTCCCGTTGCCTCTGCTGGGTGTTCACGGCAGCAGCGTGCTGCTTGAGGCAGACTCGCCGGTGTGGGGCTACCCGCTCCTGCCCGGGTTCCTGCTGACGATCGGTCTGACCCTGGCCGGCGTCGGACTGGACGTGCTCTGTGGGGTTTCTGGTGGTGCTGGGGCCTTGGCGTCGTCGGCTTCCCGGCTCAGCCGACTGCTTCCTGGCGGAAGGGATGGCGTTGACGATCAGTCGGAGACCGCCTCGGTGCAGTCACCGGAGCAGGCCCCAGGCGCGCGCCCCCAAAGCATCCCGATTCGTCGAGCCACGCCCACCACCCGTATGGCCCATGTTCCCGGGCCGCGCAGTGCCGTCCTGGCGATGGCCGGCGTTCTGCCCTGGATCGTGTGGGTGGTCCTGGCGGTCCTGCTGCTCGCCTTCCTGGGGATCCTCCACATCGTGTACCCACCCGGGTACGGGCAGAGCTTCCTCGAGCTCATGGGAGTGCCGGTTGCCGCAGCCCTCGTCGGCATCACGGTGTGGGGACGTCTCCAACCTGCCTGGCGTGCGCTCATCACCCGCCGAGGTGCCGGGGCCATCCTGACCTCAGTTGCGGTCCTGAGTGGGTTCTTCCTCATCCCGGTCCTGGGCGCCTCCTGGGGCATGACGGTCCTGGGCGACACATTGACCCGCACCGACCCGACGCTGCCGGCGGTGACCGGCCCGGTCTACGGGTTCATGGTGATGCCGGCCGTTGCCTTCATGATCGCGGCCGTCAGCCTGGCGGTGGCTCTGAGCACCCGGATCGTCGTGGCGATCGTCCTCAACATCATCCTGGTCATCATGGGTCTGCTCATCGGCGGCAACGAGGTCCTGGCGGCCACCTGGCTGTGGCGGCTGGCCCCTTGGGGCTGGATGAGTATCGCTCACCAGTTCCCCGAGCGTTGGCTGATGATCGTCGTCCTCAGCCTGCTCATCGGATCGGTGGCGATGGGGACAGCGGCCCTAGGTGCCCGGCGCGCCGCCATCCGGGACTGA","MHMYAGGFAVPLGLLTGAMAQWREQRWRQGGTAWRAVAPRRVAGARLVVLSLSALACQVALVAPVVGHALIVGNGWGPWDRYLLFATYMWIVVTGACAWGMAAFHVLRVVSVGVAPVLGFVWSVAGVVQAERSDWWMLPWAWTARVPLPLLGVHGSSVLLEADSPVWGYPLLPGFLLTIGLTLAGVGLDVLCGVSGGAGALASSASRLSRLLPGGRDGVDDQSETASVQSPEQAPGARPQSIPIRRATPTTRMAHVPGPRSAVLAMAGVLPWIVWVVLAVLLLAFLGILHIVYPPGYGQSFLELMGVPVAAALVGITVWGRLQPAWRALITRRGAGAILTSVAVLSGFFLIPVLGASWGMTVLGDTLTRTDPTLPAVTGPVYGFMVMPAVAFMIAAVSLAVALSTRIVVAIVLNIILVIMGLLIGGNEVLAATWLWRLAPWGWMSIAHQFPERWLMIVVLSLLIGSVAMGTAALGARRAAIRD$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[43-63]?$ $\"[82-102]?$ $\"[112-130]?$ $\"[169-203]?$ $\"[272-294]?$ $\"[300-320]?$ $\"[335-355]?$ $\"[381-403]?$ $\"[413-435]?$ $\"[454-476]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 83-173 are 53% similar to a (PERMEASE SPAE MUTE LANTIBIOTIC SUBUNIT SPAE/MUTE MEMBRANE FACILITATOR SRTE BACTERIOCIN) protein domain (PD232936) which is seen in O52853_BACSU.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0779","820471","819854","618","6.27","-2.68","22451","GTGAGGGCCTCGGATCCGTCGATGTGGGAGGAGCAGTCGCATCGGGAGTGCTCGCCGGAGAAGGACGCCTACGGGCTGGACAAGTACAAGTGCAACCTGGCCACCCTCAACCGCCCCGGCGGGCCCGACCAACCCACCACCGCCGGTGGTGGCCGTACGGTCACGGTCACCACCCGTCAGGCCGCCACCCTGATCGCCTCGGGCTCGGGCATCACCCGCCAGCCCCCAGGCCCCAAGGTCATCATCTCCAAGGCCTTCATCGTCTACACCAACCCCGCCGTGCGCTACCAGACCACCACCATCCTGGGCACCACCATCGACGTCGAGTTCACCCCCACCACCTACACCTGGAACTGGGGAGACGGCACCACCACAACCACCACCGACCCCGGCGCCCCCTACCCCCACCAGACCGTCACCCACCACTACCAGCACACCGCCACCGGCATCACCACCACCCTGACCACCACCTGGACCACCCGCTACCGCCCCGCCGGCGAGAACCAGTGGCGACCCATCGAAGGCACCATCACCACCACCGAGACCTCCACCCCCTACGACCTGGTCCGCATCGTCACCTACCTCACCGACGACGCCGAAGAAGCCCAAGGCCACTAA","VRASDPSMWEEQSHRECSPEKDAYGLDKYKCNLATLNRPGGPDQPTTAGGGRTVTVTTRQAATLIASGSGITRQPPGPKVIISKAFIVYTNPAVRYQTTTILGTTIDVEFTPTTYTWNWGDGTTTTTTDPGAPYPHQTVTHHYQHTATGITTTLTTTWTTRYRPAGENQWRPIEGTITTTETSTPYDLVRIVTYLTDDAEEAQGH$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

InterPro
IPR000601
Domain

PKD
PS50093	$\"[111-143]T$	PKD

InterPro
IPR008179
Domain

Phosphoribosyl-ATP pyrophosphohydrolase
PD002611	$\"[41-87]T$	Q6AF75_BBBBB_Q6AF75;
PF01503	$\"[4-87]T$	PRA-PH

noIPR
unintegrated

unintegrated
PTHR21256	$\"[7-87]T$	HISTIDINOL DEHYDROGENASE (HDH)

","BeTs to 14 clades of COG0140COG name: Phosphoribosyl-ATP pyrophosphohydrolaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0140 is -om---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB008179 (Phosphoribosyl-ATP pyrophosphohydrolase) with a combined E-value of 3e-08. IPB008179 22-50","Residues 1-40 are similar to a (PHOSPHORIBOSYL-ATP PYROPHOSPHATASE HYDROLASE BIOSYNTHESIS PRA-PH HISTIDINE) protein domain (PD585610) which is seen in Q6AF75_BBBBB.Residues 41-87 are similar to a (HISTIDINE BIOSYNTHESIS PHOSPHORIBOSYL-ATP HYDROLASE PYROPHOSPHATASE PRA-PH PHOSPHORIBOSYL-AMP INCLUDES: CYCLOHYDROLASE BIFUNCTIONAL) protein domain (PD002611) which is seen in Q6AF75_BBBBB.","","-78% similar to PDB:1YXB Crystal structure of Phosphoribosyl-ATP pyrophosphatase from Streptomyces coelicolor. NESG target RR8. (E_value = 3.2E_27);-76% similar to PDB:1Y6X The 1.25 A resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis (E_value = 1.0E_25);","Residues 4 to 87 (E_value = 3.5e-06) place ANA_0780 in the PRA-PH family which is described as Phosphoribosyl-ATP pyrophosphohydrolase.","","pyrophosphatase (hisE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0781","822467","823312","846","5.71","-4.09","30163","GTGCTGCGTATCGCTGTCCCGAACAAGGGCTCCCTGTCCGCTCCCGCCATCACCATGCTCTCCGAGGCGGGCTACCGCACCCGCCGCACGGGCCGTGAGCTCGTGCTCGTCGATGAGGCCAACGACGTCGAGCTGTTCTTCCTGCGTCCGCGCGACATCGCCGTCTACGTCGGTCAGGGCACCGTCCACGCCGGCATCACCGGCCGCGACCTGCTCCTGGACTCCGGGGTCGACGCCGTCGAGCACCTGCCCTTGGGTTTCGCCCGCTCCACCTTCCGCTTCGCCGCCCCCAAGGGCACGATGAGCTCCTTGGCCGATGTCGCCGGACGCCGCGTGGCCACCTCCTATGACGTCCTGGTGCGCAGTTACCTTGCCGCTAGGGGCGTGGATGCCCAGACCGTTCACCTCGACGGCGCCGTGGAGTCCTCCGTCCAGCTGGGCGTTGCCGACCTCATCGCCGACGTCGTCGAGACCGGAACAACGCTGCGGGCCGCCGGTCTGGAGACCTTCGGGGACCCGATCCTCATCAGCGAGGCCGTACTCATCACCACCGAGCAGTTCCGCGCAGAGCCCGGACTGGCCACGCTCGTACGGCGGCTGGAGGGGGTGCTGCGCGCCCGCGCCTACGTGCTCATCGACTACGACATCCCCATGAACAAGCTGCACCTGGCGGCGGCCCTCACCCCGGGCATCGAGTCCCCCACTGTCTCCCCGCTGCAGAACCCCGACTGGGTGGCGGTACGCTCCATGGTCCCGCGAGCCGACATGAACCGGGTCATGGACGAGCTTTACGAGGTCGGGGCGCGCGCCATCCTCGTCTCCTCACTGTTGGCCTGCCGGCTGTAG","VLRIAVPNKGSLSAPAITMLSEAGYRTRRTGRELVLVDEANDVELFFLRPRDIAVYVGQGTVHAGITGRDLLLDSGVDAVEHLPLGFARSTFRFAAPKGTMSSLADVAGRRVATSYDVLVRSYLAARGVDAQTVHLDGAVESSVQLGVADLIADVVETGTTLRAAGLETFGDPILISEAVLITTEQFRAEPGLATLVRRLEGVLRARAYVLIDYDIPMNKLHLAAALTPGIESPTVSPLQNPDWVAVRSMVPRADMNRVMDELYEVGARAILVSSLLACRL$","ATP phosphoribosyltransferase","Cytoplasm","ATP phosphoribosyltransferase","ATP phosphoribosyltransferase ","ATP phosphoribosyltransferase","","de Zamaroczy M., Delorme F., Elmerich C. Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense. Mol. Gen. Genet. 1990. 224(3):421-430. PMID: 1702507Sibold L., Henriquet M., Possot O., Aubert J.P. Nucleotide sequence of nifH regions from Methanobacterium ivanovii and Methanosarcina barkeri 227 and characterization of glnB-like genes. Res. Microbiol. 1991. 142(1):5-12. PMID: 2068380Wray Jr L.V., Atkinson M.R., Fisher S.H. The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a protein highly similar to the Escherichia coli glnB-encoded PII protein. J. Bacteriol. 1994. 176(1):108-114. PMID: 8282685Allikmets R., Gerrard B., Court D., Dean M. Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance. Gene 1993. 136(1):231-236. PMID: 7904973","","","

InterPro
IPR001348
Family

Histidine biosynthesis HisG: ATP phosphoribosyltransferase
PTHR21403	$\"[7-281]T$	ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE)
TIGR00070	$\"[1-281]T$	hisG: ATP phosphoribosyltransferase

InterPro
IPR002187
Family

Nitrogen regulatory protein P-II
G3DSA:3.30.70.120	$\"[209-281]T$	no description

InterPro
IPR013115
Domain

Histidine biosynthesis HisG, C-terminal
PF08029	$\"[205-279]T$	HisG_C

InterPro
IPR013820
Domain

ATP phosphoribosyltransferase, catalytic region
PD003516	$\"[81-202]T$	HIS1_STRCO_Q8CK28;
PF01634	$\"[48-204]T$	HisG
PS01316	$\"[141-162]T$	ATP_P_PHORIBOSYLTR

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[1-83]T$ $\"[91-176]T$	no description

","BeTs to 18 clades of COG0040COG name: ATP phosphoribosyltransferase (histidine biosynthesis)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0040 is aom---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001348 (ATP phosphoribosyltransferase) with a combined E-value of 1.4e-39. IPB001348A 9-24 IPB001348B 52-74 IPB001348C 85-97 IPB001348D 111-124 IPB001348E 138-167***** IPB013115 (Histidine biosynthesis HisG, C-terminal) with a combined E-value of 3.8e-39. IPB013115A 9-21 IPB013115B 40-71 IPB013115C 106-117 IPB013115D 147-168 IPB013115F 244-279","Residues 2-76 are 78% similar to a (TRANSFERASE ATP GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE BIOSYNTHESIS ATP-PRT HISTIDINE ATP-PRTASE METAL-BINDING MAGNESIUM) protein domain (PD824332) which is seen in HIS1_STRAW.Residues 81-202 are 73% similar to a (TRANSFERASE ATP GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE BIOSYNTHESIS ATP-PRT HISTIDINE ATP-PRTASE METAL-BINDING MAGNESIUM) protein domain (PD003516) which is seen in HIS1_STRCO.Residues 218-280 are 79% similar to a (TRANSFERASE PHOSPHORIBOSYLTRANSFERASE GLYCOSYLTRANSFERASE ATP HISTIDINE ATP-PRTASE BIOSYNTHESIS ATP-PRT METAL-BINDING MAGNESIUM) protein domain (PD931643) which is seen in HIS1_STRCO.","","-71% similar to PDB:1NH7 ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.6E_80);-71% similar to PDB:1NH8 ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AMP AND HISTIDINE (E_value = 1.6E_80);-49% similar to PDB:1H3D STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE (E_value = 1.1E_23);-49% similar to PDB:1Q1K Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP (E_value = 1.1E_23);-49% similar to PDB:1VE4 ATP-Phosphoribosyltransferase(hisG) from Thermus thermophilus HB8 (E_value = 9.3E_20);","Residues 48 to 204 (E_value = 3.3e-48) place ANA_0781 in the HisG family which is described as ATP phosphoribosyltransferase.Residues 205 to 279 (E_value = 3.9e-33) place ANA_0781 in the HisG_C family which is described as HisG, C-terminal domain.","","phosphoribosyltransferase (hisG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0782","824351","823368","984","7.49","1.95","34005","ATGCCCCTCTCGCGCCGCCACCTGCTCGCCAGTGGTCTCGTCCTGAGCGGAACCGGCGTGCTCGCCGCCTGCTCTTCACAGTCAAGCAGCCCACTGACCATCGGCCTGACCTACACGCCCAACATCCAGTTCGCCCCCATCTACACGGCAAAAAAGAACAGCAAGTACGCCTCCGGGGTGAGCCTGCGTCATCACGGGGCCCAGGAGGGGCTCTTCGACGCTCTTCTGAGCGGAAAGGAGCAGCTTGTCGTGGCGGGAGCCGATGAGGCCGTCGTCGCCGCTTCCAACGGGTCTGACCTTGTCGTCGTCGGCGGCTACTACCAGTCCTATCCGGCCTGCCTCATCGTGCCGGAGAGCTCGCCAATCAAGACACCCGCGGACCTCAAGGGCAAGACCGTCGGCACGCCGGGACGCAAGGGGGAGACCTGGTACGCCCTCCAACTGGCCATGGACACCGCCTCGCTGAGCGAGTCCGACCTGACGATCCAGGACATCGGCTACACCCAGCAGGCTGCGCTCGTGGGTGGCAAGGTTGACGCCGTCGTCGGCTTCTCCAACAACGACGCCGTGCAGATCAAGCAGGCCGGCACCGCGGTGCGCACGATCCAGCCGTCCGAGTCGATCCCCCTCATCGGCGTCTCCCTGGTGACGACCCGCAAGCTGTTGGACTCCAGGCGTGAGGACCTTCAGGCGGCGGTCAAGGCCTCAGTGGAGGGCATGACCGCGTTCGTCAAGGATCCTGACGCCGCGGTCGAGGCGACCAAGGAGTACGTGCAGGACCTGGTTGACTCCACTCAGGCCGCCAACGCCCGCGAGGTCGCCGTGGCCACGGGCAAGCTGGTCAGCGGGGAGGGCAAGGCGGCCGTCGGCTCAGTGCGGGTCGACGACTTCACACCGATGATCGAGTTCCTCGCCTCCCACAAGATCCTGGGCGACAAGAAGACACCCAAGGCCGCCGACATCTGCGTGCCCCTGGGGCAGTAG","MPLSRRHLLASGLVLSGTGVLAACSSQSSSPLTIGLTYTPNIQFAPIYTAKKNSKYASGVSLRHHGAQEGLFDALLSGKEQLVVAGADEAVVAASNGSDLVVVGGYYQSYPACLIVPESSPIKTPADLKGKTVGTPGRKGETWYALQLAMDTASLSESDLTIQDIGYTQQAALVGGKVDAVVGFSNNDAVQIKQAGTAVRTIQPSESIPLIGVSLVTTRKLLDSRREDLQAAVKASVEGMTAFVKDPDAAVEATKEYVQDLVDSTQAANAREVAVATGKLVSGEGKAAVGSVRVDDFTPMIEFLASHKILGDKKTPKAADICVPLGQ$","Sulfonate/nitrate/taurine transport system substrate-binding protein","Periplasm, Membrane, Cytoplasm","conserved hypothetical protein","K02051 sulfonate/nitrate/taurine transport system substrate-binding protein","ABC-type nitrate/sulfonate/bicarbonate transport systems periplasmic components-like","","","","","

InterPro
IPR015168
Domain

NMT1/THI5 like
PF09084	$\"[94-303]T$	NMT1

","BeTs to 6 clades of COG0715COG name: ABC-type nitrate/sulfonate/taurine/bicarbonate transport systems, periplasmic componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0715 is a-----y-vd--bcefgh---j-i--Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 85-210 are 52% similar to a (ABC PERIPLASMIC TRANSPORTER BINDING SUBSTRATE-BINDING TRANSPORTER PROTEIN PRECURSOR SIGNAL EXPORTED) protein domain (PD396701) which is seen in Q9RXP2_DEIRA.Residues 212-308 are 55% similar to a (DR0268) protein domain (PD992456) which is seen in Q9RXP2_DEIRA.","","No significant hits to the PDB database (E-value < E-10).","Residues 94 to 303 (E_value = 4.3e-27) place ANA_0782 in the NMT1 family which is described as NMT1/THI5 like.","","hypothetical protein","","1","","","Wed Aug 1 18:07:41 2007","","Wed Aug 1 18:07:41 2007","","","Wed Aug 1 18:07:41 2007","Wed Aug 1 18:07:41 2007","Wed Aug 1 18:07:41 2007","","","","","","Wed Aug 1 18:07:41 2007","","Wed Aug 1 18:07:41 2007","","Wed Aug 1 18:07:41 2007","Wed Aug 1 18:07:41 2007","","","","","yes","","" "ANA_0783","825364","824417","948","8.97","5.77","33155","GTGTACAGCCCCAGCCCCATCGGCAAGGCCGCACGCTCCTACGCTTCCCCCACCGCAGTATCCCGCGATGCCCACGAGCCGGTGACGTCCTCAGGCTCGCCAGCGCCCTCGCCGGCGGGGTCCGTCTTAGAGCCGCCGCAGACGCCGCCGCTTCATCGTCAGCCTCCTATCCGTACTGCAGGCCGCCACGGCCCGTGGCCGGCGTTCCTTCTCGGCGCTACTCTGCTCGTCGCGTGGCAGGCCGCCGCGGCCTCAGGCGCCGTTCCGGCCATCTTCCTGCCCAGTCCGCTGGCCGTCATCACGCGGATGTGGCTGGGCCTGACCCAGGCAGGACTGGCCGCCTACGCCGGGGTGACGCTCAAGGAGGCGCTCCTGGGCTGTCTGCTGGCCGCGGCCTTTGCGCTGCCACTGGCCTGGGTGCTGCACCATTGGCGGTTCTTCTCCCGGGCGGTGCTGCCCTATGTCGCTGCGAGCCAGGCGGTTCCCGGTATCGCCTTAGCCCCGCTCCTCGTCCTGTGGATCGGCTACGGCACTCTGCCGGTGGTGATTCTGTGCGCCTTCATGGTGTTCTTCCCCATCACGATCACCGTGCTGCTGGGGCTGCGGGGCCTGGACACTGACATCATCGACGCCGCCCGGCTCGACGGCGCGTACGGGCTGAGCATGCTCGTGCACATGGAGCTGCCCATGACGCTTCCGGCGATCTACACCGGACTGCGCACAGGGTTCACCCTGTCGATCACCGGCGCGGTCGTCGGAGAGATGATCATGGGCGGTGACGGCCTGGGAATGCTGTTGTCCACGCAGCGCGACAAGGTGGACACCACGGGCATGTTCTCCACCATTGCCCTCCTGTGCATTCTGGCCACCACCATCCACTGGGCGCTCCACGAGCTCGAGCAGCGCAGCCGCACGGTGGACGCCCTGCGTGGCCGGCGTGCCGGCTGA","VYSPSPIGKAARSYASPTAVSRDAHEPVTSSGSPAPSPAGSVLEPPQTPPLHRQPPIRTAGRHGPWPAFLLGATLLVAWQAAAASGAVPAIFLPSPLAVITRMWLGLTQAGLAAYAGVTLKEALLGCLLAAAFALPLAWVLHHWRFFSRAVLPYVAASQAVPGIALAPLLVLWIGYGTLPVVILCAFMVFFPITITVLLGLRGLDTDIIDAARLDGAYGLSMLVHMELPMTLPAIYTGLRTGFTLSITGAVVGEMIMGGDGLGMLLSTQRDKVDTTGMFSTIALLCILATTIHWALHELEQRSRTVDALRGRRAG$","Sulfonate/nitrate/taurine transport system permease protein","Membrane, Cytoplasm","ABC transporter, permease protein","K02050 sulfonate/nitrate/taurine transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Holt C., Sawyer L. Primary and predicted secondary structures of the caseins in relation to their biological functions. Protein Eng. 1988. 2(4):251-259. PMID: 3074304","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[112-305]T$	BPD_transp_1
PS50928	$\"[116-297]T$	ABC_TM1

InterPro
IPR001588
Family

Casein, alpha/beta
PS00306	$\"[127-134]?$	CASEIN_ALPHA_BETA

noIPR
unintegrated

unintegrated
tmhmm	$\"[68-88]?$ $\"[123-141]?$ $\"[151-171]?$ $\"[181-201]?$ $\"[232-252]?$ $\"[276-296]?$	transmembrane_regions

","BeTs to 10 clades of COG0600COG name: ABC-type nitrate/sulfonate/taurine/bicarbonate transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0600 is a-mp----vd--bcef-hs--j-i--Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 159-229 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q87JW4_VIBPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 112 to 305 (E_value = 2.5e-24) place ANA_0783 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter, permease protein (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0784","827328","825835","1494","6.55","-1.60","53094","ATGACTGCCACTACCTATCAAGCCATCGCGATGATCGTCTATTTCGTGGCGATGCTCGCCATCGGGGGCTGGGCCTACCTACGAACGGACAACTTCGACGACTACATGCTCGCCGACCGCGACCTCAATCCATGGGTGGCGGCACTGTCGGCGGGAGCCTCGGACATGTCGGGGTGGCTGCTGATGGGACTGCCGGGAACCCTGTACGTCAGTGGACTGGTCGAGGGATGGATCGCCGTCGGACTGACGGTCGGGGCCCTGGCCAACTGGCTGCTGGTGGCTCCTCGTCTGCGCGCCTACACCGAGGTCGCCAACAATTCGATCACCGTCCCCAGCTTCCTGGACAACCGACTCCACGACACGCATCGGTTGCTGCGGTGGTCCAGTGGTCTCATTATTCTGGTCTACTTCACCTTCTACGTCTCCTCCGGCATGGTCGCCGGCGGCCGTTTCTTCGAGTCCTCCTTCGGAATGGACTATCGCCTCGGCATGGTCATCGTCGCCGCCATCACCGTGGTCTACACGCTGATCGGCGGGTTCCTGGCCGTGTCCTACACCGACTTCGTCCAGGGCGTCATGATGGTGACCGCCCTGGTCATGGTGCCCGTCGCGGGTGTCATTCGGCTCGGGGGACTGTCCAACCTGAGGCAGGCCATCGCCGAGGTCGACCCTCACTACTGGGTCATCTGGGGGCCGACGACGACGCTGCTCGGCGTCATCTCGGCGCTGGCCTGGGGCCTGGGCTACTTCGGCCAGCCGCACATCATCGTCCGGTTCATGGCCATCCGCAGCCCCAGGGAGGCCGTGGCCGGAGGCACCATCGGAATCGGCTGGATGCTCTTCGCCGTGCTCGGTGCAGCCGGCACCGCGATCGTGGGCGTGGCCACCTACCAGCACGACAAGAAGCAGCTGGCCGACCCGGAGACCGTCTTCATCACCCTGGGCAAGCTGCTCTTCCACCCGTTGGTCGCCGGATTCATGCTGGCTGCCATTCTGGCCGCCATCATGTCGACGATCTCCTCCCAGCTGCTCGTGACCTCCTCGGCGCTCATCGAGGACCTGTACGGTTCCTTCGCCCGCACCCGGGAGGAGAAGATCAGCGGCAACCGCATGGTGCTCTACTCACGCATGGCAGTCTTCGCCATCGCATTGGTCGCGGCGGTCATGGCCTGGAACCCCAGTAAAACGATCCTCGACCTCGTGGCCTTCGCCTGGGCCGGCTTCGGCGCCTCCTTCGGCCCCACCATTCTGCTGTCGCTGTACTGGAAGCGCTTGAGCGCCATGGGAGCCTTCGCCGGAATGATCACCGGGGCCGTCGTCGTCATGATCTGGGGGAACGTCTCCGGTGGCCCGGGCGGCGTCTTCGACCTCTACGAGATCGTGCCCGGATTCCTGAGCAACCTCGCTGTGGCCGTGGCCGTATCTCTCGCAAGTCAGCCCTCCAAGGAGATCTCCGAGGAGTTCGACGCCGCCGTTGCGGCCTCACGGGCGTAG","MTATTYQAIAMIVYFVAMLAIGGWAYLRTDNFDDYMLADRDLNPWVAALSAGASDMSGWLLMGLPGTLYVSGLVEGWIAVGLTVGALANWLLVAPRLRAYTEVANNSITVPSFLDNRLHDTHRLLRWSSGLIILVYFTFYVSSGMVAGGRFFESSFGMDYRLGMVIVAAITVVYTLIGGFLAVSYTDFVQGVMMVTALVMVPVAGVIRLGGLSNLRQAIAEVDPHYWVIWGPTTTLLGVISALAWGLGYFGQPHIIVRFMAIRSPREAVAGGTIGIGWMLFAVLGAAGTAIVGVATYQHDKKQLADPETVFITLGKLLFHPLVAGFMLAAILAAIMSTISSQLLVTSSALIEDLYGSFARTREEKISGNRMVLYSRMAVFAIALVAAVMAWNPSKTILDLVAFAWAGFGASFGPTILLSLYWKRLSAMGAFAGMITGAVVVMIWGNVSGGPGGVFDLYEIVPGFLSNLAVAVAVSLASQPSKEISEEFDAAVAASRA$","Solute:Na+ symporter; SSS family","Membrane, Cytoplasm","sodium:proline symporter","K03307 solute:Na+ symporter; SSS family","sodium/proline symporter","","Reizer J., Reizer A., Saier Jr M.H. The Na+/pantothenate symporter (PanF) of Escherichia coli is homologous to the Na+/proline symporter (PutP) of E. coli and the Na+/glucose symporters of mammals. Res. Microbiol. 1990. 141(9):1069-1072. PMID: 1965458Reizer J., Reizer A., Saier Jr M.H. A functional superfamily of sodium/solute symporters. Biochim. Biophys. Acta 1994. 1197(2):133-136. PMID: 8031825Jung H. The sodium/substrate symporter family: structural and functional features. FEBS Lett. 2002. 529(1):73-77. PMID: 12354616","","","

InterPro
IPR001734
Family

Na+/solute symporter
PTHR11819	$\"[9-405]T$	SODIUM/SOLUTE SYMPORTER
PF00474	$\"[35-437]T$	SSF
TIGR00813	$\"[35-437]T$	sss: transporter, solute:sodium symporter (
PS50283	$\"[4-451]T$	NA_SOLUT_SYMP_3
PS00456	$\"[157-182]?$	NA_SOLUT_SYMP_1
PS00457	$\"[419-439]T$	NA_SOLUT_SYMP_2

InterPro
IPR011851
Family

Sodium/proline symporter
TIGR02121	$\"[5-496]T$	Na_Pro_sym: sodium/proline symporter

noIPR
unintegrated

unintegrated
PTHR11819:SF12	$\"[9-405]T$	SODIUM/PROLINE SYMPORTER
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[9-27]?$ $\"[68-88]?$ $\"[124-144]?$ $\"[163-183]?$ $\"[188-208]?$ $\"[227-247]?$ $\"[268-297]?$ $\"[322-351]?$ $\"[372-392]?$ $\"[402-422]?$ $\"[427-447]?$ $\"[457-477]?$	transmembrane_regions

","BeTs to 19 clades of COG0591COG name: Na+/proline, Na+/panthothenate symporters and related permeasesFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism],RThe phylogenetic pattern of COG0591 is aompkzyq-d--bcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001734 (Na+/solute symporter) with a combined E-value of 9.3e-64. IPB001734A 36-64 IPB001734B 157-210 IPB001734C 244-285 IPB001734D 408-437","Residues 9-65 are 87% similar to a (TRANSMEMBRANE SYMPORTER COTRANSPORTER PERMEASE SODIUM/PROLINE TRANSPORTER SODIUM FAMILY PROLINE SODIUM:SOLUTE) protein domain (PD001069) which is seen in Q6NHV8_CORDI.Residues 77-156 are similar to a (TRANSMEMBRANE SYMPORTER SODIUM/PROLINE PERMEASE PROLINE SODIUM/PANTOTHENATE PANTOTHENATE AFFINITY HIGH SYMPORT) protein domain (PD449950) which is seen in Q8ERF3_OCEIH.Residues 159-212 are 75% similar to a (TRANSMEMBRANE SYMPORTER COTRANSPORTER PERMEASE SODIUM/PROLINE FAMILY SODIUM PROLINE TRANSPORTER SYMPORT) protein domain (PD186798) which is seen in Q8ERF3_OCEIH.Residues 221-336 are 76% similar to a (TRANSMEMBRANE SYMPORTER COTRANSPORTER SODIUM/PROLINE SODIUM PERMEASE PROLINE FAMILY TRANSPORTER SYMPORT) protein domain (PD000991) which is seen in Q8ERF3_OCEIH.Residues 337-424 are 75% similar to a (TRANSMEMBRANE SYMPORTER SODIUM/PROLINE PERMEASE COTRANSPORTER TRANSPORTER FAMILY PROLINE SODIUM SODIUM:SOLUTE) protein domain (PD477036) which is seen in P94392_BACSU.","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 437 (E_value = 3.4e-118) place ANA_0784 in the SSF family which is described as Sodium:solute symporter family.","","symporter (putP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0785","828102","827593","510","6.79","-0.67","18341","GTGATGACAAAGCCGCGGCTTCCAGATGCTCCACAGCCTTCCCCCGGTTCCGCTGTTCTGTCAGTGGGTACGGACCTGGTGCACATTCCGGGTTTCTCCGCCCAACTCGAGCAGCCCGGCAGCGTCTTCGCACAACGCGCCTTCACGGCGCGCGAGCTCCGAGAGGCCCGAGATCGTTCGGAGGAGAGGGGAACCAACCTGGCCCAGCACCTGGCAGCGCGATGGGCGGCCAAGGAGTCCTTCATCAAGGCCTGGAGCCAGGCACACGTTCTGTGTGCAAAAAGTCGCGGAACGAGTACCTCTCCGGTTATCCTGGCCGAGGACGTCGACTGGCGTGAGATCGAGGTTGTCACCGATCGGTGGGGCCGGCCTTCTTTGCGCCTGAGCGGCACCGTTGCCCAAGCTGTTGAGCACAGCCTCGGAGAGGAGGTATCAACCCCAGGGTGTTGGCCGGTTTCCTTGAGCCATGACGGTGACTACGCCGCGGCCATCGTCCTTCACGTGCGTTGA","VMTKPRLPDAPQPSPGSAVLSVGTDLVHIPGFSAQLEQPGSVFAQRAFTARELREARDRSEERGTNLAQHLAARWAAKESFIKAWSQAHVLCAKSRGTSTSPVILAEDVDWREIEVVTDRWGRPSLRLSGTVAQAVEHSLGEEVSTPGCWPVSLSHDGDYAAAIVLHVR$","4'-phosphopantetheinyl transferase","Cytoplasm, Periplasm","Holo-[acyl-carrier protein] synthase (Holo-ACPsynthase)(4'-phosphopantetheinyl transferase acpS)","4'-phosphopantetheinyl transferase ","4'-phosphopantetheinyl transferase","","Lambalot R.H., Walsh C.T. Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J. Biol. Chem. 1995. 270(42):24658-24661. PMID: 7559576Reuter K., Mofid M.R., Marahiel M.A., Ficner R. Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily. EMBO J. 1999. 18(23):6823-6831. PMID: 10581256","","","

InterPro
IPR004568
Domain

Phosphopantethiene-protein transferase
PD004282	$\"[25-166]T$	Q74C71_GEOSL_Q74C71;
TIGR00556	$\"[18-168]T$	pantethn_trn: phosphopantethiene--protein t

InterPro
IPR008278
Domain

4'-phosphopantetheinyl transferase
PF01648	$\"[22-91]T$	ACPS

","BeTs to 11 clades of COG0736COG name: Phosphopantetheinyl transferase (holo-ACP synthase)Functional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0736 is ------yqvdrlb-e-g--nujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB008278 (4'-phosphopantetheinyl transferase) with a combined E-value of 4.7e-06. IPB008278A 22-31 IPB008278B 75-86","Residues 20-83 are 70% similar to a (SYNTHASE TRANSFERASE FATTY ACID ACPS HOLO-ACYL-CARRIER-PROTEIN 4_apos;-PHOSPHOPANTETHEINYL SYNTHESIS HOLO-ACP MAGNESIUM) protein domain (PD699989) which is seen in ACPS_CORGL.Residues 22-137 are 54% similar to a (WITH SYNTHASE HOLO-ACYL-CARRIER) protein domain (PD782840) which is seen in Q8G455_BIFLO.Residues 25-166 are 46% similar to a (SYNTHASE TRANSFERASE HOLO-ACYL-CARRIER-PROTEIN HOLO-ACP FATTY ACID 4_apos;-PHOSPHOPANTETHEINYL SYNTHESIS MAGNESIUM BIOSYNTHESIS) protein domain (PD004282) which is seen in Q74C71_GEOSL.Residues 84-164 are 55% similar to a (TRANSFERASE SYNTHASE ACPS 4_apos;-PHOSPHOPANTETHEINYL FATTY SYNTHESIS HOLO-ACP MAGNESIUM BIOSYNTHESIS HOLO-ACYL-CARRIER-PROTEIN) protein domain (PD703439) which is seen in ACPS_COREF.Residues 102-163 are 62% similar to a (SYNTHASE TRANSFERASE ACPS BIOSYNTHESIS HOLO-ACYL-CARRIER-PROTEIN ACID 4_apos;-PHOSPHOPANTETHEINYL LIPID FATTY SYNTHESIS) protein domain (PD865350) which is seen in ACPS_CORGL.","","No significant hits to the PDB database (E-value < E-10).","Residues 22 to 91 (E_value = 1.5e-12) place ANA_0785 in the ACPS family which is described as 4'-phosphopantetheinyl transferase superfamily.","","protein] synthase (Holo-ACP synthase)(4-phosphopantetheinyl transferase acpS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0786","837683","828240","9444","5.04","-123.65","328437","GTGCACACGAACTCGCAAGCCCCCAGCCCCGCGACCACCATCGCTGAGCGCCTGAGCGGAGGCGAGCCCTACATCATCACCTTCGGCGGCCAGGCCACCCCCTGGCGCCAGACGCTGGCCGACCTGGTTTCCCTGGACCACGCCCTGGCCGCTGACGTCGTGGCGGTCGACCGGGCCGTGGCCGAGCGTCTGGCCCCCGTATCCACCGACTTGCTCACCGTGACCCCGCGCGGCTCGAGGCTCCTGGACGACGAGGCGGCCCCGGTCTCCCCTCAGCACCGCACCACCGCCGACGGCGCCGATGTCTCCGTGCCCGGCATCCTCGTGGCCCAGCACGCCGCCCTAGCCTCCCTGCCCGGCGCCGGCATCGACCCGGCCGCCCACGCCCCGGTGAGCGCCATCGGCCACTCCCAGGGTGTCCTGGGCGTCAGCCTGCTCCAGGCTGTGCAGGCCGGCGAGCGCGAGCGCGTCATCGAGGTCCACGCCATCGCCCGCCTCATCGGTGCGGCGGCCACCCGCACCACCCGCCGCCTCGACCTGGGCACGGTGGGGGAGTCCACCCCGATGCTCTCGGTGCGCGGCGTCACCCGCAGCGTGCTCGACGCCGTCCTGGCCCGAGTCCCCGGCTCGGAGCGGATCTCCGTGGGCGTGACCAACGGCCGTCAGGCGCACATCCTCTCCGGGCGCCCGGCCGACCTCGAGGCCGTCGTCACCGCGCTGGAGGCCGCCGCCGCCCGCAGCGCCAAGGCCCGTAAGGACCGCCGCCGCGGGGGTGCCGTGCTGGCCCCGGTCACCGAGTTCCTCACCACCTCGGTCCCCTTCCACACCCCGCTGCTCGCCGGTGCCGTCGACGACGTCGCCGCCTGGGCGGCCGCCTGCGGCCTGAACGAGAAGCTCGCCCGCGACCTGGCCACCGCCGTGCTCATCGACCCGGTCGACTGGCCCGGTCTGGTCACCGAGGCCCTCGCAGCCGGATCGGACGCACCGGTGCGCACCGTCCTGGACCTGGGACCGGGCAACGTCCTGGTCCGCCTCACCGAGGGCGTCGTGGCCGGCACCGGCACCACCGTCGTGCCCGCCGGGACCGCCAAGGCCATCGACGACCTCGACCGCGCCGGCGCGGCCCCCCGTCCCGGCGTCGACCGCTCCCGCTTCGCCCCGCGCATCACCCGCCTGCCCGACGGCCGCCTCACCCTGGACACCGCCTTCACCCGCCTGACCGGGCGCAGCGCGGTACTCCTGGCGGGAATGACCCCCACCACCGTGGATCCCGCCATCGTGGCTGCCGCCGCCAACGCCGGCTACTGGGCCGAGCTCGCCGGCGGGGGCCAGACCACTCCCGCCGTCCTGACCGAAAACCTCGAGGGCCTGGAGAAGGCCCTCGAGCCCGGGCGCACCGCGGCCTTCAACGCCATGTTCATGGACCGCTACCTGTGGAACCTGCACCTGGGGACCCAGCGCCTGCTGTCCAAGGCCCGCGCCGGGGGCGCCCCCATCGACGGCATCACCATCTCCGCCGGGATTCCCGAGCTCGAGGAGGCCACCGCCCTGCTCGAGCGCCTCCACGCCGAGGGCTTCCCCTACATCGCCTTCAAGCCCGGCACCGTGGACCAGATCCGTCAGGTCCTGGCCATCGCCCGCGCCGTGCCCGACAGCCCCGTCATCATCCAGATCGAAGACGGACACGCCGGTGGCCACCACTCGTGGGAGGACCTGGACACCATGCTCCTGGCCACCTACGACGCCATCCGCGCCGTGACCAACGTGGTGCTCGTCGTCGGCGGCGGCATCGGTACGCCCACTCGCGCCGCCGACTACCTCACCGGCCGCTGGGCCGAGGCCTACGGCACGGCTGCCGCCCCCGTCGACGGTGTCATGATCGGCACCGCCGCCATGACCTGCCTGGAGGCCAAGACCAACGACGACGTCAAGCAGCTCCTTGTCGACACCCCTGGAATCCCCGAGGACTCCGGGGTCGAGGGCGGCTGGGTCGCCTCCGGGGAGTCCATCGGTGGGATGACCTCCGGACTGTCCCACCTACGTGCCGACCTCTACGAGATCGACAACTCCTCGGCCCGGGCCTCCCGCCTCATCCAGGAGCTAGCCGGTGACGAGGCCGCCATGGCCGCACGCCGCCAGGAGATGATCGACGCCCTGGCCAAGACCGCCAAGCCCTACTTCGGCGACGTCGAGGAGATGACCTACCTTCAGTGGGCCACCCGCTACGCCGAGCTGTGCGTCGCCCCCCACGAGGGGCGCAGCGCCACCCGCGCCGACTGGGCCGACGAGGGCTGGTACGACCGCTTCATCGACCTGCTGCACCGCATCGAGGCCCGCCTGAGCCGGGCTGACCACGGCGAGATCCCCACGCTCTTCGCCGACTACGACGCCGTCATCGACTCCGACGCCGCCCTGGCCGCACTGGCCGAGCACTACCCGTCGGCCGCCTCCACCCTCGTGGAGCCCGTCGACGCCGCCTGGTTCGTCGACCTGTGCCGCAAGCACCCCAAGCCCGTGCCCTTCGTGCCCGTGGTCGATGCCGACATCCTGCGCTGGTGGGGCACCGACTCCCTGTGGCAGTCCCAGGACCCGCGCTACACCGCTGACCAGGTGCGCATCATCCCCGGTCCGGTCGCCGTTGCCGGCATCACCACCATCAATGAGCCGGTCGGCGAGCTGCTGGGCCGCTTCGAGACCGCCGCCGTCGAGGCCCTCCAGGAGGCCGGCACGGGTGAGCAGGAGGCCGCCGGCCGCCTGGGCGCAGCCCCCGCCGTGGCCGACGGCGTCCTGGCAGCTCCCGTGGCCGACGCCAAGGAACTCGTCCAGGTGGCCCCCCACGTCCTGTGGAACGGCCACCTGACGGTCAACCCGGCCACCGTCCTGGACGACGACGCCTACAACGTCGTCGCCCGCCCGGACGTGGCCGAGGACGCCTACGACCTCGACATCCGCCTCGACACCCACTGGGACGGCACTCCCGGCGGAGATGAGATCCACGCCGTGCGCCGCCTCGTCGTGCCGCTGCGCCTGGCCCGCGCCTGGGACGGTGCCGCTCCACTGGTCGACCCCGAGCGCATCAGCGAGACGATGAACGACCTGCTGCGGGCCACCGCCGGCGTGGGGGCCGTGTCCATCACAGGAGACGACGTCGACCACCTGCCCGAGGTCCGCCCCGCGCAGGCCGGGGCCACAGACGTCCTGGGACGCCCCACCACCCAGCCCTTCGGCACCATCCACGGCTCCTTCACCCTGGCAAGCACCCTGGGCCACGACCACGCCTCGGTGACCGCCGACGCCCTGCCATCGGACCTGTCCGCCGCGCCCTTCGTGCCCGACGCCCTGCTCGGCCCCTGCTGGCCGGTGGTCTACGCCGCCCTGGGCAGCGTCGTCGAGGACGGCATGCCGCTCATCGAGGGCCTGCTCGGTGCCGTCCACCTGGACCACACCATCGACCTGCACCTCACCCTCCACCAGCTCCAGGAGGCCGCAGCCACGACCAGCCCCACGATCAACGTCACCGGCTGGGTCGCCGCCCTGGAAGAGTCCAGCGCCGGCCGCGTCGTCGACGTGCGCCTGGAGCTGACCGACGCCACCGACGGCACCGTGGTGGCACTCATGCGTGAGCGCTTCGCCATCCGCGGCCGCGCCTCCGGCAACGCCGTGCCCAGCGCCCCCGAGCTCGCCGGCGGCACCGGACGCGAGACGGCCCCGGCCGCACGCCGCATCCTGCGCCGCACCACCGTCACCGCGCCCGCGGACATGACTGCGTTCGCCCGGGTCACCGGTGACTTCAACCCGATCCACACCTCCTACAATGCCGCCCACGTGGCCGGCATGGAGGCCCCGCTCGTCCACGGCATGTGGCTGTCGGCCACCGCCCAGCAGGTGGCGGCCTCCACCGCGGCCGACGGCTCGCGCCACGTCCTGGCCGGCTGGACCTACGTCATGACCGGTCCGGTCGAGCTGAGCGACGACGTCGAGATCACCGTGGAGCGCACCGGCCTGGTGGTCGGCGGCGGCTACGTCCTGGAGGTCGTCTGCCGCATCAACGGCGAGGTCGTCTCCCGCGGCACTGCCGTGACGACGCCCGAGCCCACCGCCTACGTCTACCCCGGCCAGGGCATCCAGGCCCCCGGCATGGGCCTGGACGAGATGAACTCCTCCAAGGCCGCCCGGGAGATCTGGGAGCGGGCCGATGCCCACACCCGTGCCGAGCTGGGCTTCTCCGTCATCAACCTGGTGCGCGACAACCCCACCGAGATGACCGCCCGCGGCGTCACCTACCGCCACCCCGAGGGCCTGCTCAACCTCACCCAGTTCACCCAGGTGGCTCTGGCCACCGTCGCCATGGCGACCACTGCGCGCCTGGCCGAGGCCGGTGCCCTCGTGGACAGCGCCGCCTTCGCCGGCCACTCCCTGGGCGAGTACACGGCGCTGAGCGCCTACGGGCGCGTCATGCCCGTAGAGACGACCATCTCGATCGTCTTCCAGCGTGGCTCCACCATGCACTCGCTGGTGCCCCGTGACGCCGACGGCGCCTCGAACTACCGCATGGGCGCGCTGCGCCCCAACCAGGCGGGCATCAAGGCCGACGAGGTCGAGGCATACGTGCGCTCGATCTCCGAGGCCACCGGAGAGTTCCTCCAGATCGTCAACCACAACCTGGCCGGCGTGCAGTACGCCGTGGCCGGCACGATCAAGGGCCTGGACGCCCTGGCCACCGACGCCCGCGCCAAAGCCAAGGCCCGCGGGGGCAAGAACCCCTTCATGTTCGTCCCCGGCATCGACGTGCCCTTCCACTCCGAGGTGCTGCGCCCCGGCGTGCCGGAGTTCCGTGGCCGCCTGCTCGAGCTTGTCCCCGAGGACCTGGACGTTGCGCGCTTGGTGGGCCACTACGTGCCCAACCTGGTGGCCCGGCCCTTCGCCCTGACCCAGGACTTCGCCCGTTCGATCCTTGAGGTCGTACCCTCTGAGCCCGTCGAGGAGATCCTGGCCGACTGGGACTCCTGGGCGAAGCGCCCCACGGAGCTGGCCCGTGTCCTGCTCGTAGAGCTCCTGGCCTGGCAGTTCGCCTCCCCGGTGCGCTGGATCGAGACCCAGGAGGTCCTGCTGGCCTCCCCGAGCGAGGGCGGCCTGGGGATCGAGCACATCGTCGAGGTGGGCCTGGCCAATTCACCCACCCTGGCGAACCTGGCCGCCAACACCCTGCGTCTGCCCCAGCACGCCGGTCGCCACGTCACCGTGCACAACGCTCGCCGCGACGAGGCACGGGTGCTGGCCACCGACACCGACCCGGCCGTCGAGCTCACCGAGCCGGACTTCGATGTTCCGGCTGCCGAGGAGCCGGCTGCTGAGGCCGAGGCTCCTGCGCAGAGCGCTGCAGCCGAGCAGGCTCCCGCCCCCGCGGCCGAGGCCGCACCGGCTCCGGCCGCCGGCGGACCGGTGGACGACCTTCACTTCGGTGCGACCGATGCCCTGACGGTGCTCCTGGCCCACGCCTCGCGCATCCGTCCCGAACAGATCGGTGCCACGGACACCACCGAGACGCTCACTAACGGAGTCTCCTCGCGCCGTAACCAGCTCCTCATGGACCTGGGCACCGAGCTCGAGCTCGCCTCCATCGACGGTGCCGCTGACGCCGACATGACGGCCCTGGCCGCCACGGTCGCCAAGGGCGCTCCCGGTTACAAGGCCTTCGGTCCGGTCCTCACCGAGGCCATCCGCGTGGGGCTGGGCCGGCTCCTGGGCCCCTCCGGCGTGCGCGCCTCCCGTATCGCCGACCGCGTCACCGGCACCTGGGGACTGGGGCAGGGCTGGGTCTCCCACGTGACCGCCGCCCTGTTCCTGGGCACCCGGGAGGGCGCCTCGATGCGCGGCGAGGACCTGGCCTCCCTGGGCTCCTCGGCCCCGCTGACCAGTGCGAGCGCCGTGGACTCCCTCATCGACTCCGCCGTCCAGGCCGTCGCCGCCGACCACGGTGTGAGCGTCGCCAAGCCGAGCGCCGGAGGTGCCGGGGGCGCAGTGGTCGACTCCGCGGCCCTGGACGCCTTCGCCCAGAGCGTCACCGGCTCCGAGGGCGTCCTGGCCACCACGGCCCGCACCCTCCTGGACGCCCTGGGGCTGGCCGAGAAGGCCACTGTCCCGGCTGATGCCGACGACGAGGCCTCCCGTACCCGGGCCGCCATGGCCGCCCTGGACGCCGAGCTCGGCGCCGGATGGGTCAAGTCCGTCACCCCGGCCTTCGCCCCAGAGCGCGCCGTCCTCATCGATGACCGCTGGGCCACGGCCCGTGAGGACGTCGCCCGACTCGGCTCCGGCGAGACCGACCTGGACGCCTCCCGCCGGCTCCTGGCCCCCGAGCGCTTCGTGGGTCTGGGACAGGCAGTGGCCGATCACGCCACCTGGTGGGCCAAGCAGGCCAAGGCCTCCGACCTGGCCGACGGCGCCGAGCGCACCGCCGTCCTGACCGCGATCGCCCAGGCCGCGCCGAAGACCCCGCAGGCCGGTGACGCCACGGTGCGCTGGTCCGAGGACGTCGCCGTCGTCACAGGTGTGGCCCCCGGGTCCATCGCCGCGGCCGTCGTCGGAGAGCTGCTGGCCGGTGGCGCCACCGTGGTGGCCACCAGCTCGCGCCTGACCCACGAGCGCCTCGAGTTCGCCACCACCCTGTACCGCGAGCACGCCGCAGCCGGCGCCAAGCTGTGGATGGTTCCCGCGAACCTGTCCTCCTACCGGGACGTCGACGCCCTGGCGGAGTGGATCGGCAACGACCAGGTGGTCACCTCCGGCGGCTCCACCAAGGTCGTCAAGGAGGCCCTGGTTCCCACCCTCCTGTTCCCCTTCGCCGCGCCGCGCGTCTCAGGCACGCTGGCCGACGCCGGCCCCACGGCCGAGTCCCAGACCCGCCTGCTGCTGTGGTCGGTGGAGCGCACCATCGCCTCCCTGAGCGCCATCGGCACCGACACCCACGTCGACCACCGCCTGCACGTGGTCCTGCCCGGCTCCCCGAACCGGGGCACCTTCGGCGGTGACGGCGCCTACGGCGAGGTCAAGTCCGCCCTGGACGCGATCGTCAACCGCTGGTCCTCGGAGCGGGCCTGGGCCCAGCGCGTCACCCTGGCCCACCCGCGCATCGGCTGGGTCAAGGGCACCGGCCTCATGGGCGGTAACGACCCGCTCGTCGCCGCCGTCGAGGCAGCCGGGGTGCGCACCTGGACCACGGAGGAGATCGCCTCCGAACTCACCGGCCTGTGCACCACCGAGGTGCGCACCCAGGCGGCTCAGGCCCCGGTGAACGCCGACCTCACGGGGGGACTGGGTGACGACATCGACCTGGTGGCCCTGCGTGAGAACGCCGCCGCGCAAGCCGCTGCGCCCGCCGAGGAGACCGAGGCCCCGGCCGTCATCAAGGCCCTGCCCACCCCCGTTGTCCCGACCCAGCCCACCGCCCCCCAGTGGGGCGAGGTGAGCGCCGACCTCGATGACCTGGTCGTCATCATCTCCACCGGAGAGGTCTCCACCTGGGGATCGGGCCGTACGCGCCGCGAGGCCGAGCTGGGAATGAGCGGCGGCGAGGACGTCGACCTGACCGCCGCCGGTGTCCTCGAGCTCGCCTGGGGCATGGGTCTGCTCACCTGGCAGGACAGCCCCAAGGCCGGCTGGTACGACACCGACGGGGAGATGGTCGAGGAGTCCGACATCCTGGAGCGCTACCGCGACGAGGTCGTGGCCCGCTGCGGTATCCGCGAGTTCGTCGACGACGGCGTCATCGCGCCGATCGCCGACGAGGAGGTCACCGTCTACCTCGACCGCGACATCACCCTGTCGGTTCCTGACGAGACCACGGCCCGCACCATCGAGGCCTCCGACCCCGAGCACACGCTCGTGGTTCCCGACGCCGAGACCGGCGAGTGGACCGTCACCCGACTGGCCGGCTCACTGGCCCGGGTGCCGCGACGCGCCGCGCTGTCGCGCACGGTCGGCGGCCAGTTCCCGCGCGACTTCGACCCGGAGCGCTGGGGCATCCCCGCCTCGATGACCCAGGGCATGGACCCCATCGCCTCCTGGAACCTGGTCACCGCCGTCGACGCCTTCCTGTCGGCCGGCTTCACCCCGGCCGAGCTCCTCAAGGCCGTCCACCCCTCCGACGTGGCCTCCACGCAGGGCACCGGGTTCGGTGGCATGGAGTCGATGCGCAAGATGTTCGTCGGCCGGTTCCTTGGGGAGGAGCGTCCCAGCGACATCCTCCAGGAGGCCCTGCCCAACGTCGTGGCCGCCCACGTCATGCAGTCCTACATCGGCGGCTACGGCGCCATGGTCCAGCCGGTGAGCGCCTGCGCCACCGCGGCCGTCTCCATTGAGGAGGGCTGGGACAAGATCGCCCTGGGCAAGGCCGACGTCGTCGTGGCCGGCGCCATCGACGACATCTCGATCGAGTCGGTCGTCGGCTTCGGCAACATGAACGCCACCGCGGAGGCCGCGGCCATGCGCGCCAAGGGCATCTCCGACCGCCACTTCTCGCGTGCCAACGACCGCCGTCGCGGCGGATTCGTGGAGGCCGAGGGTGGCGGCACGGTGATCCTGGCCCGTGGCTCGGTGGCGGCCCGCATGGGGCTGCCGGTGGCCGGTGTGGTCGGTTTCGTCTCCTCCTACGCCGACGGCGCCCACACCTCGATCCCGGCACCCGGCCTGGGCGCCCTGGGCGCCGGCCGCGGCGGGCGCAGCTCGCGCCTGGCCAAGGCCCTGGCGGCCCTGGGTGTGGAGGCCGACGACATCGCACTGGTCTCCAAGCACGACACCTCCACCGGTGCCAACGACCCCAACGAGTCCGAGCTGCACACGCGTCTGGCGCGCGCCCTGGGACGCTCCGAGGGCAACTCGCTGGTGGCGGTCTCGCAGAAGACCATCACCGGTCACGCCAAGGGCGGTGCCGCCGTCTTCCAGGTCGCGGGCCTGACCGAGATCCTCGCCTCCGGTGTGGCTCCCGGTAACGCCTCCCTGGACGTTGTGGACGCCCCCCTGGCCAAGGACGCCTTCTGGGTGTGGCCGCGCAGGCCCATCCGTCTGGCCGGTCGTGGTGGCCAGGACGGGCGCGTCCCGGGCGCCGGCCCGGTGCGAGCCGGTCTGCTGACCTCGCTGGGCTTCGGACACGTCTCCGGCCTCATCGCGATCGTCCACCCCGGTGCCTTCGAGGCCGCCCTGCGGCAGGCCGAGGGCCAGGAGGCGGTTGACGCCTGGCTGGCCTCAGCCAATGCCCGCCTGGCCGCCGGCACTAGGCGCCGCCGCGCAGGCATGATCGGTCGGGCCCCGCTGTTCGAGCAGGTTCAGGGCCGTCGTCTGGGGGAGGAGTCCAAGCAGCGCGACCCGCATGAGGTCGAGGCCGCCATGCTGCTCGACCCTGATGCTCGTCTGGGCTCCGACGGCGTCTACCACGCGGGGGAGTAA","VHTNSQAPSPATTIAERLSGGEPYIITFGGQATPWRQTLADLVSLDHALAADVVAVDRAVAERLAPVSTDLLTVTPRGSRLLDDEAAPVSPQHRTTADGADVSVPGILVAQHAALASLPGAGIDPAAHAPVSAIGHSQGVLGVSLLQAVQAGERERVIEVHAIARLIGAAATRTTRRLDLGTVGESTPMLSVRGVTRSVLDAVLARVPGSERISVGVTNGRQAHILSGRPADLEAVVTALEAAAARSAKARKDRRRGGAVLAPVTEFLTTSVPFHTPLLAGAVDDVAAWAAACGLNEKLARDLATAVLIDPVDWPGLVTEALAAGSDAPVRTVLDLGPGNVLVRLTEGVVAGTGTTVVPAGTAKAIDDLDRAGAAPRPGVDRSRFAPRITRLPDGRLTLDTAFTRLTGRSAVLLAGMTPTTVDPAIVAAAANAGYWAELAGGGQTTPAVLTENLEGLEKALEPGRTAAFNAMFMDRYLWNLHLGTQRLLSKARAGGAPIDGITISAGIPELEEATALLERLHAEGFPYIAFKPGTVDQIRQVLAIARAVPDSPVIIQIEDGHAGGHHSWEDLDTMLLATYDAIRAVTNVVLVVGGGIGTPTRAADYLTGRWAEAYGTAAAPVDGVMIGTAAMTCLEAKTNDDVKQLLVDTPGIPEDSGVEGGWVASGESIGGMTSGLSHLRADLYEIDNSSARASRLIQELAGDEAAMAARRQEMIDALAKTAKPYFGDVEEMTYLQWATRYAELCVAPHEGRSATRADWADEGWYDRFIDLLHRIEARLSRADHGEIPTLFADYDAVIDSDAALAALAEHYPSAASTLVEPVDAAWFVDLCRKHPKPVPFVPVVDADILRWWGTDSLWQSQDPRYTADQVRIIPGPVAVAGITTINEPVGELLGRFETAAVEALQEAGTGEQEAAGRLGAAPAVADGVLAAPVADAKELVQVAPHVLWNGHLTVNPATVLDDDAYNVVARPDVAEDAYDLDIRLDTHWDGTPGGDEIHAVRRLVVPLRLARAWDGAAPLVDPERISETMNDLLRATAGVGAVSITGDDVDHLPEVRPAQAGATDVLGRPTTQPFGTIHGSFTLASTLGHDHASVTADALPSDLSAAPFVPDALLGPCWPVVYAALGSVVEDGMPLIEGLLGAVHLDHTIDLHLTLHQLQEAAATTSPTINVTGWVAALEESSAGRVVDVRLELTDATDGTVVALMRERFAIRGRASGNAVPSAPELAGGTGRETAPAARRILRRTTVTAPADMTAFARVTGDFNPIHTSYNAAHVAGMEAPLVHGMWLSATAQQVAASTAADGSRHVLAGWTYVMTGPVELSDDVEITVERTGLVVGGGYVLEVVCRINGEVVSRGTAVTTPEPTAYVYPGQGIQAPGMGLDEMNSSKAAREIWERADAHTRAELGFSVINLVRDNPTEMTARGVTYRHPEGLLNLTQFTQVALATVAMATTARLAEAGALVDSAAFAGHSLGEYTALSAYGRVMPVETTISIVFQRGSTMHSLVPRDADGASNYRMGALRPNQAGIKADEVEAYVRSISEATGEFLQIVNHNLAGVQYAVAGTIKGLDALATDARAKAKARGGKNPFMFVPGIDVPFHSEVLRPGVPEFRGRLLELVPEDLDVARLVGHYVPNLVARPFALTQDFARSILEVVPSEPVEEILADWDSWAKRPTELARVLLVELLAWQFASPVRWIETQEVLLASPSEGGLGIEHIVEVGLANSPTLANLAANTLRLPQHAGRHVTVHNARRDEARVLATDTDPAVELTEPDFDVPAAEEPAAEAEAPAQSAAAEQAPAPAAEAAPAPAAGGPVDDLHFGATDALTVLLAHASRIRPEQIGATDTTETLTNGVSSRRNQLLMDLGTELELASIDGAADADMTALAATVAKGAPGYKAFGPVLTEAIRVGLGRLLGPSGVRASRIADRVTGTWGLGQGWVSHVTAALFLGTREGASMRGEDLASLGSSAPLTSASAVDSLIDSAVQAVAADHGVSVAKPSAGGAGGAVVDSAALDAFAQSVTGSEGVLATTARTLLDALGLAEKATVPADADDEASRTRAAMAALDAELGAGWVKSVTPAFAPERAVLIDDRWATAREDVARLGSGETDLDASRRLLAPERFVGLGQAVADHATWWAKQAKASDLADGAERTAVLTAIAQAAPKTPQAGDATVRWSEDVAVVTGVAPGSIAAAVVGELLAGGATVVATSSRLTHERLEFATTLYREHAAAGAKLWMVPANLSSYRDVDALAEWIGNDQVVTSGGSTKVVKEALVPTLLFPFAAPRVSGTLADAGPTAESQTRLLLWSVERTIASLSAIGTDTHVDHRLHVVLPGSPNRGTFGGDGAYGEVKSALDAIVNRWSSERAWAQRVTLAHPRIGWVKGTGLMGGNDPLVAAVEAAGVRTWTTEEIASELTGLCTTEVRTQAAQAPVNADLTGGLGDDIDLVALRENAAAQAAAPAEETEAPAVIKALPTPVVPTQPTAPQWGEVSADLDDLVVIISTGEVSTWGSGRTRREAELGMSGGEDVDLTAAGVLELAWGMGLLTWQDSPKAGWYDTDGEMVEESDILERYRDEVVARCGIREFVDDGVIAPIADEEVTVYLDRDITLSVPDETTARTIEASDPEHTLVVPDAETGEWTVTRLAGSLARVPRRAALSRTVGGQFPRDFDPERWGIPASMTQGMDPIASWNLVTAVDAFLSAGFTPAELLKAVHPSDVASTQGTGFGGMESMRKMFVGRFLGEERPSDILQEALPNVVAAHVMQSYIGGYGAMVQPVSACATAAVSIEEGWDKIALGKADVVVAGAIDDISIESVVGFGNMNATAEAAAMRAKGISDRHFSRANDRRRGGFVEAEGGGTVILARGSVAARMGLPVAGVVGFVSSYADGAHTSIPAPGLGALGAGRGGRSSRLAKALAALGVEADDIALVSKHDTSTGANDPNESELHTRLARALGRSEGNSLVAVSQKTITGHAKGGAAVFQVAGLTEILASGVAPGNASLDVVDAPLAKDAFWVWPRRPIRLAGRGGQDGRVPGAGPVRAGLLTSLGFGHVSGLIAIVHPGAFEAALRQAEGQEAVDAWLASANARLAAGTRRRRAGMIGRAPLFEQVQGRRLGEESKQRDPHEVEAAMLLDPDARLGSDGVYHAGE$","Fatty acid synthase","Cytoplasm","type I multifunctional fatty acid synthase","fatty acid synthase","domain of unknown function DUF1729","","Si K., Maitra U. The Saccharomyces cerevisiae homologue of mammalian translation initiation factor 6 does not function as a translation initiation factor. Mol. Cell. Biol. 1999. 19(2):1416-1426. PMID: 9891075Sugino H., Sasaki M., Azakami H., Yamashita M., Murooka Y. A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene. J. Bacteriol. 1992. 174(8):2485-2492. PMID: 1556068","","","

InterPro
IPR001227
Domain

Acyl transferase region
G3DSA:3.40.366.10	$\"[22-352]T$ $\"[1364-1737]T$	no description

InterPro
IPR002539
Domain

MaoC-like dehydratase
PF01575	$\"[1234-1353]T$	MaoC_dehydratas

InterPro
IPR003965
Domain

Fatty acid synthase
PR01483	$\"[401-421]T$ $\"[427-445]T$ $\"[532-550]T$ $\"[552-571]T$ $\"[729-747]T$ $\"[836-860]T$ $\"[1251-1273]T$ $\"[1273-1294]T$ $\"[1358-1377]T$ $\"[1379-1402]T$ $\"[1460-1479]T$ $\"[1496-1517]T$	FASYNTHASE

InterPro
IPR013565
Domain

Domain of unknown function DUF1729
PF08354	$\"[837-894]T$	DUF1729

InterPro
IPR014030
Domain

Beta-ketoacyl synthase, N-terminal
PF00109	$\"[2667-2867]T$	ketoacyl-synt

InterPro
IPR014031
Domain

Beta-ketoacyl synthase, C-terminal
PF02801	$\"[2875-3001]T$	Ketoacyl-synt_C

InterPro
IPR014043
Domain

Acyl transferase
PF00698	$\"[1367-1490]T$	Acyl_transf_1

noIPR
unintegrated

unintegrated
G3DSA:3.10.129.10	$\"[1244-1364]T$	no description
G3DSA:3.40.47.10	$\"[2652-2878]T$ $\"[2881-3057]T$	no description
G3DSA:3.40.50.720	$\"[2169-2254]T$	no description
PTHR10982	$\"[1366-1625]T$	MALONYL COENZYME A-ACYL CARRIER PROTEIN TRANSACYLASE-RELATED
PTHR10982:SF4	$\"[1366-1625]T$	MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE

","BeTs to 14 clades of COG0304COG name: 3-oxoacyl-(acyl-carrier-protein) synthase IFunctional Class: IThe phylogenetic pattern of COG0304 is ----YqvCEBRhuj----inxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 98-261 are 54% similar to a (TRANSFERASE SYNTHASE ACID ACYLTRANSFERASE FATTY FATTY-ACID I FAS SYNTHETASE OXIDOREDUCTASE) protein domain (PD120470) which is seen in Q73XH7_MYCPA.Residues 268-363 are 60% similar to a (TYPE TRANSFERASE I FATTY SYNTHASE ACID MULTIFUNCTIONAL) protein domain (PDA1C9U4) which is seen in Q8G456_BIFLO.Residues 299-528 are 62% similar to a (SYNTHASE ACID FATTY TRANSFERASE SUBUNIT ACYLTRANSFERASE BETA HYDROXYPALMITOYL-ACYL-CARRIER-PROTEIN INCLUDES: DEHYDRATASE) protein domain (PD712063) which is seen in Q7TYD8_MYCBO.Residues 530-870 are 72% similar to a (SYNTHASE ACID FATTY TRANSFERASE SUBUNIT ACYLTRANSFERASE BETA HYDROXYPALMITOYL-ACYL-CARRIER-PROTEIN INCLUDES: DEHYDRATASE) protein domain (PD010153) which is seen in Q6NFP1_CORDI.Residues 659-757 are 56% similar to a (SYNTHASE TRANSFERASE ACID FATTY) protein domain (PD139751) which is seen in Q48926_MYCBO.Residues 888-991 are 77% similar to a (SYNTHASE ACID FATTY TRANSFERASE SUBUNIT ACYLTRANSFERASE BETA HYDROXYPALMITOYL-ACYL-CARRIER-PROTEIN INCLUDES: DEHYDRATASE) protein domain (PD682090) which is seen in Q8G456_BIFLO.Residues 1022-1184 are 57% similar to a (SYNTHASE TRANSFERASE ACYLTRANSFERASE FATTY-ACID I ACID FATTY OXIDOREDUCTASE TYPE LYASE) protein domain (PD609205) which is seen in Q8G456_BIFLO.Residues 1198-1338 are 57% similar to a (TRANSFERASE SYNTHASE ACID ACYLTRANSFERASE FATTY FATTY-ACID I FAS SYNTHETASE OXIDOREDUCTASE) protein domain (PD043822) which is seen in Q6XXM0_MYCSM.Residues 1341-1373 are 87% similar to a (FATTY SYNTHASE ACID OXIDOREDUCTASE DEHYDROGENASE TRANSFERASE MULTIFUNCTIONAL SUBUNIT INCLUDES: DEHYDRATASE) protein domain (PD281161) which is seen in Q8FR52_COREF.Residues 1409-1463 are 63% similar to a (TRANSFERASE SYNTHASE ACID ACYLTRANSFERASE FATTY FATTY-ACID I FAS SYNTHETASE OXIDOREDUCTASE) protein domain (PD711084) which is seen in Q59497_CORAM.Residues 1456-1591 are 48% similar to a (TRANSFERASE SYNTHASE POLYKETIDE PHOSPHOPANTETHEINE TRANSACYLASE CARRIER MALONYL COA-ACYL TYPE ACYLTRANSFERASE) protein domain (PD000287) which is seen in Q9A7P6_CAUCR.Residues 1464-1509 are 76% similar to a (TRANSFERASE FATTY SYNTHASE ACID ACYLTRANSFERASE FATTY-ACID FAS SYNTHETASE 2.3.1.- PROBABLE) protein domain (PDA133X3) which is seen in Q04846_CORAM.Residues 1464-1509 are 80% similar to a (SYNTHASE ACID FATTY SUBUNIT TRANSFERASE BETA ACYLTRANSFERASE HYDROXYPALMITOYL-ACYL-CARRIER-PROTEIN INCLUDES: DEHYDRATASE) protein domain (PD543221) which is seen in Q8FMV7_COREF.Residues 1515-1586 are 81% similar to a (SYNTHASE FATTY ACID TRANSFERASE ACYLTRANSFERASE SUBUNIT BETA FATTY-ACID SYNTHETASE INCLUDES:) protein domain (PD734487) which is seen in Q8G456_BIFLO.Residues 1592-1652 are 81% similar to a (SYNTHASE ACID FATTY TRANSFERASE ACYLTRANSFERASE SUBUNIT BETA FATTY-ACID HYDROXYPALMITOYL-ACYL-CARRIER-PROTEIN INCLUDES:) protein domain (PD561521) which is seen in Q8G456_BIFLO.Residues 1688-1754 are 74% similar to a (SYNTHASE ACID FATTY TRANSFERASE ACYLTRANSFERASE SUBUNIT BETA HYDROXYPALMITOYL-ACYL-CARRIER-PROTEIN INCLUDES: DEHYDRATASE) protein domain (PD007665) which is seen in Q9X7E2_MYCLE.Residues 1772-1838 are 73% similar to a (SYNTHASE TRANSFERASE ACID FATTY ACYLTRANSFERASE 3-OXOACYL-ACYL-CARRIER-PROTEIN REDUCTASE ALPHA BETA-KETOACYL SUBUNIT) protein domain (PD007280) which is seen in Q8FMV7_COREF.Residues 1901-2220 are 65% similar to a (TRANSFERASE SYNTHASE ACID ACYLTRANSFERASE FATTY FATTY-ACID I FAS SYNTHETASE OXIDOREDUCTASE) protein domain (PD003582) which is seen in Q8NS46_CORGL.Residues 2265-2515 are 78% similar to a (SYNTHASE TRANSFERASE ACID FATTY REDUCTASE 3-OXOACYL-ACYL-CARRIER-PROTEIN ALPHA SUBUNIT BETA-KETOACYL ACYLTRANSFERASE) protein domain (PD463685) which is seen in Q04846_CORAM.Residues 2570-2979 are 77% similar to a (SYNTHASE TRANSFERASE ACID FATTY ACYLTRANSFERASE 3-OXOACYL-ACYL-CARRIER-PROTEIN ALPHA REDUCTASE SUBUNIT BETA-KETOACYL) protein domain (PD011953) which is seen in Q8G456_BIFLO.Residues 2642-3159 are 40% similar to a (SYNTHASE TRANSFERASE BETA-KETOACYL PROBABLE) protein domain (PD271345) which is seen in Q9HU15_PSEAE.Residues 3003-3061 are 86% similar to a (TRANSFERASE SYNTHASE POLYKETIDE PHOSPHOPANTETHEINE I 3-OXOACYL-ACYL-CARRIER-PROTEIN ACYLTRANSFERASE II TYPE ACID) protein domain (PD580608) which is seen in Q8G456_BIFLO.Residues 3064-3227 are 71% similar to a (SYNTHASE TRANSFERASE ACID FATTY ACYLTRANSFERASE 3-OXOACYL-ACYL-CARRIER-PROTEIN ALPHA REDUCTASE SUBUNIT BETA-KETOACYL) protein domain (PD149030) which is seen in Q8G456_BIFLO.","","-41% similar to PDB:2UVA CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400 (E_value = 3.9E_66);-41% similar to PDB:2UVC CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE COMPLEXED WITH NADP+ FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE BETA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400 (E_value = 3.9E_66);-50% similar to PDB:2UV8 CRYSTAL STRUCTURE OF YEAST FATTY ACID SYNTHASE WITH STALLED ACYL CARRIER PROTEIN AT 3.1 ANGSTROM RESOLUTION (E_value = 5.8E_54);-49% similar to PDB:2UV9 CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE ALPHA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400 (E_value = 5.8E_54);-49% similar to PDB:2UVB CRYSTAL STRUCTURE OF FATTY ACID SYNTHASE COMPLEXED WITH NADP+ FROM THERMOMYCES LANUGINOSUS AT 3.1 ANGSTROM RESOLUTION. THIS FILE CONTAINS THE ALPHA SUBUNITS OF THE FATTY ACID SYNTHASE. THE ENTIRE CRYSTAL STRUCTURE CONSISTS OF ONE HETERODODECAMERIC FATTY ACID SYNTHASE AND IS DESCRIBED IN REMARK 400 (E_value = 5.8E_54);","Residues 921 to 978 (E_value = 2.8e-32) place ANA_0786 in the DUF1729 family which is described as Domain of unknown function (DUF1729).Residues 1318 to 1437 (E_value = 4.8e-22) place ANA_0786 in the MaoC_dehydratas family which is described as MaoC like domain.Residues 1451 to 1743 (E_value = 3.9e-10) place ANA_0786 in the Acyl_transf_1 family which is described as Acyl transferase domain.Residues 2709 to 2951 (E_value = 4e-10) place ANA_0786 in the ketoacyl-synt family which is described as Beta-ketoacyl synthase, N-terminal domain.Residues 2959 to 3085 (E_value = 4.2e-09) place ANA_0786 in the Ketoacyl-synt_C family which is described as Beta-ketoacyl synthase, C-terminal domain.","","I multifunctional fatty acid synthase","","1","","","Wed Aug 1 18:16:16 2007","","Wed Aug 1 18:16:16 2007","","","Wed Aug 1 18:16:16 2007","Wed Aug 1 18:16:16 2007","Wed Aug 1 18:16:16 2007","","","Wed Aug 1 18:16:16 2007","","","Wed Aug 1 18:16:16 2007","Wed Aug 1 18:16:16 2007","Wed Aug 1 18:16:16 2007","","Wed Aug 1 18:16:16 2007","Wed Aug 1 18:16:16 2007","","","","","yes","","" "ANA_0787","839439","837808","1632","5.05","-21.45","56968","GTGACCACCGCCCCCATCACCGGCCCCGGCGCACCTGCCGAGACACCGGCCCAGGGAACCACTATGGCCGACTCGGAGGCCACCACCGCCTTCCGCCAGCGCATCGCCCGCATTGACCGGGAGGCCGAGGAGCACGCCGCCGCCCGTCAGCACGCCAAGGGCAAGCGCACCGCCCGCGAGCGCATCAACGACCTGCTCGACGACTCCACCTTCCTGGAGATCGGCCGCTACTCCGGTTCGGGCGCCGGCGACAAGGCCCGCCCCTCGGGCGTCGTCACCGGCTTCGGCCAGATCGACGGCCGCCAGGTGGCCATCTACTCCCAGGACTTCTCCGTCTCCGGCGGCGCCCTGGGCACCATCGAGGGGGACAAGATCGTCCGCCTCCTGGACGACGCCCTGCGCCTACGCATCCCCGTCATCGGACTCATCGACTCCGGCGGCGCCAAGATCCAGGAGGGCGTGGGAGCCCTGCGCCAGTACGGGCGCATCTTCAACCGCACCTGCGCCGCCTCCGGACTGGTCCCGCAGATCAGCGTCATCCTGGGGCCCTGTGCCGGCGGCGCCGTCTACAGCCCGGCCCTGACCGACTTCGTCATCGCCACCCGCCAGGCCTCCCACATGTTCGTCACCGGCCCCGACGTCGTACGCGCCACAACCGGTGAGCAGATCAGCGCCGAGGACCTCGGCGGTGCGCAGATCCACGGTTCCGTCTCCGGCGTCGTCCACTACGTGGCCGACGACGAGGAGGACGCGTTGGGGCAGGTCCGCACCTTCCTGGCCTACCTGCCCTCCTCATCCGAGGTCAGCGCTCCCCTGTACGCCTACGACGACGCCGACGCCCAGGCCGACGCCGAGGCCGCCCGCAGCGTCGGCGAGATCGTCCCGGCCTCCACCCGGCAGGCCTACGACGTCGTCGAGGTGGTCTCAGCCGTCGTCGACCACGGCGAGCTCGTCCAGGTCCAGGAGGAGTTCGCTCCCAACGTCGTGGTCGGCTTCGCCTGCTTCGAGGGCCACCCGGTGGGGATCGTCGCCAACCAGCCGCTGGTGGACGCCGGCACCCTGGATGTCGACGCCTCCGAGAAGCTCGCCCGCTTCGTGCGTTTCTGCGACGCCTTCGGGCTGCCAGTGGTCACCTTCGTCGACGTCCCCGGCTACCGTCCCGGAGCCGAGCAGGAGCACGCCGGCATCATTCGCCGCGGTGCCAAGGTCATCAACGCCTACGCCACCGCCACCGTGCCGCTGGTGACGATCGTCCTGCGCAAGGCCTATGGCGGCGCCTACATCGTCATGGGCTCCAAGGCCATCGGCGCCGACCTCAACTTCTGCTGGCCGGGAGCCGAGATCGCCGTCCTGGGCGCTGCCGGAGCCGTCGGCATCATTCACCGTCGCGACCTGGCCAAGGTTCGTGACGAGCAGGGGGAGGAGGCCGCGGCCGCCGAGCACGAGCGGCTCGTGGCCGAGTACACCGACGCCGTCATCAACCCCGACAAGGCCGTGGCCATCGGTGAGATCGACGCCGTCATCGCCCCCGAGGAGACCCGCAACGTCATCGTCGACTCCCTGGCCGCGCTGCGCGCCAAGAACGACGCCCGCCCCGAGTCCCCCAAGAAGCATGACAACATCCCCCTCTGA","VTTAPITGPGAPAETPAQGTTMADSEATTAFRQRIARIDREAEEHAAARQHAKGKRTARERINDLLDDSTFLEIGRYSGSGAGDKARPSGVVTGFGQIDGRQVAIYSQDFSVSGGALGTIEGDKIVRLLDDALRLRIPVIGLIDSGGAKIQEGVGALRQYGRIFNRTCAASGLVPQISVILGPCAGGAVYSPALTDFVIATRQASHMFVTGPDVVRATTGEQISAEDLGGAQIHGSVSGVVHYVADDEEDALGQVRTFLAYLPSSSEVSAPLYAYDDADAQADAEAARSVGEIVPASTRQAYDVVEVVSAVVDHGELVQVQEEFAPNVVVGFACFEGHPVGIVANQPLVDAGTLDVDASEKLARFVRFCDAFGLPVVTFVDVPGYRPGAEQEHAGIIRRGAKVINAYATATVPLVTIVLRKAYGGAYIVMGSKAIGADLNFCWPGAEIAVLGAAGAVGIIHRRDLAKVRDEQGEEAAAAEHERLVAEYTDAVINPDKAVAIGEIDAVIAPEETRNVIVDSLAALRAKNDARPESPKKHDNIPL$","Propionyl-CoA carboxylase beta chain","Cytoplasm","propionyl-CoA carboxylase beta chain","propionyl-CoA carboxylase beta chain ","Propionyl-CoA carboxylase","","Toh H., Kondo H., Tanabe T. Molecular evolution of biotin-dependent carboxylases. Eur. J. Biochem. 1993. 215(3):687-696. PMID: 8102604Thornton C.G., Kumar G.K., Haase F.C., Phillips N.F., Woo S.B., Park V.M., Magner W.J., Shenoy B.C., Wood H.G., Samols D. Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli. J. Bacteriol. 1993. 175(17):5301-5308. PMID: 8366018","","","

InterPro
IPR000022
Domain

Carboxyl transferase
PF01039	$\"[45-541]T$	Carboxyl_trans

InterPro
IPR000438
Family

Acetyl-CoA carboxylase carboxyl transferase, beta subunit
PR01070	$\"[110-124]T$ $\"[144-162]T$	ACCCTRFRASEB

InterPro
IPR001670
Domain

Iron-containing alcohol dehydrogenase
PS00913	$\"[484-512]?$	ADH_IRON_1

InterPro
IPR011762
Domain

Acetyl-coenzyme A carboxyltransferase, N-terminal
PS50980	$\"[30-238]T$	COA_CT_NTER

InterPro
IPR011763
Domain

Acetyl-coenzyme A carboxyltransferase, C-terminal
PS50989	$\"[1-147]T$ $\"[239-533]T$	COA_CT_CTER

noIPR
unintegrated

unintegrated
G3DSA:3.90.226.10	$\"[31-266]T$ $\"[281-542]T$	no description
PTHR22855	$\"[54-221]T$ $\"[253-543]T$	ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED
PTHR22855:SF14	$\"[54-221]T$ $\"[253-543]T$	PROPIONYL-COA CARBOXYLASE

","BeTs to 19 clades of COG0777COG name: Acetyl-CoA carboxylase beta subunitFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0777 is ao--k-yqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB000022 (Carboxyl transferase family) with a combined E-value of 2.8e-24. IPB000022A 55-71 IPB000022B 91-100 IPB000022C 138-153 IPB000022D 437-460***** IPB000438 (Acetyl-CoA carboxylase carboxyl transferase beta subunit signature) with a combined E-value of 7.2e-24. IPB000438A 110-124 IPB000438B 144-162 IPB000438C 180-197 IPB000438D 209-220***** IPB013537 (Acetyl-CoA carboxylase, central region) with a combined E-value of 5.5e-08. IPB013537K 100-153 IPB013537N 310-344","Residues 53-264 are 42% similar to a (DECARBOXYLASE GLUTACONYL-COA LYASE SUBUNIT A 3D-STRUCTURE ALPHA SEQUENCING DIRECT CARBOXYLTRANSFERASE) protein domain (PD549826) which is seen in Q8RGS8_FUSNN.Residues 65-214 are 44% similar to a (ALPHA CHAIN METHYLMALONYL-COA POSSIBLE DECARBOXYLASE BLR3940) protein domain (PD806381) which is seen in Q89NA2_BRAJA.Residues 328-384 are 80% similar to a (CARBOXYLASE BETA TRANSFERASE SUBUNIT LIGASE ACETYL-COA CARBOXYL A ACETYL-COENZYME CHAIN) protein domain (PD001571) which is seen in Q745K8_MYCPA.Residues 160-214 are similar to a (BETA CARBOXYLASE SUBUNIT LIGASE PROPIONYL-COA CHAIN TRANSFERASE CARBOXYLASE DIOXIDE CARBOXYLTRANSFERASE) protein domain (PD013404) which is seen in Q8G457_BIFLO.Residues 215-303 are 66% similar to a (CARBOXYLASE BETA LIGASE SUBUNIT PROPIONYL-COA ACETYL-COA CHAIN TRANSFERASE BIOTIN CARBOXYLASE) protein domain (PD648172) which is seen in Q8G457_BIFLO.Residues 313-360 are 79% similar to a (CARBOXYLASE BETA LIGASE SUBUNIT PROPIONYL-COA ACETYL-COA CHAIN TRANSFERASE CARBOXYLASE BIOTIN) protein domain (PD471707) which is seen in Q8G457_BIFLO.Residues 328-384 are 80% similar to a (CARBOXYLASE BETA TRANSFERASE SUBUNIT LIGASE ACETYL-COA CARBOXYL A ACETYL-COENZYME CHAIN) protein domain (PD001571) which is seen in Q745K8_MYCPA.Residues 361-413 are similar to a (TRANSFERASE SUBUNIT CARBOXYLASE LIGASE ALPHA BETA CARBOXYL ACETYL-COA PROPIONYL-COA CARBOXYLASE) protein domain (PD001372) which is seen in Q8G457_BIFLO.Residues 416-514 are 73% similar to a (BETA CARBOXYLASE SUBUNIT LIGASE PROPIONYL-COA CHAIN TRANSFERASE CARBOXYLASE DECARBOXYLASE ALPHA) protein domain (PD001720) which is seen in Q8G457_BIFLO.","","-65% similar to PDB:1XNW Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #2, mutant D422I (E_value = 9.0E_135);-64% similar to PDB:1XNV Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #1 (E_value = 5.9E_134);-64% similar to PDB:1XNY Biotin and propionyl-CoA bound to Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB) (E_value = 5.9E_134);-64% similar to PDB:1XO6 Acyl-CoA Carboxylase Beta Subunit from S. coelicolor (PccB), apo form #3 (E_value = 5.9E_134);-63% similar to PDB:1VRG Crystal structure of propionyl-CoA carboxylase, beta subunit (TM0716) from THERMOTOGA MARITIMA at 2.30 A resolution (E_value = 3.2E_124);","Residues 45 to 541 (E_value = 3.6e-208) place ANA_0787 in the Carboxyl_trans family which is described as Carboxyl transferase domain.","","carboxylase beta chain (mmdA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0788","841278","839443","1836","4.96","-25.74","64686","GTGACCCTCTCGCGTATCCTCATCGCCAACCGTGGCGAGATCGCACTACGTATCGTGCGAACCGCCCGCGATCTCGGAGCGACGTCGATCCTTCCGTACACGCCCGAGGACCTGATGAGCCCTGCCGCAGAGCTCGCCGATGAGTCCTACGCACTGCCCGAGGGGTCGTCCTACACCGATGCGGCGGCGCTCCTCGAGATGGCCCGTGCCACCGGCGCCGACGCCATCCACCCCGGTTACGGGTTCCTGTCCGAGGACGCCGACTTCGCCCGCTCCATCATCGATGCCGGCATCACCTGGGTCGGGCCCTCGCCTGAGGCCATGGATGCCCTCGGGGACAAGATGAGTGCCCGAGCCACCGCCGAGCGGGCCCAGGTCGCCCCGGTGCCCGGCATCACCGACTCGGTCACCGACGCGGAGACCGTCATCGCCTTCGCCGCAACCCACGGCTACCCGGTCGCACTGAAGCGCACTGACGGCGGTGGTGGACGCGGCATCACTGTCCTGGACAACGACGACGAGGTCAGGACCACCCCGGCCTTCGAGTCCGCGGCGCAGGGCGGCGGGACCCTCATCCTGGAGCGGTTCGTCACAGCCGCACGCCATGTCGAGACCCAGTGCGCTCGCGACAGCCACGGCGGTTTCGCCGTCGTGTCCACCCGCGACTGCTCACTGCAGCGACGCAACCAGAAGCTCCTCGAGGAGGCTCCCGCGCCCTTCCTGCCCGAGGGTGTTCACGACCGTCTCGTCGCGGCCTCCCGTCGCCTCCTGGAGACGGTCGACTATGTCGGGGTGGCCACCTGCGAGTTCCTCCTGACCACCGAGGGCGATGTCTGGTTCCTGGAGGTCAATCCCCGTCTTCAGGTGGAGCACTGCGTCACCGAGGAGGTCACCGGCACCGACCTGGTCGAGGTCCAACTGCGCATCGCCCAGGGCGGACACCTCGGACAGGTCAACGAGCCCCGCGGCCACAGCCTCGAACTGCGCATCACCTGTGAGGACCCCGCCCGGGGACTGGCCCCCTCCACCGGTGCCATCACCCGCCTGCGCTGGCCGGCCGGCCCCGGGGTCCGTATCGAGTCCGGAGTCACCGAGGGCGACGTCGTCACTCCCCTGTTCGACCCGATGCTCGCCAAGATCATCATCACCGGCGCCAGCCGGGAACAGGCCATCGCCCGAGCCCGACGAGCCCTGCGAGAGACAGTGGTCGAAGGCGTCACCGTGTGCACCGCCCTGCACTCCGAGGTCCTGGCCCGCCCCGACTTCACCGCCCCCGACGAGGCCGGGCGGCTGGCCGTGACCACGCGCTGGATCGAGAACGAGGTGCTGCCCGATCTTGACGACGCCGCGGCGACGTCGCTGACCGACGGTTCGGCGGAGACGGTCGCCAACCCGCGCACCCGCTCCAGCTACATCATCGAGCTCAACGGCCGCCGCATGCAGCTGACCCTGCCCGACGGGATCCTCGCCCCCTCCAACCCGGCGCGAGGCTTCAGCCCCCGCAGCAACCGGGCCCAGCCGCTGCGCGGCCGTTCGGGCGCGACCCGCTCACCTCGAGGCGCAGCCTCTGGTGAGACCGGGACCGCCGGCGGTGAGCCCGGTGTCATCGCCGCCCCCATGCAGGCCATCGTCACCCGGATCTGCGTGGAGCCGGGCCAGCCGGTCTGCCAGGGCGATCTGCTCGTGGTCCTGGAGTCCATGAAGATGGAGAACTACGTCCACGCACCCAGCGACGGCACCATCTCGGAGATCCCCATCAGCGCCGGACGCACCGTCTCGGCCGGCGATGTCCTGGTGCGCATGAGCACCCCCGAGAACGACTCCGAGGAGGCCTGA","VTLSRILIANRGEIALRIVRTARDLGATSILPYTPEDLMSPAAELADESYALPEGSSYTDAAALLEMARATGADAIHPGYGFLSEDADFARSIIDAGITWVGPSPEAMDALGDKMSARATAERAQVAPVPGITDSVTDAETVIAFAATHGYPVALKRTDGGGGRGITVLDNDDEVRTTPAFESAAQGGGTLILERFVTAARHVETQCARDSHGGFAVVSTRDCSLQRRNQKLLEEAPAPFLPEGVHDRLVAASRRLLETVDYVGVATCEFLLTTEGDVWFLEVNPRLQVEHCVTEEVTGTDLVEVQLRIAQGGHLGQVNEPRGHSLELRITCEDPARGLAPSTGAITRLRWPAGPGVRIESGVTEGDVVTPLFDPMLAKIIITGASREQAIARARRALRETVVEGVTVCTALHSEVLARPDFTAPDEAGRLAVTTRWIENEVLPDLDDAAATSLTDGSAETVANPRTRSSYIIELNGRRMQLTLPDGILAPSNPARGFSPRSNRAQPLRGRSGATRSPRGAASGETGTAGGEPGVIAAPMQAIVTRICVEPGQPVCQGDLLVVLESMKMENYVHAPSDGTISEIPISAGRTVSAGDVLVRMSTPENDSEEA$","Biotin carboxylase","Cytoplasm","acetyl-/propionyl-coenzyme A carboxylase alphachain [includes: biotin carboxylase ; biotin carboxyl","acetyl-/propionyl-coenzyme A carboxylase alpha chain ","Carbamoyl-phosphate synthase L chain, ATP-binding","","Waldrop G.L., Rayment I., Holden H.M. Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry 1994. 33(34):10249-10256. PMID: 7915138","","","

InterPro
IPR000089
Domain

Biotin/lipoyl attachment
PF00364	$\"[534-601]T$	Biotin_lipoyl
PS50968	$\"[534-601]T$	BIOTINYL_LIPOYL

InterPro
IPR005479
Domain

Carbamoyl-phosphate synthase L chain, ATP-binding
PF02786	$\"[113-322]T$	CPSase_L_D2
PS00867	$\"[280-287]?$	CPSASE_2

InterPro
IPR005481
Domain

Carbamoyl-phosphate synthetase large chain, N-terminal
PF00289	$\"[2-111]T$	CPSase_L_chain

InterPro
IPR005482
Domain

Biotin carboxylase, C-terminal
PF02785	$\"[327-439]T$	Biotin_carb_C

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[118-311]T$	ATP_GRASP

InterPro
IPR011764
Domain

Biotin carboxylation region
PS50979	$\"[2-437]T$	BC

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[84-447]T$	no description

InterPro
IPR013817
Domain

Pre-ATP-grasp fold
G3DSA:3.40.50.20	$\"[2-83]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:2.40.50.100	$\"[526-602]T$	no description
PTHR18866	$\"[5-439]T$	CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE

","BeTs to 20 clades of COG0439COG name: Biotin carboxylaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0439 is aom---yq-drlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001882 (Biotin-requiring enzyme, attachment site) with a combined E-value of 1.2e-75. IPB001882A 5-15 IPB001882B 100-114 IPB001882C 150-167 IPB001882D 200-234 IPB001882E 262-271 IPB001882F 286-295 IPB001882G 323-341 IPB001882H 549-584***** IPB013537 (Acetyl-CoA carboxylase, central region) with a combined E-value of 4e-43. IPB013537D 126-175 IPB013537E 190-239 IPB013537F 278-325 IPB013537G 327-379 IPB013537B 52-91***** IPB003379 (Conserved carboxylase region) with a combined E-value of 1.2e-14. IPB003379H 536-589***** IPB004167 (E3 binding domain) with a combined E-value of 9.5e-07. IPB004167A 538-589","Residues 64-132 are 63% similar to a (BIOTIN CARBOXYLASE SUBUNIT ENZYME COA BIOTIN-REQUIRING LIGASE ACETYL) protein domain (PD890704) which is seen in Q747G6_GEOSL.Residues 72-115 are 90% similar to a (CARBOXYLASE BIOTIN LIGASE PYRUVATE ACETYL-COA SUBUNIT CARBOXYLASE ALPHA A ATP-BINDING) protein domain (PD584323) which is seen in Q8U917_AGRT5.Residues 116-221 are 69% similar to a (CARBOXYLASE A ALPHA ACETYL-/PROPIONYL-COENZYME CHAIN) protein domain (PDA1C963) which is seen in Q8G458_BIFLO.Residues 222-322 are similar to a (CARBOXYLASE BIOTIN LIGASE PYRUVATE ACETYL-COA SUBUNIT CARBOXYLASE ALPHA A ATP-BINDING) protein domain (PD866077) which is seen in Q8G458_BIFLO.Residues 341-441 are 61% similar to a (CARBOXYLASE BIOTIN LIGASE PYRUVATE ACETYL-COA SUBUNIT CARBOXYLASE ALPHA A ATP-BINDING) protein domain (PD002908) which is seen in Q9XCV7_BBBBB.Residues 536-601 are 74% similar to a (ACYLTRANSFERASE PYRUVATE LIPOYL BIOTIN TRANSFERASE DIHYDROLIPOAMIDE DEHYDROGENASE CARBOXYLASE COMPONENT ACETYLTRANSFERASE) protein domain (PD000268) which is seen in Q8G458_BIFLO.","","-58% similar to PDB:1ULZ Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase (E_value = 1.9E_80);-57% similar to PDB:2GPW Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli. (E_value = 6.2E_79);-57% similar to PDB:1BNC THREE-DIMENSIONAL STRUCTURE OF THE BIOTIN CARBOXYLASE SUBUNIT OF ACETYL-COA CARBOXYLASE (E_value = 1.4E_78);-57% similar to PDB:1DV1 STRUCTURE OF BIOTIN CARBOXYLASE (APO) (E_value = 1.4E_78);-57% similar to PDB:1DV2 The structure of biotin carboxylase, mutant E288K, complexed with ATP (E_value = 4.0E_78);","Residues 2 to 111 (E_value = 1e-32) place ANA_0788 in the CPSase_L_chain family which is described as Carbamoyl-phosphate synthase L chain, N-terminal domain.Residues 113 to 288 (E_value = 9.9e-06) place ANA_0788 in the ATP-grasp family which is described as ATP-grasp domain.Residues 113 to 322 (E_value = 2.4e-57) place ANA_0788 in the CPSase_L_D2 family which is described as Carbamoyl-phosphate synthase L chain, ATP binding domain.Residues 327 to 439 (E_value = 2.7e-42) place ANA_0788 in the Biotin_carb_C family which is described as Biotin carboxylase C-terminal domain.Residues 534 to 601 (E_value = 8.7e-20) place ANA_0788 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme.","","A carboxylase alpha chain [includes: biotin carboxylase ; biotin carboxyl carrier protein (BccP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0789","842352","841657","696","5.27","-12.26","24213","ATGACGGCCATCCACCCCTCGATCCTCAACTGCGACATCGCCCACCTGGCCGACGAGCTCGACCGGGTCACGGGCGACGTCGGCGCCCCGGGCGCCGACGGGATTCACGTCGATGTCATGGACAACCACTTCGTGCCCAACCTGTCATGGGGGCTGCCGGTGGTCGAGGCGGTGCTCGCCCATTCCTCGCTGCCCGTGGACGCCCACCTCATGATCCGCGACGCCGACCGCTGGGCACCGGCCTACGCCGAGGCCGGCTGCCAGATCGTCACCCCCCACGCCGAGGCCACGACGGCGCCGGTGCGTCTGGCGCGCGAGCTCCACCGGCTCGGCGCCGGCGCGGGCATCGCCCTGAGGCCCGCCACCCCCCTGGAGGCCGTCGCCGATGTCCTAGGGGAGTTCGACCTCCTCCTGCTCATGACCGTGGAGCCGGGCTTCGGGGGCCAGTCCTTCATCGAGTCGATGCTGCCCAAGATCCGCCGGGCGCGCGAGCTGGTCGGTGTCAGAGGGCTCGACCTGCGAGTGCAGGTCGATGGCGGTATCACCGCCCAGACGATTGAGCGCGCGGCCGAGGCCGGGGCGGATGTCTTCGTCGCCGGGTCGGCGGTCTATCGTGCCGACGACGCCCTGGCCGCCATTTGCGAGCTGCGTGAGGCGGCCTCCTCGCACTGCCATGGCGCTCACGGTGGACACTGA","MTAIHPSILNCDIAHLADELDRVTGDVGAPGADGIHVDVMDNHFVPNLSWGLPVVEAVLAHSSLPVDAHLMIRDADRWAPAYAEAGCQIVTPHAEATTAPVRLARELHRLGAGAGIALRPATPLEAVADVLGEFDLLLLMTVEPGFGGQSFIESMLPKIRRARELVGVRGLDLRVQVDGGITAQTIERAAEAGADVFVAGSAVYRADDALAAICELREAASSHCHGAHGGH$","Ribulose-phosphate 3-epimerase","Cytoplasm","ribulose-phosphate 3-epimerase","ribulose-phosphate 3-epimerase ","Ribulose-phosphate 3-epimerase","","Kusian B., Yoo J.G., Bednarski R., Bowien B. The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within the cfx operons of the chemoautotroph Alcaligenes eutrophus. J. Bacteriol. 1992. 174(22):7337-7344. PMID: 1429456","","","

InterPro
IPR000056
Family

Ribulose-phosphate 3-epimerase
PTHR11749	$\"[14-230]T$	RIBULOSE-5-PHOSPHATE-3-EPIMERASE
PF00834	$\"[3-207]T$	Ribul_P_3_epim
TIGR01163	$\"[3-217]T$	rpe: ribulose-phosphate 3-epimerase
PS01085	$\"[35-49]T$	RIBUL_P_3_EPIMER_1
PS01086	$\"[137-159]T$	RIBUL_P_3_EPIMER_2

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[4-229]T$	no description

","BeTs to 20 clades of COG0036COG name: Pentose-5-phosphate-3-epimeraseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0036 is --mp--yqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB000056 (Ribulose-phosphate 3-epimerase) with a combined E-value of 6.3e-79. IPB000056A 4-16 IPB000056B 31-52 IPB000056C 65-95 IPB000056D 99-153 IPB000056E 175-208","Residues 4-217 are 74% similar to a (ISOMERASE METABOLISM CARBOHYDRATE 3-EPIMERASE RIBULOSE-PHOSPHATE EPIMERASE PPE PENTOSE-5-PHOSPHATE R5P3E 3-) protein domain (PD003683) which is seen in Q827P4_STRAW.Residues 35-207 are 48% similar to a (3-EPIMERASE RIBULOSE-5-PHOSPHATE RIBULOSE-PHOSPHATE) protein domain (PD591639) which is seen in Q8Z2Y1_SALTI.","","-61% similar to PDB:1TQJ Crystal structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 angstrom resolution (E_value = 3.2E_41);-60% similar to PDB:2FLI The crystal structure of D-ribulose 5-phosphate 3-epimerase from Streptococus pyogenes complexed with D-xylitol 5-phosphate (E_value = 3.2E_41);-61% similar to PDB:1RPX D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE FROM SOLANUM TUBEROSUM CHLOROPLASTS (E_value = 9.4E_41);-58% similar to PDB:1H1Y THE STRUCTURE OF THE CYTOSOLIC D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE FROM RICE COMPLEXED WITH SULFATE (E_value = 2.0E_35);-58% similar to PDB:1H1Z THE STRUCTURE OF THE CYTOSOLIC D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE FROM RICE COMPLEXED WITH SULFATE AND ZINC (E_value = 2.0E_35);","Residues 3 to 207 (E_value = 9.9e-96) place ANA_0789 in the Ribul_P_3_epim family which is described as Ribulose-phosphate 3 epimerase family.","","3-epimerase (rpe)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0790","844028","842391","1638","9.16","13.65","58631","ATGGGGGAGCGATCGGCACGCCGGAGCGCGTCGGGCGGCCACAAGGAGAGTCGACGAGGTGCAGGCCGCGGAAAGGGCAACGAGCACGGCAGATACCGGGAGCAAGGCGGCAGGCGAAGCGGGCGTGGCGGTCACCACGAGGGTGGACGCGGCCAGGGCCGGGGCCGGCGCTCCTTCAAGCAGGACGGCCCGCAGGCGGGTGCATCGACGCGCTCGGCGCGGGGGCGATCTGACTCGGCACGTGAAGTGGCTCTGGAGGTGCTGACCCGCGTTCGCCGCGATGACGCCTTCGCCAACCTCCTTCTGCCCGAGCTGCTCGAGACCGCTGACCTGGATCGGCGTGACGCCGGCTTCGCCACTGCCCTGACCTACGGGACCCTGCGGCTCCAGGGGCGCTACGACGCGATGATCGCCGCTTGCACGGACCGCCCCCTGGAGCGCATCGATCCGGCCGTGCTCGACGTGCTGCGCCTGGGGGCCCACCAGCTCATGGGTATGAGGGTGGCCCAGCACGCCGCAGTGAGCACCACCGTGGACCTGGCCACCACCTCCTGCGGACGCGGCGCGGCCACCTTCGTCAACGCCGTCATGCGTCGCCTCAGCGGACGGGACCTGGACTCCTGGATGGATGAGCTGCGCCGGGACGCGCCCGATAAGACGGCCGCCCTGGCGCGCACCCAGTCGCACCCGGAGTGGATCGTCAAGGCGCTGCGTCAGGCCCTGGTCACCCACGGCCGCAGCGACGAGGAGCTCGAGGCCATTCTGGCCGCAGACAACGCCGACCCCGAAGTGGCCCTGTGTGCCAGGCCCGGCCTCATCGCCCCGGAGGCGCTGGCCAAGGCCGCCCGCAAGGCCGACCGGGCTCACGACGTCGAGCCGCGTCCCGGCAGGATCAGTCCCCTCGCCGTCGTCATGGTTGGGGGAGATCCGGGCCGGATCGAGGCGATCCGCGACTGCCGGGCCGGGGTCGAGGACGAGGGCAGTCAGCTGGTGGCGCTCGTTGCGGCGCACGCCCCTGTGGAGGGCCGCGATGAGCGGTGGCTCGACCTGTGCGCCGGGCCCGGTGGCAAGGCCGCCCTGCTCGCCGCGAGGGCCGCGCAGACGGGCGCCCAGCTGCTGGCCAATGAGGTCAGCCCCCATCGGGCCGACCTGGTGCGCTCCGCCCTACGCGCCATCGCGCCGGACGTCGCCCGGGCGCGTTGCGGTGATGGACGTGACCTCGGGCGCGATGAGCCTGGCGCCTACGACCGGGTCCTGGTTGACGCTCCCTGCACGGGGCTGGGGTCGCTGCGCCGCCGCCCCGAGGCCCGCTGGCGCCGACAGCCAGGGGACGTCACCGTTCTGGCCGAGCTTCAGCGCGAGCTGCTGGCCAGTGCCCTGCGCGCCGTGCGACGCGGAGGAGTGGTGACCTACGTGACCTGCTCCCCGCACGCGCTGGAGACGACCCTCGTCGTGCGCGACGTGACGCGGCTGCTGGAGCGCGAGGGCCTGCACACCGAGCCCCTGCACGCCGGGGACGTCGCCACCCGTCTGGCCCCTCATCCGCCGGCCGGATCCGACCGGGAGGCGCTCCAGCTCTGGCCCCACCTCGACGGCACCGACGCAATGTTCTGCGCCCTGCTGCGCCGCACCAGCTGA","MGERSARRSASGGHKESRRGAGRGKGNEHGRYREQGGRRSGRGGHHEGGRGQGRGRRSFKQDGPQAGASTRSARGRSDSAREVALEVLTRVRRDDAFANLLLPELLETADLDRRDAGFATALTYGTLRLQGRYDAMIAACTDRPLERIDPAVLDVLRLGAHQLMGMRVAQHAAVSTTVDLATTSCGRGAATFVNAVMRRLSGRDLDSWMDELRRDAPDKTAALARTQSHPEWIVKALRQALVTHGRSDEELEAILAADNADPEVALCARPGLIAPEALAKAARKADRAHDVEPRPGRISPLAVVMVGGDPGRIEAIRDCRAGVEDEGSQLVALVAAHAPVEGRDERWLDLCAGPGGKAALLAARAAQTGAQLLANEVSPHRADLVRSALRAIAPDVARARCGDGRDLGRDEPGAYDRVLVDAPCTGLGSLRRRPEARWRRQPGDVTVLAELQRELLASALRAVRRGGVVTYVTCSPHALETTLVVRDVTRLLEREGLHTEPLHAGDVATRLAPHPPAGSDREALQLWPHLDGTDAMFCALLRRTS$","tRNA and rRNA cytosine-C5-methylase","Cytoplasm","tRNA and rRNA cytosine-C5-methylases","K03500 Sun protein","Fmu (Sun) domain protein","","Huenges M., Rolz C., Gschwind R., Peteranderl R., Berglechner F., Richter G., Bacher A., Kessler H., Gemmecker G. Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein. EMBO J. 1998. 17(14):4092-4100. PMID: 9670024","","","

InterPro
IPR001678
Domain

Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p
PF01189	$\"[323-485]T$	Nol1_Nop2_Fmu

InterPro
IPR006027
Domain

NusB/RsmB/TIM44
G3DSA:1.10.940.10	$\"[74-220]T$	no description
PF01029	$\"[78-204]T$	NusB

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[324-544]T$	no description
PTHR22807	$\"[311-543]T$	NOP2(YEAST)-RELATED NOL1/NOP2/FMU(SUN) DOMAIN-CONTAINING
PTHR22807:SF10	$\"[311-543]T$	NOL1/NOP2/FMU(SUN) FAMILY

","BeTs to 19 clades of COG0144COG name: tRNA and rRNA cytosine-C5-methylasesFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0144 is aom-kzy-vdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB006174 (16S rRNA m5C967 methyltransferase) with a combined E-value of 9.7e-48. IPB006174A 161-203 IPB006174C 323-363 IPB006174D 415-437 IPB006174E 451-489 IPB006174F 525-543***** IPB001678 (Bacterial Sun/eukaryotic nucleolar Nop1/Nop2) with a combined E-value of 7.1e-38. IPB001678B 347-361 IPB001678C 372-388 IPB001678D 415-435 IPB001678E 464-490 IPB001678F 528-543***** IPB011023 (Nop2p) with a combined E-value of 1.6e-14. IPB011023C 374-405 IPB011023D 415-426 IPB011023E 456-487***** IPB006027 (Antitermination protein NusB) with a combined E-value of 8.7e-08. IPB006027 167-200","Residues 124-198 are similar to a (METHYLTRANSFERASE RRNA TRANSFERASE SUN 2.1.1.- 16S RNA CYTOSINE-C5--METHYLTRANSFERASE RIBOSOMAL SUBUNIT) protein domain (PD038046) which is seen in Q827P6_STRAW.Residues 208-317 are 53% similar to a (METHYLTRANSFERASE FMU RRNA TRANSFERASE SUN CYTOSINE-C5-METHYLASES SCL6.29C SUN-FAMILY RV1407/MT1451 TRNA/RRNA) protein domain (PD115220) which is seen in Q741F7_MYCPA.Residues 323-389 are 79% similar to a (METHYLTRANSFERASE RRNA TRANSFERASE SUN NUCLEOLAR 2.1.1.- 16S RNA FAMILY RIBOSOMAL) protein domain (PD003196) which is seen in Q9L0Y7_STRCO.Residues 442-543 are 53% similar to a (METHYLTRANSFERASE RRNA TRANSFERASE SUN NUCLEOLAR 2.1.1.- FAMILY RNA 16S RIBOSOMAL) protein domain (PD319848) which is seen in YE07_MYCTU.","","-39% similar to PDB:1SQF The crystal structure of E. coli Fmu binary complex with S-Adenosylmethionine at 2.1 A resolution (E_value = 1.6E_11);-39% similar to PDB:1SQG The crystal structure of the E. coli Fmu apoenzyme at 1.65 A resolution (E_value = 1.6E_11);","Residues 78 to 204 (E_value = 4.3e-30) place ANA_0790 in the NusB family which is described as NusB family.Residues 254 to 542 (E_value = 1.1e-31) place ANA_0790 in the Nol1_Nop2_Fmu family which is described as NOL1/NOP2/sun family.","","and rRNA cytosine-C5-methylases (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0791","845002","844028","975","5.91","-4.61","34217","ATGCGTGTGCTTTTCGCCGGAACCCCAGAGGCAGCCCTGCCTACCCTGGAGGCCCTCATCGCCAGTGAGCACGACGTCGTCGGGGTCCTCACCCGTGCCGACGCTCGCAAGGGACGCGGCCGGACGCTGCATCCCTCTCCGGTGGCGGCCGTGGCTCGTGACGCGGGGCTCGATGTACGCACTCCAGCCACCCTCAAGGGCGAGCAGGCCGGAGATGTGCGGGACTGGGTGCGTGCTCTCAAGGTCGACGTCGCCGTCGTGGTCGCCTACGGGCGCCTGGTGCCGGCCGATCTGCTGGAGGTACCAGAGCACGGTTGGCTGAATCTCCACTTCTCGCTGCTGCCAGCATGGCGCGGAGCCGCACCGGTCCAGCGGGCGGTCATCGCAGGCGACGAGGTCACTGGGGCATGCGTGTTCCGCCTCGAGGAGGGGCTCGACACCGGTCCCGTCTATGGCCGACTCACGGAGGCCATCAGCGGTCGGGACACCAGTGGGGACCTGCTCGAGCGGCTGGCGCAGGCCGGGGCGCCCCTGGTCCTCGATGTGCTGCGCCGCATCGAGAACGACAGCGTGCGTCCGGAGCCGCAGGATGATGCGCTGGCCACGCTGGCCCCGATGCTCTCCTCGGCCGACGGCCGGATCCGCTGGGAGGATCCGGCGCTGGCCATTGATCGTCGGATCCGGGGCGTCAGTCCGGCACCGGGTGCCCACACCACCTATCAGGGGGCCAGGTTCCGTCTGGGCCCGGTCACCCTGGTCCCGGAGGTCACCGATCTGCTGCCCGGCCAGCTGCGCGCCACCAAGCACGAGGTTCTCGCGGGAACCGGGGGCTGTGCCGTCCGTCTGGGGCAGGTCGCACCCGCCGGGCGCAGCTGGATGCCCGCTGACGCCTGGGCCAGGGGAGCGCGCCCGGAGGCGGGCGCCATCTTGGGGGACTCTTCTTCCAGGAACGACGACGCTGAGGGAACGATCTGA","MRVLFAGTPEAALPTLEALIASEHDVVGVLTRADARKGRGRTLHPSPVAAVARDAGLDVRTPATLKGEQAGDVRDWVRALKVDVAVVVAYGRLVPADLLEVPEHGWLNLHFSLLPAWRGAAPVQRAVIAGDEVTGACVFRLEEGLDTGPVYGRLTEAISGRDTSGDLLERLAQAGAPLVLDVLRRIENDSVRPEPQDDALATLAPMLSSADGRIRWEDPALAIDRRIRGVSPAPGAHTTYQGARFRLGPVTLVPEVTDLLPGQLRATKHEVLAGTGGCAVRLGQVAPAGRSWMPADAWARGARPEAGAILGDSSSRNDDAEGTI$","Methionyl-tRNA formyltransferase","Cytoplasm","methionyl-tRNA formyltransferase","methionyl-tRNA formyltransferase ","methionyl-tRNA formyltransferase","","Schmitt E., Blanquet S., Mechulam Y. Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase. EMBO J. 1996. 15(17):4749-4758. PMID: 8887566","","","

InterPro
IPR002376
Domain

Formyl transferase, N-terminal
G3DSA:3.40.50.170	$\"[1-208]T$	no description
PF00551	$\"[1-183]T$	Formyl_trans_N

InterPro
IPR005793
Domain

Formyl transferase, C-terminal
PF02911	$\"[208-303]T$	Formyl_trans_C

InterPro
IPR005794
Family

Methionyl-tRNA formyltransferase
TIGR00460	$\"[1-313]T$	fmt: methionyl-tRNA formyltransferase

InterPro
IPR015518
Family

Methionine tRNA Formyltransferase-like
PTHR11138	$\"[68-312]T$	METHIONYL-TRNA FORMYLTRANSFERASE

noIPR
unintegrated

unintegrated
G3DSA:3.10.25.10	$\"[209-303]T$	no description

","BeTs to 19 clades of COG0223COG name: Methionyl-tRNA formyltransferaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0223 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005793 (Formyl transferase, C-terminal) with a combined E-value of 8.1e-26. IPB005793 89-141","Residues 1-214 are 51% similar to a (METHYLTRANSFERASE TRANSFERASE METHIONYL-TRNA BIOSYNTHESIS FORMYLTRANSFERASE) protein domain (PDA1B137) which is seen in FMT_RHOBA.Residues 1-54 are 68% similar to a (TRANSFERASE METHIONYL-TRNA FORMYLTRANSFERASE) protein domain (PDA1A2B4) which is seen in Q6AF77_BBBBB.Residues 6-196 are 70% similar to a (TRANSFERASE FORMYLTRANSFERASE METHIONYL-TRNA PHOSPHORIBOSYLGLYCINAMIDE BIOSYNTHESIS METHYLTRANSFERASE FORMYLTETRAHYDROFOLATE DEFORMYLASE HYDROLASE TRANSFORMYLASE) protein domain (PD001209) which is seen in FMT_COREF.Residues 90-247 are 44% similar to a (METHIONYL-TRNA TRANSFERASE FORMYLTRANSFERASE) protein domain (PD739287) which is seen in Q81CW2_BACCR.Residues 107-203 are 52% similar to a (METHIONYL-TRNA WITH TRANSFERASE FORMYLTRANSFERASE SIMILARITIES) protein domain (PD988920) which is seen in Q7N6X2_PHOLL.Residues 201-308 are 46% similar to a (METHYLTRANSFERASE TRANSFERASE METHIONYL-TRNA BIOSYNTHESIS FORMYLTRANSFERASE) protein domain (PD933919) which is seen in FMT_DEIRA.Residues 216-295 are 58% similar to a (TRANSFERASE FORMYLTRANSFERASE METHIONYL-TRNA METHYLTRANSFERASE BIOSYNTHESIS FMT PROBABLE 3D-STRUCTURE SEQUENCING METHYONYL-TRNA) protein domain (PD004966) which is seen in FMT_STRAW.","","-57% similar to PDB:1FMT METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI (E_value = 1.1E_49);-57% similar to PDB:2FMT METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET (E_value = 1.1E_49);-43% similar to PDB:1YRW Crystal Structure of E.coli ArnA Transformylase Domain (E_value = 4.5E_16);-43% similar to PDB:1Z7E Crystal structure of full length ArnA (E_value = 4.5E_16);-43% similar to PDB:2BLN N-TERMINAL FORMYLTRANSFERASE DOMAIN OF ARNA IN COMPLEX WITH N-5-FORMYLTETRAHYDROFOLATE AND UMP (E_value = 4.5E_16);","Residues 1 to 183 (E_value = 2.2e-35) place ANA_0791 in the Formyl_trans_N family which is described as Formyl transferase.Residues 208 to 303 (E_value = 1.3e-20) place ANA_0791 in the Formyl_trans_C family which is described as Formyl transferase, C-terminal domain.","","formyltransferase (fmt)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0792","845722","845042","681","4.68","-14.82","24471","ATGGCGGACGTGAACGCGCCGTCCCCCTTCGCCACGACCTCCAGCCCCGCAGACGCCGTCAGTGCCGTCGTCCTCGACTACGGCAACGTCCTGTACGCCTGGGAGCCCATGGCGGCCGTCGCCGGATACGTCTCAGCCGACGACTGGGAGGAGTTCGTGGTCGACGGAGGGTTCCTGACCTGGAACGAACGACTCGACCGGGGAGAGCCCTTCGAACAGGTGCTCGCCGACTACACCCGGGCCCACCCCGGCCGCCCCGACTGGGCAGAGATCCTCTCCTTGTACCGTCAGCGCTTCGCCGAATCGCTGACGGGTCCCGTTCCCGGCATGGCCGCTCTGCTCGACGAACTCCTTGAGGAAGGCGTGGCCCTGTACGGACTGACCAACTTCGACGCCGCCCCCTTCGAGGCAGCCAGGCTCCTGGTTCCCCAGCTCGAACGCTTCGCGGGCATCGTGGTCTCCGGGCACGAGCACCTGGCCAAACCGGATGCCGCCATCTTCGACCTTCTGCTGAGCCGCTACGACCTCGTGGCCTCCAGCACCCTGTTCATCGACGACTCGGGGGTCAACATCGAGGCGGCTGGTCGGCTGGGGCTACGCACCCATCACTTCACCGGCTCAGGACGACTGCGCGCCGAGCTCATCGCCTTGGGCCTGCTCCCCACGCCGGGCCGGCGCTGA","MADVNAPSPFATTSSPADAVSAVVLDYGNVLYAWEPMAAVAGYVSADDWEEFVVDGGFLTWNERLDRGEPFEQVLADYTRAHPGRPDWAEILSLYRQRFAESLTGPVPGMAALLDELLEEGVALYGLTNFDAAPFEAARLLVPQLERFAGIVVSGHEHLAKPDAAIFDLLLSRYDLVASSTLFIDDSGVNIEAAGRLGLRTHHFTGSGRLRAELIALGLLPTPGRR$","HAD superfamily hydrolase","Cytoplasm","HAD superfamily hydrolase","K07025 putative hydrolase of the HAD superfamily","HAD-superfamily hydrolase, subfamily IA, variant 3","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317Selengut J.D. MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases. Biochemistry 2001. 40(42):12704-12711. PMID: 11601995Morais M.C., Zhang W., Baker A.S., Zhang G., Dunaway-Mariano D., Allen K.N. The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry 2000. 39(34):10385-10396. PMID: 10956028","","","

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[106-207]T$	Hydrolase

InterPro
IPR006402
Domain

HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509	$\"[44-204]T$	HAD-SF-IA-v3: HAD-superfamily hydrolase, su

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[106-206]T$	no description
PTHR12725	$\"[62-201]T$	HALOACID DEHALOGENASE-LIKE HYDROLASE

","BeTs to 6 clades of COG1011COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1011 is -ompk-yqvdrlb-efghsn-j--t-Number of proteins in this genome belonging to this COG is 2","***** IPB005833 (Haloacid dehalogenase/epoxide hydrolase family signature) with a combined E-value of 2e-07. IPB005833A 20-31 IPB005833D 117-130 IPB005833E 148-164 IPB005833F 166-186","Residues 20-109 are 54% similar to a (HYDROLASE ALPHA POSSIBLE BETA) protein domain (PD711406) which is seen in Q8G3H0_BIFLO.Residues 97-211 are similar to a () protein domain (PDA11858) which is seen in Q9WZA8_THEMA.Residues 114-220 are similar to a (HYDROLASE DEHALOGENASE-LIKE HALOACID) protein domain (PDA11883) which is seen in Q6N2K3_RHOPA.Residues 122-215 are 51% similar to a (HYDROLASE DEHALOGENASE-LIKE HALOACID) protein domain (PDA11818) which is seen in Q6MKU2_BDEBA.","","No significant hits to the PDB database (E-value < E-10).","Residues 20 to 207 (E_value = 4.2e-07) place ANA_0792 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","superfamily hydrolase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0793","846066","847289","1224","4.91","-19.17","44719","ATGGATTTTTCCGTAGATTCCGAAATCGGGAAGCTGCGCCAGGTCATTCTGCACAGGCCCGGTAACGAGATGCTCCGACTCACTCCGCAGAACAAGGACCACCTCCTGTTCGATGACGTGCTGTGGCTCGAGCGGGCCCAGGAGGAGCACGACCAGTTCGCACGAGTGCTGACCGACCGCGACATCGAGGTGCTCTATCTCAGCGACCTGCTGGCCCAGACCCTCGAGGTGCCCGAAGCCAGGCAGTACGTCCTGGACCGAGTCGTCAACGAGAACACCAACGGCCCCAGTGCCGCCGAGCCGCTGCGCGCCCTGGCTCAGGGGCTGTCCGGGGCCGAGCTGGCCGAGGTGCTCATCGCCGGGATCACGAAGGCCGAGCTGCTCGAGCGCACCTCCTGCCCGGACTCGCTCGTGCTGGCCTCCATGGAAGACGACGACCTGCTTCTGCCGCCGCTGCCCAACCACCTCTTCACTCGCGATACGTCTTGCTGGATCTACAACGGCGTCTCCATCAACTCGATGATGATGCCGGCCCGGAAGCGCGAGACCATCAACTACGAGGCGATCTACCGCTGGCACCCTCTCTTCGCCGGCTCCGACTTCCCCGTGTGGTCCGAGGGCACACAGGCCGGCCCCGCCACCGTGGAGGGTGGAGACGTCCAGATCATCGGCAACGGCGCCGTTCTGGTCGGCGTCTCCGAGCGCACCACCTCGCAGGGCATCGAGAGGCTCGCCAGCCGGCTCTTCGCCGGAGGCAAGGTGAACCAGATCGTCGCCGTCGAGATGAACCGGACGCGCGCCCAGATGCACCTGGACACGGTGATGACCATGGTCGACGTCGGCACGTTCACCATCTACGGCGGCCTGGGGAAGCTGCCGACGCTCACGCTGCGCCCGGACGGTGACAGGCAGATCAGCGTCACGCGCAACGCCCCCGAGGACATGTACCGCGTCATCGCCAAGGCCCTGGGTGTCGACGAGCTCAACGTTCTCATCACGCCCCAGGACTCGATGGCCGCCGCCCGTGAGCAGTGGGACGACGGATCCAACTCCCTGGCCATCGCCCCCGGTGTCATCGTTACCTATGAACGTAACGTCAACACGAACGAGTACCTTACTTCCCATGGCATCGAGGTCCTGACCATTCCCGGTTCGGAGGTCGGTCGCGGTCGCGGTGGTCCACACTGCATGAGCTGCCCGACCCTGCGGGACCCGCTTGCCTGA","MDFSVDSEIGKLRQVILHRPGNEMLRLTPQNKDHLLFDDVLWLERAQEEHDQFARVLTDRDIEVLYLSDLLAQTLEVPEARQYVLDRVVNENTNGPSAAEPLRALAQGLSGAELAEVLIAGITKAELLERTSCPDSLVLASMEDDDLLLPPLPNHLFTRDTSCWIYNGVSINSMMMPARKRETINYEAIYRWHPLFAGSDFPVWSEGTQAGPATVEGGDVQIIGNGAVLVGVSERTTSQGIERLASRLFAGGKVNQIVAVEMNRTRAQMHLDTVMTMVDVGTFTIYGGLGKLPTLTLRPDGDRQISVTRNAPEDMYRVIAKALGVDELNVLITPQDSMAAAREQWDDGSNSLAIAPGVIVTYERNVNTNEYLTSHGIEVLTIPGSEVGRGRGGPHCMSCPTLRDPLA$","Arginine deiminase","Cytoplasm","arginine deiminase","arginine deiminase ","Arginine deiminase","","Kanaoka M., Fukita Y., Taya K., Kawanaka C., Negoro T., Agui H. Antitumor activity of streptococcal acid glycoprotein produced by Streptococcus pyogenes Su. Jpn. J. Cancer Res. 1987. 78(12):1409-1414. PMID: 3123442","","","

InterPro
IPR003198
Domain

Amidinotransferase
PF02274	$\"[7-403]T$	Amidinotransf

InterPro
IPR003876
Family

Arginine deiminase
PR01466	$\"[1-21]T$ $\"[151-169]T$ $\"[179-194]T$ $\"[342-359]T$ $\"[362-376]T$ $\"[385-403]T$	ARGDEIMINASE

noIPR
unintegrated

unintegrated
G3DSA:3.75.10.10	$\"[149-401]T$	no description
PTHR12737	$\"[152-248]T$	DIMETHYLARGININE DIMETHYLAMINOHYDROLASE

","BeTs to 7 clades of COG2235COG name: Arginine deiminaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2235 is -o-p------rl---fg----j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB003876 (Bacterial arginine deiminase signature) with a combined E-value of 1.3e-67. IPB003876A 1-21 IPB003876B 151-169 IPB003876C 179-194 IPB003876D 342-359 IPB003876E 362-376 IPB003876F 385-403***** IPB003198 (Amidinotransferase) with a combined E-value of 7.3e-54. IPB003198A 7-38 IPB003198B 158-182 IPB003198C 269-289 IPB003198D 372-403","Residues 5-252 are similar to a (ARGININE DEIMINASE HYDROLASE DIHYDROLASE ADI AD METABOLISM ARCA GLYCOPROTEIN SEQUENCING) protein domain (PD005361) which is seen in Q93JF2_STRCO.Residues 258-404 are 72% similar to a (ARGININE DEIMINASE HYDROLASE DIHYDROLASE ADI AD METABOLISM ARCA GLYCOPROTEIN SEQUENCING) protein domain (PD478985) which is seen in Q82KQ3_STRAW.","","-60% similar to PDB:1RXX Structure of arginine deiminase (E_value = 1.2E_85);-60% similar to PDB:2ABR Structure of D280A arginine deiminase with L-arginine forming a S-alkylthiouronium reaction intermediate (E_value = 1.0E_84);-60% similar to PDB:2ACI Structure of D166A arginine deiminase (E_value = 1.0E_84);-60% similar to PDB:2A9G Structure of C406A arginine deiminase in complex with L-arginine (E_value = 1.4E_84);-60% similar to PDB:2AAF Structure of H278A arginine deiminase with L-arginine forming a S-alkylthiouronium reaction intermediate (E_value = 1.8E_84);","Residues 7 to 403 (E_value = 9.6e-146) place ANA_0793 in the Amidinotransf family which is described as Amidinotransferase.","","deiminase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0794","847355","848362","1008","5.06","-15.88","37204","ATGTCCCACCCCCTGCACAACCGCAGTTTCCTCAAAGAGCTCGACTTCACGGCTGAGGAGTGGAGCTCCCTGCTTGAGCTGGCCGCCCAGCTCAAGGCGGATAAGAAGGCCGGCCGCGAAGTGAAGCGCCTGGCCGGTAAGAATATCGCTCTCATCTTTGAGAAGACCTCGACGCGGACCCGCTGCTCCTTCGAGGTGGCGGCCTATGACCAGGGCGCACAGGTCACCTACCTCGACCCCTCCGGTTCCCAGATGGGCCACAAGGAGTCCGTGGCGGACACCGCCCGGGTGCTGGGCCGTTTCTACGACGGCATCGAGTTCCGTGGCAAGAAGCAGGAGCACGTCGAGGCCCTGGCTGAGCTCTCCGGCGTCCCCGTGTGGAACGGACTGACGGATGAGTGGCACCCCACCCAGATGCTGGCCGACCAGCTGACCATGCTGGAGCACGCCGACAAGCCGATCGAGCAGATCTCCTTCGCCTACCTGGGTGACGCGCGCAACAACGTTGCCAACTCGCTGCTGATCTCGGCGGCCCTCATGGGGATGGACGTGCGGATGGTGGCTCCCAAGGAGCTGCAGACCTCTCTCGAGGTGGTGGCTCAGGCCGAGAAGCTGGCCAAGGACAGCGGTGCCCGCATCCTCATCACCGACGACGTCGCCGAGGGCGTCAAGGGCGTCGACTTCCTCTACACCGACGTGTGGGTCTCCATGGGTGAGCCCAAGGAGGTCTGGGACCAGCGCATCGCTCTGCTTGCGCCCTACCAGGTCAACGCCCAGCTGGTGGAGGCCACCGGTAACCCTGACGTGAAGTTCCTCCACTGCCTGCCGGCCTTCCACGACCGCAACACCACGGTGGGTGAGGACATCTTCGCCAAGACCGGCATGGAGGGTCTGGAGGTGACCGACGACGTCTTCGAGACCGAGCGCAACGTCGCCTTCGACCAGGCCGAGAACCGTATGCACACCATCAAGGCCGTGATGGTCGCGACCCTGGGAATGTGGGACTGA","MSHPLHNRSFLKELDFTAEEWSSLLELAAQLKADKKAGREVKRLAGKNIALIFEKTSTRTRCSFEVAAYDQGAQVTYLDPSGSQMGHKESVADTARVLGRFYDGIEFRGKKQEHVEALAELSGVPVWNGLTDEWHPTQMLADQLTMLEHADKPIEQISFAYLGDARNNVANSLLISAALMGMDVRMVAPKELQTSLEVVAQAEKLAKDSGARILITDDVAEGVKGVDFLYTDVWVSMGEPKEVWDQRIALLAPYQVNAQLVEATGNPDVKFLHCLPAFHDRNTTVGEDIFAKTGMEGLEVTDDVFETERNVAFDQAENRMHTIKAVMVATLGMWD$","Ornithine carbamoyltransferase","Cytoplasm","ornithine carbamoyltransferase","ornithine carbamoyltransferase ","ornithine carbamoyltransferase","","Martin P.R., Cooperider J.W., Mulks M.H. Sequence of the argF gene encoding ornithine transcarbamoylase from Neisseria gonorrhoeae. Gene 1990. 94(1):139-140. PMID: 2121620Baur H., Stalon V., Falmagne P., Luethi E., Haas D. Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli. Eur. J. Biochem. 1987. 166(1):111-117. PMID: 3109911Huygen R., Crabeel M., Glansdorff N. Nucleotide sequence of the ARG3 gene of the yeast Saccharomyces cerevisiae encoding ornithine carbamoyltransferase. Comparison with other carbamoyltransferases. Eur. J. Biochem. 1987. 166(2):371-377. PMID: 3038540Upshall A., Gilbert T., Saari G., O. Hara P.J., Weglenski P., Berse B., Miller K., Timberlake W.E. Molecular analysis of the argB gene of Aspergillus nidulans. Mol. Gen. Genet. 1986. 204(2):349-354. PMID: 3020372Mosqueda G., Van den Broeck G., Saucedo O., Bailey A.M., Alvarez-Morales A., Herrera-Estrella L. Isolation and characterization of the gene from Pseudomonas syringae pv. phaseolicola encoding the phaseolotoxin-insensitive ornithine carbamoyltransferase. Mol. Gen. Genet. 1990. 222(2):461-466. PMID: 2274044","","","

InterPro
IPR002292
Family

Ornithine carbamoyltransferase
PR00102	$\"[51-65]T$ $\"[84-97]T$ $\"[124-138]T$ $\"[229-239]T$ $\"[310-321]T$	OTCASE
TIGR00658	$\"[8-332]T$	orni_carb_tr: ornithine carbamoyltransferas

InterPro
IPR006130
Family

Aspartate/ornithine carbamoyltransferase
PR00100	$\"[53-72]T$ $\"[135-146]T$ $\"[267-276]T$ $\"[296-319]T$	AOTCASE
PIRSF000416	$\"[8-335]T$	Ornithine/aspartate carbamoyltransferase
PS00097	$\"[53-60]T$	CARBAMOYLTRANSFERASE

InterPro
IPR006131
Domain

Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region
PF00185	$\"[154-330]T$	OTCace

InterPro
IPR006132
Domain

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
PF02729	$\"[8-149]T$	OTCace_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1370	$\"[138-333]T$	no description
PIRSF500170	$\"[8-333]T$	Ornithine carbamoyltransferase
PTHR11405	$\"[136-280]T$ $\"[298-331]T$	CARBAMOYLTRANSFERASE RELATED
PTHR11405:SF1	$\"[136-280]T$ $\"[298-331]T$	ORNITHINE CARBAMOYLTRANSFERASE

","BeTs to 23 clades of COG0078COG name: Ornithine carbamoyltransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0078 is aompkzyqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002292 (Ornithine carbamoyltransferase signature) with a combined E-value of 1.2e-47. IPB002292A 51-65 IPB002292B 84-97 IPB002292C 124-138 IPB002292D 229-239 IPB002292E 310-321***** IPB002082 (Aspartate carbamoyltransferase signature) with a combined E-value of 3.9e-25. IPB002082A 43-65 IPB002082B 81-90 IPB002082C 134-151 IPB002082E 271-276 IPB002082F 312-326","Residues 39-142 are 88% similar to a (TRANSFERASE CARBAMOYLTRANSFERASE ASPARTATE ORNITHINE BIOSYNTHESIS ARGININE OTCASE TRANSCARBAMYLASE PYRIMIDINE ATCASE) protein domain (PD000708) which is seen in OTC_ECOL6.Residues 88-279 are 47% similar to a (TRANSCARBAMYLASE ORNITHINE) protein domain (PD803190) which is seen in Q9AHW8_CARRU.Residues 144-332 are 80% similar to a (TRANSFERASE CARBAMOYLTRANSFERASE ASPARTATE ORNITHINE BIOSYNTHESIS ARGININE OTCASE TRANSCARBAMYLASE PYRIMIDINE ATCASE) protein domain (PD409592) which is seen in OTC_PASMU.Residues 154-220 are 65% similar to a (TRANSFERASE CARBAMOYLTRANSFERASE ORNITHINE ANABOLIC) protein domain (PDA0W312) which is seen in Q6NHG6_CORDI.","","-80% similar to PDB:1AKM ORNITHINE TRANSCARBAMYLASE FROM ESCHERICHIA COLI (E_value = 1.1E_118);-80% similar to PDB:1DUV CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN) (E_value = 1.1E_118);-80% similar to PDB:2OTC ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE (E_value = 1.9E_118);-78% similar to PDB:1DXH CATABOLIC ORNITHINE CARBAMOYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA (E_value = 6.8E_116);-77% similar to PDB:1ORT ORNITHINE TRANSCARBAMOYLASE FROM PSEUDOMONAS AERUGINOSA (E_value = 4.4E_115);","Residues 8 to 149 (E_value = 6.3e-73) place ANA_0794 in the OTCace_N family which is described as Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain.Residues 154 to 330 (E_value = 9.4e-84) place ANA_0794 in the OTCace family which is described as Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain.","","carbamoyltransferase (argF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0795","848366","849346","981","5.18","-10.62","34808","GTGAGAATCGTTGTCGCCCTCGGAGGAAACGCCCTGCTTCGTCGGGGGGAGAAGCCCGACGCCAGTACCCAGATCCGCAATGTCGAGATTGCGGCCCATGAGCTGGCCAAGTTGGCGGAGAAGCACGAGCTGGTCCTGACTCACGGGAACGGCCCCCAGGTGGGGGTCCTGGCTCTGCAGTCCGCCAATGACGAGCGCCTCTCCGAGCCCTACCCCTTCGACACCCTCGGTGCCCAGACGCAGGGCATGATCGGATACTGGTTGCTGCAGGCCATGCAGAACGCCCTGCCCGGTCGCCACGTGGCTGCCATGGTCAACCAGACCCTGGTGATGGCCGGTGACCCGGCCTTCTCCAACCCCACCAAGTTCGTCGGTGAGGTGTACACCAAGGAGGAGGCCGAGAAGCTGGCTGAGGAGCGGGGCTGGGTGGTCAAGCCCGACGGCGAGCACTACCGCCGCGTCGTCGGCTCCCCCATGCCGCAGCGCGTCATCGAGACCCGCCTGGTGCGCACCCTGCTGGATGCCGGTGCGATCGTCGTTTGCTCCGGCGGCGGCGGTGTCCCCGTCGTCCGTAGCGAGGAGGGCAAGCTCAAGGGTATTGAAGCCGTCATCGACAAGGACCTGACGGCGTCGGTCATGGCTGAGGCCCTGGAGGCTGATGCGCTTCTCATCCTCACGGACGTTGATGGAGTGTTTCAGGACTTCGGGACTGAGAACCAGAAACAGGTTCCGAGGGCGACTCCGGCAGAACTGCGGTCCATGGGACTTCCCAGTGGTTCCATGGGACCAAAGGTCGAGGCGGTGTGCCGATTTGTTGAGTTGACCGGTGATATGGCGGCAATTGGACGTCTTGAGGACGCCGTTTCCATCATTGAGGGCCAGGCAGGGACTATCGTGACTCCCGGAGGAAACTATGGGGGCCCAGACGATATCCATCCCCCAATTCCCGAGCAGCTTGACACGCGCATCCGCAGGGCCTGA","VRIVVALGGNALLRRGEKPDASTQIRNVEIAAHELAKLAEKHELVLTHGNGPQVGVLALQSANDERLSEPYPFDTLGAQTQGMIGYWLLQAMQNALPGRHVAAMVNQTLVMAGDPAFSNPTKFVGEVYTKEEAEKLAEERGWVVKPDGEHYRRVVGSPMPQRVIETRLVRTLLDAGAIVVCSGGGGVPVVRSEEGKLKGIEAVIDKDLTASVMAEALEADALLILTDVDGVFQDFGTENQKQVPRATPAELRSMGLPSGSMGPKVEAVCRFVELTGDMAAIGRLEDAVSIIEGQAGTIVTPGGNYGGPDDIHPPIPEQLDTRIRRA$","Carbamate kinase","Cytoplasm","carbamate kinase","carbamate kinase ","carbamate kinase","","Kikuchi Y., Kojima H., Tanaka T. Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli. FEMS Microbiol. Lett. 1999. 173(1):211-215. PMID: 10220897Kochhar S., Kochhar V.K., Sane P.V. Subunit structure of lysine sensitive aspartate kinase from spinach leaves. Biochem. Mol. Biol. Int. 1998. 44(4):795-806. PMID: 9584993Zhu-Shimoni J.X., Galili G. Expression of an arabidopsis aspartate Kinase/Homoserine dehydrogenase gene is metabolically regulated by photosynthesis-related signals but not by nitrogenous compounds. Plant Physiol. 1998. 116(3):1023-1028. PMID: 9501134","","","

InterPro
IPR001048
Domain

Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10	$\"[2-301]T$	no description
PF00696	$\"[1-283]T$	AA_kinase

InterPro
IPR003964
Family

Bacterial carbamate kinase
PR01469	$\"[41-60]T$ $\"[72-90]T$ $\"[103-122]T$ $\"[151-170]T$ $\"[174-192]T$ $\"[205-220]T$ $\"[256-271]T$	CARBMTKINASE
PIRSF000723	$\"[1-301]T$	Carbamate kinase
TIGR00746	$\"[2-301]T$	arcC: carbamate kinase

","BeTs to 9 clades of COG0549COG name: Carbamate kinaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0549 is -o-pkz-----l-cef-h-------wNumber of proteins in this genome belonging to this COG is 1","***** IPB003964 (Bacterial carbamate kinase signature) with a combined E-value of 2.2e-65. IPB003964A 41-60 IPB003964B 72-90 IPB003964C 103-122 IPB003964D 151-170 IPB003964E 174-192 IPB003964F 205-220 IPB003964G 256-271***** IPB001057 (Glutamate 5-kinase) with a combined E-value of 3.3e-10. IPB001057D 203-236","Residues 8-287 are 72% similar to a (KINASE TRANSFERASE CARBAMATE METABOLISM ARGININE KINASE-LIKE PLASMID PHOSPHATE YAHI SYNTHETASE) protein domain (PD004953) which is seen in ARCC_SYNY3.","","-55% similar to PDB:1E19 STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS BOUND TO ADP (E_value = 6.0E_53);-50% similar to PDB:1B7B Carbamate kinase from Enterococcus faecalis (E_value = 1.8E_36);-59% similar to PDB:2BMU UMP KINASE FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ITS SUBSTRATE UMP AND ITS SUBSTRATE ANALOG AMPPNP (E_value = 1.8E_36);-59% similar to PDB:2BRI UMP KINASE FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ITS SUBSTRATE ANALOG AMPPNP (E_value = 1.8E_36);-59% similar to PDB:2BRX UMP KINASE FROM PYROCOCCUS FURIOSUS WITHOUT LIGANDS (E_value = 1.8E_36);","Residues 1 to 283 (E_value = 8.4e-73) place ANA_0795 in the AA_kinase family which is described as Amino acid kinase family.","","kinase (arcC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0796","849556","850683","1128","5.10","-16.00","43191","ATGACGAAGATCGTCAACTCTTGGAACGACTTCGACCCTCTTAAGCGTGTCATCGTCGGACGCGCCGACTTCTCGGTTATTCCTCCCGAGGAGCCCGCCACCTCTGAGAAGGTGCCGATCGACTCCGAGATGCGCGGCATGTGGGGCCCCCGCCCCACTGCCACCGTCGAGGCCGCCAACGAGCAGCTCGACAACTACGTCAAGATCCTCGAGGGTCTGGGCGTCCAGGTGGACCGCCCCACGCCGCTGCAGTGGAACCAGGCCATCCAGACGCCTGACTTCCGCACGGAGTCGGGTTTCACCCAGATGCCCCCGCGTGACATCCTGCTCACCATCGGTGATGAGATCATGGCGTCGGCCAACTCGTTCCGCTGCCGCTACTTCGAGTACCTCGCCTACTGGCCCCTCATGAACCAGTACTTCGAGGAGGACCCGGAGTTCAAGTGGACCCAGGCCCCTCGTCCGCGGCTGACGGACAAGTCCTACAAGCACAACTACTACGACGAGCGGATCTCCCTGGAGGAGCGCCTTGAGCGCACCGCCGCCAAGGACTTCGTGACCACTGAGGTTGAGCCGATGTGGGACGCCGCCGACGTCATGCGCGTGGGTAAGGACCTGTTCATCCAGCACGGTCTGACCACCAACCGCAAGGCGATGGAGTGGTTCAAGCGCTACTACCCGGACCTGCGGGTGCACGCGGTGAACTTCCCCGGCGACCCCTACCCGATCCACATCGACGCCACCTTCGTGCCGCTGCGGCCCGGGCTCATCATCAACAACCCGCACCGCCGCCTGCCCGAGGAGCAGCGCAAGATCTTCGAGGCCAACGACTGGCAGATCGTCGACGCCGCTCCCCCGGCCCACGAGGTTCCGCCGCCGCTGTGCTACTCCTCGGTCTGGCTGTCCATGAACTGCCTGGTCATCGACCACAAGACCGTGTGTGTCGAGGCCAGCGAGGTCCACCAGATGGAGCAGATGGACAAGCTGGGCATGAATGTCATCCCGGTTCCCTTCCGCGACGCCTACGCCTTCGGCGGTGGTCTGCACTGCGCAACGGCCGACGTCTACCGTGAGGGTGGCTGCGAGGACTACTTCCCCAACCAGGTCGCTGACCCGACTCTGGTCTGA","MTKIVNSWNDFDPLKRVIVGRADFSVIPPEEPATSEKVPIDSEMRGMWGPRPTATVEAANEQLDNYVKILEGLGVQVDRPTPLQWNQAIQTPDFRTESGFTQMPPRDILLTIGDEIMASANSFRCRYFEYLAYWPLMNQYFEEDPEFKWTQAPRPRLTDKSYKHNYYDERISLEERLERTAAKDFVTTEVEPMWDAADVMRVGKDLFIQHGLTTNRKAMEWFKRYYPDLRVHAVNFPGDPYPIHIDATFVPLRPGLIINNPHRRLPEEQRKIFEANDWQIVDAAPPAHEVPPPLCYSSVWLSMNCLVIDHKTVCVEASEVHQMEQMDKLGMNVIPVPFRDAYAFGGGLHCATADVYREGGCEDYFPNQVADPTLV$","Glycine amidinotransferase","Cytoplasm","amidinotransferase family protein","glycine amidinotransferase ","Glycine amidinotransferase","","","","","

InterPro
IPR003198
Domain

Amidinotransferase
PF02274	$\"[9-357]T$	Amidinotransf

noIPR
unintegrated

unintegrated
G3DSA:3.75.10.10	$\"[3-366]T$	no description
PTHR10488	$\"[8-362]T$	AMIDINOTRANSFERASE

","No hits to the COGs database.","***** IPB003198 (Amidinotransferase) with a combined E-value of 1.2e-27. IPB003198A 9-40 IPB003198B 105-129 IPB003198C 243-263 IPB003198D 326-357","Residues 4-280 are 44% similar to a (TRANSFERASE RELATED AMIDINOTRANSFERASE L-ARGININE:LYSINE) protein domain (PD844822) which is seen in Q871A1_NEUCR.Residues are similar to a () protein domain () which is seen in .","","-59% similar to PDB:1JDW CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS (E_value = 7.2E_69);-59% similar to PDB:1JDX CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH L-NORVALINE (E_value = 7.2E_69);-59% similar to PDB:2JDW CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS (E_value = 7.2E_69);-59% similar to PDB:3JDW CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS (E_value = 7.2E_69);-59% similar to PDB:5JDW CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH GLYCINE (E_value = 7.2E_69);","Residues 9 to 357 (E_value = 0.0002) place ANA_0796 in the Amidinotransf family which is described as Amidinotransferase.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0797","850871","851884","1014","9.10","7.98","35679","ATGTCACAGACATCGTCCGCTGAATCCTCTGTCACAGAGTACGTCATGAACAAGAAGCTGGGCGCCATCGCCATGCTTCTCTCCGCCACTGGGATGGGGCTCGTCGGCACCATCAGTCGTGGCACGACCGCTGGCCTCGCTGACGCCGACAAGTCCGTCATCGGTTCGTTCCTGGCCTTCGGGCGCATGAGCGTCGGACTGCTTGGATTCATCCTCATCCTCGTTCTCACCGGGAAGGCCGGGTTGTTCAAGAGCACCCGTCTGAGCACCACCGTGATCCTGGGAGGCGTGAGCATCGGCCTGTCCCTGGGCTGCTACATCTCCTCGACGTTGATGACGACCATTTCCAATGCCGTCTTCCTCATCTACACAGGACCCTTGTTCTGTGCACTGCTCGCACGCATTTTCCGCAAAGAGAGGATCAGCGTGCTCTCCGGCATATTCCTGTCTCTTGTGTTCATAGGAATGCTGCTGACCATTGGAATCATCGACTACAAGAACGGAAGTCTGACCTTCGGGCTGGATCTGTCTGCCACAACGCCTGAGTTCCCTCAGAAGAGCCTGGGAGATCTTTTAGGCCTGCTGTCCGGCGTCTTTTACGGTCTGGCTCTGTTCTTCTACGGGTACCGCAAGGATGTCGATTCGATCGTCCGCGGTGTGTGGAACTTCTTCTGGGCCGCCTGCGCGACGCTGGTGATGTCCATCGTCTTGCGTCCTTGGCACGGCGTTTCCACCTTCACCGCCACTAACTGGATGTGGGCAGTGGCCCTCTTCCTCGTCTGCGGCCTCTTCGCACTGGGGTTCCTGGTCGTTGCAGGACGCAACCTACCTGCCGTTGAGTACTCGACGATCTCCTACTGGGAGTGTCCGGTCGCCATTCTGTGCGGCCTGCTCGTCTGGGGAGAGAAGCTCACGCCCGTGGGGATGATCGGTGGACTGCTCATTGTCGGTGGTGGGTTGGCCCCGATCATTGTCGATGCCACCGCCCGGAAATCACGTGCCTCCACTTCCTGA","MSQTSSAESSVTEYVMNKKLGAIAMLLSATGMGLVGTISRGTTAGLADADKSVIGSFLAFGRMSVGLLGFILILVLTGKAGLFKSTRLSTTVILGGVSIGLSLGCYISSTLMTTISNAVFLIYTGPLFCALLARIFRKERISVLSGIFLSLVFIGMLLTIGIIDYKNGSLTFGLDLSATTPEFPQKSLGDLLGLLSGVFYGLALFFYGYRKDVDSIVRGVWNFFWAACATLVMSIVLRPWHGVSTFTATNWMWAVALFLVCGLFALGFLVVAGRNLPAVEYSTISYWECPVAILCGLLVWGEKLTPVGMIGGLLIVGGGLAPIIVDATARKSRASTS$","Permease of the drug/metabolite transporter (DMT) superfamily","Membrane, Extracellular","Integral membrane protein domain protein","hypothetical transporter","protein of unknown function DUF6, transmembrane","","","","","

InterPro
IPR000620
Domain

Protein of unknown function DUF6, transmembrane
PF00892	$\"[57-161]T$ $\"[198-318]T$	DUF6

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[20-38]?$ $\"[57-77]?$ $\"[92-112]?$ $\"[118-136]?$ $\"[141-163]?$ $\"[191-209]?$ $\"[219-239]?$ $\"[253-273]?$ $\"[283-301]?$ $\"[307-325]?$	transmembrane_regions

","BeTs to 8 clades of COG0697COG name: Permeases of the drug/metabolite transporter (DMT) superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],RThe phylogenetic pattern of COG0697 is aompkzyqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","Residues 16-89 are 68% similar to a (PROTEIN PERMEASE) protein domain (PD968476) which is seen in Q6AA27_PROAC.Residues 106-163 are similar to a (MEMBRANE TRANSMEMBRANE PERMEASE DRUG/METABOLITE TRANSPORTER PROTEIN FAMILY TRANSPORTER EXPORTER SUPERFAMILY) protein domain (PD062115) which is seen in Q6LTH5_PHOPR.Residues 260-305 are similar to a (MEMBRANE TRANSMEMBRANE PROTEIN INTEGRAL FAMILY TRANSPORTER DRUG/METABOLITE TRANSPORTER PERMEASE EXPORTER) protein domain (PD058316) which is seen in Q6AA27_PROAC.Residues 198-255 are 64% similar to a (TRANSPORTER PROTEIN PERMEASE) protein domain (PD894761) which is seen in Q6AA27_PROAC.Residues 260-305 are similar to a (MEMBRANE TRANSMEMBRANE PROTEIN INTEGRAL FAMILY TRANSPORTER DRUG/METABOLITE TRANSPORTER PERMEASE EXPORTER) protein domain (PD058316) which is seen in Q6AA27_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 38 to 161 (E_value = 7.1e-06) place ANA_0797 in the DUF6 family which is described as Integral membrane protein DUF6.Residues 198 to 324 (E_value = 0.00099) place ANA_0797 in the DUF6 family which is described as Integral membrane protein DUF6.","","membrane protein domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0798","852016","853392","1377","7.91","3.72","49853","ATGAACACCTCCCACTCAGGAAGCACGAAGGACCATCATCTGGATTCAGAACGAAGTCTCGCACTGAGGCGTGCAGCGAAGGCGAGCTTCATCGGCAACTTCATTGAGTGGTTCGACTATGCCTCGTACGGATACCTGGTTACCGTCATTGGTCACGCATTCTTCCCCGCCGCTGACAAATCAGTCCAGTTGCTCTCGACATACGCAGTGTTCGCGATGTCTTTCATTCTGCGCCCGATCGGAGCCGTCGTATGGGGGGCATGGGGAGACCGTTGGGGGCGCCGTTGGGCACTGTCGTGGTCGATTCTTATCATGTCCGGATCGACATTCTTCATCGGTCTCCTTCCCACTTATGCAGCTATCGGCATGGCAAGTGCTATCGGCCTCCTTGTCCTGCGAATGATTCAGGGATTCTCCGCCTCCGGTGAGTACGCGGGTGCCGGAACCTTCCTGGCCGAGTACGCCCCTCCGGCTCGTCGCGGTATCTACACGTCGCTGGTTCCGGCTTCTACCGCCTGTGGCCTGCTTGCCGGCTCTCTCATGGTGACGGGCATGTTCTCGGTCCTCAGTGAGGATGCCATGAATACCTGGGGCTGGCGAGTCCCCTTCCTTCTGGCGGGGCCACTGGGTCTCATCGGTCGCTACATCCGGGTGCACCTGGAGGACTCTCCCGCCTACCAGGAGATGCGTGCGGAGATGCCGCAGGAACAGAAGGCGACCAGCTGGTCCGAGCCGCTGCGGCTGCTGCTGCGGGACCACCTGCATGAGACCCTCATTACCTTTGGAGTCTCCTGCCTCAACGCCGTTGCCTTCTACATGCTTCTCACCTACATGCCGACGTATGTTCACGAAGAGCTCGGGTTCTCCCAGGACACCTCCACTCTGGCTACCTCGGTGATGCTGGTCGTCTACATTGCGGCAATCTTCCTCATGGGGCACCTGTCGGACTCCTTCGGGCGCCGTCGAATGCTTATCGCTGCTTGCGTCGCATTCATTGTGCTCACGATTCCGTTGTTCGTTGTGATGACGAAGGCTGCGGGCATGCTTGCAGCGGTCATCCTGTGTCAGATCGTGTTCGCTATAGCGTTGACGGCTAATGATGGAACTCTGGCCACTTTCCTGGCTGAGTCCTTCCCGACCAACGTGCGCTACTCGGGCTTTGCCCTATCCTTCAATGGGGCCAATGCGCTTCTTGGCGGAACGACGCCGTTCATTGTCACATGGCTCATCAAGGTCACTGGTTCCCCCCTGGCGCCGGCGGTTTATCTCACGGTGATAGCGCTGATCGCCATGGTGGCAATCTTCCGTTCTCGTGCGATTCATGGGTCGGAGCTGACTGAGGAGCGGGCTCACTCCGAACTCCGACCCACTCACTGA","MNTSHSGSTKDHHLDSERSLALRRAAKASFIGNFIEWFDYASYGYLVTVIGHAFFPAADKSVQLLSTYAVFAMSFILRPIGAVVWGAWGDRWGRRWALSWSILIMSGSTFFIGLLPTYAAIGMASAIGLLVLRMIQGFSASGEYAGAGTFLAEYAPPARRGIYTSLVPASTACGLLAGSLMVTGMFSVLSEDAMNTWGWRVPFLLAGPLGLIGRYIRVHLEDSPAYQEMRAEMPQEQKATSWSEPLRLLLRDHLHETLITFGVSCLNAVAFYMLLTYMPTYVHEELGFSQDTSTLATSVMLVVYIAAIFLMGHLSDSFGRRRMLIAACVAFIVLTIPLFVVMTKAAGMLAAVILCQIVFAIALTANDGTLATFLAESFPTNVRYSGFALSFNGANALLGGTTPFIVTWLIKVTGSPLAPAVYLTVIALIAMVAIFRSRAIHGSELTEERAHSELRPTH$","Metabolite MFS transporter, MHS family","Membrane, Cytoplasm","metabolite MFS transporter, MHS family","K03762 MFS transporter; MHS family; proline/betaine transporter","major facilitator superfamily MFS_1","","Saenz H.L., Augsburger V., Vuong C., Jack R.W., Gotz F, Otto M. Inducible expression and cellular location of AgrB, a protein involved in the maturation of the staphylococcal quorum-sensing pheromone. Arch. Microbiol. 2000. 174(6):452-455. PMID: 11195102Zhang L., Gray L., Novick R.P., Ji G. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 2002. 277(38):34736-34742. PMID: 12122003","","","

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[237-418]T$	no description

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[25-438]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[29-411]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR11600	$\"[9-432]T$	SUGAR TRANSPORTER
PTHR11600:SF21	$\"[9-432]T$	PROLINE/BETAINE TRANSPORTER
tmhmm	$\"[40-58]?$ $\"[64-86]?$ $\"[96-116]?$ $\"[122-140]?$ $\"[161-190]?$ $\"[196-216]?$ $\"[257-275]?$ $\"[294-314]?$ $\"[324-342]?$ $\"[348-366]?$ $\"[387-407]?$ $\"[417-435]?$	transmembrane_regions

","BeTs to 20 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","***** IPB005829 (Sugar transporter superfamily) with a combined E-value of 1.2e-08. IPB005829B 129-176","Residues 118-169 are similar to a (TRANSMEMBRANE TRANSPORTER MEMBRANE PROLINE/BETAINE PERMEASE SUGAR FACILITATOR MAJOR MFS FAMILY) protein domain (PD216722) which is seen in Q8G868_BIFLO.Residues 171-234 are 62% similar to a (TRANSMEMBRANE PROLINE/BETAINE TRANSPORTER PROP HOMOLOGUE) protein domain (PDA1E0A0) which is seen in Q8NXW9_STAAW.Residues 174-227 are similar to a (TRANSMEMBRANE TRANSPORTER PERMEASE MEMBRANE SUGAR FACILITATOR MAJOR MFS FAMILY PROLINE/BETAINE) protein domain (PD189710) which is seen in Q8G868_BIFLO.Residues 175-231 are 64% similar to a (TRANSMEMBRANE SUGAR TRANSPORTER GLUCOSE FAMILY GLYCOPROTEIN CARRIER ORGANIC MEMBER HEXOSE) protein domain (PD197893) which is seen in Q6J1M8_YEREN.Residues 236-290 are similar to a (TRANSMEMBRANE TRANSPORTER PROLINE/BETAINE MEMBRANE MFS II PROLINE INNER SYSTEM SYMPORT) protein domain (PD522638) which is seen in Q88GQ2_PSEPK.Residues 293-339 are 72% similar to a (TRANSMEMBRANE TRANSPORTER PERMEASE MEMBRANE ALPHA-KETOGLUTARATE SUGAR METABOLITE TPHA FACILITATOR MAJOR) protein domain (PD427251) which is seen in Q88GQ2_PSEPK.Residues 297-336 are 82% similar to a (TRANSMEMBRANE TRANSPORTER SUGAR RESISTANCE FAMILY MEMBRANE MULTIDRUG FACILITATOR MAJOR PROBABLE) protein domain (PD000082) which is seen in Q8G868_BIFLO.Residues 363-434 are similar to a (TRANSMEMBRANE TRANSPORTER SUGAR PHOSPHATE FAMILY ORGANIC FACILITATOR MAJOR MEMBRANE MFS) protein domain (PD073361) which is seen in Q8G868_BIFLO.Residues 368-440 are 60% similar to a (PROP7 PROLINE/BETAINE TRANSMEMBRANE TRANSPORTER) protein domain (PDA0L5A2) which is seen in Q9ZC87_RICPR.","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 454 (E_value = 3.2e-27) place ANA_0798 in the Sugar_tr family which is described as Sugar (and other) transporter.Residues 29 to 411 (E_value = 3.1e-27) place ANA_0798 in the MFS_1 family which is described as Major Facilitator Superfamily.Residues 260 to 435 (E_value = 1.9e-14) place ANA_0798 in the MFS_1 family which is described as Major Facilitator Superfamily.","","MFS transporter, MHS family (PPII)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0799","853451","854239","789","9.20","5.82","27547","TTGTTACGGACTTCAACGCGTTGTCGTCGTAAGATGATGGGCATGGCTAGTACTGATGCAGATGCCGCTGGAGAGGCAGCGAGTAGTGATACTTCCGTTCCCGCAGGCTCTCGCACGGAATCGCGAGTGACCCCGCGAGGTGAGGACCGTCGTCAGACCATCATCGAAGCCGCGGCGGCCATCATCCGTGAGTCTGGACCTTCCGCGATCAGCCATCGCAGTGTCGCCAAGCGAGCCGGGTGCTCCTTGTCCGCGACAACCTACTACTTCGACGGCTTGGAGGATCTCCTCCACCAGGCGGGGCTGGTCAACATCGGACTGTGGGCGTCTCGGGCGGAGCACGTCGCCGACCGGGTGGAGGCCTTCAAGGGCGTTCCGGACGTCCCCCAACGGGTGCGGTTCATCCTCCAAGCGACTCTTCCCGCCCATGGCGCCTACTTCGGGCACTATCTTCAGCTCATCTCAGCCAGCCAGGCATCACCGGTGAAGCACGCCTACCGTCAGGGGCGGCAACGTCTCAATGCCGCACTGCGCCGCGTGCTGCGCCAGCTCGACAGCCCGCTCGAACCGGAGATGGTCATCGCTGTCGTGGATGGTGCTGCGGTCACCGCGCTCAGTGAGGGGTGGAACGTCAAGTCCACCGCCGCTGGGCTACTGACGGATCTCATCTCTTTGGCCCATGGCATGCCGCTCTTCCAGGCGCCTGGTGGCACAGTGAGCGCTGCGTCGCCTCATGGCTCCCCTGCCACACCGGCCGTCGCTACGGTGACGGGTAGCACCGCCGACTAG","LLRTSTRCRRKMMGMASTDADAAGEAASSDTSVPAGSRTESRVTPRGEDRRQTIIEAAAAIIRESGPSAISHRSVAKRAGCSLSATTYYFDGLEDLLHQAGLVNIGLWASRAEHVADRVEAFKGVPDVPQRVRFILQATLPAHGAYFGHYLQLISASQASPVKHAYRQGRQRLNAALRRVLRQLDSPLEPEMVIAVVDGAAVTALSEGWNVKSTAAGLLTDLISLAHGMPLFQAPGGTVSAASPHGSPATPAVATVTGSTAD$","Transcriptional regulator, TetR family","Cytoplasm, Membrane","transcriptional regulator, TetR family domainprotein","hypothetical protein","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PF00440	$\"[54-100]T$	TetR_N
PS50977	$\"[48-108]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[32-100]T$	no description

","BeTs to 3 clades of COG3226COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3226 is ----------r---ef----------Number of proteins in this genome belonging to this COG is 1","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 3.1e-11. IPB001647 54-96","Residues 42-238 are 59% similar to a (REGULATOR) protein domain (PDA02657) which is seen in Q6AA25_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 54 to 100 (E_value = 0.00055) place ANA_0799 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator, TetR family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0800","856314","854287","2028","8.64","11.56","72052","GTGACGGTGGCCGGGGTCTGTGACCCCGTGGCCAGGGTTCTCCTGGACTCCCCGGTGCCGCACCTCGACCGCACCTTCGACTACTTGGTTCCTGCGGCGATGGCGCAGCAGGCCCTGCCCGGTACCCGGGTCATGGTTCGCTTCGGTGAGCAGGAGATGCGCGGATGGATCTGGGAGCGAGGGTCCACGACCACCCATATCGGCCGGCTGTCTGCTCTGCGGCGAGTAGTCTCCGACCTCCCCGTCCTGCCGGAGGGCTCGCGTCGCCTTATCGAGGCCGTTGCCTCCCGCAGCTGCGGAACACGCTCCGACGTCGTCCGGCTTGCGGTTCCGGCCAGGCACGCCACCACGGAGAAGGCTGAGAGGGACAAGGCTCCCCTCGCACTTCCCACCTGGGAGCCGCCGTCCTCAAGTGAGCTCAGCTGGCAGCCTTACGACGGTGGTGAGGAGTTCCTGAGACGGTTGGCTCACGGTGAGGCTCCACGCGCGGTCTGGTCCGCCCTGCCGGCCCAGCTGCCGCCGCCCGAAGCACGTTCGTCGGACGACGACGGCAGGCGCGTCCCGGTGGTGTCGCCGTGGCAGCTGTGTCTGGCCCGAGCCGTCCAGGCCACCTTGGCGAGCTCTCGCGGTGCCGTCGTCGTGGTGGCAACGACCCATCAGGCTGAGACCCTGGCAGCCCAGCTCAGGCGCGACCTGGAGGGGGAACCGGTGGTGGTGCTCTCGGCCGAGCACGGTCCTGCGCGCCGTTATCGGGCGTTCCTGGCTCTCCTGCTGGGGCGAGCCCGGGTGGTCGTCGGCACCAGGGCGGCGGCCTTCGCCCCGGTGCACCGGCTTGGGCTGGCGGTCGTCTGGGACGACGGGGACAACCGGTTGGAAGAGCCTCACGCCCCCTACAGTCATACGCGCACAGTCCTGGCCCTGCGCTCGACGTTGGATGGAGCCGGCCTGCTCATCGGTGGATTCAGCCGTTCCGTGGAAGCGCAGTCGCTCGTCGAGCAGGGATGGTGTCAGAGTCTGGCGGCGCCACGGCACATTGTGCGCGGTGTTGTCCCTCGTGTGGAGGTTCCTGGCCCGGCAGAGCTGGACCGGGAGGGTGCGTCCGGGGCGGCCCGGCTCCCGTCGCTCGCCCATCAAGCACTGCGGCGGGCCCTGCAGGACGGACCGGTTCTCATCCAGGTGCCGCGCGCCGGCTACGCGCCGTTGGTGGCCTGCGCCCGGTGCCGCGAAGCCGCTCAGTGCGCTGTCTGTGGCGGCCCGCTGGCGATGGACCAACGGGGTCGCACCTCCTGCCGTTGGTGCGCTCGTACGGTGGGGCGGTGGAACTGCCCCGAGTGCGGCGGCCATGGACTGAGGATGGCGACGGTCGGTTCCACGCGTACGGGTGAGGAGCTGGGGCGGGCCTTTCCCGGCGTCCCCGTGGTGGTCTCAGGAGCCAGGGAGGCCCACGGCGTCGTCGACGAGGTAGACGACGCGCCACGTCTCGTGGTGGCCACGCCCGGGGCGGAGCCGGTGGCCGAGGGCGGATTCCGGGCTGTCCTACTTCTCGACGGCGCCGCTCTGTCCTCCCGTCCCGATCTTGGTGCTGCCAGCGAGGCATTGCGCCAGTGGTCCAATGCCGTGGTGCTGGCGGCGCCGTCGGCCCGCGTTGTCCTTCTGGGAGGCCCGGATCCGGTGGCGGCACAGGCTCTCGTGCGATGGGACCAGGCGGGATTCGCCCGCAGAGACCTTCTGGAGCGGGCCGACCTGCACCTACCGCCCGCATGGCGAGTGGCCCGCTTGGACGGGCCGGTACGCGCCGTGGAGTCCCTTCTGGCTCAGGCCGAAGCCGATGGCTTTGAGGTGCTCGGCCCGGTGGCTCCACCGCCCGTTCACGGCCAGGTGCTCCCCGGCGCGGCCAGGGCCCTGGTGCGCGCTCCGCTGTCACGTGGCAAGGCGCTTGCCACCATGCTCGGGGTACGACTGCGCGACCGATCAGCCCACCGCGAGGAGCCGGTTCGTGTTGAGCTCGATCCCACCCGTTTGTGGTGA","VTVAGVCDPVARVLLDSPVPHLDRTFDYLVPAAMAQQALPGTRVMVRFGEQEMRGWIWERGSTTTHIGRLSALRRVVSDLPVLPEGSRRLIEAVASRSCGTRSDVVRLAVPARHATTEKAERDKAPLALPTWEPPSSSELSWQPYDGGEEFLRRLAHGEAPRAVWSALPAQLPPPEARSSDDDGRRVPVVSPWQLCLARAVQATLASSRGAVVVVATTHQAETLAAQLRRDLEGEPVVVLSAEHGPARRYRAFLALLLGRARVVVGTRAAAFAPVHRLGLAVVWDDGDNRLEEPHAPYSHTRTVLALRSTLDGAGLLIGGFSRSVEAQSLVEQGWCQSLAAPRHIVRGVVPRVEVPGPAELDREGASGAARLPSLAHQALRRALQDGPVLIQVPRAGYAPLVACARCREAAQCAVCGGPLAMDQRGRTSCRWCARTVGRWNCPECGGHGLRMATVGSTRTGEELGRAFPGVPVVVSGAREAHGVVDEVDDAPRLVVATPGAEPVAEGGFRAVLLLDGAALSSRPDLGAASEALRQWSNAVVLAAPSARVVLLGGPDPVAAQALVRWDQAGFARRDLLERADLHLPPAWRVARLDGPVRAVESLLAQAEADGFEVLGPVAPPPVHGQVLPGAARALVRAPLSRGKALATMLGVRLRDRSAHREEPVRVELDPTRLW$","Primosomal protein N' (replication factor Y) - superfamily II helicase","Cytoplasm, Membrane","Primosomal protein N'' (replication factor Y) -superfamily II helicase","K04066 primosomal protein N' (replication factor Y) (superfamily II helicase)","Primosomal protein N' (replication factor Y) - superfamily II helicase-like","","Hatakeyama S., Nakayama K.I. Ubiquitylation as a quality control system for intracellular proteins. J. Biochem. 2003. 134(1):1-8. PMID: 12944364Freemont P.S. The RING finger. A novel protein sequence motif related to the zinc finger. Ann. N.Y. Acad. Sci. 1993. 684:174-192. PMID: 8317827Borden K.L., Freemont P.S. The RING finger domain: a recent example of a sequence-structure family. Curr. Opin. Struct. Biol. 1996. 6(3):395-401. PMID: 8804826Saurin A.J., Borden K.L., Boddy M.N., Freemont P.S. Does this have a familiar RING? Trends Biochem. Sci. 1996. 21(6):208-214. PMID: 8744354","","","

InterPro
IPR001841
Domain

Zinc finger, RING-type
SM00184	$\"[413-445]T$	RING

","BeTs to 8 clades of COG1198COG name: Primosomal protein N' (replication factor Y) - superfamily II helicaseFunctional Class: LThe phylogenetic pattern of COG1198 is -----qvcebrhuj--olinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 1-187 are 54% similar to a (PRIMOSOMAL N_apos; REPLICATION HELICASE FACTOR Y DNA-BINDING METAL-BINDING DNA PRIMOSOME) protein domain (PD359235) which is seen in Q9L0Y4_STRCO.Residues 212-357 are 67% similar to a (PRIMOSOMAL PRIA N_apos;) protein domain (PD891607) which is seen in Q827P9_STRAW.Residues 264-357 are 58% similar to a (PRIMOSOMAL N_apos; REPLICATION HELICASE FACTOR Y DNA-BINDING METAL-BINDING DNA PRIMOSOME) protein domain (PD686205) which is seen in Q6AF78_BBBBB.Residues 358-510 are 52% similar to a (PRIMOSOMAL N_apos;) protein domain (PD881556) which is seen in Q6AF78_BBBBB.Residues 407-517 are 50% similar to a (PRIMOSOMAL N_apos;) protein domain (PD716429) which is seen in Q9L0Y4_STRCO.Residues 407-517 are 47% similar to a (PRIMOSOMAL REPLICATION N_apos; HELICASE FACTOR Y DNA-BINDING METAL-BINDING DNA PRIMOSOME) protein domain (PD716427) which is seen in Q827P9_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein N (replication factor Y) - superfamily II helicase","","1","","","Wed Aug 15 11:14:30 2007","","Wed Aug 15 11:14:30 2007","","","Wed Aug 15 11:14:30 2007","Wed Aug 15 11:14:30 2007","Wed Aug 15 11:14:30 2007","Wed Aug 15 11:14:30 2007","","Wed Aug 15 11:04:19 2007","","","Wed Aug 15 11:14:30 2007","","Wed Aug 15 11:04:19 2007","","Wed Aug 15 11:04:19 2007","Wed Aug 15 11:04:19 2007","","","","","yes","","" "ANA_0801","857679","856474","1206","5.41","-11.73","42791","GTGAGTTCCTCCTTACGTCTGTTCACGTCCGAGTCGGTCACTGAAGGACACCCGGACAAGATCTGCGACCGTGTCTCTGACGCGATCCTCGACGCCATCCTCGAGCAGGACCCCACCGCACGCGTCGCGGTCGAGACGATGGTGACGACAGGCCTGGTGCACGTGGCCGGAGAAGTTACCACTGAGAGGGCCTACGTCGAGATCCCCGAAATCGTTCGCCAGGAGATCTCCGCCATCGGCTACACCTCCTCAGATGTCTGCTTCGACGCCCGTTCCTGTGGTGTGTCGGTATCGATCGGGCAGCAGTCCGCGGACATCGCAGCCGGAGTGGACAAGTCCCTTCAGGCCCGCCGGGATGACACGGACATCGACCCCCTCGACCTGCAGGGTGCCGGAGACCAGGGGCTCATGTTCGGCTACGCCTGCGACGACACCGCGGCCCTCATGCCTCTGCCCATCCACCTGGCGCATCGTCTTGCGGAGCGTCTGGCCGCAGTGCGCAAGCAGGGTATTGTCCCGGGACTGCGCCCCGACGGTAAGACCCAGGTGACGATCGGCTATGACGGCCAGCGTCCGGTGAGCCTGCACAACCTGGTCATCTCCACCCAGCACGACGCGGACCGCACGCGTGCCTGGCTCACTGACGCTCTGCGCACGGAGGTCATCGATCCGGTGCTGGCCGCTGAGGCCGAGGCCGGTACCGATCTCGGCACCGCCCACACCGAGGTCCTCATCAATCCCTCGGGGCAGTTCGTCATCGGTGGTCCGGCGGGTGACGCCGGGCTGACGGGACGCAAGATCATCGTGGACACCTACGGCGGGATGGCCCGTCACGGCGGTGGCGCCTTCTCCGGCAAGGATCCCTCGAAGGTGGACCGCTCCGCCAGTTACGCCATGCGTTGGGTCGCCAAGAACGTCGTCGCAGCGGGGCTGGCCAGAAGGTGCGAGATTCAGGTGGCCTACGCCATCGGCTCTGCTCACCCCGTGGGCGTCTACGTGGAGACATTCGGGACGGCGACTGTTCCTGAGGAGCGCATCATGAAGGCCGTCAACGAGGTCTTCGACCTTCGTCCGGCCGCCATTGTGCGCGACCTCGACCTGCTGCGTCCCATCTACCGCGCCACCAGCTCCTACGGCCACTTCGGGCGCCCCGGCTTCAGCTGGGAGGCCACCGACCGCGTCGAGGCCCTGCGCCAGGCCGTCTGA","VSSSLRLFTSESVTEGHPDKICDRVSDAILDAILEQDPTARVAVETMVTTGLVHVAGEVTTERAYVEIPEIVRQEISAIGYTSSDVCFDARSCGVSVSIGQQSADIAAGVDKSLQARRDDTDIDPLDLQGAGDQGLMFGYACDDTAALMPLPIHLAHRLAERLAAVRKQGIVPGLRPDGKTQVTIGYDGQRPVSLHNLVISTQHDADRTRAWLTDALRTEVIDPVLAAEAEAGTDLGTAHTEVLINPSGQFVIGGPAGDAGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSASYAMRWVAKNVVAAGLARRCEIQVAYAIGSAHPVGVYVETFGTATVPEERIMKAVNEVFDLRPAAIVRDLDLLRPIYRATSSYGHFGRPGFSWEATDRVEALRQAV$","S-adenosylmethionine synthetase","Cytoplasm","S-adenosylmethionine synthetase","S-adenosylmethionine synthetase ","Methionine adenosyltransferase","","Horikawa S., Sasuga J., Shimizu K., Ozasa H., Tsukada K. Molecular cloning and nucleotide sequence of cDNA encoding the rat kidney S-adenosylmethionine synthetase. J. Biol. Chem. 1990. 265(23):13683-13686. PMID: 1696256Sajkovski M., Simonce N., Dejanov I., Janicijevic D, Orglert G., Gligorieva B., Bojadziev L. Nature of vitamin K deficiency in the infant age. God Zb Med Fak Skopje 1975. 21:299-302. PMID: 1213535","","","

InterPro
IPR002133
Family

S-adenosylmethionine synthetase
PIRSF000497	$\"[4-401]T$	Methionine adenosyltransferase
PTHR11964	$\"[1-400]T$	S-ADENOSYLMETHIONINE SYNTHETASE
PF00438	$\"[4-104]T$	S-AdoMet_synt_N
PF02772	$\"[127-251]T$	S-AdoMet_synt_M
PF02773	$\"[253-390]T$	S-AdoMet_synt_C
TIGR01034	$\"[7-401]T$	metK: S-adenosylmethionine synthetase
PS00376	$\"[130-140]T$	ADOMET_SYNTHETASE_1
PS00377	$\"[279-287]T$	ADOMET_SYNTHETASE_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.300.10	$\"[4-116]T$ $\"[142-253]T$ $\"[264-399]T$	no description

","BeTs to 17 clades of COG0192COG name: S-adenosylmethionine synthetaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0192 is ------yqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002133 (S-adenosylmethionine synthetase) with a combined E-value of 2.1e-209. IPB002133A 7-46 IPB002133B 71-111 IPB002133C 130-150 IPB002133D 155-187 IPB002133E 192-227 IPB002133F 251-294 IPB002133G 295-333 IPB002133H 334-383","Residues 7-46 are 92% similar to a (SYNTHETASE METAL-BINDING ATP-BINDING MAGNESIUM ONE-CARBON METABOLISM POTASSIUM TRANSFERASE S-ADENOSYLMETHIONINE METHIONINE) protein domain (PD499406) which is seen in METK_CLOAB.Residues 45-134 are 74% similar to a (SYNTHETASE METAL-BINDING ATP-BINDING MAGNESIUM ONE-CARBON METABOLISM POTASSIUM TRANSFERASE S-ADENOSYLMETHIONINE METHIONINE) protein domain (PD606972) which is seen in METK_STRST.Residues 52-150 are 53% similar to a (SYNTHETASE ADOMET METHIONINE TRANSFERASE METAL-BINDING S-ADENOSYLMETHIONINE METABOLISM ATP-BINDING POTASSIUM ADENOSYLTRANSFERASE) protein domain (PDA0W4Q5) which is seen in METK_AMOPR.Residues 172-280 are 72% similar to a (SYNTHETASE METAL-BINDING ATP-BINDING MAGNESIUM ONE-CARBON METABOLISM POTASSIUM TRANSFERASE S-ADENOSYLMETHIONINE METHIONINE) protein domain (PD001322) which is seen in METK_CORGL.Residues 281-315 are 97% similar to a (SYNTHETASE METAL-BINDING ATP-BINDING MAGNESIUM ONE-CARBON METABOLISM POTASSIUM TRANSFERASE S-ADENOSYLMETHIONINE METHIONINE) protein domain (PD223485) which is seen in Q83X53_STRRO.Residues 328-376 are 87% similar to a (SYNTHETASE ATP-BINDING METAL-BINDING MAGNESIUM ONE-CARBON METABOLISM POTASSIUM TRANSFERASE S-ADENOSYLMETHIONINE METHIONINE) protein domain (PD894188) which is seen in Q6AF79_BBBBB.","","-71% similar to PDB:1FUG S-ADENOSYLMETHIONINE SYNTHETASE (E_value = 9.4E_123);-71% similar to PDB:1MXA S-ADENOSYLMETHIONINE SYNTHETASE WITH PPI (E_value = 9.4E_123);-71% similar to PDB:1MXB S-ADENOSYLMETHIONINE SYNTHETASE WITH ADP (E_value = 9.4E_123);-71% similar to PDB:1MXC S-ADENOSYLMETHIONINE SYNTHETASE WITH 8-BR-ADP (E_value = 9.4E_123);-71% similar to PDB:1P7L S-Adenosylmethionine synthetase complexed with AMPPNP and Met. (E_value = 9.4E_123);","Residues 4 to 104 (E_value = 1.7e-47) place ANA_0801 in the S-AdoMet_synt_N family which is described as S-adenosylmethionine synthetase, N-terminal domain.Residues 127 to 251 (E_value = 4.2e-47) place ANA_0801 in the S-AdoMet_synt_M family which is described as S-adenosylmethionine synthetase, central domain.Residues 253 to 390 (E_value = 2.2e-82) place ANA_0801 in the S-AdoMet_synt_C family which is described as S-adenosylmethionine synthetase, C-terminal domain.","","synthetase (metK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0802","859086","857749","1338","6.12","-5.64","46167","ATGGACGAGCCGCACACTGCTGCGAGTCAACGCGCCGTGACCGCTTTTGAGCGGCCACGGCGCGTCGTCGTCGGCGTGGCCGGGTCGATCGCCGCCTACAAGGCCCCCTTCGTCATTCGACTGCTGCGTCAGGCCGGGCACGAGGTCAAGGTCGTGGCCACCGAGTCGGCGCTGCGGTTCATTGGTGCTCCGGCACTGGCGGCGGTCAGCGGCCGGGCCGTATCCACCGGGGTCTTCGACGACCCCGCTGCGGTTGAGCACGTGTCCGTGGCTGAATGGGCCGAGCTCGTCGTGGTCGCTCCGGCCTCGGCAGATCTGCTGGCACGGGTGCGGGCAGGGCGGGCCGACGACATGCTCACCGCGACGATACTGACCTGCCAGGCCCCCGTCGTCCTGGCTCCGGCCATGCACACCCAGATGTGGGTCAACCCCGCCACCCGGGAGAACGTGGCAGTGCTGCGTGAGCGCGGTCTGACGGTCATCGAACCGGACAGCGGGCGCCTGACCGGCAAGGACTCCGGAGTGGGCCGGATGCCCGAACCCGAGCAGATCGTGTCGCAGGCCCTGGCTACCCTGACGCAGCCAGTCGCCGAGGGCGCGGCAGCGCAGGACGCCCTGGGGGAGAAGAATAGGCGTTTGGAGGGCCGGCACCTCGTCATCTCCGCGGGCGGCACACGCGAGCCCATCGATCCGGTGAGGTACCTCGGTAACCGCTCCTCAGGGCACCAGGGCTGCGCACTGGCGGCGGCAGCCGTCGAGCAGGGAGCCCGCGTCACCCTGGTGCAGGCGCACGTGGCCTCCGACCTGCTCAACGCCCTGCCGGCGGAGGTGAGCGTCGTTGCCGCCGGTACCGCCTCTGACATGCTCCGCGCCGTGCGCGAGAGCGCACGAGACGCCGACGCCGTCATCATGGCAGCAGCTGTCGCCGACTACCGGCCCGTCACCGTGGCCGCCACCAAGCTCAAGAAGCAGGCACCCGCCGGAGCGAATCACCTCAGCGAACCGGTCATGTCCATTGAGCTCACCACCAACCCGGACATCCTGGTCGGGCTGGTGAGCGACCCACCTCGGCCCGGCCAGATCATCGTCGGATTCGCCGCCGAGACCGGGGACGAGAACGGTGACGTACTCTTCCACGGCAGAGCCAAGGCTCGCCGCAAAGGGGCTCATCTTCTGGCGGTCAACGCGGTGGGGGAGGAGCTCGGCTTCGGAGACGTCCCCAATGCCGTCGTCGTCCTGGATGCCGACGGCACGGAGGTGGCGCGGGGACAGGGCAGCAAGATGGAGGTCGCGCGCCTTCTCATCTCCCTGACTGCCGACCTCGTGGATGCGACCTGA","MDEPHTAASQRAVTAFERPRRVVVGVAGSIAAYKAPFVIRLLRQAGHEVKVVATESALRFIGAPALAAVSGRAVSTGVFDDPAAVEHVSVAEWAELVVVAPASADLLARVRAGRADDMLTATILTCQAPVVLAPAMHTQMWVNPATRENVAVLRERGLTVIEPDSGRLTGKDSGVGRMPEPEQIVSQALATLTQPVAEGAAAQDALGEKNRRLEGRHLVISAGGTREPIDPVRYLGNRSSGHQGCALAAAAVEQGARVTLVQAHVASDLLNALPAEVSVVAAGTASDMLRAVRESARDADAVIMAAAVADYRPVTVAATKLKKQAPAGANHLSEPVMSIELTTNPDILVGLVSDPPRPGQIIVGFAAETGDENGDVLFHGRAKARRKGAHLLAVNAVGEELGFGDVPNAVVVLDADGTEVARGQGSKMEVARLLISLTADLVDAT$","Phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase","Cytoplasm, Membrane","phosphopantothenoylcysteinedecarboxylase/phosphopantothenate--cysteine ligase","phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase ","phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase","","Strauss E., Kinsland C., Ge Y., McLafferty F.W., Begley T.P. Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria. J. Biol. Chem. 2001. 276(17):13513-13516. PMID: 11278255Spitzer E.D., Jimenez-Billini H.E., Weiss B. beta-Alanine auxotrophy associated with dfp, a locus affecting DNA synthesis in Escherichia coli. J. Bacteriol. 1988. 170(2):872-876. PMID: 3123465","","","

InterPro
IPR003382
Domain

Flavoprotein
G3DSA:3.40.50.1950	$\"[12-203]T$	no description
PF02441	$\"[20-135]T$	Flavoprotein

InterPro
IPR005252
Family

Bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase
TIGR00521	$\"[17-439]T$	coaBC_dfp: phosphopantothenoylcysteine deca

InterPro
IPR007085
Domain

DNA/pantothenate metabolism flavoprotein, C-terminal
PF04127	$\"[213-425]T$	DFP

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.10300	$\"[208-443]T$	no description
PTHR14359	$\"[26-192]T$ $\"[210-445]T$	HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY
PTHR14359:SF6	$\"[26-192]T$ $\"[210-445]T$	PANTOTHENATE METABOLISM FLAVOPROTEIN DFP

","BeTs to 23 clades of COG0452COG name: Phosphopantothenoylcysteine synthetase/decarboxylaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0452 is aompkzyqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB007085 (DNA/pantothenate metabolism flavoprotein, C terminal) with a combined E-value of 1.5e-22. IPB007085 218-263***** IPB003382 (Flavoprotein) with a combined E-value of 5.1e-08. IPB003382 216-236","Residues 17-194 are 58% similar to a (INCLUDES: COAC PPCDC A CYSTEINE PHO PHOSPHOPANTOTHENATE-- COENZYME METABOLISM PHOSPHOPANTOTHENOYLCYSTEINE) protein domain (PDA187O0) which is seen in CABC_BORBU.Residues 27-184 are similar to a (FLAVOPROTEIN METABOLISM DNA/PANTOTHENATE LIGASE PANTOTHENATE PHOSPHOPANTOTHENOYLCYSTEINE CYSTEINE DECARBOXYLASE DFP LYASE) protein domain (PD002847) which is seen in Q741G6_MYCPA.Residues 213-291 are 70% similar to a (FLAVOPROTEIN METABOLISM LIGASE DNA/PANTOTHENATE PHOSPHOPANTOTHENOYLCYSTEINE PANTOTHENATE CYSTEINE DFP DECARBOXYLASE DECARBOXYLASE/PHOSPHOPANTOTHENATE--) protein domain (PD005411) which is seen in Q8CK27_STRCO.Residues 311-403 are 58% similar to a (FLAVOPROTEIN METABOLISM LIGASE DNA/PANTOTHENATE PANTOTHENATE PHOSPHOPANTOTHENOYLCYSTEINE CYSTEINE DFP DECARBOXYLASE DECARBOXYLASE/PHOSPHOPANTOTHENATE--) protein domain (PD136292) which is seen in DFP_MYCTU.","","-51% similar to PDB:1U7U Phosphopantothenoylcysteine synthetase from E. coli (E_value = 2.8E_22);-51% similar to PDB:1U7W Phosphopantothenoylcysteine synthetase from E. coli, CTP-complex (E_value = 2.8E_22);-51% similar to PDB:1U7Z Phosphopantothenoylcysteine synthetase from E. coli, 4'-phosphopantothenoyl-CMP complex (E_value = 2.8E_22);-51% similar to PDB:1U80 Phosphopantothenoylcysteine synthetase from E. coli, CMP complex (E_value = 2.8E_22);-50% similar to PDB:1MVL PPC decarboxylase mutant C175S (E_value = 1.4E_18);","Residues 20 to 135 (E_value = 1.6e-35) place ANA_0802 in the Flavoprotein family which is described as Flavoprotein.Residues 213 to 425 (E_value = 8e-25) place ANA_0802 in the DFP family which is described as DNA / pantothenate metabolism flavoprotein.","","decarboxylase-phosphopantothenate--cysteine ligase (coaBC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0803","859497","859099","399","4.40","-14.03","14464","ATGCTCGGAACCTCTCCCCGGCCCGAGGGCATCACCAACCCGCCGATCGACGACCTTCTGGAGAAAGTCGACTCCAAGTACGGGCTCGTGGTGGAGGCCGCCAAGCGCGCCCGCCAGATCAACACCTACACTCAGCAGCTCGAGGACAACCAGTTCGAGTTCTTCGGTCCGCTGGTCGACTCCGAGGTCGGCGAGAAGTCTCTGGGCATCGCGCTGCGTGAGATCGCCGAGGACAAGCTTGAGGTCATTCCCGGGGACGTGGCCCGCGCCCGCCGCGCCGAGGCCGAGGAGGCCCGTCGAGCCGCGGAGGCCGACATGTTCAGCGACATCTCGCTGGATTCTCCGGTCTCCCTCGAGGGCGGCGAGACTCCCACCAGCCTCGACGACATCCAGTTCTGA","MLGTSPRPEGITNPPIDDLLEKVDSKYGLVVEAAKRARQINTYTQQLEDNQFEFFGPLVDSEVGEKSLGIALREIAEDKLEVIPGDVARARRAEAEEARRAAEADMFSDISLDSPVSLEGGETPTSLDDIQF$","DNA-directed RNA polymerase, omega subunit","Cytoplasm","DNA-directed RNA polymerase omega chain","DNA-directed RNA polymerase; omega subunit","DNA-directed RNA polymerase, omega subunit","","Minakhin L., Bhagat S., Brunning A., Campbell E.A., Darst S.A., Ebright R.H., Severinov K. Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly. Proc. Natl. Acad. Sci. U.S.A. 2001. 98(3):892-897. PMID: 11158566","","","

InterPro
IPR003716
Family

RNA polymerase, omega subunit
TIGR00690	$\"[11-87]T$	rpoZ: DNA-directed RNA polymerase, omega su

InterPro
IPR006110
Family

RNA polymerase Rpb6
PF01192	$\"[22-86]T$	RNA_pol_Rpb6

","BeTs to 10 clades of COG1758COG name: DNA-directed RNA polymerase subunit K/omegaFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1758 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 22 to 86 (E_value = 2e-08) place ANA_0803 in the RNA_pol_Rpb6 family which is described as RNA polymerase Rpb6.","","RNA polymerase omega chain","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0804","860142","859543","600","5.43","-5.82","21575","GTGGCCATGACCGACATTGCTGCCACAGACCCGTCCGCCCCTGTGCTCGCCCGCCTCACAGTTCTGGCCGGCCCCACGGCGGTGGGTAAGGGCACTGTCGTCACCGAGCTGCGCAGACGCCATCCAGACCTGTTCGTCTCGGTCTCGGCCACCACCCGTCAGCCTCGTCCCGGTGAGATCGACGGCGTGCACTACCACTTCGTCAGCGATGGAGACTTCGACTCGCTCGTCGCCAGTGGCCAGATGCTGGAGTGGGCCCTGGTTCACGGCGCGTATCGCTATGGCACCCCCCGAGGCCCGGTCCAGGATCGGCTCAATGCCGGATTCCCTGCACTGCTGGAGATCGACCTGGACGGTGCCCGGCAGGTGCGTCAAGCGATGCCCGAGGCCCGCCTCGTCTTCCTCGCGCCGCCGAGCTGGGACGAGCTCGTTCGCAGGCTCGTCGGACGCGGTACCGAGGACGCCCAGGAGCGGGAGCGGCGCCTGGTCACAGCGCGCATAGAGCTGGACGCGGCCGGCGAGTTCGACCACGTCGTCATCAACGACACCGTGGCGAGCGCCACCGCAGAGCTGGAGAGACTCATGGGATTGGGCAGTTAG","VAMTDIAATDPSAPVLARLTVLAGPTAVGKGTVVTELRRRHPDLFVSVSATTRQPRPGEIDGVHYHFVSDGDFDSLVASGQMLEWALVHGAYRYGTPRGPVQDRLNAGFPALLEIDLDGARQVRQAMPEARLVFLAPPSWDELVRRLVGRGTEDAQERERRLVTARIELDAAGEFDHVVINDTVASATAELERLMGLGS$","Guanylate kinase","Cytoplasm","Guanylate kinase (GMP kinase)","guanylate kinase ","Guanylate kinase","","Stehle T., Schulz G.E. Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution. J. Mol. Biol. 1992. 224(4):1127-1141. PMID: 1314905Bryant P.J., Woods D.F. A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene. Cell 1992. 68(4):621-622. PMID: 1310897Zschocke P.D., Schiltz E., Schulz G.E. Purification and sequence determination of guanylate kinase from pig brain. Eur. J. Biochem. 1993. 213(1):263-269. PMID: 8097461Goebl M.G. Is the erythrocyte protein p55 a membrane-bound guanylate kinase?. Trends Biochem. Sci. 1992. 17(3):99-99. PMID: 1329277Woods D.F., Bryant P.J. ZO-1, DlgA and PSD-95/SAP90: homologous proteins in tight, septate and synaptic cell junctions. Mech. Dev. 1993. 44(2):85-89. PMID: 8155583","","","

InterPro
IPR008144
Family

Guanylate kinase
PF00625	$\"[52-157]T$	Guanylate_kin
PS50052	$\"[17-196]T$	GUANYLATE_KINASE_2
PS00856	$\"[51-68]T$	GUANYLATE_KINASE_1

InterPro
IPR008145
Domain

Guanylate kinase/L-type calcium channel region
SM00072	$\"[16-199]T$	GuKc

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[77-195]T$	no description
PTHR23117	$\"[37-195]T$	GUANYLATE KINASE-RELATED
PTHR23117:SF1	$\"[37-195]T$	GUANYLATE KINASE

","BeTs to 18 clades of COG0194COG name: Guanylate kinaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0194 is ------yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 1","***** IPB008144 (Guanylate kinase) with a combined E-value of 2.9e-32. IPB008144A 23-32 IPB008144B 48-69 IPB008144C 91-116 IPB008144D 133-143***** IPB004172 (L27 domain) with a combined E-value of 1.8e-08. IPB004172G 32-86","Residues 8-195 are 46% similar to a (RNI-LIKE FLJ32786 ENRICHED PRODUCT:HYPOTHETICAL FULL LIBRARY KINASE CONTAINING STRUCTURE PROTEIN) protein domain (PD401420) which is seen in Q96M69_HUMAN.Residues 21-58 are 84% similar to a (KINASE GUANYLATE TRANSFERASE ATP-BINDING GMP ACETYLATION 3D-STRUCTURE GUK1 SEQUENCING DIRECT) protein domain (PD467617) which is seen in KGUA_BIFLO.Residues 59-108 are 76% similar to a (KINASE GUANYLATE TRANSFERASE ATP-BINDING GMP INTERACTING MEMBRANE-ASSOCIATED ATROPHIN-1 HOMOLOG 3D-STRUCTURE) protein domain (PD001338) which is seen in Q6AF82_BBBBB.Residues 113-195 are similar to a (KINASE GUANYLATE TRANSFERASE ATP-BINDING GMP DOMAIN SH3 ACETYLATION GUK1 HOMOLOG) protein domain (PD003452) which is seen in Q6AF82_BBBBB.","","-70% similar to PDB:1S4Q Crystal Structure of Guanylate Kinase from Mycobacterium tuberculosis (Rv1389) (E_value = 2.3E_50);-70% similar to PDB:1ZNW Crystal Structure Of Unliganded Form Of Mycobacterium tuberculosis Guanylate Kinase (E_value = 2.3E_50);-70% similar to PDB:1ZNX Crystal Structure Of Mycobacterium tuberculosis Guanylate Kinase In Complex With GMP (E_value = 2.3E_50);-70% similar to PDB:1ZNY Crystal Structure Of Mycobacterium tuberculosis Guanylate Kinase In Complex With GDP (E_value = 2.3E_50);-70% similar to PDB:1ZNZ Crystal Structure Of The Reduced Form Of Mycobacterium tuberculosis Guanylate Kinase In Complex With GDP (E_value = 2.3E_50);","Residues 52 to 157 (E_value = 1.2e-29) place ANA_0804 in the Guanylate_kin family which is described as Guanylate kinase.","","kinase (GMP kinase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0805","860505","860194","312","10.24","5.41","11152","ATGACGCTTCCAACGCTGACACCCGAGCAACGGGCTCAGGCACTGGAGAAGGCGGCTGCGGCGCGATCGCATCGCGCCCGTATCAAGTCCGAGCTCAAGAGTGGGGAGCTCAAGCTCTCCGAGTTCTTCACCGCCTCAGAGACAGATGATGTCCTGGGCAAGATGAAGGTCAGGGCGCTGCTCGTCTCACTGCCACGTGTGGGGACCACAACTGCTGACGCCATCCTTGCTGACGTGCATATCGCCGAGTCCCGGCGGGTGCGCGGACTGGGGGCGAACCAGAGGGCGGCGCTGGTGGAGCGCTTCGGCTAG","MTLPTLTPEQRAQALEKAAAARSHRARIKSELKSGELKLSEFFTASETDDVLGKMKVRALLVSLPRVGTTTADAILADVHIAESRRVRGLGANQRAALVERFG$","Hypothetical protein","Cytoplasm","integration host factor","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-102 are similar to a (HOST INTEGRATION FACTOR MIHF CIHF PROBABLE SCO1480 CGL1607) protein domain (PD028040) which is seen in P96802_MYCSM.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","host factor","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0806","861536","860658","879","5.43","-6.65","29333","ATGAGTTCCACGGCCACTCACCAGACCAGTCGACGCCCCTTCGGAGCCCGCCTGGCGGACGCCATGGACGACCACGGGCCCCTGTGCGTCGGCATCGACCCCCACCCGAGTCTGCTCGAGGCCTGGGGCCTGGCGGACTCGGCCGCAGGCCTGCGGGACTTCTCACTGCGGACCGTTGACGCGGTCGGAGGACACGTGGCTGCCGTCAAGCCGCAGTCCGCATTCTTCGAGCGACACGGCAGCGCCGGGATCGCGGTCCTCGAGGAGACCCTGGCGGCCTTGCGTGACCTGGGCACCTTGTCCATTCTCGACGTCAAGCGCGGGGATATCGGTTCCACCATGGCTGGATACGCCCAGGCCTACCTGTCCGACGACGCTCCTCTGGCCGCCGACTCCATCACTGTCTCGCCCTACCTGGGCTACGGGTCCCTGACTCCTGCGCTCAACCTCGCTGAGGCCAGCGGTCGGGGCGTCTTCGTCCTGGCCCTGACCTCCAATCCGGAAGGAGCCGGCATCCAGCACGCCGTCAACGGGGATCAGGCGGTGGCTGCCGGCATCGTGGAGGGTGTGACCGCGTCCAACGCCCAAGCCCGTGGCGAAGACCGGCTCGGTTGCATCGGGCTGGTCATCGGGGCCACCGTCGGCGGGGCCGTCTCCGACCTGGGAATCGACCTGCAGCGCGCCAATGGCCCGTTGCTGGCGCCAGGGGTCGGCGCCCAGGGAGCAGGGCCGGCTGAGCTGGAGGCTGTTTTCGGGGCGGCTCGCCGTCAGGTCCTGGCCTCCACCTCACGCGGGGTTCTCAAGACCGGGCCCTCCATCGAGGCACTGCGAAAAGCCGCGTCGGCTTCTTCCTACGAGGCGGCAACAGCCCTGCGTTGA","MSSTATHQTSRRPFGARLADAMDDHGPLCVGIDPHPSLLEAWGLADSAAGLRDFSLRTVDAVGGHVAAVKPQSAFFERHGSAGIAVLEETLAALRDLGTLSILDVKRGDIGSTMAGYAQAYLSDDAPLAADSITVSPYLGYGSLTPALNLAEASGRGVFVLALTSNPEGAGIQHAVNGDQAVAAGIVEGVTASNAQARGEDRLGCIGLVIGATVGGAVSDLGIDLQRANGPLLAPGVGAQGAGPAELEAVFGAARRQVLASTSRGVLKTGPSIEALRKAASASSYEAATALR$","Orotidine 5'-phosphate decarboxylase","Cytoplasm, Extracellular","Orotidine 5'-phosphate decarboxylase (OMPdecarboxylase)(OMPDCase) (OMPdecase)","orotidine 5'-phosphate decarboxylase ","orotidine 5'-phosphate decarboxylase","","Jacquet M., Guilbaud R., Garreau H. Sequence analysis of the DdPYR5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases. Mol. Gen. Genet. 1988. 211(3):441-445. PMID: 2835631Kimsey H.H., Kaiser D. The orotidine-5'-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family. J. Biol. Chem. 1992. 267(2):819-824. PMID: 1730672","","","

InterPro
IPR001754
Domain

Orotidine 5'-phosphate decarboxylase, core
PF00215	$\"[26-279]T$	OMPdecase

InterPro
IPR011995
Domain

Orotidine 5'-phosphate decarboxylase, subfamily 2, core
TIGR02127	$\"[14-280]T$	pyrF_sub2: orotidine 5'-phosphate decarboxy

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[15-242]T$	no description

","BeTs to 5 clades of COG0284COG name: Orotidine-5'-phosphate decarboxylaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0284 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001754 (Orotidine 5'-phosphate decarboxylase) with a combined E-value of 2.6e-08. IPB001754A 48-75 IPB001754B 101-114","Residues 14-63 are 76% similar to a (DECARBOXYLASE OROTIDINE 5_apos;-PHOSPHATE LYASE OMPDCASE PYRIMIDINE OMP BIOSYNTHESIS OMPDECASE SIMILAR) protein domain (PD584498) which is seen in Q827Q5_STRAW.Residues 67-215 are 75% similar to a (DECARBOXYLASE OROTIDINE LYASE 5_apos;-PHOSPHATE PYRIMIDINE BIOSYNTHESIS OMPDCASE OMP OMPDECASE 5-PHOSPHATE) protein domain (PD017607) which is seen in PYRF_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 279 (E_value = 3.7e-39) place ANA_0806 in the OMPdecase family which is described as Orotidine 5'-phosphate decarboxylase / HUMPS family.","","5-phosphate decarboxylase (OMP decarboxylase)(OMPDCase) (OMPdecase) (Ura3)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0807","864892","861533","3360","4.92","-47.28","119548","ATGCCTGCTCGCCCTGATATCAGCTCCGTCCTGGTCATCGGATCGGGCCCCATCGTCATCGGGCAGGCCTGCGAGTTCGACTACTCCGGCACCCAGGCCTGCCGCGTCCTGCGCGCTGAGGGAATCCGCGTCATTCTGGTCAACTCCAACCCGGCCACGATCATGACCGACCCCGACGTCGCCGACGCCACCTATATCGAGCCGATCACCCCCGAGGTGCTGACCACCATCATCGCCAAGGAAAGGCCCGACGCCCTCCTGCCCACCCTGGGCGGGCAGACCGCCCTCAACGCCGCCATGAGCCTGGTCGAGCGGGGCGTGCTCGATGAGTACGATGTCGAGCTCATCGGCGCCTCCGCCGCGGCCATCAACGCCGGGGAGGACCGTGACGAGTTCAAGGACGTCGTCGAGCGTTGTGGCGCCGAGGTCGCCCGCAGCGTCATCGCCCACACCATGGATGAGTGCCGCGCCGGGGTCGATGCCCTTGGCGGATACCCGGTCGTCGTGCGCCCCTCCTTCACGATGGGCGGCCTGGGCAGCGGTGTCGCCTTCAATGACTCGGACCTGCATCGCATCGCCGGGGCGGGTCTGGCGGCCTCCCGCACCACCGAGGTCCTCCTGGAGGAGTCGATCCTGGGCTGGAAGGAGTACGAGCTCGAGCTCATGCGCGACACCGCCGACAACGTGGTGGTCGTGTGCTCCATCGAGAACGTCGACCCTGTGGGAGTGCACACCGGCGACTCCATCACGGTCGCCCCGGCCCTGACCCTCACCGACCGCGAGCTCCAGAGGCTGCGGGACATCGGCATCGCCGTCATCCGGGAGGTCGGGGTCGATACCGGTGGCTGCAACATCCAGTTCGCCGTCGACCCGGCCACCGGCAGGATCATCGTCATCGAGATGAACCCCCGCGTCTCGAGGTCCTCAGCCCTGGCCTCGAAGGCCACCGGCTTCCCGATCGCCAAGATCGCCGCACGCCTGGCCGTGGGGTACACGCTCGACGAGATCCCCAACGACATCACCGGCTCCACCCCGGCCTCCTTCGAACCGACCCTGGACTACGTGGTCGTCAAGGTGCCGCGCTTCGCCTTCGAGAAGTTCCGGGGCGCTGACCCCCGGCTCACCACCACCATGAAATCGGTTGGCGAGGCCATGGCGATCGGTCGGTCCTATACAGAAGCCCTCCAGAAGGCCTTACGCTCTCTGGACAAGAAGGGAACCGCCTTCCACTGGGACGGACCGGCGCCCAGCCAGCAGCAGACCGCTGAGCTGCTGAAGTCCATCGCCGTGCCCACCGAGCACCGGCTGGTCGACCTCCAGCAGGCCGTGCGCGGCGGAGCCACGATTGCCCAGCTCCACGAGGCCACCCGCATCGACCCCTGGTTCCTGGACCAGATGCTGCTTCTTGAGGAGGTGGCCCAAGAGGTCAAGGGCGCATCCGCGCTCACTGCGGACGTCCTGACCCTGGCCAAGCGCCACGGCTTCTCCGACGTCCAGGTCGCCTCCCTGCGCGGCATCAGCGAGGACACGGTGCGAGAGGTCCGCCATGCCTTCGGCCTGCGGCCCGTCTACAAGACCGTTGACACCTGCGCCGCCGAGTTCGCCTCACGCACCCCCTACCTCTACTCCAGCTACGACCTGGAGACCGAGGTGGCATCCCGCGAGCGTGAGGCCGTCATCATCCTGGGCTCGGGACCCAACCGGATCGGCCAGGGCATTGAGTTCGACTACTCCTGTGTTCACGCCGCGATGGCCCTGTCCGATCGCTACGAGACCGTCATGGTCAACTGCAACCCTGAGACCGTCTCCACCGACTACGACATCTCCGACCGGCTCTACTTCGAGCCTCTGACCTTCGAGGACGTCATCGAGATTTACGAGGCCGAGCTGGCAGCCGGACCCGTGACCGGTGTCATCGTCCAGCTCGGTGGTCAGACACCGCTGTCCTTGGCGGCCAGACTGGCCAAGGCCGGGGTGCCGATCCTGGGAACGAGTCCCGAGGCGATCGACGCCGCCGAGGACCGCGAGGCCTTCGGCACTGTTCTTCAGCGCGCAGGCCTTCCCGCACCAGCGCACGGCACCGCTCTGAGCGACGAGCAGGCGCGCTCGGTCGCCCAGAATATTGGCTATCCGGTCCTGGTGCGCCCCAGCTACGTGCTCGGCGGCCGCGGTATGGAGATCGTCTACGACGCCCAGGGACTCGACGACTATCTCCAACGCGCAGGTCTTGAGCCCGGAGGCGTCTACGGGACCGGGCCACTACTCATCGACCGTTTCCTCGACGACGCCATCGAGATCGATGTCGACGCCCTTTATGACGGCAGCGAGCTGTTCCTCGGCGGCGTCATGGAGCACATCGAGGAGGCCGGTATCCACTCCGGTGACTCCGCCTGCGTCATGCCACCCATGACCCTGTCCGACACGGAGATCGCTCGCATCCGACGCTCCACCGAGGCGATCGCCAAAGGCGTGGGCGTGCAGGGACTGCTCAACATCCAGTTCGCCCTGGTCTCCGACGTTCTCTACGTCATCGAGGCCAACCCCCGGGCCTCGCGCACAGTCCCCTTCGTCTCGAAGGCATCCGGTGTGCAGCTCGCCAAGGCGGCGGCCCTCATCATGACGGGGGAGACGATCGCCTCGCTCAGGCGCTCCGGTCACCTGCCCGAGGTCGATGCCGCCGTCACCGATCCCGATGACCCGATCGCCGTCAAGGAGGCGGTCCTGCCCTTCAAACGGTTCCGTACCACCGAGGGCCGCGTGGTCGACACGATCCTGGGGCCGGAGATGCGTTCCACCGGTGAGGTCATGGGCTACGACGTGGACTTCCCACGGGCGTTCGCCAAGTCCCAGGCCGGTGCCTACGGTGGCTTACCATGCGAGGGCACGCTGTTCGTGTCGGTGGCCGACCGGGACAAGCGGGCCATCATCCTGCCGGTGGCTCGGCTCGCGGAGCTCGGCTTCACGGTCCTGGCCACGACTGGGACCGCACAGGTGCTGCGCCGCAACGGGATCGACGCCATTGCGGTGCGCAAGATCAGCCAGGGCGTTGGCGACCACGGCGAGCAGACGATCGCCGAGCTCATCGAGTGCGGGGCCATCGACATGGTGGTCAACACCCCCAAGGGCCAGGGTGCCCGTGCCGACGGGTACTCCATCCGCGCGGCCACCACCGGTGCCGACCGTCCCATCATCACCACTGTCCAACAGCTTCAGGCAGCGGTCCAGGCCCTCGAGGCCCAGCTGCGCGGTCCCTTCCAGGTTCGCAGCCTCCAGGAGCACATCGCCGACCGCCGATCCCGGCGAGACCCGGTGTCCGAGCCCCACTCCGTGGCCCCCGTTGACGACAAGGAGACCAGATGA","MPARPDISSVLVIGSGPIVIGQACEFDYSGTQACRVLRAEGIRVILVNSNPATIMTDPDVADATYIEPITPEVLTTIIAKERPDALLPTLGGQTALNAAMSLVERGVLDEYDVELIGASAAAINAGEDRDEFKDVVERCGAEVARSVIAHTMDECRAGVDALGGYPVVVRPSFTMGGLGSGVAFNDSDLHRIAGAGLAASRTTEVLLEESILGWKEYELELMRDTADNVVVVCSIENVDPVGVHTGDSITVAPALTLTDRELQRLRDIGIAVIREVGVDTGGCNIQFAVDPATGRIIVIEMNPRVSRSSALASKATGFPIAKIAARLAVGYTLDEIPNDITGSTPASFEPTLDYVVVKVPRFAFEKFRGADPRLTTTMKSVGEAMAIGRSYTEALQKALRSLDKKGTAFHWDGPAPSQQQTAELLKSIAVPTEHRLVDLQQAVRGGATIAQLHEATRIDPWFLDQMLLLEEVAQEVKGASALTADVLTLAKRHGFSDVQVASLRGISEDTVREVRHAFGLRPVYKTVDTCAAEFASRTPYLYSSYDLETEVASREREAVIILGSGPNRIGQGIEFDYSCVHAAMALSDRYETVMVNCNPETVSTDYDISDRLYFEPLTFEDVIEIYEAELAAGPVTGVIVQLGGQTPLSLAARLAKAGVPILGTSPEAIDAAEDREAFGTVLQRAGLPAPAHGTALSDEQARSVAQNIGYPVLVRPSYVLGGRGMEIVYDAQGLDDYLQRAGLEPGGVYGTGPLLIDRFLDDAIEIDVDALYDGSELFLGGVMEHIEEAGIHSGDSACVMPPMTLSDTEIARIRRSTEAIAKGVGVQGLLNIQFALVSDVLYVIEANPRASRTVPFVSKASGVQLAKAAALIMTGETIASLRRSGHLPEVDAAVTDPDDPIAVKEAVLPFKRFRTTEGRVVDTILGPEMRSTGEVMGYDVDFPRAFAKSQAGAYGGLPCEGTLFVSVADRDKRAIILPVARLAELGFTVLATTGTAQVLRRNGIDAIAVRKISQGVGDHGEQTIAELIECGAIDMVVNTPKGQGARADGYSIRAATTGADRPIITTVQQLQAAVQALEAQLRGPFQVRSLQEHIADRRSRRDPVSEPHSVAPVDDKETR$","Carbamoyl-phosphate synthase, large subunit","Cytoplasm, Extracellular","carbamoyl-phosphate synthase, large subunit","carbamoyl-phosphate synthase large chain ","carbamoyl-phosphate synthase, large subunit","","Simmer J.P., Kelly R.E., Rinker Jr A.G., Scully J.L., Evans D.R. Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD. J. Biol. Chem. 1990. 265(18):10395-10402. PMID: 1972379Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M. The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution. Acta Crystallogr. D 1999. 55:8-24. PMID: 10089390","","","

InterPro
IPR005479
Domain

Carbamoyl-phosphate synthase L chain, ATP-binding
PF02786	$\"[128-364]T$ $\"[674-761]T$	CPSase_L_D2
PS00866	$\"[165-179]T$ $\"[710-724]T$	CPSASE_1
PS00867	$\"[298-305]T$ $\"[843-850]?$	CPSASE_2

InterPro
IPR005480
Domain

Carbamoyl-phosphate synthetase large chain, oligomerisation
PF02787	$\"[424-545]T$	CPSase_L_D3

InterPro
IPR005481
Domain

Carbamoyl-phosphate synthetase large chain, N-terminal
PF00289	$\"[6-126]T$ $\"[555-672]T$	CPSase_L_chain

InterPro
IPR005483
Domain

Carbamoyl-phosphate synthetase large chain
PR00098	$\"[19-33]T$ $\"[48-58]T$ $\"[169-181]T$ $\"[205-224]T$ $\"[240-257]T$ $\"[298-327]T$ $\"[380-398]T$	CPSASE

InterPro
IPR006275
Domain

Carbamoyl-phosphate synthase, large subunit, glutamine-dependent
TIGR01369	$\"[2-1077]T$	CPSaseII_lrg: carbamoyl-phosphate synthase,

InterPro
IPR011607
Domain

MGS-like
PF02142	$\"[974-1065]T$	MGS

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[133-329]T$ $\"[679-874]T$	ATP_GRASP

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[188-403]T$ $\"[737-954]T$	no description

InterPro
IPR013817
Domain

Pre-ATP-grasp fold
G3DSA:3.40.50.20	$\"[1-116]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.1030.10	$\"[404-551]T$	no description
G3DSA:3.40.50.1380	$\"[955-1098]T$	no description
PTHR11405	$\"[1-1098]T$	CARBAMOYLTRANSFERASE RELATED
PS51257	$\"[1-24]T$	PROKAR_LIPOPROTEIN

","BeTs to 19 clades of COG0458COG name: Carbamoylphosphate synthase large subunit (split gene in MJ)Functional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0458 is aomp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB005480 (Carbamoyl-phosphate synthetase large chain, oligomerisation) with a combined E-value of 0. IPB005480A 6-57 IPB005480B 67-118 IPB005480C 214-266 IPB005480D 281-320 IPB005480E 344-379 IPB005480F 448-463 IPB005480G 522-546 IPB005480H 579-633 IPB005480I 658-690 IPB005480J 708-729 IPB005480K 781-805 IPB005480L 841-875 IPB005480A 555-606 IPB005480C 762-814 IPB005480D 826-865 IPB005480I 112-144 IPB005480J 163-184 IPB005480K 233-257***** IPB011607 (MGS-like) with a combined E-value of 3.5e-07. IPB011607A 81-97","Residues 559-690 are 87% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING PHOSPHATE AMMONIA) protein domain (PD000704) which is seen in Q8G815_BIFLO.Residues 159-243 are 68% similar to a (SYNTHASE LIGASE PHOSPHATE CARBAMOYL-PHOSPHATE BIOSYNTHESIS CHAIN CARBAMOYL- AMMONIA PYRIMIDINE GLUTAMINE-DEPENDENT) protein domain (PD819411) which is seen in CARB_HALN1.Residues 710-741 are 90% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING REPEAT AMMONIA) protein domain (PD757669) which is seen in Q8FT42_COREF.Residues 206-243 are 97% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING REPEAT AMMONIA) protein domain (PD762054) which is seen in Q6AF84_BBBBB.Residues 792-914 are 74% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING PHOSPHATE AMMONIA) protein domain (PD111324) which is seen in Q83HU0_TROW8.Residues 374-403 are identical to a (CHAIN BIOSYNTHESIS CARBAMOYL-PHOSPHATE LARGE LIGASE SYNTHASE SYNTHETASE PHOSPHATE AMMONIA MANGANESE) protein domain (PD001706) which is seen in Q827Q7_STRAW.Residues 374-551 are 48% similar to a (CARBAMOYL-PHOSPHATE CHAIN SYNTHASE LARGE PYRIMIDINE-SPECIFIC) protein domain (PDA0W2V9) which is seen in Q74JC5_LACJO.Residues 404-460 are 74% similar to a (CARBAMOYLPHOSPHATE CHAIN SYNTHASE LARGE) protein domain (PDA1A2W8) which is seen in Q6AF84_BBBBB.Residues 404-483 are 68% similar to a (CARBAMOYL-PHOSPHATE SYNTHASE CHAIN LARGE) protein domain (PD819412) which is seen in Q8G815_BIFLO.Residues 423-550 are 78% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING AMMONIA PHOSPHATE) protein domain (PD001652) which is seen in CARB_STRCO.Residues 559-690 are 87% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING PHOSPHATE AMMONIA) protein domain (PD000704) which is seen in Q8G815_BIFLO.Residues 692-738 are 76% similar to a (SYNTHASE CARBAMOYLPHOSPHATE LARGE SUBUNIT) protein domain (PDA0W2Y1) which is seen in Q89DR2_BRAJA.Residues 710-741 are 90% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING REPEAT AMMONIA) protein domain (PD757669) which is seen in Q8FT42_COREF.Residues 748-791 are 75% similar to a (BIOSYNTHESIS CHAIN SYNTHASE LARGE CARBAMOYL- PHOSPHATE AMMONIA PYRIMIDINE CARBAMOYL-PHOSPHATE MANGANESE) protein domain (PD873195) which is seen in Q89DR2_BRAJA.Residues 755-790 are 97% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING REPEAT AMMONIA) protein domain (PD926245) which is seen in Q827Q7_STRAW.Residues 792-914 are 74% similar to a (CHAIN CARBAMOYL-PHOSPHATE BIOSYNTHESIS LARGE LIGASE SYNTHASE SYNTHETASE ATP-BINDING PHOSPHATE AMMONIA) protein domain (PD111324) which is seen in Q83HU0_TROW8.Residues 925-975 are 62% similar to a (CARBAMOYL-PHOSPHATE SYNTHASE LARGE LIGASE SUBUNIT) protein domain (PDA0W2W6) which is seen in Q72FQ1_DESVH.Residues 925-1066 are 62% similar to a (CARBAMOYL-PHOSPHATE BIOSYNTHESIS C-TERMINAL PYRIMIDINE CHAIN MANGANESE SYNTHETASE ATP-BINDING AMMONIA SYNTHASE) protein domain (PDA18359) which is seen in CAB2_METKA.Residues 925-1066 are 50% similar to a (BIOSYNTHESIS CHAIN PHOSPHATE PYRIMIDINE CARBAMOYL-PHOSPHATE MANGANESE REPEAT SYNTHETASE ATP-BINDING CARBAMOYL-) protein domain (PDA184U9) which is seen in CARB_HALER.Residues 925-976 are 65% similar to a (ADP-FORMING CARBAMATE-PHOSPHORYLATING LIGASE) protein domain (PDA0W2W5) which is seen in Q9SE38_MEDSA.Residues 925-1053 are 58% similar to a (BIOSYNTHESIS CHAIN PHOSPHATE PYRIMIDINE CARBAMOYL-PHOSPHATE MANGANESE REPEAT SYNTHETASE ATP-BINDING CARBAMOYL-) protein domain (PDA18499) which is seen in CARB_PASMU.Residues 956-1055 are 55% similar to a (CARBAMOYL-PHOSPHATE SUBUNIT SYNTHASE LARGE LIGASE) protein domain (PDA18886) which is seen in Q6F8M6_ACIAD.Residues 957-1053 are 54% similar to a (CARBAMOYL-PHOSPHATE CHAIN PYRIMIDINE MANGANESE REPEAT SYNTHETASE ATP-BINDING AMMONIA BIOSYNTHESIS SYNTHASE) protein domain (PDA185D3) which is seen in CARB_BACHD.Residues 957-1066 are 51% similar to a (CARBAMOYL-PHOSPHATE SUBUNIT PROBABLE SYNTHASE LARGE) protein domain (PDA18696) which is seen in Q6AIK5_BBBBB.Residues 964-1066 are 69% similar to a (BIOSYNTHESIS CHAIN IMP CARBAMOYL-PHOSPHATE SYNTHETASE LARGE LIGASE SYNTHASE PHOSPHORIBOSYLAMINOIMIDAZOLECARBOXAMIDE CYCLOHYDROLASE) protein domain (PD002195) which is seen in Q827Q7_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 126 (E_value = 7.2e-52) place ANA_0807 in the CPSase_L_chain family which is described as Carbamoyl-phosphate synthase L chain, N-terminal domain.Residues 128 to 364 (E_value = 4.5e-116) place ANA_0807 in the CPSase_L_D2 family which is described as Carbamoyl-phosphate synthase L chain, ATP binding domain.Residues 424 to 545 (E_value = 7.9e-46) place ANA_0807 in the CPSase_L_D3 family which is described as Carbamoyl-phosphate synthetase large chain, oligomerisation domain.Residues 555 to 672 (E_value = 2.4e-18) place ANA_0807 in the CPSase_L_chain family which is described as Carbamoyl-phosphate synthase L chain, N-terminal domain.Residues 674 to 886 (E_value = 5.6e-23) place ANA_0807 in the CPSase_L_D2 family which is described as Carbamoyl-phosphate synthase L chain, ATP binding domain.Residues 974 to 1065 (E_value = 3.5e-16) place ANA_0807 in the MGS family which is described as MGS-like domain.","","synthase, large subunit (carB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0808","866141","864894","1248","5.68","-10.97","44785","TTGAGGCTCCCGCCGGCTCAGCTCATGCCTGAGCTGAGCCACCGCCCAGCCGCCCTCCTCGTGCTGGAGGACGGCTGGGCCCTGCGGGGCCGCAGCTACGGGGCCCAAGGGCGCACCATTGGAGAGATCGTCTTCTCCACCGGGATGACCGGGTACCAGGAAACACTGACCGATCCCTCCTACCACCGCCAGATCGTCGTGCAGACCGCGCCACACATCGGTAACACCGGGGTCAACGACGAGGACGCCGAGTCGGACCGTATCTGGGTGGCCGGCTACGTCGTACGCGAGCCTGCTCGGCGGGCCTCCAGCTGGCGCTCCCGTCGGGAGCTGGAGGACGATCTGCGTGACGCCGGCATCGTTGGCCTCTGCGAGGTCGACACCCGGGCCCTGACCCGGCATCTGCGCGAGGCGGGTGCGATGCGTGGCGGCATCTTCTCCGGGGATGCCCTGCCTGCCGGAGGCACTGACCCCGGTGGTCCCAGCCAGGCCTGCATCGACATCTGCCTGGAGGCCGTGCGCAGCGAACCGCCCATGAGCGGCCGCGCCCTGGCCGCCGAGGTGACCACTCCCTCCGGGTACGTCGTCGAGCCCACCGGACCGGCCGAGGGACAGGAGCCGGTCGCGGTGCTGGTCGCCATCGACCTGGGCATCAAGTCCCGCACCCCGTGGCAGTTCGCCGAGCGCGGCGTACGCGTCCACGTCCTGCCCCAGTCCACGACTCTGTCCGAGATTCTTGCCCTCAGACCCGATGGCGTCCTGTTCTCCAACGGCCCCGGAGACCCGGGGACAGCCGACGCCGAGATCGAGCTCCTGCGAGGCGTCCTCGACGCACGCATTCCCTTCTTCGGCATTTGCTTGGGCAATCAGCTCCTGGGACGTGCCCTGGGCTACGGCACCTACAAGCTCGCTTACGGGCACCGCGGTGTCAACCAGCCCGTTGTGGACCGCGCCACCGGAAAGGTGGAGATCACGGCCCACAACCACGGCTTCGCCGTCGACGCCCCCATCGATCAGCCCTCCGTCGCCCCCTTCGACAACGGTCGCTACGGCCGGGTGGAGGTCTCCCACCTGGGACTCAATGACGGTGTGGTTGAAGGGCTACGGGCGCTGGATCTGCCGGCCTTCTCCGTCCAGTACCACCCCGAGGCCGCTGCTGGACCCCATGACGCCGAGCACCTCTTCGACCGATTCATCCGCCTCATGCGGGAGCACCGCCGGGGCCAGGACCGCGAGGACACGAACTGA","LRLPPAQLMPELSHRPAALLVLEDGWALRGRSYGAQGRTIGEIVFSTGMTGYQETLTDPSYHRQIVVQTAPHIGNTGVNDEDAESDRIWVAGYVVREPARRASSWRSRRELEDDLRDAGIVGLCEVDTRALTRHLREAGAMRGGIFSGDALPAGGTDPGGPSQACIDICLEAVRSEPPMSGRALAAEVTTPSGYVVEPTGPAEGQEPVAVLVAIDLGIKSRTPWQFAERGVRVHVLPQSTTLSEILALRPDGVLFSNGPGDPGTADAEIELLRGVLDARIPFFGICLGNQLLGRALGYGTYKLAYGHRGVNQPVVDRATGKVEITAHNHGFAVDAPIDQPSVAPFDNGRYGRVEVSHLGLNDGVVEGLRALDLPAFSVQYHPEAAAGPHDAEHLFDRFIRLMREHRRGQDREDTN$","Carbamoyl-phosphate synthase, small subunit","Cytoplasm","carbamoyl-phosphate synthase, small subunit","carbamoyl-phosphate synthase; small subunit ","carbamoyl-phosphate synthase, small subunit","","Weng M.L., Zalkin H. Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. J. Bacteriol. 1987. 169(7):3023-3028. PMID: 3298209Nyunoya H., Lusty C.J. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. J. Biol. Chem. 1984. 259(15):9790-9798. PMID: 6086650","","","

InterPro
IPR000991
Domain

Glutamine amidotransferase class-I
PF00117	$\"[212-401]T$	GATase

InterPro
IPR001317
Domain

Carbamoyl-phosphate synthase, GATase region
PR00099	$\"[211-225]T$ $\"[250-264]T$ $\"[281-297]T$ $\"[298-315]T$ $\"[323-334]T$	CPSGATASE

InterPro
IPR002474
Domain

Carbamoyl-phosphate synthase, small chain
PF00988	$\"[16-154]T$	CPSase_sm_chain

InterPro
IPR006220
Domain

Anthranilate synthase component II/delta crystallin
PR00097	$\"[253-262]T$ $\"[281-292]T$ $\"[377-390]T$	ANTSNTHASEII

InterPro
IPR006274
Domain

Carbamoyl-phosphate synthase, small subunit
TIGR01368	$\"[18-404]T$	CPSaseIIsmall: carbamoyl-phosphate synthase

InterPro
IPR011702
Domain

Glutamine amidotransferase superfamily
PR00096	$\"[253-262]T$ $\"[281-292]T$ $\"[377-390]T$	GATASE

InterPro
IPR012998
Active_site

Glutamine amidotransferase, class I, active site
PS00442	$\"[281-292]T$	GATASE_TYPE_I

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[178-408]T$	no description
G3DSA:3.50.30.20	$\"[15-164]T$	no description
PTHR11405	$\"[18-415]T$	CARBAMOYLTRANSFERASE RELATED
PTHR11405:SF4	$\"[18-415]T$	CARBAMOYL-PHOSPHATE SYNTHASE, SMALL CHAIN-RELATED

","BeTs to 19 clades of COG0505COG name: Carbamoylphosphate synthase small subunitFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0505 is aomp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002474 (Carbamoyl-phosphate synthase, small chain) with a combined E-value of 2.3e-123. IPB002474A 41-77 IPB002474B 103-145 IPB002474C 211-237 IPB002474D 251-262 IPB002474E 281-314 IPB002474F 357-399***** IPB001317 (Carbamoyl-phosphate synthase protein GATase domain signature) with a combined E-value of 5.2e-24. IPB001317B 250-264 IPB001317C 281-297 IPB001317D 298-315 IPB001317E 323-334***** IPB006220 (Anthranilate synthase component II signature) with a combined E-value of 5.5e-15. IPB006220B 253-262 IPB006220C 281-292 IPB006220F 377-390***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 4.6e-12. IPB000991A 281-298 IPB000991B 374-384","Residues 23-156 are similar to a (CHAIN GLUTAMINE BIOSYNTHESIS CARBAMOYL-PHOSPHATE SMALL LIGASE SYNTHASE SYNTHETASE PHOSPHATE ARGININE) protein domain (PD001375) which is seen in CARA_STRCO.Residues 156-234 are 60% similar to a (BIOSYNTHESIS CHAIN GLUTAMINE AMIDOTRANSFERASE CARBAMOYL- PHOSPHATE PYRIMIDINE SYNTHASE CARBAMOYL-PHOSPHATE SMALL) protein domain (PD997622) which is seen in CARA_BIFLO.Residues 227-297 are 77% similar to a (GLUTAMINE SYNTHASE AMIDOTRANSFERASE BIOSYNTHESIS LIGASE GMP SYNTHETASE CTP CHAIN COMPONENT) protein domain (PD000306) which is seen in CARA_STRCO.Residues 300-368 are 84% similar to a (CHAIN GLUTAMINE BIOSYNTHESIS CARBAMOYL-PHOSPHATE SMALL LIGASE SYNTHASE SYNTHETASE PHOSPHATE ARGININE) protein domain (PD330440) which is seen in CARA_BIFLO.Residues 376-401 are 96% similar to a (CHAIN GLUTAMINE BIOSYNTHESIS CARBAMOYL-PHOSPHATE SMALL LIGASE SYNTHASE SYNTHETASE PHOSPHATE ARGININE) protein domain (PD924342) which is seen in Q7U055_MYCBO.","","-53% similar to PDB:1BXR STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP (E_value = 1.5E_78);-53% similar to PDB:1CE8 CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP (E_value = 1.5E_78);-53% similar to PDB:1CS0 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED AT CYS269 IN THE SMALL SUBUNIT WITH THE TETRAHEDRAL MIMIC L-GLUTAMATE GAMMA-SEMIALDEHYDE (E_value = 1.5E_78);-53% similar to PDB:1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI (E_value = 1.5E_78);-53% similar to PDB:1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin (E_value = 1.5E_78);","Residues 16 to 154 (E_value = 1.5e-68) place ANA_0808 in the CPSase_sm_chain family which is described as Carbamoyl-phosphate synthase small chain, CPSase domain.Residues 212 to 401 (E_value = 1.2e-52) place ANA_0808 in the GATase family which is described as Glutamine amidotransferase class-I.","","synthase, small subunit (carA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0809","867432","866110","1323","5.20","-20.00","46356","GTGACCTCCCACCTCCTGACCGGTGTCCGCCCCTACGGCGAGGACCCCACTGACATTCTCATTACCGACGGCACCATCACCGCCATCGGCCCTGACGTAGCGGCGAAGGCCCCGGCCGATGTCCAGCGCCATGACCTGGACGGGCTCATCGCATTGCCCGGGCTCGTCGATATCCACACTCACCTGCGCGAGCCCGGAGGGGAGTCCGCCGAGACCATCTACTCCGGTACCCGCGCCGCAGCCGTCGGCGGCTACACCGCCGTCTTCGCGATGGCCAACACCACGCCCGTCCAGGACAATGCCGGTGTCGTGGAGCAGGTGCTGCGGCTGGGCCGTGAAGCCGGCTGGGTGGACGTCCATCCGGTGGGCGCAGTCTCAGCGGGACTGGCCGGCGAGCACCTGTCCGACATGGGTGCCATGGCCACCTCCGCCGCCCGAGTGCGGGTGTTCTCCGATGACGGCAAGTGCGTCTCCGACCCCGTCCTCATGCGCAGGGCCCTGGAGTACGTCAAGTCCTTCGACGGCGTCATCGCCCAGCACGCACAGGATCCCCGCCTCACCGAGGGATCCCAGATGCACGAGGGCGTCGTCTCCGCCGAGCTGGGACTGCGCGGCTGGCCGGCAGTGGCGGAGGAGTCGATCATCGCCCGCGACGTCCTGCTGGCAGAGCACGTCGGCTCGCGTCTGCACGTGTGCCACCTGTCCACTGCGGGCAGCGTCGGCATCATCCGCTGGGCCAAGTCCCGTGGCATCAATGTCACCGCTGAGGTCACGCCGCACCACCTCCTGCTGACTGACGAGATGGCCCGCACCTACTCCCCGCTGTACAAGGTCAACCCCCCGCTGCGCACGGCCGAGGACGTCGAGGCGGTTCGCGAGGCCCTGGCCGATGGCACCATCGACGTCGTCGGCACCGACCACGCCCCGCACCCGGTGGAGGACAAGGACTGCGAGTGGCAGGCCGGAGCCTTCGGCATGACCGGCCTGGAGACCGCACTGAGCGTCCTGATCGACACGATGGTCGCCCCCGGCCGCATGACCTGGCGCGACATCGCCCGGGCCATGTCCTCGACCCCCGCCCGCATCGGCCGCCTGAGCGACCAGGGCTGCGAGCTCGAGGTCGGTGCCCCGGCCAACATCACTGTGGTCGACCCCGAGGTGCGCCGCACCGTCGACGCCTCCGCCCAGTGGACCAGCTCCACCAACACCCCCTACGCCGGGATGGAGCTGCCGGGACAGGTCATGGCCACCTTCCTCCACGGCCGCCCCACCGTGCTCGACGGCGCTCCCGTTGAGGCTCCCGCCGGCTCAGCTCATGCCTGA","VTSHLLTGVRPYGEDPTDILITDGTITAIGPDVAAKAPADVQRHDLDGLIALPGLVDIHTHLREPGGESAETIYSGTRAAAVGGYTAVFAMANTTPVQDNAGVVEQVLRLGREAGWVDVHPVGAVSAGLAGEHLSDMGAMATSAARVRVFSDDGKCVSDPVLMRRALEYVKSFDGVIAQHAQDPRLTEGSQMHEGVVSAELGLRGWPAVAEESIIARDVLLAEHVGSRLHVCHLSTAGSVGIIRWAKSRGINVTAEVTPHHLLLTDEMARTYSPLYKVNPPLRTAEDVEAVREALADGTIDVVGTDHAPHPVEDKDCEWQAGAFGMTGLETALSVLIDTMVAPGRMTWRDIARAMSSTPARIGRLSDQGCELEVGAPANITVVDPEVRRTVDASAQWTSSTNTPYAGMELPGQVMATFLHGRPTVLDGAPVEAPAGSAHA$","Dihydroorotase","Cytoplasm, Extracellular","Dihydroorotase (DHOase)","dihydroorotase ","dihydroorotase, multifunctional complex type","","Nygaard P., Duckert P., Saxild H.H. Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis. J. Bacteriol. 1996. 178(3):846-853. PMID: 8550522Holm L., Sander C. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 1997. 28(1):72-82. PMID: 9144792","","","

InterPro
IPR002195
Domain

Dihydroorotase
PS00483	$\"[304-315]T$	DIHYDROOROTASE_2

InterPro
IPR003778
Domain

Allophanate hydrolase subunit 2
SM00797	$\"[152-342]T$	no description

InterPro
IPR004722
Domain

Dihydroorotase multifunctional complex type
TIGR00857	$\"[17-428]T$	pyrC_multi: dihydroorotase, multifunctional

InterPro
IPR005847
Domain

Dihydroorotase region
PD000518	$\"[372-428]T$	Q7WMP7_BORBR_Q7WMP7;

InterPro
IPR006680
Domain

Amidohydrolase 1
PF01979	$\"[50-384]T$	Amidohydro_1

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.140	$\"[54-411]T$	no description
PTHR11647	$\"[45-434]T$	AMINOHYDROLASE
PTHR11647:SF2	$\"[45-434]T$	DIHYDROOROTASE

","BeTs to 19 clades of COG0044COG name: Dihydroorotase and related cyclic amidohydrolasesFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0044 is aompkzyqvdrlbcef--s-uj----Number of proteins in this genome belonging to this COG is 1","***** IPB005847 (Dihydroorotase region) with a combined E-value of 8.7e-57. IPB005847A 1-30 IPB005847B 56-90 IPB005847E 171-218 IPB005847F 221-269 IPB005847G 311-337 IPB005847H 366-385 IPB005847I 402-439***** IPB002195 (Dihydroorotase) with a combined E-value of 3.1e-22. IPB002195A 83-97 IPB002195B 253-269 IPB002195C 303-315***** IPB013108 (Amidohydrolase 3) with a combined E-value of 1.4e-07. IPB013108A 44-63","Residues 14-138 are 51% similar to a (SUBUNIT PYRC_apos; ASPARTATE TRANSCARBAMOYLASE) protein domain (PDA188T4) which is seen in Q9A5K3_CAUCR.Residues 49-169 are 52% similar to a (DIHYDROOROTASE) protein domain (PDA1D3Z7) which is seen in Q7NEQ6_GLOVI.Residues 75-361 are similar to a (HYDROLASE DIHYDROOROTASE ZINC PYRIMIDINE BIOSYNTHESIS METAL-BINDING DHOASE DIHYDROPYRIMIDINASE COLLAPSIN MEDIATOR) protein domain (PD001085) which is seen in PYRC_STRCO.Residues 93-207 are 54% similar to a (ZINC PYRIMIDINE HYDROLASE METAL-BINDING DHOASE DIHYDROOROTASE BIOSYNTHESIS) protein domain (PD752686) which is seen in PYRC_DEIRA.Residues 229-422 are 46% similar to a (P32375 ALLANTOINASE SINGLETON DAL1 SACCHAROMYCES CEREVISIAE YIR027C) protein domain (PD946212) which is seen in Q6CUK0_EEEEE.","","-53% similar to PDB:1XRF The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution (E_value = 1.6E_62);-53% similar to PDB:1XRT The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex Aeolicus at 1.7 A Resolution (E_value = 1.6E_62);-45% similar to PDB:1GKR L-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM ARTHROBACTER AURESCENS (E_value = 1.5E_36);-43% similar to PDB:2GWN The structure of putative dihydroorotase from Porphyromonas gingivalis. (E_value = 9.8E_28);-43% similar to PDB:1YNY Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition (E_value = 8.3E_27);","Residues 50 to 382 (E_value = 0.00088) place ANA_0809 in the Amidohydro_3 family which is described as Amidohydrolase family.Residues 50 to 384 (E_value = 3.6e-20) place ANA_0809 in the Amidohydro_1 family which is described as Amidohydrolase family.","","(DHOase) (DHOase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0810","868418","867429","990","6.60","-2.43","35202","ATGAAGCACCTGCTCTCCGCCAAGGACCTGACCCACGACGAGGCGGTCATGGTCCTGGACACCGCCGAGGCGATGGCCGCCACCCAGCGTCATGCGGTCAAGAAGCTTCCGACGCTGCGCGGCAAGACCGTGGTGAACCTCTTCTTCGAGGACTCCACCCGCACCAGGCTCTCCTTCGAGGCCGCCGCCAAGCGCCTGAGCGCCGACGTCATCAACTTCTCGGCCAAGGGCTCCTCACTGTCCAAGGGCGAGTCCCTCAAGGACACCGCCCAGACGATCATGGCCATGGGGGCGGACGCCGTCGTCGTGCGCCACTCCGCCTGCGGCGCCGCACACCTGCTGGCCCACGCCGGCTGGATCAACGTGCCGGTCCTCAACGCCGGTGACGGCACCCACCAGCACCCCACTCAGGCCCTTCTGGACGCCATGACGCTGCGACGCTGGTACGTGCCCGGAGCGCCAGCCACAGCGGACGGCAGCCCCGCCCCGCAGGGGCGCGACCTGGAGGGCGCCCGCCTCATCATCGTGGGAGACGTCCTGCACTCCCGGGTGGCCCGTTCCAACGTGGACCTCATGACGGCGCTCGGCGCCAAGGTCACGCTCGTGGCGCCTCCCACACTGCTGCCCGTCGGTATGGACGACTGGCCCTGCGAGGTCTCCTACAACCTCGATGAGGCGATCGAGGAGATCCAGCCCGACGCCGTCATGATGCTGCGCGTCCAGCGTGAGCGCATGAGTGCCGCAGGAGGGGGCTTCTTCCCGAGCCCTGGCGAGTACTCCAGCGTCTACGGCCTCACTTCCGCCCGTCGCCGGGCCATGCCGGAGCACGCGATCGTCATGCACCCCGGCCCCATGAACCGCGGCCTCGAGATCACCGCCGAGGCCGCCGACGACCCCCGCTCGCGCATTATCGAGCAGGTCGGCAACGGAGTCTCCGTCCGTATGGCCGCCCTCTACCTCCTCCTCGCTGACGAAGGGAACCAGCTGTGA","MKHLLSAKDLTHDEAVMVLDTAEAMAATQRHAVKKLPTLRGKTVVNLFFEDSTRTRLSFEAAAKRLSADVINFSAKGSSLSKGESLKDTAQTIMAMGADAVVVRHSACGAAHLLAHAGWINVPVLNAGDGTHQHPTQALLDAMTLRRWYVPGAPATADGSPAPQGRDLEGARLIIVGDVLHSRVARSNVDLMTALGAKVTLVAPPTLLPVGMDDWPCEVSYNLDEAIEEIQPDAVMMLRVQRERMSAAGGGFFPSPGEYSSVYGLTSARRRAMPEHAIVMHPGPMNRGLEITAEAADDPRSRIIEQVGNGVSVRMAALYLLLADEGNQL$","Aspartate carbamoyltransferase","Cytoplasm","aspartate carbamoyltransferase","aspartate carbamoyltransferase ","aspartate carbamoyltransferase","","Lerner C.G., Switzer R.L. Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB). J. Biol. Chem. 1986. 261(24):11156-11165. PMID: 3015959Davidson J.N., Chen K.C., Jamison R.S., Musmanno L.A., Kern C.B. The evolutionary history of the first three enzymes in pyrimidine biosynthesis. Bioessays 1993. 15(3):157-164. PMID: 8098212Takiguchi M., Matsubasa T., Amaya Y., Mori M. Evolutionary aspects of urea cycle enzyme genes. Bioessays 1989. 10(5):163-166. PMID: 2662961Baur H., Stalon V., Falmagne P., Luethi E., Haas D. Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli. Eur. J. Biochem. 1987. 166(1):111-117. PMID: 3109911Houghton J.E., Bencini D.A., O. Donovan G.A., Wild J.R. Protein differentiation: a comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 1984. 81(15):4864-4868. PMID: 6379651Ke H.M., Honzatko R.B., Lipscomb W.N. Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution. Proc. Natl. Acad. Sci. U.S.A. 1984. 81(13):4037-4040. PMID: 6377306Beernink P.T., Endrizzi J.A., Alber T., Schachman H.K. Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(10):5388-5393. PMID: 10318893","","","

InterPro
IPR002082
Family

Aspartate carbamoyltransferase, eukaryotic
PR00101	$\"[38-60]T$ $\"[76-85]T$ $\"[133-150]T$ $\"[235-244]T$ $\"[279-284]T$ $\"[303-317]T$	ATCASE
TIGR00670	$\"[2-323]T$	asp_carb_tr: aspartate carbamoyltransferase

InterPro
IPR006130
Family

Aspartate/ornithine carbamoyltransferase
PR00100	$\"[48-67]T$ $\"[134-145]T$ $\"[275-284]T$ $\"[287-310]T$	AOTCASE
PIRSF000416	$\"[2-328]T$	Ornithine/aspartate carbamoyltransferase
PS00097	$\"[48-55]?$	CARBAMOYLTRANSFERASE

InterPro
IPR006131
Domain

Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region
PF00185	$\"[168-321]T$	OTCace

InterPro
IPR006132
Domain

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
PF02729	$\"[2-148]T$	OTCace_N

InterPro
IPR014695
Family

Aspartate carbamoyltransferase, bacterial/plant
PIRSF500169	$\"[2-325]T$	Aspartate carbamoyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1370	$\"[2-154]T$	no description
PTHR11405	$\"[1-153]T$ $\"[170-325]T$	CARBAMOYLTRANSFERASE RELATED

","BeTs to 20 clades of COG0540COG name: Aspartate carbamoyltransferase, catalytic chainFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0540 is aompkzyqvdrlbcefg-snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002082 (Aspartate carbamoyltransferase signature) with a combined E-value of 1.5e-44. IPB002082A 38-60 IPB002082B 76-85 IPB002082C 133-150 IPB002082D 235-244 IPB002082E 279-284 IPB002082F 303-317***** IPB002292 (Ornithine carbamoyltransferase signature) with a combined E-value of 2.4e-21. IPB002292A 46-60 IPB002292B 79-92 IPB002292C 122-136 IPB002292D 175-185 IPB002292E 301-312","Residues 25-142 are 87% similar to a (TRANSFERASE CARBAMOYLTRANSFERASE ASPARTATE ORNITHINE BIOSYNTHESIS ARGININE OTCASE TRANSCARBAMYLASE PYRIMIDINE ATCASE) protein domain (PD000708) which is seen in PYRB_STRCO.Residues 167-322 are 79% similar to a (TRANSFERASE CARBAMOYLTRANSFERASE ASPARTATE ORNITHINE BIOSYNTHESIS ARGININE OTCASE TRANSCARBAMYLASE PYRIMIDINE ATCASE) protein domain (PD409592) which is seen in PYRB_STRCO.","","-52% similar to PDB:2AT2 MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION (E_value = 1.6E_48);-48% similar to PDB:1D09 ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA) (E_value = 1.4E_28);-48% similar to PDB:2A0F Structure of D236A mutant E. coli Aspartate Transcarbamoylase in presence of Phosphonoacetamide at 2.90 A resolution (E_value = 1.4E_28);-48% similar to PDB:1EKX THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE) (E_value = 1.8E_28);-48% similar to PDB:1Q95 Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate (E_value = 1.8E_28);","Residues 2 to 148 (E_value = 1.1e-50) place ANA_0810 in the OTCace_N family which is described as Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain.Residues 168 to 321 (E_value = 5.9e-10) place ANA_0810 in the OTCace family which is described as Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain.","","carbamoyltransferase (pyrB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0811","869092","868415","678","6.41","-1.83","23775","ATGGCCGAAAGTTTGTCAGGCGCCTTGAGCGCACCAACCCAGGGCAAGGAGATCCTCGGACCTCCCGATATAGCCCGTTCCCTGTTCCGTATCGCGCACGAGATTCTGGAACGCAACCACGGGACGCAGGACATCGTCGTCCTCGGGATCCCCAGTGGGGGAGCACCGCTCGCGCACAGACTCGTCGAGGCGCTTGCTGTCGCCGCGGGAGAAGGGACGCAGTGGTCCGAGCAGGCGGGACAGGCGCGGGCCGATGCCGCCAATGCCAAGGTCCCGGTCGGCACCCTGGACATCACCATGTACCGCGATGACCTGGGACGTCACCCGATCCGAGTTCCCCGTCCCACGGAGATCCCCCAGGGCGGCATCGACGGCAAAGTCGTCATCCTCGTTGACGACGTCCTCTACTCCGGGCGCACCATCCGGGCCGCCCTCGACGCTCTGGGCGCCATCGGCCGCCCCCGGGCCGTGCAACTAGCCACACTCGTGGACCGCGGACACCGCGAGCTGCCCATCCGAGCCGACTACGTGGGTAAGAACCTGCCGACCTCCCGCTCTGAGAAAGTCGTGGTGTCCCTGACCGAGCTCGGCGCCTCCACCGACGCCGTCACCATCGTCCCCGCAGACGTCCCCACTGAGCGTTCGAGTGAGCGCAGCAACCAGGAGGCCACCCGATGA","MAESLSGALSAPTQGKEILGPPDIARSLFRIAHEILERNHGTQDIVVLGIPSGGAPLAHRLVEALAVAAGEGTQWSEQAGQARADAANAKVPVGTLDITMYRDDLGRHPIRVPRPTEIPQGGIDGKVVILVDDVLYSGRTIRAALDALGAIGRPRAVQLATLVDRGHRELPIRADYVGKNLPTSRSEKVVVSLTELGASTDAVTIVPADVPTERSSERSNQEATR$","Uracil phosphoribosyltransferase","Cytoplasm","PyrR bifunctional protein [Includes: Pyrimidineoperon regulatoryprotein; Uracil phosphoribosyltransferase","uracil phosphoribosyltransferase ","Uracil phosphoribosyltransferase","","","","","

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[14-182]T$	Pribosyltran

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2020	$\"[12-208]T$	no description
PTHR22573	$\"[123-182]T$	PHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF8	$\"[123-182]T$	HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE

","BeTs to 7 clades of COG2065COG name: Pyrimidine operon attenuation protein/uracil phosphoribosyltransferaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG2065 is ---------drlbc-f-h--------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 18-105 are 56% similar to a (TRANSCRIPTION OPERON PYRIMIDINE TRANSFERASE REGULATORY GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE URACIL PYRR UPRTASE) protein domain (PD405441) which is seen in Q7WZG7_STRGR.Residues 117-160 are 90% similar to a (TRANSCRIPTION TRANSFERASE OPERON REGULATORY PYRIMIDINE GLYCOSYLTRANSFERASE PYRR URACIL PHOSPHORIBOSYLTRANSFERASE UPRTASE) protein domain (PD746529) which is seen in PYRR_STRCO.Residues 123-160 are 86% similar to a (TRANSCRIPTION PYRIMIDINE OPERON REGULATORY TRANSFERASE GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE URACIL PYRR RNA-BINDING) protein domain (PD888968) which is seen in PYRR_ENTFA.Residues 162-195 are 85% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE TRANSCRIPTION PYRIMIDINE OPERON URACIL REGULATORY INCLUDES: PYRR) protein domain (PDA0E8U1) which is seen in Q72CA0_DESVH.","","-67% similar to PDB:1UFR Crystal Structure of TT1027 from Thermus thermophilus HB8 (E_value = 9.8E_43);-63% similar to PDB:1W30 PYRR OF MYCOBACTERIUM TUBERCULOSIS AS A POTENTIAL DRUG TARGET (E_value = 6.3E_42);-63% similar to PDB:1A3C PYRR, THE BACILLUS SUBTILIS PYRIMIDINE BIOSYNTHETIC OPERON REPRESSOR, DIMERIC FORM (E_value = 5.5E_38);-63% similar to PDB:1A4X PYRR, THE BACILLUS SUBTILIS PYRIMIDINE BIOSYNTHETIC OPERON REPRESSOR, HEXAMERIC FORM (E_value = 5.5E_38);-63% similar to PDB:1NON PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus (E_value = 1.0E_36);","Residues 14 to 182 (E_value = 9e-17) place ANA_0811 in the Pribosyltran family which is described as Phosphoribosyl transferase domain.","","bifunctional protein [Includes: Pyrimidine operon regulatoryprotein; Uracil phosphoribosyltransferase (UPRTase)] (minor)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0812","869418","870347","930","5.48","-9.70","33421","GTGGAGCAGGCACGGTCCGGTGTTGCTGCTGCGCCAGCGACTTCTTCTCAAGCAAGGAATGCCTTTATGGAACTCCCTACTCGACGTTCGATCATCACCGGCCTCGGCGCCGGAGCAGGACTGGCCGCCGCCGGTCTCACCTCCCCCTTGCCGGCAGCGGCGGCGGAGTCGTCCTACGATTTCAGCAGCGTCATCTTCAATGAGCAGTTCTCTGACGGATCGGACTTCTCCCCGTCACGATGGCGGGACAACCGCTCTGAGCCCGAGTCCTGTGCCAGCTACGACTGGGGGGTGTTCACCCATGACACCCACAGCGTCAGCAACGGCGTCGGGCACGTCCTGTGGCGCAAGCGGGCCACCCCCCTCAAGGGCTTCCAGAACCGCTTCGACAAGGAGCCGACCCTGCGCTACGTCGACCAGGCCTTTGTCACCACACAAGGGCTGTTCTCCTTCGTCTACGGCTCCTTGGAGACCCGGGCACGCTTCCCTCAGTCGGCCGAGGGACTCTTCGCCGGCATCTGGTTGCGGGCGGACGACGGCGGTAACGGCGGCGAGATCGATGTTGTGGAGACCTACGGCGGCGGCAGTGCCACCGGTATCGCCGAGTCGACTGTGCACTACGGCCAGGCGGGGGGCAAAGGAAGCAACCTGGGGGTCTCACCGCGGCCCGATCTCACCCAGTGGCACACCTACGGGATGGAGAAGACCCCCGAGAGCATTCTCTTCCTCTTCGACGGTCAGCCCTACCATGAGGTCTTGCGTTCAGCATCGCAACAGGAGTTCGATGCCTGCTTCGGTGACGACGCCGCCTACCACATCTGCCTGACCACACACAGCGGAAGCATCCACCGGGGACGACTCAAGCACGAGGGCTTCACGCAGGCCCAGGTGGATATTGACTACATCGTTGTGCGGGCCATGGATGAGTAG","VEQARSGVAAAPATSSQARNAFMELPTRRSIITGLGAGAGLAAAGLTSPLPAAAAESSYDFSSVIFNEQFSDGSDFSPSRWRDNRSEPESCASYDWGVFTHDTHSVSNGVGHVLWRKRATPLKGFQNRFDKEPTLRYVDQAFVTTQGLFSFVYGSLETRARFPQSAEGLFAGIWLRADDGGNGGEIDVVETYGGGSATGIAESTVHYGQAGGKGSNLGVSPRPDLTQWHTYGMEKTPESILFLFDGQPYHEVLRSASQQEFDACFGDDAAYHICLTTHSGSIHRGRLKHEGFTQAQVDIDYIVVRAMDE$","Beta-glucanase/beta-glucan synthetase","Extracellular","Glycosyl hydrolases family 16 family","hypothetical protein predicted by Glimmer/Critica","glycoside hydrolase, family 16","","Sanz-aparicio J., Hermoso J., Grangeiro T.B., Calvete J.J., Cavada B.S. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett. 1997. 405(1):114-118. PMID: 9094437Ackerman S.J., Liu L., Kwatia M.A., Savage M.P., Leonidas D.D., Swaminathan G.J., Acharya K.R. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. J. Biol. Chem. 2002. 277(17):14859-14868. PMID: 11834744Hahn M., Pons J., Planas A., Querol E., Heinemann U. Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett. 1995. 374(2):221-224. PMID: 7589539Michel G., Chantalat L., Duee E., Barbeyron T., Henrissat B., Kloareg B., Dideberg O. The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases. Structure 2001. 9(6):513-525. PMID: 11435116","","","

InterPro
IPR000757
Domain

Glycoside hydrolase, family 16
PF00722	$\"[100-303]T$	Glyco_hydro_16

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[26-54]T$	TAT_signal_seq: Tat (twin-arginine transloc

InterPro
IPR013320
Domain

Concanavalin A-like lectin/glucanase, subgroup
G3DSA:2.60.120.200	$\"[49-304]T$	no description

noIPR
unintegrated

unintegrated
PTHR10963	$\"[23-252]T$	SECRETED GLUCOSIDASE-RELATED

","BeTs to 3 clades of COG2273COG name: Beta-glucanase/Beta-glucan synthetaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2273 is ------y-v-r-b--------j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 100 to 303 (E_value = 2.6e-07) place ANA_0812 in the Glyco_hydro_16 family which is described as Glycosyl hydrolases family 16.","","hydrolases family 16 family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0813","871986","871270","717","8.90","4.55","25660","ATGAGTTACCTACCTCCCCAGAATCCCCATGACGACCCCCGGATCGAGGGCGCCGGTTATCTGCGGAACACCCCCATGCCGGTTCCTTACGGCCGCTACGCCTCCTCAATGGGGAACCCTCCAATGGGGCAGATTCCTCCTGTTGCTGGCTTCGGCTCGAATGACCCTGTGCTGATGGAGGTTCAGCGCAAGCGCTCCACGACCCGCAAGGTCTCGGTCTCGAGCTGCACCATCGGGCTCATCACCATGCTCATTCAGGTGTTCATCACGACTTTCTTATTCGCCGCTAATATTTTGCCGTTCCTGGGTTTCGCACTCCTTGCCGTTCTTATGATGATCGCCGGCCCGTTCGTCGTTGGCCTCGTGTGGGTCGCTACGTTCATCGTCGCTCTCATCGCTTGTATTTGGGCTCATTCCCGCACGCCTCGGGTTCAGCCTGATGGATGGGTCGAGGCCAAAATGCCAACGTCGGCAATGCTGGCCGCGAGTATTGTGGCGGGAGTTCCCACTCTCGTCATTTATGCCACTTTGTACTTGCTGATCCGCCAGGGCATCGATGATGGGTACTCCCACACCACCGTCTTCAATTCAGTGCTTCTTGCCTGCGACCTGGTGGAGGCTCTCATCGCGGTGGGCATCTTCTATCTTCTCCGTAGGAGCAAGGCGCTGAACCCGGCGGTCACGGCGTCTCAGGCCCAGGGAACGCAATACGCATGA","MSYLPPQNPHDDPRIEGAGYLRNTPMPVPYGRYASSMGNPPMGQIPPVAGFGSNDPVLMEVQRKRSTTRKVSVSSCTIGLITMLIQVFITTFLFAANILPFLGFALLAVLMMIAGPFVVGLVWVATFIVALIACIWAHSRTPRVQPDGWVEAKMPTSAMLAASIVAGVPTLVIYATLYLLIRQGIDDGYSHTTVFNSVLLACDLVEALIAVGIFYLLRRSKALNPAVTASQAQGTQYA$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[77-97]?$ $\"[103-137]?$ $\"[158-178]?$ $\"[197-217]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[115-143]?$ $\"[149-183]?$ $\"[204-224]?$ $\"[243-263]?$	transmembrane_regions

InterPro
IPR006027
Domain

NusB/RsmB/TIM44
G3DSA:1.10.940.10	$\"[4-136]T$	no description
PF01029	$\"[5-140]T$	NusB

InterPro
IPR011605
Family

NusB antitermination factor
TIGR01951	$\"[4-138]T$	nusB: transcription antitermination factor

","BeTs to 14 clades of COG0781COG name: Transcription termination factorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0781 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 7-136 are 68% similar to a (UTILIZATION SUBSTANCE N B NUSB TRANSCRIPTION TERMINATION HOMOLOG RNA-BINDING FACTOR) protein domain (PD241318) which is seen in Q741J2_MYCPA.","","-65% similar to PDB:1EYV THE CRYSTAL STRUCTURE OF NUSB FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.1E_25);-53% similar to PDB:1TZT T. maritima NusB, P21 (E_value = 6.1E_13);-53% similar to PDB:1TZU T. maritima NusB, P212121 (E_value = 6.1E_13);-53% similar to PDB:1TZV T. maritima NusB, P3121, Form 1 (E_value = 6.1E_13);-53% similar to PDB:1TZW T. maritima NusB, P3121, Form 2 (E_value = 6.1E_13);","Residues 5 to 140 (E_value = 1.1e-16) place ANA_0815 in the NusB family which is described as NusB family.","","antitermination factor NusB (nusB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0817","874274","873651","624","5.28","-5.35","22620","GTGGCGCCTCGCGGTAGGATCAGCGCGTCCCAGACGCAATGCAACAGTGAGGAAACCCTCGTGGCCACGACGAACGACCTGAAGAACGGCATGGTGCTCAACCTCGAGGGCCAGCTGTGGCAGGTAGTGGAGTTCCAGCACGTCAAGCCCGGCAAGGGCCCAGCTTTCGTGCGCACCAAGATCAAGAACGTCCTGTCCGGCAAGACCGTTGACAAGACCTTCAACGCCGGCCTCAAGGTTGAGACCGCCACCGTTGACCGGCGTGACATGCAGTACCTCTACAAGGACGGCGACGACTACGTCTTCATGGATGTCAAGTCCTACGAGCAGACCTACGTCCCCTCAGCCACCGTCGGCGACGCCGCCACCTTCATGCTGGAGAACCAGGAGGTCATCGTTGCCTTCCACGAGGACTCGGTGCTGTTCGTCGAGCTGCCGGCCTCCGTGGTCCTGACGATCTCCCACACCGAGCCGGGCCTGCAGGGCGACCGCTCCAGTGCCGGTACCAAGCCCGCCACGGTCGAAACCGGTGCTGAGATCCAGGTCCCGCTGTTCCTCAACACCGGTGACAAGGTCAAGGTCGACACCCGCTCCGGCTCCTACATCTCCCGCGTCAACGACTGA","VAPRGRISASQTQCNSEETLVATTNDLKNGMVLNLEGQLWQVVEFQHVKPGKGPAFVRTKIKNVLSGKTVDKTFNAGLKVETATVDRRDMQYLYKDGDDYVFMDVKSYEQTYVPSATVGDAATFMLENQEVIVAFHEDSVLFVELPASVVLTISHTEPGLQGDRSSAGTKPATVETGAEIQVPLFLNTGDKVKVDTRSGSYISRVND$","Translation elongation factor P","Cytoplasm, Periplasm","translation elongation factor P","translation elongation factor P","translation elongation factor P","","Nakagawa A., Nakashima T., Taniguchi M., Hosaka H., Kimura M., Tanaka I. The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome. EMBO J. 1999. 18(6):1459-1467. PMID: 10075918Kim K.K., Hung L.W., Yokota H., Kim R., Kim S.H. Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 A resolution. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(18):10419-10424. PMID: 9724718Peat T.S., Newman J., Waldo G.S., Berendzen J., Terwilliger T.C. Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution. Structure 1998. 6(9):1207-1214. PMID: 9753699","","","

InterPro
IPR001059
Domain

Translation elongation factor P/YeiP, central
PF01132	$\"[87-141]T$	EFP

InterPro
IPR011768
Family

Translation elongation factor P
PIRSF005901	$\"[21-206]T$	Translation elongation factor P
TIGR00038	$\"[21-207]T$	efp: translation elongation factor P

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[84-147]T$ $\"[148-205]T$	no description

InterPro
IPR013185
Domain

Translation elongation factor, KOW-like
PF08207	$\"[23-80]T$	EFP_N

InterPro
IPR013852
Domain

Translation elongation factor P/YeiP, C-terminal
PS01275	$\"[170-189]T$	EFP

InterPro
IPR014722
Domain

Translation protein SH3-like, subgroup
G3DSA:2.30.30.30	$\"[21-83]T$	no description

InterPro
IPR015365
Domain

Elongation factor P, C-terminal
PF09285	$\"[149-204]T$	Elong-fact-P_C

","BeTs to 23 clades of COG0231COG name: Translation elongation factor P/translation initiation factor eIF-5AFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0231 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001059 (Elongation factor P (EF-P)) with a combined E-value of 1.6e-87. IPB001059A 26-64 IPB001059B 71-110 IPB001059C 156-204","Residues 21-118 are 62% similar to a (ELONGATION FACTOR BIOSYNTHESIS EF-P P) protein domain (PDA0X3C0) which is seen in EFP1_PARUW.Residues 25-65 are 92% similar to a (ELONGATION FACTOR P EF-P BIOSYNTHESIS TRANSLATION SEQUENCING DIRECT PROBABLE EFP) protein domain (PD589283) which is seen in EFP_STRCO.Residues 74-124 are 80% similar to a (ELONGATION FACTOR P EF-P BIOSYNTHESIS TRANSLATION P-LIKE SEQUENCING DIRECT FAMILY) protein domain (PD002832) which is seen in EFP_MYCTU.Residues 127-204 are similar to a (ELONGATION FACTOR P EF-P BIOSYNTHESIS TRANSLATION P-LIKE AT4G26310 SEQUENCING DIRECT) protein domain (PD571341) which is seen in EFP_MYCPA.","","-69% similar to PDB:1YBY Conserved hypothetical protein Cth-95 from Clostridium thermocellum (E_value = 3.7E_54);-65% similar to PDB:1UEB Crystal structure of translation elongation factor P from Thermus thermophilus HB8 (E_value = 2.3E_40);","Residues 23 to 80 (E_value = 6.3e-36) place ANA_0817 in the EFP_N family which is described as Elongation factor P (EF-P) KOW-like domain.Residues 87 to 141 (E_value = 7e-26) place ANA_0817 in the EFP family which is described as Elongation factor P (EF-P) OB domain.Residues 149 to 204 (E_value = 3.6e-34) place ANA_0817 in the Elong-fact-P_C family which is described as Elongation factor P, C-terminal.","","elongation factor P (efp)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0818","874871","874305","567","6.63","-1.48","19667","TTGAGCGCCACGGCACCGGGTTCCCTCATCCTCATCGGCCCGCCCGGTGCCGGCTGCTCCAGCGTGGCCCGTGCCATCGGGAGTGCCCAGGGCCTTCCCGTGCTCGATCTGGGCCAGCTCGTCGCCGATGAGCTGGGAACTCGCCCCGAGCTGGCGCTCGTCGCGGTGGCGGAGACCGAGTACCGCCGCATCGAGGCCGGCACCGCTGAACGGCTCCTGGAGCGGGCCGAGACCGGGGGCCTCGTCGTCGCCCTGGGATCGGGCTGCCTGGAGGCCAGGGGAGTGCGTCAGGGCCTCGAGCGTCTCAGGCTCGCCGGCCGCAGTACTCACCACGTCGTGGCCCTGACCTGTGCTACCCGGGTCCTGGCCACTCGTAACGGTCTTGACGCGCCGCGGTCCGTGGCCCTGGGAACCGTCCATCACCAGTTCGTCCAGATGCTCCACGAGCGCCACACCCTGTGCCGGGACATGGCCGACGTCGTCATCGACACCACCGCGACGACCCCCGACGAGGCCGCTCAGAAGGTGATGAACGACATCGGCACCGATTTGTCCCGCCACTCGTGA","LSATAPGSLILIGPPGAGCSSVARAIGSAQGLPVLDLGQLVADELGTRPELALVAVAETEYRRIEAGTAERLLERAETGGLVVALGSGCLEARGVRQGLERLRLAGRSTHHVVALTCATRVLATRNGLDAPRSVALGTVHHQFVQMLHERHTLCRDMADVVIDTTATTPDEAAQKVMNDIGTDLSRHS$","Shikimate kinase","Cytoplasm, Membrane","putative shikimate kinase","shikimate 5-dehydrogenase ","shikimate kinase","","Griffin H.G., Gasson M.J. The gene (aroK) encoding shikimate kinase I from Escherichia coli. DNA Seq. 1995. 5(3):195-197. PMID: 7612934Matsuo Y., Nishikawa K. Protein structural similarities predicted by a sequence-structure compatibility method. Protein Sci. 1994. 3(11):2055-2063. PMID: 7703851Krell T., Coggins J.R., Lapthorn A.J. The three-dimensional structure of shikimate kinase. J. Mol. Biol. 1998. 278(5):983-997. PMID: 9600856","","","

InterPro
IPR000623
Domain

Shikimate kinase
PF01202	$\"[15-181]T$	SKI

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[5-180]T$	no description

","BeTs to 8 clades of COG0703COG name: Shikimate kinaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0703 is ------yqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 15 to 181 (E_value = 6.4e-06) place ANA_0818 in the SKI family which is described as Shikimate kinase.","","shikimate kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0819","876730","874868","1863","6.18","-6.93","64794","ATGACCTGGAAGCGTGTTCCGACCATCACTCTGCGTGATGACCAGCTGCCCCTGGTACTGGTGGGATTGCCCGGTGCGGGCAAGACCACTCAGGCCAGGCTTCTGGCTCAGGCTCTGGGCGTCCAGGTCACCGACACCGACGCCGAGATCCGCCGGCGAGCCCGCATGACGATCCCCGAGATCTTCGCCGCCGAAGGTGAGGAGTGCTTCCGTGACCGTGAGCACCGGGCCATGCGGGCCGTCTTGGACTCCCCGGCTGCGGCTCAGGGCGTCATTGCCCTGGGCGGGGGAGCGGTACTGCGTCCCGAGAACCGAGACCTGCTGCGCGGTCACACGGTCATCTACCTGTCCGCCTCCCCGAGCACTGCGGCCAAGCACGTGGGCGACGGGACCGGGCGGCCGGTCATGGCCCCGGACGCGGACTCCGACCAGACCCGCGCGGCTCAGCAGCGCACTGAGGAGCAGGGGGAGCACGCGGGCGTCCTGGCGCGCATGGAGGCCCTTTATGCTCAGCGCTCGCCGCTGTACTCCGAGGTCGCTACTCTCACTGTGCCCACCGATGGGCTCAGTCCCCAGCAGGTCGCTGCTCTCATCCTGGTGGCCCTGGGGGTCCAGACCGCTCAGGCGGTCAGTGTCCTGGCACCCATGGCCGAGGGGCAGTCGGACTCCGCCACTGTCCCGGACGGGGGCGACGCCTCGCCTCGGCGCGTCCGGCCCGCGGCAACCACGGAGGTTGGCAGCGGTGCACGGCGAGTCAGCGTCGCCGGCGAGCGCCCCTACGACGTCCTCATCGGCCACGGGATCCTGGCCGAGCTGCCCCGCATCGTGCAGGACGCCCCCGGAGCGGGTGCGGGAGGCGTGACGATCATCCACGCCAAGGCACTGGCCGACCGTGCCCGTGCTGCCGAGGCAGCGCTCACCAACGAAGGCCTGCGAGTCCTGAGCATCGAGGTCCCCAACGGAGAGGCTGCCAAGAAGGCGCGCGTCCTGGAGTATCTGTGGGACCGGCTTGGCTCCTTCCGCCTGGGTCGTGACGGACTCGTCGTCGGTCTCGGTGGCGGGGCGACGACGGACCTGGCAGGTCTCGCGGCTGCGACCTGGCTGCGAGGTGTTCCCGTGGTACAGGTGCCCACCACGCTGCTGGCCATGGTGGATGCCGCCGTCGGTGGCAAGACCGGAATCGACACGCCCGCTGGCAAGAACCTGGTGGGTGCCTTCCACCCGCCGGCCGCCGTCATCGCCGACCTGGAGACGCTCTCCACCCTCCCCGCCGCTGAGCTGCGGGCAGGACTTGGCGAGGTCATCAAGTGCGGCCTGATCGCCGACTCGGTCATTCTCGACCGGGTCCTGGCCGATCCTGCCGACTGCCTGACCTGGGACTCGCCAGTGCTGGCCGACCTGGTTGCCCGATCCGTCGCGGTCAAGGCCGCCGTCGTGGGGGAAGATCTCACCGAAGCCGGCCTGCGGGAGGTTCTCAACTACGGGCACACCTACGCCCACGCGATCGAGAAGGTCACCGGGTACTCCTGGCGTCACGGAGAGGCGGTCGCCGTCGGCTGCGTCTTCGCCGCCGAGATCGCCCACCGCAACGGCAATCTGAGCAGAGACGCGCTCGCCCTGCACCGTCAGAGCCTGGAAGCGGTCGGTCTGCCAACCCGCTTCCCCGAAGGGGAGGGGCGCTGGGAAGAGCTCAAGGAGGCCATGATGAGCGACAAGAAGGTACGCAGTGGGCGACTGCGCCTCGTCCTGCTCGACGACATCGCCAGGCCCGTGCGAGTTCAGGCACCGGCGGAGAGCGTTCTCCTATCGGCTCACGAGGCAGTCACCGGTGGGCCCAGCCCGGCAGAAGGGAACCGCGGTTGA","MTWKRVPTITLRDDQLPLVLVGLPGAGKTTQARLLAQALGVQVTDTDAEIRRRARMTIPEIFAAEGEECFRDREHRAMRAVLDSPAAAQGVIALGGGAVLRPENRDLLRGHTVIYLSASPSTAAKHVGDGTGRPVMAPDADSDQTRAAQQRTEEQGEHAGVLARMEALYAQRSPLYSEVATLTVPTDGLSPQQVAALILVALGVQTAQAVSVLAPMAEGQSDSATVPDGGDASPRRVRPAATTEVGSGARRVSVAGERPYDVLIGHGILAELPRIVQDAPGAGAGGVTIIHAKALADRARAAEAALTNEGLRVLSIEVPNGEAAKKARVLEYLWDRLGSFRLGRDGLVVGLGGGATTDLAGLAAATWLRGVPVVQVPTTLLAMVDAAVGGKTGIDTPAGKNLVGAFHPPAAVIADLETLSTLPAAELRAGLGEVIKCGLIADSVILDRVLADPADCLTWDSPVLADLVARSVAVKAAVVGEDLTEAGLREVLNYGHTYAHAIEKVTGYSWRHGEAVAVGCVFAAEIAHRNGNLSRDALALHRQSLEAVGLPTRFPEGEGRWEELKEAMMSDKKVRSGRLRLVLLDDIARPVRVQAPAESVLLSAHEAVTGGPSPAEGNRG$","3-dehydroquinate synthase","Cytoplasm","shikimate kinase/3-dehydroquinate synthase","3-dehydroquinate synthase ","3-dehydroquinate synthase","","Hawkins A.R., Lamb H.K. The molecular biology of multidomain proteins. Selected examples. Eur. J. Biochem. 1995. 232(1):7-18. PMID: 7556173Barten R., Meyer T.F. Cloning and characterisation of the Neisseria gonorrhoeae aroB gene. Mol. Gen. Genet. 1998. 258(1):34-44. PMID: 9613570","","","

InterPro
IPR000623
Domain

Shikimate kinase
PR01100	$\"[18-33]T$ $\"[42-55]T$ $\"[70-78]T$ $\"[91-100]T$ $\"[111-128]T$	SHIKIMTKNASE
PF01202	$\"[24-203]T$	SKI
PS01128	$\"[71-99]?$	SHIKIMATE_KINASE

InterPro
IPR002658
Domain

3-dehydroquinate synthase AroB
PF01761	$\"[264-575]T$	DHQ_synthase
TIGR01357	$\"[260-605]T$	aroB: 3-dehydroquinate synthase

noIPR
unintegrated

unintegrated
G3DSA:1.20.1090.10	$\"[422-595]T$	no description
G3DSA:3.40.50.1970	$\"[246-421]T$	no description
G3DSA:3.40.50.300	$\"[17-212]T$	no description
PTHR21090	$\"[301-611]T$	AROM/DEHYDROQUINATE SYNTHASE
PTHR21090:SF1	$\"[301-611]T$	3-DEHYDROQUINATE SYNTHASE

","BeTs to 18 clades of COG0337COG name: 3-dehydroquinate synthetaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0337 is ---pkzy-vdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB002658 (3-dehydroquinate synthase domain) with a combined E-value of 1e-75. IPB002658A 374-426 IPB002658B 475-503 IPB002658C 512-531 IPB002658D 571-590***** IPB000623 (Shikimate kinase family signature) with a combined E-value of 1.5e-14. IPB000623A 18-33 IPB000623C 70-78 IPB000623D 91-100 IPB000623E 111-128***** IPB000850 (Adenylate kinase) with a combined E-value of 5.7e-07. IPB000850A 18-47","Residues 26-202 are 52% similar to a (KINASE SHIKIMATE TRANSFERASE ACID AMINO ATP-BINDING AROMATIC BIOSYNTHESIS SK I) protein domain (PD004326) which is seen in Q741J8_MYCPA.Residues 367-568 are 73% similar to a (SYNTHASE 3-DEHYDROQUINATE LYASE AMINO AROMATIC BIOSYNTHESIS ACID NAD SHIKIMATE AROM) protein domain (PD194122) which is seen in Q6NH04_CORDI.","","-45% similar to PDB:1UJN Crystal structure of dehydroquinate synthase from Thermus thermophilus HB8 (E_value = 2.6E_32);-49% similar to PDB:1DQS CRYSTAL STRUCTURE OF DEHYDROQUINATE SYNTHASE (DHQS) COMPLEXED WITH CARBAPHOSPHONATE, NAD+ AND ZN2+ (E_value = 2.8E_31);-49% similar to PDB:1NR5 Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, NAD and carbaphosphonate (E_value = 2.8E_31);-49% similar to PDB:1NRX Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+ and NAD (E_value = 2.8E_31);-49% similar to PDB:1NUA Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+ (E_value = 2.8E_31);","Residues 24 to 203 (E_value = 4.8e-50) place ANA_0819 in the SKI family which is described as Shikimate kinase.Residues 264 to 575 (E_value = 5.3e-137) place ANA_0819 in the DHQ_synthase family which is described as 3-dehydroquinate synthase.","","kinase-3-dehydroquinate synthase (aroKB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0820","878039","876807","1233","7.02","0.10","43145","ATGCTTCGATGGATGACGGCCGGGGAATCCCACGGCGAGGCTCTGACCGCGGTGCTGGAAGGCGTGCCCGCGGGCGTTCGGATCACCAGTGAGGACATCCGGGCGGCACTGGCCCGGCGGCGACTGGGGCACGGGCGTGGTGCCCGCCAGGCCTTCGAGCGCGACGAGCTGCGGGTATTGGGGGGCATCCGCCACGGAAGCACCATCGGCAGCCCCATCGCCCTGCAGATCGGCAACTCCGAGTGGCCCAAGTGGTCCACGGTGATGAGCGCCGACCCCGTGGACCCCCACGACCTGCTCATCGACGCCGGCACCGGTGACGAGCGCGAGATCGCCCGTAACCGCCCGCTGACCCGCCCCAGGCCCGGGCACGCGGACCTGCCGGGGATGCTCAAGTACGACCTGCCCGAGGCTCGCCCGGTCCTGGAACGGGCCTCAGCCCGCGAGACCGCCGCCCGGGTGGCGCTGGGGGCCGTGGCCGAGGCTATTTTGGAGCAGGTAGCCGGTGTCAGGTTGGTCAGCCACGTCGTGCGGATCGGATCAGTCGCCCTGCCCGATGACGTACCCCCGCCCAGCGCTGAGGACACCTCGCGCCTGGACGCCGACCCCGTGCGCTGCACGGATCCTGCCACCAGTGCCGCCATGGTTGCCCAGATCGATGCCACCAGGAAGGACGGTGACACGCTCGGGGGCGTTGTTGAGGTCATCGCCACCGGTGTCCCGGTGGGACTGGGCACCCATGTCAGCGCCGACCGCCGCTTGGACGCGCGCCTGGCGGCCGCGCTCATGGGGATCCAGGCCGTCAAGGGCGTGGAGATCGGTGACGGCTTCGCCGAGGCGGCCCGGCGGGGCTCGGCCGCCCACGACGAGATCATCTCAGTGAACTGCGGAACGCTCACCCGGACCACCAACCGCGCCGGTGGCATCGAGGGCGGAATCTCCAACGGCTCCGCTGTGCGGGTACGGGCCGGCTTCAAGCCGATCTCCACGGTGCCCAGGGCCCTGCGCACCGTCGACCTGGCCACGGGCGAGCCCGCCACCGGGCTGCACCAGCGCTCTGACGTGTGTGCCGTCGTTCCCGGAGCGGTCATTGCTCAGGCCATGACCGCTCTGGTCCTGGCCGACCTGTTACTGGACAAGACCGGAGGCGACTCGGCCGATGAGGCTCGACGCAACCTGCGCTCCTACCTGACCCGCATTGCTGAACGGACGCAGTGGCGAACCGAGCGGTGA","MLRWMTAGESHGEALTAVLEGVPAGVRITSEDIRAALARRRLGHGRGARQAFERDELRVLGGIRHGSTIGSPIALQIGNSEWPKWSTVMSADPVDPHDLLIDAGTGDEREIARNRPLTRPRPGHADLPGMLKYDLPEARPVLERASARETAARVALGAVAEAILEQVAGVRLVSHVVRIGSVALPDDVPPPSAEDTSRLDADPVRCTDPATSAAMVAQIDATRKDGDTLGGVVEVIATGVPVGLGTHVSADRRLDARLAAALMGIQAVKGVEIGDGFAEAARRGSAAHDEIISVNCGTLTRTTNRAGGIEGGISNGSAVRVRAGFKPISTVPRALRTVDLATGEPATGLHQRSDVCAVVPGAVIAQAMTALVLADLLLDKTGGDSADEARRNLRSYLTRIAERTQWRTER$","Chorismate synthase","Cytoplasm","chorismate synthase","chorismate synthase ","Chorismate synthase","","Schaller A., Schmid J., Leibinger U., Amrhein N. Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers. J. Biol. Chem. 1991. 266(32):21434-21438. PMID: 1718979Jones D.G., Reusser U., Braus G.H. Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae. Mol. Microbiol. 1991. 5(9):2143-2152. PMID: 1837329","","","

InterPro
IPR000453
Family

Chorismate synthase
PD002941	$\"[52-371]T$	AROC_MYCTU_P95013;
PTHR21085	$\"[1-410]T$	CHORISMATE SYNTHASE
PF01264	$\"[2-381]T$	Chorismate_synt
TIGR00033	$\"[2-384]T$	aroC: chorismate synthase
PS00787	$\"[8-23]T$	CHORISMATE_SYNTHASE_1
PS00788	$\"[143-159]T$	CHORISMATE_SYNTHASE_2

","BeTs to 23 clades of COG0082COG name: Chorismate synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0082 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB000453 (Chorismate synthase) with a combined E-value of 1e-117. IPB000453A 2-43 IPB000453B 121-159 IPB000453C 226-248 IPB000453D 251-289 IPB000453E 303-339 IPB000453F 351-378","Residues 52-371 are 75% similar to a (BIOSYNTHESIS LYASE CHORISMATE AROMATIC ACID AMINO SYNTHASE AMINO-ACID PHOSPHOLYASE 5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE) protein domain (PD002941) which is seen in AROC_MYCTU.","","-67% similar to PDB:1ZTB Crystal Structure of Chorismate Synthase from Mycobacterium tuberculosis (E_value = 3.4E_120);-67% similar to PDB:2G85 Crystal structure of chorismate synthase from Mycobacterium tuberculosis at 2.22 angstrons of resolution (E_value = 3.4E_120);-51% similar to PDB:1Q1L Crystal Structure of Chorismate Synthase (E_value = 5.8E_67);-51% similar to PDB:1QXO Crystal structure of Chorismate synthase complexed with oxidized FMN and EPSP (E_value = 1.9E_62);-44% similar to PDB:1R52 Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae (E_value = 2.0E_35);","Residues 2 to 381 (E_value = 1.3e-164) place ANA_0820 in the Chorismate_synt family which is described as Chorismate synthase.","","synthase (aroC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0821","879078","878116","963","6.73","-1.16","33070","GTGATACGCCACCGCGCTGCCGTCATCGGTCGGCCGGTGAGCCACTCACTGTCTCCCGTGCTGCACCGGGCCGCCTACGCCGGGCTGGGGCTGGAGGACTGGTCCTATGAGCGGCGTGAGACGGACTCCGAATCCCTGCCGGGCCTGCTCGCCGAGCTGGCCGCTCCGGTTCAGGCCGGACCCGCCTGGGCGGGTCTGAGCGTCACCATGCCTCTCAAGCAGGTTCTCCTGGCGCACCTGGACGTCATCGATCCTCTCGCTGAGGCTGTCGGTGCCGTCAACACCGTGGTGGCACAGCGCAGCGGAGCAGGAGATGCGCTCCTGACCGGCTTCAACACCGACGTCGCAGGCATTGTCGGTGCACTAAGGGAGGCCGCCCGCACCCAGACACCGGGCTCCTCGGATGCTCAACTCCGGATCGAGCAGGCCGTGGTGCTCGGTTCGGGCGCCACCGCCTGCTCCGCCCTCGCGGCGCTCGGAGAGCTCCGGGCCGGCCGGATCACCGTCGTGGCTCGGCGTCACGCCGGCCCCGGCCGCGCACTCAGCGCCGCCCACCGTATGGGGCTGGATATCGAGCCCTTCACCTGGAAGCCGGCTGACTCGACCTCCAACACCGAGGCGGCCCAGCGCCTGGCCGCAGCCGATGTCGTCATCTCGACTCTGCCCGCGCATGCGGCCGATCCGTTGGAGGGCCCGCTCAGGCAGGCCCTGGCCCGGGCCGAGGGCACCCGAGCAGGAGCCGTGATGCTCGACGTCGTCTACGCCCCTTGGCCCACTGCCGTCGCCGGTGCTTGGGCGGACGCCGGGGGAGCCCTCGCCCCGGGCTGGCTGATGCTCCTGCACCAGGCAGTGCCCCAGGTGCAGCTCATGACCGGGCGGCAGCCAGACATCGAGTGCATGCGTACAGCGCTGCGCTCGGCGCTGGCCCCGCCCTCAACAACTCCGGTTCGCACCAACGACTGA","VIRHRAAVIGRPVSHSLSPVLHRAAYAGLGLEDWSYERRETDSESLPGLLAELAAPVQAGPAWAGLSVTMPLKQVLLAHLDVIDPLAEAVGAVNTVVAQRSGAGDALLTGFNTDVAGIVGALREAARTQTPGSSDAQLRIEQAVVLGSGATACSALAALGELRAGRITVVARRHAGPGRALSAAHRMGLDIEPFTWKPADSTSNTEAAQRLAAADVVISTLPAHAADPLEGPLRQALARAEGTRAGAVMLDVVYAPWPTAVAGAWADAGGALAPGWLMLLHQAVPQVQLMTGRQPDIECMRTALRSALAPPSTTPVRTND$","Shikimate 5-dehydrogenase","Cytoplasm, Membrane","shikimate 5-dehydrogenase","shikimate 5-dehydrogenase ","Shikimate dehydrogenase substrate binding, N-terminal domain protein","","Singh S., Korolev S., Koroleva O., Zarembinski T., Collart F., Joachimiak A., Christendat D. Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae. J. Biol. Chem. 2005. 280(17):17101-17108. PMID: 15735308","","","

InterPro
IPR006151
Domain

Shikimate/quinate 5-dehydrogenase
PF01488	$\"[114-262]T$	Shikimate_DH

InterPro
IPR013708
Domain

Shikimate dehydrogenase substrate binding, N-terminal
PF08501	$\"[8-96]T$	Shikimate_dh_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.192.10	$\"[3-124]T$	no description
PTHR21089	$\"[246-313]T$	SHIKIMATE DEHYDROGENASE

","BeTs to 23 clades of COG0169COG name: Shikimate 5-dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0169 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB006151 (Shikimate/quinate 5-dehydrogenase) with a combined E-value of 1.5e-32. IPB006151A 8-31 IPB006151B 65-91 IPB006151C 106-117 IPB006151E 251-269 IPB006151F 274-292","Residues 7-97 are 70% similar to a (SHIKIMATE OXIDOREDUCTASE 5-DEHYDROGENASE DEHYDROGENASE BIOSYNTHESIS AMINO AROMATIC ACID NADP 3-DEHYDROQUINATE) protein domain (PD120824) which is seen in Q827S1_STRAW.","","-42% similar to PDB:1WXD Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 (E_value = 1.3E_23);-42% similar to PDB:2CY0 Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with NADP (E_value = 1.3E_23);-42% similar to PDB:2D5C Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with shikimate (E_value = 1.3E_23);-42% similar to PDB:2EV9 Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with NADP(H) and shikimate (E_value = 1.3E_23);-42% similar to PDB:1NPD X-RAY STRUCTURE OF SHIKIMATE DEHYDROGENASE COMPLEXED WITH NAD+ FROM E.COLI (YDIB) NORTHEAST STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NESG) TARGET ER24 (E_value = 1.7E_15);","Residues 8 to 96 (E_value = 1.1e-30) place ANA_0821 in the Shikimate_dh_N family which is described as Shikimate dehydrogenase substrate binding domain.Residues 114 to 262 (E_value = 5e-05) place ANA_0821 in the Shikimate_DH family which is described as Shikimate / quinate 5-dehydrogenase.","","5-dehydrogenase (aroE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0822","880212","879091","1122","7.89","2.12","40222","ATGGAGAAGGTTGAGCGCCGTCAGCGCAAGCGGCGCCGGCACTGGCTGACGAGTCTTGTCATCGTCATCACCCTCGTGGCTGTCGGCGTCCTGGGCTACAAGGCCATCGGGATCATGCGCGACGCCTCCGCACAGGCGACTCACGCCGAGGACTACAAGGGCGAGGGTGAGGGCGAGGTCACCGTGACGATCCCGGAGGGGGCCTCTGGGGCGGACATCGGCGACATCCTGCAGAGCAAAGGCGTCGTCGCCTCCGGCAAGGCCTTCACCAATGCGGCGAAGAACAACCCCAAGGGAACGACGATCCAGCCGGGAACCTATAAGCTCAAGAAGAAGATGTCGGCCAGCTCTGCGCTCCAGGCACTGCTTGATCCTGAGAGCAAGGGCGATCACACGCTGACCGTCATTGCCGGCTCCACCAAGCAGAGCGTCAAGGAGCGGCTCAAGAAGGTCGGAAACTTCACCGATGAGCAGGTCGAGGCGGCGTACGCCGACTCTGCGGCCATCGGCCTGCCCGCCGAGGCCGGCGGCAACGTCGAGGGATGGCTCGCTCCGGGCACCTACGACGTCGCCGAGAACGCCACGCCGAAGGACCTGGTCAAGAAGATGGTCTCCCAGACCGTCACCCGGCTCAAAGAGCTCAAGGTACCCAAGGAGGACTACCAGAAGGTTCTGATCAAGGCCTCCATCGTCGAACGAGAGGTGAACAAGGAGCAGTACTACGGGCAGGTCGCCCGGGTCATCGAGAACCGCCTGACGCAGACTGACGGGGAGACCCACGGTCTGCTCCAGATGGACTCGACAGTGCAGTACGGCCTGGGCCGTGACGGTGGCATCCCCTCCGAGGCGGAGAATCAGGACGCCAGCAACCCGTACAACACCTACGTTCACCAGGGGCTCCCGCCAGGTCCGATCGGCAATCCCGATGAAGCGGCCATCAAGGCGGTGCTCAACCCGCCGGCGGGGAGCTGGCTCTACTTCGTCACGGTCAACCTCAAGACCGGCGAGACTCTGTTCGCCTCCACCAATGAGGAGCAGAAGGCCAACACCAAGAAGCTCTCCGACTACTGCAACAAGAACAAGGACGTCTGCGAGGGCAACGAGAGCAAGAAGAATGGCTGA","MEKVERRQRKRRRHWLTSLVIVITLVAVGVLGYKAIGIMRDASAQATHAEDYKGEGEGEVTVTIPEGASGADIGDILQSKGVVASGKAFTNAAKNNPKGTTIQPGTYKLKKKMSASSALQALLDPESKGDHTLTVIAGSTKQSVKERLKKVGNFTDEQVEAAYADSAAIGLPAEAGGNVEGWLAPGTYDVAENATPKDLVKKMVSQTVTRLKELKVPKEDYQKVLIKASIVEREVNKEQYYGQVARVIENRLTQTDGETHGLLQMDSTVQYGLGRDGGIPSEAENQDASNPYNTYVHQGLPPGPIGNPDEAAIKAVLNPPAGSWLYFVTVNLKTGETLFASTNEEQKANTKKLSDYCNKNKDVCEGNESKKNG$","Aminodeoxychorismate lyase","Extracellular, Periplasm","NovB","aminodeoxychorismate lyase","aminodeoxychorismate lyase","","Jhee K.H., Yoshimura T., Miles E.W., Takeda S., Miyahara I., Hirotsu K., Soda K., Kawata Y., Esaki N. Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry. J. Biochem. 2000. 128(4):679-686. PMID: 11011151","","","

InterPro
IPR003770
Family

Aminodeoxychorismate lyase
PF02618	$\"[60-354]T$	ADC_lyase

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[15-33]?$	transmembrane_regions

","BeTs to 14 clades of COG1559COG name: Predicted periplasmic solute-binding proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1559 is -------q-drlb-efghsnujx-t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 16-107 are 51% similar to a () protein domain (PD817570) which is seen in Q8G5X1_BIFLO.Residues 18-127 are 64% similar to a (MEMBRANE LYASE AMINODEOXYCHORISMATE PROBABLE SECRETED SOLUTE-BINDING PERIPLASMIC PROTEIN PREDICTED LYASE-LIKE) protein domain (PD669127) which is seen in Q8NQ24_CORGL.Residues 171-295 are 61% similar to a (LYASE AMINODEOXYCHORISMATE KINASE PERIPLASMIC SOLUTE-BINDING EXPORTED MEMBRANE YCEG PREDICTED 4.-.-.-) protein domain (PD686410) which is seen in Q8G5X1_BIFLO.Residues 299-353 are 70% similar to a (LYASE AMINODEOXYCHORISMATE KINASE PERIPLASMIC SOLUTE-BINDING EXPORTED MEMBRANE YCEG PREDICTED 4.-.-.-) protein domain (PD009996) which is seen in Q8G5X1_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 60 to 354 (E_value = 2e-68) place ANA_0822 in the ADC_lyase family which is described as Aminodeoxychorismate lyase.","","(fragment) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0823","880820","880305","516","8.05","1.86","18573","GTGACAGACTCATCGACTCAACCGGACTCGATGGATGTCCGCCCTGGCGTGCGCATCGCCTTCGATGTCGGACAGGCACGTATTGGTGTCGCTCGTTGCGATCAGGACGCGATCCTGTCGTTTCCTGTGGTAACTCTCAGGCGGGACCGCTATGGTGCAGACCTCGACGAGGCCGTTGACCTTGTCGAGGAGTACGGTGCCTTTGAGGTGATCGTCGGCTTGCCCAAGCACATGGGTGGTGGCAGCTCGAGCTCGACCAAGGACGCCCGAGCGTGGGCGCGAGATCTGGCGAGCCGCCTGCCACGGCGGGTGTGCGTCCGGCTGGTAGACGAGCGGCTCACCACCGTCTCCGCTCACCGGGATCTGCATGCGGCTGGCCTGAAGGAGAGGAGCTTCCGCGGTATCGTCGACCAAGCGGCGGCGGTCGTCATCCTCGAACAGGCCATCACAACTGAGCGGATGTCCGGGGTTCCGGCCGGTGAGCGAGTCCACCCGATCAAGAGAGGCAGAGCGTGA","VTDSSTQPDSMDVRPGVRIAFDVGQARIGVARCDQDAILSFPVVTLRRDRYGADLDEAVDLVEEYGAFEVIVGLPKHMGGGSSSSTKDARAWARDLASRLPRRVCVRLVDERLTTVSAHRDLHAAGLKERSFRGIVDQAAAVVILEQAITTERMSGVPAGERVHPIKRGRA$","Holliday junction resolvase YqgF","Cytoplasm","3.1.-.-","putative Holliday junction resolvase ","Holliday junction resolvase YqgF","","Aravind L., Makarova K.S., Koonin E.V. SURVEY AND SUMMARY: holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res 2000. 28(18):3417-3432. PMID: 10982859Mahdi A.A., Sharples G.J., Mandal T.N., Lloyd R.G. Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82. J. Mol. Biol. 1996. 257(3):561-573. PMID: 8648624Kaplan C.D., Laprade L., Winston F. Transcription elongation factors repress transcription initiation from cryptic sites. Science 2003. 301(5636):1096-1099. PMID: 12934008","","","

InterPro
IPR005227
Family

Resolvase, holliday junction-type, YqgF-like
PF03652	$\"[16-151]T$	UPF0081
TIGR00250	$\"[19-150]T$	TIGR00250: conserved hypothetical protein T

InterPro
IPR006641
Domain

Resolvase, RNase H-like fold
SM00732	$\"[16-118]T$	YqgFc

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.140	$\"[14-163]T$	no description

","BeTs to 16 clades of COG0816COG name: Predicted endonuclease involved in recombination (possible Holliday junction resolvase in Mycoplasmas and B. subtilis)Functional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0816 is -------qvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 1","***** IPB005227 (Conserved hypothetical protein 250) with a combined E-value of 4.1e-19. IPB005227A 19-31 IPB005227B 70-81 IPB005227C 94-118 IPB005227D 137-150","Residues 18-115 are 61% similar to a (DNA JUNCTION RESOLVASE RECOMBINATION HOLLIDAY 3.1.-.- HYDROLASE REPAIR NUCLEASE ENDONUCLEASE) protein domain (PD219509) which is seen in Q741L2_MYCPA.","","-50% similar to PDB:1NMN Structure of yqgF from Escherichia coli, a hypothetical protein (E_value = 1.0E_10);-50% similar to PDB:1OVQ Solution structure of the hypothetical protein YqgF from Escherichia coli (E_value = 1.0E_10);-50% similar to PDB:1NU0 Structure of the double mutant (L6M; F134M, SeMet form) of yqgF from Escherichia coli, a hypothetical protein (E_value = 1.4E_10);","Residues 16 to 151 (E_value = 9.2e-37) place ANA_0823 in the UPF0081 family which is described as Uncharacterised protein family (UPF0081).",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0824","883572","880861","2712","5.17","-31.61","96600","ATGCGCACATCCGAGATCCGCAGCCGCTGGCTGGACTACTTCGCCGCGAACGAGCACGAGATCCGGCCCTCGGTCTCCCTGGTGTCGCCCGAGCCCTCCATCCTGTTCACCGTGGCGGGCATGGTTCCCTTCATCCCCTACATCCTGGGGACCGAGGAGGCCCCCTGGCCCCGGGCCGCCTCGGTGCAGAAGTGCATCCGCACCAATGACATCGACAACGTCGGTATCACGACGCGCCACGGCACCTTCTTCCAGATGAACGGCAACTTCTCCTTCGGCGACTACTTCAAGGAGGGGGCCATCTCCTACGCCTGGGGCCTGCTGACAGGCAGCCGGGAGGAGGGCGGCTACGGCCTGGACGGGGACCGGCTGTGGATGACGATCTGGGAGGAGGACCAGGTCTCCTTCGACTACTGGACCCGTGAGATCGGGGTGCCTGCAGAGCGGATCCAGCTCCTTCCCTTCAAGGACATCTCCTGGTCCACGGGCCAGCCCGGCCCTGCCGGATCCTGCTGCGAGATCCACTACGACCGCGGCCCCGCCTACGGGCCCGACGGCGGTCCCGCCGTCGACACCCAGGGCGACCGCTTCCTGGAGATCTGGAACCTCGTCTTCGACGAGTTCCTGCGCGGAGAGGGCAAGGGCCACGACTTCGAACTCCTGGGCAAGCTCGACCAGACGGCCATCGATACCGGTGCCGGTCTGGAGCGCCTGGCCTTCATCATGCAGGACAAGCCCAACATGTACGAGATCGACGAGGTCTTCCCTGTCATCAAGGCCGCCGAGGAACTGTCCGGAAAGGTCTACGGCCGCGGCTCGGCCGGCCCCGAGGCGGGCGAGGCCTACCACGATGACGTGCGCATGCGGGTCGTCGCCGACCACGTGCGCTCGGCCCTCATGCTCATCTCCGATGGCGTACGTCCCGGCAACGACGGCCGCGGCTACGTCCTGCGCCGCCTCATCCGCAGGGCGGTGCGCTCCATGCGCCTGCTCGGCGTCGACGAGGCCGCCATGCCCACGCTGCTGACCGTCTCGAAGGACGCCATGAAGTCCTCCTACCCTGAGCTGGAGACCGGCTGGAGCACCATCTCCGAGGTGGCCTACGGCGAGGAGGACGCCTTCCGCCGCACCCTGGCCGCCGGCACCACGATCCTGGACACCGCGGTGGCCTCGGCCAAGAAGGAGGCGGGCAGCTCCGGGCGCCCGCTGGTGTCGGGCAAGAGCGCCTTCGAGCTGCACGACACCTACGGCTTCCCCATCGACCTGACCCTCGAGATGGCGGCCGAGCAGGGGGTCGATGTCGATGAGAGCGCCTTCCGCAGCCTCATGAACGAGCAGAAGGAGCGCGCTCGAGCTGACGCGCGCGCCAAGAAGACCGGGCACGCCGACATCCGTGTCTTCCGCGAGCTGGAGAAGGAGATGGGCGGTGGCTCTACCTTCCTGGGCTACACCGAGTCCTCCGCCGATGCCACCGTCACCGGGATCCTCGTCGATGGCGTCCCGCAGAGTGTCGTCACCGCCCCGGCCGAGGTCGAGGTCGTCCTGGACCGGACTCCGTTCTGGGCCGAGATGGGTGGCCAGCTCGCCGACCAGGGCACGATCCGCCTGGCTGACGGCGGCACCGTCGAGGTCGATGACGTCCAGGCCCCCGTCAAGGGGCTGCACGTTCACCGCGGCACCCTGACCGAGGGCACGATCGCAGTTGGGGAGAAGGCCTTCGCCCAGATCGACTCGGCGCGCCGCCTGGCGATCGCCCGAGCCCACACCTCCACCCACATGGTGCACAAGGCGCTGCACGAGATCGTCTCGGACAACGCCACCCAGGCCGGCAGCGAGAACTCGCCCTCCCGTATGCGTTTCGACTTCCGCCACGGCTCCGCCCTGGCCTCGGACCAGATCTCCGGCATTGAAGAGCGGGTCAACGCCAGGCTCTCGGAGGACCTGGCCGTCACCGACGAGATCATGGACATCGACGCAGCCCGAGCCGCCGGCGCCATGGCTCTGTTCGGGGAGAAGTACGGCAAGGAGGTGCGCGTCGTTTCCATCGGGGGTGACTGGTCCAAGGAGCTGTGCGCCGGTACCCACGTTCCCAGCACCGGCCACATCGGCCGCATCGCGGTGCTGGGCGAGTCCTCGATCGGTTCGGGCGTGCGCCGCATCGACGCCCTCGTCGGTGAGGGCGCCTACGGCTACCAGGCCAAGGAGCACGCGCTGGTCTCCCAGCTCTCCACCATGGTCGGGGGCCGCCCCGAGGACCTGCCCGAGCGGGTCGAGAGCCTCATGGCGCGACTGAAGGACGCCGAGAAGCGCCTGGCCGCCGCCGAGCAGGCGGCGCTGTCCGCGCGCACGGCCGGAATCGTCTCCGACGCCGTCCGGCTGGGTGAGATCCGTCTCGCCTCAGCCGACCTCGGAACCGTCGGCTCGGCCGACGCCGTACGCTCGCTGGTCCTCGACGCTCGCAGCCGGCTCGGTGAGGCAGAACCGGCAGTCGTCGCTGTCGGCGCGGTCGTGGGCTCGCGTCCGGTCGTGGTCGTGGCCACCAATGCCGGTGCACGTGACCAGGGCATCCGGGCCGGCGCCCTGGTGCGCACCGCCGCTCAGGTGCTGGGCGGCGGTGGCGGCGGCAAGGACGATCTGGCTCAGGGCGGCGGTCAGAACCCTCAGGCTCTGGACGAGGCTCTGCGCGCCGTCGCCGGGCAGATCCAGGCCTGA","MRTSEIRSRWLDYFAANEHEIRPSVSLVSPEPSILFTVAGMVPFIPYILGTEEAPWPRAASVQKCIRTNDIDNVGITTRHGTFFQMNGNFSFGDYFKEGAISYAWGLLTGSREEGGYGLDGDRLWMTIWEEDQVSFDYWTREIGVPAERIQLLPFKDISWSTGQPGPAGSCCEIHYDRGPAYGPDGGPAVDTQGDRFLEIWNLVFDEFLRGEGKGHDFELLGKLDQTAIDTGAGLERLAFIMQDKPNMYEIDEVFPVIKAAEELSGKVYGRGSAGPEAGEAYHDDVRMRVVADHVRSALMLISDGVRPGNDGRGYVLRRLIRRAVRSMRLLGVDEAAMPTLLTVSKDAMKSSYPELETGWSTISEVAYGEEDAFRRTLAAGTTILDTAVASAKKEAGSSGRPLVSGKSAFELHDTYGFPIDLTLEMAAEQGVDVDESAFRSLMNEQKERARADARAKKTGHADIRVFRELEKEMGGGSTFLGYTESSADATVTGILVDGVPQSVVTAPAEVEVVLDRTPFWAEMGGQLADQGTIRLADGGTVEVDDVQAPVKGLHVHRGTLTEGTIAVGEKAFAQIDSARRLAIARAHTSTHMVHKALHEIVSDNATQAGSENSPSRMRFDFRHGSALASDQISGIEERVNARLSEDLAVTDEIMDIDAARAAGAMALFGEKYGKEVRVVSIGGDWSKELCAGTHVPSTGHIGRIAVLGESSIGSGVRRIDALVGEGAYGYQAKEHALVSQLSTMVGGRPEDLPERVESLMARLKDAEKRLAAAEQAALSARTAGIVSDAVRLGEIRLASADLGTVGSADAVRSLVLDARSRLGEAEPAVVAVGAVVGSRPVVVVATNAGARDQGIRAGALVRTAAQVLGGGGGGKDDLAQGGGQNPQALDEALRAVAGQIQA$","Alanyl-tRNA synthetase","Cytoplasm","alanyl-tRNA synthetase","alanyl-tRNA synthetase ","alanyl-tRNA synthetase","","Sankaranarayanan R., Dock-Bregeon A.C., Romby P., Caillet J., Springer M., Rees B., Ehresmann C., Ehresmann B., Moras D. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 1999. 97(3):371-381. PMID: 10319817","","","

InterPro
IPR002318
Family

Alanyl-tRNA synthetase, class IIc
PR00980	$\"[69-80]T$ $\"[198-209]T$ $\"[230-243]T$ $\"[289-305]T$ $\"[313-326]T$	TRNASYNTHALA
PF01411	$\"[5-580]T$	tRNA-synt_2c
TIGR00344	$\"[5-884]T$	alaS: alanyl-tRNA synthetase
PS50860	$\"[1-734]T$	AA_TRNA_LIGASE_II_ALA

InterPro
IPR003156
Domain

Phosphoesterase, DHHA1
PF02272	$\"[826-899]T$	DHHA1

InterPro
IPR012947
Domain

Threonyl/alanyl tRNA synthetase, SAD
PF07973	$\"[677-721]T$	tRNA_SAD

InterPro
IPR013222
Domain

Glycosyl hydrolase family 98, putative carbohydrate-binding module
SM00776	$\"[644-800]T$	no description

InterPro
IPR013983
Domain

Aldehyde ferredoxin oxidoreductase, N-terminal
SM00790	$\"[646-821]T$	no description

noIPR
unintegrated

unintegrated
PTHR11777	$\"[33-903]T$	ALANYL-TRNA SYNTHETASE
signalp	$\"[1-3]?$	signal-peptide

","BeTs to 26 clades of COG0013COG name: Alanyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0013 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB003156 (Phosphoesterase, DHHA1) with a combined E-value of 1.1e-162. IPB003156A 30-50 IPB003156B 67-105 IPB003156C 162-178 IPB003156D 196-210 IPB003156E 229-243 IPB003156F 291-327 IPB003156G 409-423 IPB003156H 518-532 IPB003156I 576-613 IPB003156J 664-680 IPB003156K 687-721***** IPB002318 (Alanyl-tRNA synthetase signature) with a combined E-value of 2.9e-38. IPB002318A 69-80 IPB002318B 198-209 IPB002318C 230-243 IPB002318D 289-305 IPB002318E 313-326","Residues 5-44 are 77% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA ALANINE--TRNA ALARS BIOSYNTHESIS ATP-BINDING ZINC ZINC-FINGER) protein domain (PD656708) which is seen in Q6AFA1_BBBBB.Residues 46-85 are 85% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA ALANINE--TRNA ALARS BIOSYNTHESIS ATP-BINDING ZINC ZINC-FINGER) protein domain (PD541107) which is seen in Q6A8I8_PROAC.Residues 86-308 are 69% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA ALANINE--TRNA ALARS BIOSYNTHESIS ATP-BINDING ZINC ZINC-FINGER) protein domain (PD002561) which is seen in SYA_COREF.Residues 257-423 are 76% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA ALANINE--TRNA ALARS BIOSYNTHESIS ATP-BINDING ZINC ZINC-FINGER) protein domain (PD002924) which is seen in Q6AFA1_BBBBB.Residues 424-499 are 67% similar to a (SYNTHETASE LIGASE ALANYL-TRNA AMINOACYL-TRNA ALANINE--TRNA BIOSYNTHESIS ALARS ATP-BINDING) protein domain (PD869946) which is seen in SYA_MYCPA.Residues 427-558 are 53% similar to a (SYNTHETASE LIGASE ALANINE--TRNA ALANYL-TRNA BIOSYNTHESIS ALARS AMINOACYL-TRNA ATP-BINDING) protein domain (PD902573) which is seen in SYA_TROWT.Residues 505-569 are 76% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA ALANINE--TRNA ALARS BIOSYNTHESIS ATP-BINDING ZINC ZINC-FINGER) protein domain (PD002754) which is seen in SYA_BIFLO.Residues 564-622 are 69% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA ALANINE--TRNA ALARS BIOSYNTHESIS ATP-BINDING ZINC ZINC-FINGER) protein domain (PD861914) which is seen in SYA_STRCO.Residues 626-720 are 68% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ALANYL-TRNA ALANINE--TRNA ALARS BIOSYNTHESIS ATP-BINDING ZINC ZINC-FINGER) protein domain (PD001534) which is seen in SYA_AQUPY.Residues 722-766 are 82% similar to a (SYNTHETASE LIGASE ALANINE--TRNA ALANYL-TRNA BIOSYNTHESIS ALARS AMINOACYL-TRNA ATP-BINDING) protein domain (PD878020) which is seen in SYA_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 580 (E_value = 6e-209) place ANA_0824 in the tRNA-synt_2c family which is described as tRNA synthetases class II (A).Residues 677 to 721 (E_value = 3.1e-20) place ANA_0824 in the tRNA_SAD family which is described as Threonyl and Alanyl tRNA synthetase second additional domain.Residues 826 to 899 (E_value = 1.6e-13) place ANA_0824 in the DHHA1 family which is described as DHHA1 domain.","","synthetase (alaS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0825","884696","883806","891","11.10","27.00","33541","ATGAGCGATAGCGCGCACACCTTGAACCACCGGGGCGGGCAGAGGTTGAGGACCGCCTCACACCGGGCGGTTCCAACCTGGGTTTTCGCCGGTGAGCACGCTACAGTTCTCGAGTTGTCCACATCGGAGACGGCAGGCGCCTGCTGCAGGTGCTACCGGTCGACGACGATGCGGACCTCCTGGGGTCCCGGCCCGAACCGAGGCTTGACCCCGCGCCGTCGCCTCCCGCCACGGCGTGCGACCATCGATCCGACAGGAATGACACACATGAGCTCTTCACGCTCCCGCCGCCAGGTGCGCCTCTCTCGCGCCCTCGGCATCCCGCTGACCCCCAAGGCCGTGCGCTACTTCGAGCGCCGCCCCTACGGCCCCGGTGAGCACGGCCGCGCCCGCCGCCGCACCGAGTCCGACTACGCCGTCCGCCTCAAGGAGAAGCAGCGCCTGCGCGCCCAGTACGGCATCCGCGAGGCCCAGCTCCAGCGCGTCTTCGAGGAGGCCCGTCGCGGCCAGGGCCTGACCGGTGAGTCCCTCGTCGAGCTGCTCGAGATGCGCCTGGACGCCCTCGTCCTGCGCTCCGGGATCGCCCGCACCATCGCCCAGGCCCGCCAGGACGTGGTTCACCGCCACATCCTCGTCGACGGCAAGGTCGTGGACCGCCCCTCCTACCGCGTCAAGCCCGGACAGACCATCCAGGTTCGTCCCCGCTCCCAGGTGATGGTGCCCTTCCAGGTCGCCGCCGCCGGTGCGCACCGCGACGTGCTGCCCCCCGTCCCGGAGTACCTCAACGTGGACCTCGAGAAGCTCTCGGCCACGCTGGTGCGCCGCCCCAAGCGCGACGAGGTCCCCGTGACCTGTGACGTCCAGATGGTCGTCGAGTACTACTCGCGCTGA","MSDSAHTLNHRGGQRLRTASHRAVPTWVFAGEHATVLELSTSETAGACCRCYRSTTMRTSWGPGPNRGLTPRRRLPPRRATIDPTGMTHMSSSRSRRQVRLSRALGIPLTPKAVRYFERRPYGPGEHGRARRRTESDYAVRLKEKQRLRAQYGIREAQLQRVFEEARRGQGLTGESLVELLEMRLDALVLRSGIARTIAQARQDVVHRHILVDGKVVDRPSYRVKPGQTIQVRPRSQVMVPFQVAAAGAHRDVLPPVPEYLNVDLEKLSATLVRRPKRDEVPVTCDVQMVVEYYSR$","30S ribosomal protein S4","Cytoplasm, Extracellular","30S ribosomal protein","30S ribosomal protein S4","RNA-binding S4 domain protein","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Mizuta K., Hashimoto T., Suzuki K., Otaka E. Yeast ribosomal proteins: XII. YS11 of Saccharomyces cerevisiae is a homologue to E. coli S4 according to the gene analysis. Nucleic Acids Res. 1991. 19(10):2603-2608. PMID: 2041737","","","

InterPro
IPR001912
Family

Ribosomal protein S4
PTHR11831	$\"[179-215]T$	30S 40S RIBOSOMAL PROTEIN
PF00163	$\"[91-182]T$	Ribosomal_S4

InterPro
IPR002942
Domain

RNA-binding S4
PF01479	$\"[183-230]T$	S4
SM00363	$\"[183-245]T$	S4
PS50889	$\"[183-264]T$	S4

InterPro
IPR005709
Family

Ribosomal protein S4, bacterial and organelle form
TIGR01017	$\"[94-296]T$	rpsD_bact: ribosomal protein S4

noIPR
unintegrated

unintegrated
G3DSA:3.10.290.10	$\"[182-296]T$	no description
PTHR11831:SF4	$\"[179-215]T$	30S RIBOSOMAL PROTEIN S4P

","BeTs to 26 clades of COG0522COG name: Ribosomal protein S4 and related proteinsFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0522 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001912 (Ribosomal protein S4) with a combined E-value of 2e-24. IPB001912 170-224***** IPB002942 (RNA-binding S4) with a combined E-value of 2.7e-16. IPB002942A 144-153 IPB002942B 182-213","Residues 118-295 are 56% similar to a (RIBOSOMAL 30S S4 PROBABLE RIBONUCLEOPROTEIN) protein domain (PDA1A8X3) which is seen in Q6MIP0_BDEBA.Residues 118-288 are 67% similar to a (RIBOSOMAL CHLOROPLAST S4 30S RRNA-BINDING RNA-BINDING RIBONUCLEOPROTEIN SMALL RPS4 S4P) protein domain (PD004849) which is seen in RS4_STRAW.","","-65% similar to PDB:1FKA STRUCTURE OF FUNCTIONALLY ACTIVATED SMALL RIBOSOMAL SUBUNIT AT 3.3 A RESOLUTION (E_value = 3.5E_36);-65% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 3.5E_36);-65% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 3.5E_36);-65% similar to PDB:1HNZ STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH HYGROMYCIN B (E_value = 3.5E_36);-65% similar to PDB:1I94 CRYSTAL STRUCTURES OF THE SMALL RIBOSOMAL SUBUNIT WITH TETRACYCLINE, EDEINE AND IF3 (E_value = 3.5E_36);","Residues 91 to 182 (E_value = 7.3e-13) place ANA_0825 in the Ribosomal_S4 family which is described as Ribosomal protein S4/S9 N-terminal domain.Residues 183 to 230 (E_value = 2.6e-19) place ANA_0825 in the S4 family which is described as S4 domain.","","ribosomal protein (BS4)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0826","886089","884686","1404","6.31","-5.08","49414","ATGGACCTGTTCGAGTCGGCCGGCACGGATGACGCCGGGATCCCCGTGGACTCCCACGCGCCGCTGGCGGTGCGGATGCGGCCGCGCACACTCGATGAGCTTCAGGGGCAGGCGCACCTGCTCACCCCCGGATCGCCTCTGCGCCGCCTCGTGGAGCCGGCTGATGTGGGCAGGGGCTCTCATGCCGGTGAACGGGGCGCCGCCGCGCGGCCGTCTAGTTCCTCCCTGTCCTCGGTCATCCTGTGGGGGCCGCCCGGAACCGGCAAGACGACGCTGGCCTACCTGGTGGCACGGGGCAGCGGCCGCAGGTTCGTGGAGCTGTCAGCGGTGACGGCCGGAGTCAAGGACGTGCGCGCCGTCGTGACCGATGCCAGGCGCCGTCTGGCGGCGGGGGAGGAGACGGTGCTGTTCATCGACGAGGTGCACCGATTCTCCCGCTCCCAGCAGGACGCCCTGCTGCCCAGCGTGGAGAACCGGTGGGTGACGCTCATCGCGGCCACCACGGAGAACCCGTCCTTCAGCGTCGTCTCACCGCTCCTGTCCCGCTCCCTGCTCCTGACGCTCCAGCCTCTGGGGGCCGATGACATCGGGCGTCTGATCGATCGCGCGCTGGATGACGAGCGGGGCCTGGCCGGTGCCGTGGGCATCAGCGAGGATGCGCGCGAGCAGATCGTGCGCATGGCCGGCTCCGACGCCCGCAAGGCGCTCACCGTGCTGGAGGCCGCCGCCGGCACGGTCCTGGCGCAGACACCTGCTTCCAGCTCGTCGCCTCTCATCGAGGTGGCCGACGTCGAGCGGGCCGCGGACGTGGCAGCGGTGCGTTACGACCGCGCCGGAGACCAGCACTACGACGTCATCAGCGCCTTCATCAAGTCGATGCGCGGCTCGGACCCCGACGCCACGATGCACTACCTGGCGCGCATGATTGCCGCCGGGGAGGACCCCCGTTACATCGCCCGGCGCATCGTCATTCACGCCGCCGAGGACGTGGGGCTCGCCGACCCGACGGTGCTGTCCACCGCCGTGGCCGCCCAGCAGGCGGTTGCCATGATCGGGATGCCGGAGTCCGGGCTCATCCTGGCCGAGGCCGCGCTCGCCGTGGCCACCGCTCCCAAGTCCAACGCGGTCACTGTGGCGCTCAACGAGTCGCTGGCCGATGTGCGGGCCGGGAAGGCCGCGGCCGTGCCCGCTCACCTGCGCGATGCCCACTACGCCGGGGCCGAGGGGCTCGGGCACGGCAAGGGCTACCGCTACCCGCACGACTTCCCCCACGCCGTCGTCGGCCAGCAGTACCTGCCCGACGGGCTCGAGGGCAGCCGGTACTACCGGCCCACAGGAAACGGCTTCGAGAAGCAGCTGGCTTCCCGCCTCGAGGCGGTCCGGCGCATCCTGGATGAGCGATAG","MDLFESAGTDDAGIPVDSHAPLAVRMRPRTLDELQGQAHLLTPGSPLRRLVEPADVGRGSHAGERGAAARPSSSSLSSVILWGPPGTGKTTLAYLVARGSGRRFVELSAVTAGVKDVRAVVTDARRRLAAGEETVLFIDEVHRFSRSQQDALLPSVENRWVTLIAATTENPSFSVVSPLLSRSLLLTLQPLGADDIGRLIDRALDDERGLAGAVGISEDAREQIVRMAGSDARKALTVLEAAAGTVLAQTPASSSSPLIEVADVERAADVAAVRYDRAGDQHYDVISAFIKSMRGSDPDATMHYLARMIAAGEDPRYIARRIVIHAAEDVGLADPTVLSTAVAAQQAVAMIGMPESGLILAEAALAVATAPKSNAVTVALNESLADVRAGKAAAVPAHLRDAHYAGAEGLGHGKGYRYPHDFPHAVVGQQYLPDGLEGSRYYRPTGNGFEKQLASRLEAVRRILDER$","ATPase related to the helicase subunit of the Holliday junction resolvase","Cytoplasm","conserved ATP/GTP binding protein","K07478 putative ATPase","AAA ATPase, central domain protein","","Voisey J., Van daal A. Agouti: from mouse to man, from skin to fat. Pigment Cell Res. 2002. 15(1):10-18. PMID: 11837451Kanetsky P.A., Swoyer J., Panossian S., Holmes R., Guerry D., Rebbeck T.R. A polymorphism in the agouti signaling protein gene is associated with human pigmentation. Am. J. Hum. Genet. 2002. 70(3):770-775. PMID: 11833005","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[75-210]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[78-159]T$	AAA

InterPro
IPR007733
Family

Agouti
SM00792	$\"[175-279]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[12-191]T$	no description
PTHR13779	$\"[30-52]T$ $\"[73-467]T$	HOLLIDAY JUNCTION DNA HELICASE RUVB-RELATED
PTHR13779:SF1	$\"[30-52]T$ $\"[73-467]T$	WERNER HELICASE INTERACTING PROTEIN

InterPro
IPR004388
Domain

Sua5/YciO/YrdC/YwlC
TIGR00057	$\"[7-204]T$	TIGR00057: Sua5/YciO/YrdC/YwlC family prote

InterPro
IPR006070
Domain

SUA5/yciO/yrdC, N-terminal
PF01300	$\"[22-198]T$	Sua5_yciO_yrdC
PS51163	$\"[14-200]T$	YRDC

InterPro
IPR012200
Family

RNA-binding protein, YrdC
PIRSF004931	$\"[8-205]T$	RNA-binding protein, YrdC type

noIPR
unintegrated

unintegrated
G3DSA:3.90.870.10	$\"[1-203]T$	no description
PTHR17490	$\"[27-202]T$	SUA5

","BeTs to 23 clades of COG0009COG name: Putative translation factor (SUA5)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0009 is aompkzyqvdrlbcefghsn-jxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB004388 (Sua5/YciO/YrdC/YwlC protein family) with a combined E-value of 2.4e-22. IPB004388A 29-58 IPB004388B 88-98 IPB004388C 182-192***** IPB006070 (SUA5/yciO/yrdC, N-terminal) with a combined E-value of 1.6e-19. IPB006070A 24-67 IPB006070B 139-151","Residues 1-198 are 48% similar to a (SSO0664 ORF-C09_003) protein domain (PDA189O4) which is seen in Q9UX54_SULSO.Residues 1-205 are 46% similar to a () protein domain (PD977851) which is seen in Q9WZV6_THEMA.Residues 1-201 are 47% similar to a (SMC00984) protein domain (PDA18780) which is seen in Q92RK2_RHIME.Residues 1-205 are 50% similar to a (SUA5 TRANSLATION FACTOR) protein domain (PD977850) which is seen in Q8RD96_THETN.Residues 2-198 are 44% similar to a (TRANSLATION FACTOR) protein domain (PDA187I4) which is seen in Q7UPX2_RHOBA.Residues 3-205 are 49% similar to a (SUA5) protein domain (PD977853) which is seen in Q898Y2_CLOTE.Residues 3-199 are 46% similar to a (SUA5 TRANSLATION PREDICTED FACTOR) protein domain (PD977852) which is seen in Q97F70_CLOAB.Residues 4-198 are 48% similar to a () protein domain (PDA199K3) which is seen in Q6AL59_BBBBB.Residues 6-198 are 44% similar to a (YWLC) protein domain (PD977846) which is seen in YWLC_BACSU.Residues 7-198 are 45% similar to a () protein domain (PD977845) which is seen in Q8EM64_OCEIH.Residues 8-188 are 45% similar to a (TRANSMEMBRANE TA-2) protein domain (PD393837) which is seen in Q9DDN4_XENLA.Residues 9-201 are similar to a (FAMILY TRANSLATION SUA5/YCIO/YRDC/YWLC FACTOR SUA5/YCIO/YRDC SUA5 YRDC CASUA5 YCIO CANDIDA) protein domain (PD329321) which is seen in Q9KYM5_STRCO.Residues 10-199 are 45% similar to a (SUA5 SUPERFAMILY-RELATED) protein domain (PD977847) which is seen in Q6L0H3_PICTO.Residues 10-205 are 46% similar to a (CPE2200) protein domain (PD977844) which is seen in Q8XIC1_CLOPE.Residues 17-199 are 42% similar to a (SE1713) protein domain (PD977849) which is seen in Q8CRN1_STAEP.Residues 17-199 are 44% similar to a (SUA5/YCIO/YRDC FAMILY) protein domain (PD977855) which is seen in Q9A316_CAUCR.Residues 18-198 are 43% similar to a (SUA5/YCIO/YRDC/YWLC DOMAIN FAMILY:SUA5) protein domain (PDA185X9) which is seen in Q6NAV3_RHOPA.","","-68% similar to PDB:1K7J Structural Genomics, protein TF1 (E_value = 1.2E_52);-68% similar to PDB:1KK9 CRYSTAL STRUCTURE OF E. COLI YCIO (E_value = 1.2E_52);-49% similar to PDB:1JCU Solution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicum (E_value = 2.5E_15);-45% similar to PDB:1HRU THE STRUCTURE OF THE YRDC GENE PRODUCT FROM E.COLI (E_value = 5.5E_10);-57% similar to PDB:1GSO GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI. (E_value = 5.5E_10);","Residues 22 to 198 (E_value = 1.1e-48) place ANA_0827 in the Sua5_yciO_yrdC family which is described as yrdC domain.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0828","887639","886917","723","5.05","-11.42","26330","ATGATCTTCGGGCACCGGGGCCTGAGCTCGCTGGCCCCGGAGAACACCATGGCCGCTTTCCGTTGTGCGGTGGATCATCAGGTGAAGTGGGTGGAGGCCGACGTCGACGTCATCGCCGACGGAACAGTCATCATCTGCCATGACTCCACCCTGGACCGGACTACGAATCGCACCGGTCGGTACGACGACCTGACGGCGGCCGATCTGGCGGGCATCGACGCCGGAGGCTGGTTCTCCCCTCGGTTTGTGGGTGAGCCGCTGCCCGCCCTGAGCGATCTCATCGACCTCATGAACGACAGCGGTCTCAACGCCAACATCGAGATCAAGCCCAATGAGACCGGCAAGGAGGCGACCCTGCGCCTCATCGATGGCGTCATCACACAGCTCGAGCGCCTGCGCCCCGACGTCAAGGTCATCGTCTCCTCCTTCAGCCACCTCCTGCTCCACCTGTTCAAGCAGCGTGCCCCGGAGGTTCCCGTGGGGTGCCTCTATGAGAGTCGTGCGCTGTCGGGTGACTGGAGGAGCACCCTTGAGATCGTGGGCGCCGACTTCATCCATCCCGAGGACTCCGGCCTGACCCGGCAGCAGGTCCAGGAGTTTCGGGATTCGGGCTACGGCGTCAACGTCTGGACCGTCAACTCGCCCAGCCGAGCCGACGAGCTCTTCAGCTGGGGGGCCACCGGCGTCTTCTCCGATATCGCCCACCAGATCCCTGGCCGCTGA","MIFGHRGLSSLAPENTMAAFRCAVDHQVKWVEADVDVIADGTVIICHDSTLDRTTNRTGRYDDLTAADLAGIDAGGWFSPRFVGEPLPALSDLIDLMNDSGLNANIEIKPNETGKEATLRLIDGVITQLERLRPDVKVIVSSFSHLLLHLFKQRAPEVPVGCLYESRALSGDWRSTLEIVGADFIHPEDSGLTRQQVQEFRDSGYGVNVWTVNSPSRADELFSWGATGVFSDIAHQIPGR$","Glycerophosphoryl diester phosphodiesterase","Cytoplasm","Glycerophosphoryl diesterphosphodiesterase(Glycerophosphodiester","glycerophosphoryl diester phosphodiesterase ","Glycerophosphodiester phosphodiesterase","","Pervaiz S., Brew K. Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science 1985. 228(4697):335-337. PMID: 2580349Flower D.R., North A.C., Attwood T.K. Mouse oncogene protein 24p3 is a member of the lipocalin protein family. Biochem. Biophys. Res. Commun. 1991. 180(1):69-74. PMID: 1834059Flower D.R., North A.C., Attwood T.K. Structure and sequence relationships in the lipocalins and related proteins. Protein Sci. 1993. 2(5):753-761. PMID: 7684291Flower D.R. Multiple molecular recognition properties of the lipocalin protein family. J. Mol. Recognit. 1995. 8(3):185-195. PMID: 8573354","","","

InterPro
IPR002345
Domain

Lipocalin
PS00213	$\"[165-176]?$	LIPOCALIN

InterPro
IPR004129
Family

Glycerophosphoryl diester phosphodiesterase
PTHR23344	$\"[1-165]T$	GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE
PF03009	$\"[5-236]T$	GDPD

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.190	$\"[1-232]T$	no description

","BeTs to 15 clades of COG0584COG name: Glycerophosphoryl diester phosphodiesteraseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0584 is -o-pkzy-vdrlb-efgh---j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB004129 (Glycerophosphoryl diester phosphodiesterase) with a combined E-value of 1.2e-13. IPB004129A 0-9 IPB004129B 13-48","Residues 2-63 are similar to a (PHOSPHODIESTERASE DIESTER GLYCEROPHOSPHORYL HYDROLASE GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE FAMILY PERIPLASMIC PROBABLE RIKEN) protein domain (PD542577) which is seen in Q6A6P9_PROAC.Residues 64-157 are similar to a (PHOSPHODIESTERASE DIESTER GLYCEROPHOSPHORYL HYDROLASE GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE FAMILY PROBABLE MEMBRANE SIMILAR) protein domain (PD033459) which is seen in Q6A6P9_PROAC.Residues 160-200 are 75% similar to a (DIESTER HYDROLASE PHOSPHODIESTERASE GLYCEROPHOSPHORYL) protein domain (PD972175) which is seen in Q6A6P9_PROAC.","","-49% similar to PDB:2OTD The crystal structure of the glycerophosphodiester phosphodiesterase from Shigella flexneri 2a (E_value = 1.9E_31);-54% similar to PDB:1ZCC Crystal structure of glycerophosphodiester phosphodiesterase from Agrobacterium tumefaciens str.C58 (E_value = 2.7E_17);-46% similar to PDB:2OOG Crystal structure of glycerophosphoryl diester phosphodiesterase from Staphylococcus aureus (E_value = 6.1E_14);-46% similar to PDB:2P76 Crystal structure of a Glycerophosphodiester Phosphodiesterase from Staphylococcus aureus (E_value = 6.1E_14);-40% similar to PDB:1V8E Crystal Structure of Glycerophosphoryl Diester Phosphodiesterase from Thermus thermophilus HB8 (E_value = 8.3E_11);","Residues 5 to 236 (E_value = 4.6e-40) place ANA_0828 in the GDPD family which is described as Glycerophosphoryl diester phosphodiesterase family.","","diester phosphodiesterase(Glycerophosphodiester phosphodiesterase) (pde)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0829","887774","888103","330","6.86","-0.69","12189","ATGCGAAAGGTCGCCACACCACCGGAGGCCCCCCTTGGGGAGGACTCGGCCGTGGTGCAGCTGTTCAAGGCGCTGGCTCACCCCATGAGGGCGAGCATCGTCTACCGCCTCATCAGCTCACCGGCTGACGTCACCGAGCTGGTGACGTTCCTCGGCGTTTCCCAGCCCTTGGTCTCGCACCACCTGCGGGTCCTGCGCAACGCCCACCTGGTCGAGTCGGTCCGCGACGGCAAGCGCCAGAGCTACTCCCTCATTGACGACCATGTCGCATCCATCTTCATCGACACCCTCGAGCACACGAAGGAGCACGATCATGACTGCCACCACTGA","MRKVATPPEAPLGEDSAVVQLFKALAHPMRASIVYRLISSPADVTELVTFLGVSQPLVSHHLRVLRNAHLVESVRDGKRQSYSLIDDHVASIFIDTLEHTKEHDHDCHH$","Transcriptional regulator; ArsR family","Cytoplasm","transcription regulator","transcriptional regulator; ArsR family","regulatory protein, ArsR","","Morby A.P., Turner J.S., Huckle J.W., Robinson N.J. SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 1993. 21(4):921-925. PMID: 8451191Bairoch A. A possible mechanism for metal-ion induced DNA-protein dissociation in a family of prokaryotic transcriptional regulators. Nucleic Acids Res. 1993. 21(10):2515-2515. PMID: 8506147Eicken C., Pennella M.A., Chen X., Koshlap K.M., VanZile M.L., Sacchettini J.C., Giedroc D.P. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins. J. Mol. Biol. 2003. 333(4):683-695. PMID: 14568530Cook W.J., Kar S.R., Taylor K.B., Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J. Mol. Biol. 1998. 275(2):337-346. PMID: 9466913Busenlehner L.S., Pennella M.A., Giedroc D.P. The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 2003. 27(2):131-143. PMID: 12829264Liu T., Nakashima S., Hirose K., Shibasaka M., Katsuhara M., Ezaki B., Giedroc D.P., Kasamo K. A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPx-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II). J. Biol. Chem. 2004. 279(17):17810-17818. PMID: 14960585","","","

InterPro
IPR001845
Domain

Bacterial regulatory protein, ArsR
PR00778	$\"[22-37]T$ $\"[54-69]T$ $\"[69-84]T$	HTHARSR
PF01022	$\"[27-73]T$	HTH_5
SM00418	$\"[20-98]T$	HTH_ARSR
PS50987	$\"[12-104]T$	HTH_ARSR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[18-108]T$	no description

","BeTs to 16 clades of COG0640COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0640 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB001845 (Bacterial regulatory protein, ArsR family) with a combined E-value of 1.5e-17. IPB001845 40-84","Residues 18-99 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL ARSR FAMILY REGULATOR REGULATOR REPRESSOR RESISTANCE) protein domain (PD001992) which is seen in Q8R5P8_THETN.","","-55% similar to PDB:1R22 Crystal structure of the cyanobacterial metallothionein repressor SmtB (C14S/C61S/C121S mutant) in the Zn2alpha5-form (E_value = 5.9E_10);","Residues 27 to 73 (E_value = 8.7e-11) place ANA_0829 in the HTH_5 family which is described as Bacterial regulatory protein, arsR family.","","regulator (merR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0830","888087","888410","324","5.18","-14.81","11569","ATGACTGCCACCACTGAGCACCGCCCCGCTGAGGCCCACCAGCACACCCACGGCCCCGACTGCGGGCACCTGGCCGTCATCCACGGAGACCACGTGGACTACATTCACAACGGCCACGCCCACCACGAGGACAACGGCCACTACGACGAGTGCGACACCTGCTCGTGCGAGCACTGCTCGGACCCCTGCGCCGTGTGCGAGTGCGAGGACTGCACCTGCCCCACCTGCAACCACAACACCTGCTCGTGCGAGCACTGCTCGGACTCCTGCTCCTCGTGCACCTGCGAGGACTGCACCTGCCCGACCTGCACGCACGCCGCCTGA","MTATTEHRPAEAHQHTHGPDCGHLAVIHGDHVDYIHNGHAHHEDNGHYDECDTCSCEHCSDPCAVCECEDCTCPTCNHNTCSCEHCSDSCSSCTCEDCTCPTCTHAA$","Hypothetical protein","Extracellular, Periplasm, Cytoplasm","cobalamin biosynthesis protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG0803COG name: ABC-type Mn/Zn transport system, periplasmic Mn/Zn-binding (lipo)protein (surface adhesin A)Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0803 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 4","***** IPB001762 (Disintegrin) with a combined E-value of 5.4e-07. IPB001762 54-106 IPB001762 48-100 IPB001762 51-103 IPB001762 49-101 IPB001762 53-105 IPB001762 42-94 IPB001762 52-104 IPB001762 31-83 IPB001762 44-96 IPB001762 46-98 IPB001762 37-89 IPB001762 56-107***** IPB001007 (von Willebrand factor, type C) with a combined E-value of 1.6e-06. IPB001007A 61-73 IPB001007B 89-103 IPB001007A 88-100 IPB001007A 71-83 IPB001007A 91-103 IPB001007A 83-95 IPB001007B 76-90 IPB001007B 62-76***** IPB000877 (Bowman-Birk serine protease inhibitor) with a combined E-value of 6.6e-06. IPB000877 62-100 IPB000877 59-97 IPB000877 64-102 IPB000877 66-104 IPB000877 52-90 IPB000877 55-93 IPB000877 67-105 IPB000877 69-107 IPB000877 50-88","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","biosynthesis protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0831","888603","890186","1584","6.95","-0.29","54619","ATGCGCACGCGCAACGATCATGTGCCCATGAGCAGTCCCCTCCCTGTTTCCGGTGCTTCTGGGCACGTCGCACCGCCTGTGCCCGGTGTCCGTCTGGGACAGGTGCTGGGTCAGGGAGGATTCGCCACCGTCTACGCCGGGGAGCAGGTCTCGTTGGGGCGCCCAGTGGCTGTCAAGATCGACTCCAGGCCGCTGCACGACGAGCGAAACCGCCGACGTTTCATGCGGGAGATGGCGGCCGCCAGCCGGATCAGCGGGCACCCGAACGCGGTCTCGCTGATCGACTCCGGAGTGCTTCCCGACGGGCGCCCCTACCTGGTCATGGAACGCTGTGACGGGGGCTCCTTGGCCCAGGTCCTGCAGCACGGCGAGATCAGCGCCGCTCAGGCCGTCAGCATCGTCACGGCCGTGTGCTCCGCCCTGGGCGCTGCTCACGACGTCGGGGTCCTCCACCGCGACATCAAGCCCGGAAACATCCTCATTGACGCTTATGGAAGCCCGCGTCTGAGCGACTTCGGCCTGGCCGCCGTCCAGCGCGAGGGCATCGACTCCTCCGTCACCCTGGAGACGATGACGCCGGACTTCGCTCCCCCGGAGGCCTTCACCCTGGCCGCGCCCTCACCCAGGGGCGACGTGTGGTCGATGGGGGCCGTTCTCTTCGCGCTCTTGACCGGACGCGGTCCTCGACGCACAGCCGACGGCGCCCCCCAGAGCCTGCCGGAGATCATCAACCACCTGTCGGTGCCCATCGACACCTCCGACGCGCGCATCCCCGAGGCGTTACGTCCGCTGCTCGACCGGGCGCTGCACCCCGACCCCGCTCAGCGGTACCGCGACGGCAACGAGCTGACCGAAGCACTGACTCGGGCCGGCGGGCTCTCGAACGGCGCGTTCAGCACCCCTCACTCGGCGCTACGGGATTCCCACCCCCTGCCTGCGGCGATCTCGACGCCCACAGACGGCTCGCGCCGCTCGAGCAGGGCACTGATGCTCCTGGCACTGGGTGTGACAGCGGGCGTCGTCATCTCCGCCGCTGTGCTGGGCGCCGTGAGGCTCATCGACTCGGTGCCGTCAGCGAACCGGGCAGTCCAGCGGGCCTCTGCCTCGCCCGTCCTACATGCCGGGGCCCGAGCGGAGCAGGGCGCCGGCAGCCGCCCCTCGGCTACGGCCCGGGCAACCGTCCCCGGCTCCCGGAAGGCTTCGCCCTCCCCGACATCCGCCCCGACTCCCGCGCAGGTCAACGCCCAGGGCATCCCCTACTCCGACGACATGCCGTGGCCTCTGGGGACCTGCCTGAGCCGGACGACCTCGGTCGTGGGCGGCACGAGCGTCAGCCAGGTCGACTGCTCCCAGGCCGACTGGATCGTCTTCGCCGGCGGAACCTTCGATCCGGCCACGACCGCTTCCAGCGCCACCGAGGCCATGGCGAATGACCCTCAGGTCGAGGTCGCCTGCACCAGCGCCTACGCGCAGCGCTATGGACTCGACCTGTCCACCAGCTACACGATCAACACGCTCGGTCCCAATGATGAGGAGTGGGCCGCGGGCAGTCGGGGTTTCGCCTGCGTTCTGGGCCGGTTGTAG","MRTRNDHVPMSSPLPVSGASGHVAPPVPGVRLGQVLGQGGFATVYAGEQVSLGRPVAVKIDSRPLHDERNRRRFMREMAAASRISGHPNAVSLIDSGVLPDGRPYLVMERCDGGSLAQVLQHGEISAAQAVSIVTAVCSALGAAHDVGVLHRDIKPGNILIDAYGSPRLSDFGLAAVQREGIDSSVTLETMTPDFAPPEAFTLAAPSPRGDVWSMGAVLFALLTGRGPRRTADGAPQSLPEIINHLSVPIDTSDARIPEALRPLLDRALHPDPAQRYRDGNELTEALTRAGGLSNGAFSTPHSALRDSHPLPAAISTPTDGSRRSSRALMLLALGVTAGVVISAAVLGAVRLIDSVPSANRAVQRASASPVLHAGARAEQGAGSRPSATARATVPGSRKASPSPTSAPTPAQVNAQGIPYSDDMPWPLGTCLSRTTSVVGGTSVSQVDCSQADWIVFAGGTFDPATTASSATEAMANDPQVEVACTSAYAQRYGLDLSTSYTINTLGPNDEEWAAGSRGFACVLGRL$","Protein kinase/transcriptional regulator, LuxR family","Membrane, Extracellular","serine/threonine protein kinase","protein kinase/transcriptional regulator; LuxR family ","protein kinase","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Siezen R.J., Leunissen J.A. Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 1997. 6(3):501-523. PMID: 9070434Wlodawer A., Li M., Gustchina A., Oyama H., Dunn B.M., Oda K. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. Acta Biochim. Pol. 2003. 50(1):81-102. PMID: 12673349","","","

InterPro
IPR000209
Domain

Peptidase S8 and S53, subtilisin, kexin, sedolisin
PS00136	$\"[91-101]?$	SUBTILASE_ASP

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[41-287]T$	Q6AEZ5_BBBBB_Q6AEZ5;
PF00069	$\"[30-277]T$	Pkinase
PS50011	$\"[30-288]T$	PROTEIN_KINASE_DOM
PS00107	$\"[36-59]T$	PROTEIN_KINASE_ATP

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[149-161]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[101-277]T$	no description
PTHR22986	$\"[30-276]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES
tmhmm	$\"[330-350]?$	transmembrane_regions

","BeTs to 12 clades of COG0515COG name: Serine/threonine protein kinasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0515 is -o-p-zyq-drlbcefghs--j-i-wNumber of proteins in this genome belonging to this COG is 10","***** IPB000959 (POLO box duplicated region) with a combined E-value of 1.3e-24. IPB000959A 30-75 IPB000959C 136-175 IPB000959D 192-246***** IPB000961 (Protein kinase C-terminal domain) with a combined E-value of 8.5e-23. IPB000961A 29-63 IPB000961C 132-174 IPB000961D 188-229***** IPB008266 (Tyrosine protein kinase, active site) with a combined E-value of 2.6e-16. IPB008266A 136-176 IPB008266B 194-230***** IPB003527 (MAP kinase) with a combined E-value of 2.4e-15. IPB003527A 56-98 IPB003527C 125-175***** IPB000095 (PAK-box/P21-Rho-binding) with a combined E-value of 4.8e-12. IPB000095B 34-47 IPB000095D 113-159 IPB000095E 172-216***** IPB013695 (Wall-associated kinase) with a combined E-value of 8.3e-10. IPB013695F 33-62 IPB013695I 142-178 IPB013695J 179-228***** IPB000861 (PKN/rhophilin/rhotekin rho-binding repeat) with a combined E-value of 6.8e-09. IPB000861C 27-63 IPB000861D 108-161***** IPB000472 (Domain in TGF-beta receptor/activin receptor, type I/II) with a combined E-value of 2.3e-08. IPB000472C 87-141 IPB000472D 146-176***** IPB001772 (Kinase-associated, C-terminal) with a combined E-value of 7.8e-08. IPB001772A 27-58 IPB001772D 199-238","Residues 41-289 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA10203) which is seen in Q7UIJ7_RHOBA.Residues 41-228 are 43% similar to a (KINASE 1-LIKE RESPONSIVE ATP-BINDING STRESS) protein domain (PD099489) which is seen in O61125_DICDI.Residues 41-276 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN ACR142WP TRANSFERASE ATP-BINDING) protein domain (PDA0A7Q6) which is seen in Q75CE9_ASHGO.Residues 41-278 are 43% similar to a (YARROWIA LIPOLYTICA STRAIN CHROMOSOME CLIB99 B) protein domain (PDA12896) which is seen in Q6CFM7_EEEEE.Residues 41-224 are 40% similar to a (KINASE RECEPTOR TRANSFERASE TYROSINE-PROTEIN ATP-BINDING TYROSINE) protein domain (PD566768) which is seen in Q8WSM2_SCHMA.Residues 41-287 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD500022) which is seen in Q8YMH9_ANASP.Residues 41-321 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING PLASMID) protein domain (PD756391) which is seen in Q820A7_STRAW.Residues 41-251 are 44% similar to a (CELL DIVISION KINASE SERINE/THREONINE-PROTEIN TRANSFERASE MITOSIS ATP-BINDING HOMOLOG CONTROL CYCLE) protein domain (PDA1A0C7) which is seen in CDC2_CAEEL.Residues 41-228 are 48% similar to a (P0418B08.10 OJ1740_D06.39) protein domain (PDA10665) which is seen in Q69P46_EEEEE.Residues 41-276 are 41% similar to a (KINASE RELATED ATP-BINDING SEVERIN) protein domain (PDA0F7C6) which is seen in Q7SFV7_NEUCR.Residues 41-224 are 44% similar to a (KINASE DJFGFR1 TRANSFERASE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD611563) which is seen in Q8MY86_DUGJA.Residues 41-224 are 43% similar to a (KINASE TRANSFERASE TYROSINE-PROTEIN ATP-BINDING F11E6.8) protein domain (PD247428) which is seen in Q9XVQ7_CAEEL.Residues 41-237 are 43% similar to a (SERINE/THREONINE-PROTEIN KINASE MEK1 MEIOSIS TRANSFERASE ATP-BINDING MEIOSIS-SPECIFIC) protein domain (PDA0I4P9) which is seen in MEK1_SCHPO.Residues 41-276 are 40% similar to a (KINASE SERINE/THREONINE-PROTEIN GLP_28_16955_18661 TRANSFERASE ATP-BINDING) protein domain (PDA08641) which is seen in Q7R1Q1_EEEEE.Residues 41-237 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE BRASSINOSTEROID ATP-BINDING INSENSITIVE) protein domain (PD595107) which is seen in Q84ZJ8_EEEEE.Residues 41-228 are 47% similar to a (SIMILAR DEBARYOMYCES HANSENII DEHA0C16181G) protein domain (PD991318) which is seen in Q6C3K8_EEEEE.Residues 41-276 are 45% similar to a (ORYZA SIMILAR 36I5.3 RICE. SATIVA ATP-BINDING) protein domain (PD808911) which is seen in Q86IX1_DICDI.Residues 41-228 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD727335) which is seen in Q86JX3_DICDI.Residues 41-222 are 44% similar to a (ATP-BINDING AGCP10418) protein domain (PDA0J0F6) which is seen in Q7QGN6_EEEEE.Residues 41-287 are 50% similar to a (KINASE ATP-BINDING TRANSFERASE SERINE/THREONINE-PROTEIN RECEPTOR PHOSPHORYLATION SERINE/THREONINE TYROSINE-PROTEIN REPEAT CELL) protein domain (PD000001) which is seen in Q6AEZ5_BBBBB.Residues 41-224 are 48% similar to a (KINASE TRANSFERASE TYROSINE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD289861) which is seen in Q9Y1Y3_EEEEE.Residues 41-276 are 57% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE TRANSCRIPTION ATP-BINDING DNA-BINDING SERINE-THREONINE REGULATION) protein domain (PDA1B2W7) which is seen in Q6PV87_BBBBB.Residues 41-228 are 46% similar to a (KINASE TRANSFERASE ATP-BINDING MOS) protein domain (PD267193) which is seen in Q9GRC0_ASTPE.Residues 42-310 are 50% similar to a (KINASE SERINE-THREONINE) protein domain (PDA1D4F7) which is seen in Q6A9T0_PROAC.Residues 42-276 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA1A878) which is seen in Q72IA2_THET2.Residues 42-228 are 50% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE ATP-BINDING SHK2) protein domain (PD078766) which is seen in SHK2_SCHPO.Residues 42-228 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756060) which is seen in Q81ZY9_STRAW.Residues 42-228 are 53% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA2 PROBABLE TRANSFERASE REPEAT ATP-BINDING) protein domain (PD848557) which is seen in PKNA_BIFLO.Residues 42-289 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD810446) which is seen in Q895P6_CLOTE.Residues 42-290 are 51% similar to a (KINASE SERINE/THREONINE) protein domain (PDA1A7D8) which is seen in Q6AE50_BBBBB.Residues 42-228 are 53% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE KINASE ATP-BINDING) protein domain (PD828286) which is seen in Q9RRH3_DEIRA.Residues 43-398 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796289) which is seen in Q9S2A6_STRCO.Residues 43-318 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD842227) which is seen in Q81ZZ0_STRAW.Residues 43-276 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNA TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5E6) which is seen in Q7UX63_RHOBA.Residues 43-320 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756057) which is seen in Q81ZV7_STRAW.Residues 43-284 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA0Z806) which is seen in Q7NLM6_GLOVI.Residues 43-310 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA08789) which is seen in Q7UL45_RHOBA.Residues 43-290 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD239091) which is seen in Q9KJN8_MYXXA.Residues 43-276 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD975784) which is seen in Q7NPK1_GLOVI.Residues 43-296 are 51% similar to a (SERINE/THREONINE-PROTEIN KINASE PROBABLE TRANSFERASE PKNJ TRANSMEMBRANE ATP-BINDING) protein domain (PD063660) which is seen in PKNJ_MYCTU.Residues 44-382 are 44% similar to a (KINASE PKNB SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5H6) which is seen in Q7UFU9_RHOBA.Residues 44-199 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA18944) which is seen in Q7UPN1_RHOBA.Residues 44-269 are 52% similar to a (KINASE SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA010X1) which is seen in Q7UKY9_RHOBA.Residues 44-228 are 53% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796751) which is seen in Q81ZW2_STRAW.Residues 44-381 are 44% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE WD SERINE/THREONINE ATP-BINDING) protein domain (PD288091) which is seen in Q9RDS3_STRCO.Residues 44-381 are 43% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE TPR PHOSPHORYLATION REPEAT PKN1 ATP-BINDING) protein domain (PD052299) which is seen in PKN1_MYXXA.Residues 44-289 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN PPKA TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA025J8) which is seen in Q7UT84_RHOBA.Residues 44-288 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA191E0) which is seen in Q8DLN7_SYNEL.Residues 44-289 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA10189) which is seen in Q7UKJ3_RHOBA.Residues 44-321 are 37% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D5J2) which is seen in Q7UZ75_RHOBA.Residues 44-287 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D464) which is seen in Q7UW31_RHOBA.Residues 44-286 are 42% similar to a (KINASE SERINE/THREONINE) protein domain (PD456344) which is seen in Q98IK2_RHILO.Residues 44-276 are 45% similar to a (KINASE SER/THR TRANSFERASE ATP-BINDING) protein domain (PD126531) which is seen in O54229_STRGT.Residues 44-283 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN PKN10 TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA043E6) which is seen in Q7UGA2_RHOBA.Residues 44-317 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D3Y0) which is seen in Q7UVF2_RHOBA.Residues 44-316 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD820279) which is seen in Q81ZY2_STRAW.Residues 44-276 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD141352) which is seen in O54230_STRGT.Residues 44-289 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING PROBABLE SERINE-THREONINE) protein domain (PD736072) which is seen in Q8G6Q0_BIFLO.Residues 44-287 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA1D4Q5) which is seen in Q7ULK7_RHOBA.Residues 44-316 are 47% similar to a (KINASE PKN9 SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD268676) which is seen in Q9XBP3_MYXXA.Residues 44-287 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA19096) which is seen in Q7UJC1_RHOBA.Residues 44-276 are 51% similar to a (SERINE/THREONINE-PROTEIN KINASE PKN3 TRANSFERASE ATP-BINDING) protein domain (PD316927) which is seen in PKN3_MYXXA.Residues 44-287 are 44% similar to a (KINASE REPEAT TPR SERINE/THREONINE ATP-BINDING PKN8) protein domain (PD280760) which is seen in Q9XBP6_MYXXA.Residues 44-311 are 45% similar to a (BLR3604 KINASE TRANSFERASE ATP-BINDING) protein domain (PD828726) which is seen in Q89P79_BRAJA.Residues 44-287 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING SERINE/THREONINE-SPECIFIC PROBABLE) protein domain (PDA1D2S2) which is seen in Q7UFH1_RHOBA.Residues 44-290 are 48% similar to a () protein domain (PDA046H8) which is seen in Q73YC5_MYCPA.Residues 44-290 are 46% similar to a (PKND) protein domain (PDA18730) which is seen in Q73UI1_MYCPA.Residues 44-287 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA0K9H0) which is seen in Q7NMV0_GLOVI.Residues 44-295 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA0H1H6) which is seen in Q7UJD9_RHOBA.Residues 46-185 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN REGULATOR SERINE/THREONINE) protein domain (PD843536) which is seen in Q9L096_STRCO.Residues 52-349 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD724652) which is seen in Q81ZW8_STRAW.Residues 52-273 are 48% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA TRANSFERASE ATP-BINDING PROBABLE) protein domain (PDA188K3) which is seen in PKNA_MYCLE.Residues 52-315 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN REPEAT TRANSFERASE TPR 2.7.1.- ATP-BINDING) protein domain (PDA0F980) which is seen in Q7URL4_RHOBA.Residues 52-290 are 41% similar to a (KINASE SERINE/THREONINE-PROTEIN SERINE/THREONINE KINASE) protein domain (PD745593) which is seen in Q9RUY7_DEIRA.Residues 53-265 are 44% similar to a (T20L15_160 AT5G01890/T20L15_160 ATP-BINDING) protein domain (PD280913) which is seen in Q9LZV7_ARATH.Residues 53-249 are 44% similar to a (KINASE CELL DIVISION SERINE/THREONINE-PROTEIN 3D-STRUCTURE CYCLE TRANSFERASE PHOSPHORYLATION PLSTIRE ATP-BINDING) protein domain (PD470147) which is seen in CDK6_HUMAN.Residues 53-276 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD298418) which is seen in Q9X8G8_STRCO.Residues 53-247 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING KINASE-LIKE) protein domain (PDA183S2) which is seen in O65480_ARATH.Residues 53-313 are 44% similar to a (SERINE/THREONINE-PROTEIN KINASE REPEAT PROBABLE TRANSFERASE WD PKWA ATP-BINDING) protein domain (PD110150) which is seen in PKWA_THECU.Residues 53-276 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796214) which is seen in Q81ZX4_STRAW.Residues 53-338 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE-THREONINE ATP-BINDING) protein domain (PD319602) which is seen in Q9K3W7_STRCO.Residues 54-283 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PDA0G6B9) which is seen in Q6MAN0_PARUW.Residues 55-282 are 46% similar to a (KINASE CAMP-DEPENDENT SERINE/THREONINE-PROTEIN CATALYTIC TRANSFERASE ATP-BINDING SUBUNIT) protein domain (PD750451) which is seen in Q9BMY6_TOXGO.Residues 57-276 are 41% similar to a (ANK REPEAT GLP_160_2453_6841) protein domain (PDA13310) which is seen in Q7QVY6_EEEEE.Residues 66-276 are 45% similar to a (SERINE/THREONINE-PROTEIN KINASE YKL101W PROBABLE ATP-BINDING TRANSFERASE) protein domain (PD095148) which is seen in KKK1_YEAST.Residues 68-227 are 42% similar to a (YARROWIA LIPOLYTICA STRAIN C CLIB99 CHROMOSOME) protein domain (PD950595) which is seen in Q6CAU2_EEEEE.Residues 72-228 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD498679) which is seen in Q8Z111_SALTI.Residues 73-199 are 50% similar to a (CG17698-PA) protein domain (PD980872) which is seen in Q7PLK3_DROME.Residues 74-229 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING KINASE-LIKE) protein domain (PDA198D0) which is seen in Q8S1B9_EEEEE.Residues 76-276 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN MAP TRANSFERASE ATP-BINDING) protein domain (PD324666) which is seen in Q9N9B1_LEIMA.Residues 76-228 are 52% similar to a (KINASE CBS138 CANDIDA SEQUENCE K SERINE/THREONINE-PROTEIN GLABRATA STRAIN ATP-BINDING TRANSFERASE) protein domain (PD957660) which is seen in Q6FMF3_EEEEE.Residues 92-276 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING MAP) protein domain (PDA18314) which is seen in Q93WR7_MEDVA.Residues 97-276 are 40% similar to a (KINASE SER/THR P08458 SPS1 CEREVISIAE YDR523C SACCHAROMYCES) protein domain (PDA0B8H6) which is seen in Q6C9X8_EEEEE.Residues 99-384 are 45% similar to a () protein domain (PD743406) which is seen in Q8G5T5_BIFLO.Residues 99-276 are 44% similar to a (AFR724CP ATP-BINDING) protein domain (PDA101P3) which is seen in Q751V1_ASHGO.Residues 105-292 are 39% similar to a (KINASE LIKE NEUROSPORA RELATED STE20- B16M17.090 Q871H9 DON3 CRASSA) protein domain (PDA064R7) which is seen in Q6C8H9_EEEEE.Residues 105-276 are 42% similar to a (KINASE STRESS-RESPONSIVE PRKSD ATP-BINDING) protein domain (PD087289) which is seen in O62571_SUBDO.Residues 105-228 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE CAMP ATP-BINDING CAMP-DEPENDENT NUCLEAR) protein domain (PD061517) which is seen in O00843_PARPR.Residues 105-228 are 52% similar to a (CELL DIVISION SERINE/THREONINE-PROTEIN CONTROL KINASE CYCLE TRANSFERASE 2.7.1.- MITOSIS ATP-BINDING) protein domain (PDA0F8T7) which is seen in CC15_YEAST.Residues 105-228 are 47% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE APOPTOSIS HIPPO ATP-BINDING) protein domain (PD727337) which is seen in HPO_DROME.Residues 105-228 are 52% similar to a (KINASE P27636 SERINE/THREONINE-PROTEIN TRANSFERASE CDC15 CEREVISIAE ATP-BINDING SACCHAROMYCES YAR019C) protein domain (PDA0F8T8) which is seen in Q6FWK3_EEEEE.Residues 105-276 are 43% similar to a (KINASE STE20-LIKE ATP-BINDING DON3) protein domain (PD609771) which is seen in Q8NJX3_USTMA.Residues 106-276 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING MAP) protein domain (PD290024) which is seen in Q9P8J0_PNECA.Residues 109-241 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING PENTATRICOPEPTIDE REPEAT-CONTAINING PPR) protein domain (PDA18435) which is seen in Q7XB71_EEEEE.Residues 119-228 are 45% similar to a (KINASE TYROSINE-PROTEIN TRANSFERASE C03B1.5 ATP-BINDING X CHROMOSOME) protein domain (PD092556) which is seen in YX05_CAEEL.Residues 137-290 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING PPKA) protein domain (PDA1D587) which is seen in Q7UMX3_RHOBA.Residues 140-278 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE POSSIBLE CDC2-RELATED ATP-BINDING) protein domain (PD263960) which is seen in Q9U124_LEIMA.Residues 149-276 are 50% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN ANK ATP-BINDING TRANSFERASE GLP_39_28978_30531) protein domain (PD959207) which is seen in Q7R3P5_EEEEE.","","-49% similar to PDB:1MRU Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB. (E_value = 6.9E_23);-49% similar to PDB:1O6Y CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 6.9E_23);-49% similar to PDB:2FUM Catalytic domain of protein kinase PknB from Mycobacterium tuberculosis in complex with mitoxantrone (E_value = 6.9E_23);-49% similar to PDB:2H34 Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE (E_value = 5.5E_20);-49% similar to PDB:2BVA CRYSTAL STRUCTURE OF THE HUMAN P21-ACTIVATED KINASE 4 (E_value = 1.2E_19);","Residues 30 to 289 (E_value = 2.4e-43) place ANA_0831 in the Pkinase family which is described as Protein kinase domain.Residues 30 to 116 (E_value = 8.6e-11) place ANA_0831 in the Pkinase_Tyr family which is described as Protein tyrosine kinase.","","protein kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0832","891036","890263","774","5.60","-9.42","28574","GTGACGATCCTTGCGTTGCACGAGTGGGGCGACCCGACGGATCCGCCGCTGCTCTTAGTCCACGGCCTGACTGAATCAGCTACCGCCTGGCCGGATGCCGTAGCCCGCTGGTCCTCCCAGTATCACGTCCTCGCGATCGATCAGCGGGGACACGGGGCATCCCCGCGGTGGGACGATGAGGCCCTGGCTCGGGCGCCGCAGACGATGCACGAGGACCTTACGAGGACATTGGCCCTGTTCCCGGAGCCGCCGGTCGTCGTGGCGCACAGTCTGGGTGGGCTCATATCGCTGCGGGTGAGTGTCGCCCGGCCCGAGCTCGTTCGGGCCCTGGTCCTGGAGGACGCCGCGCGTCCCACCGGGCACTGGGCTCCGGCCCCCTGGTTCGTGGAGCATCAGGAGCACTTCCTGGACGCCTTCGCCGACGGCGGCACGGCCGAGCGGGAACGCATGAGGCGCGAGACCTCATGGACCGAGTCCGAGATCGAGGCCTGGGCCGCGTGCAAGAGGCAGGTCGACCGCCGTTACATCCGCGAAGGTACCTATCTCGGCGAGGCCGACCTCGTCAGCGCGATCAACCGGCTGAGGACGCCGACGCTCTACCTGGCGCCCCGCCGCGGTGAGATGGCTCCTGACCCCTCTGAGGTGAGCAATCCGCTCGTACGTTTGGTGCTGCTCGACGGCGTCGGCCACTGCGTGCGGAGGGACGCCCCGGAGGCCTACCACGGGCTGGTCGATCCCTTCATCGAGGAAGTTTTCGCCGGCGCCGGCCGGTGA","VTILALHEWGDPTDPPLLLVHGLTESATAWPDAVARWSSQYHVLAIDQRGHGASPRWDDEALARAPQTMHEDLTRTLALFPEPPVVVAHSLGGLISLRVSVARPELVRALVLEDAARPTGHWAPAPWFVEHQEHFLDAFADGGTAERERMRRETSWTESEIEAWAACKRQVDRRYIREGTYLGEADLVSAINRLRTPTLYLAPRRGEMAPDPSEVSNPLVRLVLLDGVGHCVRRDAPEAYHGLVDPFIEEVFAGAGR$","Alpha/beta hydrolase","Cytoplasm, Extracellular","hydrolase, alpha/beta hydrolase fold family","alpha/beta hydrolase fold","alpha/beta hydrolase fold","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[41-151]T$	Abhydrolase_1

InterPro
IPR003089
Family

Alpha/beta hydrolase
PR00111	$\"[40-55]T$ $\"[86-99]T$ $\"[100-113]T$	ABHYDROLASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[4-250]T$	no description
PTHR10992	$\"[4-249]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF17	$\"[4-249]T$	VALACYCLOVIR HYDROLASE

","BeTs to 15 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","***** IPB000639 (Epoxide hydrolase signature) with a combined E-value of 2.1e-15. IPB000639B 40-55 IPB000639C 86-99 IPB000639D 100-113 IPB000639F 225-247***** IPB003089 (Alpha/beta hydrolase fold signature) with a combined E-value of 3.9e-14. IPB003089A 40-55 IPB003089B 86-99 IPB003089C 100-113***** IPB002410 (Prolyl aminopeptidase (S33) family signature) with a combined E-value of 1.5e-06. IPB002410B 43-54 IPB002410C 86-100***** IPB000073 (Alpha/beta hydrolase fold) with a combined E-value of 2.8e-06. IPB000073A 44-54 IPB000073B 86-93","Residues 4-251 are 39% similar to a (LIPA LIPASE) protein domain (PD758064) which is seen in Q8KU34_LEGPN.Residues 4-115 are 52% similar to a (HYDROLASE ACYLTRANSFERASE OR TRANSFERASE) protein domain (PD500542) which is seen in Q8ZM62_SALTY.Residues 4-123 are 49% similar to a (HYDROLASE ALPHA/BETA FOLD HYDROLASE FAMILY) protein domain (PD461356) which is seen in Q9ABK4_CAUCR.Residues 4-115 are 51% similar to a (HYDROLASE ALPHA/BETA ENOL-LACTONE FOLD PEROXIDASE HYDROLASE FAMILY AMINOPEPTIDASE 3-OXOADIPATE BETA-KETOADIPATE) protein domain (PD036710) which is seen in Q82QI7_STRAW.Residues 13-123 are 51% similar to a (ALL2068) protein domain (PD609925) which is seen in Q8YVB3_ANASP.Residues 13-166 are 45% similar to a (HYDROLASE EPOXIDE) protein domain (PD635005) which is seen in Q82LA6_STRAW.Residues 15-166 are 44% similar to a (HYDROLASE EPOXIDE) protein domain (PD380309) which is seen in Q9XA39_STRCO.Residues 15-118 are 51% similar to a (HYDROLASE PROBABLE 3.-.-.-) protein domain (PD525401) which is seen in Q8XYI8_RALSO.Residues 16-124 are 47% similar to a (HYDROLASE) protein domain (PD732145) which is seen in Q826V8_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 41 to 246 (E_value = 0.00016) place ANA_0832 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","alpha-beta hydrolase fold family (est)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0833","892981","891188","1794","4.99","-25.68","65170","GTGCTGCGAACCCGAACCGCAGGCTCCCTGCGCGCCTCAGACATCGGCCAGGTCGTCACCCTCACCGGATGGGTGGATCGACGTCGTGACCACGGAGGCGTGGCCTTCATCGACTTGCGGGACGCCTCGGGCATCGCCCAGGTCGTCATCCGCGAGGAGATCGCCCACGACCTGCGCGCCGAGTACGTCCTGGCCGTCACCGGGGAGGTGAGCGCCAGGCCCGAGGGCAACGCCAACCCGAACCTGCCCACCGGCGAGATCGAGGTCGTCGTCTCCGACGTCGAGATTCTCAACGCCTCCGCGCCGCTGCCCTTCCAGGTCTCCGACCACGCTGAGGACGCCGGACAGGTCGGCGAGGAGGCGCGCCTGCGCTACCGCTACCTCGACCTGCGACGCAGCGCCATGCAGCACGCCATCCGCCTTCGCGCCAAGGTCAGCCAGGCCGCCCGCAGGGTCCTGGACTCCCACGACTTCGTGGAGATCGAGACCCCCACCCTGACCCGCTCCACCCCGGAGGGCGCCCGCGACTTCCTGGTCCCGGCTCGACTGGCACCGGGCTCCTGGTACGCCCTGCCGCAGAGCCCGCAGCTGTTCAAACAGCTCCTCATGGTCGCCGGCATGGAGCGCTACTACCAGATCGCCCGCTGCTACCGCGATGAGGACTTCCGCGCCGACCGCCAGCCCGAGTTCACCCAGCTCGACGTGGAGATGAGCTTCGTCGAGCAGGACGACGTCATCGCCGTCGCCGAGGACGTACTGCGCGAGGTGTGGGCGCTCATCGACTACGAGCTGCCCACTCCCATCGCCCGCATGACCTACCACGACGCCATGGAGAAGTACGGCTCGGACAAGCCCGACCTGCGCTTCGGCTGCGAGCTGGTGGACCTGACCGACTACTTCAAGGACACCACCTTCCGAGTCTTCCAGAACCCCTACGTGGGCGCCGTCGTCATGCCCGGCGGGGCCTCCCAGTCCCGCCGTACCTTCGACGCCTGGCAGGAGTGGGCCAAGCAGCGCGGCGCCAAGGGCCTGGCCTACGTCACCGTCGCCGAGGACGGGACCCTCGGCGGGCCCGTCGCCAAGAACATCACCGACGCCGAGCGCGAGGGCCTGGCCCAGGCCGCCGGCGCCGCGCCCGGCGACTGCATCTTCTTCGCCGCCGGTCCCGTGGACTCCTCGCGCGCCCTGCTGGGCGCCGCCCGCCTGGAGATCGGCAAGCGCTGCGGCCTCATCGACGACAACGAGTGGTCCTTCGTCTGGGTCGTGGACGCCCCCCTGTTCAAGCCCTCCGCCGAGGCCAAGGCCGACGGCGACGTGGCCCTGGGAAAGTCCGCCTGGACCGCGGTCCACCACGCCTTCACCTCGCCCAAGCCCGAGTGCCTGGAGACCTTCGACACCGACCCGGCAAGCGCCCTGGCCTACGCCTACGACATCGTCTGCAACGGCAACGAGATCGGCGGCGGCTCCATCCGTATCCACCGCAGCGACGTCCAGGAGCGCGTCTTCAACGTCATGGGAATCGGCGAGCAGGAGGCCCAGGAGAAGTTCGGCTTCCTGCTGGACGCCTTCAAGTTCGGTGCCCCGCCGCACGGCGGCATCGCCTTCGGCTGGGACCGCATCGTCTCCCTGCTGACCAAGGCCGACTCCATCCGCGACGTCATCGCCTTCCCCAAGTCAGGTGGCGGCTTCGACCCGCTGACCGAGGCGCCCGCCCCGATCACGCCCGAGCAGCGCAAGGAGGCCGGGGTCGACGCCGTCCCGGACAACGACTCCGGCTCTGCGGCGCAGGGCTAA","VLRTRTAGSLRASDIGQVVTLTGWVDRRRDHGGVAFIDLRDASGIAQVVIREEIAHDLRAEYVLAVTGEVSARPEGNANPNLPTGEIEVVVSDVEILNASAPLPFQVSDHAEDAGQVGEEARLRYRYLDLRRSAMQHAIRLRAKVSQAARRVLDSHDFVEIETPTLTRSTPEGARDFLVPARLAPGSWYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVEQDDVIAVAEDVLREVWALIDYELPTPIARMTYHDAMEKYGSDKPDLRFGCELVDLTDYFKDTTFRVFQNPYVGAVVMPGGASQSRRTFDAWQEWAKQRGAKGLAYVTVAEDGTLGGPVAKNITDAEREGLAQAAGAAPGDCIFFAAGPVDSSRALLGAARLEIGKRCGLIDDNEWSFVWVVDAPLFKPSAEAKADGDVALGKSAWTAVHHAFTSPKPECLETFDTDPASALAYAYDIVCNGNEIGGGSIRIHRSDVQERVFNVMGIGEQEAQEKFGFLLDAFKFGAPPHGGIAFGWDRIVSLLTKADSIRDVIAFPKSGGGFDPLTEAPAPITPEQRKEAGVDAVPDNDSGSAAQG$","Aspartyl-tRNA synthetase","Cytoplasm","aspartyl-tRNA synthetase","aspartyl-tRNA synthetase ","aspartyl-tRNA synthetase","","Koonin E.V., Wolf Y.I., Aravind L. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 2000. 54:245-275. PMID: 10829230Keshav K.F., Chen C., Dutta A. Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. Mol. Cell. Biol. 1995. 15(6):3119-3128. PMID: 7760808Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 1997. 385(6612):176-181. PMID: 8990123","","","

InterPro
IPR002312
Family

Aspartyl-tRNA synthetase, class IIb
PR01042	$\"[191-203]T$ $\"[208-221]T$ $\"[476-492]T$ $\"[520-534]T$	TRNASYNTHASP

InterPro
IPR004115
Domain

GAD
PF02938	$\"[308-397]T$	GAD

InterPro
IPR004364
Domain

tRNA synthetase, class II (D, K and N)
PF00152	$\"[118-561]T$	tRNA-synt_2

InterPro
IPR004365
Domain

Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336	$\"[19-97]T$	tRNA_anti

InterPro
IPR004524
Family

Aspartyl-tRNA synthetase bacterial/mitochondrial type
PTHR22594:SF5	$\"[84-588]T$	ASPARTYL-TRNA SYNTHETASE
TIGR00459	$\"[1-590]T$	aspS_bact: aspartyl-tRNA synthetase

InterPro
IPR006195
Domain

Aminoacyl-transfer RNA synthetase, class II
PS50862	$\"[139-565]T$	AA_TRNA_LIGASE_II

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[1-103]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[132-588]T$	no description
PTHR22594	$\"[84-588]T$	ASPARTYL/LYSYL-TRNA SYNTHETASE

","BeTs to 19 clades of COG0173COG name: Aspartyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0173 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB004115 (GAD domain) with a combined E-value of 3.3e-204. IPB004115A 23-48 IPB004115B 55-89 IPB004115C 122-132 IPB004115D 158-212 IPB004115E 216-250 IPB004115F 279-293 IPB004115G 419-428 IPB004115H 448-457 IPB004115I 476-493 IPB004115J 514-559***** IPB002312 (Aspartyl-tRNA synthetase signature) with a combined E-value of 3.3e-34. IPB002312A 191-203 IPB002312B 208-221 IPB002312C 476-492 IPB002312D 520-534***** IPB004364 (tRNA synthetase, class II (D, K and N)) with a combined E-value of 4.5e-23. IPB004364 519-557***** IPB002313 (Lysyl-tRNA synthetase signature) with a combined E-value of 6.3e-06. IPB002313A 154-164 IPB002313C 199-212 IPB002313D 217-234","Residues 2-49 are 77% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ASPARTYL-TRNA ASPARTATE--TRNA ASPRS METAL-BINDING MAGNESIUM) protein domain (PD600281) which is seen in SYD_ANASP.Residues 3-102 are 53% similar to a (BIOSYNTHESIS CG31739-PA SYNTHETASE SD02215P AMINOACYL-TRNA LIGASE ATP-BINDING) protein domain (PD753799) which is seen in Q9VJH2_DROME.Residues 58-121 are 78% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ASPARTYL-TRNA ASPARTATE--TRNA ASPRS METAL-BINDING MAGNESIUM) protein domain (PD280604) which is seen in Q6A8J1_PROAC.Residues 139-170 are 90% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS LYSYL-TRNA ASPARTYL-TRNA LYSINE--TRNA LYSRS ASPARTATE--TRNA) protein domain (PD190154) which is seen in Q741M7_MYCPA.Residues 174-221 are 85% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ASPARTYL-TRNA LYSYL-TRNA ASPARTATE--TRNA METAL-BINDING MAGNESIUM) protein domain (PD000871) which is seen in SYD1_STRMU.Residues 222-277 are 87% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ASPARTYL-TRNA ASPRS ASPARTATE--TRNA ASPS FLJ10514) protein domain (PD110933) which is seen in SYD_MYCTU.Residues 228-271 are 88% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS LYSYL-TRNA METAL-BINDING MAGNESIUM LYSINE--TRNA ASPARAGINYL-TRNA) protein domain (PD381293) which is seen in Q6NGZ4_CORDI.Residues 280-388 are 51% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ASPARTYL-TRNA ASPRS ASPARTATE--TRNA ASPARTATE-TRNA) protein domain (PD858146) which is seen in Q6N5D6_RHOPA.Residues 298-410 are similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ASPARTYL-TRNA ASPARTATE--TRNA ASPRS 3D-STRUCTURE PROBABLE) protein domain (PD037346) which is seen in SYD_MYCTU.Residues 401-487 are 62% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ASPARTYL-TRNA ASPARTATE--TRNA ASPRS MSD1 CEREVISIAE) protein domain (PD110935) which is seen in SYD_PORGI.Residues 488-522 are 94% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BIOSYNTHESIS ATP-BINDING ASPARTYL-TRNA ASPARTATE--TRNA ASPRS ASPS 3D-STRUCTURE) protein domain (PD206474) which is seen in Q6A8J1_PROAC.Residues 523-558 are 88% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS LYSYL-TRNA ASPARTYL-TRNA ASPARTATE--TRNA METAL-BINDING MAGNESIUM) protein domain (PD000848) which is seen in SYD_CORGL.","","-64% similar to PDB:1EFW CRYSTAL STRUCTURE OF ASPARTYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED TO TRNAASP FROM ESCHERICHIA COLI (E_value = 3.7E_145);-64% similar to PDB:1G51 ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION (E_value = 3.7E_145);-64% similar to PDB:1L0W Aspartyl-tRNA synthetase-1 from space-grown crystals (E_value = 3.7E_145);-60% similar to PDB:1C0A CRYSTAL STRUCTURE OF THE E. COLI ASPARTYL-TRNA SYNTHETASE : TRNAASP : ASPARTYL-ADENYLATE COMPLEX (E_value = 2.7E_140);-60% similar to PDB:1EQR CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI (E_value = 2.7E_140);","Residues 19 to 97 (E_value = 7.3e-27) place ANA_0833 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.Residues 118 to 561 (E_value = 1.6e-208) place ANA_0833 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N).Residues 141 to 280 (E_value = 0.0056) place ANA_0833 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T).Residues 308 to 397 (E_value = 4.1e-33) place ANA_0833 in the GAD family which is described as GAD domain.","","synthetase (aspS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0834","893882","893088","795","10.23","10.33","27491","ATGATCCGGACGTCCCGGACAGTTGAGCGCGTACGGCGTGATCGACGTCCTGCACTGGCTCGGCATCGGATCGGCGTGAGGTGCCTCCAGGGATCACCGCGGATGCTCGTCATCGTCTGCTCCGTCCTCCTCGCCTGCCTGGTGGCGGTGGTCTCCACGAGCCCCGTCGCCAGCGCGGACACCAAGACCGGTCCCTCCACCACCGGAACCGCCTCAACGGTCAGCCCCTCGACGGTCGCCGTCGGAGGAACGATCATGTACACGCTCTCAGGATTCCCCAGTGATGTGACGGTCCAGGTCCTCGTCGACGACGGCGCGCTGGTCGCCTCGCGACCCTCGGAGTCCGAGGTGGTCACCACGATCACCGTCAAGAAGGACGGCACCGCCGCAGGCTCCTTCGAGCTTCCCGAGTACGTCGAGCAGGGAAACCACTGGCTGCGATTCCGGGTCGTCGGGGCTCAGGGGGAGAGCGGCCAGGAGGGCGACGCGGCGGACTACACCAACAAGAGCCCCTACTTCACAGTATCGGGTGTCACGGTCATCGGTGGGTCCGCCCCTCCCACCGTTCCGCCGGCTCCCACGCCGCCGCCCCGCCAGGTCACGACCATGGGGCGGTCCAACGCGGCCGCCGCCTCCGGCATCCAGGCCGCGGGGCCGGGTCGGGAGTCGACTGGTTTCCCGATTATCGGTGCCTTCGTCCTCGGGCTCAGCGTGATCCTGGTCGTTCTGTCGGTACTCGTGGCGATCAACCGTCGCAGGATGGCTGCCTACCAACGTCGTCGGGCCATGGCCTGA","MIRTSRTVERVRRDRRPALARHRIGVRCLQGSPRMLVIVCSVLLACLVAVVSTSPVASADTKTGPSTTGTASTVSPSTVAVGGTIMYTLSGFPSDVTVQVLVDDGALVASRPSESEVVTTITVKKDGTAAGSFELPEYVEQGNHWLRFRVVGAQGESGQEGDAADYTNKSPYFTVSGVTVIGGSAPPTVPPAPTPPPRQVTTMGRSNAAAASGIQAAGPGRESTGFPIIGAFVLGLSVILVVLSVLVAINRRRMAAYQRRRAMA$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-53]?$	signal-peptide
tmhmm	$\"[36-56]?$ $\"[229-249]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-43% similar to PDB:1BS0 PLP-DEPENDENT ACYL-COA SYNTHASE (E_value = );-43% similar to PDB:1DJ9 CRYSTAL STRUCTURE OF 8-AMINO-7-OXONANOATE SYNTHASE (OR 7-KETO-8AMINIPELARGONATE OR KAPA SYNTHASE) COMPLEXED WITH PLP AND THE PRODUCT 8(S)-AMINO-7-OXONANONOATE (OR KAPA). THE ENZYME OF BIOTIN BIOSYNTHETIC PATHWAY. (E_value = );-43% similar to PDB:1DJE CRYSTAL STRUCTURE OF THE PLP-BOUND FORM OF 8-AMINO-7-OXONANOATE SYNTHASE (E_value = );-43% similar to PDB:2G6W Suicide inhibition of a-Oxamine Synthase: Structures of the Covalent Adducts of 8-Amino-7-oxonanoate Synthase with trifluoroalanine (E_value = );-54% similar to PDB:1GA1 CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF IODOTYROSTATIN (THIS ENZYME RENAMED \"SEDOLISIN\" IN 2003) (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0835","896469","893959","2511","4.77","-28.38","83811","ATGCAATATGCTCAGCGGCTGCTTGCCACCCTCCCTGTGACCAGGGCGGGCCTGCGCGCGATTCTTGCTGTTCTGACAGCCTTCGGCATTGTTCTGGCCACCGCCGGTGTGGCCGCCATGCCCCTCCTGAATGCAGGCAATGTCGTTGAGGACTATGAGAGCGGCTCGGCCTGCCACCCTATCGCCAGAATGGTCTACCCTGAGGGGCAGTCGGCACCCGAGTACGTAATGCCGGTCTATGAGACCGGATTCGGTGTGGGGGTCGATTCGGTCCTGTTGAGCTGGTGCAGTACCGCAGGGGAGGTCCTGGAGGACCCCACCATCACGCTCAACGTCGTCGAGGGGAAGAACGTCACTCCTTACCTGCTTCCTGGCATCAAGGCCGAGCTCGAGCGTCCCGCTCCCGCCAACGGCAAGCAGGAGGTATTCATCCCAACGGACTACCTCGTCAAGGGGATGCGTCAGGCCACCGGTGATAGTGGCTGGGAGGTCGGTACGAAGGTCTTCAGCCTTACATACACCAGTGGAACGGTGAGTGCGACGACGGGCCTGTTCTCCTTCGTCAAGCAGGACCCGAATGTCATCAACCCTCCGACCCCCGAGCCGACGCCGGAGCCGACTGCCGAACCCTCTGCGGAGCCCACCGCAGAACCGACGGCGGAGCCCACCGCGCAGCCGACTGCCGAACCCTCTGCGGAGCCCACCGCAGAACCGAGCGCTGCACCCGGTCCGGTGCCGACTGCTGAACCGACGACTGCACCCACTGCGGAACCGGCTCCTGATGCCACGACTGAGCCGTCGCCGACACCCTCGGCAACTCCCTCACCGACTCCTTCCGGGTCCCCCAGCCCGTCGGCATCCCCGTCACCGAGTCCCTCCGCGGCACCCAGCCCGACGGCGAGTCCTTCCGCGACTGCCTCACCCAGCTCATCGCCCTCGCCTTTAAGGTCTCCCAAGCCCAAACCGACCGCCTCTGCCCAGCCGAGTGCCTCCCCGAGTGCCACCGTCAAGACATGCCAGGTCAAGCCCGCCATCCAGGTGCTCGGCTCCGATGGCTCCGACCCCCAGGGGAGCGAGCCCACCTATGACCCGGAGACCGCCGTCAGGGTCCGCGGTACGGGCTGGTGCTCCCAGGGGGAGATGCTCGACGGCGACAAGCCGGTCGAGATCAAGGTGGCGGCCTACGGCGGATACGTGGTTCCGGGAACGCTCTCGGTTCCCGTCACCTTCCATCACGGGTCTTTCGAGGCTCAGCTCAACCTGTCGGCCCTCTACACCGGGGGGAACGTGGACAAGGGCCGCTACTACCTGCAGCTCTCGCCCATCGATTCCGGGCTGACCGCCGCCACCAACATCTTCGCCCTCAACAAGGCCGTCGCCCCACAGCCCAAGCCGTCCCCCGCGCCGAGCCCGGCTCCTACCGCGACCGCGGAGCCCTCGGCCACTGCGGAGCCCACCAGCGAACCCGCACCGGAGCCGACGGGTTCGCCCGCCAGCCCTGGTCCCACACCCTCCGCTGCGCCGTCGTCGCAGCCCTCCGCCTCGGCGGTCCCCTCGGCCCGCCCCTCCGAGTCGGCGTCCGCGGCTCCCGCACCGCAGACCACCGAACCCGATCAGAACGCTCCGAAACCGAACCCGGATGGCGGACGTCCCGGAACGGACAACGCCCCCGGCAACAACCCAGGTGGTGACTCGGGTAACTCGGGCGACACAAGCAACTCTGGCGACCATGGCTCCGGCGCGGGTACAGACACAGGCGGCCAGGCCGACTCCTCCGCGCCGCAGGGACCCGGTGCCGGATCGGAGACCGGCTCCTCGACCTCCCAGGACGGCTCCGCCCAGCAGCATGCGAACGCAGGAGGCGCGCCTGCCCCGAACGCCGGAGGCTCAGGAGGCGAGAACGCCCATGCCTCTGAAGGCTCCGCGGCCTCGGCGCAGACCTCGTCTGAGGCTGACACGGCCTCTCAGCGTACCGTTCGTCCCGACCGGAGCCCGGTGGCCCCGGTGACCAGCGCGGCTCACCTGAGTGCGGAAAACGCCGGCTCCCTGTCCGGCTCCCGCCAGGGCAACGTCGTCAACCTCGTCCTGCCTAAGTCCAAGGCGCAAGCGGGCGAGTGGGTCTCGGTGTTCGTCTTCCCCGGAGCCACCACCAAGGGCTGGGTGCAGGTTGATTCCGCCAACAGCGTCTCCATCGACATCTCAACCTTCGACTCCGGCTCCTACGAGCTGGCGGTGGCCGATCGTGACAACAGCCTCCTGGGGTGGGCGAAGCTGGAGATCTCCTCAGCCTCCTCCGACCCTCGCAGTCCGGCCCAGGCTCAGCTGCTGACCTTCCCGGATAACGTGGCTGAGCCCACCAAGAAGGGCCTCAGTGCCAACGACATGCTCCTGGGAAGCGCTGGAGGACTGCTGGTCGTCGGAGCCGTGAGCCTGCTGGTCGCAGCGTTCTCAGGGATGCCGCTGCGTGCACCACGGACCTCCCCGCGGCTGCGGCTTCCGCGCAGGCGCTGA","MQYAQRLLATLPVTRAGLRAILAVLTAFGIVLATAGVAAMPLLNAGNVVEDYESGSACHPIARMVYPEGQSAPEYVMPVYETGFGVGVDSVLLSWCSTAGEVLEDPTITLNVVEGKNVTPYLLPGIKAELERPAPANGKQEVFIPTDYLVKGMRQATGDSGWEVGTKVFSLTYTSGTVSATTGLFSFVKQDPNVINPPTPEPTPEPTAEPSAEPTAEPTAEPTAQPTAEPSAEPTAEPSAAPGPVPTAEPTTAPTAEPAPDATTEPSPTPSATPSPTPSGSPSPSASPSPSPSAAPSPTASPSATASPSSSPSPLRSPKPKPTASAQPSASPSATVKTCQVKPAIQVLGSDGSDPQGSEPTYDPETAVRVRGTGWCSQGEMLDGDKPVEIKVAAYGGYVVPGTLSVPVTFHHGSFEAQLNLSALYTGGNVDKGRYYLQLSPIDSGLTAATNIFALNKAVAPQPKPSPAPSPAPTATAEPSATAEPTSEPAPEPTGSPASPGPTPSAAPSSQPSASAVPSARPSESASAAPAPQTTEPDQNAPKPNPDGGRPGTDNAPGNNPGGDSGNSGDTSNSGDHGSGAGTDTGGQADSSAPQGPGAGSETGSSTSQDGSAQQHANAGGAPAPNAGGSGGENAHASEGSAASAQTSSEADTASQRTVRPDRSPVAPVTSAAHLSAENAGSLSGSRQGNVVNLVLPKSKAQAGEWVSVFVFPGATTKGWVQVDSANSVSIDISTFDSGSYELAVADRDNSLLGWAKLEISSASSDPRSPAQAQLLTFPDNVAEPTKKGLSANDMLLGSAGGLLVVGAVSLLVAAFSGMPLRAPRTSPRLRLPRRR$","PT repeat-containing protein","Extracellular, Periplasm, Cellwall","PT repeat family","hypothetical protein predicted by Glimmer/Critica","PT repeat-containing protein","","","","","

InterPro
IPR006970
Repeat

PT repeat
PF04886	$\"[198-224]T$ $\"[225-260]T$ $\"[492-524]T$	PT

noIPR
unintegrated

unintegrated
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[796-816]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB006706 (Extensin-like region) with a combined E-value of 2.4e-07. IPB006706A 251-293 IPB006706B 298-335 IPB006706B 270-307 IPB006706B 278-315 IPB006706B 261-298***** IPB001359 (Synapsin) with a combined E-value of 1.9e-06. IPB001359H 262-312 IPB001359H 278-328 IPB001359H 276-326 IPB001359H 268-318 IPB001359H 270-320 IPB001359H 258-308 IPB001359H 465-515 IPB001359H 264-314 IPB001359H 282-332 IPB001359H 492-542 IPB001359H 266-316 IPB001359H 272-322 IPB001359H 459-509 IPB001359H 274-324 IPB001359H 488-538","Residues 444-773 are similar to a (SURFACE ANCHOR WALL FAMILY CELL) protein domain (PD579361) which is seen in Q97P71_STRPN.","","-47% similar to PDB:1F0N MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85B (E_value = );-47% similar to PDB:1F0P MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85B WITH TREHALOSE (E_value = );-43% similar to PDB:1X8M X-ray structure of pectin degrading enzyme 5-keto 4-deoxyuronate isomerase from Escherichia coli (E_value = );-43% similar to PDB:1XRU Crystal Structure of 5-keto-4-deoxyuronate Isomerase from Eschericia coli (E_value = );-45% similar to PDB:1SFR Crystal Structure of the Mycobacterium tuberculosis Antigen 85A Protein (E_value = );","Residues 192 to 224 (E_value = 0.0036) place ANA_0835 in the PT family which is described as PT repeat.Residues 225 to 260 (E_value = 0.00062) place ANA_0835 in the PT family which is described as PT repeat.Residues 492 to 524 (E_value = 524) place ANA_0835 in the PT family which is described as PT repeat.","","repeat family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0836","898312","896879","1434","6.98","-0.22","52518","GTGCCGCAGGCACGGTGGAGACAGCTGGCCGCGACTCCTGTGGCCCAGGACGGTGGCCCGCTTCGCATCACCCCGGCGTGGTGGCCTCCGGTTCCTGACGATTCAGCCTTGGCCGCTGCCGCGGTGCACGGCACTCCCGTCCTGGGGGAGGGACACATCATCAACGGGGTTGAGATGGTGGAGGCGAGCTTCCTGTGGCGTGATGACCACCGGCACGGCGCCAGCCCCAGTGTTCTCATCCATCTCAATACCCTGACCGACAACCATCGCGCTCACATCGCGCCGGCACTGGCCGCCCGGGTTCCCGGGACCAGCTGGTGGGCGCTTCACGTCCTGCTGCCGCAGGATGCGCTCTTGAGCTACCGGATCGTTGTGACTCATGACGCCCTGCCTGACGATGCCGGGGCCCGACGCGAGTGCTGGAAGCGCGTTCACGCACTGGGACGGCCCGATCCCCTCAATCCCGACCGGCTGCATGACGGCTTCGGTCTGGTGTCCTCGCTATGGGCGGGCCCCAAGGCCATGCTGCACCCGGATTGGATGATCGGCTTGGGTGCTTCGGCAGAGGGGGCGTGGCAGGCGCTGAGCCGTCCCCAGGATGAACACGACAGGTACGTCCTCCGGTTCGACCTGGCGAACGAGGTGCTCACAGACTTTGATGAGCCGGTAGACCCCGGACGGCGAGTCACACTGTGGTGCGGGGGCCGTGTCCAGGAGGGCTCCTGCGGGCACAGTGAGCGGGGTCTGCTGATCCTGCTCGACGGAAACATCTGGCGTGGTAACCATGCCGTCGATCACCTGGCCCCCAGATCCCGCCAATGGGATGTGCTGCTCATCGACTCCGGCAGCCTGGCCATGCGCTCACGCGACCTGGGGGATCCGCGACGCAGCAGAGAACTGCTCCGTAGGTGTCTGCAGGCGGCACATCGGGCCGTCTGCGGACGAGGCTGCAGGATAGCTGTGTCCTCTGAGGATGGTGCTGGTTGCATGTGGCGCCCGGATCGGACCGTGGTGGCTGGGCAGTCTTTGGGAGGGGTTGCTGCGGCCGACCTGGTTCTGCGTCATCCCGAGCTGGCTACTCGTGCCATTGTCCAGTCCGGATCCTTCTGGCTCGGCTCTCAGCGCCGAGGCGAGGGTGAAGGGGAGCTGCTGCGCTGGTTGCGTCACCGCTCCGAGGCCCGGAGCCTGCAACGCCCAAGAAGCGACCAGCATCCTCATGATGGTCAGGGGCTGGGGGCGCGACTGGTGGTCCAGTGCGGGGTCCATGAAGACGGCCTGCGTCAGGGGGCTCGCACCGTCTCAGAGCTTCTTGGGGTCGAAGGAGCGCTGCTCGAGTATCGCGAGGAGCGAGGAGGGCACGACTACGCCTGGTGGCGTCATGCCTTGTCCTGGGGGCTTGACGCTCATGAGCAGGACCTGGGGTCCTGCTCATGA","VPQARWRQLAATPVAQDGGPLRITPAWWPPVPDDSALAAAAVHGTPVLGEGHIINGVEMVEASFLWRDDHRHGASPSVLIHLNTLTDNHRAHIAPALAARVPGTSWWALHVLLPQDALLSYRIVVTHDALPDDAGARRECWKRVHALGRPDPLNPDRLHDGFGLVSSLWAGPKAMLHPDWMIGLGASAEGAWQALSRPQDEHDRYVLRFDLANEVLTDFDEPVDPGRRVTLWCGGRVQEGSCGHSERGLLILLDGNIWRGNHAVDHLAPRSRQWDVLLIDSGSLAMRSRDLGDPRRSRELLRRCLQAAHRAVCGRGCRIAVSSEDGAGCMWRPDRTVVAGQSLGGVAAADLVLRHPELATRAIVQSGSFWLGSQRRGEGEGELLRWLRHRSEARSLQRPRSDQHPHDGQGLGARLVVQCGVHEDGLRQGARTVSELLGVEGALLEYREERGGHDYAWWRHALSWGLDAHEQDLGSCS$","Enterochelin esterase","Cytoplasm","enterochelin esterase, putative","enterochelin esterase","putative esterase","","","","","

InterPro
IPR000801
Family

Putative esterase
PF00756	$\"[222-469]T$	Esterase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[333-468]T$	no description
PTHR10907	$\"[332-407]T$	ESTERASE-RELATED
PTHR10907:SF2	$\"[332-407]T$	ENTEROCHELIN ESTERASE

","BeTs to 3 clades of COG2382COG name: Enterochelin esterase and related enzymesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2382 is ---------d--b-ef----------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-38% similar to PDB:2B20 Crystal Structure of Enterochelin Esterase from Shigella flexneri Enterochelin Esterase (E_value = 1.1E_19);","Residues 222 to 469 (E_value = 0.0013) place ANA_0836 in the Esterase family which is described as Putative esterase.","","esterase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0837","898873","900063","1191","4.85","-17.90","41552","ATGTCCACGTCCTCGTCGTCCTCTTCTTCCTCCGATCCGTCCCAGTCCTCCGATTCCTTGTCCTCCGTCCCATCGGAGGCCGAGGTCGTGGAGACTCAGGAGGTCACGGCTGAGAACGCCGCCGCGATTCTGGCAGCCGATGACGACATCGATGATCCCGACGCCAATGAGACGGATCAGTCGCATCGCGGCAAACCGTCACGGCGCACGCTGCTCACGATTGGGGGACTCGCAGCCGCTGCCGTGGTCGGTACCGGCGCGTACCTGACGATTCGGCGTACCAACCAAGGAGTCATCGGAGCCCACGAGGCACTCCCCCTGGTGATTGGCGGCGACATCTGCGCCGCACCACTGTACGCCGCGTACCACCAGGGATTCTTCGACGACGCAGGACTGAAGGTCACGCTGGCGCGCACCCAACAGACCGAGGACACCAAGGACGGCGTGGGCGCCGGTAAGTACATTGGCGCTCCAGGAATCTTCTTCTCCTGGCTGGAGCCGATCTACAACGGCCTCAACGCCAGGCTCACCGCAGGGCTCCACGCCGGCTGCCTGCGCCTGGTGGTGCGCAAGGACTCCCCGTATCAGAAGCTGGCTGACCTGAAAGGCACCACCATCGGCGTGCCGTCACTGTCGTCGTCGGCCTTCGCCTACTTCGCGATCGGGCTGTCGGAGGCCGGTATCAACGTCAAGCCGGATGGAGGCGACATCACGTGGCGCACAGTCGATGCGGACTCCTTGGGGACCGCGCTGACTGACGGCCAGGTGGACGCCATCATGGGTTCTGACCCCGGACCGCTGCTTCCCGTCTTCAATGGGACGGCCCGTGAGCTGGCCAACAACGACGCTGAGGAGTTCTGCTGCTCGGTGGCACTCAACGGGGACTTCGTACGTCGGCAGCCCAAGGAGGCGAAGGCTCTGACCGAGGCCTGGTTGAAGGGCTCGGCCTACGTGCCGGACCACATCGAGGAGATCGCCAAGATCGAGGTCGACAACGACTACGTCGCCGCCGACCAGGACGTCGTCGTCCGGGTGCTTAAGACATACGGGTTCAAGGCCTCTGCCTCCAGGTTCCGGGCCGCGATCGAGCCCGGCATCGAGAAGTTCAAGGGAACCGGTTTCATCGCATCCGACGTCTCCGCCCGGAAGCTGACCGACACCGTCATCGCCGATCTCGGCATCAAGGACTGA","MSTSSSSSSSSDPSQSSDSLSSVPSEAEVVETQEVTAENAAAILAADDDIDDPDANETDQSHRGKPSRRTLLTIGGLAAAAVVGTGAYLTIRRTNQGVIGAHEALPLVIGGDICAAPLYAAYHQGFFDDAGLKVTLARTQQTEDTKDGVGAGKYIGAPGIFFSWLEPIYNGLNARLTAGLHAGCLRLVVRKDSPYQKLADLKGTTIGVPSLSSSAFAYFAIGLSEAGINVKPDGGDITWRTVDADSLGTALTDGQVDAIMGSDPGPLLPVFNGTARELANNDAEEFCCSVALNGDFVRRQPKEAKALTEAWLKGSAYVPDHIEEIAKIEVDNDYVAADQDVVVRVLKTYGFKASASRFRAAIEPGIEKFKGTGFIASDVSARKLTDTVIADLGIKD$","ABC-type nitrate/sulfonate/taurine/bicarbonate transport system, periplasmic component","Cytoplasm, Membrane","putative ABC transporter, substrate-bindingprotein","ABC-type nitrate/sulfonate/bicarbonate transport systems periplasmic components","ABC-type nitrate/sulfonate/bicarbonate transport systems periplasmic components-like","","","","","

InterPro
IPR015168
Domain

NMT1/THI5 like
PF09084	$\"[187-261]T$	NMT1

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[181-260]T$	no description
tmhmm	$\"[71-91]?$	transmembrane_regions

","BeTs to 7 clades of COG0715COG name: ABC-type nitrate/sulfonate/taurine/bicarbonate transport systems, periplasmic componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0715 is a-----y-vd--bcefgh---j-i--Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 111-191 are 53% similar to a (ABC1) protein domain (PD824249) which is seen in Q8GGI9_LACPL.Residues 116-229 are 53% similar to a (ABC PERIPLASMIC TRANSPORTER BINDING SUBSTRATE-BINDING TRANSPORTER PROTEIN PRECURSOR SIGNAL EXPORTED) protein domain (PD396701) which is seen in Q89G90_BRAJA.Residues 236-327 are 52% similar to a (ABC TRANSPORTER SUBSTRATE-BINDING) protein domain (PD716461) which is seen in Q89G90_BRAJA.","","No significant hits to the PDB database (E-value < E-10).","Residues 187 to 261 (E_value = 1.1e-06) place ANA_0837 in the NMT1 family which is described as NMT1/THI5 like.","","ABC transporter, substrate-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0838","900070","901146","1077","9.88","10.60","39054","ATGCCCGCTGAGGTGAGCCCCACGACCACATCAACCGCATCCGTCAAGCCCATCGACAACAGGAATCCGCAACCTCCCTCCTCCACGGCCAGGAAGAGTGAACCAAGCGATCACCGTTCCAGCGCAGGCACGCTTGTGAGCACGACGGCACTGCTCTTGTGGTTGGCCTACCTGGTCCTCCTCATCGCCCTGCCGGAAGCCGACCTTCTCCGCAAGGAGTCAACCACTCCAGTCGCCGTCCTTGCCGGGACATGGCTGACCGCCCTGATCGCGTGGACACTCACCGCACGGGTCCGACCGGCCTCTTCGGCAGCGAGGTCTCTGACGCACTTCCTGCCCTGGATCAACGCCGCCGGCGCATGGTTCATCGTCTGGCAGCTGACAACATCCAAGCTCGGACTGCTCACGCCCCCGTACTTCGCCGCCCCAGAAATACTCATTGCCTCCTTCCTCGGTGACTGGAGGCTGCTGCTCAGCTGCCTGGGCGCCTCGGCGCTGCTCTTCATCATCGGGTACACGGCCGGATCGGTGCTGGGGTTCTTCACGGGCCTGCTCATGGGCTGGTCGAGGCGCGCCGACTACTGGCTCCATCCGCTCCTTCAGACCGTCGGGCCAGTTCCCGCGGCCTCACTCCTTCCGCTGGCACTGCTGCTGCTTCCGACGACGTACACCTCGGCAGCCTTCATCGTCGGCTTCGGCGCCTGGTTCCCCATGGCGACCATGACCCGCGCGGGCATACGCTCCGTGCGCCGCGACTACATCGACATGGCCCGCACACTGGGAGCCGATGAGCTCTTCCTTATCAGACGAGTGGCCGTGCCCTCAGCACTTCCGGACATGCTCACCGGCCTGTTCACAGGCCTGGGAACCTCACTCGCCGCCCTCATGACCGCCGAGCTGACCGGTGTCGACAAGGGCCTGGCCTGGTACATCAACTGGGTCAAGGGCTGGGCGGACTACCCCCGGATGTACGTGGGCCTCATCATTCTGGTGACCTTCTGCCGCACGCTCATGGTCCTGCTGTTCAAGATCCGCTCCTCGCTGCTGGCATGGCAGCAGAACCTTGTGAGGTGGTGA","MPAEVSPTTTSTASVKPIDNRNPQPPSSTARKSEPSDHRSSAGTLVSTTALLLWLAYLVLLIALPEADLLRKESTTPVAVLAGTWLTALIAWTLTARVRPASSAARSLTHFLPWINAAGAWFIVWQLTTSKLGLLTPPYFAAPEILIASFLGDWRLLLSCLGASALLFIIGYTAGSVLGFFTGLLMGWSRRADYWLHPLLQTVGPVPAASLLPLALLLLPTTYTSAAFIVGFGAWFPMATMTRAGIRSVRRDYIDMARTLGADELFLIRRVAVPSALPDMLTGLFTGLGTSLAALMTAELTGVDKGLAWYINWVKGWADYPRMYVGLIILVTFCRTLMVLLFKIRSSLLAWQQNLVRW$","ABC-type nitrate/sulfonate/taurine/bicarbonate transport system, permease component","Membrane, Cytoplasm","ABC transporter permease protein","binding-protein-dependent transport systems inner membrane component","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[157-350]T$	BPD_transp_1
PS50928	$\"[161-341]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-67]?$	signal-peptide
tmhmm	$\"[42-64]?$ $\"[78-96]?$ $\"[111-129]?$ $\"[154-188]?$ $\"[198-220]?$ $\"[226-246]?$ $\"[283-303]?$ $\"[322-342]?$	transmembrane_regions

","BeTs to 9 clades of COG0600COG name: ABC-type nitrate/sulfonate/taurine/bicarbonate transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0600 is a-mp----vd--bcef-hs--j-i--Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 108-195 are similar to a (TRANSMEMBRANE ABC PERMEASE FOR NITRATE POSSIBLY PROTEIN ABC2 TRANSPORTER TRANSPORTER) protein domain (PD696129) which is seen in Q6N6I3_RHOPA.Residues 228-276 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q6N6I3_RHOPA.Residues 296-352 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE COMPONENT NITRATE PROBABLE) protein domain (PD414592) which is seen in Q89G91_BRAJA.","","No significant hits to the PDB database (E-value < E-10).","Residues 157 to 350 (E_value = 2.2e-16) place ANA_0838 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter permease protein (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0839","901151","902032","882","6.82","-0.59","32050","ATGTCTACTGGTTCGTCGGCGGCTGCCGCCGCATCGCAAATCTCGACTCCGTCCGTCCCCCGCGGGGCACAGGTCGATCTCGCTGGTGTCTCCCACAGCTACCCGTTGTCCCATGACCTGGAGCATGGGTGGCTCCATCTGCTGCTGCGCCGGTTCTCCCCCGCTGCGAGGGCTCGCTATGAGGCTGAGGCTGCCAAGCCGGATCAGCTTGCCGTCCTCAATGACATCGACCTGACGGTGGCACCCGGGGAGTTCGTCTCACTCGTGGGGCCGTCCGGCTGCGGCAAGTCCACGATCCTGAGACTGCTGGCCGGGCTGGAGCAGCCCGTCGAGGGCCGCGTCACCGTCGACTCCACGCAGGTGACCGGCCCCTCACCTTTGCGCGCGCTCGCGTTCCAGGACGCCACGCTGCTGCCGTGGAGAACCGTGCGGGACAATGTCGCCCTGGGTCCTGAGGCAAGAAACCGCATGGAGCGCGACCGACGCCGGGTGGAGGCGGCCCTGCAGATCGTGGGGCTGCGGGACTTCGCCGACTCCTACCCCTCCACGCTCTCAGGCGGTATGGCTCAACGGGCCTCACTGGCCCGAGCCCTGGTCAACCGGCCCCGGCTCTTCCTCCTGGATGAGCCCCTGGGCAAGCTCGACGCCCTGACACGCCTCCAGCTCCAGGACGAGATCCTCAAGTTGTGGGAGTCCCAACGCTTCACGGCCGTCCTGGTCACCCACGACGTGGACGAGGCCCTACGCCTGTCCAACCGGGTGGTCGTCCTGTCAGAGCGCCCTGCGCGCATCGTCGCCGACATTGATGTGCCCGAGCACGACGAGTCGAGTGACGAGGTCCGCGAGCTGCGTCGGAAAATCCTCAGCCTGCTGGGGCGGTGA","MSTGSSAAAAASQISTPSVPRGAQVDLAGVSHSYPLSHDLEHGWLHLLLRRFSPAARARYEAEAAKPDQLAVLNDIDLTVAPGEFVSLVGPSGCGKSTILRLLAGLEQPVEGRVTVDSTQVTGPSPLRALAFQDATLLPWRTVRDNVALGPEARNRMERDRRRVEAALQIVGLRDFADSYPSTLSGGMAQRASLARALVNRPRLFLLDEPLGKLDALTRLQLQDEILKLWESQRFTAVLVTHDVDEALRLSNRVVVLSERPARIVADIDVPEHDESSDEVRELRRKILSLLGR$","ABC-type nitrate/sulfonate/taurine/bicarbonate transport system, ATPase component","Cytoplasm, Membrane","ABC transporter ATP-binding protein","ABC transporter related","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[184-226]T$	Q6N6I2_RHOPA_Q6N6I2;
PF00005	$\"[83-260]T$	ABC_tran
PS50893	$\"[58-284]T$	ABC_TRANSPORTER_2
PS00211	$\"[184-198]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[82-260]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[68-287]T$	no description
PTHR19222	$\"[25-34]T$ $\"[68-293]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF51	$\"[25-34]T$ $\"[68-293]T$	SULFONATE / NITRATE ABC TRANSPORTER

","BeTs to 9 clades of COG1116COG name: ABC-type nitrate/sulfonate/taurine/bicarbonate transport systems, ATPase componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1116 is a-mp----vd--bcef-hs--j----Number of proteins in this genome belonging to this COG is 1","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.7e-32. IPB005074C 72-119 IPB005074D 172-215***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 4.1e-29. IPB013563A 72-106 IPB013563C 181-208 IPB013563D 236-288***** IPB005116 (TOBE domain) with a combined E-value of 8.2e-29. IPB005116A 90-106 IPB005116C 184-197 IPB005116D 204-223 IPB005116E 238-251***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 2.4e-15. IPB010509B 83-108 IPB010509D 179-223","Residues 67-257 are 43% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 67-257 are 47% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 69-149 are 57% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 72-150 are 59% similar to a (ATP-BINDING TRANSPORTER) protein domain (PDA0J3Q7) which is seen in Q7M9H8_WOLSU.Residues 72-264 are 48% similar to a (ATP-BINDING ABC PROTEIN TRANSPORTER) protein domain (PD995669) which is seen in Q73R06_TREDE.Residues 73-121 are 87% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8GGJ1_LACPL.Residues 73-257 are 45% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 76-147 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3N7) which is seen in Q92T99_RHIME.Residues 78-244 are 52% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 79-256 are 43% similar to a (ATP-BINDING SECRETION PROBABLE ABC TOXIN TRANSPORTER) protein domain (PDA0C7R3) which is seen in Q7UXT8_RHOBA.Residues 83-275 are 46% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 83-150 are 63% similar to a (ATP-BINDING ABC SUBUNIT TRANSPORTER) protein domain (PDA0J3P4) which is seen in P71508_METEX.Residues 169-258 are 57% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 171-243 are 63% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q9CP80_PASMU.Residues 175-257 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD195520) which is seen in Q822T7_CHLCV.Residues 175-242 are 60% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8FAX9_ECOL6.Residues 183-269 are 59% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 184-226 are 90% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6N6I2_RHOPA.Residues 186-243 are 62% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.","","-56% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 3.3E_31);-58% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 1.3E_30);-58% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 1.3E_30);-56% similar to PDB:1G29 MALK (E_value = 6.2E_30);-56% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 1.1E_29);","Residues 83 to 260 (E_value = 1.7e-60) place ANA_0839 in the ABC_tran family which is described as ABC transporter.","","transporter ATP-binding protein (cmpC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0840","902338","904950","2613","5.18","-38.65","94722","ATGACTCACTCCAGCAGTACTGCACCTGGCGCCTCCGACGCTCAGAGCCAGGACGGCAACGGCCCCCTCAGCCTCGACGCGCTCTTCTCCGCCGAGCTCTCCGGCGGCGAGCAGACCGGCCCGGCCAAGAACGACGAGGAGAGCACTGTCGCCGCACCGCACCACCGCGACGGCACCACCTCCTCCCCCGAGGACTTCGCCACTCCCGCCTCCTCCGATTCCCCTGAGGACCCGGAGGACGTCGACCACGAGGAAGAGGCGGACGACGTCGACCGAGACCTCCCCGAGGCCGACCCGGAGGACGAGATCGACGACTCCGATGAGGACGACGGAGTCGACATTGACGAGGATGAGGTTGACGGCCACACCCCCTTCATCGACACCGATGCTGATTCCAACGCCGATTCCGACACAGATTCCGACGCTGACTCCAACGGCCACCAGCGCGACGTCGAGCGCGCCGCCTCGCCGCGCGACCGGGACAAGAGCGAGGTGAGGACCGCTCACGAGGATGAGGAGATCACCTTCGCCGACCTGGGTCTTCCCGGTGACCTGCTCAAGGCCGTCACCGACATGGGATTCGTGACCCCCACCGCCATCCAGAAGGAGGCGATCCCCGTTCTGCTGGCCGGCCGCGACGTCGTGGGCGTCGCCCAGACCGGAACCGGCAAGACGGCGGCCTTCGGGCTTCCGCTGCTCGACGCCGTCGATTCGCGCGACAACGTCGTTCAGGCGCTCGTTCTGGCCCCCACCCGCGAGCTCGCGCTCCAGAGCGCCGAGGCCATCACTGATATGGCTGCCCGCTCCCGCGGACTGGAGGTGGTGGCCGTCTACGGCGGTGCCCCATACGGCCCCCAGATCGGCGCGCTCAAGGGAGGCGCCCAGGTCGTCGTCGGCACTCCCGGGCGCGTCATCGACCTCATTGACAAGGGCGCGCTCCAGCTCGACGACGTGCGCTACTTCGTCCTAGACGAGGCCGACGAGATGCTGCGGATGGGCTTCGCCGAGGACGTGGAGACGATTGCGGAGTCCCTTCCCACCGATCGGCGCACCGCCCTGTTCTCCGCGACGATGCCTCCGGCCATCCAGGCCGTGGCGCGTCAGCACCTCCACGAGCCCGTTCAGGTGGAGGTCTCCAGGCCGGCCTCCACTGTCGCCACCGTCCACCAGACCTACGCGGTGGTTCCCTTCCGCCACAAGATCGGGGCCGTCTCCCGGGTCCTGGCCGTCACCGACGCCGAGGCCGCCATCGTCTTCGTGCGGACCAAGTCCACGGCCGAGGACGTCGCCATCGAGCTGGCGGGCAGGGGCATCCAGGCCGCCGCGATCTCCGGTGACGTTCCCCAGCGCGAGCGCGAGCGCCTGGTGGAGCGGCTGCGCGCCGGCACCCTTGACGTGCTGGTGGCCACGGACGTCGCCGCCCGAGGCCTGGACGTGGACCGCATCGGCCTGGTGGTCAACTTCGACGTGCCCCGCGAGGCCGAGGCCTACGTGCACCGTATCGGTCGCACGGGCCGCGCCGGCCGCCACGGCGAGGCCGTCACCTTCCTAACCCCCAAGGAGAAGGGCAAGCTCCGCCAGATCGAGCGCCTCACCGGAAGCCGTCTGGAAGAGATCACCCTGCCCTCCCCCGCGGACGTCTCCGAGCACCGCGCCCGCAAGCTCCTGTCCAAGGCAGCCGCCCGCCACGAGCGCGGCCGTCTGGACATGTACCTGCCGCTGGTGGCCGACTCCGCCCGGGAGCTGGACATCGACGTCGAGGAGCTGGCGGCCACGCTGCTGGCCCTGGCCGTGGGAGACGAGGGACCGCGCAGGCGCGAGGACCGGGGCGGCGAGCGCCCCCAGCGCGCCCGCCGCGAGGAGAACCTCGATTCCGAGGGGACCTTCCTGTCGGCTTCCTTCGAAGGCGGCAGGGAGAAGGGCCGTCGCGCAGAGCGGGGAGACCGCGGCGAGGGACGCCGCTCGGCCACGCGTTCCGGGCGCCGCGAGCACGATGGCCCCGGGACCGTCTACCGCGTGGAGGTCGGGCACCGCGACCGGGTCCTGCCCGGAGCGATCGTGGGCGCGCTGGCCAACGAGGGCGGTATCGAGGGCTCCGACATCGGCAAGATCGACATCCTCCAGTCCTTCTCCCTGGTCACGATCTACGCCGACCTCAGCCCCGAGCAGCTGAGCGTCATGGGGCGAGCGACCTTTGCTGGCCGCGAGCTGCGGATCCGTCCCGACGAGGGTCCGGGGCACGGCTGGTCCGGCCCCAACGGCGAGCGGCGTCCCAAGCGGCGTGACTGGGAGGACCGCAGGGACCGTGGCGAGCGGTCGGAACGCGGTTTCCGTCCCCGCCGTGAGGACGGCGAGCGCGGCTGGAAGGACCATGATGGGCGCGGCGGCAGGGGCGGCTACGACCGCTCGGAGCGCGGGGAGCGCCGTGACAACCGTCGTTGGGACGAGCGCCGTGGCGACCGCGACGGCTTCCGCGGCCGGCGCGAGGACCGGGGCGGTCGCGGCTACGACCGCGACGGGCACCGGGGCGAGCGCCGTGGCTACGGCGAGCGCAACCAGAACCGCTTCGGCGGCCACCGGGGCGGCTTCCGCGGAGGGCGCGGTGAGCGCTGA","MTHSSSTAPGASDAQSQDGNGPLSLDALFSAELSGGEQTGPAKNDEESTVAAPHHRDGTTSSPEDFATPASSDSPEDPEDVDHEEEADDVDRDLPEADPEDEIDDSDEDDGVDIDEDEVDGHTPFIDTDADSNADSDTDSDADSNGHQRDVERAASPRDRDKSEVRTAHEDEEITFADLGLPGDLLKAVTDMGFVTPTAIQKEAIPVLLAGRDVVGVAQTGTGKTAAFGLPLLDAVDSRDNVVQALVLAPTRELALQSAEAITDMAARSRGLEVVAVYGGAPYGPQIGALKGGAQVVVGTPGRVIDLIDKGALQLDDVRYFVLDEADEMLRMGFAEDVETIAESLPTDRRTALFSATMPPAIQAVARQHLHEPVQVEVSRPASTVATVHQTYAVVPFRHKIGAVSRVLAVTDAEAAIVFVRTKSTAEDVAIELAGRGIQAAAISGDVPQRERERLVERLRAGTLDVLVATDVAARGLDVDRIGLVVNFDVPREAEAYVHRIGRTGRAGRHGEAVTFLTPKEKGKLRQIERLTGSRLEEITLPSPADVSEHRARKLLSKAAARHERGRLDMYLPLVADSARELDIDVEELAATLLALAVGDEGPRRREDRGGERPQRARREENLDSEGTFLSASFEGGREKGRRAERGDRGEGRRSATRSGRREHDGPGTVYRVEVGHRDRVLPGAIVGALANEGGIEGSDIGKIDILQSFSLVTIYADLSPEQLSVMGRATFAGRELRIRPDEGPGHGWSGPNGERRPKRRDWEDRRDRGERSERGFRPRREDGERGWKDHDGRGGRGGYDRSERGERRDNRRWDERRGDRDGFRGRREDRGGRGYDRDGHRGERRGYGERNQNRFGGHRGGFRGGRGER$","ATP-dependent RNA helicase DeaD","Cytoplasm, Extracellular","ATP-dependent RNA helicase","K05592 ATP-dependent RNA helicase DeaD","DEAD/DEAH box helicase domain protein","","Schmid S.R., Linder P. D-E-A-D protein family of putative RNA helicases. Mol. Microbiol. 1992. 6(3):283-292. PMID: 1552844Linder P., Lasko P.F., Ashburner M., Leroy P., Nielsen P.J., Nishi K., Schnier J., Slonimski P.P. Birth of the D-E-A-D box. Nature 1989. 337(6203):121-122. PMID: 2563148Wassarman D.A., Steitz J.A. RNA splicing. Alive with DEAD proteins. Nature 1991. 349(6309):463-464. PMID: 1825133","","","

InterPro
IPR000629
Domain

ATP-dependent helicase, DEAD-box
PS00039	$\"[322-330]T$	DEAD_ATP_HELICASE

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[432-508]T$	Helicase_C
SM00490	$\"[427-508]T$	HELICc
PS51194	$\"[403-548]T$	HELICASE_CTER

InterPro
IPR005580
Domain

DbpA, RNA-binding
PF03880	$\"[658-743]T$	DbpA

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[198-365]T$	DEAD

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[515-626]T$	no description

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[193-391]T$	DEXDc

InterPro
IPR014014
Domain

DEAD-box RNA helicase Q motif
PS51195	$\"[174-202]T$	Q_MOTIF

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[205-376]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[161-378]T$ $\"[383-553]T$	no description
PTHR10967	$\"[72-79]T$ $\"[169-547]T$ $\"[747-870]T$	DEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF51	$\"[72-79]T$ $\"[169-547]T$ $\"[747-870]T$	ATP-DEPENDENT RNA HELICASE

","BeTs to 20 clades of COG0513COG name: Superfamily II DNA and RNA helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: K [Information storage and processing--Transcription],JThe phylogenetic pattern of COG0513 is a-mp--yq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 4","***** IPB005580 (DbpA RNA binding domain) with a combined E-value of 1.8e-84. IPB005580A 222-260 IPB005580B 321-370 IPB005580C 477-529***** IPB000629 (ATP-dependent helicase, DEAD-box) with a combined E-value of 4.4e-84. IPB000629A 193-233 IPB000629B 246-258 IPB000629C 295-306 IPB000629D 318-341 IPB000629E 470-511***** IPB012562 (GUCT) with a combined E-value of 8.7e-83. IPB012562A 197-236 IPB012562B 240-258 IPB012562C 276-309 IPB012562D 322-342 IPB012562E 350-362 IPB012562G 452-506 IPB012562H 509-562***** IPB012541 (DBP10CT) with a combined E-value of 3.2e-50. IPB012541A 197-237 IPB012541B 242-280 IPB012541C 302-356 IPB012541D 415-449 IPB012541E 478-532***** IPB013701 (DEAD/H associated) with a combined E-value of 3.5e-13. IPB013701A 188-231 IPB013701G 413-433 IPB013701H 458-491***** IPB005034 (Protein of unknown function DUF283) with a combined E-value of 3.2e-10. IPB005034C 296-330 IPB005034F 457-511***** IPB007759 (DNA-directed RNA polymerase delta subunit) with a combined E-value of 1.1e-06. IPB007759B 82-118 IPB007759B 84-120 IPB007759B 83-119 IPB007759B 77-113 IPB007759B 81-117 IPB007759B 73-109 IPB007759B 85-121 IPB007759B 79-115 IPB007759B 86-122 IPB007759B 76-112 IPB007759B 89-125 IPB007759B 72-108 IPB007759B 88-124 IPB007759B 100-136 IPB007759B 74-110 IPB007759B 101-137 IPB007759B 93-129 IPB007759B 95-131 IPB007759B 91-127 IPB007759B 65-101 IPB007759B 69-105***** IPB002121 (HRDC domain) with a combined E-value of 5.6e-06. IPB002121F 469-508","Residues 154-234 are 58% similar to a (HELICASE AT1G59990/T2K10_4 HYDROLASE ATP-BINDING) protein domain (PD509824) which is seen in Q944S1_ARATH.Residues 220-301 are similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT FACTOR DNA BOX RNA-BINDING 3.6.1.-) protein domain (PD410733) which is seen in Q725W5_DESVH.Residues 289-525 are 46% similar to a (HELICASE DEAD RNA HYDROLASE ATP-DEPENDENT BOX FAMILY ATP-BINDING) protein domain (PD605738) which is seen in Q8SRI9_EEEEE.Residues 302-351 are 80% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT BOX RNA-BINDING DEAD DEAD-BOX INITIATION) protein domain (PD000276) which is seen in Q8YXJ0_ANASP.Residues 417-481 are 78% similar to a (HELICASE ATP-BINDING HYDROLASE DNA ATP-DEPENDENT RNA EXCISION FACTOR B REPAIR) protein domain (PD000033) which is seen in Q7U0A2_MYCBO.Residues 485-522 are 89% similar to a (HELICASE ATP-BINDING HYDROLASE RNA ATP-DEPENDENT BOX RNA-BINDING DEAD DEAD-BOX HELICASE) protein domain (PD035460) which is seen in P96614_BACSU.Residues 671-746 are 63% similar to a (HELICASE HYDROLASE ATP-BINDING RNA ATP-DEPENDENT DEAD DBPA DEAD-BOX HOMOLOG A) protein domain (PD099848) which is seen in Q6AEM1_BBBBB.","","-63% similar to PDB:1HV8 CRYSTAL STRUCTURE OF A DEAD BOX PROTEIN FROM THE HYPERTHERMOPHILE METHANOCOCCUS JANNASCHII (E_value = 3.8E_69);-57% similar to PDB:1FUU YEAST INITIATION FACTOR 4A (E_value = 5.7E_65);-54% similar to PDB:2HYI Structure of the human exon junction complex with a trapped DEAD-box helicase bound to RNA (E_value = 7.7E_62);-54% similar to PDB:2J0Q THE CRYSTAL STRUCTURE OF THE EXON JUNCTION COMPLEX AT 3.2 A RESOLUTION (E_value = 7.7E_62);-54% similar to PDB:2J0S THE CRYSTAL STRUCTURE OF THE EXON JUNCTION COMPLEX AT 2.2 A RESOLUTION (E_value = 7.7E_62);","Residues 198 to 365 (E_value = 8.6e-70) place ANA_0840 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 432 to 508 (E_value = 6.4e-31) place ANA_0840 in the Helicase_C family which is described as Helicase conserved C-terminal domain.Residues 658 to 743 (E_value = 2.4e-21) place ANA_0840 in the DbpA family which is described as DbpA RNA binding domain.","","RNA helicase (deaD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0841","905787","905053","735","5.96","-5.16","25781","ATGCCGATCTGGACCTTTGACCTTCCCGATGACGTACAGCCCAGCCTCGTCCTGGATCTGTCCACCCTGAGCGTGGTGACCGCGCCTGGGACGGGAAGCGCGATCACCGTCGAGGCCGATGAGAGCCTGACCCCCCTCCTGGACGTCACCGCCGACGGGGCCAAGGTGAGCATCCGCCAGATCGCTCTTGTGGGACGTGAACGATTCGCTGGCATCTGGCCGTGGGGCCCGCAGACATCTCGAGTCCGGGTCACGGTGCCGCACGGCACGCGCCTGGACGCCCGCCTCGATGCCGGATCGATCAGCGCTGAGCACTCCTGGGATCACGTGCAGATCCGCACCTCGGCGGGATCGATCCGTCTGGGCGACTGCATGAGTGCGCAGGTGCACGCCGACGCCGGCTCCATCGTCATCGGTGCCCTGCATGAGGGGAGCGTGCGGGCCCAAGCCGGTTCGGTGCGCATCCGCTCGACCTCAGGCACAGTGTCTGCCCACACGGAGGCCGGCTCGGTCAAGATCGTCGAGGCCCTTGAAGGATCCTTGGACCTGTCCAGCGAGATGGGAACCGTGTCGGTGGGAGTGCCTGAGGGAACTGCGGTCCTGGCCGACTGCCACTCCGACTTCGGTCGAGTCGCCACCGACCTGCCGCGCCAGGACCACCCCGATGCCCTCGAACGACGCCTCGAGCTGCGGGCCCGCACCCAGATGGGGACCGTGCGGGTGCGCAGGGCCTGA","MPIWTFDLPDDVQPSLVLDLSTLSVVTAPGTGSAITVEADESLTPLLDVTADGAKVSIRQIALVGRERFAGIWPWGPQTSRVRVTVPHGTRLDARLDAGSISAEHSWDHVQIRTSAGSIRLGDCMSAQVHADAGSIVIGALHEGSVRAQAGSVRIRSTSGTVSAHTEAGSVKIVEALEGSLDLSSEMGTVSVGVPEGTAVLADCHSDFGRVATDLPRQDHPDALERRLELRARTQMGTVRVRRA$","Hypothetical protein","Cytoplasm","putative lipoprotein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-54% similar to PDB:1KBZ Crystal Structure of apo-dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) from Salmonella enterica serovar Typhimurium (E_value = );-54% similar to PDB:1KC1 Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH (E_value = );-54% similar to PDB:1KC3 Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose (E_value = );-54% similar to PDB:1M1G Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1) (E_value = );-54% similar to PDB:1M1H Crystal structure of Aquifex aeolicus N-utilization substance G (NusG), Space group I222 (E_value = );","No significant hits to the Pfam 21.0 database.","","lipoprotein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0843","906525","905902","624","5.43","-6.58","22019","ATGCATGTGGATGCCTACACCGAGACCCTGCGTCGTACCCTCGTGGAGACCTCGTCCCTGGGTGACGACCGGACCCAGGACGTGGCCCGCTCCCTGGCGGCTGCACTCGATCCGGCACTGCGCCTCGTCGCCCTGCAGATGCTCACGGACACCGCTGACGAGCTCAACGGCGAGCTCGACGGAGCTCATGTCGCCGTCGTGATGGACGGTGCGACGCCCCATCTTCTGGTGACCCAGGCTGATCGGTCTGATGAACGGAATCAGGACCACGTGACGGGCCCGGACCGCCATGCCCAGACTCCGGTGCACGCAGTACCTGAGGTGGCGGAGGGGCCGGAGGTCCGTACGACGCTGCGCCTGCCCGAGTCACTCAAGCAGCAGATCGACGCCGCTGCCCGGGGGCAGGGACGTTCGGTCAACGCCTGGCTTGTGGAAGCGGCTCGAGGCGCGCTGTTGGAACAGTCGTTCACGTCGGGCTCCCAGCGCCCGCCGAGCACCGGGAACGACGGGGCGGGACTTGATCGCTCTGCGAGTGGCTCCGACGGCGGACGCCCCACCGACTGGCGTGCCAGACCGGCACAGCGCCGGACCTCCGGGGCGACGCTCAGCGGCTGGTTCGGCTGA","MHVDAYTETLRRTLVETSSLGDDRTQDVARSLAAALDPALRLVALQMLTDTADELNGELDGAHVAVVMDGATPHLLVTQADRSDERNQDHVTGPDRHAQTPVHAVPEVAEGPEVRTTLRLPESLKQQIDAAARGQGRSVNAWLVEAARGALLEQSFTSGSQRPPSTGNDGAGLDRSASGSDGGRPTDWRARPAQRRTSGATLSGWFG$","Ribbon-helix-helix protein, copG family","Periplasm, Cytoplasm","hypothetical protein","hypothetical protein","CopG domain protein DNA-binding domain protein","","Acebo P., Garcia de Lacoba M., Rivas G., Andreu J.M., Espinosa M., del Solar G. Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and beta-sheet DNA binding proteins. Proteins 1998. 32(2):248-261. PMID: 9714164Gomis-Ruth F.X., Sola M., Acebo P., Parraga A., Guasch A., Eritja R., Gonzalez A., Espinosa M., del Solar G., Coll M. The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator. EMBO J. 1998. 17(24):7404-7415. PMID: 9857196","","","

InterPro
IPR002145
Domain

CopG-like DNA-binding
PF01402	$\"[115-153]T$	RHH_1

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 115 to 153 (E_value = 0.00021) place ANA_0843 in the RHH_1 family which is described as Ribbon-helix-helix protein, copG family.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0844","908304","906610","1695","6.78","-1.60","60227","GTGACGACCGACCGCTCCGCAGTGTCAGACCTTCCGCTGGTTCTTGAGGACCTGGCCAGGGCCGTCGACCTGGGTGAGCAGCTCGGTCTGGGCGAAGAACTCGCCCATGCCCGGGACGTCCTCACGCAGGCCTCCCACCGTCGGCGTCTGGCGCCGCAGACCACGGTGGCGGCCCTTCTCGGAGCGACAGGGTCGGGTAAGTCGAGCCTGACCAACGCCATGGCCGGCTCCGAGGTGTCCCGTACCGCCCGTACCCGCCCGACGACCACTCAGCCCCTCGCCGTCGTCCCGGACACGGCGAATGACGCCACTGAGCTGCTGGACTGGCTCGCCATCAGCCACCGGGTGCGCGTCGACGGCGACTGGGCCCTGGGCGAGAGCACGGTGCTGGTCGATCTGCCCGATATCGACTCCGACGAGCCCGCGCACCGGGCCATCGCCCAGCGCATGGCGGGAAAAGTCGATGTCCTGGTGTGGGTCCTCGATCCGGAGAAGTACGCCGACGGCGTTGTCCATCGCGACTTCCTCATCCCTATGGCGGCGCACGCCGAGGTCATGGTGGTTGCCCTTAACCAGGTGGATCGGCTCGACCCTGAGAGCCGGGACGCAGTGCTCGCCGACCTCAGGAGGATCCTGGACCGAGAGGGTCTTGGAGCCGTCTCAGTGATTCCTGTCAGTGCCCGCACTGGGCAGGGCGTTGAGACTCTGGCACGCGCCGTGGCCTCGGTCGCCTCCAACAGGCTGGCCAGCGCTCAAAGCCTCGCCGCCCACGCCCGGCGCGCAGCCAGTGAGCTGGGGGAGCGCACGGGGCTCATCGCACCATCCGGCCGTGGTGCGCCAACACCGGGCCCGGCCGCTCAGCAGGAGCCGCAGGTACGTCATTCCCTCACTGCCCTGCGGCAGGCGGCCGCGAGCCTCGCCGGGGTCGACGTCGTCTCACAGGCGGTTGAAGGATCGGACCGTCACCGGGCCAGCACCCGAGTCGGCTGGTTCTGGCTGCGGTGGATCGGGCACCTGCGACGTGACCCGCTTCGAGCCCTTCACCTGGGGACCGGGCGCCCGCCGGCCCCGAGGTCCGCAGACGCGGAACAATCCGACGGCGCTACGGGCTCCGGCGTCATCGACCTGACTTCCCTGCCCCCCGCAGGACCTGCCGCAACGGGCAGGCTGCGCAGCAGTGCTCACGTCTACGCCGTGGCGGCATGCTCCGCTCTGCCCGGTGATCTGGCCGCTCAGGCCGTTCTGCGCAGTGACGAGCGTGCTGAGAGGCTTGCCGAGCCTTTGGAACTGGCTGTGGCCCAGGTGGACTACGGGACGTGGAAGCGCCCGGTCTGGTGGAAAGCTGCGAACGTGCTGCAGTGGGTGACCGCACTGGCCGCACTCATCGGCGGGTTGTGGCTGGTGGCCATTCACGTGCTGGAGGACTACCTCCTGCTCATCAGCATCGATGTTCCGCGCTGGGGGACAGTCCCCTGGCCCACCGTCCTCCTGCTCGGAGGCCTGCTGATCGGACTGGTCCTGGCAGGTCTGGGGACGTTGCTGTCCGGCCTTCAGGCCAGGCGTCACCGCAGGCGGATCATTGAGCGCTTGCGCCGGGCCACCGACGAGGTCGTGAACGCCGAGCTCATCGAGCCGCTCAGGGCCGAGACACAGGGATGGGTGGAGCTCGCGCGGATTCTGGAACGAATCGCCTAA","VTTDRSAVSDLPLVLEDLARAVDLGEQLGLGEELAHARDVLTQASHRRRLAPQTTVAALLGATGSGKSSLTNAMAGSEVSRTARTRPTTTQPLAVVPDTANDATELLDWLAISHRVRVDGDWALGESTVLVDLPDIDSDEPAHRAIAQRMAGKVDVLVWVLDPEKYADGVVHRDFLIPMAAHAEVMVVALNQVDRLDPESRDAVLADLRRILDREGLGAVSVIPVSARTGQGVETLARAVASVASNRLASAQSLAAHARRAASELGERTGLIAPSGRGAPTPGPAAQQEPQVRHSLTALRQAAASLAGVDVVSQAVEGSDRHRASTRVGWFWLRWIGHLRRDPLRALHLGTGRPPAPRSADAEQSDGATGSGVIDLTSLPPAGPAATGRLRSSAHVYAVAACSALPGDLAAQAVLRSDERAERLAEPLELAVAQVDYGTWKRPVWWKAANVLQWVTALAALIGGLWLVAIHVLEDYLLLISIDVPRWGTVPWPTVLLLGGLLIGLVLAGLGTLLSGLQARRHRRRIIERLRRATDEVVNAELIEPLRAETQGWVELARILERIA$","Translation initiation factor 2 (GTPase)","Cytoplasm, Membrane","putative ATP-binding membrane protein","putative ABC transporter","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[53-238]T$	no description
PTHR11649	$\"[14-116]T$ $\"[134-247]T$	MSS1/TRME-RELATED GTP-BINDING PROTEIN
tmhmm	$\"[450-470]?$ $\"[495-517]?$	transmembrane_regions

","BeTs to 6 clades of COG0532COG name: Translation initiation factor 2 (GTPase)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0532 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 1.4e-06. IPB002917 59-91","Residues 18-495 are 47% similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PD318046) which is seen in Q6A790_PROAC.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","ATP-binding membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0845","910001","908301","1701","5.90","-8.43","60339","ATGCCCTATGTCCTTCAGGGAACCGCCGCCGCCTCGGACAAGGCCACGCTCATCCGTGACCAGCTCGGTGACTACGTCCTTCCCCGCCTGGCCAGCCTGGATGCCCCGCTGCTGGCCGTGGTCGGCGGATCGACAGGGGCCGGCAAGTCGACCCTCGTGTCCTCGCTCGTTCGCCGGCACGTGGCCAGGGCCTCGGCAATCCGCCCCACCACGCGCCGCCCTCTGCTGCTGCACGCGCCGACCGACGCCGCCTGGTTCGACACCGACCGGGTCCTGGGCTCCCTGTCGCGCATGCGTGTGGATGCCGATGCTCCGGCGAGCCCGGCCACGGACCACACGCCCAGAGAGCTCGAGCTACGGGCCTGTGAGGGGCTGCCCGAGGGACTGGCGATCGTGGACGCACCAGATGTTGACTCCGTGGTCGAGGACAACCGGGACCTGGCCGCCACGCTCCTGGCCGGGGCGGACCTGTGGATCTTCGTCACCACGGCGGCGCGCTACGCCGACGCCGTCCCCTGGGAGCACCTGCGGGCCGCGGCCGAGCGGCACATCACGGCCGCCATCGTCCTGGACCGCGTACCGGAGGGTGCGCAGAGCGAGGTGGAGGCAGACCTACGGCGTCGGCTCACGGAGGCCGGCCTGGCCGAGGCGCCCGTTTTCACGATTCCCGAGACGGCCCTGGATGACGACGGCTTCCTGCCCGAGTCCTGCGTCTCACCGCTGCGCCAGTGGCTGGGGGCGCTGGCCTCCGACGCGGCCGCTCGCCGGGATGTCGCACACCGCAGCCTGACCGGCGCGATCGGTTCCCTTCTGGCACAGAGCGAGCTGCTCGCCGTCGAGCTGGCCTCCCAGGAGGCTGAGCACGCCGAGCTGCGTCGAGCAGCCACCTCCGAGCATGATGATGCCCTCGAGCGTGTCATCGAGGCCACCGAGGACGGCTCCATGCTGCATGGCGAGGTGCTGGCCCGTTGGCAGGAGTTCGTGGGCACTGGGGACCTGTTCCGGTCCTTGGAGGTGCAGGTGGGGCGGGTCCGCGACCGCGTCACGTCGCTTCTGCGGGGACGTCCGGCGCCGGCCAAGCGCGTCGAGCAGGCGATCGGCTCCTCCCTGGTCGAGCTCCTGGTCGCCGAGTCCCAACGGGCCTGTCTGGCCACGGAGCGCTCCTGGAGACGAGCCGGCACCTCCCAGCAGGCGCTCAACCGGGCTCTGGCGGAGGTGCCCAGCCAGACCGGCCTGGAGGTCGTCGCCGCGGCCCTCGTCCACGACTGGCAGCGTCAGGTTCTCACTCTCGTCCGAGCCGAGGGCTCTGACAAGCGGCTCACTGCGCGCCTGCTGTCCCTGGGCGTCAATGGCGCCGGAGTCGTCCTCATGATTCTCGTCTTCGCTCACACCGGCGGACTGACCGGGGGAGAGGTGGGGATCGCGGGGGGCACGGCCATTCTGGCTCAGCGCGTTCTGGAGGCCGTGTTCGGAGACCAGGCGATGCGCGGCATGACCAAGCGGGCCCGTGAGGACCTCGGCGAACGTGCCACGGCTCTGTTCGCCAACCAGGCGAAGTGCTTCACCGACGCTCTTCCGCTGCCCATCCCGAGCGCCGATACGCTGCGAGAACAGCTTCAGGCCTGCCAGGAGGCGGCCACGTCGTTGCGCGCTTTGCCAGCTGCTGGCAGCCGCCGGTCGGCCGGGAGGAGGTCCAGGTGA","MPYVLQGTAAASDKATLIRDQLGDYVLPRLASLDAPLLAVVGGSTGAGKSTLVSSLVRRHVARASAIRPTTRRPLLLHAPTDAAWFDTDRVLGSLSRMRVDADAPASPATDHTPRELELRACEGLPEGLAIVDAPDVDSVVEDNRDLAATLLAGADLWIFVTTAARYADAVPWEHLRAAAERHITAAIVLDRVPEGAQSEVEADLRRRLTEAGLAEAPVFTIPETALDDDGFLPESCVSPLRQWLGALASDAAARRDVAHRSLTGAIGSLLAQSELLAVELASQEAEHAELRRAATSEHDDALERVIEATEDGSMLHGEVLARWQEFVGTGDLFRSLEVQVGRVRDRVTSLLRGRPAPAKRVEQAIGSSLVELLVAESQRACLATERSWRRAGTSQQALNRALAEVPSQTGLEVVAAALVHDWQRQVLTLVRAEGSDKRLTARLLSLGVNGAGVVLMILVFAHTGGLTGGEVGIAGGTAILAQRVLEAVFGDQAMRGMTKRAREDLGERATALFANQAKCFTDALPLPIPSADTLREQLQACQEAATSLRALPAAGSRRSAGRRSR$","ATP/GTP-binding protein","Cytoplasm, Membrane","possible ATP-binding protein","putative ABC transporter","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG0699COG name: Predicted GTPases (dynamin-related)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0699 is ------y--dr-bcef----u-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 15-74 are 78% similar to a (TRANSMEMBRANE GTPASE GTP-BINDING MEMBRANE 3.6.5.- COILED COIL HYDROLASE MITOCHONDRION OUTER) protein domain (PD590957) which is seen in Q6A789_PROAC.Residues 38-466 are 38% similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PD318046) which is seen in Q9KYI8_STRCO.Residues 75-517 are 63% similar to a (ATP-BINDING POSSIBLE SCC61A.06C ABC TRANSPORTER) protein domain (PD871710) which is seen in Q6A789_PROAC.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0846","911524","910094","1431","5.65","-9.68","50832","ATGGCACAGGTACGACAAGCTCTCTCCTCACTGTCCGGCTTCCCCGAGTGGCTCCCCTCGGGCCACATCGTCGAGCAGCACTTCGTCGACATCCTGCGCCGCACCTTCGAGCTCCACGGCTTCAGCGGCATCCAGACCCGCGCCGTCGAGCCACTGAGCGAGCTGACGAAGAAGGGGGAGACCTCCAAGGAGGTCTACCTGCTCAGCCGCCTGCAGGCCGATCCCGCCGAGTCCGAGGCGGATCCGCGCAAGCAGCTGGGGCTCCACTTCGACCTGACCGTCCCCTTCGCCCGCTACGTCGTCGACAACGCCGGGCTGCTGACCTTCCCGTTCAAGCGCTACCAGATCCAGAAGGTCTGGCGCGGGGAACGGCCCCAGGAGGGACGCTTCCGCGAGTTCATCCAGGCCGACATCGACATCGTCGGTGACGGTGCCCTGCCGCTCCACCACGACGTCGAGGTCCCCCTCATCATGCACGAGGCGCTCAGCGCTCTGCCGGTGCCCGAGGTCACCATCCACGTCTCCAACCGCAAGGTCGCTCAGGGCTTCTACCAGTCGATCGGCATCGACACGGACCGGCTCATCGAGGTCCTGCGTGTGGTCGACAAGCTCGACAAGATCGGTCCCGAGAAGGTGGCTGCCGAGCTCACCCAGAGCGTCGGTGTCAGCGCGCAGCAGGCGGCACAGGCCCTCAGGCTCGCCACCATCACCGGCACCGACGGCCAGGACGTCTCCGATCAGGTCCTGCGGGCGCTGGCCGGCGCCGAGCCCACCGAGCTCCTCAACGAGGGCCTGGCCGAGCTGACCGCACTGCTCGAGGCCACCGGACGCCGCCGCCCCGGCGCCGTCATCGCCGACCTCAAGATCGCTCGTGGGCTGGACTACTACACCGGTACGGTCTACGAGTCCTTCATGGCCGGCCACGAGGACCTGGGTTCAGTGTGCTCCGGGGGCCGCTACGACTCGCTGGCCACCAACGGCAAGCGCACCTTTCCCGGCGTGGGCATCTCCATCGGCCTGTCCCGGCTCCTGGCCCGTGTCATCGGCGAGGGGCTCGTGGAGGTCAGCCGCTCCGTGCCCACGGCGGTGCTCGTGGCTGTCACCGACGAGGCCCACCGCTGCGCCTCCGACGCCATCGCCGATGCGCTGCGCGCCCGTGGCATCAGTGCCGACGTGGCCCCCAGTGCCGCCAAGTTCGGCAAGCAGATCAAGGCTGCGGACAAGCGGTCTATCCCCTTCGTGTGGTTCCCCGGCGCCGAGGGGGCCCCCGACTCGGTCAAGGACATCCGCTCCGGCGCGCAGGTCGAGGCCGACGCCGCCACCTGGCAGCCGCCCACCGCCGACGCCGCCCCTCGGGTCGCCGTCAGCTCGGCTGCGGCCTGTTCCCAGGCCGGTGGCCAGGACGGCTGTGAGGTCGGCTCAGCCTCATGA","MAQVRQALSSLSGFPEWLPSGHIVEQHFVDILRRTFELHGFSGIQTRAVEPLSELTKKGETSKEVYLLSRLQADPAESEADPRKQLGLHFDLTVPFARYVVDNAGLLTFPFKRYQIQKVWRGERPQEGRFREFIQADIDIVGDGALPLHHDVEVPLIMHEALSALPVPEVTIHVSNRKVAQGFYQSIGIDTDRLIEVLRVVDKLDKIGPEKVAAELTQSVGVSAQQAAQALRLATITGTDGQDVSDQVLRALAGAEPTELLNEGLAELTALLEATGRRRPGAVIADLKIARGLDYYTGTVYESFMAGHEDLGSVCSGGRYDSLATNGKRTFPGVGISIGLSRLLARVIGEGLVEVSRSVPTAVLVAVTDEAHRCASDAIADALRARGISADVAPSAAKFGKQIKAADKRSIPFVWFPGAEGAPDSVKDIRSGAQVEADAATWQPPTADAAPRVAVSSAAACSQAGGQDGCEVGSAS$","Histidine--tRNA ligase","Cytoplasm","histidyl-tRNA synthetase","histidine--tRNA ligase ","Histidine--tRNA ligase","","Wolf Y.I., Aravind L., Grishin N.V., Koonin E.V. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999. 9(8):689-710. PMID: 10447505Aberg A., Yaremchuk A., Tukalo M., Rasmussen B., Cusack S. Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase. Biochemistry 1997. 36(11):3084-3094. PMID: 9115984","","","

InterPro
IPR002314
Domain

tRNA synthetase, class II (G, H, P and S)
PF00587	$\"[24-143]T$	tRNA-synt_2b

InterPro
IPR004154
Domain

Anticodon-binding
G3DSA:3.40.50.800	$\"[360-442]T$	no description
PF03129	$\"[361-449]T$	HGTP_anticodon

InterPro
IPR004516
Family

Histidyl-tRNA synthetase, class IIa
PIRSF001549	$\"[6-458]T$	Histidyl-tRNA synthetase

InterPro
IPR015805
Family

Histidyl-tRNA synthetase
PTHR11476	$\"[3-451]T$	HISTIDYL-TRNA SYNTHETASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[6-354]T$	no description

","BeTs to 26 clades of COG0124COG name: Histidyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0124 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB004154 (Anticodon binding domain) with a combined E-value of 7.2e-06. IPB004154B 110-123 IPB004154C 126-135","Residues 26-103 are 76% similar to a (SYNTHETASE LIGASE BIOSYNTHESIS AMINOACYL-TRNA HISTIDYL-TRNA HISTIDINE--TRNA HISRS ATP-BINDING PHOSPHORIBOSYLTRANSFERASE ATP) protein domain (PD836836) which is seen in SYH_BIFLO.Residues 114-165 are 80% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA HISTIDYL-TRNA BIOSYNTHESIS HISTIDINE--TRNA HISRS ATP-BINDING PHOSPHORIBOSYLTRANSFERASE REGULATORY) protein domain (PD001912) which is seen in Q6A8J7_PROAC.Residues 171-236 are 71% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA HISTIDYL-TRNA HISTIDINE--TRNA ATP-BINDING HISRS BIOSYNTHESIS TRNA KINASE) protein domain (PD481466) which is seen in SYH_BIFLO.Residues 286-339 are 90% similar to a (SYNTHETASE LIGASE BIOSYNTHESIS AMINOACYL-TRNA HISTIDYL-TRNA ATP-BINDING HISTIDINE--TRNA HISRS PHOSPHORIBOSYLTRANSFERASE ATP) protein domain (PD537931) which is seen in Q6A8J7_PROAC.Residues 340-446 are 72% similar to a (SYNTHETASE AMINOACYL-TRNA HISTIDYL-TRNA) protein domain (PDA150L2) which is seen in Q6A8J7_PROAC.Residues 375-414 are 82% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS THREONYL-TRNA HISTIDYL-TRNA PROLYL-TRNA HISTIDINE--TRNA HISRS) protein domain (PD000606) which is seen in SYH_BIFLO.","","-37% similar to PDB:1WU7 Crystal structure of histidyl-tRNA synthetase from Thermoplasma acidophilum (E_value = 6.1E_15);-39% similar to PDB:1HTT HISTIDYL-TRNA SYNTHETASE (E_value = 1.2E_13);-39% similar to PDB:1KMM HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE (E_value = 1.2E_13);-39% similar to PDB:1KMN HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDINOL AND ATP (E_value = 1.2E_13);-41% similar to PDB:1ADJ HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH HISTIDINE (E_value = 5.8E_13);","Residues 24 to 187 (E_value = 1e-07) place ANA_0846 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T).Residues 361 to 449 (E_value = 0.005) place ANA_0846 in the HGTP_anticodon family which is described as Anticodon binding domain.","","synthetase (hisS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0847","912400","911585","816","4.76","-20.39","28746","ATGATCTTGGAGCGCACCATCGCACCCGTGTTCGCCGCCAACTGCTACGTCCTGGCCGCAGGCCCGGGCGAACCCGCCCTCGTCGTCGACCCCGGAGCCGGTGCCGCCCGCGGCGCGCTGGCTCTGCTTCGCTCCCATCGGCTCACCCTGAGCGCCATCCTGCTCACCCACGGTCACGCAGACCACGTGTGGGACAGTCAAACACTCATCGAGGCCGCCCACGCCGAGGGCCTGCTCACCAGCGACGACGCCGTCGACGTGCCGGTATACATCCCCGAGCGCGACCGCTACCGGCTCGAGGAGCCCGACATCACCACCGGTATCAGCGCCAACGGCATGACCTTCACCGACATGGCCGGCGGCGAGTGGAAGCAGCCCGCCGACATCCGTCTCTTCCCGGGAGACGGTTTCTCCCAGGCCATCGAGCTGGCCCCCGGCATCGCGCTGCGTGCGGTCCCTGCTCCGGGTCACTCGGAGGGCTCCACGCTGTTCTTCTTCGAGGCCCGCCTGGCTGACAACGCCCTGCTCTACGAGGCCGAGGTCATCGATGACGACCCCGCCGTCGCTGACGAGGAGCACACCTACCTCATGGCCCTCGACGGAGACGTCATCTTCAAGGGCTCCGTGGGACGCACCGATCTGCCCGGCGGGGACCAGGTTCAGATGCTCGCCACCCTGCGCTTCCTGGCCAACGCCGTCGACCCGGCCACCATTCTGCTGCCCGGGCACGGCGCAGTGACCACCATGGAGCACGAGCACCACGGCAACCCCTACCTCGCTGAGGCCAAGATCCGTGGGGGAGACCTCAAGGCCTGA","MILERTIAPVFAANCYVLAAGPGEPALVVDPGAGAARGALALLRSHRLTLSAILLTHGHADHVWDSQTLIEAAHAEGLLTSDDAVDVPVYIPERDRYRLEEPDITTGISANGMTFTDMAGGEWKQPADIRLFPGDGFSQAIELAPGIALRAVPAPGHSEGSTLFFFEARLADNALLYEAEVIDDDPAVADEEHTYLMALDGDVIFKGSVGRTDLPGGDQVQMLATLRFLANAVDPATILLPGHGAVTTMEHEHHGNPYLAEAKIRGGDLKA$","Metallo-beta-lactamase family protein","Cytoplasm","possible hydrolase","metallo-beta-lactamase family protein","beta-lactamase domain protein","","Carfi A., Pares S., Duee E., Galleni M., Duez C., Frere J.M., Dideberg O. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 1995. 14(20):4914-4921. PMID: 7588620","","","

InterPro
IPR001279
Domain

Beta-lactamase-like
PF00753	$\"[12-169]T$	Lactamase_B

noIPR
unintegrated

unintegrated
G3DSA:3.60.15.10	$\"[2-259]T$	no description
PTHR11935	$\"[201-249]T$	BETA LACTAMASE DOMAIN
PTHR11935:SF8	$\"[201-249]T$	BETA LACTAMASE DOMAIN

","BeTs to 19 clades of COG0491COG name: Zn-dependent hydrolases, including glyoxylasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0491 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 1-122 are 50% similar to a (HYDROLASE POSSIBLE METALLO-BETA-LACTAMASE SUPERFAMILY) protein domain (PD515561) which is seen in Q827T1_STRAW.Residues 14-243 are 40% similar to a (HYDROLASE HYDROXYACYLGLUTATHIONE II GLYOXALASE PROBABLE ZINC GLX METALLO-BETA-LACTAMASE FAMILY GLOB) protein domain (PD000482) which is seen in Q72I73_THET2.","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 243 (E_value = 1.4e-13) place ANA_0847 in the Lactamase_B family which is described as Metallo-beta-lactamase superfamily.","","hydrolase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0848","914202","912481","1722","6.29","-7.82","61966","GTGCCCCCGCCTCGGCGACTGCTGGCGCTGTTAACATGTGACCATGCTTGCGTGACTCGCTCCTGTGCCCCCACCGCCTCATGCCAAGGACGAGTCATGCCTGCGATCAGTTTCTCCCATGTCAGCTTCTCCTACACCTCCGCCCCCTTGCTGGAGAGCATCAACCTCACGGTCTCCGACGACGAACGCGTCTGCGTCGTCGGCCCCAACGGATCGGGGAAGTCCACGCTCCTGCGCCTGGCCACCGGTGAGCTGTCGCCTGACCAGGGGACTGTCAGCATTCCCGAGCAGCATGGTCGGCCGGCGGCCGACTCGGAGGAGTCGACCGCCACGTCGATCGAGGGCTATCTCGACACCGTCTGCGTTGAGACTCTGGACGCGCTTGATCGTTTCGAGCGCATGGGCGAGGCCATCGCCCATGCCGGAGCTGAAGCCGGCTCCCTCGCTGAGGAGTTCGCTGAGGAGTACGACTCGTTACTGACCCGGCTCGAGTCGCTGGACGCCTGGAATCTGCCGGCTCGGCGGGCTGAGGCGCTCGCCGGGCTGGGACTGGGACAGGTGGACACAGGCCGCCTGGTCTCTTCCCTGTCGCCGGGCCAACGGGGGAGGCTGGAGATCGCGGCTCTGCTTCTTTCGGCCGGTCAAGCGCTGGTGCTCGACGAGCCCACCAACCACCTGGATGCCGGTAGCAGTAGCTACCTGAGCGAGATGATGGTGTCATGGCCCGGACCGGTCCTTTTCTCCTCTCACGATCGTGCCTTCATTGACGAGGTGGCCACCGCCGTCGTCGACCTCGACACAGCGCCGTGGCAGGCACTCGCCACCGCCTCCGGGGACAGCGGCCCCATGGGTGCCTACCGGTGCGCGGGGCGATACAGCGACTACCTCGTGGAGAAGGCGCACGCCAGGTCCTCCCACCGCAGTCTTCACCAGCGTCAGCAGGAGCAGCGGCGCAAGCTCGTGCGTCACCGTCGTGACTCCGAGATCGTTGGGCACAGCGGGGCAGCGCCCCGGAGTGAGGCCCGCATCGCCCGGAAGTTCTATGCCGACCGTGCCCAGCGCGTTTCCACCCGACGCCAGACGCAGGACGACCGCCGGCTGGAGGCGCTCGCCAGTACCGAGGTGCGCAGGCCCCGCTCCTACGACCTGCAGCTGCGTCTGGCTGAACCGGCGCCGCGAACAGGGACGGCGGTCTCAGCCCGGTCAGCTGCCGTACCCGGGCGCCTTGCACCGGTCACGATCGACGTCATGGCAGGCGAGCACCTGCTGGTCACCGGCGCCAATGGGAGCGGCAAGTCCACGCTTCTGACCTGGATGGGTAGACGGTCAGCACCCACGGAGGACTCCGTCGGCAGCCTCACAGTAGCTGGTTCAGTGCTCCAGATACCCCAGCACCTGCCGAAACTCGGCGACCCTGGGGTGGATGAGAGCGTGTGGACCGAGGGGATCGGGGACCGTGGCCGGGGGGCTCTGCACCCACGCCTGTGGAACCATCCCATCAGCGAGCTCTCCGACGGCAACCAGCGCCGCGTTCAGCTGGCCCTGGCCGCTGCTGCAGGGCCTGAGGTGCTCGTCATCGACGAGCCCACGAACTACCTGGACCTGGACGCCCTCGAGATGCTCGAGGCCGCTCTGAGGACATGGACGGGCACGCTCATCGTCGCCAGCCACGACCGCTGGCTCATTGAGCACTGGTGGGGGAGGCGGCTTCACCTTCGGTGA","VPPPRRLLALLTCDHACVTRSCAPTASCQGRVMPAISFSHVSFSYTSAPLLESINLTVSDDERVCVVGPNGSGKSTLLRLATGELSPDQGTVSIPEQHGRPAADSEESTATSIEGYLDTVCVETLDALDRFERMGEAIAHAGAEAGSLAEEFAEEYDSLLTRLESLDAWNLPARRAEALAGLGLGQVDTGRLVSSLSPGQRGRLEIAALLLSAGQALVLDEPTNHLDAGSSSYLSEMMVSWPGPVLFSSHDRAFIDEVATAVVDLDTAPWQALATASGDSGPMGAYRCAGRYSDYLVEKAHARSSHRSLHQRQQEQRRKLVRHRRDSEIVGHSGAAPRSEARIARKFYADRAQRVSTRRQTQDDRRLEALASTEVRRPRSYDLQLRLAEPAPRTGTAVSARSAAVPGRLAPVTIDVMAGEHLLVTGANGSGKSTLLTWMGRRSAPTEDSVGSLTVAGSVLQIPQHLPKLGDPGVDESVWTEGIGDRGRGALHPRLWNHPISELSDGNQRRVQLALAAAAGPEVLVIDEPTNYLDLDALEMLEAALRTWTGTLIVASHDRWLIEHWWGRRLHLR$","ATPase component of ABC transporter with duplicated ATPase domain","Periplasm, Membrane, Cytoplasm","ABC-type transporter, duplicated ATPasecomponent","putative ABC transporter ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[195-238]T$	Q6AF27_BBBBB_Q6AF27;
PF00005	$\"[61-268]T$ $\"[419-573]T$	ABC_tran
PS50893	$\"[36-292]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[60-269]T$ $\"[418-571]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[36-266]T$ $\"[358-573]T$	no description
PTHR19211	$\"[166-329]T$ $\"[352-563]T$	ATP-BINDING TRANSPORT PROTEIN-RELATED

InterPro
IPR007139
Repeat

Protein of unknown function DUF349
PF03993	$\"[344-420]T$ $\"[421-497]T$	DUF349

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 177-225 are 77% similar to a (INVOLVED ALANINE DNA ARGININE RICH REPAIR ATPASE SCO1511) protein domain (PD123647) which is seen in Q8G865_BIFLO.Residues 231-347 are 58% similar to a (INVOLVED ALANINE DNA ARGININE RICH REPAIR ATPASE SCO1511 B2235_F2_77) protein domain (PD039505) which is seen in Q8G865_BIFLO.Residues 297-436 are 46% similar to a () protein domain (PD697009) which is seen in Q83HV2_TROW8.Residues 392-434 are 81% similar to a (ALANINE ARGININE RICH SCO1511 INVOLVED DNA REPAIR ATPASE) protein domain (PD123649) which is seen in Q73W17_MYCPA.Residues 392-435 are 79% similar to a (INVOLVED DNA REPAIR ATPASE ALANINE ARGININE RICH) protein domain (PD871017) which is seen in Q7TY07_MYCBO.Residues 437-530 are 65% similar to a (INVOLVED DNA REPAIR ATPASE SCO1511) protein domain (PD862951) which is seen in Q6A8J9_PROAC.Residues 437-531 are 58% similar to a (PLECTIN REPEAT COILED COIL EXONUCLEASE CHROMOSOME DNA LIPOPROTEIN MEMBRANE TC3_70K14.5) protein domain (PD686717) which is seen in Q7TY07_MYCBO.","","No significant hits to the PDB database (E-value < E-10).","Residues 344 to 420 (E_value = 1.3e-19) place ANA_0850 in the DUF349 family which is described as Domain of Unknown Function (DUF349).Residues 421 to 497 (E_value = 1.2e-08) place ANA_0850 in the DUF349 family which is described as Domain of Unknown Function (DUF349).","","of Unknown Function (DUF349) family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0850.1","916293","916817","525","5.15","-5.58","19492","ATGTGCATAATCATGTTCATGCCAACACGAAACGTCTATGTTTCAGAGGATGATGTGAGCCTTTTCGCTGAGGCGGGGGAGATCGCCGGTAGTCTCTCGTCTGCCATCGTTGAGGCCCTCCGTGACTATGTCAAGAAGCGTGGCCACTCGGCCGAGGGCTATCAGGAGATCGAACTGAAGCTGTCTACGGGCGACGTGGATCGTCGGGTCACGTTCGTCGGTCGACGCCTGGTGCGCCTGACGAGACCGGATCCTGAGGGGACCCGCATCGACACGGTCTACCTCACAGCCAAGGGCCAGCTGGCTGTAGCGACAAAGGTTCAGAGGAGGCTGCCGGACTGGACTGCTGGCCAGGACGACCTTTGGTCCAACCCGGAAACATGGAGTCGGAACTTCTGGATCGCCGGGGACAGAACTCTGAGTGTCTTCCCAGACATTGATCACCTTCAAAAGGAGGATCCGGTTATGGCAGAGCAAGCCCGGGCGGCGCTGGCCACTCCGGCTCTCGAGGTCTTGGACATCTGA","MCIIMFMPTRNVYVSEDDVSLFAEAGEIAGSLSSAIVEALRDYVKKRGHSAEGYQEIELKLSTGDVDRRVTFVGRRLVRLTRPDPEGTRIDTVYLTAKGQLAVATKVQRRLPDWTAGQDDLWSNPETWSRNFWIAGDRTLSVFPDIDHLQKEDPVMAEQARAALATPALEVLDI$","Hypothetical protein","Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-174 are similar to a () protein domain (PDA0Q5O6) which is seen in Q6ABI7_PROAC.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:18:33 2007","Thu Aug 2 10:18:33 2007","Thu Aug 2 10:18:33 2007","Thu Aug 2 10:17:33 2007","","","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","Thu Aug 2 10:17:33 2007","","Thu Aug 2 10:17:33 2007","","Thu Aug 2 10:17:33 2007","yes","","" "ANA_0851","917183","917551","369","9.45","4.87","13641","GTGGGCAAAAGAGTCCGAGAACGCGACAAGGAGAAAAGGCTATCCCCGTCCAAGCGCAAGGCCAAGAGCAAACTCGTCGACGGACAGGTCACCACCGACTGGAACAAGACCCTGACCCAGTTCACCACCGCCTACCTCAACCGAATCAATCTAAACCTTACACAAAACACTGGACAGGCTCGTGAGGGACTCACCGACTACCTCGTCGATATTATTTCAGACCTTGAGACGGTGGACTGGGGGATACCGGACTCATTGCCCAACGTCTGCATGAGGTCACCAGACCTTACGGGTGGAAATCCCTCGATTCAGGCCTGGCAGATCATGGCGGTGGTGCCAGCGTCGCTCAGGTCCTGCAGACCAACCTGA","VGKRVRERDKEKRLSPSKRKAKSKLVDGQVTTDWNKTLTQFTTAYLNRINLNLTQNTGQAREGLTDYLVDIISDLETVDWGIPDSLPNVCMRSPDLTGGNPSIQAWQIMAVVPASLRSCRPT$","Hypothetical protein","Periplasm, Extracellular","ribosomal protein S3a, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein S3a, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0852","918705","917794","912","5.37","-10.89","33980","ATGTGCCAGGTGGAGCCGGTACTGAGGAAGGAGACTACGGTGAAGGACTCTCAACAGCGTCATGCTGGAGTTGAAGGGCCTGGCAGGCCAGCCGAGACCTCGGTCGATGCTGTGTCGGACGATGTTGACATCGCCATGACGGTCGGTGAGGTCTCAACGCTCCTGGGCGTCAGCGTCAGGGCGCTGCATCACTGGGACGAGTCCGGCCTGGTGCATCCCTCCCAGCGCAGTGCCGCTGGCTACCGGCTCTACAGTGAGGCGGACATCATGCGCCTCCAGCAGGTCCTCGTCTACCGGCAGACCGGCATGAGCCTGGCCGACATCAAGGCAGTCCTTGACGAGCCGGGCGCCGATGCACTGACGCACCTGCGCCGTCAGCGCGAGCTGGTGCAAGGACAGATCTCCCACTTGCAGCACAAGCTCAGCTCCATCGATATGGTGATCGATATACAGCAGCTGGGGGCGAGGATCTCCGTGGCTGAGATGGCGGAGATCTGGGGGACCGACTGGGACCCCGTCTATGTCGAGGAGGCCCGCGCTCAGTGGGGTGATACACCGGAGTGGGCCGAGTCCTACCGGCGCAAGGCTCGGATGTCTCGCGCCGACTGGGAGCAGGCGCACGAGGAGACCGTCGCTCTGGAGGCCGCGCTTGCTGAGGCGATGCGCAACGGCGTCGAACCGGGCAGCCCCGAGGCCAATGCCCTGGCGCGGTGGCACCGCAAGGACTTCAACCGGTGGTTCGAGGTCTCCACCTCTAAGCAGGTCATTATCGCCCGCAGCTATGTGGCGGACGAACGCTATGCCCGCTACTACGACAAGCGCGCGCCTGGTCTGGCGGCCTGGCTCAAGGACGTCATCGACGCATGCGCCAGGTCTGAGGGAGTGGACCCCGCGACCGCCACCTGGGAGTAG","MCQVEPVLRKETTVKDSQQRHAGVEGPGRPAETSVDAVSDDVDIAMTVGEVSTLLGVSVRALHHWDESGLVHPSQRSAAGYRLYSEADIMRLQQVLVYRQTGMSLADIKAVLDEPGADALTHLRRQRELVQGQISHLQHKLSSIDMVIDIQQLGARISVAEMAEIWGTDWDPVYVEEARAQWGDTPEWAESYRRKARMSRADWEQAHEETVALEAALAEAMRNGVEPGSPEANALARWHRKDFNRWFEVSTSKQVIIARSYVADERYARYYDKRAPGLAAWLKDVIDACARSEGVDPATATWE$","Transcriptional regulator, MerR family","Cytoplasm","Predicted transcriptional regulators","transcriptional regulator","TipAS antibiotic-recognition domain protein","","Kahmann J.D., Sass H.J., Allan M.G., Seto H., Thompson C.J., Grzesiek S. Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators. EMBO J. 2003. 22(8):1824-1834. PMID: 12682015","","","

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PR00040	$\"[47-58]T$ $\"[58-71]T$ $\"[82-102]T$	HTHMERR
PF00376	$\"[47-84]T$	MerR
SM00422	$\"[46-115]T$	HTH_MERR
PS50937	$\"[45-114]T$	HTH_MERR_2
PS00552	$\"[49-71]?$	HTH_MERR_1

InterPro
IPR012925
Domain

TipAS antibiotic-recognition
PF07739	$\"[157-290]T$	TipAS

InterPro
IPR015358
Domain

Transcription regulator MerR, DNA binding
PF09278	$\"[89-147]T$	MerR-DNA-bind

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[46-174]T$	no description

","BeTs to 12 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 8","***** IPB012925 (TipAS antibiotic-recognition) with a combined E-value of 1.6e-29. IPB012925A 56-109 IPB012925B 264-273***** IPB000551 (Bacterial regulatory protein, MerR family) with a combined E-value of 1.6e-17. IPB000551 46-86","Residues 51-145 are similar to a (DNA-BINDING TRANSCRIPTIONAL REGULATOR MERR FAMILY REGULATOR REGULATORY PLASMID TRANSCRIPTION ACTIVATOR) protein domain (PD548366) which is seen in TIPA_STRCO.Residues 174-275 are similar to a (DNA-BINDING TRANSCRIPTIONAL ACTIVATOR REGULATOR FAMILY MERR REGULATOR TIPA TRANSCRIPTION REGULATION) protein domain (PD034841) which is seen in Q8FNY6_COREF.","","-64% similar to PDB:1JBG Crystal Structure of MtaN, the Bacillus subtilis Multidrug Transporter Activator, N-terminus (E_value = 2.2E_17);-64% similar to PDB:1R8D Crystal Structure of MtaN Bound to DNA (E_value = 2.2E_17);-48% similar to PDB:1NY9 Antibiotic binding domain of a TipA-class multidrug resistance transcriptional regulator (E_value = 6.1E_12);","Residues 47 to 84 (E_value = 2.5e-12) place ANA_0852 in the MerR family which is described as MerR family regulatory protein.Residues 89 to 147 (E_value = 8e-07) place ANA_0852 in the MerR-DNA-bind family which is described as MerR, DNA binding.Residues 157 to 290 (E_value = 7e-31) place ANA_0852 in the TipAS family which is described as TipAS antibiotic-recognition domain.","","transcriptional regulators","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0853","918801","919433","633","10.99","13.61","22301","GTGGCGCCCGCGACCGGTTGCCGTCCACGATGGCATATGGCTCGTTTCGTCCCGGTACCCGGCCACGCCGCCGTGGCCCACTTGTCCGCTCGCCCGCTGACCCCCGTCCTGGGCACGCTTCCGCCCCAGGACATGGAGGTGCTCAGGTGCGCCGACCTCGATGCCCGGCTGCTGATCAACGTCCTGGGCAACCTGCAACCGGCAGACACTCTGCGCTCGGCCGAGGGACGCATGCGGGCCATTGCCGCAGCCCTGCCCTGCCGGGGTGTGCTGCTGGCAAGCACCGCCCTGTGGGTGCACGTCGGCGGGCCCCCGCCCGAATCCCTGGAGGTGAGCCTGCCCGGAGGCCGTCGAAGTCGACTGCCCTATCTGGTGACCCGACGAGGCCGGCTGCCCCACTGCGACACGACCGTGATCGGGGGCATCACCTGCGCCACGATCGCCCGAGCCGCCGTCGACATTGCCCGCCTGGGTCCACCAGTACAGGCTGTGCAGGCCATCCTGACCGCCCGCAACCACGGAGTGAGCCGAGTGCGCCTTCTGCTCACCCTCAACCACTGCCGGGGGGCCGCCAGCAGAGGCTGCCCGCGGGCGCAGCACATCATCGAGGAGGTCATGGCCTGCGTGCAGTAG","VAPATGCRPRWHMARFVPVPGHAAVAHLSARPLTPVLGTLPPQDMEVLRCADLDARLLINVLGNLQPADTLRSAEGRMRAIAAALPCRGVLLASTALWVHVGGPPPESLEVSLPGGRRSRLPYLVTRRGRLPHCDTTVIGGITCATIARAAVDIARLGPPVQAVQAILTARNHGVSRVRLLLTLNHCRGAASRGCPRAQHIIEEVMACVQ$","Hypothetical protein","Cytoplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0854","921911","919455","2457","7.31","3.36","90336","GTGGCCGGCTGCTTGACGGGTGACCGGGGCTGTTTCTCGTGCGGTGTCGCGCTCCCGAAGGATGCGACACCGCACGCCTACCAGCAGCGCCGGCACGCTTCGGTGTGCTGGCCGCTATATGATGCGTCAATGACGGCGACGAAGAACACCCCGGACACGTCAGGTGACAGTGTTGTCCCCGGCTCGCGCGTGCGCAGCCGTCTGGCGTGGTTCGGCTCCCGGGGGCACTCCACACCGGCGGCCATCGAGCCGCTGCTGCGCGCGGTGCGCGCCAACCACCCCAAGGCCGACACGAGCCTCATCGTGCGCGCCTACGAGGTGGCGGAGAAGGCTCACTCCGGCCAGCGACGCAAGTCCGGGGAGCCCTACATCACTCACCCGGTGGCAGTAGCGACCATCCTGGCTGAGCTGGGGATGACGGCCCAGACCCTGGCGGCAGCCGTCCTACACGACACCGTGGAGGACACCGACTACACCCTCGAGCGCCTGCGCGCCGACTTCGGGGACGAGATCAGCCTGCTCGTCGACGGCGTCACCAAGCTCGACAAGCTCCAGTACGGTGAGGCCGCCCAGGCCGAGACGGTGCGCAAGATGATTATCGCGATGTCCAAGGACATCCGGGTGCTGGTCATCAAGCTCGGCGATCGCCTCCACAACGCCCGCACCTGGAAGTACGTCTCCGCGGAGAACGCCGCCCGCAAGGCCAAGGAGACTCTGGAGATCTACGCGCCCCTGGCCCACCGCCTGGGAATGAACACGATCAAGTGGGAGCTGGAGGACCGGTCCTTCAAGGCCCTCTACCCGGGTGTGTACGAGGAGATCGAGCACATGGTGGCTGAGCGGGCCCCGGCTCGTGAGGAGTACCTGCGTCAGGTCCGCCTCCAGATCGAGGAGGACCTGAGGGTCAACAAGATCAAGGGTGCCGTGACCGGGAGGCCCAAGCACTACTACTCGATCTACCAGAAGATGATCGTGCGGGGGAAGGACTTCGACGACATCTACGACCTGGTGGCGGTGAGGGTCATCGTCGACACCGTCCAGGACTGCTATGCGGTGCTCGGCTCCCTGCATTCACGTTGGACCCCCATGAGCGGGCGCTTCAAGGACTACATCGCCGTCCCCAAGTTCAACCTCTATCAGTCGCTGCACACGACTGTCGTGGGGCCGGGTGGCAAACCGGTGGAGATCCAGATCCGCACCCACGAGATGCACCGCATGGCCGAGTACGGCGTGGCCGCGCACTGGCGTTACAAGGAGGACCCCAACGCCTCGGGTCCCAGCGCCCTGGGAGGCAGGCCCGGAGACTCCGACCAGGGTGACATGGGCTGGCTGCGCCAGCTCGTCGACTGGCAGAAGGAGACCCAGGACCCCACCGAGTTCCTCGATGCCCTGCGCTACGAGATGGCCGGGGACCAGGTCTACGTCTTCACCCCCCGGGGTGATGTCCTCGCACTGCCGGCGGGAGCCACCCCGGTGGACTTCGCCTACGCCGTCCACACCGAGGTCGGCCACCGCACCGTGGGCGCACGCGTCAACAGCCGACTAGTGCCCCTGGACACGCGTCTGGAGAACGGTGACACGGTGGAGGTCTTCACCTCCAAGGCCATCAACGCCGGACCCTCGCGCGACTGGCTCTCCTTCGTGGCCTCTACCCGGGCCCGCAACAAGATCCGTGCCTGGTTCTCCAAGGAGCGTCGCGAGGAGGCCATCGAGGAGGGCAAGGGCGCCATCGCCCGCACCCTGCGCAAGCAGAACCTGCCCCTGCAGCGCCTCATGAGCCACGAGACCCTCATGAACGTGGCCAAGACCCTCGACAAGGTCGACATCGACGGCCTGTACGCCGCGGTGGGTGAGGGGCACGTATCCGCCCAGCACGTCGTCGACACTCTGGTGGCCACCATGGGCGGGGAGGACGGCGCCGAGGAGACCCTCGCGGAGGGAATCCTGCCCACCCGGGCCACGGCGCACCGCCGGCCGCGCACGGCCGACGCCGGAGTCGTCGTCGCCGGCATGGATGAGGGCGACGTCTACGTCAAGCTGGCGCGCTGCTGCACCCCCATGCCGGGCGACCCCATCGTCGGTTTCATCACCCGCGGCTCGGGCGTCTCAGTGCACCGGGCCGACTGCCAGAACGTCGAACAGCTCCAGCGCGAGCCAGAGCGCCTCATCACCGTCTCCTGGGCGGATCACGCCCAGTCGGCCTACCTGGTTCAGGTGGAGGTCGAGGCCCTGGACCGCGGGGGTCTGCTCGCCGACATCACCCGGGCGCTGGCAGACAGCCACGTCAACCTGGTGAGCGCCTCCATCGCCACGAGCCGGGACCGGGTCGTCACCGGCCGGTTCGTCGTCGAGCTGGCCGAGGTCGGGCACCTGGACCACACGCTGGCGGCCCTGCGACGCATCGACGGGGTCTTCGAGGCGCGCAGAAGCCTGTCAGCCGCGCGCCGCTCCAACTGA","VAGCLTGDRGCFSCGVALPKDATPHAYQQRRHASVCWPLYDASMTATKNTPDTSGDSVVPGSRVRSRLAWFGSRGHSTPAAIEPLLRAVRANHPKADTSLIVRAYEVAEKAHSGQRRKSGEPYITHPVAVATILAELGMTAQTLAAAVLHDTVEDTDYTLERLRADFGDEISLLVDGVTKLDKLQYGEAAQAETVRKMIIAMSKDIRVLVIKLGDRLHNARTWKYVSAENAARKAKETLEIYAPLAHRLGMNTIKWELEDRSFKALYPGVYEEIEHMVAERAPAREEYLRQVRLQIEEDLRVNKIKGAVTGRPKHYYSIYQKMIVRGKDFDDIYDLVAVRVIVDTVQDCYAVLGSLHSRWTPMSGRFKDYIAVPKFNLYQSLHTTVVGPGGKPVEIQIRTHEMHRMAEYGVAAHWRYKEDPNASGPSALGGRPGDSDQGDMGWLRQLVDWQKETQDPTEFLDALRYEMAGDQVYVFTPRGDVLALPAGATPVDFAYAVHTEVGHRTVGARVNSRLVPLDTRLENGDTVEVFTSKAINAGPSRDWLSFVASTRARNKIRAWFSKERREEAIEEGKGAIARTLRKQNLPLQRLMSHETLMNVAKTLDKVDIDGLYAAVGEGHVSAQHVVDTLVATMGGEDGAEETLAEGILPTRATAHRRPRTADAGVVVAGMDEGDVYVKLARCCTPMPGDPIVGFITRGSGVSVHRADCQNVEQLQREPERLITVSWADHAQSAYLVQVEVEALDRGGLLADITRALADSHVNLVSASIATSRDRVVTGRFVVELAEVGHLDHTLAALRRIDGVFEARRSLSAARRSN$","(p)ppGpp synthetase I; SpoT/RelA","Cytoplasm","GTP pyrophosphokinase (ATP:GTP3'-pyrophosphotransferase)(ppGpp synthetase I) ((P)ppGpp","(p)ppGpp synthetase I; SpoT/RelA ","RelA/SpoT family protein","","Wolf Y.I., Aravind L., Grishin N.V., Koonin E.V. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999. 9(8):689-710. PMID: 10447505","","","

InterPro
IPR002912
Domain

Amino acid-binding ACT
PF01842	$\"[737-803]T$	ACT

InterPro
IPR003607
Domain

Metal-dependent phosphohydrolase, HD region
SM00471	$\"[119-229]T$	HDc

InterPro
IPR004095
Domain

TGS
PF02824	$\"[473-532]T$	TGS

InterPro
IPR004811
Family

RelA/SpoT protein
TIGR00691	$\"[104-809]T$	spoT_relA: RelA/SpoT family protein

InterPro
IPR006674
Domain

Metal-dependent phosphohydrolase, HD region, subdomain
PF01966	$\"[123-220]T$	HD

InterPro
IPR007685
Domain

RelA/SpoT
PF04607	$\"[311-421]T$	RelA_SpoT

InterPro
IPR012675
Domain

Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30	$\"[472-535]T$	no description

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[749-801]T$	no description

noIPR
unintegrated

unintegrated
PTHR21262	$\"[192-812]T$	GUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE

","BeTs to 16 clades of COG0317COG name: Guanosine polyphosphate pyrophosphohydrolases/synthetasesFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0317 is -------qvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB007685 (RelA/SpoT) with a combined E-value of 3.5e-196. IPB007685A 112-127 IPB007685B 146-156 IPB007685C 191-223 IPB007685D 229-267 IPB007685E 317-370 IPB007685F 379-419 IPB007685G 473-513 IPB007685H 680-706***** IPB013546 (GlnD PII-uridylyltransferase) with a combined E-value of 1.5e-06. IPB013546K 747-782 IPB013546J 735-781","Residues 94-216 are 60% similar to a (KINASE GTP PYROPHOSPHOKINASE TRANSFERASE SYNTHETASE ATP:GTP I PPPGPP 3_apos;-PYROPHOSPHOTRANSFERASE PPGPP) protein domain (PD100595) which is seen in Q6AP30_BBBBB.Residues 97-248 are 51% similar to a () protein domain (PDA022O3) which is seen in Q702A8_AAAAA.Residues 107-144 are 92% similar to a (HYDROLASE GTP KINASE PYROPHOSPHOKINASE GUANOSINE-3_apos;5_apos;-BISDIPHOSPHATE 3_apos;-PYROPHOSPHOHYDROLASE SYNTHETASE TRANSFERASE PPPGPP PPGPP) protein domain (PD529638) which is seen in Q6AFA9_BBBBB.Residues 108-216 are 56% similar to a (KINASE RELA/SPOT GTP FAMILY PYROPHOSPHOKINASE) protein domain (PD789698) which is seen in Q8A9W5_BACTN.Residues 146-193 are 91% similar to a (HYDROLASE GTP KINASE PYROPHOSPHOKINASE GUANOSINE-3_apos;5_apos;-BISDIPHOSPHATE 3_apos;-PYROPHOSPHOHYDROLASE SYNTHETASE TRANSFERASE PPPGPP PPGPP) protein domain (PD002764) which is seen in Q93AJ7_STRCL.Residues 221-306 are 77% similar to a (GTP KINASE PYROPHOSPHOKINASE HYDROLASE TRANSFERASE SYNTHETASE GUANOSINE-3_apos;5_apos;-BISDIPHOSPHATE 3_apos;-PYROPHOSPHOHYDROLASE PPPGPP PPGPP) protein domain (PD334556) which is seen in RELA_STRCO.Residues 309-418 are similar to a (KINASE GTP PYROPHOSPHOKINASE HYDROLASE TRANSFERASE SYNTHETASE GUANOSINE-3_apos;5_apos;-BISDIPHOSPHATE 3_apos;-PYROPHOSPHOHYDROLASE PPPGPP PPGPP) protein domain (PD002902) which is seen in RELA_STRCO.Residues 459-535 are 94% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA GTP KINASE PYROPHOSPHOKINASE THREONINE--TRNA HYDROLASE BIOSYNTHESIS) protein domain (PD471591) which is seen in Q93AJ7_STRCL.Residues 540-601 are 88% similar to a (GTP KINASE PYROPHOSPHOKINASE HYDROLASE SYNTHETASE TRANSFERASE GUANOSINE-3_apos;5_apos;-BISDIPHOSPHATE PPPGPP 3_apos;-PYROPHOSPHOHYDROLASE PPGPP) protein domain (PD789417) which is seen in RELA_STRAT.Residues 630-725 are 73% similar to a (GTP KINASE PYROPHOSPHOKINASE HYDROLASE SYNTHETASE TRANSFERASE GUANOSINE-3_apos;5_apos;-BISDIPHOSPHATE PPPGPP 3_apos;-PYROPHOSPHOHYDROLASE PPGPP) protein domain (PD003989) which is seen in Q827T4_STRAW.Residues 739-806 are 76% similar to a (KINASE GTP PYROPHOSPHOKINASE HYDROLASE TRANSFERASE SYNTHETASE GUANOSINE-3_apos;5_apos;-BISDIPHOSPHATE PPPGPP 3_apos;-PYROPHOSPHOHYDROLASE PPGPP) protein domain (PD387799) which is seen in RELA_STRCO.","","-67% similar to PDB:1VJ7 Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis. (E_value = 3.1E_97);","Residues 123 to 220 (E_value = 2.6e-12) place ANA_0854 in the HD family which is described as HD domain.Residues 311 to 421 (E_value = 8.4e-56) place ANA_0854 in the RelA_SpoT family which is described as Region found in RelA / SpoT proteins.Residues 473 to 532 (E_value = 2.6e-30) place ANA_0854 in the TGS family which is described as TGS domain.Residues 737 to 803 (E_value = 7.2e-10) place ANA_0854 in the ACT family which is described as ACT domain.","","pyrophosphokinase (ATP:GTP 3-pyrophosphotransferase)(ppGpp synthetase I) ((P)ppGpp synthetase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0855","922525","921965","561","5.09","-6.35","19674","ATGACCACCGCTCCCGTGGCCCATTCCGAGTCGGTGCCCGAGTCCCTGACCAAGTTGGTCATGAGCCATCTGCGCGAGATTCCCGACTTCCCCGAGCCGGGGGTCCTCTTCCGGGACATCACTCCGCTCCTGGCCGACGGACAGGCCTTCGCCGCTCTCGTCGAGGGGCTGGCCGATCACTACCGGGGTCGGATCGATGCGATCGCGGGGCTCGAGTCGCGCGGCTTCATCCTGGCAGCGCCCTTGGCGGTTCGGCTCGGGGTCGGCATGATCACGGTGCGCAAGGGCGGCAAGCTGCCCGGCCCGGTCATCGGCGTGGACTACGCACTCGAGTACGGCACGGCCCGGATGGAGCTGCGGCCCGAGACCGTCACCAAGGGCGCACGTGTCCTGGTCATCGACGATGTGCTGGCCACCGGTGGGACGGCCTCCGCCTCCATCTCCCTCATTGAGCAGGCCGGTGCCTCAGTGGAGGCCATCTGCATGCTTCTGGAGCTGTCCGATCTCGACGGTCGTCGCCAACTCCAGGGGCGTGAGGTCGACTCGATCGTCATCTTCTGA","MTTAPVAHSESVPESLTKLVMSHLREIPDFPEPGVLFRDITPLLADGQAFAALVEGLADHYRGRIDAIAGLESRGFILAAPLAVRLGVGMITVRKGGKLPGPVIGVDYALEYGTARMELRPETVTKGARVLVIDDVLATGGTASASISLIEQAGASVEAICMLLELSDLDGRRQLQGREVDSIVIF$","Adenine phosphoribosyltransferase","Cytoplasm","adenine phosphoribosyltransferase","adenine phosphoribosyltransferase ","adenine phosphoribosyltransferase","","Hershey H.V., Taylor M.W. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene 1986. 43(3):287-293. PMID: 3527873","","","

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[39-174]T$	Pribosyltran

InterPro
IPR002375
Family

Purine/pyrimidine phosphoribosyl transferase
PS00103	$\"[130-142]T$	PUR_PYR_PR_TRANSFER

InterPro
IPR005764
Family

Adenine phosphoribosyl transferase
TIGR01090	$\"[20-186]T$	apt: adenine phosphoribosyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2020	$\"[11-180]T$	no description

","BeTs to 20 clades of COG0503COG name: Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteinsFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0503 is -om-kzy-vdrlbcefgh-nuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002375 (Purine/pyrimidine phosphoribosyl transferase) with a combined E-value of 1e-07. IPB002375 127-142","Residues 20-157 are 51% similar to a (ADENINE PHOSPHORIBOSYLTRANSFERASE TRANSFERASE GLYCOSYLTRANSFERASE PLASMID) protein domain (PD546495) which is seen in Q93CK4_ENTFA.Residues 24-59 are 88% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE ADENINE PHOSPHORIBOSYLTRANSFERASE APRT SALVAGE PURINE STRAIN CHROMOSOME FORM) protein domain (PD028734) which is seen in APT_STRCL.Residues 71-122 are similar to a (TRANSFERASE GLYCOSYLTRANSFERASE ADENINE PHOSPHORIBOSYLTRANSFERASE APRT SALVAGE PURINE STRAIN CHROMOSOME FORM) protein domain (PD001933) which is seen in APT_SYNPX.Residues 127-184 are 67% similar to a (ADENINE PHOSPHORIBOSYLTRANSFERASE TRANSFERASE APRT GLYCOSYLTRANSFERASE SALVAGE PURINE) protein domain (PDA0J1P4) which is seen in APT_BIFLO.Residues 130-180 are 68% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE ADENINE PURINE SALVAGE APRT XANTHINE REPRESSOR OPERON) protein domain (PD544262) which is seen in O07491_BACAN.","","-66% similar to PDB:1ORE Human Adenine Phosphoribosyltransferase (E_value = 2.6E_37);-66% similar to PDB:1ZN7 Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P (E_value = 2.6E_37);-66% similar to PDB:1ZN8 Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution (E_value = 2.6E_37);-66% similar to PDB:1ZN9 Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms (E_value = 2.6E_37);-65% similar to PDB:2DY0 Crystal structure of project JW0458 from Escherichia coli (E_value = 3.5E_34);","Residues 39 to 174 (E_value = 2.5e-35) place ANA_0855 in the Pribosyltran family which is described as Phosphoribosyl transferase domain.","","phosphoribosyltransferase (apt)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0856","923625","922522","1104","9.53","10.13","39074","GTGAAGTCTCTCGCCACGCTCGGTAACGAGCTCTACTCGGCCAAGACATCCATCGCCTTCGTCGGCAAACGGAAGATCTGGTATCTCATCGCCGTCGTCATCATTCTTGGCTCGGCCACGCTCCTGGGCACTGTGGGACTGACTCCGGGTATCGACTTCAAGGGCGGTTCGGAGATCACCGTCACGGGGCTGTCCTCCCCCTCAGAGCGTCCTGCCAACGAGGTCCTCTCCAAGAGCGACCTGGCGGCCAGTTCCTCGGTCACCACCATGGGGTCGTCGTCGGTCAGGGTGCAGACCTCTGAGCTGAGCAAGCAGCGTCTCGACTCGCTGGCCGGTCAGCTCGCCACCGCCTACAAGACCGATGCCTCCAATGTCTCAGCGACGACCGTGGGACCGACCTGGTCCTCCGACGTCACGAAGAAGGCGATTCGAGGACTGGTCCTGTTCTTCATCTTCGTCGGACTGCTCATCTGGGCGTACTTCCGCACCTGGAAGATGGCGGCGGCGGCCCTGCTCGCCCTGTGCCACGACATCATCGTCACCGTGGGCATCTACGCCCTGTCCGGATTCGAGGTCACCCCGGCCACGATCATCGGTGTGCTGACGATTCTGGGCTACTCCCTCTACGACACGGTGGTGGTCTTCGACAAGATCCGTGAGAACACCGAGGACTTCGAGTCCCAGAGCCGATCCACCTACGCCGAGCTGGCGAACCTGGCGGTCAACCAGACCTTCATCCGATCGATCAACACCTCCGTGGTCGGTGTGCTCCCGGTGGCCTCGCTGCTGTTCGTCGGAGCCTTCATCCTGGGCGCAGGAACGCTTCGTGACATCGCCCTGACGCTGTTCATCGGTATGATCGCCGGAACCCTGTCCTCGATCTTCCTGGCCACCCCCCTCCTAGTGGACCTGCGTTCACGTGAGAAGCGCATCAAGGAACACACCGCCAAGGTCGCCGCGGCGCGCCAGCACCGTCGGGACGAGGCCGGTGACGATGCCGAGGAACTGGCTAAGATTGACGCGGCTCCGGCCGCCTCACCAGTCACTCCCGGCCACCACCTCGGCGTGGCGGCTCAGCCTAAAAGGAAGAAGAAGCGCAGATGA","VKSLATLGNELYSAKTSIAFVGKRKIWYLIAVVIILGSATLLGTVGLTPGIDFKGGSEITVTGLSSPSERPANEVLSKSDLAASSSVTTMGSSSVRVQTSELSKQRLDSLAGQLATAYKTDASNVSATTVGPTWSSDVTKKAIRGLVLFFIFVGLLIWAYFRTWKMAAAALLALCHDIIVTVGIYALSGFEVTPATIIGVLTILGYSLYDTVVVFDKIRENTEDFESQSRSTYAELANLAVNQTFIRSINTSVVGVLPVASLLFVGAFILGAGTLRDIALTLFIGMIAGTLSSIFLATPLLVDLRSREKRIKEHTAKVAAARQHRRDEAGDDAEELAKIDAAPAASPVTPGHHLGVAAQPKRKKKRR$","Protein-export membrane protein secF","Membrane, Cytoplasm","Protein-export membrane protein secF","protein-export membrane protein SecF","protein-export membrane protein SecF","","Bieker K.L., Phillips G.J., Silhavy T.J. The sec and prl genes of Escherichia coli. J. Bioenerg. Biomembr. 1990. 22(3):291-310. PMID: 2202721Driessen A.J. SecB, a molecular chaperone with two faces. Trends Microbiol. 2001. 9(5):193-196. PMID: 11336818Muller J.P. Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. FEMS Microbiol. Lett. 1999. 176(1):219-227. PMID: 10418149Breyton C., Haase W., Rapoport T.A., Kuhlbrandt W., Collinson I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 2002. 418(6898):662-665. PMID: 12167867Bolhuis A., Broekhuizen C.P., Sorokin A., Van roosmalen M.L., Venema G., Bron S., Quax W.J., van Dijl J.M. SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. J. Biol. Chem. 1998. 273(33):21217-21224. PMID: 9694879","","","

InterPro
IPR003335
Family

SecD/SecF/SecDF export membrane protein
PR01755	$\"[45-60]T$ $\"[205-223]T$ $\"[240-255]T$	SECFTRNLCASE
PF02355	$\"[113-307]T$	SecD_SecF
PF07549	$\"[41-69]T$	Sec_GG
TIGR00916	$\"[107-294]T$	2A0604s01: protein-export membrane protein,

InterPro
IPR005665
Family

SecF protein
TIGR00966	$\"[46-297]T$	3a0501s07: protein-export membrane protein

noIPR
unintegrated

unintegrated
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[26-46]?$ $\"[142-160]?$ $\"[170-190]?$ $\"[196-216]?$ $\"[254-276]?$ $\"[282-302]?$	transmembrane_regions

","BeTs to 21 clades of COG0341COG name: Preprotein translocase subunit SecFFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0341 is -om-k--qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003335 (Bacterial translocase SecF protein signature) with a combined E-value of 6.3e-19. IPB003335A 45-60 IPB003335C 205-223 IPB003335D 240-255","Residues 165-290 are 61% similar to a (EFFLUX FAMILY RESISTANCE TRANSPORTER TRANSMEMBRANE MULTIDRUG ACRB/ACRD/ACRF RND SYSTEM CATION) protein domain (PD001797) which is seen in Q83CH4_COXBU.Residues 187-265 are similar to a (MEMBRANE PROTEIN-EXPORT SECF SUBUNIT TRANSLOCASE PREPROTEIN TRANSMEMBRANE TRANSLOCATION SECDF PROTEIN) protein domain (PD000801) which is seen in Q741P5_MYCPA.Residues 228-308 are 60% similar to a (MEMBRANE PROTEIN-EXPORT SECDF) protein domain (PD642993) which is seen in Q9ZBS8_STRCO.Residues 231-267 are 83% similar to a (MEMBRANE PROTEIN-EXPORT SECF) protein domain (PD917217) which is seen in Q83NI0_TROW8.Residues 268-307 are 82% similar to a (MEMBRANE PROTEIN-EXPORT SECF SUBUNIT TRANSLOCASE TRANSMEMBRANE TRANSLOCATION PREPROTEIN SECDF SECD) protein domain (PD794746) which is seen in Q79VF7_CORGL.","","No significant hits to the PDB database (E-value < E-10).","Residues 41 to 69 (E_value = 0.0078) place ANA_0856 in the Sec_GG family which is described as SecD/SecF GG Motif.Residues 113 to 307 (E_value = 8.6e-74) place ANA_0856 in the SecD_SecF family which is described as Protein export membrane protein.","","membrane protein secF","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0857","925775","923622","2154","5.31","-17.17","75535","ATGGTCGCGCCCGCCACGCATCCCAACCCCATACTCACCTCAATCTTCGAGCCGTGCGCTCGAGCACACTCCACCCCAGGAAGGGACCACGTGTCCAGTAAGCAGCGAAAGCGCCCAGGGCGCCGCCTCCTGATGTTCGTCCTCGTCCTCGTCATCGGTTTCGGTGCGCTCGTGGCGGGAAGTATGAGGCATAAGGCCTCGCTCACCCCCGGTCTCGCCCTCGATCTGGAGGGCGGCACCCAGCTCATTTTGACGCCCACCACCTCTGATGGCTCGGCGATCAGTGATAACGACGTCGAGCAGGCCATCGAGGTGATCCGTCAGCGCGTGGATGCCTCCGGTGTCTCCGAGGCGCAGATCTCTCGCCAGGGCGGTCAGAACATCGTGGTCTCGCTGCCCGGCAAGCCCAGCCAGGCCACCCTGGAGCTGGTACGTACCTCGGCCGTCATGTACTTCCGCCCGGTCCTGCGCGTTCTTCCGGGCAGCGCCCAGCAGGCCGCTAAGAACATCGCCAGCCAGAACCCCTCCGGCGCGGTGACCCCGGCGCCGACGGTTCAGCCCAGCCCGAGCGCCGGTAGCGAGGCGACTCAGCCCGCAGAGGACTCGGAGGGCGCTGAGGAGGGCACAGGCGAGGGTGAGCAGCCGGCCGCGACCCCGGCTCCCACCGCGCAGCCCACGGCTCAGCCGACGGCGCAGCCCAGGACTCCCGAGGAGATTGCCAAGCAGCTGGCGGACGTCAACCAGGACGGCGTCATCTCCTCCGACCCGCTCCCCGCGCAGGACAAGACGAACTCATCGGACTCCTGGATCACCGAGAAGCTCCTCTACGACGGCTACATGACCGACTGCTCCGACCCGAAGAACCTCACGGGGCAGACGCAGGACCCCAAGGTCGCCGTCATCTCCTGCTCCAAGGAGGCCGGCTCCCACAGCCACGGCGCCTACATCCTCGGCCCTGCCGAGATCACCGGGACCGAGCTCAAGAGCGCCAACTCGGGTCTGGAAACCGACTCCCGGGGGCAGGCCACCCACCAGTGGGTCGTCTCGCTGGCCTTCAACGGTGACGGCACCAAGAAGTTCGCCGAGCTGTCCAAGCGGCTGCTGGCCTACCGCGACCAGGCGAGCGCCGCCGGCGCGCAGGGAGCTCAGAACCCGCAGGCCCAGAGCAGTGGGGACAAGGCCCAGTTCGCCATCGTCCTGGACGGCCTGACCATCATGGCCTCCGGCTTCAACGAGACCGTCCACTCACCGATCACCGACGGTCGGGTCCAGATCACCGGCGGCTTCACCCAGAACCAGGCCAACACGCTGGCCAACCAGCTCTCCTTCGGCTCGCTGCCGCTGAGCTTCACGGTGCAGTCCGAGCAGCAGATCTCAGCCACCTTGGGAACCGAGCAGCTGCGCAATGGCCTGATCGCCGGGCTCATCGGCTTCGCCCTCATCATCCTCTACCTGGCCTGGCAGTACCGCGGCCTGGCGGTGGTGGCCGTGGCCTCCCTGGTGGTGGCAGCAGCCGGCACCTACCTGGTCATCGCGGCCCTGAGCGCGACCATGGGCTACCGCCTGTCCCTGGCGGGGGTCGCCGGACTCATCATCTCCATCGGCATCACGGTCGACTCCTTCATCATCTACTTCGAGCGCGTCCGTGACGAGGTGCGCCAGGGACGGACTCTGAGGACCGCGATCGACGAGGGATGGAAGCACGCCAGGCGCACGATCCTCGTTTCCGACGCCGTCAACCTCGTGGCCGCGATTGTCCTGTACTTCCTGGCTGTCGGCGGGGTCCAGGGATTCGCCTTCACCCTGGGGGTGACCACGTGCGTGGACCTGGCCATCATCATCCTGTTCACCCACCCGTTGATGGAGTGGATCGTCCGATTCCGTTTCTTCGGTGAGGGGCACCGCCTTTCCGGTCTTGACCCCGAGCACCTCGGGGCGACGTCCACGACCTACGGCAAGGGACGCGAAGCGGTCGCCGATCGCGTTGCCGGGTCTCTGGCGCGCCGCAAGGCCGAGGCCCGTAGGAACGCCGAGAGCCCGGAGGACGCAGCTGAAGAGTCCGACGGCGAGGCCGTCGATGATGAGGATGAGCAGCAGGAGGGCGACGCGGTCGATGTCGCGGCCGACAAGGGAAAGGACGGTGAGACGAAGTGA","MVAPATHPNPILTSIFEPCARAHSTPGRDHVSSKQRKRPGRRLLMFVLVLVIGFGALVAGSMRHKASLTPGLALDLEGGTQLILTPTTSDGSAISDNDVEQAIEVIRQRVDASGVSEAQISRQGGQNIVVSLPGKPSQATLELVRTSAVMYFRPVLRVLPGSAQQAAKNIASQNPSGAVTPAPTVQPSPSAGSEATQPAEDSEGAEEGTGEGEQPAATPAPTAQPTAQPTAQPRTPEEIAKQLADVNQDGVISSDPLPAQDKTNSSDSWITEKLLYDGYMTDCSDPKNLTGQTQDPKVAVISCSKEAGSHSHGAYILGPAEITGTELKSANSGLETDSRGQATHQWVVSLAFNGDGTKKFAELSKRLLAYRDQASAAGAQGAQNPQAQSSGDKAQFAIVLDGLTIMASGFNETVHSPITDGRVQITGGFTQNQANTLANQLSFGSLPLSFTVQSEQQISATLGTEQLRNGLIAGLIGFALIILYLAWQYRGLAVVAVASLVVAAAGTYLVIAALSATMGYRLSLAGVAGLIISIGITVDSFIIYFERVRDEVRQGRTLRTAIDEGWKHARRTILVSDAVNLVAAIVLYFLAVGGVQGFAFTLGVTTCVDLAIIILFTHPLMEWIVRFRFFGEGHRLSGLDPEHLGATSTTYGKGREAVADRVAGSLARRKAEARRNAESPEDAAEESDGEAVDDEDEQQEGDAVDVAADKGKDGETK$","Protein-export membrane protein secD","Membrane, Cytoplasm","Protein-export membrane protein secD","protein-export membrane protein SecD","protein-export membrane protein SecD","","Bieker K.L., Phillips G.J., Silhavy T.J. The sec and prl genes of Escherichia coli. J. Bioenerg. Biomembr. 1990. 22(3):291-310. PMID: 2202721Driessen A.J. SecB, a molecular chaperone with two faces. Trends Microbiol. 2001. 9(5):193-196. PMID: 11336818Muller J.P. Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. FEMS Microbiol. Lett. 1999. 176(1):219-227. PMID: 10418149Breyton C., Haase W., Rapoport T.A., Kuhlbrandt W., Collinson I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 2002. 418(6898):662-665. PMID: 12167867Bolhuis A., Broekhuizen C.P., Sorokin A., Van roosmalen M.L., Venema G., Bron S., Quax W.J., van Dijl J.M. SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. J. Biol. Chem. 1998. 273(33):21217-21224. PMID: 9694879","","","

InterPro
IPR003335
Family

SecD/SecF/SecDF export membrane protein
PF02355	$\"[436-627]T$	SecD_SecF
TIGR00916	$\"[392-612]T$	2A0604s01: protein-export membrane protein,

InterPro
IPR005791
Family

SecD export membrane protein
TIGR01129	$\"[72-621]T$	secD: protein-export membrane protein SecD

noIPR
unintegrated

unintegrated
tmhmm	$\"[43-61]?$ $\"[467-487]?$ $\"[492-512]?$ $\"[522-544]?$ $\"[573-591]?$ $\"[597-617]?$	transmembrane_regions

","BeTs to 19 clades of COG0342COG name: Preprotein translocase subunit SecDFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0342 is -om-k--qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 72-138 are 83% similar to a (MEMBRANE PROTEIN-EXPORT SECD SUBUNIT TRANSLOCASE PREPROTEIN TRANSMEMBRANE TRANSLOCATION SECDF PROTEIN) protein domain (PD005230) which is seen in Q6AFB2_BBBBB.Residues 317-458 are 58% similar to a (MEMBRANE PROTEIN-EXPORT SECD SUBUNIT TRANSLOCASE TRANSMEMBRANE PREPROTEIN TRANSLOCATION SECDF PROTEIN) protein domain (PD122026) which is seen in Q6AFB2_BBBBB.Residues 458-629 are similar to a (EFFLUX FAMILY RESISTANCE TRANSPORTER TRANSMEMBRANE MULTIDRUG ACRB/ACRD/ACRF RND SYSTEM CATION) protein domain (PD001797) which is seen in SECD_STRCO.Residues 539-573 are 85% similar to a (MEMBRANE PROTEIN-EXPORT SECD SUBUNIT TRANSLOCASE TRANSMEMBRANE TRANSLOCATION SECDF PREPROTEIN PROTEIN) protein domain (PDA126P9) which is seen in Q6A8K5_PROAC.Residues 579-621 are 86% similar to a (SECD MEMBRANE PROTEIN-EXPORT TRANSLOCASE SUBUNIT PREPROTEIN TRANSMEMBRANE TRANSLOCATION) protein domain (PD685519) which is seen in Q83NH9_TROW8.","","No significant hits to the PDB database (E-value < E-10).","Residues 436 to 627 (E_value = 2.1e-06) place ANA_0857 in the SecD_SecF family which is described as Protein export membrane protein.","","membrane protein secD","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0859","926252","925893","360","4.44","-10.04","13338","ATGTCGTCGTATTTCATCTGGATCATGTTCATCGGGATGCTCCTGATGATGTGGTTCGTCAGTCGCAGGCAGCGCGCGATGCAGGAGGAGCAGAAGCGCCGTACCGAGAAGGGTCTGGTGCCCGGCAACTGGGTTCGTACCATCGGAGGCTTCTACGGCACGGTCGTCGAGGTCGACGGTGACGTGGTCACCCTGGCCACACCGCTGGGAGACGAGACTCTGTGGAGCAAGCGGGCGATCGCTGCCATCGAGGAGCCGCCCTTCGGCTCCGCCTCCGTCGACGAGGAGTCCGGCTCCGACGTCGAGCAGTCCGAGGACGGCCGCGAGTCCGAGCAGGACTCCGCCGAGCCGCAGTCGTGA","MSSYFIWIMFIGMLLMMWFVSRRQRAMQEEQKRRTEKGLVPGNWVRTIGGFYGTVVEVDGDVVTLATPLGDETLWSKRAIAAIEEPPFGSASVDEESGSDVEQSEDGRESEQDSAEPQS$","Preprotein translocase subunit YajC","Membrane, Cytoplasm, Extracellular","putative secreted protein","hypothetical protein predicted by Glimmer/Critica","preprotein translocase, YajC subunit","","","","","

InterPro
IPR003849
Family

YajC
PD374630	$\"[5-84]T$	Q8EPQ9_OCEIH_Q8EPQ9;
PF02699	$\"[2-84]T$	YajC
TIGR00739	$\"[2-85]T$	yajC: preprotein translocase, YajC subunit

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[4-22]?$	transmembrane_regions

","BeTs to 4 clades of COG1862COG name: Preprotein translocase subunit YajCFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1862 is -------qv-rlb-efghsnujxit-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 84 (E_value = 4.7e-09) place ANA_0859 in the YajC family which is described as Preprotein translocase subunit.","","secreted protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0860","927468","926428","1041","5.29","-9.57","36526","GTGGCTGAGCCCGATGAGCTCGATGGGCAGCGCCTGGTCGGTGGTGGTGCCGACGCCACCGAGCGCGCCGCCGAGGCGGCTCTACGGCCCAAGCGCCTGGAGGACTTCACCGGGCAGGAGGTGGTGCGAGGCCAGCTCTCGGTGGTGCTGCGCTCGGCCCTGGCCCGTGGAGTGACGGCTGATCACGTACTGCTCTCTGGGCCGCCCGGGCTGGGCAAGACCACCCTGGCCATGATCATCGCCGCCGAGGTGGACGGCTCCTTGCGCCTGACCTCGGGGCCGGCCATCCAGCACGCCGGAGACCTCGCGGCCATCCTGTCCTCCCTGGAGGAGGGGGACGTGCTGTTCATCGATGAGATCCACCGCCTGGCACGCACCGCCGAGGAGATGCTCTACCTGGCGATGGAGGACTTCCGCGTCGACATCGTCGTGGGAAAGGGACCCGGCGCCACCTCCATCCCCCTGTCCCTGCCTCCCTTCACCGTCGTCGGAGCCACCACGAGGGCGGGGCTGCTGCCCGCGCCGCTGCGGGACCGCTTCGGCTTCACCGGGCACCTCGACTACTACGGGCCGAGCGAGCTCACCCGGATCCTCACGCGCAGCGCAGGGCTGCTGGGGGTGAGCCTGGAGGCGGACGCCGCCAAGGAGCTGGCCTCACGCTCGCGCGGCACACCCCGTATCGCCAACCGGTTGCTGCGCCGCGTCCAGGACTGGGCGGAGGTGCACGGGCGGCCCGGACGACTGGACCTGACGGCGGCGCGCGGCGCCCTCGATGTCTTCGAGGTCGACGCCCTCGGGCTGGATCGTCTGGACCGCCAGGTGCTCGAGGCCCTGTGCACCCGGTTCGGTGGCGGCCCGGTGGGACTGACGACGCTGGCGGTCAGCGTGGGGGAGGAGCCCGAGACGGTGGAGACCGTGGCTGAGCCCTACCTGGTGCGCGAAGGGCTCGTGGTGCGCACCCCGCGGGGGCGGGCCGCCACGCCGGCTGCCTACAGCCACCTGGGACTCGAGCCCCCTGCCGACGGATCATTGTTCTCCTGA","VAEPDELDGQRLVGGGADATERAAEAALRPKRLEDFTGQEVVRGQLSVVLRSALARGVTADHVLLSGPPGLGKTTLAMIIAAEVDGSLRLTSGPAIQHAGDLAAILSSLEEGDVLFIDEIHRLARTAEEMLYLAMEDFRVDIVVGKGPGATSIPLSLPPFTVVGATTRAGLLPAPLRDRFGFTGHLDYYGPSELTRILTRSAGLLGVSLEADAAKELASRSRGTPRIANRLLRRVQDWAEVHGRPGRLDLTAARGALDVFEVDALGLDRLDRQVLEALCTRFGGGPVGLTTLAVSVGEEPETVETVAEPYLVREGLVVRTPRGRAATPAAYSHLGLEPPADGSLFS$","Holliday junction DNA helicase RuvB","Cytoplasm","Holliday junction DNA helicase RuvB","Holliday junction DNA helicase RuvB","Holliday junction DNA helicase RuvB","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[59-192]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[62-241]T$	AAA

InterPro
IPR004605
Family

Holliday junction DNA helicase RuvB
TIGR00635	$\"[31-336]T$	ruvB: Holliday junction DNA helicase RuvB

InterPro
IPR008823
Domain

Holliday junction DNA helicase RuvB, C-terminal
PF05491	$\"[259-337]T$	RuvB_C

InterPro
IPR008824
Domain

Holliday junction DNA helicase RuvB, N-terminal
PF05496	$\"[10-61]T$	RuvB_N

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[266-344]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.60	$\"[189-265]T$	no description
G3DSA:3.40.50.300	$\"[26-189]T$	no description
PTHR13779	$\"[32-343]T$	HOLLIDAY JUNCTION DNA HELICASE RUVB-RELATED
PTHR13779:SF2	$\"[32-343]T$	HOLLIDAY JUNCTION DNA HELICASE RUVB

","BeTs to 17 clades of COG2255COG name: Holliday junction resolvasome helicase subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2255 is --------vdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB008824 (Holliday junction DNA helicase RuvB, N-terminal) with a combined E-value of 7.2e-151. IPB008824A 28-80 IPB008824B 109-161 IPB008824C 162-194 IPB008824D 216-241 IPB008824E 282-334***** IPB000641 (CbxX/CfqX superfamily signature) with a combined E-value of 3.2e-10. IPB000641B 62-77 IPB000641D 102-121 IPB000641G 175-194***** IPB000642 (Peptidase M41) with a combined E-value of 1.5e-06. IPB000642A 43-92","Residues 36-102 are 79% similar to a (ATP-BINDING PROTEASE CELL DIVISION DNA SUBUNIT HELICASE PROTEASOME HYDROLASE ATPASE) protein domain (PD337570) which is seen in RUVB_CORGL.Residues 108-216 are similar to a (DNA HELICASE HOLLIDAY JUNCTION ATP-BINDING RUVB SOS REPAIR RECOMBINATION RESPONSE) protein domain (PD236006) which is seen in RUVB_STRCO.Residues 217-318 are 82% similar to a (DNA HELICASE HOLLIDAY JUNCTION RUVB ATP-BINDING SOS REPAIR RECOMBINATION RESPONSE) protein domain (PD005323) which is seen in Q6A8K7_PROAC.","","-67% similar to PDB:1HQC STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8 (E_value = 6.7E_82);-67% similar to PDB:1IXS Structure of RuvB complexed with RuvA domain III (E_value = 6.7E_82);-70% similar to PDB:1IXR RuvA-RuvB complex (E_value = 2.4E_79);-65% similar to PDB:1IN4 THERMOTOGA MARITIMA RUVB HOLLIDAY JUNCTION BRANCH MIGRATION MOTOR (E_value = 1.3E_77);-65% similar to PDB:1IN5 THERMOGOTA MARITIMA RUVB A156S MUTANT (E_value = 2.9E_77);","Residues 10 to 61 (E_value = 3.2e-13) place ANA_0860 in the RuvB_N family which is described as Holliday junction DNA helicase ruvB N-terminus.Residues 62 to 241 (E_value = 8.8e-29) place ANA_0860 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).Residues 62 to 188 (E_value = 5.9e-05) place ANA_0860 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).Residues 62 to 89 (E_value = 3.4e-06) place ANA_0860 in the AAA_3 family which is described as ATPase family associated with various cellular activities (AAA).Residues 259 to 337 (E_value = 2e-44) place ANA_0860 in the RuvB_C family which is described as Holliday junction DNA helicase ruvB C-terminus.","","junction DNA helicase RuvB (ruvB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0861","928114","927461","654","5.22","-5.31","22188","ATGATCGCCTCACTGCGCGGCACTGTCCTCAGTGTCAGCCTCACCAGTGCCGTCATCGAGACGGGCGGCGTCGGCATGAGTATCCAGGCCACGCCCACCACGCTGTCCGGCCTCAGGGCCGGTGAGGAGGTCCTTGTCCACACCGAGATGGTGGTCCGTGAGGACTCGCTGACGCTGTTCGGCTTCGCCGACACCGATGAGAGGGACAGCTTCCGCACCCTGATGAGCGCCAAGGGGGTCGGAGCCAAGCTGGCGCTGGCGATGCTGGCCGTCCACACGCCCAACGCGCTCAGGCGGGCCATCGCCTCCCAGGACGTGGCGGCCCTCACGCGGGTGCCTGGCCTCGGGCCCAAAGGTGCTCAGCGTGTCATCCTGGACGTGGCCGACAAGCTGGGCCCTGTCACCGGGGACGATCTGGGGGCCGCGCGGACAGCTGCTCAGACAGCGCCGGGGATGGAAGTGGTGCCCGCCGGCGGTCCCGAGCCGCACGCCGACGTCGTTGCCGCTCTAGTGCAGCTCGGCTGGAACGAGGCCAGTGCGCGCCAGGCAGTCACCTCCGTGACGGCCGATGCCGCAGAGGCCGAGCAGGAGCTGGACATGGCGGCCGTGCTGCGGGCCTCCTTGAGGTGGTTGGGGGGCGGGCAGCGTGGCTGA","MIASLRGTVLSVSLTSAVIETGGVGMSIQATPTTLSGLRAGEEVLVHTEMVVREDSLTLFGFADTDERDSFRTLMSAKGVGAKLALAMLAVHTPNALRRAIASQDVAALTRVPGLGPKGAQRVILDVADKLGPVTGDDLGAARTAAQTAPGMEVVPAGGPEPHADVVAALVQLGWNEASARQAVTSVTADAAEAEQELDMAAVLRASLRWLGGGQRG$","Holliday junction DNA helicase RuvA","Cytoplasm","Holliday junction DNA helicase RuvA","Holliday junction DNA helicase RuvA","Holliday junction DNA helicase RuvA","","Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Rafferty J.B., Sedelnikova S.E., Hargreaves D., Artymiuk P.J., Baker P.J., Sharples G.J., Mahdi A.A., Lloyd R.G., Rice D.W. Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Science 1996. 274(5286):415-421. PMID: 8832889","","","

InterPro
IPR000085
Family

Bacterial DNA recombination protein RuvA
TIGR00084	$\"[1-209]T$	ruvA: Holliday junction DNA helicase RuvA

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[72-91]T$ $\"[107-126]T$	HhH1

InterPro
IPR011114
Domain

RuvA, domain III
PF07499	$\"[161-212]T$	RuvA_C

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[1-63]T$	no description

InterPro
IPR013849
Domain

Bacterial DNA recombination protein RuvA, domain I
PF01330	$\"[1-61]T$	RuvA_N

InterPro
IPR013850
Domain

Bacterial DNA recombination protein, RuvA, central
PD006268	$\"[71-139]T$	RUVA_MYCLE_P40832;

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.20	$\"[66-157]T$	no description
signalp	$\"[1-25]?$	signal-peptide

","BeTs to 17 clades of COG0632COG name: Holliday junction resolvasome DNA-binding subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0632 is --------vdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB011132 (RuvA-like, C-terminal) with a combined E-value of 2.2e-43. IPB011132A 1-28 IPB011132B 46-90 IPB011132C 113-130 IPB011132D 169-185***** IPB000085 (Bacterial DNA recombination protein, RuvA) with a combined E-value of 6.2e-40. IPB000085A 1-22 IPB000085B 46-87 IPB000085C 113-130 IPB000085D 165-175","Residues 1-68 are similar to a (DNA HELICASE HOLLIDAY JUNCTION RUVA SOS REPAIR DNA-BINDING RECOMBINATION RESPONSE) protein domain (PD596344) which is seen in RUVA_STRAW.Residues 9-62 are 72% similar to a (DNA HELICASE HOLLIDAY JUNCTION RUVA SOS REPAIR DNA-BINDING RECOMBINATION RESPONSE) protein domain (PD704549) which is seen in Q741Q1_MYCPA.Residues 71-139 are similar to a (DNA HELICASE HOLLIDAY JUNCTION RUVA SOS REPAIR DNA-BINDING RECOMBINATION RESPONSE) protein domain (PD006268) which is seen in RUVA_MYCLE.Residues 71-212 are 50% similar to a (HELICASE HOLLIDAY DNA JUNCTION) protein domain (PDA0U895) which is seen in Q6AFB5_BBBBB.","","-61% similar to PDB:1BVS RUVA COMPLEXED TO A HOLLIDAY JUNCTION. (E_value = 2.3E_41);-61% similar to PDB:2H5X RuvA from Mycobacterium tuberculosis (E_value = 8.0E_39);-52% similar to PDB:1BDX E. COLI DNA HELICASE RUVA WITH BOUND DNA HOLLIDAY JUNCTION, ALPHA CARBONS AND PHOSPHATE ATOMS ONLY (E_value = 2.3E_25);-52% similar to PDB:1C7Y E.COLI RUVA-HOLLIDAY JUNCTION COMPLEX (E_value = 2.3E_25);-52% similar to PDB:1HJP HOLLIDAY JUNCTION BINDING PROTEIN RUVA FROM E. COLI (E_value = 2.3E_25);","Residues 1 to 61 (E_value = 1.6e-25) place ANA_0861 in the RuvA_N family which is described as RuvA N terminal domain.Residues 161 to 212 (E_value = 1.8e-10) place ANA_0861 in the RuvA_C family which is described as RuvA, C-terminal domain.","","junction DNA helicase RuvA (ruvA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0862","928798","928229","570","10.43","4.64","19751","GTGGACGTCGACCCTCGCCGTCAGGTCCGTCTGGTGGAGGTCGGCGTGGTTCGCACGCCGCCTTCCCAGAGCCCCGAGCTGAGACTGCTGACCATCACGGAGGCCATTGAGGACTGGATCGCCCGCCTGGGCCCGTCGGTGGTGTCCATCGAGCGGGTCTTCGCGCAGGACAACCTGCGCTCCGTCATCGGGGTCGCCCAGGTCATGGGTACCGCCATGGCCACGGCGGCGCGCGCGGGCCTGGAGGTCGCTCAGCACACGCCCAGTGAGGCCAAGGCGGCCGTGACCGGCTCGGGCACGGCTGACAAGGCTCAGGTCCAGGCCATGGTCACCCGCATCCTCGGCCTCGACGCCCCGCCCCGGCCGGCCGACGCCGCCGACGCTCTGGCCCAGGCGATCTGCCACGGCTGGCGCGGGGGAGGAACGGGGACGGACGACGCCACCGAGATGGTCTCCGCCGGGGGAGCGGTGCGTGTCTCGGCCCGCACACCTGCACAGCGCCATTGGGCTGCCGCCCAGGCCGCAGCCCGGCGCACCGGTGCCGTCGACCCGCGCCGGGTGCGGCGCTGA","VDVDPRRQVRLVEVGVVRTPPSQSPELRLLTITEAIEDWIARLGPSVVSIERVFAQDNLRSVIGVAQVMGTAMATAARAGLEVAQHTPSEAKAAVTGSGTADKAQVQAMVTRILGLDAPPRPADAADALAQAICHGWRGGGTGTDDATEMVSAGGAVRVSARTPAQRHWAAAQAAARRTGAVDPRRVRR$","Crossover junction endodeoxyribonuclease","Cytoplasm, Extracellular","Crossover junction endodeoxyribonuclease ruvC(Hollidayjunction nuclease ruvC) (Holliday juction","crossover junction endodeoxyribonuclease ","Crossover junction endodeoxyribonuclease","","Iwasaki H., Takahagi M., Shiba T., Nakata A., Shinagawa H. Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure. EMBO J. 1991. 10(13):4381-4389. PMID: 1661673Ariyoshi M., Vassylyev D.G., Iwasaki H., Fujishima A., Shinagawa H., Morikawa K. Preliminary crystallographic study of Escherichia coli RuvC protein. An endonuclease specific for Holliday junctions. J. Mol. Biol. 1994. 241(2):281-282. PMID: 8057369","","","

InterPro
IPR002176
Family

Crossover junction endodeoxyribonuclease RuvC
PD008333	$\"[7-135]T$	RUVC_STRAW_Q820F5;
PR00696	$\"[45-61]T$ $\"[67-83]T$ $\"[91-110]T$ $\"[123-135]T$	RSOLVASERUVC
PF02075	$\"[1-135]T$	RuvC

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[6-144]T$	no description

","BeTs to 14 clades of COG0817COG name: Holliday junction resolvasome endonuclease subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0817 is --------vdr--cefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB002176 (Crossover junction endodeoxyribonuclease RuvC) with a combined E-value of 9.7e-42. IPB002176B 28-75 IPB002176C 81-122 IPB002176D 124-135","Residues 7-135 are similar to a (RUVC JUNCTION HOLLIDAY NUCLEASE DNA ENDODEOXYRIBONUCLEASE CROSSOVER HYDROLASE JUCTION RESOLVASE) protein domain (PD008333) which is seen in RUVC_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 135 (E_value = 2.6e-43) place ANA_0862 in the RuvC family which is described as Crossover junction endodeoxyribonuclease RuvC.","","junction endodeoxyribonuclease ruvC (Hollidayjunction nuclease ruvC) (Holliday juction resolvase ruvC) (ruvC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0863","929669","928905","765","4.67","-17.55","27046","ATGTCGGGTCACTCCAAGTGGGCCACCACCAAGCACAAGAAGGCCGCCATCGACGCCAAGCGCGGCAAGCTCTTCGCACGTCTCATTAAGAACATCGAGGTTGCTGCCCGCACCGGCGGTGGTGACCCCACCGGTAACCCCACTTTGTTCGACGCCATCCAGAAGGCCAAGAAGAACTCGGTGCCGGCGGACAACATCACCCGCGCCGTCAAGCGCGGCAGCGGCGAGGAGGCCGGTGGCGCCGACTGGCAGACCATCATGTACGAGGGCTACGGCCCCGGCGGGGTCGCTTTCCTCGTCGAGTGCCTCACCGACAACCGCAACCGGGCCGCCTCCGACGTGCGCGTGGCCTTCTCCCGCAACGGCGGAAACCTGGCCGACCCCGGTTCGGTGGCCTACAACTTCACCCGCAAGGGCGTCGTCGAGGTCGCCAAGGCCGACGGCGTGGACGAGGACTCCATCCTCATGGCCGTCCTGGAGGCCGGCGCCGAGGAGGTCGAGGACATGGGCGAGTCCTTCGAGATCTACTCCGAGCCCGGTGACATCGTCGCCGTGCGTACCGCCCTGACGGAGGCGGGGATGGACTATGACTCCGCCGAGGTCCAGTTCGTCGCCGGCACCAAGGTGGAGGTCGACGTCGAAGGAGCCCGCAAGGTCTTCCGCCTCATCGACGCCCTGGAGGACTCCGACGACGTCCAGAACGTCTACACCTCGGTGGACCTCAGCCCAGAGGTGGCCGCCGAGTTCGCCGACGACGAGGACTGA","MSGHSKWATTKHKKAAIDAKRGKLFARLIKNIEVAARTGGGDPTGNPTLFDAIQKAKKNSVPADNITRAVKRGSGEEAGGADWQTIMYEGYGPGGVAFLVECLTDNRNRAASDVRVAFSRNGGNLADPGSVAYNFTRKGVVEVAKADGVDEDSILMAVLEAGAEEVEDMGESFEIYSEPGDIVAVRTALTEAGMDYDSAEVQFVAGTKVEVDVEGARKVFRLIDALEDSDDVQNVYTSVDLSPEVAAEFADDED$","Uncharacterized conserved protein","Cytoplasm","conserved hypothetical protein TIGR01033","hypothetical protein","protein of unknown function DUF28","","","","","

InterPro
IPR002876
Family

Protein of unknown function DUF28
PD004323	$\"[11-245]T$	YQ03_MYCTU_O33214;
PTHR12532	$\"[1-250]T$	UNCHARACTERIZED
PF01709	$\"[5-240]T$	DUF28
TIGR01033	$\"[1-240]T$	TIGR01033: conserved hypothetical protein T

InterPro
IPR003308
Domain

Integrase, N-terminal zinc-binding
G3DSA:1.10.10.200	$\"[1-81]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.1270.10	$\"[83-250]T$	no description

","BeTs to 19 clades of COG0217COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0217 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002876 (Protein of unknown function DUF28) with a combined E-value of 5.8e-74. IPB002876A 31-75 IPB002876B 88-133 IPB002876C 212-238","Residues 11-245 are 86% similar to a (UPF0082 YEEN YGR021W CEREVISIAE YEBC 3D-STRUCTURE P53212 SACCHAROMYCES SO3401 MG332) protein domain (PD004323) which is seen in YQ03_MYCTU.","","-69% similar to PDB:1KON CRYSTAL STRUCTURE OF E.COLI YEBC (E_value = 1.7E_65);-67% similar to PDB:1LFP Crystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex Aeolicus (E_value = 1.3E_54);-53% similar to PDB:1MW7 X-RAY STRUCTURE OF Y162_HELPY NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET PR6 (E_value = 3.4E_26);","Residues 5 to 240 (E_value = 2.3e-136) place ANA_0863 in the DUF28 family which is described as Domain of unknown function DUF28.","","hypothetical protein TIGR01033","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0864","930412","929714","699","5.82","-4.61","24267","ATGGACGCCCGCCACCCCCGGGCGCTCTTCCCCGCGCTCGCAGCGCCCGACTCCCGCCCCACAATCGGGGTCCTGGCCCTTCAGGGTGACGTGCGCGAGCACTCCTTGGCCCTCGAGGCGGCCGGAGCGCGACCCGTCGTCGTGCGCCGCGCCGCCGATCTGGGCGAGGCTCCCGGCCACCGGCTCGACGGCCTGGTGATCCCCGGAGGGGAGTCGACCACCATGAGCACGCTGCTGGCCGCCTTCGACATGCTCGCGCCCCTGCGTGAGCTCATCGGCGCGGGCCTGCCCGCCTACGGGTCCTGCGCCGGGATGATTATGCTGGCCGATCGCGTCGAGGGGGCTCAGGAGGGCCAGGCCTTCCTGGGTGGCATCGACATGACCGTGCGCCGCAATGCCTTCGGCCGACAGGTGGACTCCTACGAGGAGGATCTCCTCGCCCCGGAGCTCGGCGCGGGGCCGGACCGACCGCTGCGCGCCGTCTTCATCCGGGCTCCCTGGGTGGAGGAAGTAGGCCCGGACGTCGAGATCCTCGCCACGACCCGCGCCGGACGCGCGGCTGGGGTCGGTGGGGCCGACGGCGGTAGGATCGTCGCGGTTCGTCAAGGATCCCTGCTCGCCACGTCCTTCCACCCGGAGGTCGGAGGCGACCACCGGGTCCACGACGTCTTCGTCTCCATGGTGACGCGCCGGGCCTGA","MDARHPRALFPALAAPDSRPTIGVLALQGDVREHSLALEAAGARPVVVRRAADLGEAPGHRLDGLVIPGGESTTMSTLLAAFDMLAPLRELIGAGLPAYGSCAGMIMLADRVEGAQEGQAFLGGIDMTVRRNAFGRQVDSYEEDLLAPELGAGPDRPLRAVFIRAPWVEEVGPDVEILATTRAGRAAGVGGADGGRIVAVRQGSLLATSFHPEVGGDHRVHDVFVSMVTRRA$","Glutamine amidotransferase","Cytoplasm","amidotransferase hisH homolog","putative glutamine amidotransferase ","SNO glutamine amidotransferase","","Braun E.L., Fuge E.K., Padilla P.A., Werner-Washburne M. A stationary-phase gene in Saccharomyces cerevisiae is a member of a novel, highly conserved gene family. J. Bacteriol. 1996. 178(23):6865-6872. PMID: 8955308Padilla P.A., Fuge E.K., Crawford M.E., Errett A., Werner-Washburne M. The highly conserved, coregulated SNO and SNZ gene families in Saccharomyces cerevisiae respond to nutrient limitation. J. Bacteriol. 1998. 180(21):5718-5726. PMID: 9791124","","","

InterPro
IPR002161
Family

SNO glutamine amidotransferase
PF01174	$\"[24-230]T$	SNO
PS51130	$\"[21-229]T$	PDXT_SNO_2
PS01236	$\"[64-74]T$	PDXT_SNO_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[14-228]T$	no description
signalp	$\"[1-3]?$	signal-peptide

","BeTs to 14 clades of COG0311COG name: Predicted glutamine amidotransferase involved in pyridoxine biosynthesisFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0311 is aompkzy-vdr-b----h--------Number of proteins in this genome belonging to this COG is 1","***** IPB002161 (SNO glutamine amidotransferase) with a combined E-value of 2e-59. IPB002161A 59-75 IPB002161B 99-109 IPB002161C 122-141 IPB002161D 155-171 IPB002161E 197-230","Residues 62-103 are 80% similar to a (AMIDOTRANSFERASE TRANSFERASE GLUTAMINE PYRIDOXINE BIOSYNTHESIS SNO AMIDOTRANSFERASE UPF0030 2.4.2.- SYNTHASE) protein domain (PDA169K3) which is seen in Q73WF2_MYCPA.Residues 104-178 are 69% similar to a (AMIDOTRANSFERASE TRANSFERASE GLUTAMINE PYRIDOXINE BIOSYNTHESIS SNO AMIDOTRANSFERASE UPF0030 2.4.2.- SYNTHASE) protein domain (PD783256) which is seen in Q81ZV5_STRAW.","","-53% similar to PDB:1R9G Three-dimensional Structure of YaaE from Bacillus subtilis (E_value = 7.8E_35);-53% similar to PDB:2NV0 Structure of the glutaminase subunit Pdx2 (YaaE) of PLP synthase from Bacillus subtilis (E_value = 7.8E_35);-53% similar to PDB:2NV2 Structure of the PLP synthase complex Pdx1/2 (YaaD/E) from Bacillus subtilis (E_value = 5.0E_34);-54% similar to PDB:2ISS Structure of the PLP synthase Holoenzyme from Thermotoga maritima (E_value = 2.8E_32);-53% similar to PDB:1Q7R X-ray crystallographic analysis of a predicted amidotransferase from B. stearothermophilus at 1.9 A resolution (E_value = 8.0E_32);","Residues 24 to 230 (E_value = 3.7e-62) place ANA_0864 in the SNO family which is described as SNO glutamine amidotransferase family.Residues 54 to 219 (E_value = 2.2e-05) place ANA_0864 in the GATase_3 family which is described as CobB/CobQ-like glutamine amidotransferase domain.","","hisH homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0865","930982","930476","507","4.91","-11.64","18776","GTGACCCAGGACGGCGAGGTACTGCTGTTGGTGGGGCACGACGCCGCGGACCCGGATCACAACTGGGTCTTCACCCCGGGAGGAGGGCTGCGCAGCGGTGAGGACCCCCGTGCCGGCGCCGTGCGCGAGCTGGTTGAGGAGTCCGGGATCAAGGTCGCCCCGGAGGACCTGGAGGGGCCCATCGCCCACCGGGAGGCGATCTTCCGCTTCGCCTCGGTCACGTGCCGACAGGACGAGATCTTCTTCCTCCTGCACCTGCCGACCCGGCGCCCGATCAGGAAGGACGGATGGACGTGCCTGGAGCGCGACGTCGTCGACTCCATCTCGTGGTGGAGTGCCGAGCAGCTGCAGGCCGCCCACCAGCGGGGGCAGGAGATCTACCCGGTGCGCCTGCCTGAGATCGTGGAGGATCTCGCCTCGGGCTGGAACGGTCGGCGCCTCGACCTGACCGATCCGGTGGACCAGGAGGTCCTGGCCGAGCTCGCGAGCACCTCTCCCCGTCACTGA","VTQDGEVLLLVGHDAADPDHNWVFTPGGGLRSGEDPRAGAVRELVEESGIKVAPEDLEGPIAHREAIFRFASVTCRQDEIFFLLHLPTRRPIRKDGWTCLERDVVDSISWWSAEQLQAAHQRGQEIYPVRLPEIVEDLASGWNGRRLDLTDPVDQEVLAELASTSPRH$","NUDIX hydrolase","Cytoplasm","NUDIX domain, putative","hypothetical protein","NUDIX hydrolase","","Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 1992. 174(20):6321-6325. PMID: 1328155Koonin E.V. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 1993. 21(20):4847-4847. PMID: 8233837Mejean V., Salles C., Bullions L.C., Bessman M.J., Claverys J.P. Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydrolases. Mol. Microbiol. 1994. 11(2):323-330. PMID: 8170394Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 1993. 268(31):23524-23530. PMID: 8226881McLennan A.G. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int. J. Mol. Med. 1999. 4(1):79-89. PMID: 10373642Bessman M.J., Frick D.N., O. Handley S.F. The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes. J. Biol. Chem. 1996. 271(41):25059-25062. PMID: 8810257","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[23-37]T$ $\"[37-52]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[1-116]T$	no description
PF00293	$\"[1-133]T$	NUDIX
PS00893	$\"[28-49]T$	NUDIX

","BeTs to 20 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 1.9e-08. IPB000086 23-50","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 133 (E_value = 1.8e-05) place ANA_0865 in the NUDIX family which is described as NUDIX domain.","","domain, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0866","932013","931111","903","5.00","-12.59","31744","TTGAATACAGAGCAGACCACTCCCAGCACCGGCACCCTCACCGTTAAACGCGGCATGGCGGACATGCTCAAGGGCGGCGTCATCATGGACGTCGTCACGCCTGAGCAGGCCCGTATTGCCCAGGACGCAGGAGCCGTCGCCGTCATGGCGCTCGAGCGCGTCCCTGCCGACATCCGAGCCCAGGGCGGCGTTGCCCGCATGAGCGACCCCGACCTCATCACCGGTATCATCGAGGCGGTCTCCATCCCGGTCATGGCCAAGGCCCGTATCGGCCACTTCGTGGAGGCCCAGGTCCTCCAGAGCCTCGGCGTGGACTACATCGATGAGTCCGAGGTCCTCACCCCGGCCGACTACACCCACCACATCGACAAGCAGTCCTTCACCGTTCCTTTCGTGTGCGGGGCCACCAACCTCGGTGAGGCGCTGCGCCGCATCACCGAGGGTGCGGCCATGATCCGCTCCAAGGGAGAGGCCGGAACCGGGGACGTCTCCAACGCTGTGACCCACATGCGCACGATCCGCGACGAGATCCGTCGTCTGAGTTCGCTGCCCGAGGACGAGCTCTACCTGGCCGCCAAGGAGCTCGCCGCCCCCTACGAGCTCGTCGCCGAGGTCGCCCGCACCGGTCACCTGCCGGTCGTGCTGTTCACCGCCGGCGGCATCGCCACCCCGGCCGACGCCGCCATGATGATGCAGATGGGCGCCGAGGGCGTCTTCGTGGGCTCGGGCATCTTCAAGTCCGGTGAGCCCGCCAAGCGGGCCGCCGCCATCGTGCGCGCCACCGCGCAGTTCGACGACCCCGACGTCATCGCCGAGGTCTCGCGCGGACTGGGCGAGGCAATGGTGGGGATCAACGTCGACGAGATCCCCGAGCCCCACCGCCTGGCGGAACGCGGCTGGTGA","LNTEQTTPSTGTLTVKRGMADMLKGGVIMDVVTPEQARIAQDAGAVAVMALERVPADIRAQGGVARMSDPDLITGIIEAVSIPVMAKARIGHFVEAQVLQSLGVDYIDESEVLTPADYTHHIDKQSFTVPFVCGATNLGEALRRITEGAAMIRSKGEAGTGDVSNAVTHMRTIRDEIRRLSSLPEDELYLAAKELAAPYELVAEVARTGHLPVVLFTAGGIATPADAAMMMQMGAEGVFVGSGIFKSGEPAKRAAAIVRATAQFDDPDVIAEVSRGLGEAMVGINVDEIPEPHRLAERGW$","Pyridoxine biosynthesis protein","Cytoplasm","pyridoxine biosynthesis protein","pyridoxine biosynthesis protein","pyridoxine biosynthesis protein","","Braun E.L., Fuge E.K., Padilla P.A., Werner-Washburne M. A stationary-phase gene in Saccharomyces cerevisiae is a member of a novel, highly conserved gene family. J. Bacteriol. 1996. 178(23):6865-6872. PMID: 8955308Ehrenshaft M., Bilski P., Li M.Y., Chignell C.F., Daub M.E. A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):9374-9378. PMID: 10430950","","","

InterPro
IPR001852
Family

Vitamin B6 biosynthesis protein
PD004958	$\"[7-66]T$	Q6A948_PROAC_Q6A948;
PF01680	$\"[13-218]T$	SOR_SNZ
TIGR00343	$\"[15-300]T$	TIGR00343: pyridoxine biosynthesis protein
PS51129	$\"[15-300]T$	PDXS_SNZ_2
PS01235	$\"[211-229]T$	PDXS_SNZ_1

","BeTs to 14 clades of COG0214COG name: Pyridoxine biosynthesis enzymeFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0214 is aompkzy-vdr-b----h--------Number of proteins in this genome belonging to this COG is 1","***** IPB001852 (Vitamin B6 biosynthesis protein) with a combined E-value of 1.1e-189. IPB001852A 15-55 IPB001852B 69-121 IPB001852C 129-171 IPB001852D 209-243 IPB001852E 244-286***** IPB004136 (2-nitropropane dioxygenase, NPD) with a combined E-value of 3e-07. IPB004136D 214-244","Residues 7-66 are 93% similar to a (BIOSYNTHESIS PYRIDOXINE PDX1 PYRIDOXIN PROBABLE HOMOLOG PDX1-LIKE ETHYLENE-INDUCIBLE SNZ1 SACCHAROMYCES) protein domain (PD004958) which is seen in Q6A948_PROAC.Residues 67-189 are similar to a (BIOSYNTHESIS PYRIDOXINE PDX1 PYRIDOXIN PROBABLE HOMOLOG PDX1-LIKE SNZ1 CEREVISIAE ETHYLENE-INDUCIBLE) protein domain (PD581874) which is seen in Q73WF0_MYCPA.Residues 192-240 are 73% similar to a (OSJNBA0071I20.8) protein domain (PDA0L063) which is seen in Q8LNL0_EEEEE.Residues 205-243 are 92% similar to a (BIOSYNTHESIS DIOXYGENASE DIHYDROOROTATE OXIDOREDUCTASE PYRIDOXINE DEHYDROGENASE 2-NITROPROPANE PDX1 OXIDASE IRON-SULFUR) protein domain (PD581000) which is seen in Q73WF0_MYCPA.Residues 211-250 are 97% similar to a (BIOSYNTHESIS PYRIDOXINE PDX1 PYRIDOXIN PROBABLE HOMOLOG ETHYLENE-INDUCIBLE PDX1-LIKE SNZ1 CEREVISIAE) protein domain (PD870570) which is seen in Q6AFB9_BBBBB.Residues 264-300 are 91% similar to a (BIOSYNTHESIS PYRIDOXINE PDX1 PYRIDOXIN PROBABLE HOMOLOG PDX1-LIKE SNZ1 CEREVISIAE ETHYLENE-INDUCIBLE) protein domain (PD692651) which is seen in PDX1_CORGL.","","-75% similar to PDB:1ZNN Structure of the synthase subunit of PLP synthase (E_value = 3.5E_100);-76% similar to PDB:2NV1 Structure of the synthase subunit Pdx1 (YaaD) of PLP synthase from Bacillus subtilis (E_value = 5.0E_99);-76% similar to PDB:2NV2 Structure of the PLP synthase complex Pdx1/2 (YaaD/E) from Bacillus subtilis (E_value = 5.0E_99);-76% similar to PDB:2ISS Structure of the PLP synthase Holoenzyme from Thermotoga maritima (E_value = 4.8E_94);","Residues 13 to 218 (E_value = 6e-127) place ANA_0866 in the SOR_SNZ family which is described as SOR/SNZ family.","","biosynthesis protein (SOI7)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0868","933477","932176","1302","9.55","9.31","46911","ATGAGCATGCCCCCCAGTCCCTGGGCCCCCCGCCCCGGATACCGGCGCTCCAGCGCCCTTCCGCAGACCCCAGCCGACTCCGGCCCCCTTCCCGCAGTCGGGCAGCGGTATCAGGTTCATCGTGACACTCAGGGCACGCCTCCCTCGCGGGCCACGGATCCTGAGGATGGCTGGCAGCAGCACGGGCAGGTGGCCTCCCTCATCCCACCTGGTATTCCGGCGAAGGTCGGGGCGATCGTCATGCCGACCGCGATCGTTGTCTTCTCCCTGTACACCCTGTTTTACTTCGCGGGCCTTCAGGACGACTTCGGGCCGGTCGTGCTTCCGTCATTTCTGCTGGCGCTCATCCCGCTAGGCGGGGTGCTGGTGGCCACGATGCTGCTCGCGGGAGTGTTCTGGTACGTCCGCTGGGAGCCCAGGCCTCCCGGTGTGTTCACGGTGGTCACGCTCCTGGTGGCATTCCTGTGGGGGACGAGCGTGTCCACCCTGTGCTCCTTGGTGGTCAATAACTGGGTGGCTCAGGTCATCACCGAGGCCATGGGGGATCTGGGCGCCGCCGCGGTGATTTCGGCACCTCTGGTGGAGGAGCTGACCAAGGGACTGGGCGTCCTGTTCGTCTTCCTCATCTGGCGCCGCACGATCAATGGCACGATCGATGGGGTCGTGTATGCGGCGTTCACCGCCTCAGGTTTCGCCTTCGTTGAGAACATTCTCTACTTCGTTCAGGGATGGGAGCACGTCGGGACCATTTTTGTTACACGAGGGGTCCTGTCCCCGTTCGCTCACCTGACCTTCACCGCCTGCACCGGGGTCGCCATTGGCTTCTCCTCCCGCCGGCGGTCTCAGTACGCCTGGGCGTGGATGGCGCCTGTGGGCCTGGTCGGCGCGATCGTGCTTCATGCGACCTGGAACGGGTTCATCGCCTCAAACCTCGGGGTGTATCTGCTGTTTCAGGTTCCGTTCTACGCTCTGTGCGCCGGGCTGGTCTCGTGGCTGCGTTGGAGTGAGCGCCGGTCGATGCGTCGCGGGCTGGAGGACTACGCCCGCGCCGGCTGGTTCTCCCCGGCCGAAATCCAGATGCTCACCACCGGTGCTGGGCGCCGGTCGGGCAAGCGGTGGGCCGCCGCCAGGGGGCTGCAGGCCTCGGTGGCCATGAGTACCTTCCAGAAAGGTGCTGCGGAACTGGCCCAGCTACGCCAGCAGGCGGTGGACAGTCATGTTCAGGGCGAGCTGTCCGTCAAGGAGACCGAGCTGCTCGACCGGGTCAGCTCGGCGCGGCGGTCCTTCCTCGGGGCCGGCTAG","MSMPPSPWAPRPGYRRSSALPQTPADSGPLPAVGQRYQVHRDTQGTPPSRATDPEDGWQQHGQVASLIPPGIPAKVGAIVMPTAIVVFSLYTLFYFAGLQDDFGPVVLPSFLLALIPLGGVLVATMLLAGVFWYVRWEPRPPGVFTVVTLLVAFLWGTSVSTLCSLVVNNWVAQVITEAMGDLGAAAVISAPLVEELTKGLGVLFVFLIWRRTINGTIDGVVYAAFTASGFAFVENILYFVQGWEHVGTIFVTRGVLSPFAHLTFTACTGVAIGFSSRRRSQYAWAWMAPVGLVGAIVLHATWNGFIASNLGVYLLFQVPFYALCAGLVSWLRWSERRSMRRGLEDYARAGWFSPAEIQMLTTGAGRRSGKRWAAARGLQASVAMSTFQKGAAELAQLRQQAVDSHVQGELSVKETELLDRVSSARRSFLGAG$","Uncharacterized membrane protein","Membrane, Cytoplasm","putative membrane protein","hypothetical protein","membrane protein-like","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[76-96]?$ $\"[115-135]?$ $\"[147-169]?$ $\"[188-210]?$ $\"[220-240]?$ $\"[256-276]?$ $\"[286-306]?$ $\"[312-332]?$	transmembrane_regions

","BeTs to 3 clades of COG2339COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2339 is -o--k----d--b-------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 78-339 are 41% similar to a (MEMBRANE SE2187 SA0228 GLL0770 ALR1728 TLL1537 PROTEIN LIN1229 LMO1261 MW0212) protein domain (PD554766) which is seen in Q8NTZ5_CORGL.Residues 156-242 are 54% similar to a (MEMBRANE) protein domain (PDA049N1) which is seen in Q6A788_PROAC.Residues 156-239 are 57% similar to a (MEMBRANE GLR0655 ALL2084 PH0065 YPDC BLL4391 PROTEIN INTEGRAL DR0441 PF2049) protein domain (PD037663) which is seen in Q9F306_STRCO.Residues 254-420 are 50% similar to a (MEMBRANE INTEGRAL) protein domain (PD667761) which is seen in Q9F306_STRCO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0869","934225","933482","744","6.30","-2.64","26147","ATGACGCGGCTCGTCGATGTCCCCGCCGGTTCGACCACGGTTCTACCGGCGCTGTCCTCCACGGGGTCCGGTGTGACGACGGTGCCGATATGGAGCATCGTTGTGCTGCTGGTCGGGCTGGCGGTGGCCGCCGGGTGGGCCCTGTACGCCAGGGCAGTGCGGGTGGACCGGCTGCACCGGCAGGTGCTGGGAGCTCGAGCCACGCTTGAGGCCCAACTTGTGTACCGGGCCGAGGCCGCGGCGGAGCTGGCCACCGTCCCCGCCCTGGATCCGGCCTCCGGCCTCCTGCTCAGCCAGGCCGCTCGCGAGGCACTGGATGCCGAGGGGCGTGTCGTCGACGACGGTCTGGACACCTCCATGCCTCTTGAGGGCAGCCCCGCTTCTCACCCTGCCTCAGGTGGTGCAGCGCTCTCGGCGCCAACCACCCGCAGTCGGGCCCTCATCGAGTCCGATCTCAGCAGGGTCCTGCGGACGGTGGTCAGCGAGCCCACGCGCCGCGAGCTGTCCGCCGACCCGCTGAGCCTGCCTGCGCTCAACCGCCTGGACCGGGCCTGCTCCCGCCTGGTCCTGGCGCGCAGGTTCCACAACACCCACGTCAGCGAGGCCCAGGCGCTCAGGGGACGCCTACTCGTGCGGATGTGTCACCTGGCTGGGCACGCGCCCATGCCCCAGACCTTCGACGCCGACGACGACACAACCCCTGAAGCGCCGCCCGAGCGCGACGACGAGGTGCAACCGAGGTGA","MTRLVDVPAGSTTVLPALSSTGSGVTTVPIWSIVVLLVGLAVAAGWALYARAVRVDRLHRQVLGARATLEAQLVYRAEAAAELATVPALDPASGLLLSQAAREALDAEGRVVDDGLDTSMPLEGSPASHPASGGAALSAPTTRSRALIESDLSRVLRTVVSEPTRRELSADPLSLPALNRLDRACSRLVLARRFHNTHVSEAQALRGRLLVRMCHLAGHAPMPQTFDADDDTTPEAPPERDDEVQPR$","Secreted protein","Membrane, Cytoplasm","putative membrane protein","secreted protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[30-50]?$	transmembrane_regions

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[179-347]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-393]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF44	$\"[2-393]T$	GLYCOSYLTRANSFERASE

","BeTs to 21 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","***** IPB001296 (Glycosyl transferase, group 1) with a combined E-value of 1.4e-07. IPB001296B 273-305","Residues 1-96 are similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS TRANSFERASE GROUP FAMILY 2.4.1.- LIPOPOLYSACCHARIDE PHOSPHATIDYLINOSITOL) protein domain (PD007341) which is seen in Q827U2_STRAW.Residues 98-187 are 70% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE PHOSPHATIDYLINOSITOL ALPHA-MANNOSYLTRANSFERASE SUGAR GLYCOSYLTRANSFERASES LPS GLYCOSYL RELATED PREDICTED) protein domain (PD036198) which is seen in Q827U2_STRAW.Residues 194-276 are 54% similar to a (TRANSFERASE GLYCOSYLTRANSFERASES LPS GLYCOSYL RELATED GLYCOSYLTRANSFERASE PREDICTED 2.4.1.-) protein domain (PD704789) which is seen in Q8NPZ4_CORGL.Residues 194-265 are 65% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS GROUP TRANSFERASE SYNTHASE FAMILY STARCH LIPOPOLYSACCHARIDE) protein domain (PD000427) which is seen in Q9L284_STRCO.Residues 277-330 are 68% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE SYNTHASE GLYCOSYL GLYCOGEN BIOSYNTHESIS STARCH GROUP FAMILY TRANSFERASE) protein domain (PD064079) which is seen in Q9L284_STRCO.","","-61% similar to PDB:2GEJ Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man (E_value = 4.9E_92);-61% similar to PDB:2GEK Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP (E_value = 4.9E_92);","Residues 179 to 347 (E_value = 3.5e-25) place ANA_0870 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","transferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0871","936458","935460","999","9.86","8.84","37031","ATGAGGATGCGCCTGCCCTCCGTCTCCGACGCCTACCGCCTGGCCTGGCGCGGTACCCGCCACCTGCCCGCGCCGGTGGGCTACGGCCTGGCCCACACTGTCGCCGACGCGCTGTGGGTCTGGCAACGCCTGCGGCGCTCCACCGCCGGGGTGGGGCAGCTCGAGCGCAACCTGGCACGCATCCTCCCGGCGGGAACACCACCGCGAGCGCTGCGCCGCGCCACCCGAGCCGGCATGCGCTCCTACATGCGCTACTTCTACGAGGCCTTCGCCCTGCCCGGTATCACACCGGAGCAGATGCTGGCGCGCGTGCGCACTGACATCGACCCCCAGCTGCACGAGGACGTGCGCGCCGGCAGCGTCGTCATGGCCCTGCCACACATGGGCAACTGGGACCTCATCGGAGCCTGGGCCTGCCGTGAGCTCGCCACCGTCCTGACCGTCGCCGAGCGCCTGGAGCCCGAGGACATCTTCGAGCAGTTCGTCTCCTTCCGCCAGTCACTGGGCATGCGCATCATTGGCCAGTCCCACGGGGAGAAGGTCTTCGACCGACTCGTTGAAGCGGCGAGCCAGGGGCACTACGTCGTCGCACTCCTGGCGGACCGGGACCTGTCCTCGGCCGGCATCACTGCACGGCTGGGCGGTGCCATGGCACGGGTGGCCGCCGGCCCCGCGGCGATCGCCCAGCGCCTGGGGCGACCCCTGTACGCCGCCTCGATCCACTACGAGCCGCTCACCGGCCAGAGGCGCCGTCGGGCCGGATCGCCCTGGGGGATCGTGCTGACCGCCCGCAGGGTTCCGGCGCCCCAGCAGATGGAAGGACGAGAGCAGGTCGTGGCGCACACGCGCGCCTGGGTCGCCGCGCTGGAGCCTCTGCTTGCCGAGCACGCCGAGGACTGGCACATGCTCCAGCCCGTCTTCGACGCCGACCTGGACCAGGAGCGCCTGGCTCGCAGCCACGCCCGCGACCAGCAGGTCACCCACGAGGAGAACGCATGA","MRMRLPSVSDAYRLAWRGTRHLPAPVGYGLAHTVADALWVWQRLRRSTAGVGQLERNLARILPAGTPPRALRRATRAGMRSYMRYFYEAFALPGITPEQMLARVRTDIDPQLHEDVRAGSVVMALPHMGNWDLIGAWACRELATVLTVAERLEPEDIFEQFVSFRQSLGMRIIGQSHGEKVFDRLVEAASQGHYVVALLADRDLSSAGITARLGGAMARVAAGPAAIAQRLGRPLYAASIHYEPLTGQRRRRAGSPWGIVLTARRVPAPQQMEGREQVVAHTRAWVAALEPLLAEHAEDWHMLQPVFDADLDQERLARSHARDQQVTHEENA$","Lauroyl/myristoyl acyltransferase involved inlipid A biosynthesis","Cytoplasm","Lauroyl/myristoyl acyltransferase involved inlipid A biosynthesis","lipid A biosynthesis lauroyl acyltransferase","lipid A biosynthesis acyltransferase","","","","","

InterPro
IPR004960
Family

Bacterial lipid A biosynthesis acyltransferase
PF03279	$\"[1-309]T$	Lip_A_acyltrans

noIPR
unintegrated

unintegrated
tmhmm	$\"[21-41]?$	transmembrane_regions

","BeTs to 3 clades of COG1560COG name: Lauroyl/myristoyl acyltransferase involved in lipid A biosynthesisFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1560 is ----------r---efghsnujxi--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 12-169 are 55% similar to a (ACYLTRANSFERASE TRANSFERASE A LIPID BIOSYNTHESIS LAUROYL 2.3.1.- HEAT SHOCK IVA) protein domain (PD191353) which is seen in Q8NPZ3_CORGL.Residues 79-169 are 58% similar to a (ACYLTRANSFERASE 2.3.1.- TRANSFERASE PROBABLE) protein domain (PD040509) which is seen in O06203_MYCTU.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 309 (E_value = 3.1e-07) place ANA_0871 in the Lip_A_acyltrans family which is described as Bacterial lipid A biosynthesis acyltransferase.","","acyltransferase involved in lipid A biosynthesis","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0872","937012","936455","558","9.96","3.41","18887","GTGACTCCCAACATGCTCACCGTCACCGGAACGGTCCTGTCCGTGACGGCGGCGGTCACCCTGCTGCCGAGGGGGCACTTCGTGGTCGGGCCCCTCGTTCTGCTCGTGGTGCTGGTGGCCGACTCCTTCGACGGCATTCTGGCCCGGGCCACTGGCAAGAGCTCGGTCTTCGGGGCCTTCCTGGACTCGACCATGGACCGCCTCGCCGACGGGGCCGTTCTGGGATCCCTCGCGGCCTGGGCGGCCCTGTCCATGCCCGTCGGCGCGCTGCGCACCGTGACCGTCGCGGCTGGCCTGGTCGCCGTCGTCATGGCGGCCACTGTTCCCTACGCCCGCGCCCGGGCCGAGGCCATCGGCGCCGCCGCCTCTGTCGGGATCGCCGAGCGCACCGACCGGCTCCTGGTCGCGCTCGGTGCCACCTTCATCGTGGGTCTCGGGGCGCCCCAGTGGGTACTCACCGTCGGGCTCCTCTACGTGGCAATTGCCTCCTTCATCACCGTGATCCAACGCGTGCGCGCCGTCCACCAGCAGGTTCGGCAGGAGGGTGAGAAGGCATGA","VTPNMLTVTGTVLSVTAAVTLLPRGHFVVGPLVLLVVLVADSFDGILARATGKSSVFGAFLDSTMDRLADGAVLGSLAAWAALSMPVGALRTVTVAAGLVAVVMAATVPYARARAEAIGAAASVGIAERTDRLLVALGATFIVGLGAPQWVLTVGLLYVAIASFITVIQRVRAVHQQVRQEGEKA$","CDP-alcohol phosphatidyltransferase","Membrane, Cytoplasm","phosphatidylinositol synthase","putative membrane transferase ","CDP-alcohol phosphatidyltransferase","","Nikawa J., Kodaki T., Yamashita S. Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae. J. Biol. Chem. 1987. 262(10):4876-4881. PMID: 3031032Hjelmstad R.H., Bell R.M. sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products. J. Biol. Chem. 1991. 266(8):5094-5134. PMID: 1848238","","","

InterPro
IPR000462
Family

CDP-alcohol phosphatidyltransferase
PF01066	$\"[32-176]T$	CDP-OH_P_transf
PS00379	$\"[44-66]T$	CDP_ALCOHOL_P_TRANSF

InterPro
IPR014552
Family

CDP-diacylglycerol--inositol 3-phosphatidyltransferase
PIRSF029242	$\"[1-182]T$	CDP-diacylglycerol--inositol 3-phosphatidyltransferase

noIPR
unintegrated

unintegrated
PTHR22572	$\"[1-136]T$	SUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF2	$\"[1-136]T$	CDP-DIACYLGLYCEROL-INOSITOL 3-PHOSPHATIDYLTRANSFERASE
signalp	$\"[1-17]?$	signal-peptide
tmhmm	$\"[27-47]?$ $\"[68-86]?$ $\"[92-112]?$ $\"[133-148]?$ $\"[154-174]?$	transmembrane_regions

","BeTs to 15 clades of COG0558COG name: Phosphatidylglycerophosphate synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0558 is aompkzyqv-rlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 4","***** IPB000462 (CDP-alcohol phosphatidyltransferase) with a combined E-value of 4.9e-16. IPB000462 30-77","Residues 3-78 are 67% similar to a (TRANSFERASE SYNTHASE CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE PHOSPHATIDYLTRANSFERASE PHOSPHATIDYLGLYCEROPHOSPHATE 3-PHOSPHATIDYLTRANSFERASE CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE 3- PHOSPHATIDYLSERINE) protein domain (PD329097) which is seen in Q9UYD0_PYRAB.","","No significant hits to the PDB database (E-value < E-10).","Residues 32 to 176 (E_value = 1.1e-16) place ANA_0872 in the CDP-OH_P_transf family which is described as CDP-alcohol phosphatidyltransferase.","","synthase (pgsA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0873","937819","937205","615","5.88","-5.97","22241","GTGACTGAGGAAGTGACCGGAGAGACGATCAGCGCCCCCGGGGGCGGTGACGACGTCGAGGTGGAGGCTCCCTTCTACCACGAGGGCGCTCCGCAGGCCTTTCAGCGGCTGTGGACTCCGCACCGCATGGTCTACATCGGGGGGCAGAACAAGCCCTCCGATGACACCCCCGCACAGTGCCCGTTCTGCACCGGGCCGCAACGCGGTGACGAGGAGTCCCTCATCGTCCACCGGGGCCAGACCAGCTACGTCATCATGAACCTGTACCCGTACAACACCGGTCACCTGCTGGTGTGCCCCTACCGGCACATCTCGGACTGGACCGAGGCCACCCCGGCCGAGCGCCAGGAGATCGGTGAGCTGACCGCCACGGCCATGAGCGTCGTGCGCTCGGTGAGCCGCCCCCACGGGTTCAACCTGGGGATGAACCAGGGCGAGGTCGCCGGTGCAGGGATCGCCGCCCACCTCCACCAGCACATCGTGCCGCGCTGGAAGGGGGACGCGAACTTCATGCCCATCATCGGTCGGACCAAGCCCGTGCCCCAGCTGCTCGGGGAGCAGCGGGACATGCTCGCCGCCGCCTGGGCCACCCGGGCCGGGCAGAGCGGGGACTGA","VTEEVTGETISAPGGGDDVEVEAPFYHEGAPQAFQRLWTPHRMVYIGGQNKPSDDTPAQCPFCTGPQRGDEESLIVHRGQTSYVIMNLYPYNTGHLLVCPYRHISDWTEATPAERQEIGELTATAMSVVRSVSRPHGFNLGMNQGEVAGAGIAAHLHQHIVPRWKGDANFMPIIGRTKPVPQLLGEQRDMLAAAWATRAGQSGD$","Diadenosine tetraphosphate hydrolase","Cytoplasm","Diadenosine tetraphosphate","hypothetical protein","histidine triad (HIT) protein","","Seraphin B. The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals. DNA Seq. 1992. 3(3):177-179. PMID: 1472710Brenner C., Garrison P., Gilmour J., Peisach D., Ringe D., Petsko G.A., Lowenstein J.M. Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nat. Struct. Biol. 1997. 4(3):231-238. PMID: 9164465Bieganowski P., Garrison P.N., Hodawadekar S.C., Faye G., Barnes L.D., Brenner C. Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. J. Biol. Chem. 2002. 277(13):10852-10860. PMID: 11805111Barnes L.D., Garrison P.N., Siprashvili Z., Guranowski A., Robinson A.K., Ingram S.W., Croce C.M., Ohta M., Huebner K. Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5\"'-P1,P3-triphosphate hydrolase. Biochemistry 1996. 35(36):11529-11535. PMID: 8794732Fong L.Y., Fidanza V., Zanesi N., Lock L.F., Siracusa L.D., Mancini R., Siprashvili Z., Ottey M., Martin S.E., Druck T., Mccue P.A., Croce C.M., Huebner K. Muir-Torre-like syndrome in Fhit-deficient mice. Proc. Natl. Acad. Sci. U.S.A. 2000. 97(9):4742-4747. PMID: 10758156Pace H.C., Garrison P.N., Robinson A.K., Barnes L.D., Draganescu A., Rosler A., Blackburn G.M., Siprashvili Z., Croce C.M., Huebner K., Brenner C. Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(10):5484-5489. PMID: 9576908Brenner C. Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry 2002. 41(29):9003-9014. PMID: 12119013","","","

InterPro
IPR001310
Family

Histidine triad (HIT) protein
PTHR23089	$\"[76-202]T$	HISTIDINE TRIAD (HIT) PROTEIN
PF01230	$\"[68-166]T$	HIT
PS51084	$\"[62-170]T$	HIT_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.428.10	$\"[61-171]T$	no description

","BeTs to 21 clades of COG0537COG name: Diadenosine tetraphosphate (Ap4A) hydrolase and other HIT family hydrolasesFunctional Class: F [Metabolism--Nucleotide transport and metabolism] Functional Class: G [Metabolism--Carbohydrate transport and metabolism],RThe phylogenetic pattern of COG0537 is aompkzyq-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001310 (Histidine triad (HIT) protein) with a combined E-value of 3.2e-18. IPB001310A 62-101 IPB001310B 138-162","Residues 38-103 are 77% similar to a (HIT FAMILY HYDROLASE HIT-LIKE TRIAD LONG HISTIDINE MB2645C AQ_2159 DIADENOSINE) protein domain (PD030130) which is seen in Q6A8U2_PROAC.Residues 104-182 are similar to a (HIT FAMILY HYDROLASE HISTIDINE TRIAD HIT-LIKE KINASE REGULATION DIADENOSINE CELL-CYCLE) protein domain (PD406635) which is seen in Q827U7_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 68 to 166 (E_value = 1.1e-08) place ANA_0873 in the HIT family which is described as HIT domain.","","tetraphosphate (Ap4A)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0874","939848","937812","2037","5.44","-22.21","75177","ATGATTGAGATCACCCTCGACGGCGCGCCCCGCACCATTGAGGCGGGCAGCACGGGGGCGCTCCTCCTGCAGGACGCCGTCAAGAAGGACGGCGTCGTGGCGATGCGCGTCAACGGCGAGCCCTGGGATCTGGAGCGCCAGGTCCCGGCGGGCGCCGTCGTCGAGCCCATCACCCTGGCCAGCGAGGATGGCCTCAACATCCTGCGCCATAGCGCCACCCACGTCATGGCGCAGGCCGTCCAGGAGATGTTCCCGGACGTCAACCTCGGCATCGGCCCCTTCATCACCGACGGCTTCTACTACGACTTCGGAGCCATCGACGCCGTCACCCCCGAGATGCTGCGCGAGATCGAGAAGCGCATGAAGCGGATCGTCAAGGAGGGGCAGCGCTTCGTGCGCCGCGACATCACCGAGGACCAGGGGCGTGAGGAGCTGGCCGACCAGCCCTACAAGCTCGAGCTCATCACCACCAAGGGAGCGGGCGCCGAGGGCGCCTCGGTCGAGGTCGGCGCCGGCGGGCTGACCATGTACGACAACGTCCGACGCGACGGCACCGTCGCCTGGACCGACCTGTGCCGCGGCCCCCACCTGCCCTCGACCCGCCTCATCGGGCAGGGCTTCGCGCTGACCAAGTCCTCGTCGGCCTACTGGAAGGGCGACCAGTCCGGCGACTCCCTCCAGCGGATCTACGGCACCGCCTGGGCCACCAAGGACGATCTCAAGGCCTACCAGACCCGCCTGGCCGAGGCCGCCAAGCGCGACCACCGCAAGCTCGGCGCCGAGCTCGACCTCTACTCCTTCCCCGAGGAGATCGGCCCCGGCTTGGTGGTCTTCCACCCCAAGGGCGCCATGCTGCGCCACCAGATCGAGCAGTACGTCGTCGACCGCCACCAGGACTACGGCTTCGACTTCGTCCACACCCCCGAGATCTCCAAGGGCGGGCTCTTCCACACCTCCGGGCACCTGCCCTACTACGCCGACACCATGTTCCCGCCCATGCTCGCCGACGAGGAGCGCGACGCCGAGGGCAACATCACCAAGGCCGGCCAGGAGTACTACCTCAAGGCCATGAACTGCCCGATGCACAACCTCATCTTCCGCTCCCGCGGACGCTCCTACCGCGAGCTGCCGCTGCGCTTCTTCGAGATGGGCCACGACTACCGCTACGAGAAGTCCGGTGTCGTCCACGGGCTCACCCGCATGCGCGGCTTCACCCAGGACGACTCCCACACCTACTGCACACCGGAGCAGGCCGGCGAGGAGATCCGCGCCCAGATCGACTTCTTCCTGTCCATCCTCAAGGCCTTCGGACTGACCGACTTCTACCTCGAGCTGTCCACCCGCGACGAGGACGGCGCCAAGAAGGACAAGTTCATCGGATCCGACGCCGACTGGAACGCCGCCACACAGGCCCTCCAGGACGCCTGTGACGCCTCCGGGCTGGAGGTCGTTCCCGACCCGGGTGGCGCCGCCTTCTACGGCCCCAAAGTCTCGGTGCAGGTCAAGGACGCCATCGGCCGGACCTGGCAGATGTCCACCATCCAGTACGACTTCAACCAGCCCGAGCGCTTCGACCTGGAGTACACGGCCGCTGACGGCACCCACCAGCGCCCCATCATGATCCACTCGGCCAAGCTGGGCAGCGTGGAGCGCTTCATCGGGGTCCTCACCGAGCACTACGCGGGCGCCTTCCCCGCCTGGCTCTCCCCGGTGCAGGTCCGGCTCATCCCCGTGGCCGAGGCCTTCGACGCCTACGTCGATGACGTCGCCGCCCAGCTGCGCGCCCAGGGGGTGCGCGTCGAGGTGGACCACTCCGACGACCGCTTCGGCAAGAAGATCCGCAACGCCTCCAAGGACAAGATCCCCTTCACCCTCATCGCCGGGGGAGAGGACGCCGAGGCCGGCGCCGTCTCCTTCCGGTTCCGCGACGGCCAGCAGACCAACGGCGTGCCCGTCAAGGAGGCCGTGGCCCACATCGTCAGCGTCATCGACGCCCGTATCAACGACCCGGCGGGGGAGAAGCTGCACAGTGACTGA","MIEITLDGAPRTIEAGSTGALLLQDAVKKDGVVAMRVNGEPWDLERQVPAGAVVEPITLASEDGLNILRHSATHVMAQAVQEMFPDVNLGIGPFITDGFYYDFGAIDAVTPEMLREIEKRMKRIVKEGQRFVRRDITEDQGREELADQPYKLELITTKGAGAEGASVEVGAGGLTMYDNVRRDGTVAWTDLCRGPHLPSTRLIGQGFALTKSSSAYWKGDQSGDSLQRIYGTAWATKDDLKAYQTRLAEAAKRDHRKLGAELDLYSFPEEIGPGLVVFHPKGAMLRHQIEQYVVDRHQDYGFDFVHTPEISKGGLFHTSGHLPYYADTMFPPMLADEERDAEGNITKAGQEYYLKAMNCPMHNLIFRSRGRSYRELPLRFFEMGHDYRYEKSGVVHGLTRMRGFTQDDSHTYCTPEQAGEEIRAQIDFFLSILKAFGLTDFYLELSTRDEDGAKKDKFIGSDADWNAATQALQDACDASGLEVVPDPGGAAFYGPKVSVQVKDAIGRTWQMSTIQYDFNQPERFDLEYTAADGTHQRPIMIHSAKLGSVERFIGVLTEHYAGAFPAWLSPVQVRLIPVAEAFDAYVDDVAAQLRAQGVRVEVDHSDDRFGKKIRNASKDKIPFTLIAGGEDAEAGAVSFRFRDGQQTNGVPVKEAVAHIVSVIDARINDPAGEKLHSD$","Threonyl-tRNA synthetase","Cytoplasm","threonyl-tRNA synthetase","threonyl-tRNA synthetase ","threonyl-tRNA synthetase","","Wolf Y.I., Aravind L., Grishin N.V., Koonin E.V. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999. 9(8):689-710. PMID: 10447505Aberg A., Yaremchuk A., Tukalo M., Rasmussen B., Cusack S. Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase. Biochemistry 1997. 36(11):3084-3094. PMID: 9115984","","","

InterPro
IPR002314
Domain

tRNA synthetase, class II (G, H, P and S)
PF00587	$\"[285-458]T$	tRNA-synt_2b

InterPro
IPR002320
Family

Threonyl-tRNA synthetase, class IIa
PR01047	$\"[354-382]T$ $\"[387-410]T$ $\"[495-523]T$ $\"[538-551]T$ $\"[565-577]T$	TRNASYNTHTHR
TIGR00418	$\"[69-663]T$	thrS: threonyl-tRNA synthetase

InterPro
IPR004154
Domain

Anticodon-binding
G3DSA:3.40.50.800	$\"[562-673]T$	no description
PF03129	$\"[572-662]T$	HGTP_anticodon

InterPro
IPR006195
Domain

Aminoacyl-transfer RNA synthetase, class II
PS50862	$\"[254-565]T$	AA_TRNA_LIGASE_II

InterPro
IPR012947
Domain

Threonyl/alanyl tRNA synthetase, SAD
PF07973	$\"[174-230]T$	tRNA_SAD

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[253-561]T$	no description
G3DSA:3.30.980.10	$\"[62-244]T$	no description
PTHR11451	$\"[187-334]T$ $\"[350-669]T$	TRNA SYNTHETASE-RELATED
PTHR11451:SF5	$\"[187-334]T$ $\"[350-669]T$	THREONYL-TRNA SYNTHETASE

","BeTs to 26 clades of COG0441COG name: Threonyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0441 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB004095 (TGS domain) with a combined E-value of 7.6e-80. IPB004095A 93-102 IPB004095B 180-204 IPB004095C 248-262 IPB004095D 355-377 IPB004095E 397-410 IPB004095F 487-496 IPB004095G 512-543 IPB004095H 560-570***** IPB002320 (Threonyl-tRNA synthetase signature) with a combined E-value of 8.6e-70. IPB002320A 354-382 IPB002320B 387-410 IPB002320C 495-523 IPB002320D 538-551 IPB002320E 565-577***** IPB004154 (Anticodon binding domain) with a combined E-value of 3.4e-07. IPB004154B 377-390 IPB004154C 397-406","Residues 70-121 are 94% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA THREONINE--TRNA THRRS BIOSYNTHESIS ATP-BINDING METAL-BINDING ZINC) protein domain (PD006784) which is seen in Q6A8U3_PROAC.Residues 122-155 are 85% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA THREONINE--TRNA THRRS BIOSYNTHESIS ATP-BINDING ZINC METAL-BINDING) protein domain (PD573289) which is seen in Q6A8U3_PROAC.Residues 122-189 are 62% similar to a (SYNTHETASE THREONYL-TRNA AMINOACYL-TRNA) protein domain (PD978164) which is seen in Q70HZ0_BBBBB.Residues 174-220 are 85% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA THREONINE--TRNA THRRS BIOSYNTHESIS ATP-BINDING METAL-BINDING ZINC) protein domain (PD773296) which is seen in Q6A8U3_PROAC.Residues 225-265 are 97% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA THREONINE--TRNA THRRS BIOSYNTHESIS ATP-BINDING METAL-BINDING ZINC) protein domain (PD004144) which is seen in Q8G6C2_BIFLO.Residues 266-514 are 40% similar to a (LIGASE THREONINE-TRNA) protein domain (PDA06860) which is seen in Q6MDC4_PARUW.Residues 267-379 are similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BIOSYNTHESIS ATP-BINDING SERYL-TRNA THREONYL-TRNA SERINE--TRNA SERRS PROLYL-TRNA) protein domain (PD589298) which is seen in Q6A8U3_PROAC.Residues 382-448 are 88% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA THREONINE--TRNA BIOSYNTHESIS ATP-BINDING THRRS METAL-BINDING ZINC) protein domain (PD712581) which is seen in Q6A8U3_PROAC.Residues 458-528 are 87% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA THREONINE--TRNA BIOSYNTHESIS ATP-BINDING THRRS METAL-BINDING ZINC) protein domain (PD748778) which is seen in Q6A8U3_PROAC.Residues 532-579 are 97% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA THREONYL-TRNA THREONINE--TRNA BIOSYNTHESIS ATP-BINDING THRRS METAL-BINDING ZINC) protein domain (PD648905) which is seen in Q6A8U3_PROAC.Residues 585-656 are 79% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS THREONYL-TRNA HISTIDYL-TRNA PROLYL-TRNA HISTIDINE--TRNA HISRS) protein domain (PD000606) which is seen in Q6A8U3_PROAC.","","-57% similar to PDB:1NYQ Structure of Staphylococcus aureus threonyl-tRNA synthetase complexed with an analogue of threonyl adenylate (E_value = 4.4E_134);-57% similar to PDB:1NYR Structure of Staphylococcus aureus threonyl-tRNA synthetase complexed with ATP (E_value = 4.4E_134);-54% similar to PDB:1QF6 STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA (E_value = 1.2E_118);-55% similar to PDB:1EVK CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE WITH THE LIGAND THREONINE (E_value = 2.0E_78);-55% similar to PDB:1EVL CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE WITH A THREONYL ADENYLATE ANALOG (E_value = 2.0E_78);","Residues 174 to 230 (E_value = 4.6e-16) place ANA_0874 in the tRNA_SAD family which is described as Threonyl and Alanyl tRNA synthetase second additional domain.Residues 285 to 469 (E_value = 9.5e-45) place ANA_0874 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T).Residues 572 to 662 (E_value = 4.1e-25) place ANA_0874 in the HGTP_anticodon family which is described as Anticodon binding domain.","","synthetase (thrS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0876","941267","939951","1317","8.52","5.14","49388","ATGCCCGACAGCATCACCCCCGACGCCACGACTGATTCCGCGACTGACTCCATGACTGACTCCACCCCTGACGCCAAGGTCGAGGCCGGTGCGCCGGCCCCCGAGAACGCTCAGGCGACTCAGCCCAAGAACAGGGGGCGCAAGGGCGGCGAGCCCGAACAGTCCAAGCAGCCCGAGCAGAAGATCGACCCGACCGACAAGCCCGCCCAGCCCGCTAGGGCTGACAAGGCTGACAAACCCAAGGCGCCTCGGCTCACGCACCCCGAGCCGGTGCACTCCACCCCGGACCGCTCCGAGACCCTGCGTCGGGTCGACGGGCGCGAGATGCGCCTGGCCGTGGGCAACAGCCACTTCCCGGTTGAGCAGACCGAGGCCTGGGAGCGCTTCGAAGAGGCCATGGGCCGCCCCCTGTGGGGCCGCTACCTCTATGAGGACGAGGGCAAGCCCGTGGCCGCCATCGCCCTGTACCGCTACGAGATAGGCGGCCAGACCTTCCTGTGGGCCAAGCACGGCCCGGTCTGGCTCAAGGAGCAGTCGCCCGAGCGCGAGGCCCACCTGCGGCGCCTGCTGCGCTCCGTGGTCAAGGAGCGCGACCGCTCCGTGCGCTTCATCCGCATGCACGCCCGCTACCGCGCTGCCGACCTGCGAGAGCTGCTGTCCACCATCACCTATGACCGCACCTACGTCATCGACCTGGTGCCCAAGACACCGGAGAAGATGGCCGCGGTCATGCCCAAGGACGGGCGCCGCGCGGTCAAGCGCGCCGAGCGCGTCGCCCGGGAGGCCGGGTGCACCATCAGCGACGAGACCGGCCTGAGCCGTGAGGAGTTCGACCAGGTCTATGAGGTCCTGCGCGAGACCGCCGAGCGCGACGGCTTCAAGCCTCACGACGCCGAGGTCTACTGGACCATGCTCACCTCCCTGGGGGAGAAGAACGCTCGCCTGTTCGTTCTGCGCAAGGACGGCGTCCCTCACGCCTGGGACCTCATCCTCACCTCGGGCAAGGATGCCGTGGCCTACTATGGCGCCTCTTCCAACGAGTCGCGCACCTTCCGCGGGGCCGAGGCCCTGGACTGGTGGGCCGCCTGCACCCTGGCGCAGGAGGGCTACCGCGGCCTGGATCTCATGGGCGCCGGCTCCACCCGCGTCCCCTCGCTCTACACGGTGGGCCAGTACAAGAAGCGCTACGCCCAGCACGTCACCGAGGTGGACGGGGCCTGGGACGTCCCGGTCTCCCGAGTCATCTACTCCGGGATGTCCGCAGCCAAGCGCCTGCGTGACGCACTGCGCGCGCGGCGTGGCTCACGGGAGGACTGA","MPDSITPDATTDSATDSMTDSTPDAKVEAGAPAPENAQATQPKNRGRKGGEPEQSKQPEQKIDPTDKPAQPARADKADKPKAPRLTHPEPVHSTPDRSETLRRVDGREMRLAVGNSHFPVEQTEAWERFEEAMGRPLWGRYLYEDEGKPVAAIALYRYEIGGQTFLWAKHGPVWLKEQSPEREAHLRRLLRSVVKERDRSVRFIRMHARYRAADLRELLSTITYDRTYVIDLVPKTPEKMAAVMPKDGRRAVKRAERVAREAGCTISDETGLSREEFDQVYEVLRETAERDGFKPHDAEVYWTMLTSLGEKNARLFVLRKDGVPHAWDLILTSGKDAVAYYGASSNESRTFRGAEALDWWAACTLAQEGYRGLDLMGAGSTRVPSLYTVGQYKKRYAQHVTEVDGAWDVPVSRVIYSGMSAAKRLRDALRARRGSRED$","Methicillin resistance protein","Cytoplasm, Extracellular","FemAB family family","hypothetical protein with possible similarity to FemA involved in pentaglycine interpeptide bridge in peptidoglycan","Methicillin resistance protein","","Ehlert K., Schroder W., Labischinski H. Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J. Bacteriol. 1997. 179(23):7573-7576. PMID: 9393725Vannuffel P., Heusterspreute M., Bouyer M., Vandercam B., Philippe M., Gala J.L. Molecular characterization of femA from Staphylococcus hominis and Staphylococcus saprophyticus, and femA-based discrimination of staphylococcal species. Res. Microbiol. 1999. 150(2):129-141. PMID: 10209768","","","

InterPro
IPR003447
Family

Methicillin resistance protein
PF02388	$\"[122-424]T$	FemAB
PS51191	$\"[99-422]T$	FEMABX

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[233-396]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 100-416 are 50% similar to a () protein domain (PD845065) which is seen in Q8G4M4_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 122 to 424 (E_value = 0.00036) place ANA_0876 in the FemAB family which is described as FemAB family.","","family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0877","942527","941286","1242","6.48","-2.39","45669","ATGACGCAACGCTTCAGGCACCTGCTGCCCGTGGTTCTCGGTGGCGATATCGGCGCCTACGCCCTGGCGCGGCAGCTTCATGAGGTCACCGGTACATCGGTGATGGTCGTGGCCTCGGATCCGATCGTCGCGATCTCCGAGTCGGTCTACATCACCGTGGTTCACCAGGAGGCCGGGGCCCCGCCGGAGCGGACCATCGCGCTGCTGCGACAGCTGGCCCAGGGCAGAGGACCCCGTAGTGCTGTGCTCATGGCCAACACCGACGCCGCGGCCGCCATGATCTCGGCCCACCGCAGCGAGCTCGAGCCCACCTACGTCCTGCCCTTCCCGGACATCGACGTTCTCGACGCCGTCAGCGACAAGGCCTCCTTCTCCCGTCTGTGCGCAGAGGTCGGGGTGCTCACGCCCCGGGAGGTCGTCGTCGACCTGGCCGACCCGGACTGCGAGCCGCCGACCAGCGCCGGCGAGCTCGGCATGGAGTTCCCGCTCGTGGCCAAGGCGGCCATCGGCGCTGACTACGACCGTATCTCCTTCCCCGGCAAGCGCAAGATCTGGTTCATCGACGACGCCGCCGAGCTGGCAGGCATGTGGAGGAGCCTGAAGGAGGCCGGCTACCGCTCCACCTTCCTGGTTCAGGAGTGCATCCCCGGTGACGACACCGCCATGCGCTCGGTGACCGCCTACATGGACTCCACCGGTGAGCTGCGCCTCATCGGCTCGGCGCGTGTCCTGCTGCAGGACCACGCGCCCACCATGATCGGCAACCCGGTCGCCATGATCACCGAGGCCTTCCCCGACCTGTGGGAGGCCACTGGACGCCTGCTGCGCCACGCCGGCTACCGCGGCTTCGCCAACCTCGACATCAAGGTCGACCCCCGCGACGGACGGGAGCTCTTCTTCGAGGTCAACCCCCGTATCGGCCGCAACTCCTTCTACCTCACCGCCGCCGGCGCCAACCCCATGGCCGTCATGCTCAAGGACCTGGTCCTGGACCAGCGCGACGAGCCCATCGAGGTCACCCGGCAGGTCCTCTACTCCCTGGTTCCCGACGGCGTCATCGAACGCTACGTGTCCGACGAGGCGCTGCGCCGCAAGGCCAAGGGCCTGGGGCGGGGCGTCGACCCGCTGCGCGACCCGGCCGAGCGCTCGCTGCGCCGTCGCGTGACGATCGAGCTCCAGCGCCTCAACCACTACCGCAAGTTCGCCCGCAACTATCCGCAACGAGTCGACAGGTCCCGCTGA","MTQRFRHLLPVVLGGDIGAYALARQLHEVTGTSVMVVASDPIVAISESVYITVVHQEAGAPPERTIALLRQLAQGRGPRSAVLMANTDAAAAMISAHRSELEPTYVLPFPDIDVLDAVSDKASFSRLCAEVGVLTPREVVVDLADPDCEPPTSAGELGMEFPLVAKAAIGADYDRISFPGKRKIWFIDDAAELAGMWRSLKEAGYRSTFLVQECIPGDDTAMRSVTAYMDSTGELRLIGSARVLLQDHAPTMIGNPVAMITEAFPDLWEATGRLLRHAGYRGFANLDIKVDPRDGRELFFEVNPRIGRNSFYLTAAGANPMAVMLKDLVLDQRDEPIEVTRQVLYSLVPDGVIERYVSDEALRRKAKGLGRGVDPLRDPAERSLRRRVTIELQRLNHYRKFARNYPQRVDRSR$","Carbamoylphosphate synthase large subunit","Cytoplasm","conserved hypothetical protein","predicted ATP-grasp enzyme","ATP-grasp enzyme-like","","Pervaiz S., Brew K. Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science 1985. 228(4697):335-337. PMID: 2580349Flower D.R., North A.C., Attwood T.K. Mouse oncogene protein 24p3 is a member of the lipocalin protein family. Biochem. Biophys. Res. Commun. 1991. 180(1):69-74. PMID: 1834059Flower D.R., North A.C., Attwood T.K. Structure and sequence relationships in the lipocalins and related proteins. Protein Sci. 1993. 2(5):753-761. PMID: 7684291Flower D.R. Multiple molecular recognition properties of the lipocalin protein family. J. Mol. Recognit. 1995. 8(3):185-195. PMID: 8573354","","","

InterPro
IPR002345
Domain

Lipocalin
PS00213	$\"[188-200]?$	LIPOCALIN

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[125-329]T$	ATP_GRASP

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide

","BeTs to 13 clades of COG0458COG name: Carbamoylphosphate synthase large subunit (split gene in MJ)Functional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0458 is aomp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 82-307 are 52% similar to a (CARBOXYLASE PROBABLE SMU.49 ACETYL-COA YXBA MLL1183 LIGASE AGR_L_1972P ATU3860 SCO2715) protein domain (PD457653) which is seen in Q74LP7_LACJO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0880","943119","945386","2268","4.95","-45.08","84274","GTGACATGTCTTTCTCCCACTCTCCTGCCTTCGCACCTCAGTCGTGGCAGGGTAGTCCCCATGACCACGCCGACAACACCGACGCCTCAGGCCGCACCGGAACCTCAGGAGGGCCCCCAGCGCCAGATCTGGCCGGGCCACCCCTACCCACTCGGGGCTACCTACGACGGCTCGGGAACGAACTTCGCCCTGTACTCCTCAGCCGCCACCGGTGTCGACCTGTGCCTGTTCGACGACGAGGGCCATGAGGAGCGGGTGGCCCTCAAGGAGGTCGACGGCGACGTCTGGCACGTCTACCTGCCCGGAATCTCTCCGGGCCAGAAGTACGGCTACCGGGTGGCAGGCCCCTACGACCCGGCCTCCGGTCACCGCTGCGACCCCTCCAAGCTGCTGCTGGACCCCTACGCCAAGGCGATCGACGGCGAGGTGACCCCGTCCCAGACGCTGTACTCCTACTCCTTCGACAACCCGGAGGTGCGCAACGAGGAGGACTCGGCGGGACACACCATGCGCTCAGTGGTCATCAACCCCTACTTCGACTGGGGCCACGACCGTCCCCCGAACCACGAGTACCACGAGACGATCATCTACGAGGCCCACGTCAAGGGCATGACCAAGCTGCACCCGATGGTTCCCGAGGACCTGCGGGGCACCTACGCCGGTCTGGCACAGCCCGCCGTCATCGACCACCTCAAGAACCTGGGTGCGACGGCTATCGAGCTCATGCCGGTCCACCAGTTCGTCAACGACACCCACCTGCAGGAGAAGGGCCTGTCGAACTACTGGGGCTACAACACGATCGGATTCTTCGCCCCGCACAACACCTACGCCGCCTACGGCACCAAGGGTGAGCAGGTCCAGGAGTTCAAGTCCATGGTCAAGGCCTTCCACGAGGCCGACATCGAGGTCATCCTGGACGTGGTCTACAACCACACGGCCGAGGGCAACCACCTGGGCCCCACGCTGTCCTTCCGAGGCATCGACAACAGCTCCTACTACCGCCTCGTCGATGGATCGGCCAGCCACTACTTCGACACCACCGGTACCGGCAACTCGCTGCTCATGCGCTCGCCGGCGGTTCTCCAGCTCATCATGGACTCGCTGCGCTACTGGGTCACTGAGATGCACGTCGACGGGTTCCGCTTCGACCTGGCCTCCACTCTGGCGCGTCAGTTCCACGAGGTGGACAAGCTCAGCGCCTTCTTCGACATCATTCACCAGGACCCCGTGCTCTCCCAGGTCAAGCTCATCGCCGAGCCCTGGGACGTGGGCGACGGCGGCTACAACGTGGGCGGCTTCCCGGCCCTGTGGAGCGAATGGAACGGCAAGTACCGCGACACCGTGCGCGACTTCTGGCGCGGGGAGCCCTCCACCCTGGGCGAGTTCGCCTCCCGTATCACCGGCTCCTCCGACCTCTACCAGCATGCCGGGCGCACCCCGGTGGCCAGCATCAACTTCGTCACCGCCCACGACGGCTTCACGCTGCGTGACCTGGTCTCCTACAACGAGAAGCACAACGAGGCCAACCTCGAGGGCAACGCAGACGGGGACAACAACAACCGGTCCTGGAACTGCGGCGCCGAGGGGCCCACCGACGATCCGACGATCACCGAGCTGCGTCAGCGCCAGACCCGCAACTTCCTGGCCACCGTCCTGTTCAGTCAGGGCGTGCCCATGATCTGCCACGGCGACGAGATGGGACGCACCCAGGGGGGCAACAACAACGTCTACTGCCAGGACAACGAGATCTCCTGGGTCAACTGGGATCTCAGTGAGCAGGACAACGACCTGCTGGAGTTCACCCGCACCATGATGTGGCTGCGTCGCGACCACCCGGTGCTGCGGCGTCGGCGCTTCTTCACCGGGGACGCCCGCCACGGCGGGGAGAGCGAGCTCGGCGAGATCGAGTGGCTCACTCCGGCCGGTGAGTCCATGACCGACCAGGACTGGACCACCTGGTACGCCCGGGCCATGATGGTCTTCCTCAACGGGGAGGCGATCGCCGAGCCCGATGAGCGGGGCCAGAGGATCGTGGACGACTCCTTCCTCGTACTCATCAACGCCTCCGACGAGGACATCACCTTCACCCTGCCCGGCGAGGGGTACGCCCCCACCTGGAAGGTCGCGCTAGACACGGCTCCCGCAGTGGACGGGGACTCCGACCCGGTTCTCGCTGCTGACGACACCGTCGTGGTCGAGGCCCGCTCCATGCTCTTCCTCATCGACGCCCCCGAGTCCGCCGCCACCACGGAGCGCCACCCGAGGTAG","VTCLSPTLLPSHLSRGRVVPMTTPTTPTPQAAPEPQEGPQRQIWPGHPYPLGATYDGSGTNFALYSSAATGVDLCLFDDEGHEERVALKEVDGDVWHVYLPGISPGQKYGYRVAGPYDPASGHRCDPSKLLLDPYAKAIDGEVTPSQTLYSYSFDNPEVRNEEDSAGHTMRSVVINPYFDWGHDRPPNHEYHETIIYEAHVKGMTKLHPMVPEDLRGTYAGLAQPAVIDHLKNLGATAIELMPVHQFVNDTHLQEKGLSNYWGYNTIGFFAPHNTYAAYGTKGEQVQEFKSMVKAFHEADIEVILDVVYNHTAEGNHLGPTLSFRGIDNSSYYRLVDGSASHYFDTTGTGNSLLMRSPAVLQLIMDSLRYWVTEMHVDGFRFDLASTLARQFHEVDKLSAFFDIIHQDPVLSQVKLIAEPWDVGDGGYNVGGFPALWSEWNGKYRDTVRDFWRGEPSTLGEFASRITGSSDLYQHAGRTPVASINFVTAHDGFTLRDLVSYNEKHNEANLEGNADGDNNNRSWNCGAEGPTDDPTITELRQRQTRNFLATVLFSQGVPMICHGDEMGRTQGGNNNVYCQDNEISWVNWDLSEQDNDLLEFTRTMMWLRRDHPVLRRRRFFTGDARHGGESELGEIEWLTPAGESMTDQDWTTWYARAMMVFLNGEAIAEPDERGQRIVDDSFLVLINASDEDITFTLPGEGYAPTWKVALDTAPAVDGDSDPVLAADDTVVVEARSMLFLIDAPESAATTERHPR$","Glycogen debranching enzyme GlgX","Cytoplasm, Extracellular","glycogen debranching enzyme","glycogen debranching enzyme GlgX","glycogen debranching enzyme GlgX","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR004193
Domain

Glycoside hydrolase, family 13, N-terminal
PF02922	$\"[50-136]T$	Isoamylase_N

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[212-316]T$	Alpha-amylase

InterPro
IPR011837
Family

Glycogen debranching enzyme GlgX
TIGR02100	$\"[45-742]T$	glgX_debranch: glycogen debranching enzyme

InterPro
IPR013779
Family

Isoamylase-type debranching enzyme
PIRSF003068	$\"[45-748]T$	Isoamylase-type debranching enzyme

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[178-618]T$	no description

InterPro
IPR013783
Domain

Immunoglobulin-like fold
G3DSA:2.60.40.10	$\"[45-176]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[176-740]T$	AMYLASE
PTHR10357:SF25	$\"[176-740]T$	GLYCOGEN DEBRANCHING ENZYME

","BeTs to 10 clades of COG1523COG name: Pullulanase and related glycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1523 is --------vdrlbcefgh---j-i--Number of proteins in this genome belonging to this COG is 3","***** IPB004193 (Glycoside hydrolase, family 13, N-terminal) with a combined E-value of 7.7e-43. IPB004193B 192-207 IPB004193C 255-279 IPB004193D 297-311 IPB004193E 370-383 IPB004193F 516-525***** IPB005323 (Bacterial pullanase-associated domain) with a combined E-value of 7.4e-26. IPB005323A 194-218 IPB005323B 300-312 IPB005323C 371-382 IPB005323D 477-497 IPB005323E 547-577***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 1.5e-17. IPB006589A 226-243 IPB006589B 283-311 IPB006589C 376-387","Residues 46-141 are 84% similar to a (HYDROLASE GLYCOGEN GLYCOSIDASE DEBRANCHING ENZYME PULLULANASE ISOAMYLASE 3.2.1.- OPERON GLGX) protein domain (PD203330) which is seen in Q73UV4_MYCPA.Residues 64-143 are 61% similar to a (BRANCHING ENZYME TRANSFERASE GLYCOGEN GLYCOSYLTRANSFERASE 14-ALPHA-GLUCAN BIOSYNTHESIS BE 14-ALPHA-D-GLUCAN:14-ALPHA-D-GLUCAN 6-GLUCOSYL-) protein domain (PD376916) which is seen in Q6A8Q3_PROAC.Residues 95-191 are 50% similar to a (PROBABLE OPERON GLYCOGEN GLGX) protein domain (PD785516) which is seen in Q8G422_BIFLO.Residues 176-247 are 58% similar to a (ISOAMYLASE ENZYME STARCH ISO2 ISOAMYLASE-TYPE DEBRANCHING ISOFORM 85KDA F15K9.9) protein domain (PD861361) which is seen in Q9ZVT2_ARATH.Residues 195-248 are 88% similar to a (HYDROLASE GLYCOSIDASE ALPHA-AMYLASE GLYCOGEN PRECURSOR METABOLISM ALPHA-GLUCOSIDASE FAMILY ENZYME SIGNAL) protein domain (PD001430) which is seen in Q740S2_MYCPA.Residues 195-253 are 64% similar to a (GLYCOGEN GLGX TYPE OPERON II SECRETORY PATHWAY PULLULANASE PATHWAY) protein domain (PD791167) which is seen in Q6LK95_PHOPR.Residues 196-244 are 73% similar to a (HYDROLASE ENZYME 3.2.1.- GLYCOSIDASE PROBABLE GLYCOSYL GLYCOGEN DEBRANCHING) protein domain (PD925812) which is seen in Q92M11_RHIME.Residues 260-305 are 86% similar to a (GLYCOGEN ENZYME BRANCHING TRANSFERASE HYDROLASE 14-ALPHA-GLUCAN GLYCOSYLTRANSFERASE BIOSYNTHESIS BE GLYCOSIDASE) protein domain (PD562270) which is seen in Q9X947_STRCO.Residues 303-390 are 93% similar to a (HYDROLASE GLYCOGEN GLYCOSIDASE DEBRANCHING PULLULANASE ENZYME ISOAMYLASE OPERON 3.2.1.- GLGX) protein domain (PD000975) which is seen in Q8G5M7_BIFLO.Residues 403-533 are similar to a (GLYCOGEN HYDROLASE DEBRANCHING ENZYME GLYCOSIDASE ISOAMYLASE OPERON 3.2.1.- GLGX METABOLISM) protein domain (PD008556) which is seen in Q9LC80_ARTSQ.Residues 536-605 are 81% similar to a (HYDROLASE GLYCOSIDASE ALPHA-AMYLASE GLYCOGEN PRECURSOR CALCIUM-BINDING SIGNAL METABOLISM ENZYME DEBRANCHING) protein domain (PD002991) which is seen in Q8NNT0_CORGL.Residues 634-716 are 68% similar to a (GLYCOGEN HYDROLASE ENZYME DEBRANCHING GLYCOSYL 3.2.1.- GLYCOSIDASE PROBABLE OPERON GLGX) protein domain (PD178531) which is seen in Q8FNY3_COREF.","","-46% similar to PDB:1BF2 STRUCTURE OF PSEUDOMONAS ISOAMYLASE (E_value = 5.7E_90);-42% similar to PDB:1EH9 CRYSTAL STRUCTURE OF SULFOLOBUS SOLFATARICUS GLYCOSYLTREHALOSE TREHALOHYDROLASE (E_value = 1.5E_18);-42% similar to PDB:1EHA CRYSTAL STRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS (E_value = 1.5E_18);-41% similar to PDB:2BHU CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E_value = 1.9E_16);-41% similar to PDB:2BHY CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH TREHALOSE (E_value = 1.9E_16);","Residues 50 to 136 (E_value = 2.8e-33) place ANA_0880 in the Isoamylase_N family which is described as Isoamylase N-terminal domain.Residues 173 to 608 (E_value = 4.1e-08) place ANA_0880 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.","","debranching enzyme (treX)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0881","945480","948119","2640","4.86","-50.60","96085","ATGACCGACGCAGTGGACGCAGCAGTGGATCAGGCAGGTTCGGCGGGTTTTGCGGAGACACCCGCCTACGCACCGTGGTCGGGGCACGTGCCGGCTCCGGAGCACCGCACGCCGGTGACCACCTACCGTCTCCAGCTCGGCGAGGACCTGACCTTCGCAGACGCCAAGGCCCTGGTCCCCTATCTGGCCGACCTGGGGGTCACCGACCTCTACCTCTCCCCGATCCTCACCGCCGCACCGGGCTCCACCCACGGCTACGACGTCGTCGATCACCGCCGGGTCTCGGCGATCATGGGCGGAAGGGAGCAGCTGGAGTCCCTGGCCGCTGAGGCCGACGCCCACGGCATGGGCGTCGTGGTGGACATCGTTCCCAACCACATGGCCGTGCCCACCCCCGGCTGGCACAACCTGCCCCTGTGGTCGGTGCTGCGTGAGGGTCCGGACTCCCCCTACGCCGCCTGGTTCGATCTCTCCCTGGACGAGCCCATCCTCATGCCGATCCTGGGCAAGCGCATCGGCGCCGTCCTGGCCGATGAGGAGCTCACCCTGGAGCAGATGGTGGTTCCGGGTCAGGAGGACCTGGGCGAGCAGTGGGTCCTGCGCTACTACGACCACGCCTTCCCCGTCGCCCAGGGCACAGAGTCGCTGCCGATGCACGTCCTCGTCGACCGCCAGCACTACCGGCTGGCCTACTGGAAGGTCGGCGACGAGGAGATCAACTACCGACGGTTCTTCGATGTCGGCACCCTGGCCGCGATCCGCGTCGAGGAGCCCGACGTCTTCGCCGGAAGCCACGGCCTCATCCTCGATCTCATGAGAGACGGAGTCATCAGCGCCCTGCGGGTCGACCACCCCGACGGCCTGGCCGACCCCGGTGGCTACCTCACCCAGCTGGCCGAGGCCACCAGCGGGGCCTGGATCGCTGCGGAAAAGATCCTGGCGCCCGACGAGTCCCTGCCCACCTCCTGGCCAGTGGCCGGAACCACCGGCTACGACGCCGCCTGGCGGATCGACCAGCTCCAGGTGGACCCCGCCGGCGCGGCCCGCCTGGGCGCACTCATGCAGGAGCTCACCGGGGACGCACCCGTGGACTACGACCGCGTCGTCGAGGAGGCCAAGCGAGAGGTCATCGCCGGCTCACTGGCAGCCGAAGTCGACCGTCTGGCCCGCATCTTGGACTGCCTGACCTCACAGGACGTGCGCCTGCGTGACCACACCCTGCGCGACCTGCGGGCCTGCGTCGTCGAGCTGCTCGTGGCCGCAGACCAGTACCGGGTCTATGTCGTTCCCGGGACGCCCCCAGGCCCGGAGACGGCCGCCGTGCTCCAGGCCGACGCCGAGCGGGCCCGTCAGCGCCTTGAGCCGGACCAGGGAGAGACCCTCGACCTCGTGGTCGCCATCCTCCTGGGTGAGCCGGTCGGCTCCGAGGGACTGTCGGAGTCCCCCGAGCGAGCCGAGGCCATCATCCGTTTCCAGCAGGTGTGCGGGGCCGTCACCGCCAAGGGAGTGGAGGACACGGCCTTCTATCGCTGGACCCACCTGACCAGTCTCACCGAGGTCGGCGGCAACCCGGCCGGCTTCGCGCTGAGTGCCGACGAGGCCCACGCGTGGGCCGACCGGGTCCAGAACATCTGGCCCGACACGATGGTCACCTCCACGACCCACGACACCAAGCGCGGTGAGGACGTGCGCGCCCGCCTGGACGTGCTGGCCTCCTACGCCGAGGAGTGGAGCGACCTCATCCATCGTCTGCGCGCCATGACCGCGCAGGTCCGCCCCCTGGACCTCGACGGGCGCAGCGAGAACCTGCTGTGGCAGACCCTGTGGGGGACCTGGGCGCCCGACAGCGACGACCCCATGACCTCCGAGCGGCTGAGCGCCTATCTCATCAAGGCCTCCCGGGAGCAGAAGATCTGGACCACCTGGACCGCCCCGGACCTGGCTCGGGAGCAGGCCCTGACCGACTACGCCACCCATCTGCTCACCAGCGAGGAGGTCCGCGACGAGCTCGAGGCCTTCGCGGCCCTGACGGCCAGGTCCGTGCGCACCGCGATCCTCGCCGGCAAGGCGCTGTCGCTGACCTGGATGGGGGTCAGCGACATCTACCAGGGCAGCGAGACCACCCGCACCTCACTGGTGGACCCCGACAACCGTCGCGCGGTCGACTACGCCGGGCCCTCGGGCCTCATCAGCGCCCTGGAGCGCCTCGACTCGGGAGCCGCACCGCGCAGCCTGGATGAGGACAAGCTCTTCCTCACCTCACGCCTGGCGCGTCTGCGCGCCGCTCGCCCCCACACCTTCGTCGGTCCCCGCTCGGGCTACCGCACGATCCCGGTGACCACCTCCTTCGCCTTCGCCTACACCCGCCTGCTCGACGAGGTCCCCGACGTCGTCGTCATCGTCAGGCGCCTGTCCCGGCGGCTCGAGCAGCTGGGGGGATGGCGTGAGGAGAGCATCGTCCTGCCGGCGGGGACCTGGGAGCACGTCCTGCGCACCGGCACCGTGGAGGGAGGCAGCCAGCCTCTGACCGAGGTGGTAGGGGACGATGCCGTCGTCGTCCTGGCCAGGGTCGTCTCCCCCGACTCCCAGACCGACGCGGAGCACGCCGCCCAGCACACCACCCAGGAGGCCGCCCGATGA","MTDAVDAAVDQAGSAGFAETPAYAPWSGHVPAPEHRTPVTTYRLQLGEDLTFADAKALVPYLADLGVTDLYLSPILTAAPGSTHGYDVVDHRRVSAIMGGREQLESLAAEADAHGMGVVVDIVPNHMAVPTPGWHNLPLWSVLREGPDSPYAAWFDLSLDEPILMPILGKRIGAVLADEELTLEQMVVPGQEDLGEQWVLRYYDHAFPVAQGTESLPMHVLVDRQHYRLAYWKVGDEEINYRRFFDVGTLAAIRVEEPDVFAGSHGLILDLMRDGVISALRVDHPDGLADPGGYLTQLAEATSGAWIAAEKILAPDESLPTSWPVAGTTGYDAAWRIDQLQVDPAGAARLGALMQELTGDAPVDYDRVVEEAKREVIAGSLAAEVDRLARILDCLTSQDVRLRDHTLRDLRACVVELLVAADQYRVYVVPGTPPGPETAAVLQADAERARQRLEPDQGETLDLVVAILLGEPVGSEGLSESPERAEAIIRFQQVCGAVTAKGVEDTAFYRWTHLTSLTEVGGNPAGFALSADEAHAWADRVQNIWPDTMVTSTTHDTKRGEDVRARLDVLASYAEEWSDLIHRLRAMTAQVRPLDLDGRSENLLWQTLWGTWAPDSDDPMTSERLSAYLIKASREQKIWTTWTAPDLAREQALTDYATHLLTSEEVRDELEAFAALTARSVRTAILAGKALSLTWMGVSDIYQGSETTRTSLVDPDNRRAVDYAGPSGLISALERLDSGAAPRSLDEDKLFLTSRLARLRAARPHTFVGPRSGYRTIPVTTSFAFAYTRLLDEVPDVVVIVRRLSRRLEQLGGWREESIVLPAGTWEHVLRTGTVEGGSQPLTEVVGDDAVVVLARVVSPDSQTDAEHAAQHTTQEAAR$","Malto-oligosyltrehalose synthase","Cytoplasm, Extracellular","alpha,alpha-trehalose-phosphate synthase","malto-oligosyltrehalose synthase","malto-oligosyltrehalose synthase","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[55-128]T$	Alpha-amylase

InterPro
IPR012767
Family

Malto-oligosyltrehalose synthase
TIGR02401	$\"[38-856]T$	trehalose_TreY: malto-oligosyltrehalose syn

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[37-771]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[59-330]T$	AMYLASE
PTHR10357:SF10	$\"[59-330]T$	ALPHA-AMYLASE

","BeTs to 3 clades of COG3280COG name: Maltooligosyl trehalose synthaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG3280 is ---------dr----f----------Number of proteins in this genome belonging to this COG is 1","***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 1.3e-13. IPB006589A 57-74 IPB006589B 98-126***** IPB006048 (Alpha amylase, C-terminal all-beta domain) with a combined E-value of 2.9e-07. IPB006048A 43-77 IPB006048B 99-127***** IPB004185 (Glycoside hydrolase, family 13, N-terminal Ig-like domain) with a combined E-value of 1.1e-06. IPB004185B 46-79 IPB004185C 85-116 IPB004185H 684-729","Residues 39-83 are 72% similar to a (SYNTHASE MALTOOLIGOSYLTREHALOSE HYDROLASE TREHALOSE MALTOOLIGOSYL GLYCOSYL ISOMERASE ALPHA PROBABLE PLASMID) protein domain (PD608239) which is seen in TREY_MYCTU.Residues 120-228 are 60% similar to a (SYNTHASE MALTOOLIGOSYLTREHALOSE HYDROLASE TREHALOSE MALTOOLIGOSYL GLYCOSYL ISOMERASE ALPHA PROBABLE PLASMID) protein domain (PD608652) which is seen in Q82L60_STRAW.Residues 241-587 are 55% similar to a (SYNTHASE HYDROLASE MALTOOLIGOSYLTREHALOSE TREHALOSE MALTOOLIGOSYL GLYCOSYL ALPHA PROBABLE AMYLASE PLASMID) protein domain (PD011989) which is seen in Q53237_RHISP.Residues 343-470 are 43% similar to a (ALPHA ALPHA-AMYLASE AMYLASE) protein domain (PD722129) which is seen in Q82L60_STRAW.Residues 604-845 are 51% similar to a (SYNTHASE MALTOOLIGOSYLTREHALOSE HYDROLASE TREHALOSE MALTOOLIGOSYL GLYCOSYL ISOMERASE ALPHA PROBABLE PLASMID) protein domain (PD654395) which is seen in Q53237_RHISP.","","-47% similar to PDB:1IV8 Crystal Structure of Maltooligosyl trehalose synthase (E_value = 1.4E_74);-45% similar to PDB:1GVI THERMUS MALTOGENIC AMYLASE IN COMPLEX WITH BETA-CD (E_value = 1.1E_10);-45% similar to PDB:1SMA CRYSTAL STRUCTURE OF A MALTOGENIC AMYLASE (E_value = 1.1E_10);","Residues 41 to 763 (E_value = 0.00038) place ANA_0881 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.","","synthase (treY)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0882","948116","949915","1800","4.84","-40.42","65388","ATGAGCCCGGCATCCCGGACCTGGCAGTCACCGGCCCTGCCTGTGGGCCCCCGCGTTCCCGTATGGGCCCCCACGGCGAGGCGGGTCGAGCTGCACCTGCCCGGCGATGAGGGACTGGATGACCGGCTGGCTGACATGGTCCCGGCCCCCGACGGCTGGTGGACCGCCCCCTTCGACCTGGAGCCGGGCACCGACTACGCCTTCCGGATCGACGGCTCCCCCGACCGCCCCGATCCCCGCAGTGCCCTGCAGCCCCACGGCGTCCATGGCCCCTCTCGAACTACGGATCCGAGCGCCTGGCAGTGGACCGACCAGGACTGGATGGGCAAGGACCTGCTCGGCTCAGTCATCTACGAGCTCCACGTGGGCACGTTCACCCCCGAGGGCACCCTGGACAGCGCCATCTCCCGGCTGGGCCACCTGGCTGAGCTGGGCGTCGACATCGTCGAGCTCATGCCGCTGGCAGCCTTCCCCGGCCGAGCCGGATGGGGTTACGACGGGGTGGGCCTGTGGGCCGTCCACGAGGCATACGGGGGCCCCGAGGCCCTGATGCGCTTCGTCGACGCCGCCCACCGCGCCGGTATCGGCGTGTGCCTCGACGTCGTCTACAACCACCTGGGCCCGTCGGGCAACTATCTCAGCGTCTTCGGCCCCTACTTCACTCCCGCCCATCACACGCCCTGGGGTGAGGCCGTCAACTATGACCACGACGGCAGTCATCAGGTGCGTGCCTTCGTCATCGACTCGGCCCTGCGCTGGCTGCGGGACTTCCACGTCGACGCCCTGCGCCTGGACGCCATTCATGAGATCAAGGATGACGCTGCAGCCGCCGACCCACCGCAGGCTCACGTCCTGGCCGAACTCTCCGACGCCGTGGCCGCCCTGTCCACCGAACTGGGCCGCCCCCTGAGCCTGGTGGCCGAGGCGGACCTCAACGATGTCGGAGTCATCACCCCCACCGACCAGGAGCCCCCCGCCGCGACACCCAGCCTGGGTATGACCGCCCAGTGGGCCGACGACGTTCACCATGCCCTGCACGCACGGATCACCGGCGAGGCGCAGGCCTACTACGCCGACTTCGCCGAGCCCGGAGCGTGGATCAAGGCCTACAGCAGCGCCTTCCTCCACAACGGCATCTGGTCCACTTTCCGGGACCGGGTCTGGGGCGCCCCCGTCCCCGAGGACACCGACCCCAGGCGCTTCGTCGTCTTCGGCTCCAACCACGACCAGATCGGCAACCGAGCCGTCGGGGACCGCCCCTCGGCCGGTCTCGACGACGCCGCCCTGGCCGCCACTGCCGCCCTGGTGCTCCTGTCGCCCTACACGCCCATGCTCTTCATGGGCGAGGAGTGGGGAACCCGTACTCCCTTCCAGTTCTTCACCGACCATGAGGAGGAGGACCTGGCCCGCAGCGTCAGCCAGGGGCGCGCCCGGGAGTTCGCCGGCTTCGGCTGGGACGCCGACGAAATCCCCGACCCCCAAGACGCCGGGACCGTCGAGGCCTCACGCCTGGACTGGTCCGAGCTGGACAAGACCGAACACGCCCACATGCTGTCCTGGTACCGGGCACTGACCGCCCTACGCCGCGAGCTGGGATGGTCCCAGCGCACCGCGTGGCCGCAGATCGATGAGGCCGACGATGTTGTCACCGTGACCTACGAGGACATCGTCGTCGTCACCAACCTCTCCGGGAGGCCACGGCCCGCTGCCGAGCTGAGTGACGTGCTCCTCTCCTGGGCCCCGGTCGGCTCCGACCCGTCCTGCCTGCCGGCCGGACAGACGCTCGTCGCCCGACGCTGA","MSPASRTWQSPALPVGPRVPVWAPTARRVELHLPGDEGLDDRLADMVPAPDGWWTAPFDLEPGTDYAFRIDGSPDRPDPRSALQPHGVHGPSRTTDPSAWQWTDQDWMGKDLLGSVIYELHVGTFTPEGTLDSAISRLGHLAELGVDIVELMPLAAFPGRAGWGYDGVGLWAVHEAYGGPEALMRFVDAAHRAGIGVCLDVVYNHLGPSGNYLSVFGPYFTPAHHTPWGEAVNYDHDGSHQVRAFVIDSALRWLRDFHVDALRLDAIHEIKDDAAAADPPQAHVLAELSDAVAALSTELGRPLSLVAEADLNDVGVITPTDQEPPAATPSLGMTAQWADDVHHALHARITGEAQAYYADFAEPGAWIKAYSSAFLHNGIWSTFRDRVWGAPVPEDTDPRRFVVFGSNHDQIGNRAVGDRPSAGLDDAALAATAALVLLSPYTPMLFMGEEWGTRTPFQFFTDHEEEDLARSVSQGRAREFAGFGWDADEIPDPQDAGTVEASRLDWSELDKTEHAHMLSWYRALTALRRELGWSQRTAWPQIDEADDVVTVTYEDIVVVTNLSGRPRPAAELSDVLLSWAPVGSDPSCLPAGQTLVARR$","Malto-oligosyltrehalose trehalohydrolase","Cytoplasm, Extracellular","Malto-oligosyltrehalose trehalohydrolase(MTHase) (4-alpha-D-{(1->4)-alpha-D-glucano}trehalose","malto-oligosyltrehalose trehalohydrolase","malto-oligosyltrehalose trehalohydrolase","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR004193
Domain

Glycoside hydrolase, family 13, N-terminal
PF02922	$\"[6-81]T$	Isoamylase_N

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[119-237]T$	Alpha-amylase

InterPro
IPR012768
Family

Malto-oligosyltrehalose trehalohydrolase
TIGR02402	$\"[17-570]T$	trehalose_TreZ: malto-oligosyltrehalose tre

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[114-530]T$	no description

InterPro
IPR013783
Domain

Immunoglobulin-like fold
G3DSA:2.60.40.10	$\"[7-97]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[99-292]T$ $\"[401-530]T$	AMYLASE
PTHR10357:SF21	$\"[99-292]T$ $\"[401-530]T$	ALPHA-AMYLASE

","BeTs to 11 clades of COG0296COG name: 1,4-alpha-glucan branching enzymeFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0296 is ------yq-dr-bcefgh---j-i--Number of proteins in this genome belonging to this COG is 2","***** IPB004193 (Glycoside hydrolase, family 13, N-terminal) with a combined E-value of 2.7e-29. IPB004193B 113-128 IPB004193C 156-180 IPB004193D 191-205 IPB004193E 252-265***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 1.9e-18. IPB006589A 136-153 IPB006589B 177-205 IPB006589C 258-269***** IPB005323 (Bacterial pullanase-associated domain) with a combined E-value of 8.8e-09. IPB005323A 115-139 IPB005323B 194-206 IPB005323C 253-264***** IPB004185 (Glycoside hydrolase, family 13, N-terminal Ig-like domain) with a combined E-value of 1e-06. IPB004185B 125-158 IPB004185C 164-195","Residues 21-115 are 53% similar to a (BRANCHING ENZYME TRANSFERASE GLYCOGEN GLYCOSYLTRANSFERASE 14-ALPHA-GLUCAN BIOSYNTHESIS BE 14-ALPHA-D-GLUCAN:14-ALPHA-D-GLUCAN 6-GLUCOSYL-) protein domain (PD376916) which is seen in TREZ_ARTSQ.Residues 116-154 are 87% similar to a (HYDROLASE GLYCOSIDASE ALPHA-AMYLASE GLYCOGEN PRECURSOR METABOLISM ALPHA-GLUCOSIDASE FAMILY ENZYME SIGNAL) protein domain (PD001430) which is seen in TREZ_ARTRM.Residues 159-220 are 83% similar to a (TREHALOHYDROLASE HYDROLASE ENZYME BRANCHING ALPHA-AMYLASE TREHALOSE GLYCOSIDASE MALTOOLIGOSYLTREHALOSE MALTOOLIGOSYL MALTO-OLIGOSYLTREHALOSE) protein domain (PD872974) which is seen in Q9ADI5_STRCO.Residues 224-337 are 64% similar to a (BRANCHING ENZYME TRANSFERASE GLYCOGEN GLYCOSYLTRANSFERASE 14-ALPHA-GLUCAN BIOSYNTHESIS BE 14-ALPHA-D-GLUCAN:14-ALPHA-D-GLUCAN 6-GLUCOSYL-) protein domain (PD567709) which is seen in Q9ADI5_STRCO.Residues 339-531 are similar to a (TREHALOHYDROLASE HYDROLASE ALPHA-AMYLASE TREHALOSE GLYCOSIDASE MALTOOLIGOSYLTREHALOSE MALTOOLIGOSYL MALTO-OLIGOSYLTREHALOSE ALPHA-D-{1->4-ALPHA-D-GLUCANO}TREHALOSE ALPHA) protein domain (PD017361) which is seen in TREZ_ARTRM.","","-58% similar to PDB:1EHA CRYSTAL STRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS (E_value = 2.1E_103);-58% similar to PDB:1EH9 CRYSTAL STRUCTURE OF SULFOLOBUS SOLFATARICUS GLYCOSYLTREHALOSE TREHALOHYDROLASE (E_value = 2.7E_103);-52% similar to PDB:2BHU CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E_value = 1.2E_95);-52% similar to PDB:2BHY CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH TREHALOSE (E_value = 1.2E_95);-52% similar to PDB:2BHZ CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH MALTOSE (E_value = 1.2E_95);","Residues 6 to 81 (E_value = 0.0017) place ANA_0882 in the Isoamylase_N family which is described as Isoamylase N-terminal domain.Residues 119 to 476 (E_value = 2.9e-07) place ANA_0882 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.","","trehalohydrolase (MTHase) (4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase)(Maltooligosyl trehalose trehalohydrolase) (treZ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0883","950077","950673","597","5.13","-9.38","21187","GTGACTGTCAACGGTAGGCCGCGTCAGAATGAGGCAGGTGGCATCCCCGAACGATTCGAGGAAGCGCTCCTGTCCCTTCGCGACGCGCCCCGCCCCCGAGGGCTCCTCATGGAGGAGGTGCCCGCCCCCAAGAAGCTGGCCCCCTACTCCGCCGCCCTGAGCGCCGAAACCGTGGAGACAGTCGGCGCCACCCCCGTGGCCACCGGACGCTTCGTCGTCCTGCACGACCCCGACGGCCAGGAGGCCTGGGACGGGGACTTCCGCATCGTGGTGCAGGCGCGCGCCCGCATCGACGACGAGATCGGCATGGACCCCGTCTTCGAGTCCGCCGCCTGGAGCTGGCTCACCGACGGCCTGGAGGACTCCCGCGCCGGCTACCACTCACTGGTCGGAACCGTCACCAGGGTACTGTCCGAGACCTTCGGTGGGCTGACCCTCACCGACTCATGCGCCCACGCCGAGATCCGGGCGTCCTGGTCCCCCACGACCCCCCAGCTCGGCCCCCACCTCACCGCCTGGCACGAGCTCCTGCTGGTCGCCTCCGGCCATGAACCGGCCGCAGTCCACCCCCTCACTCTCGCCGGAGCCGGAAGGTGA","VTVNGRPRQNEAGGIPERFEEALLSLRDAPRPRGLLMEEVPAPKKLAPYSAALSAETVETVGATPVATGRFVVLHDPDGQEAWDGDFRIVVQARARIDDEIGMDPVFESAAWSWLTDGLEDSRAGYHSLVGTVTRVLSETFGGLTLTDSCAHAEIRASWSPTTPQLGPHLTAWHELLLVASGHEPAAVHPLTLAGAGR$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 37-187 are 57% similar to a (MB2699 CGL1900 U1764V ML1041 SCO6030) protein domain (PD036526) which is seen in O69860_STRCO.","","-38% similar to PDB:1TEX Mycobacterium smegmatis Stf0 Sulfotransferase with Trehalose (E_value = );-40% similar to PDB:1WX0 Crystal structure of transaldolase from Thermus thermophilus HB8 (E_value = );-65% similar to PDB:1ZYE Crystal strucutre analysis of Bovine Mitochondrial Peroxiredoxin III (E_value = );-48% similar to PDB:2ARY Catalytic domain of Human Calpain-1 (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0885","950670","952073","1404","9.26","7.86","50796","GTGACGCCCCGCCGCACCGGCGTGCCCCGCCCAACTGCTTCCTCGGCCGCGCCCCGCCCAACTGCTTCCTCGGCCGTGCCCCGCCCAACTGCTTCCTCGGCCGCGCCCCGCCCAACTGCTTCCTCGGCCGTGCCCCGCCCAGCCGTCCCCCCTGGCACAACAGATCACCCCATCAATCCGCACGACGTCGTCGACTACCCCCGTCCCAAGGACGGGCTCCCCGAGATCACCGCCACCCCCACCCAGCTGAACCGAGCCGCTCAGCTCCTGGCGGTCGGTCGGGGCCCCGTCGCCGTCGACGCCGAACGAGCCTCCGGCTTCCGCTACGGACAGGACGCCTACCTCATCCAGCTGCGCCGGGACGGCGTCGGCACCCTGCTCATCGATCCGGTCACCGCCGGGCCCCTGACCGAGCTGGCCACGGCCCTTGACGGACCCGAGTGGATCCTCCATGCCGCCGACCAGGACATCCCCTGCCTGACCGCACGCGGCCTGAAGGCCGCTTCCCTGTTCGACACCGAGCTGGCGGCCCGCCTCCTGGGCCGCCAGCACGTCGGGCTCGGCGCCGTCATCGAGGAGACCCTGGGCCTGCGCCTGGCCAAGGACCACGCGGCCGCGGACTGGTCCACCCGGCCCCTGCCCGCCTCCTGGCTCACCTACGCCGCCCTCGACGTCGAGCTGCTCATTGACCTGCGCGATGCTCTGGCCACCGAGCTCGAGGCGGCCGGCAAGGACCAGTGGGCTGCCCAGGAGTTCGAGCACGTACGCACCAAGCCGGCCAAACCCGCCAAGGTCGACCCATGGCGCAAGACCCCGCGAGCAGGAAGCTCCGTGCGATCCCCCCGCTCACTCGCCATCCTGCGCGAGCTGTGGAACTCGCGCGAGCAGCTGGCCGCAGAGCTCGACCGCACCCCCTCCAAGGTTCTCCCCCACCAGGCACTCGTCGCCGCTGCCGTCGCCCGCCCCCGGTCACGACGCAAGATGAGTGCCCTCAAGGAGTTCTCCTCCCGTCAGGCCCGCCAGAACCAGGAGCGCTGGTGGAGAGCCATCGAACGCGCCCTGGAGCTGCCCGACGACGAGCTTCCCCCCACCCGCGCACCACTGGCGCCCGGCGAGCTCCCCCATCCGCGCTCCTGGCAGCGCCACCACGCCGCGGCCGCCGAGCGGCTCACCGAGGTACGCGCGGCCATCAGGCGGCATGCTGAGGAGATCCGCGTACCCCAGGAGCTCCTTCTGACCCCGGAGTGCCAACGTCATCTGGCCTGGGACCTCGGCGAGGAGATCGAGGCCGGACGTACCAGCAGAATCACCGCTCAGGAGATCGGTGAGCGCCTGGCCGCCATGGGGGCCAGGCCCTGGCAGATCGAGCAGGCCTCCCCCGCCCTCGCCGCCGCACTGGGCTGA","VTPRRTGVPRPTASSAAPRPTASSAVPRPTASSAAPRPTASSAVPRPAVPPGTTDHPINPHDVVDYPRPKDGLPEITATPTQLNRAAQLLAVGRGPVAVDAERASGFRYGQDAYLIQLRRDGVGTLLIDPVTAGPLTELATALDGPEWILHAADQDIPCLTARGLKAASLFDTELAARLLGRQHVGLGAVIEETLGLRLAKDHAAADWSTRPLPASWLTYAALDVELLIDLRDALATELEAAGKDQWAAQEFEHVRTKPAKPAKVDPWRKTPRAGSSVRSPRSLAILRELWNSREQLAAELDRTPSKVLPHQALVAAAVARPRSRRKMSALKEFSSRQARQNQERWWRAIERALELPDDELPPTRAPLAPGELPHPRSWQRHHAAAAERLTEVRAAIRRHAEEIRVPQELLLTPECQRHLAWDLGEEIEAGRTSRITAQEIGERLAAMGARPWQIEQASPALAAALG$","3'-5' exonuclease","Cytoplasm, Periplasm","Ribonuclease D","3'-5' exonuclease","3'-5' exonuclease","","Yan H., Chen C.Y., Kobayashi R., Newport J. Replication focus-forming activity 1 and the Werner syndrome gene product. Nat. Genet. 1998. 19(4):375-378. PMID: 9697700","","","

InterPro
IPR002121
Domain

HRDC
PF00570	$\"[280-360]T$	HRDC
PS50967	$\"[280-360]T$	HRDC

InterPro
IPR002562
Domain

3'-5' exonuclease
PF01612	$\"[74-240]T$	3_5_exonuc
SM00474	$\"[74-240]T$	35EXOc

noIPR
unintegrated

unintegrated
PTHR12124	$\"[71-466]T$	POLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED
PTHR12124:SF3	$\"[71-466]T$	RIBONUCLEASE D

","BeTs to 9 clades of COG0349COG name: Ribonuclease DFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0349 is ------y---r--cefghs--jx---Number of proteins in this genome belonging to this COG is 1","***** IPB012588 (PMC2NT) with a combined E-value of 1.2e-09. IPB012588E 185-233 IPB012588F 290-314","Residues 76-148 are similar to a (RIBONUCLEASE D HYDROLASE ALANINE RICH D U1764U PROBABLE ML1040) protein domain (PD661847) which is seen in Q82KY1_STRAW.Residues 149-239 are similar to a (DNA POLYMERASE I RIBONUCLEASE D EXONUCLEASE TRANSFERASE HYDROLASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED) protein domain (PD254697) which is seen in Q82KY1_STRAW.Residues 243-337 are 54% similar to a (RIBONUCLEASE D HYDROLASE RNASE AUTOANTIGEN D TRNA NUCLEOLAR EXOSOME NUCLEASE) protein domain (PD037601) which is seen in Q8G5Q6_BIFLO.Residues 344-466 are 56% similar to a (RIBONUCLEASE D HYDROLASE ALANINE RICH D U1764U PROBABLE ML1040) protein domain (PD023226) which is seen in O69858_STRCO.","","-41% similar to PDB:1YT3 Crystal Structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing (E_value = 1.1E_13);","Residues 74 to 240 (E_value = 1.2e-31) place ANA_0885 in the 3_5_exonuc family which is described as 3'-5' exonuclease.Residues 280 to 360 (E_value = 2.9e-09) place ANA_0885 in the HRDC family which is described as HRDC domain.","","D ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0886","952928","952191","738","5.87","-4.70","27241","ATGCGCGATGGCGAGCTGGGCTCGATCCACTCCTGGGAGCTCGTGACCGCGGTGGACGGCCCCGGCACCCGGATGACGGTCTTCCTCAACGGATGCCCCCTGCGGTGCCAGTACTGCCACAATCCCGACACCTTCCTCATGAAGGACGGGGAACCGGTGGAGGCTGAGGAGCTTCTCCGCCGCATGCGCCGCTACCGGGGGGTGTTCCGCGCGTCCAAGGGCGGGATCACGCTGTCGGGCGGTGAGGTCCTCATGCAGCCGGCCTTCGCGGGCAAGCTCCTGGCCGGGGCCAAGAAGATGGGCATCCACACCTGCATCGACACCTCAGGATTCCTGGGTGCCAATGCCAGTGACGAGATGCTCGACAACATCGACCTGGTCCTGCTCGACGTCAAGAGCGGTGACGAGGAGACCTACAAGAAGGTGACGGGACGCTCCCTGGCCCCGACCATCACCTTCGGTGACCGTCTGGCAGCCAAAGGGATCGAGATCTGGGCCCGGTTCGTGCTGGTCCCGGACCTGACGGATGACCCTGAGAACGTCCACAACGTGGCCCGAATCATCGAGCGCTGGGGCTCGGTCAGCCGCGTCGAGGTGCTGCCCTTCCACCAGATGGGTACCGACAAGTGGGACGCTCTGGGACTGACGTACCAGCTTCGTGACACCAGGCCCCCGGAGCCGGAGCTGGTGGAGTCCACTCGCGCGATCTTCCGCTCCTACGGCTTCGAGGTTCACTGA","MRDGELGSIHSWELVTAVDGPGTRMTVFLNGCPLRCQYCHNPDTFLMKDGEPVEAEELLRRMRRYRGVFRASKGGITLSGGEVLMQPAFAGKLLAGAKKMGIHTCIDTSGFLGANASDEMLDNIDLVLLDVKSGDEETYKKVTGRSLAPTITFGDRLAAKGIEIWARFVLVPDLTDDPENVHNVARIIERWGSVSRVEVLPFHQMGTDKWDALGLTYQLRDTRPPEPELVESTRAIFRSYGFEVH$","Pyruvate formate-lyase activating enzyme","Cytoplasm","pyruvate formate-lyase 1 activating enzyme","radical SAM ","pyruvate formate-lyase activating enzyme","","Sofia H.J., Chen G., Hetzler B.G., Reyes-Spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 2001. 29(5):1097-1106. PMID: 11222759Hanzelmann P., Schindelin H. Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proc. Natl. Acad. Sci. U.S.A. 2004. 101(35):12870-12875. PMID: 15317939","","","

InterPro
IPR001989
Domain

Radical-activating enzyme
PS01087	$\"[20-41]T$	RADICAL_ACTIVATING

InterPro
IPR007197
Domain

Radical SAM
PF04055	$\"[26-185]T$	Radical_SAM

InterPro
IPR012838
Family

Pyruvate formate-lyase activating
TIGR02493	$\"[8-240]T$	PFLA: pyruvate formate-lyase 1-activating e

","BeTs to 12 clades of COG1180COG name: Pyruvate-formate lyase-activating enzymeFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1180 is a-mpkz-qv-rl--efgh--------Number of proteins in this genome belonging to this COG is 2","***** IPB001989 (Radical-activating enzyme) with a combined E-value of 3.4e-28. IPB001989A 18-46 IPB001989B 75-93 IPB001989C 127-132","Residues 101-203 are 80% similar to a (PYRUVATE ENZYME LYASE ACTIVATING FORMATE-LYASE 4FE-4S IRON-SULFUR OXIDOREDUCTASE METAL-BINDING IRON) protein domain (PD266006) which is seen in Q6NJL9_CORDI.Residues 194-239 are 65% similar to a (PYRUVATE ENZYME LYASE ACTIVATING FORMATE-LYASE OXIDOREDUCTASE FORMATE 4FE-4S IRON-SULFUR ACETYLTRANSFERASE) protein domain (PD869438) which is seen in Q7NY62_CHRVO.","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 185 (E_value = 1.6e-25) place ANA_0886 in the Radical_SAM family which is described as Radical SAM superfamily.","","formate-lyase 1 activating enzyme (act)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0887","953449","953090","360","9.52","4.37","13250","ATGCCGGCTTCGTCCCCGACGACTGCGCCGAGATCTGATCGAGCCGCTCAATCCGGCCGATCACACCGCAGCAATTTCCACACATCGATCACATCACCTCAGAAAGGGGCCACCATGGCCACGTACGAAGAGCGCCTCGCCTCCATGAAGGCACAGCGTCAGGACAACGGCGGCGTCAAGGGCCTGTACCACGCCAACATCAACGTCCTGGACCGCAACACCCTCGAGGACGCGATGGAGCACCCGGAGAACTACCCGAACCTCACGGTTCGCGTCTCCGGCTACGCCGTCAACTTCGTCAAGCTGACTCGCGAGCAGCAGCTTGACGTCCTCCACCGCACCTTCCACTCCCAGGCCTGA","MPASSPTTAPRSDRAAQSGRSHRSNFHTSITSPQKGATMATYEERLASMKAQRQDNGGVKGLYHANINVLDRNTLEDAMEHPENYPNLTVRVSGYAVNFVKLTREQQLDVLHRTFHSQA$","Formate acetyltransferase","Cytoplasm, Extracellular","formate acetyltransferase","formate acetyltransferase ","formate C-acetyltransferase glycine radical","","Wagner A.F., Frey M., Neugebauer F.A., Schafer W., Knappe J. The free radical in pyruvate formate-lyase is located on glycine-734. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(3):996-1000. PMID: 1310545Sun X., Harder J., Krook M., Jornvall H., Sjoberg B.M., Reichard P. A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(2):577-581. PMID: 8421692","","","

InterPro
IPR001150
Domain

Formate C-acetyltransferase glycine radical
PF01228	$\"[4-100]T$	Gly_radical
PS51149	$\"[1-119]T$	GLY_RADICAL_2
PS00850	$\"[89-97]?$	GLY_RADICAL_1

noIPR
unintegrated

unintegrated
G3DSA:3.20.70.20	$\"[49-119]T$	no description

","BeTs to 4 clades of COG1882COG name: Pyruvate-formate lyaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1882 is a-m--------l--e-gh--------Number of proteins in this genome belonging to this COG is 2","***** IPB004184 (Pyruvate formate-lyase, PFL) with a combined E-value of 2.4e-19. IPB004184C 64-97***** IPB001150 (Formate C-acetyltransferase glycine radical) with a combined E-value of 1e-14. IPB001150 80-103","Residues 61-115 are similar to a (TRANSFERASE FORMATE ACETYLTRANSFERASE PYRUVATE ACYLTRANSFERASE LYASE FORMATE-LYASE RADICAL ORGANIC PROBABLE) protein domain (PD004056) which is seen in Q8G5Q3_BIFLO.","","-77% similar to PDB:1CM5 CRYSTAL STRUCTURE OF C418A,C419A MUTANT OF PFL FROM E.COLI (E_value = 4.7E_15);-77% similar to PDB:1H16 PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH PYRUVATE AND COA (E_value = 4.7E_15);-77% similar to PDB:1H17 PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH COA AND THE SUBSTRATE ANALOG OXAMATE (E_value = 4.7E_15);-77% similar to PDB:1H18 PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH PYRUVATE (E_value = 4.7E_15);-77% similar to PDB:1MZO Crystal structure of pyruvate formate-lyase with pyruvate (E_value = 4.7E_15);","Residues 4 to 100 (E_value = 5.3e-08) place ANA_0887 in the Gly_radical family which is described as Glycine radical.","","acetyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0888","955526","953412","2115","5.02","-29.95","78314","ATGACCACTGAGGTCACAACATCTGCCACCACGGCGAGCGGCAATGACGCCTGGGAGGGCTTCGTTACCGGACCGTGGACCGAGGACATTGACGTCCGCGACTTCATCCAGCGCAACTACACCCCCTACGACGGCGACGCCTCGTTCCTCGCCGACGCCACGGACAAGACCCTGCGTCTGTGGGACACCCTGGAGAAGAACTACCTCTCTGAGGAGCGCAAGGTCCGCATCCTCGACGTCGACACCCACACCCCCGCCGACATCGACGCATTCCCGGCCGGCTACATCAGCGAGGACGACGACGTCATCGTTGGTCTGCAGACGGATTCCCCGCTGCGTCGCGCCATGATGCCCAACGGTGGCTGGCGCATGGTGGAGACCGCCATCAAGGAGGCGGGCAAGGAGGTCGACCCCGAGGTCAAGAAGATCTTCACCCGCTACCGCAAGACCCACAACGACGCGGTCTTCGACATCTACACCCCGCGCATCCGCGCGGCGCGCTCGAGCCACATCATCACCGGTCTGCCCGACGCCTACGGCCGCGGCCGCATCATCGGTGACTACCGCCGCGTGGCGCTCTACGGCGTCGACTTCCTCATCGAGCAGAAGCAGAAGGCCAAGGACGCCGTGGCGGACAAGCCCTTCTCCGAGCACTGGGCCCGCTACCGCGAGGAGCACTCCGAGCAGATCAAGGCGCTCAAGAAGCTCAAGGTCATGGCTCAGACCTACGGCTACGACATCTCCGGCCCGGCCAAGAACGCCCACGAGGCGGTCCAGTGGACCTACTTCGCCTACCTGGCCTCCGTGAAGTCCCAGGACGGCGCCGCCATGAGCATCGGTCGGCTCTCCGGCTTCCTGGACATCTACTTCGAGCGGGACCTGCGCAACGGGGTCATCGACGAGACCCGCGCCCAGGAGCTCATCGACAACATCGTCATGAAGCTGCGCATCACCCGCTTCCTGCGCACCATCGACTACGACCAGATCTTCTCCGGCGACCCCTACTGGGCCACCTGGTCCGACGCCGGTTTCGGTGAGGACGGTCGCGCCCTGGTCACCAAGACCTCCTTCCGTCTGCTGCAGACCCTGCGCAACCTCGGTCCTGCCCCGGAGCCGAACATCACGATCTTCTGGGACGAGAACCTGCCGCAGGGCTACAAGGACTTCTGCGCCCTCATCTCGATCACCACCTCCTCCATCCAGTACGAGGCCGACGAGCAGATCCGTGAGCACTGGGGCGACGACGCCGCGATCGCCTGCTGCGTGTCCCCGATGCGCGTGGGCAAGCAGATGCAGTTCTTCGGTGCCCGCGTCAACTCCGCCAAGGCCCTGCTCTACGCCATCAACGGTGGTCGTGACGAGATGACCGGCAAGCAGGTCGTCACCGGCCTGCCCGGCATCGAGGGCGACGGCCCCCTCGACTTCGACGAGGTCTGGGACAAGTACGAGAAGATGCTCGACTGGGTGGTGGCCACCTACGTCGAGGCCCTCAACATCATCCACTACTGCCACGACCGCTACGCCTACGAGTCCATCGAGATGGCGCTGCACGACTCCGACATCGTGCGCACCATGGGTTGCGGCATCGCCGGTCTGTCGATCGTGGCCGACTCGCTGGCGGCCATCAAGTACGCCAAGGTCACCCCGGTTCGCGACGAGACCGGCCTGGTGGTCGACTACGTCACCGAGGGCGACTTCCCGATCTACGGCAACGACGACGACCGCGCCGACGACATCGCCGCCACCGTGGTCCACACGATCATGTCCAAGATCAAGGCCCAGCCCTTCTACCGGGACGCCATCCCGACCCAGTCGGTGCTGACGATCACCTCCAACGTGGTCTACGGCAAGGCAACCGGCTCCTTCCCCTCGGGGCACCAGAAGGGCACCCCCTTCTCTCCCGGAGCCAACCCGGAGAACGGGATGGACACCCACGGCATGGTCGCCTCGATGCTCAGTGTCGGCAAGCTCGACTACAACGACGCCCTCGACGGCATCTCGCTGACCAACACGATCACCCCGCAGGGACTGGGTCGCACGCTCGACGAGCGCGTCGCCAACCTCGTGGGCATTCTCGATGCCGGCTTCGTCCCCGACGACTGCGCCGAGATCTGA","MTTEVTTSATTASGNDAWEGFVTGPWTEDIDVRDFIQRNYTPYDGDASFLADATDKTLRLWDTLEKNYLSEERKVRILDVDTHTPADIDAFPAGYISEDDDVIVGLQTDSPLRRAMMPNGGWRMVETAIKEAGKEVDPEVKKIFTRYRKTHNDAVFDIYTPRIRAARSSHIITGLPDAYGRGRIIGDYRRVALYGVDFLIEQKQKAKDAVADKPFSEHWARYREEHSEQIKALKKLKVMAQTYGYDISGPAKNAHEAVQWTYFAYLASVKSQDGAAMSIGRLSGFLDIYFERDLRNGVIDETRAQELIDNIVMKLRITRFLRTIDYDQIFSGDPYWATWSDAGFGEDGRALVTKTSFRLLQTLRNLGPAPEPNITIFWDENLPQGYKDFCALISITTSSIQYEADEQIREHWGDDAAIACCVSPMRVGKQMQFFGARVNSAKALLYAINGGRDEMTGKQVVTGLPGIEGDGPLDFDEVWDKYEKMLDWVVATYVEALNIIHYCHDRYAYESIEMALHDSDIVRTMGCGIAGLSIVADSLAAIKYAKVTPVRDETGLVVDYVTEGDFPIYGNDDDRADDIAATVVHTIMSKIKAQPFYRDAIPTQSVLTITSNVVYGKATGSFPSGHQKGTPFSPGANPENGMDTHGMVASMLSVGKLDYNDALDGISLTNTITPQGLGRTLDERVANLVGILDAGFVPDDCAEI$","Formate acetyltransferase","Cytoplasm","formate acetyltransferase","formate acetyltransferase ","formate acetyltransferase","","Wagner A.F., Frey M., Neugebauer F.A., Schafer W., Knappe J. The free radical in pyruvate formate-lyase is located on glycine-734. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(3):996-1000. PMID: 1310545Sun X., Harder J., Krook M., Jornvall H., Sjoberg B.M., Reichard P. A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(2):577-581. PMID: 8421692","","","

InterPro
IPR000209
Domain

Peptidase S8 and S53, subtilisin, kexin, sedolisin
PS00136	$\"[689-700]?$	SUBTILASE_ASP

InterPro
IPR001150
Domain

Formate C-acetyltransferase glycine radical
PF01228	$\"[632-693]T$	Gly_radical
PS51149	$\"[634-704]T$	GLY_RADICAL_2

InterPro
IPR004184
Domain

Pyruvate formate-lyase, PFL
PF02901	$\"[17-616]T$	PFL

InterPro
IPR005949
Family

Formate acetyltransferase
PIRSF000379	$\"[15-702]T$	Formate acetyltransferase
TIGR01255	$\"[17-704]T$	pyr_form_ly_1: formate acetyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.20.70.20	$\"[8-697]T$	no description

","BeTs to 5 clades of COG1882COG name: Pyruvate-formate lyaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1882 is a-m--------l--e-gh--------Number of proteins in this genome belonging to this COG is 2","***** IPB004184 (Pyruvate formate-lyase, PFL) with a combined E-value of 6.6e-23. IPB004184A 567-577 IPB004184B 634-679","Residues 17-100 are 78% similar to a (TRANSFERASE FORMATE ACETYLTRANSFERASE PYRUVATE ACYLTRANSFERASE FORMATE-LYASE LYASE ORGANIC RADICAL GLUCOSE) protein domain (PDA1D7F2) which is seen in Q8G5Q3_BIFLO.Residues 121-200 are 88% similar to a (TRANSFERASE FORMATE ACETYLTRANSFERASE PYRUVATE ACYLTRANSFERASE FORMATE-LYASE LYASE ORGANIC RADICAL GLUCOSE) protein domain (PD008843) which is seen in Q8G5Q3_BIFLO.Residues 223-391 are 78% similar to a (TRANSFERASE FORMATE ACETYLTRANSFERASE PYRUVATE ACYLTRANSFERASE LYASE FORMATE-LYASE ORGANIC RADICAL PROBABLE) protein domain (PD005492) which is seen in Q9KQY1_VIBCH.Residues 393-678 are 79% similar to a (TRANSFERASE FORMATE ACETYLTRANSFERASE PYRUVATE ACYLTRANSFERASE LYASE FORMATE-LYASE ORGANIC RADICAL PROBABLE) protein domain (PD552594) which is seen in Q8G5Q3_BIFLO.","","-41% similar to PDB:2F3O Crystal Structure of a glycyl radical enzyme from Archaeoglobus fulgidus (E_value = 1.9E_23);-39% similar to PDB:1R8W Native structure of the B12-independent glycerol dehydratase from clostridium butyricum (E_value = 1.5E_20);","Residues 17 to 616 (E_value = 3.9e-289) place ANA_0888 in the PFL family which is described as Pyruvate formate lyase.Residues 632 to 693 (E_value = 3.8e-11) place ANA_0888 in the Gly_radical family which is described as Glycine radical.","","acetyltransferase (pfl)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0889","957973","955913","2061","5.89","-19.01","73145","GTGCCAGCAGCTGCCGAGCGCCCGGCAGGGCCCGCCGGACAGACCGGCAAGGCGCTCCTGCCCTGCGTGCGCAAGCCCGCCGACCTCGATCGGCTCACCAGCGAGCAGCTGGTGACGCTCGCCTCGGAGATCCGCCAGCATCTTGTCGCCTCAGTGGCGCGCACCGGCGGCCACCTCGGCCCCAACCTTGGGGTCGTCGAGCTGACGATCGCGCTGCACCGCACCTTCCGCTCCCCGCGGGACACCATCGTGTTCGACACCGGCCACCAGGCCTACGTCCACAAGCTGCTCACCGGTCGTCAGGACTTCACCCATCTGCGCGAGCGCGGCGGCCTGTCCGGCTACCCCTCACGGGCCGAGTCCGTCCACGACGTCGTGGAGAACTCCCACGCCTCCACCTCCCTGTCCTGGGCCGACGGCATCGCCCGGGCCAACCACCTGCAGGGCCACGACGAGCGCCATGTCGTCGCCGTCATCGGGGACGGCGCCATGACCGGGGGAATGGCCTGGGAGGCCCTGGACAACATCGCCGACTCCTCGGACCGCCACCTGGTCATCGTCGTCAACGACAACGGCCGCTCCTACGCCCCCACCATCGGGGGACTGGCCCACCACCTCGACGCACTGCGCACCAATCCCGGCTACGAGCGTGTCCTGTCCGGGGTCAAGCGCACGCTCCTGTCGCAGGGCGTCCCCGGCCGGGCCGCCTTCGACGCCCTGCACGGACTCAAACGGGGGCTCAAGGACGTCCTGGTTCCCTCGGCCTTCTTCGAGGATCTGGGGATCAAGTACACCGGACCGGTCGACGGCCACGACATCACGGCCGTCGAGTTCGCCCTCACTCGCGCCCGCGAGTATGCCGAGCCGGTCATCGTCCACGTCATCACCGAGAAGGGACGGGGCTACACCCCGGCCGAGGAACACGTCCCCGACCGCTTCCACGCGGTGGGCCAGATTCATCCCGAGACCGGCTTGCCGGTGGTGGCCGAGCGCTTCGGCTGGACCGCCGTCTTCGCCGAGGAGATCGTCTCCCTGGCCCGCGGAGATGAACGGATCGTCGGGGTCACCGCCGCCATGCAGGCCCCGGTGGGCCTCCAGCCCCTGGCCGATGAGATGCCGACGCGGGTCATCGACGTCGGCATCGCCGAGCAGCACGCGCTGACCTTCTCCGCCGGCCTCGCCTTCGCCGGCATGCACCCGGTGGTCGCCCTCTACGCCACCTTCCTCAACCGCGCCTTCGACCAGGTGCTCATGGATGTCGCCCTGCACCGGGCCGGAGTGACGATCGTCCTGGACCGGGCCGGAATCACGGGAACTGACGGGGCCAGCCACAACGGCATGTGGGACATGGCGCTGTTGGCGCACGTTCCTGGTCTGCACCTGGCGGCCCCCCGCGACGAGGCAACGCTGCGCGAGAGCCTGCGCACAGCCGTGAGCACTGACGATTCCCCCACCGTCGTGCGCTACCCCAAGGGCGCGCTGCCCGAGCCCCTGACCGCGTTGCGACGCCTCGGTCCGGGGGCGGAAGAAGCGCAGTGCGGCGAGGAGCCGGTGCTCAAGGAGACGCCGCCGCCCGCGAGCTCCTTCGACGTCGTCGATGTCCTGCTCGAGAACCGCTCGCCGGCTGGCGGCGCGCGGATCCTGCTGGTGGGTGTGGGTGCCATGGCCACCGAGGCATACGAGGCCGGCAGGCTCCTTGAGCAGGAGGAGCGCACCATCACCGTGGTGCATCCGCACTGGGTGATTCCGGCCCCGGCTCCTCTCGTGGCGGCCGCCGCAGATGTTGATGTCGTCGTCGTGGTCGAGGACGGGCTGAGCGACGGCGGTATCGGTTCCCAGCTGCGCGACGCGGTCGAGGAGTACCGGGCCGATCACAGTGGTACCGGGGGCTGGCCGGTCTTCCGTCGCATCGGCGTGCCGCGACAGTTCGTCGATACGGCCACCCGCGCCGAGCTGATGGAGGACTTCGGTATGCGCGCGGCCGATATCGCCCGGGCGGCCCGCAGAGCCGCCGACAGCGTCTCTGGCACCTGCACCGACCAGGACCTTAGGGCCGAGTAG","VPAAAERPAGPAGQTGKALLPCVRKPADLDRLTSEQLVTLASEIRQHLVASVARTGGHLGPNLGVVELTIALHRTFRSPRDTIVFDTGHQAYVHKLLTGRQDFTHLRERGGLSGYPSRAESVHDVVENSHASTSLSWADGIARANHLQGHDERHVVAVIGDGAMTGGMAWEALDNIADSSDRHLVIVVNDNGRSYAPTIGGLAHHLDALRTNPGYERVLSGVKRTLLSQGVPGRAAFDALHGLKRGLKDVLVPSAFFEDLGIKYTGPVDGHDITAVEFALTRAREYAEPVIVHVITEKGRGYTPAEEHVPDRFHAVGQIHPETGLPVVAERFGWTAVFAEEIVSLARGDERIVGVTAAMQAPVGLQPLADEMPTRVIDVGIAEQHALTFSAGLAFAGMHPVVALYATFLNRAFDQVLMDVALHRAGVTIVLDRAGITGTDGASHNGMWDMALLAHVPGLHLAAPRDEATLRESLRTAVSTDDSPTVVRYPKGALPEPLTALRRLGPGAEEAQCGEEPVLKETPPPASSFDVVDVLLENRSPAGGARILLVGVGAMATEAYEAGRLLEQEERTITVVHPHWVIPAPAPLVAAAADVDVVVVVEDGLSDGGIGSQLRDAVEEYRADHSGTGGWPVFRRIGVPRQFVDTATRAELMEDFGMRAADIARAARRAADSVSGTCTDQDLRAE$","1-deoxy-D-xylulose-5-phosphate synthase","Cytoplasm","1-deoxy-D-xylulose-5-phosphate synthase","putative 1-deoxy-D-xylulose 5-phosphate synthase ","deoxyxylulose-5-phosphate synthase","","Nikkola M., Lindqvist Y., Schneider G. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. J. Mol. Biol. 1994. 238(3):387-404. PMID: 8176731Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y., Jordan F., Guest J.R., Furey W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry 2002. 41(16):5213-5221. PMID: 11955070Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 1999. 6(8):785-792. PMID: 10426958Chabriere E., Vernede X., Guigliarelli B., Charon M.H., Hatchikian E.C., Fontecilla-Camps J.C. Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase. Science 2001. 294(5551):2559-2563. PMID: 11752578","","","

InterPro
IPR005475
Domain

Transketolase, central region
PF02779	$\"[330-497]T$	Transket_pyr
PS00802	$\"[438-454]T$	TRANSKETOLASE_2

InterPro
IPR005476
Domain

Transketolase, C-terminal
PF02780	$\"[543-663]T$	Transketolase_C

InterPro
IPR005477
Family

Deoxyxylulose-5-phosphate synthase
PIRSF005462	$\"[17-677]T$	Deoxyxylulose-5-phosphate synthase
TIGR00204	$\"[20-672]T$	dxs: 1-deoxy-D-xylulose-5-phosphate synthas

InterPro
IPR009014
Domain

Transketolase, C-terminal-like
G3DSA:3.40.50.920	$\"[535-673]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.970	$\"[316-495]T$	no description
PTHR11624	$\"[360-495]T$ $\"[513-684]T$	DEHYDROGENASE RELATED
PTHR11624:SF20	$\"[360-495]T$ $\"[513-684]T$	1-DEOXYXYLULOSE-5-PHOSPHATE SYNTHASE

","BeTs to 16 clades of COG1154COG name: Deoxyxylulose-5-phosphate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism] Functional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1154 is -------qvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB005475 (Transketolase, central region) with a combined E-value of 2.6e-22. IPB005475A 56-73 IPB005475B 405-419 IPB005475C 437-466***** IPB005476 (Transketolase, C terminal) with a combined E-value of 4.2e-19. IPB005476A 375-400 IPB005476B 438-466","Residues 23-76 are 81% similar to a (SYNTHASE BIOSYNTHESIS THIAMINE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE-5-PHOSPHATE TRANSFERASE FLAVOPROTEIN DXP DXPS ISOPRENE) protein domain (PD957443) which is seen in DXS2_STRAW.Residues 41-191 are 42% similar to a (TRANSKETOLASE TRANSFERASE THIAMINE PYROPHOSPHATE TK CALCIUM-BINDING N-TERMINAL TRANSKETOLASE SUBUNIT ISOZYME) protein domain (PD308336) which is seen in Q8E202_STRA5.Residues 78-124 are 91% similar to a (SYNTHASE BIOSYNTHESIS THIAMINE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE-5-PHOSPHATE TRANSFERASE DXP DXPS FLAVOPROTEIN ISOPRENE) protein domain (PD000580) which is seen in Q6AFD5_BBBBB.Residues 156-191 are 94% similar to a (SYNTHASE BIOSYNTHESIS THIAMINE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE-5-PHOSPHATE TRANSFERASE DXP DXPS FLAVOPROTEIN ISOPRENE) protein domain (PD381993) which is seen in DXS1_KITGR.Residues 193-253 are 67% similar to a (SYNTHASE THIAMINE BIOSYNTHESIS PYROPHOSPHATE FLAVOPROTEIN DXP 1-DEOXY-D-XYLULOSE-5-PHOSPHATE DXPS ISOPRENE TRANSFERASE) protein domain (PD966362) which is seen in DXS2_STRCO.Residues 257-353 are similar to a (SYNTHASE BIOSYNTHESIS THIAMINE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE-5-PHOSPHATE TRANSFERASE DXP DXPS FLAVOPROTEIN ISOPRENE) protein domain (PD335294) which is seen in DXS2_STRAW.Residues 338-496 are 49% similar to a (C-TERMINAL SUBUNIT TRANSKETOLASE) protein domain (PDA191F6) which is seen in Q8KE86_CHLTE.Residues 355-421 are 61% similar to a (SYNTHASE 1-DEOXYXYLULOSE-5-PHOSPHATE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE LYASE 4.2.1.- DXS PLASMID DEHYDROGENASE PROBABLE) protein domain (PDA0Q7J3) which is seen in Q74L20_LACJO.Residues 390-467 are 69% similar to a (TRANSKETOLASE PYRUVATE TRANSFERASE DEHYDROGENASE COMPONENT THIAMINE E1 PYROPHOSPHATE CALCIUM-BINDING OXIDOREDUCTASE) protein domain (PD443507) which is seen in Q6F7N5_ACIAD.Residues 421-471 are 82% similar to a (SYNTHASE THIAMINE BIOSYNTHESIS 5-PHOSPHATE 1-DEOXY-D-XYLULOSE-5-PHOSPHATE TRANSFERASE DXP DXPS PYROPHOSPHATE FLAVOPROTEIN) protein domain (PD151765) which is seen in DXS1_STRAW.","","-59% similar to PDB:2O1S 1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Escherichia coli (E_value = 5.2E_98);-59% similar to PDB:2O1X 1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Deinococcus radiodurans (E_value = 2.6E_97);","Residues 330 to 497 (E_value = 4.6e-50) place ANA_0889 in the Transket_pyr family which is described as Transketolase, pyrimidine binding domain.Residues 543 to 663 (E_value = 3.4e-06) place ANA_0889 in the Transketolase_C family which is described as Transketolase, C-terminal domain.","","synthase (dxs)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0890","958300","960324","2025","5.40","-23.48","73074","ATGAGCACCACAGCCCCTTTCGGTACCTGGCCCTCGCCCATCACTCCAGGCACCATCACGACCCGGACGGTCCTGCTCTCTCAGGTCCGTGTGGACGGCGCAGACACCTACTGGGTGGAGCAGCGCGCCTCACAGGCGGGCCGCAACGTACTGCTCCGCCGCAACGGCGACGGCCAGATCGGCGAGGTGCTTCCGCTGACACCCGCCGACGAGCTGGTCGATGTGCGCACCCGGGTGCACGAGTACGGAGGACGGGCCTACGCCGTCGACAGCGGGATCATCGTGGTCTCGCACGCCGGGGACGGGCGCCTCTACCGGTACGACGTGGCGCACCGCATGCGAGGCCTGGTCCCGCTCACGATCTACGGGGACGTGCGACACGGCGACCTGGAGATCGACACGGGCCGGGGCCTGGTCTACGCCGTCCGCGAGGACCACCGAGGCGGCGGCGAGGCCGTGAACACCCTGGTCGCAATTCCCCTGGACGGCTCGGCCGCCCGCGATGACTCCCGCGTGCGCACACTGGTGTCGGGCACGGACTTCGTGGTCGCCCCGACACTGTCCCCCGACGGCGAGCACCTGGCCTGGATCACCTGGGACCACCCGGGGATGCCGTGGGACAACGCCAGCCTGCACGTGGGGGACCTCGGCCCGGACGGGACTCTTGGCGAGCAGACGCTGGTGGACGGCGGCGACGGGCACTCGGTCTCCGAGCCCCGCTGGACCGAGGAGTGCGAGCTCGTGCACGGCTCCAACGCCTCGGGCTTCTGGAACCTCTACCGCACTGAGGGCTTCCCGGTACGCGGCACCAACCGCACCGGCTGGTCGGAGAAGCTGCGCACCCGCCCCCTGCACCCGGCCGAGGCCACCTTCACCACCCCGGCCTGGCAGCTGGGGCCGCACTCCTTCGACGTGCTCGACTCCGAGCACATCATCACCTCCTGGGCCCGCGATGCGGTCTCGCACCTGGGGACCATCAAGCTCGCCAACGGGGAGCTCGAGGAGTGGAACGTGGGGTGGCAGCCGATCGGCAACGTCGCCTCCAACACCGGGCGCGTCGTCATGCTGGCCTCCAACGAGATGTCGATGCCCAGCATCGTGGAGGTCAAGAACGGCACGGTGAAGGTGCTGCGCGGCTCGGGCGAGTTCGTGCCCGAGGGCACCGGGGTGTCCTTCCCCGAGCCGGTCTCCTGGCCCACCAGTGACGGCGCCACCGCCCACGGCTTCTACTACCCGCCGACCTCGGCCTCTCACACTGGCCCCGATGGCGAGCTGGCGCCGCTGATCGTCAACGTCCACGGCGGCCCGACGGCCACGGCGGTCCCCGGCTACGACCTGCGCATCCAGTACTGGACCAGCCGGGGCTTCGGCTACCTGGACGTCAACTACCGCGGCTCCATGGGTTACGGGACCGGCTACCGCAAGGCCCTGGAGGGCAAGTGGGGCATCTACGACGCCGACGACTGCGTCAACGGGGCCCAGCACCTGGTCGACGCCGGGCTGGTGGACCCGCGCCGTATCGCGATCCGCGGAGGTTCGGCCGGGGGCTTCACGGTGCTGTCGGCCATCTCCCGATCCTCCGTGTTCACCGCGGCCAGCTCCTGCTTCGGCGTGACCGATCTCAAGAGGCTGGTACGCACCACCCACAAGTTCGAGTCGCACTACATCGGTCAGCTCATGGGCACGCAGGACATCGACGACCCGGTGCTCGATGAGCGCAGCCCCATCAACCACATCGAGGACATCAACGTCCCGCTGCTGCTCATCCAGGGCTCAGAGGATCCGATCGTCCCGGCAGAGCAGGCCACCGCCATGTACCAGGCCCTCAAGGAGGCCGGCGCCCCAGTGGCCCTCGAGGTCTTCCAGGGCGAAGGCCACGGCTTCCGTCTGGCGGCGAACATCCGGCGGCGTTACGAGGCCGAGCTGAGCTTCTACCGCCAGGTGTGGAGGATCGGCGCCGCTTCCTCCGAGGCCGAGGGGCAGGACGAGGAGACCTTTACGGTCAAGGTGGAGAACCTGCACTGA","MSTTAPFGTWPSPITPGTITTRTVLLSQVRVDGADTYWVEQRASQAGRNVLLRRNGDGQIGEVLPLTPADELVDVRTRVHEYGGRAYAVDSGIIVVSHAGDGRLYRYDVAHRMRGLVPLTIYGDVRHGDLEIDTGRGLVYAVREDHRGGGEAVNTLVAIPLDGSAARDDSRVRTLVSGTDFVVAPTLSPDGEHLAWITWDHPGMPWDNASLHVGDLGPDGTLGEQTLVDGGDGHSVSEPRWTEECELVHGSNASGFWNLYRTEGFPVRGTNRTGWSEKLRTRPLHPAEATFTTPAWQLGPHSFDVLDSEHIITSWARDAVSHLGTIKLANGELEEWNVGWQPIGNVASNTGRVVMLASNEMSMPSIVEVKNGTVKVLRGSGEFVPEGTGVSFPEPVSWPTSDGATAHGFYYPPTSASHTGPDGELAPLIVNVHGGPTATAVPGYDLRIQYWTSRGFGYLDVNYRGSMGYGTGYRKALEGKWGIYDADDCVNGAQHLVDAGLVDPRRIAIRGGSAGGFTVLSAISRSSVFTAASSCFGVTDLKRLVRTTHKFESHYIGQLMGTQDIDDPVLDERSPINHIEDINVPLLLIQGSEDPIVPAEQATAMYQALKEAGAPVALEVFQGEGHGFRLAANIRRRYEAELSFYRQVWRIGAASSEAEGQDEETFTVKVENLH$","Peptidase S9, prolyl oligopeptidase active site domain protein","Cytoplasm, Membrane, Extracellular","prolyl oligopeptidase family protein","peptidase S9; prolyl oligopeptidase active site region","peptidase S9, prolyl oligopeptidase active site domain protein","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290","","","

InterPro
IPR000568
Family

ATPase, F0 complex, subunit A
PS00449	$\"[625-634]?$	ATPASE_A

InterPro
IPR001375
Domain

Peptidase S9, prolyl oligopeptidase active site region
PF00326	$\"[442-652]T$	Peptidase_S9

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[393-652]T$	no description
PTHR11731	$\"[157-649]T$	PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED
PTHR11731:SF7	$\"[157-649]T$	ACYLAMINO-ACID-RELEASING ENZYME

","BeTs to 10 clades of COG1506COG name: Dipeptidyl aminopeptidases/acylaminoacyl-peptidasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1506 is -o-pkzy-vd--bc-f-hs--j----Number of proteins in this genome belonging to this COG is 1","***** IPB002471 (Prolyl endopeptidase, serine active site) with a combined E-value of 9.1e-13. IPB002471C 488-519 IPB002471D 590-609***** IPB002470 (Prolyl oligopeptidase serine protease (S9A) signature) with a combined E-value of 9.8e-13. IPB002470A 427-445 IPB002470B 453-477 IPB002470F 583-605***** IPB002469 (Dipeptidylpeptidase IV (CD26), N-terminal) with a combined E-value of 1.9e-10. IPB002469H 469-523 IPB002469J 586-605","Residues 29-324 are 51% similar to a (AMINOPEPTIDASE HYDROLASE FAMILY PROLYL OLIGOPEPTIDASE ACYL-PEPTIDE C PEPTIDASE ENZYME HYDROLASE-LIKE) protein domain (PD042129) which is seen in Q7NKK7_GLOVI.Residues 407-629 are 57% similar to a (DIPEPTIDYL PEPTIDASE HYDROLASE IV AMINOPEPTIDASE PROLYL ENZYME ACYLAMINO-ACID-RELEASING OLIGOPEPTIDASE FAMILY) protein domain (PD435174) which is seen in Q88A85_PSESM.Residues 416-602 are 46% similar to a (PROTEASE PROLYL HYDROLASE II OLIGOPEPTIDASE ENDOPEPTIDASE SERINE FAMILY B AMINOPEPTIDASE) protein domain (PD003048) which is seen in Q9HS46_HALN1.Residues 427-613 are 49% similar to a (GLL3871) protein domain (PDA1A493) which is seen in Q7NEK8_GLOVI.Residues 428-546 are 50% similar to a (HYDROLASE SPLICING F44B9.1 CHROMOSOME ALTERNATIVE III) protein domain (PD718322) which is seen in YL31_CAEEL.Residues 429-518 are 66% similar to a (HYDROLASE ENZYME ACYLAMINO-ACID-RELEASING LONG FAMILY AMINOPEPTIDASE ACYLAMINOACYL-PEPTIDASE PEPTIDASE ACYL-PEPTIDE ESTERASE/LIPASE/THIOESTERASE) protein domain (PD381984) which is seen in Q7U9D5_SYNPX.Residues 518-633 are 48% similar to a (ESTERASE/LIPASE/THIOESTERASE FAMILY ACTIVE SITE) protein domain (PDA1B3J5) which is seen in Q7V3K6_PROMP.Residues 536-628 are 63% similar to a (AMINOPEPTIDASE C) protein domain (PD971358) which is seen in Q69TI3_EEEEE.Residues 558-626 are 55% similar to a (OLIGOPEPTIDASE FAMILY PROLYL) protein domain (PDA1B345) which is seen in Q9A9E0_CAUCR.Residues 585-628 are 75% similar to a (HYDROLASE PEPTIDASE FAMILY ENZYME OLIGOPEPTIDASE ACYLAMINO-ACID-RELEASING PROLYL AMINOPEPTIDASE ACYL-PEPTIDE PROBABLE) protein domain (PD253370) which is seen in Q69Y12_EEEEE.","","-38% similar to PDB:1VE6 Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (E_value = 2.7E_11);-38% similar to PDB:1VE7 Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate (E_value = 2.7E_11);-38% similar to PDB:2HU5 Binding of inhibitors by Acylaminoacyl-peptidase (E_value = 2.7E_11);-38% similar to PDB:2HU7 Binding of inhibitors by Acylaminoacyl peptidase (E_value = 2.7E_11);-38% similar to PDB:2HU8 Binding of inhibitors by Acylaminoacyl peptidase (E_value = 2.7E_11);","Residues 442 to 652 (E_value = 3.3e-52) place ANA_0890 in the Peptidase_S9 family which is described as Prolyl oligopeptidase family.Residues 574 to 628 (E_value = 1.3e-07) place ANA_0890 in the DLH family which is described as Dienelactone hydrolase family.","","oligopeptidase family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0891","960324","962273","1950","10.83","20.28","67648","ATGGATCGCGTCTGGAAGAGGCTGTCTGCCCCCCTGTCACGGCGCACAGGCAGCCTCTTCCGCCATCATCGCTTCGGCCTCTACATCCTGGCGGTGGTGGTAGGACTCGCTTCGGGGCTGGGTGCGGTGCTGTTCCGGCTGGGGATCGACGCCTGGTCCCAGCTCCTGAGCGGAGCCGACGACTACACCCTGTCGATGGGGCCCTCAGTCGGGCTCCTGGCGCCGTTGGGGGTGTGGTTCGTCCTGGTCGCCCCGGTGCTCTCCGGTCTGCTGACAGGACCGTTGATGTCCCGGCTGGGTCGGACACCCACGGGTCACGGGGTGGCCGGCGTCATCTGGTCGACTCGTCACGGCGACGGCACCATGGCGCCCCTGCCGGCTCTGGCCGCGACGACGTCGGCCGCGCTGACGATCGGTGGCGGGGGCTCAGTCGGCCCGGAGGGGCCGATAGCAGAGCTGGGCGCGTCGACGGCGAGCATCATCGGACGGGGGCTGCGGCTGCGCCGGTCCTCGATCCGTCATCTGGCAGCCGCCGGAACGGCCGCCGGCATCGCCTCCGCCTTCAACGCACCACTGGCGGGGGCCTTCTTCGCCCTGGAGGTCATCCTCATGGGCTTCAGTGCCGACGCCTTCATCGTCATCGTCCTGGCCTGCGTGTCCTCGACCGTCCTGTCGCACCACCTGCTGGGAACGACGCTGTCGCTGTCACTGCCCTACCTGGACCTGTCCGGTGACGCCCAGCTGGGCTGGGTCGCGCTGCTGGGCGTCGTGGGCGGAGGCGTCGGTATCGGCTTCATGCGTCTTCGCTTCGTCATCCTCGACGCCCTGACCCGCGTCTGGCAGCGGTTGGGTGTACCGATCTGGGCGCGTCCGGGCATTGGCGGGCTGGCGGTCGGCGCAACCGTGCTGGTTCTGCCCGAGATGTACGGCGAGTCATCAGCCGCTCTCAACCGGGCGCTGGCGGGACGCTACGCCCTGACGCTGCTGCTGGTGCTGTGTGTGGCCAAGATGCTGGCGACCTCCTTGACCCTGGGGATGGGTTTCGTCGGCGGGGTGTTCGCCCCGTCCCTGTTCATCGGCGGGACGCTCGGCGCTGCCTTTGGCACACTCGTGGCTCCCAGTTACGCGCCTGCCGCCGGGGTCTTCGGGGTCATCGGCATGGGCGCGGTCTTTGCCGGTGCGGCTCGCGCCCCGATGACGGCGGTCCTGCTCATCATCGAGATGACCGGGCAGCACGCGCTGCTGGTGCCCCTTATGCTGGCCACGGTACTGGCCACCTTCATCAGTAGGTTCCTCTCGCGCGGTACGTTGTTCACCGAGGAGCTGCGTCGTCGCGGAGAGGATGTCGAGGATCCGATGTCCACCACGCTCCTGGGGCGAACCCGCGCCAGGCGGCTCATGGGGGACCCGCCCGCCACGATCCAGTCCACGGCGCCGCTCAACCAGGCCGCCTCCGTGATGAGCCGGCGTGGTCTCTCAGCCCTGCCCGTGGTCGTTGCCGGACAGAACGGAGCAGACGATCTGCTTGGCTGCGTGACGGCCGCCCAGCTCGCCGGAGCGCTCCTGAGCGAGCAGTCCGACGACGCCTCTGCGCGGCCGGCGACAGTGGCGGACCTGTCGCTGGTCCGTGACCGTCTGCACTGCGAGGACGAGGCGACCGACGTGCTTCAGGCCCTGACCGATACGCGCCTGGAAGGGCTTCCAGTAGTCGCCCGCACCGAAGGCTCCGGCGCGGAGGAGCTGGTGGGCTGGGTGTCCCAGAGGATCGTCGTTGAACGGGTCTACGAGGTCCAGGCCCAGGCCCGCGCCGCTGCCGCCGCCTACACCTCCTGGGGCTCACGGCTTCAGAACAAGTGGCACTCCCGCCCTGTTCCTCCGCGCAGAATCGGAAGGATCAGCCGCATCAGCCGTATCAGCCAGCGCAGCTCGCGCCGTTCCCGACGCCGGTGA","MDRVWKRLSAPLSRRTGSLFRHHRFGLYILAVVVGLASGLGAVLFRLGIDAWSQLLSGADDYTLSMGPSVGLLAPLGVWFVLVAPVLSGLLTGPLMSRLGRTPTGHGVAGVIWSTRHGDGTMAPLPALAATTSAALTIGGGGSVGPEGPIAELGASTASIIGRGLRLRRSSIRHLAAAGTAAGIASAFNAPLAGAFFALEVILMGFSADAFIVIVLACVSSTVLSHHLLGTTLSLSLPYLDLSGDAQLGWVALLGVVGGGVGIGFMRLRFVILDALTRVWQRLGVPIWARPGIGGLAVGATVLVLPEMYGESSAALNRALAGRYALTLLLVLCVAKMLATSLTLGMGFVGGVFAPSLFIGGTLGAAFGTLVAPSYAPAAGVFGVIGMGAVFAGAARAPMTAVLLIIEMTGQHALLVPLMLATVLATFISRFLSRGTLFTEELRRRGEDVEDPMSTTLLGRTRARRLMGDPPATIQSTAPLNQAASVMSRRGLSALPVVVAGQNGADDLLGCVTAAQLAGALLSEQSDDASARPATVADLSLVRDRLHCEDEATDVLQALTDTRLEGLPVVARTEGSGAEELVGWVSQRIVVERVYEVQAQARAAAAAYTSWGSRLQNKWHSRPVPPRRIGRISRISRISQRSSRRSRRR$","Voltage-gated chloride channel protein EriC","Extracellular, Membrane","Voltage-gated ClC-type chloride channel clcA","K03281 chloride channel protein; CIC family","Cl- channel, voltage-gated family protein","","Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 2004. 113(2):274-284. PMID: 14722619Carr G., Simmons N., Sayer J. A role for CBS domain 2 in trafficking of chloride channel CLC-5. Biochem. Biophys. Res. Commun. 2003. 310(2):600-605. PMID: 14521953Hebeisen S., Biela A., Giese B., Muller-Newen G., Hidalgo P., Fahlke C. The role of the carboxyl terminus in ClC chloride channel function. J. Biol. Chem. 2004. 279(13):13140-13147. PMID: 14718533","","","

InterPro
IPR000644
Domain

Cystathionine-beta-synthase
PF00571	$\"[465-595]T$	CBS
SM00116	$\"[470-522]T$ $\"[538-595]T$	CBS

InterPro
IPR001807
Family

Chloride channel, voltage gated
PR00762	$\"[130-149]T$ $\"[181-200]T$ $\"[348-368]T$ $\"[380-396]T$ $\"[398-417]T$	CLCHANNEL
PTHR11689	$\"[28-534]T$	CHLORIDE CHANNEL

InterPro
IPR014743
Domain

Chloride channel, core
PF00654	$\"[84-433]T$	Voltage_CLC

noIPR
unintegrated

unintegrated
PD140382	$\"[325-454]T$	Q9KF96_BACHD_Q9KF96;
G3DSA:1.10.3080.10	$\"[9-452]T$	no description
PTHR11689:SF14	$\"[28-534]T$	VOLTAGE-GATED CLC-TYPE CHLORIDE CHANNEL ERIC
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[25-45]?$ $\"[71-91]?$ $\"[175-197]?$ $\"[203-225]?$ $\"[246-266]?$ $\"[285-305]?$ $\"[320-338]?$ $\"[344-364]?$ $\"[374-394]?$ $\"[413-433]?$	transmembrane_regions

","BeTs to 15 clades of COG0038COG name: Chloride channel protein EriCFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0038 is aompkzyq-drlbce-gh-n-j----Number of proteins in this genome belonging to this COG is 2","***** IPB001807 (Chloride channel signature) with a combined E-value of 4.7e-36. IPB001807B 130-149 IPB001807C 181-200 IPB001807D 348-368 IPB001807E 380-396 IPB001807F 398-417 IPB001807B 336-355","Residues 73-444 are 65% similar to a (CHANNEL CHLORIDE VOLTAGE-GATED TRANSMEMBRANE ION IONIC CBS REPEAT DOMAIN MEMBRANE) protein domain (PD001036) which is seen in Q93RS4_STRCO.Residues 191-438 are 43% similar to a (MEMBRANE SPANNING) protein domain (PDA0D016) which is seen in Q72L34_THET2.Residues 276-427 are 50% similar to a (MEMBRANE SPANNING) protein domain (PDA0S2F9) which is seen in Q72KD0_THET2.Residues 301-433 are 52% similar to a (CLC CHLORIDE TYPE CHANNEL) protein domain (PDA097I7) which is seen in Q70S43_ENTHI.Residues 302-440 are 50% similar to a (PH0032) protein domain (PD107607) which is seen in O57747_PYRHO.Residues 303-446 are 56% similar to a (CHLORIDE CHANNEL) protein domain (PD791128) which is seen in Q8EHC6_SHEON.Residues 328-429 are 55% similar to a (SPBC887.02) protein domain (PD193277) which is seen in O94287_SCHPO.Residues 334-408 are 57% similar to a (BH0663 TRANSPOSASE) protein domain (PD952892) which is seen in Q9Z9W7_BACHD.Residues 340-425 are 56% similar to a (CHLORIDE CHANNEL FAMILY VOLTAGE-GATED) protein domain (PD716935) which is seen in Q8KPT6_SYNP7.","","-57% similar to PDB:1KPL Crystal Structure of the ClC Chloride Channel from S. typhimurium (E_value = 5.6E_22);-57% similar to PDB:2HTL Structure of the Escherichia coli ClC chloride channel Y445F mutant and Fab complex (E_value = 1.3E_21);-57% similar to PDB:1KPK Crystal Structure of the ClC Chloride Channel from E. coli (E_value = 2.8E_21);-57% similar to PDB:1OTS Structure of the Escherichia coli ClC Chloride channel and Fab Complex (E_value = 2.8E_21);-57% similar to PDB:1OTT Structure of the Escherichia coli ClC Chloride channel E148A mutant and Fab Complex (E_value = 2.8E_21);","Residues 84 to 433 (E_value = 3.3e-30) place ANA_0891 in the Voltage_CLC family which is described as Voltage gated chloride channel.Residues 465 to 595 (E_value = 5.1e-07) place ANA_0891 in the CBS family which is described as CBS domain pair.","","ClC-type chloride channel clcA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0892","962892","962320","573","9.82","5.61","21134","ATGGAAAGGTCGTTCCTCATGGACGAGCGCTCATCGGTACGTCCGGTTCAAGACACCCGTCGTCCCGCATACGGGTGGGGGCGGATTCTGGTCGGTGTCTTCGCCGTCTTCGGGGCGATTCTTCTCATCCCCTCTCTGACCACGCTGCTGAGAAGCCCCGACGAGGAGCCCGCGGTGTGGTCCCTCAACCTCCTGGGGGGCGGTCTGTACATCCTGCTGGCCGTCTGCGTGGCCCACAACGGGCGCCGGATGCGCAACATCGGTTGGATGTGCCTGGGGGCACTGGCCACCATGGCGGTGCTCATCGGCATCCTCACCCTGCCCGCCTCCTCTCCTGCCGAGCTCAGCGACTTGGTGTGGGCGCACTGGGGCCGGTCCCGGTGGTACCTGCCTGCGATCCTCCCGGTGGTCGCCGCTGCGTGGATGTGGATGTCTGACCCCCGGCGCATCGTGGCCAACGCCGAGCGCATCACCGAGCTGTCCGACACCCTCACCGAGAGCATCACCGAGAAGGCCCGGGCGGTCCAGGAGGGCCGGACTCACAAGACTCTGCGCAGTGGCCGGGACCGGTGA","MERSFLMDERSSVRPVQDTRRPAYGWGRILVGVFAVFGAILLIPSLTTLLRSPDEEPAVWSLNLLGGGLYILLAVCVAHNGRRMRNIGWMCLGALATMAVLIGILTLPASSPAELSDLVWAHWGRSRWYLPAILPVVAAAWMWMSDPRRIVANAERITELSDTLTESITEKARAVQEGRTHKTLRSGRDR$","Integral membrane protein","Membrane, Cytoplasm","","","","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[29-49]?$ $\"[59-77]?$ $\"[87-107]?$ $\"[126-144]?$	transmembrane_regions

InterPro
IPR000819
Domain

Peptidase M17, leucyl aminopeptidase, C-terminal
PR00481	$\"[421-438]T$ $\"[443-464]T$ $\"[480-501]T$ $\"[502-522]T$ $\"[530-545]T$	LAMNOPPTDASE
PF00883	$\"[324-653]T$	Peptidase_M17
PS00631	$\"[506-513]T$	CYTOSOL_AP

InterPro
IPR008283
Domain

Peptidase M17, leucyl aminopeptidase, N-terminal
PF02789	$\"[231-281]T$	Peptidase_M17_N

InterPro
IPR011356
Family

Peptidase M17, leucyl aminopeptidase
PTHR11963:SF3	$\"[257-400]T$ $\"[419-661]T$	LEUCINE AMINOPEPTIDASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.10	$\"[326-660]T$	no description
PTHR11963	$\"[257-400]T$ $\"[419-661]T$	LEUCINE AMINOPEPTIDASE-RELATED

","BeTs to 17 clades of COG0260COG name: Leucyl aminopeptidaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0260 is -----z-q-dr-bcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 1","***** IPB000819 (Cytosol aminopeptidase) with a combined E-value of 9.4e-100. IPB000819A 327-347 IPB000819B 360-394 IPB000819C 423-456 IPB000819D 480-522 IPB000819E 555-597 IPB000819F 620-630","Residues 328-659 are 64% similar to a (AMINOPEPTIDASE HYDROLASE CYTOSOL LEUCINE LEUCYL MANGANESE LAP PROBABLE B PEPTIDASE) protein domain (PD002804) which is seen in Q6AFG2_BBBBB.Residues 328-450 are 44% similar to a (3.4.11.- HYDROLASE PEPTIDASE B AMINOPEPTIDASE) protein domain (PDA1C0Y1) which is seen in Q6D266_BBBBB.","","-63% similar to PDB:1GYT E. COLI AMINOPEPTIDASE A (PEPA) (E_value = 3.1E_55);-51% similar to PDB:2J9A BLLAP IN COMPLEX WITH MICROGININ FR1 (E_value = 1.9E_49);-51% similar to PDB:1BLL X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE (E_value = 4.3E_49);-51% similar to PDB:1BPM DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY (E_value = 4.3E_49);-51% similar to PDB:1BPN DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY (E_value = 4.3E_49);","Residues 231 to 281 (E_value = 2e-05) place ANA_0893 in the Peptidase_M17_N family which is described as Cytosol aminopeptidase family, N-terminal domain.Residues 324 to 653 (E_value = 3.8e-142) place ANA_0893 in the Peptidase_M17 family which is described as Cytosol aminopeptidase family, catalytic domain.","","(lap) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0894","965135","966508","1374","5.58","-12.71","47665","GTGACAGAGACCGTCTACGACATGGTCATTCTGGGCGCGGGATCAGGGGGCTACGCCGCCGCCCTGCGTGGCGCCCAACTGGGCCTCAAGGTCGCCCTGATCGAGGCGGACAAGCTGGGGGGCACCTGCCTCCACCGCGGCTGTGTGCCCACCAAGGCCCTGCTGCACGCCGCCGAGACTGCTGATGCCGTGCGCGAGGCCGCCACGGTGGGCATCAAGGCCGCTTTCGAGGGCGTGGACATGCCTGGCGTCCAGAAGTACAAGAACAGCATCGTCTCGCGGATGCACAAGGGCCTGGAGGGCCTGGTGTCCTCGCGGGGCATCGACCTGATCCAGGGGTGGGGACGTTTGGTGGCCGCCGACGCCGTCGAGGTTGACGGCCGTCGCATCACCGGCCGCAACGTGGTCCTTGCCTCCGGCTCCTACTCCAAGACCATCGGGCAGGAGATCTCCGGAGGCGTCATCACCTCCGAGGAGGCCCTGGAGATGGACCACGTCCCCGCCTCGGCAGTGATCCTGGGCGGCGGCGTCATCGGGGTGGAGTTCGCCTCGGCCTGGGCCTCCATGGGCAGCCAGGTCACCATCATCGAGGGACTGCCCCACCTGGTGCCCAACGAGGACGAGGCGATCTCCAAGCAGCTCGAGCGCGCCTTCCGCAAGCGCAAGATCACCTTCCGCACCAACACGATGTTCGAGTCGGTCGAGCGCCACGACGGCGGGGTGACCGTGCGCACCCAGGATGGCAAGACCCACGAGGCCGAGGTCCTCCTCATCGCCGTGGGCCGCGGACCGGCGACCGCCAACCTCGGCTACGAGGAGGTCGGGGTCGCCATGGACCGCGGCTTCGTCCTGGCCGACGAGTACGGCCGCACCAACGTCCCGGGCGTGTGGGCCGTGGGTGACATCGTCCCCGGCGTCCAGCTCGCCCACCGCGGCTTCGCCCAGGGCATCGTCGTGGCGGAGAAGATCGCGGGCCTGGACCCGGCCCCGGTCGACGACGTCCTGGTCCCCAAGGTGACCTTCTGCGAGCCCGAGATCGCCTCGGTGGGGCTGTCGGAGGCCAAGGCCGCCGAGATCCACGGCAAGGAGAACATCACCTCCGCCGAGTTCAACGTGGCCGGCAACGCCAAGAGCCAGATCCTGGGGACGCAGGGCTTCGTCAAGCTCGTCTCCCTCAAGGACGGCCCGATCCTGGGCTTCCACGCCATCGGCGCCCGCATGGGCGAGCAGGTGGGTGAGGGCCAGCTTATGGTGTCCTGGGAGGCCGACGCCGACGACGTCGCCGCCCTGGTGCACGCCCACCCCACCCAGAACGAGACCCTCGGCGAGGCCGCCATGGCCCTCGCCGGCAAGCCGCTGCACAACCACGGCTGA","VTETVYDMVILGAGSGGYAAALRGAQLGLKVALIEADKLGGTCLHRGCVPTKALLHAAETADAVREAATVGIKAAFEGVDMPGVQKYKNSIVSRMHKGLEGLVSSRGIDLIQGWGRLVAADAVEVDGRRITGRNVVLASGSYSKTIGQEISGGVITSEEALEMDHVPASAVILGGGVIGVEFASAWASMGSQVTIIEGLPHLVPNEDEAISKQLERAFRKRKITFRTNTMFESVERHDGGVTVRTQDGKTHEAEVLLIAVGRGPATANLGYEEVGVAMDRGFVLADEYGRTNVPGVWAVGDIVPGVQLAHRGFAQGIVVAEKIAGLDPAPVDDVLVPKVTFCEPEIASVGLSEAKAAEIHGKENITSAEFNVAGNAKSQILGTQGFVKLVSLKDGPILGFHAIGARMGEQVGEGQLMVSWEADADDVAALVHAHPTQNETLGEAAMALAGKPLHNHG$","Dihydrolipoamide dehydrogenase","Cytoplasm","dihydrolipoamide dehydrogenase","dihydrolipoamide dehydrogenase","dihydrolipoamide dehydrogenase","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Rice D.W., Schulz G.E., Guest J.R. Structural relationship between glutathione reductase and lipoamide dehydrogenase. J. Mol. Biol. 1984. 174(3):483-496. PMID: 6546954Carothers D.J., Pons G., Patel M.S. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 1989. 268(2):409-425. PMID: 2643922Walsh C., Bradley M., Nadeau K. Molecular studies on trypanothione reductase, a target for antiparasitic drugs. Trends Biochem. Sci. 1991. 16(8):305-309. PMID: 1957352Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G. Cloning and sequencing of a human thioredoxin reductase. FEBS Lett. 1995. 373(1):5-9. PMID: 7589432Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P. Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). Plant J. 1992. 2(1):129-131. PMID: 1303792","","","

InterPro
IPR000815
Family

Mercuric reductase
PR00945	$\"[17-35]T$ $\"[52-71]T$ $\"[169-186]T$ $\"[189-204]T$	HGRDTASE

InterPro
IPR001100
Family

Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411	$\"[7-29]T$ $\"[39-54]T$ $\"[135-144]T$ $\"[169-194]T$ $\"[254-268]T$ $\"[296-303]T$ $\"[332-353]T$ $\"[397-412]T$ $\"[419-439]T$	PNDRDTASEI

InterPro
IPR001327
Domain

Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139	$\"[139-195]T$	Q93HV8_ARTGO_Q93HV8;
PF00070	$\"[169-261]T$	Pyr_redox

InterPro
IPR004099
Domain

Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30	$\"[335-454]T$	no description
PF02852	$\"[336-445]T$	Pyr_redox_dim

InterPro
IPR006258
Family

Dihydrolipoamide dehydrogenase
TIGR01350	$\"[5-455]T$	lipoamide_DH: dihydrolipoamide dehydrogenas

InterPro
IPR012999
Active_site

Pyridine nucleotide-disulphide oxidoreductase, class I, active site
PS00076	$\"[40-50]T$	PYRIDINE_REDOX_1

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368	$\"[7-29]T$ $\"[135-144]T$ $\"[169-194]T$ $\"[254-268]T$ $\"[296-303]T$	FADPNR
PF07992	$\"[7-306]T$	Pyr_redox_2

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[5-69]T$ $\"[125-325]T$	no description
PTHR22912	$\"[9-453]T$	DISULFIDE OXIDOREDUCTASE
PTHR22912:SF20	$\"[9-453]T$	DIHYDROLIPOAMIDE DEHYDROGENASE-RELATED

","BeTs to 20 clades of COG1249COG name: Dihydrolipoamide dehydrogenase/glutathione oxidoreductase and related enzymesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1249 is aomp-zyqvdrlbcefghsn-jxi-wNumber of proteins in this genome belonging to this COG is 4","***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 1.4e-90. IPB001100A 6-31 IPB001100B 40-52 IPB001100C 155-195 IPB001100D 254-276 IPB001100E 281-302 IPB001100F 332-356 IPB001100G 396-441 IPB001100A 168-193***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 8.5e-27. IPB013027A 7-29 IPB013027C 169-194 IPB013027D 254-268 IPB013027E 296-303***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase, class-II) with a combined E-value of 2.7e-15. IPB000103A 8-26 IPB000103D 251-266 IPB000103E 291-328***** IPB000815 (Mercuric reductase class II signature) with a combined E-value of 7.8e-10. IPB000815B 17-35 IPB000815C 52-71 IPB000815E 169-186***** IPB008150 (Bacterial-type phytoene dehydrogenase) with a combined E-value of 8.8e-06. IPB008150A 9-40 IPB008150A 171-202","Residues 43-106 are 79% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD REDOX-ACTIVE CENTER DEHYDROGENASE NAD DIHYDROLIPOAMIDE REDUCTASE GLUTATHIONE) protein domain (PD459598) which is seen in Q9S2Q6_STRCO.Residues 102-236 are 57% similar to a (OXIDOREDUCTASE FLAVOPROTEIN DEHYDROGENASE CENTER FAD NAD DIHYDROLIPOAMIDE REDOX-ACTIVE) protein domain (PDA0V4B2) which is seen in Q73M80_TREDE.Residues 139-195 are 81% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD REDOX-ACTIVE CENTER REDUCTASE DEHYDROGENASE NAD DIHYDROLIPOAMIDE THIOREDOXIN) protein domain (PD000139) which is seen in Q93HV8_ARTGO.Residues 147-197 are 75% similar to a (DEHYDROGENASE OXIDOREDUCTASE FLAVOPROTEIN FAD NAD DIHYDROLIPOAMIDE CENTER REDOX-ACTIVE ALPHA-KETO E3) protein domain (PD443343) which is seen in DLD2_BACSU.Residues 197-419 are 42% similar to a (OXIDOREDUCTASE FLAVOPROTEIN YPL017CP FAD) protein domain (PD453149) which is seen in Q02733_YEAST.Residues 238-287 are 80% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD REDOX-ACTIVE CENTER DEHYDROGENASE NAD DIHYDROLIPOAMIDE REDUCTASE GLUTATHIONE) protein domain (PD327876) which is seen in Q93HV8_ARTGO.Residues 290-347 are similar to a (OXIDOREDUCTASE FAD FLAVOPROTEIN REDOX-ACTIVE CENTER DEHYDROGENASE NAD DIHYDROLIPOAMIDE REDUCTASE GLUTATHIONE) protein domain (PD425120) which is seen in Q6AFG3_BBBBB.Residues 348-401 are 79% similar to a (OXIDOREDUCTASE FLAVOPROTEIN DEHYDROGENASE CENTER FAD NAD REDOX-ACTIVE DIHYDROLIPOAMIDE NADH-FERREDOXIN LIPOAMIDE) protein domain (PDA0E9X9) which is seen in Q6AFG3_BBBBB.Residues 403-454 are 88% similar to a (OXIDOREDUCTASE FLAVOPROTEIN DEHYDROGENASE FAD REDOX-ACTIVE CENTER NAD DIHYDROLIPOAMIDE E3 PYRUVATE) protein domain (PD855831) which is seen in Q93HV8_ARTGO.","","-55% similar to PDB:1EBD DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE (E_value = 1.8E_64);-51% similar to PDB:1DXL DIHYDROLIPOAMIDE DEHYDROGENASE OF GLYCINE DECARBOXYLASE FROM PISUM SATIVUM (E_value = 3.7E_62);-51% similar to PDB:3LAD REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE (E_value = 6.4E_62);-51% similar to PDB:1LPF THREE-DIMENSIONAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM PSEUDOMONAS FLUORESCENS AT 2.8 ANGSTROMS RESOLUTION. ANALYSIS OF REDOX AND THERMOSTABILITY PROPERTIES (E_value = 1.7E_59);-51% similar to PDB:2A8X Crystal Structure of Lipoamide Dehydrogenase from Mycobacterium tuberculosis (E_value = 1.9E_58);","Residues 7 to 326 (E_value = 4.5e-05) place ANA_0894 in the DAO family which is described as FAD dependent oxidoreductase.Residues 7 to 327 (E_value = 0.00084) place ANA_0894 in the GIDA family which is described as Glucose inhibited division protein A.Residues 7 to 306 (E_value = 2e-56) place ANA_0894 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 7 to 45 (E_value = 4.3e-06) place ANA_0894 in the FAD_binding_2 family which is described as FAD binding domain.Residues 169 to 261 (E_value = 6.5e-35) place ANA_0894 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 336 to 445 (E_value = 7.8e-36) place ANA_0894 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain.","","dehydrogenase (lpdA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0895","966539","968248","1710","4.73","-28.00","57825","ATGTCAGAGTCCGTGAAGATGCCCGCTCTGGGTGAGTCCGTCACCGAGGGGACGGTCTCCTCCTGGCTCAAGGCCGTGGGAGACACCGTCGAGGCCGACGAGCCCCTGCTGGAGGTCGCCACCGACAAGGTCGACACCGAGGTCCCCTCCCCCGCATCCGGCGTCCTGCTGGAGATCCGCGTCCCCGAGGACGAGACCGTCGAGGTCGGCACCGTCCTGGCCATCATCGGCGACCCCTCCGAGGCGGGCTCCGCCCCGGCCCCCGCCGCCCCCGCGCCGCAGGCCGCACCCGAGCCCCCGGCTCCCGCCCCGGCCCCGGCCGCTGAGGCCCCGACCCCCGCCGCCCCGCAGGCCGGCGGCTCGGCCGAGGGCACTGAGGTGACGATGCCGGCCCTGGGTGAGTCCGTCACCGAGGGGACGGTCTCCTCCTGGCTCAAGGCCGTGGGAGACACCGTCGAGGCCGACGAGCCCCTGCTGGAGGTCGCCACCGACAAGGTCGACACCGAGGTCCCCTCCCCCGCATCCGGCGTCCTGCTGGAGATCCGCGTCCCCGAGGACGAGACCGTCGAGGTCGGCACCGTCCTGGCCATCATCGGCGACCCCTCTCAGGCGGGCTCCGCCCCGGCCCCCGCCGCCCCCGCGCCGCAGGCCGCACCCGAGCCCCCGGCTCCCGCCCCGGCCGCTGAGGCCCCGGCCCCCGCCGCCCCGGCTGCGACCGAGGCGCCTGCAGCCGCCGCCCCGGTGAGCTCTGGAGCCTCGGGTTCCTACGTCACGCCGATCGTGCGCAAGCTCGCCAAGGACAAGGGTGTGGACCTGTCCAGCGTCACCGGTACGGGTGTGGGCGGACGCATCCGCAAGCAGGACGTGGAGGCTGCTGCCAAGGCCGCTGAGGAGGCCCGCGCTGCGGCAGCCGCCCAGGCTCCGGCTGCTGAGGCGTCGGCGCCTGCCGCCGCGGCCAAGCCGGCCTCGGCCAAGCCCGAGGTGGACACCACCCTGCGCGGCCGCACGGAGAAGATGAGCCGACTGCGTCAGGTCATCGCCGATCGCATGATCGACTCCCTGCAGACCTCCGCCCAGCTGACCACCGTCGTCGAGGTGGATGTGACTCGTGTGGCCGCGCTGCGGGCCCGCGCGAAGAACGACTTCCTGGCCAAGAACGGCACCAAGCTCACCTTCCTGCCCTTCTTCGTCCAGGCGGCCACGGAGGCCCTCAAGGCCCACCCGAAGATCAACGCCTCCATCGAGGGCAAGAACGTCACCTACCACGATGTCGAGCACGTCGGCATCGCGGTGGACACGCCGCGCGGCCTGCTCGTGCCGGTGGTCAAGAACGCCGGGGACCTCAACATCCCCGGGCTGGCCAAGCGCATCAACGACCTGGCCGCCCGCACCCGGGACAACAAGGTCAACCCCGATGAGCTCAGCGGCTCGACCTTCACGATCACCAACACCGGCAGCGGCGGTGCCCTGTTCGACACCCCGATCATCAACCAGCCGGAGGTCGCGATCCTGGGGCTGGGCGCTATCCAGCGCCAGCCGCGCGTCATCAAGGATGCCGACGGCGGCGAGGTCATCGCCATCCGCTCGGTGTGCTACCTGGCCCTGTCCTACGACCACCGACTGGTGGACGGCGCGGACGCGGCCCGCTACCTCATGACGGTCAAGAAGCGCCTTGAGGAGGGCGACTTCGGCGGCGAGCTGGGTCTGTGA","MSESVKMPALGESVTEGTVSSWLKAVGDTVEADEPLLEVATDKVDTEVPSPASGVLLEIRVPEDETVEVGTVLAIIGDPSEAGSAPAPAAPAPQAAPEPPAPAPAPAAEAPTPAAPQAGGSAEGTEVTMPALGESVTEGTVSSWLKAVGDTVEADEPLLEVATDKVDTEVPSPASGVLLEIRVPEDETVEVGTVLAIIGDPSQAGSAPAPAAPAPQAAPEPPAPAPAAEAPAPAAPAATEAPAAAAPVSSGASGSYVTPIVRKLAKDKGVDLSSVTGTGVGGRIRKQDVEAAAKAAEEARAAAAAQAPAAEASAPAAAAKPASAKPEVDTTLRGRTEKMSRLRQVIADRMIDSLQTSAQLTTVVEVDVTRVAALRARAKNDFLAKNGTKLTFLPFFVQAATEALKAHPKINASIEGKNVTYHDVEHVGIAVDTPRGLLVPVVKNAGDLNIPGLAKRINDLAARTRDNKVNPDELSGSTFTITNTGSGGALFDTPIINQPEVAILGLGAIQRQPRVIKDADGGEVIAIRSVCYLALSYDHRLVDGADAARYLMTVKKRLEEGDFGGELGL$","Dihydrolipoamide acyltransferase","Extracellular, Periplasm, Cytoplasm","dihydrolipoamide acetyltransferase","dihydrolipoamide acyltransferase ","Dihydrolipoyllysine-residue succinyltransferase","","Yeaman S.J. The 2-oxo acid dehydrogenase complexes: recent advances. Biochem. J. 1989. 257(3):625-632. PMID: 2649080Russell G.C., Guest J.R. Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim. Biophys. Acta 1991. 1076(2):225-232. PMID: 1825611Fujiwara K., Okamura-Ikeda K., Motokawa Y. Chicken liver H-protein, a component of the glycine cleavage system. Amino acid sequence and identification of the N epsilon-lipoyllysine residue. J. Biol. Chem. 1986. 261(19):8836-8841. PMID: 3522581Behal R.H., Browning K.S., Hall T.B., Reed L.J. Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 1989. 86(22):8732-8736. PMID: 2682658Priefert H., Hein S., Kruger N., Zeh K., Schmidt B., Steinbuchel A. Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J. Bacteriol. 1991. 173(13):4056-4071. PMID: 2061286","","","

InterPro
IPR000089
Domain

Biotin/lipoyl attachment
PF00364	$\"[3-76]T$ $\"[125-198]T$	Biotin_lipoyl
PS50968	$\"[3-76]T$ $\"[125-198]T$	BIOTINYL_LIPOYL

InterPro
IPR001078
Domain

Catalytic domain of components of various dehydrogenase complexes
PD001115	$\"[481-557]T$	ODO2_MYCTU_Q10381;
PF00198	$\"[331-569]T$	2-oxoacid_dh

InterPro
IPR003016
Binding_site

2-oxo acid dehydrogenase, lipoyl-binding site
PS00189	$\"[27-56]T$ $\"[149-178]T$	LIPOYL

InterPro
IPR004167
Domain

E3 binding
PF02817	$\"[257-293]T$	E3_binding

InterPro
IPR014276
Family

2-oxoglutarate dehydrogenase, E2 component
TIGR02927	$\"[1-569]T$	SucB_Actino: 2-oxoglutarate dehydrogenase,

noIPR
unintegrated

unintegrated
G3DSA:2.40.50.100	$\"[4-98]T$ $\"[126-220]T$	no description
G3DSA:3.30.559.10	$\"[320-560]T$	no description
G3DSA:4.10.320.10	$\"[246-296]T$	no description
PTHR23151	$\"[126-539]T$	DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED
PTHR23151:SF8	$\"[126-539]T$	DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX

","BeTs to 17 clades of COG0508COG name: Dihydrolipoamide acyltransferasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0508 is -o-p-zy--drlbcefghsn-jxi-wNumber of proteins in this genome belonging to this COG is 1","***** IPB004167 (E3 binding domain) with a combined E-value of 1.3e-103. IPB004167A 13-64 IPB004167B 257-289 IPB004167C 389-413 IPB004167D 426-444 IPB004167E 464-506 IPB004167F 533-545***** IPB001078 (Catalytic domain of components of various dehydrogenase complexes) with a combined E-value of 3.8e-75. IPB001078A 22-56 IPB001078B 426-465 IPB001078C 476-506 IPB001078D 530-566***** IPB003016 (2-oxo acid dehydrogenase, acyltransferase component, lipoyl-binding) with a combined E-value of 2.3e-14. IPB003016 27-59 IPB003016 149-181***** IPB006718 (Dec-1 repeat) with a combined E-value of 2.8e-06. IPB006718F 205-233 IPB006718F 210-238 IPB006718F 217-245 IPB006718F 95-123 IPB006718F 83-111 IPB006718F 215-243 IPB006718F 85-113 IPB006718F 81-109 IPB006718F 216-244 IPB006718F 88-116 IPB006718F 90-118 IPB006718F 207-235 IPB006718F 212-240 IPB006718F 289-317 IPB006718F 291-319 IPB006718F 221-249 IPB006718F 87-115 IPB006718F 203-231 IPB006718F 296-324 IPB006718F 97-125 IPB006718F 226-254 IPB006718F 72-100 IPB006718F 194-222 IPB006718F 74-102 IPB006718F 196-224 IPB006718F 304-332 IPB006718F 206-234 IPB006718F 208-236 IPB006718F 299-327***** IPB009464 (PCAF, N-terminal) with a combined E-value of 7.8e-06. IPB009464A 79-123 IPB009464A 81-125 IPB009464A 208-252 IPB009464A 76-120 IPB009464A 207-251 IPB009464A 83-127 IPB009464A 203-247 IPB009464A 204-248 IPB009464A 201-245 IPB009464A 217-261 IPB009464A 210-254 IPB009464A 214-258 IPB009464A 198-242 IPB009464A 212-256 IPB009464A 74-118 IPB009464A 206-250 IPB009464A 196-240 IPB009464A 77-121 IPB009464A 213-257 IPB009464A 211-255 IPB009464A 205-249 IPB009464A 89-133 IPB009464A 92-136 IPB009464A 84-128 IPB009464A 194-238 IPB009464A 218-262 IPB009464A 82-126 IPB009464A 93-137","Residues 139-198 are 91% similar to a (ACYLTRANSFERASE PYRUVATE LIPOYL BIOTIN TRANSFERASE DIHYDROLIPOAMIDE DEHYDROGENASE CARBOXYLASE COMPONENT ACETYLTRANSFERASE) protein domain (PD000268) which is seen in Q6A9W6_PROAC.Residues 139-198 are 91% similar to a (ACYLTRANSFERASE PYRUVATE LIPOYL BIOTIN TRANSFERASE DIHYDROLIPOAMIDE DEHYDROGENASE CARBOXYLASE COMPONENT ACETYLTRANSFERASE) protein domain (PD000268) which is seen in Q6A9W6_PROAC.Residues 254-289 are 91% similar to a (ACYLTRANSFERASE TRANSFERASE LIPOYL DIHYDROLIPOAMIDE PYRUVATE DEHYDROGENASE ACETYLTRANSFERASE COMPONENT E2 COMPLEX) protein domain (PD001730) which is seen in Q9S2Q5_STRCO.Residues 332-387 are 76% similar to a (ACYLTRANSFERASE LIPOYL TRANSFERASE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE ACETYLTRANSFERASE SUCB ACYLTRANSFERASES) protein domain (PDA1F5S1) which is seen in Q8NNJ2_CORGL.Residues 339-380 are 90% similar to a (ACYLTRANSFERASE TRANSFERASE LIPOYL DIHYDROLIPOAMIDE DEHYDROGENASE COMPONENT E2 PYRUVATE ACETYLTRANSFERASE COMPLEX) protein domain (PD526502) which is seen in Q6AFG4_BBBBB.Residues 390-480 are 79% similar to a (ACYLTRANSFERASE TRANSFERASE LIPOYL DIHYDROLIPOAMIDE DEHYDROGENASE PYRUVATE COMPONENT E2 ACETYLTRANSFERASE COMPLEX) protein domain (PD510157) which is seen in Q6A9W6_PROAC.Residues 481-557 are 79% similar to a (ACYLTRANSFERASE TRANSFERASE LIPOYL DIHYDROLIPOAMIDE DEHYDROGENASE PYRUVATE COMPONENT E2 ACETYLTRANSFERASE COMPLEX) protein domain (PD001115) which is seen in ODO2_MYCTU.","","-67% similar to PDB:1C4T CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E_value = 2.8E_46);-67% similar to PDB:1E2O CATALYTIC DOMAIN FROM DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E_value = 2.8E_46);-67% similar to PDB:1SCZ Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase (E_value = 2.8E_46);-65% similar to PDB:1B5S DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS (E_value = 1.3E_43);-52% similar to PDB:1DPC CRYSTALLOGRAPHIC AND ENZYMATIC INVESTIGATIONS ON THE ROLE OF SER558, HIS610 AND ASN614 IN THE CATALYTIC MECHANISM OF AZOTOBACTER VINELANDII DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) (E_value = 9.8E_31);","Residues 3 to 76 (E_value = 1.4e-30) place ANA_0895 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme.Residues 125 to 198 (E_value = 2.2e-31) place ANA_0895 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme.Residues 257 to 293 (E_value = 6.7e-18) place ANA_0895 in the E3_binding family which is described as e3 binding domain.Residues 331 to 569 (E_value = 9.8e-116) place ANA_0895 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain).","","acetyltransferase (AF235020)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0896","969365","968391","975","6.34","-2.64","35684","ATGCCCGCCGTTGACTACTACCTGACCTGGCTCAGCGCCATGCACGCGGAAGCCGCACGCCTTCGCCACCGGGAGGTCGAGCCGGAGCACATGCTCCTCGGCCTCCTCGCCCAAGGCGGGACGGCTGCAGCCGTCTTGGCGGCCCGGGGCGTGACTCTCACGCGAGCGCGTGCCGCCATTAAGGAGATGGCTGATACGGACTTTGCTCGCGTGGGCATCAGCCTTCCCGACGCCCTCAGACCTGAGCCGATCTCAGCCGAAGAGCTGACCGCGGAGGCGGGAGGAGAGATTCCCCTTTCGGACACTGCCGCCGAGTTCATTGACAACAAGGGGACTTCGTTCAACTCCAGCGCTCAGGCTCTGCAAGCCCTCATCTCCTCATCCACCGTCTCGCTCCAGTCGCCGGTCGTCAGGCTTCTTGCTCACTGCGGAGTTGATGTCGACTGCCTGCGCACCGAGCTCAGTGAGGTAGCGGCCGACAAGGAACCGGCTCGGGGACGCTACCGGATGACTGATGAATACCGTGGGTACGGCCTGGACCGGGAGCTGAGCCAGGAACGCTTCATCTCCGCCTCGGTGGCTCAGCTGGCCGCACTACTGAGGGACCCGGATCGGCTCACGTGGTGGGCCCTGCCTCGACAGCAGCTGGTTGAGGTTCTTTCCGACGGCGCCGTGCAGAGGGTGGAGGGGCGACGTCGGACCGTCTTCCTGAGGTGGCGGCTGGAGACGGCCGTGGACACGAGGGTTACCTGGTCGTGCACCGTCGTCTCAGGGCGTCGCGACGGTGAGGTGGCCTTCGTGAAGGATCTGCACCTGATCGAGGCGCCAAGTGGCACTCGTGTCCGTCTGGGTCTGGCGCATCGCACATGGGGGCGGCTGGGGGAGCTGGTCTACCCGATCGTCTGGCGCTGGACTCGTCTGGGGCTGGAGAACACGCTCACCGGTATCGCACGGGCTGCAGCGGAGGACTCCTGA","MPAVDYYLTWLSAMHAEAARLRHREVEPEHMLLGLLAQGGTAAAVLAARGVTLTRARAAIKEMADTDFARVGISLPDALRPEPISAEELTAEAGGEIPLSDTAAEFIDNKGTSFNSSAQALQALISSSTVSLQSPVVRLLAHCGVDVDCLRTELSEVAADKEPARGRYRMTDEYRGYGLDRELSQERFISASVAQLAALLRDPDRLTWWALPRQQLVEVLSDGAVQRVEGRRRTVFLRWRLETAVDTRVTWSCTVVSGRRDGEVAFVKDLHLIEAPSGTRVRLGLAHRTWGRLGELVYPIVWRWTRLGLENTLTGIARAAAEDS$","Clp amino terminal domain protein","Cytoplasm","Clp amino terminal domain protein","hypothetical protein predicted by Glimmer/Critica","Clp N terminal domain protein","","Barnett M.E., Zolkiewska A., Zolkiewski M. Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. J. Biol. Chem. 2000. 275(48):37565-37571. PMID: 10982797","","","

InterPro
IPR004176
Domain

Clp, N-terminal
PF02861	$\"[14-65]T$ $\"[133-159]T$	Clp_N

noIPR
unintegrated

unintegrated
PTHR11638	$\"[17-63]T$	ATP-DEPENDENT CLP PROTEASE
PTHR11638:SF19	$\"[17-63]T$	ATP-DEPENDENT CLP PROTEASE

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-44% similar to PDB:1F8G THE X-RAY STRUCTURE OF NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM COMPLEXED WITH NAD+ (E_value = );-44% similar to PDB:1HZZ THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE (E_value = );-44% similar to PDB:1L7D Crystal Structure of R. rubrum Transhydrogenase Domain I without Bound NAD(H) (E_value = );-44% similar to PDB:1L7E Crystal Structure of R. rubrum Transhydrogenase Domain I with Bound NADH (E_value = );-44% similar to PDB:1NM5 R. rubrum transhydrogenase (dI.Q132N)2(dIII)1 asymmetric complex (E_value = );","Residues 14 to 65 (E_value = 6.3e-12) place ANA_0896 in the Clp_N family which is described as Clp amino terminal domain.Residues 133 to 159 (E_value = 159) place ANA_0896 in the Clp_N family which is described as Clp amino terminal domain.","","amino terminal domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0897","969610","969368","243","10.36","5.13","8585","ATGGATGCGCTCACCGCAGCCACCGAGGCTGCTAACACCACTCGCCCCGAGGACGGGTTACGAGCCGTGGCGGCTCTGCGACGACTGACGGACAGCCTTGAGCTTGCGCAGGTCGAGGCCGCTCTACGTGCGGGCATGGGTTGGAGCGAGATCGCCTCCTGTCTTGGAGTCTCTCGTCAGGCAGTCCACAAGAAGTACGCCAAGCGAGTTCAGCCCGGTCTAGCCCCGACCCGAAGGAGATGA","MDALTAATEAANTTRPEDGLRAVAALRRLTDSLELAQVEAALRAGMGWSEIASCLGVSRQAVHKKYAKRVQPGLAPTRRR$","Transcription regulator","Cytoplasm, Extracellular","hsp18 transcription regulator","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 16-69 are similar to a () protein domain (PD741461) which is seen in Q82J03_STRAW.","","-55% similar to PDB:2CG4 STRUCTURE OF E.COLI ASNC (E_value = );-56% similar to PDB:1FHU CRYSTAL STRUCTURE ANALYSIS OF O-SUCCINYLBENZOATE SYNTHASE FROM E. COLI (E_value = );-56% similar to PDB:1FHV CRYSTAL STRUCTURE ANALYSIS OF O-SUCCINYLBENZOATE SYNTHASE FROM E. COLI COMPLEXED WITH MG AND OSB (E_value = );-56% similar to PDB:1R6W Crystal structure of the K133R mutant of o-Succinylbenzoate synthase (OSBS) from Escherichia coli. Complex with SHCHC (E_value = );-57% similar to PDB:1GXM FAMILY 10 POLYSACCHARIDE LYASE FROM CELLVIBRIO CELLULOSA (E_value = );","No significant hits to the Pfam 21.0 database.","","transcription regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0898","970364","969744","621","5.60","-6.43","22129","ATGACCTCTGAAACGACAGGCAACTCCGGGCGCCGCGGCGGCCGAGACTTGCGCTCCGAGCTGCTGCGAACCAGTAGGGAGCTCCTCGACGAATCCGGCCCCAGTGCCCTGAGCATGCGGGAGGTCGCGCGTCGCGCCGGCTGCACGCACCAGGCGCCGTACCACTACTTCGCAAACCGCGAGGCCATCCTGGCGGCCTTGGTGTGTGAGGGCTTCGATGAGCTCGCGGACAGGCTCGCTGTGGCGCACGAGGGACTTGGGGGTGTGGATCTGCATGCGGTCCTGGTGGCCTCGGGGAACGTCTACGTTGAGTTTGCGCTACGTCACCCCGGAGTGTTCCGGGTGATGTTCCGACCCGACGTCTGCGATCCCGAGCGCTTCCCGGAGGTGGTGCAGGCCGGTGAGCGTGCGCGTCATGAGCTGGCCCGTCTGGCGAAGGCCGTGATGGGCGATGGTGCTCAGCTCGAGGCGGAGGTGCTGATCTGGTCCGGAGTGCACGGCCTGGCCTCACTGCTCCTCGACGGCCCCTTGGCGGGCGAGTTCAGCTCCATAGAGGATCGCATCGACTTCGCTCGCGGCGTCGTCGGTCTTGCTGGGGTGCCCGAGGTTGGTAGGGGCTGA","MTSETTGNSGRRGGRDLRSELLRTSRELLDESGPSALSMREVARRAGCTHQAPYHYFANREAILAALVCEGFDELADRLAVAHEGLGGVDLHAVLVASGNVYVEFALRHPGVFRVMFRPDVCDPERFPEVVQAGERARHELARLAKAVMGDGAQLEAEVLIWSGVHGLASLLLDGPLAGEFSSIEDRIDFARGVVGLAGVPEVGRG$","Transcriptional regulator, TetR family","Cytoplasm","transcriptional regulatory protein","TetR-family transcriptional regulator","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[21-34]T$ $\"[42-65]T$	HTHTETR
PF00440	$\"[21-67]T$	TetR_N
PS50977	$\"[15-75]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[18-78]T$	no description

","BeTs to 11 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 3e-14. IPB001647 21-63","Residues 62-171 are 50% similar to a (TRANSCRIPTIONAL TRANSCRIPTION DNA-BINDING REGULATION REGULATOR TETR-FAMILY FAMILY REGULATOR REGULATORY TETR) protein domain (PD599797) which is seen in Q82M79_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 21 to 67 (E_value = 1.5e-11) place ANA_0898 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulatory protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0899","970452","972719","2268","8.07","6.95","82371","ATGTCCTACGACGTCATCGTGATCGGTTCGGGTATTGGAGGACTGACGACTGCCGGCCTGCTGGCGCGGGCCAGCGGCAAGCGAGTTCTGGTCCTGGAGCGGCATACGGAACCGGGCGGACTGACGCACACCTTCCGGCGTGACGGCGCCTCCTGGGACGTGGGGGTGCACTACATCGGTCAGCTCGGTCCCGGAAGCCAGGGCCGCGCCTACTTCGACTACCTCTCCGGCGGCGAGCTGGAGTGGAACCGCATGCCCGACTCCTACGACAGGTTCGTCTACCCGGGCGTGGAGCTGCGTGTCAGCAGCGATCCGCTTCGGTACGAGCGCGACCTGGTTGACGCATTCCCGCAGGAGGCCAGAGCCATTCACCGCTACTTCCAGGATGTTCGCCGGGTGACACGGTGGGCGACGCTGGGCTTCATCCAGGGGATGGTCCCCCGGCCTGCGGCCTCGCTGCTCAGGGCAGCCCAGCGCCTGGGAGGCCGTCGAGCCACTCAGACGACGAAGGCGTATCTGGATGCCCACTTCCGCTCCCCCAGGCTCAAGGCCGTCCTGGCCAGTCAGTGGGGGGACTACGGCCTGCCGCCGTCCCGATCGGCCTTTGCCGTGCACGCGCTAATCGTCTCCCACTACCTCGAGGGCGCCTGGTTCCCCCGCGGTGGCAGCGCTCGGATCGCCCGCACCTTCGAGAAGGGCATCGAGCAGGCCGGAGGCGCTGTCCGCGTCGCGCAGGAGGTCACCGAGATCCTCACCGAGAACGGGACGGCGGTCGGGGTCCGCGTCATGGACCACCGAGGCGCCCAGGTCCGCGAACGCGTCTACCGCGCCCCGGTCATCGTGTCCGCCATCGGCGCCTCCAACACCTTCAACCGCCTGTTGCCCACATTCGGAGAGATCGGGAGACGCACCTGGCCCGTACGCCGCTCGCTGGAGCACCTGGGTACGGGCACCTCCGCGGTTACCGTCTTCCTACGCTTGCGTGATGACCCGCGCAGCATCGGCATCGATGGTGGAAACATCTGGGTGAACCGGGACCTCGATCACGAGGGCGCACAACGGTACAGCGATTCGCTGCTCGAGGGGCATCCTCACGATGTCTTCGTGTCCTTCCCCTCTCTGAAGTCCGGCGAGTCCCCACATACCGCCGAGCTCATCTCCTTCTGTGACGCGCGAGCCTTCCGGCAGTGGGCCGAGCAGCCCCGAGAAAACCGCGGCCCCGAGTACTTCGCTCTCAAGGAGCGCATCGCCCAAGGCATGCTGGAGCTGGCTGAGAGCGCGGCCCCGGGGCTGACCGAGCTCGTGGACTACGTGGAAACCTCCACTCCTTTGACCTACGAGCACTACACCGCTCATCCCGCCGGGGCCTTCTACGGTCCTCCGGCCACTCCGCTGAGGTTCCGGTCCCGCCCCCTGGGGCCGCGCACAGCCGTCCCCGGTCTGTTCCTCTCCGGCCAGGACGCCGGGAGCGCCGGCATCATGGGAGCCATGATGGGCGGAGTCGCAGCCGCGTGCCAGGTCCTTGGGCCCCGTGGGTATCCCACCATCGCCTCCGCCCTACGAGAGAGGCCCGAGGCTCCTGAGTCTCGAGCAGTGCACCCACTGCCCGAGGGCAAGCACCTCGCCACCCTGGTCTCCAAACGGCGTCTGACTCCCAGCGTGTGGGAGGCGGAGCTGCAGTTGGACGGCAGGATCGGCTCGTGGGCACCAGGGCAGTTCGCCCGTCTGCACGTGGGCGATGACGCATGGCGTGACTACTCGATCGCGGGGCTGGAGGAGGATCGTCTTCGTCTGCTCATCTCCACCCGGACAGGCGGCCGAGGATCCCAGTTCATCAAGAACGCGGACACGGGCGCGCAGACAGTGGTGGAGCTGCCCCTGGGCGGTTTCGGGCTCGCCGACTCGGGCAGGCGCCGCCTGTTCATCGCCACTGGCACGGGGATCGCACCCATGCTGGCCATGTTCGCTCAGGCTGCCGGTCTGGAACGCGACATTCTGCTCTTCGGGTGCCGTCACCAGGAGGAGGACCTGACCACCAGGATCGGCTCCCCCTTGCCAGGGACCGTCGTGCGCTGTCTGAGCCGCCAGGAGGCTCCAGGCGCATTCCACGGACGAGTCACCCAGGCCCTCACCGCGCTCGCTCACGACCTCCAGCTCGATCCCGAGTGTACGGACGTCTACCTGTGCGGTTCAGCGGCGATGGTGGCAGACGCACGAGACGTGCTCGACCGCGAGGGCTACACGTCGGTCCTCACCGAGCCGTATTGA","MSYDVIVIGSGIGGLTTAGLLARASGKRVLVLERHTEPGGLTHTFRRDGASWDVGVHYIGQLGPGSQGRAYFDYLSGGELEWNRMPDSYDRFVYPGVELRVSSDPLRYERDLVDAFPQEARAIHRYFQDVRRVTRWATLGFIQGMVPRPAASLLRAAQRLGGRRATQTTKAYLDAHFRSPRLKAVLASQWGDYGLPPSRSAFAVHALIVSHYLEGAWFPRGGSARIARTFEKGIEQAGGAVRVAQEVTEILTENGTAVGVRVMDHRGAQVRERVYRAPVIVSAIGASNTFNRLLPTFGEIGRRTWPVRRSLEHLGTGTSAVTVFLRLRDDPRSIGIDGGNIWVNRDLDHEGAQRYSDSLLEGHPHDVFVSFPSLKSGESPHTAELISFCDARAFRQWAEQPRENRGPEYFALKERIAQGMLELAESAAPGLTELVDYVETSTPLTYEHYTAHPAGAFYGPPATPLRFRSRPLGPRTAVPGLFLSGQDAGSAGIMGAMMGGVAAACQVLGPRGYPTIASALRERPEAPESRAVHPLPEGKHLATLVSKRRLTPSVWEAELQLDGRIGSWAPGQFARLHVGDDAWRDYSIAGLEEDRLRLLISTRTGGRGSQFIKNADTGAQTVVELPLGGFGLADSGRRRLFIATGTGIAPMLAMFAQAAGLERDILLFGCRHQEEDLTTRIGSPLPGTVVRCLSRQEAPGAFHGRVTQALTALAHDLQLDPECTDVYLCGSAAMVADARDVLDREGYTSVLTEPY$","Phytoene dehydrogenase","Cytoplasm","Oxidoreductase NAD-binding domain protein","retinol saturase (all-trans-retinol 13;14-reductase) ","oxidoreductase FAD/NAD(P)-binding domain protein","","Nordlund I., Powlowski J., Shingler V. Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol. 1990. 172(12):6826-6833. PMID: 2254258Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases. J. Bacteriol. 1991. 173(17):5385-5395. PMID: 1885518Harayama S., Rekik M., Bairoch A., Neidle E.L., Ornston L.N. Potential DNA slippage structures acquired during evolutionary divergence of Acinetobacter calcoaceticus chromosomal benABC and Pseudomonas putida TOL pWW0 plasmid xylXYZ, genes encoding benzoate dioxygenases. J. Bacteriol. 1991. 173(23):7540-7548. PMID: 1938949Suzuki M., Hayakawa T., Shaw J.P., Rekik M., Harayama S. Primary structure of xylene monooxygenase: similarities to and differences from the alkane hydroxylation system. J. Bacteriol. 1991. 173(5):1690-1695. PMID: 1999388Stainthorpe A.C., Lees V., Salmond G.P., Dalton H., Murrell J.C. The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). Gene 1990. 91(1):27-34. PMID: 2205538","","","

InterPro
IPR001221
Domain

Phenol hydroxylase reductase
PR00410	$\"[568-580]T$ $\"[584-591]T$ $\"[640-659]T$ $\"[725-733]T$	PHEHYDRXLASE

InterPro
IPR001433
Domain

Oxidoreductase FAD/NAD(P)-binding
PF00175	$\"[640-740]T$	NAD_binding_1

InterPro
IPR002938
Domain

Monooxygenase, FAD-binding
PF01494	$\"[2-38]T$	FAD_binding_3

InterPro
IPR008151
Domain

Phytoene dehydrogenase-related protein
PD139017	$\"[412-485]T$	Q7NCV2_GLOVI_Q7NCV2;

InterPro
IPR008333
Domain

Oxidoreductase FAD-binding region
PF00970	$\"[541-632]T$	FAD_binding_6

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.10	$\"[536-627]T$	no description
G3DSA:3.40.50.80	$\"[628-747]T$	no description
G3DSA:3.50.50.60	$\"[2-508]T$	no description
PTHR10668	$\"[3-504]T$	PHYTOENE DEHYDROGENASE
PTHR10668:SF5	$\"[3-504]T$	PHYTOENE DEHYDROGENASE-RELATED
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","BeTs to 5 clades of COG1233COG name: Phytoene dehydrogenase and related proteinsFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1233 is -om--z---dr-bc-------j----Number of proteins in this genome belonging to this COG is 1","***** IPB001221 (Phenol hydroxylase reductase family signature) with a combined E-value of 4.8e-13. IPB001221A 568-580 IPB001221D 640-659 IPB001221F 725-733***** IPB000759 (Adrenodoxin reductase family signature) with a combined E-value of 1.4e-08. IPB000759A 4-26 IPB000759B 28-41***** IPB001433 (Oxidoreductase FAD/NAD(P)-binding) with a combined E-value of 1.3e-07. IPB001433A 641-650 IPB001433B 726-736***** IPB008333 (Oxidoreductase FAD-binding region) with a combined E-value of 1.5e-07. IPB008333B 641-650 IPB008333C 726-736***** IPB003042 (Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature) with a combined E-value of 5.9e-06. IPB003042A 4-26","Residues 35-201 are 50% similar to a (ALR4631 GLL0693) protein domain (PD869815) which is seen in Q8YND5_ANASP.Residues 43-203 are 48% similar to a (FLJ20296 FLJ90780 WLPL439) protein domain (PD483888) which is seen in Q6NUM9_HUMAN.Residues 204-285 are 63% similar to a (PHYTOENE DEHYDROGENASE DESATURASE OXIDOREDUCTASE 1.14.99.- CAROTENOID BIOSYNTHESIS NAD FLAVOPROTEIN FAD) protein domain (PD360525) which is seen in Q8N2H5_HUMAN.Residues 205-403 are 39% similar to a (ALR4631 GLL0693) protein domain (PD569607) which is seen in Q7NMS2_GLOVI.","","-46% similar to PDB:1TVC FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath) (E_value = 2.8E_12);","Residues 2 to 38 (E_value = 4.8e-10) place ANA_0899 in the FAD_binding_3 family which is described as FAD binding domain.Residues 4 to 506 (E_value = 1.5e-05) place ANA_0899 in the DAO family which is described as FAD dependent oxidoreductase.Residues 4 to 33 (E_value = 1.6e-05) place ANA_0899 in the FAD_binding_2 family which is described as FAD binding domain.Residues 4 to 40 (E_value = 8.5e-06) place ANA_0899 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 12 to 508 (E_value = 1.1e-05) place ANA_0899 in the Amino_oxidase family which is described as Flavin containing amine oxidoreductase.Residues 541 to 632 (E_value = 7.3e-06) place ANA_0899 in the FAD_binding_6 family which is described as Oxidoreductase FAD-binding domain.Residues 640 to 740 (E_value = 1.7e-12) place ANA_0899 in the NAD_binding_1 family which is described as Oxidoreductase NAD-binding domain.","","NAD-binding domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0900","974675","972795","1881","10.88","23.70","64640","ATGGAAGGGGATGAGCCGGGAACCGAGCTCCATGTCCTCACGCAGCACGGGTGCAGTCTACGTGACCACAACCGGCACCCGAACCCGGGTTATCCACAGGCCGGTCGAAAGGGCTGGTCATCACGGTGCGCCGTGGTGACCATGGAGTGCATGAGCCCGACGACGTGCCCCCGCCCCGCCGACCGCCCCGGAGATGGCGCCTCCCACCGTCCCCGGCCCCGACGCCGTCCCGTACCTCGCCGGCGACTGCGGCCGCGCCGCGCGGGCGCCCCTCGCGCCGGCTCACTGCCTCCCTCGGACGCGGAGCCGAGCATCCCTGACTCGGCGCTCGGCGCCCTGTCGCAGCAGGGCTACACCGTCGGTGAGGTCATGGGGCGCTCCACTGCCCCCAGCGCCCCTCGCCGTGGCCTCGATGCGCAGGGCCGCCATGTGGTCATCCGGGTCGTCGACCTGCCCCACGGACGTGCTGGAGCCATAGTCCTGCGGCGCCTGGCCGATCTGCGCGTCCTGCGCCACCCCGGCCTGGTCACCGTGCGGGAGGTGGTCTCGCTGCCCGAGCATCGGGCGGGCGTCATCATGGACCTCGTCGACGGGGCGGGACTCGACGTGGTTCTGGGGGCGCGAGGACGGCTGAACGTCTCCTCGCTGGCCACGCTCCTGGACGTTCTGGGCTCGGCACTGGCCTACCTGCACGAGCACGGAGCGACCCATGGGGACGTTTCGAGTGGCAACGTCCTGGTGGCCGCCGATGGGCACCCGGTTCTCGTTGACCTGCTGGGCTCCGTCATGGAGACGGGCACGCAGGAGTATGCCGCGCCGGAACGCCTCGCCGGTGCCCCGGCGTCCTCTGCCGGTGACGTCTACGCCCTGGCCCGTCTGCTGACCGAGTGCTCGGGACAGGGCGGTACCGCCTCCCGGCGCCTGGCGGGAATCCTGACTGATGCCCTGGCCGAGGAGCCCGCTGACCGTCCCACCGCACGGGATCTGGCGGCCCGGGCACCTCAGCTCGGGCAGGCCTCACCCATCGAGCTGCCTGACGGCGCCCGCATGGCTGCCGGCTCCCTGCGAGCAGCAGCCCGCACCCCGACTCGCACGGTCGGCTCCAGGCTCACGCCCAAAGCCCGACCGAGCCGCCGGCCGAGGACGAGGAGCGAGCCACGGAACAACCATGGCAGTGCCGGCCGCACCGGGCGAGGGCCCGCGGCCATACGCTGGGGGAGAAGGGGAGGATCAGGGCGCTTGCGCACCCGCGCCTGGGGACTTACGGCAGTGGCGCTGGTGACCATCTGCCTGGCCGCCTGGGGGCCGGCCAAGGCCCTGGTGTCGCACAGGCCCGCGTGGGCGCTCGGAGCGGCCGCCGGCCCGACAGCATCGGCGCGGCCGCTGACCTCCTCCCGCGCTGGAGCCATCCCTTCAGGTAGCCCGTCTCCCTTAGTCGCCGGGAGCTCAGTCGCAACGGCGTCAACGCAGGCTCCTGGCGGGAGCGGCGGCGTCGATGTGGCCAGCGTCGTCGTCGGACTGTCCGAGGCTCGAGACCGGGCCCTCATGGCCGGCGATGCCGTCGCTCTGGCTGCCACGACGGTACCGGGGTCGCCCGCGGCGCGGGCCGACACCCAGGTTCTCACTGAGCTGCTCGACTCCGGTGAAGGCGTCAAGGAACTGCACACCTCCGTCAGCCAGGTCGCTGAGGTGAGGCTGCCTGACGACGCGGCGGAGCAGTGGGCCGGCGCGAGAGCGGTCCAGGTGACGCTGTCTCAAAGCGCCTCAACGCGTTCGGGGCCTGAGGGAGCGCGGACGGTTCCGGCCCTCGCACCCCGCCAGGTCGTGCTCATCGTCGTCCCGGAGCCGTGGCGCGTTGCGGACATTCGAGCCGTGGAGTGA","MEGDEPGTELHVLTQHGCSLRDHNRHPNPGYPQAGRKGWSSRCAVVTMECMSPTTCPRPADRPGDGASHRPRPRRRPVPRRRLRPRRAGAPRAGSLPPSDAEPSIPDSALGALSQQGYTVGEVMGRSTAPSAPRRGLDAQGRHVVIRVVDLPHGRAGAIVLRRLADLRVLRHPGLVTVREVVSLPEHRAGVIMDLVDGAGLDVVLGARGRLNVSSLATLLDVLGSALAYLHEHGATHGDVSSGNVLVAADGHPVLVDLLGSVMETGTQEYAAPERLAGAPASSAGDVYALARLLTECSGQGGTASRRLAGILTDALAEEPADRPTARDLAARAPQLGQASPIELPDGARMAAGSLRAAARTPTRTVGSRLTPKARPSRRPRTRSEPRNNHGSAGRTGRGPAAIRWGRRGGSGRLRTRAWGLTAVALVTICLAAWGPAKALVSHRPAWALGAAAGPTASARPLTSSRAGAIPSGSPSPLVAGSSVATASTQAPGGSGGVDVASVVVGLSEARDRALMAGDAVALAATTVPGSPAARADTQVLTELLDSGEGVKELHTSVSQVAEVRLPDDAAEQWAGARAVQVTLSQSASTRSGPEGARTVPALAPRQVVLIVVPEPWRVADIRAVE$","Serine/threonine protein kinase","Cytoplasm, Membrane, Extracellular","Protein kinase domain protein","serine/threonine protein kinase","protein kinase","","","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[172-335]T$	Q9L0H9_STRCO_Q9L0H9;
PF00069	$\"[118-332]T$	Pkinase
PS50011	$\"[118-336]T$	PROTEIN_KINASE_DOM

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[197-329]T$	no description
PTHR22986	$\"[115-329]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES

InterPro
IPR000544
Domain

Lipoate-protein ligase B
PD006086	$\"[32-92]T$	LIPB_MYCLE_O32961;
TIGR00214	$\"[10-221]T$	lipB: lipoyltransferase
PS01313	$\"[71-86]T$	LIPB

InterPro
IPR004143
Domain

Biotin/lipoate A/B protein ligase
PF03099	$\"[44-131]T$	BPL_LipA_LipB

noIPR
unintegrated

unintegrated
PTHR10993	$\"[9-131]T$ $\"[147-213]T$	LIPOATE-PROTEIN LIGASE B

","BeTs to 11 clades of COG0321COG name: Lipoate-protein ligase BFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0321 is ------y--dr--cefghsn-jx---Number of proteins in this genome belonging to this COG is 1","***** IPB000544 (Lipoate-protein ligase B) with a combined E-value of 1.6e-32. IPB000544A 33-46 IPB000544B 71-86 IPB000544C 149-184","Residues 32-92 are 62% similar to a (LIGASE ACYLTRANSFERASE TRANSFERASE B LIPOATE-PROTEIN LIPOYLTRANSFERASE -N-LIPOYLTRANSFERASE 2.3.1.- LIPOYL-ACYL-CARRIER PROTEIN-PROTEIN) protein domain (PD006086) which is seen in LIPB_MYCLE.Residues 147-195 are 85% similar to a (LIGASE ACYLTRANSFERASE TRANSFERASE B LIPOATE-PROTEIN LIPOYLTRANSFERASE -N-LIPOYLTRANSFERASE 2.3.1.- LIPOYL-ACYL-CARRIER PROTEIN-PROTEIN) protein domain (PD006665) which is seen in LIPB_STRAW.","","-58% similar to PDB:1W66 STRUCTURE OF A LIPOATE-PROTEIN LIGASE B FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 4.8E_45);","Residues 44 to 131 (E_value = 5.2e-09) place ANA_0901 in the BPL_LipA_LipB family which is described as Biotin/lipoate A/B protein ligase family.","","ligase B (lipB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0902","975426","976457","1032","6.20","-4.31","37953","GTGAGCACCACCGTGGCCCCTGAGGGACGCAAGCTCCTGCGGGTTGAGGCGCGCAACGCCCAGACACCCATTGAGTCCAAGCCCGACTGGCTGCGCACCCGCGCCGTCGTCTCCGACACCTACCAGGAGGTCCGCGGCCTGGTGAGGGAGAAGAGCCTGCACACGGTGTGTGCTGAGGCCAACTGCCCCAACATCTACGAGTGCTGGAACGACCGTGAGGCCACCTTCCTGGTGGGCGGCGAGATGTGCACCCGACGTTGCGACTTCTGCGACATCGCCACCGGACGTCCCACCGAGTACGACGTCGATGAGCCCAGGCGCGTGGCAGTCTCGATCAAGGAGATGGACCTGCGCTACGCCACCGTCACCGGGGTGGCCCGCGACGACCGTCCCGACGGCGGCGCCTGGCTCTACGCCGAGACCGCCCGCCAGGTGCACGAGCTCTCGCCGGGCACCGGTGTCGAGCTGCTCATCCCCGACTTCAAGGGAAACCCCGACGCGCTTGAGGACGTCTTCTCCTCGCGCCCCGAGGTTCTCGGCCACAACCTGGAGACGGTCCCGCGCATCTTCAAGCGGATCCGGCCGGCCTTCTCCTACCAGGGCAGCCTCGACGTCATCACGGCCGCCGCCGAGGCGGGGCTGGTCACCAAGTCCAACCTCATCCTGGGCATGGGCGAGACCCGTGACGAGATCGAGGCGGCCATGTCCGCCCTGGTGGAGGCGCGCTGCGACATCCTCACCATCACCCAGTACCTGCGTCCCTCCAAGCTGCACCACCCCGTTGACCGCTGGGTCAAGCCACAGGAGTTCGTGGATCTCAGCCGCCTGGCCGAGGAGATCGGGTTCGCCGCTGTCATGAGCGGCCCCATGGTGCGTTCCTCCTACCGCGCCGGCATGCTGTGGGGACGGGCCATGGTCAAGCGCGGTCGCCCCATCCCCGAGCACCTCTCGCAGCTCGCCGAGCCGGCCACCGCCCGCCAGGAGGCGTCGGCCCTGCTAGGGGCTCACCCCCACCTCGCCGCCGCCTGCTGA","VSTTVAPEGRKLLRVEARNAQTPIESKPDWLRTRAVVSDTYQEVRGLVREKSLHTVCAEANCPNIYECWNDREATFLVGGEMCTRRCDFCDIATGRPTEYDVDEPRRVAVSIKEMDLRYATVTGVARDDRPDGGAWLYAETARQVHELSPGTGVELLIPDFKGNPDALEDVFSSRPEVLGHNLETVPRIFKRIRPAFSYQGSLDVITAAAEAGLVTKSNLILGMGETRDEIEAAMSALVEARCDILTITQYLRPSKLHHPVDRWVKPQEFVDLSRLAEEIGFAAVMSGPMVRSSYRAGMLWGRAMVKRGRPIPEHLSQLAEPATARQEASALLGAHPHLAAAC$","Lipoic acid synthetase","Cytoplasm","lipoic acid synthetase","lipoic acid synthetase","lipoic acid synthetase","","Sofia H.J., Chen G., Hetzler B.G., Reyes-spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 2001. 29(5):1097-1106. PMID: 11222759","","","

InterPro
IPR003698
Family

Lipoate synthase
PIRSF005963	$\"[6-307]T$	Lipoyl synthase
PTHR10949	$\"[14-318]T$	LIPOIC ACID SYNTHETASE
TIGR00510	$\"[12-308]T$	lipA: lipoic acid synthetase

InterPro
IPR006638
Domain

Elongator protein 3/MiaB/NifB
SM00729	$\"[73-279]T$	Elp3

InterPro
IPR007197
Domain

Radical SAM
PF04055	$\"[77-238]T$	Radical_SAM

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[36-287]T$	no description

","BeTs to 16 clades of COG0320COG name: Lipoate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0320 is -o---zyq-dr-bcefghsn-jxi--Number of proteins in this genome belonging to this COG is 1","***** IPB010722 (Biotin and thiamin synthesis associated) with a combined E-value of 2.7e-09. IPB010722C 181-226","Residues 16-85 are 67% similar to a (SYNTHASE ACID LIPOIC LIPOATE IRON-SULFUR LIP-SYN LIPOYL 2.8.1.- LIPOYL-ACYL-CARRIER METAL-BINDING) protein domain (PD123922) which is seen in Q6G401_BARHE.Residues 80-134 are 81% similar to a (SYNTHASE ACID LIPOIC LIPOATE IRON-SULFUR LIP-SYN LIPOYL 2.8.1.- LIPOYL-ACYL-CARRIER METAL-BINDING) protein domain (PD005028) which is seen in LIPA_MYCTU.Residues 135-172 are 84% similar to a (SYNTHASE LIPOATE LIPOYL 2.8.1.- TRANSFERASE LIPOYL-ACYL-CARRIER METAL-BINDING IRON LIPOIC INSERTION) protein domain (PDA02997) which is seen in Q6AFG7_BBBBB.Residues 177-290 are similar to a (SYNTHASE ACID LIPOIC LIPOATE IRON-SULFUR LIP-SYN LIPOYL 2.8.1.- LIPOYL-ACYL-CARRIER METAL-BINDING) protein domain (PD186201) which is seen in LIPA_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 77 to 238 (E_value = 2e-18) place ANA_0902 in the Radical_SAM family which is described as Radical SAM superfamily.","","acid synthetase (lipA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0903","976533","977288","756","10.68","19.60","28072","GTGTGCCGGCGCACCAACGTCGTCTATGGTGTGCCCGTGAGTAGTGCCCAGTCCCCCCAGCCGAAGAAGAAGCGCCGGCTGGCTCAGTACCTTCAGAACATCAAGGACTCCTACACGATCTCGCGGCGGAGCTACCCGTGGATCGGATGGGTGATGCTGGCGGTACTCGCCACCTGCCTCGCCCTGGGGGCCGCTGTCTCCTTCGGCTACGGACTGTCCCTGTGGTACTGGCTGATGGTGGGCATCCTCATGGCGCTCATGATTGACATGGTCATTCTGTCAGTCGTGGTGCGCCGTGCTTCCTTCTCCCAGATCGAGGGAATGCCAGGAGCGGCGAAGGCCGTTCTGGACCAGATCGGTCGGGGCTGGTTTGTGGAGCCCGAGCCCGTGGCCTTCACCAAGGACCAGGACCTCGTGTGGCGGCTGGTGGGACGCCCCGGTGTCGTTCTCATCGCGGAGGGACCCAGCACCCGCACCCGACGCATGTTGGCCGAGGAGGAGCGCAAGGTCCATCGGCTGCTGTCGACCGTTCCCATCCACACCCTTCAGGTGGGCACTGACGCCGGCCAGGTACGCCTGACCGACCTGTCCAAGACACTGCGCCAGCTCCCGACCAAGCCCACGTCACTGACTGACAGCGAGATCACGCAGGTCTCCAAGCGTCTGACGTCGATGGCCGGCAAGAACCTGCCGATCCCCAAGCACATCGATCCCAATCGGGTCCGCCCCGACCGCCGTGCCATGCGCGGGCGCTGA","VCRRTNVVYGVPVSSAQSPQPKKKRRLAQYLQNIKDSYTISRRSYPWIGWVMLAVLATCLALGAAVSFGYGLSLWYWLMVGILMALMIDMVILSVVVRRASFSQIEGMPGAAKAVLDQIGRGWFVEPEPVAFTKDQDLVWRLVGRPGVVLIAEGPSTRTRRMLAEEERKVHRLLSTVPIHTLQVGTDAGQVRLTDLSKTLRQLPTKPTSLTDSEITQVSKRLTSMAGKNLPIPKHIDPNRVRPDRRAMRGR$","Hypothetical protein","Periplasm, Membrane, Extracellular","putative integral membrane protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-93]?$	signal-peptide
tmhmm	$\"[46-68]?$ $\"[74-96]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 31-245 are 58% similar to a (MEMBRANE TRANSMEMBRANE INTEGRAL NARROWLY PROBABLE MLCB22.21 PRECURSOR SIGNAL RV2219/MT2276) protein domain (PD037701) which is seen in Q82AP9_STRAW.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0904","977486","978910","1425","4.94","-25.48","53502","ATGTTCAAGGACGCATCCGAGGCACTGACGTTCATCGAGAAGGAGAATGTCGCGCTGGTCGATGTGCGGTTCTGTGACCTACCCGGCGTCATGCAGCACTTCACTATTCCTGTGGCGGCCTTCAAGGATGAGGCACTCACTGACGGCCTGATGTTTGACGGCTCATCGATCCGAGGCTTCACCGCGATCCACGAGTCAGATATGAAGCTGGTTCCCGATGTGACCACCGCATTCCTGGACCCGTTCCGCGAGGAGAAGACCCTGGTCGTCAACTTCTCGATCGTCGATCCCTTCACGGACGAGGTCTACTCCCGAGACCCCCGCTCGATCGCCGCCAAGGCCGAGGACTACCTGCGCTCCACCGGAATCGCTGACACCTGCTACATCGGGGCCGAGGCCGAGTTCTACCTCTTCGACTCGGTGCGCTACGAGGCCTCACCAGCCGAGTCCTTCTACGCCATCGACTCCTGCGAGGCGGCCTGGAACACCGGGCGAGAGGAGGAGGGCGGCAACAAGGGGTACAAGACCGCTTTCAAGGGCGGCTACTTCCCCGTCTCCCCCAACGATCAGATGGCCGATATCCGGGACCGCATGGTCCGTACCTGCCTCGCCTCCGGACTGGAGATCGAACGGGCTCATCACGAGGTCGGCACTGCCGGACAGCAGGAGATCAACTACCGATTCAGCTCCCTGCTCGCCGCGGGCGACGACATGATGAAGTTCAAGTACATCATCAAGAACGAGGCCTGGCGCAACGGTAAGACGGCCACCTTCATGCCCAAGCCGATCTTCGGTGACAACGGCTCGGGCATGCACACCCACCACTCGCTGTGGAAGGACGGCAAGCCGCTGTTCTTCGACGAGCGGGGCTACGGCCAGCTCTCGGACCTCGCCCGCTGGTACATCGGTGGGATCCTGGCCCACGCCCCGGCGCTGCTGGCCTTCACCAACCCGTCGGTGAACTCCTTCCACCGCCTGGTCCCCGGCTTCGAGGCGCCGGTCAACCTGGTCTACTCGGCCCGCAACCGCTCGGCCTGCATCCGCATCCCGGTCACCGGCTCCTCCCCCAAGGCCAAGCGAGTGGAGTACCGGGTGCCGGATCCCTCCTCCAACCCCTACCTGTGCTTCGCGGCCGTCCTCATGGCCGGTATTGACGGAATCCGCAACCGCATCGAGCCCCGCGAGCCCATCGACAAGGACCTCTACGAGCTGGCTCCCGAGGAGTACTTCGACATCGACAAGCTCCCCGACAGCCTGGACCAGGCGCTGGAGGCACTGGAGGACGACCACGACTTCCTCACCGAGGGAGACGTCTTCACCCCCGACCTCATCGAGACCTGGATCGAGTACAAGCGCACCAACGAGATCGAGCCGCTGCGGCTGCGCCCCCACCCCTACGAGTTCCAGCTCTACTACGACCTGTGA","MFKDASEALTFIEKENVALVDVRFCDLPGVMQHFTIPVAAFKDEALTDGLMFDGSSIRGFTAIHESDMKLVPDVTTAFLDPFREEKTLVVNFSIVDPFTDEVYSRDPRSIAAKAEDYLRSTGIADTCYIGAEAEFYLFDSVRYEASPAESFYAIDSCEAAWNTGREEEGGNKGYKTAFKGGYFPVSPNDQMADIRDRMVRTCLASGLEIERAHHEVGTAGQQEINYRFSSLLAAGDDMMKFKYIIKNEAWRNGKTATFMPKPIFGDNGSGMHTHHSLWKDGKPLFFDERGYGQLSDLARWYIGGILAHAPALLAFTNPSVNSFHRLVPGFEAPVNLVYSARNRSACIRIPVTGSSPKAKRVEYRVPDPSSNPYLCFAAVLMAGIDGIRNRIEPREPIDKDLYELAPEEYFDIDKLPDSLDQALEALEDDHDFLTEGDVFTPDLIETWIEYKRTNEIEPLRLRPHPYEFQLYYDL$","Glutamine synthetase, type I","Cytoplasm","glutamine synthetase, type I","glutamine synthetase; type I ","glutamine synthetase, type I","","Eisenberg D., Almassy R.J., Janson C.A., Chapman M.S., Suh S.W., Cascio D., Smith W.W. Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCO. Cold Spring Harb. Symp. Quant. Biol. 1987. 52:483-490. PMID: 2900091Kumada Y., Benson D.R., Hillemann D., Hosted T.J., Rochefort D.A., Thompson C.J., Wohlleben W., Tateno Y. Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(7):3009-3013. PMID: 8096645Shatters R.G., Kahn M.L. Glutamine synthetase II in Rhizobium: reexamination of the proposed horizontal transfer of DNA from eukaryotes to prokaryotes. J. Mol. Evol. 1989. 29(5):422-428. PMID: 2575672Brown J.R., Masuchi Y., Robb F.T., Doolittle W.F. Evolutionary relationships of bacterial and archaeal glutamine synthetase genes. J. Mol. Evol. 1994. 38(6):566-576. PMID: 7916055","","","

InterPro
IPR004809
Family

Glutamine synthetase type I
TIGR00653	$\"[6-473]T$	GlnA: glutamine synthetase, type I

InterPro
IPR008146
Domain

Glutamine synthetase, catalytic region
PD001057	$\"[113-472]T$	Q6AFH0_BBBBB_Q6AFH0;
PF00120	$\"[104-387]T$	Gln-synt_C
PS00181	$\"[261-276]T$	GLNA_ATP

InterPro
IPR008147
Domain

Glutamine synthetase, beta-Grasp
PF03951	$\"[16-97]T$	Gln-synt_N
PS00180	$\"[52-70]T$	GLNA_1

InterPro
IPR014746
Domain

Glutamine synthetase/guanido kinase, catalytic region
G3DSA:3.30.590.10	$\"[107-474]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.10.20.70	$\"[1-106]T$	no description
PTHR20852	$\"[19-138]T$ $\"[160-473]T$	GLUTAMINE SYNTHETASE
PTHR20852:SF7	$\"[19-138]T$ $\"[160-473]T$	GLUTAMINE SYNTHETASE BACTERIA

","BeTs to 23 clades of COG0174COG name: Glutamine synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0174 is aompkzyqvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 2","***** IPB001637 (Glutamine synthetase class-I, adenylation site) with a combined E-value of 6.2e-227. IPB001637A 7-36 IPB001637B 46-78 IPB001637C 79-127 IPB001637D 171-221 IPB001637E 241-284 IPB001637F 286-315 IPB001637G 316-350 IPB001637H 355-407 IPB001637I 463-472","Residues 15-103 are 76% similar to a (LIGASE GLUTAMINE SYNTHETASE GLUTAMATE--AMMONIA I GS SYNTHETASE TYPE FIXATION NITROGEN) protein domain (PD228027) which is seen in GLN1_FRAAL.Residues 113-472 are similar to a (LIGASE GLUTAMINE SYNTHETASE GLUTAMATE--AMMONIA I SYNTHETASE PROBABLE GS TYPE FAMILY) protein domain (PD001057) which is seen in Q6AFH0_BBBBB.Residues 220-469 are 50% similar to a (GLUTAMINE SYNTHETASE III LIGASE) protein domain (PDA19065) which is seen in Q7NHN6_GLOVI.","","-69% similar to PDB:1F1H CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM WITH THALLIUM IONS (E_value = 2.1E_140);-69% similar to PDB:1F52 CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP (E_value = 2.1E_140);-69% similar to PDB:1FPY CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM WITH INHIBITOR PHOSPHINOTHRICIN (E_value = 2.1E_140);-69% similar to PDB:1LGR INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM (E_value = 2.1E_140);-69% similar to PDB:2GLS REFINED ATOMIC MODEL OF GLUTAMINE SYNTHETASE AT 3.5 ANGSTROMS RESOLUTION (E_value = 2.1E_140);","Residues 16 to 97 (E_value = 4.5e-39) place ANA_0904 in the Gln-synt_N family which is described as Glutamine synthetase, beta-Grasp domain.Residues 104 to 387 (E_value = 1.8e-168) place ANA_0904 in the Gln-synt_C family which is described as Glutamine synthetase, catalytic domain.","","synthetase, type I (glnA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0906","979066","979986","921","4.81","-14.70","31888","ATGAGGATCCGCCATCACGCCTCCCTCGGGCTGGCAGCCACCGCCTGCCTGGTCCTCAGCGGATGCACCAACGCCGCTGACTGGAACGCGAACCGGAGCTCGCAGATCCACTCCTTCGACACCTCGTCGATCCAGGCGCAGCCCGACATCATTGCCAAGCTCCCTCAGGGCGCCCTCGAGGACGGCGTCCTCGACGTGGCCGCCTCCACGGACTACGCGCCGGCCGAGTTCCTCGACCCCTCGGGCACGGCCGTGGGCTACGACGTCGACCTGACCAACGCGATCGCCGCCGTCCTGGGCGTCAAGGGCAAGGTGCACACCGCCGAGTTCGACTCCATCATCGCCTCGATCGGCTCGAAGTACGACGCCGGCATCTCCTCCTTCACCGTCACCCCCGAACGTACCGCGGAGGTCGACATGACCGCCTACATCAACGTGGGCTCGCGATTCAACGTCCAGGCCGGCAACCCCAAGGGCGTCGAGCCCTCCGACCACCTCCAGCTGTGCGGGCGGACCATCGGCGTCCAGGTGGGTACCGCCCAGGAGACCACCATGCGCGACGCCGCCGACAAGTGCGCGCAGGCGGGCAAGCCGGTTCTGTCCGTGCGTTCCTACTCCAAGCAGTCCGAGGCCACCACCGGCCTGGTGGGCGGCACCATCGACGCCACCTACTCCGACTCCACCGTGGCCGGCTACGCCGTCGAGCTGACCGACGGTCAGATCGTCACCCTCGGGGAGATCGAGGACGCCGCCCCCCAGGGGGTGGTGACCGCCAAGGCCGATCCGCAGTTCACCGCCGCGATCCAGGCCGCCATCCAGTACCTCATGGACCACGGCATCTGGCAGAAGATCCTGGACAACTGGGGCGTGAAGGACGCCGCCCTGACCACCGCAGAACTCAATCCCGCAGTGAAGGAGTGA","MRIRHHASLGLAATACLVLSGCTNAADWNANRSSQIHSFDTSSIQAQPDIIAKLPQGALEDGVLDVAASTDYAPAEFLDPSGTAVGYDVDLTNAIAAVLGVKGKVHTAEFDSIIASIGSKYDAGISSFTVTPERTAEVDMTAYINVGSRFNVQAGNPKGVEPSDHLQLCGRTIGVQVGTAQETTMRDAADKCAQAGKPVLSVRSYSKQSEATTGLVGGTIDATYSDSTVAGYAVELTDGQIVTLGEIEDAAPQGVVTAKADPQFTAAIQAAIQYLMDHGIWQKILDNWGVKDAALTTAELNPAVKE$","ABC-type amino acid transport system, periplasmic component","Extracellular, Cytoplasm","secreted protein","K02030 polar amino acid transport system substrate-binding protein","extracellular solute-binding protein, family 3","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670","","","

InterPro
IPR001638
Family

Bacterial extracellular solute-binding protein, family 3
PF00497	$\"[64-291]T$	SBP_bac_3
SM00062	$\"[63-292]T$	PBPb
PS01039	$\"[86-99]?$	SBP_BACTERIAL_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[59-197]T$	no description
PS51257	$\"[1-16]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[9-29]?$	transmembrane_regions

","BeTs to 16 clades of COG0834COG name: ABC-type amino acid transport system, periplasmic componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0834 is a----z--vdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001638 (Bacterial extracellular solute-binding protein, family 3) with a combined E-value of 1.9e-07. IPB001638A 82-91 IPB001638B 109-144","Residues 56-126 are 68% similar to a (ABC AMINO PERIPLASMIC TRANSPORTER ACID BINDING TRANSPORTER ACID-BINDING PROBABLE SIGNAL) protein domain (PD420372) which is seen in Q8G542_BIFLO.Residues 128-197 are 52% similar to a (ABC TRANSPORTER BINDING SUBSTRATE AMINO SOLUTE PERIPLASMIC AGR_L_2813P SYSTEM PROBABLE) protein domain (PD824865) which is seen in Q8G542_BIFLO.Residues 131-290 are 39% similar to a (ABC BLR4463 SUBSTRATE BLL3296 TRANSPORTER TRANSPORTER BINDING SUBSTRATE-BINDING) protein domain (PD866409) which is seen in Q89LT0_BRAJA.Residues 178-288 are similar to a (ABC AMINO TRANSPORTER ACID ACID-BINDING PERIPLASMIC TRANSPORTER BINDING TRANSMEMBRANE SUBSTRATE) protein domain (PD705462) which is seen in Q8G541_BIFLO.Residues 218-303 are similar to a (ABC TRANSPORTER BINDING SUBSTRATE AMINO PERIPLASMIC PLASMID TRANSPORTER ACID PROBABLE) protein domain (PD783534) which is seen in Q8G542_BIFLO.","","-44% similar to PDB:1LAF STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN (E_value = 1.4E_11);-44% similar to PDB:1LAG STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN (E_value = 1.4E_11);-44% similar to PDB:1LAH STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN (E_value = 1.4E_11);-44% similar to PDB:1LST THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A LIGAND (E_value = 1.4E_11);-44% similar to PDB:2LAO THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A LIGAND (E_value = 1.4E_11);","Residues 64 to 291 (E_value = 1.6e-30) place ANA_0906 in the SBP_bac_3 family which is described as Bacterial extracellular solute-binding proteins, family 3.","","protein (glnH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0908","980101","980955","855","9.55","7.13","31278","ATGCTCATCCACGGGCTGGTCACCAATGAGAAGTTCCACTGGTCCACGGTCTGGTTCTTCCTGCGTGAGGTCCACGTGGTCAAGGCCGTCGGCTGGACGCTGCTGCTGACCTTCATGGCGATGGCCATCGGCATCGTGCTGGCGGTCACCACGGCGATCCTGCGCCAATCCTCCAACCCGGTCCTGCGCTGGGTGGCACTGGCCTACCTGTGGTTCTTCCGCGGCACCCCGATCTACACCCAGCTGGTCTTCTGGGGGGCGCTGTCCGCGCTCTACCAGAAGCTGAGTCTGGGAATCCCCTTCGGCCCCGAGCTGCTGACCTTCAAGACGACGACGGTCTTCACCCCCTTCGTCGCGGCGGTCCTGGGGCTGGGCATCAACGAGGGCGCCTATCTGTCCGAGATCGTCCGCTCGGGCCTGAACTCGGTGGACAAGGGCCAGAGCGAGGCCGCCGGAGCCCTGGGCATGAGCAGGGGCCAGATCCTGCGCAGGATCGTCCTGCCCCAGGCGATGAGGGTCATCGTTCCGCCCACCGGCAACGAGACGATCTCCATGCTCAAGACGACCTCCTTGGTCCTGGCGGTCCCCTTCACCCTGGATCTGACCTTCGTCACCAACTCCTACGCGTCGCTGACCTACCAGATCATTCCGCTGCTTCTGGTCGCGGCCATCTGGTACATCATCATCACCTCGATCCTCATGGTGGGACAGCACTACATCGAACGCTATTACGGCAAGGGCTTCGACTCTGACAAGTCCTCCGGCTCCTCGGGCCGGGGCCTGTCGGCCCGCCAGCAGGCCATCCTCAATGCGCACACCACCAAGGACGATCCCTTCCTGGAGGTCACCCCATGA","MLIHGLVTNEKFHWSTVWFFLREVHVVKAVGWTLLLTFMAMAIGIVLAVTTAILRQSSNPVLRWVALAYLWFFRGTPIYTQLVFWGALSALYQKLSLGIPFGPELLTFKTTTVFTPFVAAVLGLGINEGAYLSEIVRSGLNSVDKGQSEAAGALGMSRGQILRRIVLPQAMRVIVPPTGNETISMLKTTSLVLAVPFTLDLTFVTNSYASLTYQIIPLLLVAAIWYIIITSILMVGQHYIERYYGKGFDSDKSSGSSGRGLSARQQAILNAHTTKDDPFLEVTP$","ABC-type amino acid transport system, permease component","Membrane, Cytoplasm","permease protein of ABC transporter system","K02029 polar amino acid transport system permease protein","polar amino acid ABC transporter, inner membrane subunit","","Osuna R., Lienau D., Hughes K.T., Johnson R.C. Sequence, regulation, and functions of fis in Salmonella typhimurium. J. Bacteriol. 1995. 177(8):2021-2032. PMID: 7536730Wilson R.L., Libby S.J., Freet A.M., Boddicker J.D., Fahlen T.F., Jones B.D. Fis, a DNA nucleoid-associated protein, is involved in Salmonella typhimurium SPI-1 invasion gene expression. Mol. Microbiol. 2001. 39(1):79-88. PMID: 11123690Goldberg M.D., Johnson M., Hinton J.C., Williams P.H. Role of the nucleoid-associated protein Fis in the regulation of virulence properties of enteropathogenic Escherichia coli. Mol. Microbiol. 2001. 41(3):549-559. PMID: 11532124Morett E., Bork P. Evolution of new protein function: recombinational enhancer Fis originated by horizontal gene transfer from the transcriptional regulator NtrC. FEBS Lett. 1998. 433(1):108-112. PMID: 9738943Kostrewa D., Granzin J., Stock D., Choe H.W., Labahn J., Saenger W. Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution. J. Mol. Biol. 1992. 226(1):209-226. PMID: 1619650Cheng Y.S., Yang W.Z., Johnson R.C., Yuan H.S. Structural analysis of the transcriptional activation on Fis: crystal structures of six Fis mutants with different activation properties. J. Mol. Biol. 2000. 302(5):1139-1151. PMID: 11183780","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[26-246]T$	BPD_transp_1
PS50928	$\"[30-237]T$	ABC_TM1

InterPro
IPR002197
Domain

Helix-turn-helix, Fis-type
PR01590	$\"[134-151]T$ $\"[151-171]T$	HTHFIS

InterPro
IPR010065
Domain

Amino acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine
TIGR01726	$\"[25-138]T$	HEQRo_perm_3TM: amino acid ABC transporter,

noIPR
unintegrated

unintegrated
signalp	$\"[1-48]?$	signal-peptide
tmhmm	$\"[29-49]?$ $\"[70-92]?$ $\"[111-131]?$ $\"[188-208]?$ $\"[214-236]?$	transmembrane_regions

","BeTs to 15 clades of COG0765COG name: ABC-type amino acid transport system, permease componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0765 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 4-172 are 42% similar to a (TRANSMEMBRANE GLTJ) protein domain (PD995723) which is seen in Q8D312_WIGBR.Residues 69-170 are 66% similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q9F3K6_STRCO.Residues 124-242 are 57% similar to a (MEMBRANE SUPERFAMILY ABC GLUTAMATE/ASPARTATE TRANSMEMBRANE) protein domain (PDA10263) which is seen in Q6FAP0_ACIAD.Residues 124-195 are 62% similar to a (ABC PERMEASE ACID AMINO TRANSPORTER) protein domain (PD965635) which is seen in Q8DK01_SYNEL.Residues 145-242 are 53% similar to a (BLR1679 TRANSMEMBRANE) protein domain (PD758531) which is seen in Q89TU6_BRAJA.Residues 171-214 are 84% similar to a (TRANSMEMBRANE PERMEASE ABC AMINO ACID TRANSPORTER TRANSPORTER SYSTEM MEMBRANE GLUTAMINE) protein domain (PD857674) which is seen in Q8G543_BIFLO.Residues 171-213 are 86% similar to a (TRANSPORTER COMPONENT ABC-TYPE PERMEASE) protein domain (PD955138) which is seen in Q6AA60_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 246 (E_value = 3.9e-23) place ANA_0908 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","protein of ABC transporter system (AL391763)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0909","980952","981752","801","5.67","-5.63","28724","ATGAGCACATCCGCCCAGGCGGCAGCCGCTACGCCCAAGGTCGAGATCAGCGCCCTGCACAAGTTCTTCGGTGAGCTGCACGTGCTGCGGGGCATCGATCTCATCGTCCCACCCGGCTCGGTGACGGTTCTCATCGGCCCGTCGGGCTCGGGAAAGTCGACACTGCTGCGCTGCATCAATGAGCTGGAGTCCATCGACGCCGGCCGGGTCAAGGTCGACGGCGAGCTCATCGGGATGCGTGAGGTCGAGCGCGGTGGTCGCGCCGAGCTGCACGCCCTGTCGGACAAGGCCCGTGCTGCTCAGCGCGCCAAGATCGGCATGGTCTTCCAGCGTTTCAACCTCTTCCCCCACATGACAGCTCTCCAGAACGTCATGGAGGCACCGGTCATGGTCAAGAAGACTCCGAAGGCCAAGGCCCGTGAGCGCGGCATCGAGCTGCTGGAGCGGGTGGGGCTCGGGGATCGCCTCGAGCACTACCCCTCCCAGCTCTCCGGTGGTCAGCAGCAGCGGGTGGCGATCGCCCGGGCTCTGGCCATGGACCCTGAGCTCATGCTCTTCGACGAGCCGACCTCCGCGCTGGATCCCGAACTGGTCGGCGAGGTCCTGCAGGTGATGCAGGACCTCGCCGCCTCCGGCATGACGATGGTCGTGGTCACCCATGAGATGGGCTTCGCCCGGGAGGTGGGTGATCAGCTGATCTTCATGGACGGCGGTGTCATCTGCGAGTCCGGTGACCCCGTGGAGGTCCTGGACAACCCGCAGGCCGAGCGCACCCGGGCCTTCCTCTCCTCGGTCCTGTAG","MSTSAQAAAATPKVEISALHKFFGELHVLRGIDLIVPPGSVTVLIGPSGSGKSTLLRCINELESIDAGRVKVDGELIGMREVERGGRAELHALSDKARAAQRAKIGMVFQRFNLFPHMTALQNVMEAPVMVKKTPKAKARERGIELLERVGLGDRLEHYPSQLSGGQQQRVAIARALAMDPELMLFDEPTSALDPELVGEVLQVMQDLAASGMTMVVVTHEMGFAREVGDQLIFMDGGVICESGDPVEVLDNPQAERTRAFLSSVL$","ABC-type polar amino acid transport system, ATPase component","Cytoplasm, Membrane","ATP-binding protein","putative ABC transporter ATP-binding protein ","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[162-205]T$	Q8CUV1_OCEIH_Q8CUV1;
PF00005	$\"[39-238]T$	ABC_tran
PS50893	$\"[14-262]T$	ABC_TRANSPORTER_2
PS00211	$\"[163-177]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[38-239]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[8-264]T$	no description
PTHR19222	$\"[14-265]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF33	$\"[14-265]T$	GLUTAMATE / GLUTAMINE ABC TRANSPORTER

","BeTs to 15 clades of COG1126COG name: ABC-type polar amino acid transport system, ATPase componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1126 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.1e-48. IPB013563A 28-62 IPB013563B 105-118 IPB013563C 160-187 IPB013563D 214-266***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.2e-36. IPB005074C 28-75 IPB005074D 151-194 IPB005074E 214-234***** IPB005116 (TOBE domain) with a combined E-value of 8.1e-29. IPB005116A 46-62 IPB005116B 103-120 IPB005116C 163-176 IPB005116D 183-202***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3.2e-19. IPB010509B 39-64 IPB010509D 158-202***** IPB010929 (CDR ABC transporter) with a combined E-value of 3.6e-09. IPB010929K 26-70 IPB010929M 160-206 IPB010929A 38-57","Residues 24-124 are 50% similar to a (LIPOPROTEIN ATP-BINDING RELEASING SYSTEM LOLD) protein domain (PDA0I1Q0) which is seen in Q7UH39_RHOBA.Residues 24-124 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 24-246 are 50% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 25-242 are 43% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 25-220 are 44% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 28-209 are 45% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 29-77 are 87% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q8FPP7_COREF.Residues 29-222 are 49% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 32-240 are 46% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 41-242 are 44% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD738131) which is seen in Q830L1_ENTFA.Residues 44-236 are 46% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 100-240 are 54% similar to a (COMPONENT ABC ATPASE ATP-BINDING TRANSPORTER) protein domain (PDA0I0K5) which is seen in Q74HP7_LACJO.Residues 108-148 are 85% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT MEMBRANE ATPASE AMINO ACID SYSTEM) protein domain (PD007166) which is seen in Q82IZ8_STRAW.Residues 109-251 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 114-232 are 48% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA184H5) which is seen in Q6W139_RHISN.Residues 117-240 are 52% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 139-252 are 53% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 140-242 are 61% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 141-220 are 57% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 144-239 are 58% similar to a (BLR8070 ATP-BINDING) protein domain (PD727315) which is seen in Q89BS8_BRAJA.Residues 145-240 are 64% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 146-240 are 56% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 147-205 are 66% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD436020) which is seen in Q9A7G4_CAUCR.Residues 147-240 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA106Q1) which is seen in Q73R37_TREDE.Residues 148-254 are 57% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 148-238 are 60% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J201) which is seen in Q73M59_TREDE.Residues 149-220 are 67% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8FAX9_ECOL6.Residues 149-251 are 53% similar to a (APRD ATP-BINDING) protein domain (PDA0I303) which is seen in Q89EV0_BRAJA.Residues 150-240 are 59% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 150-221 are 72% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q87LE8_VIBPA.Residues 150-252 are 61% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 151-243 are 58% similar to a (ATP-BINDING TRANSPORTER COBALT ABC PROTEIN) protein domain (PD944400) which is seen in Q72D73_DESVH.Residues 152-249 are 57% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 155-232 are 57% similar to a (ATP-BINDING TRANSPORTER ABC OLIGOPEPTIDE) protein domain (PDA189L6) which is seen in Q8TRD5_METAC.Residues 155-245 are 49% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.Residues 160-240 are 61% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z9) which is seen in Q8DM53_SYNEL.Residues 161-240 are 67% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K1H6) which is seen in Q73MA6_TREDE.Residues 161-250 are 63% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.Residues 162-240 are 63% similar to a (COMPONENT METHYL M-REDUCTASE COENZYME ATP-BINDING) protein domain (PD462863) which is seen in Q93RF2_TREMD.Residues 162-205 are identical to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q8CUV1_OCEIH.Residues 164-255 are 58% similar to a (SUGAR ABC ATP ATP-BINDING BINDING) protein domain (PDA0I5K8) which is seen in Q982N2_RHILO.Residues 171-220 are 80% similar to a (ATP-BINDING ABC ACID AMINO TRANSPORTER) protein domain (PD767512) which is seen in Q8DHR3_SYNEL.Residues 184-220 are 91% similar to a (PREDICTED ATP-BINDING) protein domain (PDA188F3) which is seen in Q8TSK7_METAC.Residues 205-265 are 57% similar to a (RSC1743) protein domain (PD750155) which is seen in Q8XYL5_RALSO.","","-66% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 8.9E_65);-54% similar to PDB:1G29 MALK (E_value = 1.1E_33);-60% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 4.0E_33);-60% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 9.0E_33);-53% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 5.8E_32);","Residues 39 to 238 (E_value = 6.6e-66) place ANA_0909 in the ABC_tran family which is described as ABC transporter.","","protein (AL391763)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0910","982419","981766","654","4.89","-10.91","22795","GTGAGGCTCATTCTTGTACGCCACGGTCGCACCGAGGCCAATGTCATGCAGGCACTCGACACCGCCTTCCCCGGAAATCCCCTGGATGAGGTAGGGCTGGAGCAGGCCGACGGATTGCCGGACCGTTTGGACAAGGCCGGCCTCCTCCACGGGCTGGGGTCACTGTGGGTCTCCCCGATCCTGCGCGCCAGGCAGACCATCGCCCCCATCGAGGCCGCCACCGGCCTGAGCGCCACTGTCGACTCGGGACTGCGTGAGGTGCTGGCCGCCGACCTGGAGATGAACACCGACGCGCGCTCGGTGGCCTGCTACGTGGACACAACCCGGGCCTGGATGGCGGGGCGCCCCGCCTGCCGCATCCCCGGCTCTCCGGAGGACGGGCACGACACGCTTCAGCGCTTCGACGAGGCCGTTGGCCGCATCTGTGAGCAGGCCGCCGGGGCGGGGGACTCATCGGCCCTGATCGTCTCCCACGGCACCGCGCTGCGCCTGTGGACCTCCCTGAGGGCCGCAGCTGGAGGCGGCGTGGACCCGCTGTGGGTCGCTGACCGCCCCATGCACAACACCGGGATCACCGTCGTCGACGGCGATCCCGGTGGTGGGTGGAGCCTGGCCTCCTGGGATGACGGGGCCTGGGACCAGACCCCCTCCTGA","VRLILVRHGRTEANVMQALDTAFPGNPLDEVGLEQADGLPDRLDKAGLLHGLGSLWVSPILRARQTIAPIEAATGLSATVDSGLREVLAADLEMNTDARSVACYVDTTRAWMAGRPACRIPGSPEDGHDTLQRFDEAVGRICEQAAGAGDSSALIVSHGTALRLWTSLRAAAGGGVDPLWVADRPMHNTGITVVDGDPGGGWSLASWDDGAWDQTPS$","Phosphoglycerate mutase","Cytoplasm","putative isomerase","phosphoglycerate mutase","Phosphoglycerate mutase","","Le Boulch P., Joulin V., Garel M.C., Rosa J., Cohen-Solal M. Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA. Biochem. Biophys. Res. Commun. 1988. 156(2):874-881. PMID: 2847721White M.F., Fothergill-Gilmore L.A. Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae. FEBS Lett. 1988. 229(2):383-387. PMID: 2831102","","","

InterPro
IPR013078
Domain

Phosphoglycerate mutase
PF00300	$\"[2-165]T$	PGAM

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1240	$\"[2-209]T$	no description
PIRSF001490	$\"[1-217]T$	Cofactor-dependent phosphoglycerate mutase
PTHR23029	$\"[1-214]T$	PHOSPHOGLYCERATE MUTASE

","BeTs to 7 clades of COG0406COG name: Fructose-2,6-bisphosphataseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0406 is ---p--yqvdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 3-164 are 57% similar to a (PHOSPHOGLYCERATE MUTASE PGAM ISOMERASE GLYCOLYSIS PHOSPHOGLYCEROMUTASE BPG-DEPENDENT 23-BISPHOSPHOGLYCERATE-DEPENDENT DPGM FAMILY) protein domain (PD002638) which is seen in Q9F3Q7_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 165 (E_value = 6.9e-23) place ANA_0910 in the PGAM family which is described as Phosphoglycerate mutase family.","","isomerase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0911","986129","982515","3615","7.95","8.69","129472","GTGAGAGACCGCAGCGAGAAGCGCGCGCCGATCGGATCACCCTCCCGGCACAGCTCCTCGCCCAGGACCCTGCTGCTGCGGGCCGGATTCCACGACGCCGCTCGTGCCGGAAGGCTTCTGGGCGACCCGGCGCTGCTGCCCTTCCTTTTGGACGATCCTCAGAGCGACGACGTCGGCGAAGAGGGTGTCATCCCCGGCGGATTCGCCTCAGCGGACCGCTCCAGGCGGCCGGGCGGCCGACCTGCCGAGGTGCGGCTCGGACCGGCGCGTGAGGAGCTCATCGACTCCCTGGCTCTCACCTCGGATCCTGACATGGCTCTGCTCAGCCTTGTCCGGCTCGCCGAGGCCGCGGGCACCGCCGAATCGGGCCACCTGGCTTCGGCGGGTGGTGTCGAGGCAGGGTGCGCGACGAGGCCGGCAGTACTTCTGCGGAGCGTCATGAGCGAACCGGCCGCAGGGCCGCGTGAGCACAGACGCCGCCTGCTGGCGGTCCTGGGCGCCTCGCAGGCCCTGGGTGACTTCCTCGTGGCCCATCCCGAGCACCTCACCGCGCTCGCGCCTGACAGGGCATGGGACGCTCCGCAGGAGCCCAGCGCCGGTGAGGCGCTGCGACGGGCGGTGGGCGACGTGCTGGGGCGGGCCGACCCCGCGGATGCGGCCCCCTCGGACAGCGATAAGGGACCCTCGCAGCCGGGAGACGCTGCCGTCGGCCGGGCGACCGCGGCGCTGCGACGCGCCTACCGGGACCGGCTCACGGCGATCGTCGCCGATGACCTCACCAGCGCCGACCCGATCGAGCACGTCCCCACCGTGTGCCGCCGCATGACCGCTCTGGCCGATGCCGCCCTGGACGCGGCCTTGCTCGTGGCCCGTGCCGCCGTCGGACCGCGGGCCGATGAGGTGGCCCTTGCCGTGATCGCCATGGGAAAGACGGGGGCCCGAGAGCTCAACTACGTCTCGGACGTCGACGTCGTCTACGTCGTCGGCCCCGCCCACGATCCACATGACGCTCAGGAGCCGATCAGCGAGGAGCAGCTCGTGGAGGTCGGCACGCACCTGGCCACCGAGCTCGCCCACGTCGTCTCCGCCACCGCGCCCGAGCCGCCCCTGTGGCCACTGGACACGGCGCTACGGCCTGAGGGCAAGGACGGTGCGCTCGTGCGCACTCTCGATTCCCACCTGGGCTACTACCGCAGATGGGCCGCCTCCTGGGAGTTCCAGGCCCTGCTCAAGGCCAGGGCCTGCGCCGGGGACCTCGAGCTCGGCGCTCGCTACGAGCAGGGCGTCGCACCCTATGTGTGGGAGGCCAGCCGACGGGAGAACTTCGTCGAGGACGCCCGGGCCATGCGGCGCCGGGTGGAGAAGGAGTCCGTGCCACGCGGCGGAGTGGACCGGCGTATCAAGCTGGGCCCTGGGGGACTGCGGGACGTCGAGTTCACCGTCCAGCTCCTCCAGCTCGTCCATGGCCGTTCCGACGAGAGTCTGCGCGTGCGCGGCACCCTGGAGGCCCTCGACGCTCTCAGCGCGGGCGGATACGTCAGCCGCACCGATGCCGCGGCCTTGAGCGGCTGCTACAAGGCCCTGCGGCTGCTGGAGCATCGCAGCCAGCTCTTCCGGCTGCGCCGCACCCACAACCTTCCTGACAAGGAGGAGGATCTGCGCCGCATCGAGCGGGGCGTCAGCAACTGCCTGGGCCACGCAGACAGCCTCTGGGAGGACTTCAAGGACCTGCGTCGGCGGGTACGGGCCCTCCACCAGGAGATCTACTACCGTCCCCTGCTGGCCTTCGCGGCCGCCCTCAGCGCCGATGAGATGGCTCTGAGTCCTCAGGCGGCGCGCGAGCGTCTTGCCGCCGTCGGCTACGCGGACCCCGACGGCGCCCTGCGCCACATCCAGGCCCTCACCGAGGGGGTCAGTCGTCGCGCCGCGATCCAGCGCCAGCTGTTGCCGGTCATCATCGGCTGGATCGGTGAGGGAGCCGACCCCGACTTCGGTCTGCTCTCCTTCCGGCGGCTGTCTGAGGCCATTGGGGGCTCGCACTGGTACCTGGCCATGCTGCGGGACTCCCCGGTGGCGGCACGCAGACTGTGTCAGGTCCTCTCCAGCGCACACTGGGCCACCGAACGCCTCGCGGAGTTCCCCGAGTCCATCGCCTGGCTCGACGACGACGGCGAGCTCGCCCCCCGCCGATCCGGTGCCCTGGCGGAGGAGATCGCCGCCGTCCTGCGCCGTCGCAGCCTGACCGGCCCCGATGACGCTGCTCTTACCGAGCAGGCACTCGAGGCGGTCCAGGCGATCCTGAGAGTGCGCGCCCGTGAGGAAGTGCGTGCCTCACTGGCGGACTGCCTGGACGGCATCGACCCTGAACGCACCGCCTCCATCCTCTCCGACGCCACCGACGCGGTCCTGGAGGGGGCACTGACCGTGGCCACCGGTCTGGTCATCGCCCAGCGCGACGGGGTGGAGGCAGTCTCCGCGGGGCCCGACGCAGGCGGGTGCTGGCAGGCCGCTCGCGCCCGCCACGCCATCATCGCCATGGGGCGCCTGGGAGGTCGCGAGATCGGGTACGCCTCCGACGCGGACGTCCTCTTCGTTCACCAGGTCCGTGACGGGGCGGGGGAGGAGGCCGCCGCACAAGAGGCCGAGGCCGTCGCCAAGCAGGTCATGGGACTGCTGGCCGCGGCGCTCCCGCACCCCCTTGAGGTGGACTGCGGCCTGCGGCCCGAGGGCCGCAACGGTGTCATGAGCCGCTCGCTGGACGCCTACCGCGAGTACTACGGCCGCTGGTCCGCCCTGTGGGAGCGCCAGGCGCTGTTGCGCGCCCGTCCCTGCAGCGGAGACCGCGAACTGGGCCGGCGCTTCGAGGAGCTCGTCAACCCGTTGCGCTGGGCGCAGAAGGGACTGGCGCCCCAGGACCTGCGGGAGATCCGCAGGATCAAGGCGCGGGTGGAGGCCGAGCGCCTGCCCCGGGGCATCAACCCGGCTCGCCATCTCAAGCTCGGCCCCGGGGGGCTCAGTGACGTGGAATGGAGCGCCCAAGTGCTTCAGCTCGCCCACGCCGGCCGGATACCCCAGCTTCGGACCACCTCGACCGTCGGCGCGCTCCAGGCCGCGGTTCAGGCGGGGGTCCTGAGCGCGGACGACGGAGGAGAGCTGATCGCGGCCTGGATCCTGGCCAGCCGCCTGCGCTCGGCGATCGTCCTGGGAACCGGACGCGCCTCGGGGCCGCGCTCCCAGGTCCTCCCCATCCAGATTCGGGAGATCCGCCTGGTGGGGCGCCTCATCGGCCTGGGTGCGGGCAGGGAGCGAGAGCTTGAGGATCTTTACCGCCGCAGTGCCCGCCACGCGCGCGCAGTGGCCGAGCGCATTGTCTTCGCCGACGCCGCCGCCCACGGCTCGGCCGTCTCGGCGCCGTCGAGCACTGCGTCGGCGGCTCGGCCGCACAGCCTGAAGTCGCCGTCGCGTTCATCAGGAACGTCCCGGAGCCCTCGCGCACAGTCCCGTCGGGATTCCGGGACGGCAGCCTCCAAGAGCACCAGTTCCAAGGGATCCAGGCGGGTGAACCGCCCCCGTGCTACCAGAAGGCGGCCGGAGGGGCCCTATCCCTGGAGTTGA","VRDRSEKRAPIGSPSRHSSSPRTLLLRAGFHDAARAGRLLGDPALLPFLLDDPQSDDVGEEGVIPGGFASADRSRRPGGRPAEVRLGPAREELIDSLALTSDPDMALLSLVRLAEAAGTAESGHLASAGGVEAGCATRPAVLLRSVMSEPAAGPREHRRRLLAVLGASQALGDFLVAHPEHLTALAPDRAWDAPQEPSAGEALRRAVGDVLGRADPADAAPSDSDKGPSQPGDAAVGRATAALRRAYRDRLTAIVADDLTSADPIEHVPTVCRRMTALADAALDAALLVARAAVGPRADEVALAVIAMGKTGARELNYVSDVDVVYVVGPAHDPHDAQEPISEEQLVEVGTHLATELAHVVSATAPEPPLWPLDTALRPEGKDGALVRTLDSHLGYYRRWAASWEFQALLKARACAGDLELGARYEQGVAPYVWEASRRENFVEDARAMRRRVEKESVPRGGVDRRIKLGPGGLRDVEFTVQLLQLVHGRSDESLRVRGTLEALDALSAGGYVSRTDAAALSGCYKALRLLEHRSQLFRLRRTHNLPDKEEDLRRIERGVSNCLGHADSLWEDFKDLRRRVRALHQEIYYRPLLAFAAALSADEMALSPQAARERLAAVGYADPDGALRHIQALTEGVSRRAAIQRQLLPVIIGWIGEGADPDFGLLSFRRLSEAIGGSHWYLAMLRDSPVAARRLCQVLSSAHWATERLAEFPESIAWLDDDGELAPRRSGALAEEIAAVLRRRSLTGPDDAALTEQALEAVQAILRVRAREEVRASLADCLDGIDPERTASILSDATDAVLEGALTVATGLVIAQRDGVEAVSAGPDAGGCWQAARARHAIIAMGRLGGREIGYASDADVLFVHQVRDGAGEEAAAQEAEAVAKQVMGLLAAALPHPLEVDCGLRPEGRNGVMSRSLDAYREYYGRWSALWERQALLRARPCSGDRELGRRFEELVNPLRWAQKGLAPQDLREIRRIKARVEAERLPRGINPARHLKLGPGGLSDVEWSAQVLQLAHAGRIPQLRTTSTVGALQAAVQAGVLSADDGGELIAAWILASRLRSAIVLGTGRASGPRSQVLPIQIREIRLVGRLIGLGAGRERELEDLYRRSARHARAVAERIVFADAAAHGSAVSAPSSTASAARPHSLKSPSRSSGTSRSPRAQSRRDSGTAASKSTSSKGSRRVNRPRATRRRPEGPYPWS$","Glutamate-ammonia-ligase adenylyltransferase","Cytoplasm","glutamate-ammonia-ligase adenylyltransferase","glutamate-ammonia-ligase adenylyltransferase ","[Glutamate--ammonia-ligase] adenylyltransferase","","","","","

InterPro
IPR005190
Domain

Glutamate-ammonia ligase adenylyltransferase
PF03710	$\"[158-428]T$ $\"[693-957]T$	GlnE

","BeTs to 7 clades of COG1391COG name: Glutamine synthetase adenylyltransferaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones] Functional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1391 is -------q--r---efgh-n-j----Number of proteins in this genome belonging to this COG is 1","***** IPB005190 (Glutamate-ammonia ligase adenylyltransferase) with a combined E-value of 6.2e-102. IPB005190A 271-301 IPB005190B 303-326 IPB005190C 429-463 IPB005190D 466-499 IPB005190E 523-547 IPB005190F 604-635 IPB005190G 843-865 IPB005190H 921-954","Residues 762-1074 are 60% similar to a (TRANSFERASE NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE LIGASE GLUTAMATE-AMMONIA-LIGASE URIDYLYLTRANSFERASE ENZYME PROTEIN-PII PII REMOVING) protein domain (PD008864) which is seen in Q6A9Z4_PROAC.Residues 347-407 are 68% similar to a (TRANSFERASE ADENYLYLTRANSFERASE GLUTAMATE-AMMONIA-LIGASE LIGASE NUCLEOTIDYLTRANSFERASE ADENYLTRANSFERASE GLUTAMINE SYNTHETASE) protein domain (PD882284) which is seen in Q6AFH2_BBBBB.Residues 404-536 are 51% similar to a (ADENYLYLTRANSFERASE TRANSFERASE GLUTAMATE-AMMONIA-LIGASE LIGASE NUCLEOTIDYLTRANSFERASE) protein domain (PDA088C8) which is seen in Q7NW95_CHRVO.Residues 491-548 are 68% similar to a (ADENYLYLTRANSFERASE TRANSFERASE GLUTAMATE-AMMONIA-LIGASE LIGASE NUCLEOTIDYLTRANSFERASE) protein domain (PDA088C4) which is seen in Q8G654_BIFLO.Residues 543-714 are 65% similar to a (ADENYLYLTRANSFERASE TRANSFERASE NUCLEOTIDYLTRANSFERASE LIGASE GLUTAMATE-AMMONIA-LIGASE SYNTHETASE GLUTAMINE FOR GLUTAMINE- ENZYME) protein domain (PD644677) which is seen in Q6AFH2_BBBBB.Residues 596-865 are 46% similar to a (ADENYLYLTRANSFERASE TRANSFERASE GLUTAMATE-AMMONIA-LIGASE LIGASE NUCLEOTIDYLTRANSFERASE) protein domain (PDA0E1H5) which is seen in Q7UPN2_RHOBA.Residues 762-1074 are 60% similar to a (TRANSFERASE NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE LIGASE GLUTAMATE-AMMONIA-LIGASE URIDYLYLTRANSFERASE ENZYME PROTEIN-PII PII REMOVING) protein domain (PD008864) which is seen in Q6A9Z4_PROAC.","","-45% similar to PDB:1V4A Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase (E_value = 7.8E_20);-40% similar to PDB:2J9I LENGSIN IS A SURVIVOR OF AN ANCIENT FAMILY OF CLASS I GLUTAMINE SYNTHETASES IN EUKARYOTES THAT HAS UNDERGONE EVOLUTIONARY RE-ENGINEERING FOR A TISSUE-SPECIFIC ROLE IN THE VERTEBRATE EYE LENS. (E_value = 7.8E_20);","Residues 158 to 428 (E_value = 3.7e-52) place ANA_0911 in the GlnE family which is described as Glutamate-ammonia ligase adenylyltransferase.Residues 693 to 957 (E_value = 3.1e-16) place ANA_0911 in the GlnE family which is described as Glutamate-ammonia ligase adenylyltransferase.","","adenylyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0912","987479","986148","1332","5.01","-23.70","49470","ATGGACAAGCAGCAGGAGTACGTGCTCCGAGCCATCGAGGAACGCGACATCAGCTTCATCCGCCTGTGGTTCACCGACGTCTCCGGACAGCTCCAGTCCGTGGCCATCGCACCGGCCGAGGTCGAGAGCGCCTTCGAGGAGGGCATCGGCTTCGACGGATCGGCGATCGAGGGACTGACGCGCGTCTTCGAGTCAGACATGCTCCTGGCCCCCGACCCCTCCACCTTCCAGATGCTGCCCTGGCGGGACGGGGACAACGGCGTGGCCCGCATGTTCTGCGATGTCCTCACGCCCGACGGCGAGCCCGCCCGCACCGACCCGCGCTCCGTGCTCGAGCGTCAGCTAGCTCGGGTCGCCGAGGCCGGCTTCACCTGCTACATCCACCCGGAGATCGAGTTCTACCTGGTCAACCGTGACGCCGACGGGCGCATCCGCCCCACTGACGACGCCGGCTACTTCGACCACGTGCCCGGGGGCACCGCCCACGAGTTCCGCCGCCACGCCATCCTCATGCTCGAGCAGATGGGGATCTCGGTGCAGTTCTCCCACCATGAGGGTGGCCCTGGCCAGAACGAGATCGATCTGCGCTTCGCCGACGCCCTGTCCATGGCGGACAACATCATGACCTTCCGCGCCGTCGTGGAGGAGGTGGCACTCAAGGAAGGCTGCTTGGCTACCTTCATGCCCAAGCCCTTCCCCGACCAGTTCGGCTCGGGCATGCACACCCACTTCTCCCTGTTCGAGGGTGACCGCAACGCCTTCTTCGACCCGTCCGGCCAGTACCAGCTCTCCGCCACCGGTCGCTCCTTCATCGCCGGCCTGCTGCACCACGCCTCGGAGATCACGGCTGTCACCAACCAGCACGTCAACTCCTACAAGCGCCTGTGGGGAGGGGATGAGGCCCCCAGCTACGTGTGCTGGGGCCACAACAACCGCTCCGCCCTGGTGCGCGTGCCCATGCACAAGCCCGGCAAGGCCCAGTCCGCGCGCGTGGAGTTCCGCGGCATCGACTCCTCGGCCAACCCCTACCTGGCTTACGCGGTCATCCTGGCAGCGGGGCTCAAGGGCATCGAGGAGGGCTACGAGCTTCCCCCCGAGGCCGAGGACGACGTGTGGGCACTGTCCGAGATGGAGCGCAAGGCCCTGGGGATCCACGCCCTGCCCACCTCCCTCAAGAGCGCGGTGGCCGCCATGGAGCGCTCCGACCTGGTGGCTGACACCTTTGGTGAGGACACCTTCGAGTTCTTCCTGCGCAACAAGCGCCGCGAGTACCGGGCCTACGACGCCCAGGTCACCGACTTCGAGATCAGCCAGTTCTTCCCGCGAGCCTGA","MDKQQEYVLRAIEERDISFIRLWFTDVSGQLQSVAIAPAEVESAFEEGIGFDGSAIEGLTRVFESDMLLAPDPSTFQMLPWRDGDNGVARMFCDVLTPDGEPARTDPRSVLERQLARVAEAGFTCYIHPEIEFYLVNRDADGRIRPTDDAGYFDHVPGGTAHEFRRHAILMLEQMGISVQFSHHEGGPGQNEIDLRFADALSMADNIMTFRAVVEEVALKEGCLATFMPKPFPDQFGSGMHTHFSLFEGDRNAFFDPSGQYQLSATGRSFIAGLLHHASEITAVTNQHVNSYKRLWGGDEAPSYVCWGHNNRSALVRVPMHKPGKAQSARVEFRGIDSSANPYLAYAVILAAGLKGIEEGYELPPEAEDDVWALSEMERKALGIHALPTSLKSAVAAMERSDLVADTFGEDTFEFFLRNKRREYRAYDAQVTDFEISQFFPRA$","Glutamine synthetase, type I","Cytoplasm","glutamine synthetase, type I","glutamine synthetase; type I ","glutamine synthetase, type I","","Eisenberg D., Almassy R.J., Janson C.A., Chapman M.S., Suh S.W., Cascio D., Smith W.W. Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCO. Cold Spring Harb. Symp. Quant. Biol. 1987. 52:483-490. PMID: 2900091Kumada Y., Benson D.R., Hillemann D., Hosted T.J., Rochefort D.A., Thompson C.J., Wohlleben W., Tateno Y. Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(7):3009-3013. PMID: 8096645Shatters R.G., Kahn M.L. Glutamine synthetase II in Rhizobium: reexamination of the proposed horizontal transfer of DNA from eukaryotes to prokaryotes. J. Mol. Evol. 1989. 29(5):422-428. PMID: 2575672Brown J.R., Masuchi Y., Robb F.T., Doolittle W.F. Evolutionary relationships of bacterial and archaeal glutamine synthetase genes. J. Mol. Evol. 1994. 38(6):566-576. PMID: 7916055","","","

InterPro
IPR004809
Family

Glutamine synthetase type I
TIGR00653	$\"[6-441]T$	GlnA: glutamine synthetase, type I

InterPro
IPR008146
Domain

Glutamine synthetase, catalytic region
PD001057	$\"[124-369]T$	Q6AFH3_BBBBB_Q6AFH3;
PF00120	$\"[104-357]T$	Gln-synt_C

InterPro
IPR008147
Domain

Glutamine synthetase, beta-Grasp
PF03951	$\"[16-98]T$	Gln-synt_N

InterPro
IPR014746
Domain

Glutamine synthetase/guanido kinase, catalytic region
G3DSA:3.30.590.10	$\"[107-442]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.10.20.70	$\"[1-106]T$	no description
PTHR20852	$\"[19-441]T$	GLUTAMINE SYNTHETASE
PTHR20852:SF7	$\"[19-441]T$	GLUTAMINE SYNTHETASE BACTERIA

","BeTs to 23 clades of COG0174COG name: Glutamine synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0174 is aompkzyqvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 2","***** IPB001637 (Glutamine synthetase class-I, adenylation site) with a combined E-value of 2.3e-91. IPB001637A 7-36 IPB001637B 45-77 IPB001637C 79-127 IPB001637D 141-191 IPB001637E 210-253 IPB001637F 255-284 IPB001637G 285-319 IPB001637H 325-377","Residues 14-102 are 88% similar to a (LIGASE GLUTAMINE SYNTHETASE GLUTAMATE--AMMONIA I GS SYNTHETASE TYPE FIXATION NITROGEN) protein domain (PD228027) which is seen in Q8G4S3_BIFLO.Residues 20-80 are 83% similar to a (LIGASE GLUTAMINE SYNTHETASE GS GLUTAMATE--AMMONIA) protein domain (PD755030) which is seen in Q9AEL4_CORGL.Residues 24-123 are 50% similar to a (462AA LONG GLUTAMINE SYNTHETASE LIGASE) protein domain (PD787032) which is seen in Q9Y9Z7_AERPE.Residues 26-229 are 43% similar to a (GLUTAMINE SYNTHETASE LIGASE) protein domain (PD627647) which is seen in Q92MN4_RHIME.Residues 66-124 are 64% similar to a (LIGASE GLUTAMINE SYNTHETASE PROBABLE III FAMILY SYNTHETASE DIOXYGENASE SYNTHASE GLUTAMATE-AMMONIA) protein domain (PD488431) which is seen in Q9NYJ0_HUMAN.Residues 124-369 are 83% similar to a (LIGASE GLUTAMINE SYNTHETASE GLUTAMATE--AMMONIA I SYNTHETASE PROBABLE GS TYPE FAMILY) protein domain (PD001057) which is seen in Q6AFH3_BBBBB.Residues 165-436 are 51% similar to a (GLUTAMINE SYNTHETASE III LIGASE) protein domain (PDA19065) which is seen in Q7NHN6_GLOVI.Residues 401-441 are 75% similar to a (GLUTAMINE SYNTHETASE LIGASE II TYPE I PROBABLE SYNTHASE SYNTHETASE) protein domain (PD497199) which is seen in Q9RDS6_STRCO.","","-47% similar to PDB:1HTO CRYSTALLOGRAPHIC STRUCTURE OF A RELAXED GLUTAMINE SYNTHETASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 3.2E_55);-47% similar to PDB:1HTQ Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis (E_value = 3.2E_55);-47% similar to PDB:2BVC CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS GLUTAMINE SYNTHETASE IN COMPLEX WITH A TRANSITION STATE MIMIC (E_value = 3.2E_55);-49% similar to PDB:1F1H CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM WITH THALLIUM IONS (E_value = 2.3E_53);-49% similar to PDB:1F52 CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP (E_value = 2.3E_53);","Residues 16 to 98 (E_value = 1.3e-15) place ANA_0912 in the Gln-synt_N family which is described as Glutamine synthetase, beta-Grasp domain.Residues 104 to 357 (E_value = 7.1e-124) place ANA_0912 in the Gln-synt_C family which is described as Glutamine synthetase, catalytic domain.","","synthetase, type I (glnA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0914","987682","988527","846","5.61","-5.62","28977","ATGGCTACACCCGAGTCCCCTTACGGTACGTCCGCTCCCGCCGTCGCAGGCGGTAAGCCCGTGCGCGTTCATCACCTGGCGGCTGCCAAGAAGGACGGCACCAAGCTGGTCATGCTCACCGCCTACGACGCCGTGACCGCCCAGATCCTGGATGCCGCGGGAACCGACCTGCTGCTGGTGGGCGACTCCATCGGCAACGTCATGCTGGGGCATGACTCCACGCTGCCGGTGGAGCTTGACGAGATGGTAGTGGCCACCCGCTCGGTGGCCAGGGCGACCAGGCGCGCCCTGGTTGTGGCCGACCTCCCCTTCGGCACGTACGAGGCCGGTCCGGAGCAGGCACTGGCCAGCGCGGTACGTCTCATGAAGGCCGGGGCCAACGCCGTCAAGCTCGAGGGCGGCAGCCCCCGGGCAGCCAGCGTGAGGGCACTGGCCCAGGCGGGCATTCCGGTGGTGGGGCACCTGGGGTTTACTCCACAGAGCGTCAACATGCTCGGCGGCTTCCGGGTTCAGGGCCGTGGCGAGGCCGCTGACGTGCTGCTGGCCGACGCGCAAGCACTGGCCGAAGCGGGGGCGGTCGCCCTGGTCCTGGAGATGGTGCCCGAGCCCCTGGCCGCGCGCGTCACCGAGTCGCTCACGATCCCCACGATCGGTATCGGCGCTGGCGCGCGCTGCGACGGTCAGGTCCTGGTGTGGACGGACATGGCCGGGATGACGGACTGGTCTCCGCGCTTCGCCCACCAGTTCGGACAAGTCGGCGAGGCCCTCAGGCAGGCGGCCGCCGACTACGGGACCGCGGTACGCGAGGAGTCCTTCCCCGCGGAGAAGCACTGGTTCAGCTCCTGA","MATPESPYGTSAPAVAGGKPVRVHHLAAAKKDGTKLVMLTAYDAVTAQILDAAGTDLLLVGDSIGNVMLGHDSTLPVELDEMVVATRSVARATRRALVVADLPFGTYEAGPEQALASAVRLMKAGANAVKLEGGSPRAASVRALAQAGIPVVGHLGFTPQSVNMLGGFRVQGRGEAADVLLADAQALAEAGAVALVLEMVPEPLAARVTESLTIPTIGIGAGARCDGQVLVWTDMAGMTDWSPRFAHQFGQVGEALRQAAADYGTAVREESFPAEKHWFSS$","3-methyl-2-oxobutanoate hydroxymethyltransferase","Cytoplasm","3-methyl-2-oxobutanoatehydroxymethyltransferase","3-methyl-2-oxobutanoate hydroxymethyltransferase ","3-methyl-2-oxobutanoate hydroxymethyltransferase","","Kurtov D., Kinghorn J.R., Unkles S.E. The Aspergillus nidulans panB gene encodes ketopantoate hydroxymethyltransferase, required for biosynthesis of pantothenate and Coenzyme A. Mol. Gen. Genet. 1999. 262(1):115-120. PMID: 10503542","","","

InterPro
IPR003700
Family

Ketopantoate hydroxymethyltransferase
PTHR20881	$\"[1-279]T$	3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE
PF02548	$\"[19-276]T$	Pantoate_transf
TIGR00222	$\"[19-280]T$	panB: 3-methyl-2-oxobutanoate hydroxymethyl

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.60	$\"[18-279]T$	no description

","BeTs to 17 clades of COG0413COG name: Ketopantoate hydroxymethyltransferaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0413 is -o--kzyqvdr-bcefg-snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003700 (Ketopantoate hydroxymethyltransferase) with a combined E-value of 6.6e-100. IPB003700A 54-92 IPB003700B 129-173 IPB003700C 187-238 IPB003700D 243-279","Residues 1-279 are 64% similar to a (METHYLTRANSFERASE TRANSFERASE 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE) protein domain (PDA014M1) which is seen in Q729A6_DESVH.Residues 9-277 are 62% similar to a (TRANSFERASE HYDROXY-METHYL-TRANSFERASE-LIKE 3-METHYL-2-OXOBUTANOATE) protein domain (PD445501) which is seen in Q9AWZ8_EEEEE.Residues 12-277 are 61% similar to a (TRANSFERASE HYDROXY-METHYL-TRANSFERASE-LIKE 3-METHYL-2-OXOBUTANOATE) protein domain (PD435349) which is seen in Q9AWZ7_EEEEE.Residues 19-279 are 62% similar to a (HYDROXYMETHYLTRANSFERASE METHYLTRANSFERASE KETOPANTOATE TRANSFERASE PANTOTHENATE BIOSYNTHESIS 3-METHYL-2-OXOBUTANOATE) protein domain (PD274690) which is seen in PANB_EMENI.Residues 21-279 are 62% similar to a (HYDROXYMETHYLTRANSFERASE METHYLTRANSFERASE KETOPANTOATE TRANSFERASE PANTOTHENATE BIOSYNTHESIS 3-METHYL-2-OXOBUTANOATE) protein domain (PDA014L9) which is seen in PAN1_BRAJA.Residues 23-277 are 67% similar to a (HYDROXYMETHYLTRANSFERASE METHYLTRANSFERASE TRANSFERASE 3-METHYL-2-OXOBUTANOATE KETOPANTOATE PANTOTHENATE BIOSYNTHESIS NRRL 3D-STRUCTURE KLUYVEROMYCES) protein domain (PD007676) which is seen in PANB_CHRVO.Residues 26-281 are 62% similar to a (METHYLTRANSFERASE PROBABLE TRANSFERASE 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE) protein domain (PDA014L4) which is seen in Q6AJ44_BBBBB.Residues 30-242 are 61% similar to a (METHYLTRANSFERASE KETOPANTOATE TRANSFERASE HYDROXYMETHYLTRANSFERASE) protein domain (PD821842) which is seen in Q89TZ6_BRAJA.Residues 31-279 are 61% similar to a (HYDROXYMETHYLTRANSFERASE METHYLTRANSFERASE TRANSFERASE 3-METHYL-2-OXOBUTANOATE KETOPANTOATE PANTOTHENATE BIOSYNTHESIS) protein domain (PDA182K1) which is seen in PANB_AGRT5.Residues 33-273 are 56% similar to a (HYDROXYMETHYLTRANSFERASE METHYLTRANSFERASE TRANSFERASE 3-METHYL-2-OXOBUTANOATE KETOPANTOATE PANTOTHENATE BIOSYNTHESIS) protein domain (PD577620) which is seen in PANB_YEAST.Residues 34-279 are 60% similar to a (DEBARYOMYCES HANSENII STRAIN CHROMOSOME G CBS767) protein domain (PDA014M0) which is seen in Q6BIM6_EEEEE.Residues 36-279 are 57% similar to a (P38122 CEREVISIAE YBR176W ECM31 SACCHAROMYCES) protein domain (PDA198R0) which is seen in Q6FJH7_EEEEE.Residues 38-273 are 56% similar to a (ABR186WP) protein domain (PDA186D2) which is seen in Q75D37_ASHGO.Residues 118-277 are 49% similar to a (METHYLTRANSFERASE TRANSFERASE 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE) protein domain (PDA014L8) which is seen in Q98JY0_RHILO.","","-59% similar to PDB:1OY0 The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping (E_value = 1.8E_63);-54% similar to PDB:1O66 Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase (E_value = 1.5E_46);-54% similar to PDB:1O68 Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase (E_value = 1.5E_46);-52% similar to PDB:1M3U Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate (E_value = 6.6E_42);-63% similar to PDB:1VRD Crystal structure of Inosine-5'-monophosphate dehydrogenase (TM1347) from THERMOTOGA MARITIMA at 2.18 A resolution (E_value = 6.6E_42);","Residues 19 to 276 (E_value = 7.3e-133) place ANA_0914 in the Pantoate_transf family which is described as Ketopantoate hydroxymethyltransferase.","","hydroxymethyltransferase (panB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0916","988633","989538","906","5.05","-16.47","32617","ATGACTTCTTCGGCTTCCCCTGCGTCCTCGGCCTCACTGGCCGACCGCGCGCCGCGTGGCACGCTGACTCCCGGGACGCTCAGTCCTGAGCGTCATGTGCCTGCGTCCATCGCACGCCCCGAGTACATGTTCCACGACGGCCCCGAGCGCGTGACCGCCTCGGAGATCAAGGATGCCGAGACGATCGAGCGGATCAGGGTCGCGGGGCGACTGGCCGCCCGCGCCCTGGCCGAGGCTGCCACGGCGATCGCCCCGGGGGTGAGCACCGATGAGCTGGACCGGATTGCCCACGAGTACCTGTGCGACCACGGCGCCTACCCCTCATGCTTGGGCTACATGGGTTTCCCCAAGTCGATCTGCACCTCCATCAACGAGGTCATCTGCCACGGCATCCCGGACTCGACCCGCTTGAACGAGGGAGACCTCATCAATCTTGACGTCACCGCCTACATCGGCGGGGTCCACGGCGACACGAACGCCACCTACGCCGTCGGCGAGGTCGATCGCGAGACGGAGCTGCTCATCGAGCGCACCCGCACCGCGATGGAGCGGGGCATCAAGGCCGTCAAGCCAGGTCGCGAGGTCAATGTCATCGGCCGCGTCATCGAGGCCTACGCCAAGCGCTTCGACTACGGGGTGGTGCGCGACTACACCGGACACGGCGTCGGCGAGGCGTTCCACTCCGGCCTCATCATCCCCCACTACGACGCCGCTCCCCTGCACGACGACGTCATCGAGACGGGCATGGTGTTCACCATCGAGCCGATGCTCACCCTGGGTGGCATCGAGTGGGAGCAGTGGGACGACGGCTGGACGGTGGTCACTAAGGACCGTTCCCGTACTGCGCAGTTCGAGCACACGCTCGTGGTGACCGAGGACGGCGCCGACGTGCTCACCCTGCCTTGA","MTSSASPASSASLADRAPRGTLTPGTLSPERHVPASIARPEYMFHDGPERVTASEIKDAETIERIRVAGRLAARALAEAATAIAPGVSTDELDRIAHEYLCDHGAYPSCLGYMGFPKSICTSINEVICHGIPDSTRLNEGDLINLDVTAYIGGVHGDTNATYAVGEVDRETELLIERTRTAMERGIKAVKPGREVNVIGRVIEAYAKRFDYGVVRDYTGHGVGEAFHSGLIIPHYDAAPLHDDVIETGMVFTIEPMLTLGGIEWEQWDDGWTVVTKDRSRTAQFEHTLVVTEDGADVLTLP$","Methionine aminopeptidase, type I","Cytoplasm, Extracellular","methionine aminopeptidase, type I","methionine aminopeptidase ","methionine aminopeptidase, type I","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., Bradshaw R.A. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(17):7714-7718. PMID: 7644482Keeling P.J., Doolittle W.F. Methionine aminopeptidase-1: the MAP of the mitochondrion?. Trends Biochem. Sci. 1996. 21(8):285-286. PMID: 8772380Roderick S.L., Matthews B.W. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 1993. 32(15):3907-3912. PMID: 8471602","","","

InterPro
IPR000994
Domain

Peptidase M24, catalytic core
G3DSA:3.90.230.10	$\"[56-299]T$	no description
PTHR10804	$\"[106-299]T$	PROTEASE FAMILY M24 (METHIONYL AMINOPEPTIDASE, AMINOPEPTIDASE P)
PF00557	$\"[63-300]T$	Peptidase_M24

InterPro
IPR001714
Family

Peptidase M24, methionine aminopeptidase
PR00599	$\"[119-132]T$ $\"[141-157]T$ $\"[211-223]T$ $\"[243-255]T$	MAPEPTIDASE

InterPro
IPR002467
Family

Peptidase M24A, methionine aminopeptidase, subfamily 1
PTHR10804:SF13	$\"[106-299]T$	METHIONINE AMINOPEPTIDASE 1
TIGR00500	$\"[55-301]T$	met_pdase_I: methionine aminopeptidase, typ
PS00680	$\"[217-235]T$	MAP_1

","BeTs to 26 clades of COG0024COG name: Methionine aminopeptidaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0024 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB002467 (Methionine aminopeptidase, subfamily 1) with a combined E-value of 1e-91. IPB002467A 54-95 IPB002467B 111-132 IPB002467C 137-165 IPB002467D 210-235 IPB002467E 269-299***** IPB001714 (Methionine aminopeptidase-1 signature) with a combined E-value of 8.1e-28. IPB001714A 119-132 IPB001714B 141-157 IPB001714C 211-223 IPB001714D 243-255***** IPB000587 (Creatinase) with a combined E-value of 1.4e-07. IPB000587E 57-100 IPB000587G 151-201 IPB000587I 232-265","Residues 103-299 are 43% similar to a (METHIONINE AMINOPEPTIDASE AMINOPEPTIDASE) protein domain (PD832556) which is seen in Q88AV3_PSESM.Residues 105-164 are similar to a (AMINOPEPTIDASE HYDROLASE COBALT METHIONINE PROTEASE DIPEPTIDASE XAA-PRO PEPTIDASE P PROLINE) protein domain (PD556587) which is seen in Q82AX4_STRAW.Residues 174-227 are 88% similar to a (AMINOPEPTIDASE HYDROLASE COBALT METHIONINE PROTEASE DIPEPTIDASE PEPTIDASE XAA-PRO MAP M) protein domain (PD289122) which is seen in Q6AFH6_BBBBB.Residues 234-299 are similar to a (AMINOPEPTIDASE HYDROLASE COBALT METHIONINE PROTEASE MAP M PEPTIDASE AMINOPEPTIDASE I) protein domain (PD551357) which is seen in Q6AFH6_BBBBB.","","-72% similar to PDB:1Y1N Identification of SH3 motif in M. Tuberculosis methionine aminopeptidase suggests a mode of interaction with the ribosome (E_value = 4.1E_93);-72% similar to PDB:1YJ3 Crystal structure analysis of product bound methionine aminopeptidase Type 1c from Mycobacterium Tuberculosis (E_value = 4.1E_93);-57% similar to PDB:2B3H Crystal structure of Human Methionine Aminopeptidase Type I with a third cobalt in the active site (E_value = 1.0E_59);-57% similar to PDB:2B3K Crystal structure of Human Methionine Aminopeptidase Type I in the holo form (E_value = 1.0E_59);-57% similar to PDB:2B3L Crystal structure of type I human methionine aminopeptidase in the apo form (E_value = 1.0E_59);","Residues 63 to 300 (E_value = 9e-67) place ANA_0916 in the Peptidase_M24 family which is described as metallopeptidase family M24.","","aminopeptidase, type I (map)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0918","989712","990899","1188","4.64","-20.28","40872","ATGGCTTTGCGCTTCAATCCACCGCCGAACTGGCCCGCGCCACCCGAGGGCTTCGAACCGCCTGCAGGCTGGCAGCCCGACCCGGCCTGGGGACCGGCTCCTGAGGGCTGGCAGATCTGGGTCGACGACTCCGCCGCCTCCAGCGCCTCCGCTGCCTCGGCCGCAGGTGACACCACCGAGACAGATCCGGCATGGGCTCCGACCCAGGCGGTGTCGACCGCCCCGACGGCCTCGTTGGGCACTGCCTCACAGGTTGCCGACCCGACAGGCATGTCGGCATCCGCTCCCTCAGGAGACTATGCCGGCGCTCCCGCAACTGGGGGCAGCCCTTACGCGGCCAACATGGACTACGCCCAGTCGCCCACGCCCTTCCAGCCCCAGGGGGCTGCCGGAGGCATGCAGCCTCCCACCGGCGGGTGGCAGCCCAATGCCGCCGCTCCGGCCGGCTCCGGCAATGGCTCCAAGCCGCTGACTCAGCAGTGGTGGTTCTGGACCGGTATTGCTGCAGTCGTCGTGGTCGTTCTGGTCATCGGTGGCATCTTCTTGTTCAAGGGCGATTCCAGTGAGTCCGACAACAAGGCGGACAGCACCTCAAGCTCGGAGCCGAACCACCAGAAGAAGTCCGCCCCCGACTCCGACAAGAAGTCGAGTGACTCTGACGAGACCGACAGCCCGGATCCGAAGAAGACCGGCAAGTCGGGCAGTAATGGCCCCGGCTCAAGCGAGAAGGACCCCATCGACCCCAAGGCCGGTGCAATCACCCTGAATGCAGGCAAGTACGACGACGACCCTAAGGCATCAGTGGACGTCACCTTCGGGGATGTCGAGTGGAACGCCACTGAGTCCATCAAGGCTGCCACGAACCAGTACAGCTACAAGGAGCCCCCTGCCGGCAAGGTGTATATTCGCGTTCCCGTTGAGATCACCTACCACGGTCAAGGACAGTTCGATGGGTACGATCTGAAGATCGGTTTCACCCACGACGGAAACACGGCAGAATCGGAGCTGCTTATCGGCGGGGAGTCACTCTTCAGCCGCCAAAGCATGCCCCGCGACGGAGGCAAGGCGAAGGGCGATTTCGTCTTCCTCGTTGACGAGTCCGCCGCCAATGAGAAGAAGGGCGCCTTCGCGGTGAGCGCTTTCTCTCAGGTGGACAACAAGAATGAGGTCTACGTGGCGGCGAAGTAA","MALRFNPPPNWPAPPEGFEPPAGWQPDPAWGPAPEGWQIWVDDSAASSASAASAAGDTTETDPAWAPTQAVSTAPTASLGTASQVADPTGMSASAPSGDYAGAPATGGSPYAANMDYAQSPTPFQPQGAAGGMQPPTGGWQPNAAAPAGSGNGSKPLTQQWWFWTGIAAVVVVVLVIGGIFLFKGDSSESDNKADSTSSSEPNHQKKSAPDSDKKSSDSDETDSPDPKKTGKSGSNGPGSSEKDPIDPKAGAITLNAGKYDDDPKASVDVTFGDVEWNATESIKAATNQYSYKEPPAGKVYIRVPVEITYHGQGQFDGYDLKIGFTHDGNTAESELLIGGESLFSRQSMPRDGGKAKGDFVFLVDESAANEKKGAFAVSAFSQVDNKNEVYVAAK$","Hypothetical protein","Extracellular, Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[161-183]?$	transmembrane_regions

InterPro
IPR005583
Family

Protein of unknown function DUF328
PF03883	$\"[3-250]T$	DUF328

","BeTs to 6 clades of COG3022COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3022 is -----------l--efgh-nuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 51-150 are 54% similar to a (UPF0246 YAAA CPE2152 PA3539 BB3890 YPO0462/Y3714/YP3720 VV0659 SAG2081 BT3869 VP0504) protein domain (PD017420) which is seen in Q82B26_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 250 (E_value = 6.3e-08) place ANA_0920 in the DUF328 family which is described as Protein of unknown function (DUF328).","","UPF0246 protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0921","993045","992311","735","4.92","-14.02","26801","GTGACAAGCGCCCCCATCGCCGAGCAGCGCCTTCTCATCGACCTGCAGGACCTCGACTCCCGCCTGGCACGGCTGCGTCACGAGCGCAAGCACCTTCCGGTCCTCACCCGCATCGAGGCAGTCATTGAACGCCTCAAAGTCAACAAGCGCGCAGCCATCCAGGCCGAGGCCGCCCTCGACGAAGCTAAGAAGCAGGCCACCCGTAGCGAGGACGAGGTCGGTCAGGTTGTGCGTCGGGCTGAGGTGCTGCGCGAGCGTCTCCACTCCGGAACCAGTGCGGCCCGCGACCTCTCCGCCATCCAGGGGGAGATCGACCAGCTCGGCCAACGCCAGTCAGCCTTGGAGGAGGCGCAGATCCTGGCGATGGAGGCGCTCGACTCCGCCCGGCAGGAGGCAGAACGCCTCAGCCAGGAGGAGTCGGAGATCCGTGCGGCCGGCCGCGAGCTCACCGCCAAGCGTGATGCCGAGTTCGCCCGACTCGATGAGGAGATCGACTCCCTGGAGAATCAGCGGGCAGACTTGGCTGGGACCATTGAGGCACCTCTCCTGGCCGACTATGAGGCCGTCCGCACCTCCACCGGTGGGCTCGGCGCCGTTGCCATGAGGGGCCGCACTGTTGAGGGCGGCGCTGTCGAGATCAGCCCCCAGGAGCTGGCCCGTATTGTGGCCGCCCCGGCCGAGGAAGTCATCCACGCCGAGGAGAACGACGTCATCATCGTGCGTATGGATATCTGA","VTSAPIAEQRLLIDLQDLDSRLARLRHERKHLPVLTRIEAVIERLKVNKRAAIQAEAALDEAKKQATRSEDEVGQVVRRAEVLRERLHSGTSAARDLSAIQGEIDQLGQRQSALEEAQILAMEALDSARQEAERLSQEESEIRAAGRELTAKRDAEFARLDEEIDSLENQRADLAGTIEAPLLADYEAVRTSTGGLGAVAMRGRTVEGGAVEISPQELARIVAAPAEEVIHAEENDVIIVRMDI$","Zn-ribbon protein","Cytoplasm","Uncharacterized ACR, COG1579 superfamily","hypothetical protein","protein of unknown function DUF164","","","","","

InterPro
IPR003743
Family

Protein of unknown function DUF164
PF02591	$\"[182-239]T$	DUF164

","BeTs to 5 clades of COG1579COG name: Zn-ribbon protein, possibly nucleic acid-bindingFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1579 is -------q-dr---------u--it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 91-167 are similar to a (SCO2300 DUF164) protein domain (PD708728) which is seen in Q6AFH8_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 182 to 239 (E_value = 8e-05) place ANA_0921 in the DUF164 family which is described as Putative zinc ribbon domain.","","ACR, COG1579 superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0922","993994","993092","903","5.25","-14.73","30840","ATGAGTCACACTCCTGCCCCCGCATCCCCTGAGGCCGGACACGGGCCGGCACGCAGCACGTCGGAAGGCCACCTGTCCGTCGGTGACGTCGTCGCCCTCGTGGAGGCCGCCGCACCTCCCGGCCTGGCCGCCTCCTGGGACTCCAACGGGCTCATCTGCGGCGACCCCGCCGAGCCGGTGCGCAGCATCCTGCTGGCCGTCGACCCGGTGACAGCCGTCGTCGAGGAGGCTATCGACGCCGGTGTCGACATGGTTATCACCCACCACCCCCTCTACCTGCGCGGTACCGACCACGTCGCGGCCACCGACCCCAAGGGCCGCACCGTCCACCGCCTCATCCGGGCCGGCATCGCGCTCCTCAACGCCCACACCAGCCTCGACGCCGCCCACGGGGGAGTGGCTGACGCCCTGGCCGAGCGCGTCGGTCTCGTCTCCACCGTCCCCCTCGAGCCCGACCCCGCCTCCCCGGATCAGGGCATCGGACGGATCGGCACGCTCCCGCAACCCGTCACTCTGCGCCAGCTCGCTGAGGACGTCGCCGCTGCCCTGCCCGACTCCGCCCCCGGCCTCCTCGTGGGCGGGGACCTGGACGCCGTCGTCGAACGCATTGCCGTCTCAGGTGGGGCGGGCGACTCTCTCCTGCAACGGGCCCGCGAGGCCGGAGCCGACGTGTTCCTCACCGCCGACCTGCGCCACCACCCGGCCTCCGAGCACCTGGAGGACGGCCGCCCCTACCTCCTGTGCGGCACCCACTGGGCCACCGAGTGGGTCGGCCTGGAGCCCCTGGCCCGCAGGCTCACTGAAGGTGCCCACGCCTGCGGAGCCTCGCTGTCCGTCCAGGTCTCCCGTATTGTCACGGACCCGTGGGCGCTGCGCCTGCCCACCGGACCTGACCGGGCATGA","MSHTPAPASPEAGHGPARSTSEGHLSVGDVVALVEAAAPPGLAASWDSNGLICGDPAEPVRSILLAVDPVTAVVEEAIDAGVDMVITHHPLYLRGTDHVAATDPKGRTVHRLIRAGIALLNAHTSLDAAHGGVADALAERVGLVSTVPLEPDPASPDQGIGRIGTLPQPVTLRQLAEDVAAALPDSAPGLLVGGDLDAVVERIAVSGGAGDSLLQRAREAGADVFLTADLRHHPASEHLEDGRPYLLCGTHWATEWVGLEPLARRLTEGAHACGASLSVQVSRIVTDPWALRLPTGPDRA$","Uncharacterized conserved protein","Cytoplasm","conserved hypothetical protein TIGR00486","hypothetical protein","protein of unknown function DUF34","","","","","

InterPro
IPR002678
Family

NGG1p interacting factor 3, NIF3
PTHR13799	$\"[29-266]T$	NGG1 INTERACTING FACTOR 3
PF01784	$\"[34-284]T$	NIF3
TIGR00486	$\"[25-288]T$	TIGR00486: conserved hypothetical protein T

","BeTs to 19 clades of COG0327COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0327 is aom-k-y--drlb-efgh-nu--itwNumber of proteins in this genome belonging to this COG is 1","***** IPB002678 (Protein of unknown function DUF34) with a combined E-value of 7.7e-34. IPB002678A 44-55 IPB002678B 77-94 IPB002678C 112-135 IPB002678D 221-254","Residues 86-143 are 75% similar to a (UPF0135 FACTOR STRAIN CHROMOSOME NGG1-INTERACTING SEQUENCE INTERACTING NIF3 CANDIDA YARROWIA) protein domain (PD037766) which is seen in Q73YH4_MYCPA.Residues 159-251 are 63% similar to a (UPF0135 FACTOR YBGI UNCHARACTERIZED STRAIN CHROMOSOME SEQUENCE INTERACTING 3-LIKE NGG1-INTERACTING) protein domain (PD352957) which is seen in Q6AFH9_BBBBB.","","-51% similar to PDB:2FYW Crystal structure of a conserved hypothetical protein from Streptococcus pneumoniae TIGR4 (E_value = 6.7E_27);-53% similar to PDB:2GX8 The Crystal Stucture of Bacillus cereus protein related to NIF3 (E_value = 3.9E_19);-56% similar to PDB:2NYD Crystal structure of Staphylococcus aureus hypothetical protein SA1388 (E_value = 2.2E_14);-42% similar to PDB:1NMO Structural genomics, protein ybgI, unknown function (E_value = 3.0E_11);-42% similar to PDB:1NMP Structural genomics, ybgI protein, unknown function (E_value = 3.0E_11);","Residues 34 to 284 (E_value = 1.2e-72) place ANA_0922 in the NIF3 family which is described as NIF3 (NGG1p interacting factor 3).","","hypothetical protein TIGR00486","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0923","996037","994217","1821","6.99","-0.12","68148","ATGGGTGCGCTGGTCGTCAAGGAGTTCGCCGACCGCGGCGAGTCCGCCAGGTCTGCGAACCGCCCTGAGCTACAGAAGATGCTGGCTTACCTCAAAGAAGACGGCGGGATCGACTACGTCATCGTCCACAAGTTAGATCGCCTGGCCCGGAACCGGGCGGATGATGTGGAGATAAACCGGGCGTTCGAGGATGCTGGCGTCCGGCTGGTGTCGACCAGTGAGAACATCGACCAGACGCCTGGCGGCATGCTCCTACACGGCATCATGAGCTCCATCGCTGAGTTCTACTCCCGTAACCTGGCTAATGAGGTCATCAAGGGGATGGGCGAGAAAGCCAGGAACGGTGGGACGCTGGGTAAGGCACCGCTCGGCTACCTCAACGTCCGCGCCAGAGACGAGAACGGCCGAGAAATCCGCACCATCGCCCTGGATGAGGAGCGCGCACCGCTGGTGCGGCTGGCTTTCACGGAGTATGCGACGGGGCAGTGGACGACCAAGAGGCTCGCTGCGCACCTCCATGGCCTTGGACTGACGACCGTGCCGACAGCCCGTAAGCCGGCCAAGGCGGTGACGGGTGCCCAGCTGCACCGCATGCTGCGCCACCCCTACTACAAAGGCGTCATCTCCTTCCAAGGGGTGAAGTACCCCGGGGCACATGAGCCCTTGGTGGACGAAGAAACCTGGAACCAGGTGCAGGCCGTGCTGGACTCCCATCGCTTCGGAGAACGCGAACGCCAACACAACCACCACCTCAAGACGACGGTGTACTGCGGCTTGTGTGGTGCCCGCCTGCTGGTGCAGAACACGCGCAACAGCAAAGGCGACCTCTACCCCTACTTCATCTGCGCCAAGCGCCAACGAACCCACGACTGCTCCTTCCGCGCCGTCCTCATCGACGTCGTCGAAGAGCGGATGAGCACGCTGTACCGGACGATCCAACTCAGCAGCCAGGATCGCCAGCTGGTGGAGCAGTATGTGCGGGAGGAGCTACGGCGCCTTGAGCGTGACAAAGATCGAACAATCCGCTCCCTGACGACCAGGCGGACGAACATCGAAGACAAGCGCCGCCGCCTGATGCACGCCCACTACGAAGGAGCCGTCCCCCTGGAGCTGCTCAAGGAGGAACAGACCCAGCTCACGGCCGAGCTCGACCATATTGAGCGCCAACTAACCGCCTACCAAGCCAACATAACCGAAATCCACCAACGCCTCACCCAGGCCCTTGACCTCCTCGAAGACTGCCACCGCCTCTACCAAGCCGCCCCACCGCACCTGAAGAAGCTGCTCAACCAGGTCTTCTTCGAGCGGGTGCTGGTCAATCCAGCGGTGGATGAAGACGGCCGAGTCGTCCTGCCGGAAGATGGAGCGAATGATGAGGGAGGCAGGAACGCGGCTGATGCGGCAGCTGGCGACTGCCCGATAGGGGAGAGTGACGACGGGCCATTGCAGCGGGCCGCAGCGCCGCGCCTGCTGGCCGACGCAAGCAGCGAAGCCAGTCTGGCAGCCGACCTCCGGCAGCCCTTCGACTGGCTGATCAGCCGCCTGATGCACAAGGTCGCACGGCAGCACCGTGCGACCTTGTTGCAAGACAACACACAAGAAAACTGGGACAACCAGGTGGACTGCCCCATCAACAACACCATCTACAACGACGAAGCGCTCACCAGTGGTGGTGAGCGCTTCGCATCTTCATCAACCAACCCAGACCGTGTTACTCATGACCTAGGTTTGGGTAAGGCTATCGTGGTACCCCCACTGGGATTCGAACCCAGGACCTTGTGTTTATCAGACACGATACGAGGTATAAGCTCGCTGCTCTAA","MGALVVKEFADRGESARSANRPELQKMLAYLKEDGGIDYVIVHKLDRLARNRADDVEINRAFEDAGVRLVSTSENIDQTPGGMLLHGIMSSIAEFYSRNLANEVIKGMGEKARNGGTLGKAPLGYLNVRARDENGREIRTIALDEERAPLVRLAFTEYATGQWTTKRLAAHLHGLGLTTVPTARKPAKAVTGAQLHRMLRHPYYKGVISFQGVKYPGAHEPLVDEETWNQVQAVLDSHRFGERERQHNHHLKTTVYCGLCGARLLVQNTRNSKGDLYPYFICAKRQRTHDCSFRAVLIDVVEERMSTLYRTIQLSSQDRQLVEQYVREELRRLERDKDRTIRSLTTRRTNIEDKRRRLMHAHYEGAVPLELLKEEQTQLTAELDHIERQLTAYQANITEIHQRLTQALDLLEDCHRLYQAAPPHLKKLLNQVFFERVLVNPAVDEDGRVVLPEDGANDEGGRNAADAAAGDCPIGESDDGPLQRAAAPRLLADASSEASLAADLRQPFDWLISRLMHKVARQHRATLLQDNTQENWDNQVDCPINNTIYNDEALTSGGERFASSSTNPDRVTHDLGLGKAIVVPPLGFEPRTLCLSDTIRGISSLL$","Recombinase","Cytoplasm","","","","","","","","

InterPro
IPR006119
Domain

Resolvase, N-terminal
PF00239	$\"[1-117]T$	Resolvase

InterPro
IPR011109
Family

Recombinase
PF07508	$\"[145-238]T$	Recombinase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1390	$\"[8-100]T$	no description

","BeTs to 8 clades of COG1961COG name: Site-specific recombinases, DNA invertase Pin homologsFunctional Class: LThe phylogenetic pattern of COG1961 is ---k----EBr----------Number of proteins in this genome belonging to this COG is","***** IPB006118 (Site-specific recombinase) with a combined E-value of 3.7e-11. IPB006118B 12-62 IPB006118C 82-121 IPB006118B 9-59","Residues 20-166 are 47% similar to a (SITE-SPECIFIC RECOMBINASE) protein domain (PD815460) which is seen in Q82XM1_NITEU.","","","Residues 1 to 117 (E_value = 1.6e-29) place ANA_0923 in the Resolvase family which is described as Resolvase, N terminal domain. Residues 2 to 117 (E_value = 8.1e-15) place ANA_0923 in the Resolvase family which is described as Resolvase, N terminal domain. Residues 145 to 238 (E_value = 4e-18) place ANA_0923 in the Recombinase family which is described as Recombinase.","","","","1","3","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:33:55 2007","Fri Aug 10 10:33:55 2007","Fri Aug 10 10:33:55 2007","Fri Aug 10 10:32:48 2007","","","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","Fri Aug 10 10:32:48 2007","","Fri Aug 10 10:32:48 2007","","Fri Aug 10 10:32:48 2007","yes","","" "ANA_0926","996123","996716","594","8.09","2.57","20712","GTGGAGACACGGATGTACGAGACGGCACGTTTGGGAGTCAATTGGGCGGCCATGGCGGTGAAGGGATCGGGGGCAAGTGCGTCAGGCATGGTGCACCTCCTTGCTGGGGTCGGTGGGTTCACTGGTCTGCTCGCGCTGCTGGCGTTCTTGTTCTCTCAGCTCATCGAGCTGGCGCATCCACGCGCCTTCTTCGTCGTTCCACCAGGCAGGCGGCTCACCGTCGCCAGGACGCCAGGTGTTGAGGCAGACCAGGTAGGTGCCGGCTTGGGCGAGCTGGTCAAGCACCGCGTCGGCTTCGGTGGTGGTGAGGTTGGGGGTGGGCCAGCCTGCCGTGATGACGTACGCCACCCCACCGCGCTGGCAGGCATCGAGCAGCATGCCCAGTCCATACTGGCGCTGCTGTCGGTCGTGGAACTCGGTGACCAGGTTGAGGCCCATCGCGTCGGCGTAGTCCTCCACCAGTTCCCGTTGCCAGGCCAGCTCGAAGGGGTAGCGGGCCGCGCCGTAGAAGATGGCGATCGGCCCGGTACCCGTACCACTGTCGCCTCGTGCAGTGGTTGGTACCGCCTCCAGTACCGCCGCCAGCTCATGTAG","VETRMYETARLGVNWAAMAVKGSGASASGMVHLLAGVGGFTGLLALLAFLFSQLIELAHPRAFFVVPPGRRLTVARTPGVEADQVGAGLGELVKHRVGFGGGEVGGGPACRDDVRHPTALAGIEQHAQSILALLSVVELGDQVEAHRVGVVLHQFPLPGQLEGVAGRAVEDGDRPGTRTTVASCSGWYRLQYRRQLM$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-57]?$	signal-peptide
tmhmm	$\"[31-51]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0927","998437","997010","1428","10.94","31.22","51223","ATGACGGGCGGAGGGATTGAGCGTGTCCTCCGCAGCGCGTCGGCTGCGCTGACGGGCCGTCCCTCAATCCGCAGGAGTGTGAAAACCGATCGTCATGAGCGATTTTCAGCCCAGCGCAAGAGGTCGGTATTCAGTGAATGCCGACCCTTACAGCGTTCCGGGGGAGGGGGCGGCCCAGGTAGCGCTTCAGACACCACTGGGACTGCGAAGTTCGCTGCGAAGTATCGCCCCTATCTGGCCCCTGCGCTTGTCTCCACCACTGGCTTGCCGAGACGCGTCGGGGGACGAATCGCTAGACGCATCGCTGCAGCGAGCAGGCAGGGCTATCGGCGCTGTGGTGCGGCACAGGCGCGGTTACGGGAGGCGACTGATGGCCCCCTGTGGCCATCCCATCCACCACTGACAACACCCCCGGCCTCACAGCCCCTGGCTCGCAGCAGCGACTCGATCACACACATGACGATCACAAAGGAGGAAACAGCAATGAACACAGCGATATCGGAATACGCGAGCGTCGGGACAAGCACCGGTTTGGCAGTACCGACACCCGCGACGACACCAACGACGATGAAGGGAGCAGCGACGACAGAGGCAGCGAAGTCTCAGCGCCAGGTTCCGGCCCGGATTGGCCGCGCCCAGCTGCAGGCGATCGCCGAGCGGCTCGATACCACCGATCGCGAGCTGCTGGCGCTGCTGGCGGCCCATCGCTATGCCACAACCCGCCAGCTGGCGCAGATCACCGAGCTGTCTGGGCAGTACGGTTCGGCCCGTTCGGCGCTGCGCCAGACCAGTCGGCGACTGCGACGCCAGCACGGGCTGGGACTGGTCGATCACCTGGCGCGGCGGATTGGTGGCACACGGGCAGGCTCAGCAGGGTACGTCTGGTACCTGACAGCAGCGGGGCAGCGCCTGACGAGCGAGGGGCAAGGGCGTGGAGCGCGGCGACGCTTTCAGGAGCCGTCGCCACTGTTCCTTGCTCATACGTTGGCGATCACGCAGGCGCGGGTCGTCATCGAGCAGGCCATTCACGCCGTCGGTGGACATCTAGCCCGGTTGCGTACCGAGCCGGCCTGCTGGCGCTCCTGGCTGCGGCTCGGTGGGGCGCTGGGCTGGCTCAAGCCGGATCTGGAAGCAATCACGGCGACGGATACGGGCGCAGAAGATCACTGGCTCTTCGAGGTCGACCTGGATACCGAGCATCCGGGGCGGCTGCTGGCCAAGTGCCATGACTACCAGGCTCACCTGGCCAGCGGTACCTTCCAAGCCCAGCACGGCTACTACCCGCAGGTGGTCTGGCTGCTGACCAACCCCACCCGGGCAGGCCGCCTGGCCGAGCAGATCGCCGCCGACCAGACGCTGACCCCTGGGCTGTTCAAGATCACCGCCGCCCCTGAGCAGCTCGCCGCCCTGATCCAGCGCGGCCCATGA","MTGGGIERVLRSASAALTGRPSIRRSVKTDRHERFSAQRKRSVFSECRPLQRSGGGGGPGSASDTTGTAKFAAKYRPYLAPALVSTTGLPRRVGGRIARRIAAASRQGYRRCGAAQARLREATDGPLWPSHPPLTTPPASQPLARSSDSITHMTITKEETAMNTAISEYASVGTSTGLAVPTPATTPTTMKGAATTEAAKSQRQVPARIGRAQLQAIAERLDTTDRELLALLAAHRYATTRQLAQITELSGQYGSARSALRQTSRRLRRQHGLGLVDHLARRIGGTRAGSAGYVWYLTAAGQRLTSEGQGRGARRRFQEPSPLFLAHTLAITQARVVIEQAIHAVGGHLARLRTEPACWRSWLRLGGALGWLKPDLEAITATDTGAEDHWLFEVDLDTEHPGRLLAKCHDYQAHLASGTFQAQHGYYPQVVWLLTNPTRAGRLAEQIAADQTLTPGLFKITAAPEQLAALIQRGP$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0929","1000731","998434","2298","10.27","18.33","80271","ATGGCCCGCCCCACTCAGCCCCTGGTGTGGCACCAGCCGCGTTTTGCCCTGCCGCTCGCCCAGGACGCGGCGGTGGGTCTGGTGGAGCGCATTCTGGCGGACGCTTCGCTTGGTCGGGTGGTGTTGGAGTTGCGGGCCTGTGGTGGGCAGGTGACGTGGGCGGTGGGCTCGCAGGCGGGTGAGCGGTTGGCCTCGGTGGTGCGTGAGCTGGTGCCGGGCTGCCGGGTGTCGCGTGGCTTCTCGCGGCGGGCGGTGAACCAAGCGGTGGTGGTGTCAGCCCGGCCAATCGGAGCGGGACTGGCGACGGAGCGGCTGGTGGCGGTGGTGCGAGCTGTCCTGGCGGCACTGGCGGTGACGGCTGAAGGGGAGGAGCTAGTGGTTCAGCTGCAGCTGGGGCGACGCTTCTCACCGCAAGTACTGGGGCGGGTGGAGCCGCAGGGGTGGCTGGAGCTGCTCGGGCTCGTACCACTGCCCTCTGTTACTGGTGAGCGGGGTCGGCGACTAAAGGCGCAGGTGGGGCGGCATCGGGCGGCAGCGAGTCTGCGCTTGGGGGTGCGGGCGGCCTCGCCGCTGCGCCAGCGGACGCTGCTGCAGGGGCTACTCGGGGCACTGCGTCTGCTGGAGGGGCCGGGGGCGCGGCTGCGCGCCCGCACGGAGCACCCCGCCAAGCTCGACGGAGTGCGGCGGCCGTGGCGGGCGGGGCTGGAGCTTGGTGCCGGAGAGATTGTCGCGATGGCGGGTTGGCCGGTGGGTGAGGGGGCGCTGCCGGCGACGCCGTCGGCTCATCCGCGGGTGCTGGCGCTGCCACTAGCGCGTGAGACGCAGCGGGCGTTCGCCACTGGGGTGGCGGATCAGGCGGGTGAGCGCCTTGGTATCTCGATTGGTGATGCGCTCTACCACACGGTGCTGCTGGGGCCGACGGGGGCTGGTAAGTCCACCGCCTTGGCGCATCTGGCGTTGGCGGATATCCATGCTGGTCGGGGTGTGCTCCTGATCGATCCGAAGACGGATCTGGTGGCAGACATTCTGGCGCGTATCCCTGAGCAGCGACGGGGTGACGTGGTGGTGATCGACCCGACCAGTAGCCGCCCGGTGGGGATCAATCCACTGGCCCGAGTGCAGACGGCGCGTAGCGGCGCATTGTCATCAGGCGGCGGTGTGCCAGGTGGTGGTGCGTCGCCGGAGCTAGTAGCGGATACGGTGCTGGCGACGTTGAAGGGGGTGTTTGCTGAGTCGTGGGGTGTGCGGGTGGAGCAGGTGCTCTCTGCGGCGCTGGTGACGCTCGCTCGCACGCCGGGAGCGACGCTGGTCGATCTACCCCTCTTACTGACCAATCCGGCGTACCGTCAGCGGCTCATGGCGGCCTCGGGGGCGGATCCGCTGGGGACGGGGCAGTTCTGGGCGGCCTATGAGGCGCTCAGTGAGGCGCAGCGTCAGCAGTGGGTCGGGCCGGTGCTGACGCGGCTGCAGCCTTTCCTCATCCGCCCGCACCTACGGGCCACGCTGGGGCAGGCCGCACCGTCGTTCGACCTGGGGGAGGTGTTCACGCGCCGGCGCATTGTGCTGGTCAGTCTCAACAAGGGGGTGCTGGGGGCGGAGTCGGCTCGGCTGCTCGGGTCGCTGCTGGTGGGCCAGCTCTGGCCACTCATCCTGGCCCGAGCAGCGGTGGAGCCGTCGCGGCGGCATGTGGTCAGTGTCTTCATTGATGAGGTGCAGGATTACCTGTCGCTGCCGGGCAGCCTGGCCGACGCCCTGGCCCAGGCCCGGTCACTGGGCGCAGCGTTTCATCTGGCGCATCAGTACCGCGGGCAGCTGCCCGCGGCGCTCAAGGCGGGGATCGATGCCAATGCGCGCAACAAGATCATCTTCTCCCTGAGCGCAGCGGACGCGGCCGAGCTGGCCCGTCAGGCGATTGGCCTGGAGGCGGCTGACTTCCAGCTGCTGCCGCGCTTTGGCGTCTACGCGCGCACCATGCACCACGGGCGGGAGAACCCCTGGTGCCACGCCACCACCCTGCCACCAACCCCACCAACCCAGGACGCCCTGGCACTGCGCGCCGCCAGCCAGGCGCGCTACGGCCAAGACGCCGCGCAGACTGAGGCCGCCCTGCTCGCACGGCTCGGACAGAACGGCGAGATGACCGGTGATGACGTGACTCAGATGGCAACGGACGACGCGATGGGTGAGCTCGGGGGAGAAGCCACGAACGAAGGCACTGGACCAGCGAACGGCGTACCTAACTCGACGGCTGATGTGGTGTTCGGCCGCCGGCCTGGACGGGATGGAGGAGCAGCATGA","MARPTQPLVWHQPRFALPLAQDAAVGLVERILADASLGRVVLELRACGGQVTWAVGSQAGERLASVVRELVPGCRVSRGFSRRAVNQAVVVSARPIGAGLATERLVAVVRAVLAALAVTAEGEELVVQLQLGRRFSPQVLGRVEPQGWLELLGLVPLPSVTGERGRRLKAQVGRHRAAASLRLGVRAASPLRQRTLLQGLLGALRLLEGPGARLRARTEHPAKLDGVRRPWRAGLELGAGEIVAMAGWPVGEGALPATPSAHPRVLALPLARETQRAFATGVADQAGERLGISIGDALYHTVLLGPTGAGKSTALAHLALADIHAGRGVLLIDPKTDLVADILARIPEQRRGDVVVIDPTSSRPVGINPLARVQTARSGALSSGGGVPGGGASPELVADTVLATLKGVFAESWGVRVEQVLSAALVTLARTPGATLVDLPLLLTNPAYRQRLMAASGADPLGTGQFWAAYEALSEAQRQQWVGPVLTRLQPFLIRPHLRATLGQAAPSFDLGEVFTRRRIVLVSLNKGVLGAESARLLGSLLVGQLWPLILARAAVEPSRRHVVSVFIDEVQDYLSLPGSLADALAQARSLGAAFHLAHQYRGQLPAALKAGIDANARNKIIFSLSAADAAELARQAIGLEAADFQLLPRFGVYARTMHHGRENPWCHATTLPPTPPTQDALALRAASQARYGQDAAQTEAALLARLGQNGEMTGDDVTQMATDDAMGELGGEATNEGTGPANGVPNSTADVVFGRRPGRDGGAA$","Hypothetical protein","Cytoplasm, Membrane","hypothetical protein","hypothetical protein","hypothetical protein","","Tougu K., Peng H., Marians K.J. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 1994. 269(6):4675-4682. PMID: 8308039","","","

InterPro
IPR013173
Domain

DNA primase DnaG, DnaB-binding
SM00766	$\"[434-550]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[300-639]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 486-649 are 50% similar to a (PLASMID TA1216 TVG0369160 ORF1042 VIRD-LIKE ST1326) protein domain (PD311855) which is seen in Q971N4_SULTO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0930","1002480","1001605","876","9.92","10.61","31179","ATGCAGCAGACAAAACACACAAGACGAGCGTGGGCTGGGGGAGTAGCGGCTCGGCACGGTGCGGCGGCCAAGCAGGCTGGCGCAGCAGTGAGACCAGGTGCTGGCGTGCCGCGACCTAGCGGCACAGTGAGCGATGGGCCTGGCTCGGCTGGTCGGAATGACTCTGGTGGTGCTGGCTCATCACCCGCCATCCCTGGCTTGCCGCCTGGTGGCTTTGCCACCATCCTGGTCGATCCGCCCTGGCCGCTGCAGAGCGGTGAGAAGCACTACCGGACGATGAGCCTGGCGCGGATCAAGGCTTTGCCGGTGGGGGCGTTGGCGGCCCGTGATGCCCACTTGTGGCTGTGGACGACCAACGCGCTCTTGCCAAAGGCGTATGAGGTGGCTGAGGCATGGGGCTTTACGGTGCGCAGCCCACTGACCTGGGTGAAGTTCCGCCTTGGCCTAGGTGGTCGCTACCAGCTGCGTAATGCCACCGAGCAGCTGCTGTTCTGCACCCGAGGGAAGGCCCCGCTGGGCTCGCGCTCCCAGCCGACCTGGTTCAACGCCCCAGTACAGGAGCACTCGCGTAAGCCAGCCGAGCAGTTCGCCATTATCGAGCGGGTCAGCCCCGGGCCGTACCTGGAGCTGTTTGCCCGCCGCCGGCCAGAGTCGAACCAGCCCTGGGCAGTGTGGGGAGACCAAGTAACCAGTGACATCCGCATCCCCGGCTTTGCCGTGCCGCGCTACAGCGAGCAGGCGCACAAGGCAGACGCCGAGACAACGACCACGACAGCGGAGCAGGCGGAGCCGGCACATGCGGCGGTGGCTGCTGCATCCCGTGGCGACGACAGAGATGAAACCGCTGACGTTAACAGCAAGGAGGTAACGCGATGA","MQQTKHTRRAWAGGVAARHGAAAKQAGAAVRPGAGVPRPSGTVSDGPGSAGRNDSGGAGSSPAIPGLPPGGFATILVDPPWPLQSGEKHYRTMSLARIKALPVGALAARDAHLWLWTTNALLPKAYEVAEAWGFTVRSPLTWVKFRLGLGGRYQLRNATEQLLFCTRGKAPLGSRSQPTWFNAPVQEHSRKPAEQFAIIERVSPGPYLELFARRRPESNQPWAVWGDQVTSDIRIPGFAVPRYSEQAHKADAETTTTTAEQAEPAHAAVAAASRGDDRDETADVNSKEVTR$","MT-A70 family protein","Periplasm, Extracellular","MunI-like protein","MT-A70 family protein","MT-A70 family protein","","Cheng X. Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 1995. 24:293-318. PMID: 7663118Loenen W.A., Daniel A.S., Braymer H.D., Murray N.E. Organization and sequence of the hsd genes of Escherichia coli K-12. J. Mol. Biol. 1987. 198(2):159-170. PMID: 3323532Narva K.E., Van Etten J.L., Slatko B.E., Benner J.S. The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases. Gene 1988. 74(1):253-259. PMID: 3248728Lauster R. Evolution of type II DNA methyltransferases. A gene duplication model. J. Mol. Biol. 1989. 206(2):313-321. PMID: 2541254Timinskas A., Butkus V., Janulaitis A. Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases. Gene 1995. 157(1):3-11. PMID: 7607512Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E., Schildkraut I., Saenger W. Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(23):10957-10961. PMID: 7971991","","","

InterPro
IPR002052
Domain

N-6 Adenine-specific DNA methylase
PS00092	$\"[75-81]?$	N6_MTASE

InterPro
IPR007757
Family

MT-A70
PF05063	$\"[72-228]T$	MT-A70
PS51143	$\"[37-248]T$	MT_A70

noIPR
unintegrated

unintegrated
PTHR12829	$\"[70-260]T$	N6-ADENOSINE-METHYLTRANSFERASE

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 87-169 are 57% similar to a (METHYLTRANSFERASE TRANSFERASE N6-ADENOSINE-METHYLTRANSFERASE NUCLEAR RNA-BINDING STRAIN CHROMOSOME PLASMID M6A MT-A70-LIKE) protein domain (PD043555) which is seen in Q9L8Z8_ENTFA.","","No significant hits to the PDB database (E-value < E-10).","Residues 72 to 228 (E_value = 1.8e-27) place ANA_0930 in the MT-A70 family which is described as MT-A70.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0931","1003482","1002913","570","6.53","-1.12","18778","ATGAGTCAGCCGCTGCCCGTCGGCGAGCCGCCGCTGTCGCTCTCTGCCGCGCTGCCGAGCAGCTACCAGGCCGGTCAGCTGGCCGGTGAGGTCGCAGCCAGCTGGCGCTCCGCACACCAGGCGGCCAGAACAGCTGGACCAGGCGCACCGGCCAGCTCATCCTGGGCAGCCGCCCTGGCCTTGGGCAGTGAGCTGAGCCAGCAGCGCCAAGAAGCAGGCCGAGCCATGCAAGCAGCCATGGCCCAGGTGTTGCAGGACAACGAGCAGGCAGTGCGGGAGGCAGCGGCCGGTGCGGCCGGTGGCGGGCATGACGCCAGCAATAGCGGGAGTGGTGCCAGCAGCGGTGGCGGTGTTACTGACGAGAGCAGTGGCAATAGTGTCAGTGGTGGCGGCGCGTCTCCTGAGGTGGAGCTGGACGGATCGAATGGTGACGGCAACAGTGGCGAGTCGGCGGCTGGTACGGCCCGTCCCACCTGGCCGGCTCACGCGCCCTCGCGTCGTCCGCCGCGGCCGCGTCCCAGGCGGTGCACGCAGCACAGGCCAGCTCGGTCGGATGAGCGGCAGCCGTGA","MSQPLPVGEPPLSLSAALPSSYQAGQLAGEVAASWRSAHQAARTAGPGAPASSSWAAALALGSELSQQRQEAGRAMQAAMAQVLQDNEQAVREAAAGAAGGGHDASNSGSGASSGGGVTDESSGNSVSGGGASPEVELDGSNGDGNSGESAAGTARPTWPAHAPSRRPPRPRPRRCTQHRPARSDERQP$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0932","1003531","1003683","153","6.30","-1.37","5972","GTGGGCGAACGCCCAGCCGATTGCGCCCACCACCGCCAGACCAATGAGGGCCAGAATCCCGACTATGACCGTCATGATGAAACCTCCAAAGATGAGAAGAGATTGAGAGAAGAAGAGAAAGGTGAGGAGAAGGAAAAGAAGGCGCGAAGGTAG","VGERPADCAHHRQTNEGQNPDYDRHDETSKDEKRLREEEKGEEKEKKARR$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0933","1004157","1003858","300","9.95","1.92","10432","ATGGCTTCTACCAGTCTCAGTCTCTTCTCGCCCCAGCGCACCCGGATGGGGGTGGTGCTGGGCAATGGCCAGGCCCGGGTGACCAGGCGGGAGATCGAGCAGGTCGCCGCCCAGGCAGAAGTAGCGGCCCAGGCCGAGCAGGCCCGGGCCTTCCTGACCTCCCAGGTCCTGACCAATATCGCCACGCTGGTGACCCAGGCCGAGGCCCAGACTCGCATCGCCCCCGGCGGCGCTCAGTTCTACGAAGCGATCATCACGGGGTACGCCCTGGGCGCTGGGCAGCGGATCGGGCAGTTGTAG","MASTSLSLFSPQRTRMGVVLGNGQARVTRREIEQVAAQAEVAAQAEQARAFLTSQVLTNIATLVTQAEAQTRIAPGGAQFYEAIITGYALGAGQRIGQL$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0934","1004686","1005681","996","7.13","0.61","36668","ATGTCTCGCGCTCGTCTCGATGCCGATGATGCGGCTTCCTTGCTGCGTGAGCTGGCGTGGCTGCGTAAGCGCGGTGGCTTCACGGCGGCGCGGCTAGTGCACGCCCCGATCGTCGATGAGGTGCTGCGCGGGAGCTTGGAGGACTCTTTCGAGCGGCTACGTCACCGCTTTGTCTCAGCCATCCACAGCCTGAGTGAGAGCGGGAGTGAGCAGGATGAGCCGCTGGTAGGTGTGCTGCTGGCGGCCTTTGCGCTCAGCCCTGAGACGGCGGGTAGTGGCAGCCTGTTGGAGCGGCGGCGGGCGATGGCGAGCCGCTTGGGGTGCAGTATGGAGACGATCGCTTCTCGGGAGGAGGCCGGCTTGCGTCTGCTGCACAGTCGCCTGGTGGCTGGGCGCTATGCTCAGGCACCGCTGGTGCTGGATGTGCCGGAGATGCACGGTGGGATTGTCTATGAGGAGACCACCACGCTCATCGTGGTCGAGCAGCGTCGGTGGCGGGGCACGGTGGAGCGCTACCGGTTGGCCAACATGGCTGGTGAGCTGGACTTCGTCACGATCTCCCGCTCCTACCCCGCCCATGTCACGGCGCAGCCGGGCGGAGAGTTCAGCGTCAACAGCCGCCCTGTCGAAGGGGCTGGGTGGAACGACCACTTCTGGCACATCGACCCCGCCACCGGTAGGCGCACCCCAATGCAGGACGCCACGCGCTACGACCTCGCTTTCCGGGCAGAGCCTCTGCCGGGCGAGGAGCCCACCACGCCGATCTCATTGGCTAGCCGGGCCTTCCATGCCCGCTCACTGCTGGCCACCATCCAGGTGCGCTTCGTCGGGGAGGTGCCAGCCAGCATCTGGCAGTTCACCGGGGCCAGCCCCTTCACCCGCCCCCAAGCCGCCAACCAGTACAACCGCACCCACCTGGACGCCCAGCAGCGCGCCACCCTCACCCAGCGCGACGTCCACGGTGGGCTGTTCGGTGGGTTCGGGTGGGAGTGGTGA","MSRARLDADDAASLLRELAWLRKRGGFTAARLVHAPIVDEVLRGSLEDSFERLRHRFVSAIHSLSESGSEQDEPLVGVLLAAFALSPETAGSGSLLERRRAMASRLGCSMETIASREEAGLRLLHSRLVAGRYAQAPLVLDVPEMHGGIVYEETTTLIVVEQRRWRGTVERYRLANMAGELDFVTISRSYPAHVTAQPGGEFSVNSRPVEGAGWNDHFWHIDPATGRRTPMQDATRYDLAFRAEPLPGEEPTTPISLASRAFHARSLLATIQVRFVGEVPASIWQFTGASPFTRPQAANQYNRTHLDAQQRATLTQRDVHGGLFGGFGWEW$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0934.1","1006177","1007115","939","5.93","-4.58","34969","ATGTCTACTCGGGTATCACACGGTGCCCGACTGACTGCACGCAGTGCTTTGCGCCGCGAAGCTACACAGCAACTTCTCTCATCCTTCATATCCCTCACACCCCGACAGGAGTATGGAATGACATCAGATGACAATGTAATCCCCTGGCCCAAGCCAGACCCAGAACGTAGCAATGATCGCAACTTGGTAACAATCCTCCTCGATCTATCCGGCTCGATGAACAACGAGCTGAAAGACGAAGATCCATCACGAGATGCACGAATCACGACACGCATTGCTGCTCTCGAAGACGGACTACAACGGCTGGTTTCCCCAGATAATTCAAGTAGCATGCACAGCGCAAAAAGCTTCGACGGCAGTGTCGAGTTCGCCCTCGGTTACTTCCCAAGTCGCCACTCCGCTGGACATGTCGACTGGTGCCAGTTCCCAAACGCACGCGCAACCAGCGGGCCATTCTACTACGGCGTGGATATCACGGAGCCGCCCGAACTACCAACGCCAGCTGGCCTAACACCACTTGGTGAGGCAATTATCGAGGCGTTAAGCGCCATCGAAAGGCGTCGCGTAGAGATTCGCGACGTCGAGCGTCGCACGATCACGCGCCCTTCGCTCTTCGTCATCACTGACGGCGTCTCAACAACCCCAGAACTAATCCCAGAGGCTACTCGGCAACTGCGTGCCGCCGAAGACGCAAAGCGCATCCTCTTTTTCGCGCTTGGCACGTACGATGCAAGCATCGATCGGCTCATGGAGCTCGCACCACGCTCATCGTATGACCTTCACAAACTATCGGCAGCTCGCCTTATCGAATTCCTCAGTACCAGCATGACAAACTCCATCAATATCGACTCACATGCGGATGCGGATGCAATCTACGAAAACATGAACCGAGACTACGTCAAATGGGATTTGGTGAGGCAAAGTCTCCGGAGACGATAG","MSTRVSHGARLTARSALRREATQQLLSSFISLTPRQEYGMTSDDNVIPWPKPDPERSNDRNLVTILLDLSGSMNNELKDEDPSRDARITTRIAALEDGLQRLVSPDNSSSMHSAKSFDGSVEFALGYFPSRHSAGHVDWCQFPNARATSGPFYYGVDITEPPELPTPAGLTPLGEAIIEALSAIERRRVEIRDVERRTITRPSLFVITDGVSTTPELIPEATRQLRAAEDAKRILFFALGTYDASIDRLMELAPRSSYDLHKLSAARLIEFLSTSMTNSINIDSHADADAIYENMNRDYVKWDLVRQSLRRR$","Von Willebrand factor, type A","Periplasm, Cytoplasm","","","","","Ruggeri ZM, Ware J.von Willebrand factor.FASEB J. 1993 Feb;7(2):308-16.PMID: 8440408Colombatti A, Bonaldo P, Doliana R.Type A modules: interacting domains found in several non-fibrillar collagens and in other extracellular matrix proteins.Matrix. 1993 Jul;13(4):297-306.PMID: 8412987","","","

InterPro
IPR002035
Domain

von Willebrand factor, type A
SM00327	$\"[60-269]T$	VWA
PS50234	$\"[62-280]T$	VWFA

InterPro
IPR001932
Domain

Protein phosphatase 2C-related
SM00331	$\"[5-252]T$	PP2C_SIG

noIPR
unintegrated

unintegrated
PD121216	$\"[3-203]T$	Q8YTA1_ANASP_Q8YTA1;
G3DSA:3.60.40.10	$\"[3-127]T$	no description

InterPro
IPR000719
Domain

Protein kinase, core
PD000001	$\"[151-325]T$	Q6AEZ5_BBBBB_Q6AEZ5;
PF00069	$\"[31-325]T$	Pkinase
PS50011	$\"[31-329]T$	PROTEIN_KINASE_DOM

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[168-330]T$	no description
PTHR22985	$\"[161-195]T$	SERINE/THREONINE PROTEIN KINASE
PTHR22985:SF28	$\"[161-195]T$	RHO/RAC-INTERACTING CITRON KINASE
tmhmm	$\"[415-435]?$	transmembrane_regions

","BeTs to 7 clades of COG0515COG name: Serine/threonine protein kinasesFunctional Class: TThe phylogenetic pattern of COG0515 is amtkYq-C-BR---gp-lIN-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 151-325 are 41% similar to a (KINASE ATP-BINDING TRANSFERASE SERINE/THREONINE-PROTEIN RECEPTOR PHOSPHORYLATION SERINE/THREONINE TYROSINE-PROTEIN REPEAT CELL) protein domain (PD000001) which is seen in Q6AEZ5_BBBBB.","","","No significant hits to the Pfam 21.0 database.","","","","1","3","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:12 2007","Sat Jul 14 22:56:12 2007","Sat Jul 14 22:56:12 2007","Mon Aug 20 18:12:14 2007","","","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:00 2007","Mon Aug 20 18:12:14 2007","Sat Jul 14 22:56:00 2007","Mon Aug 20 18:12:14 2007","Sat Jul 14 22:56:00 2007","Sat Jul 14 22:56:00 2007","Mon Aug 20 18:12:14 2007","","Sat Jul 14 22:56:00 2007","","Sat Jul 14 22:56:00 2007","yes","","" "ANA_0936","1009605","1010372","768","5.71","-6.38","28960","ATGACCGAGCAAGTAGAGCGCGAACAGGTTGTCCAGAACCTCGCAAAACAGATCGACCAAGTCAAGCATTTTAGCCTGCGTGGCATCGAAGAAATTTGTCATGATGCCAGCATTGGGCTACTGGGGCCCCAAGACGCCATTGCGGATGAGTTCGTCGACGACTCGCTGTACCGCCTGCTGTCCAACAACGAGCTCCTGGCAGCATTCGCCAACGCAGGCTTCACTCCACCCGGGACGGTAGAGGCGAGGAAGGAGCTCCTGTCGGTGTTCATCGATGCCATGCAACGTCTCGACGTCTTGCCGCACGCCACCCAGCGAGACGTCCAACAGTGCATTGCGGCGACGAGCAAGGCCACGCTGGAGCACATTCAATACGAGACGCAGATTGCGATTGCCCGGACGGTGGCACCAACGGATGTTGAGATCGCCAGAATCGATGCCGAAACTCGTCTTACCAACACCAGGGCAAACGCTGCTCTGGCAGAGGCCGATGCAAGAAAACGCATCAACGATGCGAGCGATCTTCACAGCGAACAAATCGCTCGTGAGTCGCAGTTTGCTCATCGAGACGAACTGAATCTGCGCAAAGCACAAGAAGAGTCGAGAAATGCAGCCTTTGCATTTTCCATCCAGCAAGCAAACAATCGCCTTGAAGAAGAAAATGAACTGCGCAAACATAGGATCAAGGAGCGACGCGTCGCGCGGGAAAAATTCTGGGAGAAGGTATTGCCTTTGACGCTGCTGGAAATGCGGAATGGGTTAAGATGA","MTEQVEREQVVQNLAKQIDQVKHFSLRGIEEICHDASIGLLGPQDAIADEFVDDSLYRLLSNNELLAAFANAGFTPPGTVEARKELLSVFIDAMQRLDVLPHATQRDVQQCIAATSKATLEHIQYETQIAIARTVAPTDVEIARIDAETRLTNTRANAALAEADARKRINDASDLHSEQIARESQFAHRDELNLRKAQEESRNAAFAFSIQQANNRLEEENELRKHRIKERRVAREKFWEKVLPLTLLEMRNGLR$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0937","1010872","1013388","2517","3.78","-184.77","87385","ATGAGCACCGAAGCTCAGATGGACGTTGAGCGATATGGCTTCAACCCCGGTGACATGCCAGATTGCTTCATTCCGGATAACTTTCATGAAGTGTTTCAACGGATCGGAATACATGGAACAAAACCGCGCTGGAACAAAAGAACTGGAGAACTAGAAACGCCACACCATGTCGAAGGAGGCGTCACCGCCGAAGATTATATTCAAATCGCAGCCGCGGTAATCACAGCGCCCGATGCAATAGTAGCCCATGATCAGGACGGAGGAGAGACGCGGTTCTACACGAAGGAAATCGACGGGCAATCCTGGGTCGCCGTTATTCCTGAACACATAATACCGGGCAGACGGGATCCGACGATGTTTCCTCTTTTAAAAGAATCACCTCAATCGTATTTCAAGAAAAAAATGTCTTCCAGATGGACGGAGAATCCAAGAGTCTTATTTGATTGTTGTGTCGACCTAAAAATACCGAAGCGGGTCCTGGATGCACGGCGAGAAGCAAATGCACAGAAACTCAGTGTCACGCCACACGCCAACGACGCAAAGAAAACCAACGAGGTCAGAGCACCGCATCCTGCAAACTCTACATCTGCACCTGCACCCGCAGCACAGCCCGTTGTAGCTACCGTTATAGACGATCAGAGCACGAGCGCGCCCGTAACCTCTCAGAACTCCACTGAGGCGACACCGTCCATCGATTCCCAGAAGTCAGTACCGGCAGAGCATGAAGTCAACTCGACGTCGCTCGAGGCTGCATCAGTTGGCGATACAACGTCATCCAATATCTCGACTGATAACAGCCTAACCTCCACTAAGGAATCGATATCTTCTGGAAGCAACCAACAAATAAGAAATGAATCATCAACGCAGCGTGATATGCTTTCGACTCCTTTAGAGGGGGAGACTACGGCAACTGATCTACAGTCAGGCGCACACATCGACACGTCGGTCGATCATGGTTCCATTTCTGCTTCCTCCCAGCCAGTCGCGGAATCCGTCACGTCTCACGATGTAGAAACAGCCGGTGTCGATACCGCCGATGTCGATGCTGTGGAAGCCACCAACGTATCATTGAGTTCTTCTGAGCTTACAAGCGGAGAGACCGGCTCTGTATCTGATGTGACCTTTGACTCTTCCGATGCTGGGAGTATTGAAGCCGTTGAGATGGATACACCTAGCCCAGATGGACTGTCTGCCGCCGGTGAGGACTCACTCGAGGCGGGAGACCAGTCTGCTGCGGTCGATGTCTCGTCGGCAGAACAGGCGGAGTCTGTGGGCGATGCGGTAGCGGTAGATACCGATGGCGTTTCGGATCGAGAGGCAGATGCTCTCTCTGCGGACGAGGATGAGTCCCCTTCCGCGCTTGATGTGGTGGCGTATGAGGCTGTCGAAAGCGGCGAGATCAGCCTTGATAGCGTCCCGTCTGAAGATGATGTGGGTGCCGAGGATGTAGCCAGCGAGGAAAACAACGGGGAGCTTGGCCCCGATTTTCTTTCTAGCGATGAGTCGTCGGTTGCAGATCAGGCAGCCGCAGCCGAGAGCGCCGACAGTGCCCTAGACGCTCTGTCTGATGCTGAGATGGACGACGGTGATGAAGTTTCCATCGAAGACGAGGCAGGACTTGAAGCAGATGTCATCACGGAGTCGGAAACGGCCGAGGATGCTCTGTCACTCGATCTATCACCACAGAGTGCAGACGGGACCGCTGCCGAGGTTGACGATGGCTCGCTAGACGTCGACGAACAGGCGGCCGTCGAAGACGTCGCCGCTCTTGAAGACGCTGCCAGCGTAGAAGACGAGGGCGATATCGACTTGGATGCTGCGCTGTCCATTGAGCCTGCGATGGAAGATCAGTCGGGGGCAGTAGATAGCGACGAGGACGAGCTGGACTTCGTATCCGAGGCCGATGTCGCGGAACTTGAGGCGTCGCTCTCCGACAGCGACGCGGCACTTGACGACGCCACCGACCTTCAAGGTGAGTTCTTAGCCGCGGACGACACTGATGTCTATGACGTCGACGAGAGTCCTCTAGCAGTTACCGGCGCGCCAGCAGATGAGGATGTCCTATCGGACGGCACAGCAGACGCCGGCGACGAGCTAGAGTTCGTATCAGAAGCCGAGATTGCAGAGCTAGAAGCGTCACTCTCCGATGGCAATGCGGCACTTGACGACGACTTTATGTCGGAAGATGAGCAGGCAGACATGGCAGTGCAAGACTCACCATCGGCTCTCGATGACACCACCGACCTTCAGGATGACGTCTTGTCCTCGGATGACACTAGTAGCATCGATGATGATTTCCTCTCCGTGGATGACTTGGCGGTAGATGAGGAGGATTTGCCGGATAGCGCCGTAGATGCCGGCGACGAACTAGGTTTCGACGAGCAGGCAGATGTCGGTCTTGACGCCGACAACGATGGTCTTGATATTGATACAGATGCAACTGACATAGATGCCGATGATGATATCGATGCCGACGACGACGATGACGTCTCAGAGAGCGGAGGTTTCTCGCTATGA","MSTEAQMDVERYGFNPGDMPDCFIPDNFHEVFQRIGIHGTKPRWNKRTGELETPHHVEGGVTAEDYIQIAAAVITAPDAIVAHDQDGGETRFYTKEIDGQSWVAVIPEHIIPGRRDPTMFPLLKESPQSYFKKKMSSRWTENPRVLFDCCVDLKIPKRVLDARREANAQKLSVTPHANDAKKTNEVRAPHPANSTSAPAPAAQPVVATVIDDQSTSAPVTSQNSTEATPSIDSQKSVPAEHEVNSTSLEAASVGDTTSSNISTDNSLTSTKESISSGSNQQIRNESSTQRDMLSTPLEGETTATDLQSGAHIDTSVDHGSISASSQPVAESVTSHDVETAGVDTADVDAVEATNVSLSSSELTSGETGSVSDVTFDSSDAGSIEAVEMDTPSPDGLSAAGEDSLEAGDQSAAVDVSSAEQAESVGDAVAVDTDGVSDREADALSADEDESPSALDVVAYEAVESGEISLDSVPSEDDVGAEDVASEENNGELGPDFLSSDESSVADQAAAAESADSALDALSDAEMDDGDEVSIEDEAGLEADVITESETAEDALSLDLSPQSADGTAAEVDDGSLDVDEQAAVEDVAALEDAASVEDEGDIDLDAALSIEPAMEDQSGAVDSDEDELDFVSEADVAELEASLSDSDAALDDATDLQGEFLAADDTDVYDVDESPLAVTGAPADEDVLSDGTADAGDELEFVSEAEIAELEASLSDGNAALDDDFMSEDEQADMAVQDSPSALDDTTDLQDDVLSSDDTSSIDDDFLSVDDLAVDEEDLPDSAVDAGDELGFDEQADVGLDADNDGLDIDTDATDIDADDDIDADDDDDVSESGGFSL$","Bifunctional autolysin","Extracellular, Periplasm, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","AAA ATPase containing von Willebrand factor type A (vWA) domain-like","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 166-694 are 37% similar to a (NRRL STRAIN LACTIS KLUYVEROMYCES E CHROMOSOME Y- Y-1140) protein domain (PDA0F960) which is seen in Q6CPZ4_EEEEE.Residues 172-620 are 36% similar to a (SURFACE ANCHOR WALL FAMILY CELL) protein domain (PD579361) which is seen in Q97P71_STRPN.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0938","1013385","1014971","1587","6.16","-7.05","57929","ATGAATGATCTACTCGTCTTATCTCGTGCCCTACTCTCGAGCGGCAAGGGGGCCTATCTTGGGGAGGACAGCGAGGGCAGCTTGATCCACCTCCCCAAAGAGCAAACACTGGCGGTGTTGGGGGCTCCTCGGTCCGGCAAGTCGACTCGCGTGTTTGTCCAATCCATCGCCGCGTTTCCAGGCCTTGCGGTGTGTACATCGACACGGGCACCTGGACAGCAGCAGCACCCAGACATCATCGAGGTCACCGAACCCGCCCGTCAGCAGTTAGCGGATACATCAGGCGGCAACGTGGTGCACGTCGCACTCGATCCGGCATCGCCCACCCACTACAAGTCTTGGAACTTCTTGGAGAGGTGCAAAGACTGGAAGGTTGCTGAGGAGCGCGCCAGATTCTTTGTATCCGCTAGCCTGGTGGGTGAACACACCGTCAACAACGCCGACTTCTTCCGAGGAGCAGCCATCCAGGCTTTGGCACCAGTCATGATGGCATGCGCTTTAAATCGTAAGCCTGCTAGCATGTTCGCAGAATTGGTGCGTAAGATGCGGCTACGTAGTTCGGAATCAGACACTGACGTATTTGATTCGATGGGCACCCTTAAGAATGCTTTCAAGAGGAAGCGAGGGGCAACACATCCTGCGAGCCTTGCATTGGCGAACTTTCTCTCGAAAGATAAGATCTCCGACGAGACTCGGCAGAATGTGATGTCTGTGATTGGCAACGTCATCTTGCCGTCGATCGAGCGGTGCTGCCCTGATGGACGCGATGAGTTCACACTATCCGAACTCTTCGACGGTGATTCAACGCTGTATCTGCAGGCACGTTCTAGCGATACACAGATCGTCGCGCCCTTCGTTGCAGCGCTGGTCGGCGCGCTGGTGACTCAGTGGCGCACCACGGCAGTAGAAGAGCGCCCAACCGGGTGCATGCTTGCCCTGGATGAGGTGGCAAACATCGCCCCCATCCATACCCTGCCCGAACTCATGTCCACAGCCGGCGGCGACGGCATCACGGTCATCCTCGGCGTGCAAGACATCGAGCGCATGAACGCGATCTGGCCCGGCCAAGGCTACGGCATCGTGGAGGGAGGCAGCCAGTTGCTCCTGGGGGGCTACCGCGACGCCGCCTACCTGCAACGTGTATCCCAGCTCACTCCCCTGGTCAACCGCTACCACACGAACGTCACGGTCGATCACGAAGCGCTCAAAGCCATCCCACATCGCGGCATCACAACGACTGACCTGATCGAATCGGCAACACGGCGAGCTCGGAGCGTTGAGCGTGTCGATCCACGTATCCGTGGCCTGTGCGACCAGTACTTTCTTCGCATGGAACGCGCCAACATGCTGATGAAGGGGCAACGCATCGACGAGATAGGCGACTCATTCGAAGAGTGGGCGCAGCGCTACGACAGTGTCGTGTCTGTCGACCACGTCGGTACCCTGCGGCACGCCCTTGAGCCACACGAGCTCTTCGAGTTGCCAGACGGTGAAGCGCTAGCCATCTCCGGCACGACCATGGCCATGCTCAAGCTACCCGGCTGGTGGGAGTCGCCCTTGTGGCGGGAGGTGCTTGGAGTGTCCTGA","MNDLLVLSRALLSSGKGAYLGEDSEGSLIHLPKEQTLAVLGAPRSGKSTRVFVQSIAAFPGLAVCTSTRAPGQQQHPDIIEVTEPARQQLADTSGGNVVHVALDPASPTHYKSWNFLERCKDWKVAEERARFFVSASLVGEHTVNNADFFRGAAIQALAPVMMACALNRKPASMFAELVRKMRLRSSESDTDVFDSMGTLKNAFKRKRGATHPASLALANFLSKDKISDETRQNVMSVIGNVILPSIERCCPDGRDEFTLSELFDGDSTLYLQARSSDTQIVAPFVAALVGALVTQWRTTAVEERPTGCMLALDEVANIAPIHTLPELMSTAGGDGITVILGVQDIERMNAIWPGQGYGIVEGGSQLLLGGYRDAAYLQRVSQLTPLVNRYHTNVTVDHEALKAIPHRGITTTDLIESATRRARSVERVDPRIRGLCDQYFLRMERANMLMKGQRIDEIGDSFEEWAQRYDSVVSVDHVGTLRHALEPHELFELPDGEALAISGTTMAMLKLPGWWESPLWREVLGVS$","Type IV secretory pathway VirD4 component","Cytoplasm","TraG/TraD family superfamily","hypothetical protein predicted by Glimmer/Critica","Type IV secretory pathway VirD4 components-like","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[35-353]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","family superfamily","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0938.1","1015216","1015437","222","9.63","4.16","8226","ATGCCAAGCAGCGTCGAGACATATAGCGAGGATGGTCGATGGAAAAATCGCATCCAAGGTAACAGCCGGGCTAGCAACACATTCGACACCAAGGCAGAGGCACAAGCCAAGGGACGCGAGATGGCGCAGAAACTCCGTAGTGAGCACATCATTAAGAAGCGAGACGGCACCATTGGTGAGCGCAACTCCTATGGCAATGATCCTTACCCACCAAAGGGCTAG","MPSSVETYSEDGRWKNRIQGNSRASNTFDTKAEAQAKGREMAQKLRSEHIIKKRDGTIGERNSYGNDPYPPKG$","Hypothetical protein","Extracellular, Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 9-73 are 69% similar to a (MYPE6190 YDAT SAG0550 BSR0071 CGL1806 SE2053) protein domain (PD617654) which is seen in Q8NPK6_CORGL.","","","No significant hits to the Pfam 21.0 database.","","","","1","3","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:55:10 2007","Fri Aug 10 15:55:10 2007","Fri Aug 10 15:55:10 2007","Fri Aug 10 15:49:26 2007","","","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","Fri Aug 10 15:49:26 2007","","Fri Aug 10 15:49:26 2007","","Fri Aug 10 15:49:26 2007","yes","","" "ANA_0938.2","1017568","1016639","930","5.66","-7.39","35558","ATGGTCGATGCCGAGCGCTACACTGTGCTCGTGAAAAAGCTAAGTCTCGAAGCCTGGGAAGCACTGGGTGAAGTTCTTGCTACGCGATGGTGGTACAAGAGGTCATTTGAGAAAGGCGTCCGACGCTTATTCCAGGATCATTCAGAGTTGGTCGCTAATATCGCATTCCAGGTACTAACCAAGCGCGAGGTTGTCGACAGTATCATTATCCGTGCTCAGGGCCAAGAGAGGATGTGCCACGACACTCTCATCCAGGTGATGATTGAGTTGGCCGATACGCGCCCTGACTCTCTAACCGACTATCGAGACGATCAAGCGGAAAAGAAAAGGGCGGCGCTGAACGCCATCGAGCACCTCAAACAAATTGTAGCTCCCTTTCGTGAAGAAGTGGCCCAACGAGAGCGTCTTGAGCGAGAAATGCTCGCACATGCGGAAGCCAAGCAGCGCCGAGACTCGTTTGATGCTGCGCATGAGGATCTTCTTGCGACATTCTTTGCGCTCGAAAAAGATCCGGATCGCCGAAAGGCTGGTAAGGGCCTGGAGCGTCTCATCGCCGATCTAGCCGACCTGTACGACATAAATCCAACCCCAGACTATTCGCTAGCAAACGAACAGATCGACGGTGCCTTCACCTTTGACCATGACGGGTACATTGTCGAAGCGAAATGGCTCAACGAGCCGGTAGGGCGCAGTGAGGGTGACGTATTCACTGCCAAAGTGCGACGAAAAGGTCGCAACACGCTCGGACTCTTCGTTTCGGTAAATGGCTTCTCGGCCGATTTCAAACAAATCTATCGAGAAGGATCATGCTTCATCACTATGGACGGAAGTGATCTATATAACGTTCTTAGTCAGCGGGTGTCCTTCGACGACCTCCTGCGCGCCAAGAAACGACATCTCGACGAAACTGGTTCATGTTTTATGGATTGA","MVDAERYTVLVKKLSLEAWEALGEVLATRWWYKRSFEKGVRRLFQDHSELVANIAFQVLTKREVVDSIIIRAQGQERMCHDTLIQVMIELADTRPDSLTDYRDDQAEKKRAALNAIEHLKQIVAPFREEVAQRERLEREMLAHAEAKQRRDSFDAAHEDLLATFFALEKDPDRRKAGKGLERLIADLADLYDINPTPDYSLANEQIDGAFTFDHDGYIVEAKWLNEPVGRSEGDVFTAKVRRKGRNTLGLFVSVNGFSADFKQIYREGSCFITMDGSDLYNVLSQRVSFDDLLRAKKRHLDETGSCFMD$","Hypothetical protein","Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 137-298 are 43% similar to a (MA3443) protein domain (PD665413) which is seen in Q8TKG4_METAC.Residues 199-309 are similar to a (MSI087 PLASMID) protein domain (PD605326) which is seen in Q88GM7_PSEPK.","","","No significant hits to the Pfam 21.0 database.","","","","1","3","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:54:58 2007","Fri Aug 10 15:54:58 2007","Fri Aug 10 15:54:58 2007","Fri Aug 10 15:53:07 2007","","","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","Fri Aug 10 15:53:07 2007","","Fri Aug 10 15:53:07 2007","","Fri Aug 10 15:53:07 2007","yes","","" "ANA_0939","1017994","1017611","384","7.13","0.35","13883","GTGTGGTCAGTCGCCACCCATGCTGCTCACCTCCCTCCACCTCGGCTGTCACCTCTAGAATGCCATACAGGTATGGTGGTGCCAAGTAGGCACCCGCTCGACGCTGGTGCCGTGCGCGACTCCTCCTCCACCAGCCAAGACGAGCAGTGGTGGCTGATCGCCCACCAGCTCGGCCTGCGGCTCCAGCGCGCCCGCATCGCCAAGGGCCTCAGCCAGGAGTCCCTGGCCCATGCCGCTGGCATCTCCACCTACACCTACCAAAAGTTCGAGAAGGGCGAGTCCCGCCCCGGCACCCCGATGAACCCACGCCTGCGCACCCTCATCGCCCTGGCAACGGCGCTGGACATGCAGGTGGAGGAGCTGGTGGGTGGGATTGAGGAGTAG","VWSVATHAAHLPPPRLSPLECHTGMVVPSRHPLDAGAVRDSSSTSQDEQWWLIAHQLGLRLQRARIAKGLSQESLAHAAGISTYTYQKFEKGESRPGTPMNPRLRTLIALATALDMQVEELVGGIEE$","Transcriptional regulator","Cytoplasm","transcriptional regulator","hypothetical protein predicted by Glimmer/Critica","helix-turn-helix domain protein","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[61-121]T$	HTH_3
SM00530	$\"[60-121]T$	HTH_XRE
PS50943	$\"[61-121]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[57-124]T$	no description

","BeTs to 9 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 61 to 121 (E_value = 9.7e-10) place ANA_0939 in the HTH_3 family which is described as Helix-turn-helix.","","regulator ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0940","1019283","1018057","1227","6.48","-2.29","46478","ATGCCCAATATCAATCCCTCCCTCCACCACCGCCTCCGCAAAGCCAAGGCCGCCCTCCTGGTCGTCTCCTTCACCCTGGCCGGCATCCTCCTCATGATGCTCAACGCTTGGCTGTCCCCGCTGCAGTTGGGTGACTGGCAGTGGCTGCATGCGCTGCCGCTAGGCGAGCTGGGTGGGACGCTGTTTGGTGCGGGGCTGCTCTCGACGTTCTTTGAGTACACCTTCCGGCGCGATCAGGAGCGGGCGGTGACAGAGCGCTTCCGCCAGACAATCCGTGATGAAGCACCGGCCCTGCGCGATGCCGTCATCGAGGCCTTTCGCTTCGACCGCCAGGACGTCGCGCGTATAGCCACACCTCAGCTGCTGGATGATCTGGCTCGCACTAGCCTGGGTCTGCGCTTCGGCGACTCTGCGTTCGGCCGTGAGGTCTATGCCGACATCCGTCACCAAGCCATGGCTGCCGAGGAGCGCTGGTACGACGCCCGCGTCGACGCGGCCCTTGGTATACCAAGGGGTAGGAGCGTTGCTCCTACCCCGTTCTTCGACTTACGTGTCCGCTGGGAGTACACCGTCATGCCGCGGCACCGCTTCCGCAAGTTTGCCGTTGTGTCCGACCGCCAGCGCTACGACCAGCTGGTAGCCGAGCGTGGAGAGACGAGTGTGTGGTATCGCCGGCCAGTGCCTGGGCTGGCTGTCTCCGATCCAGAGGTCTTCGCCCTGGAGCAGTTCACCGTCAACGGCACGCCGGTGCTGTTCACCCGGCAGTTCGATGAGGTCTCCCAGGTCTACACCGTTGATCTTGGCGAGCAGGTCATCCAGCAGGAGCAGACGGTCGTCATCTCCTTCAGCTTCCGCACCCGCACGCTCCGCAGTGGCCATGTGGTGCACCTGGACATCGACCGCCCCACGCGCGGTCTCGACGTCGAGCTGCGCTACGACCCAGAGCAAGTCGGCCAGATGCGCATCCTCGACTTCGCCTCCATCGGCGAAGGAGGACGCCTCACCCAAGTACCGAATACGCCGACGCTGCGTTACCGCTACGACGGCTGGCTCTTCCCGCGAGCTGGCATGGTCTTCGTCTGGACGCTGCCAGACGAGCAGGACGACTGGGCTGAGGTCGCGCCCGACACCAACGTCAGACCACCACGCTCAGCCGGTAGTTCTAAGAACGCCATCGAGGCAGTACCAGCCACGGAAGACGACGCCCGCCAAGCTCGCGCAGCCTGA","MPNINPSLHHRLRKAKAALLVVSFTLAGILLMMLNAWLSPLQLGDWQWLHALPLGELGGTLFGAGLLSTFFEYTFRRDQERAVTERFRQTIRDEAPALRDAVIEAFRFDRQDVARIATPQLLDDLARTSLGLRFGDSAFGREVYADIRHQAMAAEERWYDARVDAALGIPRGRSVAPTPFFDLRVRWEYTVMPRHRFRKFAVVSDRQRYDQLVAERGETSVWYRRPVPGLAVSDPEVFALEQFTVNGTPVLFTRQFDEVSQVYTVDLGEQVIQQEQTVVISFSFRTRTLRSGHVVHLDIDRPTRGLDVELRYDPEQVGQMRILDFASIGEGGRLTQVPNTPTLRYRYDGWLFPRAGMVFVWTLPDEQDDWAEVAPDTNVRPPRSAGSSKNAIEAVPATEDDARQARAA$","Hypothetical protein","Cytoplasm","","","","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[15-37]?$ $\"[51-71]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","3","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:08:19 2007","Wed Aug 15 12:08:19 2007","Wed Aug 15 12:08:19 2007","Wed Aug 15 12:04:25 2007","","","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","Wed Aug 15 12:04:25 2007","","Wed Aug 15 12:04:25 2007","","Wed Aug 15 12:04:25 2007","yes","","" "ANA_0941","1019397","1021328","1932","5.91","-12.13","71552","TTGGACACCCACCCCATCTGCATTACCATAAGTTGGAAAAACATGGAAGATAGCAAACTCGATCAGTATTCAAAGAGCGATATTGCACGGATTGCCGATGTCATTAATATCGTGGCCGCCGAAGCGAACCAACCGTGGGTGATTCTTCAGAAACTCAGCGAACGAGCTCATGCTGCACCAGATCTCAAAGACAATCCGGTGCTTCCATACGCTGAGAGATCGCTTGCCTATAGTTTTACTGAGGACAAGAAAAATCCTGGTTCTGTGACGCTTGGCGTACGTCTATCCAGCGCAAGCGATGAGTGGCCGCTGGCATTTAAAGATGTTTCTTCAATCGAGAAGCAGGCTTGGTGCGAAATTGCAAACCAGTGCACACATCATCTAGCGAAGGCACACATGCTGGATGTAGCACTATCGTCTGGCATAATCCGCGGGCGCGACGCCGCTAAGGAGATCGCTGATCTCTATCTAGCAGTCGCTCAAAATGTCAACATAGAAATATACTATCGAGGCGGCTGCCTACGTCGTTGTTGGAGTATTGCTCGTTCATATGGCTTGCATACATTAGAAGCGCAGGCAAAGAGTGCGTCCTATCAGATGGCACACCAGATGGTGCAACTTATGTTCAAACCACCTGAAATCCCCACAGGAATCCTGCTGCAGCCGTTTGAAATAATTACTGTTCTCCCGCAGTGCGGCGAATTTAACAATCCCAGTCGACAAGACGTGCAGACTCTACTAAAGCAGGTTCGCTCCCGGTCGGCAACCAACGTGTCGACCCTTGAAGGTGTATCCGAATTGCTTGTCAGAGTGGCGAGCACAGATTCTGAGCGCGACGAAGCACGCCGCTCGCTGATAGAGAGCTACCTCGCTTTAGGCGAAGGCGCGAAGGGGATGATTGCTTCCTCGTATTTCGAGGATGCAGCCAGAATAGCAAGTAAATATGGGTATATCGACTTAAGAGATCGCGCAGTACAGTTGTTGCAGGCCGTGCCGTATGAAGACCTCGGCATGCAAACACTTCCAATTGAGCTACGAATCCCCTGTTATGCCATTGATGCAACGCTGGATCACTATCGGCATTCGCGAGATGGGCTTTCTGCGCTTGACATCTGGCTAGCTGGCGCGTCCCCCACCGGCTCTTACGAAAGTAACGTTGCTTCTGCCAAGGAAAGTATGGACGGCTCTATTATTGCTGCGGTAACCAGAACCACTTTTGACGGAAACATGCCGACACGTACGAGCGCAGGCGTTGAAAGTGCGGTCGTCGATGCGACTGAGCGGCAGGAACTGATCAACGCGGGACTTTATGGGCAGATGCTTGCGCATGAGCTTAAGGCGATTAAGCATCAATACGGTATTGTCACGCCCACAAAAATTACAGCTCATCTGGTACAGACCTATCGATGTGACTCGCAACTTGCTCTTGCGCTGGGGCAAGCCATCGTTAGTTTCTGGGACGAACGCTACACCGACGCTGGACGTGCTGCTTTTCCTCTCGTCGAAGCGGGAGCTCGAGGCGTTCTGCTATTGCTTGATGACCCACTGTATCGGATCCAAACAGGCAACGCTGGAGGGCACTTCCCGTCACTCGAAAAGTACGCCGAGAAACTTGAGCAGCATAACTTCGACATCGATTGGCTTCGGTGCATCCGCAATCCTGTCGCCAAGTGGCGCAATGCTCTCGCTCATGGTCATCGGCTTGAACTAGCAGACTATGAGGCAGCCGTGCTGCTGCGTACCGCCGCGCTACTCGTTGTCTTGACGTCGAGTAACTCTTCCGAAAAAGACAAAGAGGAAATTGAGACGAACCTCCGCGACCCAATACGCTGGGCGGCCAACCAAGCCGAACTTATACAAAAGTGGGAGCAAGTATGGACGCCAGTATGGGAGCACAAAATTGATACAAATGATCTAAAGGAGTCACGATGA","LDTHPICITISWKNMEDSKLDQYSKSDIARIADVINIVAAEANQPWVILQKLSERAHAAPDLKDNPVLPYAERSLAYSFTEDKKNPGSVTLGVRLSSASDEWPLAFKDVSSIEKQAWCEIANQCTHHLAKAHMLDVALSSGIIRGRDAAKEIADLYLAVAQNVNIEIYYRGGCLRRCWSIARSYGLHTLEAQAKSASYQMAHQMVQLMFKPPEIPTGILLQPFEIITVLPQCGEFNNPSRQDVQTLLKQVRSRSATNVSTLEGVSELLVRVASTDSERDEARRSLIESYLALGEGAKGMIASSYFEDAARIASKYGYIDLRDRAVQLLQAVPYEDLGMQTLPIELRIPCYAIDATLDHYRHSRDGLSALDIWLAGASPTGSYESNVASAKESMDGSIIAAVTRTTFDGNMPTRTSAGVESAVVDATERQELINAGLYGQMLAHELKAIKHQYGIVTPTKITAHLVQTYRCDSQLALALGQAIVSFWDERYTDAGRAAFPLVEAGARGVLLLLDDPLYRIQTGNAGGHFPSLEKYAEKLEQHNFDIDWLRCIRNPVAKWRNALAHGHRLELADYEAAVLLRTAALLVVLTSSNSSEKDKEEIETNLRDPIRWAANQAELIQKWEQVWTPVWEHKIDTNDLKESR$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0942","1021325","1022995","1671","5.25","-20.94","64031","ATGACAGAACACAATGAACTTGATGACTACGAACGCGAGCAGATCCGGGATCGACTCAAGCAAGAGCGGATGATCAAATCGGCCTGCGCCAACGGCGATGGTCCATGGACGATTGTGTATGACGACTGGCGTTTCGACAATGATGACAACGGCGGTCGATACATGGCGTTCGCTCAGCCACAGATGCGCGACAAGATCCTCTCGCACGGCGGTTGGGATTTTTCGAAAGGAGACGGATTTCCTGGATTTGTGACGAACGGAGAAGAAACAAGGTATGCGAAGGGGGATAAACTACCCGAGTTTGAGCCTCTCGTAATTTACCGGCACTATTACGGTGTCGTTCCTGACGAGTTGCATATTTCAGAAGAGTTCAGGCTCCTGATGAACCTGTGGCAGGATCCGAAGTCTGGTGACTACCATGAAATCAAAGATGACGGCTCAAAAGAGCTTGCCATTAAAGTTAAAGACAAGCGAATCGAAGTGCGGACGCCGCTATTGAAGCGCTATATGGCGGCACGGCAACTCGATGCCGTGCTATTCATCGACACGAGGGTGTCTGTTGAATATGCTGGCGATGTCGCGGATTTTTCGGATCTCAAGTTTGAGGGACAAATTGGCGATGAGCTCATGTATCTTTCGCGAAGTGTTGGCAGGTCACCGCTTAGTGATGCACGTGTTGGCTCATTGGTGTTCGCCAAGCGCATTCTTCCGGCCCCTCCCCAGGAAACCTGTGGAATCTGGCCCTGGGACGAGGATGATCCTGCGGACTACCCAGAGTTCATCATTGACGAGGACGAGTACGGCAAACCAGTCAAGTACACATGCGACCCGGATCTTCTTGCCAACTACTTCGGCAAGAATCCGGACGCGCCACACTACCTCACGCCAGTATTCTTCAAGCCAGAGGTGCTCCAAAGATACTATGACGATTCCGACCTATACACAGTGAGCGATGGGCGTCTATCGTGCGCTTCCATGTGGGGCGTTAAGATCGACAATGGCAACCCAAATTGCGTCGTCGTGTTCCTTGGCGATATCGGTCGCGATATTCCTGCAAGCCACCGGACACACTGGCTCTCATACAACGTGTCACCAACACAACGCATGAGCGACGTAGGCGTGCGCCGGGCTTTTTTCGGTCAGTTCGCAGACAGTGAGAACCCAGAACACCGCTTCAAACTGGCGTACAACCAACTACAGAACTCATGGGAAGAGCACTGGGGATGGCGGCTCCACCGCAAAGCAGAGGGGCAAGACGCTGGCGTGCTTCAGCGTCTGCGCATCCCCGTCAATGACACCGACGCAGAACTGCGCGCACAGTTGATCAACCTCGCACTTGTCTTGGTGGATTACCTCAATGAGAAGCAGGTGGCCTCGTACCTCTCAGACACCAAGGGAGACAAAGGCATCGCCAAGCTCAAGAAGTTCCTCACGGCCCAGTCATACCGGCATACCGAACGAGATGTCCGTCTTCTGCAAAGAATCCAGAGGATGCGTTCCCGCATTGCGGCACATTCGTCAGGCAGCAGTGGACAGGCCTATCTCGAGGAAGAACTCGGGAAGGACACTCCGCAGGAGTACATCGCACGCCTCATGACCGAAGCAACGCAAATGCTGGACGACCTCAGGGTGTTTGCGGAGGAGCAGTCGAGGCAAGACTCGGACTCATAA","MTEHNELDDYEREQIRDRLKQERMIKSACANGDGPWTIVYDDWRFDNDDNGGRYMAFAQPQMRDKILSHGGWDFSKGDGFPGFVTNGEETRYAKGDKLPEFEPLVIYRHYYGVVPDELHISEEFRLLMNLWQDPKSGDYHEIKDDGSKELAIKVKDKRIEVRTPLLKRYMAARQLDAVLFIDTRVSVEYAGDVADFSDLKFEGQIGDELMYLSRSVGRSPLSDARVGSLVFAKRILPAPPQETCGIWPWDEDDPADYPEFIIDEDEYGKPVKYTCDPDLLANYFGKNPDAPHYLTPVFFKPEVLQRYYDDSDLYTVSDGRLSCASMWGVKIDNGNPNCVVVFLGDIGRDIPASHRTHWLSYNVSPTQRMSDVGVRRAFFGQFADSENPEHRFKLAYNQLQNSWEEHWGWRLHRKAEGQDAGVLQRLRIPVNDTDAELRAQLINLALVLVDYLNEKQVASYLSDTKGDKGIAKLKKFLTAQSYRHTERDVRLLQRIQRMRSRIAAHSSGSSGQAYLEEELGKDTPQEYIARLMTEATQMLDDLRVFAEEQSRQDSDS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0943","1023740","1023165","576","8.94","3.86","20627","ATGGTGCTTCTGGACTTCCGAAGGAAGCTGGCCGCCGGTGAGGGCGGCCAAGTGTGTACCGGCCCCAATGTAGCGCATCTGCCGGCTACTGACGGGTCGGATGGCGCGGTGGGCGATGCGGACGAGCCCATGCCGTCTCACGGGGCAGATGCGGCAGAGCCAGAAGGTGAGCTCGTGCAACGACGATGCACCGCACCGGCCACCGGTGTGGGGGAGCGGCCGAACGGTGAGAGTGATGCGCCTGACACAGCGTCACGGTCACCGCGCGTGGTCGACCGCATCAAGCAGACGAAGTTCCGGCCGCTCACACCCGAGCAGCGCCAGCAGGTGATTGACCTGTACCGCGCCGGCGTCCCCGTCAAGGAGATCGTCCGGCAGACGGGCGTCAACCGCTCGACGGTCTACCGGCTGCGTGGGCAGGCAGGGCTGGAGCGCAGCCACCGCTTCACCGACGAAGACCGCGCCCAAGCGATCCTCCTCCGCCAACAGGGCCTGACCATCGCTGAGATTGCCAAGCGGTTGGGCTTCAGTGGCATGACCATCGGGCGTCACCTGGCGGCTGCTCGCAAGGAGTGA","MVLLDFRRKLAAGEGGQVCTGPNVAHLPATDGSDGAVGDADEPMPSHGADAAEPEGELVQRRCTAPATGVGERPNGESDAPDTASRSPRVVDRIKQTKFRPLTPEQRQQVIDLYRAGVPVKEIVRQTGVNRSTVYRLRGQAGLERSHRFTDEDRAQAILLRQQGLTIAEIAKRLGFSGMTIGRHLAAARKE$","Resolvase","Cytoplasm, Extracellular","Helix-turn-helix domain of resolvase protein","hypothetical protein predicted by Glimmer/Critica","Resolvase helix-turn-helix domain protein","","Skarstad K., Boye E. The initiator protein DnaA: evolution, properties and function. Biochim. Biophys. Acta 1994. 1217(2):111-130. PMID: 8110826Yoshikawa H., Ogasawara N. Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial replication origins. Mol. Microbiol. 1991. 5(11):2589-2597. PMID: 1779750Georgopoulos C. The E. coli dnaA initiation protein: a protein for all seasons. Trends Genet. 1989. 5(10):319-321. PMID: 2558436Skovgaard O. Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli. Gene 1990. 93(1):27-34. PMID: 2172087","","","

InterPro
IPR006120
Domain

Resolvase, helix-turn-helix region
PF02796	$\"[100-136]T$	HTH_7

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[151-191]T$	no description

InterPro
IPR013249
Domain

RNA polymerase sigma factor 70, region 4 type 2
PF08281	$\"[152-190]T$	Sigma70_r4_2

","No hits to the COGs database.","***** IPB001598 (Transposase IS30) with a combined E-value of 6.1e-07. IPB001598A 148-183 IPB001598A 101-136***** IPB006118 (Site-specific recombinase) with a combined E-value of 3.3e-06. IPB006118D 117-136 IPB006118D 164-183","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 100 to 140 (E_value = 0.00032) place ANA_0943 in the HTH_7 family which is described as Helix-turn-helix domain of resolvase.Residues 152 to 190 (E_value = 3e-05) place ANA_0943 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.","","domain of resolvase protein","","1","3","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0945","1024023","1025195","1173","5.20","-11.49","42136","ATGAAGATCGCCGCCCGGGCCACAGCCGCTCAGCCCTTCTATGCGATGAGCATCGGCGAACGCGCCGGAATCCTCCAGGCGGAGGGCCACTCGATCGCCAAGCTCAGCCTGGGTGAGCCTGATTTCGGCGCCCCTCCCGCGGTCCGCGAGGAGATGTGCCGCATCATGGACGGCCGGCCACTGCCCTACTCCCCCGCCCTGGGGCTGCTCGCACTGCGTGAGGCCATTGCCGGTTTCTACCGGGACAGGCACGGCGTTGAGGTCGATCCCGCCCGGATCGTCGTCACCACTGGTGCGTCGTCGGCGCTCCTGCTGGTGGCCGCCGCCACCACGCAGGCCGGCGACGACGTCGTCATCGCCGACCCGTCCTACCCCTGCAACCGGCAGCTGGTGGAGACCTACGGCGGCCGGATCATTCTGGCACCCACCAGTCCTGCCAGCCGATACCAGATGGACCGGGCCGCAGCCGAGGCGGCGTGGACTCCTCAGACGAGCGCGGTGATGCTGGCAACCCCGTCCAACCCCACAGGCACATCCATCCCCTTCGAGGAGCTGGCATCGATCTGCGAGCTGGCGCGCGAACGCAGCGCTTGGCGCATCGTCGACGAGATCTACCTGGGTCTGGCTGATCCAGGCGAGGACGGCCGGCCTGCGCGCACCGTCCTGGAGACCGATCCTGATGCGATCGTCATCAACTCCTTCTCCAAGTACTTCGGGATGACGGGGTGGCGGCTGGGCTGGGCGATTCTTCCCGAGGAGCTGGTGGCTCCCGCGGAGAACCTGGCGGTGAACTACTTCCTGTGCGCCTCGACGCCTGTTCAGCAGGCTGCGCTGGCGGCCTTCTCCCCCGAATCCATCTCCGTGTGCGAGCAGCGCCGACACGAGCTTCTCGCCCGCAGGAGCATCGTGCTCGATGGGCTGCAGCGCATCGACCTTCCGGTTCCGGTCCTGCCCGACGGCGCCTTCTACGTCTACTTCGACGTCTCCTCCACCGGGCTTGACGCCCAGACCTTCTGTCACCGCGCCCTGGAGGAGGCACATGTGGCGCTCACCCCGGGGCAGGACTTCTCCACGACCACGGCCCGCTCCCACGTGCGACTGTCCTACGCTGCCTCCCGCGACGAGCTGCACGAAGGAATGAATCGCCTCAAAACTTTCATTAACAGCCTGTAA","MKIAARATAAQPFYAMSIGERAGILQAEGHSIAKLSLGEPDFGAPPAVREEMCRIMDGRPLPYSPALGLLALREAIAGFYRDRHGVEVDPARIVVTTGASSALLLVAAATTQAGDDVVIADPSYPCNRQLVETYGGRIILAPTSPASRYQMDRAAAEAAWTPQTSAVMLATPSNPTGTSIPFEELASICELARERSAWRIVDEIYLGLADPGEDGRPARTVLETDPDAIVINSFSKYFGMTGWRLGWAILPEELVAPAENLAVNYFLCASTPVQQAALAAFSPESISVCEQRRHELLARRSIVLDGLQRIDLPVPVLPDGAFYVYFDVSSTGLDAQTFCHRALEEAHVALTPGQDFSTTTARSHVRLSYAASRDELHEGMNRLKTFINSL$","Aminotransferase, class I and II","Cytoplasm","aminotransferase, classes I and II","aminotransferase; class I and II ","aminotransferase, class I and II","","Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K., Okamoto A., Higuchi T., Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 1991. 266(4):2567-2572. PMID: 1990006","","","

InterPro
IPR001176
Family

1-aminocyclopropane-1-carboxylate synthase
PR00753	$\"[92-112]T$ $\"[161-185]T$ $\"[227-251]T$	ACCSYNTHASE

InterPro
IPR004838
Binding_site

Aminotransferases class-I pyridoxal-phosphate-binding site
PS00105	$\"[233-246]T$	AA_TRANSFER_CLASS_1

InterPro
IPR004839
Domain

Aminotransferase, class I and II
PF00155	$\"[30-383]T$	Aminotran_1_2

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[45-289]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[47-387]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF35	$\"[47-387]T$	ASPARTATE AMINOTRANSFERASE

","BeTs to 24 clades of COG0436COG name: PLP-dependent aminotransferasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0436 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB001176 (1-aminocyclopropane-1-carboxylate synthase signature) with a combined E-value of 1.4e-41. IPB001176B 57-73 IPB001176C 92-112 IPB001176D 114-135 IPB001176E 161-185 IPB001176F 197-220 IPB001176G 227-251 IPB001176H 260-283***** IPB004839 (Aminotransferase, class I and II) with a combined E-value of 4.5e-14. IPB004839A 158-178 IPB004839B 202-209 IPB004839C 235-246***** IPB004838 (Aminotransferase, class-I) with a combined E-value of 6.5e-12. IPB004838C 167-179 IPB004838D 233-246***** IPB011715 (Tyrosine aminotransferase ubiquitination region) with a combined E-value of 2e-09. IPB011715C 94-137 IPB011715E 168-205","Residues 32-124 are similar to a (AMINOTRANSFERASE TRANSFERASE PHOSPHATE PYRIDOXAL ASPARTATE TRANSAMINASE HISTIDINOL-PHOSPHATE SYNTHASE BIOSYNTHESIS TRANSCRIPTION) protein domain (PD000087) which is seen in Q8G3L7_BIFLO.Residues 140-205 are similar to a (SYNTHASE PHOSPHATE PYRIDOXAL AMINOTRANSFERASE 1-AMINOCYCLOPROPANE-1-CARBOXYLATE TRANSFERASE LYASE ACC ALANINE TRANSAMINASE) protein domain (PD534063) which is seen in Q8Y1I0_RALSO.Residues 149-383 are 37% similar to a (AMINOTRANSFERASE TRANSFERASE AMINOTRANSFERASE VNG0981C) protein domain (PD284757) which is seen in Q9HQW2_HALN1.Residues 166-208 are 74% similar to a (AMINOTRANSFERASE TRANSFERASE ASPARTATE 2.6.1.- PHOSPHATE PYRIDOXAL LYASE I PROBABLE AMINOTRANSFERASE) protein domain (PD769199) which is seen in Q8G3L7_BIFLO.Residues 214-253 are similar to a (AMINOTRANSFERASE TRANSFERASE ASPARTATE PYRIDOXAL PHOSPHATE TRANSAMINASE I A AMINOTRANSFERASE 2.6.1.-) protein domain (PD093786) which is seen in Q8G3L7_BIFLO.Residues 225-387 are 42% similar to a (IPF3549 SIMILAR CANDIDA NEUROSPORA DEBARYOMYCES HANSENII FUNCTION Q8X012 B23H20.010 DEHA0E05104G) protein domain (PD769191) which is seen in Q8X012_NEUCR.Residues 229-369 are 46% similar to a (AMINOTRANSFERASE TRANSFERASE ASPARTATE) protein domain (PDA034S2) which is seen in Q6SHK8_BBBBB.Residues 259-322 are similar to a (AMINOTRANSFERASE TRANSFERASE ASPARTATE PYRIDOXAL PHOSPHATE TRANSAMINASE AMINOTRANSFERASE A PROBABLE I) protein domain (PD711857) which is seen in Q8G3L7_BIFLO.Residues 339-387 are similar to a (AMINOTRANSFERASE TRANSFERASE ASPARTATE PYRIDOXAL PHOSPHATE TRANSAMINASE A AMINOTRANSFERASE I 2.6.1.-) protein domain (PD001245) which is seen in Q8G3L7_BIFLO.","","-48% similar to PDB:1B5O THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1 (E_value = 3.1E_46);-48% similar to PDB:1BJW ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS (E_value = 3.1E_46);-48% similar to PDB:1BKG ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS WITH MALEATE (E_value = 3.1E_46);-48% similar to PDB:1B5P THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 (E_value = 4.0E_46);-48% similar to PDB:1GCK THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE (E_value = 4.0E_46);","Residues 30 to 383 (E_value = 2.9e-55) place ANA_0945 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.","","classes I and II (ASPAT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0946","1025332","1026324","993","6.21","-8.06","38230","GTGATCGCCACCGTCGAGATCTCCAAATCAATCCATCAAAAAATACGCTTGCGCCGCGATAAGGCAGCCTCAACCCCGCACCGGGGCGAGGAGTCCACATGGAATGAGCTCACTGAGCATCATCGGCCCGTCAGGCACTCCAAGCCCGAGGAGTTCACCGCCGGCCCGCATGAACGGCTTCTGGCGATCTGCGCGCCGTACTCCCTGTGCCGCCGTGACCCGTGGGACCACCTCACCTGTTCCGACCTTGAAGGCACGCGCACCATGCTGTCTCTCGACTGGGGAGTGCGCTCGCGCGCCGACCTTCTCTCCCAGGTCCACTGGCTCATCACCTGTGGGCACCGCACCGGTTTCGATGCCGAGCGCGCCCGCTGGGTCGACACCTCTCTCGCGGAGGCCGAACGACACGACCTACGAGAGAGTGCCGAGTCATCCTCAGACTCGGCCGAGACACTGTGGCGCCTCGAGCGCATGCTCAACAATGATCGCGACATCCGCAACGTGGACTTCTCCGCCTGGGACCTGGTGCGTGCCGGCATGCTGACGCGCTGTGGATTCGCGCTGGGGTGGCTGACCGAGGACGAGACCTGGGACACGCTCGCGATCCTGGATCAGGGGCTGCGAGAGCGTTATCGGAGCTGGACGCAGGTGTCGGAGTCGTTCCGGCTGGCACGCTGGTACTGGAGCTCCACGAGTGGCAAGGACGAGCACTTCAACGACCTGCACGATCTCAACCGCTCGCTGGTTCTCCTCAGCCCCGACGGGCCATGGGGGCTCATCGACTGGGACGTCGAGACTCCCGAGCCCTCGTTCCTGATCCTCGACGACCTGCTCGACGCCGGCGTGGCGATGCCGCTGGGGGCTGGCGAGCGGAGGCACGCCACACAGTGGGAGCGCTGGGTCGACGATCAGGTCATTGTCCGCGGACAGCACCGCCCCCAGCACTTCGGGACCCATGCCGACCAGTGCCACCGGTTCGCCAAGCGCGCCTGA","VIATVEISKSIHQKIRLRRDKAASTPHRGEESTWNELTEHHRPVRHSKPEEFTAGPHERLLAICAPYSLCRRDPWDHLTCSDLEGTRTMLSLDWGVRSRADLLSQVHWLITCGHRTGFDAERARWVDTSLAEAERHDLRESAESSSDSAETLWRLERMLNNDRDIRNVDFSAWDLVRAGMLTRCGFALGWLTEDETWDTLAILDQGLRERYRSWTQVSESFRLARWYWSSTSGKDEHFNDLHDLNRSLVLLSPDGPWGLIDWDVETPEPSFLILDDLLDAGVAMPLGAGERRHATQWERWVDDQVIVRGQHRPQHFGTHADQCHRFAKRA$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","Hershey H.V., Taylor M.W. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene 1986. 43(3):287-293. PMID: 3527873","","","

InterPro
IPR002375
Family

Purine/pyrimidine phosphoribosyl transferase
PS00103	$\"[271-283]?$	PUR_PYR_PR_TRANSFER

noIPR
unintegrated

unintegrated
PD038349	$\"[90-235]T$	Q8X521_ECO57_Q8X521;

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-38% similar to PDB:2DTC Crystal structure of MS0666 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0948","1027018","1026614","405","4.13","-18.55","14002","GTGGCGAGTACAGCGGGTGGGGCTTTCGGCTTCGCCTCCGGTCTCATCATTCAGGAGTTCGGCTACGACGACGACGTCGACGAGACCTTGCGACAGGCCGTTGAGGCGGAGACCGGAACCGCTCTGGTGGATGAGGACTACGAGGACGTGGCTGACTCGGCCATCGTGTGGTGGCGTGATGACGACGGTGACGTCGACGACCTCACCGACCTCCTCGTGGATGCCCAGGCCAACCTTGACGGTGCAGGGCTCATCTGGGTGCTGACGCCCAAGGCACGTACCACCGGAGCCGTCCAGGCCGCCGAGGTGGAGGAGGCTGCCGCGACAGCCGGCATGCACGCGACCTCCGCAGCCTCCATGGGGCAGCACTGGAGTGGCATCAGGGTCTCCAGCCGGGGGCGCTGA","VASTAGGAFGFASGLIIQEFGYDDDVDETLRQAVEAETGTALVDEDYEDVADSAIVWWRDDDGDVDDLTDLLVDAQANLDGAGLIWVLTPKARTTGAVQAAEVEEAAATAGMHATSAASMGQHWSGIRVSSRGR$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 16-131 are 69% similar to a (ML1649 SCO2370 CGL2246 MLCB1243.26 RV2239C/MT2299/MB2263C) protein domain (PD032898) which is seen in Q9KY20_STRCO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0949","1027416","1030169","2754","5.72","-20.88","102205","GTGAGCCCCACCAGTGACTCCACGCCGCTCATTGACGGCCTCCTGACGAAGGTGACCGACAACGACCCAGAGGAGACCAAGGAGTGGCACGAGTCCCTCGATGCCCTCATCGCGGACAAGGGCGCCAAGCGTGCGCGCTACATCCTGCTGAGCATGCTGGCTCAGGCCCGGCAGAAGAACGTCACGGTCCCCACCGAGACGACGACGCCGTACATCAACACCATCGACGTCGCCAACGAGCCCTACTTCCCCGGTGACGAGAGCGCCGAGCGCACCTACCGGCGCTGGCTGCGCTGGAACGCCGCCGTCATGGTCACCCGTGCCCAGCGCCCCGGGGTCGGGGTCGGCGGACACATCTCTTCCTACGCCTCGACCGCGACCCTCTACGAAGTCGGCTTCAACCACTTCTTCCGCGGTAAGGACCACCCCGGCGGCGGCGACCACGTCTTCTTCCAGGGCCACGCCTCACCGGGTAACTACGCTCGTGCCTTCGTCGAGGGCCGTCTGAGCGAGGCCGACCTAGACGGCTTCCGCCAGGAGGAGTCCCGCCCGGCCGGTGGCCGCGGCCTGCCCTCCTACCCCCACCCGCGTCGCATGGAGGACTTCTGGGAGTACCCCACCGTCTCCATGGGCCTTGGCCCGGCTGAGGCCATCTACCAGGCCTGGTTCGACAAGTACCTTCAGGGCGCCGGCATCAAGGACACCTCCCAGCAGCACACCTGGGCCTTCCTGGGTGACGGTGAGATGGACGAGCCCGAGTCGCGCGGCATGCTGCAGCTGGCCGCCAGCCAGCAGCTGGACAACCTCACCTTCGTCATCAACTGCAACCTGCAGCGCCTCGACGGACCGGTGCGCGGGAACGGCAAGATCATCCAGGAGCTCGAGGCCTTCTTCAAGGGCGCGGGCTGGAACGTCATCAAGGTGATCTGGGGCCGCGGCTGGGACCAGCTCCTCGCCGCGGACAAGGACCACGCCCTCGAGCACCTCATGATGGAGACGCTCGACGGCGACTACCAGACCTTCAAGGCCAACGACGGCGCCTACATCCGCGAGCACTTCTTCGGCCGCGACCCGCGCACCGCCGAGCTCGTCAAGGACTGGACGGATGACGAGATCTGGGCCCTGCAGCGCGGCGGCAACGACTACCGCAAGATGTACGCCGCCTACAAGGCGGCCACGGAGCACAAGGGCCAGCCCACCGTCATCCTTGCGCACACGGTCAAGGGCTACCTCCTGGGAGGCCACTTCGCCGGCCGTAACGCCACCCACCAGATGAAGAAGCTGACGCTGGACGACCTCAAGGCCCTGCGCGACCGGCTCCACATCCCGATCACCGACGAGCAGCTCGAGGCCAACCCGAAGATGCCGCCGTACTACCGGCCGGCCAACGACGACCCCTCGCTGCTCTACATGCTGGACCGGCGCCGCCAGCTCGGCGGCTTCATCCCCGAGCGTCGCGATGCCGGAGTCGAGCTCGAGCTGCCCGGTGACAAGACCTACGACATCCTCAAGGGCGGCTCGGGCAAGCAGGAGGTCGCCTCCACGATGGCCTTCGTGCGCCTGCTCAAGGAGCTCATCAAGGACAAGGGCATCGGTCGGCGCATCGTCCCGATCGTTCCGGACGAGTCGCGCACCTTCGGGCTGGAGTCACTCTTCCCCACCAAGAAGATTTTCAACACCCAGGGTCAGAACTACACGCCGGTCGACGCCGACATGATGCTGTCCTACCGGGAGTCCACCTCCGGTCAGCTCATGCACACGGGCATCAACGAGGCCGGTTCGGTCTCCCTGTTCCAGGTGGCCGGCACGAGCTACGCCACCCACGGCGAGCCCATGATCCCGGTCTACATCTTCTACTCGATGTTCGGCTTCCAGCGCACCGGCGACCAGTTCTGGGCCGCCGGCGACCAGCTGACCCGCGGCTTCATCATCGGAGCCACCGCCGGGCGCACCACCTTGACCGGTGAGGGCACCCAGCACATGGACGGCCACTCCCCCATGATCGCGGCCACCAACGACGCCGTCGTCAGCTACGACCCGGCCTACGCCTACGAGATCCGGCACATCGTGCGCGACGCCCTGGAGCGCTGGTACGGACCGGACTCGGGTCGCAACCGAGACGTCATGTACTACCTGACCGTCTACAACGAGCCGATCCACCAGCCCGCCGAGCCCGACAACGTCGACGTCGAGGGAATCCTGCGCGGTATTCACCGCATCAGCACGGCCCCCGACGGCGAGGGCCCCGAGGTCCAGCTCCTGGCCTCCGGTGTCGGAGTGCCCTGGATCGAGGAGGCCCGCCGCATCCTGGCCGAGGACTGGGGCGTGCGTGCCGCCACGTGGTCGGTCACCAGCTGGAACGAGCTGCGGCGCCAGGCCCTGGAGGTGGAGAAGGCCAACTTCCTGGCTCCCGACGGCGAGCGGCAGGTCCCCTACCTGACGCAGAAGCTCTCCGAGAGCACGGGCCCCTTCATCGCCACCAGCGACTACGATCACCTGGTTCCCGACCAGATCCGTGCCTGGGTGCCCGGCGACTACTACACCCTGGGTGCTGACGGCTTCGGATTCTCCGACACCCGTGCCGCCGCCAGGCGCCACTACCTCATTGACGCCCAGTCGGTGGTGGTGCGCGCCCTCCAGGCTCTGGTGGAGCAGGGGCGCCTCGACCGCTCCGTCCTGGCCCAAGCCGTTGCACGCTACGACTTGACCAACGTCAATGCAGGCACCTCCGGGTCCCAGGGAGGGGAGTCCTGA","VSPTSDSTPLIDGLLTKVTDNDPEETKEWHESLDALIADKGAKRARYILLSMLAQARQKNVTVPTETTTPYINTIDVANEPYFPGDESAERTYRRWLRWNAAVMVTRAQRPGVGVGGHISSYASTATLYEVGFNHFFRGKDHPGGGDHVFFQGHASPGNYARAFVEGRLSEADLDGFRQEESRPAGGRGLPSYPHPRRMEDFWEYPTVSMGLGPAEAIYQAWFDKYLQGAGIKDTSQQHTWAFLGDGEMDEPESRGMLQLAASQQLDNLTFVINCNLQRLDGPVRGNGKIIQELEAFFKGAGWNVIKVIWGRGWDQLLAADKDHALEHLMMETLDGDYQTFKANDGAYIREHFFGRDPRTAELVKDWTDDEIWALQRGGNDYRKMYAAYKAATEHKGQPTVILAHTVKGYLLGGHFAGRNATHQMKKLTLDDLKALRDRLHIPITDEQLEANPKMPPYYRPANDDPSLLYMLDRRRQLGGFIPERRDAGVELELPGDKTYDILKGGSGKQEVASTMAFVRLLKELIKDKGIGRRIVPIVPDESRTFGLESLFPTKKIFNTQGQNYTPVDADMMLSYRESTSGQLMHTGINEAGSVSLFQVAGTSYATHGEPMIPVYIFYSMFGFQRTGDQFWAAGDQLTRGFIIGATAGRTTLTGEGTQHMDGHSPMIAATNDAVVSYDPAYAYEIRHIVRDALERWYGPDSGRNRDVMYYLTVYNEPIHQPAEPDNVDVEGILRGIHRISTAPDGEGPEVQLLASGVGVPWIEEARRILAEDWGVRAATWSVTSWNELRRQALEVEKANFLAPDGERQVPYLTQKLSESTGPFIATSDYDHLVPDQIRAWVPGDYYTLGADGFGFSDTRAAARRHYLIDAQSVVVRALQALVEQGRLDRSVLAQAVARYDLTNVNAGTSGSQGGES$","Pyruvate dehydrogenase E1 component","Cytoplasm","pyruvate dehydrogenase alpha subunit","pyruvate dehydrogenase E1 component ","2-oxo-acid dehydrogenase E1 subunit, homodimeric type","","Nikkola M., Lindqvist Y., Schneider G. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. J. Mol. Biol. 1994. 238(3):387-404. PMID: 8176731Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y., Jordan F., Guest J.R., Furey W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry 2002. 41(16):5213-5221. PMID: 11955070Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 1999. 6(8):785-792. PMID: 10426958Chabriere E., Vernede X., Guigliarelli B., Charon M.H., Hatchikian E.C., Fontecilla-Camps J.C. Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase. Science 2001. 294(5551):2559-2563. PMID: 11752578","","","

InterPro
IPR004660
Family

2-oxo-acid dehydrogenase E1 component homodimeric type
PIRSF000156	$\"[14-912]T$	Pyruvate dehydrogenase, E1 component
TIGR00759	$\"[16-910]T$	aceE: 2-oxo-acid dehydrogenase E1 component

InterPro
IPR009014
Domain

Transketolase, C-terminal-like
G3DSA:3.40.50.920	$\"[735-912]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.970	$\"[83-445]T$	no description
PTHR11624	$\"[121-320]T$	DEHYDROGENASE RELATED
PTHR11624:SF2	$\"[121-320]T$	TRANSKETOLASE

","BeTs to 8 clades of COG2609COG name: Pyruvate dehydrogenase, decarboxylase componentFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2609 is ---------dr---efghsn-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 20-86 are 74% similar to a (PYRUVATE DEHYDROGENASE COMPONENT E1 OXIDOREDUCTASE DEHYDROGENASE PYROPHOSPHATE THIAMINE FLAVOPROTEIN GLYCOLYSIS) protein domain (PD008560) which is seen in Q6AET5_BBBBB.Residues 96-466 are 67% similar to a (TRANSKETOLASE TRANSFERASE THIAMINE PYROPHOSPHATE TK CALCIUM-BINDING N-TERMINAL TRANSKETOLASE SUBUNIT ISOZYME) protein domain (PD308336) which is seen in Q83E69_COXBU.Residues 107-310 are 43% similar to a (TRANSKETOLASE FAMILY) protein domain (PDA1D521) which is seen in Q9A8Z0_CAUCR.Residues 115-339 are 42% similar to a (PYRUVATE COMPONENT E1 OXIDOREDUCTASE DEHYDROGENASE) protein domain (PDA1D520) which is seen in Q6MQR6_BDEBA.Residues 455-550 are 62% similar to a (PYRUVATE COMPONENT E1 OXIDOREDUCTASE DEHYDROGENASE) protein domain (PD933168) which is seen in Q83HL6_TROW8.Residues 511-723 are 85% similar to a (TRANSKETOLASE PYRUVATE TRANSFERASE DEHYDROGENASE COMPONENT THIAMINE E1 PYROPHOSPHATE CALCIUM-BINDING OXIDOREDUCTASE) protein domain (PD443507) which is seen in Q6A924_PROAC.Residues 579-695 are 49% similar to a (PYRUVATE COMPONENT E1 DEHYDROGENASE TRANSKETOLASE FAMILY PLASMID HOMOLOG OXIDOREDUCTASE BLR2815) protein domain (PD606577) which is seen in Q98PB0_RHILO.Residues 731-843 are 75% similar to a (PYRUVATE DEHYDROGENASE COMPONENT E1 OXIDOREDUCTASE DEHYDROGENASE THIAMINE GLYCOLYSIS PYROPHOSPHATE FLAVOPROTEIN) protein domain (PD008826) which is seen in Q82BA5_STRAW.Residues 845-902 are 82% similar to a (PYRUVATE DEHYDROGENASE COMPONENT E1 OXIDOREDUCTASE DEHYDROGENASE THIAMINE GLYCOLYSIS PYROPHOSPHATE FLAVOPROTEIN) protein domain (PDA1D8H5) which is seen in Q6NG46_CORDI.","","-69% similar to PDB:1L8A E. COLI PYRUVATE DEHYDROGENASE (E_value = );-69% similar to PDB:1RP7 E. COLI PYRUVATE DEHYDROGENASE INHIBITOR COMPLEX (E_value = );-69% similar to PDB:2G25 E. Coli Pyruvate Dehydrogenase Phosphonolactylthiamin Diphosphate Complex (E_value = );-69% similar to PDB:2G28 E. Coli Pyruvate Dehydrogenase H407A variant Phosphonolactylthiamin Diphosphate Complex (E_value = );-69% similar to PDB:2G67 E. Coli Pyruvate Dehydrogenase E1 Component (Apoenzyme) (E_value = );","No significant hits to the Pfam 21.0 database.","","dehydrogenase alpha subunit (aceE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0951","1030464","1030922","459","4.40","-13.62","16410","ATGGATCCGCTGGAGTACGGCAACTGCACGTCCTCCGACATCCAGGACTACGACGACGAGCTGACCGACAACGACGCGGAAGACACCCGATCCCAGGCGGAGGCCCAGGTCACCAAGGTCATGCCGGCCTCCGACCAGGTCAGTGTCACCGCGAACGAGCTCTCCACCGATCAGGTGGTCAAGGTCTCGGCGGGCGCACGAGACGTAACAATCACCGCACAAAGTCTCGTGGTCATCATCGAAGGGGAGATCGATTCACTGACCGTCAACGGCTTTGACAACACGGTCTGGATCGGCGCTTCCAATAAAGTCACGTTCGGCTCCAACGACGGGGACAGCCAGAATTACGTCTTCTGGCACTCCAGGCCTCCACAGGCGAAGGTGGATCCACAAGGGCTCAACATCATCGGCAAGGACGTTCACGCTCCTGTCGTCCGCTCCTGCCGATCCTTCTCGTGA","MDPLEYGNCTSSDIQDYDDELTDNDAEDTRSQAEAQVTKVMPASDQVSVTANELSTDQVVKVSAGARDVTITAQSLVVIIEGEIDSLTVNGFDNTVWIGASNKVTFGSNDGDSQNYVFWHSRPPQAKVDPQGLNIIGKDVHAPVVRSCRSFS$","Hypothetical protein","Periplasm, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0952","1032498","1031020","1479","4.98","-19.25","53163","ATGACGAAGGCAACCCGCACAGAGGAAGATCTTCTTGGTGCACGGGAAGTTCCATTGGAAGCCTATTGGGGAATCCATACGCTGCGTGCGATGGAGAACTTCCAGATCTCTGGAGCGGTGGTCGGTGATGAAGAGGCCTTTGTTCGCGGCATGGTGCAGGTGAAGAAGGCGTCAGCGTTAGCGAACGGTGACCTCGGGGCTCTTGACCCGGAGGTTGCTGGTGCGATTGTGTGGGCGTGTGACCAGGTGCTGGTTGCTGAGCGCTGCCTCGATCAGTTCCCAGTCGACCAGTTCCAGGGGGGTGCTGGGACCAGCGTCAACATGAATACCAACGAGGTGATCGCCAATCTCGCGCTGGAGTACCTGGGATACGCCAAGGGTCGTTATGACATCATCAACCCCAATGATCATGTCAACAAGTCCCAGTCGACGAACGACGCCTATCCGACCGGATTCCGTCTGGGGCTGTTCACCCTAGTCGCCTCGCTCGTCGAGGAGCTCGAGCGACTCATCGTGTCGATGCGATCCAAGGGGAAGGAACTCGTCAATGTTCTGAAGATGGGACGTACCCAGCTTCAGGATGCGGTTCCGATGAGCCTAGGACAGGAGTTCGAGGCCTTCGCCGTTCTGCTGGAGGAGGAGGTGAGCCGGCTTCACAACAACGCCGCCCTACTTCTGGAGGTGAACCTCGGGGCCACGGCGATCGGCACAGGGCTCAACACGCCGCCGGACTATCAGAGCACTGTTGTCGGACGTCTGCGGGAGGTCACGGGGCTGGACATTCGAGGAGCGCATGACCTGCTGGAAGCCACGAGTGACACGGGCGCCTACGTCTCGATGCACGCGGCGATCAAACGCCTGGCGGTGAAGCTGTCCAAGATCTGTAACGACCTGCGACTACTGTCCTCCGGACCTCGTGCGGGGCTGGGGGAGATCCGGCTGCCTGAACGCCAGGCCGGTTCCTCCATCATGCCGGCCAAGGTCAATCCGGTCATCCCGGAGGTGGTGAACCAGGTCTGCTTCAAGGTCATCGGAAACGACGTGGCGCTGACCTTCGCCGCCGAGGCAGGGCAGCTTCAGCTCAATGTCATGGAACCGGTGATCGCCCAGACCATCTTCGAGTCCATCAATCTGCTCGCTCGCGGGATGTCAACCCTTCGGGAACTTTGCATCGTGGGGATCGAGGCCAATGAGGAGGTATGTCGTCGCAATGTGCTGGACTCGATCGGAATCGTCACCTATCTCAATCCGGTGATCGGTCATCACAATGGCGACCTGGTGGGCCGTGAGTGCGCCCGTTCTGGACGCAGTGTGCGAGAGGTCGTGCTGGAGATGGGGCTGCTCGAGGAGGCTGTTCTTGACGAGATTCTCAGCCCGGAGAACCTTCTGCGTCCCCATTTCCGCGATTTGAAGGTCTACTCGGGATCCGACCCGTCGACTCCGCCGGTTGTGTCCACCGCTCCTGACTTGGGGGAGTAA","MTKATRTEEDLLGAREVPLEAYWGIHTLRAMENFQISGAVVGDEEAFVRGMVQVKKASALANGDLGALDPEVAGAIVWACDQVLVAERCLDQFPVDQFQGGAGTSVNMNTNEVIANLALEYLGYAKGRYDIINPNDHVNKSQSTNDAYPTGFRLGLFTLVASLVEELERLIVSMRSKGKELVNVLKMGRTQLQDAVPMSLGQEFEAFAVLLEEEVSRLHNNAALLLEVNLGATAIGTGLNTPPDYQSTVVGRLREVTGLDIRGAHDLLEATSDTGAYVSMHAAIKRLAVKLSKICNDLRLLSSGPRAGLGEIRLPERQAGSSIMPAKVNPVIPEVVNQVCFKVIGNDVALTFAAEAGQLQLNVMEPVIAQTIFESINLLARGMSTLRELCIVGIEANEEVCRRNVLDSIGIVTYLNPVIGHHNGDLVGRECARSGRSVREVVLEMGLLEEAVLDEILSPENLLRPHFRDLKVYSGSDPSTPPVVSTAPDLGE$","Aspartate ammonia-lyase","Cytoplasm","aspartate ammonia-lyase","aspartate ammonia-lyase ","aspartate ammonia-lyase","","Woods S.A., Schwartzbach S.D., Guest J.R. Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 1988. 954(1):14-26. PMID: 3282546","","","

InterPro
IPR000362
Domain

Fumarate lyase
PR00149	$\"[138-156]T$ $\"[183-199]T$ $\"[274-301]T$ $\"[320-336]T$	FUMRATELYASE
PF00206	$\"[13-345]T$	Lyase_1
PS00163	$\"[320-329]T$	FUMARATE_LYASES

InterPro
IPR003031
Domain

Delta crystallin
PR00145	$\"[137-159]T$ $\"[178-198]T$ $\"[320-336]T$	DCRYSTALLIN

InterPro
IPR004708
Family

Aspartate ammonia-lyase
TIGR00839	$\"[6-472]T$	aspA: aspartate ammonia-lyase

noIPR
unintegrated

unintegrated
G3DSA:1.10.275.10	$\"[3-142]T$	no description
G3DSA:1.10.40.30	$\"[411-459]T$	no description
G3DSA:1.20.200.10	$\"[143-410]T$	no description
PTHR11444	$\"[1-474]T$	ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF1	$\"[1-474]T$	ASPARTATE AMMONIA LYASE

","BeTs to 10 clades of COG1027COG name: Aspartate ammonia-lyaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1027 is ---p----v---b-efgh-nu-----Number of proteins in this genome belonging to this COG is 1","***** IPB003031 (Delta crystallin signature) with a combined E-value of 5.5e-39. IPB003031A 137-159 IPB003031B 178-198 IPB003031C 229-245 IPB003031D 274-298 IPB003031E 320-336***** IPB000362 (Fumarate lyase) with a combined E-value of 7.8e-12. IPB000362 320-345***** IPB009049 (Argininosuccinate lyase) with a combined E-value of 3.4e-09. IPB009049C 184-221 IPB009049E 303-357","Residues 10-448 are similar to a (LYASE ADENYLOSUCCINATE ARGININOSUCCINATE BIOSYNTHESIS ARGININE ASAL ARGINOSUCCINASE ASPARTATE AMMONIA-LYASE ASL) protein domain (PD000660) which is seen in ASPA_HAEIN.","","-75% similar to PDB:1JSW NATIVE L-ASPARTATE AMMONIA LYASE (E_value = 6.1E_167);-65% similar to PDB:1J3U Crystal structure of aspartase from Bacillus sp. YM55-1 (E_value = 8.3E_116);-57% similar to PDB:2FUS MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING SITE (E_value = 8.7E_89);-57% similar to PDB:1KQ7 E315Q Mutant Form of Fumarase C from E.coli (E_value = 1.5E_88);-57% similar to PDB:1FUO FUMARASE C WITH BOUND CITRATE (E_value = 3.3E_88);","Residues 13 to 345 (E_value = 1.8e-141) place ANA_0952 in the Lyase_1 family which is described as Lyase.","","ammonia-lyase (aspA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0953","1032763","1033962","1200","5.22","-16.67","41871","ATGGATGAGTTGAGCGCTCCGGGAGTGTCTGCACTGCGACAGGCGCAGGACACAATTATTGAACACTCACTGGACCGCATCAGTTCGGCCCATGATTTCTACCGAACCCTGCCGGAGGGTTCGCGTGACCAGATCGCTGCGGTGGCCCGTCTGGGCGTCACCATGTTCGTCGACTCGGCGGAGGACCCCTCGACCCCGCTGGTCCCCTCCCAGATCTTCTCCGTGGCCCCTGCTGCTCTAACCGGTGTCATCACCCTTGAGCAGACCCTGGCTCTGGTACGCACGGTCCTCGACGTCGTTGTGGACGAGGCTCCCCGCGTCGTGCCGGATGAGGACCATGACGCCGTCCGCATCCTCGTCCTGACCTTCGGGCGTGACGTTGGCTTCGCCGCGGCCGAGGTGTATGCCCGGGCGGCTGAGGCCCGCGGCGCCTGGGATGCTCGGTTGGAGTCAGTAGCGGTCGACGCGATGCTTCACGACGCCCCCGAGGACGCCGCGACCCGGGCGGGAACTGCCGGCTGGAACGGCACCGGTCCTGTGGTGGCGATCGCCGCCAAGACCTCTCTTGATGCGCTCGGTGTCTCCAGGTTGCGTCACGAGTGCCGCAACCTCGCCAGCGACTGTCTGGTATCCGTGCGCGGAGACTCCGTCCTCATTGTCCTGGGCGACAGCCCGACCACCCACGTTCCGGCGTCCAAGCACTCCGGCCGAGAGGCCACCGCTGAGCAGCTGGTGGACCAGGCGGCCATGCAGGTGGCAGGCAGCCTGGGAGGGTCGGCCGTCGTCGGCCCGGTGGTGCCCGGCATCTCGCACGCGGGCCGATCGTTGCGCTCAGCCCTGGCCGGCCTACGGGCCCTGCCCGGCTGGGCTGAGGCACCCAACCCGGTTCATGCCGACGACCTCCTCCCCGAGCGGCTCCTGGCCGGCGACGAGCTTGCCGGCGAGCAGATCCTTCATCTGGTACACGCACCCCTCCACGAAATGGGCGACCCCTTCGAGAGTACGGTGGCCACCTACCTGGCACTGGGTGGGAGCCTGGAGGCCACCGCCCGGAACCTGTTCGTACACGCCAACACGGTGCGCTACCGCCTGGGTCGGGTCAGTGAACAGGTCGGCTGGGACGCAACGAACGCCCGTGACGGCCTCATGCTGCACATGGCGATTATCGTGGGCCGCCTGGCTGTCAGTCGGGAGGCCTGA","MDELSAPGVSALRQAQDTIIEHSLDRISSAHDFYRTLPEGSRDQIAAVARLGVTMFVDSAEDPSTPLVPSQIFSVAPAALTGVITLEQTLALVRTVLDVVVDEAPRVVPDEDHDAVRILVLTFGRDVGFAAAEVYARAAEARGAWDARLESVAVDAMLHDAPEDAATRAGTAGWNGTGPVVAIAAKTSLDALGVSRLRHECRNLASDCLVSVRGDSVLIVLGDSPTTHVPASKHSGREATAEQLVDQAAMQVAGSLGGSAVVGPVVPGISHAGRSLRSALAGLRALPGWAEAPNPVHADDLLPERLLAGDELAGEQILHLVHAPLHEMGDPFESTVATYLALGGSLEATARNLFVHANTVRYRLGRVSEQVGWDATNARDGLMLHMAIIVGRLAVSREA$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 4 clades of COG2508COG name: Regulator of polyketide synthase expressionFunctional Class: T,QThe phylogenetic pattern of COG2508 is -----qvcebrhuj--olinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 137-214 are 60% similar to a (ML1652 RV2242/MT2302/MB2266 MLCB1243.23C SCO2386) protein domain (PD041837) which is seen in Q6A925_PROAC.Residues 263-427 are 54% similar to a (ML1652 RV2242/MT2302/MB2266 MLCB1243.23C SCO2386) protein domain (PD858941) which is seen in Q6AET4_BBBBB.Residues 449-502 are 72% similar to a (REGULATOR TRANSCRIPTIONAL REGULATORY DNA-BINDING DIACID LEUCINE-RICH PLASMID SUGAR CARBOHYDRATE POSSIBLE) protein domain (PD007784) which is seen in Q8G462_BIFLO.","","-52% similar to PDB:1BBO HIGH-RESOLUTION SOLUTION STRUCTURE OF THE DOUBLE CYS2*HIS2 ZINC FINGER FROM THE HUMAN ENHANCER BINDING PROTEIN MBP-1 (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","Thu Aug 2 11:20:31 2007","","Thu Aug 2 11:20:31 2007","","","Thu Aug 2 11:20:31 2007","Thu Aug 2 11:20:31 2007","Thu Aug 2 11:20:31 2007","","","","","","Thu Aug 2 11:20:31 2007","Thu Aug 2 11:20:31 2007","Thu Aug 2 11:20:31 2007","","Thu Aug 2 11:20:31 2007","Thu Aug 2 11:20:31 2007","","","","","yes","","" "ANA_0954","1034224","1034475","252","4.11","-10.06","8788","ATGGCTGAGCAGAGCAACGACGACGTCCTGTCCGTCATCATCCAGATCGTCAGCGAGGAGTCCGGCGTCGCCGCCAAGGACATTACTAGGGACACCACTTTCGCCCAGGACCTCGATGTCGACTCCCTGGGTCTGCTAACCATCGCCACCCAGGTTGAGGAGCGCTTCGGTGTAACCCTGGACGACTCCCTCATCCCGACCCTGCCTACTGTTGGAGCGCTGGTCGACCTGGTGACCTCCAAGAAGGCCTGA","MAEQSNDDVLSVIIQIVSEESGVAAKDITRDTTFAQDLDVDSLGLLTIATQVEERFGVTLDDSLIPTLPTVGALVDLVTSKKA$","Acyl carrier protein","Cytoplasm","acyl carrier protein","phosphopantetheine-binding","phosphopantetheine-binding","","Roujeinikova A., Baldock C., Simon W.J., Gilroy J., Baker P.J., Stuitje A.R., Rice D.W., Slabas A.R., Rafferty J.B. X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site. Structure 2002. 10(6):825-835. PMID: 12057197Volkman B.F., Zhang Q., Debabov D.V., Rivera E., Kresheck G.C., Neuhaus F.C. Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein. Biochemistry 2001. 40(27):7964-7972. PMID: 11434765Weber T., Baumgartner R., Renner C., Marahiel M.A., Holak T.A. Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases. Structure 2000. 8(4):407-418. PMID: 10801488","","","

InterPro
IPR003231
Family

Acyl carrier protein (ACP)
PD000887	$\"[37-78]T$	Q83NH7_TROW8_Q83NH7;

InterPro
IPR006163
Domain

Phosphopantetheine-binding
PF00550	$\"[11-78]T$	PP-binding
PS50075	$\"[9-79]T$	ACP_DOMAIN

InterPro
IPR009081
Family

Acyl carrier protein-like
G3DSA:1.10.1200.10	$\"[2-78]T$	no description

noIPR
unintegrated

unintegrated
PTHR20863	$\"[7-82]T$	ACYL CARRIER PROTEIN/ZINC FINGER PROTEIN 593-RELATED

","BeTs to 19 clades of COG0236COG name: Acyl carrier proteinFunctional Class: I [Metabolism--Lipid metabolism] Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0236 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 78 (E_value = 4.9e-16) place ANA_0954 in the PP-binding family which is described as Phosphopantetheine attachment site.","","carrier protein (ACP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0955","1034484","1035737","1254","5.53","-10.46","42520","ATGAGCCCGGAAGCCGAGTGCCGCCCCGACGACGTCGTCGTCACCGGACTGGGGACCGTCAATCCTCTGGGCGCGGACATTGAGTCCACCTGGAGCGCCCTGCACGAGGGTACCTGCGCGGTTCGCACCCTCGAGCACGAGTGGGTCGAGAGCCATGACCTGCCTGTGCGGATCGGAGCCCCCCTGGCGGTCGATCCTGCCGAGATGCTTCCGCCCCGCCAGCTGCGCCGCCTCGACCGCGCCAGTCAGTGCGCACTGCTGGCCGCCCGCCAGGCCTGGGAGCAAGCGGGGGCCCCGCAGGTCGCCCCCCAGCGCCTAGCGGTGTCCGTCTCCCCGGGCATGGGGCCGGTCCTGTCGGTCATGGAGGCCTGGGACACGCTGAGGGACAAGGGGCCCCGGCGGGTTCTGCCGACGGCGGTCCCAGCGCTCATGCCCAACGCCCCGGCGGCCGCTGTCGGTATCGAGATGGGAGCCCACGGCGGCATCCATGCTCCGGTCTCGGCCTGCGCCTCCGGGGCCGAGGCAATCGCCTATGGTGCGGACCTCATCACGCTGGGACGGGCCGACGTCGTCGTGGCCGGGGGGACGGATGCGGCCCTCCACCCGATGACCGTGGCCGCCTTCGGCGCCATGCGGGCCCTGTCCACGCGCAACGCCGACCCGCAGACCGCCTCCCGCCCCTTCGCCCCGGACCGCGACGGCTTCGTCCTGGGTGAGGGCGCCGGGATCCTTGTTCTGGAGCGCGCTGGGCACGCCATCGCCCGTGGCGCACGGGTCCTGGCCGTGTTGGCGGGCTCAGGGGTGACTGCCGATGCCTACGACGTCGCACGCCCGGAGCCATCTGGCGCGGAGCAAGAGCGAGCTCTGCAGCTGGCTCTGGAACGCGCGGACCTTGGCGCCGACGCTGTTGGGCACGTCAACGCCCATGCCACCTCGACACCTGCCGGCGACGTCGTCGAGGCCGGTGTCCTGGCCAGAACGGTGCCGAACGCGGCGGTCAGCGCCACGAAGTCCGCCACCGGTCACCTCCTGGGAGGGGCCGGGGGGCTGGAGGCGGTGCTGACCGTCATGGCGCTGCGGGAGCGCTGGGCCCCGCCCACGCTGCTGCCGGCCGGAGTGGATCCGGAGCTGGCCCAGCTCGGGCTGGACGTCGTCGGGCCGCAGGGCCGGGACCTGCCCCGGCTGACGGCCGCAGCCAGCACCTCCTTCGGCTTCGGAGGGCACAACGTCGCCCTAATTTTCGCCCGCCAGTAG","MSPEAECRPDDVVVTGLGTVNPLGADIESTWSALHEGTCAVRTLEHEWVESHDLPVRIGAPLAVDPAEMLPPRQLRRLDRASQCALLAARQAWEQAGAPQVAPQRLAVSVSPGMGPVLSVMEAWDTLRDKGPRRVLPTAVPALMPNAPAAAVGIEMGAHGGIHAPVSACASGAEAIAYGADLITLGRADVVVAGGTDAALHPMTVAAFGAMRALSTRNADPQTASRPFAPDRDGFVLGEGAGILVLERAGHAIARGARVLAVLAGSGVTADAYDVARPEPSGAEQERALQLALERADLGADAVGHVNAHATSTPAGDVVEAGVLARTVPNAAVSATKSATGHLLGGAGGLEAVLTVMALRERWAPPTLLPAGVDPELAQLGLDVVGPQGRDLPRLTAAASTSFGFGGHNVALIFARQ$","3-oxoacyl-[acyl-carrier-protein] synthase","Cytoplasm","3-oxoacyl-[acyl-carrier-protein] synthase II","3-oxoacyl-","beta-ketoacyl synthase","","Kauppinen S., Siggaard-Andersen M., von Wettstein-Knowles P. beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue. Carlsberg Res. Commun. 1988. 53(6):357-370. PMID: 3076376Beck J., Ripka S., Siegner A., Schiltz E., Schweizer E. The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases. Eur. J. Biochem. 1990. 192(2):487-498. PMID: 2209605","","","

InterPro
IPR000794
Domain

Beta-ketoacyl synthase
PTHR11712	$\"[3-416]T$	POLYKETIDE SYNTHASE-RELATED

InterPro
IPR014030
Domain

Beta-ketoacyl synthase, N-terminal
PF00109	$\"[10-252]T$	ketoacyl-synt
PS00606	$\"[160-176]?$	B_KETOACYL_SYNTHASE

InterPro
IPR014031
Domain

Beta-ketoacyl synthase, C-terminal
PF02801	$\"[260-368]T$	Ketoacyl-synt_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.47.10	$\"[14-265]T$ $\"[268-416]T$	no description
PTHR11712:SF23	$\"[3-416]T$	3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE

","BeTs to 17 clades of COG0304COG name: 3-oxoacyl-(acyl-carrier-protein) synthaseFunctional Class: I [Metabolism--Lipid metabolism] Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0304 is ------yqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB000794 (Beta-ketoacyl synthase) with a combined E-value of 1.1e-17. IPB000794B 160-195 IPB000794C 302-313","Residues 8-97 are 58% similar to a (SYNTHASE TRANSFERASE I ACYLTRANSFERASE 3-OXOACYL-ACYL-CARRIER-PROTEIN) protein domain (PD973775) which is seen in Q7U957_SYNPX.Residues 12-71 are 63% similar to a (TRANSFERASE SYNTHASE 3-OXOACYL-ACYL-CARRIER-PROTEIN II ACYLTRANSFERASE I BETA-KETOACYL-ACP POLYKETIDE CARRIER BIOSYNTHESIS) protein domain (PD001987) which is seen in Q9RDP7_STRCO.Residues 70-264 are 46% similar to a (SYNTHASE TRANSFERASE ACID FATTY ACYLTRANSFERASE 3-OXOACYL-ACYL-CARRIER-PROTEIN ALPHA REDUCTASE SUBUNIT BETA-KETOACYL) protein domain (PD011953) which is seen in Q59497_CORAM.Residues 104-154 are 78% similar to a (TRANSFERASE SYNTHASE 3-OXOACYL-ACYL-CARRIER-PROTEIN II ACYLTRANSFERASE I BETA-KETOACYL-ACP CARRIER BIOSYNTHESIS ACID) protein domain (PD483857) which is seen in Q6AET0_BBBBB.Residues 156-411 are 43% similar to a (SYNTHASE TRANSFERASE BETA-KETOACYL PROBABLE) protein domain (PD271345) which is seen in Q9HU15_PSEAE.Residues 200-282 are similar to a (TRANSFERASE SYNTHASE 3-OXOACYL-ACYL-CARRIER-PROTEIN II ACYLTRANSFERASE I BETA-KETOACYL-ACP CARRIER POLYKETIDE BETA-KETOACYL) protein domain (PD063697) which is seen in Q9RDP7_STRCO.Residues 289-353 are 71% similar to a (TRANSFERASE SYNTHASE POLYKETIDE PHOSPHOPANTETHEINE I 3-OXOACYL-ACYL-CARRIER-PROTEIN ACYLTRANSFERASE II TYPE ACID) protein domain (PD580608) which is seen in Q89MV7_BRAJA.Residues 356-415 are 63% similar to a (TRANSFERASE SYNTHASE POLYKETIDE PHOSPHOPANTETHEINE I 3-OXOACYL-ACYL-CARRIER-PROTEIN II ACYLTRANSFERASE TYPE MODULAR) protein domain (PD000208) which is seen in Q9RK62_STRCO.","","-55% similar to PDB:2GP6 X-ray crystal structure of Mycobacterium tuberculosis beta-ketoacyl acyl carrier protein synthase II (mtKasB) (E_value = 4.8E_77);-53% similar to PDB:1J3N Crystal Structure of 3-oxoacyl-(acyl-carrier protein) Synthase II from Thermus thermophilus HB8 (E_value = 7.4E_70);-52% similar to PDB:1E5M BETA KETOACYL ACYL CARRIER PROTEIN SYNTHASE II (KASII) FROM SYNECHOCYSTIS SP. (E_value = 2.1E_64);-54% similar to PDB:2GQD The crystal structure of B-ketoacyl-ACP synthase II (FabF) from Staphylococcus aureus (E_value = 1.0E_63);-53% similar to PDB:1B3N BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN. (E_value = 1.1E_60);","Residues 10 to 252 (E_value = 1.7e-55) place ANA_0955 in the ketoacyl-synt family which is described as Beta-ketoacyl synthase, N-terminal domain.Residues 260 to 371 (E_value = 4.9e-36) place ANA_0955 in the Ketoacyl-synt_C family which is described as Beta-ketoacyl synthase, C-terminal domain.","","synthase II (Kas4)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0956","1035913","1036413","501","6.19","-3.39","18179","ATGATCGGTGCCTACACCCGCGGTGTACTTTTCGTGCATTCAGCACCTCGGGCGCTCTGCCCCCACATCGAGTGGGCAGCGGCCGAGGTGCTCGGCTCGCGTGTCCACCTGGACTGGACCGAGCAGCCTGCGGCTCGGGGCATGATGCGGGCCGAGACCAGCTGGGTGGGGCCTGCTGGAACAGGAGCCAGCCTTGCCTCGGCCCTGCGCGGCTGGGCGAACCTGCGCTACGAGGTGACCGAGGAGGCGAGTGTCGGCACCGACGGCGGCCGTTGGTCCCACACCCCCGATCTGGGCATTTTCCACGCCCAGACGGATGTTCACGGCAACGTCGTCGTCCCCGAGGACCGGATCCGTGCCGCGCTCGTCTACGCGACTGATCCTGAAAGGATGCGCCGCGAGCTCGATCTGGCTCTGGGGCAGGCCTGGGACGACGAGCTCGAGCCCTTCCGCTACGCCGGAGCCGGTGCGCCCGTGCGCTGGCTGCACCGCGTCGGCTAG","MIGAYTRGVLFVHSAPRALCPHIEWAAAEVLGSRVHLDWTEQPAARGMMRAETSWVGPAGTGASLASALRGWANLRYEVTEEASVGTDGGRWSHTPDLGIFHAQTDVHGNVVVPEDRIRAALVYATDPERMRRELDLALGQAWDDELEPFRYAGAGAPVRWLHRVG$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 8-151 are 76% similar to a (FABB SCO2391 FABC FABD FABH CDS ORF5 ML1781 MB2280C GENES) protein domain (PD034754) which is seen in Q6AFT1_BBBBB.","","-40% similar to PDB:1DXH CATABOLIC ORNITHINE CARBAMOYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA (E_value = );-40% similar to PDB:1ORT ORNITHINE TRANSCARBAMOYLASE FROM PSEUDOMONAS AERUGINOSA (E_value = );-52% similar to PDB:2HG4 Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS. (E_value = );-64% similar to PDB:1EF2 CRYSTAL STRUCTURE OF MANGANESE-SUBSTITUTED KLEBSIELLA AEROGENES UREASE (E_value = );-64% similar to PDB:1EJU CRYSTAL STRUCTURE OF THE H320N VARIANT OF KLEBSIELLA AEROGENES UREASE (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0957","1037002","1036511","492","4.63","-15.42","18389","ATGGCATACCGCGACATCCGCATCATTGGCGACCCGATCCTGCGCACCGAGTGCGACTGGATCACTGACATCGATGACTCCGTCAAGGCTCTGGTTGAGGACCTGCTCGAGACGGTCGATGAGGACGGCCGGGCCGGCCTGGCCGCCAATCAGATCGGGATCGGTCTGCGTGCCTTCTCCTGGAACATCGACGGCGAGATCGGCTACATCCTCAACCCCAAGATCGTCGAGGTCTCCAAGGACGAGTACCAGGACGGGGACGAGGGCTGCCTGTCAGTGCCGGGCCTGTGGTTCCCCACGGAGCGAGCGTGGTACGCCCGGGCTGAGGGAGTGGACCTGGACGGCAAGGAAGTCGTCGTCGAGGGGGAGGAGCTCATGGCTCGTTGCATCCAGCACGAGTGCGACCACCTGGAGGGCCACCTCTACCTCGACCGCCTCGACCGGAAGAACCGGGCCAAGGCGATGAAGGAGCTGCGGGCGCAGGGACTGTAA","MAYRDIRIIGDPILRTECDWITDIDDSVKALVEDLLETVDEDGRAGLAANQIGIGLRAFSWNIDGEIGYILNPKIVEVSKDEYQDGDEGCLSVPGLWFPTERAWYARAEGVDLDGKEVVVEGEELMARCIQHECDHLEGHLYLDRLDRKNRAKAMKELRAQGL$","Polypeptide deformylase","Cytoplasm","polypeptide deformylase","polypeptide deformylase ","peptide deformylase","","Becker A., Schlichting I., Kabsch W., Groche D., Schultz S., Wagner A.F. Iron center, substrate recognition and mechanism of peptide deformylase. Nat. Struct. Biol. 1998. 5(12):1053-1058. PMID: 9846875Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A.F. Structure of peptide deformylase and identification of the substrate binding site. J. Biol. Chem. 1998. 273(19):11413-11416. PMID: 9565550Meinnel T., Blanquet S., Dardel F. A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase. J. Mol. Biol. 1996. 262(3):375-386. PMID: 8845003Dardel F., Ragusa S., Lazennec C., Blanquet S., Meinnel T. Solution structure of nickel-peptide deformylase. J. Mol. Biol. 1998. 280(3):501-513. PMID: 9665852","","","

InterPro
IPR000181
Family

Formylmethionine deformylase
PD003844	$\"[31-139]T$	DEF2_BIFLO_Q8G487;
PR01576	$\"[33-62]T$ $\"[88-99]T$ $\"[100-118]T$ $\"[119-148]T$	PDEFORMYLASE
G3DSA:3.90.45.10	$\"[4-161]T$	no description
PIRSF004749	$\"[3-162]T$	Peptide deformylase
PTHR10458	$\"[7-159]T$	POLYPEPTIDE DEFORMYLASE
PF01327	$\"[3-152]T$	Pep_deformylase
TIGR00079	$\"[3-160]T$	pept_deformyl: peptide deformylase

","BeTs to 18 clades of COG0242COG name: N-formylmethionyl-tRNA deformylaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0242 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000181 (Peptide deformylase signature) with a combined E-value of 7.9e-36. IPB000181A 33-62 IPB000181B 88-99 IPB000181C 100-118 IPB000181D 119-148","Residues 31-139 are 83% similar to a (DEFORMYLASE POLYPEPTIDE PEPTIDE HYDROLASE PDF IRON BIOSYNTHESIS DEFORMYLASE-LIKE DEFORMYLASE 3D-STRUCTURE) protein domain (PD003844) which is seen in DEF2_BIFLO.","","-54% similar to PDB:1IX1 Crystal Structure of P.aeruginosa Peptide deformylase Complexed with Antibiotic Actinonin (E_value = 7.1E_22);-54% similar to PDB:1N5N Crystal Structure of Peptide Deformylase from Pseudomonas aeruginosa (E_value = 7.1E_22);-54% similar to PDB:1S17 Identification of Novel Potent Bicyclic Peptide Deformylase Inhibitors (E_value = 7.1E_22);-54% similar to PDB:1LRY Crystal Structure of P. aeruginosa Peptide Deformylase Complexed with Antibiotic Actinonin (E_value = 2.1E_21);-55% similar to PDB:1LME Crystal Structure of Peptide Deformylase from Thermotoga maritima (E_value = 2.3E_20);","Residues 3 to 152 (E_value = 2.1e-48) place ANA_0957 in the Pep_deformylase family which is described as Polypeptide deformylase.","","deformylase (def)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0960","1037897","1037331","567","6.36","-1.31","20480","ATGCCGATCCTGCGCCGTCGTCAAGGCTCATCCACCCGCTCCACCGCCACGCTTCCGCTGGAACTGCGCGAGCAGCTGCATGAGCCCGTCCTGGGGGCTGTTCCCCTGGATGCGGAGGGCTCGGCATGGGCGGTGGCCACGGCAAGCACCCTCGTGGTCTTTACCGGGAGCAGGCGGCCCGAGATCCACCCCTGGGACGAGGTGGAGCAGGGGAGCTGGGACGGGCAGGAGCGCGTCTTTACCCTGAGGTGGACGCAGCAGGATCGCGGGGACCTCGTGTTGAAGGTCCCGGCAGGAGTGCGCCGCGGCGATGCCTACGCCGCAGCGGACGTGGCCCCCTTCGCCAAGGCTCTGCGTCAACGGGTGGAGGCGGCCATCATCCACAGCGCCGTGGCAGCGCTCCCCAACGGCGCAACGGCCACGGCGAGCGTGCGTCGAGGCAGCGACGGCGAGCTCTACTCCGTCACCCGGCCACTGATCTCACAGGTCGATGAGGCGGAGGATCGCCGCGCGCTTCAGGAGCTGGAAAACCGAGTCCGTGAGGGTGTGGGCCTGCCCACACAGTAG","MPILRRRQGSSTRSTATLPLELREQLHEPVLGAVPLDAEGSAWAVATASTLVVFTGSRRPEIHPWDEVEQGSWDGQERVFTLRWTQQDRGDLVLKVPAGVRRGDAYAAADVAPFAKALRQRVEAAIIHSAVAALPNGATATASVRRGSDGELYSVTRPLISQVDEAEDRRALQELENRVREGVGLPTQ$","Hypothetical protein","Cytoplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0962","1039963","1037948","2016","7.05","0.49","72818","GTGGCGGGACTGATCAGGCGTGAGGACATCGAGGCGGTGCGCGAGCGCGCCAGGCTTGAGGACGTCGTCGGTGAGCACGTGACTCTCAAGAGCGCCGGCGTCGGCTCGCTCAAGGGACTGTGTCCCTTCCATGACGAACGCACCCCCTCCTTCCACGTCCGCCCCCAGCTCGGCTACTGGCATTGCTTCGGCTGCGGTGAGGGCGGAGACGTCATCACCTTCATCGAGAAGATTCATCACCTTGGATTCGCCGAGGCGGTCGAGTACCTCGCCGACCGCACTGGGGTCCAGCTGCGCTACGAGGAAGGCGGTGCTGTACGGCGCGGGGTGGAGCCAGGCACTCGGCAGCGCCTCATGGACGCCAACCGCCTGGCCGAGGCCTGGTTCCGCGAGCAGCTCGCCACCCCGGAGGCACAGCCGGGGCGGGACTTCCTCACCGCTCGGGGCTTCGACCGCCACGCTGCTGCGCACTTCGGCGTCGGCTACGCGCCCGCCGGATGGGACAACCTCGCCCGCTACCTGCGCAGCTCCGGCTACACCGAGGCCGAGCTGGTCGACTCCGGTCTGTGCAGCCGAGGCGGGCAGGACGGGCGCCGCGTCTACGACCGCTTCCGCGGCCGCCTCATCTGGCCCATCCGGGACGTCACCGGGGCCACCGTCGGCTTCGGGGCACGCAAGCTCTCAGAGGAGGACCAGGGCCCCAAGTACCTCAACACCCCCGAGACCCCCGTCTTCCACAAGAGCCAGGTCCTCTACGGGCTGGACCTGGCCAAGCGGGAGGTCGCCCGCTCCCACCGGATCGTTGTCGTCGAGGGCTACACCGACGTCATGGCCGCCCACCTGTCCGGGGTGACCACGGCCGTGGCCACGTGCGGGACCGCCTTCGGCGCAGACCACGTGCGGGTGGTGCGCCGCCTGCTGGGGGATGTGGACGACCCCGCGGCGGGAGTGGTCACCGGTCAGGGGCGCGAGGCCCGAGGAGGCGAGGTCATCTTCACCTTCGACGGCGACGCAGCCGGCCAGAAGGCCGCGCTGCGGGCCTACGCCGAGGACCAGCGCTTCGCCACCCAGACCTTCGTGGCTGTCGACCCCGGCGGACTGGACCCCTGCGACCTGCGGATGAAGGAGGGGGATCCGGGCATTCCGCGCCTGCTGTCCCGAAGGGTGCCGTTGTTCGAGTTCGTCATCCGCACCTCCCTGTCCCACCTGGACCTGGACACCTCCGAAGGGCGAGTCCGAGGGCTGCGCTCGGCGGCACCGGTGGTGGCCGGCATCCGGGACCGGGCGCTCAAGCGCGAGTACACCCGGCGACTGGCCGGATGGCTGGGCCTGCCTGACGCGGAGGTGCACGCCGCAGTCCAGGCCGCCGGCAGGCGAGGGGCGCAGCCCAGCGCGGGGCGGGGCGGCCAGTGGCCCGCTGATGAGACCGCAGGCCCCGACGCCGCCGCCCCCGTGCGGGGGCTGCCGCCGGTGACCGACCCCGTTGAGCAGCTCGAGCGCGAGGCGCTCGCCGTCATCATCCAGTTCCCGATGGCGGCCCACCAAGCCGGCGCCGACGAGCTCGGAGCCGACTCCTTCGGCCAGCTCACCCACCGCGCCGTCTATGAGGCCGTCGCGGCCGCCGGCGGCACTGCGGAGGTGCCGGGGCTGGTCCAGCAGGCGGTGGCCGCCGGCATGGGGGAGCAGGAGGCGCAGCGCCGGGCCACACTGCGATGGCTCCAACAGGTACGCGACGGTGCCATCGGCCTGGTTGAAGCCGCCATCACCGAGCTCGCCGTGGCGCCCCTACCACTGCCCACCGTCCGGGGACGCGGCACCGAGGTGGACGCCTCCGGGCTGGAGCGTTACGCCAAGGGCGTGCTCGACTCCCTCGCCGTCATGGGCATCAACCGCAGGCTCGTTGAGATGCGCTCACGCCACCGGCGGATGTCGCCACATGAGGAGGGCTACCGCGAGCTGTTCTCCGAGATTGCCGCTCTCGAGCAACGCCGTATGCACATACGGCAGGGGACCTGA","VAGLIRREDIEAVRERARLEDVVGEHVTLKSAGVGSLKGLCPFHDERTPSFHVRPQLGYWHCFGCGEGGDVITFIEKIHHLGFAEAVEYLADRTGVQLRYEEGGAVRRGVEPGTRQRLMDANRLAEAWFREQLATPEAQPGRDFLTARGFDRHAAAHFGVGYAPAGWDNLARYLRSSGYTEAELVDSGLCSRGGQDGRRVYDRFRGRLIWPIRDVTGATVGFGARKLSEEDQGPKYLNTPETPVFHKSQVLYGLDLAKREVARSHRIVVVEGYTDVMAAHLSGVTTAVATCGTAFGADHVRVVRRLLGDVDDPAAGVVTGQGREARGGEVIFTFDGDAAGQKAALRAYAEDQRFATQTFVAVDPGGLDPCDLRMKEGDPGIPRLLSRRVPLFEFVIRTSLSHLDLDTSEGRVRGLRSAAPVVAGIRDRALKREYTRRLAGWLGLPDAEVHAAVQAAGRRGAQPSAGRGGQWPADETAGPDAAAPVRGLPPVTDPVEQLEREALAVIIQFPMAAHQAGADELGADSFGQLTHRAVYEAVAAAGGTAEVPGLVQQAVAAGMGEQEAQRRATLRWLQQVRDGAIGLVEAAITELAVAPLPLPTVRGRGTEVDASGLERYAKGVLDSLAVMGINRRLVEMRSRHRRMSPHEEGYRELFSEIAALEQRRMHIRQGT$","DNA primase","Cytoplasm","DNA primase","DNA primase ","DNA primase","","Ziegelin G., Scherzinger E., Lurz R., Lanka E. Phage P4 alpha protein is multifunctional with origin recognition, helicase and primase activities. EMBO J. 1993. 12(9):3703-3708. PMID: 8253092","","","

InterPro
IPR002694
Domain

Zinc finger, CHC2-type
PD002988	$\"[9-90]T$	Q6AFU6_BBBBB_Q6AFU6;
G3DSA:3.90.580.10	$\"[1-104]T$	no description
PF01807	$\"[5-103]T$	zf-CHC2
SM00400	$\"[37-91]T$	ZnF_CHCC

InterPro
IPR006154
Domain

Toprim subdomain
SM00493	$\"[265-356]T$	TOPRIM

InterPro
IPR006171
Domain

TOPRIM
PF01751	$\"[265-364]T$	Toprim

InterPro
IPR006295
Domain

DNA primase
TIGR01391	$\"[4-442]T$	dnaG: DNA primase

InterPro
IPR006647
Domain

Toprim, primase
PD002276	$\"[128-425]T$	Q6AFU6_BBBBB_Q6AFU6;

InterPro
IPR013173
Domain

DNA primase DnaG, DnaB-binding
SM00766	$\"[498-654]T$	no description

InterPro
IPR013237
Domain

Phage P4 alpha, zinc-binding
SM00778	$\"[36-72]T$	no description

InterPro
IPR013264
Domain

DNA primase catalytic core, N-terminal
G3DSA:3.90.980.10	$\"[117-246]T$	no description
PF08275	$\"[128-258]T$	Toprim_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.1360.10	$\"[247-390]T$	no description

","BeTs to 18 clades of COG0358COG name: DNA primase (bacterial type)Functional Class: LThe phylogenetic pattern of COG0358 is amtk-qvcebrhujGPolinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 40-121 are 81% similar to a (DNA PRIMASE TRANSFERASE 2.7.7.- ZINC ZINC-FINGER POLYMERASE DNA-DIRECTED PRIMOSOME REPLICATION) protein domain (PD002988) which is seen in Q6AFU6_BBBBB.Residues 122-443 are 41% similar to a (DNA DNA-DIRECTED ZINC RNA TRANSFERASE METAL-BINDING POLYMERASE PRIMOSOME 2.7.7.- ZINC-FINGER) protein domain (PD180995) which is seen in PRIM_TREPA.Residues 159-456 are 72% similar to a (DNA PRIMASE TRANSFERASE 2.7.7.- NUCLEOTIDYLTRANSFERASE ZINC DNA-DIRECTED RNA METAL-BINDING POLYMERASE) protein domain (PD002276) which is seen in Q6AFU6_BBBBB.Residues 231-306 are 59% similar to a (DNA PRIMASE) protein domain (PD464287) which is seen in Q9AW16_GUITH.Residues 361-699 are 42% similar to a (DNA PRIMASE) protein domain (PD849022) which is seen in Q8G573_BIFLO.","","-46% similar to PDB:1DD9 STRUCTURE OF THE DNAG CATALYTIC CORE (E_value = 2.3E_37);-46% similar to PDB:1DDE STRUCTURE OF THE DNAG CATALYTIC CORE (E_value = 2.3E_37);-46% similar to PDB:1EQN E.COLI PRIMASE CATALYTIC CORE (E_value = 2.3E_37);-45% similar to PDB:2AU3 Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase Domains) (E_value = 2.0E_36);-60% similar to PDB:1D0Q STRUCTURE OF THE ZINC-BINDING DOMAIN OF BACILLUS STEAROTHERMOPHILUS DNA PRIMASE (E_value = 6.3E_19);","Residues 36 to 134 (E_value = 1.6e-46) place ANA_0962 in the zf-CHC2 family which is described as CHC2 zinc finger.Residues 159 to 289 (E_value = 1.6e-62) place ANA_0962 in the Toprim_N family which is described as DNA primase catalytic core, N-terminal domain.Residues 296 to 395 (E_value = 7.2e-09) place ANA_0962 in the Toprim family which is described as Toprim domain.","","primase ","","1","","","Thu Aug 2 11:31:43 2007","","Thu Aug 2 11:31:43 2007","","","Thu Aug 2 11:31:43 2007","Thu Aug 2 11:31:43 2007","Thu Aug 2 11:31:43 2007","","","Thu Aug 2 11:31:43 2007","","","Thu Aug 2 11:31:43 2007","Thu Aug 2 11:31:43 2007","Thu Aug 2 11:31:43 2007","","Thu Aug 2 11:31:43 2007","Thu Aug 2 11:31:43 2007","","","","","yes","","" "ANA_0963","1041354","1040032","1323","5.41","-13.49","48102","ATGTCAGCGCAGAAATCTGGATCCGAACCTGTGCGTATCGACGGACGGGACGCACTTGACCTGTCCGAGGGGTACCAGGCGCAGGACGTGGACCGCTTCGTTCACGAGCAGGCGAAGAATCCTCAGCGCACCCCTTTTGAACGCGACCGGGCTCGGGTCCTGCACTCCTCGGCGCTGCGGCGCCTGGGGGCCAAGACCCAGGTGCTGGGGCCCGGCGCTGACGACTTCGTGCGCACCCGGCTCACCCACTCCCTGGAAGTGGCGCAGGTGGGGCGTGCCCTGGGGCAGGCGCTGGGATGCGACCCCGACGTCGTCGATACCGCCTGCCTGTCCCACGACCTGGGCCATCCCCCCTACGGGCACAACGGTGAAAAGGCGCTCGACGTCGTGGCCCGCCAGATCGGGGGCTTCGAGGGCAATGCCCAGACCTTCCGGATCCTTACCCGGCTGGAGCCGAAGACCCTTGACGAGGCCGGGCGGCCGGTCGGCGTCAATCTGACGCGGGCCAGTCTCGACGCCGTCGCGAAGTACCCGTGGCTCAAGGGCAGGGGACCGGGTGGTCCGGACGGGTGCAGCGCGCGCAAGTACTCCTCCTACGACGACGACGCCGAGATCTTCGCCTGGATGCGTCAGGGAGCCCCGGAGGGTAGGCGCTGCATCGAGGCGCAGATCATGGACCTGTCCGACGACGTCGGCTACTCCGTCCACGACGTCGAGGACGCGATCGCCCTGGGGCGCCTGGACCCGGGCTGTCTGACCGACCCCAAGGAGGTCGATGAGCTGCTCGAGGCCACGCGGGCCTGGTACGGCACCGACCTGAGCGCCGACGCCCTTGGGGCGGCTTTCGAGAGGCTGGCCGGCCAGCCCTATTGGATCCGCTCCTACAACGGCTCCGTGGCCGACGCAGCGCACCTGAAGAACCTCACCAGCGAGATCATCGGACGCTTCGTCTCGGCTGTCGCCACCGCCACTCGACAGGCCTACGGCAACGGGCCCTTGACTCGCTACGAGGCCGAGCTCGTCATTCCCGAGGAGACGGCCGCGGAGATCCTCCTCCTCAAGGGCATCGCCGTGCGCTACGTCATGGAGCCCCGTGAGCATGAGCCGGTTTACCTGCGCCAGCGCACCCTCATCTTCGACCTCGCCGACGTCCTCATGACCGGCGGCGGGAAGGGCATCGACCCGGTTCTCCTCGATGTCTGGCACCGGGCCGAGAACGATGATGCGCGCCTGCGGGTGGTGGTCGACCAGATCGCCTCCCTGACGGACACCTCCGCACGGGCCTGGCACGCCCGGCTGTGCGGCATGTTCTCCGAGGTCTAG","MSAQKSGSEPVRIDGRDALDLSEGYQAQDVDRFVHEQAKNPQRTPFERDRARVLHSSALRRLGAKTQVLGPGADDFVRTRLTHSLEVAQVGRALGQALGCDPDVVDTACLSHDLGHPPYGHNGEKALDVVARQIGGFEGNAQTFRILTRLEPKTLDEAGRPVGVNLTRASLDAVAKYPWLKGRGPGGPDGCSARKYSSYDDDAEIFAWMRQGAPEGRRCIEAQIMDLSDDVGYSVHDVEDAIALGRLDPGCLTDPKEVDELLEATRAWYGTDLSADALGAAFERLAGQPYWIRSYNGSVADAAHLKNLTSEIIGRFVSAVATATRQAYGNGPLTRYEAELVIPEETAAEILLLKGIAVRYVMEPREHEPVYLRQRTLIFDLADVLMTGGGKGIDPVLLDVWHRAENDDARLRVVVDQIASLTDTSARAWHARLCGMFSEV$","Deoxyguanosinetriphosphate triphosphohydrolase","Cytoplasm, Extracellular","deoxyguanosinetriphosphate triphosphohydrolase","deoxyguanosinetriphosphate triphosphohydrolase ","putative deoxyguanosinetriphosphate triphosphohydrolase","","Klann A.G., Belanger A.E., Abanes-De Mello A., Lee J.Y., Hatfull G.F. Characterization of the dnaG locus in Mycobacterium smegmatis reveals linkage of DNA replication and cell division. J. Bacteriol. 1998. 180(1):65-72. PMID: 9422594","","","

InterPro
IPR003607
Domain

Metal-dependent phosphohydrolase, HD region
SM00471	$\"[76-243]T$	HDc

InterPro
IPR006261
Family

Deoxyguanosinetriphosphate triphosphohydrolase
TIGR01353	$\"[42-435]T$	dGTP_triPase: deoxyguanosinetriphosphate tr

InterPro
IPR006674
Domain

Metal-dependent phosphohydrolase, HD region, subdomain
PF01966	$\"[80-234]T$	HD

","BeTs to 8 clades of COG0232COG name: dGTP triphosphohydrolaseFunctional Class: FThe phylogenetic pattern of COG0232 is -------ce-rh--------xNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 63-110 are 66% similar to a (HYDROLASE DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE TRIPHOSPHOHYDROLASE-LIKE DGTP DGTPASE MAGNESIUM TRIPHOSPHOHYDROLASE TRIPHOSPHATE DEOXYGUANOSINE) protein domain (PD674378) which is seen in DGT1_STRCO.Residues 111-159 are 66% similar to a (HYDROLASE TRIPHOSPHOHYDROLASE DEOXYGUANOSINETRIPHOSPHATE DGTPASE DGTP TRIPHOSPHOHYDROLASE-LIKE MAGNESIUM TRIPHOSPHOHYDROLASE DEOXYGUANOSINE TRIPHOSPHATE) protein domain (PD884130) which is seen in DGT2_PSEAE.Residues 112-193 are 53% similar to a (TRIPHOSPHOHYDROLASE HYDROLASE DEOXYGUANOSINETRIPHOSPHATE DGTPASE) protein domain (PDA027S3) which is seen in Q6ME10_PARUW.Residues 113-153 are 75% similar to a (DOMAIN TRANSDUCTION SENSORY PHOSPHORYLATION RESPONSE HYDROLASE REGULATOR TRANSMEMBRANE RNA-BINDING UPF0144) protein domain (PD110558) which is seen in Q6N5W5_RHOPA.Residues 116-176 are 85% similar to a (HYDROLASE DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE-LIKE TRIPHOSPHOHYDROLASE HD SUPERFAMILY PHOSPHOHYDROLASE DOMAIN METAL HAD) protein domain (PD497720) which is seen in DGT1_STRAW.Residues 157-189 are 81% similar to a (HYDROLASE DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE-LIKE TRIPHOSPHOHYDROLASE DGTP DNTP TRIPHOSPHOHYDROLASE) protein domain (PD329354) which is seen in DGT1_CORGL.Residues 166-286 are 47% similar to a (TRIPHOSPHOHYDROLASE HYDROLASE DEOXYGUANOSINETRIPHOSPHATE DGTPASE DGTP MAGNESIUM TRIPHOSPHOHYDROLASE-LIKE TRIPHOSPHOHYDROLASE DEOXYGUANOSINE TRIPHOSPHATE) protein domain (PD152687) which is seen in Q7MBE5_CHRVO.Residues 190-246 are 61% similar to a (HYDROLASE DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE-LIKE TRIPHOSPHOHYDROLASE DGT DGTP) protein domain (PD973670) which is seen in Q73Y26_MYCPA.Residues 247-292 are 73% similar to a (HYDROLASE DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE-LIKE TRIPHOSPHOHYDROLASE DGTP DNTP TRIPHOSPHOHYDROLASE DGTPASE DGT RELATED) protein domain (PD401964) which is seen in DGT1_BIFLO.Residues 333-461 are 66% similar to a (HYDROLASE DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE-LIKE TRIPHOSPHOHYDROLASE DGT DGTP) protein domain (PD040480) which is seen in DGT1_BIFLO.","","-47% similar to PDB:2DQB Crystal structure of dNTP triphosphohydrolase from Thermus thermophilus HB8, which is homologous to dGTP triphosphohydrolase (E_value = 8.6E_41);-50% similar to PDB:2PGS Crystal structure of a putative deoxyguanosinetriphosphate triphosphohydrolase from Pseudomonas syringae pv. phaseolicola 1448A (E_value = 9.5E_32);","Residues 118 to 272 (E_value = 2.7e-13) place ANA_0963 in the HD family which is described as HD domain.","","triphosphohydrolase (DGTPASE)","","1","","","Thu Aug 2 11:25:50 2007","","Thu Aug 2 11:25:50 2007","","","Thu Aug 2 11:25:50 2007","Thu Aug 2 11:25:50 2007","Thu Aug 2 11:25:50 2007","","","Thu Aug 2 11:25:50 2007","","","Thu Aug 2 11:25:50 2007","","Thu Aug 2 11:25:50 2007","","Thu Aug 2 11:25:50 2007","Thu Aug 2 11:25:50 2007","","","","","yes","","" "ANA_0964","1041385","1042770","1386","5.62","-15.52","50280","ATGGTCGTCACCATTCCGACACCTCCGACACCGCCCCAGGGGAGCGCCGGTGCCCGATCCCTCCAGCTTGTGGTCGCCACGCATCCTCCTCACATCGATGAATCACCTCTTGGACGTCAAGTCCCTGGGCACGCGCCCGGCGGAAGGGAGACACCTGCTGTGACCACCACCACGACCCTCGTTCACCGGCCCTACGACGGTCCGGAAGAGTGGTGGCGCCATGCACTGGTCTACGAGATCCCCTCACCGGCCATGGGGGCGGCCGAGCTGGACCGCACCGATCCCATCATCGAGCACGCCCTCTACCTGGGCATGGACGCGGTGCTCATCCGTCCGAGTCTGCTCGATGTGGACACCGAGATGGACTCGATCCGCCGCTTCATCGACAAAGCCGGCGAGCAGGGACTGCGCACCATCGTGCGCATCTCCGGAGCGCTTGGTCCGATCACGGGTCCCTACGCCAAGCAGACCACGGGCTTCGTCACCGGTCTCGAGCAAGCCGCAGACGACCTGCTGCGCCGTTCGGAGGCCTACCTGCAGGCCGGTGCGGCCGGCATCGACCTGGGCACGATCGTCCCTCCCCAGCTCACCAGCGGAATCCGGCTGGATCGACTCAGTACCTACTGCGCCATGCTGCACGGCCAGCTGGCCGAGTACGTCGACGAGGGCATCATCGGTGCCGACGTGACCGCCGACTACCCGGAGTCACTGCGTCATCACCTCCAGGACGACTGGGTGCACCACCTGCGCGATGACTGTCTGACGCTGACACGGTGGAACGCCGAGTCGCTCACGTCCCACCTGACCCGGTCGCTGGACGAGCACGACCGCTTCGGGGCACCCCCCACCTGGCGATTCCTGCCTCCCCACATTCTCTCCGAGCACCTGGATCCGGGAGACGGGCAGCGCTGGTACTCCGTCAACCGAGATGAACGGCTGCGTCGAGGGCTCGCCCTGCAGGCCATGATGCTGGCCCTGCCCGGCTCGCTCTACCTGCGTCAGGGCGATGAGATCGCCCTGTCCGACTCCGACAAGCCGACCGCTCCCTTGGAGCTGGCCGACATGGTGGCTGAGCACACGCAGGTGCAGTCCTCTCAGTTCGGCTCTCCGACAGCGACCGTGCGCCACGCGGCCCACGTGCGGCACGAGTACAACCTGGCCTGCGCTCCCCTGGCCTTCGTCACTGGCCTGGAGTGGTGCCCGCCCCAGACCCTCGCCTTCCTGGTCCGCGGCGTCCTGGTCGTCGTCAACACCTCCGACTCCCCCGTCACCTTGCCGGCTGAGGCCAAAGTTCTTCTGTCCTCTCAGCCCCTGCGTCAGGACGGGGGACGTCTGCTCGTGCCCCCGGCGACGACAACGTGGCTGGAGGCCACAACCGTTGCCTAG","MVVTIPTPPTPPQGSAGARSLQLVVATHPPHIDESPLGRQVPGHAPGGRETPAVTTTTTLVHRPYDGPEEWWRHALVYEIPSPAMGAAELDRTDPIIEHALYLGMDAVLIRPSLLDVDTEMDSIRRFIDKAGEQGLRTIVRISGALGPITGPYAKQTTGFVTGLEQAADDLLRRSEAYLQAGAAGIDLGTIVPPQLTSGIRLDRLSTYCAMLHGQLAEYVDEGIIGADVTADYPESLRHHLQDDWVHHLRDDCLTLTRWNAESLTSHLTRSLDEHDRFGAPPTWRFLPPHILSEHLDPGDGQRWYSVNRDERLRRGLALQAMMLALPGSLYLRQGDEIALSDSDKPTAPLELADMVAEHTQVQSSQFGSPTATVRHAAHVRHEYNLACAPLAFVTGLEWCPPQTLAFLVRGVLVVVNTSDSPVTLPAEAKVLLSSQPLRQDGGRLLVPPATTTWLEATTVA$","Alpha-glucosidase","Cytoplasm","alpha-glucosidase","putative alpha-glucosidase ","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0965","1042913","1044169","1257","5.11","-10.15","43368","ATGGCCGCTCTGGCCTCCACCGTGCCAACGTTGGCCGCCTGCTCCGGCTCGCGCAATACTGCGGGCACGGCGGCCTCGGGCGGCGCTGCCTCACAGGCATCTGACGCCTCGGCAGGCGGCTCCGATGCCGATCTGGTCATCTGGGCGGATCAGAAGAAGGCGGACTCCCTCAAGGAGATCGCCAAGACCTGGGGCAAGCAGCAGGGCATCTCGGTGGCGGTCCAGACCGTCGCCAATGACTTGCAGCCCAACTTCATCACCGCCAACCAGGCCGGCAACGGCCCTGACATCGTCCTCGGCGCACACGACTGGATCGGCAACCTGGTGCAGAACAGCGCGATCCGGCCGGTCGTTCTGAGCCCCGAGGCCGAATCCAACTACTCCGACATCGCGCTCAAGGCGGTCACCTACGACGGCCAGATCTACGCAACGCCCTACGCCGTCGAGTGCCTGGGCCTGTTCGTCAACAAGGCACTGACCTCAGTGACCCAGCCGGCCAGCATCGAGGAGATGATCGAGGCCGGCAAGGCGGCCGGAACCGAGCTCGTCCTGTCGCAGGCCATCGACGAGAAGGGCGACGCCTACAACATGGAGCCGATCTACACCGCCGCCGGCGGCTACATGTTCGGCAAGAACCCGGACGGCTCCTACGATCCCAATGACCTCGGTATCGGCAAGGAGGGATCCATCAAGGCCGCGGAGAAGATCCGCCAGCTCGGGCAGCAGGGAGTCCTCAGGAAGTCGGTCACGGCCGCCAACCATATTTCCTTGTTCACCGATGGTAAGGCTCCCTACCTCATCTCGGGGCCATGGGCCCTGGCGGACATCAAGAAAGCCGGCATCGACTACCAGCTCACGCACATTCCGGGATTCAAAGACATCAAGGACAGTCAGGCGAGCCCCTTCGTCGGGGTCAACTGCTTCTACGTCGCCTCCAACGGAAAGAACAAGGCCTTCGCCGAGACCTTCGTGGCCGACGCGGCCAAGGACATGACCTTCGCGGCATCGATGTTCCCCACCAACGAGCTGCCCCCGGCCCAGAAGGACCTCGCGGACAAGCTCAAGGCGGAGCACCCCGACATGGTCACCTTCGCGGAGCTCTCCGCCAAGGCCGACCCCATGCCCGCGATCCCCGCCATGTCCTCAGTGTGGGAACCCCTTGGACGCGCTCAGGCCAACATCGTCGGTGGGGCCGATCCCGCCAGCACCATGACCGGGGTCGGCCAGACCATCAAGGCGTCGATCAAGGGCTCGTAA","MAALASTVPTLAACSGSRNTAGTAASGGAASQASDASAGGSDADLVIWADQKKADSLKEIAKTWGKQQGISVAVQTVANDLQPNFITANQAGNGPDIVLGAHDWIGNLVQNSAIRPVVLSPEAESNYSDIALKAVTYDGQIYATPYAVECLGLFVNKALTSVTQPASIEEMIEAGKAAGTELVLSQAIDEKGDAYNMEPIYTAAGGYMFGKNPDGSYDPNDLGIGKEGSIKAAEKIRQLGQQGVLRKSVTAANHISLFTDGKAPYLISGPWALADIKKAGIDYQLTHIPGFKDIKDSQASPFVGVNCFYVASNGKNKAFAETFVADAAKDMTFAASMFPTNELPPAQKDLADKLKAEHPDMVTFAELSAKADPMPAIPAMSSVWEPLGRAQANIVGGADPASTMTGVGQTIKASIKGS$","Maltose ABC transporter, periplasmic maltose-binding protein","Extracellular, Periplasm","putative maltose binding protein","K02027 multiple sugar transport system substrate-binding protein","extracellular solute-binding protein, family 1","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[17-325]T$	SBP_bac_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[39-375]T$	no description

","BeTs to 8 clades of COG2182COG name: Maltose-binding periplasmic proteins/domainsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2182 is ---pkz--vd-lb-e-g---------Number of proteins in this genome belonging to this COG is 1","***** IPB006060 (Maltose binding protein signature) with a combined E-value of 1.8e-17. IPB006060B 82-100 IPB006060C 142-161 IPB006060H 375-394","Residues 45-156 are 70% similar to a (ABC PERIPLASMIC SUGAR BINDING TRANSPORTER TRANSPORTER SUGAR-BINDING LIPOPROTEIN SOLUTE-BINDING SPERMIDINE/PUTRESCINE-BINDING) protein domain (PD115161) which is seen in Q9XDA2_THECU.Residues 165-266 are 69% similar to a (MALTOSE BINDING) protein domain (PDA0Y6M3) which is seen in Q9XDA2_THECU.Residues 195-263 are 60% similar to a (PERIPLASMIC MALTOSE-BINDING ABC TRANSPORTER MALTOSE/MALTODEXTRIN-BINDING PRECURSOR SIGNAL MALTOSE LIPOPROTEIN SUGAR) protein domain (PD395577) which is seen in O07009_BACSU.Residues 267-409 are 62% similar to a (ABC SUGAR PERIPLASMIC BINDING TRANSPORTER SUGAR-BINDING TRANSPORTER LIPOPROTEIN SOLUTE-BINDING PROBABLE) protein domain (PD023543) which is seen in Q9XDA2_THECU.","","-53% similar to PDB:2FNC Thermotoga maritima maltotriose binding protein bound with maltotriose. (E_value = 7.0E_52);-52% similar to PDB:2GHA Thermotoga maritima maltotriose binding protein bound with maltotriose (E_value = 9.2E_52);-52% similar to PDB:2GHB Thermotoga maritima maltotriose binding protein, ligand free form (E_value = 9.2E_52);-51% similar to PDB:2DFZ Crystal structure of cyclodextrin-binding protein complexed with gamma-cyclodextrin (E_value = 1.1E_41);-44% similar to PDB:1MDP REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN (E_value = 1.9E_28);","Residues 17 to 334 (E_value = 2.1e-10) place ANA_0965 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","maltose binding protein (mmbp)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0966","1044260","1045834","1575","9.30","9.41","57281","ATGACGTCCGCATCCACCACCCCGAGGGAGAAGACCACGACCATCAGAGGTCTCGTCGGTCGCATCATCGTGCTGTCCCTCACGCTGGTCGCAGCGATCTACCTCGTCCCACTTCTTATCGCCTACCGGATGTGGTTGTGGCTGGGAATCGTCGTCCTGACCACGGGGGCTATGTTCCTGCTGTACTCGACCAAGAGATTCGTCCCCGCCAAGTACCTCTTCCCCGGCACGTTCTTCCTCACCGTCTTCCTTATCGTCCCCATCGTGCTGACCATTCAAACCTCCTTCACCAACTTCGGGGACGGGTACCGCGGAACCAAGGAGGAGGCCATCTCCTCCATCACCAACAACTCGATGGTCCGCACGGAGGACTCTCCCACCTATGGTCTGTCAGTGGCGACCGACGGCGACGTCACCAAGGGCCCCTTCTCACTGTTCCTCGTCAATCCGCAGACCAAGGAGGTGCTGCGGGGAAGTGACGGGAAAAAGCTGGAGAAGGTCGACGCCAGCACCGTGACCATCGACAACGGCGTGGTGACCAAGGCGGAGGGATACACGATCCTGTCCCCCAGGCAGATCAACACCGCCTACGAGGACATCAGCGCCATGTCGGTTCCCTTCACGGACAAGACCACGGTCAAGGTTCAGGGCGTCAGGACCGCTTTCGAGGGAACCAAGCGGATGGTCTACAACAAGTCCTCCGACACCATCACCAACACCGCCACCGGGGATGTCTACTCGGTCAAGAAGGTGGGACTGTCCGAGCACTTCGTCAACGCCGAGGGAGAGAGCCTGGCCCAGTCCTGGAAGCAGAACGTGGGGCTGGCCAATTACTCACGGCTCTTCACTGAGGGCAACCTCGCCTCCCAGTTCCTCAAGGCCTTCGCATGGACCATCATCTTCGCCCTGGGCTCGGTGCTGCTCACCTTCGGCCTCGGTTTCTTCTTGGCGCTGACCCTCAATGATGATCGCATCAAGGGTAAGAAGCTCTACCGCTCCTTCCTCCTGCTGCCCTACGCCGTACCCGGCTTCATCTCGCTGCTCGTGTGGTCGAACTTCTACAACCAGGACTTCGGCCTCATCAATCGGATGATGCACCTCAGTATCCCGTGGCTGTCCGACCCGACCATGGCCAAGATCGCCGTCCTGCTCACCAACACGTGGATGGGCTTCCCCTACATGTTCATCGTGTGCACCGGCGCTCTGCAGTCCATCTCCGGCGATGTCAAGGAGGCGGCCAAGATGGACGGCGCCAGTGGCATGCAGGCCACATGGCGCATCGTCACCCCACTGCTCCTGGTCGCCGTCGCCCCTCTGCTGGTGAGCACCTTCGCCTTCAACTTCAACAACTTCAATGCCATCCAGCTGCTGACCGAGGGTGGGCCCTTCCCGGCCGGGGAGTACACACGCGGCGGAACCGACATCCTCATCTCCATGGTCTACCGCATCGCCTTCGGCCGTGCCGGCTCGGACTTCGGATTCGCCTCGGCCGTCTCCGTGGTCCTGTTCGCCGTCACCGGCGTCCTGGCCGCATTGCAGTTCCGAGCCACCAAGAAGCTCGAAGACGTCAACTGA","MTSASTTPREKTTTIRGLVGRIIVLSLTLVAAIYLVPLLIAYRMWLWLGIVVLTTGAMFLLYSTKRFVPAKYLFPGTFFLTVFLIVPIVLTIQTSFTNFGDGYRGTKEEAISSITNNSMVRTEDSPTYGLSVATDGDVTKGPFSLFLVNPQTKEVLRGSDGKKLEKVDASTVTIDNGVVTKAEGYTILSPRQINTAYEDISAMSVPFTDKTTVKVQGVRTAFEGTKRMVYNKSSDTITNTATGDVYSVKKVGLSEHFVNAEGESLAQSWKQNVGLANYSRLFTEGNLASQFLKAFAWTIIFALGSVLLTFGLGFFLALTLNDDRIKGKKLYRSFLLLPYAVPGFISLLVWSNFYNQDFGLINRMMHLSIPWLSDPTMAKIAVLLTNTWMGFPYMFIVCTGALQSISGDVKEAAKMDGASGMQATWRIVTPLLLVAVAPLLVSTFAFNFNNFNAIQLLTEGGPFPAGEYTRGGTDILISMVYRIAFGRAGSDFGFASAVSVVLFAVTGVLAALQFRATKKLEDVN$","Maltose ABC transporter, permease protein","Membrane, Cytoplasm","Maltose transport system permease protein malF","K02025 multiple sugar transport system permease protein","Fructose-bisphosphate aldolase","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[291-518]T$	BPD_transp_1
PS50928	$\"[295-513]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-91]?$	signal-peptide
tmhmm	$\"[12-34]?$ $\"[40-62]?$ $\"[72-92]?$ $\"[297-319]?$ $\"[334-354]?$ $\"[389-407]?$ $\"[428-448]?$ $\"[492-512]?$	transmembrane_regions

","BeTs to 7 clades of COG3834COG name: ABC-type maltose transport systems, permease componentFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG3834 is ---pk---vd-lb-e-g---------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 100-284 are 52% similar to a (MALTOSE PERMEASE SYSTEM ABC MALF TRANSMEMBRANE TRANSPORTER) protein domain (PD906739) which is seen in Q6A7G8_PROAC.Residues 298-362 are 72% similar to a (TRANSMEMBRANE PERMEASE ABC SUGAR TRANSPORTER TRANSPORTER MEMBRANE SYSTEM INTEGRAL LIPOPROTEIN) protein domain (PD582700) which is seen in Q6A7G8_PROAC.Residues 344-419 are 68% similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q9L527_VIBCH.","","-41% similar to PDB:1CF2 THREE-DIMENSIONAL STRUCTURE OF D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOTHERMUS FERVIDUS (E_value = );","Residues 291 to 518 (E_value = 7.9e-10) place ANA_0966 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transport system permease protein malF (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0968","1045862","1046791","930","9.47","6.59","33260","ATGAGCACCTCATCGCAGCCCGTGTCCCGGTCCGCATCAAACAGTTCCGAGGACAGCGTCGTCATCGAGAATCACATGCCGTTCTCACGCTGGTTCCGGGAGATCGGCTGGAGACACGTCGTCGGCGTCATTGCCCTGGTCTTCGCAGCCTTCCCCGTCCTCTACGTCATCTCCGCCTCTCTCAACCCCCTGGGCACGGTGGCATCCACCGGGTTGATCCCCACCAAGGTGAGTCTGGTCAACTACCAGAACCTGCTATCCGGGGCACGGGGCCCATTCCTGCGCTGGTACCTCAACACGATCATCATCTGCACAGTGGTGGCAACCGCTCAGGTCTTCCTGTCCCTGCTGGGGGCCTACGCCTTCTCCCGGTTCCGCTTCACTGGACGCCGCGGCGGCCTGCTCGCCCTGCTCCTGATTATGATGTTCCCCGCGATCCTGTCCATGATCGCCATCTACACGATGATCTCCGACATCGGCCAGGTCGTCCCCTTCCTCGGCCTCAACACCCTGGCCGGCTACAGCCTGGCGCTCATGGGCGGAGCACTGGGGCAGGTGTGGCTCATCAAGGGAACCTTCGACACGATTCCCCGTGAGCTCGATGAAGCCGCCATCATCGACGGCTGCACGCACTGGCAGGTCTTCCGCATCATCCTTCTGCCCACGCTCAAGCCGATCATTGCCACCACCTTCCTGCTGGCCTTCGTGGGTGTCATCAGCGAGTTCCTCCTGGGCTCGATCATTCTGACCGACAACTCCCAGAAGACGCTCGCCGTGGGGCTCTACGGCATGCTCGTCGGCGACCGCTCCAACAACCTGGGCATCTTCGCTGCCGGAGCGGTCCTCACCATGGCCCCGGTGATCGCTCTGTTCCAATACCTGCAGCGCTATATCGTCGGCGGATCGATCTCGGGTGCGGTCAAGGGCTGA","MSTSSQPVSRSASNSSEDSVVIENHMPFSRWFREIGWRHVVGVIALVFAAFPVLYVISASLNPLGTVASTGLIPTKVSLVNYQNLLSGARGPFLRWYLNTIIICTVVATAQVFLSLLGAYAFSRFRFTGRRGGLLALLLIMMFPAILSMIAIYTMISDIGQVVPFLGLNTLAGYSLALMGGALGQVWLIKGTFDTIPRELDEAAIIDGCTHWQVFRIILLPTLKPIIATTFLLAFVGVISEFLLGSIILTDNSQKTLAVGLYGMLVGDRSNNLGIFAAGAVLTMAPVIALFQYLQRYIVGGSISGAVKG$","Maltose ABC transporter, permease protein","Membrane, Cytoplasm","maltose ABC transporter, permease protein","K02026 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[97-304]T$	BPD_transp_1
PS50928	$\"[97-294]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-49]?$	signal-peptide
tmhmm	$\"[35-55]?$ $\"[97-117]?$ $\"[132-152]?$ $\"[171-189]?$ $\"[231-251]?$ $\"[270-290]?$	transmembrane_regions

","BeTs to 6 clades of COG3833COG name: ABC-type maltose transport systems, permease componentFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG3833 is ---p----vd-lb-e-g---------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 27-85 are 71% similar to a (MALTOSE PERMEASE TRANSMEMBRANE SYSTEM MALG ABC TRANSPORTER) protein domain (PD759114) which is seen in Q6A7G7_PROAC.Residues 142-221 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q8ZAS4_YERPE.","","-48% similar to PDB:1T9K X-ray crystal structure of aIF-2B alpha subunit-related translation initiation factor [Thermotoga maritima] (E_value = );-62% similar to PDB:1LRZ x-ray crystal structure of staphylococcus aureus femA (E_value = );","Residues 97 to 304 (E_value = 8.1e-14) place ANA_0968 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","ABC transporter, permease protein (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0969","1046988","1048001","1014","5.65","-7.21","36205","ATGCCACAGAGACTCACTCTCACTGACATCGCCGACCAGGCGGGCGTCTCCACCGCGACTGTCTCCCGTGTGCTCAATGGAAAGTCCAACGTGGCGGACTCGACCCGCCGGCAGGTGCTCGCTGCGCTCGACATCTTGGGTTATGAGCGTCCCGAGTCGGTGCACCAGACCTCCCGCGGTCTCATGGGGCTGATCGTGCCCGAGCTGAGCAACCCGATCTTTCCGCTGTTCGCCCAGCAGATCGAGCAGCTCCTGGCCCCCTCCGGGCACACTCCCCTGCTGTGTACCCAGACCCCCGGCGGCATCAGCGAAGACGAGTACATCGAGATGCTCGTGGACCGCGGTGTCGCCGGCATCATCTTCGTCTCCGGACGCCACGCGGACACCACCGGCGATGTCACCCGCTACCAGCGCCTGCGTGAGCGCGGCGTACCGTTGGTGACGATCAACGGCAACGCGCCTACCATCAAGGCACCGGGCTTCGCCACCGATGACCGCCGGGCGACCCGGATGGCGGTCGATCACCTCATCGCCCTGGGGCATCAGCGCGTCGGTCTGGCCATGGGGCCAATGCGCATGGTGCCGGCTCAGCGCAAGCGCTCCGGCTACGAGGACGCCATGAGCGAGAGTCTGCCCGAGGAACCCCTGCGGATCGTGGAGACGCTCTACACCTACGAGGGCGGGGTCAGCGCGGCGCTGCACCTGCTGGAGCAGGGCTGCACCGGCATCGTGTGCTCCTCGGACGTCATGGCCCTGGGAGTGGTCCACGGGGTGCGCCAGACGGGCAGGTCAGTGCCTCATGACGTCTCCGTCATCGGCTACGACGACTCACCGCTCATCCCCATGACGGACCCGCCGCTGACCACGGTGCGCCAGCCCGTGGAGTCCATCTGCCGGGCGGCCGTCTCCACGCTCCTCGCACAGCTCAACGGGCAACGACCGGCCGACACCGAGATGCTCTTCGCCCCAGACCTCATCGTGCGTGACTCAACCGCCGCGGCCCCCATCGACTGA","MPQRLTLTDIADQAGVSTATVSRVLNGKSNVADSTRRQVLAALDILGYERPESVHQTSRGLMGLIVPELSNPIFPLFAQQIEQLLAPSGHTPLLCTQTPGGISEDEYIEMLVDRGVAGIIFVSGRHADTTGDVTRYQRLRERGVPLVTINGNAPTIKAPGFATDDRRATRMAVDHLIALGHQRVGLAMGPMRMVPAQRKRSGYEDAMSESLPEEPLRIVETLYTYEGGVSAALHLLEQGCTGIVCSSDVMALGVVHGVRQTGRSVPHDVSVIGYDDSPLIPMTDPPLTTVRQPVESICRAAVSTLLAQLNGQRPADTEMLFAPDLIVRDSTAAAPID$","Maltose operon transcriptional repressor","Cytoplasm, Membrane","Transcription regulatory protein reg1","MalR repressor protein","Alanine racemase","","Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 1992. 267(22):15869-15874. PMID: 1639817Vartak N.B., Reizer J., Reizer A., Gripp J.T., Groisman E.A., Wu L.F., Tomich J.M., Saier Jr M.H. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 1991. 142(9):951-963. PMID: 1805309","","","

InterPro
IPR000843
Domain

Bacterial regulatory protein, LacI
PR00036	$\"[6-16]T$ $\"[16-26]T$	HTHLACI
PF00356	$\"[5-30]T$	LacI
SM00354	$\"[4-71]T$	HTH_LACI
PS50932	$\"[5-63]T$	HTH_LACI_2
PS00356	$\"[7-25]T$	HTH_LACI_1

InterPro
IPR001761
Domain

Periplasmic binding protein/LacI transcriptional regulator
PF00532	$\"[59-329]T$	Peripla_BP_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[5-62]T$	no description
G3DSA:3.40.50.2300	$\"[164-303]T$	no description

","BeTs to 9 clades of COG1609COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1609 is --------vdrlb-efghs--j----Number of proteins in this genome belonging to this COG is 7","***** IPB000843 (LacI bacterial regulatory protein HTH signature) with a combined E-value of 2.7e-10. IPB000843A 6-16 IPB000843B 16-26***** IPB001761 (Periplasmic binding protein/LacI transcriptional regulator) with a combined E-value of 5.1e-08. IPB001761A 5-17 IPB001761B 19-27","Residues 5-122 are 50% similar to a (TRANSCRIPTIONAL DNA-BINDING TRANSCRIPTION REGULATORY REGULATION) protein domain (PDA117I9) which is seen in Q89Q29_BRAJA.Residues 7-50 are 77% similar to a (TRANSCRIPTIONAL 5_apos;REGION AML TRANSCRIPTION DNA-BINDING HTH-TYPE REGULATOR REGULATION ORF-S1) protein domain (PDA1A769) which is seen in YAML_STRLM.Residues 7-189 are 43% similar to a (TRANSCRIPTIONAL REGULATOR LACI FAMILY) protein domain (PD984285) which is seen in Q9AAM4_CAUCR.Residues 10-50 are 85% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR OPERON FAMILY LACI REGULATOR) protein domain (PD000947) which is seen in Q9ACN9_STRLI.Residues 51-96 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL 5_apos;REGION AML REGULATORY HTH-TYPE REGULATOR ORF-S1) protein domain (PD929533) which is seen in Q9XDA3_THECU.Residues 97-144 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION REPRESSOR TRANSCRIPTIONAL REGULATOR BP LACI-FAMILY HTH-TYPE REGULATORY) protein domain (PD966937) which is seen in Q9ACN9_STRLI.Residues 145-198 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR FAMILY LACI OPERON REGULATOR) protein domain (PD275683) which is seen in YAML_STRLM.Residues 202-255 are 67% similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR FAMILY LACI OPERON REGULATOR) protein domain (PD539176) which is seen in YAML_STRLM.Residues 264-331 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR REPRESSOR FAMILY LACI OPERON REGULATOR) protein domain (PD000591) which is seen in Q9XDA3_THECU.","","-53% similar to PDB:1RZR crystal structure of transcriptional regulator-phosphoprotein-DNA complex (E_value = 1.4E_39);-53% similar to PDB:1ZVV Crystal structure of a ccpa-crh-dna complex (E_value = 2.3E_39);-53% similar to PDB:2JCG APO FORM OF THE CATABOLITE CONTROL PROTEIN A (CCPA) FROM BACILLUS MEGATERIUM, WITH THE DNA BINDING DOMAIN (E_value = 2.3E_39);-50% similar to PDB:2O20 Crystal structure of transcription regulator CcpA of Lactococcus lactis (E_value = 1.2E_30);-50% similar to PDB:1SXG Structural studies on the apo transcription factor form B. megaterium (E_value = 3.5E_27);","Residues 5 to 30 (E_value = 7.9e-11) place ANA_0969 in the LacI family which is described as Bacterial regulatory proteins, lacI family.Residues 59 to 329 (E_value = 1.9e-07) place ANA_0969 in the Peripla_BP_1 family which is described as Periplasmic binding proteins and sugar binding domain of the LacI family.","","regulatory protein reg1","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0970","1049293","1048043","1251","5.69","-7.22","42128","ATGAAGGTTCTTCTTGCTCCTGGCGGGCTGTGGCCCGAGCCCGCTGGAGTGCCTCTGGCGGGCTCGGGACCAGGTCTCGCCCCGGGCCGGGTCGCCTCCTGCCTGGCGCGTGGCTGGCGGGCGGTGCGCCCCCATGACGCCCTGACCCTGCTGCCCATGGCGGACGGCGGACCGGGCTCGGCCCAGGTGATCGCCCCCGATCAGGTCGTCTCCCGGGAGGTCATTCAGGGGCGGGGGCCGCTCGGACAGGTCAGAGAGGTCGACCTGGTGCGTCTGGTCCCCAGGGCAGCACGATCCGGGAACCGGCATCGAGGCGAGGCGAGCACCTGGTTCCTGGATGCCGCTCGGCTCTTGGCACTGCCGGCTGATCCCGATGAGGCGGCTCAGGAGGTGTTGGAGGGGAGCACCTCCGGCCTGGGAGGAGTCATCGGAGCCGCCCTGAGCCGTACCGGGCCCTTGGACACGCTCCTGGTGGGGATGTCGCGCTCCGCCGTTCACGACGGGGGCCTGGGAGCCATGGACGCGCTCGGCGGCCTACGAGCAGCCAAGGAGCTGCTGTCGCATCGCAGCCTGGGACTGGTCCTGGCCGACGACATCGCCCTGGGAGGCATGAGTGGCGCCGGGGCGGCCCTGGCGAGCATCAGTGCCATCAGCCCTGAGCGGGCACAGGAGCTGGACCGGCGCGCCTGCGCCCGGGCGATGGAAGTCGTCAGCGAGGCTCAGGATCTCGATACTGGTGCCGTCGGTCCACACAGGCCACTGCCTGTCGTCTCCGCGCTGGACGACGTCGGACCCTCCGCCTCCGCGCATGCGGGGGACTCCACCGGAACTGCTCGCCTGAGCGCGTCCACCTGGGGAACCGGGGCGGGCGGAGGCAGCGCCCTGGTGCTGCGGGCCCTGGGCGCATGGGCGCGGCCCGGGGCGCGAGTCATGGCTGAGCTCGTCAGTTTGAGCGAGGCCGCCTACGGGCAGGACCTGGTCGTCGCCGCCTGGGGAGAGCTCTACGACGTCCTGGCCGACGGCGTCGTGGGCGTCGTCGGTCAGAACGCCGCATCCCAGGCGCTGCCGTGCATCGTGGTGTGCGGGCGCTGCGCCGTCAGTCGCGGTGAGCTGGCCGCCGCCGGCGTCACCAACGCCTACGGGCTGCAGGAGTCTCATGCCACCGAGCCCTGGGAAGCGACTGACTTTCACGGGCTGGAGGCACGGCTGATGGACCTCGGCTCCCGACTGGCCCGTACGTGGTCGCGCTGA","MKVLLAPGGLWPEPAGVPLAGSGPGLAPGRVASCLARGWRAVRPHDALTLLPMADGGPGSAQVIAPDQVVSREVIQGRGPLGQVREVDLVRLVPRAARSGNRHRGEASTWFLDAARLLALPADPDEAAQEVLEGSTSGLGGVIGAALSRTGPLDTLLVGMSRSAVHDGGLGAMDALGGLRAAKELLSHRSLGLVLADDIALGGMSGAGAALASISAISPERAQELDRRACARAMEVVSEAQDLDTGAVGPHRPLPVVSALDDVGPSASAHAGDSTGTARLSASTWGTGAGGGSALVLRALGAWARPGARVMAELVSLSEAAYGQDLVVAAWGELYDVLADGVVGVVGQNAASQALPCIVVCGRCAVSRGELAAAGVTNAYGLQESHATEPWEATDFHGLEARLMDLGSRLARTWSR$","Glycerate kinase","Cytoplasm, Membrane","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","Glycerate kinase-like","","","","","No hits reported.","BeTs to 6 clades of COG1929COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG1929 is -------cEbrh---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","Thu Aug 2 11:39:22 2007","","Thu Aug 2 11:39:22 2007","","","Thu Aug 2 11:39:22 2007","Thu Aug 2 11:39:22 2007","Thu Aug 2 11:39:22 2007","","","","","","Thu Aug 2 11:39:22 2007","Thu Aug 2 11:39:22 2007","","","Thu Aug 2 11:39:22 2007","Thu Aug 2 11:39:22 2007","","","","","yes","","" "ANA_0971","1050722","1049334","1389","4.80","-31.74","48288","ATGATCACCGTTGATGCCGTGCGCACCGCCGTGCACACCTCCATGCCCACCATCGTCTCCGACCTGACGGACCTGGTCGCGATCCCCTCGGTCTCCGCCTCCAGCCACGACCAGTCCCAGGTTCAGCGCTCCGCCGAGGCCGTGGCCGCGCTCCTGCGCGACAGCGGTCTGGATGTTGAGATCCTCTCCGTGCCCGCCCCCGACGGCACCCCCGGCCGGCCCGCCGTCCTGGCCCACAAGGCCGGCCCCCAGGGCAGCCCGCACGTCCTGCTCTACTCCCACCACGACGTCCAGCCCGTCGGCGACCCGACCGGCTGGGACCAGGCCGACCCCTTCACCGCCGAGCGGCGCGGGGAACGGCTGTTCGGACGCGGAACCGCTGACGACAAGGCCGGCGTCATCACCCACGCCCACGCCCTGCGCATCCTGGCCTCCCTGGCCGACGGTGAGCTGCCGTGCTCCGTGACGGTCTTCATCGAGGGTGAGGAGGAGGTCGGCAGCCCCTCCTTCGAGAACTTCCTGACCACTCACCGCGACCGCCTGGCCTCCGACGTCATCGTCGTGGCCGACTCCTCCAACTGGAAGGTCGGCGTCCCGTCCCTGACCACCTCGCTGCGCGGCGTCGTCCAGGTCGATGTTCGTCTCGACATGCTCGACCACGCGCTTCACTCCGGCATGTACGGCGGCCCCGTGCTGGATGCCGCCACCGCCATGTGCCGACTGATCGCCTCCTGCCACGACGAGGCCGGTGACGTCTCCGTGGCAGGGCTGGTCAGCCAGTCCCAGGCCGACGCCGACTTCCCCGTCTACCCGGAGGCCGACTTCCGCGCCGATGCCGGCATCCTCGACGGCGTCGAGCTCTCCGGCACCGGCGACCTCACCGCCCGGCTGTGGACCAAGCCCTCCCTGACGCTCATCGGCATGGACGTCACGCCCCTGGACCTGGCCGGCAACGTCCTGACCCCTTCGTGCACGGCCCGACTCTCGCTGCGCATCGCACCCGGGCAGGACCCGGCCGCAGCCCAGGAGGCCCTGGTCGCCCACCTGGAGAAGCACGTACCCTTCGGGGGCCGCCTGACCGTCACCGGCCGTGAAGCCGGGCCCGCCTTCGACGGCTCCGAGGTCACCCCCGCCTCCGAGGCCGCCCACTGGGCCCTGTCCACCGCCTGGGACACCGAGGCCGTCAACATCGGACAGGGCGGCTCCATCCCCTTCATCGCCACCCTGAAGGAGACCTTCCCCGACGCCCAGGTGCTTGTCACCGGGATCGAGGACCCCGACACCCGGGCCCACAGCGAGAACGAGTCCATGCACCTGGGCGAGCTTGAGCACATCGTGGCCGCCGAAGCCCTTCTTCTGGCCCGCCTGGGCGGCGCCATCGACTCATGA","MITVDAVRTAVHTSMPTIVSDLTDLVAIPSVSASSHDQSQVQRSAEAVAALLRDSGLDVEILSVPAPDGTPGRPAVLAHKAGPQGSPHVLLYSHHDVQPVGDPTGWDQADPFTAERRGERLFGRGTADDKAGVITHAHALRILASLADGELPCSVTVFIEGEEEVGSPSFENFLTTHRDRLASDVIVVADSSNWKVGVPSLTTSLRGVVQVDVRLDMLDHALHSGMYGGPVLDAATAMCRLIASCHDEAGDVSVAGLVSQSQADADFPVYPEADFRADAGILDGVELSGTGDLTARLWTKPSLTLIGMDVTPLDLAGNVLTPSCTARLSLRIAPGQDPAAAQEALVAHLEKHVPFGGRLTVTGREAGPAFDGSEVTPASEAAHWALSTAWDTEAVNIGQGGSIPFIATLKETFPDAQVLVTGIEDPDTRAHSENESMHLGELEHIVAAEALLLARLGGAIDS$","Acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase","Cytoplasm, Extracellular","widely conserved protein in peptidase ordeacetlylase family","hypothetical protein","peptidase M20","","Rowsell S., Pauptit R.A., Tucker A.D., Melton R.G., Blow D.M., Brick P. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Structure 1997. 5(3):337-347. PMID: 9083113Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR002933
Family

Peptidase M20
PF01546	$\"[90-455]T$	Peptidase_M20

InterPro
IPR011650
Domain

Peptidase M20, dimerisation
PF07687	$\"[203-357]T$	M20_dimer

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.10	$\"[18-456]T$	no description
PTHR11014	$\"[13-254]T$ $\"[291-461]T$	PEPTIDASE M20 FAMILY MEMBER
PTHR11014:SF15	$\"[13-254]T$ $\"[291-461]T$	GLUTAMATE CARBOXYPEPTIDASE

","BeTs to 18 clades of COG0624COG name: Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase and related deacylasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0624 is a-mpkzyqvdrlb-efghsnujxi--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 2-72 are 57% similar to a (OR WIDELY FAMILY PEPTIDASE DEACETLYLASE) protein domain (PD813945) which is seen in Q8G5E2_BIFLO.Residues 15-81 are 68% similar to a (PEPTIDASE) protein domain (PDA1B5G7) which is seen in Q6AE81_BBBBB.Residues 17-173 are 43% similar to a (M20/M25/M40 PEPTIDASE FAMILY) protein domain (PD813936) which is seen in Q882Q4_PSESM.Residues 39-228 are 41% similar to a (PEPTIDASE) protein domain (PDA084Q2) which is seen in Q6D5Q3_BBBBB.Residues 44-174 are 50% similar to a (SUCCINYL-DIAMINOPIMELATE DESUCCINYLASE PEPTIDASE) protein domain (PD901650) which is seen in Q6N8Q9_RHOPA.Residues 85-166 are 65% similar to a (HYDROLASE DESUCCINYLASE SUCCINYL-DIAMINOPIMELATE DEACETYLASE ACETYLORNITHINE DIPEPTIDASE BIOSYNTHESIS CARBOXYPEPTIDASE FAMILY PEPTIDASE) protein domain (PD001449) which is seen in Q6AE81_BBBBB.Residues 174-229 are 78% similar to a (PEPTIDASE REPEAT FAMILY DIPEPTIDASE HYDROLASE CARBOXYPEPTIDASE M20/M25/M40 GLUTAMATE CARBOXYPEPTIDASE-LIKE CEREVISIAE) protein domain (PDA1A1A9) which is seen in Q6A6C5_PROAC.Residues 231-297 are 62% similar to a (PEPTIDASE M20/M25/M40 FAMILY METALLOPEPTIDASE DEACYLASES ML1193 N-ACYL-L-AMINO ZINC HYDROLASE PEPTIDASE) protein domain (PD960608) which is seen in Q73XH9_MYCPA.Residues 298-439 are similar to a (FAMILY PEPTIDASE M20/M25/M40 HYDROLASE PEPTIDASE REPEAT DIPEPTIDASE CARBOXYPEPTIDASE GLUTAMATE SUCCINYL-DIAMINOPIMELATE) protein domain (PD361106) which is seen in Q73XH9_MYCPA.","","-44% similar to PDB:2POK Crystal structure of a M20 family metallo peptidase from Streptococcus pneumoniae (E_value = 3.4E_18);","Residues 90 to 455 (E_value = 2.2e-25) place ANA_0971 in the Peptidase_M20 family which is described as Peptidase family M20/M25/M40.Residues 203 to 357 (E_value = 4.1e-18) place ANA_0971 in the M20_dimer family which is described as Peptidase dimerisation domain.","","conserved protein in peptidase or deacetlylase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0972","1050764","1051372","609","10.27","19.35","23344","GTGAGCCTGTTCAAGAAGCGCAGCCAGACCCCTGAGCCGGAGCCCGTGGCCGAGCCCTCCCCCAAGCCCGGAGGCAAGGGACGCCCCACGCCCCGGCGCAAGGACCAGCAGGCCAAGAACCTGCACCCGGTGGTCCCCAAAGACCGTGCGGCCGCCAAGCGAGAGGCGCGAGCGGCCCGTGACGCCGCTTGGGAGCGTCAGAACAAGGCCATGGTCACCGGTGAGGAGAAGTACCTCCCGTCCAGGGAGAAGGGGCCGATCAAGCGCTACATCCGTGACTACGTCGACGCGCGCTTCAACCTGGGTGAGTACTTCATGCCCCTCATCTTCGTCCTGCTCATCATCTCCTTCGGGTTCAGCAGCCTCCTGCCCCACTACCCGCTCATCAGCTTCTACACAGTGCTGGCGATGAACGGCTACCTGCTGGCGGCGATCGCCGACGCCGTCTGGTGCTGGACGCGCCTGCGCCGCCGCCTGACCGCGAAGTTCGGCCAGGAGAAGGTCAAGGACGAGGGGACGATCCTCTTCTACATCATGTCGCGCTGCTTCATGCTGCGGCGCTGGCGCCGTCCCGCCGCCCTGGTCGAGCGGGGCCAGTACCCGTCCTGA","VSLFKKRSQTPEPEPVAEPSPKPGGKGRPTPRRKDQQAKNLHPVVPKDRAAAKREARAARDAAWERQNKAMVTGEEKYLPSREKGPIKRYIRDYVDARFNLGEYFMPLIFVLLIISFGFSSLLPHYPLISFYTVLAMNGYLLAAIADAVWCWTRLRRRLTAKFGQEKVKDEGTILFYIMSRCFMLRRWRRPAALVERGQYPS$","Hypothetical protein","Periplasm, Membrane","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[104-124]?$ $\"[130-150]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 35-201 are 60% similar to a (MEMBRANE INTEGRAL TRANSMEMBRANE ML0869 RV2206/MT2262/MB2229) protein domain (PD031727) which is seen in Q6AE80_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0973","1052468","1051413","1056","8.15","2.16","37770","GTGCTCTACGACCTGCTGTACAAGACCGTGCTGACCCGTATCGACCCCGAGCTGATCCATGACGTGTGCCTGGACGCGATCGAGTTCACCGGCAAGGTTCCCCTTGTTAGGGACGTAGTGCGCCAGATGTGGGGGCGCAGGCCGGTCTTCCCGGTGCCCTCGGCCAACCAGGGCGGCCCCTTCGCCCGACCTGTGCCCGGCATCCTGGGGCTCGCCGCGGGTATGGACAAGGAGGGACAGGCCGTCGAGGGCCTGGACATGCTCGGCTTCGGCTTCATCGAGGTCGGCACCTTCACCGCCCACCCCCAGGGCGGCAACGACAAGCCCCGCATGTGGCGCTACCCGCAGATGCGTGCCGTGCGCAACCGCATGGGCTTCAACAACTCCGGGGCGGATGAGGCCGCCAAGCGCCTGCGGGCACTGCGCCGCACCCCTCGAGGGCGATCCATCGTCGTCGGAGCGAACATCGGCAAGACCAAGGTGACCCCGCTCGAGGAGGCGGTGGAGGACTACCGCTACTCGGCCGCGGCAGTGGCCCGCTGGGTCGACTACCTCGTCGTCAACGTCTCCAGCCCCAACACCCCCGGGCTGCGCAGCCTGCAGAGCGTTGAGACGCTGCGACCGATCCTTGAAGCGGTGCGCGAGGCCGCCGACCGCGCCGCCAGGCGCCACGTTCCGCTCCTGGTCAAGATCGCCCCGGACCTGGCTGACGAGGACATCGACGCCGTCGCCCAGATGGTCCTGGACATGGGCCTCGACGGGGTGGTGGCCACCAACACGACCATCGACCACGACCTGGGGGAGGGCGGCCTGTCCGGCGCCCCACTTCTGCCCCGCGCCCTGGAGGTCGTGCGCCGCCTGCGCCACGGGCTGGGGCAAGGGCCTACGATCATCGGCGTCGGCGGCATCTCCTCCGTCATGGATGCCGAGCTCATGCTCGACGCGGGAGCGGACCTGCTTCAGGCCTACACGGCCTTCATCTACAACGGCCCCGCCTGGCCGGGGCGCATCAACCGGGCCCTGGCCACCGGTTCCGCCGCCCGGGCGACTGCCTGA","VLYDLLYKTVLTRIDPELIHDVCLDAIEFTGKVPLVRDVVRQMWGRRPVFPVPSANQGGPFARPVPGILGLAAGMDKEGQAVEGLDMLGFGFIEVGTFTAHPQGGNDKPRMWRYPQMRAVRNRMGFNNSGADEAAKRLRALRRTPRGRSIVVGANIGKTKVTPLEEAVEDYRYSAAAVARWVDYLVVNVSSPNTPGLRSLQSVETLRPILEAVREAADRAARRHVPLLVKIAPDLADEDIDAVAQMVLDMGLDGVVATNTTIDHDLGEGGLSGAPLLPRALEVVRRLRHGLGQGPTIIGVGGISSVMDAELMLDAGADLLQAYTAFIYNGPAWPGRINRALATGSAARATA$","Dihydroorotate dehydrogenase","Cytoplasm","dihydroorotate dehydrogenase","dihydroorotate dehydrogenase ","Dihydroorotate oxidase","","Nagy M., Lacroute F., Thomas D. Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):8966-8970. PMID: 1409592","","","

InterPro
IPR001295
Domain

Dihydroorotate dehydrogenase, core
PF01180	$\"[60-345]T$	DHO_dh
PS00911	$\"[91-110]T$	DHODEHASE_1
PS00912	$\"[297-317]T$	DHODEHASE_2

InterPro
IPR005719
Family

Dihydroorotate dehydrogenase, class 2
TIGR01036	$\"[3-348]T$	pyrD_sub2: dihydroorotate oxidase

InterPro
IPR012135
Family

Dihydroorotate dehydrogenase, classes 1 and 2
PIRSF000164	$\"[61-348]T$	Dihydroorotate oxidase

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[2-341]T$	no description

noIPR
unintegrated

unintegrated
PTHR11938	$\"[1-342]T$	FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF7	$\"[1-342]T$	DIHYDROOROTATE DEHYDROGENASE

","BeTs to 22 clades of COG0167COG name: Dihydroorotate dehydrogenaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0167 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001295 (Dihydroorotate dehydrogenase) with a combined E-value of 1.2e-48. IPB001295B 89-113 IPB001295C 119-130 IPB001295D 187-196 IPB001295E 226-235 IPB001295F 251-264 IPB001295G 269-303","Residues 58-193 are 63% similar to a (DIHYDROOROTATE DEHYDROGENASE OXIDOREDUCTASE OXIDASE FLAVOPROTEIN DHODEHASE PYRIMIDINE BIOSYNTHESIS DHODASE DHOD) protein domain (PD001761) which is seen in PYRD_COREF.Residues 195-282 are 75% similar to a (DIHYDROOROTATE DEHYDROGENASE OXIDOREDUCTASE OXIDASE DHODEHASE FLAVOPROTEIN PYRIMIDINE BIOSYNTHESIS DHODASE DHOD) protein domain (PD123506) which is seen in PYRD_STRCO.","","-54% similar to PDB:1F76 ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE (E_value = 2.9E_56);-53% similar to PDB:1D3G HUMAN DIHYDROOROTATE DEHYDROGENASE COMPLEXED WITH BREQUINAR ANALOG (E_value = 2.1E_51);-53% similar to PDB:1D3H HUMAN DIHYDROOROTATE DEHYDROGENASE COMPLEXED WITH ANTIPROLIFERATIVE AGENT A771726 (E_value = 2.1E_51);-53% similar to PDB:2B0M Human dihydroorotate dehydrogenase bound to a novel inhibitor (E_value = 2.1E_51);-53% similar to PDB:2BXV DUAL BINDING MODE OF A NOVEL SERIES OF DHODH INHIBITORS (E_value = 2.1E_51);","Residues 60 to 345 (E_value = 1.7e-85) place ANA_0973 in the DHO_dh family which is described as Dihydroorotate dehydrogenase.","","dehydrogenase (pyrD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0974","1052619","1053527","909","4.98","-13.28","31975","GTGTCCTTCAACCGCGATATCCAGCTCGACCCCAACCGGGTCCAGACCCGTTCCGGCGGAGGTCGGGGCGCCGTGATCGGTGGCGGCTCGATCCTGACCGTCATCGCCGTCGTCCTCATCTCCCAGCTCACGGGAGTGGACCTGACGTCCATGCTGGGGACGCAGCAGCAGACCGGGACGACGACGTCGACGGCCTCATCGATCGACACCTCCGTGTGCACCAGCGGGGACAGTGCCAACAAGTACACCCAGTGCCGCATGGTGGCCACCGCGGAGTCCCTCGACGCGGTGTGGACCGAGCAGCTGCCTTCCCAGGCGGGGCTCAAGTACGCCAAGCCCGAGTTCGTCCTGTGGGACGGCAGCCAGATCTCCTCGGCCTGCGGTAATGCCTCCTCAGCGGTGGGTCCCTTCTACTGCTCTGGGGACCGGACCGTCTACCTGGACATGAGCTTCTTCTCCGAGATGGAGCGCTCCTTGGGGGCCGCTGACACGCCCCTGGCGGAGGAGTACATCGTGGCCCACGAGTTCGGCCACCACATCCAGCACCTGACCGGGCAGATGGCCAAGGCCGACCGCTCGGGCAGCGGTGCGACGTCGGACTCGGTGCGACTGGAGCTCCAGGCGGACTGCTACGCGGGAATCTGGGTCAACCACGCCTCCTCCACCCCAGACCCGGACACCGGCAAGCCCTTCCTCAACCGTCCCAGCAGTGAGGAGATCAAGGGCGCGCTGGGCGCGGCCGAGGCCGTGGGTGATGACCACATCCAGGAGCGGGCCAAGGGGCACGTCGACTCCGACACGTGGACCCACGGCTCCTCCGAGCAGCGCGTGCGCTGGTTCACCACCGGAATGGACTCCGGCTCGATGCAGGCCTGCAACACCTTCGCCGTCGACGCCTCCCAGCTCTGA","VSFNRDIQLDPNRVQTRSGGGRGAVIGGGSILTVIAVVLISQLTGVDLTSMLGTQQQTGTTTSTASSIDTSVCTSGDSANKYTQCRMVATAESLDAVWTEQLPSQAGLKYAKPEFVLWDGSQISSACGNASSAVGPFYCSGDRTVYLDMSFFSEMERSLGAADTPLAEEYIVAHEFGHHIQHLTGQMAKADRSGSGATSDSVRLELQADCYAGIWVNHASSTPDPDTGKPFLNRPSSEEIKGALGAAEAVGDDHIQERAKGHVDSDTWTHGSSEQRVRWFTTGMDSGSMQACNTFAVDASQL$","Metalloprotease","Periplasm, Extracellular","Predicted metalloprotease","protein of unknown function; zinc metallopeptidase putative","protein of unknown function, zinc metallopeptidase putative","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 1989. 242(2):211-214. PMID: 2914602Murphy G.J., Murphy G., Reynolds J.J. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett. 1991. 289(1):4-7. PMID: 1894005","","","

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[171-180]?$	ZINC_PROTEASE

InterPro
IPR007343
Family

Protein of unknown function, zinc metallopeptidase putative
PF04228	$\"[12-295]T$	Zn_peptidase

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

","BeTs to 4 clades of COG2321COG name: Predicted metalloproteaseFunctional Class: RThe phylogenetic pattern of COG2321 is -------cEbrh---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 412-600 are 66% similar to a (MEMBRANE METALLOPROTEASE TRANSMEMBRANE PROTEASE ZINC YPFJ METALLOPEPTIDASE PREDICTED INNER RV2575/MT2651/MB2605) protein domain (PD668707) which is seen in Q741N0_MYCPA.","","-46% similar to PDB:2FLT The X-ray structure of the cis-3-chloroacrylic acid dehalogenase cis-CaaD inactivated with (R)-Oxirane-2-carboxylate (E_value = );-46% similar to PDB:2FLZ The X-ray structure of cis-3-chloroacrylic acid dehalogenase (cis-CaaD) with a sulfate ion bound in the active site (E_value = );","Residues 351 to 634 (E_value = 2e-55) place ANA_0974 in the Zn_peptidase family which is described as Putative neutral zinc metallopeptidase.","","metalloprotease ","","1","","","Thu Aug 2 11:46:21 2007","","Thu Aug 2 11:46:21 2007","","","Thu Aug 2 11:46:21 2007","Thu Aug 2 11:46:21 2007","Thu Aug 2 11:46:21 2007","","","Thu Aug 2 11:45:04 2007","","","Sat Jul 14 23:20:27 2007","","Sat Jul 14 23:20:27 2007","","Sat Jul 14 23:20:27 2007","Sat Jul 14 23:20:27 2007","","","","","yes","","" "ANA_0975","1053720","1054229","510","8.19","1.16","17372","ATGACCAGGGCACTCATCATTGTTGAGTCCTGCTTCGGCAATACCCGGGCCATCGCCGAGGCCGTTGCCGCCGGGTTGATCGAGGGCGGCGTCGAGGCGCAGATGGTCGACGTCGCCCAGGCGCCAGAAGCTCTGCCCGAGGACCTGGATCTGCTCGTCCTGGCAGCCCCCACTCACAACCGGGGTCTGCCCACTGCGGCTACGCGGGCCAAGGCCCGTGCGCAGGCGGGGCCGGGCAACAACTCCCCGGGGATCAGCGAGTGGCTGGGAGACGCAGAGGTTCCAGCCGCTCTCAGCGTCGCCGCCTTCGACACGGTCATCTCCAAGGGCTGGCTCAGCGGCTCAGCGGCCAAGGCGATCGCCAAGACGCTACAGCGGCGTCAGGGTCGGCGGACGGTGTCGGTCAGAAGCTTCGTGGTCACGGCGAGCAAGGGCCCGCTGGCCACCGGCCAGGAGAGTGACGCCCGCAGCTGGGGACGCGAGCTCGCGGACTCGGTGAAGACCGGATAG","MTRALIIVESCFGNTRAIAEAVAAGLIEGGVEAQMVDVAQAPEALPEDLDLLVLAAPTHNRGLPTAATRAKARAQAGPGNNSPGISEWLGDAEVPAALSVAAFDTVISKGWLSGSAAKAIAKTLQRRQGRRTVSVRSFVVTASKGPLATGQESDARSWGRELADSVKTG$","Flavodoxin","Cytoplasm","flavodoxin, putative","possible flavodoxin","flavodoxin/nitric oxide synthase","","Wakabayashi S., Kimura T., Fukuyama K., Matsubara H., Rogers L.J. The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus. Biochem. J. 1989. 263(3):981-984. PMID: 2597140","","","

InterPro
IPR008254
Domain

Flavodoxin/nitric oxide synthase
PF00258	$\"[6-65]T$	Flavodoxin_1
PS50902	$\"[4-163]T$	FLAVODOXIN_LIKE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[4-63]T$	no description

","BeTs to 5 clades of COG0655COG name: Multimeric flavodoxin WrbAFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0655 is a-m---yq-dr-b-efg-s--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 158 (E_value = 0.0013) place ANA_0975 in the Flavodoxin_1 family which is described as Flavodoxin.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0976","1054288","1054647","360","8.94","4.03","12445","ATGACAGCAACGAACCGCGACAAGTCGTCCCGGCAGCAGCTGAGCGGACGAGACATCGCCGGAGCATGCCTGGCCGTCTGCGGTCTCCTCATCATCATCTGGGGAGCGACACTCGAGCCCGTCAACGTCACTGACCCAGGCTTCATGTCCTTCGCCGTCAGTGGGCTGGTGATCGTTGGAGCCGGAGCATGCCTGGCGACGGCACTTCCTCGCGCTGCTCGTGTCACGCTCATCTGGCTGGCAACACTGGCGGCAATGCACTATCTGTTCATCATCGGCATGGCAGTCATCATGTCCCTCATGAGCTGTGTGGTGGTCGCTGGGATCGCCGCCTGGCTGTCCATCAGAATCTTGAGATGA","MTATNRDKSSRQQLSGRDIAGACLAVCGLLIIIWGATLEPVNVTDPGFMSFAVSGLVIVGAGACLATALPRAARVTLIWLATLAAMHYLFIIGMAVIMSLMSCVVVAGIAAWLSIRILR$","Hypothetical protein","Membrane, Cytoplasm","benzoate transport protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[20-38]?$ $\"[48-68]?$ $\"[73-91]?$ $\"[95-115]?$	transmembrane_regions

InterPro
IPR001045
Family

Spermine synthase
PTHR11558	$\"[14-504]T$	SPERMIDINE/SPERMINE SYNTHASE
PF01564	$\"[230-454]T$	Spermine_synth
PS51006	$\"[212-500]T$	SPERMIDINE_SYNTHASE_2
PS01330	$\"[288-301]?$	SPERMIDINE_SYNTHASE_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[263-452]T$	no description
PTHR11558:SF2	$\"[14-504]T$	SPERMIDINE SYNTHASE, BACTERIA
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[15-37]?$ $\"[43-65]?$ $\"[74-96]?$ $\"[106-126]?$ $\"[141-161]?$ $\"[167-189]?$ $\"[198-216]?$	transmembrane_regions

","BeTs to 13 clades of COG0421COG name: Spermidine synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0421 is a-mpkzyqvdr-b-ef--snuj----Number of proteins in this genome belonging to this COG is 2","***** IPB001045 (Spermine synthase) with a combined E-value of 1.5e-57. IPB001045A 226-274 IPB001045B 278-329 IPB001045C 338-355 IPB001045D 361-385 IPB001045E 433-447","Residues 80-172 are 67% similar to a (SPERMIDINE BIOSYNTHESIS SYNTHASE TRANSFERASE AMINOPROPYLTRANSFERASE PROBABLE PUTRESCINE POLYAMINE SPDSY TRANSMEMBRANE) protein domain (PD338256) which is seen in SPE1_LEPIN.Residues 230-446 are 64% similar to a (SPERMIDINE TRANSFERASE BIOSYNTHESIS SYNTHASE PUTRESCINE AMINOPROPYLTRANSFERASE SPDSY POLYAMINE METHYLTRANSFERASE PROBABLE) protein domain (PD002785) which is seen in SPE2_RALSO.","","-46% similar to PDB:1UIR Crystal Structure of Polyamine Aminopropyltransfease from Thermus thermophilus (E_value = 4.6E_16);-46% similar to PDB:1IY9 Crystal structure of spermidine synthase (E_value = 2.5E_14);-39% similar to PDB:1INL Crystal Structure of Spermidine Synthase from Thermotoga Maritima (E_value = 3.4E_11);-39% similar to PDB:1JQ3 Crystal Structure of Spermidine Synthase in Complex with Transition State Analogue AdoDATO (E_value = 3.4E_11);-45% similar to PDB:2HTE The crystal structure of spermidine synthase from p. falciparum in complex with 5'-methylthioadenosine (E_value = 8.4E_10);","Residues 199 to 454 (E_value = 2.5e-49) place ANA_0977 in the Spermine_synth family which is described as Spermine/spermidine synthase.","","synthase (SPDSY)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0978","1056604","1056281","324","4.47","-8.34","11469","GTGGGGGCGGAGGCGTCGGAAAATGACCTGGAGCCCACGGACTCAATCCCCTCGACGGTCACACACGAAGGAGAAGACATGTTGCTCATGACCATCGCTCACCACTCATCGGTCGACCTCAACTGGCAGTCGCTGCTGAGCACCGTCGTCTACGCGGTGCTCGGAGTGGTGCTGCTCATGGTGTTCGCGCTGCTCGTCAACCGCATCTTCCGCCTCGACCTCAGACGCGAGCTCATCGAGGACCAGAACATCGGCCTGGGGGTCGCCTTCGCCGGCACGGCGCTGGCCATCGCCATCATCATCGCCGCCACCATCCTGAGCTGA","VGAEASENDLEPTDSIPSTVTHEGEDMLLMTIAHHSSVDLNWQSLLSTVVYAVLGVVLLMVFALLVNRIFRLDLRRELIEDQNIGLGVAFAGTALAIAIIIAATILS$","Hypothetical protein","Membrane, Cytoplasm","Domain of Unknown Function (DUF350) family","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF350","","","","","

InterPro
IPR007140
Repeat

Protein of unknown function DUF350
PF03994	$\"[43-106]T$	DUF350

noIPR
unintegrated

unintegrated
tmhmm	$\"[45-65]?$ $\"[86-106]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 43 to 106 (E_value = 9.9e-10) place ANA_0978 in the DUF350 family which is described as Domain of Unknown Function (DUF350).","","of Unknown Function (DUF350) family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0979","1057693","1057346","348","7.02","0.07","11980","GTGAGTGCGGTGAGCCTGTGTTCCGTCAGCTACAAGATCAGTGGCGCCGAGCCGCATGCGCTCAACGACCTGTCCACCGTGGAGTCGATTCTCCTTGGTGCCGCCCAGACGGCGGGACTGACTGCCGTCTCCAGTGCTCACCACCGCTTCGAGCCCCAGGGACTGAGCGCCGTCATCATTCTGTCCGAGTCGCATATCGCCGCCCACACCTGGCCCGAGTCCGGTACCGGCTACGTGACGCTCACCAGCTGCCGCACACTGACCCCCGCCCAGCTCGAGTCCGTGGGGGAGCTGGTGCGCAAGCGCCTGCGGGCCCAGCAGGTGACCAGCTCGGGGATCACACTGTGA","VSAVSLCSVSYKISGAEPHALNDLSTVESILLGAAQTAGLTAVSSAHHRFEPQGLSAVIILSESHIAAHTWPESGTGYVTLTSCRTLTPAQLESVGELVRKRLRAQQVTSSGITL$","S-adenosylmethionine decarboxylase","Periplasm, Membrane, Cytoplasm, Extracellular","4.1.1.50","hypothetical protein predicted by Glimmer/Critica","S-adenosylmethionine decarboxylase related","","Ekstrom J.L., Mathews I.I., Stanley B.A., Pegg A.E., Ealick S.E. The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Structure 1999. 7(5):583-595. PMID: 10378277","","","

InterPro
IPR001985
Family

S-adenosylmethionine decarboxylase
G3DSA:3.60.90.10	$\"[11-109]T$	no description

InterPro
IPR003826
Family

S-adenosylmethionine decarboxylase related
PF02675	$\"[19-105]T$	AdoMet_dc

","BeTs to 10 clades of COG1586COG name: S-adenosylmethionine decarboxylaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1586 is a-mpkz-qv---b-ef--s-------Number of proteins in this genome belonging to this COG is 1","***** IPB003826 (S-adenosylmethionine decarboxylase related) with a combined E-value of 9.5e-11. IPB003826 54-93","Residues 12-84 are similar to a (DECARBOXYLASE S-ADENOSYLMETHIONINE CHAIN PROENZYME SAMDC ALPHA CONTAINS: BETA ADOMETDC LYASE) protein domain (PD012690) which is seen in SPEH_THETN.","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 75 (E_value = 8.5e-20) place ANA_0979 in the AdoMet_dc family which is described as S-adenosylmethionine decarboxylase.Residues 19 to 105 (E_value = 7.4e-09) place ANA_0979 in the AdoMet_dc family which is described as S-adenosylmethionine decarboxylase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0980","1058534","1057785","750","6.78","-0.76","26987","GTGAACGGCACGCGAGGCAACCTGCAGGTCGGCGACCTGCTCCAGGGCAGTGCAGGCGCCCTGTCAGTCACAGGTTGCCTGCTCTTCAAGGAATGGGACTCCCAGGACCACTGCTTCTACTACTGGGAGGAGTGGCAGCTCATCGGGGCCAGCAACTCCGACACCTGGGTCGAGGTCGACCACGATCCCGGCGAGGTCCTCTTCTACGAACCCGTTCGTCTCCAGGAGAAGATCGAGCCGTGGGCCCTGACCGTCGGTCAGACGATGCAGATGACGATCAACGGCGTCCTGCACCGCGGCATGGTTGAGGAGGTGACCACCGGAACGCTCGAGAACGTCATCGGTTCCCCGGTGTGCCCACTCAACATCGGCGAGACCATGACCTACGCCGAGGTACGGCTGACGGACCCGGCCGGCGTGACCAGCAGGCTGACCATCGACAGCCACCGTTTCCGTGACCTCCTGGCATACCGCAAAACCTCCCTGTCCACTGCGCAGCAGAAGCAGCTCTTCGGGCGGGTCCTGTACAACCGCCGATCCGTCACCGGAAGAACCGGCCGGAACATCGGCTGCGCGGTCGTCGCCGCCCTCGTCAGTATCGTGCTCGTCGGCGGGCTGTTCTCCGCGTGCTCCAACCTCAGCCGCACCAGTGGCGACGCCGACCCCACCAGCACCTCGCACTCGGGCTCCTCACGGAGCTACCGCCACCGCCCGGTCTACGGAGGCGGCGGAGGCGGAGTCGGCAAGTAG","VNGTRGNLQVGDLLQGSAGALSVTGCLLFKEWDSQDHCFYYWEEWQLIGASNSDTWVEVDHDPGEVLFYEPVRLQEKIEPWALTVGQTMQMTINGVLHRGMVEEVTTGTLENVIGSPVCPLNIGETMTYAEVRLTDPAGVTSRLTIDSHRFRDLLAYRKTSLSTAQQKQLFGRVLYNRRSVTGRTGRNIGCAVVAALVSIVLVGGLFSACSNLSRTSGDADPTSTSHSGSSRSYRHRPVYGGGGGGVGK$","Hypothetical protein","Membrane, Periplasm","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[189-209]?$	transmembrane_regions

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PF00376	$\"[69-105]T$	MerR
SM00422	$\"[68-136]T$	HTH_MERR
PS50937	$\"[67-135]T$	HTH_MERR_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[68-196]T$	no description

","BeTs to 10 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 8","***** IPB000551 (Bacterial regulatory protein, MerR family) with a combined E-value of 4e-11. IPB000551 68-108","Residues 68-179 are 51% similar to a (TRANSCRIPTIONAL DNA-BINDING REGULATOR) protein domain (PD822168) which is seen in Q9KY77_STRCO.Residues 73-133 are 62% similar to a (DNA-BINDING TRANSCRIPTIONAL REGULATOR MERR FAMILY REGULATOR REGULATORY PLASMID TRANSCRIPTION ACTIVATOR) protein domain (PD548366) which is seen in Q82M74_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 69 to 105 (E_value = 4.4e-10) place ANA_0981 in the MerR family which is described as MerR family regulatory protein.","","MerR-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0982","1060036","1059626","411","4.59","-10.59","15219","ATGCGGATCCGAGACAACTACCCGATCGTTGTCACCGACCGGAAGGACGAGGCGCGAGACTTCTGGCAGCGATTCCTTGGCTTCCGTCCTGTTTTCGACAGTTCCTGGTTCACCTTGATGACGGATGAGGGCAGCGGATCATCGATTGCCTTCATGACGCCGGACCACCCCTCTGCTCCTCCAGGGCCCGATGCCTTCGCCGGAACCGGCGCCTGCTTCGAACTGGAGGTCGACGACGCAGCAGCGGCTCATGCCGAGCTGACGGGCAGAGGACTGGCGGCGACGTACCCGCTCACCGACGAGCCCTTCGGCCAGCGCCGGTTCGGGTTCGCCGACCCCAGCGGCCTGTGGATCGACGTCGTCGAGCAGATTGAATCGGAGGCCGGCTACTGGGATCGGTACATGCGGTGA","MRIRDNYPIVVTDRKDEARDFWQRFLGFRPVFDSSWFTLMTDEGSGSSIAFMTPDHPSAPPGPDAFAGTGACFELEVDDAAAAHAELTGRGLAATYPLTDEPFGQRRFGFADPSGLWIDVVEQIESEAGYWDRYMR$","Glyoxalase/bleomycin resistance protein/dioxygenase","Cytoplasm","glyoxalase family protein superfamily","hypothetical protein","Glyoxalase/bleomycin resistance protein/dioxygenase","","Kim N.S., Umezawa Y., Ohmura S., Kato S. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 1993. 268(15):11217-11221. PMID: 7684374","","","

InterPro
IPR004360
Domain

Glyoxalase/bleomycin resistance protein/dioxygenase
PF00903	$\"[4-120]T$	Glyoxalase

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.10	$\"[1-125]T$	no description

","BeTs to 6 clades of COG0346COG name: Lactoylglutathione lyase and related lyasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0346 is aom-kzy--drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","Residues 1-130 are 51% similar to a (DR0670) protein domain (PD308152) which is seen in Q9RWJ8_DEIRA.Residues 7-130 are 47% similar to a () protein domain (PDA0U4E4) which is seen in Q7VHC4_HELHP.Residues 58-116 are 59% similar to a () protein domain (PD751232) which is seen in Q939I7_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 120 (E_value = 1.5e-08) place ANA_0982 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.","","family protein superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0983","1060130","1061149","1020","5.40","-10.21","37116","ATGGCAGGAACGAGAGCAGCCCAGCGCAGGGCGACGCAGGCGGCACTTATCACCGTGGCTCGGCAGCGCTTCGCCTCCGAGGGATACAGCGCGGTGCGGCTAAGCGACGTCGTCGACGCGCTCGGAATGACCAAGGGCGCGCTCTACCATCAGTTCGCTGGCAAGAAGGATCTCTTCCTCGCAGTCCTTCGGCAGGTGCAGCAGGAGGTCGCTGACCGGGTTCAGGACGCCGCTCGGCCGTGCGCGGATCCCTGGAAGGAGCTCGTCGCAGGCTGCGAGGCGTTTCTTACCTCCTACAGTGACCCCGAGATCCGGCAGATCATGCTCATTGACGCACCGATAGTGCTGGGTTGGCGCGAATGGAAGGAGATGGACGAAGCATGCTCCGAAAGGCTCCTCACGGAGGTGCTGACCAGCCTCATGGAGGACGGCATTCTCGTCTCCCGGCCGGTGGCACCCTTGGTTCGTCTGCTATCCGGTGCAATGAACGAGGCCGCGTTGTGGCTTGCCGAGACCGAGTCACCAACGGCACTGAAAGACACCATGGACGCATTGCTCTGCATGCTCGGTTCACTGCGAGCCGATGGGACCGCACCGACGGATGGGGCGAGTAGCGTCGCTGGTATGAGTCAACGCCTTCCTTCATCTGCCAACGTGGTTCTCAAAGGCATCCGTGAGGAGCCCAGCGCCGAGGACGGAGCACGGGTCCTGGTGGACCGGCTCTGGCCCCGTGGCGTGTCCAAGGAGCGCGCCGCTCTCGACGAGTGGGCCAAGGACGCCGCCCCCACCACCGAGCTGCGGCGGGCCTTCCACAGCGGGGACCTGCCCTGGCCCCAGTTCGTCGAGGCCTACCGAGCCGAGCTCACCGAGAGGCCCGAGGCGGTCACCGCCGTCGAGCACCTGCGTCACGAGGCCCTTACGGGGCGCGTGACACTCCTGTTCGCCGGCCACGACCACGTCCACTGCCACGCGCGTGTCCTGCGAGAGGCGGTTCTCGGCGTCGAGGAGGACCTGTCCTGA","MAGTRAAQRRATQAALITVARQRFASEGYSAVRLSDVVDALGMTKGALYHQFAGKKDLFLAVLRQVQQEVADRVQDAARPCADPWKELVAGCEAFLTSYSDPEIRQIMLIDAPIVLGWREWKEMDEACSERLLTEVLTSLMEDGILVSRPVAPLVRLLSGAMNEAALWLAETESPTALKDTMDALLCMLGSLRADGTAPTDGASSVAGMSQRLPSSANVVLKGIREEPSAEDGARVLVDRLWPRGVSKERAALDEWAKDAAPTTELRRAFHSGDLPWPQFVEAYRAELTERPEAVTAVEHLRHEALTGRVTLLFAGHDHVHCHARVLREAVLGVEEDLS$","Transcriptional regulator, TetR family","Cytoplasm","probable transcription regulator Rv0078","transcriptional regulator; TetR family","protein of unknown function DUF488","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[16-29]T$ $\"[37-60]T$	HTHTETR
PF00440	$\"[16-62]T$	TetR_N
PS50977	$\"[10-70]T$	HTH_TETR_2

InterPro
IPR007438
Family

Protein of unknown function DUF488
PF04343	$\"[218-332]T$	DUF488

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[3-62]T$	no description

noIPR
unintegrated

unintegrated
PD031313	$\"[219-329]T$	Q746S6_GEOSL_Q746S6;

InterPro
IPR002744
Domain

Protein of unknown function DUF59
PD005595	$\"[36-115]T$	Q7U009_MYCBO_Q7U009;
PF01883	$\"[32-105]T$	DUF59

","BeTs to 11 clades of COG2151COG name: Predicted metal-sulfur cluster biosynthetic enzymeFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2151 is --mpkz--vdrlb-e---s--j----Number of proteins in this genome belonging to this COG is 1","***** IPB002744 (Protein of unknown function DUF59) with a combined E-value of 3.7e-36. IPB002744A 36-58 IPB002744B 69-94 IPB002744C 106-130","Residues 36-115 are 83% similar to a (MRP ATP-BINDING HOMOLOG ACID PHENYLACETIC DEGRADATION PAAD PROTEIN COMPLEX RING) protein domain (PD005595) which is seen in Q7U009_MYCBO.","","-66% similar to PDB:1UWD CONSERVED HYPOTHETICAL PROTEIN TM0487 FROM THERMOTOGA MARITIMA (E_value = 2.0E_14);-66% similar to PDB:1WCJ CONSERVED HYPOTHETICAL PROTEIN TM0487 FROM THERMOTOGA MARITIMA (E_value = 2.0E_14);-62% similar to PDB:2CU6 Crystal Structure Of The dTDP-4-keto-L-rhamnose reductase-related Protein From Thermus Thermophilus HB8 (E_value = 7.0E_12);-49% similar to PDB:1IWG Crystal structure of Bacterial Multidrug Efflux transporter AcrB (E_value = 7.0E_12);-49% similar to PDB:1OY6 Structural Basis of the Multiple Binding Capacity of the AcrB Multidrug Efflux Pump (E_value = 7.0E_12);","Residues 32 to 105 (E_value = 8.9e-29) place ANA_0984 in the DUF59 family which is described as Domain of unknown function DUF59.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0985","1062171","1061695","477","4.70","-12.92","16684","ATGAACGAACTCGACCAGCTCTACCAGCAAGTCATCCTCGACCACTCCCGGGAGCGCCACGGCTCCGGCGCCCTCGATGCCCCGGACGCCACCAGCCACCAGGTCAACCCCACCTGTGGTGACGACGTGACCCTGGGGGTGCGCGTCAAGGACGGCAAGATCGAGGCCATCGGCTGGGAGGGGGACGGCTGCTCCATCTCCCAGGCCTCCATCTCCGTCATGCACGACCTCGTCAACGGCGCCGACCTGGCCACCGTGGCCCGCCTCGAGGCGGACTTCGATACCCTCATGCACTCGCGCGGCAAGGGCGTCGACGACGCCGTCCTGGATGACCTGGAGGACGGGGCCGCCTTCGAGGGCGTCTCGAAGTACCCCAACCGCGTCAAGTGCGCCCTGCTGGGGTGGATGGCCCTCAAGGACGCCCTGGCCAAGTCCGGCGTCGCCCTGCCCGCCGTTGAGCCGAACGGCGCCGAGTAG","MNELDQLYQQVILDHSRERHGSGALDAPDATSHQVNPTCGDDVTLGVRVKDGKIEAIGWEGDGCSISQASISVMHDLVNGADLATVARLEADFDTLMHSRGKGVDDAVLDDLEDGAAFEGVSKYPNRVKCALLGWMALKDALAKSGVALPAVEPNGAE$","SUF system FeS assembly protein, NifU family","Cytoplasm","SUF system FeS assembly protein, NifU family","K04488 nitrogen fixation protein NifU and related proteins","SUF system FeS assembly protein, NifU family","","","","","

InterPro
IPR002871
Domain

Nitrogen-fixing NifU-like, N-terminal
PF01592	$\"[7-131]T$	NifU_N

InterPro
IPR011341
Family

SUF system FeS assembly protein
TIGR01994	$\"[4-143]T$	SUF_scaf_2: SUF system FeS assembly protein

noIPR
unintegrated

unintegrated
G3DSA:3.90.1010.10	$\"[6-142]T$	no description
PTHR10093	$\"[5-144]T$	IRON-SULFUR CLUSTER ASSEMBLY ENZYME (NIFU HOMOLOG)

","BeTs to 12 clades of COG0822COG name: NifU homologs involved in Fe-S cluster formationFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0822 is ao----yqv-rlb-efgh-nujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002871 (Nitrogen-fixing NifU-like, N-terminal) with a combined E-value of 1.5e-28. IPB002871A 8-22 IPB002871B 32-47 IPB002871C 56-86 IPB002871D 123-146","Residues 7-78 are 75% similar to a (NIFU NITROGEN FIXATION NIFU-LIKE CLUSTER FAMILY HOMOLOG ISCU NIFU-RELATED FE-S) protein domain (PD002743) which is seen in Q6AFL5_BBBBB.Residues 89-142 are 70% similar to a (NIFU NITROGEN FIXATION NIFU-LIKE FAMILY INVOLVED FE-S FORMATION CLUSTER HOMOLOG) protein domain (PD639455) which is seen in Q8G5Y3_BIFLO.","","-58% similar to PDB:1XJS Solution structure of Iron-Sulfur cluster assembly protein IscU from Bacillus subtilis, with Zinc bound at the active site. Northeast Structural Genomics Consortium Target SR17 (E_value = 9.2E_24);-58% similar to PDB:2AZH Solution structure of iron-sulfur cluster assembly protein SUFU from Bacillus subtilis, with zinc bound at the active site. Northeast Structural Genomics Consortium target SR17 (E_value = 9.2E_24);-55% similar to PDB:1SU0 Crystal structure of a hypothetical protein at 2.3 A resolution (E_value = 1.0E_22);","Residues 7 to 131 (E_value = 2.4e-14) place ANA_0985 in the NifU_N family which is described as NifU-like N terminal domain.","","system FeS assembly protein, NifU family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0986","1063526","1062174","1353","5.63","-11.74","47181","ATGACCCAGTCCACCGCCCCGCTCACCGGGGCGCCTTCGGCCGGCGCACTCAACGTGGAGGAGATCGCCGCGATCCGCGCCGACTTCCCCTACCTGGAGCGGCCCGCCCGCAACGGTCAGGCGCTGGCCTACCTGGACTGGGCGGCCACGAGCCAGAAACCCGCCGGCGTCATCACCACGGAGGCCGACTTCTACCGTATGTCCAACGGCGCGGCGGGACGCTCGACCTACCAGCTCGCCGATGAGGCCACCGCCACCTTTGAGGACGCTCGCGACGCCGTCGCCGCCTTCGTCGGGGCGCGCGGCAGTGAGCTCGTCTTCACCAAGAACGCCACCGAGGCCATCAACCTCGTGGCTCTGGCCATCGGGCACGCCAGCCAGGGCCGGTCGGCGGCCCGCGGTGGAGGGCCCGCCGCGGCCGATGACCCGGCTCGGCGCCTCATCATCGGGCAGGGCGACGAGGTCGTCGTCACCCGAGCTGAGCACCACGCCAACCTCGTGCCCTGGCAGGAGCTGTGCGCCCGCACCGGCGCCACCCTGCGCTGGCTGGACCTGACCGAGGACGGGCGCATCGATGCCGCCACCCTGGACGTCATCACCGAGCGAACCCGCGTCCTGGCCCTGACCCATGCCTCCAACGTCACCGGTGCGATCAGCCCGCTCGACCTCATCCTCCCGCGCGCCCAGCAGGCCGGCGCGCTCGTTGTCCTGGACACCTGCCAGTCCGCTGCCCACCTGCCGCTGGACTTCGGCGCCCTGAAGACCGCCGGCGTGGACGCCATGGCGCTCTCCAGCCACAAGATGCTCGGCCCCACCGGCATCGGCGCGCTCGTGGCCACCGAGGAGCTTCTGGCGGCGATGCCACCAGTGCTCACCGGTGGCTCCATGATCGAGATCGTCACCATGGAGTCGTCGACCTTCATGAGCGGCCCGCCCCGTTTCGAGGCCGGCAGCCAGCCGCTGGCGCAGGCCGCGGGATGGCGCACCGCCGTGGAGTACCTGGCCCAGATCGGCCTGGACCGGCTCCACGCCACCGAGCAGGCCCTGACCCAGCAGGTGCTCGAGGGCCTGGCCCAGGTCCCCGGGCTGCGCCTGGTCGGCCCGGCCGACACGACCGACCGCCTGGGCGTGGTCGCCTTCTCCATCGAGGGAGTCCACCCTCACGACGTCGGCCAGGTCCTCGACGCCGCCGGCGTCGCCGTGCGCACCGGCCACCACTGCGCCCAGCCCATCCACCAGCACTTCGGCATCCACGCCTCCTCGCGCCTGTCCTTCGGGGCCTGCTCCACGCCCGAGGAGGTGGACCGCTTCCTGTCCGCCATCGCCGACGTCCGGCGCTACTTCCAGAGGTGA","MTQSTAPLTGAPSAGALNVEEIAAIRADFPYLERPARNGQALAYLDWAATSQKPAGVITTEADFYRMSNGAAGRSTYQLADEATATFEDARDAVAAFVGARGSELVFTKNATEAINLVALAIGHASQGRSAARGGGPAAADDPARRLIIGQGDEVVVTRAEHHANLVPWQELCARTGATLRWLDLTEDGRIDAATLDVITERTRVLALTHASNVTGAISPLDLILPRAQQAGALVVLDTCQSAAHLPLDFGALKTAGVDAMALSSHKMLGPTGIGALVATEELLAAMPPVLTGGSMIEIVTMESSTFMSGPPRFEAGSQPLAQAAGWRTAVEYLAQIGLDRLHATEQALTQQVLEGLAQVPGLRLVGPADTTDRLGVVAFSIEGVHPHDVGQVLDAAGVAVRTGHHCAQPIHQHFGIHASSRLSFGACSTPEEVDRFLSAIADVRRYFQR$","Cysteine desulfurase, SufS subfamily","Cytoplasm","aminotransferase-like protein Cg1761","putative cysteine desulfurase ","cysteine desulfurase, SufS subfamily","","Ouzounis C., Sander C. Homology of the NifS family of proteins to a new class of pyridoxal phosphate-dependent enzymes. FEBS Lett. 1993. 322(2):159-164. PMID: 8482384","","","

InterPro
IPR000192
Family

Aminotransferase, class V
PF00266	$\"[43-437]T$	Aminotran_5
PS00595	$\"[258-277]?$	AA_TRANSFER_CLASS_5

InterPro
IPR010970
Family

Cysteine desulphurases, SufS
TIGR01979	$\"[23-449]T$	sufS: cysteine desulfurases, SufS subfamily

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[57-337]T$	no description

noIPR
unintegrated

unintegrated
PTHR11601	$\"[42-128]T$ $\"[152-450]T$	CYSTEINE DESULFURYLASE

","BeTs to 19 clades of COG0520COG name: Selenocysteine lyaseFunctional Class: EThe phylogenetic pattern of COG0520 is --t---vcEbrhujgpolin-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 52-113 are 61% similar to a (CYSTEINE TRANSFERASE AMINOTRANSFERASE DESULFURASE LYASE PYRIDOXAL NIFS PHOSPHATE 4.4.1.- PROBABLE) protein domain (PD351786) which is seen in CSD_MYCTU.Residues 117-185 are 60% similar to a (AMINOTRANFERASE DESULFURASE CYSTEINE NIFS-LIKE) protein domain (PD892054) which is seen in Q6AFL6_BBBBB.Residues 167-362 are 49% similar to a (AMINOTRANSFERASE TRANSFERASE NIFS-LIKE DUPR11.6 Y71H2B.5 AMINOTRANSFERASE NIFS_2 SMC00277) protein domain (PD328533) which is seen in Q7VFD8_HELHP.Residues 169-420 are 45% similar to a (SULFURASE COFACTOR MOLYBDENUM P0623F08.34 OJ1323_A06.1 AT4G37100 C7A10.260 ARABIDOPSIS HXB FLJ20733) protein domain (PD278490) which is seen in Q826J0_STRAW.Residues 258-307 are 70% similar to a (CYSTEINE TRANSFERASE AMINOTRANSFERASE DESULFURASE LYASE PYRIDOXAL PHOSPHATE NIFS PROBABLE 4.4.1.-) protein domain (PD558816) which is seen in Q8FT87_COREF.Residues 309-368 are 70% similar to a (LYASE TRANSFERASE AMINOTRANSFERASE CYSTEINE DESULFURASE PROBABLE SELENOCYSTEINE PYRIDOXAL PHOSPHATE CLASS) protein domain (PD186234) which is seen in Q829T0_STRAW.Residues 370-439 are similar to a (AMINOTRANSFERASE TRANSFERASE LYASE CYSTEINE DESULFURASE SELENOCYSTEINE PROBABLE PYRIDOXAL PHOSPHATE CLASS) protein domain (PD820769) which is seen in Q8G5Y2_BIFLO.","","-56% similar to PDB:1T3I Structure of slr0077/SufS, the Essential Cysteine Desulfurase from Synechocystis PCC 6803 (E_value = 6.6E_83);-56% similar to PDB:1I29 CRYSTAL STRUCTURE OF CSDB COMPLEXED WITH L-PROPARGYLGLYCINE (E_value = 1.6E_81);-56% similar to PDB:1JF9 Crystal Structure of selenocysteine lyase (E_value = 1.6E_81);-56% similar to PDB:1KMJ E. coli NifS/CsdB protein at 2.0A with the cysteine persulfide intermediate (residue CSS). (E_value = 1.6E_81);-56% similar to PDB:1KMK E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ). (E_value = 1.6E_81);","Residues 56 to 450 (E_value = 3.1e-152) place ANA_0986 in the Aminotran_5 family which is described as Aminotransferase class-V.","","protein Cg1761","","1","","","Thu Aug 2 11:54:15 2007","","Thu Aug 2 11:54:15 2007","","","Thu Aug 2 11:54:15 2007","Thu Aug 2 11:54:15 2007","Thu Aug 2 11:54:15 2007","","","Thu Aug 2 11:54:15 2007","","","Thu Aug 2 11:54:15 2007","Thu Aug 2 11:54:15 2007","Thu Aug 2 11:54:15 2007","","Thu Aug 2 11:54:15 2007","Thu Aug 2 11:54:15 2007","","","","","yes","","" "ANA_0987","1064436","1063687","750","5.19","-10.33","27399","ATGAGCACTCTGCAGATCAAGAACCTCCACGTCCAGGTCGCCACCAACGACGGCCCCAAGCCCATCCTCAAGGGCGTGGACCTGACCATCGACTCCAACCAGGTCCACGCCATCATGGGCCCCAACGGCTCGGGCAAGTCCACCCTGGCCTACTCCATCGCCGGTCACCCCGACTACGAGGTCACCGACGGCGAGGTCCTCCTCGACGGCGTCGACCTGCTGGAGATGAGCGTGGACGAGCGCGCCCGGGCCGGCCTCTTCCTGGCCATGCAGTACCCCGTCGAGGTCCCCGGCGTCACCGTGGCCAACTTCCTGCGCACGGCCAAGACCGCCATCGACGGCCAGGCTCCCAAGGTGCGCCAGTGGGTCGGCGAGGTCAACCAGGCCATGAAGAACCTGCGGATGGACCCCGCTTTCTCCCAGCGCGACGTCAACGCCGGCTTCTCCGGCGGTGAGAAGAAGCGCTTCGAGATCCTCCAGATGGAGCTGCTCCGTCCCCGCTTCGCCGTCCTGGACGAGACCGACTCCGGCCTGGACGTCGACGCCCTGCGCATCGTCTCCGAGGGCGTCAACCGCCTCCACGACGAGTCTGACGCCGGCTTCCTCCTCATCACCCACTACACGCGCATCCTGCGCTACATCAAGCCCGACCACGTCCACGTCTTCGTCGACGGGCGCGTGGCCGAGGCCGGCGGCCCTGACCTGGCCGACCGCCTCGAGGAAGAGGGCTACGACCGCTACCTGGCCTGA","MSTLQIKNLHVQVATNDGPKPILKGVDLTIDSNQVHAIMGPNGSGKSTLAYSIAGHPDYEVTDGEVLLDGVDLLEMSVDERARAGLFLAMQYPVEVPGVTVANFLRTAKTAIDGQAPKVRQWVGEVNQAMKNLRMDPAFSQRDVNAGFSGGEKKRFEILQMELLRPRFAVLDETDSGLDVDALRIVSEGVNRLHDESDAGFLLITHYTRILRYIKPDHVHVFVDGRVAEAGGPDLADRLEEEGYDRYLA$","FeS assembly ATPase SufC","Cytoplasm, Membrane","FeS assembly ATPase SufC","K09013 Fe-S cluster assembly ATP-binding protein","FeS assembly ATPase SufC","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[33-225]T$	ABC_tran
PS50893	$\"[4-249]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[32-226]T$	AAA

InterPro
IPR010230
Family

FeS assembly ATPase SufC
PTHR19222:SF6	$\"[4-233]T$	ABC TRANSPORTER
TIGR01978	$\"[4-247]T$	sufC: FeS assembly ATPase SufC

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-234]T$	no description
PTHR19222	$\"[4-233]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 16 clades of COG0396COG name: Iron-regulated ABC transporter ATPase subunit SufCFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0396 is aompkz--vdrlbce---s--j-it-Number of proteins in this genome belonging to this COG is 1","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.2e-15. IPB005074C 22-69 IPB005074D 136-179***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1e-13. IPB013563A 22-56 IPB013563C 145-172***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 5.5e-11. IPB010509B 33-58 IPB010509D 143-187","Residues 23-206 are 49% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 23-62 are 92% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q6A7H4_PROAC.Residues 89-234 are 48% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K5M4) which is seen in Q897H9_CLOTE.Residues 89-161 are similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER ATP-DEPENDENT PROBABLE ATPASE SUFC SUBUNIT YCF16) protein domain (PD374973) which is seen in Q9XAD4_STRCO.Residues 165-206 are 88% similar to a (ATP-BINDING TRANSPORTER ABC PROBABLE ATP-DEPENDENT TRANSPORTER SUFC ATPASE COMPONENT SUBUNIT) protein domain (PD195750) which is seen in Q83HR9_TROW8.Residues 207-245 are 92% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER ATP-DEPENDENT PROBABLE ATPASE SUFC SUBUNIT COMPONENT) protein domain (PD005991) which is seen in Q6AF29_BBBBB.","","-69% similar to PDB:2D2E Crystal structure of atypical cytoplasmic ABC-ATPase SufC from Thermus thermophilus HB8 (E_value = 5.8E_63);-69% similar to PDB:2D2F Crystal structure of atypical cytoplasmic ABC-ATPase SufC from Thermus thermophilus HB8 (E_value = 5.8E_63);-64% similar to PDB:2D3W Crystal Structure of Escherichia coli SufC, an ATPase compenent of the SUF iron-sulfur cluster assembly machinery (E_value = 9.0E_56);-43% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 8.0E_12);-43% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 8.0E_12);","Residues 33 to 225 (E_value = 6.8e-31) place ANA_0987 in the ABC_tran family which is described as ABC transporter.","","assembly ATPase SufC (sufC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0989","1065767","1064505","1263","5.01","-23.47","44741","ATGCCTGAACTCTCGACCGACCACTCGAGCGCCACGCTCGACGGCGCCCACTCCCACGGCGGGCCGCGCTACGTCTCCTCGCGCGCCGACCGCCCCACCTCCTTCGACCCCGCCGACATCCCGGTGCCGCGCGGCCGTGAGGAGGAGTGGCGCTTCACGCCGATGAAGCGCTTCGCCCCGCTGTTCGACCTCGACGCCATCCGCGCGGCCACCGCCGGCCAGAGCGATGCCGGCGCCGTCCGTATTGAGGCGGACCTGCCCGACGGCGTGAGCCTGGAGACGGTCGCGCGCAGCGACGCCCGCATCGGCACCGTGGGTGCCCCGGTCGACCGCACCGGCGTCACCGCCTGGAACGGCACAGAGACCGCCACCGTGCTCACGCTGGAGCCCGGCGCCCAGCTGGAGCGGGCCGCCCGACTGAACATCATTGGCCAGGACCCACAGCTCGCCCGCCCCACCGCCCAGCACATTCTCGTCGCTGCCGAGGACGGTTCCAAGGGAACCGTCGTCCTGGACCACACCGGCACCGCCGCCCTGACCCAGGGTGTCGAGGTGACGGTCGCCGACGGCGCCGAGCTCACCCTGGTGACCGTCCAGGGCTGGGAGGACGGGGCCGTCCATGCCTCCAACCACCGGGTCAAGGTCTGTGACCGCGGCGTCCTCAAGCACGTCGTCGTCAGCCTCGGCGGAGATGTGCGCATCTGCCCTGACCTGGGCTTCTCCGGCGAGGGCGGCCACATCGACGCCTACGGCGTCTACTTCACCGATGCCGGCCAGCACCAGGAGCACCGCCCCTACGTGGCTCACACCGAGCCCCACTGCTACTCGCGCGTCACCTACAAGGGTGCCCTCCAGGGCGAGGGCGCGCACGCCGTGTGGGTGGGGGACTGCCTCATCGGTCAGGCCGCCCGCGGCACGGACACCTACGAGCTCAACCGCAACCTGGTCCTCACCGAGGGGGCCAAGGCCGACTCCGTGCCGAACCTGGAGATCGAGAACGGCAACATCGAGGGGGCCGGCCACGCCAGCGCCACCGGCCGCTTCGACGACCAGCAGCTGTTCTACCTGCGTGCCCGCGGCATCCCCGAGACCGAGGCCCGCCGCCTCGTCGTCCTGGGCTTCTTCAACGAGATCGTCGCCGAGATCGGTGTCGATGAGGTCGAGGAGCGGCTCATGGCCGCCATCGAGAAGGAGCTCGAGCTCACCGGACTCATCACCGCCCGCACCGACCAGGACCCCGCCGCCCAGCCGGCAGCCGAGTGA","MPELSTDHSSATLDGAHSHGGPRYVSSRADRPTSFDPADIPVPRGREEEWRFTPMKRFAPLFDLDAIRAATAGQSDAGAVRIEADLPDGVSLETVARSDARIGTVGAPVDRTGVTAWNGTETATVLTLEPGAQLERAARLNIIGQDPQLARPTAQHILVAAEDGSKGTVVLDHTGTAALTQGVEVTVADGAELTLVTVQGWEDGAVHASNHRVKVCDRGVLKHVVVSLGGDVRICPDLGFSGEGGHIDAYGVYFTDAGQHQEHRPYVAHTEPHCYSRVTYKGALQGEGAHAVWVGDCLIGQAARGTDTYELNRNLVLTEGAKADSVPNLEIENGNIEGAGHASATGRFDDQQLFYLRARGIPETEARRLVVLGFFNEIVAEIGVDEVEERLMAAIEKELELTGLITARTDQDPAAQPAAE$","FeS assembly protein SufD","Cytoplasm, Extracellular","FeS assembly protein SufD","hypothetical protein","FeS assembly protein SufD","","","","","

InterPro
IPR000825
Family

SufBD
PF01458	$\"[148-374]T$	UPF0051

InterPro
IPR011542
Family

FeS assembly protein SufD
TIGR01981	$\"[42-391]T$	sufD: FeS assembly protein SufD

","BeTs to 15 clades of COG0719COG name: Predicted membrane components of an uncharacterized iron-regulated ABC-type transporter SufBFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0719 is aompkz--vdrlbce---s--j-it-Number of proteins in this genome belonging to this COG is 2","***** IPB011542 (FeS assembly protein SufD) with a combined E-value of 5.7e-52. IPB011542A 42-58 IPB011542C 197-244 IPB011542D 244-278 IPB011542E 340-391***** IPB000825 (Protein of unknown function UPF0051) with a combined E-value of 1.1e-16. IPB000825B 325-371","Residues 34-108 are 62% similar to a (UPF0051 UNCHARACTERIZED MEMBRANE AN ABC-TYPE COMPONENTS TRANSPORTER COMPONENT ABC SCO1924) protein domain (PD040896) which is seen in Q829T3_STRAW.Residues 110-215 are 50% similar to a (ABC TRANSPORTER UPF0051 SUFB MEMBRANE ATP-BINDING ABC-TYPE COMPONENT IRON-REGULATED UNCHARACTERIZED) protein domain (PD005891) which is seen in Q9XAD2_STRCO.Residues 110-227 are 52% similar to a (COMPONENT ABC MEMBRANE TRANSPORTER UPF0051 IRON PROTEIN POSSIBLE REGULATED TRANSPORTER) protein domain (PDA1E3C3) which is seen in Q6AF31_BBBBB.Residues 229-295 are 76% similar to a (ABC TRANSPORTER MEMBRANE SUFB COMPONENT UPF0051 ABC-TYPE UNCHARACTERIZED IRON-REGULATED ATP-BINDING) protein domain (PD581536) which is seen in Q829T3_STRAW.Residues 303-400 are similar to a (ABC TRANSPORTER MEMBRANE UPF0051 SUFB COMPONENT ABC-TYPE ATP-BINDING IRON-REGULATED UNCHARACTERIZED) protein domain (PD003219) which is seen in YE97_MYCBO.","","-44% similar to PDB:1VH4 Crystal structure of a stabilizer of iron transporter (E_value = 1.5E_14);-41% similar to PDB:2C82 X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.5E_14);-41% similar to PDB:2JCV X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS, IN COMPLEX WITH FOSMIDOMYCIN AND NADPH (E_value = 1.5E_14);-41% similar to PDB:2JCX X-RAY STRUCTURE OF MUTANT 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS, IN COMPLEX WITH FOSMIDOMYCIN AND NADPH (E_value = 1.5E_14);-41% similar to PDB:2JCY X-RAY STRUCTURE OF MUTANT 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.5E_14);","Residues 148 to 374 (E_value = 9.6e-19) place ANA_0989 in the UPF0051 family which is described as Uncharacterized protein family (UPF0051).","","assembly protein SufD (sufD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0990","1067299","1065860","1440","5.13","-20.92","53825","ATGACACTGCCGACAACCGAGACCACGCGTAGCACCGACGACGAGATCATCGACTCGATCTCGACGAGCTACGACTTCGGCTGGCACGACTCCGACGAGGCCGGTGAGAAGGCCAAGCGAGGCCTTGATGAGCAGGTGGTCCGCGAGATCTCCGCCATCAAGGGAGAGCCGGAGTGGATGCTGGCCAAGCGTCTCAAGGCCTACTCCACCTTCGAGCGCAAGCCCATGCCCATCTGGGGCGTGGACCTCTCCCAGCTCGACATGGACGCCGTCAAGTACTACGTGCGCTCCACGGACCGGCCGGCCAACTCCTGGGACGACCTGCCCGAGGACATCAAGAACACCTACGACCGCATCGGCATCCCCGAGGCCGAGCGCGAGCGCCTGGTGGCGGGCGTGGCCGCCCAGTACGAGTCGGAGGTCGTCTACCACCAGATCCGCGGTGACCTGGAGGAGCAGGGCGTCATCTTCGTGGACACCGACACCGCGGTGCGCGAGTACCCCGAGCTCGTCAAGGAGTACTTCGGGACCGTGGTGCCCGCCGGCGACAACAAGTTCGCCGCCCTCAACACGGCCGTGTGGTCCGGGGGCTCCTTCATCTACGTCCCCAAGGGCGTCCACGTCGAGATCCCGCTCCAGGCCTACTTCCGCATCAACACGGAGAACATGGGCCAGTTCGAGCGCACGCTCATCATCGCTGACGAGGACTCCTACGTTCATTACGTCGAGGGCTGCACCGCCCCCATCTACTCCACCGACTCCCTGCACTCGGCGATCGTGGAGATCGTGGTCAAGAAGAACGCCCGCGTGCGCTACACGACCATCCAGAACTGGTCCAATAACGTCTACAACCTGGTGACCCAGCGCGCTACCTGCGAGGAGGGCGCCACCATGGAGTGGATCGACGGCAACATCGGCTCCAAGCGCAACATGAAGTACCCGGCCGTCTTCCTCATGGGCCCCCACGCCCGCGGCGAGGCCCTGTCCATCGCCTTCGCCGGCGCGGACCAGCACCAGGACACCGGCGCCAAGATGGTCCACATGGCGCCCCACACCTCCAGCCACATCGTCTCCAAGTCGATCGCCCGCCACGGTGGCCGCAGCGCCTACCGCGGACTGGTGCAGATCATGAAGAACGCCCGGCACTCCAAGTCCAACGTGCTGTGCGACGCGCTCCTGGTCGATGAGATCTCCCGCTCGGACACCTACCCCTACGTCGATGTGCGCACCGACGACGTCGAGATGGGCCACGAGGCGACCGTCTCCAAGGTGAGCGCCGACCAGCTCTTCTACCTCATGCAGCGCGGGCTGACCGAGACCGAGGCCATGGCCACGATCGTGCGCGGCTTCGTCGAGCCCATCGCCCGGGAGCTGCCCATGGAGTACGCCCTCGAGCTCAACCGGCTCATCGAGCTGCAGATGGAGAACTCGGTGGGCTGA","MTLPTTETTRSTDDEIIDSISTSYDFGWHDSDEAGEKAKRGLDEQVVREISAIKGEPEWMLAKRLKAYSTFERKPMPIWGVDLSQLDMDAVKYYVRSTDRPANSWDDLPEDIKNTYDRIGIPEAERERLVAGVAAQYESEVVYHQIRGDLEEQGVIFVDTDTAVREYPELVKEYFGTVVPAGDNKFAALNTAVWSGGSFIYVPKGVHVEIPLQAYFRINTENMGQFERTLIIADEDSYVHYVEGCTAPIYSTDSLHSAIVEIVVKKNARVRYTTIQNWSNNVYNLVTQRATCEEGATMEWIDGNIGSKRNMKYPAVFLMGPHARGEALSIAFAGADQHQDTGAKMVHMAPHTSSHIVSKSIARHGGRSAYRGLVQIMKNARHSKSNVLCDALLVDEISRSDTYPYVDVRTDDVEMGHEATVSKVSADQLFYLMQRGLTETEAMATIVRGFVEPIARELPMEYALELNRLIELQMENSVG$","FeS assembly protein SufB","Cytoplasm, Extracellular","FeS assembly protein SufB","K09014 Fe-S cluster assembly protein SufB","FeS assembly protein SufB","","","","","

InterPro
IPR000825
Family

SufBD
PF01458	$\"[218-450]T$	UPF0051

InterPro
IPR010231
Family

FeS assembly protein SufB
TIGR01980	$\"[22-470]T$	sufB: FeS assembly protein SufB

","BeTs to 16 clades of COG0719COG name: Predicted membrane components of an uncharacterized iron-regulated ABC-type transporter SufBFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0719 is aompkz--vdrlbce---s--j-it-Number of proteins in this genome belonging to this COG is 2","***** IPB000825 (Protein of unknown function UPF0051) with a combined E-value of 3.8e-40. IPB000825A 233-258 IPB000825B 401-447***** IPB011542 (FeS assembly protein SufD) with a combined E-value of 4.3e-19. IPB011542D 371-405 IPB011542E 416-467 IPB011542D 322-356","Residues 42-77 are 83% similar to a (ABC TRANSPORTER SUFB MEMBRANE UPF0051 COMPONENT ABC-TYPE IRON-REGULATED CHLOROPLAST YCF24) protein domain (PD815780) which is seen in Q6NH51_CORDI.Residues 91-136 are 95% similar to a (ABC TRANSPORTER UPF0051 MEMBRANE COMPONENT SUFB ABC-TYPE PERMEASE SUBUNIT YCF24) protein domain (PD815775) which is seen in Q8FT84_COREF.Residues 137-195 are 94% similar to a (ABC TRANSPORTER SUFB MEMBRANE UPF0051 COMPONENT CHLOROPLAST YCF24 ABC-TYPE IRON-REGULATED) protein domain (PD583482) which is seen in Q829T4_STRAW.Residues 141-195 are 92% similar to a (PPS1 UNCHARACTERIZED MEMBRANE INTEIN AN AUTOCATALYTIC UPF0051 ABC-TYPE IRON-REGULATED ML0593) protein domain (PD604737) which is seen in YE61_MYCLE.Residues 197-302 are similar to a (ABC TRANSPORTER UPF0051 SUFB MEMBRANE ATP-BINDING ABC-TYPE COMPONENT IRON-REGULATED UNCHARACTERIZED) protein domain (PD005891) which is seen in Q6AF32_BBBBB.Residues 306-374 are 88% similar to a (ABC TRANSPORTER MEMBRANE SUFB COMPONENT UPF0051 ABC-TYPE UNCHARACTERIZED IRON-REGULATED ATP-BINDING) protein domain (PD581536) which is seen in Q6A7H1_PROAC.Residues 380-475 are similar to a (ABC TRANSPORTER MEMBRANE UPF0051 SUFB COMPONENT ABC-TYPE ATP-BINDING IRON-REGULATED UNCHARACTERIZED) protein domain (PD003219) which is seen in Q9XAD1_STRCO.","","-52% similar to PDB:1VH4 Crystal structure of a stabilizer of iron transporter (E_value = 2.9E_12);","Residues 218 to 450 (E_value = 3.8e-123) place ANA_0990 in the UPF0051 family which is described as Uncharacterized protein family (UPF0051).","","assembly protein SufB (sufB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0992","1068030","1067296","735","9.16","7.53","26202","ATGACTCAGAGTGACGACGACTCTACCCGGGCACGCGTTCTCGACCTCATCGCTGAGAAGGGACCGGTGTCGGCGGCGCAGCTCGCCAAGGTCCTGAGGCTGACGCCGGCCGCCGTGCGCAGGCACATCACCGCCCTTGAGGACGCTGAGCAGATCGAGGTGCACACGCCGGCCCAGACGGGCAAGCGCGGCCGCGGTCGCCCGGCCCGGCACTACGTCTTGACGCCCAAGGCTCGCACCTCCTTCGCGGAGGGCTACTCCGACCTGGCCAACCGTGCCCTGCACTACCTGTCCCAGGTGGCTGGTGACAAGGCGGTCGACTCCTTCGCCGCGGCCAGGGGCCGTGACCTCGAGCGCCGCTACGCCACCGTCGTCGAGGCGGCCGGCAAGGATCCCTCGGAGAGGGCCCGCGCCCTGGCGGACGCCCTGACTCTCGACGGCTACGCGGCCTCGGTGCGCGACGTCGGGGACGGCTCCTTCGCCGTCCAGCTGTGCCAGGGCAACTGCCCGGTGCGCGACGTCGCCGGGGAGTTCCACGAGCTGTGCGACGCCGAGACCCAGGCCATCTCCCGGCTCGTGGGCGTCCCCGTCCAGCGTCTGGCCACCCTGGCCGGAGGCGAGCACGTCTGTACCACCCACATTCCGATCGCCATGCCCGCGCTGCGCAAGCGCGCGGTTCGGGCGGCGGCTAAGACGCGAGGCCTTGAGACCAAGCGAATGGAAGGAACCCGATGA","MTQSDDDSTRARVLDLIAEKGPVSAAQLAKVLRLTPAAVRRHITALEDAEQIEVHTPAQTGKRGRGRPARHYVLTPKARTSFAEGYSDLANRALHYLSQVAGDKAVDSFAAARGRDLERRYATVVEAAGKDPSERARALADALTLDGYAASVRDVGDGSFAVQLCQGNCPVRDVAGEFHELCDAETQAISRLVGVPVQRLATLAGGEHVCTTHIPIAMPALRKRAVRAAAKTRGLETKRMEGTR$","Transcriptional regulator, ArsR family","Cytoplasm","Predicted transcriptional regulator","putative DNA-binding protein","regulatory protein, ArsR","","Morby A.P., Turner J.S., Huckle J.W., Robinson N.J. SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 1993. 21(4):921-925. PMID: 8451191Bairoch A. A possible mechanism for metal-ion induced DNA-protein dissociation in a family of prokaryotic transcriptional regulators. Nucleic Acids Res. 1993. 21(10):2515-2515. PMID: 8506147Eicken C., Pennella M.A., Chen X., Koshlap K.M., VanZile M.L., Sacchettini J.C., Giedroc D.P. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins. J. Mol. Biol. 2003. 333(4):683-695. PMID: 14568530Cook W.J., Kar S.R., Taylor K.B., Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J. Mol. Biol. 1998. 275(2):337-346. PMID: 9466913Busenlehner L.S., Pennella M.A., Giedroc D.P. The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 2003. 27(2):131-143. PMID: 12829264Liu T., Nakashima S., Hirose K., Shibasaka M., Katsuhara M., Ezaki B., Giedroc D.P., Kasamo K. A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPx-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II). J. Biol. Chem. 2004. 279(17):17810-17818. PMID: 14960585","","","

InterPro
IPR001845
Domain

Bacterial regulatory protein, ArsR
PF01022	$\"[7-54]T$	HTH_5

","BeTs to 7 clades of COG2345COG name: Predicted transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2345 is ---p-----dr-bc--g---------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 147-215 are similar to a (TRANSCRIPTIONAL DNA-BINDING REGULATOR FAMILY REGULATOR PREDICTED DEOR PROBABLE TRANSCRIPTION REGULATORY) protein domain (PD332564) which is seen in Q741A6_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 7 to 54 (E_value = 9e-07) place ANA_0992 in the HTH_5 family which is described as Bacterial regulatory protein, arsR family.Residues 9 to 63 (E_value = 0.00094) place ANA_0992 in the HTH_11 family which is described as HTH domain.Residues 9 to 50 (E_value = 4.4e-05) place ANA_0992 in the MarR family which is described as MarR family.","","transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0993","1069330","1068410","921","5.27","-16.47","34232","ATGGCACTTGCACTGAATGACCACTGGCTGTGGGACCACTGGATCTGTGACGACGGCGATCGTTATCACCTCTTCTTCCTACGGGCGTCGCGTGCGTTACACGACCCGGAGCGGCGGCACTTCCGTGCTTCCATGGGGCACGCCGTTTCCAGCGATGCGCGTACGTGGCAACTTTTGCCCGATGCCCTAGTGCATTCCGACGGGCCGGCGTTCGACGACAAGGCCATCTGGACCGGCTCCACCATCGTCAAGCCCGACGGTGCTATGCGTGTCTTCTACACCGGTATCTCTCGAGCAGAGGACGGGCTGGTTCAGCGCATCGGCTGGGCTGACTCCACTGACGGAGTGACGTTTGAACGCACGTGCGATGTTCCTCTGGAGGCGGACTCCAGGTGGTACGAGAGGAGGGAAACCGACGTCTCTGGCGCCGAGCACTGGAGGGATCCCTTTGTCTTCAGGCACGACGGGCGCTGGCACATGCTCATCACCGCCAGGGCGAAGGGGGCTGAGCACTTTGGTGCCGGCGTCATCGGTCATGCCGTCTCCGATGACCTGGACCACTGGCAGATCGGGCCGCCGCTGACCAGCCCGTCGGTCTTCGGTCAGCTGGAGGTTTCCCAGAGCCGGAGCGTTGACGACCGTCATCTCCTCGTCTTCTCCTGCGGTGACGACATGAAGGCTGAACCTGGTCCGGGCGGGGTGTGGGTCGCCGAGGGGGAGGGGGCGCTGGGGCCCTGGGATATCGACGGCGCCAGGTACGTGCGCCCAGAGCACCTCTATGCCGGTCAGCTGCTTCAGCTGCGCGACGGGGCGTGGGTCTTCACGGGCTTCGAGGACATCGTCAACGGTGAGTTCGTCGGTGCGGTTCCGGACCTTCTGCCGTGGGCTGATGTCGAGCTTCTCCCAAGAGGCGGGCGCTAG","MALALNDHWLWDHWICDDGDRYHLFFLRASRALHDPERRHFRASMGHAVSSDARTWQLLPDALVHSDGPAFDDKAIWTGSTIVKPDGAMRVFYTGISRAEDGLVQRIGWADSTDGVTFERTCDVPLEADSRWYERRETDVSGAEHWRDPFVFRHDGRWHMLITARAKGAEHFGAGVIGHAVSDDLDHWQIGPPLTSPSVFGQLEVSQSRSVDDRHLLVFSCGDDMKAEPGPGGVWVAEGEGALGPWDIDGARYVRPEHLYAGQLLQLRDGAWVFTGFEDIVNGEFVGAVPDLLPWADVELLPRGGR$","Glycoside hydrolase, family 32","Cytoplasm","putative sucrose hydrolase","hypothetical protein","Glycosyl hydrolase family 32, N terminal domain protein","","Alberto F., Bignon C., Sulzenbacher G., Henrissat B., Czjzek M. The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. J. Biol. Chem. 2004. 279(18):18903-18910. PMID: 14973124","","","

InterPro
IPR013148
Domain

Glycosyl hydrolases family 32, N-terminal
PF00251	$\"[12-302]T$	Glyco_hydro_32N

InterPro
IPR001362
Family

Glycoside hydrolase, family 32
SM00640	$\"[18-458]T$	Glyco_32

InterPro
IPR013148
Domain

Glycosyl hydrolases family 32, N-terminal
PF00251	$\"[18-340]T$	Glyco_hydro_32N

InterPro
IPR013189
Domain

Glycosyl hydrolase family 32, C-terminal
PF08244	$\"[373-458]T$	Glyco_hydro_32C

noIPR
unintegrated

unintegrated
G3DSA:2.60.120.560	$\"[360-494]T$	no description
signalp	$\"[1-26]?$	signal-peptide

","BeTs to 5 clades of COG1621COG name: Beta-fructosidases (levanase/invertase)Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1621 is ------y-v--lb-e-gh--------Number of proteins in this genome belonging to this COG is 5","***** IPB013148 (Glycosyl hydrolases family 32, N terminal) with a combined E-value of 2.2e-11. IPB013148A 271-286 IPB013148B 442-468","Residues 14-177 are 66% similar to a (HYDROLASE GLYCOSIDASE INVERTASE SUCROSE-6-PHOSPHATE PRECURSOR SIGNAL BETA-FRUCTOFURANOSIDASE ACID TRANSFERASE WALL) protein domain (PD581674) which is seen in Q9EVQ9_BBBBB.Residues 185-361 are 71% similar to a (HYDROLASE GLYCOSIDASE INVERTASE SUCROSE-6-PHOSPHATE PRECURSOR SIGNAL ACID BETA-FRUCTOFURANOSIDASE TRANSFERASE WALL) protein domain (PD186064) which is seen in O50585_ARTNI.Residues 372-438 are 70% similar to a (GLYCOSIDASE HYDROLASE TRANSFERASE FRUCTOTRANSFERASE LEVAN LEVANASE YVEB 26-BETA-D-FRUCTAN 6-LEVANBIOHYDROLASE) protein domain (PD863092) which is seen in Q9KJD0_BBBBB.Residues 440-484 are 80% similar to a (HYDROLASE GLYCOSIDASE SUCROSE-6-PHOSPHATE INVERTASE PRECURSOR SIGNAL SUCRASE CARBOHYDRATE METABOLISM LEVANASE) protein domain (PD682098) which is seen in Q9KJD0_BBBBB.","","-42% similar to PDB:1Y4W Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21 (E_value = 4.1E_30);-42% similar to PDB:1Y9G Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose (E_value = 4.1E_30);-42% similar to PDB:1Y9M Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 (E_value = 4.1E_30);","Residues 18 to 340 (E_value = 6.7e-35) place ANA_0994 in the Glyco_hydro_32N family which is described as Glycosyl hydrolases family 32 N terminal.Residues 373 to 458 (E_value = 5.9e-10) place ANA_0994 in the Glyco_hydro_32C family which is described as Glycosyl hydrolases family 32 C terminal.","","fructotransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_0995","1072056","1071085","972","9.40","6.60","35803","ATGCTCACTGAGACAACTAGGACCGATGCAGTACCTGCGACTACAGCCGTCGATGCCCTCGAGGCTCCCGAAAGGAGCCCGCGTTGCCGTGGCCGCGCCGCCACCAGGAAAAGGTCCAGGGTGCTGACGTACGTCGGCCTTGTCTTCGCCTCGTGCGTCGCTGTGTTCCCGCTGCTGTTCATGGTCTTCTCATCCTTCAAAGAAGACCACCAGATCTTCGCTGATCTCGGCTCCCTTAAGGCGTTCCTTCCGACCGGTCACCTATCACTGGATAACTACTCCGGAGTATTCGAGCGGGTCCCGGCTGTACGGTTTATCACAAACTCGCTCATCGTGACCGTTGCGATAGTATTGCTCGGTCTCATTGTCAACTCCATGATCGGATTTGCGATATCGCGTATGCGCTGGAGGGGCAAGAACATTGTGCTCTCGCTTGTCCTAGCCACCCTCATGGTTCCTTTCGAGACCATCGCTGTGCCGCTCGTATACTGGGTCGCCAAGTTGCCATCGCTGCAGTGGGTCGTTGACGGTTTTCTTGTCAAACAGGGAATGCTCAACACTTATCAGGTGCAGATTCTGCCCTTCGTTGCCAATGCACTCTCCATCTTCCTGTTCGCCCAGCACTTTGGTGATATCCCCAAGGAGATCGACGAGGCGGCCCGCGTTGATGGTGCGTCCTGGTGGGTGATCTACTCACGAATCATCGTGCCACTGTCTGGTCCGACCTTCGCCACAGTCGCCATCATCACGATGCTGCCGGCGTGGAACTCCTACCTGTGGCCGCTCATGGTCATCCAGGAGGAGTCTATGCGGCCCGCGAGTGTCGGTATGCAGTACTTCTTCCAACTCAACCCGGTATGGGGGCAGATCATGGCTTACGGCACACTCATCACTCTGCCTGTTCTTATCATTTTCGTTCTGTTCCAGCGCTCGTTCGTAGCGTCGTTGGCAGGTACCGCCGTCAAAGGCTGA","MLTETTRTDAVPATTAVDALEAPERSPRCRGRAATRKRSRVLTYVGLVFASCVAVFPLLFMVFSSFKEDHQIFADLGSLKAFLPTGHLSLDNYSGVFERVPAVRFITNSLIVTVAIVLLGLIVNSMIGFAISRMRWRGKNIVLSLVLATLMVPFETIAVPLVYWVAKLPSLQWVVDGFLVKQGMLNTYQVQILPFVANALSIFLFAQHFGDIPKEIDEAARVDGASWWVIYSRIIVPLSGPTFATVAIITMLPAWNSYLWPLMVIQEESMRPASVGMQYFFQLNPVWGQIMAYGTLITLPVLIIFVLFQRSFVASLAGTAVKG$","ABC-type multiple sugar transport system, permease component","Membrane, Cytoplasm","Sugar permeases","K02026 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[106-321]T$	BPD_transp_1
PS50928	$\"[106-308]T$	ABC_TM1

noIPR
unintegrated

unintegrated
tmhmm	$\"[41-61]?$ $\"[111-131]?$ $\"[141-163]?$ $\"[188-206]?$ $\"[234-254]?$ $\"[286-308]?$	transmembrane_regions

","BeTs to 15 clades of COG0395COG name: Sugar permeasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0395 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","Residues 57-130 are 67% similar to a (TRANSMEMBRANE PERMEASE ABC SUGAR TRANSPORTER MEMBRANE TRANSPORTER SYSTEM PROBABLE PLASMID) protein domain (PD031935) which is seen in Q8UK60_AGRT5.Residues 143-323 are 48% similar to a (SUGAR PERMEASE TRANSMEMBRANE) protein domain (PD997667) which is seen in Q6YPH7_ONYPE.Residues 145-238 are 76% similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q8UK60_AGRT5.Residues 239-284 are 70% similar to a (TRANSMEMBRANE PLASMID MEMBRANE TRANSPORTER ABC AGR_PAT_376P SPANNING) protein domain (PD893950) which is seen in Q8UK60_AGRT5.Residues 245-322 are 52% similar to a (TRANSMEMBRANE BINDING-PROTEIN-DEPENDENT) protein domain (PD758539) which is seen in Q9RK90_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 106 to 321 (E_value = 1.4e-10) place ANA_0995 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","permeases (permease)","","1","","","","","","","","","","","Tue Aug 14 11:35:19 2007","","Tue Aug 14 11:34:08 2007","","","Tue Aug 14 11:34:08 2007","","Tue Aug 14 11:34:08 2007","","Tue Aug 14 11:34:08 2007","Tue Aug 14 11:34:08 2007","","","","","yes","","" "ANA_0996","1072957","1072058","900","10.06","6.90","33457","ATGAGGCGCCGCGGCAGGACCGCCGCATTGCGCAGAGAGGCTAGGACGGCGTGGCTCATGAGCTCGCCGGCCCTCCTGCTCCTCCTGCTTTTCATGGGCATTCCGATCCTGCTTACCTTCATCCTGTCCTTCACGAATACGCGTCTCATCTCCCCCAACCCTCCGCAGTTCATCGGGATGGAGAACTTCGTACGGGCGTTCACCGACGACCCGACCTTCATCCGGTCTCTGGCGAATACTGTCTTGTTCGCGCTCGTTGTCGTGCCCTTCCAGTCCATCCTTGCCCTAGCGCTGGCGATTCTTGTCAACCAGAAGGTCAAGGGAGTCACTGCTTTCCGGACAATGATCTTCATGCCCGTGGTGACCTCCATGGTTGTGGTCTCCATCCTGTGGAGCTTCTTCTATCAGGACAATGGCCTGTTCAACTCGATGCTCAACACCGTCACTGGCGGCGGGTGGTCCACCATTGCCTGGCTCAACCACCCTGGCACCGCGATGCCTGCCATTATCGTGCTGTCTATCTGGCAAGCGGTCGGTTTCCATATGATCATCTGGCTCTCCGGCCTGCAAATGATTGACCCGGTTCTCTACGAGGCCGCTGACCTCGACGGCGTCAACGGTTGGCAGCGCTTCCGCTACATAACATGGCCGGGGCTGCATTCGACGATGGTCTTCATCCTCGTCACCATCACGATTGCTGCGCTGGGCCTGTTCGTCCAGGTCGACGTTATGACATCCGGAGGTCCCCAAGATGCCACCTCGACAATCGTCTACCACGCGGTGCGCAGGGGTTACCGTGAGCAGGACATGGGGTACGGCAGCTCCATCTCACTCATATTCTTCATTGCCGTCCTGCTCATCAGTCTCATCCAGCGCTGGCTCACCAGGGAGAAGGACTGA","MRRRGRTAALRREARTAWLMSSPALLLLLLFMGIPILLTFILSFTNTRLISPNPPQFIGMENFVRAFTDDPTFIRSLANTVLFALVVVPFQSILALALAILVNQKVKGVTAFRTMIFMPVVTSMVVVSILWSFFYQDNGLFNSMLNTVTGGGWSTIAWLNHPGTAMPAIIVLSIWQAVGFHMIIWLSGLQMIDPVLYEAADLDGVNGWQRFRYITWPGLHSTMVFILVTITIAALGLFVQVDVMTSGGPQDATSTIVYHAVRRGYREQDMGYGSSISLIFFIAVLLISLIQRWLTREKD$","ABC-type multiple sugar transport system, permease component","Membrane, Cytoplasm","transmembrane permease MsmF","K05814 sn-Glycerol 3-phosphate transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[73-298]T$	BPD_transp_1
PS50928	$\"[77-291]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[24-44]?$ $\"[80-100]?$ $\"[115-135]?$ $\"[168-188]?$ $\"[219-239]?$ $\"[272-290]?$	transmembrane_regions

","BeTs to 15 clades of COG1175COG name: ABC-type sugar transport systems, permease componentsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1175 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","Residues 68-290 are 49% similar to a (TRANSMEMBRANE) protein domain (PD057516) which is seen in O30423_CALSA.Residues 70-117 are 70% similar to a (TRANSMEMBRANE PERMEASE SUGAR ABC TRANSPORTER SYSTEM TRANSPORTER MEMBRANE PLASMID PROBABLE) protein domain (PD330158) which is seen in Q8UK59_AGRT5.Residues 73-217 are 50% similar to a (SUGAR PERMEASE TRANSMEMBRANE COMPONENT ABC-TYPE SYSTEM ABC GLYCEROL-3-PHOSPHATE TRANSPORTER) protein domain (PD705073) which is seen in Q9KRT6_VIBCH.Residues 168-217 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q8UK59_AGRT5.Residues 219-277 are similar to a (TRANSMEMBRANE PERMEASE ABC SUGAR TRANSPORTER TRANSPORTER MEMBRANE SYSTEM INNER INTEGRAL) protein domain (PD748016) which is seen in Q8UK59_AGRT5.","","No significant hits to the PDB database (E-value < E-10).","Residues 73 to 298 (E_value = 4e-09) place ANA_0996 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","permease MsmF (permease)","","1","","","","","","","","","","","Tue Aug 14 11:35:45 2007","","Tue Aug 14 11:35:45 2007","","","Tue Aug 14 11:35:45 2007","","Tue Aug 14 11:35:45 2007","","Tue Aug 14 11:35:45 2007","Tue Aug 14 11:35:45 2007","","","","","yes","","" "ANA_0997","1074389","1073112","1278","5.32","-6.60","46041","ATGATGACCACCCGCCGTATGTTTCTTGGCGCCAGCGCCGCCGCCTTGACCACGCTTGCCGCATGCTCCTCTCAGTCCGGAAAGGGGGCGGGCGGCCTGACGCTCTGGACCCACAACGGAGGCAACAAGGAGGAGCTCGACGTCGTCAACAGCGCGGTCAAGGACTTCAACGCCGCGAACCCCAACACCCCGGTCACGGTGAAGTCTTTCCCGCAGGAGTCCTACAACGATGCCATCGCCTCAGCCGCAGTCTCCGGCAATCTGCCCGACATCCTCGACCTTGACGGCCCGATCATGTCCAACTGGGCCTGGGCCGGATACCTCTCGCCACTGACAATCTCGCAAGATCTCCAGGGAAAGATCATCGACTCCGCTAAAGGCGTCTGGAACAACAAGCTCTACTCCGTCGGCCCCTACGACACCTCGCTGTGCTTCCTCGGACGTAAGTCGGCCTTCGACAAAGCCGGTGTCACCATCCCCACGGTCAACAAGCCGTGGACGAAGGACGAGTTCATGGGTGCCCTCGACAAGCTCTCAAAGCTCGACGGCTTCAGCTACGCCATTGACATGTCGGTGTGGGACACCGCCGAGTGGTGGCCCTACGCCTACGCTCCCATGCTCCAGTCCTTCGGTGGCGACCTCATCGACCGCAAGAGCTATGAGACCGCCGAGGGCTTCCTCAACGGGGACAAGGCCGTCGAGTGGGGCACCTGGTTCCGCTCGCTGTTCACCTCCAACTACGCCTCTCAGACCCCGGCCAAGGACGGCCAGGACTTCCTTCAAGGCAAGGTGCCGCTCGTCTATGCCGGCGGATGGAAGGTCCTCAAGGCTCAGGAGACCTTCGGCGAGGACGAGGTCCTCATCCTCCCCCCTGTCGACTTCGGCGCGGGTGCTCACGTAGGCGGCGGCTCCTGGCAATGGGGTGTGTCCTCCTCCTCGAAGAACACCGACGCTGCGAACAAGTTCATTGAGTTCCTCATGCAGGACAAGTACCTCGTTCAGTACTCCGACGCCATCGGCAACTTCCCGTCAATCGAGTCGGCCACCCCGAAGACGAAGTACTACGGCGAGGGCAAGCCGCTGGAGCCTGTTTACGAGATCGGTAAAAAGTACGCCCTCCTGCGTCCTGCGACACCCGGATACAAGGTCATCTCATCGACTTTCGACAAGGCCGCTCGGGACATCGTTTCCGGTTCCGATGTCAAGTCGACCCTCGACCAGGCCGTCAAGGACATCAACGCGGATATCAAGTCGAACGATGGCTACAAGGCCAAGTAG","MMTTRRMFLGASAAALTTLAACSSQSGKGAGGLTLWTHNGGNKEELDVVNSAVKDFNAANPNTPVTVKSFPQESYNDAIASAAVSGNLPDILDLDGPIMSNWAWAGYLSPLTISQDLQGKIIDSAKGVWNNKLYSVGPYDTSLCFLGRKSAFDKAGVTIPTVNKPWTKDEFMGALDKLSKLDGFSYAIDMSVWDTAEWWPYAYAPMLQSFGGDLIDRKSYETAEGFLNGDKAVEWGTWFRSLFTSNYASQTPAKDGQDFLQGKVPLVYAGGWKVLKAQETFGEDEVLILPPVDFGAGAHVGGGSWQWGVSSSSKNTDAANKFIEFLMQDKYLVQYSDAIGNFPSIESATPKTKYYGEGKPLEPVYEIGKKYALLRPATPGYKVISSTFDKAARDIVSGSDVKSTLDQAVKDINADIKSNDGYKAK$","ABC-type multiple sugar transport system, substrate-binding component","Periplasm, Membrane, Extracellular","sugar binding protein","K02027 multiple sugar transport system substrate-binding protein","extracellular solute-binding protein, family 1","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[7-333]T$	SBP_bac_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[30-370]T$	no description
PS51257	$\"[1-22]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 5 clades of COG1653COG name: Sugar-binding periplasmic proteins/domainsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1653 is -o-pkz--vdrlbcefghs--j--t-Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","Residues 33-149 are 65% similar to a (ABC PERIPLASMIC SUGAR BINDING TRANSPORTER TRANSPORTER SUGAR-BINDING LIPOPROTEIN SOLUTE-BINDING SPERMIDINE/PUTRESCINE-BINDING) protein domain (PD115161) which is seen in Q8UK58_AGRT5.Residues 150-284 are 67% similar to a (PLASMID SUGAR AGR_PAT_379P BINDING) protein domain (PD564388) which is seen in Q8UK58_AGRT5.Residues 289-411 are 65% similar to a (ABC SUGAR PERIPLASMIC BINDING TRANSPORTER SUGAR-BINDING TRANSPORTER LIPOPROTEIN SOLUTE-BINDING PROBABLE) protein domain (PD023543) which is seen in Q8UK58_AGRT5.","","No significant hits to the PDB database (E-value < E-10).","Residues 7 to 333 (E_value = 8.9e-17) place ANA_0997 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","binding protein","","1","","","","","","","","","","","Tue Aug 14 11:36:04 2007","","Tue Aug 14 11:32:23 2007","","","Tue Aug 14 11:32:23 2007","","Tue Aug 14 11:32:23 2007","","Tue Aug 14 11:32:23 2007","Tue Aug 14 11:32:23 2007","","","","","yes","","" "ANA_0998","1075500","1074487","1014","6.13","-3.61","36047","ATGACGACTCTCGCCGATGTCGCTGCCGCGGCTGGTGTCTCCAAGGCTGCGGCCTCCCTCGTGCTCTCCGGCAAGTTCGAGGGGCGCGTGAGTGAGCGCAAGGCTGAGCGGGTCCGTATGGCCGCTGATGAGCTCGGCTACGTTCGTGACGCCATTGCCGGTGGCATGCGCAACGGTCGAACCCGGACGATCGGGGTCATCGGCGAGCGTGTCCTGTCCACGCCCTACGCCGTCTCCATGATCGACGCTGTTCTGTCCACCAGTCAGAGCCTCGGGTGGTCCGTCCTTCTCACTGACGCAGGACGCGACGGCGTTGCCGCCAAGGAGGCAGTCCGCGAAATGGTCGCCCGGCGCGTCGGCCAGGTGGTCATTGCCTCGATGTATCACCGCGTTGTTCCGGTTCCTGAGCAGATCAAGGATGTCGTCGTGCTCAACGGCGTTGCTGACCGCCCTGGGGTTCCTGGTGTCGTTCCCGATGAGCGTCAAGGCGCCAGCGATGCCGTTGCCCACCTCGTCGACCTCGGCCACCGCCGTATCGGCTACCTTGGGCACGACGACGCCGAGAGTATCGCTGTGCGTGAGCGTTCCGACTCCTACCGCCACAGCCTTCGAGAGGCCGGGCTGGCGGTGGACGAGTCGCTCCTCGTCACCGGGGGACTCGACCCCGATAGTGTCGACGCCACTGCCCGCCGTCTCCTCGACCGGCCTGATCGTCCGACCGCCGTCTTCTGCTACAACGACGCCCTGGCGGCCGGCGTCTTCCGGCAGGCGGTACGCCTGGGGATCTCCATTCCCAACGACCTCTCTGTTATCGGCTTTGACGACCTCGCGCTCATCTCTACGAACCTCGATCCCAGGCTCACCACGATGCGCCTGCCGCACTGGGAGATGGCCGAGTGGCTCACTCGCGAGCTCGCTGCGGGCCGTACAGCCGAGCTCCCGGACGTCACTCGTTTCCCCTGCCCTCTCATCGAGCGAGCCTCCACGGCGCCTCCCGCCACCTCGCTGCCGTAG","MTTLADVAAAAGVSKAAASLVLSGKFEGRVSERKAERVRMAADELGYVRDAIAGGMRNGRTRTIGVIGERVLSTPYAVSMIDAVLSTSQSLGWSVLLTDAGRDGVAAKEAVREMVARRVGQVVIASMYHRVVPVPEQIKDVVVLNGVADRPGVPGVVPDERQGASDAVAHLVDLGHRRIGYLGHDDAESIAVRERSDSYRHSLREAGLAVDESLLVTGGLDPDSVDATARRLLDRPDRPTAVFCYNDALAAGVFRQAVRLGISIPNDLSVIGFDDLALISTNLDPRLTTMRLPHWEMAEWLTRELAAGRTAELPDVTRFPCPLIERASTAPPATSLP$","Transcriptional regulator, lacI family","Cytoplasm","transcriptional regulatory protein","transcriptional regulator; LacI family","Alanine racemase","","Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 1992. 267(22):15869-15874. PMID: 1639817Vartak N.B., Reizer J., Reizer A., Gripp J.T., Groisman E.A., Wu L.F., Tomich J.M., Saier Jr M.H. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 1991. 142(9):951-963. PMID: 1805309","","","

InterPro
IPR000843
Domain

Bacterial regulatory protein, LacI
PF00356	$\"[2-27]T$	LacI
SM00354	$\"[1-73]T$	HTH_LACI
PS50932	$\"[2-58]T$	HTH_LACI_2
PS00356	$\"[4-22]?$	HTH_LACI_1

InterPro
IPR001761
Domain

Periplasmic binding protein/LacI transcriptional regulator
PF00532	$\"[61-327]T$	Peripla_BP_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[2-65]T$	no description
G3DSA:3.40.50.2300	$\"[159-299]T$	no description

InterPro
IPR000086
Domain

NUDIX hydrolase
G3DSA:3.90.79.10	$\"[21-234]T$	no description
PF00293	$\"[63-180]T$	NUDIX

noIPR
unintegrated

unintegrated
PTHR11839	$\"[12-229]T$	UDP/ADP-SUGAR PYROPHOSPHATASE
PTHR11839:SF1	$\"[12-229]T$	ADP-RIBOSE PYROPHOSPHATASE

","BeTs to 18 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 7","No significant hits to the Blocks database.","Residues 82-123 are 73% similar to a (ADP-RIBOSE PYROPHOSPHATASE) protein domain (PD929717) which is seen in Q829A6_STRAW.Residues 82-123 are similar to a (HYDROLASE FAMILY ADP-RIBOSE MUTT/NUDIX PYROPHOSPHATASE PHOSPHOHYDROLASE DIPHOSPHATASE NUDIX ADENOSINE ADP) protein domain (PD189280) which is seen in Q9S225_STRCO.Residues 124-199 are 59% similar to a (HYDROLASE FAMILY MUTT/NUDIX ADP-RIBOSE PYROPHOSPHATASE PHOSPHOHYDROLASE DIPHOSPHATASE ADENOSINE ADP DIPHOSPHORIBOSE) protein domain (PD063277) which is seen in Q6AGG4_BBBBB.","","-49% similar to PDB:1MK1 Structure of the MT-ADPRase in complex with ADPR, a Nudix enzyme (E_value = 2.7E_27);-49% similar to PDB:1MP2 Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis (E_value = 2.7E_27);-49% similar to PDB:1MQE Structure of the MT-ADPRase in complex with gadolidium and ADP-ribose, a Nudix enzyme (E_value = 2.7E_27);-49% similar to PDB:1MQW Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme (E_value = 2.7E_27);-49% similar to PDB:1MR2 Structure of the MT-ADPRase in complex with 1 Mn2+ ion and AMP-CP (a inhibitor), a nudix enzyme (E_value = 2.7E_27);","Residues 63 to 207 (E_value = 3.4e-17) place ANA_0999 in the NUDIX family which is described as NUDIX domain.","","pyrophosphohydrolases including oxidative damage repair enzymes","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1000","1077710","1076553","1158","7.20","0.64","40413","ATGAGCGACGTCGACGCCACGAACAAGCCCGGTGCCGTACAGGACCCGCAGGTCGGACGCCGGAGGATCCTCCAAGTGTGTGGATCAGCCGCCGGAGGGGTGCGGGCCCACCTGGCCGACTGCGCCCGGATCCTGGCCGCCGACGGCCACGACGTCATTGTCGAGGCGCCCGCCGTGGTCCTTGACGGACTGGATATCGAGCCGGCTCGCGCCGAGCCACTCGAGATCGGACCCCGACCCAGCCTCAACGACACCCTGGCCGTGGCCAGGCTGCGTCGCCTGGGCCGGCGCGCCGACGTCCTTCACGCCCACGGCCTGCGAGCCGGGGCCCTGGCCGCCCTGGCCCTGGGACGACGCCGCCGCGGACGCACACGGCTGGTCGTCACCCTTCACAACCTCACCGTCGGGGGGCGCCTGACCACCTTGGTGGGGGACAGGCTCGAGCGGCTCATCGCCCGGCGCGCCGACCTCGTCCTGGCGGTCAGCCCCGACCTGGCCGAACGGGCCCAGGATCTTGGCGCCCCACACGTCGAGGTCGCCATCATCCCCGCGGTGCCACCACAGCAGCCCGCCGAACCGAGCCCCTCCGACGCGGCCGCGGCGGAGGATGCCTGGCCGCGAAGCGGGGCCCGCCTCCTGACCGTCGCCCGCCTGGCTCCCCAGAAGGGCCTGCCGCTGCTGCTCGAAGCCGCCGCGATCCTCTCCCGCGAGGTCGACGCCGGCCGGCTGACCGCCTTCACCTGGGCCCTCGCCGGGGACGGCCCCGGCCGCGAGCAGGCCGCTGAGCGCATCGCCGCCGAACAGCTCCCGGTCACCCTCCTGGGGCGGCGAAACGATGCTCCGGCCCTCATGGAGGCCGCTGACATCGTCGTCCAGACCAGCCTGTGGGAGGGCCAGCCCCTCACCATCCAGGAGGCCCTGCGCGCAGGCACCGCGATCGTGGCCACCGACGTCGGAGGCACCGCCGTGACCGCCAGAGGAGGAGCCCTCCTCGTGGACCCTCAGGCCCAGACCATCGCGGAGGCACTTCGAACCCTCCTGAGCGACCCCGAGGCCCGCACCCGCGCCGCTGAACGCGCGCAGGCGGCGGCCAGGCGCCTTCCCGGGCTCGAGGACCTGGCGACCCAGCTGCGACAGACGGTCCTCGACCTGCACTGA","MSDVDATNKPGAVQDPQVGRRRILQVCGSAAGGVRAHLADCARILAADGHDVIVEAPAVVLDGLDIEPARAEPLEIGPRPSLNDTLAVARLRRLGRRADVLHAHGLRAGALAALALGRRRRGRTRLVVTLHNLTVGGRLTTLVGDRLERLIARRADLVLAVSPDLAERAQDLGAPHVEVAIIPAVPPQQPAEPSPSDAAAAEDAWPRSGARLLTVARLAPQKGLPLLLEAAAILSREVDAGRLTAFTWALAGDGPGREQAAERIAAEQLPVTLLGRRNDAPALMEAADIVVQTSLWEGQPLTIQEALRAGTAIVATDVGGTAVTARGGALLVDPQAQTIAEALRTLLSDPEARTRAAERAQAAARRLPGLEDLATQLRQTVLDLH$","Putative glycosyl transferase","Cytoplasm","putative glycosyl transferase","putative glycosyl transferase","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[196-363]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[22-384]T$	GLYCOSYLTRANSFERASE

","BeTs to 10 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","***** IPB001296 (Glycosyl transferase, group 1) with a combined E-value of 9.2e-10. IPB001296B 293-325***** IPB013534 (Starch synthase catalytic region) with a combined E-value of 2.2e-08. IPB013534B 98-112 IPB013534C 127-137 IPB013534F 285-325","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 196 to 363 (E_value = 7.5e-30) place ANA_1000 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","glycosyl transferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1001","1079356","1077707","1650","10.14","14.30","55660","ATGGCATCTCAGCAACGCCGCGGCGGCCTGCTCTCAGCGGCCGGGTCCGTCGCCGGCCTGACCCTCGTCTCCCGTGTCCTGGGGTTCCTGCGCTGGCTCGTCCAGGCCGCCACCGTCGGCACCGGCACGGTGGCGGGCGCCTACACCACGGCCAACCAGCTGCCCAACACCCTCTACGAGGTCGTCGTCGGCGGGGTTCTGGCCGCCACCGTCGTTCCGCTCCTGGCGGCACCGATCGCCGCGGGCAGGCGTGAGGAGGTTACCGCCACCGCCTCGGGGCTGCTGGGCCTGGTCCTGGCGGTCCTGACCCCGCTGTCCCTGGGGCTCATCGTCCTGGCCGCCCCGATCGCCTCCCTGTTCCCCACCTCCCAGGGCGTGGACCCGACGCTTCAGCATGAGCTCGTCACCTCCTTCCTGCGCATGTTCGCCCTGCAGGTGCCCATGTACGGGGTGGCCGTCGTCCTCACCGGCGTCCTCCAGGCTCACAACCGCTTCACCTGGCCAGCGCTGACACCGATGCTCTCCAGCCTCGTGGTCATGGCGACCTACGGCCTCTACGGGGTGCTGGCCGGCGGCGACGACGCAGCCGCCTCCAGGCTCGCCCTCCAGGTGCTGGGCTGGGGGACGACCCTTGGGGTGGCCGCCCTCAGCCTGCCGTTGCTGTGGCCGGTCCACCGACTGGGACTGGGACTGCGCCCCACCCTGCGACTGGGGGGCGGCCAGGCCCGGCGGGCGCTGCGGCTCGGCGGGGCCGGGGTGTGGACGATCCTCGCCCAGCAGGTGAGCGTCCTGGTGGTCCTGGCCATGGCCCGCTGGGGCGGGCAGACCGGAACCGCGGCGGTCTACCAGTACACGCAAGCCGTCTACGTCCTTCCCTACGCAGTGCTGGCCGTCCCCGTGGCCACCGTCCTCTACCCCCGCCTGACCGCCGCCTTCGAGGCCCGCGAGCTGTCGGCGGGCAGTCCCGGCGGCACAGGTGTGGATGAGGACGCCACGAGGCTGGTGGCCACCTCCACGGCCCTGGTCACCGCCGTCGCTGTGGCCGGAACCGCCATGCTGCTGGCCGCCAGCGCCGCCGCCGAGCGCTTCTTCTCCTTCAAGCAGGTCGACGGGATGGGCCAGGCGCTGGCCGTCCTGGCGCCTGGACTGATCGGCTACGCCCTCATCTACCAGGTCACCCGGGTCCTGTTCGCCGCCGACCGCTCTCGGCCCGCCGCTCACGCCACCGCGGCCGGCTGGCTGACCGTGGCGGTGGCCTGTGCCGCCTGCGTGTGCCTCATGGCGCCCGCAGGTGGGGACGGGCGCGCCACCCTCGTGGCCCTGGGAATGGGCACGACCATTGGGATGACGGTGGCGGGAGCGAGCCTGCTGATCGTTCTGGCCCGAGTCATGGGGGGCCGGGTGCTGCACGCGACCCTGACCGCGCTCGGTGCGGGGCTGCCCGTGGCCCTCGTCCTCGGGCTGGCCGTCCGAGAGGCAACCACTCGCGTCACCTCCCTGCCCCTGGCCGTCATCACCGCCGTGATCGGTGCCGCTGCGGCCGCGGCCCTCGTCCTGGTGGTCATCCACCTGGCTGACCGCAGCCTCCTGGCATCGGTACGTGGCGGCAGGCCGACGGTGACAACGAAGGACGACAAGGAGCAACCATGA","MASQQRRGGLLSAAGSVAGLTLVSRVLGFLRWLVQAATVGTGTVAGAYTTANQLPNTLYEVVVGGVLAATVVPLLAAPIAAGRREEVTATASGLLGLVLAVLTPLSLGLIVLAAPIASLFPTSQGVDPTLQHELVTSFLRMFALQVPMYGVAVVLTGVLQAHNRFTWPALTPMLSSLVVMATYGLYGVLAGGDDAAASRLALQVLGWGTTLGVAALSLPLLWPVHRLGLGLRPTLRLGGGQARRALRLGGAGVWTILAQQVSVLVVLAMARWGGQTGTAAVYQYTQAVYVLPYAVLAVPVATVLYPRLTAAFEARELSAGSPGGTGVDEDATRLVATSTALVTAVAVAGTAMLLAASAAAERFFSFKQVDGMGQALAVLAPGLIGYALIYQVTRVLFAADRSRPAAHATAAGWLTVAVACAACVCLMAPAGGDGRATLVALGMGTTIGMTVAGASLLIVLARVMGGRVLHATLTALGAGLPVALVLGLAVREATTRVTSLPLAVITAVIGAAAAAALVLVVIHLADRSLLASVRGGRPTVTTKDDKEQP$","Virulence factor MVIN family protein","Membrane, Cytoplasm, Extracellular","probable transmembrane protein, putative","similar to uncharacterized membrane protein putative virulence factor","virulence factor MVIN family protein","","Kutsukake K., Okada T., Yokoseki T., Iino T. Sequence analysis of the flgA gene and its adjacent region in Salmonella typhimurium, and identification of another flagellar gene, flgN. Gene 1994. 143(1):49-54. PMID: 8200538Rudnick P.A., Arcondeguy T., Kennedy C.K., Kahn D. glnD and mviN are genes of an essential operon in Sinorhizobium meliloti. J. Bacteriol. 2001. 183(8):2682-2685. PMID: 11274131","","","

InterPro
IPR004268
Family

Virulence factor MVIN-like
PR01806	$\"[40-59]T$ $\"[59-75]T$ $\"[165-186]T$ $\"[276-302]T$ $\"[379-398]T$	VIRFACTRMVIN
PF03023	$\"[35-515]T$	MVIN

noIPR
unintegrated

unintegrated
PTHR11946	$\"[6-192]T$	ISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES
PTHR11946:SF10	$\"[6-192]T$	LEUCYL-TRNA SYNTHETASE
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[61-81]?$ $\"[96-116]?$ $\"[135-155]?$ $\"[170-190]?$ $\"[204-224]?$ $\"[340-360]?$ $\"[370-390]?$ $\"[411-431]?$ $\"[441-461]?$ $\"[471-491]?$ $\"[497-519]?$	transmembrane_regions

","BeTs to 5 clades of COG0728COG name: Uncharacterized membrane protein, putative virulence factorFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0728 is -------qvdr--cefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB004268 (Virulence factor MVIN-like) with a combined E-value of 6.3e-20. IPB004268A 39-73 IPB004268B 277-308","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 515 (E_value = 1.6e-12) place ANA_1001 in the MVIN family which is described as MviN-like protein.Residues 81 to 185 (E_value = 0.0002) place ANA_1001 in the MatE family which is described as MatE.","","transmembrane protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1002","1080273","1079356","918","9.89","10.48","30033","ATGGCTGGCACGATCACGCGAGTAAGCTCCTACGCCCGAGACCTGGCAAGGGTGGGTATTAAGGCAGCGGGCACCGCCCTGTCCTGCTCCGTATGCCTGGCTCCCATCGCCCAGGGACTGGAGCGCATCAACTTCCACGGCCGTACCGTGAGCCTGCGCGGAGGCGTCGGGGCCGCAGCCGGCGCCGTGACGGCTGGGATCGAGGCCGGCAGGCTCCTGCGGGGCAGGACGGGCTCACCCTCGCGGGCAGGACTCGCCGCCACCCTCGCGTCTGCGGCCGGTGGGTGCGCCGGCCTGGTCGACGACCTCGATGCCGGGGCCCACGACGGCGACACCCCCGCCAAGGGCCTCAAGGGTCACCTCACCGCCCTCGCCCACGGGCGCGTCACCACCGGAGCCCTCAAGATCGCCGTCATCGGCTCAGGGGCGCTTGTCGGCGGTGTCCTCCTGGCCCGCCACCGCAGCTCGGGTGCCGGCGCACGTCCGCCAGTGTCCAGCGCCGTTGACGTCGTGTCCAGTGCCGTGGTCATCGCGGCCTGGGCGAACCTGCTCAACCTGCTCGACCTGCGCCCCGGACGGGCCCTCAAGACCGCCTGCATCGTGAGCACCCCGCTGCTGGCCACCCCCGGACGCGACGGCGAGCCCACCCGGATGCTGGCCGCGGGCACCCTGGGAGTCAGCCTCATGGCCCTGCCGGAGGACCTCCTGGAGAATACGATGCTGGGGGACACCGGGGCCAATGCCATTGGCGCCCTGCTGGGAACCGCCCTGGCCTGCCACCCCCACGCCGTGGTGCGCGCCGGAGCCGCCCTGAGCGGGGTGAGCCTCATCCTGGTCAGCGAGAAGGTGTCCTTCTCCCGCGTCATCTCCGACACCCCGGTGCTGGCCGCACTCGACGGGCTGGGGCGCCGCCCCTGA","MAGTITRVSSYARDLARVGIKAAGTALSCSVCLAPIAQGLERINFHGRTVSLRGGVGAAAGAVTAGIEAGRLLRGRTGSPSRAGLAATLASAAGGCAGLVDDLDAGAHDGDTPAKGLKGHLTALAHGRVTTGALKIAVIGSGALVGGVLLARHRSSGAGARPPVSSAVDVVSSAVVIAAWANLLNLLDLRPGRALKTACIVSTPLLATPGRDGEPTRMLAAGTLGVSLMALPEDLLENTMLGDTGANAIGALLGTALACHPHAVVRAGAALSGVSLILVSEKVSFSRVISDTPVLAALDGLGRRP$","Hypothetical protein","Membrane, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1004","1081305","1080370","936","5.23","-6.31","31908","ATGATCGACTTCCGCTATCACCTGGTATCGCTCATCTCCGTGTTCCTGGCCCTCGCCGTCGGGGTCGTCCTGGGAGCCGGCCCCCTGCAGAACTCTCTGGGAACCGCGCTCAACGATCAGGTCACCGCCCTGCGAGAGAACCGCAACGCCACCCAGGCCAAGCTCGAGCAGACGGAGACGGCCGTCAACGAGAGGGACTCCTACATCACTCAGGCCGCCAGCGGCCTCGTGCCCGGGACCCTGGCCTCCAAGAATGTGGCCATGGTGCTCCTGCCCGAGGCCAAGGCCGAGGACGCCGACGCCATCACCACCCAGCTCAAGAACGCAGGTGCCACCGTCACCGGCCGGGTGAGTCTGACCAGCACCTGGGTGGACCTGTCCCGGGAGAACTACCGCTCCACCTTCTCCGGACAGGTCCAGGGGCACCTGGACAGCACTACCTCCAAGGACGCCAACGGCATTCTGGGGGAGGCACTGGCCAAGGCCCTGACCGCCAACGACGACTCCTCCCGAGTCCTCATGGACATGCTGTCGGTGACAGCGGACAAGTCCGGCACGCCCTTCGTCTCCGTGGACTCCACACCCACCGCCCCTGCGGAGATGATCGTCGTCGTCGGGCCGCGCCCGCAGGCCTCCTCCGGCAATGGGGCGACGGTCGAGGCCACACCGGGGCAGGACCCCAAGGCCTGGGCCAAGGCGTTGGAGGGGACGGCCGGCCGGGCGCCCACAGTCGTCGTTGGCTCAGCCGACGGTGACGACGGCGTCGTCAGCATCATCCGCTCGGAGAAGGCGAAGGTGACCACTGTCGACTCCGTCGGCCAGATCGCCGCCTCCGTGTCCACCCCTCTGGCCCTGGCCTCCACCCGAGCGGGAACCATTGGCCACTACGGCTTCGATAAGGGAGCCGAGGCAGTCATGCCGCCAGTGACCAAGTAG","MIDFRYHLVSLISVFLALAVGVVLGAGPLQNSLGTALNDQVTALRENRNATQAKLEQTETAVNERDSYITQAASGLVPGTLASKNVAMVLLPEAKAEDADAITTQLKNAGATVTGRVSLTSTWVDLSRENYRSTFSGQVQGHLDSTTSKDANGILGEALAKALTANDDSSRVLMDMLSVTADKSGTPFVSVDSTPTAPAEMIVVVGPRPQASSGNGATVEATPGQDPKAWAKALEGTAGRAPTVVVGSADGDDGVVSIIRSEKAKVTTVDSVGQIAASVSTPLALASTRAGTIGHYGFDKGAEAVMPPVTK$","Hypothetical protein","Extracellular, Periplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PD032573	$\"[1-305]T$	YG98_MYCTU_P58212;
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[9-29]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 54-358 are 44% similar to a (SECRETED PRECURSOR SIGNAL ML1362 CGL1416 RV1698/MT1737/MB1724) protein domain (PD032573) which is seen in YG98_MYCTU.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","Thu Aug 2 12:01:53 2007","","Thu Aug 2 12:01:53 2007","","","Thu Aug 2 12:01:53 2007","Thu Aug 2 12:01:53 2007","Thu Aug 2 12:01:53 2007","","","","","","Thu Aug 2 12:01:53 2007","","Thu Aug 2 12:01:53 2007","","Thu Aug 2 12:01:53 2007","Thu Aug 2 12:01:53 2007","","","","","yes","","" "ANA_1005","1082569","1081364","1206","5.58","-9.65","42788","GTGAGGAATCCCTTCCGCAGGAAGTCTGCGTCCGTCTCCGAGCATCCCAGCGGTGTCGTACGCGTCGACGCGCGCACGAAGAAGCTCACCAAGCGTCTCCAGCCCGGGGAAATTGCCATCATCGACCACACCGACCTCGATCGGGTGGCCGCCGAGGCTCTGGTGGAGTGCGGTGCCTTAGCGGTCCTCAACGCCTCCCCGTCCATCTCCGGGCGCTACCCGAACCTCGGCCCCGGAATCCTCCTTGACGCGGGAATCCCGCTCGTGGACGACCTGGGCCCCGACATCATGCGCCTGCATGACGGTCAGCACGTCACTGTCGAGGACGGCTCGGTGCGGGTTGAGGGCAAGGAGCAGGTCATCGCCGAAGGAGCGGTCCAGACCAAGCAGACCGTTGCCGAGGCCATGGAGGAGGCTCAGAAGGGCCTGTCCGTCCAGCTGGAGGCTTTCGCCGCCAACACCATGGAGTACATGCGCGGAGAGTGGGACCTACTCCTCAACGGCGTCGGCATGCCCTCACTGACCACGCAGATGAGTGGCAAGCACGTCCTGGTGGTCGTGCGCGGTTACTCCTACAAGGAGGACCTGCAGGCGCTCAGGCCCTACATCCGCGAGTACAAGCCCGTCATCATCGGTGTCGACGGAGGCGCCGACGCCGTCCTGGACGCAGGCTTCAAACCGACCATGATCGTGGGCGACATGGACTCCGTGTCCGACAAGGCAATGACCTGCGGCGCCGAGATCGTCGTCCACGCCTACCGTGACGGACGCGCCCCGGGCCTGGCCCATGTCGAGGAGCTCGGGGTCGAGCACCATGTCTTTGCGGCCACCGGTACCAGTGAGGACATCGCCATGCTCATGGCCGATGAGGCCGGTGCCGAGATCATCGTGGCCCTGGGGACGCACGCCACCCTGCTGGAATTCCTCGACAAGGGGCGCGCCGGCATGTCCTCGACCTTCCTGACCCGGCTCAAGGTCGGTGGCCGACTCATCGACGCCAAGGGCGTCTCCCAGCTCTACCGCACTCGCATCTCGGGGTGGTGGCTACTGTTCCTGGCCCTGGCGGGCACCTTCGCCCTGGCCATCGCCCTGATGTCCACGCCCGGTGGACAGACCTTCCTGGGCCTGTCCGGTGCCGTGTGGGACGACGTCGTCAACTTCTTCCGCTCACTGGTGGGCCTTGCCCCGAACTCACCCACCGTCTAA","VRNPFRRKSASVSEHPSGVVRVDARTKKLTKRLQPGEIAIIDHTDLDRVAAEALVECGALAVLNASPSISGRYPNLGPGILLDAGIPLVDDLGPDIMRLHDGQHVTVEDGSVRVEGKEQVIAEGAVQTKQTVAEAMEEAQKGLSVQLEAFAANTMEYMRGEWDLLLNGVGMPSLTTQMSGKHVLVVVRGYSYKEDLQALRPYIREYKPVIIGVDGGADAVLDAGFKPTMIVGDMDSVSDKAMTCGAEIVVHAYRDGRAPGLAHVEELGVEHHVFAATGTSEDIAMLMADEAGAEIIVALGTHATLLEFLDKGRAGMSSTFLTRLKVGGRLIDAKGVSQLYRTRISGWWLLFLALAGTFALAIALMSTPGGQTFLGLSGAVWDDVVNFFRSLVGLAPNSPTV$","Thiamin pyrophosphokinase","Cytoplasm","conserved membrane protein ML1361","hypothetical protein","Thiamin pyrophosphokinase, catalytic region","","Baker L.J., Dorocke J.A., Harris R.A., Timm D.E. The crystal structure of yeast thiamin pyrophosphokinase. Structure 2001. 9(6):539-546. PMID: 11435118","","","

InterPro
IPR002826
Family

Protein of unknown function DUF115
PD016917	$\"[167-255]T$	Q6LZP5_METMP_Q6LZP5;

InterPro
IPR007371
Domain

Thiamin pyrophosphokinase, catalytic region
PF04263	$\"[208-252]T$	TPK_catalytic

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.10240	$\"[181-243]T$	no description
tmhmm	$\"[347-367]?$	transmembrane_regions

","BeTs to 4 clades of COG1634COG name: Uncharacterized Rossmann fold enzymeFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1634 is aompkz--------------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 17-210 are 66% similar to a (MEMBRANE MLC1351.11C BH2771 MB1723 CGL1415) protein domain (PD678034) which is seen in Q8RAB8_THETN.Residues 211-253 are 81% similar to a (KINASE PYROPHOSPHOKINASE THIAMIN TRANSFERASE THIAMINE YLOS NUCLEOTIDE-BINDING B.SUBTILIS DR0552 CPE1735) protein domain (PD546058) which is seen in Q8RAB8_THETN.Residues 255-341 are 85% similar to a (MEMBRANE MLC1351.11C BH2771 MB1723 CGL1415) protein domain (PD340270) which is seen in Q8RAB8_THETN.","","No significant hits to the PDB database (E-value < E-10).","Residues 198 to 311 (E_value = 1e-05) place ANA_1005 in the TPK_catalytic family which is described as Thiamin pyrophosphokinase, catalytic domain.","","membrane protein ML1361","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1006","1084374","1082566","1809","5.10","-24.80","63800","GTGATCGAGTCTTTGCACATCGAGGACCTCGGTGTCATCGAGGAGGCTGATCTTCCCCTCAGCCGCGGCCTGACCGCCCTGACCGGTGAGACCGGCGCCGGTAAGACGATGGTGCTCACCTCGCTCGGGCTGCTGCTGGGGCAGCGGGCTGAGACCACCATCGTGCGCACCGGTGCCGAGCGCAGCCTGGTTGAGGGCGCCTTCCTGGTTGACCCGGACTCGCGCGTCGCCGCCCGCGTCGTCGAGGCCGGCGGCGATCTCGACGACGACCTCCTCCTGGCCTCTCGCACGGTCCCCGCCTCCGGACGCTCCCGCGCCTACCTGGGAGGGCGCTCCGTACCGGCCTCGGTCCTCAGTGAGGTGGGCGGCAGGCTGGTCTCCGTCCACGGCCAGGCCGACCAGCTGCGGCTGCGCTCGACCGCGGCCCAACGCGCTGCCCTGGACTCACTTGGCGGTCAGGACCACGCCGCCCTGTGCCGCCGCTACGCCCAGGCCTACCAGGCGCGCCGACAGGCCGACCAGGAGCTCCAGGACTGGCAGGCATCGGCTCAGGCCCGAGCCGTCGAGGTGGCCCAGCTGCGCACCTGGCTCGAGGCCCTGGAGGAGGTCGCCCCCCGCAGCGGTGAGGACCGGGAGCTGACGGCGGAGGCCGAGAGACTCGACCACGCCGAGGACCTGCGCAGAGCCGCCACCGGAGCCCGCACTGCCCTCAGCGGGGAGGAGTCCGCCACCGGGCAGGCGCCCGATGTCGTCTCCCTCATCGCCTACGCGCACCGCAGCCTGAGTGCCGAGTCCGACCGGGACCCCGCCCTGGCTGAGCTGGCCGCGCGCACCCAGCGCCTGGGCATCGACGCAGCCGACATCGCCGCCGAGCTGGGCGGGTACCTGTCCGCGCTGAGCGCCGACCCGGCTCGCCTCGCCCAGGTCCAGGACCGCCGCGGAGAGCTCGCCCGCGCCTGCCGGGAGATCGGCGGACCCCAGGAGCAGCTCGACGACGTCGATGCCCTCCTGGCCTGGGGCGAGCGGGCGGCCGCGCGTCTGGCCGAGCTCGACGGGCCCCAGGACACCGCCACCGTCCTGGCCGAGCGCCTGGCTGCTGCTGACGAGGAGCTGGCCGGTGTTGGTGCCGAGCTGAGCCAGGCCCGTCAGCAGCTCGGCGAGCGTCTTGAGCAGGCCGTCACCGCAGAGCTGGAGGGCCTGGAGATGAAGGGTGCCCGACTCGTCGTCGAGCTGGACCGGCTCGATGAGCCCGGGCCCACCGGCCTGGAGAGCGTTGCCCTCACCCTCGTCTCACACCCCGGCGCACCCGGCCTGCCCCTGGGCAAGGGGGCATCGGGAGGTGAGCTCTCCCGCATCATGCTCGCCCTGGAGGTGGTGCTCGCCGACGCCGCGGCCTTAGCGCGCCCCTCCACCCACACCCGCACCCTCGTCTTCGACGAGATCGACGCCGGGGTGGGAGGCCGGGCCGCCCGGGAGATCGGCAGGAGGCTGGCCCGTCTGGCGCGACACCACCAGGTCATCGTCGTCACCCACCTGGCGCAGGTGGCGGCTTGGGCCGACACCCACCTCGTGGTGCGCAAGGAGACGGTCACCGATGCTGAAGCCCGTCCCAGCTCCGCAGAGACGTCCGCAAGGAATGTGAGAAAGTCCCAGCCAGGACGCACCCGTACACAGGTCTTCGTCGTCGAAGGCCAGGAGAGAGAACGAGAGCTGGCCCGGATGCTCTCCGGGCACGAGGACTCCCAGGCAGCGCTCCGGCACGCCGCTGAGCTTCTCCAGGAAGCAGTCGTGGGACAATCCGAGCCGTGA","VIESLHIEDLGVIEEADLPLSRGLTALTGETGAGKTMVLTSLGLLLGQRAETTIVRTGAERSLVEGAFLVDPDSRVAARVVEAGGDLDDDLLLASRTVPASGRSRAYLGGRSVPASVLSEVGGRLVSVHGQADQLRLRSTAAQRAALDSLGGQDHAALCRRYAQAYQARRQADQELQDWQASAQARAVEVAQLRTWLEALEEVAPRSGEDRELTAEAERLDHAEDLRRAATGARTALSGEESATGQAPDVVSLIAYAHRSLSAESDRDPALAELAARTQRLGIDAADIAAELGGYLSALSADPARLAQVQDRRGELARACREIGGPQEQLDDVDALLAWGERAAARLAELDGPQDTATVLAERLAAADEELAGVGAELSQARQQLGERLEQAVTAELEGLEMKGARLVVELDRLDEPGPTGLESVALTLVSHPGAPGLPLGKGASGGELSRIMLALEVVLADAAALARPSTHTRTLVFDEIDAGVGGRAAREIGRRLARLARHHQVIVVTHLAQVAAWADTHLVVRKETVTDAEARPSSAETSARNVRKSQPGRTRTQVFVVEGQERERELARMLSGHEDSQAALRHAAELLQEAVVGQSEP$","DNA repair protein RecN","Cytoplasm","DNA repair protein RecN","DNA repair protein RecN","DNA repair protein RecN","","Skaar E.P., Lazio M.P., Seifert H.S. Roles of the recJ and recN genes in homologous recombination and DNA repair pathways of Neisseria gonorrhoeae. J. Bacteriol. 2002. 184(4):919-927. PMID: 11807051","","","

InterPro
IPR003395
Domain

SMC protein, N-terminal
PF02463	$\"[1-531]T$	SMC_N

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[21-529]T$	AAA

InterPro
IPR004604
Family

DNA repair protein RecN
TIGR00634	$\"[1-594]T$	recN: DNA repair protein RecN

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[15-165]T$ $\"[445-529]T$	no description

","BeTs to 15 clades of COG0497COG name: ATPases involved in DNA repairFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0497 is -------q-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB001238 (RecF protein) with a combined E-value of 3.3e-06. IPB001238A 5-52","Residues 95-152 are similar to a (REPAIR DNA RECOMBINATION RECN GENETIC N ATP-BINDING USED ATPASES INVOLVED) protein domain (PD348650) which is seen in Q6AGG6_BBBBB.Residues 180-306 are 44% similar to a (GENETIC DNA REPAIR RECOMBINATION) protein domain (PDA0M4P9) which is seen in Q72IH1_THET2.Residues 305-400 are 53% similar to a (REPAIR DNA RECOMBINATION RECN GENETIC N ATP-BINDING USED ATPASES INVOLVED) protein domain (PD863813) which is seen in Q829B2_STRAW.Residues 402-509 are 68% similar to a (REPAIR DNA RECOMBINATION RECN GENETIC N ATP-BINDING USED ABC ATPASES) protein domain (PD431423) which is seen in Q8FTL5_COREF.Residues 510-595 are 58% similar to a (REPAIR DNA RECOMBINATION RECN GENETIC N ATP-BINDING USED ABC ATPASES) protein domain (PD684756) which is seen in RECN_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 531 (E_value = 1.8e-06) place ANA_1006 in the SMC_N family which is described as RecF/RecN/SMC N terminal domain.","","repair protein RecN (recN)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1009","1085330","1084371","960","4.98","-12.97","33831","ATGCTGCTGCAGCGCGAGCTCAACGACAAGCCCGTCCCCGTCCCCAGGCCCAGTGCTCCCACGGCCAGCGCCGTGGCCCGGGCCTCGGAGGCGCTGCGCGCCCGAGGAGTTGAGCCAGTCGGCCCGGACTGCACCGACCACGTCGACCTCGTCCTGGTGCTCGGCGGCGACGGCACGATCCTGCGCGCCTTCGAGATCGCCCGCGAACGCGACATCCCCCTGGTAGGCATCAACACCGGCCACGTTGGCTTCCTGGCCGAGGCCGACCCCGACGGTATCGAGCAGGTCGTCGCGGATCTGGTCGCCGGCCACTACACGGTCGAGACCCGCACCACCTTGGACGTGGAGGTCATCTGTCCTGACGGGACAGTCACACGCGACTGGGCACTCAACGAGGCGGCCCTGGAGAAGCGCGACCGCGCCCGCATGATCGAGGTCGCCATCGGCGTTGACGGCCAGGCCGTGTCCTCCTTCGGCTGCGACGGCCTCATCATGTCCACCCCCACCGGCTCGACCGCCTACGCCTTCTCCTGTGGTGGCCCCGTCATCTGGCCCGAGGTCGAGGCGCTCCTCCTGGTGCCCGTGGCTGCGCACGCCCTGTTCACCCGCCCCCTGGTCCTGGGCCCCAACTCCTGCATGGAGGTCGTCGTCCAGCGGGTGGGCTTCGGAGGTGCCGAGATCTGGTGCGATGGCAGACGCAGCCTGGACGTGCCGGTCGGCGCCAGGATCCGGGTCACCCGAGCGGCGCGTCCGGTACGCCTGGCACGTTTCAACCAGGCCCCCTTCGCCAGCCGCCTGGTGCGCAAGTTCGACCTGCCCGTGGAGGGCTGGCGGGCCTCCAGCAGCGCCGATGAGGCCTACTCACCCGAGGAGGACGCGCTGCACCAGCCAATGGACACCTCCGCTGACACGAGCACCGACGGCGGGAGCCGGCCGGACTCCTCGGGAGGCACGGCGTGA","MLLQRELNDKPVPVPRPSAPTASAVARASEALRARGVEPVGPDCTDHVDLVLVLGGDGTILRAFEIARERDIPLVGINTGHVGFLAEADPDGIEQVVADLVAGHYTVETRTTLDVEVICPDGTVTRDWALNEAALEKRDRARMIEVAIGVDGQAVSSFGCDGLIMSTPTGSTAYAFSCGGPVIWPEVEALLLVPVAAHALFTRPLVLGPNSCMEVVVQRVGFGGAEIWCDGRRSLDVPVGARIRVTRAARPVRLARFNQAPFASRLVRKFDLPVEGWRASSSADEAYSPEEDALHQPMDTSADTSTDGGSRPDSSGGTA$","ATP-NAD/AcoX kinase","Cytoplasm","poly(P)/ATP-NAD kinase","NAD(+) kinase ","ATP-NAD/AcoX kinase","","","","","

InterPro
IPR002504
Family

ATP-NAD/AcoX kinase
PF01513	$\"[14-257]T$	NAD_kinase

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.30	$\"[118-247]T$	no description
G3DSA:3.40.50.10330	$\"[46-115]T$	no description
PTHR20275	$\"[43-307]T$	POLY(P)/ATP NAD KINASE

","BeTs to 24 clades of COG0061COG name: Predicted kinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0061 is aompkzyqv-rlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 1","***** IPB002504 (ATP-NAD kinase) with a combined E-value of 1.3e-29. IPB002504A 49-61 IPB002504B 73-87 IPB002504C 161-183","Residues 46-137 are 68% similar to a (KINASE NAD TRANSFERASE INORGANIC POLYPHOSPHATE/ATP-NAD PROBABLE NADP POLYP/ATP PREDICTED SUGAR) protein domain (PD120253) which is seen in PPNK_MYCTU.Residues 142-256 are similar to a (KINASE NAD TRANSFERASE INORGANIC POLYPHOSPHATE/ATP-NAD PROBABLE NADP POLYP/ATP PREDICTED SUGAR) protein domain (PD002781) which is seen in Q8VUL9_MICLU.","","-63% similar to PDB:1U0R Crystal structure of Mycobacterium tuberculosis NAD kinase (E_value = 2.1E_63);-63% similar to PDB:1U0T Crystal structure of Mycobacterium tuberculosis NAD kinase (E_value = 2.1E_63);-63% similar to PDB:1Y3I Crystal Structure of Mycobacterium tuberculosis NAD kinase-NAD complex (E_value = 2.1E_63);-63% similar to PDB:1Y3H Crystal Structure of Inorganic Polyphosphate/ATP-NAD kinase from Mycobacterium tuberculosis (E_value = 3.7E_63);-51% similar to PDB:2AN1 Structural Genomics, The crystal structure of a putative kinase from Salmonella typhimurim LT2 (E_value = 2.5E_27);","Residues 14 to 257 (E_value = 4.3e-63) place ANA_1009 in the NAD_kinase family which is described as ATP-NAD kinase.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1010","1086328","1085456","873","7.25","0.85","30514","ATGGCCAGGCTCATCCGCATCGACTCAGAGCTCGTGCGCCGCGGGCTGGCCCGCTCCCGCACCCACGCCGCCACGCTCATCGCCGACGGTCACGTCACCCTCGACGGCGAGGTCGTCACCAAACCCGCCCGTCAGGTCAACCCGGCCCAGGCCATCGAGATCCTGGTGCCCTCAGCAGACGACTACGTCTCCCGCGGTGCCCACAAGCTCGCCGGCGCGCTGGATGCGCTGGGCCGCCGCGGCCTGGCACCCCGCGTCGAGGGACGCCGCTGCCTGGACGCCGGCGCCTCGACCGGCGGCTTCACCGACGTCCTCCTGCGCCGCGGTGCTGAGCACGTCGTGGCCGTCGACGTCGGCTACGGCCAGCTGGCCTGGTCGCTGCGCTCCGACCCCCGCGTCACCGCCCTGGACCGTACCAACATCCGCACACTGGATCCCGAGGTCGTCGCCCCCGCCCCGGAGCTGGTCGTGGGCGATCTGTCCTTCATCTCCCTGACCCTGGTCCTCGAACCGCTGCTGCGCGCCGCGGCCGACGACGCCGACCTCCTGCTCATGGTCAAGCCCCAGTTCGAGGTGGGCAAGGACCGGGTCGGGCACGGGGGAGTGGTGCGCGACCCAGAGCTCCATGTGGCCACCGTCATGACGGTGGCCGAGCGGGCCCATGCTCTGGGTGTGGGAGTCGAGGCCGTGACCGCCTCCCCTCTGCCGGGGCCCGCCGGTAACGTTGAGTACTTCCTGAGCATGCACGCCTCCCGCGCCGGTTGCCCCGGGGACCTGAGCGGGGACGAGCTGCGCTCCAGCATCGAGGACGCCGTCGCCGCCGGCCCCGCGGCGGGCGGTGCGCGACGACGCAGAACAAGGACCCGCCCATGA","MARLIRIDSELVRRGLARSRTHAATLIADGHVTLDGEVVTKPARQVNPAQAIEILVPSADDYVSRGAHKLAGALDALGRRGLAPRVEGRRCLDAGASTGGFTDVLLRRGAEHVVAVDVGYGQLAWSLRSDPRVTALDRTNIRTLDPEVVAPAPELVVGDLSFISLTLVLEPLLRAAADDADLLLMVKPQFEVGKDRVGHGGVVRDPELHVATVMTVAERAHALGVGVEAVTASPLPGPAGNVEYFLSMHASRAGCPGDLSGDELRSSIEDAVAAGPAAGGARRRRTRTRP$","Hemolysin A","Cytoplasm, Extracellular","hemolysin A","K06442 putative hemolysin","hemolysin A","","Tan J., Jakob U., Bardwell J.C. Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. J. Bacteriol. 2002. 184(10):2692-2698. PMID: 11976298Bugl H., Fauman E.B., Staker B.L., Zheng F., Kushner S.R., Saper M.A., Bardwell J.C., Jakob U. RNA methylation under heat shock control. Mol. Cell 2000. 6(2):349-360. PMID: 10983982","","","

InterPro
IPR002877
Domain

Ribosomal RNA methyltransferase RrmJ/FtsJ
PF01728	$\"[62-252]T$	FtsJ

InterPro
IPR002942
Domain

RNA-binding S4
PF01479	$\"[5-52]T$	S4
SM00363	$\"[5-71]T$	S4
PS50889	$\"[5-67]T$	S4

InterPro
IPR004538
Family

Hemolysin A
TIGR00478	$\"[6-243]T$	tly: hemolysin A

noIPR
unintegrated

unintegrated
G3DSA:3.10.290.10	$\"[4-54]T$	no description

","BeTs to 12 clades of COG1189COG name: Predicted rRNA methylasesFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1189 is a------qv-rlbc------ujx-twNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 4-82 are 58% similar to a (FOUND HEMOLYSIN-LIKE PLANTS S4 WITH BACTERIA DOMAIN) protein domain (PD947047) which is seen in Q8G5G4_BIFLO.Residues 6-54 are 71% similar to a (TLYA CYTOTOXIN/HEMOLYSIN HAEMOLYSIN RRNA PREDICTED MEMBRANE HOMOLOGUE METHYLTRANSFERASE MLC1351.14C METHYLASE) protein domain (PD402872) which is seen in Q9S218_STRCO.Residues 11-70 are 70% similar to a (HEMOLYSIN) protein domain (PD947060) which is seen in Q6AGB9_BBBBB.Residues 92-123 are 93% similar to a (HEMOLYSIN A HEMOLYSIN-LIKE RRNA METHYLTRANSFERASE CELL TLYA PREDICTED METHYLASE HAEMOLYSIN) protein domain (PDA0Q5D1) which is seen in Q9S218_STRCO.Residues 127-217 are similar to a (HEMOLYSIN A HEMOLYSIN-LIKE RRNA TLYA METHYLTRANSFERASE CELL PREDICTED METHYLASE HAEMOLYSIN) protein domain (PD007579) which is seen in Q6NHF8_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 52 (E_value = 4.9e-13) place ANA_1010 in the S4 family which is described as S4 domain.Residues 62 to 252 (E_value = 0.00011) place ANA_1010 in the FtsJ family which is described as FtsJ-like methyltransferase.","","A ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1011","1086315","1086590","276","11.56","7.59","9787","ATGAGCCTGGCCATATCAGCCTTCCGCCTTGTGCAGGACGGAGGCGAGGTCCTCGTGAATGGCGGCCAGGGCGGCTGCGCGCTGCTCCAGGGGCATCTGAGCGATCTGGGCGAGCTCATCGGTGTGGTCATGGAGCCCTTGGGCCGCCGTCAGGGCGACGTCGGCACGCGGAGGCGCAGGCACCGGCGGCCGAGGAGCAGGCCGGAGCGCGGAGTCCGACGTTGCGGGCTTCTCCTCCCCGACGTCGGTTCTCGCCTCGTTGCCGCTCATTCCTGA","MSLAISAFRLVQDGGEVLVNGGQGGCALLQGHLSDLGELIGVVMEPLGRRQGDVGTRRRRHRRPRSRPERGVRRCGLLLPDVGSRLVAAHS$","Hypothetical protein","Membrane, Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Mueckler M., Caruso C., Baldwin S.A., Panico M., Blench I., Morris H.R., Allard W.J., Lienhard G.E., Lodish H.F. Sequence and structure of a human glucose transporter. Science 1985. 229(4717):941-945. PMID: 3839598Maiden M.C., Davis E.O., Baldwin S.A., Moore D.C., Henderson P.J. Mammalian and bacterial sugar transport proteins are homologous. Nature 1987. 325(6105):641-643. PMID: 3543693Kayano T., Fukumoto H., Eddy R.L., Fan Y.S., Byers M.G., Shows T.B., Bell G.I. Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues. J. Biol. Chem. 1988. 263(30):15245-15248. PMID: 3170580","","","

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[40-56]?$	SUGAR_TRANSPORT_1

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[24-250]T$	Hydrolase

InterPro
IPR006357
Family

HAD-superfamily hydrolase, subfamily IIA
TIGR01460	$\"[27-250]T$	HAD-SF-IIA: HAD-superfamily hydrolase, subf

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[8-278]T$	no description
PTHR19288	$\"[14-284]T$	4-NITROPHENYLPHOSPHATASE-RELATED
PTHR19288:SF3	$\"[14-284]T$	N-ACETYLGLUCOSAMINE-6-PHOSHATASE (P-NITROPHENYL PHOSPHATASE)

","BeTs to 12 clades of COG0647COG name: Predicted sugar phosphatases of the HAD superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0647 is ao--kzyqv-rlb-ef----ujx---Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 24-102 are similar to a (HYDROLASE PHOSPHATASE NAGD 4-NITROPHENYLPHOSPHATASE HALOACID N-ACETYL-GLUCOSAMINE DEHALOGENASE-LIKE HYDROLASE HAD TRANSFERASE) protein domain (PD005233) which is seen in Q829C1_STRAW.Residues 104-155 are similar to a (HYDROLASE PHOSPHATASE SUGAR HAD PROBABLE THE SUPERFAMILY SCO1788 4-NITROPHENYLPHOSPHATASE PREDICTED) protein domain (PD846218) which is seen in Q6AHC9_BBBBB.Residues 159-201 are similar to a (HYDROLASE PHOSPHATASE NAGD N-ACETYLGLUCOSAMINE SUGAR N-ACETYL-GLUCOSAMINE HALOACID METABOLISM DEHALOGENASE-LIKE HYDROLASE) protein domain (PD355291) which is seen in Q8NQM4_CORGL.Residues 204-276 are similar to a (HYDROLASE 4-NITROPHENYLPHOSPHATASE CEREVISIAE HAD SUPERFAMILY SACCHAROMYCES PHOSPHATASE TRANSFERASE PHO13 N-ACETYL-GLUCOSAMINE) protein domain (PD286054) which is seen in Q829C1_STRAW.","","-52% similar to PDB:1ZJJ Crystal structure of hypothetical protein PH1952 from Pyrococcus horikoshii OT3 (E_value = 7.0E_29);-50% similar to PDB:1YDF Crystal Structure of a Hypothetical protein, hydrolase haloacid dehalogenase-like family (E_value = 1.8E_24);-49% similar to PDB:1WVI Crystal structure of putative phosphatase from Streptococcus mutans UA159 (E_value = 6.8E_24);-47% similar to PDB:1YV9 Crystal Structure of a Hypothetical protein from hydrolase haloacid dehalogenase-like family (E_value = 4.4E_23);-45% similar to PDB:1YS9 Crystal sructure of hypothetical protein SPy1043 from Streptococcus pyogenes (E_value = 1.4E_21);","Residues 24 to 250 (E_value = 1.1e-10) place ANA_1012 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","sugar phosphatases of the HAD superfamily (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1014","1089120","1087771","1350","5.23","-25.56","50244","ATGGCGTATCAGGACCGTCAGCACGGCTCGGACCACGGCGAGACAGGTCGGCGTCGCCACAATGGCGAGCGTCACGGCTTCGGAGCGCGTCACCGTTCCGCAGGGGAAGACGCTCACTCTCGCCGTAGCGGACGCCCGGGACGGGACGATGACTCCTACGGCTCGCGGGGACGTTCCGAGCGGTCGAGCCGCGGGGAGCACTCTTCGCACAATGATCGCCGGCGCCGCGACGACTGGCGTGACGAACGGCGTCGTGATGGTGAGAACGGTGATAGGCGCGGCGGCCGTCATGGTCGCAGGCCTGGGCGTGTCAACGACCGCTCCGGACGGAAGGACTCGCGTGGCAGGCGTGATGACCGGAGTGGTCGTCCACCGCAGCGTCAGCGCGTCCCCGAGCCCACGGTTCCGGACAACGTCGAGCCTGCAGATCTTGAACGCGGCGCCAGGGCCGAGCTGCGCGCCCTGGGGCGTGCCAACGCTGAGAACGTCGCCCGGCACCTGGTCATGGTTCAGCGCCTCCTCAACGACGATCCTCAAGCCGCCTACGAGCACGCGCGCTACGCCGCCTCCCATGCGGGCCGTGTCGCCGTCGTCCGGGAGACGGCAGGAATCGCGGCATATCTCGCCGGCCACTACAGCGAGGCGCTCCGAGAGATTCGCGCCGCCAGGCGCCTGTCCGGTCTTGACCTGCACCGGGCCATCGAGGTCGACTGCGAGCGTGCACTGGGCAACCTCGACAAGGCCCTCCAAGCCGCTCAAGCGGCAGACCCGCGCCAGCTCGACGAGATCGAACGGGCCGAGTTGGCCATGGTCGTCTCCAGTCTTCGCCATGACATGGGCCAGACCGATCTTGGCCTGCTCATCATCGAGGACGCCATCAGGGCGCGTCCCTCCGACAGTGACACCCTCAGACGCCTGCACTCGGTGCGTGCCGACCGGCTCGAAGAGCTCGGACGCAACCGGGAGGCTGAGGCCATCCGTGACCGGATCGGTCCAGAGCCGGTGGAGGAGGACGAGGTCGAGGTCTTCGACATCGAGGACGACTACGACTCCGAGACCCACGAAGAGAGCACCTCGGAGAGTTCCGGCACTCAGCCCGCCACCGATTCTGATGGTGACACGAATGACGAGGCGGTGAGCGAGACGACCGAGACCTCACAGGCTCCTGGAGAGGCGGCTCAGGACGAGGCCTCACTGGACATCGAGGAGCACGACGAGCCTGTGGACCGGGACGAGGACGCTCAGTGGTCGCAGTCCTTCGCCGAGCGCGTCGAGGCCGAGATGGCCGAGCTGCTCCAGGACGCGCAGGACACGTCGACGCCTTCCGCAAACACCTCTGAGGAGCCCTGA","MAYQDRQHGSDHGETGRRRHNGERHGFGARHRSAGEDAHSRRSGRPGRDDDSYGSRGRSERSSRGEHSSHNDRRRRDDWRDERRRDGENGDRRGGRHGRRPGRVNDRSGRKDSRGRRDDRSGRPPQRQRVPEPTVPDNVEPADLERGARAELRALGRANAENVARHLVMVQRLLNDDPQAAYEHARYAASHAGRVAVVRETAGIAAYLAGHYSEALREIRAARRLSGLDLHRAIEVDCERALGNLDKALQAAQAADPRQLDEIERAELAMVVSSLRHDMGQTDLGLLIIEDAIRARPSDSDTLRRLHSVRADRLEELGRNREAEAIRDRIGPEPVEEDEVEVFDIEDDYDSETHEESTSESSGTQPATDSDGDTNDEAVSETTETSQAPGEAAQDEASLDIEEHDEPVDRDEDAQWSQSFAERVEAEMAELLQDAQDTSTPSANTSEEP$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","***** IPB013957 (Protein of unknown function DUF1777) with a combined E-value of 1.2e-06. IPB013957A 82-125 IPB013957A 78-121 IPB013957A 51-94 IPB013957A 54-97 IPB013957A 74-117 IPB013957A 80-123 IPB013957A 56-99 IPB013957A 57-100 IPB013957A 71-114 IPB013957A 17-60 IPB013957A 60-103 IPB013957A 84-127 IPB013957A 73-116 IPB013957A 45-88 IPB013957A 49-92 IPB013957A 55-98 IPB013957A 72-115 IPB013957A 46-89 IPB013957A 81-124 IPB013957A 41-84 IPB013957A 47-90 IPB013957A 53-96 IPB013957A 5-48 IPB013957A 62-105 IPB013957A 43-86 IPB013957A 85-128 IPB013957A 37-80 IPB013957A 76-119 IPB013957A 59-102 IPB013957A 27-70 IPB013957A 87-130 IPB013957A 29-72 IPB013957A 39-82 IPB013957A 83-126 IPB013957A 31-74 IPB013957A 77-120 IPB013957A 35-78 IPB013957A 25-68 IPB013957A 42-85 IPB013957A 89-132 IPB013957A 50-93 IPB013957A 63-106 IPB013957A 91-134 IPB013957A 33-76 IPB013957A 52-95 IPB013957A 86-129 IPB013957A 23-66 IPB013957A 79-122 IPB013957A 38-81 IPB013957A 75-118 IPB013957A 48-91 IPB013957A 36-79 IPB013957A 61-104 IPB013957A 64-107 IPB013957A 69-112 IPB013957A 70-113 IPB013957A 90-133 IPB013957A 68-111 IPB013957A 93-136 IPB013957A 19-62 IPB013957A 58-101 IPB013957A 94-137 IPB013957A 21-64 IPB013957A 95-138 IPB013957A 67-110 IPB013957A 44-87 IPB013957A 16-59 IPB013957A 40-83 IPB013957A 15-58 IPB013957A 96-139 IPB013957A 65-108 IPB013957A 14-57 IPB013957A 98-141 IPB013957A 66-109 IPB013957A 11-54 IPB013957A 92-135 IPB013957A 7-50 IPB013957A 28-71","Residues 168-323 are similar to a (MB1717 SCO1790 CGL1409) protein domain (PD358388) which is seen in Q8FTL9_COREF.","","-45% similar to PDB:1MOJ Crystal structure of an archaeal dps-homologue from Halobacterium salinarum (E_value = );-45% similar to PDB:1TJO Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states (E_value = );-45% similar to PDB:1TK6 Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states (E_value = );-45% similar to PDB:1TKO Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states (E_value = );-45% similar to PDB:1TKP Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1018","1096593","1095331","1263","5.58","-11.19","45325","GTGACGGACATCCTGGACGAACTGCAGTGGCGCGGGCTCATCGCCCAGCACACCGACATTGACGCGCTGCGAGCGGCGCTCAGCGACGGGGCCGTCACCTTCTATTGCGGGTTCGACCCCACGGCGCCGAGCCTTCACCACGGGCACCTCGTAGCCGTCAAGGTCATGCGCCATCTTCAGCTGGCCGGGCACCGTCCGCTGGCGCTGGTGGGTGGGGCGACCGGCCTCATCGGCGACCCGCGCGCCAAGGGGGAGCGCAGCCTCAACACCAAGGACGTCGTTGCCGGCTGGGCGGCCAGCCTGCAGGAACAGCTCGAGAACCTTCTCGACTTCAGCGGGGACAACCCGGCGCAGATTGTCAACAACCTGGACTGGACCCAGGCGATGAGCGCCATTGACTTCCTGCGGGACCTGGGCAAGCACTTCCGCATGGGCACCATGCTCTCCAAGGACATCGTCGCCCGGCGCCTGGCCAGCGAGGAGGGCATCTCCTACACCGAGTTCAGCTACCAGGTCCTCCAGGCCAACGACTACCTCGAGCTCTACCGACGCTACGGCTGCACCCTGGAGGTCGGCGGCAACGACCAGTGGGGCAACCTCGTGGGCGGGATGGACCTCATCCACAAGGTCGAGGGCGCCTCGGTCCACGTCATGACCAACCCCCTCATCACCAAGGCCGACGGCACCAAGTTCGGTAAGTCCGAGGGCGGGGCGATCTGGCTCAACCCCGAGATGCTCAGCCCCTACGGCTTCTACCAGTTCTGGCTCCAGGTCGACGACGCCGACGTTGTGCGCTTCCTCAAGGTCTTCACCTTCCTGGAGCGCGAGGAGATTGAGCGCCTGGAGGCGGTGACGGCCGAGAACCCGAAGGCACGTGAGGCGCAGCGGGTTCTGGCGCACGAAGTCTGCACGTGGGTCCACGGAGCCGGCGCGACTGCCCAGGCCGAAGCGGCGACCTCCGCACTGTGGGGCCGCGGCGACCTCGCCGACATCGATGAGGCGACGATCCTGGCGGCTACGGCTGATCTCGCCTCCGGTGACGTGACAGTCGGACAGACCACGATCGTGGACCTGCTTGTGGGCACGGGGCTGGAGCGCGGGCGCAATGCGGCCCGCAAAACCATTGCCGGAGGCGGGGCCTACATCAACAACGTCAAGGTGGCCGACGAGACCGCGGTCATCGGTCCCGAGCATCTGCTCGCCGGGGGAGTGGTGCTGGTGCGCAAGGGACGGCGGAACCTAGCCGTCGGACGTGCGGCTTAG","VTDILDELQWRGLIAQHTDIDALRAALSDGAVTFYCGFDPTAPSLHHGHLVAVKVMRHLQLAGHRPLALVGGATGLIGDPRAKGERSLNTKDVVAGWAASLQEQLENLLDFSGDNPAQIVNNLDWTQAMSAIDFLRDLGKHFRMGTMLSKDIVARRLASEEGISYTEFSYQVLQANDYLELYRRYGCTLEVGGNDQWGNLVGGMDLIHKVEGASVHVMTNPLITKADGTKFGKSEGGAIWLNPEMLSPYGFYQFWLQVDDADVVRFLKVFTFLEREEIERLEAVTAENPKAREAQRVLAHEVCTWVHGAGATAQAEAATSALWGRGDLADIDEATILAATADLASGDVTVGQTTIVDLLVGTGLERGRNAARKTIAGGGAYINNVKVADETAVIGPEHLLAGGVVLVRKGRRNLAVGRAA$","Tyrosyl-tRNA synthetase","Cytoplasm","tyrosyl-tRNA synthetase","tyrosyl-tRNA synthetase ","tyrosyl-tRNA synthetase","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Aravind L., Koonin E.V. Novel predicted RNA-binding domains associated with the translation machinery. J. Mol. Evol. 1999. 48(3):291-302. PMID: 10093218","","","

InterPro
IPR002305
Domain

Aminoacyl-tRNA synthetase, class Ib
PF00579	$\"[27-324]T$	tRNA-synt_1b

InterPro
IPR002307
Family

Tyrosyl-tRNA synthetase, class Ib
PR01040	$\"[44-66]T$ $\"[162-177]T$ $\"[183-205]T$ $\"[216-228]T$	TRNASYNTHTYR
PTHR11766	$\"[1-420]T$	TYROSYL-TRNA SYNTHETASE
TIGR00234	$\"[1-420]T$	tyrS: tyrosyl-tRNA synthetase

InterPro
IPR002942
Domain

RNA-binding S4
PS50889	$\"[353-418]T$	S4

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[3-222]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.240.10	$\"[223-324]T$	no description

","BeTs to 20 clades of COG0162COG name: Tyrosyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0162 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002307 (Tyrosyl-tRNA synthetase signature) with a combined E-value of 2.3e-33. IPB002307A 44-66 IPB002307B 162-177 IPB002307C 183-205 IPB002307D 216-228***** IPB002305 (Aminoacyl-tRNA synthetase, class Ib) with a combined E-value of 5.2e-15. IPB002305A 38-52 IPB002305B 131-147 IPB002305C 190-211 IPB002305D 226-239","Residues 5-60 are 76% similar to a (SYNTHETASE AMINOACYL-TRNA TYROSYL-TRNA LIGASE TYRRS TYROSINE--TRNA BIOSYNTHESIS ATP-BINDING TRNA SYNTHETASE) protein domain (PD131900) which is seen in Q8G5G1_BIFLO.Residues 62-164 are similar to a (SYNTHETASE AMINOACYL-TRNA TYROSYL-TRNA LIGASE TYROSINE--TRNA TYRRS BIOSYNTHESIS ATP-BINDING TYROSINE-TRNA TRNA) protein domain (PD005447) which is seen in Q8G5G1_BIFLO.Residues 94-178 are 61% similar to a (KINASE ATP-BINDING TRANSFERASE BINDING REPEAT SUBUNIT DNA RNA POLYMERASE NUCLEOMORPH) protein domain (PD012172) which is seen in Q8D2L6_WIGBR.Residues 172-243 are 86% similar to a (SYNTHETASE AMINOACYL-TRNA TYROSYL-TRNA LIGASE TYROSINE--TRNA TYRRS BIOSYNTHESIS ATP-BINDING TYROSINE-TRNA TRNA) protein domain (PD131906) which is seen in Q9RJ50_STRCO.Residues 239-307 are 68% similar to a (SYNTHETASE AMINOACYL-TRNA TYROSYL-TRNA LIGASE TYROSINE--TRNA TYRRS BIOSYNTHESIS ATP-BINDING TYROSINE-TRNA PEPTIDE) protein domain (PD040475) which is seen in SYY_BACST.Residues 354-415 are 66% similar to a (SYNTHETASE AMINOACYL-TRNA TYROSYL-TRNA LIGASE TRNA TYROSINE-TRNA TYROSINE--TRNA TYROSYL TYRRS TYROSINE) protein domain (PD863508) which is seen in Q8FTM1_COREF.Residues 364-415 are 73% similar to a (SYNTHETASE AMINOACYL-TRNA TYROSYL-TRNA LIGASE TYROSINE--TRNA ATP-BINDING TYRRS BIOSYNTHESIS TYROSYL TRNA) protein domain (PD004483) which is seen in Q829F2_STRAW.","","-63% similar to PDB:2TS1 STRUCTURE OF TYROSYL-T/RNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE (E_value = 1.5E_110);-63% similar to PDB:3TS1 STRUCTURE OF TYROSYL-T/RNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE (E_value = 1.5E_110);-70% similar to PDB:1TYA STRUCTURAL ANALYSIS OF A SERIES OF MUTANTS OF TYROSYL-TRNA SYNTHETASE: ENHANCEMENT OF CATALYSIS BY HYDROPHOBIC INTERACTIONS (E_value = 1.3E_98);-70% similar to PDB:1TYD STRUCTURE OF TYROSYL-TRNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE (E_value = 2.9E_98);-70% similar to PDB:1TYB STRUCTURAL ANALYSIS OF A SERIES OF MUTANTS OF TYROSYL-TRNA SYNTHETASE: ENHANCEMENT OF CATALYSIS BY HYDROPHOBIC INTERACTIONS (E_value = 3.8E_98);","Residues 27 to 324 (E_value = 3.6e-104) place ANA_1018 in the tRNA-synt_1b family which is described as tRNA synthetases class I (W and Y).","","synthetase (tyrS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1019","1097372","1096758","615","10.34","9.07","22526","GTGGCCAGTGACTACTGGAACCACAACGTCGCCTTTCACCGGCGCATCGCGCGGGACGCGGCGCTGCGCGGTGGAAGCGCGCTCGATGTCGGATGCGGTGACGGGCTCCTGCTCGCACGCCTGACGGCGGTGTGCCGGCGCGCCGTCGGACTTGAAACCGACGGGCAGGCAGTTGCTCGAGCGCGCAGACGTCTCGAACGGACTCCGCAGGCCGAGGTGCTGCTCGACGACGTCATGGATCTGGACCTTCCTCAGCGCATCGGCACCTTTGAGACGGTCACCTGCGTGGCCACGCTGCACCACCTCCCACTGGAACCCGCCCTGGTGAGGCTGAGTCAGCTGGTGGCACCCGGCGGGCGTCTGATCGTCGTCGGCTTGGCCGCCAACAAGAGCCTGTGGGACTGGACGCTGTCCGCACTGGCCGTCCTGCCTCTGCACGTGGTCGGCGCCCTGCGACGGGAGAGCTCAGACATCGGTGTGGTCACTCGTGTTCCACGAGAGTCCCTGGCCGAGATTCGTCGGGCGGCAGTCCGGCTGCTTCCCGGGGCCAGGACTCGACGGCGCTTCTACTACCGATACACCCTCATATGGGATCGCCCGACTGAGGGCTCGTGA","VASDYWNHNVAFHRRIARDAALRGGSALDVGCGDGLLLARLTAVCRRAVGLETDGQAVARARRRLERTPQAEVLLDDVMDLDLPQRIGTFETVTCVATLHHLPLEPALVRLSQLVAPGGRLIVVGLAANKSLWDWTLSALAVLPLHVVGALRRESSDIGVVTRVPRESLAEIRRAAVRLLPGARTRRRFYYRYTLIWDRPTEGS$","SAM-dependent methyltransferase","Cytoplasm","conserved hypothetical protein","hypothetical protein","Methyltransferase type 11","","","","","

InterPro
IPR013216
Domain

Methyltransferase type 11
PF08241	$\"[28-123]T$	Methyltransf_11

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[9-139]T$	no description
PTHR10108	$\"[28-124]T$	METHYLTRANSFERASE
PTHR10108:SF26	$\"[28-124]T$	METHLYTRANSFERASE, UBIE/COQ5 FAMILY

","BeTs to 11 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 6","***** IPB008715 (NodS) with a combined E-value of 2.5e-08. IPB008715B 30-64","Residues 89-200 are similar to a (METHYLTRANSFERASE SAM-DEPENDENT TRANSFERASE SCO2653 CGL2556) protein domain (PD444733) which is seen in Q8NML7_CORGL.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 170 (E_value = 0.00099) place ANA_1019 in the NodS family which is described as Nodulation protein S (NodS).Residues 28 to 123 (E_value = 5.4e-15) place ANA_1019 in the Methyltransf_11 family which is described as Methyltransferase domain.Residues 28 to 121 (E_value = 8.3e-15) place ANA_1019 in the Methyltransf_12 family which is described as Methyltransferase domain.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1020","1097922","1097362","561","7.45","0.65","19743","GTGAAGACACGGTTCCAGGGTCCTGAGGCGAGCCCCGGCTTCCTCATGTGGAGGGCCGCGCTGGCCTGGCAGCGAGACATCGCTGCCGCCCTGGAGCCAGTTGGACTGACACACTCCCAGTTCGTCCTCCTGGCCTGCACGCAGTGGCTCGAGGAGCACGGGGACGGGGCCAGCCAGGTGATGGTCGCGACCCAGGCGGGGATCGACGTGAAGACCACCAGCCAGGTGCTGCGCCGGCTGGAGCGGGCCGGTCTGGTGTCGCGGCAGCTGGATCCCAAGGACGCCCGTGCCCGGATCGTGACCATGACGCCGGCAGGCAGAGATGTCGGGGCCCGGGCAACGCGTCTGGTGGAGGACGCCGATGAGGCGTACTTCGCAGCAGTGCCCCACCTGCGCGAGGCACTGCTGCGTGAAGCCGGCGTCGTAGCGCGCGGATCAGCGACGCAGCCCAACCAGGAGACCGCTGCGTCTACCGACCGGGCTGAGAGCCCCAAGACCTCGAGCGACACAGCCAGTCCGACCACGGCGGCTGCTCCACCAGGCTCCCGCAGTGGCCAGTGA","VKTRFQGPEASPGFLMWRAALAWQRDIAAALEPVGLTHSQFVLLACTQWLEEHGDGASQVMVATQAGIDVKTTSQVLRRLERAGLVSRQLDPKDARARIVTMTPAGRDVGARATRLVEDADEAYFAAVPHLREALLREAGVVARGSATQPNQETAASTDRAESPKTSSDTASPTTAAAPPGSRSGQ$","Transcriptional regulator, MarR family","Cytoplasm, Periplasm, Extracellular","transcription regulator","putative transcriptional regulator","regulatory protein, MarR","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR000835
Family

Bacterial regulatory protein, MarR
PF01047	$\"[36-109]T$	MarR
SM00347	$\"[29-133]T$	HTH_MARR
PS50995	$\"[9-145]T$	HTH_MARR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[36-113]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide

","BeTs to 9 clades of COG1846COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1846 is aompkz--vdrlb-efg-sn-j----Number of proteins in this genome belonging to this COG is 6","***** IPB000835 (Bacterial regulatory protein, MarR family) with a combined E-value of 1e-11. IPB000835 73-106","Residues 3-64 are similar to a (REGULATION DNA-BINDING TRANSCRIPTION TRANSCRIPTIONAL REGULATOR YDCH MARR FAMILY REGULATOR) protein domain (PD751751) which is seen in P96625_BACSU.Residues 11-69 are similar to a (TRANSCRIPTION REGULATION DNA-BINDING TRANSCRIPTIONAL REGULATOR SLYA ACTIVATOR REPRESSOR MARR FAMILY) protein domain (PD581714) which is seen in Q98E58_RHILO.Residues 70-128 are similar to a (TRANSCRIPTION REGULATOR REGULATION DNA-BINDING) protein domain (PD749074) which is seen in Q98E58_RHILO.","","No significant hits to the PDB database (E-value < E-10).","Residues 36 to 109 (E_value = 2.8e-12) place ANA_1020 in the MarR family which is described as MarR family.","","regulator ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1021","1098344","1097919","426","4.33","-14.58","15360","ATGTGGTCGACTGAGTGCCAACGGACAGTGGATCTCCCGGCGGAGGTCCTGTGGGAGACCTGGATCAAGGTTCTCTCCGGTGACATCGAGCTCCCCCAGGGAGATCGCTACGAGCCGCGCGAGCCTGTGGGACCCGGCGCCTCGATCACGATGACTCCGGAGGGGCAGGACAGTATCGAGATCACGGTGATCCGCTGGGAACCCCCTCATGTCCAGGCGGACCGGGTCTCCTACGGGGGAGTGGAGCTGACCTTCACCCACTCCTTCATGCCCGCGCAGACACAAGGGAAGAGCGTTGTGACCACCCGCCTCGACATCGACGGCCCCGGTGCCGACGATGTAGGCCCGACGATCGGTCCGGGAATCGCCGAGGACTTTCCGCAGGCCATCGACTCGCTCGTTGAGGCTGCTAGGGTCGATATGTGA","MWSTECQRTVDLPAEVLWETWIKVLSGDIELPQGDRYEPREPVGPGASITMTPEGQDSIEITVIRWEPPHVQADRVSYGGVELTFTHSFMPAQTQGKSVVTTRLDIDGPGADDVGPTIGPGIAEDFPQAIDSLVEAARVDM$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-135 are 50% similar to a (MLR4396 BLR0750) protein domain (PD460488) which is seen in Q98E59_RHILO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1022","1099156","1098485","672","8.84","4.56","23594","ATGTCAGACGCTTCCCTGAGAGAGACGGCGATCGAGCTGAGCGCCGAAGCTGCCTCGCTGCTCAGATGTGACAGCCTGGAGGCGGCCCCGGCGCTGCTGGGCGCCGTCATCACCGTTGCCGACCCGGCCGGGCGCGTCGCGATCCGCCTGACCGAGGTGGAGGCCTACCGCGGCGAGAAGGACCCGGGCTCCCACGCCTTCCGGGGACGCACAGCGCGCAACACCTCCATGTTCGAGGCCGGCGGGTGCATCTACGTCTACTTCACCTACGGCATGCACCACTGCCTCAACATCGTCACCGGACCTGCCGGGGTCTCACGCGCGGTGCTGCTGCGCGGGGGAGAGGTCGTCGAAGGGCTCGAGCAGGCCAGGGGACGCCGCCCCGCAGCCCGCACTGACCGCGACCTAGCCCGTGGCCCGGCCAGACTGTGCACCGCACTGGGACTGGACCGCTCCGACGACGGCGCGCTGCTGGGCGGGCCGGGATCACGCATCAGCCTGACGCTGCCGCAGCAGGCACCGGATGCCGGACGCATCCGCCGTGGGCCACGCACCGGGGTGGCTGGCCCCGGGGGAGACGGAGAAGCCTTCCCGTGGCGCTTCTGGCTGGACGGAGAGCCCACCGTCTCGCCATACCGGCCGGCCGTCACCAGGCGACGCTCACAGGGCTGA","MSDASLRETAIELSAEAASLLRCDSLEAAPALLGAVITVADPAGRVAIRLTEVEAYRGEKDPGSHAFRGRTARNTSMFEAGGCIYVYFTYGMHHCLNIVTGPAGVSRAVLLRGGEVVEGLEQARGRRPAARTDRDLARGPARLCTALGLDRSDDGALLGGPGSRISLTLPQQAPDAGRIRRGPRTGVAGPGGDGEAFPWRFWLDGEPTVSPYRPAVTRRRSQG$","DNA-3-methyladenine glycosylase","Extracellular, Cytoplasm","DNA-3-methyladenine glycosylase II","DNA-3-methyladenine glycosylase ","DNA-3-methyladenine glycosylase","","","","","

InterPro
IPR003180
Family

Methylpurine-DNA glycosylase (MPG)
PD009649	$\"[26-203]T$	3MGH_STRAW_Q829C5;
G3DSA:3.10.300.10	$\"[10-222]T$	no description
PTHR10429	$\"[40-220]T$	DNA-3-METHYLADENINE GLYCOSYLASE
PF02245	$\"[17-208]T$	Pur_DNA_glyco
TIGR00567	$\"[18-210]T$	3mg: DNA-3-methyladenine glycosylase

","BeTs to 9 clades of COG2094COG name: 3-methyladenine DNA glycosylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2094 is -----z---dr-b--f-----jxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003180 (Methylpurine-DNA glycosylase (MPG)) with a combined E-value of 1.4e-37. IPB003180A 20-38 IPB003180B 46-56 IPB003180C 71-91 IPB003180D 103-119 IPB003180E 136-150 IPB003180G 198-210","Residues 26-203 are 69% similar to a (DNA GLYCOSYLASE HYDROLASE 3-METHYLADENINE REPAIR 3.2.2.- DNA-3-METHYLADENINE GLYCOSIDASE METHYLPURINE-DNA POSSIBLE) protein domain (PD009649) which is seen in 3MGH_STRAW.","","-48% similar to PDB:1F4R CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA (E_value = 8.7E_20);-48% similar to PDB:1F6O CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH DNA (E_value = 8.7E_20);-48% similar to PDB:1BNK HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA (E_value = 1.5E_19);-48% similar to PDB:1EWN CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA (E_value = 1.9E_19);","Residues 17 to 208 (E_value = 8.9e-51) place ANA_1022 in the Pur_DNA_glyco family which is described as Methylpurine-DNA glycosylase (MPG).","","glycosylase II (MAG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1023","1100742","1099174","1569","4.74","-33.33","55923","ATGAGCCAGTTCTCCAGCCAGCCCGCAAAGCCATCCGCTGCCCAGTCCGTCGCCTCAGAAGCTCAGCAGGACGCGGCTCCCGCCGGCGTCAGCCTGTGGGGTGGACGCTTCTCAGGAGGACCCGCTGACGCGCTGGCCGCGCTGTCGGTGAGCACCCACTTCGACTGGCGCCTGGCCCGTTATGACATTGCCGGCTCCCGGGCCCACGCCCGCGCCCTGGCGCAGGCCGGTCTGCTGGACGCGGAGCAGCTGTCCGGCATGCTGGAGGCCCTGGAGCGTCTCGAGGCCGACGTCGTCGCCGGCATCTTCGTCCCGGAGGCCACCGACGAGGACGTTCACACCGCCCTGGAGCGCGGCCTCATCGAGCGTGCCGGTGACGATCTGGGGGGCCGTCTGCGCGCCGGGCGCAGCCGCAACGACCAGATCGCCACTCTCATCCGCATGTACCTGCGCGACCAGGCCCGCCACGTCGCCGGACTCGTCCTCGACGTCGTCGACGCCCTCATCTACCAGGCCGCCCAGGCCTCTGACGCCATCATGCCCGGACGCACCCACATGCAGCACGCCCAGCCGGTGCTCGTCGCCCACCAGCTGCTGGCCCACGCCTGGCCGCTCATGCGCGACGTTGAGCGCCTGGAGGACTGGGACTCCCGGGCCGCCGTGAGCCCCTACGGCTCCGGTGCGCTGGCGGGCAACACTCTCGGCATGGACCCCGATGCCGTGGCCGCCGACCTCGGGTTCGAGGCCGCCGTGGAGAACTCCATTGACGGCACCGCCGCTCGCGACGTCGTTGCCGAGCTCAGCTTCGTGCTGACGATGACCGCCGTCGACGTCTCGCGCCTGAGCGAGGAGATCATCGTCTGGAACACCAAGGAGTTCGACTTCGTCACCTTAGACGACTCCTACTCCACGGGCTCGTCCATCATGCCGCAGAAGAAGAACCCGGACGTGGCCGAGCTCGCCCGCGGCAAGGCCGGGCGCCTCATCGGCGACCTGACCGGGCTGCTCGCCACCCTCAAGGCCCTGCCCCTGGCCTACAACCGGGACCTGCAGGAGGACAAGGAACCGGTCTTCGACGCCGTCGATACCCTGGCCGTCCTCCTGCCGGCCGTCAGCGGCATGGTGAGCACGATGACCCTCCACTACGAGCGCATGGCGGAGCTCGCCCCCCAGGGGTTCTCCCTGGCCACCGATATTGCGGAGTGGCTGGTCAAGAACGGCGTGCCCTTCCGCAGCGCCCACGAGATCTCCGGTGCCTGCGTGCGCGAGTGCGAGAAGCGCGGCATTGAGCTGTGGGACCTGACCGACGCCGACTTCGCCGCCATTGATGAGCGGCTCACCCCGGGGGTGCGGGAGGTCCTCTCGGCCGAGGGGTCGGTGGCCGCTCGCACCGGGCACGGCGGCACCGCCCCGGTGCGAGTGGTGGAGCAGCTCGCCCGCGCCATCGCCCGCAGCGCCGAGCTGCGAGTCTTTGCCTGGGAGGGATCCTTGCTGGATGGCCCCGCCGGTCCCCAGTGGCCCGAACCCAGTCAGACCGATGAGGAATGGGGCGAGGAGGACCAGGACTGA","MSQFSSQPAKPSAAQSVASEAQQDAAPAGVSLWGGRFSGGPADALAALSVSTHFDWRLARYDIAGSRAHARALAQAGLLDAEQLSGMLEALERLEADVVAGIFVPEATDEDVHTALERGLIERAGDDLGGRLRAGRSRNDQIATLIRMYLRDQARHVAGLVLDVVDALIYQAAQASDAIMPGRTHMQHAQPVLVAHQLLAHAWPLMRDVERLEDWDSRAAVSPYGSGALAGNTLGMDPDAVAADLGFEAAVENSIDGTAARDVVAELSFVLTMTAVDVSRLSEEIIVWNTKEFDFVTLDDSYSTGSSIMPQKKNPDVAELARGKAGRLIGDLTGLLATLKALPLAYNRDLQEDKEPVFDAVDTLAVLLPAVSGMVSTMTLHYERMAELAPQGFSLATDIAEWLVKNGVPFRSAHEISGACVRECEKRGIELWDLTDADFAAIDERLTPGVREVLSAEGSVAARTGHGGTAPVRVVEQLARAIARSAELRVFAWEGSLLDGPAGPQWPEPSQTDEEWGEEDQD$","Argininosuccinate lyase","Cytoplasm","argininosuccinate lyase","argininosuccinate lyase ","argininosuccinate lyase","","Woods S.A., Schwartzbach S.D., Guest J.R. Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 1988. 954(1):14-26. PMID: 3282546","","","

InterPro
IPR000362
Domain

Fumarate lyase
PR00149	$\"[132-150]T$ $\"[177-193]T$ $\"[261-288]T$ $\"[305-321]T$	FUMRATELYASE
PF00206	$\"[35-330]T$	Lyase_1
PS00163	$\"[305-314]T$	FUMARATE_LYASES

InterPro
IPR003031
Domain

Delta crystallin
PR00145	$\"[131-153]T$ $\"[172-192]T$ $\"[223-239]T$ $\"[261-285]T$ $\"[305-321]T$ $\"[340-359]T$	DCRYSTALLIN

InterPro
IPR009049
Domain

Argininosuccinate lyase
TIGR00838	$\"[32-489]T$	argH: argininosuccinate lyase

noIPR
unintegrated

unintegrated
G3DSA:1.20.200.10	$\"[149-419]T$	no description
PTHR11444	$\"[22-488]T$	ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF3	$\"[22-488]T$	ARGININOSUCCINATE LYASE

","BeTs to 19 clades of COG0165COG name: Argininosuccinate lyaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0165 is aomp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB009049 (Argininosuccinate lyase) with a combined E-value of 7.3e-147. IPB009049A 33-73 IPB009049B 110-144 IPB009049C 178-215 IPB009049D 227-281 IPB009049E 288-342 IPB009049F 396-421***** IPB003031 (Delta crystallin signature) with a combined E-value of 1.4e-52. IPB003031A 131-153 IPB003031B 172-192 IPB003031C 223-239 IPB003031D 261-285 IPB003031E 305-321 IPB003031F 340-359***** IPB000362 (Fumarate lyase) with a combined E-value of 5e-14. IPB000362 305-330","Residues 32-101 are 70% similar to a (LYASE ARGININOSUCCINATE PLASMID BIOSYNTHESIS ASAL ARGINOSUCCINASE ARGININE) protein domain (PD668087) which is seen in ARL2_RHIME.Residues 51-95 are 80% similar to a (LYASE ARGININOSUCCINATE BIOSYNTHESIS ASAL ARGINOSUCCINASE ARGININE ARGH) protein domain (PD698996) which is seen in Q6AGC8_BBBBB.Residues 51-428 are similar to a (LYASE ADENYLOSUCCINATE ARGININOSUCCINATE BIOSYNTHESIS ARGININE ASAL ARGINOSUCCINASE ASPARTATE AMMONIA-LYASE ASL) protein domain (PD000660) which is seen in ARLY_BIFLO.Residues 139-415 are 44% similar to a (LYASE ADENYLOSUCCINATE) protein domain (PDA1A6R3) which is seen in Q701W7_AAAAA.Residues 172-438 are 40% similar to a (LYASE PROBABLE) protein domain (PDA1B3O3) which is seen in Q9HY93_PSEAE.","","-59% similar to PDB:1K7W Crystal Structure of S283A Duck Delta 2 Crystallin Mutant (E_value = 7.6E_91);-59% similar to PDB:1HY1 CRYSTAL STRUCTURE OF WILD TYPE DUCK DELTA 2 CRYSTALLIN (EYE LENS PROTEIN) (E_value = 1.7E_90);-59% similar to PDB:1TJU Crystal Structure of T161S Duck Delta 2 Crystallin Mutant (E_value = 5.0E_90);-58% similar to PDB:1TJV Crystal Structure of T161D Duck Delta 2 Crystallin Mutant (E_value = 8.4E_90);-58% similar to PDB:1TJW Crystal Structure of T161D Duck Delta 2 Crystallin Mutant with bound argininosuccinate (E_value = 8.4E_90);","Residues 35 to 330 (E_value = 1.5e-63) place ANA_1023 in the Lyase_1 family which is described as Lyase.","","lyase (argH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1024","1100752","1101819","1068","7.55","2.00","38528","ATGGCCCATCTGCCCGAGCAGGTTCCTCAACGATCAGTCTGGACAGGCCCTGTCGTGGCTCGCAGACAAAACGATCCCCACTTTCTTGAGGAAGACGCAGTAAGTGGAACCAGGACCGGAGATCCCAACCAACGGGAAGGAAGAAAGGCCTGTGTCTCGGATGGCGGGCAATGCCATGATGAGCCAATGCCCGCCGAACAAGACGCACTTTTCCCAGGCAAGCAGTTCATCTCCACCGTGCTCGAGGCCCTCGAGACCAAGACCCGGATGACCGGGGTGATCGCCCACCGCTATCTCATGCGCGCGGCGATGGCCGGCATGATCGTGGCGGTCTTCTATGTCGTGAACTACGCCATCGTCGGTGTCTTCGATGGCCTGCGCCTCGGGGACACCTCGCTCGCGGGGATCGGGAAGATGCTCGGGGCTCTGTCCTTCGGACCCGCTCTCGTCTTCATCTACTACACGAAGTCCGAGCTGCTCACCAGCAACATGATGGTGGTGGCCATCGGCCACTACTACAGGCGGATCTCGACGTGGCGGGCTCTGAGGGTGCTGGTCATGTGCCTGGCCGGCAACTTCGCCGGAGGGCTGGTCTTCGCGGCCATGTACCGCTTCTCCACCCTCGTAGAGGCGGCAACCGGTGAACAGGCCACCCACTCAGTGGCCGCCAAGCTCCACTACCTGTCGTCGGCCTCGGGGATCGGCGACCTCTTCGTGCGGGCGGTCCTGTGCAACTTCATGATCAACCTGGCGATGCTCCTCATCTACAACGGCTTCATCCGCGAGGACTGGTCCAAGATCATCGCGATGCTCATCTCCGTGTTCGTCTTCGCCTTCCTCGGCCTTGAGCACTCCGTGGCCAACACGGTCCTGTTCACGGTCGTCGGTCTGACGCATGGGATCGATGTCTTGCCGGCGCTGGGGAATGTGGCTGTGGCACTGCTGGGCAACTTCGTGGGCGGCGGGCTGCTGATCGGCGGCTACTACGCCTACGCCAACGACGACTCCCGCTGGCTGCGCCGACAGCCCCAGAAGAACGGGGCACAAGCGGCTGAGTCGACTGAGTGA","MAHLPEQVPQRSVWTGPVVARRQNDPHFLEEDAVSGTRTGDPNQREGRKACVSDGGQCHDEPMPAEQDALFPGKQFISTVLEALETKTRMTGVIAHRYLMRAAMAGMIVAVFYVVNYAIVGVFDGLRLGDTSLAGIGKMLGALSFGPALVFIYYTKSELLTSNMMVVAIGHYYRRISTWRALRVLVMCLAGNFAGGLVFAAMYRFSTLVEAATGEQATHSVAAKLHYLSSASGIGDLFVRAVLCNFMINLAMLLIYNGFIREDWSKIIAMLISVFVFAFLGLEHSVANTVLFTVVGLTHGIDVLPALGNVAVALLGNFVGGGLLIGGYYAYANDDSRWLRRQPQKNGAQAAESTE$","Formate/nitrite transporter","Membrane, Cytoplasm","Formate/nitrite transporter family","hypothetical protein","formate/nitrite transporter","","Suppmann B., Sawers G. Isolation and characterization of hypophosphite--resistant mutants of Escherichia coli: identification of the FocA protein, encoded by the pfl operon, as a putative formate transporter. Mol. Microbiol. 1994. 11(5):965-982. PMID: 8022272","","","

InterPro
IPR000292
Family

Formate/nitrite transporter
PF01226	$\"[72-336]T$	Form_Nir_trans

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[173-355]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[98-120]?$ $\"[134-154]?$ $\"[181-201]?$ $\"[237-257]?$ $\"[267-287]?$ $\"[310-332]?$	transmembrane_regions

","BeTs to 6 clades of COG2116COG name: Formate/nitrite family of transportersFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2116 is ------y----lb-efgh--------Number of proteins in this genome belonging to this COG is 1","***** IPB000292 (Formate/nitrite transporter) with a combined E-value of 7.9e-27. IPB000292A 139-165 IPB000292B 229-254 IPB000292C 266-289","No significant hits to the ProDom database.","","-39% similar to PDB:1GWY CRYSTAL STRUCTURE OF THE WATER-SOLUBLE STATE OF THE PORE-FORMING CYTOLYSIN STICHOLYSIN II (E_value = );-39% similar to PDB:1O71 CRYSTAL STRUCTURE OF THE WATER-SOLUBLE STATE OF THE PORE-FORMING CYTOLYSIN STICHOLYSIN II COMPLEXED WITH GLYCEROL (E_value = );-39% similar to PDB:1O72 CRYSTAL STRUCTURE OF THE WATER-SOLUBLE STATE OF THE PORE-FORMING CYTOLYSIN STICHOLYSIN II COMPLEXED WITH PHOSPHORYLCHOLINE (E_value = );-41% similar to PDB:1BCC CYTOCHROME BC1 COMPLEX FROM CHICKEN (E_value = );-41% similar to PDB:2BCC STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN (E_value = );","Residues 72 to 336 (E_value = 3.6e-10) place ANA_1024 in the Form_Nir_trans family which is described as Formate/nitrite transporter.","","transporter family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1025","1103222","1101990","1233","5.09","-15.41","45234","GTGATCCCATTGAGCATCCACAAGGACCGTGTCGTCCTGGCCTACTCCGGAGGCCTGGACACGTCCGTCGCCATCGGCTGGATCGGCGAGGCCACTGGTCGAGAGGTTGTGGCCGTCGCCGTTGACGTCGGCCAGGGCGGCGAGGACCTTGAGGTGATCCGTCAGCGAGCCCTCGACTGCGGAGCCGTCGAGGCCTATGTCGCCGACGCCCGAGACGAGTTCGCCAACGACTACTGCATGCCGGCGCTCAAGGCCAACGCCCTCTACGAGGGGACCTATCCGCTCGTGTCGGCCCTGTCCCGCCCGGTCATCGCCCGCCACCTGGTCAAGGCCGCCCGCGAGTTCGGCGCGAACACCGTGGCCCACGGCTGCACCGGCAAGGGCAACGACCAGGTCCGCTTCGAGGTCTCCATCACCTCCATGGCCCCCGACATGGACTGCATCTCCCCGGTACGCGACCTGGCGCTGACCCGTGACGTGGCCATCGACTACGCCGAGAAGCACAACCTGCCGATCGAGACCACCAAGCACAACCCCTTCTCCATCGACCAGAATGTTTGGGGCCGTGCCATTGAGACCGGGTACCTCGAGGACCTGTGGAACGCTCCCACCAAGGACGTCTACGTCTATACCGATGACCCCGCCTACCCGCCCCTGCCCGACGAAGTGACCCTCACCTTCAAGGAAGGAATCCCTGTGGCCATCGACGGCCGCGACGTCAGCCCCCTGGAAGCGATTCAGGAGCTCAACCGTAGGGCAGGCACCCAGGGCGTGGGGCGCATCGACATGGTCGAGGACCGGCTCGTGGGGATCAAGTCCCGCGAGATCTACGAGGCCCCCGGCGCCGTGGCCCTGATCGAGGCCCACCGAGCGCTCGAGGCCGTCACCCTGGAGCGCATGCAGCGCCGCTACAAGCGGAGCATGGAGCAGACCTGGGCCGAGCTCGTCTACGAGGCCCAGTGGTACTCCCCGCTCAAGCGCTCCATGGACGCCTTCATCGAGGACACGCAGCGCTATGTCAACGGTGACATCCGAATGGTCCTGCACGGCGGCCGGGCGACCGTCAACGGGCGTCGCTCCGAGACGGGCCTGTACGACTTCAACCTGGCCACCTATGAGAGCGGAGACACCTTCGACCAGTCCTCCTCGCGGGGCTTCATCGAGATCTACGGGATGCAGTCCAAGCTCGCCGCCGCCCGCGACGTGCGCGCTGGCAACGGTCAGGGGTTCTGA","VIPLSIHKDRVVLAYSGGLDTSVAIGWIGEATGREVVAVAVDVGQGGEDLEVIRQRALDCGAVEAYVADARDEFANDYCMPALKANALYEGTYPLVSALSRPVIARHLVKAAREFGANTVAHGCTGKGNDQVRFEVSITSMAPDMDCISPVRDLALTRDVAIDYAEKHNLPIETTKHNPFSIDQNVWGRAIETGYLEDLWNAPTKDVYVYTDDPAYPPLPDEVTLTFKEGIPVAIDGRDVSPLEAIQELNRRAGTQGVGRIDMVEDRLVGIKSREIYEAPGAVALIEAHRALEAVTLERMQRRYKRSMEQTWAELVYEAQWYSPLKRSMDAFIEDTQRYVNGDIRMVLHGGRATVNGRRSETGLYDFNLATYESGDTFDQSSSRGFIEIYGMQSKLAAARDVRAGNGQGF$","Argininosuccinate synthase","Cytoplasm","argininosuccinate synthase","argininosuccinate synthase ","Argininosuccinate synthase","","Van Vliet F., Crabeel M., Boyen A., Tricot C., Stalon V., Falmagne P., Nakamura Y., Baumberg S., Glansdorff N. Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals. Gene 1990. 95(1):99-104. PMID: 2123815Morris C.J., Reeve J.N. Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii. J. Bacteriol. 1988. 170(7):3125-3130. PMID: 3133361","","","

InterPro
IPR001518
Family

Argininosuccinate synthase
PTHR11587	$\"[6-407]T$	ARGININOSUCCINATE SYNTHASE
PF00764	$\"[12-400]T$	Arginosuc_synth
TIGR00032	$\"[10-402]T$	argG: argininosuccinate synthase
PS00564	$\"[14-22]T$	ARGININOSUCCIN_SYN_1
PS00565	$\"[123-134]T$	ARGININOSUCCIN_SYN_2

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[9-179]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.90.1260.10	$\"[180-407]T$	no description

","BeTs to 19 clades of COG0137COG name: Argininosuccinate synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0137 is aomp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001518 (Argininosuccinate synthase) with a combined E-value of 2.8e-92. IPB001518A 10-21 IPB001518B 45-90 IPB001518C 177-199 IPB001518D 216-237 IPB001518E 249-293 IPB001518F 315-324","Residues 9-69 are 93% similar to a (LIGASE BIOSYNTHESIS GMP ATP-BINDING SYNTHASE GLUTAMINE AMIDOTRANSFERASE TRNA SYNTHETASE METHYLTRANSFERASE) protein domain (PD034321) which is seen in ASSY_MYCPA.Residues 70-365 are 44% similar to a (ARGININOSUCCINATE SYNTHASE) protein domain (PD934365) which is seen in Q8D4C5_VIBVU.Residues 93-186 are 87% similar to a (LIGASE BIOSYNTHESIS ARGININOSUCCINATE ATP-BINDING ARGININE SYNTHASE CITRULLINE--ASPARTATE AMINO-ACID UREA CYCLE) protein domain (PD580210) which is seen in ASSY_BIFLO.Residues 192-405 are similar to a (LIGASE BIOSYNTHESIS ARGININOSUCCINATE ATP-BINDING ARGININE SYNTHASE CITRULLINE--ASPARTATE AMINO-ACID UREA CYCLE) protein domain (PD341294) which is seen in ASSY_BIFLO.","","-60% similar to PDB:1J1Z Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with substrate (E_value = 8.3E_82);-60% similar to PDB:1J20 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with product (E_value = 8.3E_82);-60% similar to PDB:1J21 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with ATP and citrulline (E_value = 8.3E_82);-60% similar to PDB:1KH1 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase (E_value = 8.3E_82);-60% similar to PDB:1KH2 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with ATP (E_value = 8.3E_82);","Residues 12 to 400 (E_value = 8.5e-242) place ANA_1025 in the Arginosuc_synth family which is described as Arginosuccinate synthase.","","synthase (argG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1026","1103881","1103294","588","6.54","-1.14","20416","ATGAGCGCCACCATCGAGGCCTCTCAGCGCGACCTGGAGGCAACGGCCCCCCTGGTACCCGGGACCAAGACCGCCCGGCACGCCAGCATCGTCCAGATCCTGTCGCGGGAACGTATCAGCTCCCAGGCCCAGCTGCGCAAGGCCCTGGCACAGCGCGGCATCAGTACTACCCAGGCCACGCTTTCACGGGATCTGGTGGAGCTGCGGGCGACGAAGATCCGCGCCCCGGGCGGAGAACTCATCTACTCCATGCCCGAGGCCGGCGCCCCCGGCCAGGTCCATACCGGTGCCCTTTCCGAGCCGGAGGAGACCGAGGACTCTTTGCGTGCCCACACCACCCCCCGTCTGTCCCGGTGGTGCGCAGAGCTACTCGTTACTGCCGAGTGGGCCGGCCCCCAGGTGGTCCTGCGAACGCCCGCCGGCGCCGCCCAGCTGCTCGCCGGGGCCGTTGACGACGCCATGATGCCGGGCGTCATGGGGTGCATAGCCGGCGACGACACCGTCCTGGTCATCACCCGCGGCGCTCAGGTCGCAGCCGATGTGGCCAGGCACTTGCTCGCTCTGGCTGACCCCTCAGCCCGAGCCTGA","MSATIEASQRDLEATAPLVPGTKTARHASIVQILSRERISSQAQLRKALAQRGISTTQATLSRDLVELRATKIRAPGGELIYSMPEAGAPGQVHTGALSEPEETEDSLRAHTTPRLSRWCAELLVTAEWAGPQVVLRTPAGAAQLLAGAVDDAMMPGVMGCIAGDDTVLVITRGAQVAADVARHLLALADPSARA$","Arginine repressor","Cytoplasm","Arginine repressor","arginine repressor","arginine repressor","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR001669
Family

Arginine repressor
PD007402	$\"[130-178]T$	ARGR_MYCTU_P94992;
PR01467	$\"[41-54]T$ $\"[57-72]T$	ARGREPRESSOR
PF01316	$\"[21-90]T$	Arg_repressor
PF02863	$\"[119-188]T$	Arg_repressor_C

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[21-87]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.1360.40	$\"[119-189]T$	no description

","BeTs to 8 clades of COG1438COG name: Arginine repressorFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1438 is --------vdrlb-e-gh-----i--Number of proteins in this genome belonging to this COG is 1","***** IPB001669 (Bacterial arginine repressor signature) with a combined E-value of 7.2e-20. IPB001669A 41-54 IPB001669B 57-72 IPB001669D 158-173","Residues 26-85 are similar to a (ARGININE REPRESSOR TRANSCRIPTION DNA-BINDING TRANS-ACTING FACTOR BIOSYNTHESIS REGULATION TRANSCRIPTIONAL REGULATOR) protein domain (PD203445) which is seen in ARGR_STAEP.Residues 116-190 are similar to a (ARGININE REPRESSOR) protein domain (PD949646) which is seen in Q6AA75_PROAC.Residues 124-182 are similar to a (REPRESSOR ARGININE TRANSCRIPTION DNA-BINDING BIOSYNTHESIS REGULATION ARGR TRANS-ACTING FACTOR) protein domain (PD738667) which is seen in Q740I4_MYCPA.Residues 130-178 are 69% similar to a (ARGININE REPRESSOR TRANSCRIPTION DNA-BINDING TRANS-ACTING FACTOR REGULATION BIOSYNTHESIS METABOLISM TRANSCRIPTIONAL) protein domain (PD007402) which is seen in ARGR_MYCTU.","","-44% similar to PDB:1F9N CRYSTAL STRUCTURE OF AHRC, THE ARGININE REPRESSOR/ACTIVATOR PROTEIN FROM BACILLUS SUBTILIS (E_value = 3.3E_14);-46% similar to PDB:1B4A STRUCTURE OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS (E_value = 4.8E_13);","Residues 21 to 90 (E_value = 8.4e-24) place ANA_1026 in the Arg_repressor family which is described as Arginine repressor, DNA binding domain.Residues 119 to 188 (E_value = 2.6e-11) place ANA_1026 in the Arg_repressor_C family which is described as Arginine repressor, C-terminal domain.","","repressor (AHRC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1027","1105152","1103878","1275","5.77","-8.41","43752","ATGACCCCCTCCTCGCGAGCTCAGGCTCCCACCGCGGAGGCGAAAGGGGCCGGCACCGGCAACGCCGGCTGGCTGGCCCGCTACACCGACGCCGTGATGAACACCTTCGGCACCCCCAGCCGGGTCCTGGTGCGGGGGAGTGGCGCCCACGTCTGGGACGCCGACGGCCAGGAGTACATCGACCTGCTGGCGGGCATCGCCGTCAACTGCCTGGGACACGCGCACCCTGCGATCGTCGAGGCTGTGTCCACCCAGATCTCCACCCTGGGGCACGTCTCCAACTTCTTCACCACCCCGGCCCAGGTCGGCCTCGCCGAGGAGCTCGTCCGCCTCACCTTCCCTGACCATCCCGCTCACGACTCCCGCGTCTTCCTGGCCAACTCCGGTACCGAGGCCAATGAGGCCGCTTTCAAGATCGCCCGCCGTCACGGCGGTAGCCGACGCCCCCGGGTCCTGGCCCTCCAGGACGCCTTCCACGGCAGGACCATGGGCGCCCTGGCCCTGACCTACAAGGCCGCCTACCGGGAGCCCTTCGAGCCGCTGCCCGGTGGGGTCGAGTTCATCCCCGCCGGTGACGTCGAAGCACTGCGCACCGCGCTGGGGCCGGACGTGGCGGCACTCGTTGTCGAACCCATACAGGGCGAGGCCGGGGTGCGTGAGCTGCCTGCCGGGTACCTGGAGGCGGCCCGCGAGCTGACTGAGGCCGCTGGCGCGCTGCTCATCATCGATGAGGTTCAGACCGGAATGGGACGCACCGGCGCCTGGATGGCGCACCATCTGCTGGCACCGGGCATCGTCCCCGACGTCGTCACCCTGGCCAAGGGACTGGGCGGAGGCGTCCCCATCGGCGCAGTCGTCGCCAGTGGGCAGGCCGCCGCTCTTCTCGAGCCGGGGCAGCACGGCACCACCTTCGGCGGCAACCCGGTGGCCTGCGCAGCAGCGCTCGCCGTCATCGGGACTATCCGTAGCCAGTCCCTGCTGGAGAGGGTTCAGCAGCTCGGCTCGGCCTGGTCCCGGGAGCTGGCGGTCGTGGACGGAGTCAACCAGGTGCGCGGCCGGGGCCTGCTGCTCGGCGTCGGGCTGGACGACGGGCTCCCGCCCGCTGCTGAGATCGCCGCTGCCCTGGCGGCTCGCGGTTTCATTGTCAATGCGCCGCGCCCCGACACGATCCGCCTGGCTCCGCCCTTCATCCTCTCCGACGATGACGCCAGGGCCTTCACCACCACGCTGTCCGAGGTCCTTGACCGGGCACTGTCAGAGAAAGCCGGTTCATGA","MTPSSRAQAPTAEAKGAGTGNAGWLARYTDAVMNTFGTPSRVLVRGSGAHVWDADGQEYIDLLAGIAVNCLGHAHPAIVEAVSTQISTLGHVSNFFTTPAQVGLAEELVRLTFPDHPAHDSRVFLANSGTEANEAAFKIARRHGGSRRPRVLALQDAFHGRTMGALALTYKAAYREPFEPLPGGVEFIPAGDVEALRTALGPDVAALVVEPIQGEAGVRELPAGYLEAARELTEAAGALLIIDEVQTGMGRTGAWMAHHLLAPGIVPDVVTLAKGLGGGVPIGAVVASGQAAALLEPGQHGTTFGGNPVACAAALAVIGTIRSQSLLERVQQLGSAWSRELAVVDGVNQVRGRGLLLGVGLDDGLPPAAEIAAALAARGFIVNAPRPDTIRLAPPFILSDDDARAFTTTLSEVLDRALSEKAGS$","Acetylornithine and succinylornithine aminotransferase","Cytoplasm","Acetylornithine aminotransferase (ACOAT)","acetylornithine aminotransferase ","acetylornithine and succinylornithine aminotransferase","","Yonaha K., Nishie M., Aibara S. The primary structure of omega-amino acid:pyruvate aminotransferase. J. Biol. Chem. 1992. 267(18):12506-12510. PMID: 1618757","","","

InterPro
IPR004636
Family

Acetylornithine and succinylornithine aminotransferase
PTHR11986:SF19	$\"[30-420]T$	ACETYLORNITHINE AMINOTRANSFERASE
TIGR00707	$\"[31-415]T$	argD: acetylornithine and succinylornithine

InterPro
IPR005814
Family

Aminotransferase class-III
PTHR11986	$\"[30-420]T$	AMINOTRANSFERASE CLASS III
PF00202	$\"[42-363]T$	Aminotran_3
PS00600	$\"[240-279]?$	AA_TRANSFER_CLASS_3

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[75-324]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[17-75]T$	no description

","BeTs to 21 clades of COG0160COG name: PLP-dependent aminotransferasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0160 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB005814 (Aminotransferase class-III) with a combined E-value of 2e-74. IPB005814A 45-82 IPB005814B 127-141 IPB005814C 225-253 IPB005814D 267-281 IPB005814E 300-318","Residues 68-141 are 72% similar to a (AMINOTRANSFERASE PYRIDOXAL PHOSPHATE TRANSFERASE BIOSYNTHESIS GLUTAMATE-1-SEMIALDEHYDE ACETYLORNITHINE ARGININE 21-AMINOMUTASE ISOMERASE) protein domain (PD000493) which is seen in Q6AGD0_BBBBB.Residues 68-143 are 58% similar to a (AMINOTRANSFERASE 2.6.1.- PYRIDOXAL PHOSPHATE TRANSFERASE) protein domain (PD866357) which is seen in Q8Y398_RALSO.Residues 121-333 are 41% similar to a (AMINOTRANSFERASE PHOSPHATE TRANSFERASE PYRIDOXAL L-LYSINE 6-AMINOTRANSFERASE) protein domain (PD308202) which is seen in Q8P865_XANCP.Residues 127-334 are 40% similar to a (AMINOTRANSFERASE PROBABLE TRANSFERASE ACETYLORNITHINE) protein domain (PDA0F4W8) which is seen in Q7UQZ7_RHOBA.Residues 152-208 are 70% similar to a (AMINOTRANSFERASE PYRIDOXAL PHOSPHATE TRANSFERASE BIOSYNTHESIS ARGININE ACETYLORNITHINE ACOAT TRANSAMINASE 4-AMINOBUTYRATE) protein domain (PD082173) which is seen in ARGD_STRCL.Residues 209-273 are 76% similar to a (AMINOTRANSFERASE PYRIDOXAL PHOSPHATE TRANSFERASE BIOSYNTHESIS GLUTAMATE-1-SEMIALDEHYDE ACETYLORNITHINE ARGININE 21-AMINOMUTASE ISOMERASE) protein domain (PD000465) which is seen in Q6AGD0_BBBBB.Residues 264-344 are 58% similar to a (PHOSPHATE RHBA PYRIDOXAL) protein domain (PD262795) which is seen in Q9RFF8_RHOSH.Residues 274-336 are 73% similar to a (AMINOTRANSFERASE PHOSPHATE PYRIDOXAL TRANSFERASE BIOSYNTHESIS ACETYLORNITHINE ACOAT ARGININE ARGD) protein domain (PD861374) which is seen in ARGD_MYCTU.Residues 274-331 are similar to a (AMINOTRANSFERASE PYRIDOXAL PHOSPHATE TRANSFERASE BIOSYNTHESIS GLUTAMATE-1-SEMIALDEHYDE ACETYLORNITHINE ARGININE ISOMERASE 21-AMINOMUTASE) protein domain (PD066084) which is seen in ARGD_STRAW.Residues 276-341 are 59% similar to a (AMINOTRANSFERASE BIOSYNTHESIS 2.6.1.- PHOSPHATE TRANSFERASE LYSINE ACOAT PYRIDOXAL ARGININE ACETYLORNITHINE/ACETYL-LYSINE) protein domain (PD647282) which is seen in ARGD_PYRAE.","","-64% similar to PDB:2ORD Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution (E_value = 8.7E_74);-54% similar to PDB:1VEF Acetylornithine aminotransferase from Thermus thermophilus HB8 (E_value = 2.1E_72);-54% similar to PDB:1WKG Acetylornithine aminotransferase from thermus thermophilus HB8 (E_value = 2.1E_72);-54% similar to PDB:1WKH Acetylornithine aminotransferase from thermus thermophilus HB8 (E_value = 2.1E_72);-49% similar to PDB:2BYJ ORNITHINE AMINOTRANSFERASE MUTANT Y85I (E_value = 1.1E_49);","Residues 42 to 363 (E_value = 9.6e-124) place ANA_1027 in the Aminotran_3 family which is described as Aminotransferase class-III.","","aminotransferase (ACOAT) (argD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1028","1106075","1105149","927","6.08","-3.61","32572","ATGAAACGTACCCCTCTCGACCCACAGACCAAGGCATCCGTCCTGCTGGAGGCCGTGCCGTGGCTGCGCACCTACAAGGGCGCCACCATGGTCATCAAGTACGGCGGCAACGCCATGGTCAACGATGAGCTCAAGCGCGCCTTCGCCCAGGACATCCTCTTCCTGCACCAGGTCGGGGTGCGCCCCGTCGTCGTTCACGGCGGCGGGCCCCAGATCAACGCGATGCTCAAGCGGCTGGGTATCAGCTCGGAGTTCCGCGGAGGACTGCGCGTCACCACCCCCGAGATCATGGACGTGGTCCGCATGGTGCTCACCGGCTCCGTACAGCGCGAGCTCGTCTCCCTGCTCAACACCGACGGCTCTGCCGCCGTCGGCATCAGCGGTGAGGACGGCGGGCTCCTGCGGGCTCGGCAGCGCCTGGCCACAGTGGACGGGCACAAGGTCGACGTCGGCCTGGTCGGCGACGTCGTCGACGTCAGTCCGCAGCCCATCATCGACCTGCTCGACCAGGGCCGTATCCCGGTCATCTCCTCGGTCGCTCCACTGATGACGGACTCCGAGACCGTCCTCAACGTTAACGCCGACACGGCTGCCGCCGCGATCGCCGTGTCCCTCAAGGCCCGCACCCTGCTCATGCTCACCGACGTCGAGGGACTCTACTCGGCCTGGCCCGACCGCAGCACGCTGGTGCCCTTCATCAGTACCGCCGCGCTGGAGGAGCTCCTGCCCACGCTCGAGGCCGGGATGATCCCCAAGATGGAGGCCTGTTTGCGGGCCGTCTACGGGGGAGTCGCGCAGGCGCACGTCGTCGACGGACGCCAGGCCCACAGCATGCTGCTCGAGATCGTCACCGACCAGGGCGTCGGCACCGTCATCCACCCCGGAGACGCCCCGGTCCCACCGCTGAACGGAGGCAAGAGCCTATGA","MKRTPLDPQTKASVLLEAVPWLRTYKGATMVIKYGGNAMVNDELKRAFAQDILFLHQVGVRPVVVHGGGPQINAMLKRLGISSEFRGGLRVTTPEIMDVVRMVLTGSVQRELVSLLNTDGSAAVGISGEDGGLLRARQRLATVDGHKVDVGLVGDVVDVSPQPIIDLLDQGRIPVISSVAPLMTDSETVLNVNADTAAAAIAVSLKARTLLMLTDVEGLYSAWPDRSTLVPFISTAALEELLPTLEAGMIPKMEACLRAVYGGVAQAHVVDGRQAHSMLLEIVTDQGVGTVIHPGDAPVPPLNGGKSL$","Acetylglutamate kinase","Cytoplasm, Membrane","acetylglutamate kinase","acetylglutamate kinase ","acetylglutamate kinase","","Li W., Brandriss M.C. Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase. J. Bacteriol. 1992. 174(12):4148-4156. PMID: 1350780Ogura M., Kawata-Mukai M., Itaya M., Takio K., Tanaka T. Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis. J. Bacteriol. 1994. 176(18):5673-5680. PMID: 8083159","","","

InterPro
IPR001048
Domain

Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10	$\"[26-294]T$	no description
PF00696	$\"[28-271]T$	AA_kinase

InterPro
IPR001057
Domain

Glutamate 5-kinase
PR00474	$\"[59-73]T$ $\"[193-220]T$ $\"[244-264]T$	GLU5KINASE

InterPro
IPR004662
Domain

Acetylglutamate kinase
TIGR00761	$\"[29-269]T$	argB: acetylglutamate kinase

InterPro
IPR011148
Family

N-acetylglutamate kinase
PIRSF000728	$\"[9-294]T$	N-acetylglutamate kinase

","BeTs to 18 clades of COG0548COG name: Acetylglutamate kinaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0548 is a-m-kzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001057 (Glutamate 5-kinase) with a combined E-value of 5.7e-52. IPB001057A 27-41 IPB001057B 61-95 IPB001057C 159-188 IPB001057D 191-224 IPB001057E 242-271 IPB001057F 281-294 IPB001057C 99-128***** IPB006855 (Protein of unknown function DUF619) with a combined E-value of 2.5e-09. IPB006855A 36-90","Residues 35-276 are similar to a (KINASE TRANSFERASE ACETYLGLUTAMATE NAG BIOSYNTHESIS AGK ARGININE 5-PHOSPHOTRANSFERASE GLUTAMATE N-ACETYL-L-) protein domain (PD414861) which is seen in ARGB_BIFLO.Residues 210-259 are 88% similar to a (KINASE TRANSFERASE ACETYLGLUTAMATE AGK 5-PHOSPHOTRANSFERASE GLUTAMATE NAG ARGB BIOSYNTHESIS ARGININE) protein domain (PD841448) which is seen in Q740I7_MYCPA.","","-59% similar to PDB:2AP9 Crystal structure of acetylglutamate kinase from Mycobacterium tuberculosis CDC1551 (E_value = 2.1E_63);-52% similar to PDB:2BUF ARGININE FEED-BACK INHIBITABLE ACETYLGLUTAMATE KINASE (E_value = 2.1E_39);-51% similar to PDB:2BTY ACETYLGLUTAMATE KINASE FROM THERMOTOGA MARITIMA COMPLEXED WITH ITS INHIBITOR ARGININE (E_value = 5.7E_37);","Residues 28 to 271 (E_value = 2.8e-58) place ANA_1028 in the AA_kinase family which is described as Amino acid kinase family.","","kinase (argB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1030","1107268","1106072","1197","4.62","-20.18","40452","GTGAGCGTGACCGCAGCACAGGGCTTCCGCGCCGCCGGCGTGCGCGCCGGCCTCAAGGCCTCCGGCAAGCCCGACCTCGCCCTTGTCGTCAATGACGGGCCGCTGGACACCGCGGCCGGGGTGTTCACCACCAACCGCGTCGTTGCAGCCCCCGTGGTCTGGTCACGCCGGCTCCTGGCCGGTCCTGAAGGCGGGCAGCCGGGCCGCGCCCGCGCCGTCGTCCTCAACTCCGGCAGCGCCAACGCCTGCACCGGAGCGCAGGGCATGCACGACACCGAGGCCACCGCTGTCCGTGCCGCCGGCCTGCTGGGCGCCGAACCGGACCAGGTCCTGGTCTGCTCCACGGGCGTCATCGGGGAGCGCATCGACATGCCCGTCCTCCTGGAGGGCGTCGACGTCGCGGCCCTCGCCCTGGCCGATACGCCTCAGGCCGGGACCGACGCCGCCACCGCCATCATGACCACCGACACCGTCTCCAAGGAGGACGCCCTCACGGTCGGTGCCGGCGAGCAGAGCTGGACCATCGGCGGCATGATTAAGGGCGTGGGCATGCTGGCCCCAGGGTTGGCCACCATGCTCGCCGTCATCACCACCGACGCCGTCCTCACCCCTCAGCAGGCGCAGGACGCCCTGGCCTCCGCCACGATGCGCACCGTCAACCGGATCAACTCCGACGGGTGCATGTCCACCAACGACACGGTTCTCCTGCTGGCCTCCGGAGCCTCCGGTACCACGCCCTCCCAGGACGAGCTCGACGAGGCGCTCACCGAGGTGATGAGCCGGCTCGGCCGGCGCCTGGTGGCCGACGCCGAGGGTGCCACCCACGACATCGCCATCACCGTCTCCGGAGCCGTCAGCGAGCAGGCCGCCGAGGCCGCAGCCCGCACCGTCAGCTCCTCCAACCTCCTCAAGTGCGCCGTCGCCGGGGCCGACCCCAACTGGGGGCGCATCCTCTCCCAACTGGGGACCGTGCCGGAGGACGTGTGCCCCTTCAACCCCGACGAGGTCGACGTCGCCATCAACGGCATCACGATCTTCAGCCACGGCGCCCCACAACCCAACCGGGACGCGGTGGACATGAGCCCACGCGAGACCCGCATCGACATCGAGCTGTCGGCGGGCCCGGCCCAGGCCACCGTGTGGACCAATGACCTCACTCACGGATACGTCACCATCAACGCGGACTACACGACATGA","VSVTAAQGFRAAGVRAGLKASGKPDLALVVNDGPLDTAAGVFTTNRVVAAPVVWSRRLLAGPEGGQPGRARAVVLNSGSANACTGAQGMHDTEATAVRAAGLLGAEPDQVLVCSTGVIGERIDMPVLLEGVDVAALALADTPQAGTDAATAIMTTDTVSKEDALTVGAGEQSWTIGGMIKGVGMLAPGLATMLAVITTDAVLTPQQAQDALASATMRTVNRINSDGCMSTNDTVLLLASGASGTTPSQDELDEALTEVMSRLGRRLVADAEGATHDIAITVSGAVSEQAAEAAARTVSSSNLLKCAVAGADPNWGRILSQLGTVPEDVCPFNPDEVDVAINGITIFSHGAPQPNRDAVDMSPRETRIDIELSAGPAQATVWTNDLTHGYVTINADYTT$","Arginine biosynthesis bifunctional protein ArgJ","Cytoplasm, Extracellular","arginine biosynthesis bifunctional protein ArgJ","arginine biosynthesis bifunctional protein ArgJ ","arginine biosynthesis bifunctional protein ArgJ","","Sakanyan V., Charlier D., Legrain C., Kochikyan A., Mett I., Pierard A., Glansdorff N. Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase. J. Gen. Microbiol. 1993. 139:393-402. PMID: 8473852","","","

InterPro
IPR002813
Family

Arginine biosynthesis protein ArgJ
PD004193	$\"[3-211]T$ $\"[218-398]T$	Q6A813_PROAC_Q6A813;
PTHR23100	$\"[15-398]T$	ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ
PF01960	$\"[9-398]T$	ArgJ
TIGR00120	$\"[1-398]T$	ArgJ: arginine biosynthesis bifunctional pr

","BeTs to 13 clades of COG1364COG name: Predicted kinase related to thiamine pyrophosphokinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1364 is a-m---yqvdrlbc-f---n-j----Number of proteins in this genome belonging to this COG is 1","***** IPB002813 (Arginine biosynthesis protein ArgJ) with a combined E-value of 3.8e-110. IPB002813A 39-51 IPB002813B 70-85 IPB002813C 114-134 IPB002813D 149-160 IPB002813E 177-215 IPB002813F 221-240 IPB002813G 259-303 IPB002813H 304-324 IPB002813I 371-398","Residues 1-95 are 66% similar to a (ACETYLTRANSFERASE ORNITHINE GLUTAMATE N-ACETYLTRANSFERASE BIFUNCTIONAL BIOSYNTHESIS ARGININE TRANSACETYLASE OATASE ARGJ) protein domain (PD437059) which is seen in Q6A813_PROAC.Residues 218-398 are 63% similar to a (ACETYLTRANSFERASE ORNITHINE GLUTAMATE N-ACETYLTRANSFERASE TRANSACETYLASE OATASE BIFUNCTIONAL BIOSYNTHESIS ARGININE ARGJ) protein domain (PD004193) which is seen in ARGJ_MYCPA.Residues 177-215 are 74% similar to a (ACETYLTRANSFERASE ORNITHINE GLUTAMATE N-ACETYLTRANSFERASE TRANSACETYLASE OATASE BIFUNCTIONAL BIOSYNTHESIS ARGININE ARGJ) protein domain (PDA0Q1M9) which is seen in Q6AGD2_BBBBB.Residues 218-398 are 63% similar to a (ACETYLTRANSFERASE ORNITHINE GLUTAMATE N-ACETYLTRANSFERASE TRANSACETYLASE OATASE BIFUNCTIONAL BIOSYNTHESIS ARGININE ARGJ) protein domain (PD004193) which is seen in ARGJ_MYCPA.","","-44% similar to PDB:1VZ6 ORNITHINE ACETYLTRANSFERASE (ORF6 GENE PRODUCT- CLAVULANIC ACID BIOSYNTHESIS) FROM STREPTOMYCES CLAVULIGERUS (E_value = 2.3E_36);-44% similar to PDB:1VZ7 ORNITHINE ACETYLTRANSFERASE (ORF6 GENE PRODUCT- CLAVULANIC ACID BIOSYNTHESIS) FROM STREPTOMYCES CLAVULIGERUS (E_value = 2.3E_36);-44% similar to PDB:1VZ8 ORNITHINE ACETYLTRANSFERASE (ORF6 GENE PRODUCT- CLAVULANIC ACID BIOSYNTHESIS) FROM STREPTOMYCES CLAVULIGERUS (SEMET STRUCTURE) (E_value = 2.3E_36);-45% similar to PDB:1VRA Crystal structure of Arginine biosynthesis bifunctional protein argJ (10175521) from Bacillus halodurans at 2.00 A resolution (E_value = 1.2E_21);","Residues 9 to 398 (E_value = 1.1e-147) place ANA_1030 in the ArgJ family which is described as ArgJ family.","","biosynthesis bifunctional protein ArgJ (argJ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1031","1108389","1107265","1125","5.31","-12.29","37822","ATGTATGGTTGCTGCATGACTTGGTCAGTTGCTGTTGCTGGAGCCACCGGGTACGCCGGTGGCGAGGTTCTGCGCCTGCTCACGGCCCACCCGGAAGTGGAGGTCGGCGCACTCACCGCGGCCTCGTCCGCCGGCAGTCGGCTCGGTGAGCACCATCCGCACCTGCTGTCCCTGGCGGACCGCATCGTCCAGCCCACCGAGGCGGAGATCCTCGCCGGGCACGACGTCGTCGTCCTGGCCCTGCCGCACGGGGCCTCCGGAGCCGTCACGGCGGCCCTCGAGGAGCTCGCCTCGGGCGGCAGCAACGCACCGCTACTCATTGACTGCGGCGCGGACCACCGTCTGACCAGTCAGCAGGCGTGGGAGGCCTTCTACGGCTCGGACTACGCCGGCGCCTGGACCTACGGCATGCCCGAGCTCCTGCACCACGGTGAGACGCGAGCCCGCGCCCAGCGCGAGGAGCTGGCAGCCTCCAGGCGCATCGCCGTCCCCGGCTGCAACGTCACCGCCGTCACCCTGCCGGTCCAGCCCGGCATCGCCGCCGGACTTCTCGACCCCTCCCGGCTGACCGCGGTGCTGGCCGTCGGATACTCCGGCGCAGGCAAGGCCCTCAAGCCCCATCTCACCGCTGCCGAGGCGCTGGGATCGGCTCAGCCCTACGCCGTCGGAGGCACTCACCGGCACATTCCCGAGATCGTTCAGAACCTGGAGGTGGCCGGAGCCGCCGCCGGAGCAGCACGCCTGTCCTTCACCCCGGTCCTGGTCCCCATGAGCCGCGGCATCCTGGCCACCGTCACCGCCCCCATGACTGCGGCTCTGCGCGAGGCCCCCGACCCCGAAGCCGCCCTGCGAGCCGCCTGGGATGACGCCTATGGGGCCACCGGTAGTGGCGAGAGCCTCATCCAGCTGCTGCCCGAGGGGACCTGGCCCATCACCGGCACCGTCCTGGGGAGCGGAACCGCTACCGTTCAGGTCGCCATCGACCGTGGTGCGGAGGCCGTCGTGGCCATGTGCGCCATCGACAACCTCGGCAAGGGCACCGCCAGCGCCGCCGTTCAGTCCCTCAACCTCGCCCTCGGGCTGGAGGAGACCACCGCCATCGTCGCCCAAGGAGTCGCACCGTGA","MYGCCMTWSVAVAGATGYAGGEVLRLLTAHPEVEVGALTAASSAGSRLGEHHPHLLSLADRIVQPTEAEILAGHDVVVLALPHGASGAVTAALEELASGGSNAPLLIDCGADHRLTSQQAWEAFYGSDYAGAWTYGMPELLHHGETRARAQREELAASRRIAVPGCNVTAVTLPVQPGIAAGLLDPSRLTAVLAVGYSGAGKALKPHLTAAEALGSAQPYAVGGTHRHIPEIVQNLEVAGAAAGAARLSFTPVLVPMSRGILATVTAPMTAALREAPDPEAALRAAWDDAYGATGSGESLIQLLPEGTWPITGTVLGSGTATVQVAIDRGAEAVVAMCAIDNLGKGTASAAVQSLNLALGLEETTAIVAQGVAP$","N-acetyl-gamma-glutamyl-phosphate reductase","Cytoplasm, Membrane","N-acetyl-gamma-glutamyl-phosphate reductase","N-acetyl-gamma-glutamyl-phosphate reductase ","N-acetyl-gamma-glutamyl-phosphate reductase","","Hadfield A., Kryger G., Ouyang J., Petsko G.A., Ringe D., Viola R. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. J. Mol. Biol. 1999. 289(4):991-1002. PMID: 10369777","","","

InterPro
IPR000534
Domain

Semialdehyde dehydrogenase, NAD - binding
PF01118	$\"[9-150]T$	Semialdhyde_dh

InterPro
IPR000706
Domain

N-acetyl-gamma-glutamyl-phosphate reductase
PD003765	$\"[195-363]T$	ARGC_BIFLO_P59305;
TIGR01850	$\"[8-374]T$	argC: N-acetyl-gamma-glutamyl-phosphate red
PS01224	$\"[161-177]T$	ARGC

InterPro
IPR011137
Family

N-acetyl-gamma-glutamyl-phosphate reductase, monofunctional
PIRSF000150	$\"[8-374]T$	N-acetyl-gamma-glutamyl-phosphate reductase

InterPro
IPR012280
Domain

Semialdehyde dehydrogenase, dimerisation region
PF02774	$\"[198-345]T$	Semialdhyde_dhC

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 18 clades of COG0002COG name: Acetylglutamate semialdehyde dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0002 is a-m-kzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000706 (N-acetyl-gamma-glutamyl-phosphate reductase) with a combined E-value of 4e-59. IPB000706A 12-31 IPB000706B 106-118 IPB000706C 161-178 IPB000706D 189-205 IPB000706E 221-232 IPB000706F 250-265 IPB000706G 334-367***** IPB012280 (Semialdehyde dehydrogenase, dimerisation region) with a combined E-value of 6.6e-07. IPB012280A 107-127 IPB012280B 161-178","Residues 58-177 are 64% similar to a (DEHYDROGENASE REDUCTASE N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE SEMIALDEHYDE OXIDOREDUCTASE NAGSA AGPR ARGININE BIOSYNTHESIS NADP) protein domain (PD811676) which is seen in ARGC_BIFLO.Residues 195-363 are 64% similar to a (DEHYDROGENASE REDUCTASE N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE SEMIALDEHYDE OXIDOREDUCTASE NAGSA AGPR ARGININE BIOSYNTHESIS NADP) protein domain (PD003765) which is seen in ARGC_BIFLO.","","-61% similar to PDB:2I3A Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis (E_value = 5.5E_85);-61% similar to PDB:2I3G Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis in complex with NADP+. (E_value = 5.5E_85);-61% similar to PDB:2NQT Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution (E_value = 5.5E_85);-48% similar to PDB:1VKN Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from Thermotoga maritima at 1.80 A resolution (E_value = 1.2E_36);-46% similar to PDB:1XYG X-RAY STRUCTURE OF GENE PRODUCT FROM ARABIDOPSIS THALIANA AT2G19940 (E_value = 3.4E_34);","Residues 9 to 150 (E_value = 2.3e-30) place ANA_1031 in the Semialdhyde_dh family which is described as Semialdehyde dehydrogenase, NAD binding domain.Residues 175 to 345 (E_value = 1.3e-10) place ANA_1031 in the Semialdhyde_dhC family which is described as Semialdehyde dehydrogenase, dimerisation domain.","","reductase (argC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1032","1108996","1108478","519","5.30","-4.55","19119","ATGAAGATCCTGCTGACCTCTTCCTCCAAGCACGGGTCCACCGACGAGGTGGCCGCGGTGATTGCTGAGCGGCTCCAGGCCGCCCAGATCGATGTGGAGACCAAGCGCCCCGAGGATGTCGACAGCGTCGAGGAGTATGACGCCTTCATCCTGGGCAGCGCGGTCTACATGACCAAGTGGACGCCGCAGGCCGTCGACTTCACCGAGCGCTTCCGTGACGTCCTCAGGGCCAGACCCGTGTGGGCCTTCTCCGTGGGGCTCTCCGGCCTGCCCAAGGGAAAGGTCGCCGACCCCATGCGCATCGGTCCGGTGCTGCTGGCCATCGACCCGGAGGACCACATGACCTTCGCGGGCCGCTTCGACCCCTCCAAGCTCAGTCTGCGGGAGCGCTCCATCGCCAAGCTCGGAGGAGCGAGTGAGGGCGACTACCGCAACTGGGACGAGGTGCGCGCGTGGGCCGACGCCATCGCGACCTCCCTCTATGACGACACACTCACCAGTCGCCGCGACCGCTCCTAG","MKILLTSSSKHGSTDEVAAVIAERLQAAQIDVETKRPEDVDSVEEYDAFILGSAVYMTKWTPQAVDFTERFRDVLRARPVWAFSVGLSGLPKGKVADPMRIGPVLLAIDPEDHMTFAGRFDPSKLSLRERSIAKLGGASEGDYRNWDEVRAWADAIATSLYDDTLTSRRDRS$","Flavodoxin-like protein","Cytoplasm","flavodoxin, putative","flavodoxin-like protein","Flavodoxin-like","","Wakabayashi S., Kimura T., Fukuyama K., Matsubara H., Rogers L.J. The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus. Biochem. J. 1989. 263(3):981-984. PMID: 2597140","","","

InterPro
IPR008254
Domain

Flavodoxin/nitric oxide synthase
PS50902	$\"[3-157]T$	FLAVODOXIN_LIKE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[2-83]T$	no description

","BeTs to 5 clades of COG0716COG name: FlavodoxinsFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0716 is a-m---y----lbcefghs-uj--t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1033","1111794","1109137","2658","5.22","-31.24","94186","ATGCCCTACGTCCCCATTGAATGGCTGCGCGAGCACGTCGACGTCCCCACCGGCCTGAGCGCCGAGCAGCTCGCCGCCGACCTTGTCCGCGTGGGCCTGGAGGAGGAGCGCATCGTTCCTCCGGCCGTCACCGGCCCCCTCGTCGTCGGCAAGGTCCTCACCCGCGAGGCCAAGGAGCAGTCCAACGGCAAGGTCATCAACTACTGCCGCGTCGACGTCGGCCCCGAGCACAACGACGCGCCCGGCACCGGCAAGGAGCCCTCCGACCTGCCCAGCCGCGGCATCGTCTGCGGCGCCCACAACTTCGACGTCGGTGACTACGTCGTCGTGTGCCTGCCCGGCGCCGTCCTGCCCGGCGACTTCCGCATCGCCGCGCGCAAGACCTACGGGCACGTCTCCGACGGCATGATCTGCTCGGCCCGCGAGCTCGGCATCGGGGAGGACCACTCCGGCATCATCGTGCTCCAGCAGTGGCTGGCCGAGCACGGTCATGAGGGAGAGGAGCCGCCCGCACCCGGGACCGACGCCATCGGCATCCTCGGCCTGGGGGAGGAGGTCCTGGAGATCAACGTGACCCCGGACCGCGGCTACTGCTTCGCCATGCGCGGCGTGGCCCGCGAGTACTCCCACTCCACCGGCGCCCGCTTCACCGACCCTGCCGACGCCACCAACACGGGGCTGTACCCCAACGGCGTGGCCGGCGCCGGGCAGGGCGGCTACGACGTCGTCGTCCCCGAGGATCCCCGCCCCATTCACGGGCGCCCCGGATGCGACCGCTACGTCGCCCGCCTCGTGCGCGGCATCGACCCGAGCGCACCGTCGCCGACCTGGATGCAGGACCGTCTCACCGCCGCAGGCATGCGCCCCATCTCCCTGGCCGTGGACGTCACCAACTACGTCATGCTCGACCTGGGCCAGCCGCTGCACGCCTTCGACGCCGGCAAGCTCACCGCCCCCATCGTCGTTCGTCGGGCGAAGGACGGCGAGCGCCTCACCTTCCTCGATGAGGTCACCCGCAGCCTCGACCCCGAGGACCTGGTCATCGCCGACTCCCCGGACGGTGAGGGCTCACGGGCCCTGGTCCTGGCCGGTGTCTTCGGCGGGGCCCTCAGCGAGGTCGACGCCGACACCCGTGACGTCCTCATCGAGGCCGCCCACTTCGACCCGGTCAGCGTGGCCCGTTCCTCGCGACGCCACAAGCTGCCCACCGAGTCCTCCAAGCGCAACGAGCGCGGCGTGGACACCGAGCTGGCCCCCATTGCCGCCCAGCGCGCCGTTGACCTGCTCGTGGAGTACGGCGGCGGCACCGCCGAGGCCGTGGCCACCGACATCAACCGCACCCGGGTCCCCGAGCCCATCACCATGCGCGCCGACGCCGCCGAGCGCCTCACCGGCGTCGCCTACGGAACCGAGCGCGTCACCGAGCTGCTCGCCACCATCGGCTGCACCGTGGAGCGCGGTGGCTCCACCGAGGACGGAACCGAGCTGCTGACCGTCACCCCGCCGACCTGGCGCCCGGACCTGGTGGGGCCTGCCCACCTGGCCGAGGAGATCGCCCGCCTCGACGGATACGATGCCATCCCGGTCATCGTGCCCACGGCCCCCGCCGGCACGGGGCTGAGCGCTGACCAGAGGGCCCGCCGCGACATCGTGCGCGCCCTGGCCGACGCCGGACTCACCCAGGTCCTGTCCTACCCCTTCATCGGGGACATCCACGACCTGCTCGAGATCCCGGCGGACGATGCTCGCCGCCAGAGGGTCCGCCTGGCCAACCCCCTGGCCGAGGACGCCCCCTACCTGCGCACCAGCGTGCTCGACTCCCTGGTCGATGTCACCCGGCGCAACGTCTCGCGCGGCCTGACTGACGTCGCCGTCTTCGAGCTCGGCTCCGTCACCCACCCGGCCGGCACCGTTCCCGCCCCGATCCCCGGCACCTCCGGGCGCCCCACCGACTCCGAGCAGGCAGCCCTCGAGGCGGGCATTCCCGCCCAGCCCACCCATATCGGCGCTGTCATGACCGGTGAGCACGAGCGCAGTGGAGTCCTGGGGGCCGGCCGTCCCTGGGACTGGGCCGACGCCGTCGAGGTGGTCCGCACCGTGGCCGCCGCGCTCGGGGTCACGATCGAGGTCCGCGCCCCCGAGTACCCCTACGCCCCCTGGCACCCCGGCCGCACCGCGGAGATCCGCCTGCCCGGCCGACGTCGGGGCAAGGAGATCGAGCCCGGCAGGCTCATCGCTCACGCCGGCGAGCTCCACCCGCGGGTGGTGCGCGCACTCGGCCTTCCGGAGCGGGCCTGCGCCGTCGAGATCGACCTCGACCCGCTGCTGGAGGCCGCCCGCAGCGCCGGAGCGCTCCAGGTCAAGGCCGTCTCCACCTTCCCGGCCGCCAAGGAGGACATCGCCCTCGTCGTCGACGAGACCACCACCGCGGCCGAGGTCGAGGCCCTGGTCAGGCAGGCCGCCGGGGACCTGGCCGAGGAGGTTCGCCTCTTCGACGTCTTCCGCGGACCCCAGCTCGGCGAGGGTAAGAAGTCGTTGGCGTTCTCCCTGGTGCTGCGAGCCCCTGACCGCACGCTGACCGCCGAGGAGACCGCCGGTGTGCGCAAGCGCGTGGTCAAGAGGGCCGCCAAGCTCCTCGGAGCCGAGCTGCGCAGCTGA","MPYVPIEWLREHVDVPTGLSAEQLAADLVRVGLEEERIVPPAVTGPLVVGKVLTREAKEQSNGKVINYCRVDVGPEHNDAPGTGKEPSDLPSRGIVCGAHNFDVGDYVVVCLPGAVLPGDFRIAARKTYGHVSDGMICSARELGIGEDHSGIIVLQQWLAEHGHEGEEPPAPGTDAIGILGLGEEVLEINVTPDRGYCFAMRGVAREYSHSTGARFTDPADATNTGLYPNGVAGAGQGGYDVVVPEDPRPIHGRPGCDRYVARLVRGIDPSAPSPTWMQDRLTAAGMRPISLAVDVTNYVMLDLGQPLHAFDAGKLTAPIVVRRAKDGERLTFLDEVTRSLDPEDLVIADSPDGEGSRALVLAGVFGGALSEVDADTRDVLIEAAHFDPVSVARSSRRHKLPTESSKRNERGVDTELAPIAAQRAVDLLVEYGGGTAEAVATDINRTRVPEPITMRADAAERLTGVAYGTERVTELLATIGCTVERGGSTEDGTELLTVTPPTWRPDLVGPAHLAEEIARLDGYDAIPVIVPTAPAGTGLSADQRARRDIVRALADAGLTQVLSYPFIGDIHDLLEIPADDARRQRVRLANPLAEDAPYLRTSVLDSLVDVTRRNVSRGLTDVAVFELGSVTHPAGTVPAPIPGTSGRPTDSEQAALEAGIPAQPTHIGAVMTGEHERSGVLGAGRPWDWADAVEVVRTVAAALGVTIEVRAPEYPYAPWHPGRTAEIRLPGRRRGKEIEPGRLIAHAGELHPRVVRALGLPERACAVEIDLDPLLEAARSAGALQVKAVSTFPAAKEDIALVVDETTTAAEVEALVRQAAGDLAEEVRLFDVFRGPQLGEGKKSLAFSLVLRAPDRTLTAEETAGVRKRVVKRAAKLLGAELRS$","Phenylalanyl-tRNA synthetase, beta subunit","Cytoplasm","Phenylalanyl-tRNA synthetase betachain(Phenylalanine--tRNA ligase beta chain) (PheRS)","phenylalanyl-tRNA synthetase; beta subunit ","phenylalanyl-tRNA synthetase, beta subunit","","Wolf Y.I., Aravind L., Grishin N.V., Koonin E.V. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999. 9(8):689-710. PMID: 10447505Goldgur Y., Mosyak L., Reshetnikova L., Ankilova V., Lavrik O., Khodyreva S., Safro M. The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. Structure 1997. 5(1):59-68. PMID: 9016717","","","

InterPro
IPR002547
Domain

t-RNA-binding region
PF01588	$\"[47-157]T$	tRNA_bind
PS50886	$\"[41-167]T$	TRBD

InterPro
IPR004532
Family

Bacterial phenylalanyl-tRNA synthetase, beta subunit
TIGR00472	$\"[4-884]T$	pheT_bact: phenylalanyl-tRNA synthetase, be

InterPro
IPR005121
Domain

Ferredoxin-fold anticodon-binding
G3DSA:3.30.70.380	$\"[793-877]T$	no description
PF03147	$\"[791-884]T$	FDX-ACB

InterPro
IPR005146
Domain

B3/4
PF03483	$\"[256-434]T$	B3_4

InterPro
IPR005147
Domain

tRNA synthetase, B5
G3DSA:3.30.56.20	$\"[450-529]T$	no description
PF03484	$\"[450-524]T$	B5

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[40-173]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[541-773]T$	no description
G3DSA:3.50.40.10	$\"[251-449]T$	no description
PTHR10947	$\"[95-636]T$ $\"[653-885]T$	PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN

","BeTs to 24 clades of COG0072COG name: Phenylalanyl-tRNA synthetase beta subunitFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0072 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005121 (Ferredoxin-fold anticodon binding domain) with a combined E-value of 6.5e-36. IPB005121A 2-14 IPB005121B 95-108 IPB005121C 133-144 IPB005121D 295-312 IPB005121E 502-525***** IPB005147 (tRNA synthetase B5 domain) with a combined E-value of 1e-32. IPB005147A 193-208 IPB005147B 502-527 IPB005147C 587-609 IPB005147D 736-770***** IPB005146 (B3/4 domain) with a combined E-value of 3.6e-28. IPB005146A 95-108 IPB005146B 189-208 IPB005146C 502-527 IPB005146D 732-753","Residues 1-46 are 78% similar to a (CHAIN SYNTHETASE BETA LIGASE PHENYLALANYL-TRNA TR METAL-BINDING TRNA PHERS BIOSYNTHESIS) protein domain (PD773812) which is seen in SYFB_BIFLO.Residues 47-145 are 70% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BETA CHAIN BIOSYNTHESIS ATP-BINDING RNA-BINDING METAL-BINDING PHENYLALANYL-TRNA) protein domain (PD002123) which is seen in Q6A7V6_PROAC.Residues 146-271 are 62% similar to a (SYNTHETASE BETA CHAIN LIGASE PHENYLALANYL-TRNA METAL-BINDING PHERS AMINOACYL-TRNA ATP-BINDING RNA-BINDING) protein domain (PD773815) which is seen in SYFB_BIFLO.Residues 210-473 are 64% similar to a (PHENYLALANYL-TRNA SYNTHETASE AMINOACYL-TRNA BETA SUBUNIT SYNTHETASE) protein domain (PDA18991) which is seen in Q6AGD6_BBBBB.Residues 254-475 are 54% similar to a (SYNTHETASE BETA CHAIN LIGASE PHENYLALANYL-TRNA METAL-BINDING PHERS AMINOACYL-TRNA ATP-BINDING RNA-BINDING) protein domain (PDA190R3) which is seen in SYFB_DEIRA.Residues 254-465 are 58% similar to a (SYNTHETASE BETA CHAIN LIGASE PHENYLALANYL-TRNA METAL-BINDING PHERS AMINOACYL-TRNA ATP-BINDING RNA-BINDING) protein domain (PDA196G9) which is seen in SYFB_SYNP7.Residues 260-476 are 50% similar to a (SYNTHETASE BETA CHAIN LIGASE PHENYLALANYL-TRNA METAL-BINDING PHERS AMINOACYL-TRNA ATP-BINDING RNA-BINDING) protein domain (PDA1A135) which is seen in SYFB_SYNPX.Residues 272-435 are 76% similar to a (SYNTHETASE BETA LIGASE CHAIN PHENYLALANYL-TRNA AMINOACYL-TRNA METAL-BINDING PHERS ATP-BINDING MAGNESIUM) protein domain (PD351643) which is seen in SYFB_BIFLO.Residues 520-883 are 41% similar to a (SYNTHETASE PHENYLALANYL-TRNA AMINOACYL-TRNA BETA CHAIN LIGASE) protein domain (PDA1C7V4) which is seen in Q7UP77_RHOBA.Residues 520-609 are 69% similar to a (SYNTHETASE BETA LIGASE CHAIN AMINOACYL-TRNA PHENYLALANYL-TRNA TRNA PHERS ATP-BINDING BIOSYNTHESIS) protein domain (PD511632) which is seen in SYFB_STRCO.Residues 614-683 are 59% similar to a (SYNTHETASE CHAIN BETA LIGASE PHENYLALANYL-TRNA AMINOACYL-TRNA TR METAL-BINDING TRNA PHERS) protein domain (PDA0D9E2) which is seen in Q740J0_MYCPA.Residues 625-773 are 62% similar to a (SYNTHETASE BETA LIGASE CHAIN AMINOACYL-TRNA PHENYLALANYL-TRNA PHERS TRNA ATP-BINDING PHENYLALANINE--) protein domain (PD003388) which is seen in SYFB_STRCO.Residues 794-884 are 71% similar to a (SYNTHETASE BETA LIGASE CHAIN AMINOACYL-TRNA PHENYLALANYL-TRNA PHERS ATP-BINDING TRNA METAL-BINDING) protein domain (PD554800) which is seen in SYFB_COREF.","","-45% similar to PDB:1B70 PHENYLALANYL TRNA SYNTHETASE COMPLEXED WITH PHENYLALANINE (E_value = 1.4E_95);-45% similar to PDB:1B7Y PHENYLALANYL TRNA SYNTHETASE COMPLEXED WITH PHENYLALANINYL-ADENYLATE (E_value = 1.4E_95);-45% similar to PDB:1EIY THE CRYSTAL STRUCTURE OF PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH COGNATE TRNAPHE (E_value = 1.4E_95);-45% similar to PDB:1JJC Crystal structure at 2.6A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese (E_value = 1.4E_95);-45% similar to PDB:1PYS PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (E_value = 1.4E_95);","Residues 47 to 157 (E_value = 1.8e-08) place ANA_1033 in the tRNA_bind family which is described as Putative tRNA binding domain.Residues 256 to 434 (E_value = 1.3e-91) place ANA_1033 in the B3_4 family which is described as B3/4 domain.Residues 450 to 524 (E_value = 1.8e-16) place ANA_1033 in the B5 family which is described as tRNA synthetase B5 domain.Residues 791 to 884 (E_value = 3.8e-40) place ANA_1033 in the FDX-ACB family which is described as Ferredoxin-fold anticodon binding domain.","","synthetase beta chain(Phenylalanine--tRNA ligase beta chain) (PheRS) (pheT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1034","1112881","1111796","1086","4.96","-19.46","38837","ATGACTGACGCTCCCGGCGCGCTCTCTCCCCTGGACGAGGACGGCATCAATGCCGCCGTCGAGGAGGCCCTGGCCGCCTTCGCCGCAGCCGGCACCCTCGCCGAGCTCAAGGAGGCCCGCCTGGCCCACACCGGCGACGCCTCGCCCCTGACCCTGGCCAACCGGCTCATCGGCACCCTGGACAAGGCGGACAAGCCCACCGCCGGCAAGCTCCTGGGCGGCGCTCGCGGGCGCATCGCCAAGGCTCTGACCGCCAGGCAGGAGACCCTCGAGGCCGCCGCCGAGGAGGAGATGCTGCGCACCGAGGCCGTCGATGTCACCATCCCCACCTCGCGCACGCAGGCCGGTGCCCGGCACCCCCTCGACGTGCTCATCGACGAGGTCTGCGACTTCTTCACCTCCATGGGCTGGTCCATCGCCGAGGGGCCGGAGGTCGAGCACGAGTGGTTCGACTTCGACGCCCTCAACTTCGACGCCGACCACCCCGCCCGCCAGATGCAGGACACCTTCTACATCGACGGCGCCAGCGTCGGGGCCGGAGAGGGGCAGGCTGCCAACCTCGTGCTGCGCACCCACACCTCCCCGGTCCAGGCCCGCGTCATGCTCGAGCAGCAGCCCCCGCTCTACGTGGCCTGCCCCGGCAAGGTCTTCCGCTCCGACGAGCTCGACGCCACCCACACCCCCGTCTTCCACCAGGTCGAGGGCCTGGCCGTGGACAAGGGCCTGACGATGGCGCACCTCAAGGGCGTCCTGGACCACTTCGCCAAGGCCATGTTCGGCCCCGAGGCACGCACTCGCCTGCGCCCCTCCTTCTTCCCCTTCACCGAGCCCAGCGCCGAGATGGACCTGTGGTTCCCCCAGAAGAAGGGCGGTGCAGGCTGGATCGAGTGGGGAGGCTGCGGCATGGTCAACCCCAACGTGCTCACCGCCTGCGGCATCGACCCCGAGGTCTACACGGGCTTCGCCTTCGGCATGGGCCTGGAGCGTACCCTCATGCTGCGCCACGGAATCGCCGACATGCATGACATCGTCGAGGGCGACATCCGCTTCTCCCAGCAGTTCGGCACCACCGGAAAGGGAAACTGA","MTDAPGALSPLDEDGINAAVEEALAAFAAAGTLAELKEARLAHTGDASPLTLANRLIGTLDKADKPTAGKLLGGARGRIAKALTARQETLEAAAEEEMLRTEAVDVTIPTSRTQAGARHPLDVLIDEVCDFFTSMGWSIAEGPEVEHEWFDFDALNFDADHPARQMQDTFYIDGASVGAGEGQAANLVLRTHTSPVQARVMLEQQPPLYVACPGKVFRSDELDATHTPVFHQVEGLAVDKGLTMAHLKGVLDHFAKAMFGPEARTRLRPSFFPFTEPSAEMDLWFPQKKGGAGWIEWGGCGMVNPNVLTACGIDPEVYTGFAFGMGLERTLMLRHGIADMHDIVEGDIRFSQQFGTTGKGN$","Phenylalanyl-tRNA synthetase, alpha subunit","Cytoplasm","phenylalanyl-tRNA synthetase, alpha subunit","phenylalanyl-tRNA synthetase alpha chain ","phenylalanyl-tRNA synthetase, alpha subunit","","Eriani G., Delarue M., Poch O., Gangloff J., Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 1990. 347(6289):203-206. PMID: 2203971Sugiura I., Nureki O., Ugaji-Yoshikawa Y., Kuwabara S., Shimada A., Tateno M., Lorber B., Giege R., Moras D., Yokoyama S., Konno M. The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. Structure 2000. 8(2):197-208. PMID: 10673435Perona J.J., Rould M.A., Steitz T.A. Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry 1993. 32(34):8758-8771. PMID: 8364025","","","

InterPro
IPR002319
Family

Phenylalanyl-tRNA synthetase, class IIc
PTHR11538	$\"[102-354]T$	PHENYLALANYL-TRNA SYNTHETASE
PF01409	$\"[103-354]T$	tRNA-synt_2d

InterPro
IPR004188
Domain

Aminoacyl tRNA synthetase, class II, N-terminal
PF02912	$\"[28-100]T$	Phe_tRNA-synt_N

InterPro
IPR004529
Family

Phenylalanyl-tRNA synthetase, alpha subunit
TIGR00468	$\"[49-356]T$	pheS: phenylalanyl-tRNA synthetase, alpha s

InterPro
IPR006195
Domain

Aminoacyl-transfer RNA synthetase, class II
PS50862	$\"[130-333]T$	AA_TRNA_LIGASE_II

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[19-354]T$	no description

","BeTs to 26 clades of COG0016COG name: Phenylalanyl-tRNA synthetase alpha subunitFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0016 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB004188 (Aminoacyl tRNA synthetase, class II, N-terminal) with a combined E-value of 4.9e-136. IPB004188A 63-111 IPB004188B 132-172 IPB004188C 188-201 IPB004188D 207-251 IPB004188E 266-283 IPB004188F 303-354***** IPB002319 (Phenylalanyl-tRNA synthetase, class IIc) with a combined E-value of 6.6e-83. IPB002319A 142-172 IPB002319B 188-199 IPB002319C 223-236 IPB002319D 266-282 IPB002319E 294-308 IPB002319F 320-350","Residues 105-251 are 80% similar to a (SYNTHETASE ALPHA LIGASE CHAIN AMINOACYL-TRNA PHENYLALANYL-TRNA PHENYLALANINE--TRNA PHERS ATP-BINDING BIOSYNTHESIS) protein domain (PD002080) which is seen in SYFA_STRAW.Residues 258-354 are 92% similar to a (SYNTHETASE ALPHA LIGASE CHAIN AMINOACYL-TRNA PHENYLALANYL-TRNA PHENYLALANINE--TRNA PHERS ATP-BINDING BIOSYNTHESIS) protein domain (PD006935) which is seen in SYFA_BIFLO.","","-60% similar to PDB:1B70 PHENYLALANYL TRNA SYNTHETASE COMPLEXED WITH PHENYLALANINE (E_value = 3.5E_57);-60% similar to PDB:1B7Y PHENYLALANYL TRNA SYNTHETASE COMPLEXED WITH PHENYLALANINYL-ADENYLATE (E_value = 3.5E_57);-60% similar to PDB:1EIY THE CRYSTAL STRUCTURE OF PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH COGNATE TRNAPHE (E_value = 3.5E_57);-60% similar to PDB:1JJC Crystal structure at 2.6A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese (E_value = 3.5E_57);-60% similar to PDB:1PYS PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (E_value = 3.5E_57);","Residues 28 to 100 (E_value = 9.1e-13) place ANA_1034 in the Phe_tRNA-synt_N family which is described as Aminoacyl tRNA synthetase class II, N-terminal domain.Residues 103 to 354 (E_value = 1.8e-147) place ANA_1034 in the tRNA-synt_2d family which is described as tRNA synthetases class II core domain (F).","","synthetase, alpha subunit (pheS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1035","1113096","1113959","864","6.81","-0.90","31737","ATGAACGTCAAGGAGCTCGCCCGGATCGCCGGAACCACGCCGAGGGCGGTGCGCTACTACCACCACCTGGGTCTGCTGGAGATTCCGCCCACGGTGCGGGGGCGGCGCGAGTACGGCGTCGAGCACGTGGCCCGTCTGCTGCGTATCCGGTGGCTGGCCGACGGCGGACTGTCGCTGACCCAGGTGGCGGAGATGCTCGCCTCGGACACGATCGGCACCGATCAGGACTCCCGCCGTGAGGCGGTGCTGCGCGATCTGCGCGCCACGCGAGGCACGATCGAGGCCCAGCAGCGCAGCCTGGCCGAGCAGGCGTCCCGGGTCGATGAGCTCATCGCCCGGGTGGAGCGCGGTGAGGGCCTGTCCCCCGCTCCCAGTGCCCTGACTCGTTTCTATGACGACATCGAGGCTCGGATCGTCCGGCTGGGCGGCAGTGTGCGCGGCCTGCGGGCTGAGCGCCAGATGATGGTGGTGCTCGCCTCTCTGGGCATGGTGCCCGACAGTGCGATCCCCTTCATCGAGGCGCTCGATGAGGACGATCGCGAGCTGTCCGCCCAGCAGGTTGCGGACTTCGCCCGCCTGGCCACGCTGAGCGAGGCCGAGGGGCGCGCTGAGGCGCACCGGCTCGCGCACAACAGCTGGACACTGGCGTGCCGCCACAAGAAGCACGCCCTGGCAGTCCTGAACGATCTTCCCTCGGGAGCCCTGGGGCGCGCTATGTGGCGACTGACCCATGTGCTGACCACTTGCAGCTACCCCCATCCTGCTCAACAGGCCTTCGTGGCTGAGCTCATCGAGCTCATGCTCACCGATCCGGACTTCGCCGCAACAATCCGCCGCTCGGCGGGAGAGGAACCAGTGCTGTGA","MNVKELARIAGTTPRAVRYYHHLGLLEIPPTVRGRREYGVEHVARLLRIRWLADGGLSLTQVAEMLASDTIGTDQDSRREAVLRDLRATRGTIEAQQRSLAEQASRVDELIARVERGEGLSPAPSALTRFYDDIEARIVRLGGSVRGLRAERQMMVVLASLGMVPDSAIPFIEALDEDDRELSAQQVADFARLATLSEAEGRAEAHRLAHNSWTLACRHKKHALAVLNDLPSGALGRAMWRLTHVLTTCSYPHPAQQAFVAELIELMLTDPDFAATIRRSAGEEPVL$","Transcriptional regulator, MerR family","Cytoplasm","conserved hypothetical protein","hypothetical protein","regulatory protein, MerR","","Holmes D.J., Caso J.L., Thompson C.J. Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 1993. 12(8):3183-3191. PMID: 7688297Helmann J.D., Wang Y., Mahler I., Walsh C.T. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons. J. Bacteriol. 1989. 171(1):222-229. PMID: 2492496Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 1995. 177(14):3904-3910. PMID: 7608059Nakano Y., Kimura K. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 1991. 109(2):223-228. PMID: 1677938Sadowsky M.J., Cregan P.B., Gottfert M., Sharma A., Gerhold D., Rodriguez-Quinones F., Keyser H.H., Hennecke H., Stacey G. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(2):637-641. PMID: 1988958Helmann J.D., Ballard B.T., Walsh C.T. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. Science 1990. 247(4945):946-948. PMID: 2305262","","","

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PF00376	$\"[2-38]T$	MerR
SM00422	$\"[1-69]T$	HTH_MERR
PS50937	$\"[1-68]T$	HTH_MERR_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[1-116]T$	no description

","BeTs to 9 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 8","***** IPB000551 (Bacterial regulatory protein, MerR family) with a combined E-value of 1.9e-09. IPB000551 1-41","Residues 1-116 are 51% similar to a (TRANSCRIPTIONAL DNA-BINDING REGULATOR) protein domain (PD822168) which is seen in Q9KY77_STRCO.Residues 6-100 are 52% similar to a (DNA-BINDING TRANSCRIPTIONAL REGULATOR MERR FAMILY REGULATOR REGULATORY PLASMID TRANSCRIPTION ACTIVATOR) protein domain (PD548366) which is seen in Q82M74_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 38 (E_value = 3.4e-08) place ANA_1035 in the MerR family which is described as MerR family regulatory protein.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1036","1113995","1114972","978","5.39","-7.15","34622","ATGTCAGCAGCGACGTCCCGCTCGGATAGGGATGAGCCCACCACGGACTCCTCTCCCACCGCGGTTCGTGACCTGGGCGCCGGCGGCGAGCCGCCGGTACGCGTGTGCGGCTTGGTCAAGCGCTTCGGGCGCTTCAGGGCGCTCGACGGCCTGGACCTGACGGTGGAGGCGGGCAGCGTCCACGGTTTCCTCGGCCCCAATGGGGCCGGGAAATCCACCACGATCCGTGTCCTGCTGGGGCTCTACCGGCCCGATGGTGGAAGCGTGAGCGTGCTGGGCTGCGAGCCGTGGCGGCAGGCCGCGCTCATCAACCGGCAGGTCTCCTATGTTCCCGGTGACGTGGCGCTGTGGCCGGCCCTGACCGGTGGCCAGGTGCTCGACGCCCTGGCCGGGCTGCGCGGCTCTCGCGACGCCGAGCGGGAGGCCGAGCTCATTGAGCGCTTTGACTTGGATCCGAGCAAACGAGTACGGACCTACTCCAAGGGGAACCGGCAGAAGGTGGCACTCGTGGCCGCCCTGGCCGCGCCCACGAGCCTGCTGGTGCTCGATGAGCCCACCAGCGGCCTGGATCCGCTCATGGAACGGGTCTTCACCGAGGAGGTTGCCAGAGCCGCTGCCGAGGGCCGCACGGTTCTGCTCTCCAGTCACATCCTGGCCGAGGTCCAGCGCCTGTGCAGTGCGGTGACGATCATCAAGGACGGCCGGGTCGTCGAGCAGGGCGACCTGGGGACCCTGCGGCGGCTGTCGCGCACCCGCATCGAGCTGGGGGCCGCAAGCGACAAGCTCGGCACCGTCAGGCAGGCGGTGGAGGCCCTGGGGCTCGACGTCGTCGAGGATGGTGGCCGCCTGAGCCTTGAGGTGGCGGCGGAGCAGGTGCCGGCGGTGCTGAGCCTGGCGGGCGAGCACCGGATCCAGGACGTCACCTGCGAGCCGGCCAGCTTGGAGGATCTCTTCCTGCGTCACTACGAGGAGGCCTGA","MSAATSRSDRDEPTTDSSPTAVRDLGAGGEPPVRVCGLVKRFGRFRALDGLDLTVEAGSVHGFLGPNGAGKSTTIRVLLGLYRPDGGSVSVLGCEPWRQAALINRQVSYVPGDVALWPALTGGQVLDALAGLRGSRDAEREAELIERFDLDPSKRVRTYSKGNRQKVALVAALAAPTSLLVLDEPTSGLDPLMERVFTEEVARAAAEGRTVLLSSHILAEVQRLCSAVTIIKDGRVVEQGDLGTLRRLSRTRIELGAASDKLGTVRQAVEALGLDVVEDGGRLSLEVAAEQVPAVLSLAGEHRIQDVTCEPASLEDLFLRHYEEA$","ABC-type multidrug transport system, ATPase component","Membrane, Cytoplasm","ABC transporter, ATP-binding protein","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[158-199]T$	Q9Z9N6_BACHD_Q9Z9N6;
PF00005	$\"[58-234]T$	ABC_tran
PS50893	$\"[33-258]T$	ABC_TRANSPORTER_2
PS00211	$\"[159-173]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[57-259]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[27-247]T$	no description
PTHR19222	$\"[33-247]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[33-247]T$	ABC TRANSPORTER

","BeTs to 20 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 8.9e-23. IPB005074C 47-94 IPB005074D 147-190***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3.5e-22. IPB013563A 47-81 IPB013563C 156-183 IPB013563D 210-262***** IPB005116 (TOBE domain) with a combined E-value of 4.9e-15. IPB005116A 65-81 IPB005116B 105-122 IPB005116C 159-172 IPB005116D 179-198 IPB005116E 212-225***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.3e-08. IPB010509B 58-83 IPB010509D 154-198***** IPB013283 (ABC transporter family E signature) with a combined E-value of 4.1e-06. IPB013283D 62-87","Residues 1-127 are 48% similar to a (ATP-BINDING PROTEIN CYDCD) protein domain (PDA1B3E1) which is seen in Q6ABD5_PROAC.Residues 25-109 are 61% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 29-92 are 57% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3K8) which is seen in Q9A6K2_CAUCR.Residues 33-146 are 46% similar to a (ATP-BINDING NATA ABC TRANSPORTER) protein domain (PD742287) which is seen in O83851_TREPA.Residues 35-146 are 56% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 38-152 are 50% similar to a (ABC-TYPE ATP-BINDING) protein domain (PD253636) which is seen in Q9HQA8_HALN1.Residues 40-245 are 45% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 42-135 are 48% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 43-240 are 45% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 46-182 are 47% similar to a (BLL4315 ATP-BINDING) protein domain (PD728322) which is seen in Q89M78_BRAJA.Residues 47-245 are 44% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 47-239 are 41% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 48-150 are 53% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187K3) which is seen in Q897D7_CLOTE.Residues 48-93 are 86% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q7U0D2_MYCBO.Residues 48-214 are 46% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 48-246 are 49% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 51-233 are 47% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD398054) which is seen in Q9CDL6_LACLA.Residues 53-218 are 50% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 62-246 are 43% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 96-157 are 74% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD330782) which is seen in Q8FNV6_COREF.Residues 123-231 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737529) which is seen in Q8ET36_OCEIH.Residues 153-231 are 59% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18641) which is seen in Q8EG59_SHEON.Residues 154-246 are 58% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 158-199 are 85% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9Z9N6_BACHD.Residues 160-282 are 52% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD957735) which is seen in Q73JF3_TREDE.Residues 160-231 are 59% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ABC-TYPE MULTIDRUG LMO2240 LMO2769 ABC-NBD) protein domain (PD353124) which is seen in Q8DTX3_STRMU.Residues 217-316 are 56% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE ABC-TYPE BACITRACIN MULTIDRUG SYSTEM) protein domain (PD424436) which is seen in Q8NLB0_CORGL.","","-55% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 2.0E_32);-49% similar to PDB:2ONK ABC transporter ModBC in complex with its binding protein ModA (E_value = 1.4E_17);-48% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 6.9E_17);-49% similar to PDB:1JI0 Crystal Structure Analysis of the ABC transporter from Thermotoga maritima (E_value = 1.5E_16);-51% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.3E_15);","Residues 58 to 234 (E_value = 3.8e-38) place ANA_1036 in the ABC_tran family which is described as ABC transporter.","","transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1037","1114972","1116642","1671","8.45","4.77","59352","ATGAGCGCCGTATTGAGCACAGCTGCGGGCGAGTCAGCACCAGCTATCAGCTCTAACGCAACCAGCCCCCTTGCCGGCTGGGAGGCCTACCTGTGGATTCTGCTCAGACGATTCCGGTTTCAGATCGTGGCCTGGCTGGCGCCCCTGTGGCTGTTGGTCGGTGTCACCGCACCGAGCTACGAGAGCGTCTACCCCTCATTGGCGACCCGGACGGTGCTCATCGAGCAGATGCGCAAGTCTCCGGGAACGCGCCTCCTCTACGGCTATGTCCCCTTGCCCGGCCGGCTCGGTCAGCTCCTGCAGTGGGAGACGGGGACCTTCCTGCTCGTGTGCACCGCACTCATGGCGATTCTGCTGACCTGCCGGGTATTGCGGGCCGATGAGGATGAGGGGCTCGTCGAGGTTCTGCGCGCCACGGGCGCGGGCAGGTCGGTTCCTTTTCTCGTACCGGTAGCCCTGATCTGGGTGGTGGTCGTCGCCCTGTCTGCGGGCGTCGGAGGCATTCTGACCTGGCAGACCGAGAGCATCGAGGAGCTGACGGTGAGCGGGGCCTGGGCACTGGCCGGGACGATCTGCGTGACGGGCTGGGCGTTCTCGGCAATCGCGGCAGTGGCCTGCCAGCTGGGTCGTCAAGTGGGCCAGGCCAGGGGCCTGTCCATGCTAGTGCTCGCACTCGCCTTCGCGATGCGGGTGAGCGCCGACCAGATCTCAGACGACACCGACTCGGACTGGCTCCGGTGGCTGACTCCCCTGGGGTGGCGCGACCTCGTACGCCCGTACACCGATGACCGGTTCGCGGTGCTCCCGGTGTGCTGCACCGTAGCCATCACTGTGGCACTGAGCGCCATGGTGCTCGCCGCGCGCCGCGAGTACCTGGACGGCTACCTGCCCGACCGCAGCTCGTCTCGGCGCCGGTGGCGGGTGCGGGGGCACATGGATCTGCTCGGGCGCCTGTCATGGCGGAGCCTCATCGGCTGGGCACTGGCCTCGACGGCTCTGGCACTCCTGTACGGCTCGGTGTCCGGCAGCATCAAGGACCTGCTGGCCCCCGGTTCTCCGACGGCCTCCTGGGTCGGCAAGATGGCCGTGGGGTCCCCGGTGGAGCAGTTCATGTCCCTCATGACGGTGGTCACGACGCTGCTTGTGGCCGTGGCGGCGGTGCGACGGGTGAACGGGTTGGCGGGCCTGGAGCGCGCGGGACTGGTGGAGGTCGAGCTCGCTGCCGGGGTCAGTCGTGGCCGAGTCCTCCTCTCCCAGGTTCTATACGCGCTGATCGAGTCGATCGTCCTACTGCTGGTCTCGGCGACGGTTCTGGCGGCGACGACGGCGACTCAGCTCACCGACGACCACGCCGTAGGGCGCTCCTTCGTGTTCACGGTGAGTCAGCTGCCCGGCATGGTGGCAGCCATCGGGATCGCAGCCGCCCTGGTGGGTCTGGCGCCAAGACTGACCGGCCTGTCCTGGGCGGCCGTCACCTGGAGCGCTTTCGCCCAGTTCTTCGGCGGACTCGTCGAGCTTAAGGACTGGGCCAAGGATCTCAGCGTGCTCGGGCACCATCTCGACGTCGTCGGAACCCCCGACTGGAAGCCCCTGGCCGTCCAGACCGTGGTTGGCCTCATCGGCATCACGATCGGCCTGGTCGCCTACACCCGCCGCGACCTGCCCTCCTGA","MSAVLSTAAGESAPAISSNATSPLAGWEAYLWILLRRFRFQIVAWLAPLWLLVGVTAPSYESVYPSLATRTVLIEQMRKSPGTRLLYGYVPLPGRLGQLLQWETGTFLLVCTALMAILLTCRVLRADEDEGLVEVLRATGAGRSVPFLVPVALIWVVVVALSAGVGGILTWQTESIEELTVSGAWALAGTICVTGWAFSAIAAVACQLGRQVGQARGLSMLVLALAFAMRVSADQISDDTDSDWLRWLTPLGWRDLVRPYTDDRFAVLPVCCTVAITVALSAMVLAARREYLDGYLPDRSSSRRRWRVRGHMDLLGRLSWRSLIGWALASTALALLYGSVSGSIKDLLAPGSPTASWVGKMAVGSPVEQFMSLMTVVTTLLVAVAAVRRVNGLAGLERAGLVEVELAAGVSRGRVLLSQVLYALIESIVLLLVSATVLAATTATQLTDDHAVGRSFVFTVSQLPGMVAAIGIAAALVGLAPRLTGLSWAAVTWSAFAQFFGGLVELKDWAKDLSVLGHHLDVVGTPDWKPLAVQTVVGLIGITIGLVAYTRRDLPS$","ABC-type multidrug transport system, permease component","Membrane, Cytoplasm","putative membrane protein","K01992 ABC-2 type transport system permease protein","Putative exporter of polyketide antibiotics-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-57]?$	signal-peptide
tmhmm	$\"[42-60]?$ $\"[99-119]?$ $\"[151-171]?$ $\"[185-205]?$ $\"[217-237]?$ $\"[265-285]?$ $\"[322-340]?$ $\"[369-387]?$ $\"[421-441]?$ $\"[460-480]?$ $\"[485-503]?$ $\"[530-550]?$	transmembrane_regions

","BeTs to 3 clades of COG3559COG name: Putative exporter of polyketide antibioticsFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG3559 is ----------rlb-------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 35-140 are similar to a (ABC TRANSPORTER PERMEASE MEMBRANE TETRONASIN-TRANSPORT PROBABLE INTEGRAL TRANSPORTER ABC-TRANSPORTER TNRB3) protein domain (PD015782) which is seen in Q8NLA9_CORGL.Residues 182-341 are 50% similar to a (ABC TRANSPORTER PERMEASE MEMBRANE TETRONASIN-TRANSPORT PROBABLE INTEGRAL TRANSPORTER ABC-TRANSPORTER TNRB3) protein domain (PD034539) which is seen in Q9X8Q1_STRCO.","","-52% similar to PDB:2FAF The structure of chicken mitochondrial PEPCK. (E_value = );-52% similar to PDB:2FAG The structure of chicken mitochondrial PEPCK. (E_value = );-52% similar to PDB:2FAH The structure of mitochondrial PEPCK, Complex with Mn and GDP (E_value = );","No significant hits to the Pfam 21.0 database.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1038","1118291","1117416","876","9.81","8.15","31949","ATGAGCTCAGACATCATGCCGATGACAGAGCCCCGTCCACGCCGTCAGCGGAGTCAGGACTCCGGGGCGACGGATGCGGCACTGCTCTTCGATGAGCCCGGGCCGCGGGGGCGCATCCTGATCGCCATCGGATCAGTCGTCGCCGTCATCGGAATCGCGGGGCTGGCGGCCGCGGTCCTCTACCGGCTGGACCTCGCGGGACAGCTCGATTATCCCAAGTGGCGCTACTTCCTGGGGCAGTCGGTCGTCAGTCAGCTTCTGGAGGCGGCCGGGACCACGTTGACCCTGGGGGGCGTTGCTGCGGTACTCACCTTTCCCCTGGGAATCGCCTTGGGCTGGCTCCGCCTGCTGGACAACCGCCCCATCAAGTGGCTGGTCGGCCTGTGGGTCGATGCCATGCGGGCGGTGCCGATGCTGCTGCTCGTCTACTTCTTCCTCCTGGTGGTTCCCCGCTTCGCCACGATCTCGGACTTCTGGAAGCTGGCACTGCCCATCGTCATGTGCACCTCGGCGACGACGGCGGAGGTCTTCCGCTCCGGTGTCCGGGCGCTGGACCGCGGCCAGACGGAGGCCGCTTGGGCACTGGGGATGAGTCCATCGCTCACCATGCGCCTCATCCTGGCGCCGCAGGCCCTGCGCCTCATGCTCCCAACCCTGATCACGCAGATGGTGACCATCATCAAGGGGACGACGCTGGCGTACGTGCTCGCCTACCCCGAGCTCATGTATCGCGGCTCCACCATGATCGGCCAGGCCAAGATCGATGCCCATTTGTCGGTCTTCTTCCAGACCTACGTCATCATCGCCGTGCTCTACATCATCGTGAACTGGTCCCTGGGGGCACTGGCCCGCTACATCGAGTCGCGTACCCGATGA","MSSDIMPMTEPRPRRQRSQDSGATDAALLFDEPGPRGRILIAIGSVVAVIGIAGLAAAVLYRLDLAGQLDYPKWRYFLGQSVVSQLLEAAGTTLTLGGVAAVLTFPLGIALGWLRLLDNRPIKWLVGLWVDAMRAVPMLLLVYFFLLVVPRFATISDFWKLALPIVMCTSATTAEVFRSGVRALDRGQTEAAWALGMSPSLTMRLILAPQALRLMLPTLITQMVTIIKGTTLAYVLAYPELMYRGSTMIGQAKIDAHLSVFFQTYVIIAVLYIIVNWSLGALARYIESRTR$","ABC-type glutamate transporter, permease component","Membrane, Cytoplasm","Glutamate/glutamine/aspartate/asparaginetransport system permeaseprotein bztB","glutamate transporter permease protein GluD","polar amino acid ABC transporter, inner membrane subunit","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[86-288]T$	BPD_transp_1
PS50928	$\"[90-283]T$	ABC_TM1

InterPro
IPR010065
Domain

Amino acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine
TIGR01726	$\"[82-179]T$	HEQRo_perm_3TM: amino acid ABC transporter,

noIPR
unintegrated

unintegrated
tmhmm	$\"[39-61]?$ $\"[94-114]?$ $\"[135-155]?$ $\"[218-238]?$ $\"[259-279]?$	transmembrane_regions

","BeTs to 15 clades of COG0765COG name: ABC-type amino acid transport system, permease componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0765 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 152-211 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in BZTB_RHOCA.","","-62% similar to PDB:1JRH COMPLEX (ANTIBODY/ANTIGEN) (E_value = );","Residues 86 to 288 (E_value = 1.1e-14) place ANA_1038 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transport system permeaseprotein bztB","","1","","","","","","","","","","","Tue Aug 14 11:44:19 2007","","Tue Aug 14 11:44:19 2007","","","Tue Aug 14 11:44:19 2007","","Tue Aug 14 11:44:19 2007","","Tue Aug 14 11:44:19 2007","Tue Aug 14 11:44:19 2007","","","","","yes","","" "ANA_1040","1118944","1118288","657","10.01","7.04","22710","GTGAGTGCCATTACCGACAATCTCCCCGCTATCGGTTGGGGGCTGCTGGTCACGCTGGTGATCTCCGTCCTGTCCTACCTGGGTGGGCTGCTCCTGGGGTCGCTCATGGCCATCTTCCGGGTCGGTCCCATCCCTCCGCTGCGTGCGCTGGGTGCGGCGTGGGTGACAGTGGCCTGCAATATCCCCAATCTGTGCCTCATGGTGCTTGTCGGGCTGGCGCTACCTCATGTCGGTATCACCATCCCGCTGTTCTGGTCGGTGATCGTGGCGCTGGTCTTCTCCTCATCGGGATTCGTGTGTGAGACGGTCCGCAGCGGGATCAACTCGGTGCCCAAGGGGCAGATCGAGGCCGCCCGTGCGCTGGGCATGCCCTTCGGGCTCATCATTCGCGGCATCGTTCTGCCTCAGGCGCTGGCCCGCACGATCCAGCCACTGGTCAACATCTTCATCGCCTGCCTTATCGGCTCCTCGCTCGCCGCGGCGATCGGTGTCGTCGAGCTGACGGCCGTGACGCAGAGAATCAACCAGGAACGAGCCGCGGGAGTCATCACCTTCCTCACCTCCGGCCTTACCTACCTGGCCATCGCCTTCGCCGCCACGAAGGTCGGCGGGCTCCTTGAGAGGCGCCTCGAGTTCATGGGGAGGGGGCGAGCATGA","VSAITDNLPAIGWGLLVTLVISVLSYLGGLLLGSLMAIFRVGPIPPLRALGAAWVTVACNIPNLCLMVLVGLALPHVGITIPLFWSVIVALVFSSSGFVCETVRSGINSVPKGQIEAARALGMPFGLIIRGIVLPQALARTIQPLVNIFIACLIGSSLAAAIGVVELTAVTQRINQERAAGVITFLTSGLTYLAIAFAATKVGGLLERRLEFMGRGRA$","ABC-type glutamate transporter, permease component","Membrane, Cytoplasm","glutamate transport protein gluC","K02029 polar amino acid transport system permease protein","polar amino acid ABC transporter, inner membrane subunit","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[11-212]T$	BPD_transp_1
PS50928	$\"[15-203]T$	ABC_TM1

InterPro
IPR010065
Domain

Amino acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine
TIGR01726	$\"[7-105]T$	HEQRo_perm_3TM: amino acid ABC transporter,

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[53-75]?$ $\"[81-99]?$ $\"[145-165]?$ $\"[179-199]?$	transmembrane_regions

","BeTs to 15 clades of COG0765COG name: ABC-type amino acid transport system, permease componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0765 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 53-137 are similar to a (TRANSMEMBRANE PERMEASE ABC TRANSPORTER TRANSPORTER SYSTEM MEMBRANE SUGAR COMPONENT AMINO) protein domain (PD015756) which is seen in Q82LP9_STRAW.Residues 88-216 are 50% similar to a (MEMBRANE SUPERFAMILY ABC GLUTAMATE/ASPARTATE TRANSMEMBRANE) protein domain (PDA10263) which is seen in Q6FAP0_ACIAD.","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 212 (E_value = 2.5e-22) place ANA_1040 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transport protein gluC (permease)","","1","","","","","","","","","","","Tue Aug 14 11:44:55 2007","","Tue Aug 14 11:44:55 2007","","","Tue Aug 14 11:44:55 2007","","Tue Aug 14 11:44:55 2007","","Tue Aug 14 11:44:55 2007","Tue Aug 14 11:44:55 2007","","","","","yes","","" "ANA_1041","1120050","1119070","981","5.92","-1.10","33410","ATGACCACCCTCTCCCGCCGCGGACTCCTGGCCACGACCGGCGCCCTCTCCCTGGCAGGCGTCCTGGCCGCCTGCGCTGACACGGGCGCCGATGGCAAGGCCGTCGCCTCGTCGTCGGCCTCCGACGCCGACTACGACAAGGCCATCAACTCCGGTCCGGTGGCCGCCGCCGACGTCGTGGCCGCCTCCCCCTGGGCCGCCTCCGTGAAGCAGGCGAAAAAGCTCGTCACCGGCGGGACCAAAACCTCCGAGGTCTTCTCCTGGGAGGACTCCAAGACGAAGAAGATCTCCGGCTTCGATGCGGCCATCGCCCAGGCGCTGGCCCGCTACATCATCGGCGGCGACGACGCCCGCTCCCTCCTCGAGGTCCAGCAGGTCACCTCCGAGACGCGCGAGACCGTCCTGACCAACGGCACGGTCAAGGCCGTCATCGCCACCTACACGATCACCCCGGAGCGGGCCAAGAAGATCGACTTCGCAGGCCCCTACTACGCCTCCAGCCAGGCCATCCTGGTCAAGGCCGATAACAAGGACATCACCGGCGTCGACACCCTCACCGGGGACGTCGCGGTCCAGTCCAACTCCTCGTCTGCCGCCGCCCTGAAGAAGTACGCCCCTAAGGCCACCGCCAAGCCCTTCGACACCCAGGCCAAGTGCGTCGCCGCCGTCGAGAGCGGGCAGGTCAAGGCCTACGTCGTGGACCAGTCCCTGCTCAAGAGCGAGGTTCTGTCCAATGACAAGGTCAAGATCGTCGGTGACACCTTCGCCGAGGACCCCTACGGCATCGGACTTCCCAAGGACTCCGGGGCACAGGCCTTCGTCAACACCTTCCTCAAGACGATCGAGGACGACGGCACCTGGAAGCGGATCTGGGAGGCGACAATCGGCAAGTCCCTCGGCGGCACCGCCCCTCAGCCCCCGGCCATCGGCTCGGTGCCCGGGTCCTCGGCCAGCGGCGACGCGACCGCGCAGAGCTCCTGA","MTTLSRRGLLATTGALSLAGVLAACADTGADGKAVASSSASDADYDKAINSGPVAAADVVAASPWAASVKQAKKLVTGGTKTSEVFSWEDSKTKKISGFDAAIAQALARYIIGGDDARSLLEVQQVTSETRETVLTNGTVKAVIATYTITPERAKKIDFAGPYYASSQAILVKADNKDITGVDTLTGDVAVQSNSSSAAALKKYAPKATAKPFDTQAKCVAAVESGQVKAYVVDQSLLKSEVLSNDKVKIVGDTFAEDPYGIGLPKDSGAQAFVNTFLKTIEDDGTWKRIWEATIGKSLGGTAPQPPAIGSVPGSSASGDATAQSS$","ABC-type glutamate transporter, periplasmic component","Membrane, Periplasm, Extracellular","glutamine ABC transporter, substrate bindingprotein","K02030 polar amino acid transport system substrate-binding protein","extracellular solute-binding protein, family 3","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670","","","

InterPro
IPR001638
Family

Bacterial extracellular solute-binding protein, family 3
PF00497	$\"[86-297]T$	SBP_bac_3
SM00062	$\"[74-298]T$	PBPb

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[4-36]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[70-203]T$	no description
PTHR18966	$\"[220-268]T$	IONOTROPIC GLUTAMATE RECEPTOR-RELATED
PTHR18966:SF10	$\"[220-268]T$	GLUTAMATE RECEPTOR, IONOTROPIC, N-METHYL-D-ASPARTATE 3B (NMDA 3B)
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-23]?$	signal-peptide

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[155-198]T$	Q82KB9_STRAW_Q82KB9;
PF00005	$\"[46-231]T$	ABC_tran
PS50893	$\"[21-255]T$	ABC_TRANSPORTER_2
PS00211	$\"[156-170]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[45-232]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[15-257]T$	no description
PTHR19222	$\"[21-258]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF33	$\"[21-258]T$	GLUTAMATE / GLUTAMINE ABC TRANSPORTER

","BeTs to 15 clades of COG1126COG name: ABC-type polar amino acid transport system, ATPase componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1126 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.2e-54. IPB013563A 35-69 IPB013563B 98-111 IPB013563C 153-180 IPB013563D 207-259***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2e-41. IPB005074C 35-82 IPB005074D 144-187 IPB005074E 207-227***** IPB005116 (TOBE domain) with a combined E-value of 1.8e-27. IPB005116A 53-69 IPB005116B 96-113 IPB005116C 156-169 IPB005116D 176-195 IPB005116E 209-222***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3.8e-19. IPB010509B 46-71 IPB010509D 151-195***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.7e-07. IPB010929K 33-77 IPB010929M 153-199 IPB010929B 92-138***** IPB000764 (Uridine kinase signature) with a combined E-value of 8.5e-07. IPB000764A 46-63 IPB000764F 179-192","Residues 18-117 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD616033) which is seen in Q8PV90_METMA.Residues 19-228 are 51% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 20-119 are 52% similar to a (LIPOPROTEIN ATP-BINDING RELEASING SYSTEM LOLD) protein domain (PDA0I1Q0) which is seen in Q7UH39_RHOBA.Residues 21-213 are 49% similar to a (ATP-BINDING/PERMEASE ABC TOXIN TRANSPORTER ATP-BINDING PLASMID) protein domain (PD416779) which is seen in Q82YJ4_ENTFA.Residues 29-239 are 49% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 30-119 are 50% similar to a (ATP-BINDING TRANSPORTER) protein domain (PDA0J3Q7) which is seen in Q7M9H8_WOLSU.Residues 31-233 are 46% similar to a (ATP-BINDING ABC PRECURSOR TRANSPORTER SIGNAL) protein domain (PDA0X2Z3) which is seen in Q6MM73_BDEBA.Residues 32-122 are 60% similar to a (ABC ATP TRANSPORTER ATP-BINDING BINDING) protein domain (PDA0J3R3) which is seen in Q97VF4_SULSO.Residues 34-234 are 48% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 35-233 are 46% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 36-202 are 50% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 36-84 are 77% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in O50495_STRCO.Residues 37-235 are 48% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 46-215 are 54% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 146-213 are 60% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 146-241 are 59% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 146-225 are 58% similar to a (ATP-BINDING TRANSPORTER ABC OLIGOPEPTIDE) protein domain (PDA189L6) which is seen in Q8TRD5_METAC.Residues 146-230 are 51% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.Residues 146-233 are 56% similar to a (ATP-BINDING COBALT) protein domain (PD638981) which is seen in Q8YQ85_ANASP.Residues 147-245 are 57% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 147-233 are 57% similar to a (COMPONENT ABC ATPASE ATP-BINDING TRANSPORTER) protein domain (PDA0I0K5) which is seen in Q74HP7_LACJO.Residues 147-243 are 54% similar to a (APRD ATP-BINDING) protein domain (PDA0I303) which is seen in Q89EV0_BRAJA.Residues 149-226 are 63% similar to a (ATP-BINDING TRANSPORTER ABC-TYPE ABC) protein domain (PD891090) which is seen in Q73Y59_MYCPA.Residues 149-213 are 72% similar to a (ATP-BINDING ABC TRANSPORTER YDDO TRANSPORTER DIPEPTIDE ATP OLIGOPEPTIDE BINDING) protein domain (PD507594) which is seen in Q8ZBG3_YERPE.Residues 149-241 are 57% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 149-214 are 73% similar to a (ATP-BINDING ABC COMPONENT TRANSPORTER SYSTEM TRANSPORTER A ABC-TYPE ATPASE RESISTANCE) protein domain (PD334824) which is seen in Q87LE8_VIBPA.Residues 150-235 are 68% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 150-234 are 56% similar to a (IRONIII ABC-TYPE SYSTEM ATP ATP-BINDING BINDING) protein domain (PDA106C0) which is seen in Q6M0S1_METMP.Residues 150-259 are 58% similar to a (ATP-BINDING IRONIII ABC TRANSPORTER) protein domain (PDA0K3T3) which is seen in Q8TRE7_METAC.Residues 151-234 are 61% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 151-245 are 57% similar to a (ATP-BINDING CBIO-2 COBALT) protein domain (PD051511) which is seen in O28437_ARCFU.Residues 152-234 are 61% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z9) which is seen in Q8DM53_SYNEL.Residues 152-213 are 67% similar to a (ATP-BINDING TRANSPORTER ABC RESISTANCE TRANSMEMBRANE SIMILAR MULTIGENE POLYMORPHISM FAMILY GLYCOPROTEIN) protein domain (PD250423) which is seen in Y742_STRCO.Residues 152-242 are 57% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 153-225 are 60% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA184H5) which is seen in Q6W139_RHISN.Residues 153-235 are 65% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 153-233 are 60% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PD052393) which is seen in Q55649_SYNY3.Residues 154-233 are 66% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K1H6) which is seen in Q73MA6_TREDE.Residues 155-258 are 54% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD957735) which is seen in Q73JF3_TREDE.Residues 155-239 are 58% similar to a (BLR8070 ATP-BINDING) protein domain (PD727315) which is seen in Q89BS8_BRAJA.Residues 155-243 are 56% similar to a (COMPONENT METHYL M-REDUCTASE COENZYME ATP-BINDING) protein domain (PD462863) which is seen in Q93RF2_TREMD.Residues 155-198 are identical to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q82KB9_STRAW.Residues 155-236 are 58% similar to a (ATP-BINDING TRANSPORTER COBALT ABC PROTEIN) protein domain (PD944400) which is seen in Q72D73_DESVH.Residues 156-241 are 60% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 156-229 are 60% similar to a (ATP-BINDING) protein domain (PD727310) which is seen in Q8FQ82_COREF.Residues 156-247 are 57% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 156-235 are 65% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 156-241 are 62% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J201) which is seen in Q73M59_TREDE.Residues 157-246 are 60% similar to a (SUGAR ABC ATP ATP-BINDING BINDING) protein domain (PDA0I5K8) which is seen in Q982N2_RHILO.Residues 157-228 are 65% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA198U3) which is seen in Q72IT9_THET2.Residues 157-233 are 59% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA106Q1) which is seen in Q73R37_TREDE.Residues 160-244 are 58% similar to a (ATP-BINDING PLASMID) protein domain (PD244274) which is seen in Q9WW89_LACLC.Residues 160-245 are 61% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD476601) which is seen in Q89GD9_BRAJA.Residues 164-213 are 78% similar to a (ATP-BINDING ABC ACID AMINO TRANSPORTER) protein domain (PD767512) which is seen in Q8DHR3_SYNEL.Residues 177-213 are 91% similar to a (PREDICTED ATP-BINDING) protein domain (PDA188F3) which is seen in Q8TSK7_METAC.Residues 201-258 are 58% similar to a (RSC1743) protein domain (PD750155) which is seen in Q8XYL5_RALSO.Residues 214-261 are 75% similar to a (ATP-BINDING AGR_L_671P ABC BINDING/ATPASE NUCLEOTIDE TRANSPORTER) protein domain (PD914511) which is seen in Q8U7B6_AGRT5.","","-61% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 2.7E_50);-51% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 3.3E_32);-51% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 3.3E_32);-51% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 3.3E_32);-51% similar to PDB:2AWN Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg) (E_value = 3.3E_32);","Residues 46 to 231 (E_value = 9.1e-73) place ANA_1042 in the ABC_tran family which is described as ABC transporter.","","uptake system ATP-binding protein","","1","","","","","","","","","","","Tue Aug 14 11:45:59 2007","","Tue Aug 14 11:45:59 2007","","","Tue Aug 14 11:45:59 2007","Tue Aug 14 11:45:59 2007","Tue Aug 14 11:45:59 2007","","Tue Aug 14 11:45:59 2007","Tue Aug 14 11:45:59 2007","","","","","yes","","" "ANA_1043","1121191","1121853","663","5.73","-6.92","24341","ATGAGTCCAGCGAATGCCACCGATCCGCGTCGCCGCCTCCAGCCCGAGCAGCGTCGGGAGGAGCTGGTGAGAGTCGGCGTCGAGCTGTTCGCGGAAGGAACACTGGACCGCACTCACGTCAACGAGATCATCAAGCGGGCCGGCGTCTCACGCACGCTCTTCTATCACTACTTCCCCTCCAAGATCGCTTTCGCCCGAGCCATCGTGGAGCACGAGATCCTTCACCTTCACGGCCTGGTCGAGCAGCAGACGGCACTGACCCTGGAAGGGGCGATCTCCACCTTCGCGGGCTACGTGAAGGCCAGGCCCGACAGCCTTCGAGCGCTTCACACCGGAGGCCTTGACCAGGACCCTGAGATCGCGGCCGCCCTGGCAACCAGCTTCGAGCGTTACGAACGCCTCGTCCTCATGCTCATGGGCATCGCCGAGCCCGACGAGTGCGCCATGTTCGCCGCCGAGGTGTGGATCAGCACGATGATCACCCTGTGCCTGGCCTGGCTGGATCACCCCGAGATCAGTCAGGAGACCATCACGAACATGTCCGCCCAGACGCTGCGGAGCCTGGTGTCTCAGGCTCGACAGGGTGCCGAGCACGCCTCCGAGCCGGCCACGACACCGGCCACGACGCCGGCCACCGCCCACGAGCCGGTGAGCGACCGCTGA","MSPANATDPRRRLQPEQRREELVRVGVELFAEGTLDRTHVNEIIKRAGVSRTLFYHYFPSKIAFARAIVEHEILHLHGLVEQQTALTLEGAISTFAGYVKARPDSLRALHTGGLDQDPEIAAALATSFERYERLVLMLMGIAEPDECAMFAAEVWISTMITLCLAWLDHPEISQETITNMSAQTLRSLVSQARQGAEHASEPATTPATTPATAHEPVSDR$","Transcriptional regulator, TetR family","Cytoplasm","B1308_C2_181","TetR-family transcriptional regulator","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PF00440	$\"[22-68]T$	TetR_N
PS50977	$\"[16-76]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[9-68]T$	no description

","No hits to the COGs database.","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 1.4e-11. IPB001647 22-64","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 22 to 68 (E_value = 2.1e-10) place ANA_1043 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","(ttk) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1045","1122071","1123351","1281","8.24","5.92","46903","ATGCCTCAAGGCACCACTGGTGATGTGGTGGCTGTACGCCGCAGGACATCGCGTGTCCTCTTCGCTCCGGAGACATTCAACTTTGCCGAGGTGACCCGTGCGATCGAGGTGGCTCGCCGGATGCCCTCGCACGTCGAGTGCGTCTTCGCCGGCTTCTCGCCACGCAACACCGAGTACATCAGGGCCGCGGGCTTCGAGTTCCGCCTGCTGACCCCCTACCTCAGTGAGGAGGAGGGACGGCAGGCGCTGGACTTCGACCAGGGTCGCAGCCTGCGTCACCCGTTCACGGAGAAGATGCTCGCGCAGCGGGTGACAAGTGAGCGCGTCCTGCTGCGTTCCTTGCGTCCCGACGCCGTTGTCATCGGAGTAACTCCCAGCCAGTTTATTTCTGCGCGGGCGGAGTGCGTGCCACTAGTTTTCGTACGGCCCTTCGCCTACTCCCTGGCGCACCTGGAGGCGGCGCGCTCCACCGGCGCCACCGGCTTCCTGCCCCGCACCCGCCCGGAGGAGTGCCTGGTCGACAACGTGGCCGCCCACGCGCTCCATGCGCTCGGGACCCGGCTCCCCCTGCCTCGTTCCTTCCATTCTGTGGCCAGGACCAATGGTGTTTCGCTGCCCCAGGGGGTGCTCAACGGACTCACTGCCGACCTCAATCTCATCGCCACTGCCCCGCACCTGCTGCCCGGGTGGCTGAGGATGCCGGAGGGTCACCGGGTGGTGGGGCCGGTCTACGCCCGCCTACCCGGGGAGCTCCCCGAGTTCCTGGCCGAACTGGTCGCCGGACCCCAACCCCTGGTGTACTTCGCCATGGGCTCATCGGGGAACCGTGACCTCGTCCTTCACGTGCTGGCAGGCCTGGGCCGGGCGGACTGCCAAGTGCTGGCTCCGGTGCGTTCCCACCTTCGCCAAGAGGACCTGGAGACTCTTCCACGCAATGTCCACGTCACTGACTGGATCCCGGCCCACCAGCTGGGCGACGCCGTCGACCTGGCCATCACTCACGGCGGAGAGGGAACGGTGCAGACCAGCTGCGTCCAGGGGTGGCCCTTCATCGGGATTCCGTTGCAGTTCGAGCAGCGTTTCAACGTGCAGCGTTGTGTGGCCTTCGGCTCGGCCAGGCTCGTGTCGCAGCGGGAGGCTCGCAGGACCGACTGGGCGGAGCTGGTGCGCCAGGCCCTGGCCGACGAAGGCATGCGTTCGCGCGCCCGGCGGATGGCCAGGCTCATGGAGGGACTCGACGGACCGGGCCGGGCCGCTGAGGCGATCTGCGAGCTGCTGTGA","MPQGTTGDVVAVRRRTSRVLFAPETFNFAEVTRAIEVARRMPSHVECVFAGFSPRNTEYIRAAGFEFRLLTPYLSEEEGRQALDFDQGRSLRHPFTEKMLAQRVTSERVLLRSLRPDAVVIGVTPSQFISARAECVPLVFVRPFAYSLAHLEAARSTGATGFLPRTRPEECLVDNVAAHALHALGTRLPLPRSFHSVARTNGVSLPQGVLNGLTADLNLIATAPHLLPGWLRMPEGHRVVGPVYARLPGELPEFLAELVAGPQPLVYFAMGSSGNRDLVLHVLAGLGRADCQVLAPVRSHLRQEDLETLPRNVHVTDWIPAHQLGDAVDLAITHGGEGTVQTSCVQGWPFIGIPLQFEQRFNVQRCVAFGSARLVSQREARRTDWAELVRQALADEGMRSRARRMARLMEGLDGPGRAAEAICELL$","Glycosyl transferase related to UDP-glucuronosyltransferase","Cytoplasm, Extracellular","probable glycosyl transferase ML0125 , putative","putative glycosyl transferase","Glycosyl transferase related to UDP-glucuronosyltransferase-like","","Burchell B., Nebert D.W., Nelson D.R., Bock K.W., Iyanagi T., Jansen P.L., Lancet D., Mulder G.J., Chowdhury J.R., Siest G. The UDP glucuronosyltransferase gene superfamily: suggested nomenclature based on evolutionary divergence. DNA Cell Biol. 1991. 10(7):487-494. PMID: 1909870","","","

InterPro
IPR002213
Family

UDP-glucuronosyl/UDP-glucosyltransferase
PTHR11926	$\"[264-375]T$	GLUCOSYL/GLUCURONOSYL TRANSFERASES

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2000	$\"[244-409]T$	no description
PTHR11926:SF2	$\"[264-375]T$	GLYCOSYLTRANSFERASE

","BeTs to 6 clades of COG1819COG name: Glycosyl transferases, related to UDP-glucuronosyltransferaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1819 is --m---y--dr-bcefg----j----Number of proteins in this genome belonging to this COG is 2","***** IPB002213 (UDP-glucoronosyl/UDP-glucosyl transferase) with a combined E-value of 1.6e-08. IPB002213 316-359","Residues 96-381 are 40% similar to a (CYLJ) protein domain (PD322553) which is seen in Q8E6C2_STRA3.Residues 308-376 are 59% similar to a (F54C1.1) protein domain (PD083321) which is seen in P91326_CAEEL.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","glycosyl transferase ML0125 , putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1046","1124285","1123353","933","5.63","-7.87","32072","ATGAGCCCTACCGCCTCCGCCGTCCCCGATGAGTTCCTCGACGACTCCGCCGAGCGTCCTCAGATCCGCGGGCCGCGGCGGCGCACCGTCAGTGAGGGGCCGGCCGCCGGCCACGAGGTGCTGAGCAATCCGACCTCGGCCCGTATCTCCCGGGTGGCGGGCCTGTCGCGCCGCAATGCGCGGGCCAAGCACCGTCGCTTCCTCGTCGAAGGCCCCCAGGGCGTGCGCGAGGCCGTCCGGCACGCCCCCGGTCGCGTGCTCGACGTCTACCTCACCGAGGCGGCCCTCGAGCGCCACAGCGAGATCTGGGACGAGGCCGTGGCCGCCGGGCTCTACGTGCACGTCACCACCCAGCAGGTCATGGACGCCATGAGCCCAGATGCCCAGGGCCTCCTCGCCGTCGTGGCCACCGAGGAGGCCACCGGCTCCGAGGCGCTGGCCGCCGCCCTGGAGGGGGCCAGGCTCGTCGCCGTCCTCACCCAGGCCCAGGACCCCGGCAACGCCGGCACCATCATCCGGGCCGCCGACGCCGCCGGAGCCGACGCCGTCGTCCTCGTGCGTGGCAGCGTGGACCCCACCGCACCGAAGGTCGTGCGCTCCACCGCCGGAAGCCTCTTCCACCTGCCCGTTGTCACCGGCGTGGCCCTCGACGACGCCGTCACCGCCCTCCACAACGCCGGACTCACCGTCCTGGCCGCCGACGGACGCGGGGACTTCGACCTCTTCGAGGCCGAGTCGCTCCTGGAGGCCCCCAGCGCGTGGCTGCTCGGCAACGAGGCGCACGGACTGCCCTCAGAGGCGCTGAGCCGAGCCGACGCCGTCGTCTCCATCCCCATCTACGGCAAGGCGGAGTCCCTCAACGTCGCCGCCGCCGCGGCCGTCTGTCTCTACGCCAGCGCCCGGGCACAGGCCCAGCACTCTGGCCGCAGCTGA","MSPTASAVPDEFLDDSAERPQIRGPRRRTVSEGPAAGHEVLSNPTSARISRVAGLSRRNARAKHRRFLVEGPQGVREAVRHAPGRVLDVYLTEAALERHSEIWDEAVAAGLYVHVTTQQVMDAMSPDAQGLLAVVATEEATGSEALAAALEGARLVAVLTQAQDPGNAGTIIRAADAAGADAVVLVRGSVDPTAPKVVRSTAGSLFHLPVVTGVALDDAVTALHNAGLTVLAADGRGDFDLFEAESLLEAPSAWLLGNEAHGLPSEALSRADAVVSIPIYGKAESLNVAAAAAVCLYASARAQAQHSGRS$","tRNA/rRNA methyltransferase, SpoU","Cytoplasm","possible rRNA methylase","K03437 RNA methyltransferase; TrmH family","tRNA/rRNA methyltransferase (SpoU)","","Sirum-Connolly K., Mason T.L. Functional requirement of a site-specific ribose methylation in ribosomal RNA. Science 1993. 262(5141):1886-1889. PMID: 8266080Yu L., Petros A.M., Schnuchel A., Zhong P., Severin J.M., Walter K., Holzman T.F., Fesik S.W. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nat. Struct. Biol. 1997. 4(6):483-489. PMID: 9187657","","","

InterPro
IPR001537
Domain

tRNA/rRNA methyltransferase, SpoU
PD001243	$\"[163-282]T$	Q828C9_STRAW_Q828C9;
PF00588	$\"[154-297]T$	SpoU_methylase

InterPro
IPR013123
Domain

RNA 2-O ribose methyltransferase, substrate binding
PF08032	$\"[68-141]T$	SpoU_sub_bind

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.30	$\"[39-139]T$	no description
G3DSA:3.40.1280.10	$\"[149-303]T$	no description
PTHR12029	$\"[113-303]T$	RNA METHYLTRANSFERASE
PTHR12029:SF12	$\"[113-303]T$	RNA METHYLTRANSFERASE-RELATED

","No hits to the COGs database.","***** IPB001537 (tRNA/rRNA methyltransferase (SpoU)) with a combined E-value of 1.4e-28. IPB001537A 157-181 IPB001537B 254-294","Residues 39-99 are 60% similar to a (METHYLTRANSFERASE RRNA TRANSFERASE POSSIBLE 23S TSNR METHYLASE 2.1.1.- TRNA/RRNA RNA) protein domain (PD599489) which is seen in Q8G5E6_BIFLO.Residues 163-282 are 72% similar to a (METHYLTRANSFERASE TRANSFERASE RRNA METHYLASE TRNA/RRNA 2.1.1.- RNA FAMILY SPOU METHYLTRANSFERASE) protein domain (PD001243) which is seen in Q828C9_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 68 to 141 (E_value = 1.9e-06) place ANA_1046 in the SpoU_sub_bind family which is described as RNA 2'-O ribose methyltransferase substrate binding.Residues 154 to 297 (E_value = 2.6e-50) place ANA_1046 in the SpoU_methylase family which is described as SpoU rRNA Methylase family.","","rRNA methylase (AP001517)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1047","1124789","1124409","381","11.34","18.17","14291","ATGGCACGTGTGAAGCGGGCTGTTAACGCCCAGAAGAAGCGTCGTTCCGTTCTCGAGAAGGCCTCGGGCTACCGCGGCCAGCGCTCGCGCCTCTACCGCAAGGCCAAGGAGCAGGTCACCCACTCCGGCGTCTACGCGTTCCGCGACCGTCGCGCCCGCAAGGGCGACTTCCGTCGCCTGTGGATCCAGCGCATCAACGCTGCCGCCCGCGCCGAGGGCCTGACCTACAACCGCTTCATCCAGGGGCTTGGCCTGGCCGGCGTGGAGATCGACCGCCGTATGCTCGCCGAGCTGGCCGTCAACGAGCCCGCGGGCTTCAAGGCCCTCGTTGAGGTGGCCCGCAAGGCCCTCCCCGAGGACGTCAACGCCCCCAAGGCCTGA","MARVKRAVNAQKKRRSVLEKASGYRGQRSRLYRKAKEQVTHSGVYAFRDRRARKGDFRRLWIQRINAAARAEGLTYNRFIQGLGLAGVEIDRRMLAELAVNEPAGFKALVEVARKALPEDVNAPKA$","Ribosomal protein L20","Cytoplasm","ribosomal protein L20","ribosomal protein L20","ribosomal protein L20","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR005812
Family

Ribosomal protein L20, bacterial and organelle form
PR00062	$\"[12-41]T$ $\"[42-71]T$ $\"[75-101]T$	RIBOSOMALL20
TIGR01032	$\"[1-114]T$	rplT_bact: ribosomal protein L20
PS00937	$\"[54-70]T$	RIBOSOMAL_L20

InterPro
IPR005813
Family

Ribosomal protein L20
PD002389	$\"[3-69]T$	RL20_STRCO_O88058;
PTHR10986	$\"[1-119]T$	50S RIBOSOMAL PROTEIN L20
PF00453	$\"[2-109]T$	Ribosomal_L20

","BeTs to 18 clades of COG0292COG name: Ribosomal protein L20Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0292 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005812 (Ribosomal protein L20, bacterial and organelle form) with a combined E-value of 3.6e-38. IPB005812A 3-32 IPB005812B 45-77","Residues 3-69 are similar to a (RIBOSOMAL RRNA-BINDING L20 50S CHLOROPLAST RNA-BINDING RIBONUCLEOPROTEIN L20 3D-STRUCTURE SEQUENCING) protein domain (PD002389) which is seen in RL20_STRCO.Residues 70-100 are similar to a (RIBOSOMAL L20 RRNA-BINDING 50S CHLOROPLAST RNA-BINDING RIBONUCLEOPROTEIN 3D-STRUCTURE SEQUENCING DIRECT) protein domain (PD708599) which is seen in Q6ADC9_BBBBB.","","-64% similar to PDB:1VS6 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 50s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.2E_23);-64% similar to PDB:1VS8 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.2E_23);-64% similar to PDB:1P85 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 4.7E_23);-64% similar to PDB:1P86 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 4.7E_23);-64% similar to PDB:2AW4 Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 50S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 4.7E_23);","Residues 2 to 109 (E_value = 8.3e-45) place ANA_1047 in the Ribosomal_L20 family which is described as Ribosomal protein L20.","","protein L20 (rplT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1049","1125011","1124817","195","11.93","16.39","7345","ATGCCGAAGAACAAGACGCACTCCGGTGCCAAGAAGCGCTTCCGGGTCACCGGCAGCGGCAAGCTCATGCGCGAGCAGGCCAACAAGCGCCACCTGCTGGAGGTCAAGTCCTCCCGCCGCAAGCGCAAGCTGTCCCAGGACCAGCCGGTCGCCCCGGCCGACGTCCGCCAGGTCAAGAAGCTGCTCGGTCGCTGA","MPKNKTHSGAKKRFRVTGSGKLMREQANKRHLLEVKSSRRKRKLSQDQPVAPADVRQVKKLLGR$","Ribosomal protein L35","Periplasm, Extracellular","ribosomal protein L35","ribosomal protein L35","ribosomal protein L35","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Kashiwagi K., Igarashi K. Nonspecific inhibition of Escherichia coli ornithine decarboxylase by various ribosomal proteins: detection of a new ribosomal protein possessing strong antizyme activity. Biochim. Biophys. Acta 1987. 911(2):180-190. PMID: 3542048Smooker P.M., Choli T., Subramanian A.R. Ribosomal protein L35: identification in spinach chloroplasts and isolation of a cDNA clone encoding its cytoplasmic precursor. Biochemistry 1990. 29(41):9733-9736. PMID: 2271612","","","

InterPro
IPR001706
Family

Ribosomal protein L35
PD003417	$\"[5-62]T$	Q828D1_STRAW_Q828D1;
PR00064	$\"[3-20]T$ $\"[21-35]T$ $\"[36-54]T$	RIBOSOMALL35
PF01632	$\"[5-62]T$	Ribosomal_L35p
TIGR00001	$\"[2-64]T$	rpmI_bact: ribosomal protein L35
PS00936	$\"[5-31]T$	RIBOSOMAL_L35

","BeTs to 19 clades of COG0291COG name: Ribosomal protein L35Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0291 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 5-62 are similar to a (RIBOSOMAL L35 50S RIBONUCLEOPROTEIN CHLOROPLAST YNL122C SEQUENCING DIRECT CEREVISIAE P53921) protein domain (PD003417) which is seen in Q828D1_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 62 (E_value = 7.6e-24) place ANA_1049 in the Ribosomal_L35p family which is described as Ribosomal protein L35.","","protein L35 (rpmI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1050","1125734","1125135","600","9.76","10.87","22245","GTGCGTCTCGTCGGCCCCAGCGGCGAGCAGGTCGGCGTTGTCCGCGTGGAGGACGCCCTGCGTCTGGCTGAGGAGGCCGATCTCGACCTGGTCGAGGTGGCACCCGACGCCCGCCCCCCGGTGTGCAAGCTCATGGACTACGGCAAGTTCAAGTACGAGTCGGCCATGAAGGCGCGCGACGCGCGACGCAACCAGGCAAACACCCAGCTCAAGGAAATCCAGTTCCGCCCCAAGATCGATGAGCACGACTACGCCACCAAGCGCGGCCACGTCGAGCGATTCCTCAAAGGCGGGGACAAGGTCAAGTGCATCGTCCGCTTCCGCGGCCGCGAGCAGTCCCGGCCCGAGCTCGGGATCAGGCTCCTGCAGGGCCTGGCCGAGGAGATGGCCGAGCTGGGCACCATCGAGTCCCACCCCCGTCAGGACGGCCGCAACATGGTCATGGTCCTGGCCCCGGTCCGCAAGAAGGCCGAGGTCAAGTCCGACCAGCGCCGCCGCCGCGAGGAGGCCCGCGCCGCCCGCCGCGCCGAGAAGCACGCGGGCCGGGCACCCAAGGGCGCCAAGGCCTCGGACGGGGCAGCTGCCGGCGAGAACGCCTGA","VRLVGPSGEQVGVVRVEDALRLAEEADLDLVEVAPDARPPVCKLMDYGKFKYESAMKARDARRNQANTQLKEIQFRPKIDEHDYATKRGHVERFLKGGDKVKCIVRFRGREQSRPELGIRLLQGLAEEMAELGTIESHPRQDGRNMVMVLAPVRKKAEVKSDQRRRREEARAARRAEKHAGRAPKGAKASDGAAAGENA$","Translation initiation factor IF-3","Cytoplasm","Translation initiation factor IF-3","translation initiation factor IF-3","translation initiation factor IF-3","","Liveris D., Schwartz J.J., Geertman R., Schwartz I. Molecular cloning and sequencing of infC, the gene encoding translation initiation factor IF3, from four enterobacterial species. FEMS Microbiol. Lett. 1993. 112(2):211-216. PMID: 8405963Lin Q., Ma L., Burkhart W., Spremulli L.L. Isolation and characterization of cDNA clones for chloroplast translational initiation factor-3 from Euglena gracilis. J. Biol. Chem. 1994. 269(13):9436-9444. PMID: 8144528","","","

InterPro
IPR001288
Family

Initiation factor 3
PD002880	$\"[76-156]T$	IF3_STRCO_O88060;
G3DSA:3.10.20.80	$\"[1-63]T$	no description
G3DSA:3.30.110.10	$\"[64-157]T$	no description
PTHR10938	$\"[7-152]T$	TRANSLATION INITIATION FACTOR IF-3
PF00707	$\"[67-154]T$	IF3_C
PF05198	$\"[1-62]T$	IF3_N
TIGR00168	$\"[1-155]T$	infC: translation initiation factor IF-3

","BeTs to 18 clades of COG0290COG name: Translation initiation factor IF3Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0290 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001288 (Initiation factor 3) with a combined E-value of 1.8e-76. IPB001288A 8-57 IPB001288B 64-118 IPB001288C 139-153","Residues 76-156 are similar to a (INITIATION FACTOR TRANSLATION IF-3 BIOSYNTHESIS CHLOROPLAST IF-3 SEQUENCING DIRECT 3D-STRUCTURE) protein domain (PD002880) which is seen in IF3_STRCO.","","-71% similar to PDB:1I96 CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS IN COMPLEX WITH THE TRANSLATION INITIATION FACTOR IF3 (C-TERMINAL DOMAIN) (E_value = 2.9E_21);-67% similar to PDB:2IFE TRANSLATION INITIATION FACTOR IF3 FROM ESCHERICHIA COLI RIBOSOME BINDING DOMAIN (RESIDUES 84-180) (E_value = 1.2E_17);-70% similar to PDB:1TIG TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN (E_value = 1.5E_17);","Residues 1 to 62 (E_value = 8.7e-33) place ANA_1050 in the IF3_N family which is described as Translation initiation factor IF-3, N-terminal domain.Residues 67 to 154 (E_value = 1.6e-46) place ANA_1050 in the IF3_C family which is described as Translation initiation factor IF-3, C-terminal domain.","","initiation factor IF-3 (IF3)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1051","1127651","1126098","1554","11.54","22.61","53429","ATGGCCCTTCCCGATGGGGCCGCGTTGCGCACGTGGGTGCGGCGCCGTACTCGGCGGCACCTCCACGGTGTCTGGGCGCTCGTGGGGGACGTCTACTCCGTACTCCTGACACTCATCGTCGTCGTGACGATCCTGGCCCCGTATCTGCGCCGGATGCTCGTGGCTCAGCCTGGCTCAGTCGGGGCCGGTGCGTACGGCGACTTCGCCACGGTGGGCCTCGACCCCGGGTGGGGGTTCCTGGCGCTGATCGTGCTGCTGGCGGCGGTCGGTGTCGGTTCACTCGGCCGGCTCGGCCCGCTCTTCCTGCGCCCCCACGAGGCGGCCTGGTGGCTGCCCATGCCTGGAGACCGGGCCAGTCTCTTGGTGCCGATGGCCCGCGTCGAGTACCTCATCGCGGCCACCGCGGGAGCCGCGGCGGGCGTGCTCCCGGCAGTGGCGGCCGGAGGCGGCTGGATCGCTGCCGCGGCGTGGCCTGCCCTGATGTCGGCCGGGACCTGCCTGGTCCTCACCGAGCTCATCAAGGCCCAGATTCATGACCGTGACGTCGAGCCGCTGCGGCGTCGTCTCATCGTGGCCGGGGTCGCGGCATTCCTGGCCGGTGTGGTGCTTGCCTTCCCGAGCTCCTTGCTCAGCAACACGGCGGTCGCCCTCCTGGCCGGGGCACTGGCCTTCCTGGCCGTGCTGGGATGGCGGCGGGCCAGAGGCAGCCTGGGTAAGGTGCATGATGCTGCGCTCCTGGCCGTCGTCGCTCGGTCCTTCGGCGCGCACGTCTCGCTGCTGTCGTTGGACACCAGGGCCCTGGGGCGGCTGCTTTCCCCGGATCCCAACCGGCCCGCGGATCCTTCGCCGCTGCGGGCGGCGCGGATCGGGAGCCGACTGCCCCGACCCCTGGGGGTGCTGATAGCAGTGGCTCAGGCGGACTGGATCCTGCTGCGTCGCCAGCGCAGGCGCCTGCTTCAGATGGGGGTCGGGCTGGCCATCGCGATGCTGCCGCTGCTGTCCGGGACGGTCGGCGCCCCGCTGCGCGCCGTCGGCTACCTCATCGGAGGCTGGATCGCGACCCTGGCCGTTGCCGAGCCGGCGCGCCAGGCCTGGTTCGACGGCGGTCCTGACGCCTCCTGGCCGGTGGCGCCCTGGGTGGTGCGAGCAGGCCACCTGCTCGTGCCGGCCGTCCTCATGAGCGCCTGGTCCCTGCTGAGCCTAGCCCCGGCCATGGCGGCCCTCGGGGCCGCGGCCGTCTGGAAGGGGCTGGTCATCGTGGTTGCCCTGGCCCTGGTGAGCGGCTGGGCCTGGGCCGGGGTGGCGCTGCGCTCCGGGTACCGGGAGATGCCCGACTTCGCGGCCGGACTCATCGCCTCTCCCATGGGCTCCCTGCCGCCAGGAGTGGTGCAGATGCTGACTCAAGGTCCCGACGCCGTCGTTGTCGGAGCACTGACCACGGCGCTGGTCGCCAGTGGAATCGCGGTGCCGACGACGGCGCTGCTCGGGATCCAGGCCGCCGCCGGCGCCATCGCCGTCGTGTGGGGAGTCCGCACGAACCGCCGGGCCTCTTGA","MALPDGAALRTWVRRRTRRHLHGVWALVGDVYSVLLTLIVVVTILAPYLRRMLVAQPGSVGAGAYGDFATVGLDPGWGFLALIVLLAAVGVGSLGRLGPLFLRPHEAAWWLPMPGDRASLLVPMARVEYLIAATAGAAAGVLPAVAAGGGWIAAAAWPALMSAGTCLVLTELIKAQIHDRDVEPLRRRLIVAGVAAFLAGVVLAFPSSLLSNTAVALLAGALAFLAVLGWRRARGSLGKVHDAALLAVVARSFGAHVSLLSLDTRALGRLLSPDPNRPADPSPLRAARIGSRLPRPLGVLIAVAQADWILLRRQRRRLLQMGVGLAIAMLPLLSGTVGAPLRAVGYLIGGWIATLAVAEPARQAWFDGGPDASWPVAPWVVRAGHLLVPAVLMSAWSLLSLAPAMAALGAAAVWKGLVIVVALALVSGWAWAGVALRSGYREMPDFAAGLIASPMGSLPPGVVQMLTQGPDAVVVGALTTALVASGIAVPTTALLGIQAAAGAIAVVWGVRTNRRAS$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[21-43]?$ $\"[75-95]?$ $\"[129-147]?$ $\"[153-173]?$ $\"[188-206]?$ $\"[212-230]?$ $\"[318-340]?$ $\"[346-366]?$ $\"[387-407]?$ $\"[413-433]?$ $\"[443-463]?$ $\"[473-507]?$	transmembrane_regions

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[26-203]T$	ABC_tran
PS50893	$\"[1-221]T$	ABC_TRANSPORTER_2
PS00211	$\"[130-144]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[25-206]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-204]T$	no description
PTHR19222	$\"[1-201]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 4 clades of COG1136COG name: ABC-type transport systems, involved in lipoprotein release, ATPase componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1136 is aom--z-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 10","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.7e-20. IPB005074C 15-62 IPB005074D 118-161***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 4.8e-14. IPB013563A 15-49 IPB013563C 127-154***** IPB005116 (TOBE domain) with a combined E-value of 1.4e-11. IPB005116A 33-49 IPB005116C 130-143 IPB005116D 150-169 IPB005116E 183-196***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 2.7e-10. IPB010509B 26-51 IPB010509D 125-169","Residues 1-188 are 46% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 5-83 are 56% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 10-119 are 50% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA188U2) which is seen in Q9RXA9_DEIRA.Residues 16-115 are 50% similar to a (ATP-BINDING NATA ABC TRANSPORTER) protein domain (PD742287) which is seen in O83851_TREPA.Residues 20-60 are 78% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q88TH7_LACPL.","","-44% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 5.1E_12);-44% similar to PDB:1G29 MALK (E_value = 2.2E_10);-44% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 2.8E_10);","Residues 26 to 203 (E_value = 1.4e-35) place ANA_1053 in the ABC_tran family which is described as ABC transporter.","","transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1054","1128483","1128875","393","5.00","-5.59","14159","GTGCTCATCGGAACTATTCCAACACACGTTTTTTTCGGTGGCCTGGTTGAATCGGATGCCTTACGCTCCGCAGTCATGGATTGGAACAGCGTGAGGACCCCGGACCCTAATGGCGCGTCCGACGACGATTCCGCCCTCTCTCGTGAGGCAGGAACCGACTGGAGCACCACGAGGGACCCGGGTCCCGGCCGGGTGACGGTATCGACCCGAGACCTCACCCAGATCCGAACGATCGCTGAGGCCTGTGCCCGGATCGCCCAGAGATCCGACCGCCCCCAGGACGGCCAGGCTCTGCGCGATGTCGTTGCCCGCTTCGACCAGGTGGCTGGGCCGCTGGAGGACCACTACGGACAGGTCGAGCAGTGGGAGGCCCGTATCCTGGGGCGCTCCTGA","VLIGTIPTHVFFGGLVESDALRSAVMDWNSVRTPDPNGASDDDSALSREAGTDWSTTRDPGPGRVTVSTRDLTQIRTIAEACARIAQRSDRPQDGQALRDVVARFDQVAGPLEDHYGQVEQWEARILGRS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1055","1129755","1128898","858","4.83","-14.68","29989","ATGAGCACGTCTTCGGATCAACCGCTGCCGACTGCGCGGCCTGAGGCGGCACCCCAGGTGGCTGCCGCCATAGCCGCACGGGCCAAGCTGGAGCGTCTTCTGGCTGCGCCTGCCCCCTTCGCCGACGACGACGGCTCGATCAGTCCAGAGGTGCGCCAGGCGCTGGAGGCTGTGGACCTGCCGCGTCATCAGTACCTCGATGAGCTGTGGGCGGCCCTCGTCGCTGGCCGGCTGATCGTTCCCGTGGCCGCTCACGCCCTTCCCGGACGCCTGGAGGGGAATCTGACGCAGTCCGCGGGCCTGCCGCATGGCCCGTCGGGCGACGGCGCACCGCAGGTCCCGGCTCATGAGGTGCACACCGCCGACGCCTGCCAGGACGCGGCGACCCTGGCGGTGAGCCTGCCTGACGGGCACGTCGCCCTACCGGTGTTCACCAGCGCTGAGGCCATGAGCCGCTGGCGCAGCGACGTGCGTCCCGTGCCCGTCTCGCCCCAGCGAGCGGCCCAGGTCGCCTGCCTGTCCACCGACCAGCTGTGGGTGCTCGACCCCGGTAGCCGGGACCTGCGACTGCCGCGTCCCGCCGTCGTGGCCCTGGCCGGGGGAGAGGAGTGGGTGCCCTCATGGCGCAACGAGCCGGTTCAGGCCGAGGTACGCGCCCAGCTCCAGGAGATCGACGGCGTCACCGGCGTGGCCTTTGGACCCGGCGAGGACGCCGAGCTGCGGGTGTTCATCCGCATTGACGCCGCAGACGGTCGCGCCGGTGTGGCCCGCAGCCTGGAGGGCTGTCAGTACGTCATGATCAACCCGGCCTGGGGCGACCTCATCGACACCGTGGAGCTGTGCCCGCTTCCCGCCTGA","MSTSSDQPLPTARPEAAPQVAAAIAARAKLERLLAAPAPFADDDGSISPEVRQALEAVDLPRHQYLDELWAALVAGRLIVPVAAHALPGRLEGNLTQSAGLPHGPSGDGAPQVPAHEVHTADACQDAATLAVSLPDGHVALPVFTSAEAMSRWRSDVRPVPVSPQRAAQVACLSTDQLWVLDPGSRDLRLPRPAVVALAGGEEWVPSWRNEPVQAEVRAQLQEIDGVTGVAFGPGEDAELRVFIRIDAADGRAGVARSLEGCQYVMINPAWGDLIDTVELCPLPA$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 122-251 are 51% similar to a () protein domain (PDA176Z9) which is seen in Q6AE16_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1056","1129920","1130552","633","9.27","3.84","21076","GTGCGCCGCGGCATCTCCCCTGACGTGTGGACTGCCGTCGGCGTCATCGCTGCCGCGCTGGGCTGCGGGGCACTGGTCATGGGCTGGTGGATTCTGGCATTCATCCTGCTGGCCGCCCGGCTCGGGGGCGCGAATCTCGACGGCGCCGTGGCTCGGGCCCGTGGAGTATCGAGACCCTTCGGCTTCGTCCTCAACGAGATCGGGGACCGGCTCTCCGACCTGTTCATCATGGCCGGTCTCGTGGGCCTCGCCCTGCGCACCGGTTCATCGACCACCACGGTCTACCTGACCCTCATCGCTCTAGCGACGGCAACACTACCGACCTTCATCTCCCTGGCCGCCGCAGGCGCTGGCGCCGCCAGGCTCAACGGCGGCCCGTTCGGCAAGACCGAGCGGTGCCTGGCCGCGGTCGTAGGGGCCGCCCTCCCCCAGTATTTGTCGATCATCGCCTGGGTCATCATCGTGGGCTCGGCGGCGACGGCCTGCGTACGGCTGGCGCGAACCGCCGCCGCGCTCGCAGGACGCACCGGCCCGGCCATGGCCGACACCATGGCCCCACCGCCGCCGCAGGACATCAGCCTCATCGGCCGCAGTGCCCCTGAGGACGAGGCCGCCCCGGGAGCCCAGTCGTGA","VRRGISPDVWTAVGVIAAALGCGALVMGWWILAFILLAARLGGANLDGAVARARGVSRPFGFVLNEIGDRLSDLFIMAGLVGLALRTGSSTTTVYLTLIALATATLPTFISLAAAGAGAARLNGGPFGKTERCLAAVVGAALPQYLSIIAWVIIVGSAATACVRLARTAAALAGRTGPAMADTMAPPPPQDISLIGRSAPEDEAAPGAQS$","CDP-alcohol phosphatidyltransferase","Membrane, Cytoplasm","phosphatidylinositol synthase","hypothetical protein predicted by Glimmer/Critica","CDP-alcohol phosphatidyltransferase","","Nikawa J., Kodaki T., Yamashita S. Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae. J. Biol. Chem. 1987. 262(10):4876-4881. PMID: 3031032Hjelmstad R.H., Bell R.M. sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products. J. Biol. Chem. 1991. 266(8):5094-5134. PMID: 1848238","","","

InterPro
IPR000462
Family

CDP-alcohol phosphatidyltransferase
PF01066	$\"[32-171]T$	CDP-OH_P_transf

noIPR
unintegrated

unintegrated
signalp	$\"[1-46]?$	signal-peptide
tmhmm	$\"[9-27]?$ $\"[33-53]?$ $\"[74-92]?$ $\"[98-118]?$ $\"[133-155]?$	transmembrane_regions

","BeTs to 10 clades of COG0558COG name: Phosphatidylglycerophosphate synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0558 is aompkzyqv-rlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 4","***** IPB000462 (CDP-alcohol phosphatidyltransferase) with a combined E-value of 1e-09. IPB000462 33-80","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 32 to 171 (E_value = 0.00058) place ANA_1056 in the CDP-OH_P_transf family which is described as CDP-alcohol phosphatidyltransferase.","","synthase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1057","1130549","1131484","936","10.48","7.87","32262","GTGAACACCGCGATCAGCTCCTGGGAGGGGCATGAGGCAGACGGCGGAGTGATCGACTGGATCGTGGGCGGCAACCGCTCGTGGACCGTAACCGTTCCCGGGCCGGGGTGGGTCCTCACGGGCCGAGCGGTGTTCCTTGCGGCCACGGCCGTGGCGATCCTGCTCCTGGCCGGCATCGGCGTGGCCCTGTCCCGTAAGGCGGAGCTGCGCCGCCGCTGGACGACGTGGGCCATCATTGTCCCGGCGGTCGGCATTCCTATCTGGGTCGGACGGGGGACGACGGCGCTGCTTGCCACCGCCCTCGGGTTGCAGTCGGTTCGTGAGCTCTCCCGACTCACTCGGCTGCCCAAAGCGGAGACCCTGATGCTGGCGTCACTGGCGGTGATCTATCCGCTAGCCGCCTGGTTGCGCCCGGGACTCATGGCGCTGGCTCCGCTCACGGTACTCGTGTGCGCCGTGCCCGCCATCCTGTCCGGCGACGTCGAGCATGGTCTGAGGAGGGCGACGATCGCCGGTTTCGCCTCGATCTGGATTCCCTGGTCCCTGGCGCACCTCGTGGTGCTGTGGCACGACGCGTTCCTCATCGCCTTCGCGGCTGCGGCCGCCGATGTGGCCGCGTGGGCCGGCGGGACCTTCCTGCGCCCCATGGCCTGGGCACGACGACCGCTGTCCCCCTTGTCCCCGAACAAGACGCTCGGCGGACTGGCGGGGGCCGTCATCGGGGCCACCCTCATTCTCACCCTGCTGGGCCAGATCACGCCCGGCCTGGTGATCGCCGTCGGTCTGGGCGGAGTCCTGGGGGACCTGCTGGAGTCTCTCGTCAAACGCACAGCCGGAGTCAAGGACGCCGGTGCCTGGCTGCCCGGGTTCGGCGGTCTGCTGGACCGCGTCGACTCCCTGCTCCTGGTCCTGCCCCTGGCCGCCGTCATGGGGTGA","VNTAISSWEGHEADGGVIDWIVGGNRSWTVTVPGPGWVLTGRAVFLAATAVAILLLAGIGVALSRKAELRRRWTTWAIIVPAVGIPIWVGRGTTALLATALGLQSVRELSRLTRLPKAETLMLASLAVIYPLAAWLRPGLMALAPLTVLVCAVPAILSGDVEHGLRRATIAGFASIWIPWSLAHLVVLWHDAFLIAFAAAAADVAAWAGGTFLRPMAWARRPLSPLSPNKTLGGLAGAVIGATLILTLLGQITPGLVIAVGLGGVLGDLLESLVKRTAGVKDAGAWLPGFGGLLDRVDSLLLVLPLAAVMG$","Phosphatidate cytidylyltransferase","Membrane, Cytoplasm","phosphatidate cytidylyltransferase, putative","hypothetical protein predicted by Glimmer/Critica","phosphatidate cytidylyltransferase","","Sparrow C.P., Raetz C.R. Purification and properties of the membrane-bound CDP-diglyceride synthetase from Escherichia coli. J. Biol. Chem. 1985. 260(22):12084-12091. PMID: 2995359Shen H., Heacock P.N., Clancey C.J., Dowhan W. The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth. J. Biol. Chem. 1996. 271(2):789-795. PMID: 8557688Saito S., Goto K., Tonosaki A., Kondo H. Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain. J. Biol. Chem. 1997. 272(14):9503-9509. PMID: 9083091","","","

InterPro
IPR000374
Family

Phosphatidate cytidylyltransferase
PF01148	$\"[70-309]T$	CTP_transf_1

noIPR
unintegrated

unintegrated
tmhmm	$\"[43-63]?$ $\"[78-98]?$ $\"[139-159]?$ $\"[169-187]?$ $\"[193-211]?$ $\"[226-246]?$ $\"[252-270]?$	transmembrane_regions

","BeTs to 9 clades of COG0575COG name: CDP-diglyceride synthetaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0575 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB000374 (Phosphatidate cytidylyltransferase) with a combined E-value of 6e-15. IPB000374B 225-238 IPB000374C 267-298","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 70 to 309 (E_value = 4.7e-25) place ANA_1057 in the CTP_transf_1 family which is described as Cytidylyltransferase family.","","cytidylyltransferase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1058","1131481","1132872","1392","11.30","30.83","50640","GTGAGTGGGACGGTTCGCAGCCGTCCGCCCCAGCCCTGCCCCTCTCGACTCCGAGCCGTCTCCTTCAATCGCCAGCACCACCCACGGAAAGGTAGCCCGATGCCCCTTCAGATTCCCTCGGTTCCAGGTTCGGCCGAGATCGCCTCAGCCGGACGCCGCCTGCAATCGATCGTGCGAACACCCCAGAAGGTCACCTGGCGCGCGGTACTGCGGCAGCGTTTCTGGTCCGCCGTCATCGCTCCGTTCGGGGGCGTGCGGGTCGAGGGCGAGTTCGAGACCGACGGCCCCTACGTCGTCGTTGCCAACCACGGCTCCCATGCGGACACGATCGCAATGATGAGTGCCTCCCCCACCCTCATGAGGGTGGTCACCGTCGCTGCCCAGGACTACTGGTTCACCCGTCGCTCGCGTCGCCTCGTGGCCAGGGGGCTGCTGGGCGCCTATCCGGTACGGCGCGACGGCGAGGGCGCCTACGAGGAGCTGCGGGGAACACTGGCCAATCGGGTGGCCGAGTCGATGAGTATTCTCATCTTCCCCGAGGGCACCCGCTCCACGGACGGCCACATGAGCCGCTTTCACTCCGGGGCCGCCCGGCTCGCACGAGACTTCGGGATCCCGGTGCTGCCGGTCGCGCTGGTGGGGACGCGAGAGATGATGCCGAAGAAGGGCGGCCTGCCCCGTTACTCCCCCGTCGAGGTCCGTGTCGGTGAGCCGATCGCCCCCAGTGATGACGTGGAGGGCGTCAGCGACCTGGCGCGCGAGCGGATCGTGGAGATGCTCCAGCGTCCTCGCAGACCCGAGCCGGTCTCAGACGTCTTCACCGTCCTGCACACCGCGATGGAGGGCGGTCGAGGAGACGCCGTGATGTTCGTCTGGGGCATGGCTGAGGCCATCTCCTTCCCGATCATGGCGGAGATGAGCCAGGTCTGGCTGGGGCTGACCCACCCCGAGCGGATGTGGCGGCGGGCAGCGATGGTGGTGGCGGGCTCGGTCACCGGAGTGGCGGTCACGCACCTGCTGACTCGGAGTGGACTCCAGCCTCCCGCGCCGTGGACCGCTCCGGAGATGAGGGCGGCGACATCCCGTTACCTGAGCCGAGGGCCACGCGGGTACTGGAAGCAAGCACTGACCGGGATTCCGGTGAAGCTCTTCGCCGCCGAATCCGGGCGCAGCAACCTGCCTCTGCCCTCTGTCGTCCTTCACGCGGCCGGGGAGCGTGCCGCGCGCATGACGGCCTCCACCGCCATCGTCAAGACACTGGGCAAGCCGCTGGGACCGATCACCCGTCAGCACTACGGCACCTACCTGGCAACCACCGGCGTCGTCTTCGCCACCGCGCTTCGAGGCGTCATCAGGCACTGGCAGCGCCCGAAGCGTCCTGGGCGCCCTTAG","VSGTVRSRPPQPCPSRLRAVSFNRQHHPRKGSPMPLQIPSVPGSAEIASAGRRLQSIVRTPQKVTWRAVLRQRFWSAVIAPFGGVRVEGEFETDGPYVVVANHGSHADTIAMMSASPTLMRVVTVAAQDYWFTRRSRRLVARGLLGAYPVRRDGEGAYEELRGTLANRVAESMSILIFPEGTRSTDGHMSRFHSGAARLARDFGIPVLPVALVGTREMMPKKGGLPRYSPVEVRVGEPIAPSDDVEGVSDLARERIVEMLQRPRRPEPVSDVFTVLHTAMEGGRGDAVMFVWGMAEAISFPIMAEMSQVWLGLTHPERMWRRAAMVVAGSVTGVAVTHLLTRSGLQPPAPWTAPEMRAATSRYLSRGPRGYWKQALTGIPVKLFAAESGRSNLPLPSVVLHAAGERAARMTASTAIVKTLGKPLGPITRQHYGTYLATTGVVFATALRGVIRHWQRPKRPGRP$","Phospholipid/glycerol acyltransferase","Extracellular, Membrane","putative 1-acyl-sn-glycerol-3-phosphateacyltransferase","1-acyl-sn-glycerol-3-phosphate acyltransferase ","phospholipid/glycerol acyltransferase","","","","","

InterPro
IPR002123
Domain

Phospholipid/glycerol acyltransferase
PF01553	$\"[84-213]T$	Acyltransferase
SM00563	$\"[97-215]T$	PlsC

noIPR
unintegrated

unintegrated
PTHR10434	$\"[66-301]T$	1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE
tmhmm	$\"[431-451]?$	transmembrane_regions

","BeTs to 19 clades of COG0204COG name: 1-acyl-sn-glycerol-3-phosphate acyltransferaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0204 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB002123 (Phospholipid/glycerol acyltransferase) with a combined E-value of 8.9e-10. IPB002123A 98-116 IPB002123B 177-190","Residues 177-257 are 61% similar to a (ACYLTRANSFERASE TRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE FAMILY 2-ACYLGLYCEROPHOSPHOETHANOLAMINE ACYLTRANSFERASE PROBABLE PHOSPHOLIPID) protein domain (PD462158) which is seen in O33970_STRCJ.","","No significant hits to the PDB database (E-value < E-10).","Residues 84 to 213 (E_value = 2e-25) place ANA_1058 in the Acyltransferase family which is described as Acyltransferase.","","1-acyl-sn-glycerol-3-phosphate acyltransferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1059","1133686","1132934","753","4.95","-11.11","26249","ATGCTCACTCTACTTCCCGCCGTCGATGTCGCCGATGGCAAGGCCGTTCGCCTCCTTCAGGGAGAGGTCGGCTCAGAGACGGACTACGGCAGTCCCGTCGACGCCGCCCGGGACTGGGTGCGCGCCGGGGCCGAGTGGATCCACCTGGTGGACCTCGACGCCGCTTTCGGGCGCGGCTCCAACCATGAGCTGCTGGCTCGCATCGTCGGCGAGGTCGGCATCAAGGTGGAGCTCTCCGGGGGTATCCGTGATGATGCCTCACTGGCCCGCGCCCTGTCCGCCGGAGCCGCGCGGGTCAACCTGGGGACGGCTGCTCTCGAGGACCCTGAGTGGACTGAACGGGTCATCGCCGAGCACGGGGAGAAGATCGCCGTCGGCCTCGACGTGCGCGGCTCCACCTTGGCGGCCCGCGGCTGGACCAAGGAGGGCGGAGACCTGTGGGAGTCCCTCGAGCGGCTCAACGCCGCAGGGTGCGCGCGCTACGTCGTCACCGACGTGACCCGGGACGGGACGCTGAGCGGCCCCAACACCGCCCTGCTCACCGAGGTCTGCCAGCGCACCGCGGCACCGGTGGTCGCCTCCGGAGGTATCGCCCATCTCGACGACCTGGTCGCGCTGCGCCGTCTGGTGCCGCTGGGACTGGAGGGCGCGATTGTCGGCAAGGCGCTCTACAACGGCAACTTCACCCTTCAGGAGGCGCTGGTCGTGGCCGGTGACGAGGAGAGGCGCGAGCCTTCGCAGGCTCGTTCCTGA","MLTLLPAVDVADGKAVRLLQGEVGSETDYGSPVDAARDWVRAGAEWIHLVDLDAAFGRGSNHELLARIVGEVGIKVELSGGIRDDASLARALSAGAARVNLGTAALEDPEWTERVIAEHGEKIAVGLDVRGSTLAARGWTKEGGDLWESLERLNAAGCARYVVTDVTRDGTLSGPNTALLTEVCQRTAAPVVASGGIAHLDDLVALRRLVPLGLEGAIVGKALYNGNFTLQEALVVAGDEERREPSQARS$","Bifunctional HisA/TrpF protein","Cytoplasm","bifunctional HisA/TrpF protein","bifunctional HisA/TrpF protein ","bifunctional HisA/TrpF protein","","Barona-Gomez F., Hodgson D.A. Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis. EMBO Rep. 2003. 4(3):296-300. PMID: 12634849","","","

InterPro
IPR006062
Domain

Histidine biosynthesis
PF00977	$\"[3-229]T$	His_biosynth

InterPro
IPR010188
Family

Bifunctional HisA/TrpF
TIGR01919	$\"[1-238]T$	hisA-trpF: bifunctional HisA/TrpF protein

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[2-238]T$	no description

noIPR
unintegrated

unintegrated
PTHR21235	$\"[99-247]T$	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H (IGP SYNTHASE SUBUNIT HISF/H)
PTHR21235:SF15	$\"[99-247]T$	1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE

","BeTs to 17 clades of COG0106COG name: Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomeraseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0106 is aom---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB006062 (Histidine biosynthesis protein) with a combined E-value of 3.3e-51. IPB006062A 4-17 IPB006062B 30-55 IPB006062C 74-122 IPB006062D 157-177 IPB006062E 187-203 IPB006062E 72-88","Residues 2-63 are similar to a (ISOMERASE CARBOXAMIDE PHOSPHORIBOSYLFORMIMINO-5-AMINOIMIDAZOLE RIBOTIDE HISTIDINE IMIDAZOLE-4-CARBOXAMIDE BIOSYNTHESIS 1-5-PHOSPHORIBOSYL-5-5-PHOSPHORIBOSYLAMINOMETHYLIDENEAMINO I PHOSPHORIBOSYLAMINOMETHYLIDENEAMINO) protein domain (PD828336) which is seen in HIS4_BIFLO.Residues 121-227 are 52% similar to a (ISOMERASE BIOSYNTHESIS HISTIDINE CARBOXAMIDE PHOSPHORIBOSYLFORMIMINO-5-AMINOIMIDAZOLE RIBOTIDE SIMILAR OXIDATION MJ0703 I) protein domain (PD589932) which is seen in HIS4_PYRAE.Residues 123-179 are similar to a (SUBUNIT SYNTHASE HISF ISOMERASE HISTIDINE IGP BIOSYNTHESIS IMIDAZOLE PHOSPHATE GLYCEROL) protein domain (PD625483) which is seen in Q6AE15_BBBBB.Residues 183-230 are 79% similar to a (ISOMERASE CARBOXAMIDE PHOSPHORIBOSYLFORMIMINO-5-AMINOIMIDAZOLE RIBOTIDE IMIDAZOLE-4-CARBOXAMIDE HISTIDINE 1-5-PHOSPHORIBOSYL-5-5-PHOSPHORIBOSYLAMINOMETHYLIDENEAMINO BIOSYNTHESIS I PHOSPHORIBOSYLAMINOMETHYLIDENEAMINO) protein domain (PD364501) which is seen in Q6A8L1_PROAC.","","-76% similar to PDB:1VZW CRYSTAL STRUCTURE OF THE BIFUNCTIONAL PROTEIN PRIA (E_value = 2.5E_82);-46% similar to PDB:1QO2 CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA) (E_value = 4.1E_16);-45% similar to PDB:2CFF CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE MUTANT D127V (EC 3.1.3.15, HISA) (E_value = 4.5E_15);-43% similar to PDB:1H5Y HISF PROTEIN FROM PYROBACULUM AEROPHILUM (E_value = 1.0E_11);-43% similar to PDB:1KA9 Imidazole Glycerol Phosphate Synthase (E_value = 2.3E_11);","Residues 3 to 229 (E_value = 3.2e-88) place ANA_1059 in the His_biosynth family which is described as Histidine biosynthesis protein.","","HisA-TrpF protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1060","1134365","1133727","639","6.20","-3.42","22657","ATGCAAGCGCCACGCGTCACCGTCCTGTCCTACGGATCCGGCAATGTCCGCTCGGCGGTGCGTGCTCTGGAGCGCGTCGGAGCGCAGGTGACCCTCACCAGCGACCCGCACGAGGTCGCCGAGGCCGACGGACTCGTGGTACCCGGGGTGGGCGCATTCGGCGCGGTCATGGAGCAGCTGCGGGCAGTCGACGCGCCTCGGCTCATCGAGCGGCGCCTGGCCGGCGGCAGGCCGGTCCTGGGAATCTGCGTGGGCATGCAGGTCATGTTCGAGCGCTCCCAGGAGCATGGGACCGCTGAGGATGGGCTGGGACAATGGCCCGGTACCGTGTCCCGCCTGAGAGCCGACGTCGTTCCGCACATGGGATGGAGCCTGGTCCGGCCTCCAGCCGCCTCCGTTCTGTTCGACGGCGTCGCCGAGGAGCGCTTCTACTTCGTCCACTCCTATGCGGCCACCCAGGACCCCGCCGAGCTGCTCGGTCCCGGTCCCACCCGACTGCCTCAGGTCACGTGGGCCACTCACGGCCACGACTTCATCGCCGCCGTGGAGAACGGCTCGCTGTGCGCCACGCAGTTCCACCCTGAGAAGTCCGGTGACGCAGGGGCTCAGCTGCTGCGCAACTGGCTGACGACCCTCTGA","MQAPRVTVLSYGSGNVRSAVRALERVGAQVTLTSDPHEVAEADGLVVPGVGAFGAVMEQLRAVDAPRLIERRLAGGRPVLGICVGMQVMFERSQEHGTAEDGLGQWPGTVSRLRADVVPHMGWSLVRPPAASVLFDGVAEERFYFVHSYAATQDPAELLGPGPTRLPQVTWATHGHDFIAAVENGSLCATQFHPEKSGDAGAQLLRNWLTTL$","Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit","Cytoplasm","imidazole glycerol phosphate synthase, glutamineamidotransferase subunit","amidotransferase ","imidazole glycerol phosphate synthase, glutamine amidotransferase subunit","","Weng M.L., Zalkin H. Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. J. Bacteriol. 1987. 169(7):3023-3028. PMID: 3298209Nyunoya H., Lusty C.J. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. J. Biol. Chem. 1984. 259(15):9790-9798. PMID: 6086650","","","

InterPro
IPR000991
Domain

Glutamine amidotransferase class-I
PF00117	$\"[7-212]T$	GATase

InterPro
IPR010139
Domain

Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit H
TIGR01855	$\"[6-211]T$	IMP_synth_hisH: imidazole glycerol phosphat

InterPro
IPR012998
Active_site

Glutamine amidotransferase, class I, active site
PS00442	$\"[78-89]T$	GATASE_TYPE_I

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[6-209]T$	no description
PTHR21235	$\"[56-212]T$	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H (IGP SYNTHASE SUBUNIT HISF/H)
PTHR21235:SF1	$\"[56-212]T$	IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH (IGP SYNTHASE SUBUNIT HISH)

","BeTs to 18 clades of COG0118COG name: Glutamine amidotransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0118 is aom---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 1.7e-09. IPB000991A 78-95 IPB000991B 186-196***** IPB002161 (SNO glutamine amidotransferase) with a combined E-value of 1.9e-09. IPB002161A 39-55 IPB002161B 80-90 IPB002161E 179-212***** IPB006220 (Anthranilate synthase component II signature) with a combined E-value of 5.1e-07. IPB006220C 78-89 IPB006220F 189-202","Residues 5-69 are 78% similar to a (SUBUNIT SYNTHASE HISH GLUTAMINE IGP AMIDOTRANSFERASE 2.4.2.- PHOSPHATE IMIDAZOLE GLYCEROL) protein domain (PD329941) which is seen in HIS5_CORDI.Residues 25-89 are 66% similar to a (GLUTAMINE SYNTHASE AMIDOTRANSFERASE BIOSYNTHESIS LIGASE GMP SYNTHETASE CTP CHAIN COMPONENT) protein domain (PD000306) which is seen in HIS5_LACLA.Residues 90-209 are 70% similar to a (SUBUNIT SYNTHASE HISH GLUTAMINE IGP AMIDOTRANSFERASE 2.4.2.- PHOSPHATE IMIDAZOLE GLYCEROL) protein domain (PD579466) which is seen in Q6AE14_BBBBB.","","-51% similar to PDB:1KA9 Imidazole Glycerol Phosphate Synthase (E_value = 3.5E_31);-53% similar to PDB:1JVN CRYSTAL STRUCTURE OF IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE: A TUNNEL THROUGH A (BETA/ALPHA)8 BARREL JOINS TWO ACTIVE SITES (E_value = 3.1E_24);-53% similar to PDB:1OX4 TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE (E_value = 3.1E_24);-53% similar to PDB:1OX5 TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE (E_value = 3.1E_24);-53% similar to PDB:1OX6 TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE (E_value = 3.1E_24);","Residues 7 to 212 (E_value = 3.3e-30) place ANA_1060 in the GATase family which is described as Glutamine amidotransferase class-I.Residues 35 to 155 (E_value = 0.00078) place ANA_1060 in the GATase_3 family which is described as CobB/CobQ-like glutamine amidotransferase domain.","","glycerol phosphate synthase, glutamine amidotransferase subunit (hisH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1061","1134620","1136377","1758","6.21","-4.24","59482","ATGCAGTTCCCCTCCGGCCAGGCGTCTGCGCCGCCTTGGCCGGCTTCGCCTCCTCCACCGTCTTCTCAGGCCTCCGCGAGCCACTCCCCCGCAGCGGCGGGGGCAGGTTCGGGCAGTTCCAGCGGGTCGCGCAGTGCTGCGCCGTTCTCCATTCCCGGGGTGCGGATCACCTCGGTGCTGGGGCGTGGCGGCTTCGCCACGGTCTATGCCGGCGTCCAGGACTCCCTGGAGCGCCCGGTCGCCGTCAAGGTGGACTCCCGCCCCTTGGACGATCCCCGCAATGAGCGGCGCTTCATGCGCGAGGTGCAGGCGGCCTCGAGGATCTCGGGGCATCCTCACGTCGTCTCGCTGGTGGATACCGGCAAGCTGCCCGATCTGCGCCCCTACCTCGTCATGGAGCTGTGCGCGGGCGGCAGCCTCTACGACCTCGTCTCGCGTGGCCCGACACCCGCCTCCGACGCCGTGGCCCTGGTGGAGGCCGCTGCCTCGGCCCTGGGAGCTGCCCATGCAGCCGGCGTCACGCACCGGGACGTCAAACCAGCCAATATCCTTCTGGACTCCTACGGCTCTCCTCGGCTGTCGGACTTCGGTATCGCCGCTGTCCAGCGCGAGGGTCAGGACCCCACCGTGACCCTGGAGTGCCTCACCCCCGACTTCGCCGCGCCGGAGGCGTTCATGCTGGCCAGCCCCGGCCCCGAGGGGGACGTGTGGTCCATGGGGGCGGTTCTCTTCGCCCTGCTGACGGGCCGGGGTCCTCGGCGTGGTCGCGACGGAGTGCAGCGCAGCCTGCCGGAGATCGTCCGGTCCCTCGACGATCCCCTGGACCTCACCGACCCGAATGTCCCTGAGATCCTGCTGCCGATCCTGAGCAAGGCGATGGCTCCGGATCCCACGCACCGCTACCGCAACGGCACGGAGCTCACCGGAGCCCTGGGGCAGATCCGTGAGGCTCTGGGGACGGGGAACCTGGCTGTCGGCGGGCCAGTGACCTCTTTGCGGCTGGTTGAGGCCGGGCTCGCGCCGCCTCCGCGCAGTGAAGAGGCGGGCTCACCCAACTCGTACGCTCCTAGCGGGGCATCGCAGTGGGCGGCATCGGACTCCGTCTTCCCGGTCCGCCCCACCGGCTCCTCGGGGTCCGCCGCCTCGGCGCCCTCCATCGTCTCAGGCGGGCTGGAGCGCTCCGACAAGGCGCTGCTGAACGCGCCCGTGTCAGCGCAGCAGAGTCAGTCGCTGCAGCTCTCTAGCCGAGAACGGAGGCGGACCGCTCTGCGCTCCGCGGCGATCGGCGCGGTTGTCGGCCTGGTCGTCGGTCTGAGCGCAGGATGGGTGGCGGGTGCCCGTCTGGCTCCTGCGGCCAGTGCCACCAGAGCGTCGGGGGCCGTCTCCCAGCCCTCGTCGTCGAGTCAGGACAACTCCTCGACCCCACCGCACCCGGTGGGTACCTGCCTGGCGGGAACCACCTCGATCTCGGGTCAGACCACGGCCAGGAAGGTCAGCTGCAACGAGCCCCACTCCTGGGAGGTCTTCCAGGTGGGGACCCTGGCGGAGAGCACCTCAGGGTCCAGCGATGACGACCTGGCCGCAGATCCCAATGTGCAGGCCGCCTGCACCGCACAGGCCGCTCAACAGTACGGGGCCAGTGATCCGAACACGTCGGTGCTGGGCCCGGGGGAGGCCGGGTGGAACGCCGGGAAGCGAGGCTTCTCCTGCATCGCCTCCGACAAGGACGGGCAGCGGACGAGCTCCTACGCCGGATAG","MQFPSGQASAPPWPASPPPPSSQASASHSPAAAGAGSGSSSGSRSAAPFSIPGVRITSVLGRGGFATVYAGVQDSLERPVAVKVDSRPLDDPRNERRFMREVQAASRISGHPHVVSLVDTGKLPDLRPYLVMELCAGGSLYDLVSRGPTPASDAVALVEAAASALGAAHAAGVTHRDVKPANILLDSYGSPRLSDFGIAAVQREGQDPTVTLECLTPDFAAPEAFMLASPGPEGDVWSMGAVLFALLTGRGPRRGRDGVQRSLPEIVRSLDDPLDLTDPNVPEILLPILSKAMAPDPTHRYRNGTELTGALGQIREALGTGNLAVGGPVTSLRLVEAGLAPPPRSEEAGSPNSYAPSGASQWAASDSVFPVRPTGSSGSAASAPSIVSGGLERSDKALLNAPVSAQQSQSLQLSSRERRRTALRSAAIGAVVGLVVGLSAGWVAGARLAPAASATRASGAVSQPSSSSQDNSSTPPHPVGTCLAGTTSISGQTTARKVSCNEPHSWEVFQVGTLAESTSGSSDDDLAADPNVQAACTAQAAQQYGASDPNTSVLGPGEAGWNAGKRGFSCIASDKDGQRTSSYAG$","Protein kinase/transcriptional regulator, LuxR family","Periplasm, Membrane, Extracellular","serine/threonine protein kinase","protein kinase/transcriptional regulator; LuxR family ","protein kinase","","Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995. 9(8):576-596. PMID: 7768349Hunter T. Protein kinase classification. Meth. Enzymol. 1991. 200:3-37. PMID: 1835513Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth. Enzymol. 1991. 200:38-62. PMID: 1956325Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988. 241(4861):42-51. PMID: 3291115Knighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991. 253(5018):407-414. PMID: 1862342","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[59-311]T$	Q6AEZ5_BBBBB_Q6AEZ5;
PF00069	$\"[54-301]T$	Pkinase
PS50011	$\"[54-318]T$	PROTEIN_KINASE_DOM
PS00107	$\"[60-83]T$	PROTEIN_KINASE_ATP

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[173-185]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[127-301]T$	no description
PTHR22982	$\"[101-302]T$	CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE-RELATED
tmhmm	$\"[426-446]?$	transmembrane_regions

","BeTs to 11 clades of COG0515COG name: Serine/threonine protein kinasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0515 is -o-p-zyq-drlbcefghs--j-i-wNumber of proteins in this genome belonging to this COG is 10","***** IPB000961 (Protein kinase C-terminal domain) with a combined E-value of 1e-19. IPB000961C 156-198 IPB000961D 212-253***** IPB000959 (POLO box duplicated region) with a combined E-value of 9.6e-18. IPB000959A 54-99 IPB000959C 160-199 IPB000959D 216-270***** IPB008266 (Tyrosine protein kinase, active site) with a combined E-value of 3e-16. IPB008266A 160-200 IPB008266B 218-254***** IPB003527 (MAP kinase) with a combined E-value of 6.4e-14. IPB003527A 80-122 IPB003527C 149-199 IPB003527D 230-272***** IPB000861 (PKN/rhophilin/rhotekin rho-binding repeat) with a combined E-value of 2.9e-10. IPB000861C 51-87 IPB000861D 132-185 IPB000861E 218-267***** IPB013695 (Wall-associated kinase) with a combined E-value of 2.5e-09. IPB013695I 166-202 IPB013695J 203-252***** IPB000472 (Domain in TGF-beta receptor/activin receptor, type I/II) with a combined E-value of 1.1e-08. IPB000472C 111-165 IPB000472D 170-200***** IPB001772 (Kinase-associated, C-terminal) with a combined E-value of 1.5e-07. IPB001772A 51-82 IPB001772D 223-262***** IPB000095 (PAK-box/P21-Rho-binding) with a combined E-value of 5.1e-07. IPB000095D 137-183 IPB000095E 196-240***** IPB010513 (Ribonuclease 2-5A) with a combined E-value of 1.7e-06. IPB010513D 164-185 IPB010513E 235-255","Residues 49-252 are 40% similar to a (KINASE LIKE NEUROSPORA RELATED STE20- B16M17.090 Q871H9 DON3 CRASSA) protein domain (PDA064R7) which is seen in Q6C8H9_EEEEE.Residues 49-313 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA10189) which is seen in Q7UKJ3_RHOBA.Residues 49-319 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D3Y0) which is seen in Q7UVF2_RHOBA.Residues 50-204 are 55% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA18944) which is seen in Q7UPN1_RHOBA.Residues 50-311 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD500022) which is seen in Q8YMH9_ANASP.Residues 50-300 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA1D4Q5) which is seen in Q7ULK7_RHOBA.Residues 50-359 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE-THREONINE ATP-BINDING) protein domain (PD319602) which is seen in Q9K3W7_STRCO.Residues 50-282 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING MAP) protein domain (PDA18314) which is seen in Q93WR7_MEDVA.Residues 51-316 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA10203) which is seen in Q7UIJ7_RHOBA.Residues 51-311 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756060) which is seen in Q81ZY9_STRAW.Residues 52-311 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA08789) which is seen in Q7UL45_RHOBA.Residues 52-328 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN PKN10 TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA043E6) which is seen in Q7UGA2_RHOBA.Residues 52-300 are 44% similar to a (BLR3604 KINASE TRANSFERASE ATP-BINDING) protein domain (PD828726) which is seen in Q89P79_BRAJA.Residues 53-310 are 48% similar to a (SERINE/THREONINE-PROTEIN KINASE PROBABLE TRANSFERASE PKNJ TRANSMEMBRANE ATP-BINDING) protein domain (PD063660) which is seen in PKNJ_MYCTU.Residues 54-255 are 42% similar to a (KINASE SER/THR P08458 SPS1 CEREVISIAE YDR523C SACCHAROMYCES) protein domain (PDA0B8H6) which is seen in Q6C9X8_EEEEE.Residues 54-300 are 41% similar to a (KINASE TRANSFERASE TYROSINE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD523147) which is seen in Q8WPV5_SCHMA.Residues 55-365 are 48% similar to a (KINASE PKNB SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5H6) which is seen in Q7UFU9_RHOBA.Residues 55-359 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796289) which is seen in Q9S2A6_STRCO.Residues 55-361 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD298418) which is seen in Q9X8G8_STRCO.Residues 55-252 are 53% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796751) which is seen in Q81ZW2_STRAW.Residues 55-300 are 46% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE WD SERINE/THREONINE ATP-BINDING) protein domain (PD288091) which is seen in Q9RDS3_STRCO.Residues 55-314 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING PLASMID) protein domain (PD756391) which is seen in Q820A7_STRAW.Residues 55-311 are 47% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE TPR PHOSPHORYLATION REPEAT PKN1 ATP-BINDING) protein domain (PD052299) which is seen in PKN1_MYXXA.Residues 55-314 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN PPKA TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA025J8) which is seen in Q7UT84_RHOBA.Residues 55-321 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNA TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D5E6) which is seen in Q7UX63_RHOBA.Residues 55-327 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA191E0) which is seen in Q8DLN7_SYNEL.Residues 55-365 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD756057) which is seen in Q81ZV7_STRAW.Residues 55-298 are 40% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA1D5J2) which is seen in Q7UZ75_RHOBA.Residues 55-350 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA1D464) which is seen in Q7UW31_RHOBA.Residues 55-361 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD724652) which is seen in Q81ZW8_STRAW.Residues 55-284 are 45% similar to a (SERINE/THREONINE-PROTEIN KINASE REPEAT PROBABLE TRANSFERASE WD PKWA ATP-BINDING) protein domain (PD110150) which is seen in PKWA_THECU.Residues 55-285 are 47% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA TRANSFERASE ATP-BINDING PROBABLE) protein domain (PDA188K3) which is seen in PKNA_MYCLE.Residues 55-301 are 43% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA0Z806) which is seen in Q7NLM6_GLOVI.Residues 55-297 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD141352) which is seen in O54230_STRGT.Residues 55-318 are 46% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING PROBABLE SERINE-THREONINE) protein domain (PD736072) which is seen in Q8G6Q0_BIFLO.Residues 55-252 are 47% similar to a (KINASE P27636 SERINE/THREONINE-PROTEIN TRANSFERASE CDC15 CEREVISIAE ATP-BINDING SACCHAROMYCES YAR019C) protein domain (PDA0F8T8) which is seen in Q6FWK3_EEEEE.Residues 55-308 are 50% similar to a (SERINE/THREONINE-PROTEIN KINASE PKNA2 PROBABLE TRANSFERASE REPEAT ATP-BINDING) protein domain (PD848557) which is seen in PKNA_BIFLO.Residues 55-353 are 48% similar to a (SERINE/THREONINE-PROTEIN KINASE PKN3 TRANSFERASE ATP-BINDING) protein domain (PD316927) which is seen in PKN3_MYXXA.Residues 55-335 are 44% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD975784) which is seen in Q7NPK1_GLOVI.Residues 55-318 are 52% similar to a (KINASE SERINE/THREONINE) protein domain (PDA1A7D8) which is seen in Q6AE50_BBBBB.Residues 55-320 are 48% similar to a (PKND) protein domain (PDA18730) which is seen in Q73UI1_MYCPA.Residues 56-252 are 44% similar to a (KINASE 1-LIKE RESPONSIVE ATP-BINDING STRESS) protein domain (PD099489) which is seen in O61125_DICDI.Residues 56-373 are 46% similar to a (KINASE SERINE-THREONINE) protein domain (PDA1D4F7) which is seen in Q6A9T0_PROAC.Residues 56-252 are 48% similar to a (CELL DIVISION SERINE/THREONINE-PROTEIN CONTROL KINASE CYCLE TRANSFERASE 2.7.1.- MITOSIS ATP-BINDING) protein domain (PDA0F8T7) which is seen in CC15_YEAST.Residues 56-300 are 47% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PDA1A878) which is seen in Q72IA2_THET2.Residues 56-300 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD796214) which is seen in Q81ZX4_STRAW.Residues 56-316 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD239091) which is seen in Q9KJN8_MYXXA.Residues 56-252 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING) protein domain (PD727335) which is seen in Q86JX3_DICDI.Residues 56-318 are 48% similar to a (KINASE PKN9 SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD268676) which is seen in Q9XBP3_MYXXA.Residues 56-255 are 45% similar to a (KINASE REPEAT TPR SERINE/THREONINE ATP-BINDING PKN8) protein domain (PD280760) which is seen in Q9XBP6_MYXXA.Residues 56-314 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING SERINE/THREONINE-SPECIFIC PROBABLE) protein domain (PDA1D2S2) which is seen in Q7UFH1_RHOBA.Residues 56-361 are 47% similar to a () protein domain (PDA046H8) which is seen in Q73YC5_MYCPA.Residues 56-252 are 43% similar to a (AFR724CP ATP-BINDING) protein domain (PDA101P3) which is seen in Q751V1_ASHGO.Residues 56-320 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE KINASE ATP-BINDING) protein domain (PD828286) which is seen in Q9RRH3_DEIRA.Residues 56-257 are 46% similar to a (KINASE TRANSFERASE ATP-BINDING MOS) protein domain (PD267193) which is seen in Q9GRC0_ASTPE.Residues 59-255 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN ACR142WP TRANSFERASE ATP-BINDING) protein domain (PDA0A7Q6) which is seen in Q75CE9_ASHGO.Residues 59-252 are 44% similar to a (P0418B08.10 OJ1740_D06.39) protein domain (PDA10665) which is seen in Q69P46_EEEEE.Residues 59-301 are 44% similar to a (SERINE/THREONINE-PROTEIN KINASE MEK1 MEIOSIS TRANSFERASE ATP-BINDING MEIOSIS-SPECIFIC) protein domain (PDA0I4P9) which is seen in MEK1_SCHPO.Residues 59-361 are 38% similar to a (KINASE SERINE/THREONINE-PROTEIN GLP_28_16955_18661 TRANSFERASE ATP-BINDING) protein domain (PDA08641) which is seen in Q7R1Q1_EEEEE.Residues 59-250 are 45% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE BRASSINOSTEROID ATP-BINDING INSENSITIVE) protein domain (PD595107) which is seen in Q84ZJ8_EEEEE.Residues 59-260 are 48% similar to a (SIMILAR DEBARYOMYCES HANSENII DEHA0C16181G) protein domain (PD991318) which is seen in Q6C3K8_EEEEE.Residues 59-311 are 51% similar to a (KINASE ATP-BINDING TRANSFERASE SERINE/THREONINE-PROTEIN RECEPTOR PHOSPHORYLATION SERINE/THREONINE TYROSINE-PROTEIN REPEAT CELL) protein domain (PD000001) which is seen in Q6AEZ5_BBBBB.Residues 60-252 are 42% similar to a (KINASE STRESS-RESPONSIVE PRKSD ATP-BINDING) protein domain (PD087289) which is seen in O62571_SUBDO.Residues 60-302 are 42% similar to a (YARROWIA LIPOLYTICA STRAIN CHROMOSOME CLIB99 B) protein domain (PDA12896) which is seen in Q6CFM7_EEEEE.Residues 60-291 are 50% similar to a (KINASE SERINE/THREONINE-PROTEIN PROBABLE TRANSFERASE 2.7.1.- SERINE/THREONINE ATP-BINDING) protein domain (PDA010X1) which is seen in Q7UKY9_RHOBA.Residues 60-349 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD842227) which is seen in Q81ZZ0_STRAW.Residues 60-252 are 44% similar to a (KINASE RELATED ATP-BINDING SEVERIN) protein domain (PDA0F7C6) which is seen in Q7SFV7_NEUCR.Residues 60-291 are 41% similar to a (KINASE DJFGFR1 TRANSFERASE TYROSINE-PROTEIN ATP-BINDING) protein domain (PD611563) which is seen in Q8MY86_DUGJA.Residues 60-310 are 43% similar to a (KINASE SERINE/THREONINE) protein domain (PD456344) which is seen in Q98IK2_RHILO.Residues 60-300 are 45% similar to a (KINASE SER/THR TRANSFERASE ATP-BINDING) protein domain (PD126531) which is seen in O54229_STRGT.Residues 60-252 are 44% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE APOPTOSIS HIPPO ATP-BINDING) protein domain (PD727337) which is seen in HPO_DROME.Residues 60-260 are 47% similar to a (SERINE/THREONINE-PROTEIN KINASE TRANSFERASE ATP-BINDING SHK2) protein domain (PD078766) which is seen in SHK2_SCHPO.Residues 60-357 are 42% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD820279) which is seen in Q81ZY2_STRAW.Residues 60-252 are 44% similar to a (KINASE STE20-LIKE ATP-BINDING DON3) protein domain (PD609771) which is seen in Q8NJX3_USTMA.Residues 60-314 are 49% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE SERINE/THREONINE ATP-BINDING) protein domain (PD810446) which is seen in Q895P6_CLOTE.Residues 60-300 are 56% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE TRANSCRIPTION ATP-BINDING DNA-BINDING SERINE-THREONINE REGULATION) protein domain (PDA1B2W7) which is seen in Q6PV87_BBBBB.Residues 60-252 are 51% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB TRANSFERASE 2.7.1.- ATP-BINDING PROBABLE) protein domain (PDA19096) which is seen in Q7UJC1_RHOBA.Residues 60-330 are 48% similar to a (KINASE SERINE/THREONINE-PROTEIN PKNB PROBABLE TRANSFERASE 2.7.1.- ATP-BINDING) protein domain (PDA0H1H6) which is seen in Q7UJD9_RHOBA.Residues 70-323 are 41% similar to a (KINASE SERINE/THREONINE-PROTEIN SERINE/THREONINE KINASE) protein domain (PD745593) which is seen in Q9RUY7_DEIRA.Residues 79-252 are 50% similar to a (KINASE CAMP-DEPENDENT SERINE/THREONINE-PROTEIN CATALYTIC TRANSFERASE ATP-BINDING SUBUNIT) protein domain (PD750451) which is seen in Q9BMY6_TOXGO.Residues 90-252 are 52% similar to a (KINASE CBS138 CANDIDA SEQUENCE K SERINE/THREONINE-PROTEIN GLABRATA STRAIN ATP-BINDING TRANSFERASE) protein domain (PD957660) which is seen in Q6FMF3_EEEEE.Residues 100-252 are 54% similar to a (SERINE/THREONINE-PROTEIN KINASE YKL101W PROBABLE ATP-BINDING TRANSFERASE) protein domain (PD095148) which is seen in KKK1_YEAST.Residues 136-303 are 46% similar to a (DOMAIN KINASE TRANSFERASE PHOSPHORYLATION TRANSDUCTION SENSORY SENSOR KINASE/GAF HISTIDINE) protein domain (PD781329) which is seen in Q88CD9_PSEPK.Residues 173-300 are 49% similar to a (KINASE REPEAT SERINE/THREONINE-PROTEIN ANK ATP-BINDING TRANSFERASE GLP_39_28978_30531) protein domain (PD959207) which is seen in Q7R3P5_EEEEE.Residues 173-311 are 47% similar to a () protein domain (PD743406) which is seen in Q8G5T5_BIFLO.Residues 173-255 are 57% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE CAMP ATP-BINDING CAMP-DEPENDENT NUCLEAR) protein domain (PD061517) which is seen in O00843_PARPR.Residues 173-253 are 62% similar to a (KINASE SERINE/THREONINE-PROTEIN TRANSFERASE ATP-BINDING KINASE-LIKE) protein domain (PDA198D0) which is seen in Q8S1B9_EEEEE.","","-48% similar to PDB:1MRU Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB. (E_value = 1.7E_22);-48% similar to PDB:1O6Y CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.7E_22);-48% similar to PDB:2FUM Catalytic domain of protein kinase PknB from Mycobacterium tuberculosis in complex with mitoxantrone (E_value = 1.7E_22);-45% similar to PDB:2H34 Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE (E_value = 8.9E_19);-49% similar to PDB:2HAK Catalytic and ubiqutin-associated domains of MARK1/PAR-1 (E_value = 2.6E_18);","Residues 54 to 318 (E_value = 3.3e-38) place ANA_1061 in the Pkinase family which is described as Protein kinase domain.Residues 54 to 142 (E_value = 1.2e-11) place ANA_1061 in the Pkinase_Tyr family which is described as Protein tyrosine kinase.","","protein kinase (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1062","1137254","1136424","831","4.36","-27.08","28585","ATGGGCGACGTGGAGATCCCCGCCGACCTCTCGGATGATGACCTGGGGAATGTGCAGGAGGCCGGCAGTGAACCGGGCCGGCAGACCCCGGTGGAGGACGACTCCGTATCGACCGGCTCTACGGGGGAGAGCGGACCGGCAGACATCAGGCCCGACGACGTCCCCCACAACACCTACCATCCCCTGAACGGGGGACAGGGGCGAGCAGAGGATGCTCAACGCTCGTCCCGGCTCACTGATGCCCAGGAGGCGCAGATCGCCGCCGCGGCCGACTCCCTGAGCGCCTACGTGCCCGATCAGTCCGAGGAGGAGGCTCCCCGGGCGGTCAAGGTCGCCGTCGTCATGACGCCGCTGAACCGGGCCGACGGCCTGGCCGGAATGTGCTCCCTGCTGGACCTCGACTGCACCGTGGTGCCCTCCTCCAGCGGGGCCTTCGCGGTCAAGCAGTTCGTCTCCGCCCACTCGGACTGGGATGTGGCCGAGCTGCTTGGCGGCTCCGACTCCGAGCCCGCAGAGGCCGCGGAGCTGGCCGCCCAGCTCTCTCGTCTGTCCCGGGCCGGGGCGGTGCTCATGACGGCCGACCTGGCCACCGACGTCGGTATCGAGTCCGGTCTGTCCGGGACGATCACTGCTCGTCACTTCACCAACGGCCAGCCCGGCGAGGAGGCATCGGCGGGGCTCCTACTGGCCTCCATGGATCAGGTCGTCGAGGACATCCTCCTGGGAGTCATCGATGCCGACGACGTCCCCGGAGCGGTGAAGTCCTCCGAGATCCAGCCGCCCCGGGCGATGCGCTGGTTCGGACGCGGACTGCGCCGTCCCCCGCAGTGA","MGDVEIPADLSDDDLGNVQEAGSEPGRQTPVEDDSVSTGSTGESGPADIRPDDVPHNTYHPLNGGQGRAEDAQRSSRLTDAQEAQIAAAADSLSAYVPDQSEEEAPRAVKVAVVMTPLNRADGLAGMCSLLDLDCTVVPSSSGAFAVKQFVSAHSDWDVAELLGGSDSEPAEAAELAAQLSRLSRAGAVLMTADLATDVGIESGLSGTITARHFTNGQPGEEASAGLLLASMDQVVEDILLGVIDADDVPGAVKSSEIQPPRAMRWFGRGLRRPPQ$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-46% similar to PDB:1DEQ THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION) (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1063","1137937","1137338","600","6.17","-6.72","21533","ATGAGCCGTACCGCGCGCATTGAGCGAGCCACGAGCGAGTCGAGCGTCGTCGTCGAGATCAACCTCGATGGCACGGGCCAGACCGACATCTCCACCACCGTCCCCTTCTACGACCACATGCTCACCGCGCTGGGGCGCCACTCACTCATCGATCTGACGGTGCGCGCCACCGGTGACACCGAGATCGACGTGCACCACACCGTGGAGGACACCGCCATCTGCATCGGTGAGGCCCTGCGCGTCGCCCTGGGGGACAAGCGCGGCATCCGCCGCTTCGGCGAGGCCAGCGTTCCCCTGGACGAGGCCCTGGCGCATGCAGTCGTCGACATCTCCGGGCGCCCCTACCTGGTGCACGAGGGGGAGTCCGAGGCCTTCATCCACCACCTCATCGGCGGTCACTTCACCGGTTCCATGGTGCGCCACGTGCTGGAGGCCATCGCCTACCATGCCGGCATCTGCCTGCACGTGCGGGTCCTGGCCGGTCGCGATCCCCACCACATCGCCGAGGCCGAGTTCAAGGCCCTGGCTCGCGCCCTGCGCGCAGCCGTGGAGGACGACCCCCGCGTTGAGACCATCCCATCGACGAAGGGAAGCCTGTGA","MSRTARIERATSESSVVVEINLDGTGQTDISTTVPFYDHMLTALGRHSLIDLTVRATGDTEIDVHHTVEDTAICIGEALRVALGDKRGIRRFGEASVPLDEALAHAVVDISGRPYLVHEGESEAFIHHLIGGHFTGSMVRHVLEAIAYHAGICLHVRVLAGRDPHHIAEAEFKALARALRAAVEDDPRVETIPSTKGSL$","Imidazoleglycerol-phosphate dehydratase","Cytoplasm","imidazoleglycerol-phosphate dehydratase","imidazoleglycerol-phosphate dehydratase ","Imidazoleglycerol-phosphate dehydratase","","Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B. Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. J. Mol. Biol. 1988. 203(3):585-606. PMID: 3062174","","","

InterPro
IPR000807
Domain

Imidazole glycerol-phosphate dehydratase
PD002282	$\"[7-199]T$	HIS7_BIFLO_Q8G4S7;
PF00475	$\"[32-180]T$	IGPD
PS00954	$\"[62-75]T$	IGP_DEHYDRATASE_1
PS00955	$\"[161-173]T$	IGP_DEHYDRATASE_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.230.40	$\"[3-90]T$ $\"[91-199]T$	no description
PTHR23133	$\"[1-199]T$	IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7
PTHR23133:SF2	$\"[1-199]T$	IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7

","BeTs to 18 clades of COG0131COG name: Imidazoleglycerol-phosphate dehydrataseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0131 is aom---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000807 (Imidazoleglycerol-phosphate dehydratase) with a combined E-value of 2.4e-55. IPB000807A 3-38 IPB000807B 58-93 IPB000807C 161-182 IPB000807C 61-82","Residues 7-199 are similar to a (BIOSYNTHESIS HISTIDINE LYASE DEHYDRATASE IMIDAZOLEGLYCEROL-PHOSPHATE IGPD HYDROLASE BIFUNCTIONAL HISTIDINOL-PHOSPHATASE INCLUDES:) protein domain (PD002282) which is seen in HIS7_BIFLO.","","-65% similar to PDB:2F1D X-Ray Structure of imidazoleglycerol-phosphate dehydratase (E_value = 5.7E_49);-62% similar to PDB:1RHY Crystal structure of Imidazole Glycerol Phosphate Dehydratase (E_value = 4.1E_39);-55% similar to PDB:2AE8 Crystal Structure of Imidazoleglycerol-phosphate Dehydratase from Staphylococcus aureus subsp. aureus N315 (E_value = 5.5E_28);-45% similar to PDB:1L8W Crystal Structure of Lyme Disease Variable Surface Antigen VlsE of Borrelia burgdorferi (E_value = 5.5E_28);-43% similar to PDB:2F8M Ribose 5-phosphate isomerase from Plasmodium falciparum (E_value = 5.5E_28);","Residues 32 to 180 (E_value = 1.9e-71) place ANA_1063 in the IGPD family which is described as Imidazoleglycerol-phosphate dehydratase.","","dehydratase (hisB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1064","1139191","1138049","1143","5.18","-12.13","40567","GTGAACGCGAACCTGCCCCTGAGACCGGACCTGGAGGGCGAGGCCCCCTACGGGGCCCCCGAGATCGACGTCCCCGTGAGACTGAACGTCAACGAGAATCCCTACCCTCCGTCGGCCGCGGTCATCGAGTCGATCGCCACCGCCGTGGCTCAGGCCGCCCAGGGACTTAACCGCTACCCGGAGCGGGACTTCCCCCGGCTGCGGGCCGCGCTCGCGGACTATCTCGCGGTCGAGTCCGGCGCGCACCTGGCTCCCGAGCAGATCTGGGCGGCCAATGGCTCCAACGAGGTCATGCTCCACGTGCTCCAGGCCTTCGGTGGTCCCGGGCGCACCTGCCTGACCTTCACCCCCACCTACTCGATGTACCCCGAGTACGCCCGCGACACCCTGACCGACTACGCCACCCGAGCGCGCCGCCAGGACTTCACCCTCGATACGGACGCCGCGGTGGCCGCGATCAACGAGCTGCGGCCGGCCGTCATCATCCTGGCCAGCCCCAACAACCCGACCGGAACCGCCCTGCCGCTGGAGGACATCACGCGGATCCTTGAGGCCGCCCGCGGCCACGGCCCCATGCTCGGAGCCGAGATCGGCTCGCCCACCCGGGCCAGCGACTGCGTCGTCGTCATCGACGAGGCTTACGCCGAGTTCCGCCGCCCGGGCGTGCCCAGCGCCCTGGAGCTGGTGGGACCGGACAACCCGCACCTGGCCGTCACCCGCACCATGTCCAAGGCCTTCGGAGCGGCCGGCCTGCGCCTGGGCTACCTGGCCGCCGACCGCGCCTTGGTAGACGCCCTGCGCGTGGTGCGCCTGCCCTACCACCTCTCCGCCCTCACCCAGGCCGCCGCCCTGGCCGCCCTGTCCCACCGCGACGAGCTCATGGCTCAGGTGGCCTCCCTGCGCGATGAGCGTGATGCCTTCGTGGACTGGCTGCACAGCCAGGGCCTGAGCGCGCACGCATCGGACGCCAACTTCGTCCTGTTCGGGCCCTTCCCCGACCGCGAGGCTGTCTGGCAGGCCCTGCTCGACGCCGGGGTCCTCATCCGTGTCGTCGGCCCCGAGGGTTTCCTGCGCGCCAGCATCGGCACGCCGGAGGAGATGGCACGTCTGCGCGGTGCCCTGGCCACGGCCATCGGCGGATGA","VNANLPLRPDLEGEAPYGAPEIDVPVRLNVNENPYPPSAAVIESIATAVAQAAQGLNRYPERDFPRLRAALADYLAVESGAHLAPEQIWAANGSNEVMLHVLQAFGGPGRTCLTFTPTYSMYPEYARDTLTDYATRARRQDFTLDTDAAVAAINELRPAVIILASPNNPTGTALPLEDITRILEAARGHGPMLGAEIGSPTRASDCVVVIDEAYAEFRRPGVPSALELVGPDNPHLAVTRTMSKAFGAAGLRLGYLAADRALVDALRVVRLPYHLSALTQAAALAALSHRDELMAQVASLRDERDAFVDWLHSQGLSAHASDANFVLFGPFPDREAVWQALLDAGVLIRVVGPEGFLRASIGTPEEMARLRGALATAIGG$","Histidinol-phosphate aminotransferase","Cytoplasm","histidinol-phosphate aminotransferase","histidinol-phosphate aminotransferase ","histidinol-phosphate aminotransferase","","Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K., Okamoto A., Higuchi T., Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 1991. 266(4):2567-2572. PMID: 1990006","","","

InterPro
IPR001917
Binding_site

Aminotransferase, class-II
PS00599	$\"[241-250]?$	AA_TRANSFER_CLASS_2

InterPro
IPR004839
Domain

Aminotransferase, class I and II
PF00155	$\"[23-374]T$	Aminotran_1_2

InterPro
IPR005861
Family

Histidinol-phosphate aminotransferase
TIGR01141	$\"[8-377]T$	hisC: histidinol-phosphate aminotransferase

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[41-289]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[43-190]T$ $\"[206-378]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF3	$\"[43-190]T$ $\"[206-378]T$	HISTIDINOL-PHOSPHATE AMINOTRANSFERASE

","BeTs to 18 clades of COG0079COG name: Histidinol-phosphate aminotransferase/Tyrosine aminotransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0079 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB004839 (Aminotransferase, class I and II) with a combined E-value of 2.8e-13. IPB004839A 152-172 IPB004839B 211-218 IPB004839C 243-254***** IPB001917 (Aminotransferase, class-II) with a combined E-value of 3.2e-12. IPB001917A 207-219 IPB001917B 237-254***** IPB001176 (1-aminocyclopropane-1-carboxylate synthase signature) with a combined E-value of 1.3e-09. IPB001176E 155-179 IPB001176G 235-259***** IPB004838 (Aminotransferase, class-I) with a combined E-value of 2.2e-09. IPB004838C 161-173 IPB004838D 241-254","Residues 26-119 are 76% similar to a (AMINOTRANSFERASE TRANSFERASE PHOSPHATE PYRIDOXAL ASPARTATE TRANSAMINASE HISTIDINOL-PHOSPHATE SYNTHASE BIOSYNTHESIS TRANSCRIPTION) protein domain (PD000087) which is seen in Q6A8L4_PROAC.Residues 120-174 are 74% similar to a (AMINOTRANSFERASE PHOSPHATE TRANSFERASE HISTIDINOL-PHOSPHATE TRANSAMINASE BIOSYNTHESIS PYRIDOXAL IMIDAZOLE HISTIDINE ACETOL-) protein domain (PD769230) which is seen in Q6A8L4_PROAC.Residues 138-214 are 57% similar to a (SYNTHASE PHOSPHATE PYRIDOXAL AMINOTRANSFERASE 1-AMINOCYCLOPROPANE-1-CARBOXYLATE TRANSFERASE LYASE ACC ALANINE TRANSAMINASE) protein domain (PD534063) which is seen in HIS8_MYCLE.Residues 272-364 are 67% similar to a (AMINOTRANSFERASE PHOSPHATE TRANSFERASE HISTIDINOL-PHOSPHATE PYRIDOXAL BIOSYNTHESIS TRANSAMINASE IMIDAZOLE HISTIDINE ACETOL-) protein domain (PD164716) which is seen in Q6A8L4_PROAC.","","-40% similar to PDB:1FG3 CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH L-HISTIDINOL (E_value = 2.9E_17);-40% similar to PDB:1FG7 CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE WITH PYRIDOXAL-5'-PHOSPHATE (E_value = 2.9E_17);-40% similar to PDB:1GEW CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE (E_value = 2.9E_17);-40% similar to PDB:1GEX CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH HISTIDINOL-PHOSPHATE (E_value = 2.9E_17);-40% similar to PDB:1GEY CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH N-(5'-PHOSPHOPYRIDOXYL)-L-GLUTAMATE (E_value = 2.9E_17);","Residues 23 to 374 (E_value = 1.4e-63) place ANA_1064 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.","","aminotransferase (hisC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1065","1141222","1139294","1929","7.30","1.85","67437","ATGGACCTCCTCATCATCGCCGTGCTGGGCACTCTGGCCATCGCTGCGGCCTCTCAGCTCAGCGACCGCATCGGGGTCGCCCCGGCGCTGATCCTCCTGGCGGGCGGCACTGCGGTGGGCTTCCTACCCTTCATCCCGGCGATCGAGCTGAACCCCCAGGTGGTCCTGGAGGGGATCCTCCCCCCGCTGCTGTTCTCCACGGCGGTGCGTATCTCCACCATCAACTTCCGCCGCGAGCTCGCCCCGGTGGCAGTGCTGGCCATCCTGCTGGTTCCCCTGTCCGCCGCGGTGATCGGCGCGGTCCTCACCGTTCTGGTTCCGGGACTCTCCCTGGCCTGGGCCATCGCCATGGGGGCAATCCTCAGCCCCACCGACGCCGTGGCCATCTCCATCGCCCGCCGGCTGGGAGTCTCCCAACGCATCATCACTGTCCTGGAGGGGGAGGGACTGCTCAACGACGCCACCGCTCTGGTGGTCCTGTCCTCCGCGGTCTCCGCGGCCACCTCCGGCGGTGTCAGCATCGGAGGCGTCCTGGGCGGCTTCGCCCTGGCGGTCCTCGTGGCCCTGGGGGTGGGCTGGCTCGTCGGCGAGGCGAGCCTGCGGGTGCGCTCCCACATCACCGACCCCACCGTGGACACGGTGGTGTCCTTCACCGTCCCCTTCCTCGCGGCGATCCCGGCCGAGCACATGCACGGCTCCGGTCTTGTGGCAGCCGTTGTCGCCGGGCTCATCACCGGTCACCGTGGTCCCCGGATGCTGCCGCCCGCCCACCGGGTGGCCTCACGCACCAACTGGCACACTGTCGAGCTCACCCTGGAAGGACTCATCTTCCTGGTCATGGGGCTGGAGTTCTTCGGCGTCGTGGAGAAGGTCGGCGCCTCAGCTCTCGGTGTTGTCCGGGCCGTCGCGGTCGCTGTCGTCGCCGGGGCGCTGACCGTCGTCATCCGGGCGCTCGTGGTGGCACCCATGCTCAAGGTCCTCAGCCACCGGACCACGCGCTGGGCGATCCACTGGCAGGAGAATGAGGAGGCCATCCACCAGTTCCAGAACCGCTGCTCGGCCATCGTGCGCGGAGAGTCCGAGATGCCGCCGGTCCCTTGGGACCGGCGCCCCTTCGCGCAGGTCCAGCGTAAGCTCCGCCGGGCAACCAACCACGAGAGCATCGCTCGGCGCGCACGCAGCCTCTCCAGCCGAGTCAGACGTAGGGGCGCCGACCTGGACTACTTCGCAGCCGAGCCCCTGGGCAGACGTGAGGGAGCCGTCATCGTCTGGGCGGGCATGCGCGGCGCCATCACCCTGGCAGCCGCCCAGACCCTGCCGGTCACAGCGCCTCACCACTCCTTCCTGCTCCTGGTGGCCATGCTCGTGGCCGCCGGCTCACTGACGATCCAGGGACTCACGCTGCCCGCCCTGGTCCGTCTCGCCAGACCCGCCATGGCCGGTCCCGCCGACGAGGAGGAGAAGGCCGCCGTCATCTCCCTGCTGGTCAACGCCGCCCGCGATGTCGCCTCCTCCGACACTCGCGGCGCCTCCCAGCAGGCCGCCCCCACAGTGCTCACCAATGCCTCAGGCCCCAACGCCTCAGACGTACAGACGACGACGAGCGCTCCGGGCCTGGACAAGGAGCCACAGGCCGCCCCTGAGAACACCGAGAGCCTCAGCCTCACCACTGAGCCGCACGGCCTCGTACGCAGGCAGGGCAAAGACGTCGTCGTCTCGCCGGCAGCCGTTGCCAAGGCCTGGGCCGACCCCACCTGGCGCCACGACGAGCTCGCCCCCATGCGAGAACGTGCCCTGGACATGATCCGAGCCCAGCGCGAGGCCCTTCTCGACGCCGGCGACGAGGGCCTCTACTCGGCCGACTCCCTGGAGCACGCCCTGAACCGCCTCGACTACCAGGAGATCATGCTCACCAGCGATCCGCACTGA","MDLLIIAVLGTLAIAAASQLSDRIGVAPALILLAGGTAVGFLPFIPAIELNPQVVLEGILPPLLFSTAVRISTINFRRELAPVAVLAILLVPLSAAVIGAVLTVLVPGLSLAWAIAMGAILSPTDAVAISIARRLGVSQRIITVLEGEGLLNDATALVVLSSAVSAATSGGVSIGGVLGGFALAVLVALGVGWLVGEASLRVRSHITDPTVDTVVSFTVPFLAAIPAEHMHGSGLVAAVVAGLITGHRGPRMLPPAHRVASRTNWHTVELTLEGLIFLVMGLEFFGVVEKVGASALGVVRAVAVAVVAGALTVVIRALVVAPMLKVLSHRTTRWAIHWQENEEAIHQFQNRCSAIVRGESEMPPVPWDRRPFAQVQRKLRRATNHESIARRARSLSSRVRRRGADLDYFAAEPLGRREGAVIVWAGMRGAITLAAAQTLPVTAPHHSFLLLVAMLVAAGSLTIQGLTLPALVRLARPAMAGPADEEEKAAVISLLVNAARDVASSDTRGASQQAAPTVLTNASGPNASDVQTTTSAPGLDKEPQAAPENTESLSLTTEPHGLVRRQGKDVVVSPAAVAKAWADPTWRHDELAPMRERALDMIRAQREALLDAGDEGLYSADSLEHALNRLDYQEIMLTSDPH$","Na+/H+ antiporter","Membrane, Cytoplasm","Na+:H+ antiporter","Na+/H+ antiporter","sodium/hydrogen exchanger","","Orlowski J., Grinstein S. Na+/H+ exchangers of mammalian cells. J. Biol. Chem. 1997. 272(36):22373-22376. PMID: 9278382Numata M., Petrecca K., Lake N., Orlowski J. Identification of a mitochondrial Na+/H+ exchanger. J. Biol. Chem. 1998. 273(12):6951-6959. PMID: 9507001Dibrov P., Fliegel L. Comparative molecular analysis of Na+/H+ exchangers: a unified model for Na+/H+ antiport?. FEBS Lett. 1998. 424(1):1-5. PMID: 9537504","","","

InterPro
IPR004705
Family

Bacterial Na+/H+ antiporter
PTHR10110:SF1	$\"[36-289]T$	SODIUM/HYDROGEN EXCHANGER YJCE

InterPro
IPR006153
Family

Sodium/hydrogen exchanger
PF00999	$\"[5-474]T$	Na_H_Exchanger

noIPR
unintegrated

unintegrated
PTHR10110	$\"[36-289]T$	SODIUM/HYDROGEN EXCHANGER
signalp	$\"[1-17]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[54-74]?$ $\"[83-103]?$ $\"[109-129]?$ $\"[150-170]?$ $\"[176-196]?$ $\"[206-226]?$ $\"[232-247]?$ $\"[268-288]?$ $\"[298-320]?$ $\"[448-468]?$	transmembrane_regions

","BeTs to 12 clades of COG0025COG name: NhaP-type Na+/H+ and K+/H+ antiportersFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0025 is aompk-y--drlbcefghs--j----Number of proteins in this genome belonging to this COG is 2","***** IPB006153 (Sodium/hydrogen exchanger) with a combined E-value of 6.6e-11. IPB006153B 125-160 IPB006153C 273-282","Residues 33-128 are 59% similar to a (TRANSMEMBRANE ANTIPORTER NA/H EXCHANGER ANTIPORT SODIUM SYSTEM ION GLUTATHIONE-REGULATED POTASSIUM-EFFLUX) protein domain (PD306538) which is seen in Q8UBF7_AGRT5.Residues 144-281 are similar to a (TRANSMEMBRANE NA/H EXCHANGER ANTIPORTER SODIUM ANTIPORT ION SODIUM/HYDROGEN FAMILY GLYCOPROTEIN) protein domain (PD552515) which is seen in Q73WE3_MYCPA.Residues 414-506 are 55% similar to a (TRANSMEMBRANE NA/H RV2287/MT2345/MB2309 YJCE EXCHANGER SODIUM ANTIPORT) protein domain (PD294081) which is seen in Q73YB3_MYCPA.Residues 417-473 are similar to a (TRANSMEMBRANE NA/H EXCHANGER SODIUM ANTIPORT ANTIPORTER ION SODIUM/HYDROGEN FAMILY MULTIGENE) protein domain (PD017855) which is seen in Q6AH33_BBBBB.","","-51% similar to PDB:1IW7 Crystal structure of the RNA polymerase holoenzyme from Thermus thermophilus at 2.6A resolution (E_value = );-51% similar to PDB:1SMY Structural basis for transcription regulation by alarmone ppGpp (E_value = );-51% similar to PDB:1ZYR Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin (E_value = );-51% similar to PDB:2A68 Crystal structure of the T. thermophilus RNA polymerase holoenzyme in complex with antibiotic rifabutin (E_value = );-51% similar to PDB:2A69 Crystal structure of the T. Thermophilus RNA polymerase holoenzyme in complex with antibiotic rifapentin (E_value = );","Residues 5 to 474 (E_value = 1.1e-31) place ANA_1065 in the Na_H_Exchanger family which is described as Sodium/hydrogen exchanger family.","","antiporter (nhe2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1066","1141278","1143617","2340","5.90","-8.73","83753","GTGACGATCACAGGCTTCCAGGACCCTGAAGACGCTGAGCGCTCTGAGTGCTCCGAGTGCCCCGATTTGCCCGGCTCGCCCGTGCGCGAGCGGGCCGAGGCCGTCCTGCGCGAGCTCGTGGGTCGCAGCGACGCGCGCCTGCGTGAGGACCAGTGGCGGGCGATCGAGGCGCTGGTCATCGCACGCCGCCGCGCGCTGGTGGTCCAGCGCACCGGGTGGGGCAAGTCGGCGGTGTACTTCGTGGCGACGGTCCTGCTGCGAGAGGGCTGGGGAGGCTGGTGCCCGGGCTCCCCTCTGCCCTCCCCCGGTGCTCGCTCCGGCGCCGGAGCGAGCTTCATCATCTCGCCGCTACTGGCGCTTATGCGTGACCAGGTCGCCGCTGCAAGCCGCGCCGGGATCCGGGCCGTGACCATGAACTCAGCCAATGTCACCCAGTGGAATGAGATTCAGGACCAGGTGAGCGCTGGTGAGGTCGATGTCCTGCTGGTTTCCCCGGAGCGCCTCAACAACCCGGTCTTCCGTGATGAGGTCCTCCCCCACCTGGCTGTGAGCGCCGCGCTTGTCGTCATCGACGAGGCCCACTGCATCTCGGACTGGGGACACGACTTCCGCCCTGACTACCGGCGCATCGGCACCCTGCTGGCCGGCCTGCCGCCGCGCACCCCGGTCCTGGCGACCACGGCGACTGCCAACTCCCGGGTCAGCACCGATGTCGCTGAGCAGCTGGGGGCGTCCCTGGAGGAAGCCGGGTCGGGCGGTGAGCAAGTCCTGGTGCTGCGGGGGACCCTGGAGCGTGGCTCTCTCCACCTGGGGGTCAGGATGCTGCCTGATACCGCCTCCCGCCTGGCCTGGCTGGCCGCCTACATCGGTGGCACTCCCGGCAGCGGCATCGTCTACTGCCTGACGGTCTCGGCGGCGATGGAGGTCGCCGAGCACCTGCGCACAGCCGGTGTGGAGGTGGCCGCCTACACGGGGCAGACCGACGCCACTGAGCGCGAGCGCCTGGAGGAGGACCTCAAGGCCAACCGGGTCAGGGCGCTGGTGGCCACCTCCGCTCTGGGCATGGGCTTCGACAAGCCGGACCTGGCCTTCGTGGTGCACGTGGGGGCCCCGTCCTCGCCGGTGAGCTACTACCAGCAGGTGGGTCGCGCCGGTCGTGGTGTGGAGCGGGCTGAGGTGGTCCTGCTGCCCGGCCCGGAGGACCGGGCCATCTGGGAGTGGTTCGGATCGCAGGGCTTTCCGCCTGAGGAGCAGGTTCGCTTGGTCCTGGACGCCTTGGAGGAGCGCAGGGCCGCGGGCGACGGGGCGGTGTCCACGGCGGTGCTGGAGACGGTGACCTCGTTGCGGCGCAGCCGGCTGGAGTCCATGCTCAAGGTCCTTGACGTCGACGGCGCCGTGCGCCGGGTTCGTGGCGGCTGGGAGTCCACTGGCCGCCCCTGGCGCTATGACGCCGAGCGTTATGCGCGAGTCGAGGCCGCGCGCCGCGCCGAGCAGGAGGCGATGCTCACCTATGAGCGTCTCGGTACTGAGCCCTCCCCATATCAGGGCTCATCCTCCTGCCGGATGGCCTTCTTAAGGTCGGTGCTCGATGACCCCCTGCTTGAGCCGGGATGGCGCTGCGGCGCCTGCGACCTGTGCGGGGGCCTGGACCTGCTTGACGCCCCCGACCGGGAACAGGTCGGTGCCGCTCGACAGACGCTGGGGCGCGCAGGGGTCGAGTTGCGGGCGCGCCGCCAGTGGCCCACCGGGATGGATCGGCTGGGCCTGGGCGACCTCAAGGGCCGCATCAGAGCCGACCGGCAGGCGGCGACCGGGTTGGCGGTGGGCAGGCTGGACGGATTGGGAACCTCGGTGGCGCTGCGCGAGCTGGCGGGCTCCGGCGCTGACGGCGAGGTCCCGGTGGCGATCAGGCCGCAGGTGCTTGCGGCGGTGGATCGGCTCGCTGAGCTCATCCGCGGTGAGCAGGAAGCCGCCGGGCAGGGCCGTCCGAGCAGGCCGCTGGCCGTCGTCGTCGTGGACTCCCGCACCCGCCCCCACATGGTTCGCCGGCTGGGGCACGCCGTAGCCGCACAGCTGGGAGCACAGCCCTTGGGCGTCGTGGGTCTGGGCAGTCAGGAGCCGCCGCAGCACGATGTGGGCTCTGCGTTTCGTCTGGCACAGGTGGCCCGCAGCCTGACGCTGCGGGGCTGGTCCGCCCAAACGCTCGACGAGCTGCGCGAGCGCGTCGTGGTCCTCGTGGACGACTGGAGTGACTCCGGCTGGACGCTCACACTGGCGGCCTCCCTCCTGCGCGAGGCGGGGGCGGAGGCGGTCCACCCCTTCGTCCTGGCACAGAAGTAG","VTITGFQDPEDAERSECSECPDLPGSPVRERAEAVLRELVGRSDARLREDQWRAIEALVIARRRALVVQRTGWGKSAVYFVATVLLREGWGGWCPGSPLPSPGARSGAGASFIISPLLALMRDQVAAASRAGIRAVTMNSANVTQWNEIQDQVSAGEVDVLLVSPERLNNPVFRDEVLPHLAVSAALVVIDEAHCISDWGHDFRPDYRRIGTLLAGLPPRTPVLATTATANSRVSTDVAEQLGASLEEAGSGGEQVLVLRGTLERGSLHLGVRMLPDTASRLAWLAAYIGGTPGSGIVYCLTVSAAMEVAEHLRTAGVEVAAYTGQTDATERERLEEDLKANRVRALVATSALGMGFDKPDLAFVVHVGAPSSPVSYYQQVGRAGRGVERAEVVLLPGPEDRAIWEWFGSQGFPPEEQVRLVLDALEERRAAGDGAVSTAVLETVTSLRRSRLESMLKVLDVDGAVRRVRGGWESTGRPWRYDAERYARVEAARRAEQEAMLTYERLGTEPSPYQGSSSCRMAFLRSVLDDPLLEPGWRCGACDLCGGLDLLDAPDREQVGAARQTLGRAGVELRARRQWPTGMDRLGLGDLKGRIRADRQAATGLAVGRLDGLGTSVALRELAGSGADGEVPVAIRPQVLAAVDRLAELIRGEQEAAGQGRPSRPLAVVVVDSRTRPHMVRRLGHAVAAQLGAQPLGVVGLGSQEPPQHDVGSAFRLAQVARSLTLRGWSAQTLDELRERVVVLVDDWSDSGWTLTLAASLLREAGAEAVHPFVLAQK$","ATP-dependent DNA helicase","Cytoplasm","Superfamily II DNA helicase","putative ATP-dependent DNA helicase ","ATP-dependent DNA helicase, RecQ family","","Schmid S.R., Linder P. D-E-A-D protein family of putative RNA helicases. Mol. Microbiol. 1992. 6(3):283-292. PMID: 1552844Linder P., Lasko P.F., Ashburner M., Leroy P., Nielsen P.J., Nishi K., Schnier J., Slonimski P.P. Birth of the D-E-A-D box. Nature 1989. 337(6203):121-122. PMID: 2563148Wassarman D.A., Steitz J.A. RNA splicing. Alive with DEAD proteins. Nature 1991. 349(6309):463-464. PMID: 1825133Harosh I., Deschavanne P. The RAD3 gene is a member of the DEAH family RNA helicase-like protein. Nucleic Acids Res. 1991. 19(22):6331-6331. PMID: 1956796Koonin E.V., Senkevich T.G. Vaccinia virus encodes four putative DNA and/or RNA helicases distantly related to each other. J. Gen. Virol. 1992. 73:989-993. PMID: 1321883Hodgman T.C. A new superfamily of replicative proteins. Nature 1988. 333(6168):22-23. PMID: 3362205","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[312-388]T$	Helicase_C
SM00490	$\"[307-388]T$	HELICc
PS51194	$\"[281-427]T$	HELICASE_CTER

InterPro
IPR002464
Domain

ATP-dependent helicase, DEAH-box
PS00690	$\"[186-195]?$	DEAH_ATP_HELICASE

InterPro
IPR004589
Family

ATP-dependent DNA helicase RecQ
PTHR13710	$\"[36-87]T$ $\"[108-424]T$ $\"[508-550]T$	DNA HELICASE RECQ FAMILY MEMBER
TIGR00614	$\"[34-510]T$	recQ_fam: ATP-dependent DNA helicase, RecQ

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[48-238]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[43-264]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[56-248]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[33-232]T$ $\"[263-408]T$	no description
PTHR13710:SF4	$\"[36-87]T$ $\"[108-424]T$ $\"[508-550]T$	ATP-DEPENDENT DNA HELICASE

","BeTs to 12 clades of COG0514COG name: Superfamily II DNA helicases, RecQ familyFunctional Class: LThe phylogenetic pattern of COG0514 is ----y--ceB-h-----l---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 48-101 are 82% similar to a (HELICASE DNA ATP-DEPENDENT ATP-BINDING HYDROLASE 3.6.1.- WITH II SUPERFAMILY ADJACENT) protein domain (PD788726) which is seen in Q82KF3_STRAW.Residues 67-159 are 65% similar to a (HELICASE HYDROLASE ATP-BINDING DNA ATP-DEPENDENT RECQ 3.6.1.- DNA-BINDING NUCLEAR PROBABLE) protein domain (PD209099) which is seen in Q6AR89_BBBBB.Residues 167-218 are 82% similar to a (HELICASE HYDROLASE ATP-BINDING DNA ATP-DEPENDENT RECQ 3.6.1.- DNA-BINDING NUCLEAR PROBABLE) protein domain (PD003883) which is seen in Q8FQZ9_COREF.Residues 219-260 are 85% similar to a (HELICASE HYDROLASE ATP-BINDING DNA ATP-DEPENDENT RECQ 3.6.1.- DNA-BINDING NUCLEAR PROBABLE) protein domain (PD533455) which is seen in Q82KF3_STRAW.Residues 308-377 are 78% similar to a (HELICASE ATP-BINDING HYDROLASE DNA ATP-DEPENDENT RNA EXCISION FACTOR B REPAIR) protein domain (PD000033) which is seen in O69992_STRCO.Residues 380-439 are similar to a (HELICASE HYDROLASE ATP-BINDING DNA ATP-DEPENDENT RECQ 3.6.1.- DNA-BINDING NUCLEAR PROBABLE) protein domain (PD215317) which is seen in O69992_STRCO.Residues 432-502 are 71% similar to a (HELICASE DNA ATP-DEPENDENT HYDROLASE ATP-BINDING 3.6.1.- PROBABLE SIMILAR WITH ADJACENT) protein domain (PD796255) which is seen in Q82KF3_STRAW.Residues 596-748 are 51% similar to a (HELICASE DNA ATP-DEPENDENT HYDROLASE ATP-BINDING 3.6.1.- PROBABLE SIMILAR WITH ADJACENT) protein domain (PD590765) which is seen in O69992_STRCO.","","-48% similar to PDB:1OYW Structure of the RecQ Catalytic Core (E_value = 2.8E_42);-48% similar to PDB:1OYY Structure of the RecQ Catalytic Core bound to ATP-gamma-S (E_value = 2.8E_42);-53% similar to PDB:1HV8 CRYSTAL STRUCTURE OF A DEAD BOX PROTEIN FROM THE HYPERTHERMOPHILE METHANOCOCCUS JANNASCHII (E_value = 1.2E_10);","Residues 67 to 257 (E_value = 1.8e-18) place ANA_1066 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 331 to 407 (E_value = 5e-23) place ANA_1066 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","II DNA helicase (recQ)","","1","","","Thu Aug 2 15:34:04 2007","","Thu Aug 2 15:34:04 2007","","","Thu Aug 2 15:34:04 2007","Thu Aug 2 15:34:04 2007","Thu Aug 2 15:34:04 2007","","","Thu Aug 2 15:34:04 2007","","","Thu Aug 2 15:34:04 2007","Thu Aug 2 15:34:04 2007","Thu Aug 2 15:34:04 2007","","Thu Aug 2 15:34:04 2007","Thu Aug 2 15:34:04 2007","","","","","yes","","" "ANA_1067","1144784","1143666","1119","5.12","-14.91","38836","ATGGCGGATCTACCGTCCTCCGGCGAGCACGATCTCCTGGAGCTGGCGGCCCGGACCCTTCACGGGCGGCAGGCCGAGCGCCTCGCGCAGGCCACCGCGAAGGGGTACAAGGGGGCTGACGAGGCGGTGAAGCTGCGGGCATCCGCCCAGCAGTCCCTGGATGCCTGCTCCAAGGCCCAGGCCTGGACCGAGCGGGGCCGCCTGGCGAACTCCGCCCTGGACTCGGCCGCAGGGGCCCAGCTCTCCCTGGACCGGGCACTGGCCGCTCAGGCGCCGCAGGACGCCGTCATCGGGGTGACCTTCACTCGGGTGCCCACGTCCGCGGAGGTCACCGCCGCGCTGGCCCCCAGTGGTCCCGGGGGCGGCAAGCGGAAGGTGTCGGCTCGTCTCGTGATCAGTGACCCCAATGACGCCGAGGAGATGGCCGGATGGCGCAGCACGGTGGAGGCCCTGCACGCGCAGGGCGGTCAGGCCCTGGCCCAGATCTGCGACTCCCACGACATGGTCGCCCTGACCGACTCCGCCTGGGACACCCGGGTCGCTACCCTGATCAAGGCGCTTCCCAATGTCGACGCCTGGGAGGTCGGCAACGAGATCGGCGGGGACTGGCTGGGCGCCGGGCCGGTGGCCAAGGTCCAGCGAGCGGCCAAGGCCGTGCGCGAGCGCACCAGTGCCACGACCGTGCTGACCCTGTACTACCAGCTCGGGCAGGCGGACCCGACGTACTCCCTGTTCAGCTATGCCGCCAGGGAGATCCCTGCGTCGATCAGGGAACTGATCGACGTCGTGGGACTGTCCGTCTACCCCCAGCTCCATCCGCTGGGAACAGCCGCTGACCGAGTCCTCAGTACTCTGGAGACCGCCTTCGCCTCCTCCCGGATCGCCGTGACCGAGCTCGGGTACGGGGGTGCAGACCTCAATACCGGTCCCTGGTGGTTCGGCTCGGCCTCCGACCCCGTGGCGGCCCGCACCGCCGTCGCTGAGCATGTCACCGGCGCAGCGTTGGGACGGTCCGACGCCTGGGGAGCCCCCTTCTGGTGGTACTACCTCGAGGACCAGATCGGAACCCCGGGGGGCCAGGTGGCTCCGGCGCTGGCCGCAGTGTCCACTGGCTTCTAG","MADLPSSGEHDLLELAARTLHGRQAERLAQATAKGYKGADEAVKLRASAQQSLDACSKAQAWTERGRLANSALDSAAGAQLSLDRALAAQAPQDAVIGVTFTRVPTSAEVTAALAPSGPGGGKRKVSARLVISDPNDAEEMAGWRSTVEALHAQGGQALAQICDSHDMVALTDSAWDTRVATLIKALPNVDAWEVGNEIGGDWLGAGPVAKVQRAAKAVRERTSATTVLTLYYQLGQADPTYSLFSYAAREIPASIRELIDVVGLSVYPQLHPLGTAADRVLSTLETAFASSRIAVTELGYGGADLNTGPWWFGSASDPVAARTAVAEHVTGAALGRSDAWGAPFWWYYLEDQIGTPGGQVAPALAAVSTGF$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","putative transmembrane protein","hypothetical protein","","Pervaiz S., Brew K. Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science 1985. 228(4697):335-337. PMID: 2580349Flower D.R., North A.C., Attwood T.K. Mouse oncogene protein 24p3 is a member of the lipocalin protein family. Biochem. Biophys. Res. Commun. 1991. 180(1):69-74. PMID: 1834059Flower D.R., North A.C., Attwood T.K. Structure and sequence relationships in the lipocalins and related proteins. Protein Sci. 1993. 2(5):753-761. PMID: 7684291Flower D.R. Multiple molecular recognition properties of the lipocalin protein family. J. Mol. Recognit. 1995. 8(3):185-195. PMID: 8573354","","","

InterPro
IPR002345
Domain

Lipocalin
PS00213	$\"[284-296]?$	LIPOCALIN

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 279-358 are 53% similar to a (TRANSMEMBRANE FN0230 PROBABLE PLASMID SMU.1153C) protein domain (PD690486) which is seen in Q8XSG3_RALSO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","Thu Aug 2 16:03:37 2007","","Thu Aug 2 16:03:37 2007","","","Thu Aug 2 16:03:37 2007","Thu Aug 2 16:03:37 2007","Thu Aug 2 16:03:37 2007","","","Thu Aug 2 16:03:37 2007","","","Thu Aug 2 16:03:37 2007","","Thu Aug 2 16:03:37 2007","","Thu Aug 2 16:03:37 2007","Thu Aug 2 16:03:37 2007","","","","","yes","","" "ANA_1068","1144800","1145183","384","7.60","1.56","13146","ATGACTGGTCGGCCACGACATGGTCAGAGTGCACTCGCGTCCGGTAGGCACATCAATGCCGATGACGCCGCCTTCGTCCTGGTAGAGGGGACCGACGGCGATGACCTCCAGGGTCTTGGCATCCAGGAGCGCGTCGTCATAGCCGACCTCGCCCTTGCCGTTGGACTGAATGCGTCGCAGCGCCTCGAGGTTGAGGGCGTTGCCCTGAGCATCACTGATGTGAAGGCTCAGGTGGGTGGTCGCCCCGTCCCCCATGGCCGGCGGAGTCACGTTCGCGTGCCCGCAGGAGGACACTGCCGCTCCCAGAACGCCAGTGCCCAGGAGCGCCAGCATCCTTCTGCGGTTGGTCTCACATGTCATGGGAGCAGTATTCCAGTCTTATGA","MTGRPRHGQSALASGRHINADDAAFVLVEGTDGDDLQGLGIQERVVIADLALAVGLNASQRLEVEGVALSITDVKAQVGGRPVPHGRRSHVRVPAGGHCRSQNASAQERQHPSAVGLTCHGSSIPVL$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1069","1147209","1145254","1956","5.07","-22.26","69888","ATGAGTCTCCCAACCCTTGCGTCCTCACGACGCCGCCGCTGTGCGCTGGCCGCCATCGCGGTGTGCCTGGGCAGCTCCATCACCGCCGTCGGCCCTGCTCAGGCCGCACCCGCCCCCGACGCGCAGCCTCCGATCGCTGCCCAGGCCGCCGCGGTCAACCCGGCCGGCGGTGCCCAGGCCAATGACGCCGACCCGGCCAAGAAGCCGCTTCCGGCTCCGCCCGAGCCCGCCGCCGCGGCCAAGAAGGAGCTCCCCCTCAAGGGAGACAAGCAGGCCGACGTGGATCTCAACAAGCCCGCCCCCGCCGCCGGTCAGGTCAAGATCCGTGACCTGAAGCAGAACGCCCCCGAGGTTCCTGCCGGTGCGGTGACCTTCTCCAACCAGGAGGCGGGACCGGCATCGACCCTGGTCCTGTTCGACACCACGGGTGACTACGCCAAGCTGGGGGAGTACTACGCCCTGAGCATGGGCACCCTTGCCAGCCACTCCGGGACCGTGACGACCCTCCCGGTCAAGGACTACGTCGCCGGCCTGGCCGGTCGCTTCACCAACGTGGTCTACATCGGCTCCACCTACGACGAGCCCCTGCCGCGGGCCTTCATCGACGATGCCCTGACCGGCAACATCCCCGTCATGTGGTCCGGCTTCAACATCTGGCAGCTGGCCAAGACCGACGCCGACCGCGCCGCCTTCACCCAGCGCTACGGCTGGGACGCGGCCACCTCCTACATTGATTCCGCCGACCGGGTCACCAAGATCAGCTACAACGGCGCCTCCTTGAAGCGCAACGAGCTCAACTCCGGTGGCATCATCGCTCCGCACATCACCCGCGAGAAGGACGTCAAGGTCCTGGGGCGTGCTGAGTGCTCCAAGCCCGACGGTGCGGCCACCGCGTGCGCCTCCGTCGCACAGTCCGGCACTACCTCCTTCCCCTGGGCGGTCAGCTCCTCGGGAATGACCTTCATCGGTGAGATTCCGCTGACCTACCTGGGTGAGCAGGACCGGTACATCGCGGCTGCCGACATCCTCCTGGACTTCCTCCAGCCCGGTGCCCAGCAGTTCCGTCAGGCCGCTGTGCGTCTGGAGGACGTGACCCCGGACAGCGACCCCGAGGAGCTGCAGGCGATCGTCGACTACCTCCACAGTCAGAACGTGCCCTTCCAGATGGCGGTGGTGCCCAAGTACATCGACCCCAAGGGCACTGAGAACAACGGGACACCCAAGGAGCTCACTCTGGAGGACGCCCCGGAGCTGGTGGAAGTCCTGCAGGATGCGGTGAACAAGGGCGGAACGATCGTTCAGCACGGCACCACCCACCAGTTCGGGACCCTGGACAACCCCTACAACGCCGTCTCCGCCGACGACTTCGAGTTCATCCGCTCGTGGTGCTCGGCCACCAACGACACCAAGGCCCCACCCATCGACTGCCAGGACAAGTCCTTCGTGCAGATCGGAGGCACCCTGCCGGGCACCTCCCAGGAATGGGCTTCCGAGCGCGTGGATCAGGGACGCCAGATCTTCGGGGCGGTCGACCTGCCGACTCCAGAGATCTTCGAGACTCCGCACTACTCGGCCACCCGTGAGGCCTACTACGGCATCGGGGAGCACTACTCGGTGCGTTACGAGCGTGAGCTCCTCTATGCCGGCACCCTGACCAACACCCAGGCCGGCCCCCATGACTACTACGGGCAGTTCTTCCCCTACGCGGTCAACGACCCCTACGGGACCCACGTCCTGCCTGAGAACCTGGGCAACTTCGAGCCCAACGAGATCAACCAGCACCCGCCGCGCCTGGCTCAGGAGGTCATCGACGCGGCCAAGCTCAACCTGGTCAACACTCACGCCACCGCCAGCTTCTTCTTCCACCCCTACTACCCGCTGCCCGAGCTGAAGAAGATCGTCGCCGGCATCAAGGCCGAGGGGTACACCTTCGTGCCGGCCTCGGAGCTGAAATGA","MSLPTLASSRRRRCALAAIAVCLGSSITAVGPAQAAPAPDAQPPIAAQAAAVNPAGGAQANDADPAKKPLPAPPEPAAAAKKELPLKGDKQADVDLNKPAPAAGQVKIRDLKQNAPEVPAGAVTFSNQEAGPASTLVLFDTTGDYAKLGEYYALSMGTLASHSGTVTTLPVKDYVAGLAGRFTNVVYIGSTYDEPLPRAFIDDALTGNIPVMWSGFNIWQLAKTDADRAAFTQRYGWDAATSYIDSADRVTKISYNGASLKRNELNSGGIIAPHITREKDVKVLGRAECSKPDGAATACASVAQSGTTSFPWAVSSSGMTFIGEIPLTYLGEQDRYIAAADILLDFLQPGAQQFRQAAVRLEDVTPDSDPEELQAIVDYLHSQNVPFQMAVVPKYIDPKGTENNGTPKELTLEDAPELVEVLQDAVNKGGTIVQHGTTHQFGTLDNPYNAVSADDFEFIRSWCSATNDTKAPPIDCQDKSFVQIGGTLPGTSQEWASERVDQGRQIFGAVDLPTPEIFETPHYSATREAYYGIGEHYSVRYERELLYAGTLTNTQAGPHDYYGQFFPYAVNDPYGTHVLPENLGNFEPNEINQHPPRLAQEVIDAAKLNLVNTHATASFFFHPYYPLPELKKIVAGIKAEGYTFVPASELK$","Hypothetical protein","Extracellular, Periplasm, Cytoplasm","HYPOTHETICAL TRANSMEMBRANE PROTEIN, putative","hypothetical protein","Uncharacterized protein-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 136-236 are 54% similar to a (TRANSMEMBRANE PRECURSOR PLASMID SIGNAL) protein domain (PD907491) which is seen in Q8XSG4_RALSO.Residues 357-526 are 51% similar to a (YDAL TRANSMEMBRANE CPE1529 CPE0658 PLASMID) protein domain (PD043496) which is seen in Q8XSG4_RALSO.Residues 541-651 are 55% similar to a (TRANSMEMBRANE PLASMID) protein domain (PD574654) which is seen in Q8XSG4_RALSO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","TRANSMEMBRANE PROTEIN, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1070","1148408","1147206","1203","5.41","-13.27","43509","ATGACAACCGACTCCACGCAAACGGGCCGCCCCCTGAGGGTCATGCTCGTCTACGGCACCCGCCCGGAGGCGATCAAGCTCGCCCCCCTGGTGGCCGCCATGCGCGACGACGAGCGTTTCAATCCGATCGTCGTCGTCACCGGACAGCACCGTGAGATGCTCGACCAGGTGCACGAGTTCTTCGGCATCGTGCCCGACGATGACCTCGACATCCACTCACCGGGACAGACCCTCACCCAGATCACCAACCGCTGCCTGCAAGGGGTGGGGCGGGCCATTGAGGCCCACCGGCCCGACGCCGTCGTCGTCCAGGGGGACACCACCTCCGCCTTCGCCGCTGCGCTGGCGGCTTTCTACCACGAGGTACCCGTCCTCCACGTCGAGGCCGGTCTGCGCACCGGGGACATCTCCTCGCCCTTCCCCGAGGAGGCCAACCGGCGGCTCATCAGCCAGGTGACCACCCTGCACCTGTGCCCCACCACCACCAGTCGGGACAACCTGCTGCGCGAGAACACCGACCCGCAGACCGTCAGTGTCACGGGCAACACGGTCATCGACGCGCTCCTGGTCGCCGTGGACCGTCGGGTCCCGCCACCGGATGAGGAGCTGGCCGCAGCACTGAAGGACGCCTCTCGGCGAGTCGTGCTCGTCACCGCCCACCGCCGTGAGTCCTGGGGCGAGCCGATGCGGGCCATCGGCCGCGCCGTCGCGCGCCTGGCCGGCAAGCACCCCGAGGTGCTCTTCGTGCTGCCGGTTCACCGCAACCCCAAGGTTCGCCAGGACCTCCTGCCGCAGATCGAGGGCCACGCCAACGTCATCTGGTGCGACCCGCTGGAGTACGGCGCCTTCTGCGCACTCATCGACCGCTGCGACGTCGTGCTCACCGACTCCGGCGGCGTCCAGGAGGAGGCCCCCGCGCTGTCCAAGCCCGTCCTGGTCATGAGGGACAACACCGAGCGTCCTGAGGCGGTCGCCTTCGGGGTTGCCGAGCTGGTCGGAACCGACGAGGAGCGCATCGTCGAGAGGGTCTCCACGCTGCTGACCGACGAGGCGGCCTACACGACCATGGCCCAGGCCGCAAACCCCTACGGCGACGGACACGCGAGCAAGCGCATCCTGGCCGCCACCGCCGCCCTGTTCGGCCGCGGTGTTCCCCTTCCCGAGTTTGAACCCGTTCCCACCTCATCGAAGGAGTGTTCATGA","MTTDSTQTGRPLRVMLVYGTRPEAIKLAPLVAAMRDDERFNPIVVVTGQHREMLDQVHEFFGIVPDDDLDIHSPGQTLTQITNRCLQGVGRAIEAHRPDAVVVQGDTTSAFAAALAAFYHEVPVLHVEAGLRTGDISSPFPEEANRRLISQVTTLHLCPTTTSRDNLLRENTDPQTVSVTGNTVIDALLVAVDRRVPPPDEELAAALKDASRRVVLVTAHRRESWGEPMRAIGRAVARLAGKHPEVLFVLPVHRNPKVRQDLLPQIEGHANVIWCDPLEYGAFCALIDRCDVVLTDSGGVQEEAPALSKPVLVMRDNTERPEAVAFGVAELVGTDEERIVERVSTLLTDEAAYTTMAQAANPYGDGHASKRILAATAALFGRGVPLPEFEPVPTSSKECS$","UDP-N-acetylglucosamine 2-epimerase","Cytoplasm","UDP-N-acetylglucosamine 2-epimerase","UDP-N-acetylglucosamine 2-epimerase ","UDP-N-acetylglucosamine 2-epimerase","","Swartley J.S., Liu L.J., Miller Y.K., Martin L.E., Edupuganti S., Stephens D.S. Characterization of the gene cassette required for biosynthesis of the (alpha1-->6)-linked N-acetyl-D-mannosamine-1-phosphate capsule of serogroup A Neisseria meningitidis. J. Bacteriol. 1998. 180(6):1533-1539. PMID: 9515923Kiser K.B., Lee J.C. Staphylococcus aureus cap5O and cap5P genes functionally complement mutations affecting enterobacterial common-antigen biosynthesis in Escherichia coli. J. Bacteriol. 1998. 180(2):403-406. PMID: 9440531Stasche R., Hinderlich S., Weise C., Effertz K., Lucka L., Moormann P., Reutter W. A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase. J. Biol. Chem. 1997. 272(39):24319-24324. PMID: 9305888","","","

InterPro
IPR003331
Family

UDP-N-acetylglucosamine 2-epimerase
PTHR18964:SF2	$\"[38-375]T$	UDP-N-ACETYLGLUCOSAMINE-2-EPIMERASE
PF02350	$\"[32-377]T$	Epimerase_2
TIGR00236	$\"[12-380]T$	wecB: UDP-N-acetylglucosamine 2-epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2000	$\"[9-238]T$	no description
PTHR18964	$\"[38-375]T$	ROK FAMILY

","BeTs to 15 clades of COG0381COG name: UDP-N-acetylglucosamine 2-epimeraseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0381 is -om-k---vd-lbcefghsnu-x---Number of proteins in this genome belonging to this COG is 1","***** IPB003331 (UDP-N-acetylglucosamine 2-epimerase) with a combined E-value of 8.3e-84. IPB003331A 13-50 IPB003331B 104-150 IPB003331C 211-226 IPB003331D 293-327 IPB003331E 353-366","Residues 20-375 are 67% similar to a (2-EPIMERASE UDP-N-ACETYLGLUCOSAMINE ISOMERASE SYNTHESIS ENZYME POLYSACCHARIDE CAPSULAR EPIMERASE BIOSYNTHESIS UDP-GLCNAC) protein domain (PD004092) which is seen in Q8XSG6_RALSO.","","-65% similar to PDB:1F6D THE STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE FROM E. COLI. (E_value = 8.8E_97);-65% similar to PDB:1VGV Crystal structure of UDP-N-acetylglucosamine_2 epimerase (E_value = 8.8E_97);-61% similar to PDB:1O6C Crystal structure of UDP-N-acetylglucosamine 2-epimerase (E_value = 5.0E_84);-57% similar to PDB:1V4V Crystal Structure Of UDP-N-Acetylglucosamine 2-Epimerase From Thermus Thermophilus HB8 (E_value = 7.5E_72);","Residues 32 to 377 (E_value = 1.3e-147) place ANA_1070 in the Epimerase_2 family which is described as UDP-N-acetylglucosamine 2-epimerase.","","2-epimerase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1071","1149210","1148494","717","4.83","-12.74","25761","ATGACAGCTGCCAACGCACCTCAGCACGCAGGAGCCGTCGACGGATCGCGTCGCGGCAGAATCCTGCGTCGCGCCCTTCTGACGGTCTGCGTCTTGGCACTGGTTCTAGGAGTCACCGTGTACTGCCACGCCCGAGAGGCAACAGAGACCCCGGACTGCTCCCAGTGGGAGATCATCTTCGACGGTTACGGCGAGGCCTCGTGCTCTGAGGGCCTGCTGCGCCTCAAGCCGACGTCGGCCAACTCCTCGGACACGACCCACGCCGGTCTGGCCACCTCCACCACGGTCGAGATCGAAGCGGGAGGCGTGCAGACCATCCACACCACGATGACCACTGTCAAGCAGCTGCGAGAGGACGGCGAGCCCAACGCGTGGGAGGTCGCCTGGCTCCTGTGGAACTACACCGACAACAACCACTTCTACGCCCTGGCTCTCAAGCCCAACGGATGGGAGGTCTCCAAGCAGGACACCGCCTACCCGGGGTACCAGCGATTCCTGTCATCGGGCAACACGCCCGTCTACCCACCCGGTGAGAGCCATGACGTCACCGTCACCATTGATACCACCTCATCGTCAGAGGCCACCTTCACCATCACCGTGGACGGGCAGGAGCTCGGAACCGTCACCGACAAGCAGTCCCCCTACCGCTCCGGCACCGTGGCGGCCTACTGCGAGGACTCCGACGTCACCTTCACCCCGATCACCGAGGACAAGTAG","MTAANAPQHAGAVDGSRRGRILRRALLTVCVLALVLGVTVYCHAREATETPDCSQWEIIFDGYGEASCSEGLLRLKPTSANSSDTTHAGLATSTTVEIEAGGVQTIHTTMTTVKQLREDGEPNAWEVAWLLWNYTDNNHFYALALKPNGWEVSKQDTAYPGYQRFLSSGNTPVYPPGESHDVTVTIDTTSSSEATFTITVDGQELGTVTDKQSPYRSGTVAAYCEDSDVTFTPITEDK$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[35-212]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[33-235]T$	no description
PTHR22913	$\"[17-78]T$	HYALURONAN SYNTHASE
PTHR22913:SF1	$\"[17-78]T$	gb def: Putative glycosyltransferase
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[289-323]?$ $\"[329-349]?$ $\"[364-382]?$	transmembrane_regions

","BeTs to 5 clades of COG1215COG name: Glycosyltransferases, probably involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1215 is a-mpk-yq---lbcef-----j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 7-140 are 50% similar to a (TRANSFERASE N-ACETYL-GLUCOSAMINE GLYCOSYLTRANSFERASE) protein domain (PD796993) which is seen in Q6ACT7_BBBBB.Residues 147-262 are similar to a (TRANSFERASE SYNTHASE GLYCOSYLTRANSFERASE CHITIN TRANSMEMBRANE CELLULOSE WALL CELL FAMILY MULTIGENE) protein domain (PD007872) which is seen in Q6AEH8_BBBBB.Residues 173-282 are 49% similar to a (TRANSFERASE GLYCOSYL) protein domain (PD390372) which is seen in Q9CG45_LACLA.","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 212 (E_value = 2.8e-14) place ANA_1073 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","N-acetyl-glucosamine transferase (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1074","1151173","1150778","396","11.78","12.82","14351","GTGCGCCGTGCCCGACGGGCTGAGTTCCCACATCCCGTCATCCCCGGGCGCGCCGCACCGAGGCGTTGGTGCCGACTGGAGTTGCTCGCACGTGCGGTGTTGACGGTCGGTGCCGGCCCTACCCCTTGGATCCAGATGGATGGCCTCATGCACTACTCCCCATTCGCCGCCGGAACCGGACTGTTCGTCGTGTGGTATGTAGCCCCGGCAGGTTCCCTTCCCGCTCTCGTCGCCCGTTTCCTCATTGACTGCGCCGGCCTGGTGTTTGTCGCCATCCTGGCCTTCTTCCTGCTGACCAATCTGTACGGCGCGGTCCGTGCCCTGCTCCCGCACCCCAGGCGCAGCGCCGGGCGTCACGTCCAGCAGCGCAGCGGTCTGATGAGTCTGCGAGCGTGA","VRRARRAEFPHPVIPGRAAPRRWCRLELLARAVLTVGAGPTPWIQMDGLMHYSPFAAGTGLFVVWYVAPAGSLPALVARFLIDCAGLVFVAILAFFLLTNLYGAVRALLPHPRRSAGRHVQQRSGLMSLRA$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[56-74]?$ $\"[80-98]?$	transmembrane_regions

InterPro
IPR001692
Domain

Histidinol dehydrogenase
PD002680	$\"[13-444]T$	HISX_MYCTU_O08396;
PR00083	$\"[35-59]T$ $\"[136-162]T$ $\"[246-267]T$ $\"[268-287]T$ $\"[338-363]T$ $\"[379-397]T$	HOLDHDRGNASE
PF00815	$\"[17-446]T$	Histidinol_dh
TIGR00069	$\"[9-450]T$	hisD: histidinol dehydrogenase
PS00611	$\"[246-278]T$	HISOL_DEHYDROGENASE

InterPro
IPR012131
Family

Histidinol dehydrogenase, prokaryotic
PIRSF000099	$\"[1-448]T$	Histidinol dehydrogenase
PTHR21256:SF2	$\"[33-445]T$	HISTIDINOL DEHYDROGENASE (HDH)

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1980	$\"[252-415]T$	no description
PTHR21256	$\"[33-445]T$	HISTIDINOL DEHYDROGENASE (HDH)

","BeTs to 18 clades of COG0141COG name: Histidinol dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0141 is aom---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001692 (Histidinol dehydrogenase) with a combined E-value of 2e-139. IPB001692A 35-60 IPB001692B 79-101 IPB001692C 122-162 IPB001692D 172-223 IPB001692E 246-287 IPB001692F 325-346 IPB001692G 362-406 IPB001692H 428-444","Residues 1-83 are 60% similar to a (ZINC HISTIDINOL METAL-BINDING NAD HISTIDINE OXIDOREDUCTASE HDH DEHYDROGENASE BIOSYNTHESIS) protein domain (PDA1A286) which is seen in HISX_CORDI.Residues 6-200 are 69% similar to a (ZINC HISTIDINOL METAL-BINDING NAD HISTIDINE OXIDOREDUCTASE HDH DEHYDROGENASE BIOSYNTHESIS) protein domain (PDA18679) which is seen in HISX_MYCPA.Residues 10-437 are 49% similar to a (ZINC HISTIDINOL METAL-BINDING NAD HISTIDINE PLASMID OXIDOREDUCTASE HDH DEHYDROGENASE BIOSYNTHESIS) protein domain (PD728476) which is seen in HIX2_RHIME.Residues 13-444 are 70% similar to a (HISTIDINOL DEHYDROGENASE OXIDOREDUCTASE HISTIDINE BIOSYNTHESIS NAD HDH ZINC METAL-BINDING SEQUENCING) protein domain (PD002680) which is seen in HISX_MYCTU.Residues 14-444 are 55% similar to a (ZINC HISTIDINOL METAL-BINDING NAD HISTIDINE OXIDOREDUCTASE HDH DEHYDROGENASE BIOSYNTHESIS) protein domain (PD725548) which is seen in HISX_RALSO.Residues 23-449 are 57% similar to a (ZINC HISTIDINOL METAL-BINDING NAD HISTIDINE OXIDOREDUCTASE HDH DEHYDROGENASE BIOSYNTHESIS) protein domain (PDA190T9) which is seen in HISX_PROMA.Residues 32-444 are 54% similar to a (ZINC HISTIDINOL METAL-BINDING NAD HISTIDINE OXIDOREDUCTASE HDH DEHYDROGENASE BIOSYNTHESIS) protein domain (PD724193) which is seen in HISX_NITEU.","","-54% similar to PDB:1K75 The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication. (E_value = 1.5E_68);-54% similar to PDB:1KAE L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINOL (SUBSTRATE), ZINC AND NAD (COFACTOR) (E_value = 1.5E_68);-54% similar to PDB:1KAH L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINE (PRODUCT), ZN AND NAD (COFACTOR) (E_value = 1.5E_68);-54% similar to PDB:1KAR L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH HISTAMINE (INHIBITOR), ZINC AND NAD (COFACTOR) (E_value = 1.5E_68);","Residues 17 to 446 (E_value = 1.1e-190) place ANA_1075 in the Histidinol_dh family which is described as Histidinol dehydrogenase.","","dehydrogenase (hisD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1076","1155228","1152841","2388","4.98","-36.11","86110","ATGAGCGCCACCCCTGAGTCGGTCGCCGCCACCTCACCGGCTGAGATCGCCGTGACCGAGTCACAGGTCCCCTCCGCACCCCTGCCGGGGGCCACCATTCTGGGATACCCCCGCATCGGAAGGGACCGTGAGCTCAAGCGCGCCGTCGAGTCCTTCTGGAAGGGGAACCTGAGCGTCGACGAGCTCAAGCACGCCGCAGCCGAACTGCGCGGGGCGACTCGTTCGCGTCTGATGGACCTGGGGCTGACTCAGCCCGCATCGGTTCCAGCGGACTTCACTCTTTACGACCAGGTACTTCAGGTGACCGCCACCCTGGGGGCCGCGCCGGCCCGCTTCCGTGACCTGCTCAATGCCGATGGTGCTCTCGACGTCGAGGGCTATTTCACGCTGGCCCGCGGTGAGGGCGCCCGTCCGGCCATGGAGATGACCAAGTGGCTGGACTCCAACTACCACTACCTGGTCCCCGAGATCGACGCCTCCACCCCCTTCGACTACGTCGACACCGCCATCGCCGACCAGGTCCGCGAGGCCCAGGCCGCTGGTACCGAGGTGCGCCCCGTCGTCGTAGGACCGGTGAGCTACCTGCTCATGGCCAAGCCCTCCGACGAGGCTGCCGAGGGCTTCCATCCTCTGGACCGTCTTAATGACGTCCTGCACGCCTACGGCCACCTCCTCATGGACCTGCGCGAGGCCGGTGCCACCTGGGTCCAGCTCGACGAGCCCGCCCTGGTCTCCGACTCCTGGAACGTGGAGCGCCAGCGTGTCCTCGATGCCGTGCGCGACGCCTACACCTGGTTGGGCGCCATCGTGGAGCGCCCCCAGATCCTGGTGGCCGGAACCTACGGCTCCCTGGGTGACGCCCTGCCCGTGCTCGCTCAGGCCCCGATCGAGGCCGTGGGCCTCGACCTCGTGGCCGGCGCCCTGCCCGAGGCCGGCGACCTGGCCGCCCTGAAGGGCAAGGCCGTTGTTGCCGGGGTTGTCTCAGGACGCAACATCTGGCGCACCGACCTGAACCGAGCCATGGACGTGCTTGAGCAGCTGCGCGAGCGCCTCCCCGAGGGCACCCCCATCACCGTGGCGACCTCCACCTCCTTGCAGCACGTGCCCCACGACGTCGAGCGCGAGACCGCCATCGACCCGGAGATCCGCTCCTGGCTGGCCTTCGCCGATCAGAAGGTCGGGGAGGTCATCACCCTGGCCAAGGGCCTGGAGCAGGGCCGTGAGGCCATCGCCGCAGAGCTGTCCCAGGACGCCGACCTGCGCAAGCAGCGCGCCGCCCACCCCGGCGTGCACCGCGACGAGGTCCGCACCGCCGTCGGCGCCGTCACGGACGCCGACCGCACCCGCGCCCCCTACAGTGAGCGCAAGGCGGCCCAGGACGAGCGCCTCGGCCTGCCCGAACTGCCCACCACCACCATCGGCTCCTTCCCGCAGACCGCTGAGATCCGTAAGGCCCGCGCCGCCTGGCGCAAGGGCGAGATCGACGACGCCGCCTACGACGCCGCCATGCGCGCCGAGATCGCCAGCGTCGTCGCCCTTCAGGAACGCCTCGGCCTGGACGTCCTGGTTCACGGCGAGGCCGAGCGCAACGACATGGTCCAGTACTTCGCCGAGCTGCTCGACGGCTTCGTCACCACCGAGCACGGCTGGGTCCAGTCCTACGGCTCGCGCTGCACCCGTCCCTCCATCCTGTGGGGAGACGTCACTCGTCCCGAGCCGATGACGGTCACCTGGTCGGCCTATGCCCAGTCCTTGACCGACAAGCCCCTCAAGGGCATGCTCACTGGCCCGGTGACGATCATGGCCTGGTCCTTCGTGCGCGACGACATCCCGCGCGCCCAGGTCGCCGACCAGCTGGGTCTGGCCCTGCGCGCGGAGGTGGCGGACCTTGAGGCCGCCGGTATCGGCGTCATCCAGGTCGACGAGCCTGCCATCCGCGAGACCCTGCCGCTGCGGCGCGCCGACCGCCCCACCTACCTGGAGTGGTCCGTCGGCTCCTTCCGTCTGGCTACCGGAGGAGCGGCTCCCGCCACCCAGATCCACACCCACCTGTGCTACTCGGAGTTCGACGTCGTCATCGACGCGGTTGACCACCTCGACGCCGACGTGACCTCCATCGAGGCTTCCCGCTCGCGCATGGACATCCTGCCCGCAGTGGCAGAGCACGGCTTCGAGCGCCAGCTCGGCCCGGGCGTATGGGACATCCACTCCCCGCGCGTGCCCAGCCAGGCCGAGTGCACCGAGCTGCTCCAGCGGGCCGTCGATGCCCTGGGCGCCGAGAAGGTCTGGGTCAACCCCGACTGCGGTCTCAAGACCCGCGGCTACGCCGAGACCGAGGCGAGCCTGACCAGCCTGGTCGGTGCCGCCCGTGCGGTGCGTGAGGCCTGA","MSATPESVAATSPAEIAVTESQVPSAPLPGATILGYPRIGRDRELKRAVESFWKGNLSVDELKHAAAELRGATRSRLMDLGLTQPASVPADFTLYDQVLQVTATLGAAPARFRDLLNADGALDVEGYFTLARGEGARPAMEMTKWLDSNYHYLVPEIDASTPFDYVDTAIADQVREAQAAGTEVRPVVVGPVSYLLMAKPSDEAAEGFHPLDRLNDVLHAYGHLLMDLREAGATWVQLDEPALVSDSWNVERQRVLDAVRDAYTWLGAIVERPQILVAGTYGSLGDALPVLAQAPIEAVGLDLVAGALPEAGDLAALKGKAVVAGVVSGRNIWRTDLNRAMDVLEQLRERLPEGTPITVATSTSLQHVPHDVERETAIDPEIRSWLAFADQKVGEVITLAKGLEQGREAIAAELSQDADLRKQRAAHPGVHRDEVRTAVGAVTDADRTRAPYSERKAAQDERLGLPELPTTTIGSFPQTAEIRKARAAWRKGEIDDAAYDAAMRAEIASVVALQERLGLDVLVHGEAERNDMVQYFAELLDGFVTTEHGWVQSYGSRCTRPSILWGDVTRPEPMTVTWSAYAQSLTDKPLKGMLTGPVTIMAWSFVRDDIPRAQVADQLGLALRAEVADLEAAGIGVIQVDEPAIRETLPLRRADRPTYLEWSVGSFRLATGGAAPATQIHTHLCYSEFDVVIDAVDHLDADVTSIEASRSRMDILPAVAEHGFERQLGPGVWDIHSPRVPSQAECTELLQRAVDALGAEKVWVNPDCGLKTRGYAETEASLTSLVGAARAVREA$","5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase","Cytoplasm","5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase","5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase ","5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase","","Ravanel S., Gakiere B., Job D., Douce R. The specific features of methionine biosynthesis and metabolism in plants. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(13):7805-7812. PMID: 9636232","","","

InterPro
IPR002629
Domain

Methionine synthase, vitamin-B12 independent
PD004692	$\"[692-786]T$	Q9KHC5_BBBBB_Q9KHC5;
PF01717	$\"[468-791]T$	Meth_synt_2

InterPro
IPR006276
Family

5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
TIGR01371	$\"[34-795]T$	met_syn_B12ind: 5-methyltetrahydropteroyltr

InterPro
IPR013215
Domain

Cobalamin (vitamin B12)-independent methionine synthase MetE, N-terminal
PF08267	$\"[30-352]T$	Meth_synt_1

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.210	$\"[43-403]T$ $\"[462-793]T$	no description

","BeTs to 17 clades of COG0620COG name: Methionine synthase II (cobalamin-independent)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0620 is a-mpkzyqv-rlb-efghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB002629 (Methionine synthase, vitamin-B12 independent) with a combined E-value of 4.5e-251. IPB002629A 35-49 IPB002629B 141-153 IPB002629C 186-199 IPB002629D 217-247 IPB002629E 324-337 IPB002629F 362-375 IPB002629G 463-498 IPB002629H 514-558 IPB002629I 570-618 IPB002629J 619-662 IPB002629K 678-711 IPB002629L 728-741 IPB002629M 762-793 IPB002629D 619-649***** IPB013215 (Cobalamin-independent synthase MetE, N-terminal) with a combined E-value of 2.7e-50. IPB013215A 468-478 IPB013215B 518-543 IPB013215C 618-652 IPB013215C 216-250***** IPB011254 (Prismane-like) with a combined E-value of 4.6e-31. IPB011254A 468-479 IPB011254B 481-499 IPB011254C 523-535 IPB011254D 545-562 IPB011254E 590-599","Residues 31-99 are 59% similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE COBALAMIN-INDEPENDENT ISOZYME INDEPENDENT SYNTHASE VITAMIN-B12 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE BIOSYNTHESIS) protein domain (PD886733) which is seen in METE_PSEAE.Residues 127-161 are 82% similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE ISOZYME COBALAMIN-INDEPENDENT 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE INDEPENDENT SYNTHASE VITAMIN-B12 BIOSYNTHESIS) protein domain (PD006455) which is seen in METE_ALCEU.Residues 173-382 are 60% similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE ISOZYME COBALAMIN-INDEPENDENT 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE INDEPENDENT SYNTHASE VITAMIN-B12 BIOSYNTHESIS) protein domain (PD186546) which is seen in METE_STRCO.Residues 380-426 are 72% similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE ISOZYME COBALAMIN-INDEPENDENT 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE INDEPENDENT SYNTHASE VITAMIN-B12 BIOSYNTHESIS) protein domain (PDA1D876) which is seen in METE_CHRVO.Residues 382-476 are 53% similar to a (METHYLTRANSFERASE TRANSFERASE METHIONINE SYNTHASE 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE) protein domain (PD712692) which is seen in Q83HG9_TROW8.Residues 430-499 are 71% similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE ISOZYME COBALAMIN-INDEPENDENT 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE INDEPENDENT SYNTHASE VITAMIN-B12 BIOSYNTHESIS) protein domain (PD041263) which is seen in METE_CAUCR.Residues 468-651 are 43% similar to a (TRUNCATED METHYLTRANSFERASE SYNTHASE-LIKE ZINC METHIONINE TRANSFERASE) protein domain (PD841318) which is seen in Q8GMI7_STRGL.Residues 503-555 are 83% similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE ISOZYME COBALAMIN-INDEPENDENT 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE INDEPENDENT SYNTHASE VITAMIN-B12 BIOSYNTHESIS) protein domain (PDA0I073) which is seen in METE_RALSO.Residues 546-689 are similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE COBALAMIN-INDEPENDENT ISOZYME 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE INDEPENDENT BIOSYNTHESIS SYNTHASE VITAMIN-B12) protein domain (PD191524) which is seen in METE_ALCEU.Residues 692-786 are 76% similar to a (METHIONINE METHYLTRANSFERASE SYNTHASE COBALAMIN-INDEPENDENT ISOZYME 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE BIOSYNTHESIS INDEPENDENT SYNTHASE VITAMIN-B12) protein domain (PD004692) which is seen in Q9KHC5_BBBBB.","","-61% similar to PDB:1U1H A. thaliana cobalamine independent methionine synthase (E_value = 5.2E_174);-61% similar to PDB:1U1J A. thaliana cobalamine independent methionine synthase (E_value = 5.2E_174);-61% similar to PDB:1U1U A. thaliana cobalamine independent methionine synthase (E_value = 5.2E_174);-61% similar to PDB:1U22 A. thaliana cobalamine independent methionine synthase (E_value = 5.2E_174);-59% similar to PDB:2NQ5 Crystal structure of methyltransferase from Streptococcus mutans (E_value = 9.2E_155);","Residues 30 to 352 (E_value = 4.6e-116) place ANA_1076 in the Meth_synt_1 family which is described as Cobalamin-independent synthase, N-terminal domain.Residues 468 to 791 (E_value = 2.6e-185) place ANA_1076 in the Meth_synt_2 family which is described as Cobalamin-independent synthase, Catalytic domain.","","S-methyltransferase (metE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1078","1156436","1155225","1212","8.20","4.28","42415","GTGCACGACAACGAGCCCACCGGGCCGACCGCCGCGGCAGGAAGCCGCGCAGCGGGTCTGAGCAGCGCCGAGACCGGAAGTGCCCGGCGACTGCCCACCGTCAGCCTGGAGCTGTTCCCGCCTCGGCCGGGTAAGGCGGCCTCTGCCACCTGGGGTCGCATTGACAGGCTCCTGGCCACAGGGCCCGACTTCGTCTCGGTGACCTACCGGCCCACCTTCGTCACCGATCCCGCCGGCGGCATTAACGGCGGTGAGTATGAAGGGAGTGTGCGAGGGACGGAGGTGAGTCGGTGCAAGGCCGTGCCCTGCGTGCGCGCGGTTCAGGAGCAGACCAACCCCTCCGAGTTCGTGCTCGCCCACGTGCTGGAGTCCAGCACCATCCCCCTCATGGCGCACCTGACCTGCATTGGCTACCGCAAGCAGGAGGCCGTTGAGATCGTCACCCGCTTCCTTCGCATGGGAGTGCGGCGCTTCCTCGCCCTGCGCGGCGACCCGCCGGCCGGCACCCGGGCCGACGAGGTCGCCGGGGAGCTGCGCCACGCCGACGACCTCGTTCGGGTCATCCGGGAGGTCGAGGCGGACTTCTTCGGTGACGGCAAGCGCCACGTCACGATCGCCGTGGCCGCCTACCCGGCCACCAGCGACCACATCGAGGCCATTGAGGTCCTGGCCGCCAAGCAGGCCGCCGGCGCCGACATGGCAATCACCCAGGTGTTCTACGATGCGGCCGACTACGTGGCCCTGACCAACGCGGCCTCCTATGCGGGGGTGAGCATCCCGATCCTTCCCGGGGTGATCCCCCTGACCGACCTACGTCGGCTCACCCGCCTCGAGGCGCTCACCGGGGTGCGAGTGCCCGCCGGCCTGCGATCCACGCTGGGATCGGCCAGCGGCGCCACCCTCGTGGAACGCGGCATCGGAGCGACGCTTGACCTGGCCACCGCGCTGCTACGTGCCGGCGCCCCCGGTCTGCACCTGTACACCTTCAACCGCACCCGTCCGGCCCTCGACGTCATCAGCCACCTGCGTCTGGGTGGCATCCTGGCCGGAGCCACGCCCGATCGGGAGGTGCGCGACGCCGTTGATCGCGGGTACCTCCAGGCCACTCCCGGACGCGGTCCCTCCTTCCTGCGCTGCGGCTCTCCCGGTGCAGCACTGTCTTCCCGCCACCCCGTTCCGCCCCACACCACCATCACCAAGGAGAATGCATGA","VHDNEPTGPTAAAGSRAAGLSSAETGSARRLPTVSLELFPPRPGKAASATWGRIDRLLATGPDFVSVTYRPTFVTDPAGGINGGEYEGSVRGTEVSRCKAVPCVRAVQEQTNPSEFVLAHVLESSTIPLMAHLTCIGYRKQEAVEIVTRFLRMGVRRFLALRGDPPAGTRADEVAGELRHADDLVRVIREVEADFFGDGKRHVTIAVAAYPATSDHIEAIEVLAAKQAAGADMAITQVFYDAADYVALTNAASYAGVSIPILPGVIPLTDLRRLTRLEALTGVRVPAGLRSTLGSASGATLVERGIGATLDLATALLRAGAPGLHLYTFNRTRPALDVISHLRLGGILAGATPDREVRDAVDRGYLQATPGRGPSFLRCGSPGAALSSRHPVPPHTTITKENA$","5,10-methylenetetrahydrofolate reductase","Cytoplasm","5,10-methylenetetrahydrofolate reductase","5;10-methylenetetrahydrofolate reductase ","Methylenetetrahydrofolate reductase (NAD(P)H)","","Guenther B.D., Sheppard C.A., Tran P., Rozen R., Matthews R.G., Ludwig M.L. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat. Struct. Biol. 1999. 6(4):359-365. PMID: 10201405","","","

InterPro
IPR003171
Family

Methylenetetrahydrofolate reductase
PF02219	$\"[24-343]T$	MTHFR

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.220	$\"[20-342]T$	no description
PTHR21091	$\"[132-344]T$	METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
PTHR21091:SF1	$\"[132-344]T$	METHYLENETETRAHYDROFOLATE REDUCTASE

","BeTs to 11 clades of COG0685COG name: 5,10-methylenetetrahydrofolate reductaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0685 is ---pkzyqvd-lbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003171 (Methylenetetrahydrofolate reductase) with a combined E-value of 7.9e-36. IPB003171A 34-44 IPB003171B 62-71 IPB003171C 126-159 IPB003171D 180-190 IPB003171F 219-248 IPB003171G 321-344","Residues 24-286 are 38% similar to a (GLABRATA CBS138 SEQUENCE CANDIDA OXIDOREDUCTASE FLAVOPROTEIN STRAIN J CHROMOSOME FAD) protein domain (PDA18399) which is seen in Q6FNS2_EEEEE.Residues 24-345 are 45% similar to a (REDUCTASE OXIDOREDUCTASE FLAVOPROTEIN 510-METHYLENETETRAHYDROFOLATE FAD) protein domain (PDA1B466) which is seen in Q8KCP5_CHLTE.Residues 28-291 are 39% similar to a (METHYLENETETRAHYDROFOLATE REDUCTASE OXIDOREDUCTASE FLAVOPROTEIN FAD NADP) protein domain (PD127878) which is seen in MTHR_YEAST.Residues 30-342 are 39% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD) protein domain (PDA0A4T4) which is seen in Q7S830_NEUCR.Residues 32-338 are 45% similar to a (REDUCTASE OXIDOREDUCTASE FLAVOPROTEIN 510-METHYLENETETRAHYDROFOLATE FAD) protein domain (PDA1B415) which is seen in Q72DD2_DESVH.Residues 32-286 are 39% similar to a (NRRL KLUYVEROMYCES STRAIN LACTIS Y- D CHROMOSOME Y-1140) protein domain (PDA185G6) which is seen in Q6CR34_EEEEE.Residues 32-344 are 37% similar to a (OXIDOREDUCTASE FLAVOPROTEIN METHYLENETETRAHYDROFOLATE FAD REDUCTASE NADP) protein domain (PDA0A4T5) which is seen in MTHS_YEAST.Residues 32-343 are 46% similar to a (REDUCTASE OXIDOREDUCTASE FLAVOPROTEIN 510-METHYLENETETRAHYDROFOLATE FAD) protein domain (PD726527) which is seen in Q8GGL6_STRAZ.Residues 32-342 are 44% similar to a (510-METHYLENETETRAHYDROFOLATE RELATED REDUCTASE) protein domain (PDA05119) which is seen in Q6AMT4_BBBBB.Residues 33-343 are 47% similar to a (METHIONINE REDUCTASE OXIDOREDUCTASE FLAVOPROTEIN 510-METHYLENETETRAHYDROFOLATE BIOSYNTHESIS FAD) protein domain (PD724440) which is seen in METF_AQUAE.Residues 33-344 are 40% similar to a (OXIDOREDUCTASE FLAVOPROTEIN METHYLENETETRAHYDROFOLATE FAD REDUCTASE NADP) protein domain (PDA0A4T7) which is seen in MTHR_SCHPO.Residues 33-343 are 43% similar to a (REDUCTASE OXIDOREDUCTASE FLAVOPROTEIN 510-METHYLENETETRAHYDROFOLATE FAD) protein domain (PD725529) which is seen in Q83A63_COXBU.Residues 34-344 are 48% similar to a (REDUCTASE OXIDOREDUCTASE FLAVOPROTEIN 510-METHYLENETETRAHYDROFOLATE FAD) protein domain (PDA1B4K6) which is seen in Q7UNJ7_RHOBA.Residues 35-344 are 40% similar to a (OXIDOREDUCTASE AAR170WP FLAVOPROTEIN FAD) protein domain (PDA0A4T6) which is seen in Q75EA7_ASHGO.Residues 39-338 are 44% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD REDUCTASE 510-METHYLENETETRAHYDROFOLATE METHYLENETETRAHYDROFOLATE PROBABLE CG7560-PA NADPH2 REDUCTASE) protein domain (PD406226) which is seen in Q7WQX3_BORBR.Residues 118-296 are 47% similar to a (OXIDOREDUCTASE FLAVOPROTEIN METHYLENETETRAHYDROFOLATE FAD REDUCTASE NADP) protein domain (PD445464) which is seen in MTHS_SCHPO.Residues 153-342 are 46% similar to a (OXIDOREDUCTASE FLAVOPROTEIN FAD REDUCTASE 5 10-METHYLENETETRAHYDROFOLATE) protein domain (PDA05117) which is seen in Q8KTS2_CANTP.","","-44% similar to PDB:1V93 5,10-Methylenetetrahydrofolate Reductase from Thermus thermophilus HB8 (E_value = 5.9E_32);-48% similar to PDB:1B5T ESCHERICHIA COLI METHYLENETETRAHYDROFOLATE REDUCTASE (E_value = 4.8E_26);-48% similar to PDB:1ZP3 E. coli Methylenetetrahydrofolate Reductase (oxidized) (E_value = 4.8E_26);-48% similar to PDB:1ZPT Escherichia coli Methylenetetrahydrofolate Reductase (reduced) complexed with NADH, pH 7.25 (E_value = 4.8E_26);-48% similar to PDB:1ZRQ Escherichia coli Methylenetetrahydrofolate Reductase (reduced) complexed with NADH, pH 6.0 (E_value = 4.8E_26);","Residues 24 to 343 (E_value = 1.6e-29) place ANA_1078 in the MTHFR family which is described as Methylenetetrahydrofolate reductase.","","reductase (FADH2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1079","1156905","1156591","315","7.40","0.60","11257","ATGCGCCGACTCACCCCGAGGCTGGCCCAGGCCACCAACGCAGCACGCTCCGTTCTGATAGAGGTCGCTCAGCACCGTGAGGTCATCACCTACGGTGAGCTCAGCGACTCGATCGGACGGAGCGTGCTGCCGCGTCATATGGGTCCGTTGCTCTCCATGATCGGCCACGACTGCGCTGCTCGCGGCGAACCGAGTCTGGCCTCCCTGGTGGTCTCAGCGGCCACAGGAGAGGTCGGCACCAGGGACGAGACCTGGGCTCCGCCGCAGCGACTCGCCTGCTGGGCGGTATGGGGTACGAACCGGCCCGACGACTGA","MRRLTPRLAQATNAARSVLIEVAQHREVITYGELSDSIGRSVLPRHMGPLLSMIGHDCAARGEPSLASLVVSAATGEVGTRDETWAPPQRLACWAVWGTNRPDD$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-49% similar to PDB:1OEP STRUCTURE OF TRYPANOSOMA BRUCEI ENOLASE REVEALS THE INHIBITORY DIVALENT METAL SITE (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1080","1159476","1157035","2442","5.36","-18.52","83895","ATGAAGCGTCGAATCGTCGCCCAGATGGCGATACTCGCTCTATCGCTGTCGGCGCCTGTTCTGGCCGTGACTCATGCACCACAAGCCGCCGCCGCCGACGGCAACATCATTCATGTCTCGGCCGAGGGAGGCTCGGACGCGGGAGACGGAACCGCTGCCAAGCCCCTTCAGACCATTGGAGCCGCCCTGAAGAAGGCCGGCGGCGGAGACACCATCGAGCTGGCCAACGGCACCTACCGTGAGGGCGAGCTCGCCGTCGACAAGGGCGTGACCATCAAGGCGGCCGAGGGTGCCAAGCCGGTCCTCACCGGTGCCGAGGTCCCCAAGAGCTGGAGTGCCGGCGGTGACGGGAAGTGGTCCACGGGCAAGGACATGGTCCGCTTCTGCACGGTCTGCACCATCAATGCCGACCCCGCCAAGGAGGGGATCGCCGCCCACCCCGAGCAGGTGTTCGTGGACGGTAAGCCCCTGACCCAGGTGCTCAGCCGCGCCGAGGTCACCGAGTCCACCTTCTACGTGGACGACCCCGACCCGGTCACCCTGAAGAACCCGAAGAACAACCAGGCCGGCTACAACGTCAAGCCGCACCGGGGCACCTCTTACGTCATCGGTGTTGACCCCAACCAGCACCAGGTCGAGGTGGTCCAGCACTCCCGGGCCCTGTCCTTCAACACCGACAACATCACCCTGTCGGGACTGACCGTGGAGAAGTACTCCGCGGTGCAGCGCTGGGACTACGAGGACCCTGAGATCGGCACCATCTCCGGCGGTGGAATGGTCGTGGCCGCACACGGTGCTCCTCGTGTCGAGAACTCCACCTTCCGCTACTCCTCGACGGCCGGTGCGCTGCAGGTCATCGACTCCACCAACGCGGCCATCTCGAACAACCTGTTCGAGAACAACGGCTCCAACGCCTTCGGCATCAATGACTCCAGTGGCGCCAAGGTGGAGAACAACCTGTGGAGGAACAACAACACCTCCGGCTTCATCACGAAGGACTGCGGTGCCTACTGCACCCTGGCCGACACCAAGATCACCCACTCCAAGAACATCCGCTTCGCCAACAACACAGTGGACTACTCGGCCACCGGCACGGACATCTCCGACCCCGCGGCCTATGACCAGAACCGTGCCGCAGGCGTGTGGTTCGACGAGGGCGTGATCGACTCCGAGATCGTTGGCAACTACTTCGTCAACGTCCCGGTGGCGATCTTCAACGAGGTCTCCTCCAACAACCTCATCGCCTCCAACATCGTGGCCGGGGCCGGTATCGGTATCCACATCTCCGGGTCCAACGACACCCGCGTGTGGAACAACACCGTCTCCCACGCGCTCACCAGCCTGTGGATCCAGGAGGACACCCGTTCCGACGGCTGCAACGCCCGCAACGCCCAGGGTGTGTGCACTCAGGTGCAGAAGTGGAGCGCCGAGCACGGACTGAGCTGGGACACCACCAACACCCAGGTGATGAACAACATCTTCTCCTCCGAGCAGACCACCCCCATGCCCGGGGACCCGTGGCGCTACTCCGCCATGGTCCAGGTCCTGGGTGGGGCCAACCAGGACGGCTCCGGCGCGGTCTACGCCAATGAGATGGTCACCGGCATCGACTACGACGTCTACTACCGCCACGAGAACCCCCAGACCCTGTCGACCACGGTCCTGTGGAACTGGGGCGCCGACCGTATGAACCAGTCGGTCAACGCCGAGAAGCTCTCCGACTTCACCGCCAGCTCGAGCGTCAAGGCATCGGGCAAGGAGGCCAACGGTCTGGACCTGCACGGCTCCCCGGAGAACAACCCGTTCTTCGTCAAGGAGTCCGCAAACCCGATGGACAAGACCTCGGACTTCCACCTCAAGGAGGGAAGCCCCGCCTCCGGTAACGGTCACGCCCTGCCCGAGGACATCGCCAAGACCCTCGGCGTCAACGCCAACGTCGCCGTGGACCGCGGTGCGCTCGTCAACGTCGCCTGGGGCGGCGGCGCCGTTCCCGGTGCCGGGGACGCCCCCGCTGACAACGCCAACAACGGCGGCAAGGCCGCTAACAACGGCGACAAGGCCGCCAACAACAATGGCGGTAACGCCAACAACGGTGGTAAGGCCGACAACAACGGTGGCAATGGTGGCAACGCCAACAACGGTGGCAAGGCCGACAACAACGGCTCCACCGTCGCCGACGGGGCCGCTAGCACCGGCGGCCAGGACGCACAGAGCGCCAGCCCCTCTGACTCCAAGGCAGGGGCCGGCCAGAAGAACTCCAGCATCGCCAAGCCCGGCGGCAACGCTCAGGGCGGTCAGGGTCAGGCTGCTGCGGCTGCAGCGGCTACCGGTGATAGCCGTCTTCCGCTCACCGGTGCCAGCTTGACCGGCATCGTCCTGGCGGTGGCCGCCATCGTCATGGGCGGCGGATTCATCCTGGTACGCCGTCGTATGGCCAGCTGA","MKRRIVAQMAILALSLSAPVLAVTHAPQAAAADGNIIHVSAEGGSDAGDGTAAKPLQTIGAALKKAGGGDTIELANGTYREGELAVDKGVTIKAAEGAKPVLTGAEVPKSWSAGGDGKWSTGKDMVRFCTVCTINADPAKEGIAAHPEQVFVDGKPLTQVLSRAEVTESTFYVDDPDPVTLKNPKNNQAGYNVKPHRGTSYVIGVDPNQHQVEVVQHSRALSFNTDNITLSGLTVEKYSAVQRWDYEDPEIGTISGGGMVVAAHGAPRVENSTFRYSSTAGALQVIDSTNAAISNNLFENNGSNAFGINDSSGAKVENNLWRNNNTSGFITKDCGAYCTLADTKITHSKNIRFANNTVDYSATGTDISDPAAYDQNRAAGVWFDEGVIDSEIVGNYFVNVPVAIFNEVSSNNLIASNIVAGAGIGIHISGSNDTRVWNNTVSHALTSLWIQEDTRSDGCNARNAQGVCTQVQKWSAEHGLSWDTTNTQVMNNIFSSEQTTPMPGDPWRYSAMVQVLGGANQDGSGAVYANEMVTGIDYDVYYRHENPQTLSTTVLWNWGADRMNQSVNAEKLSDFTASSSVKASGKEANGLDLHGSPENNPFFVKESANPMDKTSDFHLKEGSPASGNGHALPEDIAKTLGVNANVAVDRGALVNVAWGGGAVPGAGDAPADNANNGGKAANNGDKAANNNGGNANNGGKADNNGGNGGNANNGGKADNNGSTVADGAASTGGQDAQSASPSDSKAGAGQKNSSIAKPGGNAQGGQGQAAAAAAATGDSRLPLTGASLTGIVLAVAAIVMGGGFILVRRRMAS$","Hypothetical protein","Extracellular, Membrane, Cellwall","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","LPXTG-motif cell wall anchor domain","","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
TIGR01167	$\"[780-812]T$	LPXTG_anchor: LPXTG-motif cell wall anchor
PS50847	$\"[781-813]T$	GRAM_POS_ANCHORING

InterPro
IPR006626
Repeat

Parallel beta-helix repeat
SM00710	$\"[288-310]T$ $\"[311-333]T$ $\"[348-369]T$ $\"[409-430]T$ $\"[431-452]T$	PbH1

InterPro
IPR011459
Domain

Protein of unknown function DUF1565
PF07602	$\"[43-79]T$	DUF1565

InterPro
IPR012334
Domain

Pectin lyase fold
G3DSA:2.160.20.10	$\"[21-111]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[787-807]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 45-417 are 37% similar to a (TLR0125) protein domain (PD852797) which is seen in Q8DMJ1_SYNEL.","","No significant hits to the PDB database (E-value < E-10).","Residues 43 to 79 (E_value = 1.9e-06) place ANA_1080 in the DUF1565 family which is described as Protein of unknown function (DUF1565).","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1081","1159522","1159929","408","8.12","2.80","14822","GTGATAAATTTTGTTTGGCATCCGTTATATCCGCATACTTCTGAGAGACGCTTCTCTCACTCGCCTCGCTACCGGCCGCTCTGGCGGGGTGCTACCTGCTCCGACGTGCGTACCTCACGCCCCGTCTGCGAGGATCCACCTATGACGCACGCAACATCTCGACGGCCATCCCAGCACCCGCTCATCTCAGTGTCCGGAAGCATCAGGCTCGGCCAGTTCCTCAAGCTGGCGAGCATGGTGGAGGACGGCGCACAGGCGCGCATCGCCATCCAGTCCGGAGACGTCACTGTCAACGGCGTCGTGGAGACACGTCGCGGGCACCACCTGGCTGATGGTGACGTCGTCGTCGTCGATCACCCCGCCGGCCAGGTGGGCGCCACCGTTGAGCAGCTGGGGACCGAGCAATGA","VINFVWHPLYPHTSERRFSHSPRYRPLWRGATCSDVRTSRPVCEDPPMTHATSRRPSQHPLISVSGSIRLGQFLKLASMVEDGAQARIAIQSGDVTVNGVVETRRGHHLADGDVVVVDHPAGQVGATVEQLGTEQ$","RNA-binding S4 domain protein","Cytoplasm, Extracellular","S4 domain protein","hypothetical protein","RNA-binding S4 domain protein","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Aravind L., Koonin E.V. Novel predicted RNA-binding domains associated with the translation machinery. J. Mol. Evol. 1999. 48(3):291-302. PMID: 10093218","","","

InterPro
IPR002942
Domain

RNA-binding S4
PF01479	$\"[68-115]T$	S4
SM00363	$\"[68-126]T$	S4
PS50889	$\"[68-121]T$	S4

noIPR
unintegrated

unintegrated
G3DSA:3.10.290.10	$\"[65-126]T$	no description

","BeTs to 6 clades of COG2501COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2501 is ---------d-lb-e-g--n-----wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 68 to 115 (E_value = 0.015) place ANA_1081 in the S4 family which is described as S4 domain.","","domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1083","1161782","1159974","1809","4.82","-19.19","63797","ATGGACAAGGTGGTCTTCGGCGTCGCCGCGGCCGCGACCATCGCCTTCGTCGTGTGGGGCTTCATCTCTCCGCACGGTCTGGGGAGGGCCTCCAAGTGGGCCCTGGGGGGAACGATCAGCAACTTCGGCTGGCTGTTCGTCCTGTCCTCGACCCTGTTCGTCGTCTTCGTCGTCTTCGTGGCGGCCTCCCGGTTCGGCAAGATCCCCCTGGGTGGGGACGGAGAGGAGCCCGAGTACTCCACCGGCTCCTGGGTCTCCATGATGTTCGCCACGGGAATGGGTATCGGACTGATTTTTTATGGGGTCGGTGAGCCGCTCTACTTCTACATGTCGCCCCCGCCGGAGACGGTCGACCCTCAGACCGCCCAGGCCGCCAGCACTGCCCTAGGTACGGCCATGTTCCACTGGACCATCTACCCGTGGGCGATGTACGCCCTGGTGGGGCTCGGGATGGCATACGGGACCTACCGCCTGGGACGCTCCCAGCTCTTCTCGGCCATGTTCACCTCCCTGTTCGGGCGCCAGGCCATCGACGGGATCGGTGGGCGCATCATCAACATCCTGGCGATCGTGGCCACCCTGTTCGGGTCGGCCTGCTCCCTGGGACTGGGGGCCCTGCAGATCGGCGGGGGAATGGTGTCGACCAATCTCGTCACCAAGTCCACCCCCGCGATGATGGTCGGCATCATCGCGATCCTGACGGCCTGCTTCGTGGCCTCCGCGATCTCCGGCATTGAGAAGGGCATCCAGTGGCTGTCGAACATCAACATGGTGCTGGCTGTGCTGCTGGCGATCATCGTCTTCATCGGCGGACCCACCCTGTTCATCCTCAATATCATCCCCTCGGCGATCGGCAACTTCATCGACGAGCTGCCCGCCATGGCCTCGCGCACCGCGGCCGTGGGCAATCAGGACATGGCCCAGTGGCTGTCCTCCTGGACGATCTTCTACTGGGCCTGGTGGATCTCCTGGACGCCCTTCGTGGGAATGTTCATCGCCCGCATCTCGCGCGGCCGCACCATCCGGCAGTTCGTCACCGGGGTCATGCTCGTCCCCTCAGTCGTCTCTCTCATCTGGTTCGCCATCTTCGGTGGGGGCGCCATCGGGCTCCAGGAACGCGCCGAGCGCGCCGGCCAGGCGGCGCACGCCCTGGTTCACCTCAAGGCCGATGGCACGCCCGACCTGAACTTCGACACGATCCTGTTCGACCTGCTCAACGCCATGCCCGTGCACAAGGTGGTCCTCATCGTCCTCATGGTCCTGGCCGTCGTCCTGGTGGCGATCTTCTTCGTCACCGGTGCCGACTCGGCCTCCATCGTCATGGGAGGGCTCTCCGAGAACGGTGCCACCGATCCGAGCCGCTTCACGGTCGTCTTCTGGGGCGTGGCCACCGGTGGCGTGGCCTCAGCCATGCTGCTCGCCGGCGGGGATGATCCGCGCGAGGTCCTCACCGGTCTGCGCGACATCACGATCGTCTCGGCGCTGCCCTTCGTCTTCGTCATGCTGCTGCTGTGCGTCTCGCTCTACAAGGACCTCAACAACGACCCCATGCTGCTGCGGCACTCGCTGGCCAACCAGGTCCTGGTCGACTCGGTCACCACCGCGGTCACGACCGCCAACGAGCCGCATGAGGTCGAGACCATCGAGCTGCACACCAGCCTGTCATCGACCACTGACGGCGACGACGCAGCCGGTGAGGGCTGCCAGGACGGCACCGACGAGGCCGCGCAGGACCTCAGGGTTGACGACCTCGCCGTCGACGGTGCGGATGATGCGCAGGCTGGAGCCGACCAGAGGCAGGAGAACTAG","MDKVVFGVAAAATIAFVVWGFISPHGLGRASKWALGGTISNFGWLFVLSSTLFVVFVVFVAASRFGKIPLGGDGEEPEYSTGSWVSMMFATGMGIGLIFYGVGEPLYFYMSPPPETVDPQTAQAASTALGTAMFHWTIYPWAMYALVGLGMAYGTYRLGRSQLFSAMFTSLFGRQAIDGIGGRIINILAIVATLFGSACSLGLGALQIGGGMVSTNLVTKSTPAMMVGIIAILTACFVASAISGIEKGIQWLSNINMVLAVLLAIIVFIGGPTLFILNIIPSAIGNFIDELPAMASRTAAVGNQDMAQWLSSWTIFYWAWWISWTPFVGMFIARISRGRTIRQFVTGVMLVPSVVSLIWFAIFGGGAIGLQERAERAGQAAHALVHLKADGTPDLNFDTILFDLLNAMPVHKVVLIVLMVLAVVLVAIFFVTGADSASIVMGGLSENGATDPSRFTVVFWGVATGGVASAMLLAGGDDPREVLTGLRDITIVSALPFVFVMLLLCVSLYKDLNNDPMLLRHSLANQVLVDSVTTAVTTANEPHEVETIELHTSLSSTTDGDDAAGEGCQDGTDEAAQDLRVDDLAVDGADDAQAGADQRQEN$","Choline/carnitine/betaine transporter","Membrane, Cytoplasm","choline/carnitine/betaine transporter familyprotein","choline/carnitine/betaine transport","choline/carnitine/betaine transporter","","Kappes R.M., Kempf B., Bremer E. Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD. J. Bacteriol. 1996. 178(17):5071-5079. PMID: 8752321","","","

InterPro
IPR000060
Family

BCCT transporter
PD010111	$\"[5-176]T$	Q88GT9_PSEPK_Q88GT9;
PF02028	$\"[5-515]T$	BCCT
TIGR00842	$\"[43-515]T$	bcct: transporter, betaine/carnitine/cholin
PS01303	$\"[312-321]T$	BCCT

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[5-23]?$ $\"[42-62]?$ $\"[83-103]?$ $\"[136-156]?$ $\"[184-204]?$ $\"[223-243]?$ $\"[258-280]?$ $\"[313-333]?$ $\"[343-363]?$ $\"[414-434]?$ $\"[455-475]?$ $\"[489-509]?$	transmembrane_regions

","BeTs to 9 clades of COG1292COG name: Choline-glycine betaine transporterFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1292 is -o--------r-b-efgh-n----t-Number of proteins in this genome belonging to this COG is 2","***** IPB000060 (BCCT transporter) with a combined E-value of 1.2e-99. IPB000060A 74-104 IPB000060B 128-156 IPB000060C 229-276 IPB000060D 313-347","Residues 5-176 are similar to a (TRANSPORTER BETAINE GLYCINE CHOLINE FAMILY HIGH-AFFINITY BCCT TRANSPORTER TRANSMEMBRANE MEMBRANE) protein domain (PD010111) which is seen in Q88GT9_PSEPK.Residues 185-251 are 82% similar to a (TRANSPORTER BETAINE GLYCINE CHOLINE FAMILY HIGH-AFFINITY BCCT TRANSPORTER TRANSMEMBRANE MEMBRANE) protein domain (PD583790) which is seen in Q9X7P5_STRCO.Residues 253-442 are 68% similar to a (TRANSPORTER BETAINE GLYCINE CHOLINE FAMILY HIGH-AFFINITY TRANSPORTER BCCT TRANSMEMBRANE MEMBRANE) protein domain (PD583457) which is seen in Q88GT9_PSEPK.Residues 452-515 are 75% similar to a (TRANSPORTER BETAINE GLYCINE CHOLINE FAMILY HIGH-AFFINITY BCCT TRANSPORTER TRANSMEMBRANE MEMBRANE) protein domain (PD835550) which is seen in Q88GT9_PSEPK.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 515 (E_value = 8.2e-191) place ANA_1083 in the BCCT family which is described as BCCT family transporter.","","transporter family protein (betT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1086","1165891","1162307","3585","5.39","-35.43","132194","ATGAGCAGTCAGGAAGAAGCAGCCCCCAAGGACGACTTCGTCCACCTCCACGTTCACACCGACTACTCCATGCTGGACGGCGCCGGGAAGATCAAGGACTACGTGGCCGAGGCCAAGCGGCTGGGCCAGCCCGCCCTGGCGATCACCGACCACGGCTACATGTTCGGAGCCTACGAGTTCTACGCGGCCGCCACGGCCGCCGGTATCAAGCCGATCATCGGGGTCGAGGCGTACATGACGCCGGGCACCTCCCGCTTCGACAAGACCCGTGTGTTCTGGGGCGATGAGTCCCAGCGGAGCGACGACGTCTCCGCCCGCGGCTCCTACACGCACATGACGCTGCTCTCACGCAACAACGAGGGCCTGCACAACCTCATGCGCATGGACTCCTTCGCCTCTCTGGAGGGTCAGTGGGGCAAGGCGCCGCGCATCGACCGTGAGCTGCTCTCGCGCTATGCGAGCGGCCTCATCGGCTCCACCGGCTGCCCCTCCTCGGAGGTCCAGACCCGCCTGCGCCTGGGCCAGTGGGACGAGGCCCTGCGCGTCGCCGGGGAGCTGCAGGACATCTTCGGCAAGGAGTTCTTCTACGTCGAGCTCATGGACCACGGCCTGGAGATCGAGCAGCGCGTCACCAAGGATCTGCTGCGCATCGCCAAGGAGATCGGGGCCCCGCTGCTGGCCACCAACGACTCCCACTACGTGCGCCCCGAGGACCGCACCATCCAGGACGCGATGCTGTGCATCAACTCCGGCTCCGTGCTCTCCGATCCCGACCGCTTCAAGTTCGACGGTGACACCTACTACCTGCGCCCCGGCGCCGAGATGCGCCGCCTCTTCTCCGAGATGCCCCAGGCCTGCGACAACACCCTGCTTGTGGCCGAGCAGTGCGACGTGCACTTCCGTACCGTGGACGAGGGGGCCTCATACATGCCGGCCTTCCCCGTCCCCGAGGGGGAGACCGACGAGTCCTGGTTCATCAAGGAGTGCTGGCGCGGCATGGACCGCCGGTTCAACGGCGACATCCCCGAGGACTGCCGCAAGCAGGCCGAGTACGAGATCAGCGTCATCACCCAGATGGGGTTCCCCGGCTACTTCCTCGTTGTGGCCGACTACATCAACTGGGCCAAGGCCCACGGCATCCGGGTCGGGCCGGGGCGTGGATCGGGAGCCGGCTCCATGGTTGCCTACGCCATGGGCATCACCGAGCTCAACCCGCTGCGCCACGGGCTCATCTTCGAGCGCTTCCTCAACCCCGAGCGCATCTCCATGCCCGATATCGACGTCGACTTCGACGAGCGCCGGCGTGACGAGGTCATTGAGTACGTGCGTGAGAAGTACGGCGCCGACCGCATCAGCCAGGTGGTCACCTACGGCGTCATCAAGGCCAAGCAGTCCTTGAAGGACTCCAGCCGCGTCATGGGCTACCCCTACGCCGTCGGCGACCGGCTCACCAAGGCCATGCCCCCCTCCGTCCAGGGCAAGGACATCTCCATCAAGGGCATCTTCAACCCCGCCGACGAGCGCTACGGCGAGGCCGAGGAGTTCCGCAAGCTCCACGCCGAGGACCCCGACGCCCAGAAGATCGTCGAGCTGGCCAAGGGGCTGGAGGGCATGACCCGTCAGTGGGGCGTCCACGCCTGCGCCGTCATCATGTCCTCAGCCACCCTGACCGACATCATCCCCATGATGCAGCGCCTGCAGGATGGCGCCGTCATCACCCAGTTCGACTACCCCACCTGCGAGCACCTGGGCCTGCTCAAGATGGACTTCCTGGGACTGCGCAACCTCACGGTCATCTCCGACGCCCTGGAGAACATTGTCGCCAACGGCAAGCCGGCCCTGGACATCGACCACGTCGAGCTTGACGACCGCGCCACCTACGAACTGCTCTCACGCGGCGAGACCCTGGGCGTCTTCCAGCTCGACGGCGGGGGGATGCGCACCCTGCTGCGCCTGATGAAGCCCGACAACTTCGAGGACATCTCCGCCGTCGGCGCCCTCTACCGGCCCGGCCCCATGGGGGCGGAGTCCCACACCAACTACGCGCTGCGCAAGAACGGCCTGCAAGAGGTCATCCCGATCCACCCCGAGCTCAAGGAGGCCCTCGACCCGATCCTGGGGACCACGCACGGTCTCATCGTCTACCAGGAGCAGGTCATGAAGATCGCCACCGACCTGGCGGGATTCTCCATGGGCAAGGCCGACGCGCTGCGCAAGGCCATGGGTAAGAAGAAGATGGACATCCTGGCCAAGATGTTCGTCGAGTTCGAGGCCGGGATGGTCCAGTCCGGCTTCTCCAAGGAGAGCGTCAAGACACTGTGGGACGTCGTCGTTCCCTTCGCCAAGTACGCCTTCAACAAGGCCCACTCGGCCGCCTACGGCGTTGTGTCCTACTGGACGGCCTACCTCAAGGCGCACTATCCCACCGAGTACATGGCCGCCCTGCTCACCAGTCAGAAGGACAACAAGGACAAGCTGGCCGTCTACCTGGGGGAGTGCCGCCACATGGGCATCACCGTCCTGCCCCCGGACGTCAACGCCTCGCGGGCCCAGTTCTCCGCGGTCGGTGAGGACGTGCGCTTCGGGCTGTCCGCGGTGCGCAACGTCGGCATCAACGTCGTCGACGCGATCGTGGCCGCCAGGGAGGACAAGGGCGAGTTCACCTCCTTCGAGGACTTCCTGGACAAGGTTCCCGCGGTCGTGTGCAACAAGCGCACCATCGACTCGCTCATCAAGGCCGGAGCCTTCGACTCCCTGGGGCACACCCGGCGCTCCCTGCAGGCCTGCCACGAGGACTTCGTCGATGAGGTCATCGGCGTCAAGCGCAACGAGGCCGCCGGCCAGTTCGACCTGTTCGCCTCCCTCATGGGCGGGTCCGACGACGCCGACGACTCACCCTTCGGCAACGGCCCGGTCTTCTCCTCCGATGTTCCCAACCTGCCGGAGTGGGACAAGAAGGACAAGCTCGCCTACGAGCGCGACATGCTGGGCCTCTACGTCTCCGACCACCCCCTCATGGGCCTGGAGGGGCTGCTGGGCAAGCTCGCGGACAAGGAGATCTCCGAGCTCCACGAGAACGATGAGCTGCCCGACGGCGCCATGGTCACCATCGCCGGGCTCATCACCTCCCTGACCCGCAAGACCACCAAGCAGGGCAACCTGTGGGCCATCGCCCAGGTCGAGGACCTGGCCGGAAGCATCGAGGTGCTCTTCTTCCCCCAGACCTATCAGACCGTCTCCACCATGCTGGCCCCGGACACGGTGGTCACGGTGCGCGGACGTCTCAACCGGCGTGACGGGCAGGTCGCCCTGTACGCCCAGGAGATGACGATCCCGGACATCTCCAGCGCCGCCCACGAGGCGGTCCTCATCACCCTTCCCACCAACCGGTGCACTGGGCCTCTGGTGGAGCAGTTCAAGGACGTGCTCACCAAGCACCCGGGTGGCTCGACGGTCCGTCTGACGCTGACCAGCCCGGGGCGCGAGGTGCGCACCCAGCTGGACGCCTCGCTACGGGTGGAGGCCTCGCCCGCCTTCTACTCCGACATCAAGGCCCTCCTCGGCCCGGGGTGCCTGCGCCACTAG","MSSQEEAAPKDDFVHLHVHTDYSMLDGAGKIKDYVAEAKRLGQPALAITDHGYMFGAYEFYAAATAAGIKPIIGVEAYMTPGTSRFDKTRVFWGDESQRSDDVSARGSYTHMTLLSRNNEGLHNLMRMDSFASLEGQWGKAPRIDRELLSRYASGLIGSTGCPSSEVQTRLRLGQWDEALRVAGELQDIFGKEFFYVELMDHGLEIEQRVTKDLLRIAKEIGAPLLATNDSHYVRPEDRTIQDAMLCINSGSVLSDPDRFKFDGDTYYLRPGAEMRRLFSEMPQACDNTLLVAEQCDVHFRTVDEGASYMPAFPVPEGETDESWFIKECWRGMDRRFNGDIPEDCRKQAEYEISVITQMGFPGYFLVVADYINWAKAHGIRVGPGRGSGAGSMVAYAMGITELNPLRHGLIFERFLNPERISMPDIDVDFDERRRDEVIEYVREKYGADRISQVVTYGVIKAKQSLKDSSRVMGYPYAVGDRLTKAMPPSVQGKDISIKGIFNPADERYGEAEEFRKLHAEDPDAQKIVELAKGLEGMTRQWGVHACAVIMSSATLTDIIPMMQRLQDGAVITQFDYPTCEHLGLLKMDFLGLRNLTVISDALENIVANGKPALDIDHVELDDRATYELLSRGETLGVFQLDGGGMRTLLRLMKPDNFEDISAVGALYRPGPMGAESHTNYALRKNGLQEVIPIHPELKEALDPILGTTHGLIVYQEQVMKIATDLAGFSMGKADALRKAMGKKKMDILAKMFVEFEAGMVQSGFSKESVKTLWDVVVPFAKYAFNKAHSAAYGVVSYWTAYLKAHYPTEYMAALLTSQKDNKDKLAVYLGECRHMGITVLPPDVNASRAQFSAVGEDVRFGLSAVRNVGINVVDAIVAAREDKGEFTSFEDFLDKVPAVVCNKRTIDSLIKAGAFDSLGHTRRSLQACHEDFVDEVIGVKRNEAAGQFDLFASLMGGSDDADDSPFGNGPVFSSDVPNLPEWDKKDKLAYERDMLGLYVSDHPLMGLEGLLGKLADKEISELHENDELPDGAMVTIAGLITSLTRKTTKQGNLWAIAQVEDLAGSIEVLFFPQTYQTVSTMLAPDTVVTVRGRLNRRDGQVALYAQEMTIPDISSAAHEAVLITLPTNRCTGPLVEQFKDVLTKHPGGSTVRLTLTSPGREVRTQLDASLRVEASPAFYSDIKALLGPGCLRH$","DNA polymerase III, alpha subunit","Cytoplasm","DNA polymerase III alpha subunit","DNA polymerase III; alpha subunit ","DNA polymerase III, alpha subunit","","Koonin E.V., Wolf Y.I., Aravind L. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 2000. 54:245-275. PMID: 10829230Keshav K.F., Chen C., Dutta A. Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. Mol. Cell. Biol. 1995. 15(6):3119-3128. PMID: 7760808Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 1997. 385(6612):176-181. PMID: 8990123","","","

InterPro
IPR003141
Domain

Polymerase and histidinol phosphatase, N-terminal
SM00481	$\"[14-81]T$	POLIIIAc

InterPro
IPR004013
Domain

PHP, C-terminal
PF02811	$\"[14-235]T$	PHP

InterPro
IPR004365
Domain

Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336	$\"[1035-1112]T$	tRNA_anti

InterPro
IPR004805
Family

DNA polymerase III, alpha subunit
TIGR00594	$\"[13-1072]T$	polc: DNA polymerase III, alpha subunit

InterPro
IPR011708
Domain

Bacterial DNA polymerase III, alpha subunit
PF07733	$\"[267-764]T$	DNA_pol3_alpha

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.140	$\"[11-96]T$	no description

","BeTs to 18 clades of COG0587COG name: DNA polymerase III alpha subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0587 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB011708 (Bacterial DNA polymerase III, alpha subunit) with a combined E-value of 3e-169. IPB011708A 42-74 IPB011708B 389-430 IPB011708C 435-472 IPB011708D 532-551 IPB011708E 581-597 IPB011708F 639-669 IPB011708G 705-749 IPB011708H 783-817 IPB011708I 992-1005***** IPB003141 (Phosphoesterase PHP, N-terminal) with a combined E-value of 2e-88. IPB003141A 14-51 IPB003141B 358-367 IPB003141C 382-425 IPB003141D 540-549 IPB003141E 783-811","Residues 13-50 are 78% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III DNA-DIRECTED NUCLEOTIDYLTRANSFERASE REPLICATION) protein domain (PDA1D5T9) which is seen in DP3A_MYCTU.Residues 14-51 are 78% similar to a (DNA POLYMERASE ALPHA III TRANSFERASE SUBUNIT DNA-DIRECTED REPLICATION NUCLEOTIDYLTRANSFERASE III) protein domain (PD001693) which is seen in Q8DHA3_SYNEL.Residues 69-140 are 76% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED III CHAIN) protein domain (PD490478) which is seen in Q740T5_MYCPA.Residues 142-196 are 85% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE DNA-DIRECTED III REPLICATION NUCLEOTIDYLTRANSFERASE) protein domain (PD668096) which is seen in Q6AE74_BBBBB.Residues 221-318 are 75% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED REPLICATION) protein domain (PD126687) which is seen in Q8G7V8_BIFLO.Residues 332-383 are 82% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD216927) which is seen in Q6AE74_BBBBB.Residues 384-452 are 86% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD005473) which is seen in DP3A_NEIMA.Residues 451-562 are 55% similar to a (ALPHA III DNA POLYMERASE SUBUNIT) protein domain (PDA079B7) which is seen in Q8KE50_CHLTE.Residues 460-661 are 78% similar to a (DNA POLYMERASE ALPHA III SUBUNIT TRANSFERASE DNA-DIRECTED III NUCLEOTIDYLTRANSFERASE REPLICATION) protein domain (PD004180) which is seen in Q8G7V8_BIFLO.Residues 481-524 are 77% similar to a (DNA POLYMERASE ALPHA SUBUNIT TRANSFERASE III III DNA-DIRECTED CHAIN REPLICATION) protein domain (PDA0M4I0) which is seen in Q6A8L7_PROAC.Residues 666-698 are 90% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD949751) which is seen in Q6AE74_BBBBB.Residues 727-786 are 76% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE DNA-DIRECTED CHAIN) protein domain (PD847062) which is seen in Q8W6C3_VVVVV.Residues 788-922 are 81% similar to a (DNA POLYMERASE ALPHA III TRANSFERASE SUBUNIT DNA-DIRECTED REPLICATION NUCLEOTIDYLTRANSFERASE III) protein domain (PD352075) which is seen in Q6AE74_BBBBB.Residues 878-926 are 81% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE DNA-DIRECTED III REPLICATION NUCLEOTIDYLTRANSFERASE) protein domain (PD867790) which is seen in DP3A_STRCO.Residues 982-1109 are 71% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE III NUCLEOTIDYLTRANSFERASE CHAIN DNA-DIRECTED) protein domain (PD679201) which is seen in Q82AB6_STRAW.Residues 1111-1192 are 61% similar to a (DNA POLYMERASE ALPHA SUBUNIT III TRANSFERASE DNA-DIRECTED REPLICATION NUCLEOTIDYLTRANSFERASE III) protein domain (PD572408) which is seen in Q740T5_MYCPA.","","-57% similar to PDB:2HNH Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III (E_value = 3.7E_171);-57% similar to PDB:2HQA Crystal structure of the catalytic alpha subunit of E. Coli replicative DNA polymerase III (E_value = 3.7E_171);","Residues 14 to 235 (E_value = 1.6e-69) place ANA_1086 in the PHP family which is described as PHP domain.Residues 267 to 764 (E_value = 6e-266) place ANA_1086 in the DNA_pol3_alpha family which is described as Bacterial DNA polymerase III alpha subunit.Residues 1035 to 1112 (E_value = 1.4e-12) place ANA_1086 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.","","polymerase III alpha subunit (dnaE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1088","1167130","1166120","1011","5.09","-8.41","33987","ATGTGCGCGTGCCGAGAGCAGCAGGACCGAGAGGAGACACTCGTGCGGATCGTCGTCATCGGCGCCGGAGGCATCGGAGGATGGCTCGGCGCCCGCCTGGCCGCGAGCGGCCAGCAGGTCGGGTTCCTCGTTCACGATCGCACCCTGGCTGCCCTGCGCTCAGGCGGGCTGACGCTGCGCGACTGCTCCGGTGGCGAGCCCGGTACCGTGACCGCCCGCATCGAGACGCCACTGGCCAGTGATGACCCGCGGGCTCTCACCGAGACCCTGGGAGGTCAGCCGGACCTGGTCCTGGTGACCACGAAGGTCGATGCGCTGGTCGGGCTGGCTCCTGCGCTCAGAGTCCTGACCGGCCCCGACACCGGTGTCGTCTCCACCCAGAACGGGATCAGCGCGCCCGGAGTTCTCGCCGACGCCGTCGGCATGGAGCACGTCCTGCCCGGGGTCGCTCGCGTCTACTCCGCCATCGTCTCGCCCGGGGACGTGCGTACCATCGGCAGCGCCGGGTCGCTGGCCCTAGGGGAGTGGGACGGCAGCACGACGGCTCGCAGCCGCGCCGCCGCCCGGGCCCTGGAGGCGGCTGGAATCCGCGCCTGGGTCCCGGGCTCCATCTGGGCGGAGCTGTGGCGCAAGGTCTCCTTCGTCGTCGTCCAGGGCTCCCTCGGTGCCGCCGCGAACGCGCCCATCGGCGTCCTGCGCACCGACCTGAGAGACGCCTTCACCCGGGCCGTGGGCGAAGTCATCGCCGTCGCCGCGGCCCAGGGGCACGATCTGGCTACCGACGACGCCCCCGACCCGGTCGCTGCAGCCCTGCGCATGGCCGACGCCCAGCCGGCCGGCGCCACCACCTCGATGCAGCGGGACATCGCCGCGGGCCTTCCCAGTGAGCTCGACGCCCAGCTCGGCGCCCTGTGCCGCGCCGGCGACGAGGCGGGTGTACCCACCCCCGTGCTCGACCTCGCGCTCAGCGTCCTGGCTCCGCAAGAGGCTGCAGCCAGGGCGCGTGTCTGA","MCACREQQDREETLVRIVVIGAGGIGGWLGARLAASGQQVGFLVHDRTLAALRSGGLTLRDCSGGEPGTVTARIETPLASDDPRALTETLGGQPDLVLVTTKVDALVGLAPALRVLTGPDTGVVSTQNGISAPGVLADAVGMEHVLPGVARVYSAIVSPGDVRTIGSAGSLALGEWDGSTTARSRAAARALEAAGIRAWVPGSIWAELWRKVSFVVVQGSLGAAANAPIGVLRTDLRDAFTRAVGEVIAVAAAQGHDLATDDAPDPVAAALRMADAQPAGATTSMQRDIAAGLPSELDAQLGALCRAGDEAGVPTPVLDLALSVLAPQEAAARARV$","2-dehydropantoate 2-reductase","Cytoplasm, Membrane","2-dehydropantoate 2-reductase","2-dehydropantoate 2-reductase ","2-dehydropantoate 2-reductase","","Frodyma M.E., Downs D. The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium. J. Bacteriol. 1998. 180(17):4757-4759. PMID: 9721324Frodyma M.E., Downs D. ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway. J. Biol. Chem. 1998. 273(10):5572-5576. PMID: 9488683","","","

InterPro
IPR003710
Family

Ketopantoate reductase ApbA/PanE
TIGR00745	$\"[16-335]T$	apbA_panE: 2-dehydropantoate 2-reductase

InterPro
IPR013328
Domain

Dehydrogenase, multihelical
G3DSA:1.10.1040.10	$\"[203-329]T$	no description

InterPro
IPR013332
Domain

Ketopantoate reductase ApbA/PanE, N-terminal
PF02558	$\"[17-178]T$	ApbA

InterPro
IPR013752
Domain

Ketopantoate reductase ApbA/PanE, C-terminal
PF08546	$\"[203-329]T$	ApbA_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[15-201]T$	no description
PTHR21708	$\"[16-335]T$	PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE
tmhmm	$\"[15-35]?$	transmembrane_regions

","BeTs to 6 clades of COG1893COG name: Ketopantoate reductaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1893 is ao--kzyq--rlb-efg----j----Number of proteins in this genome belonging to this COG is 1","***** IPB003710 (Ketopantoate reductase ApbA/PanE) with a combined E-value of 6.2e-22. IPB003710A 15-37 IPB003710C 209-232 IPB003710D 281-302","Residues 113-246 are similar to a (OXIDOREDUCTASE BIOSYNTHESIS PANTOTHENATE NADP REDUCTASE 2-DEHYDROPANTOATE 2-REDUCTASE KETOPANTOATE KPA KPR) protein domain (PD007657) which is seen in Q6A928_PROAC.Residues 274-313 are 77% similar to a (OXIDOREDUCTASE BIOSYNTHESIS NADP PANTOTHENATE 2-DEHYDROPANTOATE REDUCTASE 2-REDUCTASE KETOPANTOATE KPA KPR) protein domain (PD527540) which is seen in Q6NI29_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 178 (E_value = 7.4e-29) place ANA_1088 in the ApbA family which is described as Ketopantoate reductase PanE/ApbA.Residues 203 to 329 (E_value = 7.6e-32) place ANA_1088 in the ApbA_C family which is described as Ketopantoate reductase PanE/ApbA C terminal.","","2-reductase (panE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1089","1167782","1167153","630","6.53","-2.14","22204","GTGACTGATCACCTGCATCCCCCGGCCAAGGGCCCGACGGCAAGGCCGAGCGCGGGCGGGACGGTCTTGGGAACTCCAGTCCTCGAGATCCGCCCGGCCACCGCCGTCCATGAACCCATCGGCTTCGCAACCGCACGCGGAGATGAGACAGGCCCCGAGGCCGACCGGCTTCGCACGGCCGTGGCCGACGTGCGCCTCGAGGTCTTCGTTGTTGAGCAGGCGGTTCCCTTCGCCCTGGAGATCGACGCTCGTGACGAGGAGCCGACTACGATCCATCTCCTGGCCAGCGGAGCTGACGGAACACCCCTGGGCGCCGGACGTCTCCTGATGGAGCCCGAACACCCCGGTCGGGTCCATCTGGGCCGCTTGGCTGTACGGAGCATCGTGCGCGGTACGGGGCTTGGTGCCCGCATCGTCGCTGCCCTCGAGCAGACTGCACTGAGCCACTCCGGCCGGTCCCGCGTGGAGGTGGTTCTCTCAGCTCAGGAGCAGGCCATGGGCTTCTATGAGCGCTGCGGATACCGGGTCCTCGATGGGCGCCGCTACCTCGACGCCGGCATCTGGCACCAGGACATGGCCCGCACCGTCAGTAGCGTGGGCGCCGAGGACCGTTCCGGCCGTACCGCCTAG","VTDHLHPPAKGPTARPSAGGTVLGTPVLEIRPATAVHEPIGFATARGDETGPEADRLRTAVADVRLEVFVVEQAVPFALEIDARDEEPTTIHLLASGADGTPLGAGRLLMEPEHPGRVHLGRLAVRSIVRGTGLGARIVAALEQTALSHSGRSRVEVVLSAQEQAMGFYERCGYRVLDGRRYLDAGIWHQDMARTVSSVGAEDRSGRTA$","GCN5-related N-acetyltransferase","Cytoplasm","B. subtilis YjcF protein homolog lmo0976","hypothetical protein","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[94-175]T$	Acetyltransf_1
PS51186	$\"[48-197]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[52-195]T$	no description

","BeTs to 9 clades of COG0454COG name: Histone acetyltransferase HPA2 and related acetyltransferasesFunctional Class: K [Information storage and processing--Transcription] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0454 is aompkzyqvdrlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","Residues 55-117 are 65% similar to a (TRANSFERASE ACETYLTRANSFERASE FAMILY GNAT ACYLTRANSFERASE ACETYLTRANSFERASE ELAA 2.3.1.- UPF0039 PROBABLE) protein domain (PD020491) which is seen in Q7WKX8_BORBR.","","-53% similar to PDB:1Q2Y Crystal structure of the protein YJCF from Bacillus subtilis: a member of the GCN5-related N-acetyltransferase superfamily fold (E_value = 1.9E_13);-51% similar to PDB:1XEB Crystal Structure of an Acyl-CoA N-acyltransferase from Pseudomonas aeruginosa (E_value = 3.3E_10);","Residues 94 to 175 (E_value = 8e-14) place ANA_1089 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","subtilis YjcF protein homolog lmo0976","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1090","1168733","1167813","921","5.94","-9.48","33015","ATGAGCGTGCGCCTGCTGCCCGTGCCCGACGGCTTCGACGGCGAACGGGTCGACGCTGCGCTGGCCCGGATGACGGGCCTGTCCCGCAGCCGGGTCGAGGACCTCTGCGAGGCCGGAGAGGTGCGCCGAGGCGGCGAGACGCTGGCCAAGTCCTCTCGTCTGCGCGCGGGGGAGCTCCTCGAGGTCGACCTGCCCGATCCCCGTCCCGTCGAACCGGTCGCCACTCCCGTGGAGGGCATGGAGCTGCTCTACGAGGACGAGGACATCGTCGTCGTCGACAAGCCCGCAGGCGTGGCCGCGCACCCCTCCATGGGATGGGACGGCCCAGACGTCCTTGGCGCCCTGAAAGCCATGCACGTGCGAGTGGCTACCTCCGGCGCTGCCGAGCGCCAGGGCATCGTCTCGCGCCTGGACGTGGGCACCTCGGGCGTCATGATCGTGGCCAAGGGGGAGCGGGCCTACTCGGTGCTCAAACGCGCCTTCCGGGAGCACACGGTGGACAAGGTCTACCACGCCCTGGTGCAGGGCCACCTCGACCCCTCCAGCGGCACCATCGACGCCCCCATCGGCCGTCACCCCAGCCGAGAGTGGAAGATGGCCATCATCGAGGGCGGGCGCGAGTCCATCACCCACTACGACGTCATCGAGGCGATGCCCGGGGCCTGCCTGGCCGAGATCCACCTCGAGACCGGGCGCACCCACCAGATCCGCGTCCACATGGCCGCCGTCGGCCACCCCTGCGTCGGAGACGCCACCTACGGCGCCGACCCGGCCATCAGTGCGCGCACCGGTCTGATCCGCCAGTGGCTCCACGCCCGCGAGCTCGGCATCGCCCACCCCATCACCGGCGAGCACATGGTCTTCACCTCCGACTACCCCGACGACCTAGTCCACGCTCTGGATGTGCTGCGCTTACCATGA","MSVRLLPVPDGFDGERVDAALARMTGLSRSRVEDLCEAGEVRRGGETLAKSSRLRAGELLEVDLPDPRPVEPVATPVEGMELLYEDEDIVVVDKPAGVAAHPSMGWDGPDVLGALKAMHVRVATSGAAERQGIVSRLDVGTSGVMIVAKGERAYSVLKRAFREHTVDKVYHALVQGHLDPSSGTIDAPIGRHPSREWKMAIIEGGRESITHYDVIEAMPGACLAEIHLETGRTHQIRVHMAAVGHPCVGDATYGADPAISARTGLIRQWLHARELGIAHPITGEHMVFTSDYPDDLVHALDVLRLP$","Pseudouridylate synthase, 23S rRNA-specific","Cytoplasm","Pseudouridine synthases, 23S RNA-specific","putative ribosomal large subunit pseudouridine synthase ","pseudouridine synthase, RluA family","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Aravind L., Koonin E.V. Novel predicted RNA-binding domains associated with the translation machinery. J. Mol. Evol. 1999. 48(3):291-302. PMID: 10093218","","","

InterPro
IPR002942
Domain

RNA-binding S4
PF01479	$\"[15-60]T$	S4
SM00363	$\"[15-78]T$	S4
PS50889	$\"[15-89]T$	S4

InterPro
IPR006145
Domain

Pseudouridine synthase
PD001819	$\"[134-176]T$	Q8NNQ0_CORGL_Q8NNQ0;
PF00849	$\"[88-242]T$	PseudoU_synth_2

InterPro
IPR006225
Domain

Pseudouridine synthase, RluD
TIGR00005	$\"[10-304]T$	rluA_subfam: pseudouridine synthase, RluA f

noIPR
unintegrated

unintegrated
PTHR10436	$\"[1-303]T$	RIBOSOMAL PSEUDOURIDINE SYNTHASE

","BeTs to 19 clades of COG0564COG name: Pseudouridylate synthases, 23S RNA-specificFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0564 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB006224 (Pseudouridine synthase, Rlu) with a combined E-value of 2.7e-51. IPB006224A 82-97 IPB006224B 134-172 IPB006224C 230-254 IPB006224D 267-280***** IPB000748 (Pseudouridine synthase, Rsu) with a combined E-value of 6e-08. IPB000748A 16-41 IPB000748C 134-166 IPB000748D 226-260***** IPB002942 (RNA-binding S4) with a combined E-value of 1.2e-07. IPB002942B 220-251","Residues 4-65 are 70% similar to a (SYNTHASE PSEUDOURIDINE LYASE RIBOSOMAL SUBUNIT LARGE PSEUDOURIDYLATE RV1540/MT1592/MB1567 HYDROLYASE URACIL) protein domain (PD845354) which is seen in Q9S2X8_STRCO.Residues 4-66 are 69% similar to a (SYNTHASE PSEUDOURIDINE LYASE LARGE RIBOSOMAL SUBUNIT) protein domain (PD879104) which is seen in Q8G7W2_BIFLO.Residues 6-97 are 56% similar to a (D SYNTHASE LYASE LARGE RIBOSOMAL SUBUNIT PSEUDOURIDINE) protein domain (PD982380) which is seen in Q74H11_GEOSL.Residues 67-133 are similar to a (SYNTHASE LYASE PSEUDOURIDINE PSEUDOURIDYLATE RV1540/MT1592/MB1567 HYDROLYASE SYNTHASE-LIKE URACIL LARGE RIBOSOMAL) protein domain (PD112933) which is seen in Q9S2X8_STRCO.Residues 73-117 are 80% similar to a (SYNTHASE PSEUDOURIDINE LYASE RIBOSOMAL LARGE SUBUNIT PSEUDOURIDYLATE C URACIL HYDROLYASE) protein domain (PD483014) which is seen in Q82AC6_STRAW.Residues 134-176 are 86% similar to a (SYNTHASE LYASE PSEUDOURIDINE RIBOSOMAL LARGE SUBUNIT PSEUDOURIDYLATE URACIL HYDROLYASE PROCESSING) protein domain (PD001819) which is seen in Q8NNQ0_CORGL.Residues 188-246 are similar to a (SYNTHASE LYASE PSEUDOURIDINE RIBOSOMAL LARGE SUBUNIT PSEUDOURIDYLATE URACIL HYDROLYASE PROCESSING) protein domain (PD350148) which is seen in Q6AE73_BBBBB.Residues 249-295 are 74% similar to a (SYNTHASE LYASE PSEUDOURIDINE RIBOSOMAL LARGE SUBUNIT PSEUDOURIDYLATE HYDROLYASE URACIL PROCESSING) protein domain (PD544685) which is seen in Q6AE73_BBBBB.","","-54% similar to PDB:1QYU Structure of the catalytic domain of 23S rRNA pseudouridine synthase RluD (E_value = 1.1E_43);-54% similar to PDB:1V9F Crystal structure of catalytic domain of pseudouridine synthase RluD from Escherichia coli (E_value = 1.1E_43);-54% similar to PDB:2IST crystal structure of RluD from E. coli (E_value = 1.1E_43);-56% similar to PDB:1PRZ Crystal structure of pseudouridine synthase RluD catalytic module (E_value = 3.2E_40);-51% similar to PDB:2I82 Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure (E_value = 3.4E_26);","Residues 15 to 60 (E_value = 0.0019) place ANA_1090 in the S4 family which is described as S4 domain.Residues 88 to 242 (E_value = 1.3e-52) place ANA_1090 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase.","","synthases, 23S RNA-specific","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1091","1169635","1168730","906","5.65","-5.64","31351","GTGACACGGCCTCCTACGAAGGGCGGCGACCCGCACGGGTCGCCGCCCTTCGCTGGGTGTATAGCCCATTCATCACACGTTCCCCTTCGAGTGCAATGCGAGAAAGCCCCCATGCCTGACCATGTCGATCCCGCCTCCCGTGTGGAGGAGGCCGCTGACAACGTCGGTAACGCCGTCGACTCCGACAACGTTGTCCCACCGCCCACAGACAATCCCCTCAGCGCCATGGATGAAGCCCTGACGTCGCCGGCGGCAGATGGGAAGCGATCCAAACGTCTTCCGGTGATCGTCCTGTGGCTGGTGGCGCTCATCGTCATCGTCGTGGACCAGGTCACCAAGCAGTGGGCGCTTTCCGCGCTGTCCGACGGTCGGCACACGGCGCTGCTCGGCCGTGCCCTGGGGCTGGTCCTGGTACGCAACCCGGGCGCCGCCTTCTCCTTCGCCACCGGACAGACGTGGATCTTCGCACTCATCGCGTCTTTCGTTGTGGCCATCATCATCCGTGTCTCCCGGAACCTGGCGTCCCGCTCCTGGGCGGTGGCCCTCGGGCTGGTTCTCGGTGGGGCGGTCGGCAACCTCATCGACCGCCTTCTGCGGGAGCCCGGATTCCTACGTGGCCACGTCATCGACTTCATTGACTACGGCGGCTACTTCGTGGGCAATGTCGCCGACATCGCCATCGTGGCGGCCGCCGCGGGCATCATCATTCTGTCCCTGGGAGGCTGGGAGATCGACGGCACACGGGCCGGTGCCGTGGACAACCCGGAGGTGGAGGCTACCGACGGATCGACCTCCTCAGCCGACCGAGGCACTCGAGCCCGCCGAAGGGATCGCGCCGAGGCGCCCATAGAGTCGGAAGAGTCCGCCGGGGCATCGACGCAGGGTTCCTCTGCGGAGTTGCCATGA","VTRPPTKGGDPHGSPPFAGCIAHSSHVPLRVQCEKAPMPDHVDPASRVEEAADNVGNAVDSDNVVPPPTDNPLSAMDEALTSPAADGKRSKRLPVIVLWLVALIVIVVDQVTKQWALSALSDGRHTALLGRALGLVLVRNPGAAFSFATGQTWIFALIASFVVAIIIRVSRNLASRSWAVALGLVLGGAVGNLIDRLLREPGFLRGHVIDFIDYGGYFVGNVADIAIVAAAAGIIILSLGGWEIDGTRAGAVDNPEVEATDGSTSSADRGTRARRRDRAEAPIESEESAGASTQGSSAELP$","Lipoprotein signal peptidase","Membrane, Cytoplasm, Extracellular","signal peptidase II","lipoprotein signal peptidase ","lipoprotein signal peptidase","","Szecsi P.B. The aspartic proteases. Scand. J. Clin. Lab. Invest. Suppl. 1992. 210:5-22. PMID: 1455179Rawlings N.D., Barrett A.J. Families of aspartic peptidases, and those of unknown catalytic mechanism. Meth. Enzymol. 1995. 248:105-120. PMID: 7674916Tokunaga M., Loranger J.M., Wu H.C. Prolipoprotein modification and processing enzymes in Escherichia coli. J. Biol. Chem. 1984. 259(6):3825-3830. PMID: 6368552","","","

InterPro
IPR001872
Family

Peptidase A8, signal peptidase II
PD004304	$\"[140-222]T$	Q740U2_MYCPA_Q740U2;
PR00781	$\"[140-148]T$ $\"[182-197]T$ $\"[220-236]T$	LIPOSIGPTASE
PF01252	$\"[96-245]T$	Peptidase_A8
TIGR00077	$\"[89-248]T$	lspA: signal peptidase II
PS00855	$\"[185-197]T$	SPASE_II

noIPR
unintegrated

unintegrated
tmhmm	$\"[93-111]?$ $\"[143-163]?$ $\"[178-198]?$ $\"[217-239]?$	transmembrane_regions

","BeTs to 7 clades of COG0597COG name: Lipoprotein signal peptidaseFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0597 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001872 (Signal peptidase II, family A8) with a combined E-value of 6e-28. IPB001872A 101-113 IPB001872B 132-150 IPB001872C 181-204 IPB001872D 217-235","Residues 140-222 are similar to a (SIGNAL PEPTIDASE PROTEASE LIPOPROTEIN HYDROLASE TRANSMEMBRANE ASPARTYL II PROLIPOPROTEIN SPASE) protein domain (PD004304) which is seen in Q740U2_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 96 to 245 (E_value = 1.7e-33) place ANA_1091 in the Peptidase_A8 family which is described as Signal peptidase (SPase) II.","","peptidase II (lspA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1092","1170379","1169771","609","4.79","-13.29","22074","ATGACGCTGCTGACAGCAGACGACGTCCTCAACAAGAAGTTCCAGGCGACCAAGTTCCGTGAGGGCTACGAGCAGGACGAGGTCGACGAGTTCCTCGACGAGGTAGTCGAGGCCATGCGTCAGCTGGAGGCTGAGAACGCCGACCTCAAGGCCAAGCTCGAGGCCGCCAACCGTCGAGTTGCCCAGCTCGGCGAGGGAGCTGCCATCCCCTCCGCCCCCGCTTCCCCCGTATCTCCGGTCCAGGCAGAGCCCGCCATGTCCATGCCGGCCGTCGCTGCCGGCGAGACCGGCGGCCAGGGCCCGGCTGCTGCCTCCGGCATGCTCGAGCTGGCCCAGCGCCTCCACGACGAGCACGTCGCCAACGGCAAGGCCGAGGGTGAGCGCATCGTCACCGAGGCCCGCTCCACCGGTGAGCAGATCGTGCGAGAGGCTGAGGACCAGCGCAACCGCACCCTCGCCCAGCTGGAGAAGGAGCGCGCCAACCTCGAGCACAAGATCGACGAGCTGCGGCGCTTCGAGTCCGACTACCGCACTCGCCTCAAGAGCTACCTGCAGAACCTGCTGGCCAACGTCGAGGACGGCGGAGAGAGCTCCATCTCCAGCCTGTGA","MTLLTADDVLNKKFQATKFREGYEQDEVDEFLDEVVEAMRQLEAENADLKAKLEAANRRVAQLGEGAAIPSAPASPVSPVQAEPAMSMPAVAAGETGGQGPAAASGMLELAQRLHDEHVANGKAEGERIVTEARSTGEQIVREAEDQRNRTLAQLEKERANLEHKIDELRRFESDYRTRLKSYLQNLLANVEDGGESSISSL$","Cell division protein DivIVA","Cytoplasm","cell division protein DivIVA-like protein","hypothetical protein","DivIVA family protein","","Cha J.H., Stewart G.C. The divIVA minicell locus of Bacillus subtilis. J. Bacteriol. 1997. 179(5):1671-1683. PMID: 9045828","","","

InterPro
IPR007793
Family

DivIVA
PF05103	$\"[1-196]T$	DivIVA

","BeTs to 3 clades of COG2811COG name: Archaeal/vacuolar-type H+-ATPase subunit HFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2811 is aompk----d----------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 94-192 are similar to a (DIVISION CELL DIVIVA-LIKE) protein domain (PD709768) which is seen in Q83MU1_TROWT.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 196 (E_value = 8.5e-10) place ANA_1092 in the DivIVA family which is described as DivIVA protein.","","division protein DivIVA-like protein (CIE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1094","1170841","1170545","297","11.54","4.91","11002","GTGAACCTTGTCTCCGCGGTAGCCGGGATCCTGTCGAGCATTCTGAGCCTGTACTTCCTCATCCTCCTGGTCAGGGTTGTGCTCGACTGGATTCAGGTCTTCGCCCGCCAGTGGCGCCCCCGGGGGATCGTCCTGGTGCTGGCCAACCTTGTCTACGCTCTGACGGATCCGCCTCTGCGAGTGATCCGTCAGAGGGTTCCCCTGGCACGCCTGGGAGGGGTCGGTATCGACCTGAGCTTCCTGGTCCTGGTCTTCGGGATCTGGATCATCCAGTGGTTCCTCGGACTTCTCATCTGA","VNLVSAVAGILSSILSLYFLILLVRVVLDWIQVFARQWRPRGIVLVLANLVYALTDPPLRVIRQRVPLARLGGVGIDLSFLVLVFGIWIIQWFLGLLI$","Hypothetical protein","Membrane, Cytoplasm","YGGT family, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[74-94]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 24-91 are 61% similar to a (MEMBRANE YGGT INTEGRAL FAMILY TRANSMEMBRANE RESISTANCE YCF19 CHLOROPLAST YLMG PROTEIN) protein domain (PD005585) which is seen in Q6A9P6_PROAC.Residues 24-91 are similar to a (MEMBRANE TRANSMEMBRANE POSSIBLE) protein domain (PD823524) which is seen in Q8G7W5_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","family, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1095","1171318","1170854","465","4.40","-16.31","16812","ATGGGCGCGCTGCGCAGTATGACCAGTTTCCTCGGCTACTCGGAGCCGGAGGAGGAGACCTACGAGGACAGCTATGAGGCTGCCGACGCGGGTTACGCCGTGCAGGAGCACGAGCAGGACTTCAGCGACGAGGGGTACGAGGACTTCTCTGCTCCGGCTGTGCCCGAGCCCGTTGCTGCCGCCCCCGACCTTCGCCGTATCGTCACGGTTCACCCCTCGACCTACAACGAGGCCAGGATCATCGGTGAGTCCTTTCGTGACGGCGTCCCCGTCATCATCAACCTTACTGGTATGAGCGAGTCTGACGCGCGTCGCATGGTGGACTTCTCCGCCGGTCTGGTCTTCGGATTGCACGGTGCTATTGAGCGTGTCACTCCGCGGGTGTTCCTACTGACCCCGGCCAGCGTGGAGATCGACGGCGGTGAGGTCGCCGAGGCCCGCGGTCGCTTCTTCAACCAGAGCTGA","MGALRSMTSFLGYSEPEEETYEDSYEAADAGYAVQEHEQDFSDEGYEDFSAPAVPEPVAAAPDLRRIVTVHPSTYNEARIIGESFRDGVPVIINLTGMSESDARRMVDFSAGLVFGLHGAIERVTPRVFLLTPASVEIDGGEVAEARGRFFNQS$","Uncharacterized conserved protein","Cytoplasm","Uncharacterized BCR","hypothetical protein","protein of unknown function DUF552","","","","","

InterPro
IPR007561
Family

Protein of unknown function DUF552
PF04472	$\"[62-141]T$	DUF552

noIPR
unintegrated

unintegrated
PD312742	$\"[64-138]T$	Q6A9P7_PROAC_Q6A9P7;

","BeTs to 4 clades of COG1799COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1799 is ----------rlbc------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 64-138 are similar to a (YLMF CYTOSOLIC YCF50 UNCHARACTERIZED DIVISION CELL B.SUBTILIS LIN2136 SPR1508 YAK) protein domain (PD312742) which is seen in Q6A9P7_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 62 to 141 (E_value = 1.1e-33) place ANA_1095 in the DUF552 family which is described as Protein of unknown function (DUF552).","","BCR (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1096","1172285","1171470","816","5.33","-7.85","28167","ATGTGCGATACCACCGCCGTTGAGGCCTCGGACCTGATCGAAGTGGATTTGGGCCCGCGGGCTCGTGGGTACTTCACTACCCGCGGTCTGCGGGCCCTTCCCGTCTCGGCCCCGGGTGGCGGCGCTCAGGACCGGGGTGCGGAGCGCGAGGGAGGGGCCTCCTATGACGGGTGGAACCTGGCGCTTCACGTCGGGGACGACCCGCAACGTGTTCAATGTCATCGTCGTCGGCTCGAGGAGCTGCTCGGGCTCGAGCAGGGGCGTCACCTGGCCTGGATGAACCAGGTTCACTCCGCCGTCGTGGCCACGGCCCAGGCCGGTGAGGTGCCCACGGCGGATGCGCTCGTGCTGGACTCCCGGACAGGCGGGGCGCCCGCGGGTTGCTGCGTTCTCGTGGCCGACTGCGTCCCTGTCCTGCTGGCGTCCGGGGACGGTGCTCTGACGGCCGCAGTGCACGCCGGGCGGAGAGGCATGCTCGACGGCGTCGTGCCTGCCACGATCGATTCCCTCCGACGCGGTGGAGTGGAGCCGGCGGATCTGTGGGCCGCCGTGGGGCCGTCGATCTGCGGCTCCTGCTACGAGGTCCCCGAGGAGATGCTTGTACTGTCCGCTCAGCGCGAACCGGCATGCGCTTCGAGCACATCGTGGGGAACGCCTGGCATCGACGTCGCCGCAGGCGTCCTCGCTCAGCTCGAGCGTGCCGGTGTTGGTCACATCAGTGCTGGTCAATGGTGCACCTATGAGGACCCTCGCTTCTTCTCCTATCGGCGTGATGGAGTGACGGGACGCCTGGCAGGCGTTGGAGTTCCGCGATAG","MCDTTAVEASDLIEVDLGPRARGYFTTRGLRALPVSAPGGGAQDRGAEREGGASYDGWNLALHVGDDPQRVQCHRRRLEELLGLEQGRHLAWMNQVHSAVVATAQAGEVPTADALVLDSRTGGAPAGCCVLVADCVPVLLASGDGALTAAVHAGRRGMLDGVVPATIDSLRRGGVEPADLWAAVGPSICGSCYEVPEEMLVLSAQREPACASSTSWGTPGIDVAAGVLAQLERAGVGHISAGQWCTYEDPRFFSYRRDGVTGRLAGVGVPR$","Uncharacterized conserved protein","Cytoplasm","DUF152","K05810 conserved hypothetical protein","protein of unknown function DUF152","","","","","

InterPro
IPR003730
Family

Protein of unknown function DUF152
PF02578	$\"[53-270]T$	DUF152

noIPR
unintegrated

unintegrated
G3DSA:3.60.140.10	$\"[23-267]T$	no description

","BeTs to 15 clades of COG1496COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1496 is -------q-dr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003730 (Protein of unknown function DUF152) with a combined E-value of 4.8e-39. IPB003730B 91-102 IPB003730C 117-157 IPB003730D 184-195 IPB003730E 233-246 IPB003730F 248-266","Residues 130-266 are similar to a (UPF0124 YFIH CYTOSOLIC DUF152 BH2551 3_apos;REGION FAMILY FTSZ YLMD HI0175) protein domain (PD006200) which is seen in YK81_STRCO.","","-49% similar to PDB:1RV9 Crystal Structure of a hypothetical protein NMB0706 (E_value = 1.3E_26);-46% similar to PDB:1RW0 Crystal Structure of Hypothetical protein yfiH (E_value = 2.4E_20);-44% similar to PDB:1U05 Crystal Structure of Conserved Hypothetical Protein (E_value = 2.0E_19);-44% similar to PDB:1XAF Crystal Structure of Hypothetical Protein YfiH from Shigella flexneri 2a str. 2457T (E_value = 2.0E_19);-43% similar to PDB:1Z9T Crystal structure of Hypothetical UPF0124 protein yfiH (np_417084.1) from Escherichia coli K12 at 1.54 A resolution (E_value = 9.9E_19);","Residues 53 to 270 (E_value = 1.2e-32) place ANA_1096 in the DUF152 family which is described as Uncharacterised ACR, YfiH family COG1496.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1097","1173685","1172315","1371","4.49","-34.26","46691","ATGACGAAACTCGCGGAGGGGACGCCAGTGGTCGAGAGCATGGCTGTGGACGACTCACAGCACTACCAGGCAGAGATCAAGGTCGTCGGTGTTGGCGGAGGCGGCGTTAACGCCGTCAACCGCATGATCGAGGCCGATCTGCGTGGCGTGGAGTTCATCGCCGTGAACACCGACGCCCAGGCGCTGCTCATGTCCGACGCTGACGTCAAGCTCGACGTCGGGCGGGACCTGACCCGAGGTCTGGGGGCGGGAGCCGACCCGGCGATCGGCCGCAAGGCCGCAGAGGACCACGAGTCTGAGATCCGCGAGGCCCTCGACGGCTCGGACATGGTCTTCGTCACCGCGGGTGAAGGGGGCGGTACCGGCACCGGAGCGGCCCCCGTCGTCGCCCGCCTGGCCAAGAGCATTGGCGCGCTGACCATCGGTGTGGTCACCCGTCCCTTCTCCTTCGAGGGGCGCCGCCGCTCGGCCCAGGCTGAGGACGGTGTCCAGGCGCTGCGCGAGGAAGTCGACACCCTCATCGTCATCCCCAATGACCGCCTCCTGCAGATCGCCGACAAGAACATCTCCGTCGTTGACGCCTTCAAGCAGGCCGACCAGGTTCTTCTTCAGGGTGTCCAGGGCATCACCGAGCTCATCACCACCCCCGGTCTCATTAACGTCGACTTCAACGATGTCAAGTCCGTCATGCAGGGTGCCGGCAGCGCTCTCATGGGTATTGGCTCGGCCACCGGCGAGGGGCGTGCGATCACGGCGACCGAGGAGGCCATCGCCTCGCCGTTGCTGGAGACCTCGATCGACGGCGCACACGGTGTGCTGCTCTTCTTCCAGGGCGGTTCCGACCTGGGCCTGTTCGAGATGAACGAGGCCGCCAACCTCGTGCGCGAGGCTGTCCACCCCGAGGCCAACATCATCGTCGGAAACGTGGTCGACGGTGCCCTGGGCGACGAGGTGCGGGTGACGGTCATCGCCGCCGGCTTCGACTCCGAGCCGATCGTCGGCGGCCTGGCCGATCCGATGACTCGGCTGTCGCGGGCTGCCGCCGTGCCGCCGGTGCCCTCCTCCCCGGTCGATGACCTGCCTCCGGCCCCCGCTCCTCGCGGTGGCGCTCATGCCGCCCAGAACCCGGTGACTCGTCCGGTCCCGCTGGCACCTCCGCCCTCCGCCTCACCGGCGGTCGCGGCGCACCTGTCGGAGGTCAGTGCGGCTGAGGCCCTCTCCTCGGGGAGCATGCCGGCCTATGTGGATGAGTCCTACGGCTCCTACGGCTCGGTGCCTGCACAGCACTCGGTCTCCGAGCTTGAGGTTCCTCAGGTGATCGGGGTTGACGCCGACGATGATGGCATCGACCTGCCCGACTTCCTGCGCTGA","MTKLAEGTPVVESMAVDDSQHYQAEIKVVGVGGGGVNAVNRMIEADLRGVEFIAVNTDAQALLMSDADVKLDVGRDLTRGLGAGADPAIGRKAAEDHESEIREALDGSDMVFVTAGEGGGTGTGAAPVVARLAKSIGALTIGVVTRPFSFEGRRRSAQAEDGVQALREEVDTLIVIPNDRLLQIADKNISVVDAFKQADQVLLQGVQGITELITTPGLINVDFNDVKSVMQGAGSALMGIGSATGEGRAITATEEAIASPLLETSIDGAHGVLLFFQGGSDLGLFEMNEAANLVREAVHPEANIIVGNVVDGALGDEVRVTVIAAGFDSEPIVGGLADPMTRLSRAAAVPPVPSSPVDDLPPAPAPRGGAHAAQNPVTRPVPLAPPPSASPAVAAHLSEVSAAEALSSGSMPAYVDESYGSYGSVPAQHSVSELEVPQVIGVDADDDGIDLPDFLR$","Cell division protein FtsZ","Cytoplasm","Cell division protein ftsZ","cell division protein FtsZ","cell division protein FtsZ","","Lutkenhaus J. FtsZ ring in bacterial cytokinesis. Mol. Microbiol. 1993. 9(3):403-409. PMID: 8412689Erickson H.P. FtsZ, a prokaryotic homolog of tubulin?. Cell 1995. 80(3):367-370. PMID: 7859278Addinall S.G., Holland B. The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis. J. Mol. Biol. 2002. 318(2):219-236. PMID: 12051832Osteryoung K.W., Vierling E. Conserved cell and organelle division. Nature 1995. 376(6540):473-474. PMID: 7637778Margolin W., Wang R., Kumar M. Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin. J. Bacteriol. 1996. 178(5):1320-1327. PMID: 8631708","","","

InterPro
IPR000158
Family

Cell division protein FtsZ
PR00423	$\"[72-90]T$ $\"[110-130]T$ $\"[138-159]T$ $\"[201-223]T$ $\"[224-245]T$ $\"[268-286]T$	CELLDVISFTSZ
TIGR00065	$\"[12-355]T$	ftsZ: cell division protein FtsZ
PS01134	$\"[56-90]T$	FTSZ_1
PS01135	$\"[109-130]T$	FTSZ_2

InterPro
IPR003008
Domain

Tubulin/FtsZ, GTPase
PF00091	$\"[24-217]T$	Tubulin

InterPro
IPR008280
Domain

Tubulin/FtsZ, C-terminal
PF03953	$\"[219-345]T$	Tubulin_C

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.20	$\"[237-343]T$	no description
G3DSA:3.40.50.1440	$\"[13-232]T$	no description

","BeTs to 23 clades of COG0206COG name: Cell division GTPaseFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0206 is aompk--qvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 1","***** IPB000158 (Cell division protein FtsZ) with a combined E-value of 9.6e-105. IPB000158A 38-89 IPB000158B 105-152 IPB000158C 206-259 IPB000158C 167-220","Residues 37-113 are 56% similar to a (DIVISION CHLOROPLAST GTP-BINDING CMFTSZ2-2) protein domain (PDA142G3) which is seen in Q76DQ3_CYAME.Residues 37-216 are similar to a (GTP-BINDING MICROTUBULE TUBULIN DIVISION CELL CHAIN FAMILY MULTIGENE FTSZ BETA) protein domain (PD000099) which is seen in FTSZ_STRGR.Residues 42-113 are 58% similar to a (DIVISION CELL FTSZ) protein domain (PD710075) which is seen in Q8RT91_MYCHO.Residues 44-196 are 48% similar to a (DIVISION CELL FTSZ SEPTATION GTP-BINDING) protein domain (PD824296) which is seen in FTSZ_MYCPN.Residues 48-113 are 72% similar to a (DIVISION CELL FTSZ) protein domain (PDA142G2) which is seen in Q7VI30_HELHP.Residues 50-87 are 97% similar to a (CELL DIVISION FTSZ GTP-BINDING SEPTATION CYCLE HOMOLOG MITOCHONDRIAL DICTYOSTELIUM MULTIGENE) protein domain (PD245129) which is seen in Q73YR1_MYCPA.Residues 89-214 are 68% similar to a (CELL DIVISION SEPTATION GTP-BINDING NEQ473 CYCLE) protein domain (PDA1A9E1) which is seen in Q74M90_NANEQ.Residues 159-217 are 72% similar to a (FTSZ) protein domain (PD931213) which is seen in Q6QWI1_BBBBB.Residues 218-263 are 84% similar to a (DIVISION CELL FTSZ GTP-BINDING SEPTATION PLASTID HOMOLOG CYCLE FAMILY MULTIGENE) protein domain (PD001349) which is seen in Q83NQ0_TROW8.","","-79% similar to PDB:1RLU Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S (E_value = 4.9E_115);-79% similar to PDB:1RQ2 MYCOBACTERIUM TUBERCULOSIS FTSZ IN COMPLEX WITH CITRATE (E_value = 4.9E_115);-79% similar to PDB:1RQ7 MYCOBACTERIUM TUBERCULOSIS FTSZ IN COMPLEX WITH GDP (E_value = 4.9E_115);-63% similar to PDB:1OFU CRYSTAL STRUCTURE OF SULA:FTSZ FROM PSEUDOMONAS AERUGINOSA (E_value = 4.8E_70);-59% similar to PDB:1W5E FTSZ W319Y MUTANT, P1 (M. JANNASCHII) (E_value = 8.9E_64);","Residues 24 to 217 (E_value = 1.1e-95) place ANA_1097 in the Tubulin family which is described as Tubulin/FtsZ family, GTPase domain.Residues 219 to 345 (E_value = 7.7e-28) place ANA_1097 in the Tubulin_C family which is described as Tubulin/FtsZ family, C-terminal domain.","","division protein ftsZ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1098","1175187","1173955","1233","11.50","23.94","43028","ATGAGGAAGCCCTCGGCCCCCCGTCCTGAGCGCTCCAACCGTGCTCAGGACGCCCCGGCCAGCATCCCGCCGCGCCGCTCCGGCCCCAGGCGTCCGCGTCCCTCCCGCTCGGCGCAGGGACCATCCGCGCCGAGCACCCCGACGGATCACAGGACCGAGCAGGCCGGGCCGGCGGCCCCCGCCAAGCGGCCCCGGAGCGCTTCCGCCAGGGCCCCCAAGGAGCCGAGCGGCAGCGCCGGGTCAGCCTCGCGACCCAGGCGTCCGTCGACGTCGAGGAGCGCGTCCAGCTCCTCGCCGGCTCCGCGTCGCGGTGGCGAGAGCGCCGGCCGCACCAGCCCCCGCCAGGACTCCTCCAGCCCCGACGCGGCGGCGAGCACCGAGCTGACCGTCTTCGGCCGCAGGCAGGTGGCTCTTCCCGGTAGAGACGACCGGGTCGTCTCCACCGGCCTGGCCGATCGGCTCAAGGAGCGTCAGGCCGCCCTGCGCCAGTTGCGGCTGCGACGGGTGGTGAGGGCCGCCGTCGTGGTGGTCGCCATCGTCCTGGTGGTCTGGGCCCTGGCCTTCTCACCCCTCCTGGGCCTGCAGACCCAGAGGATTTCCGTGGCCGGATCGGACGGCAGCGTCTCGGACAAGCAGGTCCGCGAGGTTCTGGCCGCCTACGAGGGCGACTCGTTGCTGCGGCTGGATACCGGCCGGCTCTCCACCCAGGTCAGCGACAAGCTGGTCCGGGTGCGCTGGGCGCAGGTGACCAGGGCTTGGCCCCACGGGCTGCGGGTGCACCTGACGATGCGCGTGCCGGTGGCCACCGTGCAGGACTCGGACGGCTACCAGGTCCTCGACAACGAGGCCGTGGTCCTCGAGCGGGTCTCCGAGCCGCCATCAGGCCTGGTGAACATCGTGCCCGATCCCGCCGCGCAGGCATCGGGGCCACAGAGGATCTCCGCCAAGCAGGTCGCCGCTGTCACCCAGGTGGTGGGCTCCCTCACGCCGGAGACTCTGGCCCAGGTGAGCAGCGGCAGCGCCACTGAGGCGGGGCAGGTCACACTGACCTTGTCCAGCGGGGCCAGCGTGGTCTGGGGGAACAATCAGGACAACGCGCTCAAGGCGCGCGTCCTGGCGACTCTCATGACCACCACCGCATCGATTTACGACGTCTCCTCACCGCATCGCCCCACCACACGATCCGCCGACGCAGCGGCCACGACCACCGCGGCGCCATCGCCGACGTCCTGA","MRKPSAPRPERSNRAQDAPASIPPRRSGPRRPRPSRSAQGPSAPSTPTDHRTEQAGPAAPAKRPRSASARAPKEPSGSAGSASRPRRPSTSRSASSSSPAPRRGGESAGRTSPRQDSSSPDAAASTELTVFGRRQVALPGRDDRVVSTGLADRLKERQAALRQLRLRRVVRAAVVVVAIVLVVWALAFSPLLGLQTQRISVAGSDGSVSDKQVREVLAAYEGDSLLRLDTGRLSTQVSDKLVRVRWAQVTRAWPHGLRVHLTMRVPVATVQDSDGYQVLDNEAVVLERVSEPPSGLVNIVPDPAAQASGPQRISAKQVAAVTQVVGSLTPETLAQVSSGSATEAGQVTLTLSSGASVVWGNNQDNALKARVLATLMTTTASIYDVSSPHRPTTRSADAAATTTAAPSPTS$","Cell division protein FtsQ","Membrane, Periplasm, Extracellular","Cell division protein ftsQ homolog","K03589 cell division protein FtsQ","Polypeptide-transport-associated domain protein, FtsQ-type","","Sanchez-Pulido L., Devos D., Genevrois S., Vicente M., Valencia A. POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem. Sci. 2003. 28(10):523-526. PMID: 14559180","","","

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[97-168]T$	no description

InterPro
IPR013685
Domain

Polypeptide-transport-associated, FtsQ-type
PF08478	$\"[194-264]T$	POTRA_1

noIPR
unintegrated

unintegrated
tmhmm	$\"[172-192]?$	transmembrane_regions

","BeTs to 6 clades of COG1589COG name: Cell division septal proteinFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1589 is ---------drlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB005548 (Cell division protein FtsQ) with a combined E-value of 5.3e-06. IPB005548 242-271","Residues 197-284 are 57% similar to a (DIVISION CELL FTSQ TRANSMEMBRANE SEPTATION HOMOLOG DIVIB INNER MEMBRANE SEPTUM) protein domain (PD467902) which is seen in FTSQ_STRCO.Residues 320-388 are 53% similar to a (DIVISION CELL FTSQ HOMOLOG SEPTATION TRANSMEMBRANE FTSQ-FAMILY) protein domain (PD665221) which is seen in FTSQ_MYCTU.","","-43% similar to PDB:1J1Z Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with substrate (E_value = );-43% similar to PDB:1J20 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with product (E_value = );-43% similar to PDB:1J21 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with ATP and citrulline (E_value = );-43% similar to PDB:1KH1 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase (E_value = );-43% similar to PDB:1KH2 Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with ATP (E_value = );","Residues 194 to 264 (E_value = 1e-08) place ANA_1098 in the POTRA_1 family which is described as POTRA domain, FtsQ-type.","","division protein ftsQ homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1099","1176758","1175184","1575","5.14","-22.87","53754","ATGACCGCCACGACACCCCAGGACATCCCCCGCACTGCCGACCGGCCGGCCGGCGCCGATCAGCGCACACTGGCAGACAGAGCCTTTCACCTCATTGGCATCGGGGGAGCGGGGATGAGCGTGGTCGCCCAGCTGCTCGCCGCCCGCGGCGCCCGAGTATCCGGCTCCGACGCCCACGGGGGCCCCGCCTTCGACAACCTGGCCGATCTGGGCATCACGACCCACCTGGGGCATGACGCCGCGAATGTGCCCGAGCGGAGCACCGTCGTGGTGTCCACCGCGATCAAGGAGACCAACCCTGAGCTCGCCCAGGCCCGCAGGCGGGATCAGGAGATCATCCACCGGTCCCAGGCTCTGGCGCTGGCCGCTCAGGGCCTGGATTTCGTCGCCGTGGCGGGGGCGCACGGCAAGACCACGACCTCGGGCATGCTCGCCGAGGCCCTCACCGAGGCCGGAGCCGACCCCTCCTTCGCCATCGGCGGGGTCGTGCGGGCCCTGGGCACCGGCGCCCACCTGGGCGGCGGCCCCGCACTGGTTGCCGAGGCCGATGAGTCCGACCGCTCCTTCCTCAACTACACCCCCCGCGTGGAGATCGTCACCAACGTCGAGCCCGACCACCTCGACAGCTACGGCACCGCGGAGGCCTTCGAGACGGCATTCGTCGACTTCGCTCACCGGCTGGTGCCCGGGGGCCTGCTGGTCGCCTGCGCCGCCGACGCCGGCGCACTGCGCCTGGCGCAGTCCGCAGCCGCCGAGGGCCTGCGCGTCGTCACCTACTCCTTCGCAGGCCCCGACACCCTCCCCGGCGGAGTGCTCGTGGGGGAGGGGCACGTCCACCTGGACATCCAGGAACGCGGGGCCTCATCCACTCGGGGGCTGCTGACCCTCACCAAGGCGACTGGCCGCGAGCCCGCCGGCGGTGTGGGTGAGGAGGCGCATCTTGGCCCGGTGGAGCTGGTGCTGGCCGTTCCGGGTGACCACGTGGCCCTTGACGCCGCCGGCGCCTGGGCAGCGGGCATCGAGCTCGGCGTCGAACCGGCCCTGATGGCCCGGGCGCTGGGGGCCTTCGGGGGGACAGGACGGCGCTTCGAGGACCGGGGCGAGGCTGACGGCGTGCGCGTCATCGACGACTACGCCCACCACCCCACGGAGATCGAGGCCCTGCTGCGCACGGCGCGGGGCGTGGCCCAGGAGCGCGGCGGCCGGGTCCTGGTCCTGTTCCAGCCGCATCTGTTCTCCCGCACCCGGGCCTTCGCCGACCGCTTCGGACAGGCGCTGGCCCTGGCCGACGCCGTTGTCATCACTGACGTCTACCCCGCCAGGGAGACTCAGGCGGACTTCCCCGACATCACCGGGGACACGGTCGCCCAGCGCGTCCCCGGTGGCACCGCCAGGTTCGTCGCCGAGCGTCTTGAGGCCGCGCACGCGGTGGCCGACCTGGCGCGCCCGGGCGACCTGCTGCTGACAGTCGGTGCCGGCGACGTCACTGAGCTCGCCGGTACGGTACTGGGCGACCTGGCGGCACGCGAGGGCGGTGCAGCCCCCTCGCCCGCCGACCGGGACGAGCAGGCATGA","MTATTPQDIPRTADRPAGADQRTLADRAFHLIGIGGAGMSVVAQLLAARGARVSGSDAHGGPAFDNLADLGITTHLGHDAANVPERSTVVVSTAIKETNPELAQARRRDQEIIHRSQALALAAQGLDFVAVAGAHGKTTTSGMLAEALTEAGADPSFAIGGVVRALGTGAHLGGGPALVAEADESDRSFLNYTPRVEIVTNVEPDHLDSYGTAEAFETAFVDFAHRLVPGGLLVACAADAGALRLAQSAAAEGLRVVTYSFAGPDTLPGGVLVGEGHVHLDIQERGASSTRGLLTLTKATGREPAGGVGEEAHLGPVELVLAVPGDHVALDAAGAWAAGIELGVEPALMARALGAFGGTGRRFEDRGEADGVRVIDDYAHHPTEIEALLRTARGVAQERGGRVLVLFQPHLFSRTRAFADRFGQALALADAVVITDVYPARETQADFPDITGDTVAQRVPGGTARFVAERLEAAHAVADLARPGDLLLTVGAGDVTELAGTVLGDLAAREGGAAPSPADRDEQA$","UDP-N-acetylmuramate--alanine ligase","Cytoplasm","UDP-N-acetylmuramate--alanine ligase","UDP-N-acetylmuramate--alanine ligase ","UDP-N-acetylmuramate--alanine ligase","","Kisker C., Schindelin H., Rees D.C. Molybdenum-cofactor-containing enzymes: structure and mechanism. Annu. Rev. Biochem. 1997. 66:233-267. PMID: 9242907Kletzin A., Adams M.W. Tungsten in biological systems. FEMS Microbiol. Rev. 1996. 18(1):5-63. PMID: 8672295White H., Strobl G., Feicht R., Simon H. Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes. Eur. J. Biochem. 1989. 184(1):89-96. PMID: 2550230Trautwein T., Krauss F., Lottspeich F., Simon H. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. Eur. J. Biochem. 1994. 222(3):1025-1032. PMID: 8026480Mukund S., Adams M.W. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 1995. 270(15):8389-8392. PMID: 7721730Ma K., Hutchins A., Sung S.J., Adams M.W. Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(18):9608-9613. PMID: 9275170Chan M.K., Mukund S., Kletzin A., Adams M.W., Rees D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 1995. 267(5203):1463-1469. PMID: 7878465","","","

InterPro
IPR000713
Domain

Cytoplasmic peptidoglycan synthetase, N-terminal
PF01225	$\"[28-127]T$	Mur_ligase

InterPro
IPR003778
Domain

Allophanate hydrolase subunit 2
SM00797	$\"[231-483]T$	no description

InterPro
IPR004101
Domain

Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875	$\"[359-447]T$	Mur_ligase_C

InterPro
IPR005758
Family

UDP-N-acetylmuramate--alanine ligase
TIGR01082	$\"[28-503]T$	murC: UDP-N-acetylmuramate--alanine ligase

InterPro
IPR012237
Family

UDP-N-acetylmuramate-alanine ligase
PIRSF001562	$\"[27-503]T$	UDP-N-acetylmuramate-alanine ligase

InterPro
IPR013221
Domain

Mur ligase, middle region
PF08245	$\"[129-265]T$	Mur_ligase_M

InterPro
IPR013982
Domain

AICARFT/IMPCHase bienzyme, formylation region
SM00798	$\"[88-299]T$	no description

InterPro
IPR013983
Domain

Aldehyde ferredoxin oxidoreductase, N-terminal
SM00790	$\"[378-512]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.10	$\"[115-358]T$	no description
G3DSA:3.40.50.720	$\"[27-114]T$	no description
G3DSA:3.90.190.20	$\"[358-521]T$	no description
PTHR23135	$\"[131-263]T$ $\"[279-515]T$	MUR LIGASE FAMILY MEMBER
PTHR23135:SF5	$\"[131-263]T$ $\"[279-515]T$	UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE

","BeTs to 17 clades of COG0773COG name: UDP-N-acetylmuramate-alanine ligaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0773 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000713 (Cytoplasmic peptidoglycan synthetases, N-terminal) with a combined E-value of 7.3e-22. IPB000713A 129-140 IPB000713B 198-208 IPB000713C 374-393***** IPB013221 (Mur ligase, middle region) with a combined E-value of 4e-06. IPB013221A 131-140 IPB013221B 197-208","Residues 27-108 are 64% similar to a (LIGASE CELL ATP-BINDING SYNTHETASE DIVISION WALL PEPTIDOGLYCAN UDP-N- SYNTHESIS ACETYLMURAMOYL-L-ALANINE) protein domain (PD446223) which is seen in MURC_VIBCH.Residues 101-157 are 61% similar to a (LIGASE CELL ATP-BINDING DIVISION WALL PEPTIDOGLYCAN SYNTHESIS ACETYLMURAMOYL-L-ALANINE SYNTHETASE UDP-N-) protein domain (PD001083) which is seen in Q6AE65_BBBBB.Residues 159-211 are 75% similar to a (LIGASE CELL ATP-BINDING SYNTHETASE DIVISION WALL SYNTHESIS PEPTIDOGLYCAN UDP-N-ACETYLMURAMATE--L-ALANINE ACETYLMURAMOYL-L-ALANINE) protein domain (PD587021) which is seen in MURC_NEIMB.Residues 361-506 are 63% similar to a (LIGASE CELL ATP-BINDING SYNTHETASE DIVISION WALL PEPTIDOGLYCAN SYNTHESIS ACETYLMURAMOYL-L-ALANINE UDP-N-) protein domain (PD039273) which is seen in MURC_STRAW.","","-48% similar to PDB:2F00 Escherichia coli MurC (E_value = 1.9E_65);-50% similar to PDB:1GQQ MURC- CRYSTAL STRUCTURE OF THE APO-ENZYME FROM HAEMOPHILUS INFLUENZAE (E_value = 5.5E_65);-50% similar to PDB:1GQY MURC- CRYSTAL STRUCTURE OF THE ENZYME FROM HAEMOPHILUS INFLUENZAE COMPLEXED WITH AMPPCP (E_value = 5.5E_65);-50% similar to PDB:1P31 Crystal Structure of UDP-N-acetylmuramic acid:L-alanine Ligase (MurC) from Haemophilus influenzae (E_value = 5.5E_65);-50% similar to PDB:1P3D Crystal Structure of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) in Complex with UMA and ANP. (E_value = 5.5E_65);","Residues 28 to 127 (E_value = 2.2e-24) place ANA_1099 in the Mur_ligase family which is described as Mur ligase family, catalytic domain.Residues 129 to 339 (E_value = 7.4e-09) place ANA_1099 in the Mur_ligase_M family which is described as Mur ligase middle domain.Residues 359 to 447 (E_value = 2e-26) place ANA_1099 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain.","","ligase (murC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1100","1178014","1176755","1260","6.07","-4.46","43049","GTGCCCGAGACAAGTGAGAGCGCAGGCTCGCCCCAGCAGGAGCGTCCTAGCTGCTCGGAGCGGCCCCGGCCGTTGCGGGTACTGCTGGCCGGCGGGGGCACCGCCGGCCACGTCAACCCGCTGCTGGCCACGGCCGCGGCCCTGCGGGACCCGGCCCTGGGTGGTGATCCTGACACGCAGATCCTCGTTCTGGGGACCGCTGAGGGGCTGGAGAAGCGGCTGGTGCCCGAGGCCGGCTTGGAGCTGGCTCTCGTTCCCAGGGTCCCTCTGCCGCGGCGTCCCAGCGGAGACCTGCTGCGTCTGCCGCACCGGCTGGGAAAGGCGATCAGCGCGGCCACGGAGGCCATTGAGGCGGTCAGGGCCGACGTCGTCGTTGGCTTCGGCGGCTACGTGTCGACCCCGGCCTACCTGGCCGCCAGGAAGGCCGGGGTGCCGGTCGTCATCCATGAGCAGAACGCCCGCCCTGGGCTGGCCAACCGGCTGGGGGCCTCCTGGGCCCAGGCCGTGGCCCTGACCTTCGCCTCCACCCGTCTCAGGGCGTCCAAGGGTTGCACTGAGGTCACGGGGTTGCCGCTGCGCCCGGCCATCGCCACCCTGGTGTCGCGGCGGGCCGCGAGCGAGGGGGCCCGCCGAGCTCGTGTCGAGGGCGCCCAGGCGCTGGGACTCGACCCCGACCTGCCCACGCTGCTGGTGACGGGCGGTTCCCTGGGGGCCCAGCACCTCAACGAGGTCCTGAGCGAGTCACTGGGTTCCCTGCCCGCAGGGCTTCAGGTGCTGCACCTGACCGGTAAGGACAAGGATGCCCCGGTGCGCGCCGCCCTCGAGGCGGCAGTGGCCTCGGGTGCTGCACAGGACCTCTCCGAGCGGTACCACGTGCTCGACTACCTGACCTCGATGGAGCAGGCCTATGCCTGCGCCGACGGGGTCCTGTGCCGCTCCGGCGCCGGCACCGTCGCAGAGATCACGGCACTGGGGCTTCCAGCGCTCTACGTCCCCCTGCCGATCGGCAACGGGGAGCAGCGTCTCAACGCCGCTGACGTCCTGGCCTCCGGAGGCGGTCGTATGGTGCTCGACGCCGACCTCAAGTCCTCGGACATTCTTGACTTCGCCATGCTCATCTCCGACCCTGAGCGGCAGGCCGCCATGGCCCGGGCCGCGGCCTCCACCGGCGTCCAGGATGCGGCGGCCCGCCTGGCCGCCCTCATCCGGCAGTGCGCCTCCATCCACGACACTCCCACTGACGAGGAGAACGCGGCATGA","VPETSESAGSPQQERPSCSERPRPLRVLLAGGGTAGHVNPLLATAAALRDPALGGDPDTQILVLGTAEGLEKRLVPEAGLELALVPRVPLPRRPSGDLLRLPHRLGKAISAATEAIEAVRADVVVGFGGYVSTPAYLAARKAGVPVVIHEQNARPGLANRLGASWAQAVALTFASTRLRASKGCTEVTGLPLRPAIATLVSRRAASEGARRARVEGAQALGLDPDLPTLLVTGGSLGAQHLNEVLSESLGSLPAGLQVLHLTGKDKDAPVRAALEAAVASGAAQDLSERYHVLDYLTSMEQAYACADGVLCRSGAGTVAEITALGLPALYVPLPIGNGEQRLNAADVLASGGGRMVLDADLKSSDILDFAMLISDPERQAAMARAAASTGVQDAAARLAALIRQCASIHDTPTDEENAA$","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","Cytoplasm, Extracellular","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase ","UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase","","Poland B.W., Silva M.M., Serra M.A., Cho Y., Kim K.H., Harris E.M., Honzatko R.B. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 1993. 268(34):25334-25342. PMID: 8244965Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 2000. 296(2):569-577. PMID: 10669609","","","

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[121-346]T$	no description

InterPro
IPR004276
Domain

Glycosyl transferase, family 28
PF03033	$\"[27-171]T$	Glyco_transf_28

InterPro
IPR006009
Family

N-acetylglucosaminyltransferase, MurG
TIGR01133	$\"[20-402]T$	murG: undecaprenyldiphospho-muramoylpentape

InterPro
IPR007235
Domain

Glycosyltransferase 28, C-terminal
PF04101	$\"[228-398]T$	Glyco_tran_28_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2000	$\"[19-217]T$	no description
PTHR21015	$\"[25-347]T$	GLYCOSYLTRANSFERASE

","BeTs to 17 clades of COG0707COG name: UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0707 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB004276 (Glycosyl transferase, family 28) with a combined E-value of 4.6e-59. IPB004276A 26-41 IPB004276B 126-160 IPB004276D 229-238 IPB004276E 306-333 IPB004276F 337-358","Residues 33-361 are 62% similar to a (TRANSFERASE CELL N-ACETYLGLUCOSAMINE PYROPHOSPHORYL-UNDECAPRENOL UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-PENTAPEPTIDE UNDECAPRENYL-PP-MURNAC-PENTAPEPTIDE-UDPGLCNAC GLCNAC DIVISION WALL COM) protein domain (PD005948) which is seen in MURG_BIFLO.","","-46% similar to PDB:1F0K THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG (E_value = 8.6E_34);-46% similar to PDB:1NLM CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX (E_value = 8.6E_34);-66% similar to PDB:1PN3 Crystal Structure of TDP-epi-Vancosaminyltransferase GtfA in complexes with TDP and the acceptor substrate DVV. (E_value = 8.6E_34);-66% similar to PDB:1PNV Crystal Structure of TDP-epi-Vancosaminyltransferase GtfA in complexes with TDP and Vancomycin (E_value = 8.6E_34);-46% similar to PDB:1YD7 Conserved hypothetical protein Pfu-1647980-001 from Pyrococcus furiosus (E_value = 8.6E_34);","Residues 27 to 171 (E_value = 3.4e-37) place ANA_1100 in the Glyco_transf_28 family which is described as Glycosyltransferase family 28 N-terminal domain.Residues 228 to 398 (E_value = 3.5e-34) place ANA_1100 in the Glyco_tran_28_C family which is described as Glycosyltransferase family 28 C-terminal domain.","","pyrophosphoryl-undecaprenol N-acetylglucosamine transferase (murG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1101","1179527","1177998","1530","11.02","30.03","53503","GTGAAGACCGGGCCCACCTCGGCCACCGCCGCCCGCTCGTCGAGCCCCTCCTCGGCAGGAGCCTCTCGGGCGACCGGAGCCCCGTCAAGGACAGCCGGTGCCGGCCGCAAGCCGGAGCGGGACGCCCCCCGGAAGGGCGCTGCCACAGCGTCCCAACGGACCAGGAAGCCCTCCGGCTCTCGGCCCACGGGAGCGGGCGGTCGCCTGGGTGACGCCTGGCGCAAGCGGCTGGCTCACTGGGGCGAGCGGCTCTCAAGACCCTGGGACGGGGGTGCTCCCCAGACCGATGGCGGCTCGCAGGAGCGTCGTCGGCGCTCCTCCGAGGGGTCCGACTCCCCCCAGAGCTCCGAGCAGGTGACTCTGACCTACTACTGCCTGCTCGTGTCCACCCTGGTGCTGGAGACCTTCGGGCTCATCATGGTCTTCTCCGTGCAGTCGGTGACCGTGGCCGCCACCGGTGGCAATGCCTTCACCGACTTCGCCAAGTACCTCATCTTCGCTGCGGTGGGGACGCTGGGCATGGTGGGGGTCTCCCGCATCCCGCTGTCCTGGTTCCCGCGGATGGCGTGGGTGCTCCTGGCACTGACGATCGCCATGCAGTGCCTGGTGTTCACACCAGTCGGGGTCAACGTCTACGGCAACCGCAACTGGATCCAGGTCCCGGGGGTCGGCACCGCCCAGCCCTCGGAGTTCATCAAAGTGGCCCTCGCCCTGGTCCTGGGCACCCTGGTGACCTGGTACGCGGACAAGCGCCCCCGGGACCGGGCGTGGAAGGCGGGCTGGGGCGGTGTTGCCGTCGCGATCCTGAGCGTCTTCGGCGGACAGGATCTGGGAACCGTCATCATCCTGGTGATCATCGTCGCTGGGGCCCTGTGGGTGGGGGGAATGCGCAAGCGCTGGTTCGCTCTCCTGGGTGCCGGCGGCATCGTCATGTTCGCGGCCGCATCCATGCTCAGCGCCAACCGGCGCGCCCGAATCACCGCCTGGATCCATCCCGAGGGCGCCGACCCCATGGGCGTGGGCTACCAGCCCAAGCACGGGATGTGGGCGCTGGGGACCGGGGGCTGGCTCGGTGTGGGGCCCGGATCGTCGCGCCAGAAGTGGGGCTACCTCACCCAGGCGGACTCCGACTACATCTTCGCCGTGCTTGGTGAGGAGTTCGGGCTGGTGGGTACGCTCGTCGTCATCGCCCTGTTCGCCGGTATCGGAGCCTGCTGCCTGCGGCTCATGAGGCGCCACACCTCCCTGTACGTGGTGGCCACGACCTCGGCCATCGGGGCGTGGATCGTGGGGCAGGCAATCATCAACATGGGGGTTGTCACTGGTGCGTTGCCGGTGCTGGGCGTCCCCCTTCCCCTCGTCAGCCGTGGAGGCACCGCACTGGTGTCAGTCCTCCTGGCCATCGGGGTGCTTCTGGCCTTCGCGCGTCACGAACCCGGCGCGCAGGAGGCCCTGTCCACGAGTCCCGGGGCGCTGCGTCGTTCCCTGGCAGTCATTGTCCCAAGGAGGAACCGTGCCCGAGACAAGTGA","VKTGPTSATAARSSSPSSAGASRATGAPSRTAGAGRKPERDAPRKGAATASQRTRKPSGSRPTGAGGRLGDAWRKRLAHWGERLSRPWDGGAPQTDGGSQERRRRSSEGSDSPQSSEQVTLTYYCLLVSTLVLETFGLIMVFSVQSVTVAATGGNAFTDFAKYLIFAAVGTLGMVGVSRIPLSWFPRMAWVLLALTIAMQCLVFTPVGVNVYGNRNWIQVPGVGTAQPSEFIKVALALVLGTLVTWYADKRPRDRAWKAGWGGVAVAILSVFGGQDLGTVIILVIIVAGALWVGGMRKRWFALLGAGGIVMFAAASMLSANRRARITAWIHPEGADPMGVGYQPKHGMWALGTGGWLGVGPGSSRQKWGYLTQADSDYIFAVLGEEFGLVGTLVVIALFAGIGACCLRLMRRHTSLYVVATTSAIGAWIVGQAIINMGVVTGALPVLGVPLPLVSRGGTALVSVLLAIGVLLAFARHEPGAQEALSTSPGALRRSLAVIVPRRNRARDK$","Cell division protein FtsW","Membrane, Extracellular","cell division protein FtsW","cell division protein FtsW","cell cycle protein","","Ikeda M., Sato T., Wachi M., Jung H.K., Ishino F., Kobayashi Y., Matsuhashi M. Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively. J. Bacteriol. 1989. 171(11):6375-6378. PMID: 2509435Joris B., Dive G., Henriques A., Piggot P.J., Ghuysen J.M. The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures. Mol. Microbiol. 1990. 4(3):513-517. PMID: 2113157","","","

InterPro
IPR001182
Family

Cell cycle protein
PF01098	$\"[124-480]T$	FTSW_RODA_SPOVE

noIPR
unintegrated

unintegrated
tmhmm	$\"[124-144]?$ $\"[163-185]?$ $\"[190-210]?$ $\"[229-247]?$ $\"[257-272]?$ $\"[278-296]?$ $\"[301-321]?$ $\"[378-400]?$ $\"[415-435]?$ $\"[454-474]?$	transmembrane_regions

","BeTs to 16 clades of COG0772COG name: Bacterial cell division membrane proteinFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0772 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001182 (Cell cycle protein) with a combined E-value of 7.6e-27. IPB001182A 212-232 IPB001182B 370-391 IPB001182C 435-460","Residues 124-222 are 56% similar to a (CELL DIVISION FTSW ROD SHAPE-DETERMINING RODA MEMBRANE SHAPE FAMILY PROTEIN) protein domain (PD041336) which is seen in Q82AD7_STRAW.Residues 126-290 are 50% similar to a (DIVISION CELL) protein domain (PDA04088) which is seen in Q6ADT5_BBBBB.Residues 295-388 are 58% similar to a (CELL DIVISION FTSW ROD SHAPE-DETERMINING RODA FAMILY MEMBRANE SHAPE PROTEIN) protein domain (PD169806) which is seen in Q8G4Q5_BIFLO.","","-57% similar to PDB:1IS7 Crystal structure of rat GTPCHI/GFRP stimulatory complex (E_value = );-57% similar to PDB:1IS8 Crystal structure of rat GTPCHI/GFRP stimulatory complex plus Zn (E_value = );-57% similar to PDB:1WPL Crystal structure of the inhibitory form of rat GTP cyclohydrolase I/GFRP complex (E_value = );-49% similar to PDB:2BIW CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, NATIVE ENZYME (E_value = );-49% similar to PDB:2BIX CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, FE-FREE APOENZYME (E_value = );","Residues 124 to 480 (E_value = 9.6e-64) place ANA_1101 in the FTSW_RODA_SPOVE family which is described as Cell cycle protein.","","division protein FtsW","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1102","1181083","1179524","1560","5.10","-18.99","53090","GTGACCAGCCTGACTGAAGTCCCCGGTGAGCCGACCAGCGCCGTCACCGGCCCCGGCGGGTCTTTGAGCGACCAGCTCGACGGCGCCCACGTGGCCGTCGTCGGCCTAGGGCGCACCGGGCGCGCCGTCGTAGACGCCCTGGCCACGCTGGGGGCCCGCATCCACGTCTTCGACAGCCGTGAGTCCTCCCTCGAGATGCTGCAGACCCCCGTGGCCTCCACGACGGTCGCCGACGCCGAGGCGACCGCGGCCGCCCTGGTACAGTCCCCGGCCAGGCTCCTCGTCGTCTCACCCGGGGTCCCGGCCACCGGGCCGGTCCTGCGAGGCGCCGCGGCGGCGGGTATCGAGACCTGGAGCGAGGTCGAGCTGGCCTGGAGGATTCAGCAGGAATCAGCGCGTCCGCACGTCCCATGGCTGACTCTGACCGGGACAGACGGCAAGACCACTACGGTCAGCATGCTCTCAGCGATCCTGACGGCCCACGGGCTCACGGCCCCGGCCGTGGGCAACATTGGCACCCCCGTTATCGAGGCGGTGCTGGCCGGCAGCGCCGACGCCCTGGCCGTGGAGCTGTCCAGCTTCCAGCTGCACACCACCAGGACCCTGGCGCCCCTGGCGTCGGCCTGCCTCAACCTGGCCGCCGACCACCTCGACTGGCACGGGGGCCTGGAGGCCTACGCCCAGGACAAGGCTCGGGTCTACTCCCGCACCCGGCTCGCCGCCATCTACAACCTCGCCGACTCCGCCACCGAGGACATGGTCCGCCAGGCCGACGTCGTCGAGGGCTGCCGAGCCGTCGGCTTCACCCTGGCCGCACCGGGATTGGGACAGGTCGGCATGGTCGAGGACCTTCTGGTCGACCGCGCCTTCCACGCCGAGCGGCGCTCCAGCGGCGTCGAGCTGGCCACCACCGCCGACCTGGCGCACCTCGCCCCGGCAGGACGCGTCCAGAACCTGCCCGCGCACCTGCTGGCCGACGCCCTGGCGGCCGCCGCGCTGGCCCGGGCGGCCGGAGCTGACCCGCAGGCGGTCTCCGCCGGACTGCGCGCCTACAGTCCCGGGGCCCACCGGATCGTCACCGTCGCCGAGGCGGACGGCATCACCTGGGTCGATGACTCCAAGGCCACCAACCCGCACTCCGCCGAGGCCGCACTGACCTCCCTGCCGCAGGGGACCGCCGTGTGGATCTGCGGCGGCGACACCAAGGGTGCACAGTTCTTCGACCTGGTCCGCACGGTGCGCCCCCACCTGCGCGGCGCCGTCGTCATCGGCAAGGACCAGAGCGACATTCTGGCGGCTCTGGAGCAGGAGGCCCCTGGCCTTCCCCTCACTCGCGTCAGCGACGGCAGCGCCGAGCAGGTGAGCGCCGCCGCGGTGGAGGCCGCCGGCGCCATGGCCCGCAACGGTGACACCGTCATGCTGGCCCCGGCTTGCGCCTCCTGGGACCAGTTCACGTCCTATGCCCAGCGCGGCGACCTGTTCGCCGCCTGCGCCCGGGCCTTCACCCAAGGCGATGGTGCCCGGGACGGGGACGCCTCCGGCGACCAGGAGCGGCTGTGA","VTSLTEVPGEPTSAVTGPGGSLSDQLDGAHVAVVGLGRTGRAVVDALATLGARIHVFDSRESSLEMLQTPVASTTVADAEATAAALVQSPARLLVVSPGVPATGPVLRGAAAAGIETWSEVELAWRIQQESARPHVPWLTLTGTDGKTTTVSMLSAILTAHGLTAPAVGNIGTPVIEAVLAGSADALAVELSSFQLHTTRTLAPLASACLNLAADHLDWHGGLEAYAQDKARVYSRTRLAAIYNLADSATEDMVRQADVVEGCRAVGFTLAAPGLGQVGMVEDLLVDRAFHAERRSSGVELATTADLAHLAPAGRVQNLPAHLLADALAAAALARAAGADPQAVSAGLRAYSPGAHRIVTVAEADGITWVDDSKATNPHSAEAALTSLPQGTAVWICGGDTKGAQFFDLVRTVRPHLRGAVVIGKDQSDILAALEQEAPGLPLTRVSDGSAEQVSAAAVEAAGAMARNGDTVMLAPACASWDQFTSYAQRGDLFAACARAFTQGDGARDGDASGDQERL$","UDP-N-acetylmuramoylalanine-D-glutamate ligase","Cytoplasm","UDP-N-acetylmuramoylalanine--D-glutamate ligase","UDP-N-acetylmuramoylalanine-D-glutamate ligase ","UDP-N-acetylmuramoylalanine--D-glutamate ligase","","Ziegelin G., Scherzinger E., Lurz R., Lanka E. Phage P4 alpha protein is multifunctional with origin recognition, helicase and primase activities. EMBO J. 1993. 12(9):3703-3708. PMID: 8253092","","","

InterPro
IPR004101
Domain

Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875	$\"[354-430]T$	Mur_ligase_C

InterPro
IPR005762
Family

UDP-N-acetylmuramoylalanine-D-glutamate ligase
TIGR01087	$\"[30-500]T$	murD: UDP-N-acetylmuramoylalanine--D-glutam

InterPro
IPR012237
Family

UDP-N-acetylmuramate-alanine ligase
PIRSF001562	$\"[29-509]T$	UDP-N-acetylmuramate-alanine ligase

InterPro
IPR013221
Domain

Mur ligase, middle region
PF08245	$\"[139-334]T$	Mur_ligase_M

InterPro
IPR013237
Domain

Phage P4 alpha, zinc-binding
SM00778	$\"[476-507]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.10	$\"[119-353]T$	no description
G3DSA:3.40.50.720	$\"[24-118]T$	no description
G3DSA:3.90.190.20	$\"[354-502]T$	no description
PTHR23135	$\"[141-503]T$	MUR LIGASE FAMILY MEMBER
PTHR23135:SF2	$\"[141-503]T$	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE

","BeTs to 18 clades of COG0771COG name: UDP-N-acetylmuramoylalanine-D-glutamate ligaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0771 is --m----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000713 (Cytoplasmic peptidoglycan synthetases, N-terminal) with a combined E-value of 7.8e-10. IPB000713A 139-150 IPB000713B 208-218 IPB000713C 370-389","Residues 22-127 are 47% similar to a (LIGASE CELL DIVISION ENZYME ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE MURD D-GLUTAMIC WALL ACID UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE) protein domain (PD779974) which is seen in MURD_MYCLE.Residues 169-257 are 58% similar to a (LIGASE UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE) protein domain (PD933341) which is seen in Q83HK0_TROW8.Residues 190-234 are 75% similar to a (LIGASE SYNTHETASE CELL ATP-BINDING ENZYME DIVISION UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--26-DIAMINOPIMELATE UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE UDP-MURNAC-TRIPEPTIDE MESO-) protein domain (PD212530) which is seen in MURD_BIFLO.Residues 240-311 are 54% similar to a (LIGASE CELL DIVISION ENZYME ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE S D-GLUTAMIC WALL ACID UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE) protein domain (PD790118) which is seen in MURD_BIFLO.Residues 258-355 are 64% similar to a (LIGASE UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE UDP-N-ACETYLMURAMOYLALANINE-D-GLUTAMATE CELL DIVISION ENZYME ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE S D-GLUTAMIC WALL) protein domain (PD286321) which is seen in Q82AD8_STRAW.Residues 356-495 are 65% similar to a (LIGASE CELL UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE ENZYME D-GLUTAMIC ACID ADDING SYNTHETASE DIVISION ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE) protein domain (PD039274) which is seen in MURD_STRCO.","","-42% similar to PDB:1E0D UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE (E_value = 1.9E_33);-42% similar to PDB:1EEH UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE (E_value = 1.9E_33);-42% similar to PDB:1UAG UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE (E_value = 1.9E_33);-42% similar to PDB:2JFF CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH D-GLU CONTAINING SULFONAMIDE INHIBITOR (E_value = 1.9E_33);-42% similar to PDB:2JFG CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH UMA AND ADP (E_value = 1.9E_33);","Residues 139 to 334 (E_value = 4.2e-39) place ANA_1102 in the Mur_ligase_M family which is described as Mur ligase middle domain.Residues 354 to 430 (E_value = 7.1e-12) place ANA_1102 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain.","","ligase (murD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1104","1182286","1181186","1101","9.14","7.50","39307","ATGACCGCCATCCTCATCTCCGGTGTGGTCGGACTGGTGGGCACCCTGCTGGGGACCCCCCTGCTCATCCGCTACCTCCACGCCAAGGAGTACGGACAGTTCATCCGCCAGGACGGGCCCCAGGGACACTTCACCAAGCGCGGCACGCCGACCATGGGCGGCCTCGTCATCATCATCTCCACTGTCCTGGGCTACACCCTGGCCAATCTCAGCCAGCTGCGCACACCGCGCGCCTCCGGGGTCCTGCTGCTCTTCCTCGTCGTCGGGCTCGGGCTCATCGGATTCCTGGACGACTTCGAGAAGATCTCCAAGCAGCGCTCCCTGGGACTGAGGGCATGGCAGAAGATCGTGGGGCAGGCGCTCATCGGCGTCGGATTCTCGGTGGCGGCCCTGCACTTCGCGGACCGCAACGGACTGACCCCCGCCTCCACCCGGATCTCCTTCGCCCGGGACTCGGCGATCAACCTGGCCTTCGCCGGCAGCGTCGTCGGGCTCATTCTGTTCATCCTGTGGGCCAACTTCCTCATCACCGCCTGGTCCAACGCCGTCAACCTCACCGACGGGCTCGATGGACTGGCCGCCGGCGCCTCGGCCATGGTCTTCGGCGCCTACACGCTCATCGGCGTGTGGCAGACCAACCAGTCCTGCAACTACGGCCACGAGACCATGGTCCCCACCACCTGCTATCAGGTCAGGGACCCGCGAGACCTGGCCATGATCGCCGCCGCCCTCATGGGGGCCTGCTTCGGCTTCCTGTGGTGGAACGCCTCACCGGCCAAGATCTTCATGGGTGACACCGGGTCCCTGGCCCTGGGTGGGGCGGTCGCCGGCCTGTCGATCCTGACCCGCACGGAGTTCCTGGCCGTCATCCTGGGTGGACTCTTCCTGGCCGAGGTCATGAGCGACATCATCCAGATCGTCTCATTCAAGTCAACAGGCCGACGCGTCTTCCGCATGGCTCCACTGCATCACCACTTCGAACTGGGAGGATGGACCGAGGTCAACGTGGTGATCCGCTTCTGGATCATTGCCGGCCTGTGCGTCATCGCGGGACTCGGACTCTTCTACGCCGAGTACCTGCGCCAGCTCATCTTCGGATGA","MTAILISGVVGLVGTLLGTPLLIRYLHAKEYGQFIRQDGPQGHFTKRGTPTMGGLVIIISTVLGYTLANLSQLRTPRASGVLLLFLVVGLGLIGFLDDFEKISKQRSLGLRAWQKIVGQALIGVGFSVAALHFADRNGLTPASTRISFARDSAINLAFAGSVVGLILFILWANFLITAWSNAVNLTDGLDGLAAGASAMVFGAYTLIGVWQTNQSCNYGHETMVPTTCYQVRDPRDLAMIAAALMGACFGFLWWNASPAKIFMGDTGSLALGGAVAGLSILTRTEFLAVILGGLFLAEVMSDIIQIVSFKSTGRRVFRMAPLHHHFELGGWTEVNVVIRFWIIAGLCVIAGLGLFYAEYLRQLIFG$","Phospho-N-acetylmuramoyl-pentapeptide-transferase","Membrane, Cytoplasm, Extracellular","phospho-N-acetylmuramoyl-pentapeptide-transferase","phospho-N-acetylmuramoyl-pentapeptide-transferase ","phospho-N-acetylmuramoyl-pentapeptide-transferase","","","","","

InterPro
IPR000715
Family

Glycosyl transferase, family 4
PTHR22926	$\"[25-222]T$ $\"[243-360]T$	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
PF00953	$\"[80-288]T$	Glycos_transf_4

InterPro
IPR003524
Family

Phospho-N-acetylmuramoyl-pentapeptide transferase
PTHR22926:SF3	$\"[25-222]T$ $\"[243-360]T$	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
TIGR00445	$\"[15-361]T$	mraY: phospho-N-acetylmuramoyl-pentapeptide
PS01347	$\"[46-58]T$	MRAY_1
PS01348	$\"[181-192]T$	MRAY_2

noIPR
unintegrated

unintegrated
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[48-68]?$ $\"[78-96]?$ $\"[115-135]?$ $\"[156-176]?$ $\"[190-210]?$ $\"[237-255]?$ $\"[261-281]?$ $\"[286-306]?$ $\"[337-357]?$	transmembrane_regions

","BeTs to 19 clades of COG0472COG name: UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N- acetylglucosamine-1-phosphate transferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0472 is --m-k-yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB003524 (Phospho-N-acetylmuramoyl-pentapeptide transferase) with a combined E-value of 1.8e-92. IPB003524A 32-58 IPB003524B 77-116 IPB003524C 181-193 IPB003524D 243-280 IPB003524E 313-343","Residues 52-200 are 71% similar to a (TRANSFERASE PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE TRANSMEMBRANE SYNTHESIS PHOSPHOTRANSFERASE CELL DIVISION UDP- PEPTIDOGLYCAN MURNAC-PENTAPEPTIDE) protein domain (PD558062) which is seen in Q82AD9_STRAW.Residues 236-352 are similar to a (TRANSFERASE PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE TRANSMEMBRANE SYNTHESIS PHOSPHOTRANSFERASE CELL DIVISION UDP- PEPTIDOGLYCAN MURNAC-PENTAPEPTIDE) protein domain (PD001416) which is seen in Q82AD9_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 80 to 288 (E_value = 2.4e-52) place ANA_1104 in the Glycos_transf_4 family which is described as Glycosyl transferase family 4.","","(mraY) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1105","1183722","1182283","1440","5.07","-19.10","48729","ATGAGGCTCAGCCTGAGTCAGATCGCCGCCGCCGTCGGCGGCAGGCTCATCGGCCCGGACGCGCCGGTGACCGGGCCGGTCGTCACCGACTCCCGCCAGGCCGCCGAGGGCTCACTGTTCATCGCCGTTCACGGTGAGCGCACCGACGGCCACGCCCACCTGGGATCGGCCGGGGCGCTGGGTGCTGTCGGCGCCATCGTCTCCGACCTGGAGGCCGCCCGCAGCGGACTGTCCCAGGGGCAGGCCGAGGAGCCGACCATGGGGCTCGTCCTCGTGGAGGACACGGTAGTGGCTCTCGGTGCTCTGGCCCGCACCCACCTGGAAGGGCTGCGCCAGGCAGCGGCCGAGCGAGGCGAGCGTCTCACCGTGGTGGCGATGACCGGCTCGGTGGGCAAGACCACCACCAAGGACCTCACCCGCCAGCTCCTGGCAGCCTCCGGCCCCACGGTGGCGCCCCGGGCCAGCTTCAACAACGAGATCGGTCTGCCGCTGACCGTGCTGGAGGCCGACGAGTCCACCCGCTACCTCGTCCTGGAGATGGGGGCCTCCGGACCTGGCCATATCGCCTACCTCACTGACATCGCCCCCCTGGACGCGGCCGGAGTCCTCATGATCGGCCACGCCCACATGGGCGGCTTCGGCTCCATCGAGGGAGTCGCCGCGGCCAAGGCGGAGATCATCGCCGGCCTGCGGCCTGACGGGACCGCCATCCTCAACGCCGACGATGCCCGCGCCGCCGCCATGGCCGAGCTCGCACCGGCACGCGTCCTGACCTTCTCCGCCCAAGGGCGACAGGCCGACCTGAGGGCCGAGAACGTGGATCTGGACGCGGTCGCCCGAGCGGCCTTCGACCTCCACCTGCCCGGTCTCGCCGAGCCCCGCCGCGTCCAGCTGGCCGTGGCGGGAGTGCACAACGTGTCCAACGCCCTGGCCGCCGCGGGGCTGGCCCTGGCCGCGGGCATCGCCCCCGAGCTCGTCGCCGAGCGGCTCGGCTCAGTGAGCATCGAGAGCCCCCACCGGATGGATATTTCGGAACTCAGTGGTGATCTTCTCCTTATCGACGACTCCTACAACGCCAACATCGACTCCATGACGGCGGCGCTGGCGGTGCTGCCGGCTCTGGCCGGGGACCGACGTCGCGTCGTCGTGATTTCCGAGATGCTTGAGCTGGGGGAGTCCTCTGCGGCCGATCACGCGCGCACCGGAGAGCTCGCGGCCCGAGCCGGAGCCGCTATGCTCATCGGCATCGGCTCCACCCAGGAGGCACTCGAGGCGGCCAGGGCGCGAGGGGTCGAGGTCGTCGGTTTCGATGATGCCGCGACCGCCATCTCCCAGATCGACGCCCTGCTCTGCGACGGCGACGCCGTCCTGGTCAAGGGTTCAAACGGCTCGGGCGCCTGGCGCCTGGCCGACCACCTCAAGGAGGTTCGTCCCCGATGA","MRLSLSQIAAAVGGRLIGPDAPVTGPVVTDSRQAAEGSLFIAVHGERTDGHAHLGSAGALGAVGAIVSDLEAARSGLSQGQAEEPTMGLVLVEDTVVALGALARTHLEGLRQAAAERGERLTVVAMTGSVGKTTTKDLTRQLLAASGPTVAPRASFNNEIGLPLTVLEADESTRYLVLEMGASGPGHIAYLTDIAPLDAAGVLMIGHAHMGGFGSIEGVAAAKAEIIAGLRPDGTAILNADDARAAAMAELAPARVLTFSAQGRQADLRAENVDLDAVARAAFDLHLPGLAEPRRVQLAVAGVHNVSNALAAAGLALAAGIAPELVAERLGSVSIESPHRMDISELSGDLLLIDDSYNANIDSMTAALAVLPALAGDRRRVVVISEMLELGESSAADHARTGELAARAGAAMLIGIGSTQEALEAARARGVEVVGFDDAATAISQIDALLCDGDAVLVKGSNGSGAWRLADHLKEVRPR$","UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase","Cytoplasm","UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase","UDP-N-acetylmuramoylalanyl-D-glutamyl-2;6-diaminopimelate--D-alanyl-D-alanine ligase ","UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase","","","","","

InterPro
IPR000713
Domain

Mur ligase, N-terminal
PF01225	$\"[23-107]T$	Mur_ligase

InterPro
IPR004101
Domain

Mur ligase, C-terminal
PF02875	$\"[337-427]T$	Mur_ligase_C

InterPro
IPR005863
Family

UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
PTHR23135:SF3	$\"[126-466]T$	UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE--D-ALANYL-D- ALANYL LIGASE
TIGR01143	$\"[29-473]T$	murF: UDP-N-acetylmuramoyl-tripeptide--D-al

InterPro
IPR012237
Family

Mur ligase
PIRSF001562	$\"[8-472]T$	UDP-N-acetylmuramate-alanine ligase

InterPro
IPR013221
Domain

Mur ligase, central
PF08245	$\"[124-316]T$	Mur_ligase_M

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.10	$\"[93-334]T$	no description
G3DSA:3.40.1390.10	$\"[1-69]T$	no description
G3DSA:3.90.190.20	$\"[336-479]T$	no description
PTHR23135	$\"[126-466]T$	MUR LIGASE FAMILY MEMBER

","BeTs to 17 clades of COG0770COG name: UDP-N-acetylmuramyl pentapeptide synthaseFunctional Class: MThe phylogenetic pattern of COG0770 is -mt--qvcebrhuj--olinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 58-229 are 50% similar to a (LIGASE ATP-BINDING UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE) protein domain (PDA1A0D4) which is seen in Q728U4_DESVH.Residues 382-453 are 65% similar to a (LIGASE ATP-BINDING UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2 6-DIAMINOPIMELATE--D-ALANYL- D-ALANYL ENZYME CELL UDP-MURNAC-PENTAPEPTIDE SYNTHETASE ALANYL) protein domain (PD292385) which is seen in Q8ZRU6_SALTY.","","-46% similar to PDB:1GG4 CRYSTAL STRUCTURE OF ESCHERICHIA COLI UDPMURNAC-TRIPEPTIDE D-ALANYL-D-ALANINE-ADDING ENZYME (MURF) AT 2.3 ANGSTROM RESOLUTION (E_value = 2.2E_45);-43% similar to PDB:2AM1 sp protein ligand 1 (E_value = 4.9E_21);-43% similar to PDB:2AM2 sp protein ligand 2 (E_value = 4.9E_21);","Residues 67 to 151 (E_value = 1.2e-08) place ANA_1105 in the Mur_ligase family which is described as Mur ligase family, catalytic domain.Residues 168 to 360 (E_value = 2.4e-55) place ANA_1105 in the Mur_ligase_M family which is described as Mur ligase middle domain.Residues 381 to 471 (E_value = 1.2e-13) place ANA_1105 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain.","","ligase (murF)","","1","","","Thu Aug 2 16:46:43 2007","","Thu Aug 2 16:46:43 2007","","","Thu Aug 2 16:46:43 2007","Thu Aug 2 16:46:43 2007","Thu Aug 2 16:46:43 2007","","","","","","Thu Aug 2 16:46:43 2007","Thu Aug 2 16:46:43 2007","Thu Aug 2 16:46:43 2007","","Thu Aug 2 16:46:43 2007","Thu Aug 2 16:46:43 2007","","","","","yes","","" "ANA_1106","1185305","1183719","1587","5.23","-20.31","55639","ATGAGCAACCACGCCTACGAGTCGGCCGCCGCCCTACGGCCGAGCTCCAATGGTCCCATCCCCATCAGCACCCTGTGCGAGCGCTTCTCCCTGACTCCTGCCTCAGCTGAGGATGCCGCCGCGCTCAACGACCTGAGCACCCTGGGGGTTAGCGTCGACTCCGGCGACATCGCAGCGGGCGAGCTCTTCGTGGGACTGCCCGGTTTCACCGTCCACGGGGCCCGCTTCGCCGCCCAGGCCGTCGCCTCCGGTGCCGTTGCCGTCCTGACCGATGCCGACGGCGCCCAGATCGTCCACGAGACCGCTCCTGGTACGCCGGTCCTCGTGCACAGCGACCCCCGCGCCGTCGTCGGTCCCCTGAGCGCCGAGGTCTACCACCATCCGGCACGCGGACTGGTCACGACCGCCGTCACCGGAACCAACGGCAAGACGACCACCGCCTACTTCCTCGACGCCATTCTGTCCGCTCACGTCGGCGGCTGCATGGTGGCCGGAACCGTCGAGTTGCGCGTGGGGGAGCGCTCCGTGGAGTCCCCGCGCACCACCGTCGAGGCCCCCGTCCTGCAGCGGATGATGGCCCTGGCCGTGGAGGACAGGGTCGGCGCCGCCTCCCTGGAGGCCTCCAGCCACGCCATCGTCCTGCACCGGCTCGATGGGCTCGTCGTCGACGTCGCCGGCTTCACCAACCTCCAGCGCGACCACCTCGACTTCCACAAGACCATGGAGGGCTACCTGGAGGCCAAGGCGCAGCTGTTCACCCCCGAGCACGCCCGCCGCGGCGTGGTCTGCGTCGACGACCAGTGGGGTGCGGCCCTGGCCGCCGAGGCCCCCATCGAGATCGACCGCGTGCGCGCCTACCCCGGTGAGACTCCCGCCGACTGGTGGGTCAGTGACGCCGCCGTCTCCCTGACCGACTCCGCCACCACCTTCACCCTCCACGGGCCCGACGGCGAGCAGATCGAGGCCTCCTGCCCCCTGCCCGGGCTCGTCAACGTCCAGAACGCCGCCCTGGCCCTGGTCATGGCCATCCGTGCGGGGGTGCCCGCCGCCACGGCCACCGCCGCCCTGGCCGGTGCCCACAACATCCCCGGCCGCATGCAGCGCATCAGCCAGCGCGACGGTCGACGTGGCCTGTGCATCGTCGACTTCGCCCACACCCCCGAGGCCATGGAGCTGGCCCTCAAGGCCGTGCGTCCCATCACCCCGGGGCGCCTCATCGTGGTCTTCGGATCCGACGGCGACCGGGACCAGGGCAAGCGGCCCATGCTGGGCGAGGTGTGCGCCCGCCTGGCCGATGTTCTGGTCGTCACCGACGAGAACCCCCGCAGCGAGGACCCCCAGCTCATCCGCAACGCCATCCTCGAGGGCGTGCGCGGCGTGCGTCCCGACCTGACGGACGTCGAGGAGATCACCACCTGGCGCGGCGACGCCGTACGCCGGGGCGTCGAGCTGTGCGGACCCGACGACACCGTCATCGTCACCGGCAAGGGCCACGAGCCCTTCCTGGAGATGGCCGGGGAGTTCATCCGCTACAACGACGCGCCCGTGATGGCCGAGGCCGTCGAGAAGAAATGGGGACGGGCATGA","MSNHAYESAAALRPSSNGPIPISTLCERFSLTPASAEDAAALNDLSTLGVSVDSGDIAAGELFVGLPGFTVHGARFAAQAVASGAVAVLTDADGAQIVHETAPGTPVLVHSDPRAVVGPLSAEVYHHPARGLVTTAVTGTNGKTTTAYFLDAILSAHVGGCMVAGTVELRVGERSVESPRTTVEAPVLQRMMALAVEDRVGAASLEASSHAIVLHRLDGLVVDVAGFTNLQRDHLDFHKTMEGYLEAKAQLFTPEHARRGVVCVDDQWGAALAAEAPIEIDRVRAYPGETPADWWVSDAAVSLTDSATTFTLHGPDGEQIEASCPLPGLVNVQNAALALVMAIRAGVPAATATAALAGAHNIPGRMQRISQRDGRRGLCIVDFAHTPEAMELALKAVRPITPGRLIVVFGSDGDRDQGKRPMLGEVCARLADVLVVTDENPRSEDPQLIRNAILEGVRGVRPDLTDVEEITTWRGDAVRRGVELCGPDDTVIVTGKGHEPFLEMAGEFIRYNDAPVMAEAVEKKWGRA$","UDP-N-acetylmuramyl-tripeptide synthetase","Cytoplasm","UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase(EC 6.3.2.13)","putative UDP-N-acetylmuramoylalanyl-D-glutamate- 2;6-diaminopimelate ligase ","UDP-N-acetylmuramyl-tripeptide synthetase","","","","","

InterPro
IPR000713
Domain

Cytoplasmic peptidoglycan synthetase, N-terminal
PF01225	$\"[46-125]T$	Mur_ligase

InterPro
IPR004101
Domain

Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875	$\"[362-450]T$	Mur_ligase_C

InterPro
IPR005761
Family

UDP-N-acetylmuramyl-tripeptide synthetase
TIGR01085	$\"[44-522]T$	murE: UDP-N-acetylmuramyl-tripeptide synthe

InterPro
IPR012237
Family

UDP-N-acetylmuramate-alanine ligase
PIRSF001562	$\"[27-516]T$	UDP-N-acetylmuramate-alanine ligase

InterPro
IPR013221
Domain

Mur ligase, middle region
PF08245	$\"[135-342]T$	Mur_ligase_M

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.10	$\"[128-365]T$	no description
G3DSA:3.40.1390.10	$\"[27-127]T$	no description
G3DSA:3.90.190.20	$\"[369-521]T$	no description
PTHR23135	$\"[137-155]T$ $\"[176-524]T$	MUR LIGASE FAMILY MEMBER
PTHR23135:SF4	$\"[137-155]T$ $\"[176-524]T$	UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE

","BeTs to 18 clades of COG0769COG name: UDP-N-acetylmuramyl tripeptide synthaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0769 is --m----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001645 (Folylpolyglutamate synthetase) with a combined E-value of 3.3e-24. IPB001645A 134-176 IPB001645B 184-219 IPB001645C 225-258 IPB001645D 382-394***** IPB000713 (Cytoplasmic peptidoglycan synthetases, N-terminal) with a combined E-value of 1.8e-16. IPB000713A 135-146 IPB000713B 226-236 IPB000713C 379-398***** IPB013221 (Mur ligase, middle region) with a combined E-value of 2.1e-12. IPB013221A 137-146 IPB013221B 225-236 IPB013221C 328-338","Residues 50-129 are 63% similar to a (SYNTHETASE ATP-BINDING LIGASE DIVISION ENZYME UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--26-DIAMINOPIMELATE CELL UDP-MURNAC-TRIPEPTIDE CEL) protein domain (PD932781) which is seen in Q6NGC3_CORDI.Residues 205-252 are 72% similar to a (LIGASE SYNTHETASE CELL ATP-BINDING ENZYME DIVISION UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--26-DIAMINOPIMELATE UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE UDP-MURNAC-TRIPEPTIDE MESO-) protein domain (PD212530) which is seen in Q6A9Q7_PROAC.Residues 363-421 are 72% similar to a (SYNTHETASE LIGASE ATP-BINDING UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--26-DIAMINOPIMELATE UDP-MURNAC-TRIPEPTIDE ENZYME MESO- UDP-N-ACETYLMURAMYL-TRIPEPTIDE DIAMINOPIMELATE-ADDING CELL) protein domain (PD858988) which is seen in MURE_SYNY3.Residues 423-521 are 59% similar to a (SYNTHETASE LIGASE ATP-BINDING UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--26-DIAMINOPIMELATE UDP-MURNAC-TRIPEPTIDE ENZYME MESO- UDP-N-ACETYLMURAMYL-TRIPEPTIDE DIAMINOPIMELATE-ADDING CELL) protein domain (PD266823) which is seen in Q6NGC3_CORDI.","","-44% similar to PDB:1E8C STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI (E_value = 9.9E_46);","Residues 46 to 125 (E_value = 2.1e-10) place ANA_1106 in the Mur_ligase family which is described as Mur ligase family, catalytic domain.Residues 135 to 342 (E_value = 6.3e-43) place ANA_1106 in the Mur_ligase_M family which is described as Mur ligase middle domain.Residues 362 to 450 (E_value = 1.3e-24) place ANA_1106 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain.","","ligase(EC 6.3.2.13) (UDP-N-acetylmuramyl-tripeptide synthetase) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-tripeptide synthetase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1108","1187211","1185412","1800","4.91","-21.73","63402","GTGAATCCCTCGCGTCGTCAGGCGCTCCAGCTCGGAGGGCTGCTCATGTTCACCGCACTGGCCGGGCGCACCGTCTACGTCCAGGCGGTCGAGGGGCCCGAGCTGGCTGAGAAGGCGAAGGCCGAGCGCACGGTCACCTGGGTCAACCGAGCCCCCCGTGGCGACATCACCGGACGCGACGGCACCGTCCTGGCCTCCTCGGCGGTCAGCTACGACGTCGGTGTCAACCAGTCCGCCATCGCCCAGTACGAGCGCACCGAGATGCGCCTCAATGAGTCCACCGGCGCCAATGAGAAGGTCGTCGTCGACTACGGGGCGACCGCGGTCGCGGCCCAGCTTGCCCCGATCCTCAACGTCGATCCTCTCGAGCTCGGAGCCAAGCTGGTGGGAAACCGGAGCTATGAGGTCATCGCCCAGGAGGTCTCTCCTGACACCTGGCGCAAGATCAAGGCCCTGGACATTCCCGGGGTCGAGCCCGACCAGCGCACCCGACGTACCTACCCGGCTGGGACCGTGGCCGGCAACGTCCTGGGCTTCACCCACGAGGGTGAGCACAACCGCGAGCTCATCGGGGCGGCTGGGCTGGAGCTCACCCAGAACAAGGTCTTGACGGGAACCGACGGCAAGGGCAGCGAGGAGGTGGGGCGCAGCGGTGTCATCATCCCCACCGGCGAGCAGGAGGACGAACCGGCCAGACCCGGTTCCACGGTGCGCACCACCCTCAACCCCGACCTGCAGTCCATCGCCCAGGAGACCATCGACAAAACGGTTGCAGCCCAGCACGCCGACTGGGGCATCGTCATGGCCATGGAACCGGCCACCGGGAAGGTCGTGGTCCTGGCCGACTCCAACTCGGTCGACCCCTCCGACCCTGCGGCCACAGCCGAGGAGAACCGCACCGCCCGCAGCGTTCAAGCCGTCTTCGAGCCCGGAAGTGTCGGCAAGGTCGTCACCTTCGCCACCGCTCTGGAGGAGGGGGTCGTCAAGCCCGAGGACACCTGGACCGTCCCGTACACCTGGACCTCGGCCAACGGGCAGACCTTCAAGGACTCCCACGAGCACGAGACCCAGACCATGACCACCGCCGGAGTCCTGGCGGAGTCCTCCAACGTCGGCACCGTGCAGATCGGCGAGAAGCTCGCCGACGACGTCCGCTACAAGTACATGAAGCGCTTCGGCTGGGGGCAGGCCACGGGCATCGAGATGCCGGCGGAGTCCGACGGCATCCTCTACCCGCCCAGCTCCTGGGACGACCGCACCCGCTACACCACCATGTTCGGGCAGGGTGTGGCCGGTACCACCCTCCAGTCGATCCAGGTGCTGGCCACCGTGGCCAACAAGGGAGTGCGCGTGGCCCCGCGCGTCATCGACGCCTGGATCGACGCCGACGGCAAGGAGACTCCGCAGAAGCGCCCCGAGGAGGTGCGGGTCATCTCCGAGGCGACGGCCAAGACCCTCACCGAGATGCTCATCGGAGTCACCCAGGAGGGCGGTACCGCGGAGTCCGCCTCCATCAACGGCTACCTGGTGGCCGGTAAGACCGGAACCACCGAGATCCTCAGCGACGACTCCACCGTGGCCTCCTTCGTCGGCTTCCTGCCGGCCCGTGACCCGGTGCTGGCCATCGCAGTCATCGTCAACCGGCCCGAGGGAATCTACGGAGGCACTGTTGCCGCCCCCGTCTTCCGAGAAGTGGCGCTGGCCGCCATGCAGGCACTCAACATTGCCCCGGACCCGAGCGTCGTGGCGGCCCAGGCCGCTCGCAACGGGGCCGGGGGAGAGCGTGACGCGAACCAGTGA","VNPSRRQALQLGGLLMFTALAGRTVYVQAVEGPELAEKAKAERTVTWVNRAPRGDITGRDGTVLASSAVSYDVGVNQSAIAQYERTEMRLNESTGANEKVVVDYGATAVAAQLAPILNVDPLELGAKLVGNRSYEVIAQEVSPDTWRKIKALDIPGVEPDQRTRRTYPAGTVAGNVLGFTHEGEHNRELIGAAGLELTQNKVLTGTDGKGSEEVGRSGVIIPTGEQEDEPARPGSTVRTTLNPDLQSIAQETIDKTVAAQHADWGIVMAMEPATGKVVVLADSNSVDPSDPAATAEENRTARSVQAVFEPGSVGKVVTFATALEEGVVKPEDTWTVPYTWTSANGQTFKDSHEHETQTMTTAGVLAESSNVGTVQIGEKLADDVRYKYMKRFGWGQATGIEMPAESDGILYPPSSWDDRTRYTTMFGQGVAGTTLQSIQVLATVANKGVRVAPRVIDAWIDADGKETPQKRPEEVRVISEATAKTLTEMLIGVTQEGGTAESASINGYLVAGKTGTTEILSDDSTVASFVGFLPARDPVLAIAVIVNRPEGIYGGTVAAPVFREVALAAMQALNIAPDPSVVAAQAARNGAGGERDANQ$","Peptidoglycan glycosyltransferase","Cytoplasm, Membrane, Extracellular","peptidoglycan synthetase; penicillin-bindingprotein 3 precursor","peptidoglycan glycosyltransferase ","Peptidoglycan glycosyltransferase","","Pares S., Mouz N., Petillot Y., Hakenbeck R., Dideberg O. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 1996. 3(3):284-289. PMID: 8605631","","","

InterPro
IPR001460
Domain

Penicillin-binding protein, transpeptidase
PF00905	$\"[265-567]T$	Transpeptidase

InterPro
IPR005311
Domain

Penicillin-binding protein, dimerisation domain
PF03717	$\"[48-225]T$	PBP_dimer

noIPR
unintegrated

unintegrated
G3DSA:3.40.710.10	$\"[244-566]T$	no description
signalp	$\"[1-29]?$	signal-peptide

","BeTs to 17 clades of COG0768COG name: Cell division protein FtsI/penicillin-binding protein 2Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0768 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB005311 (Penicillin-binding Protein dimerisation domain) with a combined E-value of 3.5e-16. IPB005311A 53-65 IPB005311B 156-180 IPB005311C 191-208","Residues 51-237 are 49% similar to a (PENICILLIN-BINDING 2X PENICILLIN BINDING CELL PENA PEPTIDOGLYCAN DIVISION SPORULATION SYNTHETASE) protein domain (PD002485) which is seen in Q8CWF2_BIFLO.Residues 203-303 are 53% similar to a (PENICILLIN-BINDING) protein domain (PD920728) which is seen in Q83NG6_TROW8.Residues 302-461 are 63% similar to a (PENICILLIN-BINDING BINDING 1A CELL PENICILLIN PEPTIDOGLYCAN DIVISION 2B GLYCOSYLTRANSFERASE 1B) protein domain (PD000435) which is seen in Q8CWF2_BIFLO.","","-44% similar to PDB:1PYY Double mutant PBP2x T338A/M339F from Streptococcus pneumoniae strain R6 at 2.4 A resolution (E_value = 8.2E_36);-44% similar to PDB:1QME PENICILLIN-BINDING PROTEIN 2X (PBP-2X) (E_value = 8.2E_36);-44% similar to PDB:1QMF PENICILLIN-BINDING PROTEIN 2X (PBP-2X) ACYL-ENZYME COMPLEX (E_value = 8.2E_36);-44% similar to PDB:1RP5 PBP2x from Streptococcus pneumoniae strain 5259 with reduced susceptibility to beta-lactam antibiotics (E_value = 3.1E_35);-44% similar to PDB:1PMD PENICILLIN-BINDING PROTEIN 2X (PBP-2X) (E_value = 2.9E_33);","Residues 48 to 225 (E_value = 5.7e-23) place ANA_1108 in the PBP_dimer family which is described as Penicillin-binding Protein dimerisation domain.Residues 265 to 567 (E_value = 1.9e-75) place ANA_1108 in the Transpeptidase family which is described as Penicillin binding protein transpeptidase domain.","","synthetase; penicillin-binding protein 3 precursor","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1109","1187682","1187218","465","9.98","5.41","15833","ATGAGCGCCACTGCTACTGCTCGAGTCACCCGCCCGATCGCGACGCGGCGCACCGCCCAGGCAAGTGGTACCACCAGCACCCAGGGGCGCGCGGAGGCGGGCTCCGCCAACCGGCCCCAGCTGCGCGTCGTCAGCGGCGCCTCCCAGGCCGCCTCGTCATCCCTTCCCTTCCTGACCGTCATCATCCTCGTGCTGGCCGGTGCACTCATCACCTCGATGCTCCTCAACGCCAAGATGGCTGACACCGCCTACCGGATGAAGGAGAAGCAGATCGAGCTCAACGTCGCCGAGGACCACGTCGAGACCCTGCGTACCCAGGTGCAGGAGGCCTCGGCACCCGACGCGCTGGCCGGCCGCGCCAAGGAGCTCGGGATGGTGCCCGCCGCCGCGCCCGGCGTCGTCGACGTCAACAAGGGGCAGCTCACCGAGGGAACCCCCGCCCACGCCGCCAAGAGCGGGAAGTAG","MSATATARVTRPIATRRTAQASGTTSTQGRAEAGSANRPQLRVVSGASQAASSSLPFLTVIILVLAGALITSMLLNAKMADTAYRMKEKQIELNVAEDHVETLRTQVQEASAPDALAGRAKELGMVPAAAPGVVDVNKGQLTEGTPAHAAKSGK$","Hypothetical protein","Cytoplasm, Extracellular","probable membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[57-77]?$	transmembrane_regions

InterPro
IPR002903
Family

Bacterial methyltransferase
PTHR11265	$\"[1-291]T$	S-ADENOSYL-METHYLTRANSFERASE MRAW
PF01795	$\"[1-289]T$	Methyltransf_5
TIGR00006	$\"[1-289]T$	TIGR00006: S-adenosyl-methyltransferase Mra

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[2-294]T$	no description
PIRSF004486	$\"[2-290]T$	S-adenosyl-methyltransferase, MraW type

","BeTs to 18 clades of COG0275COG name: Predicted S-adenosylmethionine-dependent methyltransferase involved in cell envelope biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0275 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002903 (Bacterial methyltransferase) with a combined E-value of 1.2e-80. IPB002903B 24-37 IPB002903C 74-107 IPB002903D 125-165 IPB002903E 180-197 IPB002903F 215-231 IPB002903G 263-288 IPB002903C 73-106","Residues 193-278 are 68% similar to a (METHYLTRANSFERASE TRANSFERASE S-ADENOSYL-METHYLTRANSFERASE 2.1.1.- MRAW FAMILY METHYLASE ENRICHED 3D-STRUCTURE KIDNEY) protein domain (PD579631) which is seen in MRAW_STRAW.Residues 1-96 are 53% similar to a (METHYLTRANSFERASE TRANSFERASE S-ADENOSYL-METHYLTRANSFERASE MRAW 2.1.1.-) protein domain (PDA14207) which is seen in MRAW_CAUCR.Residues 1-235 are 40% similar to a (METHYLTRANSFERASE TRANSFERASE POSSIBLE L2719.09) protein domain (PD299699) which is seen in Q9U1A5_LEIMA.Residues 79-238 are 46% similar to a (METHYLTRANSFERASE TRANSFERASE S-ADENOSYL-METHYLTRANSFERASE 2.1.1.- MRAW) protein domain (PD663474) which is seen in MRAW_CANTP.Residues 100-191 are 75% similar to a (METHYLTRANSFERASE TRANSFERASE S-ADENOSYL-METHYLTRANSFERASE 2.1.1.- MRAW FAMILY METHYLASE AT5G10910/T30N20_180 SEQUENCING T30N20_180) protein domain (PD681949) which is seen in MRAW_MYCPA.Residues 193-278 are 68% similar to a (METHYLTRANSFERASE TRANSFERASE S-ADENOSYL-METHYLTRANSFERASE 2.1.1.- MRAW FAMILY METHYLASE ENRICHED 3D-STRUCTURE KIDNEY) protein domain (PD579631) which is seen in MRAW_STRAW.","","-56% similar to PDB:1M6Y Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAH (E_value = 3.1E_41);-56% similar to PDB:1N2X Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAM (E_value = 3.1E_41);-55% similar to PDB:1WG8 Crystal structure of a predicted S-adenosylmethionine-dependent methyltransferase TT1512 from Thermus thermophilus HB8. (E_value = 6.1E_37);","Residues 1 to 289 (E_value = 1.8e-112) place ANA_1110 in the Methyltransf_5 family which is described as MraW methylase family.","","MraW (mraW)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1112","1189607","1189176","432","5.99","-1.61","15851","GTGTTCCTGGGGACGCATGCACCCAAGCTGGACGAGAAGGGCCGTCTCATCCTCCCGGCGAAGTTCCGTGAGGAGCTTGCGGGCGGTGTGGTTCTGACTCGAGGTCAGGAGCACTGCCTGTACGCCTTCACCGCCGCCGAGTTCGAGCGCATGTACGCCCAGCTGCGCGAGGCCCCCCTCGCTCAGAAGCAGGCGCGCGACTACGTGCGAGTCATGCTCTCGGGAGCGGACTCGCAGATCCCGGACAAGCAGGGGCGTATCACCCTGCCGGCACCACTGAGGGCCTACGCAGGCCTGAAGAAGGACCTGGCGGTGATTGGAGCCGGCGCCCGGGTGGAGATCTGGGACTCCGAGTCCTGGAACACCTACCTGGCCGCCCAGGAACAGGTCTTCGCCGACACGGCCGAGGAGATCATCCCCGGCTTCTTCTGA","VFLGTHAPKLDEKGRLILPAKFREELAGGVVLTRGQEHCLYAFTAAEFERMYAQLREAPLAQKQARDYVRVMLSGADSQIPDKQGRITLPAPLRAYAGLKKDLAVIGAGARVEIWDSESWNTYLAAQEQVFADTAEEIIPGFF$","MraZ protein","Cytoplasm","conserved hypothetical protein TIGR00242","K03925 MraZ protein","MraZ protein","","","","","

InterPro
IPR003444
Family

MraZ
PD006745	$\"[19-128]T$	Q6AE55_BBBBB_Q6AE55;
PF02381	$\"[1-71]T$ $\"[72-142]T$	MraZ
TIGR00242	$\"[1-143]T$	TIGR00242: mraZ protein

","BeTs to 11 clades of COG2001COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2001 is ---------dr-b-ef-hsn-jx-twNumber of proteins in this genome belonging to this COG is 1","***** IPB003444 (Protein of unknown function UPF0040) with a combined E-value of 1.4e-46. IPB003444A 1-26 IPB003444B 39-55 IPB003444C 66-120","Residues 19-128 are similar to a (MRAZ DIVISION CELL 3D-STRUCTURE PROTEIN) protein domain (PD006745) which is seen in Q6AE55_BBBBB.","","-52% similar to PDB:1N0E CRYSTAL STRUCTURE OF A CELL DIVISION AND CELL WALL BIOSYNTHESIS PROTEIN UPF0040 FROM MYCOPLASMA PNEUMONIAE: INDICATION OF A NOVEL FOLD WITH A POSSIBLE NEW CONSERVED SEQUENCE MOTIF (E_value = 9.0E_17);-52% similar to PDB:1N0F CRYSTAL STRUCTURE OF A CELL DIVISION AND CELL WALL BIOSYNTHESIS PROTEIN UPF0040 FROM MYCOPLASMA PNEUMONIAE: INDICATION OF A NOVEL FOLD WITH A POSSIBLE NEW CONSERVED SEQUENCE MOTIF (E_value = 9.0E_17);-52% similar to PDB:1N0G Crystal Structure of A Cell Division and Cell Wall Biosynthesis Protein UPF0040 from Mycoplasma pneumoniae: Indication of A Novel Fold with A Possible New Conserved Sequence Motif (E_value = 9.0E_17);-49% similar to PDB:1VCO Crystal Structure of T.th. HB8 CTP synthetase complex with Glutamine (E_value = 9.0E_17);-67% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 9.0E_17);","Residues 1 to 71 (E_value = 2.2e-21) place ANA_1112 in the MraZ family which is described as MraZ protein.Residues 72 to 142 (E_value = 4.9e-17) place ANA_1112 in the MraZ family which is described as MraZ protein.","","hypothetical protein TIGR00242","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1113","1189938","1189765","174","9.65","2.12","6111","GTGCGGATCCGCTCGCATCTCCGCTCGGAGACCCTGAACCCCACCGGAACCCTGCATGCAGGCCGAGTGGACTCTGCTTTTTTCCTGGGTATCCACCACGCCGAGGAGGGTGGTGGTGAAGGCCTCCCTCCACCTGTCCTCCACCTCCCTCCACCCCGCATGAGCGGGCGGTGA","VRIRSHLRSETLNPTGTLHAGRVDSAFFLGIHHAEEGGGEGLPPPVLHLPPPRMSGR$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1114","1190663","1190250","414","9.66","2.67","14935","ATGGCACTGTCAGAGCGAGAGCAGCAGGTCCTACGAGACCTGGAATCGCAGCTCCATGAGGATGACCCCGAGCTGGCTCAGACCTTCCAGCGTCAAGAGCGCCGACTCTCGCGCCCCTCACCGCGCCATATCGGCGGTGGCGTGGCCCTGGTCCTCATCGGCCTGGCGCTCCTCATCGCAGGGGTCTCAGTGCCCCACAGCGTCCTGTCCATCCTGCTGGGGGTCGCCGGCTTCCTCGTGGCCGTCGGTGGGGTCGCACTGGCACTGACCCGGGTCGAGAGCACGACGAGCCCGCGTCAGTCCGAGGCTGGCCGGGACAGGCCCGCCAAGGGTGGTAGTGGCGCGAAGAAGCGTTCCTCCTTCATGGACCGCCAGTCAGAGCGCTGGGATCGCCGGCGCGACTCAGAGGACTGA","MALSEREQQVLRDLESQLHEDDPELAQTFQRQERRLSRPSPRHIGGGVALVLIGLALLIAGVSVPHSVLSILLGVAGFLVAVGGVALALTRVESTTSPRQSEAGRDRPAKGGSGAKKRSSFMDRQSERWDRRRDSED$","Conserved transmembrane protein","Membrane, Periplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[45-65]?$ $\"[71-89]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-61% similar to PDB:2AFT Formylglycine generating enzyme C336S mutant (E_value = );-61% similar to PDB:2AIJ Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide CTPSR (E_value = );-61% similar to PDB:2AIK Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide LCTPSRA (E_value = );-61% similar to PDB:2HI8 human formylglycine generating enzyme, C336S mutant, bromide co-crystallization (E_value = );-61% similar to PDB:2HIB human formylglycine generating enzyme, C336S mutant, iodide co-crystallization (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1115","1192062","1190710","1353","10.21","13.58","48712","ATGAGCAGAGCACCCCGTTCCCAGGCCGCACGCCGGTCCTGGGGGGACGATGACTCCGCCACCCCCATCATCCACGTCGACATGGACGCCTTCTTCGCCTCGGTCGAGCTCCTCGAGCACCCCGAGCTGGCCGGCCGTCCCGTCATCGTCGGCGGCCGCGACGGCCGGGGCGTCGTCTCGGCAGCCTCCTACGAGGCCCGCGCCTTCGGTGTCTCCTCGGCGATGTCCATGGCCGAGGCCTCCCGTCGCTGCCCCCAGGCCGTGGTCCTCCCCGTGCGCCACGGCCTCTACTCCCAGGTCTCCGCCCAGGTCATGGCCGTCCTGGCCGAGGTCACCCCCGCCCTGGAGAAGGTGAGCATCGATGAGGCCTTCCTGGACGTGAGCGGGGCCAGGCGCCGCATGGGCTCCCCGGTGACCATCGGCCGCTGGATCCGCGCCGAGATACGCCGGCGAGTGGGTGTTCCGGCCTCGGTGGGCATCGCCTCCACCAAGTTCATCGCCAAGCTCGCCTCCTCTCACGCCAAGCCCGACGGTCTGCTCCTGGTGCCGGCCGCCGCCACGCAGGACTTCCTCAACGTGCTGCCGGTCGGGGCCCTGTGGGGCGTCGGCACCCGGACGCAGGAGGTCCTGGCCAGGTGGGGGATCCAGGACGTGCGCACCCTGGCGGGCACTGACGTACGTCACCTGGAGAGGATCCTCGGCCGGGCCGCCGGACGCCACCTGCACGAGCTCTCCCACGGTGTCGACCCCCGCCGGGTCGAGCCGGTGCGCGAGGAGAAGTCGGTGGGCACCGAGACCACCTTCTTCGAGAACCTGACCGATCGGGAGCACGCACGGCGGGTCCTGCTGGACCAGACTCACCAGTGTGCCGCCCGCCTGCGCGCGGTGGACCTGCGCTGCCGTGTCGCTGTGCTCAAGGCCCGAGGGGCTGACTTCACCACCGTCACCCGCTCACGCACCCTGGCCACCCCCACCGACCTCGCCCAGGACATCTGGGAGACCATCTCCTCGCTCTACTCCGCCCTGCCCACCCCGCCCGGCGGCTTCCGCCTCCTGGGGGTCCGGGTCGAAGGACTGCTGCGCCCCGACGACGGTGTGCAGCTCCTCCTGGACGAGGACCCGCGGCGCGGCGCCCCAGAGCGTGCCGCCGACGCCGTACGCCGCAGGTGGGGCGCCAACGCACTGGCCCCGGCCAGCCTCCTGCCAGGAGACGGTGCCACCCGGACACCGCGCGGCTCGACAGAGGACCACCGAGAGGGCGGGGCCGTCGGTGATCCGAGCAGAAGAGCCGGTTCTCGCCCCGACCAACCTCCCAGGAAAGTTTCTCCTGAGCGGCCACAGCGCCTATCCTGA","MSRAPRSQAARRSWGDDDSATPIIHVDMDAFFASVELLEHPELAGRPVIVGGRDGRGVVSAASYEARAFGVSSAMSMAEASRRCPQAVVLPVRHGLYSQVSAQVMAVLAEVTPALEKVSIDEAFLDVSGARRRMGSPVTIGRWIRAEIRRRVGVPASVGIASTKFIAKLASSHAKPDGLLLVPAAATQDFLNVLPVGALWGVGTRTQEVLARWGIQDVRTLAGTDVRHLERILGRAAGRHLHELSHGVDPRRVEPVREEKSVGTETTFFENLTDREHARRVLLDQTHQCAARLRAVDLRCRVAVLKARGADFTTVTRSRTLATPTDLAQDIWETISSLYSALPTPPGGFRLLGVRVEGLLRPDDGVQLLLDEDPRRGAPERAADAVRRRWGANALAPASLLPGDGATRTPRGSTEDHREGGAVGDPSRRAGSRPDQPPRKVSPERPQRLS$","DNA-directed DNA polymerase","Cytoplasm, Membrane","DNA-damage-inducible protein P","DNA-directed DNA polymerase ","DNA-directed DNA polymerase","","Smith B.T., Walker G.C. Mutagenesis and more: umuDC and the Escherichia coli SOS response. Genetics 1998. 148(4):1599-1610. PMID: 9560379","","","

InterPro
IPR001126
Domain

UMUC-like DNA-repair protein
PF00817	$\"[26-361]T$	IMS
PS50173	$\"[23-203]T$	UMUC

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.20	$\"[183-249]T$	no description
G3DSA:3.30.1490.100	$\"[256-372]T$	no description
G3DSA:3.30.70.270	$\"[84-182]T$	no description
PTHR11076	$\"[25-361]T$	DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER
PTHR11076:SF12	$\"[25-361]T$	DNA POLYMERASE IV / KAPPA

","BeTs to 10 clades of COG0389COG name: Nucleotidyltransferase/DNA polymerase involved in DNA repairFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0389 is -o----y---rlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is 2","***** IPB001126 (UMUC-like DNA-repair protein) with a combined E-value of 4.6e-72. IPB001126A 23-50 IPB001126B 56-85 IPB001126C 97-128 IPB001126D 154-178 IPB001126E 190-221","Residues 23-88 are similar to a (DNA POLYMERASE IV TRANSFERASE REPAIR DNA-DIRECTED POL MUTATOR DNA-BINDING REPLICATION) protein domain (PD002051) which is seen in DP43_RHILO.Residues 166-214 are similar to a (DNA POLYMERASE IV TRANSFERASE REPAIR DNA-DIRECTED POL MUTATOR DNA-BINDING REPLICATION) protein domain (PD186422) which is seen in Q6AEF3_BBBBB.Residues 166-243 are similar to a (DNA POLYMERASE PLASMID REPAIR IV UMUC TRANSFERASE MUCB MUTAGENESIS SOS) protein domain (PD683433) which is seen in Q73P36_TREDE.","","-46% similar to PDB:1JX4 Crystal Structure of a Y-family DNA Polymerase in a Ternary Complex with DNA Substrates and an Incoming Nucleotide (E_value = 1.6E_25);-46% similar to PDB:1JXL Crystal Structure of a Y-Family DNA Polymerase in a Ternary Complex with DNA Substrates and an Incoming Nucleotide (E_value = 1.6E_25);-46% similar to PDB:1N48 Y-family DNA polymerase Dpo4 in complex with DNA containing abasic lesion (E_value = 1.6E_25);-46% similar to PDB:1N56 Y-family DNA polymerase Dpo4 in complex with DNA containing abasic lesion (E_value = 1.6E_25);-46% similar to PDB:1RYR REPLICATION OF A CIS-SYN THYMINE DIMER AT ATOMIC RESOLUTION (E_value = 1.6E_25);","Residues 26 to 361 (E_value = 2.4e-97) place ANA_1115 in the IMS family which is described as impB/mucB/samB family.","","protein P (PA0923)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1116","1192210","1192986","777","5.56","-4.37","27867","GTGCGCACTTCCCTGGCCACGGCCGAGCTCGTGGCGCGAGACACCGGGATCCTTCTCATGCTCGACGGCGCGGAGTCCTCCTTCCTGGACCTGCGCGACCCCTCCCACCTGGACTTCGAGTACCACCAGCAGATGGACGCGGTGCTCACGGCGCTGCGCGGTGAGGGCGAACCCCTCAGGGCACTCCACCTGGGTGGGGCGGGCTGCGCCCTGGCCAGGGCGTGGGACGTGACCCGTCCCGGCTCCCAGCAGGTCGCCGTCGAGATCGATGAGATCCTCGCGAGCCAGGTGCGGACCTGGTTCGACCTGCCCCGGTCCCCCAGGCTGCGGATCCGGGTCGGCGACGCCGCCGAGGTGGTGGCGGGGCTGCGGCCGGGCCAGTGGGACGTCGTGGTGCGCGACGTGTTCGACGGCGGGAGCGTGCCGGCCTCCTGCAGGAGCCGGGAGTTCTTCGACTCCTGCCTGAGGGCGCTGGCGCCCGACGGCCTGCTGCTGGTCAACACCGCCTCCATGCCGCGCGCCATGGCCGGCGCTGAGATCGCCGCGCTCTCCGGCGCCCTGGACGGGGACATCTCCCGCGCGTTCATCGTCGCCGATCCCGCCTCGGCGCGTGGCCGGCGCCGGGGCAACCTGGTGCTGGTGGCCCGCCAGGACCCCTTCACGGTGGGCGAGCTCGAGGAGGTCGAGCGCGCAGTGCGCCGCCTGCTGCTGCCGGTGCGCACCTGGTCGCTCGATGACGCCGCGCTACCGCGCCCTGAGGGCGGCCGGGCCCGCTAG","VRTSLATAELVARDTGILLMLDGAESSFLDLRDPSHLDFEYHQQMDAVLTALRGEGEPLRALHLGGAGCALARAWDVTRPGSQQVAVEIDEILASQVRTWFDLPRSPRLRIRVGDAAEVVAGLRPGQWDVVVRDVFDGGSVPASCRSREFFDSCLRALAPDGLLLVNTASMPRAMAGAEIAALSGALDGDISRAFIVADPASARGRRRGNLVLVARQDPFTVGELEEVERAVRRLLLPVRTWSLDDAALPRPEGGRAR$","Spermidine synthase","Cytoplasm","Spermidine synthase","hypothetical protein","Spermidine synthase-like","","Hashimoto T., Tamaki K., Suzuki K., Yamada Y. Molecular cloning of plant spermidine synthases. Plant Cell Physiol. 1998. 39(1):73-79. PMID: 9517003Korolev S., Ikeguchi Y., Skarina T., Beasley S., Arrowsmith C., Edwards A., Joachimiak A., Pegg A.E., Savchenko A. The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nat. Struct. Biol. 2002. 9(1):27-31. PMID: 11731804","","","

InterPro
IPR001045
Family

Spermine synthase
PTHR11558	$\"[87-171]T$	SPERMIDINE/SPERMINE SYNTHASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[33-171]T$	no description

","BeTs to 4 clades of COG0421COG name: Spermidine synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0421 is a-mpkzyqvdr-b-ef--snuj----Number of proteins in this genome belonging to this COG is 2","***** IPB001045 (Spermine synthase) with a combined E-value of 2.3e-07. IPB001045B 51-102 IPB001045C 104-121 IPB001045D 128-152","Residues 78-163 are 61% similar to a (SPERMIDINE SCO2803 SCO1320 SYNTHASE) protein domain (PDA1D9Z5) which is seen in Q6ACX4_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","synthase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1117","1193986","1193048","939","4.60","-26.11","33360","GTGAGACCACTGTTCACCATCCAGCACCCCGCGGATCAGCCGATCTCCCCGAGGGTCCTCATCCACTACTTCGAGGGCGCCATGGACGCCGGCAACGCCGGCGCCCTGGCCGTCGACCAGCTGCTCATGACGCTTCCCAGCGAGCGTGTCGCTACCTTCGACATCGACGCCCTCGTGGACTATCGCGCCAGGCGTCCCACGATGACCTTCGTCCACAACAACTACTCCTCAGTCATCATGCCCGAGCTGGTCCTGGACCTCCTCCATGACGACGACGGCGAGGACGTCCTCCTGCTCCACGGCAGCGAGCCGGACTACCGCTGGGACGAGTTCGTCGGAGCCGTGGCCCACCTGGCCGTCTCCATGGGCGTGAGCCAGGCCGTCGGCATGAGTGGCATCCCCATGGCAGTGCCTCACACACGCCCGACCTACGTGCACCATCACGGCAGCCAGCCCGACCTGCTGCCCAACCAGCCCGAGCTCTTCGGGCACGTCGAGCTGCCCGGGTCGATGTCGGCCTACCTCGAGCTGCGTCTGGGCGAGCTGGGCCTGGACTCCCGGGGAGTCTCGGCCGCGATCCCGCACTACGTGGCCCGCGACGAGTTCCCGCAGGGAGCCTCGGCGCTGCTGACCGCCGTCGTGCAGGCCACTGGCCTGGCACTGCCGGTGGGGGACCTCGAGGCCGCCGCCAGCATCAACCGTGCCGAGATCAACGCCGAGGCCGCCCAGCAGCCGGAGGTCAGCGCCGTCGTCTCCGCCCTGGAGGCCCAGTACGACGCCATGGCCCCCAGGATCGCCATCGATGAGGTCGACACCTCCGCGCCGATCCTCAACCTGCCCAGCGCCGAGGAGATCGGCGCACGCCTGGAGGCCTTCCTGGAGGCCAACGACTCCGGGGACATGGGGCCCCAGGGCTGGAACCCCGGCCGCGAGGGCTGA","VRPLFTIQHPADQPISPRVLIHYFEGAMDAGNAGALAVDQLLMTLPSERVATFDIDALVDYRARRPTMTFVHNNYSSVIMPELVLDLLHDDDGEDVLLLHGSEPDYRWDEFVGAVAHLAVSMGVSQAVGMSGIPMAVPHTRPTYVHHHGSQPDLLPNQPELFGHVELPGSMSAYLELRLGELGLDSRGVSAAIPHYVARDEFPQGASALLTAVVQATGLALPVGDLEAAASINRAEINAEAAQQPEVSAVVSALEAQYDAMAPRIAIDEVDTSAPILNLPSAEEIGARLEAFLEANDSGDMGPQGWNPGREG$","Uncharacterized conserved protein","Cytoplasm","Protein of unknown function (DUF774)superfamily","hypothetical protein","protein of unknown function DUF75","","","","","

InterPro
IPR002766
Family

Protein of unknown function DUF75
PF01908	$\"[16-261]T$	DUF75

InterPro
IPR008492
Family

Protein of unknown function DUF774
PIRSF028754	$\"[2-305]T$	Uncharacterised conserved protein

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 24-262 are 57% similar to a (ALANINE LEUCINE RICH SCO1997 ML1306 MLCB2533.03C B2235_F1_6 ML1009 CGL1923 MB2149) protein domain (PD017725) which is seen in Q9S2K6_STRCO.","","-50% similar to PDB:2P90 The crystal structure of a protein of unknown function from Corynebacterium glutamicum ATCC 13032 (E_value = 9.1E_43);-42% similar to PDB:2BYZ STRUCTURE OF E. COLI KAS I H298Q MUTANT IN COMPLEX WITH C12 FATTY ACID (E_value = 9.1E_43);-42% similar to PDB:2BZ4 STRUCTURE OF E. COLI KAS I H298Q MUTANT (E_value = 9.1E_43);-41% similar to PDB:1H4F E. COLI BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I K328R (E_value = 9.1E_43);-47% similar to PDB:2BYW STRUCTURE OF ESCHERICHIA COLI BETA-KETOACYL (ACYL CARRIER PROTEIN) SYNTHASE I LYS328ALA MUTANT (E_value = 9.1E_43);","Residues 16 to 261 (E_value = 3.3e-36) place ANA_1117 in the DUF75 family which is described as Protein of unknown function DUF75.","","of unknown function (DUF774) superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1120","1194490","1197087","2598","6.05","-9.60","93598","GTGAGTCAGACGATCCCCTCTCGCCCACCGCACTCCCAGCAGGAAGCGCAGCCGCGGGCAGAGGACGATGCGGGCAGTGTCCGCGAGCGCGAGATGCGCGGTGAGCAGGTCGTCGTCGATCTGGCCTACAACGAGCTGGACCGCCAGCTGGCTCAGGCCCGTCACTCCCTGGCCCGTACCGAGGCCCAGGGCGTCAGCGGCACCCACCAGTCCCGCGGGGAGCGGGACGCCTACGCCGTGCACTACTCGTCGCTGGTCTCTTCCCTGGAGGGGGTCGAGGACCGTCTGGTCTTCGGGCGGATGGATATGAGCACCTCGCCCGATGACACGCCGGACTCGGAGGCCTCGGGGAGAGCCTCATCCTCCGGCTCCGGCAGGGGCGTGGGCGGTTCCTCCCCCGTCACTGACGGGGGCCGGCGCCACTATGTGGGTCGTATTGGCCTGCAGGACGCCCAGCACCGTGAGGTGATCCTGGACTGGCGCGCCCCTCTGGCCCGGGCCTTCTATCAGGCCACGGCCTCCGAGCCCATGGGGCTGGTGCGTCGGCGGCACATCGATACCCGGGCCCGTCAGGTGCTCGGGGTGGAGGACGAGGTCCTGGACCTGGACGCCCTGGAGGCCGGCGAGGGCCTGTCCGACTCATCCGGGACGGCCGTGACCGCCGAGGACCTGCAGGGCGAGGGTGCACTCATCGCCGCGATGTCCAGCGCCCGTGACGGCCGTATGGGTGACATCGTGGCCACGATCCAGGCCGAGCAGGACCGGGTCGTCACCTCCTCGGGCCGGGGTGTGCTCGTGGTCCAGGGCGGCCCGGGCACGGGTAAGACGGCCGTGGCACTGCACCGGGTGGCCTACCTGTTCTACTCCGAGCGCGAGCGCCTGGAGCGTTCCGGCGTGCTCCTGGTGGGGCCGTCGCGCACCTTCCTGCGCTATGTGGAGCAGGTGCTGCCCTCCCTGGGTGAGACGGGGGTGGTTTCCACGACGATTGGCGACCTGGTTCCCGGAGTGCGGGCCACGGCGCAGGAGGACGCCCGCGTCGCCGAGCTCAAGGGGCGCTCCCTGTGGGTCAAGGCCCTGGAGCGGGCGGTGCGGGGCCTGCAGCGCGTCCCGGATGCTCCCCGCGAGATCGAGGTCCAGGGTGTGCGCCTGTCCCTGGAGCCCGACGACGTGCGTGAGGCGGCCTCCCGGGCCCGTCGGGGCGGCAAGCCCCACAACCTGGCCCGCGAGGCCTTCGTGATCTGGCTCCTGGAGCGCCTGACCGACCAGTACGCGGCGGCCACGAACCAGGATGCCTCGGACGCTGACACGCGCGCCTGGATCCGGGAGGACATCCGTACCGCCCGTGACGCCCGCCGAGAGATCAACCTGTGCTGGATGCCGACAACGCCCCAGGGGCTGCTGGAGCGCCTGTGGAGCCGGCCCGCCCTCCTGGAGCAGGTGGCGCCGTCCTTGAGCGAGCAGGAGCGTGCGCTGCTGCACCGTGGGCCCGGGAGCGCTCTGAGTGCGGCGGACATCCCGCTCATTGACGAGCTGGCCGAGCTGCTGGGCCCCAGTGAGGACGCCCAGGCCCGGCGCGCCCGGCTGGAGGCCCGCCGCCGCGAGGACCTGGTGGCCTACGCGGCCCAGGCGATCGAGTCCCAGGAGCTGGGCGGCGGGATGGTCAGTGCCGAGATGCTGGCCGACCGGGTCTCCCAGGGCGGTCCGACTCTGACTCTGGCCGAGCGGGCCCGGGCGGATCGGACGTGGACCTACGGGCACGTCGTCGTCGATGAGGCTCAGGAGCTGGGCACCATGGCGTGGCGGGCGCTGGCGCGTCGCTGCCCGGTGCGCTCCTTCACCGTGGTGGGGGACCTGGCCCAGTACTCGGGCCCCCACGCCCCGGGCAGCTGGGGCGGGGTGCTCACCGCCCTGGGGACGGCGTCGGCTGATGATGCTGCGGAGGCCCAGGGCCGGTCCCGGTCGCAGTCGCGTCACCGGGCCCGTTCGCGCTCGCGGCAGGGCCGGCAGTCGGGGCGCTCGCGTGGAGGGTCGACCCCGCTGCGCGAGGAGGCCCTCAGCGTCTGCTACCGCACGCCGGCCACGATCATGGAGGCGGCCGAGGAGACGGTGACGCAACTGGGCCACCCGCCGGTCTACCCGGTGCGCTCGGTGCGCGACCTGCCCGACTGCCTGGAGGTCACCGACCTGTCACAGTCCCCTGAGGGTGGGCAGCCCGAGGCCTGGGCGAGCCTCCTGCGCAAGGTCGTGGCCCAGGAGTCGGCCCGCCTGGACGAGCAGGTGGGGGCCGGCGTCGGGCGCATCGCGGTCATCTGCCCCTCCCCCGGGCGCACTGAGGCGCTGCTGCGCCAGGACCCGGACCTGGTCGCGGCGATGGAGGCTCCGGGAGGTGACGTGCTGCGCTCGCGGCTGCTGGTGGTCGACCCGGTGCTGTCCAAGGGGCTGGAGTTCGACGTCGTGGTGCTCGTGGATCCCACTGAGATCGGTGAGCGCAGCGCGGGAGACCTGTACGTGGCGATGACTCGTCCCACGCGCCGCCTGCGGGTGGTCAGCCGCCTACCGCTCCTCCGGGGCCTGGAGCCGCGTTCCTCCGGCCGGTGA","VSQTIPSRPPHSQQEAQPRAEDDAGSVREREMRGEQVVVDLAYNELDRQLAQARHSLARTEAQGVSGTHQSRGERDAYAVHYSSLVSSLEGVEDRLVFGRMDMSTSPDDTPDSEASGRASSSGSGRGVGGSSPVTDGGRRHYVGRIGLQDAQHREVILDWRAPLARAFYQATASEPMGLVRRRHIDTRARQVLGVEDEVLDLDALEAGEGLSDSSGTAVTAEDLQGEGALIAAMSSARDGRMGDIVATIQAEQDRVVTSSGRGVLVVQGGPGTGKTAVALHRVAYLFYSERERLERSGVLLVGPSRTFLRYVEQVLPSLGETGVVSTTIGDLVPGVRATAQEDARVAELKGRSLWVKALERAVRGLQRVPDAPREIEVQGVRLSLEPDDVREAASRARRGGKPHNLAREAFVIWLLERLTDQYAAATNQDASDADTRAWIREDIRTARDARREINLCWMPTTPQGLLERLWSRPALLEQVAPSLSEQERALLHRGPGSALSAADIPLIDELAELLGPSEDAQARRARLEARRREDLVAYAAQAIESQELGGGMVSAEMLADRVSQGGPTLTLAERARADRTWTYGHVVVDEAQELGTMAWRALARRCPVRSFTVVGDLAQYSGPHAPGSWGGVLTALGTASADDAAEAQGRSRSQSRHRARSRSRQGRQSGRSRGGSTPLREEALSVCYRTPATIMEAAEETVTQLGHPPVYPVRSVRDLPDCLEVTDLSQSPEGGQPEAWASLLRKVVAQESARLDEQVGAGVGRIAVICPSPGRTEALLRQDPDLVAAMEAPGGDVLRSRLLVVDPVLSKGLEFDVVVLVDPTEIGERSAGDLYVAMTRPTRRLRVVSRLPLLRGLEPRSSGR$","DNA helicase","Cytoplasm, Periplasm","DNA helicase","hypothetical protein","Superfamily I DNA and RNA helicase-like","","Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 1997. 90(4):635-647. PMID: 9288744","","","

InterPro
IPR000212
Family

UvrD/REP helicase
PTHR11070	$\"[262-373]T$ $\"[508-620]T$	UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580	$\"[249-286]T$	UvrD-helicase

InterPro
IPR014016
Domain

Helicase superfamily 1, UvrD-related
PS51198	$\"[248-692]T$	UVRD_HELICASE_ATP_BIND

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[238-620]T$	no description

","BeTs to 9 clades of COG0210COG name: Superfamily I DNA and RNA helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0210 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 4","***** IPB000212 (UvrD/REP helicase) with a combined E-value of 6.5e-12. IPB000212A 269-279 IPB000212D 580-596 IPB000212G 805-821 IPB000212H 830-842","Residues 138-248 are 63% similar to a (HELICASE DNA ATP-DEPENDENT 3.6.1.- HYDROLASE FAMILY UVRD/REP I SUPERFAMILY RNA) protein domain (PD883795) which is seen in Q8G4R2_BIFLO.Residues 249-342 are 81% similar to a (HELICASE DNA ATP-DEPENDENT 3.6.1.- HYDROLASE UVRD/REP I FAMILY SUPERFAMILY RNA) protein domain (PD332785) which is seen in Q6ACW6_BBBBB.Residues 288-516 are 55% similar to a (HELICASE DNA ATP-DEPENDENT ATP/GTP BINDING OR ATP/GTP-BINDING RNA I SCO5439) protein domain (PD856986) which is seen in Q8FTQ9_COREF.Residues 444-588 are 64% similar to a () protein domain (PDA08965) which is seen in Q8G4R2_BIFLO.Residues 588-634 are 68% similar to a (HELICASE DNA ATP-DEPENDENT HYDROLASE 3.6.1.- II EXONUCLEASE SUBUNIT ATP-BINDING BETA) protein domain (PD003735) which is seen in Q9L1K5_STRCO.Residues 589-637 are 61% similar to a (HELICASE DNA ATP-DEPENDENT ATP/GTP BINDING) protein domain (PD682604) which is seen in Q8G4R2_BIFLO.","","No significant hits to the PDB database (E-value < E-10).","Residues 249 to 286 (E_value = 9.2e-06) place ANA_1120 in the UvrD-helicase family which is described as UvrD/REP helicase.","","helicase (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1121","1197248","1199164","1917","6.36","-4.49","67237","ATGAGTGCTTCACACGCGTCGGTAGCCGCGCTCACGCGTGGCGCCGCGTCGGCGGCCGGCTCGGACGCCTTTGGCGCTGAGGCCCTTGAGGCCGTCTACCAACAGGCGGGGGTGCCCTCCACGATCCCTGCGGTGGGCGAGCCCCTGTCCTGCATGCTGCGCGACGCCGCCCGGGACTTCCCGGACCGAGTGGCCCTGGACTTCCTGGGAGCGACCACCACCTACTCCCAGATGGAGACTCAGGTGGCGCGGGCCGCGGAGGCCCTGCGGGGCCTGGGGGTCGGGCGCGGGGACGTTGTCGGGCTCATTCTTCCCAACTGCCCTCAGCACGTGGTCGTGGCCTACGCGGCCTGGCGCATCGGGGCGATCGTGGCCGAGCACAACCCGCTGGCGCCCGCCGCCCAGCTGCGCGAACAGTTCCACATCCACCGCGGGCGCGTCATCATCGCCTGGGAGAAGACCCTCGAGCGCCTCGTGGCGGCAGTGGGCTCCCTGGAGGCGGCGGGCCTGGGGGGCCTGAGCGTGTACTCAGTGGACCTGTCCCGTCACCTTCCTCTGCGCAGCCGCCTGGCCCTGAGGCTGCCGGTGGCGGCCGCCCGCACCCAGCGCCGCGAGCTGCGCGGGAGGATCCCGGCCGGGGTGCGCTCCTGGGACGACCTGGCCGCCTCCGCTATCCCCTTGGCCACGGGCTTCCCGCTGCCGAGCGTCTCGGAGGCGGCGGCTCTGCTGTACACCGGCGGGACGACGGGCACGCCCAAGGCCGTGTGCCTGACCCACGAGAACCTGCGCTCCAACGCCGAGATGTCCTTGGCCTGGGCGTCGGGCACCACGAGCGCGGGCAAGGAGACCTTCTACGCGGTCCTGCCCTTCTTCCACGCCTTCGGCATGTCCCTGTCGCTGCTGTGCGCGGTGGGGCTGGCCGCCACCCAGGTGGTGCTGCCCAAGTTCGGGGCGGACCTGGTGCTGGCCGCCTGGAAGCGGCGCCCGGCCACCTTCTTCCCGGGGGTGCCGGTCATGTTCGACCGTCTGGTGACCCGGGCGCGGGCCACCGGGGCGAACCTGTCCTCCTGCAAGATCGCCGTGTGCGGGGCGGCCCCCAACCCGCTGGCGGTGGCGCAGGCCTGGGAGGAGGCCACCGGGGGCACCATCATCGAGGGCTACGGGATGACCGAGTCCTCCCCCATCATCCTGGGCAACCCGATCTCGCCGGCGCGTCGGCCCGGCACCCTGGGGGTGCCCTACCCCTCCACGCAGGTGCGCCTGGTGGACCCTGAGGACGTCGAGCGCGAGGTGGCTCCCGGGGAGGTCGGCGAGCTGCTGGCCCGCGGCCCCCAGGTGTTCTCCGGCTACTGGGACAACCCCGAGGAGAGCGCCGAGGTGCTGCTGGACGGGGGCTGGCTGCGCACGGGCGACCTGGTGCGCCAGGAGGCGGACGGCTTCTACGTCATCGCCGACCGCCGCAAAGAGCTCATCATCTCCGGGGGCTTCAACATCTACCCCACGGAGGTGGAGGCCGCGGTCCGCTCGATGCCGCAGGTGGAGGAGGTCGCCGTCGTCGGGCTGCCGGCCGAGGCCGGCAATGAGTCCGTGGTCGCCGCGATCCTGCCCAAGGAGGGCCAGACGGTCACCTTGGAGCAGGTGCGCGAGTGGGCGGCCAAGAACCTGTCCAACTATGCCCTGCCGCGCCAGATCGCGATCCTGACCGAGATGCCCCGCTCCCAGATCGGCAAGGTGCTGCGGCGCGTGGTGCGCGACGAGCTCCTGGCGGCCCGAGAGGCGGCCTCCGGGGCGGCGACGGCGGCGGCCGTGTCCATCGTCGAGCACTTCCCCGGCAGGGGTGAGCGCAGGGACGGCGGTCAGCAGGAGGGCAGCCAGGACGGCAAGGCCGGGCCGCATGACAGCGCGGCCTCACACTGA","MSASHASVAALTRGAASAAGSDAFGAEALEAVYQQAGVPSTIPAVGEPLSCMLRDAARDFPDRVALDFLGATTTYSQMETQVARAAEALRGLGVGRGDVVGLILPNCPQHVVVAYAAWRIGAIVAEHNPLAPAAQLREQFHIHRGRVIIAWEKTLERLVAAVGSLEAAGLGGLSVYSVDLSRHLPLRSRLALRLPVAAARTQRRELRGRIPAGVRSWDDLAASAIPLATGFPLPSVSEAAALLYTGGTTGTPKAVCLTHENLRSNAEMSLAWASGTTSAGKETFYAVLPFFHAFGMSLSLLCAVGLAATQVVLPKFGADLVLAAWKRRPATFFPGVPVMFDRLVTRARATGANLSSCKIAVCGAAPNPLAVAQAWEEATGGTIIEGYGMTESSPIILGNPISPARRPGTLGVPYPSTQVRLVDPEDVEREVAPGEVGELLARGPQVFSGYWDNPEESAEVLLDGGWLRTGDLVRQEADGFYVIADRRKELIISGGFNIYPTEVEAAVRSMPQVEEVAVVGLPAEAGNESVVAAILPKEGQTVTLEQVREWAAKNLSNYALPRQIAILTEMPRSQIGKVLRRVVRDELLAAREAASGAATAAAVSIVEHFPGRGERRDGGQQEGSQDGKAGPHDSAASH$","AMP-dependent synthetase and ligase","Cytoplasm, Membrane","Acyl-CoA synthetases (AMP-forming)/AMP-acidligases II","acyl-CoA synthase ","AMP-dependent synthetase and ligase","","Smith D.J., Earl A.J., Turner G. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 1990. 9(9):2743-2750. PMID: 2118102Schroder J. Protein sequence homology between plant 4-coumarate:CoA ligase and firefly luciferase. Nucleic Acids Res. 1989. 17(1):460-460. PMID: 2911486Mallonee D.H., White W.B., Hylemon P.B. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 1990. 172(12):7011-7019. PMID: 2254270","","","

InterPro
IPR000873
Domain

AMP-dependent synthetase and ligase
PR00154	$\"[237-248]T$ $\"[249-257]T$	AMPBINDING
PF00501	$\"[74-518]T$	AMP-binding
PS00455	$\"[242-253]?$	AMP_BINDING

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[543-582]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:2.30.38.10	$\"[410-486]T$	no description
G3DSA:3.30.300.30	$\"[488-597]T$	no description
G3DSA:3.40.50.980	$\"[44-154]T$ $\"[235-410]T$	no description
PTHR11968	$\"[38-152]T$ $\"[182-593]T$	ATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF44	$\"[38-152]T$ $\"[182-593]T$	LONG-CHAIN-FATTY-ACID--COA LIGASE

","BeTs to 18 clades of COG0318COG name: Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases IIFunctional Class: I [Metabolism--Lipid metabolism] Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0318 is aomp-zy--drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 298-483 are 46% similar to a (LIGASE CORONAFACATE COMPONENT ACID SYNTHETASE CORONAFACIC) protein domain (PD091477) which is seen in Q87W76_PSESM.Residues 383-440 are 82% similar to a (LIGASE SYNTHETASE A ACETYL-COENZYME ACETYL-COA ENZYME LONG-CHAIN-FATTY-ACID--COA ACETATE--COA ACYL-COA FATTY-ACID-COA) protein domain (PD167005) which is seen in Q6NJL4_CORDI.Residues 385-474 are 52% similar to a (LIGASE ACYL-COA) protein domain (PDA0W9W0) which is seen in Q9AH08_RHOER.Residues 414-484 are 54% similar to a (LIGASE LONG-CHAIN-FATTY-ACID-COA) protein domain (PD923676) which is seen in Q7WNB5_BORBR.Residues 463-587 are 51% similar to a (LIGASE 4-COUMARATE:COA) protein domain (PD724490) which is seen in Q8GGM9_STRAZ.Residues 486-580 are 52% similar to a (LIGASE FATTY-ACID-COA SYNTHASE SYNTHETASE POSSIBLE FADD10 6.2.1.- LONG ACID-COA CHAIN) protein domain (PD874272) which is seen in Q50176_MYCLE.Residues 486-524 are 84% similar to a (LIGASE SYNTHETASE PHOSPHOPANTETHEINE PEPTIDE A ENZYME SYNTHASE ACETYL-COENZYME NON-RIBOSOMAL ACETYL-COA) protein domain (PD265446) which is seen in Q9Z442_PSEPU.","","-47% similar to PDB:1ULT Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.8E_33);-47% similar to PDB:1V25 Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.8E_33);-47% similar to PDB:1V26 Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.8E_33);-47% similar to PDB:2D1Q Crystal structure of the thermostable Japanese Firefly Luciferase complexed with MgATP (E_value = 1.3E_31);-47% similar to PDB:2D1R Crystal structure of the thermostable Japanese firefly Luciferase complexed with OXYLUCIFERIN and AMP (E_value = 1.3E_31);","Residues 74 to 518 (E_value = 9.5e-111) place ANA_1121 in the AMP-binding family which is described as AMP-binding enzyme.","","synthetases (AMP-forming)-AMP-acid ligases II (fadD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1122","1199240","1201024","1785","6.81","-1.49","64296","ATGACTGACAGCACGATCAACGCCGCCGCCTCACCACAGCAGGCCACCCAGGACCACCGCCACTACCTGCGCCCTCACTACCAGCCCGGCATCCCCGCGGCGATCGAGGTTCCCGACGCGCCGCTCAGCGAGCTGCTGGAGACGGCGGCGCGCTTCTACCCCGACCGGGTCGCCATCGACTTCCTGGGTGCGGCGATGACCTACCGCGAGCTGCTGGAGGCCTCGGAGCGGGCGGCGCAGGTGCTGCGGACCTCGGGGGTGCACAAGGGCGACCGGGTGGCCCTCATCATGCCGAACTGTCCGCAGCACGCCGTGGCCCTCTACGGGGCGCTGCGCATCGGCGCGGTCGTAGCCGAGCACAACCCGCTGGCGCCCGCCGAGGAGATCCGCTCCCAGCTGGACGCGCACGGAGCCCGCGTCGTCATCGTGTGGGAGAAGGGCGTCGGCCTCGTCACGGATCCAGGTCCGGCTTCACGCGCCGACGGCGATGCGCTCCAGGGACGCACGGTCTTCAGCGTGGACCTCTCAGCCGCAATGCCGGTGCGTCTGCGCGCCGCGCTGCGTCTTCCGGTGGAGCGGGCCCGCCGGCAGCGGGCCGCCTTCCGCGCCCGGAGCCTGCCTGCGGGGGTGCGCTCCTGGGACAAGGAGGTGGCCGGTGCTCACCGGATCCCCTCACGCTTCCCCTACCCGGCCGGCTCCGACATCGCGGTCCTGCTGCACACCGGTGGGACGACCGGCACGCCCAAGGCGGCGATGCTCACGCACACCAATCTGCGGGCCAACGCCAACCAGGCCATCGCCTGGGTGCCGATGCTGCATGAGGGCGGGGAGAACTTCCTGTGCCTGCTGCCCTTCTTCCACGCCTTCGGGCTGACCTTCAACCTCTTCTGCGCGGTGCAGAAGGCCGCCACCCAGGTGATGCTGCCCAAGTTCTCGGTGGATCAGGTGCTGACCGCGCACGAGCGGCGTCCCTTCACCTTCTTCGTCGGCGTGCCGGTCATGTTCGAGAGGATCCTCGACGGCGCCCAGAAGCGGGGCACGAACCTGGGCACCCTGCGCTACGGGGTGTGCGGGGCGGCCCCGATGCCGCCGGAGGTCGGGGCCCGGTGGGAGAAGGCGACCGGCGGCTTCTTCGTCGAGGGCTACGGCATGACTGAGACCAGCCCGATCGTCGCGGGCACGCCCATGGGACCCTCGCGCCGCATGGGTGCGCTGGGCCTGCCCTTCCCCTCCACGGATGTACGCGTCGTGGACCCCGAGGACCCGGACCCCGCTCGGGAGGTGCCCGACGGCGAGCCGGGCGAGCTGCTGGTGCGCGGCCCCCAGGTCTTCGCCGGCTACTGGGAGGACGAGGCGGCCACGCAGGCCGCGATCCTGCCGGGCGGTTGGCTGCGCACGGGCGACATCGTGCGCCGGGAGGACTCCTTCCTGTGGATGGCCGACCGCAAGCGCGAGCTGATCCTCACCGGCGGCTTCAACGTCTACCCCAGTCAGGTGGAGGCGGCGATCCGCTCCATGAAGGGCGTGGCCGACGTCGCGGTCGTGGGGCTTCCCGACGGTGCGATGGGCGAGCTCGTGTGCGCCGCTGTGGTCCTGGCCGAGGGGACCGAGCCGGGGTCGGTGACCCTGGAGGCGGTGCGGGAGCACGCCGAGCGGACGGTCCCGCGTTACGCGCTGCCGCACCGCCTGGAGGTCATTGAGGAGATGCCCCGCTCCCAGATCGGCAAGATCCTGCGTCGCGTCGTGCGCGAGCAGGTGCTCGCCAGAGCCGCGGAAGAGGACTGA","MTDSTINAAASPQQATQDHRHYLRPHYQPGIPAAIEVPDAPLSELLETAARFYPDRVAIDFLGAAMTYRELLEASERAAQVLRTSGVHKGDRVALIMPNCPQHAVALYGALRIGAVVAEHNPLAPAEEIRSQLDAHGARVVIVWEKGVGLVTDPGPASRADGDALQGRTVFSVDLSAAMPVRLRAALRLPVERARRQRAAFRARSLPAGVRSWDKEVAGAHRIPSRFPYPAGSDIAVLLHTGGTTGTPKAAMLTHTNLRANANQAIAWVPMLHEGGENFLCLLPFFHAFGLTFNLFCAVQKAATQVMLPKFSVDQVLTAHERRPFTFFVGVPVMFERILDGAQKRGTNLGTLRYGVCGAAPMPPEVGARWEKATGGFFVEGYGMTETSPIVAGTPMGPSRRMGALGLPFPSTDVRVVDPEDPDPAREVPDGEPGELLVRGPQVFAGYWEDEAATQAAILPGGWLRTGDIVRREDSFLWMADRKRELILTGGFNVYPSQVEAAIRSMKGVADVAVVGLPDGAMGELVCAAVVLAEGTEPGSVTLEAVREHAERTVPRYALPHRLEVIEEMPRSQIGKILRRVVREQVLARAAEED$","AMP-dependent synthetase and ligase","Cytoplasm, Membrane","Acyl-CoA synthetases (AMP-forming)/AMP-acidligases II","acyl-CoA synthase ","AMP-dependent synthetase and ligase","","Smith D.J., Earl A.J., Turner G. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 1990. 9(9):2743-2750. PMID: 2118102Schroder J. Protein sequence homology between plant 4-coumarate:CoA ligase and firefly luciferase. Nucleic Acids Res. 1989. 17(1):460-460. PMID: 2911486Mallonee D.H., White W.B., Hylemon P.B. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 1990. 172(12):7011-7019. PMID: 2254270","","","

InterPro
IPR000873
Domain

AMP-dependent synthetase and ligase
PR00154	$\"[233-244]T$ $\"[245-253]T$	AMPBINDING
PF00501	$\"[67-514]T$	AMP-binding
PS00455	$\"[238-249]?$	AMP_BINDING

noIPR
unintegrated

unintegrated
G3DSA:2.30.38.10	$\"[405-482]T$	no description
G3DSA:3.30.300.30	$\"[484-586]T$	no description
G3DSA:3.40.50.980	$\"[37-145]T$ $\"[232-405]T$	no description
PTHR11968	$\"[31-145]T$ $\"[178-594]T$	ATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF44	$\"[31-145]T$ $\"[178-594]T$	LONG-CHAIN-FATTY-ACID--COA LIGASE

","BeTs to 16 clades of COG0318COG name: Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases IIFunctional Class: I [Metabolism--Lipid metabolism] Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0318 is aomp-zy--drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 26-79 are 66% similar to a (LIGASE LONG-CHAIN-FATTY-ACID--COA LONG-CHAIN ACYL-COA SYNTHETASE LONG-CHAIN-FATTY-ACID-COA FATTY ACID METABOLISM MAGNESIUM) protein domain (PD428926) which is seen in Q72IN3_THET2.Residues 50-142 are 50% similar to a (LIGASE SYNTHETASE FATTY-ACID-COA SYNTHASE PEPTIDE 6.2.1.- LONG-CHAIN-FATTY-ACID--COA PROBABLE ACYL-COA FERULOYL-COA) protein domain (PD350381) which is seen in Q7U2E6_MYCBO.Residues 82-123 are 76% similar to a (LIGASE SYNTHETASE PHOSPHOPANTETHEINE PEPTIDE A ACYL-COA ENZYME SYNTHASE LONG-CHAIN-FATTY-ACID--COA NON-RIBOSOMAL) protein domain (PD000102) which is seen in Q8FSH2_COREF.Residues 267-374 are 46% similar to a (LIGASE LONG-CHAIN-FATTY-ACID--COA ACYL-COA SYNTHETASE LONG-CHAIN-FATTY-ACID-COA LONG-CHAIN MEMBRANE ACID METABOLISM FATTY) protein domain (PD374777) which is seen in Q6D4L8_BBBBB.Residues 306-474 are 44% similar to a (LIGASE CORONAFACATE COMPONENT ACID SYNTHETASE CORONAFACIC) protein domain (PD091477) which is seen in Q87W76_PSESM.Residues 379-412 are 76% similar to a (LIGASE SYNTHETASE A ACETYL-COENZYME ACETYL-COA ENZYME LONG-CHAIN-FATTY-ACID--COA ACETATE--COA ACYL-COA FATTY-ACID-COA) protein domain (PD167005) which is seen in Q8NTA7_CORGL.Residues 451-591 are 57% similar to a (LIGASE 4-COUMARATE:COA) protein domain (PD724490) which is seen in Q8GGM9_STRAZ.Residues 482-579 are 55% similar to a (LIGASE FATTY-ACID-COA SYNTHASE SYNTHETASE POSSIBLE FADD10 6.2.1.- LONG ACID-COA CHAIN) protein domain (PD874272) which is seen in Q50176_MYCLE.Residues 486-582 are 54% similar to a (LIGASE O-SUCCINYLBENZOIC ACYLTRANSFERASE ACID-COA ACID--COA SYNTHETASE TRANSFERASE ACYL-ACYL MENE PROBABLE) protein domain (PD918751) which is seen in Q8NT60_CORGL.","","-42% similar to PDB:1ULT Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.7E_33);-42% similar to PDB:1V25 Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.7E_33);-42% similar to PDB:1V26 Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.7E_33);-40% similar to PDB:1BA3 FIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORM (E_value = 5.5E_32);-40% similar to PDB:1LCI FIREFLY LUCIFERASE (E_value = 5.5E_32);","Residues 67 to 514 (E_value = 1.1e-109) place ANA_1122 in the AMP-binding family which is described as AMP-binding enzyme.","","synthetases (AMP-forming)-AMP-acid ligases II (fadD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1123","1202527","1202084","444","7.56","1.34","16678","ATGCGCATGTGGTCGCTGCACCCGCACCACCTGGACCGTGCGGGACTGGTGGCCTGCTGGCGCGAGTCACTCCTGGCCCAGGCGGTCCTGGCGGGGCGCACCCGCGGCTACCGCAACCACCCCCAGCTCGAACGCTTCCGCGCCTCCCCCGAACCGGTCACTCCGGCGGTGGCGGTGGGCGCCTACCTGTGGGGGCTGCGCGAGGAGGCCGTCCGGCGCGGCTACCGATTCGACGCCTCCCGCATCGACCTGCCTGAGGCGGAGTGCACCGGCGTCAGCCTGACGGTCACCGAGGGGCAGATGGACCTGGAGCGCAGGCATCTTGAGGCCAAGCTGGCTGGGCGCGCCCCCGAGCTTCTGCCCCTGCCCGAGCGGCTTGAGGCGCACCCGATCTTCCGGGTCGTCCCCGGCGACGTCGAGTCTTGGGAGAGAAGCCTTCTATGA","MRMWSLHPHHLDRAGLVACWRESLLAQAVLAGRTRGYRNHPQLERFRASPEPVTPAVAVGAYLWGLREEAVRRGYRFDASRIDLPEAECTGVSLTVTEGQMDLERRHLEAKLAGRAPELLPLPERLEAHPIFRVVPGDVESWERSLL$","Pyrimidine dimer DNA glycosylase","Cytoplasm","pyrimidine dimer DNA glycosylase","pyrimidine dimer DNA glycosylase","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-144 are 63% similar to a (PYRIMIDINE DNA GLYCOSYLASE DIMER) protein domain (PD092007) which is seen in P94957_MICLU.","","-47% similar to PDB:1ZAT Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution (E_value = );-47% similar to PDB:2HKL Crystal structure of Enterococcus faecium L,D-transpeptidase C442S mutant (E_value = );-63% similar to PDB:1AZS COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE (E_value = );-63% similar to PDB:1AZT GS-ALPHA COMPLEXED WITH GTP-GAMMA-S (E_value = );-63% similar to PDB:1CJK COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN (E_value = );","No significant hits to the Pfam 21.0 database.","","dimer DNA glycosylase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1124","1203446","1202550","897","5.49","-8.09","31202","ATGAGCGCAGCCCCCTCCCGCAGCTTCGGTTCCGTCGGCGTCGCCATGGTCACCCCCTTCACGCCCAGTGGGGAGGTCGACTTCGACGCCGCCCGAGCCCTGGCGGTCAGCCTGGTCGACGACGGCGCCGACCTGATCCTCCTGTCGGGCACCACCGGTGAGTCCCCGACCACCCACACTCCCGAGAAGCAGGAGCTGATCCGCCAGGTCAAGGACGCCCTGGGCGGGCGCGCGATGGTCATGGCCGGAGCCGGCTCCAACGACACCGCCCACGCGGTGCGCATCGGCGTGGCCTCCCAGGAGGCCGGCGCCGAGGGCCTGCTCATCAACGCCCCCTACTACAACCGCCCCAGCCAGGAGGGCGTCTACCGGCACATCAACGCCGTCGTGGAGGCCACCGACCTGCCTGTCATGGTCTACGACATCCCCGGACGCACCGGCGTGAAGATCACCGAGGAGACCCTGGCCCGCCTGGCCGAGAACCCCCGCGTCAAGGCCGTCAAGGACGCGACCGGGGACGTCGAGCAGGGCTTCCGCCGCATGGAGTCCACCGGCCTGGAGTACTACTCCGGCGACGACGGCCTCAACTTCGCCTGGCTCACCCACGGCGCTTCCGGCGTCATCTCCGTGGCCGCCCACGCCGACGCCCACTCCTGGCGCCAGATGATCGATGCCGTCGACGCCGGCGACCTGGCCAGCGCCCGTACCCTCGCCCGCAGCCTGCGCCCCCTGGTTCACGCCATCATGGGCGGTGGGCAGGGGGCCGTCATGGCCAAGGAGGCCCTGCACCTCCAGGGACGCTTGCCCAGCCCCGCTCTGCGCCTGCCCCTCGTGCGCGCCGAGGAGGCCGAGGTCGCCGCCCTGCGCGAGGTCCTGGCCACCTCCGGGCTGCTCTGA","MSAAPSRSFGSVGVAMVTPFTPSGEVDFDAARALAVSLVDDGADLILLSGTTGESPTTHTPEKQELIRQVKDALGGRAMVMAGAGSNDTAHAVRIGVASQEAGAEGLLINAPYYNRPSQEGVYRHINAVVEATDLPVMVYDIPGRTGVKITEETLARLAENPRVKAVKDATGDVEQGFRRMESTGLEYYSGDDGLNFAWLTHGASGVISVAAHADAHSWRQMIDAVDAGDLASARTLARSLRPLVHAIMGGGQGAVMAKEALHLQGRLPSPALRLPLVRAEEAEVAALREVLATSGLL$","Dihydrodipicolinate synthase","Cytoplasm","Dihydrodipicolinate synthase (DHDPS)","dihydrodipicolinate synthase ","dihydrodipicolinate synthase","","Mirwaldt C., Korndorfer I., Huber R. The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. J. Mol. Biol. 1995. 246(1):227-239. PMID: 7853400Murphy P.J., Trenz S.P., Grzemski W., De Bruijn F.J., Schell J. The Rhizobium meliloti rhizopine mos locus is a mosaic structure facilitating its symbiotic regulation. J. Bacteriol. 1993. 175(16):5193-5204. PMID: 8349559","","","

InterPro
IPR002220
Family

Dihydrodipicolinate synthetase
PD001859	$\"[2-74]T$	Q829R6_STRAW_Q829R6;
PR00146	$\"[42-63]T$ $\"[78-96]T$ $\"[110-126]T$ $\"[135-152]T$	DHPICSNTHASE
PIRSF001365	$\"[8-298]T$	Dihydrodipicolinate synthase
PTHR12128	$\"[1-293]T$	DIHYDRODIPICOLINATE SYNTHASE
PF00701	$\"[8-296]T$	DHDPS
PS00666	$\"[140-170]T$	DHDPS_2

InterPro
IPR005263
Family

Dihydrodipicolinate synthase subfamily
TIGR00674	$\"[11-295]T$	dapA: dihydrodipicolinate synthase

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[9-298]T$	no description

","BeTs to 22 clades of COG0329COG name: Dihydrodipicolinate synthase/N-acetylneuraminate lyaseFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0329 is aompkz-qv-rlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB002220 (Dihydrodipicolinate synthetase) with a combined E-value of 8.7e-47. IPB002220A 11-20 IPB002220B 34-84 IPB002220C 103-146 IPB002220D 190-216","Residues 2-74 are similar to a (LYASE DIHYDRODIPICOLINATE SYNTHASE BIOSYNTHESIS DHDPS LYSINE DIAMINOPIMELATE N-ACETYLNEURAMINATE ACID ALDOLASE) protein domain (PD001859) which is seen in Q829R6_STRAW.Residues 78-213 are 49% similar to a (SYNTHASE FAMILY DIHYDRODIPICOLINATE) protein domain (PDA04063) which is seen in Q6NFS2_CORDI.Residues 80-129 are 78% similar to a (DIHYDRODIPICOLINATE SYNTHASE BIOSYNTHESIS LYASE DHDPS DIAMINOPIMELATE LYSINE DEHYDRATASE PROBABLE CHLOROPLAST) protein domain (PD728475) which is seen in DAPA_BIFLO.Residues 80-276 are 43% similar to a (SYNTHASE DIHYDRODIPICOLINATE PLASMID BLL5331 BLL7953 RELATED SYNTHASE DIHYDRODIPICOLINE AGR_PAT_671P POSSIBLE) protein domain (PD485876) which is seen in Q7WEB4_BORBR.Residues 131-200 are similar to a (LYASE DIHYDRODIPICOLINATE SYNTHASE BIOSYNTHESIS DHDPS LYSINE DIAMINOPIMELATE ACID N-ACETYLNEURAMINATE DEHYDRATASE) protein domain (PD485872) which is seen in DAPA_COREF.Residues 220-276 are 70% similar to a (LYASE DIHYDRODIPICOLINATE SYNTHASE BIOSYNTHESIS DHDPS LYSINE DIAMINOPIMELATE N-ACETYLNEURAMINATE DEHYDRATASE PROBABLE) protein domain (PD213669) which is seen in DAPA_BIFLO.","","-64% similar to PDB:1XXX Crystal structure of Dihydrodipicolinate Synthase (DapA, Rv2753c) from Mycobacterium tuberculosis (E_value = 1.5E_63);-60% similar to PDB:1XKY Crystal Structure of Dihydrodipicolinate Synthase DapA-2 (BA3935) from Bacillus Anthracis at 1.94A Resolution. (E_value = 1.2E_49);-60% similar to PDB:1XL9 Crystal Structure of Dihydrodipicolinate Synthase DapA-2 (BA3935) from Bacillus Anthracis. (E_value = 1.2E_49);-59% similar to PDB:1O5K Crystal structure of Dihydrodipicolinate synthase (TM1521) from Thermotoga maritima at 1.80 A resolution (E_value = 1.5E_42);-58% similar to PDB:2EHH Crystal structure of dihydrodipicolinate synthase from aquifex aeolicus (E_value = 1.3E_38);","Residues 8 to 296 (E_value = 6.7e-76) place ANA_1124 in the DHDPS family which is described as Dihydrodipicolinate synthetase family.","","synthase (DHDPS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1125","1203525","1203653","129","9.98","3.37","4724","ATGTACTCAGAGAACAGGAAGGGCCGTCACTTAGGCTCGGTCCATGACCTCCTCGACCCCCTCGCCTGCATCGTCCTCATCGCCTTCATCGCCCTCCGGGAGCCGGGACGGCTCCGTCCTGGGCGCTGA","MYSENRKGRHLGSVHDLLDPLACIVLIAFIALREPGRLRPGR$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1126","1203679","1204335","657","5.61","-9.21","22037","ATGGGCGCGCGCACGCCGCATCACCACTCCCCCGGTGCTGACGACTGTGCGGAGCATGACCATGGCACCCCCCAGACACCGGGGGGCTTCGTGCGCCCAGCTGGTGCGGAGGACCTGACGGCGATCGGGCAGGTCCAGGCCGCCACCATGCTCGCCTCCCTTCAGGCCGGCCACACCGCCGAGCACGGTACGCCTCTGCCCCAGGGCGTGCGGGCGATGATCGCCGCCCCCGTCATCGCGGCAGGCTGGGAGGCAGCAGTGACTGAGCCGCCCTCGCCCGAGCACCACGTCCTAGTGGCCACCACCGCCCAAGCCGACGCTGCGAGCCGGACGGTGGTGGGCCTGCTGGGCCTGGCCCCCACCCAGTCCATGGACGCCGAGGGCCACGTCGACGAGGCCGGGGTGCAGGCCGTGGAGGTCACGGCTCTGGGTGTGGAACCCGCCAGTCAGCGCCGCGGGCACGGCTCCCGGCTCCTGGCGGCTGCCGTGGACCTGGCCCGTCAGGACGGGGCCAGGGCGCTCGTGGCCTGGGCGGTGCGCGGGGACGAGTCGGTCAGCCGGCTCCTGAGCTCGGTCGGCATGGCACCCACCGGCGCCCACCGGGTGCTCGGTGTCGGTGAGGGCATCACTGAGGACTGCTGGGCGGCCTCGCTGTAG","MGARTPHHHSPGADDCAEHDHGTPQTPGGFVRPAGAEDLTAIGQVQAATMLASLQAGHTAEHGTPLPQGVRAMIAAPVIAAGWEAAVTEPPSPEHHVLVATTAQADAASRTVVGLLGLAPTQSMDAEGHVDEAGVQAVEVTALGVEPASQRRGHGSRLLAAAVDLARQDGARALVAWAVRGDESVSRLLSSVGMAPTGAHRVLGVGEGITEDCWAASL$","GCN5-related N-acetyltransferase","Cytoplasm","flagellar hook length determination proteinhomolog","hypothetical protein","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[104-195]T$	Acetyltransf_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[30-218]T$	no description

","BeTs to 6 clades of COG0454COG name: Histone acetyltransferase HPA2 and related acetyltransferasesFunctional Class: K [Information storage and processing--Transcription] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0454 is aompkzyqvdrlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 104 to 195 (E_value = 1.4e-06) place ANA_1126 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","hook length determination protein homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1127","1205122","1204370","753","4.87","-14.12","25653","ATGACGATTCGCGTAGCTGTTGTGGGCGCCGCCGGGCGCATGGGATCGACCGTCTGCCAGGCGGTCCAGGACGCCGAGGGCCTTGAGCTCGTGGCCCGCCTGGACGTGGGGGACACCCTCGACGCCGAGCACCTGGCGGGCGCCGACGTCGCCGTCGACTTCACTGTCCCCAGCGTCACCGAGGCCAATGTCCACGCCCTGCTCGACGCCGGAGTGGACGTCGTCGTGGGCACCACCGGCTGGACCGAGGAGTCCTACGGGCGCGTCCGTGAGCACCTGGCCCAGCCCGAGGCCGTCGGCCGCAGCGTCCTCATCGCCCCGAACTTCGCCCTGTCCGCCGTGCTGGCCATGAGCTTCGCAGCGAAGGCCGCCCCCTACTTTGAGTCCGCCGAGGTCATCGAGCTCCACCACCCGAACAAGGTCGACGCGCCCTCGGGCACCGCGGTCGCCACCGCCCAGGGCATCGCCGCAGCCCGTGCCGAGGCGGGCCTGGGCGCCATGCCGGACGCCACCCAGGCCGACCCCGACGGTGCTCGCGGGGCGGTGGTCGACGGCGTCCACGTCCACGCCGTGCGCCTGCGGGGGCTGACCGCCCACGAGGAGGTCGTGCTCGGCAACCCCGGCGAGCAGCTGACCATCCGCACCGACTCCTTCGACCGGGCCTCCTTCATGCCCGGCGTGGTCCTCGCCGTGCGGCAGGTCTCCAGCCGCCCCGGCCTGACCATCGGCCTGGACGCCCTGCTCGACCTTTAA","MTIRVAVVGAAGRMGSTVCQAVQDAEGLELVARLDVGDTLDAEHLAGADVAVDFTVPSVTEANVHALLDAGVDVVVGTTGWTEESYGRVREHLAQPEAVGRSVLIAPNFALSAVLAMSFAAKAAPYFESAEVIELHHPNKVDAPSGTAVATAQGIAAARAEAGLGAMPDATQADPDGARGAVVDGVHVHAVRLRGLTAHEEVVLGNPGEQLTIRTDSFDRASFMPGVVLAVRQVSSRPGLTIGLDALLDL$","Dihydrodipicolinate reductase","Cytoplasm","dihydrodipicolinate reductase","dihydrodipicolinate reductase ","Dihydrodipicolinate reductase","","","","","

InterPro
IPR000846
Family

Dihydrodipicolinate reductase
PD004105	$\"[3-250]T$	Q6A7P7_PROAC_Q6A7P7;
PF01113	$\"[3-109]T$	DapB_N
PF05173	$\"[112-249]T$	DapB_C
PS01298	$\"[131-148]T$	DAPB

InterPro
IPR011770
Family

Dihydrodipicolinate reductase, bacterial and plant
PIRSF000161	$\"[3-250]T$	Dihydrodipicolinate reductase
TIGR00036	$\"[2-250]T$	dapB: dihydrodipicolinate reductase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[3-142]T$	no description
PTHR20836	$\"[2-250]T$	DIHYDRODIPICOLINATE REDUCTASE

","BeTs to 18 clades of COG0289COG name: Dihydrodipicolinate reductaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0289 is a-m----qv-rlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB000846 (Dihydrodipicolinate reductase) with a combined E-value of 3.3e-70. IPB000846A 3-30 IPB000846B 49-81 IPB000846C 101-127 IPB000846D 129-149 IPB000846E 186-228","Residues 3-250 are 72% similar to a (BIOSYNTHESIS DIHYDRODIPICOLINATE REDUCTASE OXIDOREDUCTASE DIAMINOPIMELATE DHPR LYSINE NADP REDUCTASE-LIKE DAPB) protein domain (PD004105) which is seen in Q6A7P7_PROAC.Residues 193-248 are 67% similar to a (BIOSYNTHESIS OXIDOREDUCTASE DIAMINOPIMELATE DHPR LYSINE REDUCTASE DIHYDRODIPICOLINATE NADP) protein domain (PD717260) which is seen in DAPB_STRMU.","","-55% similar to PDB:1C3V DIHYDRODIPICOLINATE REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND PDC (E_value = 2.5E_45);-55% similar to PDB:1P9L Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC (E_value = 2.5E_45);-55% similar to PDB:1YL5 Crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (RV2773C) (crystal form A) (E_value = 3.2E_45);-55% similar to PDB:1YL6 crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) (crystal form B) (E_value = 3.2E_45);-55% similar to PDB:1YL7 the crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) in complex with NADH (crystal form C) (E_value = 3.2E_45);","Residues 3 to 109 (E_value = 3.5e-34) place ANA_1127 in the DapB_N family which is described as Dihydrodipicolinate reductase, N-terminus.Residues 3 to 32 (E_value = 0.00027) place ANA_1127 in the GFO_IDH_MocA family which is described as Oxidoreductase family, NAD-binding Rossmann fold.Residues 112 to 249 (E_value = 3.6e-52) place ANA_1127 in the DapB_C family which is described as Dihydrodipicolinate reductase, C-terminus.","","reductase (dapB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1128","1205289","1206224","936","7.68","1.42","33410","ATGATGGATGCTGAAGGCACTCCCACATCTTCAGAAAGGGAACCGCTCGTGACTACAACTGCGGAGCAAGCACCGGCCGACGCGCCCCAGGCATTCTCCAAGGCGCCCGGTACCAGGGTCGCCCTCGTCACCGGCGCCTCCTCCGGCATCGGCGAGGACACCGCCCACAAGCTCCGGGCACTGGGCTACATCGTCTACGGCGCAGCCCGTCGTACCGACCGTCTCCAGGCCCTGACCGCCGACGGCATCCGCCCGCTGGCCATGGACGTCACCGACGACGCCTCCATGAGCTCCGGCGTCAACCGCATCCTGGAGGAGACCGGACGCATCGACGTCCTGGTCAACAACGCCGGCTACGGCTCCTACGGTGCCATCGAGGACGTCCCGATCAACGAGGCCCGCCGCCAGTTCGAGGTCAACGTCTTCGGTCTGGCGCGCCTGACCCAGCTCATCACCCCGCACATGCGAACCCGGGGCTCGGGCACCGTCATCAACATCTCCTCCATCGGCGGGAGGCTGACCACACCACTGGGCGGCTGGTACCACGCCACCAAGTACGCCGTCGAGGCCCTGAGCGACGCGCTACGCATCGAACTGTCTCCTTTCGGGATCGACGTCGTCGTGGTCGAGCCCGGCGGCATCCGCACCGAATGGGCATCGATCGCCGCCGACCACCTGGAGGCAACGGCCGAGGGCAGTGCCTACGCCGACCAGATCCGAGACGTGGCCGGAGCCATGCGCAGCGAGTCAAACCGACGGCACTACTCCCCGCCGGAGGTCATCGCCCGTACCGTCGGCAAAATCGTCACCGCCCGTCACCCCCGGACCCGCTACGCCGTGGGCTTCATGGCCAAGCCGCTCATTGCCGCACGCCGATTCCTGCCCGACCGCGCCTTCGATCAGCTCATCAGTGCCGCCTTCGGCTTCCGGCGCTGA","MMDAEGTPTSSEREPLVTTTAEQAPADAPQAFSKAPGTRVALVTGASSGIGEDTAHKLRALGYIVYGAARRTDRLQALTADGIRPLAMDVTDDASMSSGVNRILEETGRIDVLVNNAGYGSYGAIEDVPINEARRQFEVNVFGLARLTQLITPHMRTRGSGTVINISSIGGRLTTPLGGWYHATKYAVEALSDALRIELSPFGIDVVVVEPGGIRTEWASIAADHLEATAEGSAYADQIRDVAGAMRSESNRRHYSPPEVIARTVGKIVTARHPRTRYAVGFMAKPLIAARRFLPDRAFDQLISAAFGFRR$","Short-chain dehydrogenase/oxidoreductase","Cytoplasm","short-chain dehydrogenase/oxidoreductase","short chain dehydrogenase","short-chain dehydrogenase/reductase SDR","","Jornvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 1995. 34(18):6003-6013. PMID: 7742302Villarroya A., Juan E., Egestad B., Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 1989. 180(1):191-197. PMID: 2707261Persson B., Krook M., Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 1991. 200(2):537-543. PMID: 1889416Neidle E., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 1992. 204(1):113-120. PMID: 1740120Benyajati C., Place A.R., Powers D.A., Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 1981. 78(5):2717-2721. PMID: 6789320","","","

InterPro
IPR002198
Family

Short-chain dehydrogenase/reductase SDR
PR00080	$\"[108-119]T$ $\"[161-169]T$ $\"[181-200]T$	SDRFAMILY
PTHR19410	$\"[39-219]T$ $\"[236-288]T$	SHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106	$\"[39-200]T$	adh_short

InterPro
IPR002347
Family

Glucose/ribitol dehydrogenase
PR00081	$\"[40-57]T$ $\"[108-119]T$ $\"[155-171]T$ $\"[181-200]T$ $\"[202-219]T$	GDHRDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[38-291]T$	no description
PTHR19410:SF46	$\"[39-219]T$ $\"[236-288]T$	SHORT-CHAIN DEHYDROGENASE-RELATED

","BeTs to 16 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 4","***** IPB002347 (Glucose/ribitol dehydrogenase family signature) with a combined E-value of 1.9e-32. IPB002347A 40-57 IPB002347B 108-119 IPB002347C 155-171 IPB002347D 181-200 IPB002347E 202-219***** IPB002198 (Short-chain dehydrogenase/reductase SDR) with a combined E-value of 6.5e-21. IPB002198A 110-119 IPB002198B 161-209***** IPB003560 (2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature) with a combined E-value of 6.8e-14. IPB003560A 45-62 IPB003560B 111-128 IPB003560C 131-151 IPB003560D 196-219","Residues 37-122 are 56% similar to a (OXIDOREDUCTASE) protein domain (PD738693) which is seen in Q8G6F2_BIFLO.Residues 42-206 are 50% similar to a (EG:BACR37P7.9 RE15974P GH26015P CG8888-PA CG13377-PA) protein domain (PD312894) which is seen in Q9V653_DROME.Residues 88-143 are 68% similar to a (OXIDOREDUCTASE DEHYDROGENASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE REDUCTASE FAMILY SHORT CHAIN PROBABLE OXIDOREDUCTASE) protein domain (PD126102) which is seen in Q6LND6_PHOPR.Residues 108-140 are 96% similar to a (OXIDOREDUCTASE REDUCTASE DEHYDROGENASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY CHAIN SHORT PROBABLE OXIDOREDUCTASE) protein domain (PD072978) which is seen in Q9CG02_LACLA.Residues 147-201 are similar to a (OXIDOREDUCTASE DEHYDROGENASE REDUCTASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY CHAIN SHORT PROBABLE OXIDOREDUCTASE) protein domain (PD003795) which is seen in Q8NRL2_CORGL.Residues 202-306 are 62% similar to a (OXIDOREDUCTASE DEHYDROGENASE/OXIDOREDUCTASE SHORT-CHAIN) protein domain (PDA0T2X8) which is seen in Q88ZF7_LACPL.Residues 203-300 are similar to a (OXIDOREDUCTASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE OXIDOREDUCTASE FAMILY DEHYDROGENASE PROBABLE 1.-.-.- CHAIN SHORT) protein domain (PD862983) which is seen in Q8NRL2_CORGL.","","-54% similar to PDB:2JAH BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE CLAVULANIC ACID DEHYDEOGENASE (CAD) FROM STREPTOMYCES CLAVULIGERUS (E_value = 1.1E_32);-54% similar to PDB:2JAP CLAVULANIC ACID DEHYDROGENASE: STRUCTURAL AND BIOCHEMICAL ANALYSIS OF THE FINAL STEP IN THE BIOSYNTHESIS OF THE BETA-LACTAMASE INHIBITOR CLAVULANIC ACID (E_value = 1.1E_32);-51% similar to PDB:1IOL ESTROGENIC 17-BETA HYDROXYSTEROID DEHYDROGENASE COMPLEXED 17-BETA-ESTRADIOL (E_value = 4.7E_23);-51% similar to PDB:1A27 HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 C-TERMINAL DELETION MUTANT COMPLEXED WITH ESTRADIOL AND NADP+ (E_value = 1.0E_22);-51% similar to PDB:1BHS HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE (E_value = 1.0E_22);","Residues 39 to 200 (E_value = 1.9e-19) place ANA_1128 in the adh_short family which is described as short chain dehydrogenase.","","dehydrogenase-oxidoreductase (SDR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1129","1207884","1206478","1407","4.89","-25.67","50213","ATGTGCGCCGGCTCAGCCCGGCAGGCGGCCTCTCAGTCCTCCTCGACCCCCGCGACCGGGGAGTCCTCGAGCCCGACCGACTACGCCGAGGTGGATCTCGGCCGTGGGCGGCCCGGCCGCGACGGCACCGAGCTGACCCTGCACGACGACGGGGCACTCACCCGCCGCTCCGTCCTGCCCGGTGGGGTTCGCGTCATCACCGAGTCCGTGCCGGGGCTGCGCTCGGCCTCGATCGGCATGTGGTTCGGTGTCGGCAGCCGTGACGAGGTGCCCGGCCAGGAGGGCTCCACCCACTTCCTGGAGCACCTGCTGTTCAAGGGCACCGCCACGCGGGATGCCCACGAGATCGCCGAGGCCTTCGACATGATCGGCGGGGAGTCCAACGCCGCCACCTCCAAGGAGCACACCTCCTACTACGCCCGTGTGCTCGCCCCTGACGGTATGCAGGCCCTTGATGTGCTCGCCGACATGGTGACCTCCTCCCTCCTGGAGCCGGCCGACGTCGAGACCGAGCGCGGCGTCATCGTCTCCGAGCTCGCCGACGCTGCCGACGACCCGGCCGACGTCGCCCAGGAGGCCTTCGCCCGCGCCGCCTTCGGTGAGGACACACCGCTGGGCCGCCCCATTGGCGGTACTAACGAGACCGTCACTGCGGTTCCGCGCGACGCCGTGTGGGAGCACTACAAGCGCACCTACGCTTCCGACACCCTCGTGGTGGCCGCTGCCGGCGCCGTCGACCATGACGAGGTCTGCGAGCGGGTCCTGGCCGACCTGGCCGCGGCCGGCTGGGACGCCTCACCCGACGCCGTCCCGCGCGAGCGCCGCTTCGAGGTCGAGTCCTTCGCGCCCCTGGATGTCCACGACATCACTGTCCCGCGCGAGAGTGAGCAGAGCCACCTGTACCTGACGTGCCAGGGCATCGCCGTACGCGATGAGCGGCGCTGGGCCATGAGCGTGCTCACCACCATCCTGGGCGGGGGCATGTCCTCGCGCCTGTTCCAGGAGGTGCGTGAGAAGCGGGGCCTGGCCTACACCACCTACGCCTTCGACACCTCCTACGCCGGTGCCGGAGCCTTCGGGCTCTACGCGGGCTGCGCCCCCAGCGACGTCGACGAGGTGTGCGCCGTCATGATCGGTGAGTTCGAGAAGCTCGCCGAGCACGGCGTCACTGAGCGGGAGATGATGCGCGCCCGCGGCCAGCTGCGCGGGGCCATGGTGCTGGGCGGAGAGGACTCCCTGGCGCGTATGGGGCGCCTGGGGCGGGCCGAGGTCGTCACCGGGCGCCTGCGCTCTATGGAGGACAACCTGCGCCGCCTGGAGGCCGTCACCCCCGAGGAGGTGCGGGAGATGGCCGCCTGGCTGGTGGAGCAGAAGCGCGCCCGCATCCTCGTGGGACCGGTTGGCTGA","MCAGSARQAASQSSSTPATGESSSPTDYAEVDLGRGRPGRDGTELTLHDDGALTRRSVLPGGVRVITESVPGLRSASIGMWFGVGSRDEVPGQEGSTHFLEHLLFKGTATRDAHEIAEAFDMIGGESNAATSKEHTSYYARVLAPDGMQALDVLADMVTSSLLEPADVETERGVIVSELADAADDPADVAQEAFARAAFGEDTPLGRPIGGTNETVTAVPRDAVWEHYKRTYASDTLVVAAAGAVDHDEVCERVLADLAAAGWDASPDAVPRERRFEVESFAPLDVHDITVPRESEQSHLYLTCQGIAVRDERRWAMSVLTTILGGGMSSRLFQEVREKRGLAYTTYAFDTSYAGAGAFGLYAGCAPSDVDEVCAVMIGEFEKLAEHGVTEREMMRARGQLRGAMVLGGEDSLARMGRLGRAEVVTGRLRSMEDNLRRLEAVTPEEVREMAAWLVEQKRARILVGPVG$","Peptidase, M16 family","Cytoplasm, Extracellular","peptidase, M16 family","peptidase M16 domain protein","peptidase M16 domain protein","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Rawlings N.D., Barrett A.J. Homologues of insulinase, a new superfamily of metalloendopeptidases. Biochem. J. 1991. 275:389-391. PMID: 2025223Braun H.P., Schmitz U.K. Are the 'core' proteins of the mitochondrial bc1 complex evolutionary relics of a processing protease?. Trends Biochem. Sci. 1995. 20(5):171-175. PMID: 7610476Fujita A., Oka C., Arikawa Y., Katagai T., Tonouchi A., Kuhara S., Misumi Y. A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Nature 1994. 372(6506):567-570. PMID: 7990931Becker A.B., Roth R.A. An unusual active site identified in a family of zinc metalloendopeptidases. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(9):3835-3839. PMID: 1570301Becker A.B., Roth R.A. Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria. Meth. Enzymol. 1995. 248:693-703. PMID: 7674956","","","

InterPro
IPR001431
Binding_site

Peptidase M16, zinc-binding site
PS00143	$\"[85-108]T$	INSULINASE

InterPro
IPR007863
Domain

Peptidase M16, C-terminal
PF05193	$\"[218-401]T$	Peptidase_M16_C

InterPro
IPR011765
Domain

Peptidase M16, N-terminal
PF00675	$\"[64-213]T$	Peptidase_M16

noIPR
unintegrated

unintegrated
G3DSA:3.30.830.10	$\"[54-254]T$ $\"[287-467]T$	no description
PTHR11851	$\"[80-467]T$	METALLOPROTEASE

","BeTs to 16 clades of COG0612COG name: Predicted Zn-dependent peptidasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0612 is -----zyqvdrlbcefghs-ujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB001431 (Insulinase-like peptidase, family M16) with a combined E-value of 3.4e-06. IPB001431B 95-108","Residues 80-154 are similar to a (PROTEASE ZINC METALLOPROTEASE HYDROLASE MITOCHONDRIAL PROCESSING PEPTIDASE FAMILY PRECURSOR INSULINASE) protein domain (PD000718) which is seen in YMXG_BACSU.Residues 156-260 are 64% similar to a (PROTEASE ZINC HYDROLASE METALLOPROTEASE PROCESSING PEPTIDASE MITOCHONDRIAL FAMILY PRECURSOR PEPTIDASE) protein domain (PD375420) which is seen in Q6ADY8_BBBBB.Residues 261-327 are 58% similar to a (PROTEASE ZINC) protein domain (PDA0V5Z7) which is seen in Q6ADY8_BBBBB.Residues 328-467 are similar to a (PROTEASE ZINC PROCESSING MITOCHONDRIAL PEPTIDASE HYDROLASE FAMILY METALLOPROTEASE M16 PRECURSOR) protein domain (PD001445) which is seen in Q82K81_STRAW.","","-47% similar to PDB:1HR6 YEAST MITOCHONDRIAL PROCESSING PEPTIDASE (E_value = 1.3E_38);-47% similar to PDB:1HR7 YEAST MITOCHONDRIAL PROCESSING PEPTIDASE BETA-E73Q MUTANT (E_value = 3.0E_38);-47% similar to PDB:1HR8 YEAST MITOCHONDRIAL PROCESSING PEPTIDASE BETA-E73Q MUTANT COMPLEXED WITH CYTOCHROME C OXIDASE IV SIGNAL PEPTIDE (E_value = 3.0E_38);-47% similar to PDB:1HR9 YEAST MITOCHONDRIAL PROCESSING PEPTIDASE BETA-E73Q MUTANT COMPLEXED WITH MALATE DEHYDROGENASE SIGNAL PEPTIDE (E_value = 3.0E_38);-45% similar to PDB:1BCC CYTOCHROME BC1 COMPLEX FROM CHICKEN (E_value = 6.4E_33);","Residues 64 to 213 (E_value = 8.9e-43) place ANA_1129 in the Peptidase_M16 family which is described as Insulinase (Peptidase family M16).Residues 218 to 401 (E_value = 6.9e-42) place ANA_1129 in the Peptidase_M16_C family which is described as Peptidase M16 inactive domain.","","M16 family (U33883)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1130","1210735","1208069","2667","5.80","-15.67","95599","GTGGCATCCGGTGGCGCTGATCGGCATCATGTGGCCGCGCACGATAGAATCTGCGCGGCTGTGCCCTCGTGTACTCGCCGGCTCATTGATGCTCTCCCAGCGTGCGAGCCGGCCAGGAGTACGGAGGAGTCGCAGTCCGCCCCCGGGAAGAGACCCGGGGAGCGGCCGGCCCCGTCGGTTTTCGGTGGTGGCCTCCGGAACCGCGCTCGCGCCGTCGGATCAAAAAGATCCGCGTATGGCAGCACTCGGCTCCGTGGGCCTCGATCGAAGGCCACGGACCCGGCACGACGATCGCGAGAAAGAGACTTCATGTTCATTGACGACCCCGAGGTCACCGCCGCCGAGGCAGTGATCGACAACGGCTCCTTCGGCAAGCGCGTGGTGCGCTTCGAGACGGGCCGCCTGGCCAAGCAGGCCGCTGGAAGCGCCATGGCCTACCTCGACGGTGAGACCGCCGTCCTGTCCGCCACCACCGTGGGCAAGCACCCCAAGGACCAGTTCGACTTCTTCCCCCTGACCGTGGACGTCGAGGAGCGCCAGTACGCCGCCGGCCGCATCCCCGGCTCCTTCTTCCGCCGCGAGGGCCGCGCCGGAACCGCCGCCATCCTGGCCTGCCGCCTCATCGACCGTCCGCTGCGCCCCTCCTTCGTCAAGGGCCTGCGCAACGAGGTCCAGGTCGTTGAGACCGTCCTGGCCATCCACCCCGACGACGACTACGACGTCCTGGCCATCAACGCCGCCTCGATGTCCACCCAGATCGCCGGCCTGCCCTTCTCCGGGCCCGTGGCCGGTACCCGCCTGGCTCTCATCGACGGGCACTGGGTGGCCTTCCCCCGCTACTCCGAGCAGCAGCGCGCCACCTTCCAGATGGTGGTGGCCGGCCGCGTCCTGGAGTCCGGCGACGTCGCCATCATGATGGTCGAGGCCGGCGCCACCGAGCACGCCTGGGAGCTCATCAACGCCGGGGCCGTCGCCCCCACCGAGGCCGTCGTCGCCGAGGGCCTGGAGGCCGCCAAGCCCCACATCAAGGCCCTGTGCGAGGCCCAGCTCGAGGTCGCCCAGCACGCCTCGAAGCCCACCGCCGAGTTCCCCCTCTACCTGGACTACTCCGACGAGCAGTACGACGCCGTGGAGAAGGCCGCCGAGGCCCACGGCCTGGCCGCCGCCATCGCCACCGAGGGCAAGCAGGCCCGCGACCTGGCCACCGACGCCGTGCGTGACGAGGTCCTGGCCGAGCTCGCCGAGTCCTTCCCCACCGAGGAGGACACCAAGGCCCTCAAGGCGGCCTTCCGCTCCGTGACCAAGAAGATCGTGCGCCACCGCACCCTCACCGAGGGCGTGCGCATGGACGGGCGCGGCCTGAAGGACATCCGCACCCTGGCCGCCGAGGTCGAGGTCCTGCCCCGCGTGCACGGCTCGGCCATCTTCGAGCGCGGCGAGACCCAGATCCTGGGCGTGACCACCCTCAACATGCTGCGCATGGAGCAGCAGGTGGACGACCTCTCCCCGGTCACCCACAAGCGCTACATGCACAACTACAACTTCCCGCCCTTCTCCACCGGTGAGACCGGCCGCGTGGGCGCCCCCAAGCGCCGCGAGATCGGCCACGGCAACCTGGCCGAGCGGGCCCTTGTGCCCGTCCTGCCCACCCGCGAGGACTTCCCCTACGCGATCCGCCAGGTCTCCGAGGCCCTGGGCTCCAACGGCTCGACCTCCATGGGCTCGGTGTGCGCCTCCACCCTGTCCCTGCTCAACGCCGGTGTGCCGCTGCGCGCGCCCGTGGCCGGTATCGCCATGGGCCTCATGCACGAGGTCATCGACGGCGAGACCAAGTGGGCCACCCTCACCGACATCCTCGGCTCCGAGGACGCCTTCGGGGACATGGACTTCAAGGTCGCCGGAACCCGTGACTTCATTACGGCCCTCCAGCTGGACACCAAGCTCGACGGCCTGCCCTCCGAGGTGCTGGCCGGCGCGCTCGGCCAGGCCCGTGACGCCCGCCTGTTCATCCTCGACGTCCTGGCCCAGGCCATCGACGCCCCCGACGAGATGGCCCCCACGGCCCCGCGTGTCCTGGCCGTGCGCATCCCGGTGGACAAGATCGGTGAGGTCATCGGCCCCAAGGGCAAGATGATTAACCAGATCCAGGAGGACACCGGCGCGGACCTGACGGTCGAGGACGACGGCACCGTCTACATCGGCGCCTCCGACGGCCCCTCGGCCGAGGCGGCCCGCGACGCCGTCAACGCCATCGCCAACCCGCAGATGCCCGAGATCGGTGAGCGCTTCGTGGGCACCGTGGTCAAGACCACGACCTTCGGCGCCTTCGTCTCGCTGACCCCCGGCAAGGATGGCCTGCTCCACATCTCCCAGATCCGCCGGCTCGTCGGCGGCAAGCGCGTGGAGAACGTCGAGGACGTCCTCAACGTCGGTGACAAGGTCCAGGTCGAGCTGGCCGAGATCGACCAGCGCGGCAAGCTGAGCCTGCACGCGGTCCTCACCGACGAGCAGCTCGCTGCCGAGGCCGAGGGCGAGGCCTCCCGTAAGGCCTCCCGTGAGGGCGGCTCGCGCCGCGAGGCCAAGGACGAGGACGGCGAGCAGCCGCGCCGCGAGCGTCGTCCGCGCCGTCGCCGCATGCGCAGCGCCGAGTCCTCCGAGGAGGAGTGA","VASGGADRHHVAAHDRICAAVPSCTRRLIDALPACEPARSTEESQSAPGKRPGERPAPSVFGGGLRNRARAVGSKRSAYGSTRLRGPRSKATDPARRSRERDFMFIDDPEVTAAEAVIDNGSFGKRVVRFETGRLAKQAAGSAMAYLDGETAVLSATTVGKHPKDQFDFFPLTVDVEERQYAAGRIPGSFFRREGRAGTAAILACRLIDRPLRPSFVKGLRNEVQVVETVLAIHPDDDYDVLAINAASMSTQIAGLPFSGPVAGTRLALIDGHWVAFPRYSEQQRATFQMVVAGRVLESGDVAIMMVEAGATEHAWELINAGAVAPTEAVVAEGLEAAKPHIKALCEAQLEVAQHASKPTAEFPLYLDYSDEQYDAVEKAAEAHGLAAAIATEGKQARDLATDAVRDEVLAELAESFPTEEDTKALKAAFRSVTKKIVRHRTLTEGVRMDGRGLKDIRTLAAEVEVLPRVHGSAIFERGETQILGVTTLNMLRMEQQVDDLSPVTHKRYMHNYNFPPFSTGETGRVGAPKRREIGHGNLAERALVPVLPTREDFPYAIRQVSEALGSNGSTSMGSVCASTLSLLNAGVPLRAPVAGIAMGLMHEVIDGETKWATLTDILGSEDAFGDMDFKVAGTRDFITALQLDTKLDGLPSEVLAGALGQARDARLFILDVLAQAIDAPDEMAPTAPRVLAVRIPVDKIGEVIGPKGKMINQIQEDTGADLTVEDDGTVYIGASDGPSAEAARDAVNAIANPQMPEIGERFVGTVVKTTTFGAFVSLTPGKDGLLHISQIRRLVGGKRVENVEDVLNVGDKVQVELAEIDQRGKLSLHAVLTDEQLAAEAEGEASRKASREGGSRREAKDEDGEQPRRERRPRRRRMRSAESSEEE$","Polyribonucleotide nucleotidyltransferase","Cytoplasm","polyribonucleotide nucleotidyltransferase alphachain [similarity]","polyribonucleotide nucleotidyltransferase ","Polyribonucleotide nucleotidyltransferase","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Bycroft M., Hubbard T.J., Proctor M., Freund S.M., Murzin A.G. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 1997. 88(2):235-242. PMID: 9008164","","","

InterPro
IPR001247
Domain

Exoribonuclease
PF01138	$\"[124-257]T$ $\"[456-589]T$	RNase_PH
PF03725	$\"[260-325]T$ $\"[592-666]T$	RNase_PH_C
PF03726	$\"[374-453]T$	PNPase

InterPro
IPR003029
Domain

RNA binding S1
PF00575	$\"[756-830]T$	S1
SM00316	$\"[758-832]T$	S1
PS50126	$\"[760-832]T$	S1

InterPro
IPR004087
Domain

KH
SM00322	$\"[688-752]T$	KH

InterPro
IPR004088
Domain

KH, type 1
PF00013	$\"[691-748]T$	KH_1
PS50084	$\"[689-748]T$	KH_TYPE_1

InterPro
IPR012162
Family

Polyribonucleotide nucleotidyltransferase
PTHR11252	$\"[258-888]T$	POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[757-830]T$	no description

InterPro
IPR014069
Family

guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase
TIGR02696	$\"[110-831]T$	pppGpp_PNP: guanosine pentaphosphate synthe

noIPR
unintegrated

unintegrated
G3DSA:1.10.10.400	$\"[368-452]T$	no description
G3DSA:3.30.1370.10	$\"[688-729]T$	no description

","BeTs to 17 clades of COG1185COG name: Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1185 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000110 (Ribosomal protein S1 signature) with a combined E-value of 8.9e-07. IPB000110H 773-792","Residues 456-589 are similar to a (NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE POLYNUCLEOTIDE PHOSPHORYLASE PNPASE RNA-BINDING GUANOSINE PENTAPHOSPHATE ALPHA) protein domain (PD333034) which is seen in Q53597_STRAT.Residues 124-466 are 46% similar to a (BE0003N10.1) protein domain (PD520107) which is seen in Q965N3_CAEEL.Residues 138-257 are 53% similar to a (NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE) protein domain (PDA189P5) which is seen in Q7VIL0_HELHP.Residues 598-685 are 82% similar to a (NUCLEOTIDYLTRANSFERASE POLYRIBONUCLEOTIDE TRANSFERASE POLYNUCLEOTIDE PHOSPHORYLASE GUANOSINE PENTAPHOSPHATE PNPASE SYNTHETASE RNA-BINDING) protein domain (PD002075) which is seen in Q8G447_BIFLO.Residues 394-454 are 70% similar to a (NUCLEOTIDYLTRANSFERASE GUANOSINE PENTAPHOSPHATE POLYRIBONUCLEOTIDE TRANSFERASE SYNTHETASE SYNTHETASE/POLYRIBONUCLEOTIDE 2.7.6.- PHOSPHORYLASE BIFUNCTIONAL) protein domain (PD513385) which is seen in Q73VX0_MYCPA.Residues 456-589 are similar to a (NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE POLYNUCLEOTIDE PHOSPHORYLASE PNPASE RNA-BINDING GUANOSINE PENTAPHOSPHATE ALPHA) protein domain (PD333034) which is seen in Q53597_STRAT.Residues 598-685 are 82% similar to a (NUCLEOTIDYLTRANSFERASE POLYRIBONUCLEOTIDE TRANSFERASE POLYNUCLEOTIDE PHOSPHORYLASE GUANOSINE PENTAPHOSPHATE PNPASE SYNTHETASE RNA-BINDING) protein domain (PD002075) which is seen in Q8G447_BIFLO.Residues 692-757 are 89% similar to a (NUCLEOTIDYLTRANSFERASE RNA-BINDING BINDING REPEAT TRANSFERASE POLYRIBONUCLEOTIDE NUCLEAR SPLICING RIBONUCLEOPROTEIN DNA-BINDING) protein domain (PD000456) which is seen in Q53597_STRAT.Residues 759-829 are 91% similar to a (RIBOSOMAL S1 30S NUCLEOTIDYLTRANSFERASE TRANSFERASE POLYRIBONUCLEOTIDE RNA-BINDING RIBONUCLEASE R NUCLEASE) protein domain (PD594032) which is seen in Q53597_STRAT.","","-80% similar to PDB:1E3H SEMET DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/GPSI ENZYME (E_value = );-80% similar to PDB:1E3P TUNGSTATE DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/ GPSI ENZYME (E_value = );-49% similar to PDB:2BR2 RNASE PH CORE OF THE ARCHAEAL EXOSOME (E_value = 6.1E_14);-49% similar to PDB:2C37 RNASE PH CORE OF THE ARCHAEAL EXOSOME IN COMPLEX WITH U8 RNA (E_value = 6.1E_14);-49% similar to PDB:2C38 RNASE PH CORE OF THE ARCHAEAL EXOSOME IN COMPLEX WITH A5 RNA (E_value = 6.1E_14);","Residues 124 to 257 (E_value = 3.1e-33) place ANA_1130 in the RNase_PH family which is described as 3' exoribonuclease family, domain 1.Residues 260 to 325 (E_value = 0.0067) place ANA_1130 in the RNase_PH_C family which is described as 3' exoribonuclease family, domain 2.Residues 374 to 453 (E_value = 3.6e-17) place ANA_1130 in the PNPase family which is described as Polyribonucleotide nucleotidyltransferase, RNA binding domain.Residues 456 to 589 (E_value = 3.2e-45) place ANA_1130 in the RNase_PH family which is described as 3' exoribonuclease family, domain 1.Residues 592 to 666 (E_value = 3.7e-18) place ANA_1130 in the RNase_PH_C family which is described as 3' exoribonuclease family, domain 2.Residues 691 to 748 (E_value = 6.5e-15) place ANA_1130 in the KH_1 family which is described as KH domain.Residues 756 to 830 (E_value = 1.3e-13) place ANA_1130 in the S1 family which is described as S1 RNA binding domain.","","nucleotidyltransferase alpha chain [similarity] (PNPase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1131","1210861","1211667","807","4.81","-13.14","28259","ATGACCCACCGCATGATCTTCAACCAGACCGGCTACTTCGGCAGAGGCGCGATCGCCCACATCGCCCCCGAGATCGCCCGCCGGAGCCTGACCAAGGCCTTCATCGTCACCGACCCGGTCCTGGCCGACAACGGCACCGCCGCCCGCATCACCGACCTGCTCGACGAGGCCGGCATCGGCTGGGAGGTCTTCTCCGACGTCATCCCCAACCCGCCGATCGAGAAGGTCCAGGCCGGTCTGGCCGCCTTCCGGGCCTCGGGCGCCGACGTGCTCATCGGCCTGGGCGGGGGCTCGCCCCAGGACACGTGCAAGGCGATCTCGGTGATCGCCACCAACCCCGACTTCGAGGACGTGCTGAGCCTGGAGGGCCTGTCCCCCACGACCCGGCCGGGCGTGCCGATCATCGGCGTGCCCACCACCGCGGGCACGGCCAGCGAGACCACCATCAACTACGTCATCACCGACAGCTCCAAGCAGCGCAAGTTCGTGTGCGTCGACCCCCACGACATCCCGGTCATGGCCTTCAACGCCGAGCACACCGGGGAGAAGTACCGCGACATCGCCGAGGCCTTCGGGGTTGACGGAGCCCGGACCATGCCGCTGGAGGAGGCGCGCGCCGCAGCCGTGGAGGCCGTGGCCCAGCTGACGAGGGACCTGGGCAACCCCACCCGGATCTCGCAGGTCGGGGTGGAGGCCGACGGCATCGAGGCCCTGGCCGATGACGCCTTCGCCGACGTGTGCACGCCGGGCAACCCGCGCCCCGCGACCCGTGAGGACATCAAGGCGCTCTACACCTCACTGCTCTGA","MTHRMIFNQTGYFGRGAIAHIAPEIARRSLTKAFIVTDPVLADNGTAARITDLLDEAGIGWEVFSDVIPNPPIEKVQAGLAAFRASGADVLIGLGGGSPQDTCKAISVIATNPDFEDVLSLEGLSPTTRPGVPIIGVPTTAGTASETTINYVITDSSKQRKFVCVDPHDIPVMAFNAEHTGEKYRDIAEAFGVDGARTMPLEEARAAAVEAVAQLTRDLGNPTRISQVGVEADGIEALADDAFADVCTPGNPRPATREDIKALYTSLL$","Iron-containing alcohol dehydrogenase","Cytoplasm","possible lactaldehyde reductase","L-1;2-propanediol oxidoreductase ","iron-containing alcohol dehydrogenase","","","","","

InterPro
IPR001670
Domain

Iron-containing alcohol dehydrogenase
PF00465	$\"[8-260]T$	Fe-ADH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1970	$\"[1-175]T$	no description

","BeTs to 12 clades of COG1454COG name: Alcohol dehydrogenase IVFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1454 is aompkzyqv--lb-efgh---j----Number of proteins in this genome belonging to this COG is 1","***** IPB001670 (Iron-containing alcohol dehydrogenase) with a combined E-value of 3.9e-08. IPB001670A 89-101 IPB001670B 139-148","Residues 9-176 are 47% similar to a (TCC44H21-2.8) protein domain (PDA1A402) which is seen in Q8T1Q1_TRYCR.Residues 12-194 are 75% similar to a (DEHYDROGENASE ALCOHOL OXIDOREDUCTASE GLYCEROL IRON-CONTAINING DEHYDROGENASE NADP GLYCEROL-1-PHOSPHATE BUTANOL ALDEHYDE-ALCOHOL) protein domain (PD002227) which is seen in Q8G3T1_BIFLO.Residues 13-148 are 47% similar to a (FOMC) protein domain (PD263402) which is seen in P96075_STRWE.Residues 16-153 are 50% similar to a (4-HYDROXYBUTYRATE OXIDOREDUCTASE DEHYDROGENASE NAD-DEPENDENT) protein domain (PDA1A401) which is seen in Q59104_ALCEU.Residues 222-266 are 71% similar to a (DEHYDROGENASE ALCOHOL OXIDOREDUCTASE REDUCTASE IRON-CONTAINING ALDEHYDE-ALCOHOL NAD MALEYLACETATE PLASMID DEHYDROGENASE) protein domain (PD094797) which is seen in Q8G3T1_BIFLO.","","-74% similar to PDB:1RRM Crystal Structure of Lactaldehyde reductase (E_value = 3.0E_60);-74% similar to PDB:2BI4 LACTALDEHYDE:1,2-PROPANEDIOL OXIDOREDUCTASE OF ESCHERICHIA COLI (E_value = 3.0E_60);-74% similar to PDB:2BL4 LACTALDEHYDE:1,2-PROPANEDIOL OXIDOREDUCTASE OF ESCHERICHIA COLI (E_value = 3.0E_60);-52% similar to PDB:1O2D Crystal structure of Alcohol dehydrogenase, iron-containing (TM0920) from Thermotoga maritima at 1.30 A resolution (E_value = 5.9E_16);-52% similar to PDB:1VHD Crystal structure of an iron containing alcohol dehydrogenase (E_value = 5.9E_16);","Residues 8 to 260 (E_value = 3.1e-40) place ANA_1131 in the Fe-ADH family which is described as Iron-containing alcohol dehydrogenase.","","lactaldehyde reductase (PA1146)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1132","1212022","1211753","270","9.52","4.38","10391","ATGTCGGTTACCGCAGAGCGCAAGCAAGAGATCATCGCCGAGTACGCCACCCACGAGGGTGACACGGGCTCCCCGGAGGTCCAGGTCGCCATCCTCACCGAGCGCATCTCCAACCTCACCGAGCACTTCAAGGGCCACGCCCACGACCACCACTCGCGTCGCGGCCTCTACCTGCTCATCGGTAAGCGCCGTCGCCTGCTCGACTACCTCATGAAGGAGGACATCGAGCGCTACCGTGCTCTTATCGCCCGCCTCGGCATCCGCCGCTGA","MSVTAERKQEIIAEYATHEGDTGSPEVQVAILTERISNLTEHFKGHAHDHHSRRGLYLLIGKRRRLLDYLMKEDIERYRALIARLGIRR$","Ribosomal protein S15","Cytoplasm","ribosomal protein S15","ribosomal protein S15","ribosomal protein S15","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Serganov A., Ennifar E., Portier C., Ehresmann B., Ehresmann C. Do mRNA and rRNA binding sites of E.coli ribosomal protein S15 share common structural determinants? J. Mol. Biol. 2002. 320(5):963-978. PMID: 12126618","","","

InterPro
IPR000589
Family

Ribosomal protein S15
PF00312	$\"[6-88]T$	Ribosomal_S15
PS00362	$\"[39-69]T$	RIBOSOMAL_S15

InterPro
IPR005290
Family

Ribosomal protein S15, bacterial chloroplast and mitochondrial type
PD157043	$\"[10-88]T$	Q8G448_BIFLO_Q8G448;
PTHR23321:SF10	$\"[4-88]T$	30S RIBOSOMAL PROTEIN S15
TIGR00952	$\"[4-89]T$	S15_bact: ribosomal protein S15

InterPro
IPR009068
Domain

S15/NS1, RNA-binding
G3DSA:1.10.287.10	$\"[2-89]T$	no description

noIPR
unintegrated

unintegrated
PTHR23321	$\"[4-88]T$	RIBOSOMAL PROTEIN S15, BACTERIAL AND ORGANELLAR

","BeTs to 25 clades of COG0184COG name: Ribosomal protein S15P/S13EFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0184 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 10-88 are similar to a (RIBOSOMAL S15 RRNA-BINDING RIBONUCLEOPROTEIN 30S CHLOROPLAST MITOCHONDRIAL S15 SEQUENCING PROBABLE) protein domain (PD157043) which is seen in Q8G448_BIFLO.","","-80% similar to PDB:1A32 RIBOSOMAL PROTEIN S15 FROM BACILLUS STEAROTHERMOPHILUS (E_value = 8.3E_28);-77% similar to PDB:1EG0 FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME (E_value = 1.6E_26);-77% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 1.6E_26);-77% similar to PDB:1GIX Crystal structure of the ribosome at 5.5 A resolution. This file, 1GIX, contains the 30S ribosome subunit, three tRNA, and mRNA molecules. 50S ribosome subunit is in the file 1GIY (E_value = 1.6E_26);-77% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 1.6E_26);","Residues 6 to 88 (E_value = 8e-37) place ANA_1132 in the Ribosomal_S15 family which is described as Ribosomal protein S15.","","protein S15 (rpsO)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1133","1213241","1212243","999","5.27","-11.15","35892","GTGCCAGCGAGCCTGAGCGCTCCGGGAGGGCCGGGCGCCGTGGTCACGATGGGCATCTTCGACGGCGTCCACCGCGGGCATCAGGCGGTCCTGGGGCGCGTCGTCGAGCTCTCCCATGAGCTCGCCCACGGCGACCGGCGGCCCCTGGCCGTCGCGGTCACCTTCGACCCCCACCCCCGTAGCGTCCACCAGCCCGAGGCCGACCTGCCCCTCATCGCCTCCCTGACCGACCGCCTGGCCTCCCTGGGGGACCTCGGTCTCGACGCGGTCCTGGTCATCACCTACACCCTCGACTTCGCCGCCCAGAGCCCGCAGGACTTCGTGCGCACCTGGCTGGAGGAGCTACTCGGGGCTCGCGCGGTCGTCGTCGGCGACGACGTCCGCTTCGGTTGGCGCAACTCCGGGGACGCAGCCACCCTGGAGCAGATCGGCCGCCAGGACGGCTTCGAGGTGGAGATCGTCTCCACCATCTGCTCCGACGAGGGGCGTCGCTGGTCCTCGACGTGGATCCGCCAGTGCCTCAAGGACGGGAACATGCGGCAGGTCAGCCGGGTCCTGGGCCGTCCCCACCGGCTGCGCGGCGTCGTCGTGCGAGGTCTGCGCCGCGGCCGCGAGCTCGGGTTCCCCACCGCCAACCTGGAGGCCGCCACCGCCGGTGTCGTGCCGCCCGACGGGGTCTACGCCGGCTGGCTGATTCGCGGCTGCGCAGACGAAGGCGATGTCCAGCGGCTGCCCGCCGCCATCTCGATCGGCACCAATCCCACCTTCGACGACGTCCCCCAGCGCACGGTCGAGGCTCATGTCCTGGGGCGAGCCGACCTCAATCTCTATGGCGAGGAGGTGGGGGTCGAGCTCGTCGAGCGCCTGCGCCCCATGCTCGCCTTCGATGGGCTCGACGCGCTCCTGGTGCAGATGCGCGCCGATATCGAGGACACCGCCCGGATTCTGGGAGTCCCGGTCCCCGAGCCGATCCGTCCCGAGGACGTCACCGCGCAGTAG","VPASLSAPGGPGAVVTMGIFDGVHRGHQAVLGRVVELSHELAHGDRRPLAVAVTFDPHPRSVHQPEADLPLIASLTDRLASLGDLGLDAVLVITYTLDFAAQSPQDFVRTWLEELLGARAVVVGDDVRFGWRNSGDAATLEQIGRQDGFEVEIVSTICSDEGRRWSSTWIRQCLKDGNMRQVSRVLGRPHRLRGVVVRGLRRGRELGFPTANLEAATAGVVPPDGVYAGWLIRGCADEGDVQRLPAAISIGTNPTFDDVPQRTVEAHVLGRADLNLYGEEVGVELVERLRPMLAFDGLDALLVQMRADIEDTARILGVPVPEPIRPEDVTAQ$","Riboflavin biosynthesis protein RibF","Cytoplasm","riboflavin biosynthesis protein RibF","putative riboflavin kinase ","riboflavin biosynthesis protein RibF","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR002606
Family

Riboflavin kinase / FAD synthetase
PD003662	$\"[208-316]T$	Q6A7P4_PROAC_Q6A7P4;
PF01687	$\"[185-317]T$	Flavokinase
PF06574	$\"[11-169]T$	FAD_syn
TIGR00083	$\"[14-317]T$	ribF: riboflavin biosynthesis protein RibF

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[13-188]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.30	$\"[190-328]T$	no description
PTHR22749	$\"[186-325]T$	RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE

","BeTs to 16 clades of COG0196COG name: FAD synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0196 is ------yqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB002606 (Riboflavin kinase / FAD synthetase) with a combined E-value of 7.1e-51. IPB002606A 18-27 IPB002606B 55-69 IPB002606C 116-130 IPB002606D 194-215 IPB002606E 224-231 IPB002606F 246-258 IPB002606G 266-308","Residues 13-154 are 52% similar to a (RIBF) protein domain (PD835238) which is seen in Q8G3Y3_BIFLO.Residues 50-108 are 64% similar to a (RIBOFLAVIN KINASE BIOSYNTHESIS TRANSFERASE FAD NUCLEOTIDYLTRANSFERASE RIBF FMN ADENYLYLTRANSFERASE SYNTHASE) protein domain (PD186238) which is seen in Q9Z530_STRCO.Residues 116-179 are 64% similar to a (RIBOFLAVIN KINASE BIOSYNTHESIS TRANSFERASE FAD NUCLEOTIDYLTRANSFERASE RIBF ADENYLYLTRANSFERASE FMN SYNTHASE) protein domain (PD004889) which is seen in Q6AG39_BBBBB.Residues 208-316 are 64% similar to a (RIBOFLAVIN KINASE BIOSYNTHESIS TRANSFERASE FAD RIBF NUCLEOTIDYLTRANSFERASE FMN ADENYLYLTRANSFERASE SYNTHASE) protein domain (PD003662) which is seen in Q6A7P4_PROAC.","","-43% similar to PDB:1MRZ Crystal structure of a flavin binding protein from Thermotoga Maritima, TM379 (E_value = 3.7E_13);-43% similar to PDB:1S4M Crystal structure of flavin binding to FAD synthetase from Thermotoga maritina (E_value = 3.7E_13);-43% similar to PDB:1T6X Crystal structure of ADP bound TM379 (E_value = 3.7E_13);-43% similar to PDB:1T6Y Crystal structure of ADP, AMP, and FMN bound TM379 (E_value = 3.7E_13);-43% similar to PDB:1T6Z Crystal structure of riboflavin bound TM379 (E_value = 3.7E_13);","Residues 11 to 169 (E_value = 1.5e-53) place ANA_1133 in the FAD_syn family which is described as FAD synthetase.Residues 185 to 317 (E_value = 3e-44) place ANA_1133 in the Flavokinase family which is described as Riboflavin kinase.","","biosynthesis protein RibF (ribF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1135","1213572","1215902","2331","8.84","6.86","82475","ATGCTGATGCGACTTCTCAAGGCGGACCTGGCGCGCGGCGCCGTCGTGGCCGCCACCCTGACCGCCCTCATCGCCCTGGCGGCCACACTGATGTCGGCTGGGACGTCCCTGGTGGTGGACAGCCTGTCGGCCACGCACCGGCTCTCGCAGCGGGCCAAGCTTCCGGACCTGGTACAGATGCACTCCGGCCGGATTGACGACCGCGACCTACAGGCGATCGAGACGTGGGTGCAGGCGCGCAGCGACGTCACCGACCACGAGGTCATCACAACCCTTCCGGTAGCGCGCCAGGAGCTGTCCATCAACGGCGTCAACCAGTCCAAGTCCTACAACGAGCCCGCCTTCGTCACCTCTCCCAAGCACCTCGACCTCCTGCTCGACGACGACGGCGAACCCGTGAGCCCGGGGCCGGGAGAGGTGGTGCTGCCGATCCACTACCGGGCGATCAACAGCGCCGATGTCGGCGACAGCGTGACCGTCAGCAGCGCCGGCAGGACCACGACCCTGACCATCGTGGGATTCGCCCGCGACGCCCAGATGAATGCCGCCATGATCCCCTCCAAGCGCCTGGTGGTCTCGCCCGAGGACTTCTCCGCCCTGGAGCAGCAGATCACCGAGCCCGAGTACCTCATTGAGATGCGCCTGACCGACTCCGCCCCTCCCGGCGGCGTCATCGACGCCTACAAGGAGGCGGGTCTGCCCAGTAACGGCATCAACGTCAGCGCCTCGATGATCCAGCTCATGAACTCACTCAACGCCATGCTCATCGTGGCAGTGGCCCTGGTGGTGGCTGTCATTCTGGCGGTTGTCGCCGTCCTCGCCCTGCGCTACACGGTGCTGGCGGCCGTCGAGACGGACCTGGCCCAGATCGCCGTGCTCAAGGCCATTGGGGCGCCACTGAGGCGGATACGCCGCCTCTACGTGGCCAAGTACCTGGCTCTGTCAGTGCTGGGGGCGGCCCTGGGCTACGTGGCCGGCCAGCCCCTGGCCACCGCCTTGGAGGCCCCGACGACCCTCTACCTGGGCCGGCCCGCGACAACCCTGTGGAGCGTGGGGCTGCCGATCCTCACGGTTCTGGTTCTGGCGCTCGGAGTCATCGGCTTTACCTGGTTGGCTCTGCGGCGCATCGGCCGCATCTCGGCCATCGAGGCCCTGCGCAGCGGCACCAGCGCCTCCCTACGCCCACGCCGGCAGCGCTGGAGACTGACCACCCTTCGCCGCCTTCCGGTCCAGGTGTGGCTCGGGGCGCGCGAGTCACTGCGCCCCTCCAACGCCCTGATGCTCGGTGTCCTGGCGCTGTGCACCTTCACCATGGTGCTGCCGACGAATGTCTCCTCGACTCTGAGCGACCCACGTGTGGCCACCTACCTGGGGGCTGGTCGGGCCGATCTGCGTATCGACGTACGCACCGGGGTCCAGGACCTGGCCGCCGTGGAGAAGACCGTCGACTCCGACCCCCGCGTCACCCGGCACACCACGATGCTGCGCCGCAGCTACAAGATGTCCACTGCCACCGGCGGCTGGCAGACGGCGCTCATTGATATCGGGGACCATGAGGCCTTCCCCATGGAGTACCTCTCCGGGCGCGCCCCCACCACCGACGACGAGATCGCCCTGTCCTACAGTCAGGCCCAGGACACGGGCGCCAAGGAAGGCGCCACGGTCACCGTCCGCACCGCCGACGGCGACAAGGACCTGACAGTCACGGGTGTCTACCAGGACATCACCAACAACGGGCATACCGCCAAGGCCACCTTCGACGACGGCGCCCCCGCACTGTGGCAGATCGTCTACGCCGACTCCGGCTCCACTCAGCAGGCCAGCGCCCTCGCCAAGCAGCTGAGCGGCGAGTACCCGGGGATCCAGGCGATCAGCATGAATCAGTATGCCGCCCAGTTCTTCGGGGCCACCGGCTCCCAGGTCCGCGTCGTCACCACGCTGGCCTGCGCCATCGCGCTGGGGCTGTCCTTCCTCATCACGGTGCTGTTCACCGTCCTCATTGTCTCGCGGGAGCGGCCTCAGATCGGCGTCCTGATGGCGCTGGGGTGCACCAGACGGGCCGTTGCGAGGCAGTACCTCATCCGTTTCGGCCTCCTGGCGCTGGTGGGGACCGCCCTGGGGCTCCTGGGGGCCTCCGCTCTGGGCAGCCTCGCGATCGGGGCGGTCATGGCCTCGCGCGGAGCCCCCGACCTTCAGCTCCTCCCCAACTGGTGGCTGATGGGGCTCGTCCTACCAGGGGCACTGCTGGCCACCGTCATCGGCGCTGTCGCCCTGGCCCTCAGACGCCTACGCACCATGCCCCTGACCATGACCCTGACCACCGGCGAGTAA","MLMRLLKADLARGAVVAATLTALIALAATLMSAGTSLVVDSLSATHRLSQRAKLPDLVQMHSGRIDDRDLQAIETWVQARSDVTDHEVITTLPVARQELSINGVNQSKSYNEPAFVTSPKHLDLLLDDDGEPVSPGPGEVVLPIHYRAINSADVGDSVTVSSAGRTTTLTIVGFARDAQMNAAMIPSKRLVVSPEDFSALEQQITEPEYLIEMRLTDSAPPGGVIDAYKEAGLPSNGINVSASMIQLMNSLNAMLIVAVALVVAVILAVVAVLALRYTVLAAVETDLAQIAVLKAIGAPLRRIRRLYVAKYLALSVLGAALGYVAGQPLATALEAPTTLYLGRPATTLWSVGLPILTVLVLALGVIGFTWLALRRIGRISAIEALRSGTSASLRPRRQRWRLTTLRRLPVQVWLGARESLRPSNALMLGVLALCTFTMVLPTNVSSTLSDPRVATYLGAGRADLRIDVRTGVQDLAAVEKTVDSDPRVTRHTTMLRRSYKMSTATGGWQTALIDIGDHEAFPMEYLSGRAPTTDDEIALSYSQAQDTGAKEGATVTVRTADGDKDLTVTGVYQDITNNGHTAKATFDDGAPALWQIVYADSGSTQQASALAKQLSGEYPGIQAISMNQYAAQFFGATGSQVRVVTTLACAIALGLSFLITVLFTVLIVSRERPQIGVLMALGCTRRAVARQYLIRFGLLALVGTALGLLGASALGSLAIGAVMASRGAPDLQLLPNWWLMGLVLPGALLATVIGAVALALRRLRTMPLTMTLTTGE$","ABC-type transport system, involved in lipoprotein release, permease component","Membrane, Cytoplasm","ABC transporter, permease protein, putative","K02004","protein of unknown function DUF214","","","","","

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[208-381]T$ $\"[592-767]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[253-275]?$ $\"[311-331]?$ $\"[350-372]?$ $\"[425-445]?$ $\"[649-669]?$ $\"[699-719]?$ $\"[738-760]?$	transmembrane_regions

","BeTs to 10 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","Residues 123-217 are 56% similar to a (ABC PERMEASE TRANSPORTER TRANSPORTER) protein domain (PD706725) which is seen in Q737Y3_BACC1.Residues 430-678 are 52% similar to a (ABC PERMEASE TRANSPORTER) protein domain (PD839021) which is seen in Q81QE5_BACAN.","","No significant hits to the PDB database (E-value < E-10).","Residues 208 to 381 (E_value = 3.1e-06) place ANA_1135 in the FtsX family which is described as Predicted permease.Residues 592 to 767 (E_value = 1.2e-12) place ANA_1135 in the FtsX family which is described as Predicted permease.","","transporter, permease protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1136","1215914","1216735","822","5.60","-6.43","28853","ATGCGTGCCTCCACCCCATCGCGTTCCTCATGGCGCACCGGTTCAGTAGCCGCGGGATCAGCTGTCCCCGTGGGAGCCGGGCAACCAGTTCTGCGGACCCAGCACCTGTCCAAGAGCTACCACTCCCCCGTCCTGCGAGACCTCGACCTGGATGTGGTGCAGGGGCAGTTCGTCGCCATCATGGGGCCTTCCGGGTCCGGGAAGTCCACCCTTCTGCACTGCCTGAGCGGTATGGACCGGCCCGACGCCGGTTCGGTACTCCTGGGCGGCCAGGAGATCACGAGCCTGAGTGAGAAGGAGCTGGCGGCGCTGCGGCTGACGCGTTTCGGATTCGTCTTCCAGCAGGCGCATCTCCTAACCACCCTGTGCCTGCTGGATAACATCGTCCTGCCCGGGTTCCTGGCGGGTCTGCGTCCGCGCCCCGAGGTCACGGCGCGTGGAGAGGAGCTCATGGAGCGCATGGGGATCGACGAGCTGGCCACCAGCGCCGTCACCGAGGTCTCCGGCGGCCAGCTGCAGCGCGCAGGCATCTGCCGGGCCCTCATCAACGACCCCGGGATCGTCTTCGCCGACGAACCCACCGGAGCGCTCAACTCCGCCACCGCGCTGCAGATCCTCGACCTGCTCGGGGAGATTCACGCCTCGGGGACGACTCTGGTCATGGTCACCCACGACTCCCAGGTTGCGGCCCGGGCCGATCGTGTCCTGGTGCTCGTGGACGGGCAGATCACGGAGGACCTGCTCCTGGGACGATACGAGGAGGCTGACGGCCCCTCACGCCTGACGGCGGTCACCGAGGCCCTCCAGCGCCACAGTGTGTGA","MRASTPSRSSWRTGSVAAGSAVPVGAGQPVLRTQHLSKSYHSPVLRDLDLDVVQGQFVAIMGPSGSGKSTLLHCLSGMDRPDAGSVLLGGQEITSLSEKELAALRLTRFGFVFQQAHLLTTLCLLDNIVLPGFLAGLRPRPEVTARGEELMERMGIDELATSAVTEVSGGQLQRAGICRALINDPGIVFADEPTGALNSATALQILDLLGEIHASGTTLVMVTHDSQVAARADRVLVLVDGQITEDLLLGRYEEADGPSRLTAVTEALQRHSV$","ABC-type transport system, involved in lipoprotein release, ATPase component","Membrane, Cytoplasm","ABC transporter, ATP-binding protein","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[166-209]T$	Q9ZAX8_STRMU_Q9ZAX8;
PF00005	$\"[55-241]T$	ABC_tran
PS50893	$\"[31-265]T$	ABC_TRANSPORTER_2
PS00211	$\"[167-181]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[54-242]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[25-245]T$	no description
PTHR19222	$\"[31-255]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32	$\"[31-255]T$	ABC TRANSPORTER

","BeTs to 23 clades of COG1136COG name: ABC-type transport systems, involved in lipoprotein release, ATPase componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1136 is aom--z-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 10","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.8e-35. IPB005074C 44-91 IPB005074D 155-198 IPB005074E 218-238***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 8.9e-27. IPB013563A 44-78 IPB013563C 164-191 IPB013563D 217-269***** IPB005116 (TOBE domain) with a combined E-value of 1.3e-16. IPB005116A 62-78 IPB005116C 167-180 IPB005116D 187-206 IPB005116E 220-233***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 7.8e-16. IPB010509B 55-80 IPB010509D 162-206 IPB010509E 216-246","Residues 31-225 are 47% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 31-130 are 55% similar to a (LIPOPROTEIN ATP-BINDING RELEASING SYSTEM LOLD) protein domain (PDA0I1Q0) which is seen in Q7UH39_RHOBA.Residues 33-158 are 47% similar to a (PHNL ATP-BINDING) protein domain (PDA1B9K8) which is seen in Q6RCD1_PSEST.Residues 37-223 are 46% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 43-216 are 48% similar to a (ATP-BINDING ABC PRECURSOR TRANSPORTER SIGNAL) protein domain (PDA0X2Z3) which is seen in Q6MM73_BDEBA.Residues 44-224 are 45% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 44-209 are 47% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 44-188 are 50% similar to a (ATP-BINDING PLASMID ABC TRANSPORTER IRON) protein domain (PD957736) which is seen in Q6U5Y8_KLEPN.Residues 44-136 are 60% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 44-112 are 60% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3K8) which is seen in Q9A6K2_CAUCR.Residues 45-225 are 49% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 45-96 are 86% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q74E02_GEOSL.Residues 45-249 are 50% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 45-105 are 62% similar to a (ARD1 ATP-BINDING) protein domain (PD071350) which is seen in Q53912_STRCP.Residues 46-226 are 42% similar to a (ATP-BINDING) protein domain (PD845659) which is seen in Q82AF2_STRAW.Residues 50-227 are 44% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 55-224 are 46% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 146-224 are 63% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 150-226 are 60% similar to a (BLR8070 ATP-BINDING) protein domain (PD727315) which is seen in Q89BS8_BRAJA.Residues 166-209 are 86% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q9ZAX8_STRMU.Residues 169-225 are 70% similar to a (ATPA_apos; ATP-BINDING) protein domain (PD238075) which is seen in Q9LCW1_STRCL.","","-62% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 2.1E_32);-62% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 4.6E_32);-54% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 7.9E_24);-57% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 1.0E_23);-52% similar to PDB:1G29 MALK (E_value = 1.3E_21);","Residues 55 to 241 (E_value = 1e-55) place ANA_1136 in the ABC_tran family which is described as ABC transporter.","","transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1137","1217048","1216746","303","6.74","-0.51","9550","ATGAGCCAGACCGGAGGATGCCGCTGCGGATGCGGCGGGCACGGCAAGCGCAACGAGCAGGACGAGCGGGCTGCCGCGCCCGCAGTCGCCCAGCCGGTGGGTGAGGGATACCGGCCCGAGCCCGTGCAGACCTCCCCGGAGGTCGTCGACGCCGTCGCCATCGCCTCAGCGGTGACGACGGCCCTGGGAGCGGGAGCGCCGCAGGGCGTCACCCCCGGGCACAAGGCCGGTAACCTGCTGGGCCTGCGTGATGTCTCCGCCTCCGCCTCGGGTGGTGGCGGTTGCGGCTGCGGAGGCCACTGA","MSQTGGCRCGCGGHGKRNEQDERAAAPAVAQPVGEGYRPEPVQTSPEVVDAVAIASAVTTALGAGAPQGVTPGHKAGNLLGLRDVSASASGGGGCGCGGH$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","-52% similar to PDB:1WOQ Crystal Structure of Inorganic Polyphosphate/ATP-Glucomannokinase From Arthrobacter sp. strain KM At 1.8 A Resolution (E_value = );-53% similar to PDB:1Y1N Identification of SH3 motif in M. Tuberculosis methionine aminopeptidase suggests a mode of interaction with the ribosome (E_value = );-53% similar to PDB:1YJ3 Crystal structure analysis of product bound methionine aminopeptidase Type 1c from Mycobacterium Tuberculosis (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1139","1218208","1217120","1089","6.67","-1.42","38430","ATGGGGCGGACCGGCCGCGATAACGGCCCCGACCGCGCACGTCGTCGCCCCGATGTTCCCCGCGGCGCGGTCACGGCGGCCGACGGGATCCTCGTGGTGGACAAGCCCCAAGGGCTGACCAGCCACGACGTCGTCGGCGCCACCCGCCGCCTGGCCGCCACCCGCAAGGTGGGGCACGCCGGCACCCTCGACCCCATGGCCACCGGCCTGCTGCTGCTGGGCATCGGGCGCGCCACCCGCTTCCTCACCTACCTGGTGGGAGCCGACAAGACCTACGAGGCCACCGTTCGCCTGGGGGCAGAGACCACGACGGAGGATGCCGACGGGCAGATCGTCGCAGCCCGCGGCTGCCGGATCGAGGACGTACCCGAGGCCCGCCTTCGGGAGGCGCTCACAACCCTGACCGGGCCGATCCAGCAGGTGCCCAGTGCGGTCTCCGCCATCAAGGTCGACGGCGTGCGTGCCTACCAACGCGTCCGTGACGGGCAGGACGTCGAGCTGCAGTCCAGGCCCGTCACCATCCACGAGCTGCGCCTGACCGCAGAGGCCCGGAAGGCGATCGTCGAAGCCGACGGTGCCCTCAGCGACGGCCCAGCGGTGGTGGAAGCGGTCGATATCGACATCCTCGTCTCCTGCTCGTCGGGCACCTACGTGCGCGCCCTGGCCCGGGACCTGGGGCGGGCGCTGGGCTGCGGGGCTCATCTGACTGCGCTGCGGCGCACCGCAGTGGGCCCCTTCGACATCGATGAGGCTCACACCCTGGCGGACCTGTCCGCCCAGGTCGAGACCGACGCCTCCAGCCCTGAGCCTCACGGGGTCACCACGCTCCCGCTGGAGGAGGTCGCCCGGCGCTGCTTCGAGCAGCTGGCTCTGACCGAGGGCGAGGCACGTGCACTGCGCTACGGCCAGCCCCTTGACGCCGAGGTCCTGGAGAGGGCCGAGGCACCCGAGGGCCGTCGGCTGCAGGCCTTTGCGAAGACGGCCGAGCAGCGCGTCGTCGCCGGATTCGCCCCCGGTGGGCGCCTCGTGGCACTGTTGAGGCACCAGGGCCCACGTGCGCGCCCGGTACTGGTCCTGGACCCTGCCTGA","MGRTGRDNGPDRARRRPDVPRGAVTAADGILVVDKPQGLTSHDVVGATRRLAATRKVGHAGTLDPMATGLLLLGIGRATRFLTYLVGADKTYEATVRLGAETTTEDADGQIVAARGCRIEDVPEARLREALTTLTGPIQQVPSAVSAIKVDGVRAYQRVRDGQDVELQSRPVTIHELRLTAEARKAIVEADGALSDGPAVVEAVDIDILVSCSSGTYVRALARDLGRALGCGAHLTALRRTAVGPFDIDEAHTLADLSAQVETDASSPEPHGVTTLPLEEVARRCFEQLALTEGEARALRYGQPLDAEVLERAEAPEGRRLQAFAKTAEQRVVAGFAPGGRLVALLRHQGPRARPVLVLDPA$","tRNA pseudouridine synthase B","Cytoplasm","4.2.1.70","tRNA pseudouridine synthase B ","tRNA pseudouridine synthase B","","Lafontaine D.L., Bousquet-Antonelli C., Henry Y., Caizergues-Ferrer M., Tollervey D. The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase. Genes Dev. 1998. 12(4):527-537. PMID: 9472021","","","

InterPro
IPR002501
Domain

tRNA pseudouridine synthase B, N-terminal-2
PF01509	$\"[49-218]T$	TruB_N

InterPro
IPR004510
Family

tRNA pseudouridine synthase B
PIRSF004489	$\"[27-348]T$	tRNA pseudouridine synthase B

InterPro
IPR014780
Domain

tRNA pseudouridine synthase B, N-terminal
TIGR00431	$\"[27-257]T$	TruB: tRNA pseudouridine synthase B

InterPro
IPR015225
Domain

tRNA pseudouridine synthase II, C-terminal
PF09142	$\"[286-361]T$	TruB_C

noIPR
unintegrated

unintegrated
PTHR13767	$\"[123-182]T$ $\"[203-257]T$	TRNA-PSEUDOURIDINE SYNTHASE

","BeTs to 25 clades of COG0130COG name: Pseudouridine synthaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0130 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002501 (Pseudouridylate synthase TruB, N-terminal) with a combined E-value of 5.2e-70. IPB002501A 33-80 IPB002501B 90-112 IPB002501C 136-149 IPB002501D 212-240***** IPB012960 (DKCLD) with a combined E-value of 3.1e-29. IPB012960B 25-74 IPB012960D 208-260","Residues 27-257 are 37% similar to a (CHLOROPLAST MRNA PEPTIDE TRANS-SPLICING PROCESSING TRANSIT PRECURSOR SPLICING RAA2 FACTOR) protein domain (PD301024) which is seen in RAA2_CHLRE.Residues 29-65 are 89% similar to a (SYNTHASE TRNA PSEUDOURIDINE B LYASE HYDROLYASE PSEUDOURIDYLATE URACIL PSI55 PROCESSING) protein domain (PD006841) which is seen in TRUB_MYCTU.Residues 29-112 are 55% similar to a (SYNTHASE TRNA PSEUDOURIDINE HYDROLYASE PSEUDOURIDYLATE LYASE PROCESSING URACIL PSI55 B) protein domain (PD988491) which is seen in TRUB_RHOBA.Residues 66-110 are 82% similar to a (SYNTHASE TRNA PSEUDOURIDINE B LYASE PSEUDOURIDYLATE PSI55 HYDROLYASE URACIL PROCESSING) protein domain (PD977343) which is seen in Q6AG41_BBBBB.Residues 122-213 are 60% similar to a (SYNTHASE TRNA PSEUDOURIDINE B LYASE PSEUDOURIDYLATE PSI55 HYDROLYASE URACIL PROCESSING) protein domain (PD292997) which is seen in Q6AG41_BBBBB.Residues 214-248 are 85% similar to a (SYNTHASE TRNA PSEUDOURIDINE B LYASE PSEUDOURIDYLATE PSI55 HYDROLYASE URACIL PROCESSING) protein domain (PD002765) which is seen in Q6A7P0_PROAC.","","-59% similar to PDB:1SGV STRUCTURE OF TRNA PSI55 PSEUDOURIDINE SYNTHASE (TRUB) (E_value = 7.1E_66);-56% similar to PDB:1K8W Crystal structure of the E. coli pseudouridine synthase TruB bound to a T stem-loop RNA (E_value = 1.4E_42);-56% similar to PDB:1R3F Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit (E_value = 1.4E_42);-56% similar to PDB:1ZL3 Coupling of active site motions and RNA binding (E_value = 5.5E_42);-48% similar to PDB:1R3E Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit (E_value = 3.1E_37);","Residues 49 to 218 (E_value = 1.3e-50) place ANA_1139 in the TruB_N family which is described as TruB family pseudouridylate synthase (N terminal domain).Residues 286 to 361 (E_value = 8.2e-10) place ANA_1139 in the TruB_C family which is described as tRNA Pseudouridine synthase II, C terminal.","","(AE006113) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1140","1218729","1218232","498","4.76","-11.54","17854","ATGGCCGACGCCGCCCGCGCCCGCAAGGTCGCCGACCGTATTCATGAGACTGTCGCCCGCCTCCTTCAAGGGCGCATCAAGGACCCGCGCCTGGGCTTCGTCACCGTCACCGACGTCCGTGTCACCGGCGACCTCCAGCAGGCCACCGTCTTCTACACCGTCTACGGCAGCGATGAGGAGCGGGAGGAGACGGCCAAGGCGCTGCGCTCAGCCAAGGGACTCATCCGTTCCGAGGTCGGCAAGGCCCTCGGCATTCGCCTGACCCCCTCACTGTCCTTCCAGCTCGACGCCCTCCCCACCACCGCCAAGACCCTCGAGGACGCCCTGGCCCAGGCCCGGGTGCGCGACGCCCAGATCGCCAAGGCCGCCGAGGGAGCCACCTACGCCGGTGACGCCGACCCCTACCGCCACGATGAGGAGGATGAGGAGGCTGTGGGCGGTGACCCCCAGGCCGAGGAGGGCGAGCAGGAGCCCGCAACGGACACCGAGGACCTGTGA","MADAARARKVADRIHETVARLLQGRIKDPRLGFVTVTDVRVTGDLQQATVFYTVYGSDEEREETAKALRSAKGLIRSEVGKALGIRLTPSLSFQLDALPTTAKTLEDALAQARVRDAQIAKAAEGATYAGDADPYRHDEEDEEAVGGDPQAEEGEQEPATDTEDL$","Ribosome-binding factor A","Cytoplasm","Ribosome-binding factor A","K02834 ribosome-binding factor A","ribosome-binding factor A","","Wimberly B.T., Brodersen D.E., Clemons W.M., Morgan-warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V. Structure of the 30S ribosomal subunit. Nature 2000. 407(6802):327-339. PMID: 11014182Chen X., Court D.L., Ji X. Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(15):8396-8401. PMID: 10411886Worbs M., Bourenkov G.P., Bartunik H.D., Huber R., Wahl M.C. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol. Cell 2001. 7(6):1177-1189. PMID: 11430821","","","

InterPro
IPR000238
Family

Ribosome-binding factor A
PD007327	$\"[14-96]T$	RBFA_STRCO_Q9Z527;
PF02033	$\"[6-109]T$	RBFA
TIGR00082	$\"[1-112]T$	rbfA: ribosome-binding factor A
PS01319	$\"[75-96]T$	RBFA

InterPro
IPR009019
Domain

KH, prokaryotic type
G3DSA:3.30.300.20	$\"[6-103]T$	no description

","BeTs to 15 clades of COG0858COG name: Ribosome-binding factor AFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0858 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000238 (Ribosome-binding factor A) with a combined E-value of 5e-21. IPB000238A 34-53 IPB000238B 68-109","Residues 14-96 are 78% similar to a (FACTOR A RIBOSOME-BINDING RRNA PROCESSING 3D-STRUCTURE RIBOSOMAL-BINDING P15B CHLOROPLAST SEQUENCING) protein domain (PD007327) which is seen in RBFA_STRCO.Residues 96-143 are 75% similar to a (A RIBOSOME-BINDING FACTOR RRNA PROCESSING) protein domain (PD200429) which is seen in RBFA_STRAW.","","-59% similar to PDB:1JOS Ribosome Binding Factor A(rbfA) (E_value = 1.5E_11);-60% similar to PDB:1KKG NMR Structure of Ribosome-Binding Factor A (RbfA) (E_value = 4.9E_10);-43% similar to PDB:2GX8 The Crystal Stucture of Bacillus cereus protein related to NIF3 (E_value = 4.9E_10);-47% similar to PDB:1BHS HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE (E_value = 4.9E_10);-47% similar to PDB:1DHT ESTROGENIC 17-BETA HYDROXYSTEROID DEHYDROGENASE COMPLEXED DIHYDROTESTOSTERONE (E_value = 4.9E_10);","Residues 6 to 109 (E_value = 1.1e-45) place ANA_1140 in the RBFA family which is described as Ribosome-binding factor A.","","factor A (rbfA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1141","1220693","1219869","825","5.39","-5.29","29930","ATGACAACCACCACCATCGCCATTGCGGCCGTGACCGTCCTCGTCCTGCTCGCCTTGGCCCTCTCGCTCAAGATCATCACCCAGTACGAGCGGGGCATCGTGTTCAGGCTGGGGCGTCTGCGACCTGTCTACGATCCCGGCCTGCACCTGGTCGTCCCCTTCCTCGAGCGCCTGGTGCGGGTTGATACCCGCGTGGTCACCCTGACCATCCCGCCCCAGGAGGTCATCACGGAGGACAACGTGCCGGCGCGCGTCAACGCCGTCGTCCTGTTCAACGTCACCGACCCGGTCAAGGCCGTCATGGCGGTGGAGAACTACGCGATCGCCACCTCCCAGATCGCGCAGACCACGCTGAGGTCCGTTCTTGGACGCGTCGACCTGGACACCGTGCTCGCCCACCGCAGCGCCTTGAACGCCGATCTGCGAGACATCATTGAGAAGCTCACCGAGCCGTGGGGTGTGGAGGTCAGTGTCGTCGAGATCAAGGACGTCGAGATCCCCGAGCAGATGCAGCGGGCCATGGCCCGTGGGGCTGAGGCCGAGCGTGAGCGCCGTGCCAAGATCATCAACGCCCGTGGTGAGCTCCAGGCCTCCGAGGAGCTGCGTCAGGCGGCGGACACGCTCTCGAAGTCACCGGCTTCTCTCCAGCTGCGCTACCTGCAGACCCTCCTGGAGCTCGGCGCCGACCAGAACTCCACGGTCGTCTTCCCCCTGCCGATGGACATCATCGGACCGCTCCTGGAGCGCTTCGGTCCCCAGGGCGGCCTGCCGGAGGCTAACGAGGGCGAGGGCGGCGAAGGAGCTGGCGCACCGCGTCACCGATGA","MTTTTIAIAAVTVLVLLALALSLKIITQYERGIVFRLGRLRPVYDPGLHLVVPFLERLVRVDTRVVTLTIPPQEVITEDNVPARVNAVVLFNVTDPVKAVMAVENYAIATSQIAQTTLRSVLGRVDLDTVLAHRSALNADLRDIIEKLTEPWGVEVSVVEIKDVEIPEQMQRAMARGAEAERERRAKIINARGELQASEELRQAADTLSKSPASLQLRYLQTLLELGADQNSTVVFPLPMDIIGPLLERFGPQGGLPEANEGEGGEGAGAPRHR$","Stomatin/prohibitin homolog","Membrane, Cytoplasm","Membrane protease subunits, stomatin/prohibitinhomologs","band 7 protein","band 7 protein","","Stewart G.W. Stomatin. Int. J. Biochem. Cell Biol. 1997. 29(2):271-274. PMID: 9147127Foley M., Tilley L. Quinoline antimalarials: mechanisms of action and resistance. Int. J. Parasitol. 1997. 27(2):231-240. PMID: 9088993","","","

InterPro
IPR001107
Family

Band 7 protein
PF01145	$\"[22-195]T$	Band_7
SM00244	$\"[21-178]T$	PHB

InterPro
IPR001972
Family

Stomatin
PR00721	$\"[28-50]T$ $\"[75-96]T$ $\"[110-127]T$ $\"[130-153]T$ $\"[154-172]T$ $\"[173-194]T$ $\"[198-221]T$	STOMATIN

noIPR
unintegrated

unintegrated
PTHR10264	$\"[1-260]T$	STOMATIN-RELATED
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-23]?$	transmembrane_regions

","BeTs to 21 clades of COG0330COG name: Membrane protease subunits, stomatin/prohibitin homologsFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0330 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB001972 (Stomatin) with a combined E-value of 1.2e-80. IPB001972A 22-38 IPB001972B 45-87 IPB001972C 88-126 IPB001972D 127-161 IPB001972E 164-194 IPB001972F 218-227","Residues 35-93 are similar to a (TRANSMEMBRANE PROTEASE MEMBRANE HFLC HFLK FAMILY STOMATIN BAND HYDROLASE STOMATIN-LIKE) protein domain (PD300956) which is seen in Q73V33_MYCPA.Residues 95-167 are similar to a (TRANSMEMBRANE PROTEASE MEMBRANE HFLK STOMATIN FAMILY BAND STOMATIN-LIKE SPFH DOMAIN/BAND) protein domain (PD186090) which is seen in Q6A6C4_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 22 to 195 (E_value = 8.5e-73) place ANA_1141 in the Band_7 family which is described as SPFH domain / Band 7 family.","","protease subunits, stomatin-prohibitin homologs","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1142","1219037","1219918","882","10.31","13.48","31861","ATGGCGCTGGTCGTCGGCTGCTACTGCCTGTGGGGCTTCTTCCCCCTCTACTTCCACCTCCTCTCGGCCGCCGGCAGTGTGGAGATCATCGGTCACCGGATCCTCTGGACGCTGGTGACCTGCCTGACGCTCATCACTCTGCGGCGCCGCTGGGCACAGCTGGTTCACGTGGTGCGCTCACCGCGCCTGCTGGGGATGCTGGCCGTCTGCGGGCTGCTGGTCTCAGTCAACTGGCTCGTCTACGTCTACGGCGTCAACACCGCGCGCACGGCCGACGCCGCCCTGGGCTACTTCATCAACCCGTTGGTGACGGTGGCCCTGGCTGCACTGGTGCTGCATGAGCGGTTGCGCCCCGCTCACCGGGTCTCGATCGCGTTGGCGGGCGCCGCCGTGGCCCTCCTCGTGGTGCTGCAGGGCTCGCTGCCGTGGATCTCCCTGGTGCTGGCTTTCTCCTTCGCCTTGTACGGGCTGGTCAAGAAGCAGCTCGGGCCCGACGTGGACGCTCTGACCGGGCTGACGGTGGAAAGCGCCCTCGTGACTCCCATCGCACTCGCCTACCTGGGCCATATGGCCTGGCAGGGGCAGTCGGCCTGGCAGGCCCCCGATCAAGGGTGGTGGATCCTGGCGCTGCTCGTGGTGGCCGGCCCGGTCACGGCCGTGCCCCTGCTGCTCTTCGCCGCCGGGACCAGGCGCGTGCCGTTGTCCGTGGTCGGGATGGGACAGTACATCGCCCCAACCATCCAGTTCCTGCTGGCCTGGGGCGCCTTCCACGAGCGGATCCCGCCGGCCCGATGGGCGGCCATGATCCTGGTGTGGGCGGCGGTCGCGGTCTTCATCGGTGACGCGGTGCGCCAGCTCCTTCGCCGCCCTCGCCCTCGTTAG","MALVVGCYCLWGFFPLYFHLLSAAGSVEIIGHRILWTLVTCLTLITLRRRWAQLVHVVRSPRLLGMLAVCGLLVSVNWLVYVYGVNTARTADAALGYFINPLVTVALAALVLHERLRPAHRVSIALAGAAVALLVVLQGSLPWISLVLAFSFALYGLVKKQLGPDVDALTGLTVESALVTPIALAYLGHMAWQGQSAWQAPDQGWWILALLVVAGPVTAVPLLLFAAGTRRVPLSVVGMGQYIAPTIQFLLAWGAFHERIPPARWAAMILVWAAVAVFIGDAVRQLLRRPRPR$","DMT superfamily transporter RarD","Membrane, Cytoplasm","rarD protein, chloamphenicol sensitive","K05786 chloramphenicol-sensitive protein RarD","RarD protein, DMT superfamily transporter","","","","","

InterPro
IPR000620
Domain

Protein of unknown function DUF6, transmembrane
PF00892	$\"[9-136]T$ $\"[150-280]T$	DUF6

InterPro
IPR004626
Family

RarD protein
TIGR00688	$\"[1-256]T$	rarD: RarD protein

noIPR
unintegrated

unintegrated
signalp	$\"[1-52]?$	signal-peptide
tmhmm	$\"[2-24]?$ $\"[30-48]?$ $\"[63-83]?$ $\"[93-113]?$ $\"[122-137]?$ $\"[143-163]?$ $\"[168-188]?$ $\"[207-227]?$ $\"[237-257]?$ $\"[263-283]?$	transmembrane_regions

","BeTs to 5 clades of COG2962COG name: Predicted permeasesFunctional Class: RThe phylogenetic pattern of COG2962 is -mt--qvcebrhuj--olinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 106-172 are 59% similar to a (RARD MEMBRANE TRANSMEMBRANE INTEGRAL CHLORAMPHENICOL-SENSITIVE PREDICTED PERMEASE PROTEIN RELATED SENSITIVE) protein domain (PD862290) which is seen in Y195_VIBCH.Residues 318-380 are 67% similar to a (MEMBRANE TRANSMEMBRANE PROTEIN INTEGRAL FAMILY TRANSPORTER DRUG/METABOLITE TRANSPORTER PERMEASE EXPORTER) protein domain (PD058316) which is seen in Q6NGE5_CORDI.Residues 242-301 are 75% similar to a (RARD MEMBRANE TRANSMEMBRANE INTEGRAL CHLORAMPHENICOL-SENSITIVE PREDICTED PERMEASE PROTEIN RELATED SENSITIVE) protein domain (PD010728) which is seen in Q74F40_GEOSL.Residues 318-380 are 67% similar to a (MEMBRANE TRANSMEMBRANE PROTEIN INTEGRAL FAMILY TRANSPORTER DRUG/METABOLITE TRANSPORTER PERMEASE EXPORTER) protein domain (PD058316) which is seen in Q6NGE5_CORDI.","","No significant hits to the PDB database (E-value < E-10).","Residues 112 to 239 (E_value = 5.2e-09) place ANA_1142 in the DUF6 family which is described as Integral membrane protein DUF6.Residues 253 to 383 (E_value = 2.1e-06) place ANA_1142 in the DUF6 family which is described as Integral membrane protein DUF6.","","protein, chloamphenicol sensitive (RARD)","","1","","","Tue Aug 14 11:53:14 2007","","Tue Aug 14 11:53:14 2007","","","Tue Aug 14 11:53:14 2007","Tue Aug 14 11:53:14 2007","Tue Aug 14 11:53:14 2007","Tue Aug 14 11:49:57 2007","","","","","Tue Aug 14 11:49:57 2007","","Tue Aug 14 11:49:57 2007","","Tue Aug 14 11:49:57 2007","Tue Aug 14 11:49:57 2007","","","","","yes","","" "ANA_1143","1221674","1220745","930","7.87","3.47","33281","ATGGACTCACCCGACTTGAGCGTGTGGCTCATCGCCGTCTACGCGCTCATCATGCTGGCTGCTGCGTGGGCCGTGGACGTCCTCGGCTCGCGCAGCGCCCGGCACTCCATGTCCTGGCGGCACTCGGACTTCATGTACCACGACGACGTCGACGGCTGGAGGTGCCACGAGGACCAGTGGCTGTGGCCCACCGCCTTCGACCCGGACAAGCGCGTCATCCGCTATGAGGGCGCTCATGCGATCTGCGGGCGCTGCCCGTCCAAGGACAGCTGCTCGCCCACCCCCGGCCCACGGGAGATCACCCGGCCTGTCGACCCCTGGCCCTACTCCGACGCCGGACGCTTCCACCGTGGCGTGGGCCTGGTCATCGCCTGCGTTGGCGTCTTCATCCCGGTGCTGCTCATGGTGGTCTTTCACGCCACCGGCGACCTCATCGTCCTGGGCACGACGACCGTCGTCGTCATTGTGGCCGGAGTCCTGCCGCTGGCCCGTCACCTGTGGAATACCCCCGACAACGCGCCGGCACACCTGCCCCACGTCGGCTCGCAGGAGTACCAGGAGGCGGAGGAGGCGCGCCGTTCTGCGAGTACTGGTCCCGTCCCGGTGTCGATCAGCGCACGCCCCTCGGGATACCGTTCAGTGCGTGAGGCGGCCGAGGCGATCGCCACCGCTCAGGCCCGTGCAGCCGCCACTGGGCGCACCGTGCATGTCTCCTTCCTCTCCGGGGCTGACGGCACCGGGAAGGCGGACGGCGGGACTGTCGCCTCCGCTGCCTCCGTGGAGCCCGAGCTGCGTCGCGTCACCGCCCTGCGCACCCGCAAGCGCGTCCCGACCACCGGCGCCGAGCTCGGGGCGGATGGAACCCGCGGCGGGGCCCGGCGCTCATGGTCCTCGGCATGGAACGAGGCCACCGACACCACACGCAGATGA","MDSPDLSVWLIAVYALIMLAAAWAVDVLGSRSARHSMSWRHSDFMYHDDVDGWRCHEDQWLWPTAFDPDKRVIRYEGAHAICGRCPSKDSCSPTPGPREITRPVDPWPYSDAGRFHRGVGLVIACVGVFIPVLLMVVFHATGDLIVLGTTTVVVIVAGVLPLARHLWNTPDNAPAHLPHVGSQEYQEAEEARRSASTGPVPVSISARPSGYRSVREAAEAIATAQARAAATGRTVHVSFLSGADGTGKADGGTVASAASVEPELRRVTALRTRKRVPTTGAELGADGTRGGARRSWSSAWNEATDTTRR$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[118-138]?$ $\"[144-162]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 3-188 are 62% similar to a () protein domain (PD905155) which is seen in Q73V34_MYCPA.","","-58% similar to PDB:2J6L STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE (E_value = );-43% similar to PDB:1KOA TWITCHIN KINASE FRAGMENT (C.ELEGANS), AUTOREGULATED PROTEIN KINASE AND IMMUNOGLOBULIN DOMAINS (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1144","1223908","1221674","2235","7.21","1.75","83399","ATGGGCCTGCTGGCCTACCGCACCTACACCAATTCCATGCCTCAGCCGCAGAAGGTGGTCACCGAGAGTGGTGAGACCCTCTTCACGACGCAGGACATCACCGAGGGGCAGAAGCTCTTCCAGGCCAGAGGCCTCATGGAGTACGGCTCCATCCTGGGCCACGGCGGCTATCTCGGTCCCGACTTCACCGCCGAGTACCTTCGCATGGAGGCCACGAGCGTCAAGAACCAGCTCGCCGCCCAAGGGGTCGCCGACCCGGCGGCCGCCACCAAGGAGATGATGCGGACCAACCGCTACGACTCCTCCACGGGAACCCTGGTGTGGACCGATGAGCAGGTCAAGGCCTACAACGAGGCCGTCAACCACTACACCAAGATGTTTGGGCCCGATGCCCACAGCCACGGCCTCAAGCCGGATCTCATCACCGACCCCGTCCAGGTCAAACAGGTGACGGCCTTCTTCGGCTGGACCGCCTGGGGATCGTCCGCACAGCGCCCGGGCCACGACTACTCGTACACGAACAACTGGCCCGCCGAGTCCCTGGTCGGCAACGCACCCACCGGTGACCTCATGATCTGGTCGGTCCTGTCGCTGATCGTCCTCATCGGTGGAACCGGGGTCATGTTCGCCATCTACGGCCGCTGGAGTCAGAAGATCGGCTGGCACTCCGAGGAGGCCCCGGCCCTGTCCTTCCGTCAACCCGAGGACGTCGGGCTGACCAAGTCGCAGCGGGTGGTGGCTTGGTACGTCTTCACCATCGCCGCCCTCTTCCTCGTCCAGACGCTGCTGGGAGCCCTCGCCGAGCACTACCGGGCCGACGTTCTGTCCTTCTTCGGATTCGACCTGGGCCGACTTCTGCCCTTCTCCCTGGCCCGCACCTGGCACGTCCAGCTCTCCTTGTTCTGGACCGCCATCGGTCTGCTCGCGGCCGGCCTGTTCCTGACCCCGTTCATCGCCAGACGCGAGCCCAAGAAGCAGCACGTGCTGGTGTGGACCCTGTTCATCGCGGCCACGGTCGTCGTCGTCCTGTCCTGCTTGGCGGAGGGGGCCAGCCAACACGGCCTGAGCTGGGCCAAGGGGCCGCTGTTCGCCCAGCAGTGGGAGTACCTCGATCTTCCCTTCGTCTTCCAGGTGCTGCTGACCCTGGCCCTGTTCGTCTGGGTGTTCATCATCTGGCGCGCCATGCGCTCGCGCCTGCGCAACGAGCACGTGGCCAACATGCCCTGGCTGTTCATGTTCGCGGCCCTGGCGATCCCCGCCTTCTACGCCGTGGGGATGATGGCGCGCACCGGAACCCACGTGACCGTCGCCGAGTTCTGGCGCTTCTGGGTGGTGCACCTGTGGGTCGAGGACTTCCTCGAGCTGTTCACCACCGTCATGGTCGCCTATGTCTTCGTCCTGCTGGGTGTTGTCCGCGAGAGGATCGCACTGGGCATCATCTTCATGGACATCATCCTGTACTCCGCCGGCGGCGTCATCGGCACCATGCACCACCTCTACTTCTCCGGCACGCCGGTGGAGCACATGGCCCTGGGTGCCTTCTTCTCAGCCGCCGAGGTGATCCCCCTGACCTTCCTGACGGTGGAGGCCTGGGCCTTCATGCAGCTGGGAGCCAACCGCCACGGCAAGGAGGCCGGTCCCTTCCCGCACCGCTGGGCCGTCATGTTCCTCATGGCCGTCGGCTTCTGGAACTTCCTGGGGGCCGGTGTCTTCGGCTTCCTGGTCAACCTGCCCATCGTGTCCTACTACGAGATCGGGACCGCGCTGACGGCCAACCACGCCCACGCCTCCATGATGGGCGTGTACGGCTTCATGGCGCTGGCGCTGGGGATGTTCGCCCTGCGCTACCTGGTGCCGGCCGACAAGTGGCCCGAGAAGCTCGCCAAGACCTCCTTCTGGAGCCTCAACATCGGTCTGGCCTGGATGTGCTTCGCCACCCTGCTGCCGCTGGGCATCCTCCAGCTGCGCTACTCGGTGAGCACGGGTTACTTCGAGGCCCGCCAGCTCACCTACGTCACCAACTCGGTCAACACGATCATCGAGTGGGGGCGGATGCCCGGAGACCTCATCTTCATCCTCGGCGGAGTCCTGCCCTACCTCTACATCGCCTTCCTGGGACTGAGAAACTGGCGTCGAGGGCGGACGGTGGACACCTTCGCCGAGGACGCCCTCTACGAGGAGATCCAGGGTGGGCGCAAGGCCTGGCGCGGTGAGCGCGCGGAGCTGAACGACTGA","MGLLAYRTYTNSMPQPQKVVTESGETLFTTQDITEGQKLFQARGLMEYGSILGHGGYLGPDFTAEYLRMEATSVKNQLAAQGVADPAAATKEMMRTNRYDSSTGTLVWTDEQVKAYNEAVNHYTKMFGPDAHSHGLKPDLITDPVQVKQVTAFFGWTAWGSSAQRPGHDYSYTNNWPAESLVGNAPTGDLMIWSVLSLIVLIGGTGVMFAIYGRWSQKIGWHSEEAPALSFRQPEDVGLTKSQRVVAWYVFTIAALFLVQTLLGALAEHYRADVLSFFGFDLGRLLPFSLARTWHVQLSLFWTAIGLLAAGLFLTPFIARREPKKQHVLVWTLFIAATVVVVLSCLAEGASQHGLSWAKGPLFAQQWEYLDLPFVFQVLLTLALFVWVFIIWRAMRSRLRNEHVANMPWLFMFAALAIPAFYAVGMMARTGTHVTVAEFWRFWVVHLWVEDFLELFTTVMVAYVFVLLGVVRERIALGIIFMDIILYSAGGVIGTMHHLYFSGTPVEHMALGAFFSAAEVIPLTFLTVEAWAFMQLGANRHGKEAGPFPHRWAVMFLMAVGFWNFLGAGVFGFLVNLPIVSYYEIGTALTANHAHASMMGVYGFMALALGMFALRYLVPADKWPEKLAKTSFWSLNIGLAWMCFATLLPLGILQLRYSVSTGYFEARQLTYVTNSVNTIIEWGRMPGDLIFILGGVLPYLYIAFLGLRNWRRGRTVDTFAEDALYEEIQGGRKAWRGERAELND$","Nitric oxide reductase","Membrane, Cytoplasm, Extracellular","nitric oxide reductase","putative nitric-oxide reductase","Nitric-oxide reductase","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[192-212]?$ $\"[245-267]?$ $\"[272-292]?$ $\"[298-318]?$ $\"[327-347]?$ $\"[372-392]?$ $\"[407-425]?$ $\"[452-470]?$ $\"[475-495]?$ $\"[514-534]?$ $\"[555-575]?$ $\"[598-618]?$ $\"[633-653]?$ $\"[689-707]?$	transmembrane_regions

","BeTs to 3 clades of COG3256COG name: Nitric oxide reductase large subunitFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG3256 is -------------c-f---n------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 1-135 are 69% similar to a (NITRIC OXIDE REDUCTASE SUBUNIT B OXIDOREDUCTASE TRANSMEMBRANE REDUCTASE PLASMID CYTOCHROME) protein domain (PD025755) which is seen in Q73V36_MYCPA.Residues 134-188 are 54% similar to a (NITRIC REDUCTASE OXIDE SUBUNIT B CYTOCHROME) protein domain (PD451985) which is seen in P74677_SYNY3.Residues 141-187 are 72% similar to a (REDUCTASE NITRIC OXIDE OXIDOREDUCTASE TRANSMEMBRANE SUBUNIT B PLASMID NITRIC-OXIDE RESPIRATORY) protein domain (PDA06927) which is seen in Q6A6C2_PROAC.Residues 190-430 are similar to a (NITRIC OXIDE REDUCTASE SUBUNIT B OXIDOREDUCTASE TRANSMEMBRANE REDUCTASE PLASMID CYTOCHROME) protein domain (PD467904) which is seen in Q6A6C2_PROAC.Residues 439-571 are 96% similar to a (SUBUNIT REDUCTASE NITRIC OXIDE OXIDOREDUCTASE B TRANSMEMBRANE RESPIRATORY HEME CHAIN) protein domain (PD003369) which is seen in Q73V35_MYCPA.Residues 550-590 are 73% similar to a (RESPIRATORY OXIDOREDUCTASE ELECTRON NITRIC-OXIDE HEME CHAIN REDUCTASE TRANSMEMBRANE) protein domain (PDA0Z6Z5) which is seen in Q6NEM3_CORDI.Residues 572-706 are 82% similar to a (OXIDOREDUCTASE HEME CHAIN TRANSMEMBRANE RESPIRATORY ELECTRON SUBUNIT CYTOCHROME OXIDASE C) protein domain (PD003684) which is seen in Q6A6C2_PROAC.","","-42% similar to PDB:2J13 STRUCTURE OF A FAMILY 4 CARBOHYDRATE ESTERASE FROM BACILLUS ANTHRACIS (E_value = );","No significant hits to the Pfam 21.0 database.","","oxide reductase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1146","1224382","1225953","1572","7.40","2.42","59009","ATGTCCCTCCTGCCCCTAGCCGCACAGACCGTCAACGACGTCGCCCAACAGTGTGTCGACACTGAGACCTTCCCGCTGTGGTTGCGCGTCACCCACTTCATCAACTTCCTCCTCATGGGCGTCCTCATCCGCTCCGGTATCGAGATCATCGCCTCTCATCCCCGCTTCTACTTCAAGGACCAGTGCGAGCCCGGCTCCGAGTGGCTCCGGTTCACCAGGGACAAGGTGCCCCTCGAGGAGGGGGCCTTCACCGCCCGGGATGATCAGCGCGACCTCTCCCCCCTGCTGTCCCTGCCCGGCCGAGCCAAGATCGGGCTGGGGCGCGCCTGGCATGGGGTGGCCACCAGCTTCTGGCTGCTCAACGGCATCATCTACGTCGCCCTCCTCGTGGGCACCGGAGCGTGGCACCGCCTGGTTCCCACCACGTGGCGAATCCTGCCCGACGCCTGGGACTCCCTGCTGACCTACGCACACCTGCGCACTCCATCCTTGTGCGACTTCACTCCCTACGACAGCCTCCAGCAGCTGGGGTACTTCTTCATCGTCTTCATCGCCGCTCCGCTGATGATCATCACGGGGCCGGTCATGTCTCCCGCCGTCGTGGGCCGCTTCCCCTGGTACGCCAAGATGTTCGGTGGCCGCCAGGCCGCCCGCTCCCTGCACCTGATCGGCATGTTCGCCTACCTGGGCTTCGCCGTCGTTCACGTGGGCCTGGTGTTCATCGTGCACGCTCCTCACAACCTCACCCACATCGTCTTCGGCTACTACGACCCGAGTCGGGTGGGTCAGGCCTACGTCACCGTGATCGCGACGATCATCGTCGTGGTGGCGCTGTGGATCGCCATGTCCTACTGGACGCTGACGGACACCCGCCGCAGCCAGCGGATCCTGTGGGACGCCACGCGGGGGATCCGCCGCGTCACGGTGGACCGCTTCAGCTCGCAGCAGGCCGTCAAGAAGCCGTGGACGGAGAAGGACATCTCCAGGTTCCACTGGGTCAACACCCGTACCCCCTCACGGGAGGAGTCCCCGGAGTACCAGGAGCTGGCGGCGAATGACTTCGCCGACTTCCGCCTCGAGGTGGGTGGCATGGTCTCGGCTCCGGCGTCCTTCTCCCTGGCGGAGCTCAAGGCGATCTCCAGCCAGTCCCAGATCACCATGCACACCTGCATGCAGGGTTGGACGGGGATCGCCAAGTGGACGGGGATCCGCGTGCGGGATCTGCTCGCGCAGGTCGGTCAGATCGATCCTGAGGCAGGATGGGTGATGTTCGAGTCCTTCGGCATGGCCCAGAACATGCACGATGGGCGTCCGGTCGAGCCGTACTACACGTGCCTGCCTCTGGACATGGCCCTCGAGGATGACACGATCCTGGCCTGGGGCCGCAATGACGAGCCGCTGTCGGGCATGTTCGGTGCTCCGCTGCGCCTGCGCTGCGAGACGAGCCACGGGTACAAGATGATCAAGTGGGTCCGGTCGGTGACGTTGATCCGTCACTACAGCGAGGTCGGTGACGGCATGGGCGGCACCCGCGAAGACTCCGGTTACCAGGACGTCAACGCGCGCATCTGA","MSLLPLAAQTVNDVAQQCVDTETFPLWLRVTHFINFLLMGVLIRSGIEIIASHPRFYFKDQCEPGSEWLRFTRDKVPLEEGAFTARDDQRDLSPLLSLPGRAKIGLGRAWHGVATSFWLLNGIIYVALLVGTGAWHRLVPTTWRILPDAWDSLLTYAHLRTPSLCDFTPYDSLQQLGYFFIVFIAAPLMIITGPVMSPAVVGRFPWYAKMFGGRQAARSLHLIGMFAYLGFAVVHVGLVFIVHAPHNLTHIVFGYYDPSRVGQAYVTVIATIIVVVALWIAMSYWTLTDTRRSQRILWDATRGIRRVTVDRFSSQQAVKKPWTEKDISRFHWVNTRTPSREESPEYQELAANDFADFRLEVGGMVSAPASFSLAELKAISSQSQITMHTCMQGWTGIAKWTGIRVRDLLAQVGQIDPEAGWVMFESFGMAQNMHDGRPVEPYYTCLPLDMALEDDTILAWGRNDEPLSGMFGAPLRLRCETSHGYKMIKWVRSVTLIRHYSEVGDGMGGTREDSGYQDVNARI$","Oxidoreductase, molybdopterin binding","Membrane, Cytoplasm","Oxidoreductase molybdopterin binding domainprotein","hypothetical protein","oxidoreductase, molybdopterin binding","","Wootton J.C., Nicolson R.E., Cock J.M., Walters D.E., Burke J.F., Doyle W.A., Bray R.C. Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim. Biophys. Acta 1991. 1057(2):157-185. PMID: 2015248Campbell W.H., Kinghorn K.R. Functional domains of assimilatory nitrate reductases and nitrite reductases. Trends Biochem. Sci. 1990. 15(8):315-319. PMID: 2204158Kisker C., Schindelin H., Pacheco A., Wehbi W.A., Garrett R.M., Rajagopalan K.V., Enemark J.H., Rees D.C. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell 1997. 91(7):973-983. PMID: 9428520","","","

InterPro
IPR000572
Domain

Oxidoreductase, molybdopterin binding
G3DSA:3.90.420.10	$\"[307-502]T$	no description
PF00174	$\"[338-513]T$	Oxidored_molyb

noIPR
unintegrated

unintegrated
PTHR19372	$\"[353-502]T$	SULFITE REDUCTASE
tmhmm	$\"[33-53]?$ $\"[117-139]?$ $\"[179-201]?$ $\"[222-242]?$ $\"[261-281]?$	transmembrane_regions

","BeTs to 10 clades of COG2041COG name: Uncharacterized enzymes, related to nitrate reductaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2041 is ao-p-z-q-dr-b-ef-h--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB000516 (Nickel-dependent hydrogenase b-type cytochrome subunit) with a combined E-value of 7.7e-18. IPB000516A 22-55 IPB000516D 203-256***** IPB008335 (Eukaryotic molybdopterin domain signature) with a combined E-value of 3e-07. IPB008335E 393-408 IPB008335F 451-467 IPB008335H 484-497***** IPB011577 (Cytochrome B561, bacterial) with a combined E-value of 1.7e-06. IPB011577A 24-46 IPB011577C 221-240","Residues 24-79 are 82% similar to a (MEMBRANE) protein domain (PD649347) which is seen in Q6M1Q9_CORGL.Residues 100-162 are 68% similar to a (MEMBRANE CGL2953) protein domain (PD695230) which is seen in Q8NLI9_CORGL.Residues 173-240 are 73% similar to a (MEMBRANE OXIDOREDUCTASE TRANSMEMBRANE HYDROGENASE 1.-.-.- FAMILY MLR0877 BMEII0074 ALR2943 BLL0506) protein domain (PD580944) which is seen in Q6M1R1_CORGL.Residues 260-362 are 61% similar to a (MEMBRANE CGL2952) protein domain (PD676378) which is seen in Q8NLJ0_CORGL.Residues 353-500 are 46% similar to a (APE0071) protein domain (PD292775) which is seen in Q9YG30_AERPE.Residues 356-478 are 56% similar to a (UPF0190 YEDY DOMAIN BMEII0305/BRA0990 EXPORTED PATHWAY RSC0620 R01383 MOLYBDOPTERIN XCC1588) protein domain (PD329119) which is seen in Q73ZV4_MYCPA.Residues 356-496 are 56% similar to a (NITRATE HEME REDUCTASE OXIDOREDUCTASE MOLYBDENUM FLAVOPROTEIN FAD ASSIMILATION SULFITE NR) protein domain (PD001253) which is seen in Q98LU0_RHILO.","","No significant hits to the PDB database (E-value < E-10).","Residues 338 to 513 (E_value = 1e-46) place ANA_1146 in the Oxidored_molyb family which is described as Oxidoreductase molybdopterin binding domain.","","molybdopterin binding domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1147","1229013","1226071","2943","9.20","12.52","101712","GTGGCTAAACCACGCGTTCATGAGCTTGCGAAAGAGCTCGACCCCACTGGCAAGAAGGTCACCTCGAAGGTGATCCTGGCCTGGCTCAAGGACCAGGGAGAGTTCGTCAAGGCGGCCTCCTCCGCCGTTGAGCCTCCCGTCGCTCGCCGGGTTCGCGAGCACTTCGCCGCCCAGGTGCAGGAAGCACCGGCGGACACCCAGGCCGACAAGCCTGCCAAGACTGCCTCTCAGGCCCCCAAGCCCTCCAAGAGTGCCCCCAAGCCGGGAGCTCAGGCCGCCAAGCCCGGTCCCGCCGGGGCTCAGGACCAGGCCCCGAGCCCCGCCGTCAAGCCGGCCGCTCCCAAGCCCTCCAAGAGTGCCCCCAAGCCAGGTGCTCAGGCCGCCAAGCCGAGTGACGGAGCCCAGGCCCCGAGTGCCGCCAAGCCGGCGCCCCAGCGGGGAGCCGCGGGCGAGGCGCCCAAGGCCCCCAAGCCTGGAGCCGGAGCTCCCAAGCCTGCGGCCGCCTCCGGTACCCCGGCGTCCGGCTCGCGTCGCAGTGCTCCGACCCCGGGGCCTCGCCCCAGTGCTCCGCGTCCCGGCAACAACCCCTTCGCCACCTCCCAGGGCATGCCCCGTCAGGGCGGTCAGACAGGCCGAGGAGGCCAGCGTTCGGGCCAGTCGCGCTCGGGTGCTCCGCGTCCCGGCAACAACCCCTTCGCCACCTCCCAGGGCATGCCCCGTCCGGGTGGCTCCGGTGGTCCCCGTCCTCAGGGCGGTCCGCGTCCCGGTGGCCCCCGTCCTCAGGGCGGTCCACGGCCTCAGGGAGCCGGCCGCTCCGGTGCTCCGCGTCCGGGCGGTCCGCGTCCCAACCCGGGCATGATGCCCGGCCAGTCCTCCATCGGGCGCCCCGGTGCTCCGGCACGAGGCGGAGCCGGCGGCGGTGGCCGCGGCTCGCGCCCCGGCGGCGGTGGCCGTCCCGGTGGCGGCGGTCGTCCCGGTGGCGGCTTCGGCGGACCCCGCGGTGGCCGCGGTGGTCGCGGTTCCACCCAGGGCGCCTTCGGGCGCGGTGGCGGTGCCCCGCGGGGACGCAAGTCCAAGCGGGCCAAGCGCCAGGAGTTCGAGCAGCAGAGTGCGCCGTCGATCGGCGGTGTCATCGTCCCTCGCGGTGACGGCTCCACCCCGGTGCGCGTGCGCCAGGGGGCCACGCTCACGGACCTGGCCGAGAAGATCAACGCCAACCCCGCGGCCCTGGTGACCGTCCTGTTCCACCTCGGTGAGATGGCCACGGCCACCCAGTCCCTCGACGAGGACACCTTCGCCCTCCTGGGGGCCGAGCTGGGCTACAACGTCCAGATCGTCTCGCCTGAGGACGAGGACCGCGAGCTCCTGGAGTCCTTCGACATCGACCTCGACCCCGATGAGGACGACGCCAACCTCGTGCCCCGGCCCCCGGTGGTCACGGTCATGGGACACGTCGACCACGGTAAGACCAAGCTGCTGGACGCCATCCGCTCCACCGACGTCGTCGCCGGTGAGGCCGGGGGCATCACCCAGTCCATTGGTGCCTACCAGGTCCGCGTCAACCTGAACGACGAGGAGCGCCCGATCACCTTCATCGACACCCCCGGTCACGAGGCCTTCACGGCCATGCGTGCCCGCGGTGCCGAGGTGACCGACATCGCCATCCTCGTCGTGGCCGCCGACGACGGCGTCATGCCTCAGACCGTTGAGGCCCTCAACCACGCCCAGGCGGCCAACGTGCCGATCGTCGTGGCGGTCAACAAGATCGACAAGGAGGGCGCCAACCCGGACAAGATCCGCGGCCAGCTCACCGAGTACGGTCTGGTCCCCGAGGAGTACGGCGGCGACACGATGTTCGTGGACATCTCCGCCAAGCAACGTCTCCACATCGACGAGCTCCTCGAGGCCGTCCTGCTGACTGCGGACGCCGCCCTGGACCTGCGGGCCAACCCGGACACCGAGGCCCGCGGCGTGACCATCGAGGCCAAGCTCGACAAGGGCCGCGGCGCGGTGAGCACCATTCTGGTCGAGCGCGGCACGCTGCGGGTCGGCGACCCGATCGTGGCCGGAAGCGCCTACGGGCGCGTGCGCGCCATGTTCAACGAGCACGGGGAGAACCTCACCGAGGCCGGCCCCGCCCGCCCGGCCCTGGTTCTGGGACTGACCAACGTGCCCAGCGCCGGTGACTCCTTCATCGTCGCCCCCGACGACCGCACGGCCCGCCAGATCGCCGACAAGCGTGAGGCTGCTGAGCGCGCCGCCCTGCTGGCCAAGCGCCGCAAGCGGGTCTCCCTGGAGAACCTCACCGACGTCCTCAAGGAGGGCAAGGTCGACACCCTCAACCTTATCCTCAAGGGCGACAGCTCGGGTGCGGTCGAGGCCCTGGAGGACTCCCTGCTCAAGATCGACGTCGGCGAGGAGGTCGCCCTGCGCGTCATCCACCGCGGCGTGGGTGCCATCACGCAGAACGACGTCAACCTGGCCACGGTGGACTCCGCCGTCATCATCGGCTTCAACGTCCGGCCCGCCGAGCGCGTCTCGGAGATCGCCGACCGCGAGGGCGTCGACATGAAGTTCTACTCGGTCATCTACAACGCGATCGAGGACGTCGAGGCCGCCATGAAGGGCATGCTCAAGCCCGTCTACGAGGAGGTCGAGCTCGGCACCGCCGAGATCCGGCAGATCTTCCGCTCCTCGAAGTTCGGCTCCATCGCCGGCTCCATCGTCCGCTCGGGCATCATCAAGCGGGGGGCCAAGGCCCGCCTGGTGCGCGACGGCGTCGTCATCAACGGAGAGCTGTCCATCGAGACACTGCGCCGCGAGAAGGACGACGTCACCGAGGTCCGCGAGGGCTACGAGTGCGGTATCAACCTGGGCTTCAAGGACCTCGCCGAGGGCGACGTCATCGAGACCTGGGAGATGCGCGAGAAGCCTCGCGACTGA","VAKPRVHELAKELDPTGKKVTSKVILAWLKDQGEFVKAASSAVEPPVARRVREHFAAQVQEAPADTQADKPAKTASQAPKPSKSAPKPGAQAAKPGPAGAQDQAPSPAVKPAAPKPSKSAPKPGAQAAKPSDGAQAPSAAKPAPQRGAAGEAPKAPKPGAGAPKPAAASGTPASGSRRSAPTPGPRPSAPRPGNNPFATSQGMPRQGGQTGRGGQRSGQSRSGAPRPGNNPFATSQGMPRPGGSGGPRPQGGPRPGGPRPQGGPRPQGAGRSGAPRPGGPRPNPGMMPGQSSIGRPGAPARGGAGGGGRGSRPGGGGRPGGGGRPGGGFGGPRGGRGGRGSTQGAFGRGGGAPRGRKSKRAKRQEFEQQSAPSIGGVIVPRGDGSTPVRVRQGATLTDLAEKINANPAALVTVLFHLGEMATATQSLDEDTFALLGAELGYNVQIVSPEDEDRELLESFDIDLDPDEDDANLVPRPPVVTVMGHVDHGKTKLLDAIRSTDVVAGEAGGITQSIGAYQVRVNLNDEERPITFIDTPGHEAFTAMRARGAEVTDIAILVVAADDGVMPQTVEALNHAQAANVPIVVAVNKIDKEGANPDKIRGQLTEYGLVPEEYGGDTMFVDISAKQRLHIDELLEAVLLTADAALDLRANPDTEARGVTIEAKLDKGRGAVSTILVERGTLRVGDPIVAGSAYGRVRAMFNEHGENLTEAGPARPALVLGLTNVPSAGDSFIVAPDDRTARQIADKREAAERAALLAKRRKRVSLENLTDVLKEGKVDTLNLILKGDSSGAVEALEDSLLKIDVGEEVALRVIHRGVGAITQNDVNLATVDSAVIIGFNVRPAERVSEIADREGVDMKFYSVIYNAIEDVEAAMKGMLKPVYEEVELGTAEIRQIFRSSKFGSIAGSIVRSGIIKRGAKARLVRDGVVINGELSIETLRREKDDVTEVREGYECGINLGFKDLAEGDVIETWEMREKPRD$","Translation initiation factor If-2","Cytoplasm, Extracellular","translation initiation factor If-2","translation initiation factor IF-2","translation initiation factor IF-2","","Paduch M., JeleD F., Otlewski J. Structure of small G proteins and their regulators. Acta Biochim. Pol. 2001. 48(4):829-850. PMID: 11995995","","","

InterPro
IPR000178
Family

Initiation factor 2
PD186100	$\"[600-705]T$	IF2_BIFLO_Q8G3Y5;
TIGR00487	$\"[383-980]T$	IF-2: translation initiation factor IF-2
PS01176	$\"[933-955]?$	IF2

InterPro
IPR000795
Domain

Protein synthesis factor, GTP-binding
PR00315	$\"[478-491]T$ $\"[530-540]T$ $\"[546-557]T$ $\"[582-591]T$	ELONGATNFCT
PF00009	$\"[474-645]T$	GTP_EFTU

InterPro
IPR004161
Domain

Translation elongation factor EFTu/EF1A, domain 2
PF03144	$\"[669-732]T$	GTP_EFTU_D2

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[474-639]T$	small_GTP: small GTP-binding protein domain

InterPro
IPR006847
Domain

Translation initiation factor IF-2, N-terminal
PF04760	$\"[391-442]T$	IF2_N

InterPro
IPR015760
Domain

Translation initiation factor 2 related
PTHR23115:SF41	$\"[414-765]T$	TRANSLATION INITIATION FACTOR IF-2

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.10	$\"[882-980]T$	no description
G3DSA:3.40.50.10050	$\"[780-860]T$	no description
G3DSA:3.40.50.300	$\"[475-650]T$	no description
PTHR23115	$\"[414-765]T$	TRANSLATION FACTOR

","BeTs to 26 clades of COG0532COG name: Translation initiation factor 2 (GTPase)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0532 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB000178 (Initiation factor 2) with a combined E-value of 7.4e-192. IPB000178A 418-428 IPB000178B 475-513 IPB000178C 529-564 IPB000178D 565-591 IPB000178E 687-740 IPB000178F 780-823 IPB000178G 846-896 IPB000178H 933-956***** IPB000640 (Elongation factor G, C-terminal) with a combined E-value of 5.8e-17. IPB000640A 477-497 IPB000640C 529-568 IPB000640D 580-590***** IPB004160 (Elongation factor Tu, C-terminal) with a combined E-value of 5.4e-14. IPB004160A 476-496 IPB004160B 521-571***** IPB005517 (Elongation factor G, domain IV) with a combined E-value of 8.4e-14. IPB005517A 477-501 IPB005517C 529-568***** IPB000817 (Prion protein) with a combined E-value of 4.8e-07. IPB000817A 295-336 IPB000817A 298-339 IPB000817A 297-338 IPB000817A 305-346 IPB000817A 299-340 IPB000817A 308-349 IPB000817A 240-281 IPB000817A 304-345 IPB000817A 314-355 IPB000817A 293-334 IPB000817A 309-350 IPB000817A 316-357 IPB000817A 300-341 IPB000817A 245-286 IPB000817A 281-322 IPB000817A 296-337 IPB000817A 286-327 IPB000817A 289-330 IPB000817A 272-313 IPB000817A 292-333 IPB000817A 223-264 IPB000817A 294-335 IPB000817A 311-352 IPB000817A 284-325 IPB000817A 291-332 IPB000817A 238-279 IPB000817A 317-358 IPB000817A 310-351 IPB000817A 283-324 IPB000817A 280-321 IPB000817A 302-343 IPB000817A 225-266 IPB000817A 239-280 IPB000817A 275-316 IPB000817A 234-275 IPB000817A 231-272 IPB000817A 307-348 IPB000817A 312-353 IPB000817A 290-331 IPB000817A 211-252 IPB000817A 263-304 IPB000817A 229-270 IPB000817A 221-262 IPB000817A 237-278 IPB000817A 282-323 IPB000817A 288-329 IPB000817A 257-298 IPB000817A 301-342 IPB000817A 303-344 IPB000817A 201-242 IPB000817A 153-194 IPB000817A 287-328 IPB000817A 278-319 IPB000817A 285-326 IPB000817A 256-297 IPB000817A 220-261","Residues 3-55 are 75% similar to a (INITIATION FACTOR GTP-BINDING BIOSYNTHESIS TRANSLATION IF-2 E RIBONUCLEASE PROBABLE SEQUENCING) protein domain (PD015373) which is seen in IF2_MYCTU.Residues 388-441 are 92% similar to a (INITIATION FACTOR TRANSLATION GTP-BINDING BIOSYNTHESIS IF-2 CHLOROPLAST ALTERNATIVE IF-2 3D-STRUCTURE) protein domain (PD004037) which is seen in Q6AG49_BBBBB.Residues 443-481 are 87% similar to a (INITIATION FACTOR IF-2 BIOSYNTHESIS TRANSLATION GTP-BINDING INFB) protein domain (PD958346) which is seen in Q6A7M5_PROAC.Residues 479-568 are 53% similar to a (INITIATION FACTOR GTPASE 2 BIOSYNTHESIS TRANSLATION GTP-BINDING) protein domain (PD971532) which is seen in Q8TV36_METKA.Residues 482-547 are 90% similar to a (INITIATION FACTOR GTP-BINDING BIOSYNTHESIS TRANSLATION IF-2 PROBABLE IF-2 IF-2MT CHLOROPLAST) protein domain (PD032196) which is seen in IF2_STRCO.Residues 551-599 are 77% similar to a (INITIATION FACTOR BIOSYNTHESIS TRANSLATION GTP-BINDING IF-2 FACTOR-LIKE) protein domain (PD920774) which is seen in Q7RBF3_PLAYO.Residues 565-606 are 92% similar to a (GTP-BINDING FACTOR INITIATION BIOSYNTHESIS TRANSLATION IF-2 LEPA ELONGATION TYPA TYPA/BIPA) protein domain (PD103945) which is seen in IF2_OCEIH.Residues 600-705 are similar to a (INITIATION FACTOR GTP-BINDING BIOSYNTHESIS TRANSLATION IF-2 PROBABLE IF-2 IF-2MT CHLOROPLAST) protein domain (PD186100) which is seen in IF2_BIFLO.Residues 774-837 are 95% similar to a (INITIATION FACTOR GTP-BINDING BIOSYNTHESIS TRANSLATION IF-2 IF-2MT IF-2 CHLOROPLAST PEPTIDE) protein domain (PD002098) which is seen in IF2_TROWT.Residues 776-876 are 72% similar to a (INITIATION FACTOR GTP-BINDING BIOSYNTHESIS TRANSLATION IF-2 PROBABLE IF2 INTEIN 5B) protein domain (PD867209) which is seen in Q6T719_STRAG.Residues 880-972 are similar to a (INITIATION FACTOR GTP-BINDING BIOSYNTHESIS TRANSLATION IF-2 IF-2MT CHLOROPLAST IF-2 PEPTIDE) protein domain (PD398681) which is seen in Q73VV4_MYCPA.","","-67% similar to PDB:1ZO1 IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex (E_value = 4.2E_133);-44% similar to PDB:1G7R X-RAY STRUCTURE OF TRANSLATION INITIATION FACTOR IF2/EIF5B (E_value = 1.0E_33);-44% similar to PDB:1G7S X-RAY STRUCTURE OF TRANSLATION INITIATION FACTOR IF2/EIF5B COMPLEXED WITH GDP (E_value = 1.0E_33);-44% similar to PDB:1G7T X-RAY STRUCTURE OF TRANSLATION INITIATION FACTOR IF2/EIF5B COMPLEXED WITH GDPNP (E_value = 1.0E_33);-74% similar to PDB:1Z9B Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2 (E_value = 6.5E_25);","Residues 391 to 442 (E_value = 7.4e-11) place ANA_1147 in the IF2_N family which is described as Translation initiation factor IF-2, N-terminal region.Residues 474 to 645 (E_value = 7.1e-49) place ANA_1147 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain.Residues 669 to 732 (E_value = 1.4e-10) place ANA_1147 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2.","","initiation factor If-2 (GTPase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1148","1229419","1229105","315","10.32","5.09","11345","GTGCCCGAGCGCACCTGTATCGGCTGTCGACAAAAGGCCCCGCGGACGCAGCTGCTGCGTCTCGTCCTGACGCCGAGCGGTGAGCTCGACGTCGATGCCCGGGCCGTCAGACCCGGGCGCGGCGCCTGGATCCACCCGGATCCGGTGTGCCTCGACCTCACTGAGCGACGACGCGCCGCTTCACGTGCTCTGCGCACCGGTGGACCACTGGATGTGGCCCGGGTGCGCGGGTTCCTGGAGCGGAGGCTGGTCAACGACGGCGAGGTCCCCGCCGCCCGACCGGGTGAGCGGACCACCGATAGCGAAGGCGGGTAG","VPERTCIGCRQKAPRTQLLRLVLTPSGELDVDARAVRPGRGAWIHPDPVCLDLTERRRAASRALRTGGPLDVARVRGFLERRLVNDGEVPAARPGERTTDSEGG$","Nucleic-acid-binding protein implicated in transcription termination","Cytoplasm, Extracellular","Predicted nucleic-acid-binding proteinimplicated in transcription termination","K07742 hypothetical protein","protein of unknown function DUF448","","","","","

InterPro
IPR007393
Family

Protein of unknown function DUF448
PF04296	$\"[1-82]T$	DUF448

noIPR
unintegrated

unintegrated
G3DSA:3.30.1230.10	$\"[1-87]T$	no description

","BeTs to 5 clades of COG2740COG name: Predicted nucleic-acid-binding protein implicated in transcription terminationFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2740 is ---------drlb-------uj---wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 4-53 are 72% similar to a (TERMINATION IMPLICATED YLXR NUCLEIC-ACID-BINDING PREDICTED TRANSCRIPTION RIBOSOMAL FAMILY CYTOSOLIC HYPOTEHTICAL) protein domain (PD027364) which is seen in Q6AG50_BBBBB.","","-49% similar to PDB:1G2R Hypothetical Cytosolic Protein Coded by Gene from NUSA/INFB, YLXR Homologue (E_value = );-52% similar to PDB:2GSX Complement Receptor Type 2 (E_value = );-42% similar to PDB:1CHR CRYSTAL STRUCTURE OF CHLOROMUCONATE CYCLOISOMERASE FROM ALCALIGENES EUTROPHUS JMP134 (PJP4) AT 3 ANGSTROMS RESOLUTION (E_value = );-42% similar to PDB:2CHR A RE-EVALUATION OF THE CRYSTAL STRUCTURE OF CHLOROMUCONATE CYCLOISOMERASE (E_value = );-43% similar to PDB:1H3D STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE (E_value = );","Residues 1 to 82 (E_value = 2.8e-18) place ANA_1148 in the DUF448 family which is described as Protein of unknown function (DUF448).","","nucleic-acid-binding protein implicated in transcription termination","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1149","1230596","1229556","1041","5.14","-15.07","37598","ATGGACATCAATATGCCGGAGCTGCGAGGCGCTGCCGACGAGCTCGGTATTGACCTGGACAACCTGCTGCCCGCTATCGAGGACGCCATCCTGGGGGCCTACTCCAAGGTGCCCGGGGCCATCCGTGGTGCCCACGTCGAGATTGACCGTCGCACCGGGCACATGAGCGTCCTGGCCCCGGAGGTCGACGAGGAGGACCAGCCCACGGGGGAGTACTTCGACGACACCCCCGATGACTTCGGTCGCATCGCCCAGGCCACTGCCCGCAGCGTCATCGTCCAGCGCATCCAGGACCGCCGCGACTTCGAGGTCCTGGGCGCCTTCAAGGACAAGACCGGCGAGCTGATCTCCGGCACCGTCGAGCAGGGGCGCGACCCCCGCATCGTCTACGTGCGCCTGGACGAGGAGCACGAGGGCATCATGCCTCCCCATGAGCAGGTCCCCGGCGAGCGCTACCGCCATGGCGATCGTGTGCGCGCCTACGTCACCGACGTCTCGCGCGGCACCCGCGGGGCTCAGATCATCCTGTCGCGCACCCACCCGGGTCTGGTTCGCAAGCTCTTCGAGCGCGAGGTTCCCGAGCTCTCCTCCGGTGACGTCGAGATCGTCTCCGTCGCCCGGGAGGCCGGGCACCGAACCAAGATGGCTGTGCGCTCCAAGGTGCGCGGCGTCAACGCCAAGGGCGCCTGCATCGGTCCCATGGGGCAGCGGGTGCGCGCGGTCATGACCGAGCTCGGTGGAGAGAAGATCGACATCGTGGACTACTCGGAGGACCCGGCCCGCTTCATCGCCAACGCCCTGTCCCCGGCCCGCGTGGCCGCCGTGGGCGTCATCGACGCCGAGGAGCGCACCGCTCGCGCCATCGTCCCCGACTTCCAGCTCTCCCTGGCCATCGGCAAGGAGGGGCAGAACGCCCGTCTGGCCGCGCGCCTGACCGGCTGGAAGATCGACATCCACGCTGATGCCGAGTCCGGTGAGATCACCCCCGGCCAGGGGTCTCAGTCCGACGACGTGACAGGTCCCTCAGAGCTGGGCGACTGA","MDINMPELRGAADELGIDLDNLLPAIEDAILGAYSKVPGAIRGAHVEIDRRTGHMSVLAPEVDEEDQPTGEYFDDTPDDFGRIAQATARSVIVQRIQDRRDFEVLGAFKDKTGELISGTVEQGRDPRIVYVRLDEEHEGIMPPHEQVPGERYRHGDRVRAYVTDVSRGTRGAQIILSRTHPGLVRKLFEREVPELSSGDVEIVSVAREAGHRTKMAVRSKVRGVNAKGACIGPMGQRVRAVMTELGGEKIDIVDYSEDPARFIANALSPARVAAVGVIDAEERTARAIVPDFQLSLAIGKEGQNARLAARLTGWKIDIHADAESGEITPGQGSQSDDVTGPSELGD$","Transcription termination factor NusA","Cytoplasm","transcription termination factor NusA","putative transcriptional termination/antitermination factor","transcription termination factor NusA","","Wimberly B.T., Brodersen D.E., Clemons W.M., Morgan-warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V. Structure of the 30S ribosomal subunit. Nature 2000. 407(6802):327-339. PMID: 11014182Chen X., Court D.L., Ji X. Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(15):8396-8401. PMID: 10411886Worbs M., Bourenkov G.P., Bartunik H.D., Huber R., Wahl M.C. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol. Cell 2001. 7(6):1177-1189. PMID: 11430821","","","

InterPro
IPR003029
Domain

RNA binding S1
SM00316	$\"[111-179]T$	S1
PS50126	$\"[113-179]T$	S1

InterPro
IPR004087
Domain

KH
SM00322	$\"[209-282]T$	KH

InterPro
IPR004088
Domain

KH, type 1
PS50084	$\"[282-346]T$	KH_TYPE_1

InterPro
IPR009019
Domain

KH, prokaryotic type
G3DSA:3.30.300.20	$\"[193-271]T$ $\"[272-324]T$	no description

InterPro
IPR010213
Domain

Transcription termination factor NusA
TIGR01953	$\"[7-323]T$	NusA: transcription termination factor NusA

InterPro
IPR013735
Domain

NusA N-terminal
PF08529	$\"[7-103]T$	NusA_N

noIPR
unintegrated

unintegrated
G3DSA:3.30.1480.10	$\"[1-135]T$	no description
PTHR22648	$\"[1-327]T$	TRANSCRIPTION TERMINATION FACTOR NUSA

","BeTs to 23 clades of COG0195COG name: Transcription elongation factorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0195 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB013735 (NusA N-terminal) with a combined E-value of 2.8e-103. IPB013735A 82-125 IPB013735B 170-216 IPB013735C 217-266 IPB013735D 277-318","Residues 1-98 are 69% similar to a (TERMINATION/ANTITERMINATION TRANSCRIPTIONAL FACTOR TERMINATOR N TRANSCRIPTION RELATED UTILIZATION) protein domain (PD786983) which is seen in Q6A7M4_PROAC.Residues 8-101 are 62% similar to a (TRANSCRIPTION SUBSTANCE N UTILIZATION A NUSA FACTOR TERMINATION ANTITERMINATION ELONGATION) protein domain (PD244709) which is seen in Q9KYR1_STRCO.Residues 104-210 are 76% similar to a (TRANSCRIPTION SUBSTANCE N UTILIZATION A FACTOR NUSA TERMINATION ELONGATION ANTITERMINATION) protein domain (PD004993) which is seen in Q8G3Y6_BIFLO.Residues 228-318 are similar to a (TRANSCRIPTION SUBSTANCE UTILIZATION N A NUSA FACTOR TERMINATION ANTITERMINATION ELONGATION) protein domain (PD002633) which is seen in NUSA_MYCLE.","","-70% similar to PDB:1K0R Crystal Structure of Mycobacterium tuberculosis NusA (E_value = 4.6E_99);-75% similar to PDB:2ASB Structure of a Mycobacterium tuberculosis NusA-RNA complex (E_value = 9.9E_78);-75% similar to PDB:2ATW Structure of a Mycobacterium tuberculosis NusA-RNA complex (E_value = 9.9E_78);-59% similar to PDB:1HH2 CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA (E_value = 1.9E_57);-59% similar to PDB:1L2F Crystal structure of NusA from Thermotoga maritima: a structure-based role of the N-terminal domain (E_value = 1.9E_57);","Residues 7 to 103 (E_value = 2.4e-10) place ANA_1149 in the NusA_N family which is described as NusA N-terminal domain.","","termination factor NusA (nusA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1150","1231308","1230790","519","4.74","-13.05","18269","ATGGCAGCCTCTGATCAGCGCAAGGATCCGCGACAGCGCGCTGACGCGCTGGCCCGCAGTCTCGCCGATCTGCTCTCTCCGATCGTCAACGACGCCGGGCTTCATCTTGAGAGCGTGGAGACCACCCGGGCAGGAAAGTACTCGGTCGTGCGCGTCTTCGTGGACCTGCTGGATGGTCCCGGAGACCTCGATCTCGACGCCCTGGGGCCCGTGACCGCGGCCATCTCCCAGGCCCTCGACGAGGCCGACCCCGTCAAGGGTCAGTACACCCTCGAGGTCTCCACCCCCGGAGCCGAGCGGGAGCTGACCACCCTGCGTCACTTCCGGCGTGCCGTTGGTCATAGTGCCCGGGTGCGCACGGCCGACGACGAGCTCACCGGCGTCGTCACCGCGGCCGAGGAGGACGACGAGGCCAGTGACCACAACGGTGGCATGGTCGGGATCGAGGTCGACGGCGTCGAGCGCCGCATCGCGTTGGGGGACATCACCGAGGCGAGGATGGTGCTGGCCGGGCTCTAG","MAASDQRKDPRQRADALARSLADLLSPIVNDAGLHLESVETTRAGKYSVVRVFVDLLDGPGDLDLDALGPVTAAISQALDEADPVKGQYTLEVSTPGAERELTTLRHFRRAVGHSARVRTADDELTGVVTAAEEDDEASDHNGGMVGIEVDGVERRIALGDITEARMVLAGL$","Uncharacterized conserved protein","Cytoplasm","Hypothetical UPF0090 protein","hypothetical protein","protein of unknown function DUF150","","","","","

InterPro
IPR003728
Family

Protein of unknown function DUF150
PF02576	$\"[24-167]T$	DUF150

noIPR
unintegrated

unintegrated
G3DSA:3.30.300.70	$\"[8-96]T$	no description

","BeTs to 15 clades of COG0779COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0779 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB003728 (Domain of unknown function DUF150) with a combined E-value of 1.2e-17. IPB003728 63-116","Residues 27-119 are 58% similar to a (UPF0090 YHBC SLR0742 SAV2554 ACIAD0367 BD1545 SYNW0601 PLU4531 YHHE CTC01272) protein domain (PD007388) which is seen in YE34_COXBU.","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 167 (E_value = 2.4e-36) place ANA_1150 in the DUF150 family which is described as Uncharacterised BCR, YhbC family COG0779.","","UPF0090 protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1153","1231433","1232482","1050","8.67","2.42","34992","GTGAACACTCGCCGCCCTCCCCTGCCCACTCAGTCGAACGGCTCTCAGCCGCCCTATCGTGACCAGGTCGGCGTCAGGCCCCGTACCAGTGGCGGCACCGGTGCGGCAGGTCACGGCTTGACGCGCCGTACCGCGGTGCTCGCGGTGGGAACGGCTCTGACCGCGACGCTGAGCGGTTGCGGGCTGCGCCTGGGGAAGGGCTCCCCGGCGTCCCTGCCGTCAGCCTCAGCGGCGGAGACGGCTCGAGATGGCCTGGCCAGGCAGGCCGCGCTCATCTCTTCCACTGCCGGTGTGGTCGCACAGGCCGGCGGCGGGGATGCCACGACCGCGGCCCTGGCCGAGGGGGTCAAGCAGACGGCTGACGCCCAGCTCGAGACCTTGGGCGGGGTATGGCAGCCCTGGCCCTCACAGGTGCCCTCCGCCTACCCCACGGTGGCTCCGGTGCCGTCGGCCTCGGCGGGTGCCTCCGCACAGGACCTGGCCGCGGCCCTGGCCGATGGATCGACGCTGGCCCGCCGGGCGGCGATCGCCGCCGCCTCGGAGCAGGATGTCCGGCTCTTCACCTCGCTGACGGTGGCCTGGAGTCTCCAGCATGATCTCTTCCAGCCGCCGAGCTCAGCGGACAAGTCACGGGTGGAGGTGGCGCAGGGCTCCAAGATCAGCTCCGGTCTGCTGACCTCCTACGACGCGGCCCGCTACGCCATGGAGGCGCTTGCGGCGCGCAGTGACGACTCCCAGCGCACTCGGGCGGTCGCTGACGCCAAGGCCGCCACCTCCGTGGTCAACGCCGCGGTGGCTGCAGGCTCCGAGGACAAACGGTTGGGCGCCTACGCCGCACCGAGTGAGTCCACAGACCCCAGCGTGAGCACCCAGGTGCTCTGGGCCCGGCAGGTGTGGTCCAACGTCGTGTCGGCAGAGGTGCAGGAGGCCGGTTCCGCCAAGGCCTCCAGCCCGGCCCGCGAAGCGGCCGTCACCGGTGCGGTCGACGCCGCCCGGCGCGCCACCGCCTGGGGCGCGGATTTCTCCTCCCTGCCCGGCTACGCCGCCTGA","VNTRRPPLPTQSNGSQPPYRDQVGVRPRTSGGTGAAGHGLTRRTAVLAVGTALTATLSGCGLRLGKGSPASLPSASAAETARDGLARQAALISSTAGVVAQAGGGDATTAALAEGVKQTADAQLETLGGVWQPWPSQVPSAYPTVAPVPSASAGASAQDLAAALADGSTLARRAAIAAASEQDVRLFTSLTVAWSLQHDLFQPPSSADKSRVEVAQGSKISSGLLTSYDAARYAMEALAARSDDSQRTRAVADAKAATSVVNAAVAAGSEDKRLGAYAAPSESTDPSVSTQVLWARQVWSNVVSAEVQEAGSAKASSPAREAAVTGAVDAARRATAWGADFSSLPGYAA$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1154","1232484","1232720","237","6.79","-0.34","8950","ATGCATCTTCTTGTGATGGCCGTGGCCGCCATCGCCGCCCTTGCGGCCGTGGACCAGCTCTTGTTGTGGATGGAGCGCCGCGGCTGGATCTACTGGCGGCGGCGCAAGCGCGACCCTCGTGGCGCCCTCCTGGGTCCCATCGACAACGTCTTCAACCCGGCCCACGAGCATGTGATTGAGCAGCAGGAGACCGAGGAGCGCCTGGCCGACCTCCAGGGCGACGCAGCCCCGAGGTGA","MHLLVMAVAAIAALAAVDQLLLWMERRGWIYWRRRKRDPRGALLGPIDNVFNPAHEHVIEQQETEERLADLQGDAAPR$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-15]?$	signal-peptide
tmhmm	$\"[4-24]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1155","1232724","1235747","3024","6.78","-3.62","108047","ATGACGAGCGCAGCCGCCCCCACTGCGCAGCACCCGCTGCGCCGGTGGACACGTCGAGTGCCGTTACACGACTACCAGCAGAGTCTCCTTGACCGGCTCCATCCCGACGACGGAGCCACGCTTCACCTGCTGGCGCCACCGGGAGCGGGAAAGACCCTCATGGGGCTGGAGCTGGCCGTGCGCAACGGCCGTCGTGCGCTCGTCCTCGTACCCACCACCGTCATCGGGGCCCAGTGGATCCATCAGGCACAGGAGCTCTTCACCTCCTCCTTCGGCTCCCCTTCGGTCACTGGTTCCGTCGGCGCCCACCTGCCGGGCACACGTCCAGATCAGGCGGCAGAAGCCGCCGACCTGACAGTGCTGACCTATCAGTCCCTGGCCGTCGTCGGCTCCTCCCCCACCTGGAGCAACGTGGCCCGCTCGCACTGGGTCACTGAGCTCACGGCCGGCGGACGAAGCGCCGTGAGCGCCGAGGCATGGCTGAAGCGGCTGGAGGCCGATAATCCTCGGGCCTACACCCGTGGACTCCGTTCACGCACTGCCACCATCCGCCGTCAGGTCGATGAGCTCGACGACGACGCCATCGACTCGATTCTGGGGCCCGGTGCCCGGGCACGCCTGGACGCACTCGTCACGGCGGGAGTCGCCACCATCGTCCTCGACGAGTGCCACCACCTCAAGGCCCACTGGGCCGTCGTCGTCCACTACCTCGTACGACGTCTGAAACGGGTCGGCCTGTCCCCCACGCTCATCGGCCTGACGGCCACTGAGCCCTCGGGTGAGGACCGGTCGGCCCGCCGTTATCGTGCGCTCCTGGGCGACGTCGACGCTGAGGTTCCGGTTCCGGCCGTCATCCGCGCCGGTCACCTCGCCCCCTGCCGTCAACTGGCCTGGTTCACGCTCCCGTCCCCGGAGGAGACGGAGTTCCTGGCTACCGCCGGAGAGGAGCTCCATCACCGGGTGGGCGAGCTGCTGCTGAGCCCCGACGGCATCGACTACCTGCTTGAGGTCGTCGCCCCGCCCATGTCGTCCACGGCTCCAGGTGACGGGAGCGAGTCGGGGCCACTGCCTCGTACTGGTGGGCCGGATGACGACCATGTCTCCGCGACATCGAAGCCTCTTGAGGAGGACGAACTGGTGCGTCGGATCGTCGCGGGTTTCGACGCCGACCCGCTGCTGGCCGCGACCGCAGCAGCGCTGCTGCGCAGGACAGGCAGCTACCGGGGCACGGCTCTGAGTACTCGAGTTGTCCCGCTCCTGCCCGAGCTCGACCTGCTTGATCTTGACGATGAGCTCAGGCTCCTGGGGCGGTACGCTCATGACCGGCTCCTGGCAGTGCCGGAGCGCCGGCGGGACTGGGAGTCCACACGCGAGCTGCTGAGAGGTTTCGGGCTGTACCTGACCGATTCCGGTATCCGGGCGGGACGATCCCCGGTGGATACCATCACTGCCGTCTCCAGGGCCAAGGACACGGCTGTCATCGACATCCTGCGTCACGAGCTCGACTCCATCGGTGATCGGCTGCGGGCAGTGGTTGTCACCGATGCGGCCGAGCACTCGGCTCCTCACCGAGCGCTTGACGTCCTGGTCCCGGGGTCACACCCCGGCCCTGCGGGAGGCGCGGTGCGTTGTATGAGTACGCTGCTCAGTGATGCGGATCTTCGCTCCTTGCACCCGGTGCTGCTGACCGGCTCTCGCCTGAGCCTGGCCAGCGGTGATACCTCGCTACTGGATCGGCTGCGTCGGAGCACCGGTCTCGCACTCCCCGCCACCGATGACGGCTGGATGCTCTCGGTCACCGGGCAGGGAGTTGGCAGCGCCGGGCTCGTCCTGGCCGTCAGTGAGCTGGTCACTGCCGGGGAGATACGGCTCGTCGTGGGCACCCGGGGGCTTCTCGGCGAGGGCTGGGACTGCCCCGCCGTGAACACGCTCATCGATCTCACGGCGGCGACGACCTCGGCCTCAACGCAGCAGCTGCGCGGCCGCACGATGCGTCTGGACCCTGGCTGGGGCGACAAGGTCGCTCACAACTGGTCCGTCACCTGCCTCCTGCCAAGCCATCCCCGCCTGCGCTCGGCCCCGGACCTGAACCGACTGCGTCGCAAGGCCGAGCACCTGTGGTCACTGGTTCGGATCGATGACCCCGAGGCCTCCCCAGTCTCGGCCTCCGACGAGCCTTGTGGCACTCCTGTCGTCGAGACGGGCCTCGACGCCATGCTGGCACCGGTCCAGCGCCGCCTTCTCGACAAACTGGGTGACGGCGCCGCCCCGGAGGATATTGATGCCCTCAACTCCGCCACCCTGGCAGGCCTCGATCGTCGGGTTGAGTCGCGGCGATGGCTCGCTCAAGCACCCACGGCGCACCGGGTGTCACGACGCGGCCATGGCCGAGCGCTGGAGGCGGTCGAGATCACGAGTGCCCCGGGTCTGCTGCGCCGGGGATCACCCACGGCCTTCTGGAGCGCTGCGGCTCGCGCCGTTCTCGATGTCGCCCTGTCGCGATGCGACCTCACTGCGGACGGGGACTCCTCTGACAGGCCCCTTCCCGACCTCGTGGTTCGCGAGAGTCCCACCGATTCGCTCGGCGAATCTCGTCCGCGGGTGCTGATCGGCCTGGACGGGGTAGAGACCCGTCAGAGCGCTCATTTCGCCGACATCCTCACCGAGCTCCTGAGCTCCCCGGGGCGCCGTCCCCGTTTCATCCTCGAGGCCGCTGCCACAACATTGGCTCGAGGTACGGCTGAGCGGCCTCTGAGTAGGCTGCGGCGCCTCCTGGGAGGGCTGCTGACGCTGGGGGCATGGAACCACGATGACAGTGTTCACCTTATGGTTCCGACGGCCCTGGCCCGCTCGCGAGCCGATTTGGAGGCCCTCGTTCACTCCTGGTCCACACGGGTGGGGCCGTGCCGGCTTCACCTGGTTGCCGATGCCGATGACGCGGCAGCGCTCCTGTCCTGCCTCGGCAGCGGTGGTCCCACCGGACGAGTCGAGCTGCGTCGTACCAGGCGCTGGCTGGAGGACTGA","MTSAAAPTAQHPLRRWTRRVPLHDYQQSLLDRLHPDDGATLHLLAPPGAGKTLMGLELAVRNGRRALVLVPTTVIGAQWIHQAQELFTSSFGSPSVTGSVGAHLPGTRPDQAAEAADLTVLTYQSLAVVGSSPTWSNVARSHWVTELTAGGRSAVSAEAWLKRLEADNPRAYTRGLRSRTATIRRQVDELDDDAIDSILGPGARARLDALVTAGVATIVLDECHHLKAHWAVVVHYLVRRLKRVGLSPTLIGLTATEPSGEDRSARRYRALLGDVDAEVPVPAVIRAGHLAPCRQLAWFTLPSPEETEFLATAGEELHHRVGELLLSPDGIDYLLEVVAPPMSSTAPGDGSESGPLPRTGGPDDDHVSATSKPLEEDELVRRIVAGFDADPLLAATAAALLRRTGSYRGTALSTRVVPLLPELDLLDLDDELRLLGRYAHDRLLAVPERRRDWESTRELLRGFGLYLTDSGIRAGRSPVDTITAVSRAKDTAVIDILRHELDSIGDRLRAVVVTDAAEHSAPHRALDVLVPGSHPGPAGGAVRCMSTLLSDADLRSLHPVLLTGSRLSLASGDTSLLDRLRRSTGLALPATDDGWMLSVTGQGVGSAGLVLAVSELVTAGEIRLVVGTRGLLGEGWDCPAVNTLIDLTAATTSASTQQLRGRTMRLDPGWGDKVAHNWSVTCLLPSHPRLRSAPDLNRLRRKAEHLWSLVRIDDPEASPVSASDEPCGTPVVETGLDAMLAPVQRRLLDKLGDGAAPEDIDALNSATLAGLDRRVESRRWLAQAPTAHRVSRRGHGRALEAVEITSAPGLLRRGSPTAFWSAAARAVLDVALSRCDLTADGDSSDRPLPDLVVRESPTDSLGESRPRVLIGLDGVETRQSAHFADILTELLSSPGRRPRFILEAAATTLARGTAERPLSRLRRLLGGLLTLGAWNHDDSVHLMVPTALARSRADLEALVHSWSTRVGPCRLHLVADADDAAALLSCLGSGGPTGRVELRRTRRWLED$","DNA or RNA helicase of superfamily II","Cytoplasm","conserved hypothetical protein","hypothetical protein","DEAD/DEAH box helicase domain protein","","Gorbalenya A.E., Koonin E.V., Donchenko A.P., Blinov V.M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989. 17(12):4713-4730. PMID: 2546125","","","

InterPro
IPR006935
Family

Type III restriction enzyme, res subunit
PF04851	$\"[19-81]T$	ResIII

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[18-286]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[32-275]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
PTHR11274	$\"[46-88]T$	RAD25/XP-B DNA REPAIR HELICASE

","BeTs to 8 clades of COG1061COG name: DNA or RNA helicases of superfamily IIFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1061 is ao-pkzy--drl--e-g-------t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 440-734 are 50% similar to a (MB1212C) protein domain (PD493854) which is seen in Q8VK53_BBBBB.Residues 440-734 are 50% similar to a (MB1212C) protein domain (PD493854) which is seen in Q8VK53_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 19 to 81 (E_value = 1.2e-05) place ANA_1155 in the ResIII family which is described as Type III restriction enzyme, res subunit.Residues 23 to 264 (E_value = 9.6e-08) place ANA_1155 in the DEAD family which is described as DEAD/DEAH box helicase.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1156","1237593","1235761","1833","5.25","-22.38","66541","GTGCTGCACAGACTCTCCACCTCCTTCATCCGTACCCTGCGCGAGGACCCGGCCGACGCCGAGGTCGCCAGCCACCGCCTGCTCGTGCGCGCCTGCTACGTCCGCCGGGCCGCCCCCGGGGTCTACACCTGGCTGCCGCTGGGGCTGCGGACGCTGCGCAAGATCGAGGACATCGTGCGCCAGGAGATGGACGCCATGGGCGGCCAGGAGGTCCACTTCCCGGCCCTCCTGCCGGCCGAGCCCTACCAGGCCACCGGACGCTGGGACGACTACGGCCCCACCCTGTTCAAGCTCCGCGACCGCAAGGACGGGGACTACCTGCTGGCCCCCACCCACGAGGAGATGTTCACCCTCGCGGTCAAGGACCTCTACTCCTCCTACAAGGACCTGCCGGCCGTCATCTACCAGATTCAGACCAAGTACCGTGACGAGGCCCGCCCCCGCGCCGGCATCATCCGCGGCCGCGAGTTCGTCATGAAGGACTCCTACTCCTTCGACATCGACGACGCCGGCCTGGCCGCCGCCTACCAGGCCCACCGGGACACCTACGAGCGGATCTTCACCCGCCTGGGCCTGGACTACGTCATCGTCAACGCCATGGCCGGCGCCATGGGCGGCTCCCACTCCGAGGAGTTCCTCCACCCCTGCGAGATCGGTGAGGACACCTTCGTGCGCTCCTCAAGCGGCTACGCGGCCAACGCCGAGGCCGTCACCACCGTGGTCCCCGAGGCCGTGGACGCCTCCGGGATCGGCCCGGCGCGCGTGGTGGACACCCCCGACACCCCCACCATCGACTCCCTGGTCGAGCTGTGCAACCGGGCCTACCCGCGCTCCGACGGGCGGGCCTGGACGGCCGCCGACACCCTCAAGAACGTCGTCGTCACCCTCATCCACCCCGGCGGCGAGCGCGAGCTGCTGGTCGTCGGCGTGCCCGGGGACCGCGACGTCGACATGAAGCGCCTGGAGGCCGCCGTCGCCCCCGCCGAGGTCGAGATGGCCGGCGACACCGACTTCGAGACCCACCCCGAGCTCGTGCGCGGCTACATCGGCCCCACCGCCATCGGCCCGAACTCCCCGCTGCGGCGTGTGGAGAAGCTCGAGGACGGCACCGAGGTCCTCACCGGCTCCGTGCGCTACCTCGTCGACCCCAGGATCGTGGAGGGAACCAGCTGGGTCACCGGTGCCAACACCGACAAGAAGCACGTCCTGGACCTGGTCATGGGGCGCGACTTCACCGCCGACGGCACCATCGAGGCCGCCGAGGTCCGTGAGGGCGACCCCGCCCCCGACGGCTCCGGCCCTCTCCACCTGGCTCGCGGTATCGAGATCGGCCACATCTTCGAGCTGGGACGCAAGTACTCCCAGGCCCTGGGACTGACCGTCCTGGACGAGAACGGCAAGGCCCGCGTAGTCACCATGGGCTCCTACGGCATCGGCGTCAGCCGCGTCATGGCCGCCCTGGCCGAGGCCAACCACGACGACAAGGGGCTGACCTGGCCCGTCCAGATCGCCCCCTACCACGTGCAGGTCCTGGCCACCGGCAAGGACCAGTCCGTCTTCGACGTCGCCGAGCAGATCGCCTCATCCCTGGATGCCGACGGCGTCGAGGTCCTCTACGACGACCGCCGCAAGGTCTCCGCCGGCGTGAAGTTCGCCGACGCCGAGCTCCTCGGCCTGCCCTATACGCTGGTCGTCGGCCGGGACCTGGCCAAGGAGGGAACCGTGGAGATCCGCGATCGCCGCACCGGCGAGCGCCGCTCCGTGCCCGCCGACGCCGCAGCGGCCGAGCTCAGCACCACCGTCCGCGCCGCCCTGGAGGCCGCCCGTCACTGA","VLHRLSTSFIRTLREDPADAEVASHRLLVRACYVRRAAPGVYTWLPLGLRTLRKIEDIVRQEMDAMGGQEVHFPALLPAEPYQATGRWDDYGPTLFKLRDRKDGDYLLAPTHEEMFTLAVKDLYSSYKDLPAVIYQIQTKYRDEARPRAGIIRGREFVMKDSYSFDIDDAGLAAAYQAHRDTYERIFTRLGLDYVIVNAMAGAMGGSHSEEFLHPCEIGEDTFVRSSSGYAANAEAVTTVVPEAVDASGIGPARVVDTPDTPTIDSLVELCNRAYPRSDGRAWTAADTLKNVVVTLIHPGGERELLVVGVPGDRDVDMKRLEAAVAPAEVEMAGDTDFETHPELVRGYIGPTAIGPNSPLRRVEKLEDGTEVLTGSVRYLVDPRIVEGTSWVTGANTDKKHVLDLVMGRDFTADGTIEAAEVREGDPAPDGSGPLHLARGIEIGHIFELGRKYSQALGLTVLDENGKARVVTMGSYGIGVSRVMAALAEANHDDKGLTWPVQIAPYHVQVLATGKDQSVFDVAEQIASSLDADGVEVLYDDRRKVSAGVKFADAELLGLPYTLVVGRDLAKEGTVEIRDRRTGERRSVPADAAAAELSTTVRAALEAARH$","Prolyl-tRNA synthetase","Cytoplasm","prolyl-tRNA synthetase","prolyl-tRNA synthetase ","prolyl-tRNA synthetase","","Wolf Y.I., Aravind L., Grishin N.V., Koonin E.V. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999. 9(8):689-710. PMID: 10447505Aberg A., Yaremchuk A., Tukalo M., Rasmussen B., Cusack S. Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase. Biochemistry 1997. 36(11):3084-3094. PMID: 9115984","","","

InterPro
IPR001063
Family

Ribosomal protein L22/L17
PS00464	$\"[272-296]?$	RIBOSOMAL_L22

InterPro
IPR002314
Domain

tRNA synthetase, class II (G, H, P and S)
PF00587	$\"[51-221]T$	tRNA-synt_2b

InterPro
IPR002316
Family

Prolyl-tRNA synthetase, class IIa
PR01046	$\"[70-88]T$ $\"[106-117]T$ $\"[136-144]T$ $\"[146-157]T$	TRNASYNTHPRO

InterPro
IPR004154
Domain

Anticodon-binding
G3DSA:3.40.50.800	$\"[501-602]T$	no description
PF03129	$\"[507-600]T$	HGTP_anticodon

InterPro
IPR004500
Family

Prolyl-tRNA synthetase, bacterial
TIGR00409	$\"[4-600]T$	proS_fam_II: prolyl-tRNA synthetase

InterPro
IPR006195
Domain

Aminoacyl-transfer RNA synthetase, class II
PS50862	$\"[35-500]T$	AA_TRNA_LIGASE_II

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[38-500]T$	no description
PTHR11451	$\"[40-254]T$ $\"[363-598]T$	TRNA SYNTHETASE-RELATED
PTHR11451:SF3	$\"[40-254]T$ $\"[363-598]T$	PROLYL-TRNA SYNTHETASE

","BeTs to 26 clades of COG0442COG name: Prolyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0442 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002316 (Prolyl-tRNA synthetase signature) with a combined E-value of 2.9e-23. IPB002316A 70-88 IPB002316B 106-117 IPB002316C 136-144 IPB002316D 146-157***** IPB007214 (YbaK/prolyl-tRNA synthetase associated region) with a combined E-value of 1.2e-17. IPB007214A 140-157 IPB007214B 182-206 IPB007214C 440-453 IPB007214D 473-482","Residues 38-131 are similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA BIOSYNTHESIS ATP-BINDING SERYL-TRNA THREONYL-TRNA SERINE--TRNA SERRS PROLYL-TRNA) protein domain (PD589298) which is seen in Q6NGM7_CORDI.Residues 135-169 are 85% similar to a (SYNTHETASE AMINOACYL-TRNA PROLYL-TRNA LIGASE PROLINE--TRNA PRORS BIOSYNTHESIS ATP-BINDING TRNA PROLINE-TRNA) protein domain (PD965815) which is seen in Q6C8Z3_EEEEE.Residues 175-230 are 83% similar to a (SYNTHETASE AMINOACYL-TRNA PROLYL-TRNA LIGASE PROLINE--TRNA PRORS BIOSYNTHESIS ATP-BINDING TRNA PROLINE-TRNA) protein domain (PD969276) which is seen in Q6AEX8_BBBBB.Residues 249-306 are 68% similar to a (SYNTHETASE PROLYL-TRNA AMINOACYL-TRNA LIGASE PRORS PROS PROLINE--TRNA GLOBAL RNA PROBABLE) protein domain (PDA0K084) which is seen in Q6AEX8_BBBBB.Residues 258-302 are 73% similar to a (SYNTHETASE PROLYL-TRNA AMINOACYL-TRNA) protein domain (PD978270) which is seen in Q8G3N0_BIFLO.Residues 308-418 are 66% similar to a (SYNTHETASE AMINOACYL-TRNA PROLYL-TRNA LIGASE PRORS PROS PROLINE--TRNA PROLINE GLOBAL RNA) protein domain (PD985826) which is seen in SYP_MYCTU.Residues 310-418 are 55% similar to a (SYNTHETASE AMINOACYL-TRNA PROLYL-TRNA LIGASE PROLINE--TRNA DNA-BINDING PRORS BIOSYNTHESIS ATP-BINDING TRNA) protein domain (PD006954) which is seen in SYP_STRCO.Residues 422-513 are similar to a (SYNTHETASE AMINOACYL-TRNA PROLYL-TRNA LIGASE PROLINE--TRNA ATP-BINDING PRORS BIOSYNTHESIS TRNA PROLINE-TRNA) protein domain (PD120576) which is seen in Q6A7L9_PROAC.Residues 520-597 are 70% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS THREONYL-TRNA HISTIDYL-TRNA PROLYL-TRNA HISTIDINE--TRNA HISRS) protein domain (PD000606) which is seen in Q6AEX8_BBBBB.","","-56% similar to PDB:2J3L PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE) (E_value = 1.1E_109);-56% similar to PDB:2J3M PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH ATP, MANGANESE AND PROLINOL (E_value = 1.1E_109);-65% similar to PDB:2I4L Rhodopseudomonas palustris prolyl-tRNA synthetase (E_value = 3.8E_52);-65% similar to PDB:2I4M Rhodopseudomonas palustris prolyl-tRNA synthetase in complex with ProAMS (E_value = 3.8E_52);-65% similar to PDB:2I4N Rhodopseudomonas palustris prolyl-tRNA synthetase in complex with CysAMS (E_value = 3.8E_52);","Residues 51 to 221 (E_value = 2.8e-50) place ANA_1156 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T).Residues 507 to 600 (E_value = 5.6e-23) place ANA_1156 in the HGTP_anticodon family which is described as Anticodon binding domain.","","synthetase (proS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1157","1237853","1238815","963","5.65","-7.21","33398","ATGGACAGGCACTCCTCCATCCGTGAGGGACACGGCCAGACGTGGGCGAAGGCCATTCTCCTGGGTGAGCACTCGGTCGTCTACGGGCACCCCGCTGTGGCCGTACCGTTGCAGGACCTGCGGATGCGAGCCACGGCGAGCCCGACCTCGGGTCCCTCCACGCTGAGCAGCCTGGACTACTCGGGGCCCCTGGACCAGGCCGGGTCCCGGTTCGCCAGTGTCGCACGGGCCTTCGAGGTGGCCCGCGAGTTCTCCGGGGGCCTGGTCCAGGCCTTCGATATCACCACCGTGAGCGACTTCCCCCATGAGCGCGGGCTCGGCTCGTCGGCGGCGGCGGCCGGCGCGATCATTCGCGCTGTCCTAGACGCCTGCGGGCGCGAGGCCAGCTCCGATGAGCTGTTCGCGCTGACGCAGATGGCTGAGCAGATCGCGCACGGCAAGCCCTCGGGGCTGGACGCCGCCGCCACCTGCTCACCGTGCCCCATCCGGTTCCAGGGCGGACAGATGCGCCCCTTAAGCCAGCGCATCGACAACGCTTTCCTGGTCATCGCCGACTCCGGGATCCACGGCTCCACCCGAGAGGCCGTTGGAGGCCTGCGCCGGCGCTACGAGAGCGATCCTGACAACATCGGCCCGCGTATCAACCGACTGGGAGCACTCACCCAGAACGCGATCATGGCCCTGGACCAGGCCGACGCCCCGGCCCTCGGGGTCGCCATGGATGAGGCGCACGCGGTGCTGACCGAACTCAGCCTGAGCCTGCCGATCCTCGATGACCTCACCGAGGCCGCCCGCAGCGCCGGGGCACTGGGCGCCAAGCTCACCGGCGGAGGACTCGGCGGCTGCGTCATCGCCCTGGTCACCGGCGAGTCCGCCACGCGCCGGGTGCGTGCCGCCCTGGAACAGGCCGGCGCACCGGAGACATGGAGCTATCGGATGCGCATCAGCGAGGTGGACGAGTGA","MDRHSSIREGHGQTWAKAILLGEHSVVYGHPAVAVPLQDLRMRATASPTSGPSTLSSLDYSGPLDQAGSRFASVARAFEVAREFSGGLVQAFDITTVSDFPHERGLGSSAAAAGAIIRAVLDACGREASSDELFALTQMAEQIAHGKPSGLDAAATCSPCPIRFQGGQMRPLSQRIDNAFLVIADSGIHGSTREAVGGLRRRYESDPDNIGPRINRLGALTQNAIMALDQADAPALGVAMDEAHAVLTELSLSLPILDDLTEAARSAGALGAKLTGGGLGGCVIALVTGESATRRVRAALEQAGAPETWSYRMRISEVDE$","Mevalonate kinase","Cytoplasm","mevalonate kinase","mevalonate kinase ","mevalonate kinase","","Tsay Y.H., Robinson G.W. Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase. Mol. Cell. Biol. 1991. 11(2):620-631. PMID: 1846667Lee M., Leustek T. Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene. Arch. Biochem. Biophys. 1999. 372(1):135-142. PMID: 10562426","","","

InterPro
IPR006204
Domain

GHMP kinase
PF00288	$\"[93-159]T$	GHMP_kinases_N

InterPro
IPR006205
Family

Mevalonate kinase
PIRSF500058	$\"[9-313]T$	Mevalonate kinase
PTHR10457:SF4	$\"[89-303]T$	MEVALONATE KINASE
TIGR00549	$\"[16-286]T$	mevalon_kin: mevalonate kinase

InterPro
IPR006206
Family

Mevalonate and galactokinase
PR00959	$\"[14-38]T$ $\"[98-120]T$ $\"[271-288]T$	MEVGALKINASE

InterPro
IPR012197
Family

Mevalonate kinase/phosphomevalonate kinase
PIRSF000546	$\"[9-319]T$	Mevalonate kinase/phosphomevalonate kinase

InterPro
IPR013750
Domain

GHMP kinase, C-terminal
PF08544	$\"[224-305]T$	GHMP_kinases_C

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[12-173]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.890	$\"[178-302]T$	no description
PTHR10457	$\"[89-303]T$	MEVALONATE KINASE/GALACTOKINASE

","BeTs to 9 clades of COG1577COG name: Mevalonate kinaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1577 is aom-kzy----l------------t-Number of proteins in this genome belonging to this COG is 2","***** IPB000705 (Galactokinase) with a combined E-value of 3.1e-09. IPB000705C 91-112 IPB000705H 271-284***** IPB006203 (GHMP kinase, ATP-binding region) with a combined E-value of 3.4e-08. IPB006203A 14-29 IPB006203B 100-114 IPB006203C 272-281","Residues 185-309 are similar to a (KINASE TRANSFERASE ATP-BINDING MEVALONATE MK MAGNESIUM BIOSYNTHESIS LIPOLYTICA YARROWIA STRAIN) protein domain (PD696214) which is seen in Q9FD64_ENTFC.","","-45% similar to PDB:2OI2 Streptococcus pneumoniae Mevalonate Kinase in Complex with Diphosphomevalonate (E_value = 8.3E_31);","Residues 93 to 159 (E_value = 4.4e-16) place ANA_1157 in the GHMP_kinases_N family which is described as GHMP kinases N terminal domain.Residues 224 to 305 (E_value = 8.6e-11) place ANA_1157 in the GHMP_kinases_C family which is described as GHMP kinases C terminal.","","kinase (mvk)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1159","1238776","1239837","1062","7.06","0.15","36195","ATGGAGCTATCGGATGCGCATCAGCGAGGTGGACGAGTGACCGCCGTACCCCCTGGAGCCGCTGCCGGCTCCTCCCCGGCCGCTGCCCCGACGGCGACAGCCAGCGCCAACACCAACATCGCGCTCATCAAGTACTGGGGCAAGGTGGATGAGGCGCTGGCGATCCCCGCCACCTCGAGCCTGTCCCTCACCCTCGCAGGGACCCGTACGACGACGACGGTCTCCTTCGACGGCGGGGACGGTGCCGCAGACTCGGTGACGATCAACGGGGTCTCCCCCAGCGCCGTGGAGCTGGGGCGAGTGACCCGGTTCCTCGACCTGGTACGTTCCCGCTCAGGCGTCGCCACACCGGCTACCGTCATCTCCCGGGCCTCGGTGCCGCTGGCGGCCGGGCTGGCGAGCTCGGCGGCGGGCTTTGCGGCGCTTGCGGCGGCCGCCTCCCGCGCCGCCGGCATGAACCTCGACGACCGTGCCCTCTCCCGGCTGGCCCGGCGCGGCTCGGGGTCGGCCACGCGCTCCGTCTTCGGTGGGCTGGTCCTGTGGAACGCGGGCCACGACGACGCCTCCTCCTACGCCGAGCCGGTCGCCTGCGAGATGGACCTGGCAATGGTCGTCGTCGTGCTCTCGCAGCGTTACAAGCCCATCAGCTCGACCCGTGCCATGCGGGCCACCATGTCGTCCTCCCCTCTCTTCCCCGCCTGGGTCGAGGCCAGCTGGAGAGACCTTCAGGTGGCGCTGGAGGCGGTCCGGGCGGGCGACCTGGCGCGGCTCGGAGAGATCGTCGAGGGTAACGCCCTGGGCATGCACGCCACGATGATCGCGGCCCGCCCGGGCATCGTCTACTGGCTGCCGCAGACCGTTGCGGCGCTGCACGCGATCCACGCCATGCGCGATGAAGGACTGCCCGTGTGGGCGACGATCGATGCGGGTCCCAATGTCAAGGTGCTCACTGAGGGTGCCCGGGCTGAGGAGATCGCCGCCGCGCTGCGCGACCGTCTGCCCGGCACCACCGTCTCGGTGAGGTATCCCGGCGGCGGGGTGCGTATCGAGGAAGACTCATGA","MELSDAHQRGGRVTAVPPGAAAGSSPAAAPTATASANTNIALIKYWGKVDEALAIPATSSLSLTLAGTRTTTTVSFDGGDGAADSVTINGVSPSAVELGRVTRFLDLVRSRSGVATPATVISRASVPLAAGLASSAAGFAALAAAASRAAGMNLDDRALSRLARRGSGSATRSVFGGLVLWNAGHDDASSYAEPVACEMDLAMVVVVLSQRYKPISSTRAMRATMSSSPLFPAWVEASWRDLQVALEAVRAGDLARLGEIVEGNALGMHATMIAARPGIVYWLPQTVAALHAIHAMRDEGLPVWATIDAGPNVKVLTEGARAEEIAAALRDRLPGTTVSVRYPGGGVRIEEDS$","Diphosphomevalonate decarboxylase","Membrane, Cytoplasm","diphosphomevalonate decarboxylase","mevalonate diphosphate decarboxylase ","diphosphomevalonate decarboxylase","","Tsay Y.H., Robinson G.W. Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase. Mol. Cell. Biol. 1991. 11(2):620-631. PMID: 1846667Lee M., Leustek T. Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene. Arch. Biochem. Biophys. 1999. 372(1):135-142. PMID: 10562426","","","

InterPro
IPR005935
Family

Diphosphomevalonate decarboxylase
PIRSF015950	$\"[30-353]T$	Diphosphomevalonate decarboxylase
PTHR10977	$\"[110-334]T$	DIPHOSPHOMEVALONATE DECARBOXYLASE
TIGR01240	$\"[32-334]T$	mevDPdecarb: diphosphomevalonate decarboxyl

InterPro
IPR006204
Domain

GHMP kinase
PF00288	$\"[119-177]T$	GHMP_kinases_N

InterPro
IPR013750
Domain

GHMP kinase, C-terminal
PF08544	$\"[245-335]T$	GHMP_kinases_C

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[29-210]T$	no description

","BeTs to 5 clades of COG3407COG name: Mevalonate pyrophosphate decarboxylaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG3407 is -o-p--y----l------------t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 248-325 are similar to a (DECARBOXYLASE MEVALONATE DIPHOSPHATE DIPHOSPHOMEVALONATE LYASE PYROPHOSPHATE BIOSYNTHESIS STRAIN CHROMOSOME STEROL) protein domain (PD011623) which is seen in Q9KWG4_STRC1.","","-41% similar to PDB:2GS8 Structure of mevalonate pyrophosphate decarboxylase from Streptococcus pyogenes (E_value = 4.7E_22);","Residues 119 to 177 (E_value = 8.8e-11) place ANA_1159 in the GHMP_kinases_N family which is described as GHMP kinases N terminal domain.Residues 245 to 335 (E_value = 4.3e-09) place ANA_1159 in the GHMP_kinases_C family which is described as GHMP kinases C terminal.","","decarboxylase (mvaD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1160","1239834","1240973","1140","5.91","-4.68","39455","ATGACCCCTCACGCTGACGGCGTGGTCTCCAGGGCGCCGGGCAAGCTCTACATCGCCGGTGAGTACGCCGTCGTCGAGCCCGGCCACCGAGCGGTCCTGGTGGCGGTCAACCGATTCATCACCGTACGCATCACGCCCTGCTCCCCCACCGGCGGGTACGCGGGCACGATCAGCTCGCGGCTCTACGACACCGGCTCCAGGCCCTGGCGTCACCGCCCGCAGGACGGCCTGGCTGAGGCTGTCGGGGGTGATGACGACTACGTGATCTCGGCGATCCGCGTCGTCGAGGCGCTGGTGGCCGAGGGTGGTGGCCGGCTGGGGTCCTTCAACCTGGGCATCTCCAGCGAGCTGGACGAGGCGGACGGGCGCAAGCTGGGCCTGGGATCCTCCGCGGCGGTGACCGTGGCGACGGTGCGCGCCGTCGCGGGCTTCTACGGCCTGAGTCTGGACGACTCGCGTGTCTACAAGCTGGCGATGCTGGCCAGTGACGCGGTCCAGCCGATCGGCTCGGGGGGCGACATCGCGGCCAGCGCCGTGACCGGCTGGGTGGACTACGCCTCACCCGACCGCGTGTGGCTGCACCGGGCCAGGCAACGGGCGCAGGCCCGTGGCGGCACAGGAGACCTGCTGGAATCCGACTGGCCCGGCCTGTGCCTGCGTCGACTGCCGGTTCCCTCCGTGAGGCTTCAGGTGGGATGGACCGGGGCTCCCGCCTCCACCCCGGCCCTGGTTGCCGGCGTCCAGGCGGGCTCCCGCGGGGTCGACGACGTCTACTCGTCCTTCCTGCGCGCCAGCCAGGACACCCTGGCCTCCCTGACCACGGCCATCGAGGACGACGACGCCGGCCAGGTCATGAGCGCAATCACGCGAAACCGGGTGCTTCTGGTGCAGCTCGGACGGATCAGCGGCCGTGTCATCGAGACTCCCGAGCTGACGCGGCTGGTCGAGATCGCCCGCGATCACGGGGCCGCTGCCAAGAGCTCGGGGGCCGGCGGCGGGGATTGCGGTATCGCCCTGTGCCCGCCGGACAAGGACATCGCCGCCATGAGCTCCGCCTGGAGGGCGGCCAGTATCCAGCCCCTGGACCTGGCGATCTACACCCACGACTCCCCCGTGCCCCCTATGGAGGTCACCTCATGA","MTPHADGVVSRAPGKLYIAGEYAVVEPGHRAVLVAVNRFITVRITPCSPTGGYAGTISSRLYDTGSRPWRHRPQDGLAEAVGGDDDYVISAIRVVEALVAEGGGRLGSFNLGISSELDEADGRKLGLGSSAAVTVATVRAVAGFYGLSLDDSRVYKLAMLASDAVQPIGSGGDIAASAVTGWVDYASPDRVWLHRARQRAQARGGTGDLLESDWPGLCLRRLPVPSVRLQVGWTGAPASTPALVAGVQAGSRGVDDVYSSFLRASQDTLASLTTAIEDDDAGQVMSAITRNRVLLVQLGRISGRVIETPELTRLVEIARDHGAAAKSSGAGGGDCGIALCPPDKDIAAMSSAWRAASIQPLDLAIYTHDSPVPPMEVTS$","Phosphomevalonate kinase","Cytoplasm, Membrane","phosphomevalonate kinase","phosphomevalonate kinase ","phosphomevalonate kinase","","Tsay Y.H., Robinson G.W. Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase. Mol. Cell. Biol. 1991. 11(2):620-631. PMID: 1846667Romanowski M.J., Bonanno J.B., Burley S.K. Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily. Proteins 2002. 47(4):568-571. PMID: 12001237Chambliss K.L., Slaughter C.A., Schreiner R., Hoffmann G.F., Gibson K.M. Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence. J. Biol. Chem. 1996. 271(29):17330-17334. PMID: 8663599Houten S.M., Waterham H.R. Nonorthologous gene displacement of phosphomevalonate kinase. Mol. Genet. Metab. 2001. 72(3):273-276. PMID: 11243736Bork P., Sander C., Valencia A. Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci. 1993. 2(1):31-40. PMID: 8382990Zhou T., Daugherty M., Grishin N.V., Osterman A.L., Zhang H. Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily. Structure 2000. 8(12):1247-1257. PMID: 11188689Thoden J.B., Holden H.M. Molecular structure of galactokinase. J. Biol. Chem. 2003. 278(35):33305-33311. PMID: 12796487Wada T., Kuzuyama T., Satoh S., Kuramitsu S., Yokoyama S., Unzai S., Tame J.R., Park S.Y. Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis. J. Biol. Chem. 2003. 278(32):30022-30027. PMID: 12771135","","","

InterPro
IPR005917
Family

Gram positive phosphomevalonate kinase
TIGR01220	$\"[8-369]T$	Pmev_kin_Gr_pos: phosphomevalonate kinase

InterPro
IPR006204
Domain

GHMP kinase
PF00288	$\"[110-181]T$	GHMP_kinases_N

InterPro
IPR006205
Family

Mevalonate kinase
PTHR10457:SF4	$\"[234-352]T$	MEVALONATE KINASE

InterPro
IPR006206
Family

Mevalonate and galactokinase
PR00959	$\"[12-36]T$ $\"[119-141]T$ $\"[324-341]T$	MEVGALKINASE

InterPro
IPR012197
Family

Mevalonate kinase/phosphomevalonate kinase
PIRSF000546	$\"[7-372]T$	Mevalonate kinase/phosphomevalonate kinase

InterPro
IPR013750
Domain

GHMP kinase, C-terminal
PF08544	$\"[272-356]T$	GHMP_kinases_C

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[3-194]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.890	$\"[273-372]T$	no description
PTHR10457	$\"[234-352]T$	MEVALONATE KINASE/GALACTOKINASE

","BeTs to 5 clades of COG1577COG name: Mevalonate kinaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1577 is aom-kzy----l------------t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","Residues 11-51 are 87% similar to a (KINASE TRANSFERASE ATP-BINDING MEVALONATE PHOSPHOMEVALONATE MK MAGNESIUM BIOSYNTHESIS KINASE STRAIN) protein domain (PD243513) which is seen in Q9KWF7_KITGR.Residues 87-185 are 63% similar to a (KINASE TRANSFERASE ATP-BINDING BIOSYNTHESIS 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL CMK ISOPRENE 4-CYTIDINE-5_apos;-DIPHOSPHO-2-C-METHYL-D-ERYTHRITOL GALACTOSE HOMOSERINE) protein domain (PD008614) which is seen in Q9FD77_STAHA.Residues 87-193 are 67% similar to a (KINASE PHOSPHOMEVALONATE TRANSFERASE ATP-BINDING) protein domain (PD819544) which is seen in Q9KWG3_STRC1.Residues 208-368 are 53% similar to a (KINASE TRANSFERASE ATP-BINDING PHOSPHOMEVALONATE LIN0012 MEVALONATE LMO0012) protein domain (PD263891) which is seen in Q9FD67_ENTFA.","","-40% similar to PDB:1K47 Crystal Structure of the Streptococcus pneumoniae Phosphomevalonate Kinase (PMK) (E_value = 2.0E_18);","Residues 110 to 181 (E_value = 1.1e-10) place ANA_1160 in the GHMP_kinases_N family which is described as GHMP kinases N terminal domain.Residues 272 to 356 (E_value = 1.8e-09) place ANA_1160 in the GHMP_kinases_C family which is described as GHMP kinases C terminal.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1161","1240970","1242058","1089","5.63","-10.95","38319","ATGAGCCACGAGTCCACCGACTCACAGCGGGCCTCCCGCAAGGACGAGCACCTGGAGCTGGCGGTGCACCTGCACCGCCAGGACCGTGCGAACGCCTTCGACGACGTCTCCTTCATCCACCACAGCCTGCCGGGCGTCAGCGCTGAGCAGGTCGATATCGGCACCACCGTGCTGGGCTCCCGCTGGGAGGCCCCGTTCTACATCAACGCCATGACCGGCGGGACGCAGGCGACGGCGGCCATCAACGCCGACCTGGCCGAGGCGGCCGCTGAGGCAGGAGTCGCGATCGCCTGCGGTTCCCAGCACGTGGCCCTGCACGACCCCGAGCGGGCAGATGGCTTCCACGTCATCCGCCGTCGGGCCCCGGGCGCCTTCGTGCTGGCCAATGTTGGGCCGACGGTCAGCCCGCAGGAGGCGGCGCGGGCCGTGGAGATGCTTGAGGCCGATGCCTTGCAGATCCACCTCAACGCGGCCCAGGAGCTGGTCATGCCCGAGGGCGACCGCGATTTCAGCGGCTGGGAGGAGGCGGTCGCCACCATTGTCACGGCCGTGCCCGTCCCGGTGGTGGTCAAGGAGGTGGGCTTCGGGCTCTCACGCCGGAGCATCGAATCCCTGGCGCGTACCGGTGTCGCGGCCGTCGACGTGGCCGGAGCGGGGGGCACGGACTTCATCGCCATTGAGAACGAGCGCCGCCCGCAGCGCGACCTGTCCTACCTGGTCGGCTGGGGCCAGTCGACGGCGCTGTGCCTGCTGGAGTCGCTGAGCGGATCGGAGCCGGTCAGCCTGCCGGTACTGGCCTCCGGCGGCGTGCGCAACCCGCTCGACGTCGTGCGGTCACTGGCCCTGGGGGCCTGCGCCGTCGGGGCCTCCGGGCATGTGCTGCGCACCCTGGTCAAGGAGGGCCCCGAGGCCCTGCGCCGCGAGCTGAGCACCTGGGGCGACCACGTGCGCACGCTCATGACCCTGCTGGGAGCGGCCGATGTCGCCCAGCTGCGCCGTACCGATGTGGTCGTGACCGGACGCACCGCCGAACAGGCGCGTCTGCTCGGCGTCGACCTGACCCGTCTGGCGCACCGCAGCGATACCTAA","MSHESTDSQRASRKDEHLELAVHLHRQDRANAFDDVSFIHHSLPGVSAEQVDIGTTVLGSRWEAPFYINAMTGGTQATAAINADLAEAAAEAGVAIACGSQHVALHDPERADGFHVIRRRAPGAFVLANVGPTVSPQEAARAVEMLEADALQIHLNAAQELVMPEGDRDFSGWEEAVATIVTAVPVPVVVKEVGFGLSRRSIESLARTGVAAVDVAGAGGTDFIAIENERRPQRDLSYLVGWGQSTALCLLESLSGSEPVSLPVLASGGVRNPLDVVRSLALGACAVGASGHVLRTLVKEGPEALRRELSTWGDHVRTLMTLLGAADVAQLRRTDVVVTGRTAEQARLLGVDLTRLAHRSDT$","Isopentenyl-diphosphate delta-isomerase (IPPisomerase)","Cytoplasm","Isopentenyl-diphosphate delta-isomerase (IPPisomerase)(Isopentenyl pyrophosphate isomerase)","isopentenyl-diphosphate delta-isomerase ","isopentenyl-diphosphate delta-isomerase, type 2","","Yamashita S., Hemmi H., Ikeda Y., Nakayama T., Nishino T. Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae. Eur. J. Biochem. 2004. 271(6):1087-1093. PMID: 15009187Steinbacher S., Kaiser J., Gerhardt S., Eisenreich W., Huber R., Bacher A., Rohdich F. Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis. J. Mol. Biol. 2003. 329(5):973-982. PMID: 12798687","","","

InterPro
IPR000262
Domain

FMN-dependent alpha-hydroxy acid dehydrogenase
PF01070	$\"[25-339]T$	FMN_dh

InterPro
IPR011179
Family

Isopentenyl-diphosphate delta-isomerase, FMN-dependent
PIRSF003314	$\"[10-349]T$	Isopentenyl-diphosphate delta-isomerase, FMN-dependent
PTHR10578:SF3	$\"[15-361]T$	ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE
TIGR02151	$\"[12-340]T$	IPP_isom_2: isopentenyl-diphosphate delta-i

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[29-359]T$	no description

noIPR
unintegrated

unintegrated
PTHR10578	$\"[15-361]T$	(S)-2-HYDROXY-ACID OXIDASE-RELATED

","BeTs to 18 clades of COG1304COG name: L-lactate dehydrogenase (FMN-dependent) and related alpha-hydroxy acid dehydrogenasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1304 is aompkzy--drlbcefgh-n-jx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB000262 (FMN-dependent alpha-hydroxy acid dehydrogenase) with a combined E-value of 5.2e-12. IPB000262B 55-106 IPB000262E 259-312***** IPB001093 (IMP dehydrogenase/GMP reductase) with a combined E-value of 5.6e-06. IPB001093D 263-302","Residues 40-246 are similar to a (ISOMERASE ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE ISOPENTENYL BIOSYNTHESIS IPP PYROPHOSPHATE FLAVOPROTEIN FMN ISOPRENE) protein domain (PD007378) which is seen in IDI2_KITGR.Residues 250-359 are 54% similar to a (ISOPENTENYL DELTA DIPHOSPHATE ISOMERASE ISOMERASE) protein domain (PD959847) which is seen in Q837E2_ENTFA.Residues 257-336 are 58% similar to a (ISOMERASE BIOSYNTHESIS ISOPENTENYL IPP PYROPHOSPHATE ISOPRENE FLAVOPROTEIN NADP DELTA-ISOMERASE ISOPENTENYL-DIPHOSPHATE) protein domain (PD959846) which is seen in IDI2_LACPL.","","-50% similar to PDB:1P0K IPP:DMAPP isomerase type II apo structure (E_value = 9.3E_50);-50% similar to PDB:1P0N IPP:DMAPP isomerase type II, FMN complex (E_value = 9.3E_50);-41% similar to PDB:1VCF Crystal Structure of IPP isomerase at I422 (E_value = 1.0E_19);-41% similar to PDB:1VCG Crystal Structure of IPP isomerase at P43212 (E_value = 1.0E_19);","Residues 25 to 339 (E_value = 0.00016) place ANA_1161 in the FMN_dh family which is described as FMN-dependent dehydrogenase.","","delta-isomerase (IPP isomerase)(Isopentenyl pyrophosphate isomerase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1162","1243584","1242229","1356","9.94","13.07","47308","ATGATGGTGGCCGCCATTCTGGCCGCCGTGGTGCTGTACACGTTCATCGGGTTCATTCCCGGCACGGATGAGACCGGGGTGCTCGCGCCCGTCACCCTGGCGATCATCCTGGCCGGAGCCCCGCCGCACGTGGTCCTCGCCTTCTTCATCTCCGCCGTGGTCACGCTCAACCTCATGAACGGCATCCCAACGGCGCTGGTGGGCCTTCCCGGCGGGGTCATGTCCGCTCCGCTCATGGATCATGCCATGGTGCTGCGCACCAAGGGCCTGGCCTCCGACACGATCCGGAAGATGGCGGTGGGCTCGGCCATCGGAACCCTCATCTCCATTCCCCTGAGCTTCCTCCTGGCCAGTCTGCTGCTTCCCATGGCCGACTGGATCAAGACCCATTCCGATATCGTCCTTGCGGCCGGAGCCGTGGTCCTGGCCCTGCTCGGAAAGAATCGCATCCTCTCACTGGTGTCGATTCTTCCCATGGCGCTGCTGTTTCAGGCGCTTCCGGCCCTCTACCGGGGCGCGGGCATCATCCCGGAGAAGGCCAGCGTCAACACCTCCTTTTTCCTCGGGATCACTGTGGGACCCATGCTCCTGACCCTCCTGGAGCTGCTCAACGCCAAGCGCCGGGAGGAGCTGCCGCACGGTAACCGCACCAAGGCCGAGCTGCTGCGCTCCGGTTTCGGCCGACAGGCGCTGCGGCCGGGTCGGCTCATCACCAGGTCCGAGGGATGGTGGAGTGCCGCTATGGCCGCCGCCTCCACCCCGCTGTTCATTCTCAGCCCGGTGGGCCTGACCTTCTTGCTGGGGGAGGCCTCCGTGGCCCGCCAGAACGAGGACCGGGTGCCCCGCGCACAGCGTGCGGTGACCGTTATGAGCGCCCTGGCCCACTCGACCTACCTCGCCGGCGTCATTATCCCGTTGGTGGCGCTCGGGGTCCCGATCTCCGGGGTGTCCGTCGGACCCGCCGGCCCGCTGTTCAATGCGGGCTCGGTCTACACCAAGCAGCACAACCTGCACCACCTGCTGGACTTGCCCGGGTTCATCATCACCGTGACCATTGGGGCTCTGATCGCGCTTGCGATCACCTACGTCATTGCGGTGCGCTGGTCCTCGCAGATCACCTACTTCGTCATGCGTCGGATCCCTCACGAGGCGGTACTGGCGCTGTTCGTCGCCTTCGTCATCCTGCTGGCCTACATCGACGCTGACCAGAAGGCGGGCCTGGCCAACGTCTTCGGGGTCCTGCTCGTAGGAGTCGTGTGCGGATCACTCAACCGCCTGGGAGTTGCCTACGGCGTCCAGTTCATGTCGCTTTACGCCGCCCCCGGCATCGTCAAGGCCCTGGCCGCTCTGGCCTGA","MMVAAILAAVVLYTFIGFIPGTDETGVLAPVTLAIILAGAPPHVVLAFFISAVVTLNLMNGIPTALVGLPGGVMSAPLMDHAMVLRTKGLASDTIRKMAVGSAIGTLISIPLSFLLASLLLPMADWIKTHSDIVLAAGAVVLALLGKNRILSLVSILPMALLFQALPALYRGAGIIPEKASVNTSFFLGITVGPMLLTLLELLNAKRREELPHGNRTKAELLRSGFGRQALRPGRLITRSEGWWSAAMAAASTPLFILSPVGLTFLLGEASVARQNEDRVPRAQRAVTVMSALAHSTYLAGVIIPLVALGVPISGVSVGPAGPLFNAGSVYTKQHNLHHLLDLPGFIITVTIGALIALAITYVIAVRWSSQITYFVMRRIPHEAVLALFVAFVILLAYIDADQKAGLANVFGVLLVGVVCGSLNRLGVAYGVQFMSLYAAPGIVKALAALA$","Tripartite Tricarboxylate Transporter (TTT) Family protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[32-52]?$ $\"[58-78]?$ $\"[99-121]?$ $\"[127-145]?$ $\"[150-170]?$ $\"[180-200]?$ $\"[298-318]?$ $\"[346-366]?$ $\"[381-399]?$ $\"[409-429]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 13-450 are 58% similar to a (OB2748) protein domain (PD851174) which is seen in Q8EMU2_OCEIH.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","Tue Aug 14 12:01:21 2007","","","","","Tue Aug 14 12:01:21 2007","","Tue Aug 14 12:01:21 2007","","Tue Aug 14 12:01:21 2007","Tue Aug 14 12:01:21 2007","","","","","yes","","" "ANA_1163","1243892","1243602","291","4.34","-7.18","10316","GTGCGCAGTACGGATGACGTCGACTCCGAGACCACGGAGCGTCAGAACAATATCGAGGTCTGGAACGATCTCGTCTCGCCCAGAGATTTGCTCATCTGTCTTCTGATTTCGGTGATGTGTATCGTTGCGGCGGTACTTTTATCCGCCTCTTTCGGGGGAAAGCCGCTGTTCTGGGGGCTGGGAGCCTCAACGATCGGATTTATCGCCTGCTGCTTCCTGGTGAGTCCCAAGCGCGAGGTCACCATTGTCGAGGAGCTGAGCATCGGCACGAGTGAGGGGGCGGACCAGTGA","VRSTDDVDSETTERQNNIEVWNDLVSPRDLLICLLISVMCIVAAVLLSASFGGKPLFWGLGASTIGFIACCFLVSPKREVTIVEELSIGTSEGADQ$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-44]?$	signal-peptide
tmhmm	$\"[31-51]?$ $\"[56-76]?$	transmembrane_regions

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[213-289]T$	Acetyltransf_1
PS51186	$\"[142-299]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[140-293]T$	no description
PTHR23091	$\"[237-293]T$	N-TERMINAL ACETYLTRANSFERASE
PTHR23091:SF1	$\"[237-293]T$	RIBOSOMAL-PROTEIN-ALANINE ACETYLTRANSFERASE

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 67-235 are 45% similar to a (TRANSFERASE FAMILY GNAT ACETYLTRANSFERASE MB2892C SCO5697 ACETYLTRANSFERASE) protein domain (PD359018) which is seen in Q73VS4_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 213 to 289 (E_value = 3.4e-08) place ANA_1164 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","GNAT family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1165","1246190","1245042","1149","5.49","-8.59","40316","ATGCGTGCCCAGGCCCCGGTCCTGGCGGCGCGCCGACCCACCCGCAAGATCCGGGTCGGCAGCCTTAACGTCGGTGGAGACGCCCCCATCACCGTGCAGTCGATGACCACCACGAAGACTCACGACATCGGCGCCACTCTGCAGCAGATCGCCGAGCTGACGGCCGCGGGCTGCGACATCGTCCGCGTGGCCTGCCCCACCGACAAGGACGCCGAGGCGCTGCCGATCATCGCCAAGCAGTCGCGCATCCCCGTCATCGCGGACATCCACTTCAACCCCAAGTACGTCTTCGCCGCCATCGAGGCCGGCTGCGGCGCGGTGCGCGTCAACCCCGGCAACATCCGCAAGTTCGACGACCAGGTCGCCGACATCTGCAAAGCCGCCTCCGACGCCGGCGTCTCCCTGCGCATCGGCGTCAACGCTGGTTCCCTGGACAAGCGCCTGCTCAAGAAGTACGGGAAGGCCACCCCTGAGGCGCTCGTGGAGTCCGCCACCTGGGAGGCCGGACTGTTCGAGGAGAACGACTTCCACGACTTCAAGATCTCCGTCAAGCACCACGACGTCGTCACCATGGTGCAGGCCTACCGGCTGCTGTCGGAGGCCGGCCAGTGGCCCCTCCACCTGGGCGTGACCGAGGCCGGCCCCGCCTTCCAGGGCACCATCAAGTCCTGTGCCGCCTTCGGCACCCTGCTCGCTGAGGGCATCGGCGACACCATCCGGGTCTCGCTGTCCGCTCCTCCGGTTGAGGAGGTCAAGGTGGGCACCAAGCTCCTGGAGTTCATGGGGCTGCGCGAGCGCCAGCTCGAGATCGTCTCCTGTCCCTCCTGCGGGCGGGCTCAGGTGGATGTGTGGACCCTGGCGGAGGAGGTCGAGGCCGGGCTCAAGAACATCACCGCTCCGCTGCGCGTGGCCGTCATGGGCTGTGTCGTCAACGGCCCCGGCGAGGCCCGCGAGGCGGACCTGGGCTGCGCCTCGGGCAACGGCAAGGGCCAGATCTTCGTGCGCGGCCAGGTCGTGGAGACCGTCCCGGAGGACCAGGTCGTCGAGACCCTCCTCAAACACGCCGAGGCCATGGCCGCCGAGATGGCCGAGGAGCTCGGGGAGGAGGCCCTGGCCGGCACCAGCCCCATGGTCTCCGCAGCCGGCTGA","MRAQAPVLAARRPTRKIRVGSLNVGGDAPITVQSMTTTKTHDIGATLQQIAELTAAGCDIVRVACPTDKDAEALPIIAKQSRIPVIADIHFNPKYVFAAIEAGCGAVRVNPGNIRKFDDQVADICKAASDAGVSLRIGVNAGSLDKRLLKKYGKATPEALVESATWEAGLFEENDFHDFKISVKHHDVVTMVQAYRLLSEAGQWPLHLGVTEAGPAFQGTIKSCAAFGTLLAEGIGDTIRVSLSAPPVEEVKVGTKLLEFMGLRERQLEIVSCPSCGRAQVDVWTLAEEVEAGLKNITAPLRVAVMGCVVNGPGEAREADLGCASGNGKGQIFVRGQVVETVPEDQVVETLLKHAEAMAAEMAEELGEEALAGTSPMVSAAG$","1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase","Cytoplasm","1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphatesynthase","1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase ","1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase","","","","","

InterPro
IPR004588
Family

IspG protein
PF04551	$\"[11-363]T$	GcpE
TIGR00612	$\"[11-356]T$	ispG_gcpE: 4-hydroxy-3-methylbut-2-en-1-yl

","BeTs to 16 clades of COG0821COG name: Essential bacterial protein, involved in density-dependent regulation of peptidoglycan biosynthesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0821 is -------qvdr-bcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 15-353 are similar to a (SYNTHASE 4-DIPHOSPHATE 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE IRON 4FE-4S IRON-SULFUR ISOPRENE BIOSYNTHESIS METAL-BINDING) protein domain (PD008743) which is seen in ISPG_TROWT.","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 363 (E_value = 1.7e-222) place ANA_1165 in the GcpE family which is described as GcpE protein.","","4-diphosphate synthase (ispG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1168","1247660","1246326","1335","9.25","8.32","45797","GTGAGCACCACCCTGGCCTACATCCTGGGCATCGTCATCCTCGTCATCGGGATCGGTGTCTCAGTGGCCCTTCACGAGCTCGGGCACATGATCCCCGCCAAGAAGTTCGGTGTGAAGGTACCCGAGTACTTCATCGGCTTCGGACCCAAGATCTGGTCGTTCAAGCGCGGGGAGACCGAGTACGGCGTCAAGGCCATCTGGCTGGGCGGCTACGTCAAGCTCGTCGGCATGCTGCCGCCGGCCAGGCCCGGCAGACCGGACCGCCGACGCAAGGACGGAAGCCTGGGCATGGTGGGCGAGGCTCGCGCCGAGGCCCTGGAGGAGATCCAGCCCGGCGAGGAGCACCGGGCCTTCTACCACCTCAGCGTCCCCAAGAAGCTCATCGTCATGGCCGGGGGAATCCTCACCAACCTGGTCCTGGGGATCGTGCTGCTGGCCGTGGCCGTCGGCGTGGTCGGCATCCCCGGACGCACGACGACGCTGTCGACCGTGGCGCCCTGCGTGTCGTCCGACATCGACGCGGGCGCCCCCTGCCAGGACTCCGACCCGGTCGGCCCCGCCAGCGCCGCCGGCATACGGGTCGGCGACAGGATCGTCTCCTGGGGCGGGGTGAAGGTCTCCACCTGGGAGGAGCTGCAGGCCCGGATCGCCGCCCAAGGCACCAGCCCCACCGAGGTCGTCATCGAGCGCGACGGAGCCGAGCGCACCGTGAGCGTCACCGCGGTCGAGGCCCAGCGCACCGTTCGCGACGCGCAGGGCGCCCCGGTCAAGGACGCCTCCGGGGCCGTGCGCACCCAGGCCCGCCCCTATGTCGGCATCTCCCCGTCGCTGGGAACCATTCCCCTGAGCCCCACCAAGATCCCCGGCATCATCGGGCAGGCCATCGGAGGCACGGTCAAGGCCATCGCCACCCTTCCGGTGGGCCTCTATCACGCCGTTCAGGCGGCGCTGGGCGTGGAGCAGCGCAGCGCCGACAGCGGCGTCGTGGGCCTGGTAGGCATGGGGCGCATGGCCGGAAACGCCACCAGCGGCGGTGTGGCCGGAGGCGGGGCGGTCCCCCTGTCGATGCGAGTGAGCACCATGCTCATGCTGCTGGGCAGCCTCAACCTGGCACTGTTTGCCTTCAACCTGGTGCCCCTGCTGCCACTGGACGGCGGGCACGTGCTCGGAGCCTGCTGGGAGGGCATCCGGCGCTCGATCGCCAAGGTGCAGGGTAAGCCCGATCCGGGCCCGGTGGACACGGCCAGGATGCTGCCGGTCGGTCAGGTCGTCTTCGGTCTGCTCATCGCCATGGCCCTGGTCCTGGTGTGGGTGGACATCGCCGCGCCGCTGTGA","VSTTLAYILGIVILVIGIGVSVALHELGHMIPAKKFGVKVPEYFIGFGPKIWSFKRGETEYGVKAIWLGGYVKLVGMLPPARPGRPDRRRKDGSLGMVGEARAEALEEIQPGEEHRAFYHLSVPKKLIVMAGGILTNLVLGIVLLAVAVGVVGIPGRTTTLSTVAPCVSSDIDAGAPCQDSDPVGPASAAGIRVGDRIVSWGGVKVSTWEELQARIAAQGTSPTEVVIERDGAERTVSVTAVEAQRTVRDAQGAPVKDASGAVRTQARPYVGISPSLGTIPLSPTKIPGIIGQAIGGTVKAIATLPVGLYHAVQAALGVEQRSADSGVVGLVGMGRMAGNATSGGVAGGGAVPLSMRVSTMLMLLGSLNLALFAFNLVPLLPLDGGHVLGACWEGIRRSIAKVQGKPDPGPVDTARMLPVGQVVFGLLIAMALVLVWVDIAAPL$","Membrane-associated Zn-dependent protease","Membrane, Cytoplasm, Extracellular","membrane-associated Zn-dependent protease-likeprotein","putative metalloprotease ","peptidase M50","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 1989. 242(2):211-214. PMID: 2914602Murphy G.J., Murphy G., Reynolds J.J. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett. 1991. 289(1):4-7. PMID: 1894005","","","

InterPro
IPR001478
Domain

PDZ/DHR/GLGF
PF00595	$\"[185-229]T$	PDZ
SM00228	$\"[138-232]T$	PDZ

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[22-31]?$	ZINC_PROTEASE

InterPro
IPR008915
Family

Peptidase M50
PF02163	$\"[13-439]T$	Peptidase_M50

noIPR
unintegrated

unintegrated
G3DSA:2.30.42.10	$\"[147-245]T$	no description
PTHR22939	$\"[170-240]T$	SERINE PROTEASE FAMILY S1C HTRA-RELATED
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[134-154]?$ $\"[361-381]?$ $\"[418-438]?$	transmembrane_regions

","BeTs to 17 clades of COG0750COG name: Predicted membrane-associated Zn-dependent proteases 1Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0750 is aompkz-qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB008915 (Peptidase M50) with a combined E-value of 4.7e-52. IPB008915A 20-49 IPB008915B 65-74 IPB008915C 124-145 IPB008915D 187-211 IPB008915E 366-394 IPB008915F 424-440","Residues 52-137 are similar to a (METALLOPROTEASE ZINC PROTEASE 3.4.24.- HYDROLASE TRANSMEMBRANE MEMBRANE INNER MEMBRANE-ASSOCIATED ZN-DEPENDENT) protein domain (PD004820) which is seen in Q82K42_STRAW.Residues 390-444 are 67% similar to a (METALLOPROTEASE ZINC PROTEASE TRANSMEMBRANE 3.4.24.- HYDROLASE PREDICTED ZN-DEPENDENT MEMBRANE-ASSOCIATED MEMBRANE) protein domain (PD627656) which is seen in YKJ5_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 439 (E_value = 2.7e-49) place ANA_1168 in the Peptidase_M50 family which is described as Peptidase family M50.Residues 185 to 229 (E_value = 6.1e-07) place ANA_1168 in the PDZ family which is described as PDZ domain (Also known as DHR or GLGF).","","Zn-dependent protease-like protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1169","1248949","1247657","1293","5.52","-11.10","44269","ATGACCAGCCACGCAGCAGCGCCCTCCCACAACCCACAGCGACTGGTCCTCCTGGGATCCACCGGGTCGATCGGCACCCAGACGCTCGAGGTCCTCTCCCGCCTGGGGGAGCACGCCCCGCGAGTGGCCGCCCTGGCCGCCGGCGGATCGCGCCTGGAGCTCCTGGCCCGCCAGGCCATCACCTGGGAGGTTCCCGTCCTGGCCGTCACCGGCGGGGGAGAGGACCTCGCCGGCCGCCTGCGCCAGGCCCTGAGAGCCGCAGCCGCCCAGGCCGGCCGCCCCGACCCGGTCACCACCATCCTCACCGGCCCCGACGCCGCCACCACGGCCGTCCAGGCCGCCGAGCTCGGGGCAGGCGACACGGTCGTCAACGGCATCACCGGCTCGGTGGGACTGCTGCCCACACTGGCCGCCCTGGCCAGCGGAGCCCGCCTGGCCCTGGCCAACAAGGAGTCCCTCGTCGTCGGGGGCGCCCTGGTCCGCCAGGCGCTGACCCGACCCGGCCAGATCGTCCCCGTGGACTCCGAGCACTCCGCCATCGCCCAGGCCCTGGCCAGCGGGCGCCACGAGAAGGGACTGACCAGCCCCGTCCTCAGCGGACGCAGCGAGGTCAGGCGGCTGGTCCTGACCGCCTCCGGCGGCCCCTTCCGCGGGCGCAGCCGCGCCGAGCTCACCGGGATCAGTGCCGCCGCCGCCCTCAAGCACCCCACCTGGGACATGGGGCCGGTGGTGACCATCAACTCCTCGACCCTCATCAACAAGGGGCTCGAGCTCATCGAGGCCCACCTCCTGTTCGACGTGGCACCCGAGCGGATCGACGTCGTCGTCCACCCCCAGTCCGTCATCCACTCCATGGTGGAGTTCACCGACGGCGCCACCATCGCCCAGGCCTCCCCGCCCGACATGCGCCTGCCCATCGCCCTGGGCCTGACCTGGCCCGAGCGCCCCGACCTGTCGGGCCTGGTGGCTCCCAACGACTGGCGCGAACCGGTCAGCTGGACCTTCGAGCCGCTGGATGTCGCCGCCTTCCCCGCCGTCGACCTGGCCCGCAGCGCCGTGGCGGCCTCGGACACCCACCCGGCCGTGCTCAACGCGGCCAACGAGCAGGCCGTCGCCGCCTTCCTCACCGGTGGCCTGGAGTGGCTCGACATCGTCGAGATCGATGCGGCCGTCGTCGGGGAGCACGAGGGGCTGTCCGCTCCGGGCCTCGACGACGTCCTGGCCGTGGAGACCTGGGCACGCGCCCGCGCCGACGAGCTCATCGCGGCACGAAACGGAGGAACACACTCGTGA","MTSHAAAPSHNPQRLVLLGSTGSIGTQTLEVLSRLGEHAPRVAALAAGGSRLELLARQAITWEVPVLAVTGGGEDLAGRLRQALRAAAAQAGRPDPVTTILTGPDAATTAVQAAELGAGDTVVNGITGSVGLLPTLAALASGARLALANKESLVVGGALVRQALTRPGQIVPVDSEHSAIAQALASGRHEKGLTSPVLSGRSEVRRLVLTASGGPFRGRSRAELTGISAAAALKHPTWDMGPVVTINSSTLINKGLELIEAHLLFDVAPERIDVVVHPQSVIHSMVEFTDGATIAQASPPDMRLPIALGLTWPERPDLSGLVAPNDWREPVSWTFEPLDVAAFPAVDLARSAVAASDTHPAVLNAANEQAVAAFLTGGLEWLDIVEIDAAVVGEHEGLSAPGLDDVLAVETWARARADELIAARNGGTHS$","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Cytoplasm, Membrane","1-deoxy-D-xylulose 5-phosphate reductoisomerase","1-deoxy-D-xylulose 5-phosphate reductoisomerase ","1-deoxy-D-xylulose 5-phosphate reductoisomerase","","Takahashi S., Kuzuyama T., Watanabe H., Seto H. A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(17):9879-9884. PMID: 9707569","","","

InterPro
IPR003821
Family

1-deoxy-D-xylulose 5-phosphate reductoisomerase
PIRSF006205	$\"[12-427]T$	1-deoxy-D-xylulose 5-phosphate reductoisomerase
TIGR00243	$\"[13-425]T$	Dxr: 1-deoxy-D-xylulose 5-phosphate reducto

InterPro
IPR013512
Domain

1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02670	$\"[15-157]T$	DXP_reductoisom

InterPro
IPR013644
Domain

1-deoxy-D-xylulose 5-phosphate reductoisomerase, C-terminal
PF08436	$\"[170-265]T$	DXP_redisom_C

","BeTs to 16 clades of COG0743COG name: 1-deoxy-D-xylulose 5-phosphate reductoisomeraseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0743 is -------qvdr-bcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB013512 (1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal) with a combined E-value of 1e-98. IPB013512A 17-31 IPB013512B 122-157 IPB013512C 170-184 IPB013512D 228-282 IPB013512E 343-384","Residues 13-69 are 75% similar to a (REDUCTOISOMERASE 1-DEOXY-D-XYLULOSE 5-PHOSPHATE OXIDOREDUCTASE DXP BIOSYNTHESIS 1-DEOXYXYLULOSE-5-PHOSPHATE ISOPRENE NADP ISOMERASE) protein domain (PD010039) which is seen in Q6A7K8_PROAC.Residues 121-261 are 80% similar to a (REDUCTOISOMERASE 1-DEOXY-D-XYLULOSE 5-PHOSPHATE OXIDOREDUCTASE DXP BIOSYNTHESIS 1-DEOXYXYLULOSE-5-PHOSPHATE ISOPRENE NADP ISOMERASE) protein domain (PD833444) which is seen in DXR_STRAW.Residues 265-296 are 87% similar to a (REDUCTOISOMERASE 1-DEOXY-D-XYLULOSE 5-PHOSPHATE OXIDOREDUCTASE DXP BIOSYNTHESIS 1-DEOXYXYLULOSE-5-PHOSPHATE ISOPRENE NADP ISOMERASE) protein domain (PDA092I6) which is seen in DXR_BIFLO.Residues 265-316 are 65% similar to a (REDUCTOISOMERASE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE OXIDOREDUCTASE DXP BIOSYNTHESIS 1-DEOXYXYLULOSE-5-PHOSPHATE ISOPRENE NADP) protein domain (PDA1B5R4) which is seen in DXR_TREPA.Residues 336-394 are 71% similar to a (REDUCTOISOMERASE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE OXIDOREDUCTASE DXP BIOSYNTHESIS 1-DEOXYXYLULOSE-5-PHOSPHATE ISOPRENE NADP ISOMERASE) protein domain (PD671218) which is seen in DXR_BIFLO.Residues 339-421 are 63% similar to a (REDUCTOISOMERASE 1-DEOXY-D-XYLULOSE 5-PHOSPHATE OXIDOREDUCTASE DXP BIOSYNTHESIS 1-DEOXYXYLULOSE-5-PHOSPHATE ISOPRENE NADP ISOMERASE) protein domain (PD580160) which is seen in Q74BW4_GEOSL.","","-58% similar to PDB:2C82 X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 5.8E_86);-59% similar to PDB:2JCV X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS, IN COMPLEX WITH FOSMIDOMYCIN AND NADPH (E_value = 1.0E_85);-59% similar to PDB:2JCZ X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS, IN COMPLEX WITH FOSMIDOMYCIN, MANGANESE AND NADPH (E_value = 1.0E_85);-59% similar to PDB:2JD1 X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS, IN COMPLEX WITH MANGANESE AND NADPH (E_value = 1.0E_85);-59% similar to PDB:2JD2 X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS, IN COMPLEX WITH MANGANESE (E_value = 1.0E_85);","Residues 15 to 157 (E_value = 8.2e-43) place ANA_1169 in the DXP_reductoisom family which is described as 1-deoxy-D-xylulose 5-phosphate reductoisomerase.Residues 170 to 265 (E_value = 7.8e-52) place ANA_1169 in the DXP_redisom_C family which is described as 1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal.","","5-phosphate reductoisomerase (dxr)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1170","1249536","1248991","546","5.31","-3.79","20305","ATGAGCGACATGTTCCCCAAGGCAGCGCTCCTGCGACCGGGCTACCGCCCCGAGCAGGTGGACCGCTACTTCGAGACGGCTCACGAGATCTACGACGCCGGTGAGCTCGACGAGATGGACTCCGAGGGCGTGCGCACCGTCGCCTTCGACGTCGTCCTGCGCGGCTACCAGCCCCAGGCCGTGGATGCCGCCCTCGACCGGCTCGAGGCCGCCTTCCTCCAGCGCCGTCGCGCGGCCTTCGTGGCCAAGAACGGCCGCCAGGCCTGGATGGACCAGGTCACCCAGCTCGCCACCACCCTCTACCCGCGTCTGCTGCGCCCGGCCGGCGAGCGCTTCGCCCCGGCCTCCGGACAGGGCTACGACAAGACCGACGTCGATGCCCTCATGGACCGTATCGCCGGCTACTTCGACTCCGACACCACCCTGACCTCCAGCGAGGTGCGCGGAGCGGTCTTCCGCCGCGCCCGGGGGAACAAGGCCTACGGGGAGCCCAGCGTCGACCGTTACCTGGCGCGCGTCGTCGAGGTCCTCCTGTCCGTCGAGTGA","MSDMFPKAALLRPGYRPEQVDRYFETAHEIYDAGELDEMDSEGVRTVAFDVVLRGYQPQAVDAALDRLEAAFLQRRRAAFVAKNGRQAWMDQVTQLATTLYPRLLRPAGERFAPASGQGYDKTDVDALMDRIAGYFDSDTTLTSSEVRGAVFRRARGNKAYGEPSVDRYLARVVEVLLSVE$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 75-181 are 52% similar to a () protein domain (PD715222) which is seen in Q83HZ3_TROW8.","","-44% similar to PDB:1TXV Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen (E_value = );-44% similar to PDB:1TY3 Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen (E_value = );-44% similar to PDB:1TY5 Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen (E_value = );-44% similar to PDB:1TY6 Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen (E_value = );-44% similar to PDB:1TY7 Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1171","1250795","1249533","1263","7.75","3.65","45586","GTGAGTCCATCACGAGCACAGCAGCGCCCCCGGCGCCCGCAGCCCGTCAGCATCACCGGGCGGCCACATGACGGCCGGGTCCAGGTCATGCCCACCGACCAGCCCCCGGAGGGCGCCACCAGCCCCGACGCCAAACCGCGCCTGTCCTTCGCGGTGCCCGCCGCGCGCGGCAAGGCCCCCCGCCACCTGGCCGACCTCGACCTGGCCGGGCGCAAGGCCGCCTGTAAGGACTCGGGCCTGCCCTCCTTCCGGGCCGACCAGCTCTCACGCCACTACTTCACGCACTTCACCCGCGACAGCGCGGACATGACCGACCTGCCCGCCGCCCAGCGCGAGCAGCTGTGCGCCGAGCTGCTGCCCGAGCTCATCACCCCAGTGCGCGCCCTGCGCGCCGACGGCGGGCGCACCATCAAGCACCTGTGGGAGCTGCACGACGGCGTACGCGTCGAGAGCGTCCTCATGCGCTACAAGGAGCGCACCACCCTGTGCGTCTCCTCCCAGGCCGGCTGCGGCATGGCCTGCCCCTTCTGCGCCACCGGCCAGATGGGCCTGACCCGCAACCTGTCCACCGGGGAGATCGTGGAGCAGGTGCGCCACGCCGCCCAGGCCTCGGCCGCCGGGGAGCTGACCGGGGGACCGGCCCGCCTGTCCAACGTGGTCTTCATGGGCATGGGCGAGCCGATGGTCAACTACAAGAACGTCGTCGGCGCCCTCCACCGGCTCATCGACCCGGCCCCGGAGGGCTTCGGCCTGTCGGCGCGCGGCATCACCGTCTCCACCGTGGGACTCGTCCCCCTCATCCGCCGGCTCGCCGGCGAGGGGCTGCCGGTGACACTGGCCGTCTCCCTGCACGCCCCCGACGACGAGCTGCGCGACGAGCTCATCCCGGTCAACTCCAAGTGGAAGGTCGGCGAGCTGCTCGACGCCGCCCACGACTACTTCCTGGCCACCGGCCGGCGCGTGTCCATCGAGTACGCGCTCATCAAGGACATGAACGACCACGCCTGGCGCGCCCAGCTGCTCGCTGACGAGCTCAACCGCAGGGACACCGGATGGGCCCATGTCAACCCCATCCCGCTCAACCCCACTCCGGGGTCCATCTGGACCTGCTCGGAGGTTGCGGTTCAGGATATGTTCGTCGACACGCTCCGGCGTGCCGGAATTACCACGACAGTGCGAGACACTCGTGGCAGCGACATCGACGGTGCCTGCGGTCAGCTCGCGACCGAGGTACTCAACCAGGAGAGGGCCAAGACGACATGA","VSPSRAQQRPRRPQPVSITGRPHDGRVQVMPTDQPPEGATSPDAKPRLSFAVPAARGKAPRHLADLDLAGRKAACKDSGLPSFRADQLSRHYFTHFTRDSADMTDLPAAQREQLCAELLPELITPVRALRADGGRTIKHLWELHDGVRVESVLMRYKERTTLCVSSQAGCGMACPFCATGQMGLTRNLSTGEIVEQVRHAAQASAAGELTGGPARLSNVVFMGMGEPMVNYKNVVGALHRLIDPAPEGFGLSARGITVSTVGLVPLIRRLAGEGLPVTLAVSLHAPDDELRDELIPVNSKWKVGELLDAAHDYFLATGRRVSIEYALIKDMNDHAWRAQLLADELNRRDTGWAHVNPIPLNPTPGSIWTCSEVAVQDMFVDTLRRAGITTTVRDTRGSDIDGACGQLATEVLNQERAKTT$","Radical SAM enzyme, Cfr family","Cytoplasm","radical SAM enzyme, Cfr family","hypothetical protein","radical SAM enzyme, Cfr family","","Sofia H.J., Chen G., Hetzler B.G., Reyes-spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 2001. 29(5):1097-1106. PMID: 11222759","","","

InterPro
IPR004383
Family

Conserved hypothetical protein 48
TIGR00048	$\"[56-419]T$	TIGR00048: radical SAM enzyme, Cfr family

InterPro
IPR006638
Domain

Elongator protein 3/MiaB/NifB
SM00729	$\"[160-385]T$	Elp3

InterPro
IPR007197
Domain

Radical SAM
PF04055	$\"[164-342]T$	Radical_SAM

","BeTs to 16 clades of COG0820COG name: Predicted Fe-S-cluster redox enzymeFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0820 is -------qvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 46-138 are 59% similar to a (ENZYME RV2880C/RV2879C/MT2947/MB2904C FE-S-CLUSTER UPF0063 PREDICTED SCO5645 REDOX) protein domain (PD353364) which is seen in YS80_MYCTU.Residues 132-263 are 70% similar to a (UPF0063 ENZYME RESISTANCE YFGB FE-S-CLUSTER FAMILY REDOX FLORFENICOL PREDICTED SAM) protein domain (PD336815) which is seen in Q6A7K4_PROAC.Residues 254-359 are 65% similar to a (BIOSYNTHESIS COFACTOR MOLYBDENUM A IRON-SULFUR METAL-BINDING IRON 3FE-4S PQQ SYNTHESIS) protein domain (PD000790) which is seen in Q72HC1_THET2.Residues 267-358 are 78% similar to a (UPF0063 ENZYME YFGB FE-S-CLUSTER REDOX RESISTANCE FAMILY PREDICTED FLORFENICOL SAM) protein domain (PD006794) which is seen in Q8G481_BIFLO.Residues 359-408 are 76% similar to a (UPF0063 ENZYME RESISTANCE YFGB FE-S-CLUSTER FAMILY REDOX FLORFENICOL PREDICTED SAM) protein domain (PD007453) which is seen in Q6A7K4_PROAC.","","-51% similar to PDB:2DVY Crystal structure of restriction endonucleases PabI (E_value = );-44% similar to PDB:1W61 PROLINE RACEMASE IN COMPLEX WITH 2 MOLECULES OF PYRROLE-2-CARBOXYLIC ACID (HOLO FORM) (E_value = );-44% similar to PDB:1W62 PROLINE RACEMASE IN COMPLEX WITH ONE MOLECULE OF PYRROLE-2-CARBOXYLIC ACID (HEMI FORM) (E_value = );-45% similar to PDB:2AIP Crystal structure of native protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix (E_value = );-45% similar to PDB:2AIQ Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix (E_value = );","Residues 164 to 342 (E_value = 2.2e-10) place ANA_1171 in the Radical_SAM family which is described as Radical SAM superfamily.","","SAM enzyme, Cfr family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1172","1251805","1250867","939","7.80","2.24","32248","GTGAGCCCCGTGTCGCCTCTGCTGAACCCGCGCCCCACGCGCAACCACGACCCCCTGCCCGCCACCGGGCGGGCGGGACGCAACCTGCCCGCCGCCATCGGGGTGGCGGTCGTGCTCATCGCCGTGGTCCTGGGGTCCCTGGCCTTCTACAAGGTCATCTTCGTGGGCGTCGTCGTCCTGGCCGTGTGCGGGGCGCTGTGGGAACTGGCGGCGGCCTTCGCCCGCAAGCGCATCCGCCTGCCCCTGGCGCCGCTGTGGCTGGGGACCCTGGGAATCTCCGTGTGCGCCTGGGAGGTGGGAGCGGAGGCGGCCTTCGGGGCCTACGTCGCCACCGTCGGCGCCTGCGTCCTGTGGAGCTTCATGGACCAGGCCGAGGCGGAGGTCGGCACCGTCCTGGAGCAGGCCGGCCACGACATCCCCCGCACCGAGGCCCACGACGAGGTCCGCCGCTCGCGCTCCAGCGCCGCGGCCGCCTCGGTCTTTGCCGCCACCTACCTGCCCTTCCTGGCAGGCTTCGCCGTCCTGCTCCTGGTACAGGAGCACGGAGTGGGAAAAGTCATGATGCTCATCGCCCTGGCGGCCGCCAACGACACCGGCGGGTGGATGGCCGGCATCACCTTCGGCCGTCACCCCCTGGCGCCCTCGGTCTCACCCAAGAAGTCCTGGGAGGGGCTCATGGGCTCCCTCATCGCAGCTGTCGCCACCGGTGCCGGCTGCGTCTGGGCCATCGGCGGCCCCTGGTGGGCCGGGGCCGCACTGGGCGCCTGCACCGTGATCGTCTCCACCCTGGGCGACCTGGGGGAGTCCCTGCTCAAGCGGGACCTGGGACTCAAGGACATGGGCACGCTCCTGCCCGGGCACGGCGGAATCATGGACCGGCTCGACTCGATCCTCGTGGCCGCTCCACTTGTCTACGCCTTCACCCTCCTGGTGAAATAG","VSPVSPLLNPRPTRNHDPLPATGRAGRNLPAAIGVAVVLIAVVLGSLAFYKVIFVGVVVLAVCGALWELAAAFARKRIRLPLAPLWLGTLGISVCAWEVGAEAAFGAYVATVGACVLWSFMDQAEAEVGTVLEQAGHDIPRTEAHDEVRRSRSSAAAASVFAATYLPFLAGFAVLLLVQEHGVGKVMMLIALAAANDTGGWMAGITFGRHPLAPSVSPKKSWEGLMGSLIAAVATGAGCVWAIGGPWWAGAALGACTVIVSTLGDLGESLLKRDLGLKDMGTLLPGHGGIMDRLDSILVAAPLVYAFTLLVK$","Phosphatidate cytidylyltransferase","Membrane, Cytoplasm","phosphatidate cytidylyltransferase","phosphatidate cytidylyltransferase ","phosphatidate cytidylyltransferase","","Sparrow C.P., Raetz C.R. Purification and properties of the membrane-bound CDP-diglyceride synthetase from Escherichia coli. J. Biol. Chem. 1985. 260(22):12084-12091. PMID: 2995359Shen H., Heacock P.N., Clancey C.J., Dowhan W. The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth. J. Biol. Chem. 1996. 271(2):789-795. PMID: 8557688Saito S., Goto K., Tonosaki A., Kondo H. Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain. J. Biol. Chem. 1997. 272(14):9503-9509. PMID: 9083091","","","

InterPro
IPR000374
Family

Phosphatidate cytidylyltransferase
PF01148	$\"[30-311]T$	CTP_transf_1
PS01315	$\"[269-295]T$	CDS

noIPR
unintegrated

unintegrated
PD002096	$\"[259-290]T$	O86769_STRCO_O86769;
PTHR13773	$\"[190-237]T$	PHOSPHATIDATE CYTIDYLYLTRANSFERASE
signalp	$\"[1-48]?$	signal-peptide
tmhmm	$\"[29-49]?$ $\"[53-73]?$ $\"[158-178]?$ $\"[184-204]?$ $\"[225-245]?$ $\"[251-273]?$	transmembrane_regions

","BeTs to 19 clades of COG0575COG name: CDP-diglyceride synthetaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0575 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB000374 (Phosphatidate cytidylyltransferase) with a combined E-value of 1.6e-23. IPB000374B 215-228 IPB000374C 264-295","Residues 169-236 are similar to a (CYTIDYLYLTRANSFERASE TRANSFERASE PHOSPHATIDATE NUCLEOTIDYLTRANSFERASE TRANSMEMBRANE CDP-DIGLYCERIDE SYNTHETASE SYNTHASE CDP-DAG PYROPHOSPHORYLASE) protein domain (PD339398) which is seen in Q6AEV3_BBBBB.Residues 259-290 are 96% similar to a (CYTIDYLYLTRANSFERASE TRANSFERASE PHOSPHATIDATE NUCLEOTIDYLTRANSFERASE TRANSMEMBRANE CDP-DIGLYCERIDE SYNTHETASE SYNTHASE CDP-DAG PYROPHOSPHORYLASE) protein domain (PD002096) which is seen in O86769_STRCO.","","-53% similar to PDB:1A6C STRUCTURE OF TOBACCO RINGSPOT VIRUS (E_value = );-39% similar to PDB:1PC3 Crystal structure of the extracellular phosphate ABC transport receptor (PstS-1) and immunodominant antigen of M. tuberculosis. (E_value = );","Residues 30 to 311 (E_value = 3.3e-51) place ANA_1172 in the CTP_transf_1 family which is described as Cytidylyltransferase family.","","cytidylyltransferase (cdsA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1173","1252477","1251869","609","5.57","-3.54","22220","ATGGCCGCCCACTACCTGACGAACCCACGACCGCCCAGTAAAGGAAGCACCATGATCGACGACGTCATGCTCGAGACCGAGGACAAGATGGACAAGGCCCTCCAGGCCGCCAAGAGCGAGCTGGCCACCATCCGCACCGGCCGCGCCAACCCCTCGATGTTCAACGGGATCGTCGTGGACTACTACGGCGCCCCCACCCCGCTCCAGCAGCTCGCCTCCCTGACGATCCCCGAGGCCCGCACCGTCCTGGTCAGCCCCTTCGACCGCTCCGCCATGAAGGACATCGTCACCGCCATCCGCGAGTCCGACCTCGGCGTCAACCCCACCGATGACGGCACCGTCATCCGCGTCACCCTGCCGGCACTGACCGAGGAGCGCCGCAAGGACTACGTCAAGCTCGCCCGCTCCCGCGCCGAGGACTCCCGCGTCCAGGTGCGCGGTATCCGCGGCAAGGCCAAGAAGGAGCTCGAGGCCATCAAGAAGGACGGTGAGGCCGGCGAGGACGACGTCAAACGCGCCGAGCACGAGCTCGACGGCCTCACCAAGCGCTTCGTCGAGCAGATCGACGCCGCCCTGAGCGCCAAGGAGGCCGAGCTCCTCGAGGTCTGA","MAAHYLTNPRPPSKGSTMIDDVMLETEDKMDKALQAAKSELATIRTGRANPSMFNGIVVDYYGAPTPLQQLASLTIPEARTVLVSPFDRSAMKDIVTAIRESDLGVNPTDDGTVIRVTLPALTEERRKDYVKLARSRAEDSRVQVRGIRGKAKKELEAIKKDGEAGEDDVKRAEHELDGLTKRFVEQIDAALSAKEAELLEV$","Ribosome recycling factor","Cytoplasm","ribosome recycling factor","ribosome recycling factor","ribosome recycling factor","","Janosi L., Shimizu I., Kaji A. Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(10):4249-4253. PMID: 8183897","","","

InterPro
IPR002661
Family

Ribosome recycling factor
PD004103	$\"[25-189]T$	RRF_STRCO_O86770;
PTHR20982:SF3	$\"[18-202]T$	RIBOSOME RECYCLING FACTOR (RIBOSOME RELEASING FACTOR) (RRF)
PF01765	$\"[36-200]T$	RRF
TIGR00496	$\"[27-202]T$	frr: ribosome recycling factor

noIPR
unintegrated

unintegrated
G3DSA:1.10.132.20	$\"[83-202]T$	no description
PTHR20982	$\"[18-202]T$	RIBOSOME RECYCLING FACTOR

","BeTs to 19 clades of COG0233COG name: Ribosome recycling factorFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0233 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002661 (Ribosome recycling factor) with a combined E-value of 3.8e-75. IPB002661A 29-82 IPB002661B 111-162 IPB002661C 165-200","Residues 25-189 are similar to a (RIBOSOME FACTOR RECYCLING RELEASING RRF BIOSYNTHESIS CYCLIN CHLOROPLAST 3D-STRUCTURE FACTOR) protein domain (PD004103) which is seen in RRF_STRCO.Residues 64-189 are 51% similar to a (SPBC1709.09) protein domain (PD177367) which is seen in O74734_SCHPO.","","-78% similar to PDB:1WQF Crystal structure of Ribosome recycling factor from Mycobacterium Tuberculosis (E_value = 3.9E_53);-78% similar to PDB:1WQG Crystal structure of ribosome recycling factor from Mycobacterium Tuberculosis (E_value = 3.9E_53);-78% similar to PDB:1WQH Crystal structure of ribosome recycling factor from Mycobacterium tuberculosis (E_value = 3.9E_53);-71% similar to PDB:1EK8 CRYSTAL STRUCTURE OF THE RIBOSOME RECYCLING FACTOR (RRF) FROM ESCHERICHIA COLI (E_value = 1.8E_42);-71% similar to PDB:1ZN0 Coordinates of RRF and EF-G fitted into Cryo-EM map of the 50S subunit bound with both EF-G (GDPNP) and RRF (E_value = 1.8E_42);","Residues 36 to 200 (E_value = 2.8e-81) place ANA_1173 in the RRF family which is described as Ribosome recycling factor.","","recycling factor (frr)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1174","1253335","1252583","753","6.94","-0.16","26660","ATGAGTCAGGAACCGGCTCGTGACGACCGCGTCGCCCACGGCACGCACCCCAGACGTGTTCTACTCAAGCTCTCCGGTGAGGTCTTCGGTGGCGGATCCATAGGTCTGGACCCCGACGTCGTCTCCGACGCCGCCCGCCAGATCGCCGAGGCCGTGCGCGCCGGAGTCCAGGTCTCCGTCGTCGTCGGAGGCGGGAACTTCTTCCGCGGAGCCGAGCTCTCCTCACGCGGCATGGACCGCGCCCGCGCCGACTACATGGGCATGCTGGGAACCGTCATGAACGCCCTGGCCCTGCAGGACTTCATTGAGAAGGCGGGGGTGCCCGCCCGTGTCCAGACCGCCATCGCCATGGGACAGGTCGCCGAGTCCTACATCCCCCTGCGCGCCATCCGCCACATGGAGAAGAACCGCGTCGTCGTCTTCGGCGCCGGTGCCGGCCTGCCCTACTTCTCCACGGACACCGTCTCGGCCCAGCGCGCCCTGGAGACCCACTGCGATGAGCTGCTCGTGGGCAAGAACGGGGTCGACGGCGTCTACACCGCCGATCCCCGTAAGAACCCCGATGCCCGGCGCCTGGACCGGCTCACCTACGAGCGCGCCCTGGCCGACGGCCTCCAGGTGGTCGACGCCTCCGCCTTCGCCCTGTGCCGCGACAACGGCCTGACCATGCGCGTCTTCGGCATGGGGGAGCCCGGTAACATCACCCGCGCCCTGCTGGGTGAGAGAATCGGGACACTCGTCAGCTGCGACTGA","MSQEPARDDRVAHGTHPRRVLLKLSGEVFGGGSIGLDPDVVSDAARQIAEAVRAGVQVSVVVGGGNFFRGAELSSRGMDRARADYMGMLGTVMNALALQDFIEKAGVPARVQTAIAMGQVAESYIPLRAIRHMEKNRVVVFGAGAGLPYFSTDTVSAQRALETHCDELLVGKNGVDGVYTADPRKNPDARRLDRLTYERALADGLQVVDASAFALCRDNGLTMRVFGMGEPGNITRALLGERIGTLVSCD$","Uridylate kinase","Cytoplasm","uridylate kinase","uridylate kinase ","uridylate kinase","","Kikuchi Y., Kojima H., Tanaka T. Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli. FEMS Microbiol. Lett. 1999. 173(1):211-215. PMID: 10220897Kochhar S., Kochhar V.K., Sane P.V. Subunit structure of lysine sensitive aspartate kinase from spinach leaves. Biochem. Mol. Biol. Int. 1998. 44(4):795-806. PMID: 9584993Zhu-Shimoni J.X., Galili G. Expression of an arabidopsis aspartate Kinase/Homoserine dehydrogenase gene is metabolically regulated by photosynthesis-related signals but not by nitrogenous compounds. Plant Physiol. 1998. 116(3):1023-1028. PMID: 9501134","","","

InterPro
IPR001048
Domain

Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10	$\"[11-249]T$	no description
PF00696	$\"[18-227]T$	AA_kinase

InterPro
IPR011817
Family

Uridylate kinase
PIRSF005650	$\"[18-249]T$	Uridylate kinase
TIGR02075	$\"[17-248]T$	pyrH_bact: uridylate kinase

noIPR
unintegrated

unintegrated
PTHR21499	$\"[175-225]T$	ASPARTATE KINASE

","BeTs to 25 clades of COG0528COG name: Uridylate kinaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0528 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 19-114 are similar to a (KINASE TRANSFERASE URIDYLATE 2.7.4.- URIDINE MONOPHOSPHATE UMP PYRIMIDINE BIOSYNTHESIS UK) protein domain (PD421181) which is seen in Q73VR6_MYCPA.Residues 110-152 are 83% similar to a (KINASE TRANSFERASE URIDYLATE 2.7.4.- URIDINE PYRIMIDINE UMP BIOSYNTHESIS MONOPHOSPHATE UK) protein domain (PDA0T8W4) which is seen in Q83HZ6_TROW8.Residues 131-190 are 93% similar to a (KINASE TRANSFERASE URIDYLATE 2.7.4.- URIDINE MONOPHOSPHATE UMP PYRIMIDINE UK BIOSYNTHESIS) protein domain (PD800039) which is seen in Q8G484_BIFLO.Residues 192-250 are 66% similar to a (KINASE URIDINE PYRIMIDINE TRANSFERASE UMP 2.7.4.- MONOPHOSPHATE UK BIOSYNTHESIS URIDYLATE) protein domain (PDA1B3D6) which is seen in PYRH_THEMA.","","-64% similar to PDB:1Z9D Crystal structure of a putative uridylate kinase (UMP-kinase) from Streptococcus pyogenes (E_value = 8.7E_59);-66% similar to PDB:1YBD Crystal structure analysis of uridylate kinase from Neisseria meningitidis (E_value = 9.0E_56);-60% similar to PDB:2BND THE STRUCTURE OF E.COLI UMP KINASE IN COMPLEX WITH UDP (E_value = 7.2E_45);-60% similar to PDB:2BNE THE STRUCTURE OF E. COLI UMP KINASE IN COMPLEX WITH UMP (E_value = 9.4E_45);-60% similar to PDB:2BNF THE STRUCTURE OF E. COLI UMP KINASE IN COMPLEX WITH UTP (E_value = 9.4E_45);","Residues 18 to 227 (E_value = 5.8e-61) place ANA_1174 in the AA_kinase family which is described as Amino acid kinase family.","","kinase (pyrH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1175","1254432","1253593","840","5.21","-8.28","29570","ATGGCGAACTACACCACCGCTGACATCAAGGCGCTGCGCGAGAAGACCGGCGCGGGCATGCTCGACGTCAAGAAGGCCCTCGACGAGGCCAACGGCGACGCCGAGAAGGCCATCGAGATCATTCGCGTCAAGGGCCTCAAGGGCATTGCCAAGCGCGAGGGCCGCGCCGCCTCCGCTGGCCTCATCGCCGCCAAGGTCGTCGACTCCGGCAACGGCCAGGTCGGCGTCCTCGTCGAGATCAACGCCGAGACCGACTTCGTGGCCAAGAACCAGAAGTTCCTCGACTACGCCGAGCAGGTCCTCACCGCCGCTCTGGACTCCGGCGCCACCGACGCCGAGGCCCTGGCCGAGGTTGAGGTCGACGGCTCCACCGTCAAGGAGCTCACCGACGGCATGCAGGCCGTCATCGGCGAGAAGATCGTCGTGCGCCGTGTCGGCCGCCTCGAGGCCGACAAGATCGAGCTCTACCTGCACCGCACCAACCCCGACCTGCCCGCCCAGGTCGGCGTCCTGGTGGGCACCGACGCCAAGGCCGCCGAGGTGGCTCACGACGTCGCCATGCACATCGCCGCCTACTCCCCGGCCTACGCCACCCGCGAGGACGTCCCGGCTGAGGTCGTGGACAAGGAGCGCGCCATCGCCGAGGAGACCACCCGCGCCGAGGGCAAGCCCGAGAAGGCCATCCCCAAGATCGTCGAGGGGCGTCTCAACGGCTTCTTCAAGGAGAACGTCCTGGTCGACCAGGCCTTCGCCAAGGACCCCAAGACCACGGTCGGCAAGGTCGTTGAGGCCACCGGTGGCGAGCTGACCGGCTTCGTGCGCTTCCGCGTCGGCGCCTGA","MANYTTADIKALREKTGAGMLDVKKALDEANGDAEKAIEIIRVKGLKGIAKREGRAASAGLIAAKVVDSGNGQVGVLVEINAETDFVAKNQKFLDYAEQVLTAALDSGATDAEALAEVEVDGSTVKELTDGMQAVIGEKIVVRRVGRLEADKIELYLHRTNPDLPAQVGVLVGTDAKAAEVAHDVAMHIAAYSPAYATREDVPAEVVDKERAIAEETTRAEGKPEKAIPKIVEGRLNGFFKENVLVDQAFAKDPKTTVGKVVEATGGELTGFVRFRVGA$","Translation elongation factor Ts","Cytoplasm","translation elongation factor Ts","translation elongation factor Ts","translation elongation factor Ts","","Hofmann K., Bucher P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 1996. 21(5):172-173. PMID: 8871400Dieckmann T., Withers-Ward E.S., Jarosinski M.A., Liu C.F., Chen I.S., Feigon J. Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr. Nat. Struct. Biol. 1998. 5(12):1042-1047. PMID: 9846873Mueller T.D., Feigon J. Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. J. Mol. Biol. 2002. 319(5):1243-1255. PMID: 12079361","","","

InterPro
IPR000449
Domain

Ubiquitin-associated/Translation elongation factor EF1B, N-terminal
PF00627	$\"[4-44]T$	UBA

InterPro
IPR001816
Family

Translation elongation factor EFTs/EF1B
PTHR11741	$\"[7-278]T$	ELONGATION FACTOR TS
TIGR00116	$\"[1-278]T$	tsf: translation elongation factor Ts
PS01126	$\"[12-27]T$	EF_TS_1
PS01127	$\"[79-89]T$	EF_TS_2

InterPro
IPR014039
Domain

Translation elongation factor EFTs/EF1B, dimerisation
PF00889	$\"[57-279]T$	EF_TS

noIPR
unintegrated

unintegrated
G3DSA:1.10.286.20	$\"[199-243]T$	no description
G3DSA:1.10.8.30	$\"[2-55]T$	no description
G3DSA:3.30.479.20	$\"[57-155]T$	no description

","No hits to the COGs database.","***** IPB001816 (Elongation factor Ts) with a combined E-value of 4e-72. IPB001816A 4-54 IPB001816B 77-93 IPB001816C 133-144 IPB001816D 185-194 IPB001816E 222-258 IPB001816F 271-279***** IPB014039 (Translation elongation factor EFTs/EF1B, dimerisation) with a combined E-value of 3.1e-42. IPB014039A 9-45 IPB014039B 64-93 IPB014039C 131-145 IPB014039D 183-194","Residues 8-115 are 55% similar to a (ELONGATION FACTOR BIOSYNTHESIS EF-TS PV1H14170_P) protein domain (PD460641) which is seen in Q962K0_PLAVI.Residues 10-51 are 83% similar to a (FACTOR ELONGATION TS BIOSYNTHESIS EF-TS TRANSLATION CHLOROPLAST SEQUENCING DIRECT 3D-STRUCTURE) protein domain (PD552616) which is seen in EFTS_STRRA.Residues 112-208 are 58% similar to a (ELONGATION FACTOR EF-TS BIOSYNTHESIS TS) protein domain (PDA0T6E7) which is seen in EFTS_BIFLO.Residues 136-207 are 58% similar to a (ELONGATION FACTOR TS BIOSYNTHESIS EF-TS TRANSLATION SEQUENCING DIRECT PREDICTED) protein domain (PD683437) which is seen in EFTS_MYCPA.Residues 136-278 are 69% similar to a (ELONGATION FACTOR BIOSYNTHESIS TS EF-TS TRANSLATION CHLOROPLAST SEQUENCING DIRECT PEPTIDE) protein domain (PD106461) which is seen in EFTS_COREF.Residues 222-278 are 70% similar to a (ELONGATION FACTOR EF-TS BIOSYNTHESIS TS) protein domain (PD872864) which is seen in EFTS_STRCO.","","-56% similar to PDB:1EFU ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI (E_value = 1.6E_48);-49% similar to PDB:1AIP EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS (E_value = 2.7E_19);-51% similar to PDB:1TFE DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS (E_value = 6.4E_13);-38% similar to PDB:1XB2 Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex (E_value = 4.6E_11);","Residues 4 to 44 (E_value = 3.8e-09) place ANA_1175 in the UBA family which is described as UBA/TS-N domain.Residues 57 to 279 (E_value = 4.5e-69) place ANA_1175 in the EF_TS family which is described as Elongation factor TS.","","elongation factor Ts (tsf)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1176","1255387","1254539","849","5.46","-5.32","30807","ATGGCCGTCGTTACCATGCGCCAGCTCCTTGACAGCGGTGTCCACTTCGGGCACCAGACTCGTCGCTGGAACCCCAAGATGAAGCGCTTCATCCTCACCGAGCGCAACGGCATCTACATCATCGACCTCCAGCAGTCCATTGAGGGCATCAACACCGCCTACGACTTCGTCAAGGAGATCGTCGCTCGCGGCGGCAACATCCTGTTCGTCGGAACCAAGAAGCAGGCCCAGGCCGCCGTGGCCGAGCAGGCCCAGCGCGTCGGCATGCCCTACGTCAACCAGCGCTGGCTGGGCGGCATGCTCACCAACTTCTCCACCGTGCGCGCCCGCCTGGACCGCATGAAGGAGCTCGAGCAGATCGACTTCGACGACGTGGCCGGCTCCGGCCGCACCAAGAAGGAGCTGCTCATGATGCGCCGCGAGAAGGACAAGCTCCAGCGCACCCTGGGCGGTATCCGCGACATGAGCAAGCTCCCCGCGGCCGTGTGGGTCGTGGACACCAAGAAGGAGCACCTGGCCATCTCCGAGGCCCAGAAGCTCGGGATCCCGGTCATCGCCATCCTGGACACCAACTGCGACCCGGACGAGGCCACCTACGGCATCCCCGGCAACGACGACGCCATCCGCGCCGTCACCCTGCTCACCCGTGTCGTCGCCGACGCCACCGCCGAGGGCCTGCTGGCCCGCTCCGGCGGCCGTGCCCGCACTGGTGAGGAGGCCGAGGTCGCCCCCGCCGACGCCGAGCCGCTGCCCGAGTGGGAGGCCCAGCTCCTCGCCGGAGCCGAGGCCGACGTCCCGGCCGCTGAGGCTGCTGAGACCGCCGAGGCCCCCGCCGCCGAGCAGGCCTGA","MAVVTMRQLLDSGVHFGHQTRRWNPKMKRFILTERNGIYIIDLQQSIEGINTAYDFVKEIVARGGNILFVGTKKQAQAAVAEQAQRVGMPYVNQRWLGGMLTNFSTVRARLDRMKELEQIDFDDVAGSGRTKKELLMMRREKDKLQRTLGGIRDMSKLPAAVWVVDTKKEHLAISEAQKLGIPVIAILDTNCDPDEATYGIPGNDDAIRAVTLLTRVVADATAEGLLARSGGRARTGEEAEVAPADAEPLPEWEAQLLAGAEADVPAAEAAETAEAPAAEQA$","Ribosomal protein S2","Cytoplasm","ribosomal protein","30S ribosomal protein S2","ribosomal protein S2","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Davis S.C., Tzagoloff A., Ellis S.R. Characterization of a yeast mitochondrial ribosomal protein structurally related to the mammalian 68-kDa high affinity laminin receptor. J. Biol. Chem. 1992. 267(8):5508-5514. PMID: 1531984Tohgo A., Takasawa S., Munakata H., Yonekura H., Hayashi N., Okamoto H. Structural determination and characterization of a 40 kDa protein isolated from rat 40 S ribosomal subunit. FEBS Lett. 1994. 340(1):133-138. PMID: 8119397Ouzonis C., Kyrpides N., Sander C. Novel protein families in archaean genomes. Nucleic Acids Res. 1995. 23(4):565-570. PMID: 7899076","","","

InterPro
IPR001865
Family

Ribosomal protein S2
PR00395	$\"[6-24]T$ $\"[37-46]T$ $\"[87-104]T$ $\"[159-176]T$ $\"[176-187]T$ $\"[197-211]T$	RIBOSOMALS2
PF00318	$\"[9-226]T$	Ribosomal_S2
PS00962	$\"[6-17]T$	RIBOSOMAL_S2_1

InterPro
IPR005706
Family

Ribosomal protein S2, bacterial and organelle form
PTHR12534	$\"[1-264]T$	30S RIBOSOMAL PROTEIN S2 (PROKARYOTIC AND ORGANELLAR)
TIGR01011	$\"[3-228]T$	rpsB_bact: ribosomal protein S2

","BeTs to 26 clades of COG0052COG name: Ribosomal protein S2Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0052 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001865 (Ribosomal protein S2) with a combined E-value of 3.1e-74. IPB001865A 8-31 IPB001865B 67-114 IPB001865C 173-214","Residues 9-234 are similar to a (RIBOSOMAL S2 30S CHLOROPLAST RIBONUCLEOPROTEIN MITOCHONDRION SUBUNIT S2P MITOCHONDRIAL SEQUENCING) protein domain (PD328397) which is seen in Q6A7J7_PROAC.Residues 15-204 are 42% similar to a (RIBOSOMAL MITOCHONDRION S2) protein domain (PD241081) which is seen in Q9XPI7_DICDI.Residues 45-188 are 46% similar to a (RIBOSOMAL MITOCHONDRION S2) protein domain (PDA187K9) which is seen in Q8W9Q7_MESVI.Residues 202-237 are 83% similar to a (RIBOSOMAL 30S S2 RPSB RIBONUCLEOPROTEIN) protein domain (PD220789) which is seen in RS2_STRAW.","","-70% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 4.6E_59);-70% similar to PDB:1GIX Crystal structure of the ribosome at 5.5 A resolution. This file, 1GIX, contains the 30S ribosome subunit, three tRNA, and mRNA molecules. 50S ribosome subunit is in the file 1GIY (E_value = 4.6E_59);-70% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 4.6E_59);-70% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 4.6E_59);-70% similar to PDB:1HNZ STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH HYGROMYCIN B (E_value = 4.6E_59);","Residues 9 to 226 (E_value = 5.2e-89) place ANA_1176 in the Ribosomal_S2 family which is described as Ribosomal protein S2.","","protein (rpsB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1177","1255651","1256673","1023","10.51","16.17","35182","ATGCTCGGGTGCAGGCACGCGAAGTCAGCATTCCGGGCCCGTTTCCCGCTGACGCCGGAGCGATCCGCAGAATGCTGCGGAGGCAAGGCTACCACAGGACTGGACCAGCGGCCGAGGCCGAATCCGCGGTATTCGGAGTCGTCCCGGTCACCACAGGCCGCTTCCTCGAGGGGCTTTCCACAGGGCGGACGACGCCCCCGGCGCCGAGGGCCGCTCGGCACGCACTCTGAGGGCATGCAGCCACAGCAGCCTCGGCAAAGCCGCCACCTCCGAGATCCTCGCACGCCCCACTGCCTCGCGGCGCTGGCAACGGCCCTGATCGCCTGCGGCTCACTGGCTGCGCTGCCCGGTGCACCACCGGCTCAGGGCATGAGCACTCTCCCCGGCCCAGCCACCAGCACGGCCGTGACCACGGTTCCGCCTCCGCGGGTCCAGGATCCGTTACTTCCCGATCTCACGGAAAGTGCGCCAGGGCCGGCCGGGGCCGCCCACTGGTTGAGCTCGTCAGCCTCGCTCGTAACGAGCCTCAGCCCCTCCTCCCCGCTCATCAACGGCACGGGAACGGCCGGCCCGGCACTGACGGACCAATCTGCGGGCCCCCGGCGGCCGCGGGGCCACTACCAGTGGCCGACCGGCGCGCCGGCCACCGTGGTGGAGGATTTCGACCCGCCTGCCGTCGTGTGGGGACGCGGACACCGGGGAGTGGATCTCGCGGCCGCTGAGGGCACGCAGATCCGCAGCGCCGCCGCGGGGACGGTCGCCTTCGCCGGCATGGTGGCCGGGCGCCCCGTGGTGTCCATCGACCACGCCGACGGGATCCGCACCACCTATGAGCCGGTAGAACCGGCCGTCAGCGCGGGTGACGCGGTGGCTGCGGGGCAGGTCATCGGCACCCTGCTGCCGGGGCACCGCTCGGACGGGGTCTGCGCCCTGCACTGGGGGGCGCGCACCGGCCCCAAGACGTACATCAACCCGCTGCGCCTGCTGCAACCTGCCGTCATCCGTCTCAAGCCCCTTCAATGA","MLGCRHAKSAFRARFPLTPERSAECCGGKATTGLDQRPRPNPRYSESSRSPQAASSRGFPQGGRRPRRRGPLGTHSEGMQPQQPRQSRHLRDPRTPHCLAALATALIACGSLAALPGAPPAQGMSTLPGPATSTAVTTVPPPRVQDPLLPDLTESAPGPAGAAHWLSSSASLVTSLSPSSPLINGTGTAGPALTDQSAGPRRPRGHYQWPTGAPATVVEDFDPPAVVWGRGHRGVDLAAAEGTQIRSAAAGTVAFAGMVAGRPVVSIDHADGIRTTYEPVEPAVSAGDAVAAGQVIGTLLPGHRSDGVCALHWGARTGPKTYINPLRLLQPAVIRLKPLQ$","Peptidase M23B","Extracellular, Membrane","M23/M37 peptidase domain protein protein","hypothetical protein","peptidase M23B","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR002886
Family

Peptidase M23B
PTHR21666:SF7	$\"[232-299]T$	M23/M37 PEPTIDASE FAMILY MEMBER
PF01551	$\"[230-325]T$	Peptidase_M23

noIPR
unintegrated

unintegrated
PTHR21666	$\"[232-299]T$	PEPTIDASE-RELATED
tmhmm	$\"[98-118]?$	transmembrane_regions

InterPro
IPR002104
Domain

Integrase, catalytic core, phage
PF00589	$\"[146-298]T$	Phage_integrase

InterPro
IPR004107
Domain

Integrase, N-terminal SAM-like, phage
PF02899	$\"[9-98]T$	Phage_integr_N

InterPro
IPR013762
Domain

Integrase-like, catalytic core, phage
G3DSA:1.10.443.10	$\"[120-301]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.130	$\"[4-108]T$	no description

","BeTs to 25 clades of COG0582COG name: IntegraseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0582 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB004107 (Phage integrase, N-terminal SAM-like) with a combined E-value of 2.7e-21. IPB004107A 157-167 IPB004107B 183-189 IPB004107C 251-265 IPB004107D 276-286","Residues 98-307 are 46% similar to a (INTEGRASE/RECOMBINASE) protein domain (PDA027R6) which is seen in Q7NNG2_GLOVI.Residues 146-205 are similar to a (DNA INTEGRASE/RECOMBINASE RECOMBINASE INTEGRASE RECOMBINATION INTEGRATION PLASMID TYROSINE DIVISION DNA-BINDING) protein domain (PD000548) which is seen in Q73VQ5_MYCPA.Residues 260-300 are 87% similar to a (DNA INTEGRASE RECOMBINASE INTEGRASE/RECOMBINASE INTEGRATION RECOMBINATION TYROSINE DIVISION DNA-BINDING CHROMOSOME) protein domain (PD254221) which is seen in Q81WK4_BACAN.","","-49% similar to PDB:1A0P SITE-SPECIFIC RECOMBINASE, XERD (E_value = 8.4E_33);","Residues 9 to 98 (E_value = 8.1e-16) place ANA_1178 in the Phage_integr_N family which is described as Phage integrase, N-terminal SAM-like domain.Residues 129 to 298 (E_value = 1.8e-43) place ANA_1178 in the Phage_integrase family which is described as Phage integrase family.","","integrase family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1179","1258455","1257880","576","5.44","-6.67","19955","GTGTCAGCATGTTCATGGACGAAACCTCCTGGAGACGAGGGTGGGGACGGTGGAGCCGGAGCCGGTGGCCCGGGGCGGCGTGATGTCGTCAATCTGCGTATAGGTGTCCGAGGAGGCGTCGGACATGACGACCTGGGAGCTGGACTGGTCGACGTCGAAGCTCGTCGAGGAGGTGCGCAGGCCCCTGTTGAGCGTCTGCGAGCGGTAGCTGAGGTGGGCGACCATCGCCATCTTCCCGTTGGTCGCCCGCACTCCACCGCCATGAAGATCGACAACATGGGTGACCATCCCCGGGTGCAGGACGACGGCGACCAGAGCGGCAGCGGTCAGGACCGCGATGACGCCGACGTGGACGCCGCGCCTGGAGAACCGTTTCACAGTGCTGCGCTCCAGCAGGAAATAGGGATGAGCCAGGAAGGGATGGAGTTCGTCAGAACGACCAAGATTTTAACTTCCTCGTTGGATGGCAACAAATGCTCCGAATGTGGGGAAACACAGAGGAAAGATGGGTTTTTCGTTGGGATCAAGGAGAAGGGGAGGTTGGTATCCGTAGTGCCACCTGGATGGTTGTTATGA","VSACSWTKPPGDEGGDGGAGAGGPGRRDVVNLRIGVRGGVGHDDLGAGLVDVEARRGGAQAPVERLRAVAEVGDHRHLPVGRPHSTAMKIDNMGDHPRVQDDGDQSGSGQDRDDADVDAAPGEPFHSAALQQEIGMSQEGMEFVRTTKILTSSLDGNKCSECGETQRKDGFFVGIKEKGRLVSVVPPGWLL$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1180","1258530","1260068","1539","5.32","-18.31","53437","ATGGAAGCGATGTGGACCGAGCTCGGTGAGCACCGCTGCCTCGGCGACCTGCTCAAAAGCCTGAGCCGGCTGCACGACAACGAGGTCTTCACCCTCCCCGACTTCCTCATGATGGCCATCGACGGCCAGGAGCTGCGAGTGGCCGCCCGAGGCCGCTTCTGCCTCCACCTGGACACTGCCGACGGCGAGCGCAGCTTCAGTGCCTCCGAGGTCGTCGTGTGGGAGGAGTCCCGCTATGAGCGGGTCAACCAGTGCATCCTCGAGCTCACCCCGGCCACCAGACACCCAGCCGGTCCCGAAGGGCTCGACGAGTTCCTCCCCCTGCGCTCGGGGATCGTCCGAGCCTCGCAGCTGCACATCGGCTTCGGAGACCACCAGCTCCCACTATCCTCACCGGCTCAGACCGGCGCTCACGGGGGTCAGGGGGCACCGCAACCATCGGCGGCCCAGGAGATCCTCCAACAGGCTCAGGCCGACGGCGCCCCCGAGCGGGACGACCCACCGCCGTCGTCATCGCTACCTGCGAGGCAGGAGCAGGGCAAGGCCGCCTACCAGTCCCGCCCCGATCCCGGACAGACGCTGGAACCGCAGTCCATGGGCCCGATGGACAGTGCGGGCTCCCCGCAGGGGACCGAGGCGGGGGATCCGGCCGCGGTGCTGGGACCCAACGACGTTCCGGCGGCCGAGGCCGCAGCCCCGCAGGCGCATGGACAGCAGGCCCAGGACGACAAGGCCGGTCGTCTTGTTGAGCGCACGATGATGCAGGGGGCCGAGGCGGCCGTCGGCCCGGCCTCCTCTCAGGACATGGATCCGTTGGCCCGGCTCGCCGCAGGGCCCGGACGTCACCGGGCCTCCCCTCTGGGCGAGAGCGCCTCCGGCCGACACTCGTCACAGGCCGCTGAGCCGCTCCCGGCTCAGCGGCAGGCCCCGGACGGCGGCGCAGATGCAGCGTCCCCGAATGGCTCAGCGCCCTCGGGCGCGCAGGGCAAGCACGACGGGCGCACCGTCTCGGCTGTAGGACTTCATGCCGCCAGGAACGCACTAGGCGGGCAGACCGGGCTCGACGAGCCCTCCGGCACCGGCCCCAGCGTGATGGCCATCTTCTGCGAGGCGGGGCACCCCAATCCGGTGCACGCCTCCTCGTGCCGCGAGTGCGACAGCACCATCACCTCCAGGACCGGCCAGGTCGAGCGACCGGTCCTGGGCGTTCTGCGTGTCTCCTCAGGCGCCACGGCGATCCTGGACAGTGATGTCATCATCGGCCGACTGCCCCAGGGCACGAGCAGCACCGCCGCTCAGCGCCCCCGCCTGTTGACCGTCCCCAGCCCGGGCAAGGCGATCTCGAAGACTCACTGCGCCGTGAGGGTCGAAGGCTGGGACATGCGCGTGGAGGACCTGGGCTCCACCAACGGGACCTTCCTGCTGCGCGCCGGGGAGGAGCCCCGCCGCGTGCCCGAGCACCAGCAGCTTCTCCTGCGCGCCGGCGACATCATCGACATCGGTGATGGCACCACCCTGACAGTGGAGCGTGAGGCGTGA","MEAMWTELGEHRCLGDLLKSLSRLHDNEVFTLPDFLMMAIDGQELRVAARGRFCLHLDTADGERSFSASEVVVWEESRYERVNQCILELTPATRHPAGPEGLDEFLPLRSGIVRASQLHIGFGDHQLPLSSPAQTGAHGGQGAPQPSAAQEILQQAQADGAPERDDPPPSSSLPARQEQGKAAYQSRPDPGQTLEPQSMGPMDSAGSPQGTEAGDPAAVLGPNDVPAAEAAAPQAHGQQAQDDKAGRLVERTMMQGAEAAVGPASSQDMDPLARLAAGPGRHRASPLGESASGRHSSQAAEPLPAQRQAPDGGADAASPNGSAPSGAQGKHDGRTVSAVGLHAARNALGGQTGLDEPSGTGPSVMAIFCEAGHPNPVHASSCRECDSTITSRTGQVERPVLGVLRVSSGATAILDSDVIIGRLPQGTSSTAAQRPRLLTVPSPGKAISKTHCAVRVEGWDMRVEDLGSTNGTFLLRAGEEPRRVPEHQQLLLRAGDIIDIGDGTTLTVEREA$","Forkhead-associated protein","Cytoplasm, Periplasm, Extracellular","FHA domain protein","hypothetical protein","Forkhead-associated protein","","Hofmann K., Bucher P. The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors. Trends Biochem. Sci. 1995. 20(9):347-349. PMID: 7482699Durocher D., Jackson S.P. The FHA domain. FEBS Lett. 2002. 513(1):58-66. PMID: 11911881","","","

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[418-501]T$	FHA
SM00240	$\"[417-479]T$	FHA
PS50006	$\"[418-474]T$	FHA_DOMAIN

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.20	$\"[416-502]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 404-502 are 55% similar to a () protein domain (PDA1F097) which is seen in Q6AEZ7_BBBBB.Residues 407-507 are 56% similar to a (ATP-BINDING KINASE DOMAIN FHA TRANSCRIPTION ABC ZINC-FINGER NUCLEAR TRANSPORTER TRANSFERASE) protein domain (PD001303) which is seen in Q6A653_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 418 to 501 (E_value = 0.00018) place ANA_1180 in the FHA family which is described as FHA domain.","","domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1181","1260263","1261333","1071","6.69","-1.73","37949","ATGGCCCGTCTGTCATCGCACCCCTCCATCGTGTCGCTCTACGGGGCCGGGACGGTGGAGGAAGAGCGCAGCTACCTCATCATGGAGTACTGTCCCCCTCCCCACCTGGGCAAGCTGGCCGCCTCGCAGCCCTTGTCCCTCACACGCGCCCTGGAGATCGGTATCCAGCTGGCGGGCGCGGTGGAGACCATTCACCGGGTCGGCTACCTCCACCGCGACATCAAGCCTGCCAGCATCCTGCTCACCCCCTTCGGGCGTCCGGTGCTCGGCGACTTCGGGATCGCCGCGCCCATCGGGCTCAGCATCGAGAAGGACGAGTTCGGAGGGGCGTCCCCGCCGTGGGCCTCACCCGAGCAGCAGCTCGACCGGGAGAGCCTGACTCCGGCCTCGGATGTCTACGCCCTGGCCGCGACCATCTACACGCTGCTGGCGGGACGCTCACCCCACGTCGATGTCTCAGGAGCCGACCGCAACGACCAGCTCTCGATGATCGACCGAGTGCTCCACCGACAAATCCCCCCGATCGGGCGACACGACATACCCGAGCAGCTCGAGCGGATCCTGGCCATGGCGATGGCCAAGTCTCCCCGCGCACGGTATGCCAGCGCCGTCGCCCTGGCTCGGGCGCTGCAACAGGTACAGACCGACCTGTGCATGACCATCACCCAGCTCGATGTCATGGAGGAGGCGTCCGGACGACACACGAGCGGGAACCGGAACCAGGACTCCACGATGCTGCGGCCGGCCGTCATAGTGGACCCGGACGGGCCGACCGGAGCCGTGCCCGCCGCACACCGGCACGACGACGCCGCCACGACCTTCGCGCCTCGTCGTGTCAAGGCCCAGCCCACCGGCTCCGCCTCGCTGTGCGACCGTCCCCGGCCCGGTTCCGCTCTCCCGCCCCAGGGCGATGAGGCCGAGGTCGCGAGAGACGACCCGGGCTCGCAGGAGGCCGAGGCGGGCCTGCAGCGGCGGCGCAGCCGCCCGTCGGGGCGAGCCGTGGCCGTCACCGTGGTGGGCGCCGCCGTCATGGTCTGCCTGAGCGCGATCGGAGTGTGGTCGTTGCTGTGA","MARLSSHPSIVSLYGAGTVEEERSYLIMEYCPPPHLGKLAASQPLSLTRALEIGIQLAGAVETIHRVGYLHRDIKPASILLTPFGRPVLGDFGIAAPIGLSIEKDEFGGASPPWASPEQQLDRESLTPASDVYALAATIYTLLAGRSPHVDVSGADRNDQLSMIDRVLHRQIPPIGRHDIPEQLERILAMAMAKSPRARYASAVALARALQQVQTDLCMTITQLDVMEEASGRHTSGNRNQDSTMLRPAVIVDPDGPTGAVPAAHRHDDAATTFAPRRVKAQPTGSASLCDRPRPGSALPPQGDEAEVARDDPGSQEAEAGLQRRRSRPSGRAVAVTVVGAAVMVCLSAIGVWSLL$","Serine/threonine protein kinase","Membrane, Cytoplasm","serine/threonine protein kinase","protein kinase/transcriptional regulator; LuxR family ","protein kinase","","","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[1-196]T$	Q6AEZ5_BBBBB_Q6AEZ5;
PF00069	$\"[1-173]T$	Pkinase
PS50011	$\"[1-217]T$	PROTEIN_KINASE_DOM

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[18-206]T$	no description
PTHR22986	$\"[1-247]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES
tmhmm	$\"[333-353]?$	transmembrane_regions

InterPro
IPR003488
Family

SMF protein
PF02481	$\"[111-361]T$	SMF

noIPR
unintegrated

unintegrated
signalp	$\"[1-1]?$	signal-peptide

","BeTs to 15 clades of COG0758COG name: Predicted Rossmann fold nucleotide-binding protein involved in DNA uptakeFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0758 is -------qvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB003488 (SMF protein) with a combined E-value of 3.1e-37. IPB003488A 200-225 IPB003488B 228-267 IPB003488C 295-338","Residues 116-307 are 51% similar to a (DNA PROCESSING SMF A CHAIN FAMILY NUCLEOTIDE-BINDING DPRA DPRA UPTAKE) protein domain (PD007421) which is seen in O69892_STRCO.Residues 310-379 are 67% similar to a (DNA SMF PROCESSING A CHAIN FAMILY DPRA NUCLEOTIDE-BINDING UPTAKE DPRA) protein domain (PD295569) which is seen in Q73VQ2_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","Residues 111 to 361 (E_value = 1.8e-58) place ANA_1182 in the SMF family which is described as SMF family.","","family protein (AF088896)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1183","1264426","1262855","1572","7.16","0.94","54091","ATGGGGCTAGCTCGCACACTCGCTGTCACGCTGACCGGGCTGGCCGGACACATCGTTGAGGTCGAGGCTCATGCCGCCCAAGGCCTGCCCGGATTCACCCTCGTGGGCCTGCCCGACGCCGCCGTGCGTGAGTCGCGCGAGCGCGTCCGGGCCGCGTTGAGCACCTGCGGCGTCACCTGGGGCGAGCAGCGCCTGACCGTCAACCTCTCCCCGGCGGACCTGCGCAAGACCGGGACCGGGCTGGACCTGGCTCTGGCCCTGGCCGTCCTGGGGGCCCGCGGTTGGCTCGGACGGAGCGCGGCCGGCATCCTGGGCCGGACCGTCTACATCGGCGAGCTCGGGCTGGACGGCTCCGTGCACTCGGTGCGCGGCGTCCTGCCCAGCGTCCAGGCCGCGGTGGCCGCCGGTGTGGAGGAGATCGTCGTCGCCCAGGAGGCCGCGGCTGAGGCCGAGCTCGTCCCCGGCGCCTGCGTCACCGCCGTCAGGCACATCGGCCAGCTCGTCGAGCGCTACGGAGGACGCCTGAGCGCTGCCGTGGTCGCCGCACTGGAGCAGATCGCCGAAGCCGCCACAGACGATGCCCCCACGACCCCGCCGTGGGATGCCGAGCTGCCGGACCTGGCCGACGTCGTCGGACAGCATGATGCCCGCCAGGCCCTTGAGGTTGCCGCCGCCGGGGGCCATCACCTTCTCATGGTGGGGCCTCCGGGGACGGGAAAGACCATGCTCGCTGAAAGGCTCCCCTCGATCCTGCCGCCCCTGGAGCAGGCCGATGCTGTGACGGTCACCTCCCTGCACTCCGTGGCCGGCATCTTCGACCCCGCCCGCGGACTCATCACCCGGCCTCCGTTGCGCGCGCCGCACCACACGGCGACCCGGGCCGCCGTCGTCGGGGGAGGCTCCGGCCTGCCCCGCCCCGGGGACGTCTCCCTGGCTCACCGCGGCGTGCTCTTCCTCGACGAGGCCCCCGAGTTCAGCGCTGGCGTCCTGGACTGCCTGCGCCAGCCGCTGGAGTCGGGAGTGGTCACCATCGACCGGGTGGGTGGGCGCGCCAGCTACCCGGCCGCCTTCCAGCTCATCCTGGCCGCCAACCCCTGCCCCTGCGGCAAGGCCGGCGGCCGGGGCCTGGAGTGCACCTGCACCTCCCTGCAGCGGCGGCGCTACTTCTCACGCCTGTCCGGTCCACTGCTGGACCGGGTCGACATCCAGGTCGAGGTCAGTGCCGTCAGCGCAGCCGACCTCGCGTCTACCGGTCAGGGAGAGTCCAGCGCTGAGGTGGCGCAGCGCGTCCTGCACGCCCGACGAGCCGCGGAGCGCAGACTGGCCGGCACCCCGTGGCGCCTCAACGCCGAGGTACCCGGCTCCTACCTCAGAGGCCCCGACGGAGGACTCAGCGCTCCGCTCAGCCGCCGGCTCATGACCGCCCTCGAACGCGGTGACCTCTCCCTGCGCGGGGTGGACCGGGTCCTCAGACTGGCCTGGACCCTCGCCGACCTCGAGGGGGTCAAGACCCTCGCCCTTGCCCACATCGGGACCGCCCTGGCCCTGAGAACCTCAGGAGTGCGGCCATGA","MGLARTLAVTLTGLAGHIVEVEAHAAQGLPGFTLVGLPDAAVRESRERVRAALSTCGVTWGEQRLTVNLSPADLRKTGTGLDLALALAVLGARGWLGRSAAGILGRTVYIGELGLDGSVHSVRGVLPSVQAAVAAGVEEIVVAQEAAAEAELVPGACVTAVRHIGQLVERYGGRLSAAVVAALEQIAEAATDDAPTTPPWDAELPDLADVVGQHDARQALEVAAAGGHHLLMVGPPGTGKTMLAERLPSILPPLEQADAVTVTSLHSVAGIFDPARGLITRPPLRAPHHTATRAAVVGGGSGLPRPGDVSLAHRGVLFLDEAPEFSAGVLDCLRQPLESGVVTIDRVGGRASYPAAFQLILAANPCPCGKAGGRGLECTCTSLQRRRYFSRLSGPLLDRVDIQVEVSAVSAADLASTGQGESSAEVAQRVLHARRAAERRLAGTPWRLNAEVPGSYLRGPDGGLSAPLSRRLMTALERGDLSLRGVDRVLRLAWTLADLEGVKTLALAHIGTALALRTSGVRP$","Magnesium chelatase, subunit ChlI","Cytoplasm","Mg chelatase-related protein","K07391 magnesium chelatase family protein","Mg chelatase, subunit ChlI","","Nelson R.E., Fessler L.I., Takagi Y., Blumberg B., Keene D.R., Olson P.F., Parker C.G., Fessler J.H. Peroxidasin: a novel enzyme-matrix protein of Drosophila development. EMBO J. 1994. 13(15):3438-3447. PMID: 8062820Li H., Poulos T.L. Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures. Structure 1994. 2(6):461-464. PMID: 7922023Welinder K.G. Superfamily of plant, fungal and bacterial peroxidases. 388 Ascorbate peroxidase.. 1992(Dalton D.A.):393-2. PMID: Curr. Opin. Struct. Biol.","","","

InterPro
IPR000408
Repeat

Regulator of chromosome condensation, RCC1
PS00626	$\"[223-233]?$	RCC1_2

InterPro
IPR000523
Domain

Magnesium chelatase, ChlI subunit
PF01078	$\"[206-414]T$	Mg_chelatase

InterPro
IPR001208
Family

MCM
PR01657	$\"[225-240]T$ $\"[307-321]T$ $\"[335-348]T$	MCMFAMILY

InterPro
IPR002016
Family

Haem peroxidase, plant/fungal/bacterial
PS00435	$\"[258-268]?$	PEROXIDASE_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[226-410]T$	AAA

InterPro
IPR004482
Family

Mg chelatase-related protein
TIGR00368	$\"[6-517]T$	TIGR00368: Mg chelatase homolog

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[202-407]T$	no description
signalp	$\"[1-23]?$	signal-peptide

","BeTs to 15 clades of COG0606COG name: Predicted ATPase with chaperone activityFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0606 is --m----qvdr--cefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB000523 (Magnesium chelatase, ChlI subunit) with a combined E-value of 5.8e-98. IPB000523A 210-252 IPB000523B 276-324 IPB000523C 330-381 IPB000523D 408-461 IPB000523E 484-523***** IPB001208 (MCM family) with a combined E-value of 3.1e-63. IPB001208B 39-79 IPB001208C 102-135 IPB001208D 225-264 IPB001208E 288-342 IPB001208F 372-426***** IPB000641 (CbxX/CfqX superfamily signature) with a combined E-value of 1.1e-08. IPB000641B 229-244 IPB000641D 304-323","Residues 209-274 are 59% similar to a (ATP-BINDING ACTIVITY WITH CHAPERONE PREDICTED ATPASE AAA VP2421 RB10364 CLASS) protein domain (PD042735) which is seen in Q8TXG6_METKA.Residues 217-319 are 55% similar to a (HOMOLOG COMPETENCE COMM ATP-BINDING) protein domain (PDA060G0) which is seen in Q6MKT4_BDEBA.Residues 218-253 are 97% similar to a (ATP-BINDING CHELATASE COMPETENCE FAMILY COMM MG2 MAGNESIUM PROBABLE CHELATASE RELATED) protein domain (PDA0U033) which is seen in Q8UII4_AGRT5.Residues 254-319 are similar to a (ATP-BINDING CHELATASE COMPETENCE FAMILY COMM MG2 MAGNESIUM PROBABLE CHELATASE RELATED) protein domain (PD586207) which is seen in Q73VQ1_MYCPA.Residues 320-368 are 79% similar to a (ATP-BINDING CHELATASE COMPETENCE FAMILY COMM MG2 MAGNESIUM PROBABLE CHELATASE RELATED) protein domain (PD587240) which is seen in Q6AEA9_BBBBB.Residues 378-430 are 75% similar to a (ATP-BINDING COMPETENCE CHELATASE COMM FAMILY MAGNESIUM MG2 PROBABLE CHELATASE RELATED) protein domain (PDA130E8) which is seen in Q6AKX8_BBBBB.Residues 443-518 are 57% similar to a (ATP-BINDING CHELATASE COMPETENCE FAMILY COMM MAGNESIUM MG2 PROBABLE CHELATASE RELATED) protein domain (PD412471) which is seen in Q82JX2_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 206 to 414 (E_value = 4.3e-135) place ANA_1183 in the Mg_chelatase family which is described as Magnesium chelatase, subunit ChlI.Residues 229 to 395 (E_value = 0.00035) place ANA_1183 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).Residues 229 to 245 (E_value = 6.6e-08) place ANA_1183 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).","","chelatase-related protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1184","1264974","1264417","558","10.51","6.85","19760","ATGACCGACCAGGTCGTAGCCACAAGGGGACGAACGGTGATCGCAGCCAGGTGCGGCGATCACGCGCTCACGCCGCCATTCCAGGGCCCGGGAGGCGCAGGAGCTGTCCGCGCAGGGGCGTCCCGCCAGAGCACCGGACGGCGTGGAGAGGATCTTGCCGCCACCTACCTGGAGGACATCGGCTGGCAGGTCCTGGAGCGCAACTGGCGTCCGGACCACGGCCTGCGCGGAGAGCTCGACATCATCGCCCTGGAACCCGGTCACGCGCACCGTGAGCCGGGCAGTGAGTCCGTCGCCGACCCAGCTCAGGGGCGGACAGGACCGAGGCTCGTCATCGTCGAGGTCAAGACCCGCAGCTCCCTGCGCCAGGGACCGCCGGCCGCCGCGGTCGACGCCCGCAAGGTCGCCCGGCTGCGGGCCCTGGCGGCCGCCTGGGCGAGCACCCATGAAACCCCGCCGCACGCCGGGATGCGACTGGACGTGGTCTCCATCCTCCTGCGCGACGCGCGTCCTGCGCTGCTGCGCCACCACCGGGCGGTGGATGCGTCATGGGGCTAG","MTDQVVATRGRTVIAARCGDHALTPPFQGPGGAGAVRAGASRQSTGRRGEDLAATYLEDIGWQVLERNWRPDHGLRGELDIIALEPGHAHREPGSESVADPAQGRTGPRLVIVEVKTRSSLRQGPPAAAVDARKVARLRALAAAWASTHETPPHAGMRLDVVSILLRDARPALLRHHRAVDASWG$","Endonuclease","Cytoplasm","Uncharacterised protein family UPF0102 family","hypothetical protein predicted by Glimmer/Critica","protein of unknown function UPF0102","","","","","

InterPro
IPR003509
Family

Protein of unknown function UPF0102
PF02021	$\"[48-165]T$	UPF0102

","BeTs to 10 clades of COG0792COG name: Predicted endonuclease distantly related to archaeal Holliday junction resolvaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0792 is -------qvdr--cefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 48 to 165 (E_value = 9.8e-21) place ANA_1184 in the UPF0102 family which is described as Uncharacterised protein family UPF0102.","","protein family UPF0102 family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1185","1265445","1265137","309","4.44","-10.81","11924","GTGAGCGCAGAAGACCTCGAGTCCTATGAGAACGAGCTGGAGCTCTCGCTGTACCGGGAGTACCGCGATGTCGCCTCCCTGTTCTCCTACGTGGTGGAGACTGAACGGCGGTTCTACCTGGCCAATGCCGTTGACGTCCAGGTACGCACCAGCGGCGGGGAGGTCTTCTTCGAGCTCACCCTCGAGGACGCCTGGGTGTGGGACATCTACCGGGCCTCCCGGTTCGTCAAGTCCGTCCACGTCGTCACCTTCAAGGACGTCAACGTCGAGGAGCTCACCAAGCTCGAGATGGACATCCCCTCCTCCTAG","VSAEDLESYENELELSLYREYRDVASLFSYVVETERRFYLANAVDVQVRTSGGEVFFELTLEDAWVWDIYRASRFVKSVHVVTFKDVNVEELTKLEMDIPSS$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PD020280	$\"[24-100]T$	Q73VP4_MYCPA_Q73VP4;

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 24-100 are similar to a (LYASE ORF3 MLCB250.41 CGL2032 UTP-AMMONIA RV2901C/MT2969/MB2925C SYNTHASE ML1610 SCO5601 CTP) protein domain (PD020280) which is seen in Q73VP4_MYCPA.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1186","1266273","1265539","735","6.66","-2.17","25915","GTGAGCCCTCGGGGACGTACCCGTCCTGACCGGCGTCTGGAGAAGGCCCTGCTGGAGAGCCACGACTACGTCGGCGGCCTGGACGAGGTCGGTCGCGGCGCTCTGGCCGGACCGGTCAGTGTCGGGCTGGCGATCGTGTCGCGGCGCACCGATGACGACTTCCCCACGGGGCTCGCCGACTCCAAGCAGCTGACGGCCCGGGCGCGCACCGGCCTGATCGAGCCCGTGCGCGGCTGGTTGGTGGACCACGCCGTCGCCCACGCCTCACCCGCTGAGATCGATGAGCACGGCATCGTCGCGGCCTTGAGGATGGCGGGCTTGCGGGCCCTGCAGCAGGTCGCAGATCGCGGTCACGCCCCCCGAATCATCATCCTCGACGGCGTGGCCGACTGGCTCACCGCCCCCCAGCCCGACCTGCTCACCGCCCTGGAGGGGGCTCATGTCCCCGAGACTGCTCCGGTGCCCGCTGAGGTTCCCTCCACCCCTCCGGTTCACATGGAGGTCAAGGCCGACGCCCGATGCGCCGTCGTCGCCGCGGCCAGTGTTCTGGCCAAGGTCGAACGTGACCGCCTCATGGCCGATCTTGACGACCCGGGCTACGGGTGGGCGTCCAACAAGGGCTATGCCTCACCGGCCCACGTCCGGGGAATCACTGCCCTGGGGGCCAGTGACCAGCATCGACGCAGCTGGCACCTGCCCGGCCTGGATCAGCACCATGACCGAGGCGCCGTCTGA","VSPRGRTRPDRRLEKALLESHDYVGGLDEVGRGALAGPVSVGLAIVSRRTDDDFPTGLADSKQLTARARTGLIEPVRGWLVDHAVAHASPAEIDEHGIVAALRMAGLRALQQVADRGHAPRIIILDGVADWLTAPQPDLLTALEGAHVPETAPVPAEVPSTPPVHMEVKADARCAVVAAASVLAKVERDRLMADLDDPGYGWASNKGYASPAHVRGITALGASDQHRRSWHLPGLDQHHDRGAV$","Ribonuclease HII","Cytoplasm","ribonuclease HII","ribonuclease H ","Ribonuclease H","","","","","

InterPro
IPR001352
Family

Ribonuclease HII/HIII
PTHR10954	$\"[12-130]T$ $\"[159-230]T$	RIBONUCLEASE HII
PF01351	$\"[25-233]T$	RNase_HII

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[23-197]T$	no description

","BeTs to 25 clades of COG0164COG name: Ribonuclease HIIFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0164 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001352 (Ribonuclease HII/HIII) with a combined E-value of 9.1e-23. IPB001352A 26-40 IPB001352B 57-76 IPB001352C 169-189","Residues 24-119 are 64% similar to a (HII HYDROLASE ENDONUCLEASE NUCLEASE RIBONUCLEASE RNASE MANGANESE HIII LARGE SUBUNIT) protein domain (PD003015) which is seen in RNH2_STRAW.Residues 188-227 are 69% similar to a (HII HYDROLASE ENDONUCLEASE NUCLEASE RIBONUCLEASE RNASE MANGANESE LARGE SUBUNIT HI) protein domain (PD005501) which is seen in Q6AEA6_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 25 to 233 (E_value = 2.1e-31) place ANA_1186 in the RNase_HII family which is described as Ribonuclease HII.","","HII (rnhB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1188","1267469","1266270","1200","4.63","-29.06","42265","GTGCAGGATGGGACCGACGACGTCGGGCTGGACCTGAAGCAGGCCGATCCCTCTCAGATCGGTCGAACCTCCAGGTCCGCGATCACACCGGCCTGCACTTCCCCGTCCGCGGACTCCCCCCAGGAGAGTCGGCAGGCTGCTGAGACCGCAGGCGAGGCTCCGGTCGACGACAGCGACGAGTGGGACTACGACCCGTTCATCGACCCCGACGCCGAGCCTGAGCCCGATGAGGAGCTCACCGAGCTGCCTCCCTCTATCCAACCCCGCAGGCAGGTGGCCCCGGCCATCCCCCCGCCGCAGACCAGCCCCCTGTATCAGCGGGTGATCAGGCTGGTGCTCGTCGTCGCCGTCGTCATTCTGGTACCGGCGCTCCTGCGGGCCTACGTCGTCCAGATCTACGAGATCCCCTCGGGCTCCATGGAACGCACCCTGCGGGACGGGGACAAGGTCGCAGTCCCCATGTACGGCTCCGACAACGTCGAACGGGGTGACGTCATCGTCTTCTCCGATCCTGATGACTGGCTTCACGTCAAGGAACCGACGGGGCTGCGCGGCGCCACCCAGAGGCTCAAGGTCTTAGTGAACCTTCTGCCGGAGAACACCGGCCATCACCTCGTCAAACGGGTCATCGGTGTCGGTGGCGACCATGTGGTCGCCGACGGGAAGGGAACCCTGACCGTCAACGGCGTCGCGATCAAGGAGCCCTACGTCAAGGATGGTCAGTCCTCGTCCCTGACCTCCTTCGATGTCACCGTCCCCCAGGGCTATGTGTGGGTCATGGGGGACAACCGCTCCAACTCGGCCGACTCCCGCTACCACCGCGACGACGCCCACGGAGGCTTCGTGCCACTCAAGAACGTGGTCGGGGTGGCCAAGGTGGTCTTCCAGTGGACGCACCTGAGTCGCTGGGGGCTTCTGGGAGGAGGGGAGAGCGCTTTCTCAGACGTCCCGGCGCAAGAGACGACGCCGTCTGCGCGGCCCTCGCCTCCCCCTGCTCCGGCGAGCGACGGGGAGACGGCTTCCGAGGAGGAAGCACCCTCCCCGGTCCCCGAGGGCAGGGACTCCGAGGATGCAGGCGCTGTGGGAGAGGGGCACAGCAACGACGAGGCCCCACAGCCCACGACCGGCGGGTTGGCCGATGGCCCGGACACTTACGGCGGCATGGCCGACCAGGGGCAGCCTCCAGGGGGAACGAGGTGA","VQDGTDDVGLDLKQADPSQIGRTSRSAITPACTSPSADSPQESRQAAETAGEAPVDDSDEWDYDPFIDPDAEPEPDEELTELPPSIQPRRQVAPAIPPPQTSPLYQRVIRLVLVVAVVILVPALLRAYVVQIYEIPSGSMERTLRDGDKVAVPMYGSDNVERGDVIVFSDPDDWLHVKEPTGLRGATQRLKVLVNLLPENTGHHLVKRVIGVGGDHVVADGKGTLTVNGVAIKEPYVKDGQSSSLTSFDVTVPQGYVWVMGDNRSNSADSRYHRDDAHGGFVPLKNVVGVAKVVFQWTHLSRWGLLGGGESAFSDVPAQETTPSARPSPPPAPASDGETASEEEAPSPVPEGRDSEDAGAVGEGHSNDEAPQPTTGGLADGPDTYGGMADQGQPPGGTR$","Signal peptidase I","Membrane, Periplasm, Cytoplasm, Extracellular","signal peptidase I","signal peptidase I ","signal peptidase I","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Paetzel M., Dalbey R.E., Strynadka N.C. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature 1998. 396(6707):186-190. PMID: 9823901Bell C.E., Frescura P., Hochschild A., Lewis M. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. Cell 2000. 101(7):801-811. PMID: 10892750Luo Y., Pfuetzner R.A., Mosimann S., Paetzel M., Frey E.A., Cherney M., Kim B., Little J.W., Strynadka N.C. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell 2001. 106(5):585-594. PMID: 11551506Peat T.S., Frank E.G., Mcdonald J.P., Levine A.S., Woodgate R., Hendrickson W.A. The UmuD' protein filament and its potential role in damage induced mutagenesis. Structure 1996. 4(12):1401-1412. PMID: 8994967Mustard J.A., Little J.W. Analysis of Escherichia coli RecA interactions with LexA, lambda CI, and UmuD by site-directed mutagenesis of recA. J. Bacteriol. 2000. 182(6):1659-1670. PMID: 10692372Ferentz A.E., Walker G.C., Wagner G. Converting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C). EMBO J. 2001. 20(15):4287-4298. PMID: 11483531Mcdonald J.P., Peat T.S., Levine A.S., Woodgate R. Intermolecular cleavage by UmuD-like enzymes: identification of residues required for cleavage and substrate specificity. J. Mol. Biol. 1999. 285(5):2199-2209. PMID: 9925794Goldsmith M., Sarov-blat L., Livneh Z. Plasmid-encoded MucB protein is a DNA polymerase (pol RI) specialized for lesion bypass in the presence of MucA', RecA, and SSB. Proc. Natl. Acad. Sci. U.S.A. 2000. 97(21):11227-11231. PMID: 11016960Sutton M.D., Kim M., Walker G.C. Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage. J. Bacteriol. 2001. 183(1):347-357. PMID: 11114935","","","

InterPro
IPR000223
Family

Peptidase S26A, signal peptidase I
PR00727	$\"[128-144]T$ $\"[205-217]T$ $\"[252-271]T$	LEADERPTASE
TIGR02227	$\"[111-299]T$	sigpep_I_bact: signal peptidase I
PS00761	$\"[257-270]T$	SPASE_I_3

InterPro
IPR006198
Domain

Peptidase S24, S26A and S26B
PF00717	$\"[134-230]T$	Peptidase_S24

InterPro
IPR011056
Domain

Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10	$\"[123-320]T$	no description

InterPro
IPR014037
Family

Peptidase S26A
PTHR12383	$\"[118-175]T$ $\"[203-295]T$	PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED

noIPR
unintegrated

unintegrated
PTHR12383:SF1	$\"[118-175]T$ $\"[203-295]T$	SIGNAL PEPTIDASE I

InterPro
IPR001857
Family

Ribosomal protein L19
PD002979	$\"[19-100]T$	RL19_BACST_P30529;
PR00061	$\"[3-32]T$ $\"[33-62]T$ $\"[87-112]T$	RIBOSOMALL19
PTHR15680	$\"[1-114]T$	RIBOSOMAL PROTEIN L19
PF01245	$\"[1-113]T$	Ribosomal_L19
TIGR01024	$\"[1-113]T$	rplS_bact: ribosomal protein L19
PS01015	$\"[85-100]T$	RIBOSOMAL_L19

","BeTs to 18 clades of COG0335COG name: Ribosomal protein L19Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0335 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001857 (Ribosomal protein L19) with a combined E-value of 9.3e-64. IPB001857A 16-66 IPB001857B 73-111","Residues 19-100 are similar to a (RIBOSOMAL L19 50S CHLOROPLAST RIBONUCLEOPROTEIN PLASTID MITOCHONDRION MITOCHONDRIAL PEPTIDE PRECURSOR) protein domain (PD002979) which is seen in RL19_BACST.","","-73% similar to PDB:1P85 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 1.0E_30);-73% similar to PDB:1P86 Real space refined coordinates of the 50S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 1.0E_30);-73% similar to PDB:1VS6 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 50s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.0E_30);-73% similar to PDB:1VS8 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 1.0E_30);-73% similar to PDB:2AW4 Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 50S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 1.0E_30);","Residues 1 to 113 (E_value = 1.4e-75) place ANA_1189 in the Ribosomal_L19 family which is described as Ribosomal protein L19.","","protein L19 (rplS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1190","1269089","1268181","909","6.53","-3.66","32635","ATGAGCAGCGCACCCGACCAGAGCCCTCAGGGCAGGATCCATGTTGAGGTGGATGAGGACGTGACTTCGGGCAGGCATCTGCGGACCGACCATGACCGCCGGAATGGCCACCGGCACAAGGCCGGTGCCGGCGAGGACAGAGCCGGGGACAGCCAGGCCGCTGAGCCGGCCTCCTTGGGGGAGCGGATCGTCTTCCGTCTCAAGCAGTGGGGCATCACCTTGTCCTACCTGGTCGTCGCGGTGGCAATCATCGCCTTCATCCGCACCTTCATCATCCAGAGCTTCACCATCCCGTCGGGGTCGATGGAGAACACCCTCAACGAGGGCGACCGCGTCACGGTGACGATGTACGACTCCGACAAGGTCCACCGGGGTGACGTCGTCGTCTTCACTGATCCGGACCACTGGCTGACGACCCAGGAGCCCACCGGCCTGCAAGGCGCCGCGCAGGACTTCCTCGTCGCGATCCGTATCTTCCCCCAGAACGCCGGTCACCACCTCATCAAGCGGGTCATCGGAATGCCCGGTGACCACGTCGTCGCCGACGGGAAGGGCTCCTTGACGGTCAACGGCGTCGAGCTTCACGAGAGCTACCTCAAGCCCGGCCGGTCAGCCTCCGAGGTCGCCTTCGACGTCACCGTCCCCGAGGGCTACATCTGGGTCATGGGTGACAACCGCTCCAACTCCTCGGACTCCCGCTACCACCAGAACGATGTCCACCGCGGCTTCGTGCCCGTGGGCAACGTCGTCGGCGTCGCCAAGAACGTCGTGTGGCCATACTCCCACTGGTCCAGCCTCACCTCCGGCCAGGAGGTCTTCTCCCAGGTGCCCAAGCCGACGTCAACCCCTGCGGCTGTGCCCACCGGAGCGGCCGCGCCGGCGAGCAGGCTGGCGGGCTCCGGGGACTGA","MSSAPDQSPQGRIHVEVDEDVTSGRHLRTDHDRRNGHRHKAGAGEDRAGDSQAAEPASLGERIVFRLKQWGITLSYLVVAVAIIAFIRTFIIQSFTIPSGSMENTLNEGDRVTVTMYDSDKVHRGDVVVFTDPDHWLTTQEPTGLQGAAQDFLVAIRIFPQNAGHHLIKRVIGMPGDHVVADGKGSLTVNGVELHESYLKPGRSASEVAFDVTVPEGYIWVMGDNRSNSSDSRYHQNDVHRGFVPVGNVVGVAKNVVWPYSHWSSLTSGQEVFSQVPKPTSTPAAVPTGAAAPASRLAGSGD$","Signal peptidase I","Extracellular, Membrane, Cytoplasm","signal peptidase I","signal peptidase I ","signal peptidase I","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Paetzel M., Dalbey R.E., Strynadka N.C. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature 1998. 396(6707):186-190. PMID: 9823901Bell C.E., Frescura P., Hochschild A., Lewis M. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. Cell 2000. 101(7):801-811. PMID: 10892750Luo Y., Pfuetzner R.A., Mosimann S., Paetzel M., Frey E.A., Cherney M., Kim B., Little J.W., Strynadka N.C. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell 2001. 106(5):585-594. PMID: 11551506Peat T.S., Frank E.G., Mcdonald J.P., Levine A.S., Woodgate R., Hendrickson W.A. The UmuD' protein filament and its potential role in damage induced mutagenesis. Structure 1996. 4(12):1401-1412. PMID: 8994967Mustard J.A., Little J.W. Analysis of Escherichia coli RecA interactions with LexA, lambda CI, and UmuD by site-directed mutagenesis of recA. J. Bacteriol. 2000. 182(6):1659-1670. PMID: 10692372Ferentz A.E., Walker G.C., Wagner G. Converting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C). EMBO J. 2001. 20(15):4287-4298. PMID: 11483531Mcdonald J.P., Peat T.S., Levine A.S., Woodgate R. Intermolecular cleavage by UmuD-like enzymes: identification of residues required for cleavage and substrate specificity. J. Mol. Biol. 1999. 285(5):2199-2209. PMID: 9925794Goldsmith M., Sarov-blat L., Livneh Z. Plasmid-encoded MucB protein is a DNA polymerase (pol RI) specialized for lesion bypass in the presence of MucA', RecA, and SSB. Proc. Natl. Acad. Sci. U.S.A. 2000. 97(21):11227-11231. PMID: 11016960Sutton M.D., Kim M., Walker G.C. Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage. J. Bacteriol. 2001. 183(1):347-357. PMID: 11114935","","","

InterPro
IPR000223
Family

Peptidase S26A, signal peptidase I
PR00727	$\"[90-106]T$ $\"[167-179]T$ $\"[214-233]T$	LEADERPTASE
TIGR02227	$\"[73-261]T$	sigpep_I_bact: signal peptidase I
PS00761	$\"[219-232]T$	SPASE_I_3

InterPro
IPR006198
Domain

Peptidase S24, S26A and S26B
PF00717	$\"[96-192]T$	Peptidase_S24

InterPro
IPR011056
Domain

Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10	$\"[85-280]T$	no description

InterPro
IPR014037
Family

Peptidase S26A
PTHR12383	$\"[80-137]T$ $\"[165-267]T$	PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED

noIPR
unintegrated

unintegrated
PTHR12383:SF1	$\"[80-137]T$ $\"[165-267]T$	SIGNAL PEPTIDASE I
tmhmm	$\"[72-92]?$	transmembrane_regions

","BeTs to 19 clades of COG0681COG name: Signal peptidase IFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0681 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB000223 (Bacterial leader peptidase 1 (S26) family signature) with a combined E-value of 1e-29. IPB000223A 90-106 IPB000223B 167-179 IPB000223C 214-233","Residues 67-199 are 47% similar to a (I PEPTIDASE SIGNAL) protein domain (PDA119P1) which is seen in Q7NHQ4_GLOVI.Residues 101-233 are 45% similar to a (I PEPTIDASE SIGNAL HYDROLASE SPASE LEADER TRANSMEMBRANE PROTEASE S TYPE) protein domain (PD001438) which is seen in Q8EQZ6_OCEIH.Residues 134-242 are 56% similar to a (I PEPTIDASE SIGNAL) protein domain (PDA0K0F2) which is seen in Q6A7T2_PROAC.Residues 212-243 are 84% similar to a (PEPTIDASE I SIGNAL HYDROLASE PROTEASE LEADER SPASE TRANSMEMBRANE MEMBRANE PROBABLE) protein domain (PD522864) which is seen in Q6ADJ5_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 96 to 192 (E_value = 1.3e-09) place ANA_1190 in the Peptidase_S24 family which is described as Peptidase S24-like.","","peptidase I (lepB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1191","1270504","1269086","1419","5.62","-14.94","50791","GTGAGGATCGACGTCGTCACCATCTTCCCCGACTATCTCAAGGTCCTCGACCTCTCCCTCATCGGGAAGGCAGCCGACCGCGGCCCCCTCGACCTGCACGTCCACGATCTGCGCGACCACGCCCACGACCGGCACCGCACCGTCGATGACACGCCCCTGGGCGGTGGGGCCGGCATGGTCATGAAGCCTGACGTGTGGGGCGAGGCCCTCGATGAGGTGCTCGCCGCGGACAGCCCCGGAGTCGGCCGTCAGGTCCTCATCATCCCCACCCCCGCAGGTGAGGTCTTCACCCAGCGCACCGCCGAGGACCTGGCCGGCGCCGACCGCCTGGTCTTCGCCTGCGGCCGCTACGAGGGCATCGACGCGCGCGTGGCCGAGCACTACGCCTCCCGCGGCATCGAGGTGCGCGAGCTGAGCATCGGCGACTACGTGCTCAACGGGGGAGAGGTCGCCACCATTGTCATGATCGAGGCCATCGCCCGGCTCCTGCCCGGGGTCCTGGGCAACCCCGAGTCCCTGGTCGAGGAGTCCCACGGAGTCGCAGGCCTGCTGGAGTACCCCGTCCACACCCGCCCCACCCGGTGGCGAGATCTGGAGGTTGACCCCGTCCTGCTCTCCGGCGACCACGGCCGTATCGCCCGAGCCAGACGGGACCGGGCCCTCACCCGCACCGTTGAGCGTCGACCCGACATGATCCGGGCCCTGGACCCCGCCGGCCTGGATCGTGAGGACCGCGCGCTCCTGGCTCGCCTGGGGTGGGCGGTCCCGGCCGGGGCGGACCACCCGGTTCCGGTGCGCCTTCGCAACGCCACCGCCGACGACGCCCATGCCCTGGCCGAGCTCGCGGCCCGCACCTTCCCCGATGCCTGCGGCAACGTCATCGACCCCGAGTTCCTCGAGCGCCACATCGCCACGAACCTGGTTCCCGAGCTGTTCGCCACCTGGGCAGACGACGACCGCGTCGACCTCATTCTTGCCGAGCTGCTCGAGCCTTCATCGGTACAGGAACCCTCCCACGGGGCGCCAGCGGGCGCGAGCACTGCCCCGGCCCTGGTCGGCTACGCCGCAGTGCTGCGCGAGGAGGTCGACTCCGAGGGGGAACAGCCCCACGGGATCGATCCCCGCCCCGCCTGTGTGCGGCCTGTCGGGGGAGAGGTCGTCGGCGAGCTGTCCAAGGTGTACGTCGACGCCGCCATGAGGGGATCGGGACTGACCCCTGCGCTCATGGATGCCGTGATGCGCCAGGCCGCCGCCCATGGGACGAGCCTGCTCTGGCTCGGCACCCACGTCACCAATAAACGCGCCCAGAAGGCCTACAAGCGGGCCGGCTTCCGCCAGGTCGGCACCCGCACCTACAACGTCGGCGGCCAGGCCGCCCACGACGTCGTCATGACCCGGCGGACAGGAGAAGGCCTATGA","VRIDVVTIFPDYLKVLDLSLIGKAADRGPLDLHVHDLRDHAHDRHRTVDDTPLGGGAGMVMKPDVWGEALDEVLAADSPGVGRQVLIIPTPAGEVFTQRTAEDLAGADRLVFACGRYEGIDARVAEHYASRGIEVRELSIGDYVLNGGEVATIVMIEAIARLLPGVLGNPESLVEESHGVAGLLEYPVHTRPTRWRDLEVDPVLLSGDHGRIARARRDRALTRTVERRPDMIRALDPAGLDREDRALLARLGWAVPAGADHPVPVRLRNATADDAHALAELAARTFPDACGNVIDPEFLERHIATNLVPELFATWADDDRVDLILAELLEPSSVQEPSHGAPAGASTAPALVGYAAVLREEVDSEGEQPHGIDPRPACVRPVGGEVVGELSKVYVDAAMRGSGLTPALMDAVMRQAAAHGTSLLWLGTHVTNKRAQKAYKRAGFRQVGTRTYNVGGQAAHDVVMTRRTGEGL$","tRNA (guanine-N1)-methyltransferase","Cytoplasm","tRNA (Guanine-N(1)-)-methyltransferase(M1G-methyltransferase) (tRNA [GM37] methyltransferase)","tRNA (guanine-N1)-methyltransferase ","tRNA (guanine-N1)-methyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[343-445]T$	Acetyltransf_1
PS51186	$\"[265-469]T$	GNAT

InterPro
IPR002649
Family

tRNA (guanine-N1-)-methyltransferase
PD004978	$\"[47-232]T$	Q8CY56_BIFLO_Q8CY56;
PF01746	$\"[21-229]T$	tRNA_m1G_MT
TIGR00088	$\"[1-244]T$	trmD: tRNA (guanine-N1)-methyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.40.1280.10	$\"[1-167]T$	no description
G3DSA:3.40.630.30	$\"[263-467]T$	no description

","BeTs to 18 clades of COG0336COG name: tRNA-(guanine-N1)-methyltransferaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0336 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002649 (tRNA (guanine-N1-)-methyltransferase) with a combined E-value of 7.5e-93. IPB002649A 19-61 IPB002649B 86-124 IPB002649C 137-174 IPB002649D 182-231","Residues 47-232 are 73% similar to a (TRNA METHYLTRANSFERASE TRANSFERASE PROCESSING GUANINE-N1--METHYLTRANSFERASE M1G- GM37 GUANINE-N1-METHYLTRANSFERASE TRNA-GUANINE-N1-METHYLTRANSFERASE 24-CYCLODIPHOSPHATE) protein domain (PD004978) which is seen in Q8CY56_BIFLO.","","-54% similar to PDB:1OY5 Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus (E_value = 3.5E_31);-51% similar to PDB:1P9P The Crystal Structure of a M1G37 tRNA Methyltransferase, TrmD (E_value = 7.9E_31);-49% similar to PDB:1UAJ Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition (E_value = 7.4E_29);-49% similar to PDB:1UAK Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition (E_value = 7.4E_29);-49% similar to PDB:1UAL Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition (E_value = 7.4E_29);","Residues 21 to 229 (E_value = 8e-58) place ANA_1191 in the tRNA_m1G_MT family which is described as tRNA (Guanine-1)-methyltransferase.Residues 343 to 445 (E_value = 1.1e-12) place ANA_1191 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","(Guanine-N(1)-)-methyltransferase (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (guanine-N1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1192","1271049","1270501","549","4.50","-17.29","19233","GTGCTGCTCACCGTTGCTGTCATCGGTCCCGCCCATGCCCTCAAGGGCGAGGTGCGGCTCGAGATCCGTACCGATGACCCCGAGGGGCGTCTCGCACCCGGAACCACTATCCCCACGGAGCCGGCCCACGCAGGCCCGCTGACGGTCAGCCGTCTGCGTTTCGACGGTTCGCGCTGGTTCGCCGCCTTCGAGCAGGCGCGTGACCGCACGGCCGCTGAGGCCCTGCGAGGAGTGAGGCTCCTGGTCGAGACCGACGACGACGCCCCTGGCGGTGAGGGCTCTGAGGAGTCCGAGGAGGCCTGGTACCGCCACGAGCTCGTCGGTCTACGAGCGCTGAGCGTCTCCGGTGAGGAACTGGGAGAGGTCACTGACGTAGAGCCCGGCGTCGCCCAGGACCGGCTCGTGGTCACCACCCCTGAGGGGGACGATGTGGCCGTGCCCTTCGTTGAGGTTCTCGTACCGGCCATCGACCCCGAGGCCGGCACCGTGACGCTGGCCCCACCCGGTGGCCTGTTTCCCGGACGCGGCCAGGCGGAGGAGGCCCGGTGA","VLLTVAVIGPAHALKGEVRLEIRTDDPEGRLAPGTTIPTEPAHAGPLTVSRLRFDGSRWFAAFEQARDRTAAEALRGVRLLVETDDDAPGGEGSEESEEAWYRHELVGLRALSVSGEELGEVTDVEPGVAQDRLVVTTPEGDDVAVPFVEVLVPAIDPEAGTVTLAPPGGLFPGRGQAEEAR$","16S rRNA processing protein RimM","Cytoplasm","possible Rim-like protein involved in efficientprocessing of 16S rRNA","16S rRNA processing protein RimM","16S rRNA processing protein RimM","","Bylund G.O., Wipemo L.C., Lundberg L.A., Wikstrom P.M. RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli. J. Bacteriol. 1998. 180(1):73-82. PMID: 9422595","","","

InterPro
IPR002676
Domain

RimM protein
PF01782	$\"[4-86]T$	RimM

InterPro
IPR007903
Domain

PRC-barrel
PF05239	$\"[98-172]T$	PRC

InterPro
IPR011961
Family

16S rRNA processing protein RimM
TIGR02273	$\"[2-171]T$	16S_RimM: 16S rRNA processing protein RimM

","BeTs to 11 clades of COG0806COG name: RimM protein, required for 16S rRNA processingFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0806 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB007903 (PRC-barrel) with a combined E-value of 1.1e-12. IPB007903A 5-25 IPB007903B 98-111 IPB007903C 119-136","Residues 3-58 are 66% similar to a (RRNA PROCESSING 16S RIMM PROBABLE) protein domain (PD343630) which is seen in RIMM_STRCO.Residues 63-171 are 55% similar to a (PROCESSING RRNA 16S RIMM PROBABLE ARABIDOPSIS RNA CHROMOSOME GENOMIC RELATED) protein domain (PD358463) which is seen in RIMM_COREF.","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 86 (E_value = 1.7e-11) place ANA_1192 in the RimM family which is described as RimM N-terminal domain.Residues 98 to 172 (E_value = 6.5e-08) place ANA_1192 in the PRC family which is described as PRC-barrel domain.","","Rim-like protein involved in efficient processing of 16S rRNA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1193","1271597","1271361","237","7.29","0.18","8513","ATGCTGGCCGACGCCCTCGAGCACCTCGTACGGGGCATTGTCGACAACCCTGACGACGTCACCGTCACCTCCCGATCGCTGCGCCGCGGCGACCTGTTGGAGGTGCGGGTCAATCCCGAGGACCTCGGCCGAGTCATCGGCCGCTCGGGCCGTACTGCTCGAGCACTGCGCACAGTGGTCGGAGCGCTGGCGGACTCGCCGGTGCGCGTCGACGTCGTCGACACCGACCGCCGCTGA","MLADALEHLVRGIVDNPDDVTVTSRSLRRGDLLEVRVNPEDLGRVIGRSGRTARALRTVVGALADSPVRVDVVDTDRR$","RNA-binding protein","Cytoplasm","Hypothetical UPF0109 protein-related protein","hypothetical protein","RNA-binding protein (contains KH domain)-like","","Burd C.G., Dreyfuss G. Conserved structures and diversity of functions of RNA-binding proteins. Science 1994. 265(5172):615-621. PMID: 8036511Musco G., Kharrat A., Stier G., Fraternali F., Gibson T.J., Nilges M., Pastore A. The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome. Nat. Struct. Biol. 1997. 4(9):712-716. PMID: 9302998Baber J.L., Libutti D., Levens D., Tjandra N. High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor. J. Mol. Biol. 1999. 289(4):949-962. PMID: 10369774Grishin N.V. KH domain: one motif, two folds. Nucleic Acids Res 2001. 29(3):638-643. PMID: 11160884","","","

InterPro
IPR004088
Domain

KH, type 1
PS50084	$\"[30-78]T$	KH_TYPE_1

","BeTs to 11 clades of COG1837COG name: Predicted RNA-binding protein (KH domain)Functional Class: R [General function prediction only]The phylogenetic pattern of COG1837 is -------qvdrlbc------u--it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 2-63 are similar to a (RNA-BINDING UPF0109 DOMAIN KH BINDING RNA ALR1954 LP_1637 DR2009 LMO1796/LIN1910) protein domain (PD009089) which is seen in YJJ2_STRCO.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","UPF0109 protein-related protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1194","1272351","1271599","753","7.76","1.33","26488","GTGAATCAATCGGCGTGGTGTACCGCTGAAGGGGCGCGCAAGCTCGGAGTCGACGTCGCCTGTGGGCGATCTCGCACCGAGTGGCGGGGTGGTGTCCCGGCTCGGGCTGGCGACCTCCTCGGAGGCTCTGGCAGAATGTCTGGCTGTACTCGGTCGGACGTCGGTCCCTCTCCCGACCCCGGTCGCGTCTCGGCTCACGCCGGAAACCGTTGCTTGACCCCACCGGGGACCAGCGCGCGCCAAACCATCCAGAACCAGGAGTTCAACCAAGTGGCAGTCAAGATTCGCCTCAAGCGCATGGGCAAGAAGTTCGCCCCCTTCTACCGGGTCGTCGTCCTCGACTCCCGCAAGAAGCGCGATGGCCGTGTCATTGAGGAGATCGGCGTCTACGACCCGATGCAGGAGCCCTCGCTCATCAGCATCGACTCCGAGCGCGTCCAGTACTGGCTCGGCGTGGGCGCTCAGCCCTCCGACGCTGTCTACAAGCTGATCAAGATCACCGGCGACTATCACCAGTTCAAGGGCCTCAAGGGTGTCGAGAGCACCCTCAAGGTCAAGGACGCCGACGCCGCCGCGGTCGCCAAGGAGGCCGCGGTCAAGGCCGCCGCCGACGACGCTGAGAAGCGCAAGGCCGCCGCGGCCAAGGCCAAGGCTGACGAGGAGGCCGCTGCAGCGGCCGAGGCCGCCGAGTCCAAGGCTGAGGATTCCGCTGAGGACCAGGCCTCTGATGAGGCCGTCGCCGAGGAGGCCTGA","VNQSAWCTAEGARKLGVDVACGRSRTEWRGGVPARAGDLLGGSGRMSGCTRSDVGPSPDPGRVSAHAGNRCLTPPGTSARQTIQNQEFNQVAVKIRLKRMGKKFAPFYRVVVLDSRKKRDGRVIEEIGVYDPMQEPSLISIDSERVQYWLGVGAQPSDAVYKLIKITGDYHQFKGLKGVESTLKVKDADAAAVAKEAAVKAAADDAEKRKAAAAKAKADEEAAAAAEAAESKAEDSAEDQASDEAVAEEA$","Ribosomal protein S16","Cytoplasm, Periplasm","ribosomal protein S16, putative","30S ribosomal protein S16","ribosomal protein S16","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000307
Family

Ribosomal protein S16
PD003791	$\"[101-168]T$	RS16_THETN_Q8R9X1;
G3DSA:3.30.1320.10	$\"[92-178]T$	no description
PTHR12919	$\"[92-231]T$	30S RIBOSOMAL PROTEIN S16
PF00886	$\"[99-157]T$	Ribosomal_S16
TIGR00002	$\"[93-170]T$	S16: ribosomal protein S16
PS00732	$\"[93-102]T$	RIBOSOMAL_S16

noIPR
unintegrated

unintegrated
PTHR12919:SF4	$\"[92-231]T$	30S RIBOSOMAL PROTEIN S16

","BeTs to 19 clades of COG0228COG name: Ribosomal protein S16Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0228 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000307 (Ribosomal protein S16) with a combined E-value of 1.2e-33. IPB000307A 92-132 IPB000307B 149-160***** IPB010528 (TolA) with a combined E-value of 6.3e-11. IPB010528B 210-240 IPB010528A 199-247 IPB010528A 200-248 IPB010528A 186-234 IPB010528A 190-238 IPB010528A 184-232 IPB010528A 185-233 IPB010528A 195-243 IPB010528A 191-239 IPB010528A 175-223 IPB010528A 183-231 IPB010528A 187-235 IPB010528A 173-221 IPB010528A 198-246 IPB010528A 196-244 IPB010528A 182-230 IPB010528A 192-240 IPB010528A 194-242 IPB010528A 193-241 IPB010528A 201-249 IPB010528A 179-227 IPB010528A 176-224 IPB010528A 188-236 IPB010528A 189-237 IPB010528A 174-222 IPB010528A 180-228 IPB010528A 181-229 IPB010528A 202-250 IPB010528A 206-250 IPB010528A 205-250 IPB010528A 177-225 IPB010528A 171-219 IPB010528A 178-226 IPB010528A 197-245 IPB010528A 168-216 IPB010528B 196-226 IPB010528B 203-233 IPB010528B 195-225 IPB010528B 211-241 IPB010528B 202-232 IPB010528B 188-218 IPB010528B 190-220 IPB010528B 205-235 IPB010528B 194-224 IPB010528B 204-234 IPB010528B 193-223 IPB010528B 201-231 IPB010528B 217-247 IPB010528B 187-217 IPB010528B 215-245 IPB010528B 186-216 IPB010528B 198-228 IPB010528B 192-222 IPB010528B 197-227 IPB010528B 208-238 IPB010528B 206-236 IPB010528B 212-242 IPB010528B 179-209 IPB010528B 207-237 IPB010528B 200-230 IPB010528B 209-239 IPB010528B 220-250 IPB010528B 219-249 IPB010528B 181-211 IPB010528B 218-248 IPB010528B 189-219 IPB010528B 182-212 IPB010528B 216-246 IPB010528B 213-243 IPB010528B 221-250 IPB010528B 185-215","Residues 91-163 are 57% similar to a (RIBOSOMAL MITOCHONDRION PROBABLE S24 MITOCHONDRIAL) protein domain (PD765604) which is seen in RT24_SCHPO.Residues 91-164 are 70% similar to a (RIBOSOMAL S16 AT4G34620/T4L20_200) protein domain (PD057814) which is seen in O65686_ARATH.Residues 91-175 are similar to a (RIBOSOMAL S16 30S) protein domain (PDA105C8) which is seen in Q6A7S4_PROAC.Residues 91-165 are 75% similar to a (RIBOSOMAL S16 30S) protein domain (PD167364) which is seen in RS16_TREPA.Residues 91-167 are 68% similar to a (RIBOSOMAL S16 30S) protein domain (PDA0K4X0) which is seen in Q6MDH0_PARUW.Residues 91-165 are 67% similar to a (RIBOSOMAL S16 30S) protein domain (PDA0K4W5) which is seen in RS16_WOLPM.Residues 91-185 are similar to a (RIBOSOMAL S16 30S) protein domain (PDA0K4X3) which is seen in Q6AE98_BBBBB.Residues 101-168 are 69% similar to a (RIBOSOMAL S16 30S CHLOROPLAST SEQUENCING MITOCHONDRION CEREVISIAE Q02608 YPL013C DIRECT) protein domain (PD003791) which is seen in RS16_THETN.","","-69% similar to PDB:1EMW SOLUTION STRUCTURE OF THE RIBOSOMAL PROTEIN S16 FROM THERMUS THERMOPHILUS (E_value = 1.2E_18);-69% similar to PDB:1FJG STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN (E_value = 1.2E_18);-69% similar to PDB:1HNW STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH TETRACYCLINE (E_value = 1.2E_18);-69% similar to PDB:1HNX STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH PACTAMYCIN (E_value = 1.2E_18);-69% similar to PDB:1HNZ STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH HYGROMYCIN B (E_value = 1.2E_18);","Residues 99 to 157 (E_value = 3.2e-31) place ANA_1194 in the Ribosomal_S16 family which is described as Ribosomal protein S16.","","protein S16, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1195","1272414","1273946","1533","6.72","-2.38","54596","ATGAGGCTTATCCCCTTCGGTAACCGCGGCATCCAGCCGCCTGGCAAGAGCTCATCGATCCGACCGCCACGCTCCGGACAGGGCACTCCGACGTCGGTCCGTCCTCCCAGCACCCCCTCGACGGACGGACTGCCCCCAGCCGCCCACCACGAAGGCGCCACAACCGGACCGAAGCACACCCGGCGCACCCCACAGCCCCTGACCGGGAACGTGCGGGCCATCAAGCCCCGCCACGCAGTAGGGCTGTGGCCCGCGGTCCTTCTTGGAACCTTCTGCGTGGCGGCACTGGTCATTGCTGGGCGAGTGGCCGTGGACTCCATGTCACCCGCTGCGCCGAGCGCCTCCCCTCCACCACCTCCACCTGCCTCCTGCGAGATGGAAGGACATCAAACGGAAGGCTCTTCATGGAAGGAGACGTGGAGTCTTGACACCGGTCTCCCGGCGTGGAAGAAAAATTTTACGTGGGACACGTACTCGTGCGGACACTATATCGTTGTCATTCACCACAAGAACGACGATACAACAGACCTGATGGGATTCCACATTGAAGGCAATACACCCAAGAAGATCTGGTCGACGTCGCTAGGATATACGTTCACCACCGGCTACCGACATTGGTGGGGAGGGCACCTGCTACTGAACGGCCAGGTTCTTGACCCAACAACAGGAAAGACGACTGAACTCCCAACGGGTCTCCAGTCTTTAACCTTCGTCGCCAATGACAACACAGCCGTCTCATGCAGTTCCTCGTACTCGGACGCGAACAGCACCTGCACGGGTTGGGACTGGAATAATGGAGAGCCGGCTCAGCGCTGGCAGCAGACCTATGACTTCACGTCAGTCCACCCGCTCTGGCACCATGCCGATGGAACACCGTCTTCAGAGTCGATCGCGATGTCCGTTGAAAACTCCCCCAAAGACTCTTCCAGCATCGGAGTTCTTTCGACGAGCGACGGCTCCCTTGTGACCCTCTCACCGGAAAAGAACAGTCAAGGGCACCCCATTCAACTGCTTTCCGCCAGCGACGGCTGGGTCACCATCGATCCAGACAGCTCGTCAGCGTTCACCTTCTCCAAGAATGGGTCACCCGCGGAGTCCTTCACCCTCAGGGGCTCCACTGCGTCCCTCCTCATCAAGGATGGTCAGCAACCCTCACTGTCCCAGTTCAGGGCCGCTTACGAGTCGGGCGACACGAGCTGGGCCGATATCGACCTCACCTGCACCGATGCCACGCACTGCAGTCTCAATGGAAACCCATTGACGCTGTCCGACGACGTAGCCACGTGGAACACCCCGGCCCGTGCGCAGTTCCAGAGCTCCTGGAAACTGAGTACCGACAAGCGCACGCTCACCATACGCGGCCGCTCCGCCAGCAGTGAGATCGGTGCGGTGCTCATGATCGACACGGCCTCAAAGACGCAGATGGCTCCTCTGCCCATCACATCCCGTGGAGCAGTCATCCCCGTCTGGCGCCAGGATTTCATTATCGCGATCGAGGGCTCCACATTGGTCGGCTATGCACCGCAGTCCTGA","MRLIPFGNRGIQPPGKSSSIRPPRSGQGTPTSVRPPSTPSTDGLPPAAHHEGATTGPKHTRRTPQPLTGNVRAIKPRHAVGLWPAVLLGTFCVAALVIAGRVAVDSMSPAAPSASPPPPPPASCEMEGHQTEGSSWKETWSLDTGLPAWKKNFTWDTYSCGHYIVVIHHKNDDTTDLMGFHIEGNTPKKIWSTSLGYTFTTGYRHWWGGHLLLNGQVLDPTTGKTTELPTGLQSLTFVANDNTAVSCSSSYSDANSTCTGWDWNNGEPAQRWQQTYDFTSVHPLWHHADGTPSSESIAMSVENSPKDSSSIGVLSTSDGSLVTLSPEKNSQGHPIQLLSASDGWVTIDPDSSSAFTFSKNGSPAESFTLRGSTASLLIKDGQQPSLSQFRAAYESGDTSWADIDLTCTDATHCSLNGNPLTLSDDVATWNTPARAQFQSSWKLSTDKRTLTIRGRSASSEIGAVLMIDTASKTQMAPLPITSRGAVIPVWRQDFIIAIEGSTLVGYAPQS$","Hypothetical protein","Extracellular, Periplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[80-100]?$	transmembrane_regions

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[163-204]T$	Q9F341_STRCO_Q9F341;
PF00005	$\"[53-237]T$	ABC_tran
PS50893	$\"[28-261]T$	ABC_TRANSPORTER_2
PS00211	$\"[162-176]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[52-238]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[21-250]T$	no description
PTHR19222	$\"[28-250]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[28-250]T$	ABC TRANSPORTER

","BeTs to 15 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.2e-27. IPB005074C 42-89 IPB005074D 150-193***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.4e-25. IPB013563A 42-76 IPB013563C 159-186 IPB013563D 213-265***** IPB005116 (TOBE domain) with a combined E-value of 7.8e-18. IPB005116A 60-76 IPB005116B 98-115 IPB005116C 162-175 IPB005116D 182-201 IPB005116E 215-228***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3.7e-11. IPB010509B 53-78 IPB010509D 157-201***** IPB010929 (CDR ABC transporter) with a combined E-value of 3.1e-07. IPB010929A 52-71 IPB010929C 144-177 IPB010929D 178-206***** IPB000897 (GTP-binding signal recognition particle (SRP54) G-domain) with a combined E-value of 9.4e-06. IPB000897A 55-70","Residues 8-241 are 43% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 23-125 are 48% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA188U2) which is seen in Q9RXA9_DEIRA.Residues 23-125 are 53% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 23-255 are 42% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 26-262 are 46% similar to a (C24F3.5 ATP-BINDING) protein domain (PD574736) which is seen in Q21213_CAEEL.Residues 30-114 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 31-93 are 67% similar to a (ATP-BINDING PLASMID TRANSPORTER PEPTIDE FR) protein domain (PDA18258) which is seen in Q6W139_RHISN.Residues 38-262 are 44% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 39-217 are 49% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 43-123 are 62% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187K3) which is seen in Q897D7_CLOTE.Residues 43-89 are 89% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q6AAQ3_PROAC.Residues 43-269 are 45% similar to a (TRANSPORTER-LIKE ABC ATP-BINDING) protein domain (PD635134) which is seen in Q8SQU5_EEEEE.Residues 43-249 are 49% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 48-221 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 56-274 are 48% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 128-252 are 48% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 132-250 are 53% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 145-256 are 50% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 155-240 are 59% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 161-267 are 55% similar to a (PROBABLE ATP-BINDING ABC TRANSPORTER ATP BINDING) protein domain (PD763654) which is seen in Q8G625_BIFLO.Residues 220-330 are 58% similar to a (ATP-BINDING ABC TRANSPORTER YVFR SYSTEM ATP SUBUNIT BINDING) protein domain (PD060250) which is seen in Q6NFA4_CORDI.","","-49% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 3.4E_22);-49% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 3.4E_22);-48% similar to PDB:1G29 MALK (E_value = 2.9E_21);-48% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 2.9E_21);-48% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 3.2E_20);","Residues 53 to 237 (E_value = 5.8e-52) place ANA_1196 in the ABC_tran family which is described as ABC transporter.","","transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1197","1275132","1276016","885","10.77","11.59","31124","ATGACCGCGACATCCCAGACACCCTCTGATTCCTCAGCATCCGAGTCCCCTGTCGATCCCGACGCGGGCAAGCTCGTAGGCCGATCACCTCGCCCGGGAAGGCTCAGGCCCGCGCGCCCTGTCCTGACCTACCTCCGGCTCGACCTGTTACGGAGCCTGCGCGAGCCGGCCAACCTCTTCTTCGTCGTCACCTTCCCTCTGGCGATGTACCTCGTCTTCGGCCGGTTGAACGCGTCGGCCGGGAACTACGGCCCGCACGCTCACGGCAATGTCTCGGCCTCGGTGATGCTCGCGATGGCCTCCTTCAGCGCCTGTCTGGGTGCCACGAGTGCCTCGGCGGCGGCCGCTGTCGAGCAGTCGGCGGGCTGGGGCCGGCAGATGGCGGTCACCTCCCGGGGCCTGCGCGGCTACCTGGTGGTCAAGACCGGAACCGCGGTGGGAACGGCGGCTCTTCCGGTCACCGTGGTCCTCACCGCCGGGGCACTGACGGACTCGAGCATGGAGGGCTGGGTCTGGGGCGTCAGTCCCTTCATCTGCCTGATCGGGGTTCTGCCCTTCGTCCTGTGGGGTCTGGCCGCCGGGATGTGGCTGCCGTCCTCGGCATCGATCGGTATCGCGACCTCCTTGGTCTCCTTGTTCGCCTTCATCGGCAACACCTTCATGCCCCTGAGCCACACACTGTTGACGATCAGTCGCTTCACCCCGATGTACGGGGCAACGGCGCTGGCCCGGTGGCCGCTGGGTGAGGGGTGGGCCTACGTGCCGGATCGGCAAGCGGGTGTTCAGGACCCGTTGTGGATGCCGTTGGCTAACCTGGTGGTGTGGACACTCATCTTCGGGCTGCTGGTGATCGGGGCTCGACGTCGGGCGACCAGGCGCCGGTGA","MTATSQTPSDSSASESPVDPDAGKLVGRSPRPGRLRPARPVLTYLRLDLLRSLREPANLFFVVTFPLAMYLVFGRLNASAGNYGPHAHGNVSASVMLAMASFSACLGATSASAAAAVEQSAGWGRQMAVTSRGLRGYLVVKTGTAVGTAALPVTVVLTAGALTDSSMEGWVWGVSPFICLIGVLPFVLWGLAAGMWLPSSASIGIATSLVSLFAFIGNTFMPLSHTLLTISRFTPMYGATALARWPLGEGWAYVPDRQAGVQDPLWMPLANLVVWTLIFGLLVIGARRRATRRR$","ABC-type multidrug transport system, permease component","Membrane, Extracellular","putative ABC transporter integral membraneprotein","K01992 ABC-2 type transport system permease protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[58-78]?$ $\"[97-117]?$ $\"[172-192]?$ $\"[198-216]?$ $\"[226-246]?$ $\"[265-285]?$	transmembrane_regions

","BeTs to 3 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","No significant hits to the Blocks database.","Residues 95-195 are similar to a (ABC PERMEASE TRANSPORTER MEMBRANE ATP-BINDING TRANSPORTER TRANSMEMBRANE PROTEIN COMPONENT INTEGRAL) protein domain (PD115342) which is seen in Q6AAQ2_PROAC.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","ABC transporter integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1198","1276031","1277245","1215","9.19","5.83","43825","ATGCCGCAGCCTCTGCGTGACTCAGCCGACCTGACGGCATCATCGTCTGGGGCAGGGCGGTCCGGTTCCCGCCCCTGGCACCGCTATCGCCGTCATATCGTCTGGGACGCCACAGTATGGGTGCTGTTCCTAGCCCTTCCCATCATCCAGCTTCTCCTCGGCTCCTTCGCCTGGTGGGAGCGTCTGCTGGGGCTGACCGGCGTGCTGGGGTTCATCGCCGGCTACGTCTGGGCGTTTTCGACGCCGGACAACCGCGCATCGAGGGTCGGAGTCCCTCCTCCTGACCTCCGGACTCGCATTCTCCTCAGAGAGCTCGCGGTCCAGGCCTTCTTCACCGTACTGACGCTGCCGGCACTGGGATGGTGGACGATCTGCTTCTTCCCCTTCTTCTGCTCGTTGGTCCTGTTCTCCACGACATTGCGCCAGGGCATCCCCACCGTCGTCATGGCGACGGGGCTTCTGGTTGCCGCCTCGCTGTTATGGAACACGCATCCAGAGTCGCACTGGCAGGTACTGGGCATATCGCTCACCGAGGTTCCCATCATCATCGCCCGCATCGCGGTGGAGCTCCAGGAGCGCAGAACAGCCGCCGAGCGCGAGCTCGCCCTTGTCTCCCAGCGAGAGGCGCTCGGGCGCGACGTCCACGACATCTTGGGGCACTCCTTGACAGTGCTCACTCTCAAGGCCGAGGTCGCCCGCCGGCTCATCGAGCGTGACCCGGCCGCCGCATCCCGGGAGCTCGACGAAGTCATCACGCTGGCCCGTGGAGCCCTTGCCGACGTGCGCTCCACGGTGACACGCCTGCGGTCCCCGGACCTGGCCAGCCAGGTGGAGGCCACGCGTACCGCCTTGAGCGCCGCCCGGATCCGTGTGGAGGTGACCGGTAGTGCCCAGGACATTCCTGAGCGTCAGCGTGCCCTCATGGCCTGGGCCTTGCGTGAGGCCACCACGAACGTCGTCCGGCACGCGAAGGCGGCCACTGTGGCAGTGCATCTGGAGCCGGGGCTGCTGCGGGTGAGCGATGACGGTGTCGGCCTGGCCGGTGACCAGCCCGGCAACGGCTTGGCGGGCCTGCGTGCCCGTTGCGAGCAGGAGGGCGGTTCCCTCACCATGACCAGTCCGCTCACGCCTCGCACTGACTCATCCGGCGCCGGCACGACAGACACCGCTGGCGTGACGACCGGCGGAACCAGACTGGAGGTGAGGCTGCCGTGA","MPQPLRDSADLTASSSGAGRSGSRPWHRYRRHIVWDATVWVLFLALPIIQLLLGSFAWWERLLGLTGVLGFIAGYVWAFSTPDNRASRVGVPPPDLRTRILLRELAVQAFFTVLTLPALGWWTICFFPFFCSLVLFSTTLRQGIPTVVMATGLLVAASLLWNTHPESHWQVLGISLTEVPIIIARIAVELQERRTAAERELALVSQREALGRDVHDILGHSLTVLTLKAEVARRLIERDPAAASRELDEVITLARGALADVRSTVTRLRSPDLASQVEATRTALSAARIRVEVTGSAQDIPERQRALMAWALREATTNVVRHAKAATVAVHLEPGLLRVSDDGVGLAGDQPGNGLAGLRARCEQEGGSLTMTSPLTPRTDSSGAGTTDTAGVTTGGTRLEVRLP$","Two-component system sensor kinase","Membrane, Cytoplasm","two-component system sensor protein","two-component system sensor protein","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[303-404]T$	HATPase_c
SM00387	$\"[303-404]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[206-273]T$	HisKA_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-78]?$	signal-peptide
tmhmm	$\"[36-56]?$ $\"[62-80]?$ $\"[118-136]?$ $\"[142-162]?$	transmembrane_regions

","BeTs to 9 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 6.2e-15. IPB011712A 205-222 IPB011712B 308-328 IPB011712C 339-348","Residues 206-292 are similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM TRANSFERASE 2.7.3.- SENSORY TRANSDUCTION NITRATE/NITRITE) protein domain (PD288674) which is seen in Q8PFI7_XANAC.Residues 283-371 are 52% similar to a (KINASE REGULATOR HISTIDINE RESPONSE PROBABLE FAMILY GAF) protein domain (PD771047) which is seen in Q7VET1_MYCBO.Residues 312-369 are 65% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM SENSORY TRANSFERASE TRANSDUCTION 2.7.3.- TWO) protein domain (PD005700) which is seen in Q6AAQ0_PROAC.","","No significant hits to the PDB database (E-value < E-10).","Residues 206 to 273 (E_value = 8.9e-20) place ANA_1198 in the HisKA_3 family which is described as Histidine kinase.Residues 303 to 404 (E_value = 2e-06) place ANA_1198 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","system sensor protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1199","1277242","1277853","612","4.93","-9.36","21437","GTGAGCCCGATCCGCGTGCTCATCGCCGATGACCAGGCACTCGTGCGCGGTGCTTTGGCGACGCTCCTGGGGCTCGAGAGCGATCTGGAGGTCGTGGCCCAGGTGGGGCGGGGCGACGAGGTCCTGGACGCAGTGCGCGAGCACACCGTGGATGTGGCCCTGGTGGATATCGACATGCCGGGGCGCGACGGGCTGGCGGCCACCGCCGAGGTCGTCGACTCGGATCTGCCGTGCCGGTGCCTCATCGTGACGACCTTCGGTCGCCCGGGCTATCTCTCACGGGGCATGGAGGCAGGGGCTGCGGGCTTCATCGTCAAGGACACCCCTCCCGAGGCGCTGGCTGAGGCGATCCGCAAGGTTCACGCGGGCCTGCGGGTCATCGACCCCGAGCTCGCCCAGGAGTCGGTGCTGCTCGGGCCGAACCCGCTGACCGAGCGGGAGAAGGAGGTTCTGCTGGCGGCGGCCACGGGTGCGGAGGCCCGAGAGATCGCCACCCGGCTGAGCCTGGGTGAGGGCACGGTGCGCAACTACCTGTCCTCGGCGATCGCCAAGACCCACGCCCGCAACCGCACCGAGGCGGCCCGCACCGCCGAGACCAACGGCTGGTTGTGA","VSPIRVLIADDQALVRGALATLLGLESDLEVVAQVGRGDEVLDAVREHTVDVALVDIDMPGRDGLAATAEVVDSDLPCRCLIVTTFGRPGYLSRGMEAGAAGFIVKDTPPEALAEAIRKVHAGLRVIDPELAQESVLLGPNPLTEREKEVLLAAATGAEAREIATRLSLGEGTVRNYLSSAIAKTHARNRTEAARTAETNGWL$","Two-component system response regulator","Cytoplasm","luxR family two component system responseregulator","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[142-184]T$	Q82IK1_STRAW_Q82IK1;
PR00038	$\"[143-157]T$ $\"[157-173]T$ $\"[173-185]T$	HTHLUXR
PF00196	$\"[140-197]T$	GerE
SM00421	$\"[140-197]T$	HTH_LUXR
PS50043	$\"[136-201]T$	HTH_LUXR_2
PS00622	$\"[157-184]?$	HTH_LUXR_1

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[4-120]T$	Q6AAP9_PROAC_Q6AAP9;
PF00072	$\"[4-118]T$	Response_reg
SM00448	$\"[4-117]T$	REC
PS50110	$\"[5-121]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[141-203]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[4-130]T$	no description
PTHR23283	$\"[5-74]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF49	$\"[5-74]T$	TWO-COMPONENT SENSOR PROTEIN HISTIDINE PROTEIN KINASE (DHKK, DHKJ)

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000673 (CheB methylesterase) with a combined E-value of 2.8e-16. IPB000673A 7-16 IPB000673B 23-76 IPB000673C 77-107***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 7.8e-16. IPB000792 143-189***** IPB005143 (Autoinducer binding domain) with a combined E-value of 1.7e-09. IPB005143B 143-186***** IPB001789 (Response regulator receiver) with a combined E-value of 8.2e-07. IPB001789A 51-64 IPB001789B 99-109***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 9e-07. IPB001867A 51-64 IPB001867B 79-123","Residues 4-120 are similar to a (SENSORY TRANSDUCTION PHOSPHORYLATION REGULATOR DNA-BINDING TRANSCRIPTION REGULATION RESPONSE TWO-COMPONENT KINASE) protein domain (PD000039) which is seen in Q6AAP9_PROAC.","","-52% similar to PDB:1S8N Crystal structure of Rv1626 from Mycobacterium tuberculosis (E_value = 9.5E_15);-52% similar to PDB:1SD5 Crystal structure of Rv1626 (E_value = 9.5E_15);-46% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 1.1E_13);-46% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 1.1E_13);-53% similar to PDB:1TMY CHEY FROM THERMOTOGA MARITIMA (APO-I) (E_value = 2.9E_11);","Residues 4 to 118 (E_value = 9.4e-30) place ANA_1199 in the Response_reg family which is described as Response regulator receiver domain.Residues 140 to 197 (E_value = 5.4e-14) place ANA_1199 in the GerE family which is described as Bacterial regulatory proteins, luxR family.","","family two component system response regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1200","1279564","1277879","1686","8.95","5.70","58957","GTGTTCGGCAACCTCTCCGATCGCATCACCGCCTCCTTCAACCAGCTGCGCGGCAAGGGTCGTCTCACCGAGGCCGACGTCAACGCCACAGTCACCGAGATCCGCCGCGCCCTCCTGGAGGCCGACGTCGCCCTGCCCGTGGTGCGCGCCTTCACCGCAGCGGTGCGCGAGAAGGCGGTCGACGCCGCCCGCTCTCAGGCCCTCAACCCGGGCCAGCAGGTCGTCAAGATCGTCAACGAGGAGCTCATTGAGGTCCTGGGTGGCCAGACCCGGGAGATCCACTGGGCTGACCGCGGCCCCACAATCATCATGCTCGCCGGTCTCCAAGGTGCCGGTAAGACCACCCTGGCCGGAAAGCTCGGACGCTGGCTGCGCGACCAGGGCAAGCGCGTCCTGCTGGTGGCCTCCGACCTCCAGCGCCCCAACGCCGTGACCCAGCTGAGCGTCGTCGCCGAGCGCGCCGGGGTGCACGTGTGGGCGCCCGAACCCGGCAACGGCGTGGGCGACCCGGTGGCAGTGGCCCGCTCCGGCGTCGAGCACGCGCGTACCAACGGCTACGACGTCGTCGTCGTGGACACCGCCGGACGCCTGGGCGTGGACGCCGAGATGATGGACCAGGCGATCCGCATCCGCGATGCCGTCTCCCCCCACGAGATCCTCTTCGTCCTGGACGCCATGGTCGGTCAGGACGCTGTCAACACCTCGGTCGCCTTCCGCGACGGCGTCGGCTTCACCGGCGTGGTCCTCTCCAAGCTCGACGGCGACGCCCGCGGCGGCGCGGCCCTGTCCGTGCGCGGCGTCACCGGTGCCCCGGTCCTGTTCTCCTCCACCGGTGAGGGCCTGACCGACTTCGAGCGCTTCCACGCCGACCGCATGGCATCGCGCATCCTGGACATGGGTGACCTGCTCACCCTCATCGAGCAGGCCGAGCGGACCCTGGACCGCCAGGAGGCCGAGGACGCCGCCGCCAAGCTCGCCAAGGGCACCTTCACCCTCGACGACTTCCTGGGCCAGCTGCGCCAGATCCGCAAGATGGGCTCCATGAAGAAGCTTCTGGGCATGATGCCCGGGATGGGGCAGATGCGTGAGGCCCTGGACAACTTCGACGAGCGCGAGGTCGACCGCATTGAGGCGATCGTGTGCTCCATGACGCCCGCCGAGCGCAAGGACCTGTCCATCCTCAACGGCTCTCGCCGCAGCCGTATCGCCAAGGGCTCGGGGACCACGGTCCAGGCCGTCAACGAGCTCGTGGACCGCTTCGAGCAGGCCAAGAAGATGATGGAGGCCATGGCCTCCGGCGGTATGGGCGGACTCGGTGAGGGCGGTCCTATGCCCGGCATGGGGTCGCTGCCCGGCATGGGCAAGCACTCCAAGGCCCGTCAGGCCCCCAAGGCCAAGCGCGGCAAGGGCGGCAAGAAGGGGCGCAGCGGCAACCCCGCCAAGGCCGCCCGTCAGGCCAAGGAGGCGGCGGCCGCCAAGCAGGCAAAGATCGAGGGCGGACAGGGGGCTGCGCCCGCAGCCGGCTCCTCCTTCGGGCTCGGAGGTGGCCAGGGCGATACCTCCGGCTACGGGATCATGCCTCAGGCCCAGCCGCAGGCTCAGACCGGCGCACAGCCCTCGGGCGACGACGTCGCCGACGCCATGAGCGCCCTGCCCGATGACTTGCGTCGCCACCTCGGACTGTAG","VFGNLSDRITASFNQLRGKGRLTEADVNATVTEIRRALLEADVALPVVRAFTAAVREKAVDAARSQALNPGQQVVKIVNEELIEVLGGQTREIHWADRGPTIIMLAGLQGAGKTTLAGKLGRWLRDQGKRVLLVASDLQRPNAVTQLSVVAERAGVHVWAPEPGNGVGDPVAVARSGVEHARTNGYDVVVVDTAGRLGVDAEMMDQAIRIRDAVSPHEILFVLDAMVGQDAVNTSVAFRDGVGFTGVVLSKLDGDARGGAALSVRGVTGAPVLFSSTGEGLTDFERFHADRMASRILDMGDLLTLIEQAERTLDRQEAEDAAAKLAKGTFTLDDFLGQLRQIRKMGSMKKLLGMMPGMGQMREALDNFDEREVDRIEAIVCSMTPAERKDLSILNGSRRSRIAKGSGTTVQAVNELVDRFEQAKKMMEAMASGGMGGLGEGGPMPGMGSLPGMGKHSKARQAPKAKRGKGGKKGRSGNPAKAARQAKEAAAAKQAKIEGGQGAAPAAGSSFGLGGGQGDTSGYGIMPQAQPQAQTGAQPSGDDVADAMSALPDDLRRHLGL$","Signal recognition particle protein subunit","Cytoplasm","signal recognition particle protein subunit","K03106 signal recognition particle; subunit SRP54","signal recognition particle protein","","Althoff S., Selinger D., Wise J.A. Molecular evolution of SRP cycle components: functional implications. Nucleic Acids Res. 1994. 22(11):1933-1947. PMID: 7518075Rosendal K.R., Wild K., Montoya G., Sinning I. Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication. Proc. Natl. Acad. Sci. U.S.A. 2003. 100(25):14701-14706. PMID: 14657338","","","

InterPro
IPR000897
Domain

GTP-binding signal recognition particle SRP54, GTPase
PD000819	$\"[103-196]T$	Q8VVP8_BBBBB_Q8VVP8;
PF00448	$\"[99-298]T$	SRP54

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[99-303]T$	AAA

InterPro
IPR004125
Domain

GTP-binding signal recognition particle SRP54, M-domain
G3DSA:1.10.260.30	$\"[329-430]T$	no description
PF02978	$\"[329-427]T$	SRP_SPB

InterPro
IPR004780
Family

Signal recognition particle protein
PTHR11564:SF7	$\"[74-500]T$	SIGNAL RECOGNITION PARTICLE PROTEIN
TIGR00959	$\"[2-429]T$	ffh: signal recognition particle protein

InterPro
IPR013822
Domain

GTP-binding signal recognition particle SRP54, helical bundle
G3DSA:1.20.120.140	$\"[1-90]T$	no description
PF02881	$\"[1-87]T$	SRP54_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[93-300]T$	no description
PTHR11564	$\"[74-500]T$	GTPASE CONTAINING FAMILY OF SIGNAL RECOGNITION PARTICLE PROTEINS

","BeTs to 26 clades of COG0541COG name: Signal recognition particle GTPaseFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0541 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000897 (GTP-binding signal recognition particle (SRP54) G-domain) with a combined E-value of 2.1e-37. IPB000897A 102-117 IPB000897B 133-148 IPB000897C 187-196 IPB000897D 216-258***** IPB000062 (Thymidylate kinase) with a combined E-value of 7.9e-06. IPB000062A 102-128","Residues 1-102 are 63% similar to a (RECOGNITION SIGNAL PARTICLE) protein domain (PD933491) which is seen in Q83MV0_TROWT.Residues 16-88 are 86% similar to a (SIGNAL RECOGNITION PARTICLE GTP-BINDING RNA-BINDING SRP54 FFH HOMOLOG FIFTY-FOUR GTPASE) protein domain (PD399504) which is seen in Q8VVP8_BBBBB.Residues 103-196 are similar to a (SIGNAL RECOGNITION PARTICLE DIVISION CELL GTP-BINDING FTSY RNA-BINDING RECEPTOR HOMOLOG) protein domain (PD000819) which is seen in Q8VVP8_BBBBB.Residues 199-296 are similar to a (SIGNAL RECOGNITION PARTICLE DIVISION CELL GTP-BINDING FTSY RNA-BINDING RECEPTOR HOMOLOG) protein domain (PD589625) which is seen in Q8VVP8_BBBBB.Residues 297-420 are similar to a (SIGNAL RECOGNITION PARTICLE GTP-BINDING RNA-BINDING SRP54 HOMOLOG FFH FIFTY-FOUR GTPASE) protein domain (PD001802) which is seen in Q8VVP8_BBBBB.","","-66% similar to PDB:2J28 MODEL OF E. COLI SRP BOUND TO 70S RNCS (E_value = 4.8E_99);-61% similar to PDB:2FFH THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM THERMUS AQUATICUS (E_value = 1.6E_86);-57% similar to PDB:2IY3 STRUCTURE OF THE E. COLI SIGNAL RECOGNITION PARTICLE BOUND TO A TRANSLATING RIBOSOME (E_value = 3.5E_73);-64% similar to PDB:1RJ9 Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY) (E_value = 7.0E_66);-64% similar to PDB:1O87 A NEW MGGDP COMPLEX OF THE FFH NG DOMAIN (E_value = 2.0E_65);","Residues 1 to 87 (E_value = 2.7e-29) place ANA_1200 in the SRP54_N family which is described as SRP54-type protein, helical bundle domain.Residues 99 to 298 (E_value = 8.5e-100) place ANA_1200 in the SRP54 family which is described as SRP54-type protein, GTPase domain.Residues 329 to 427 (E_value = 1.7e-49) place ANA_1200 in the SRP_SPB family which is described as Signal peptide binding domain.","","recognition particle protein subunit (ffh)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1203","1279916","1280908","993","5.56","-8.88","35064","ATGAGCACAGCAACGCCTCGGACCAGCCGGGAGGCCACCGTCACGGAAGACCCCCGGACGGACCATGTGGACGCCGTCCGACTGACCGATCTGCACAAGTCCTTCGGTGACGTCACCGCCGTCGACGGTATCGACCTGACCATCCGCCCCGGCGAGGTCGTCGCCCTCCTGGGCCCCAACGGCGCAGGCAAGACGACGACGATCGACATGATCCTGGGACTGAGCCGCCCCACCAACGGCGATGCGAGAGTCTTCGGGATGAGCCCGCGCCAAGCGGTCGACCGGGGCCTGGTCGCCGCAGTCATGCAGACCGCCGGTCTCCTGCCCGACATCACCGTGCGTGAGACGGTGCAGCTGACGGCGAGTCTCTTCTCGCATCGAATCGACGCCGAGGAGGCCATGCACCGCGCCGGCGTCACCGACTTCGCCTCACGCATCGTCAAGAAGTGCTCCGGAGGCCAGCAGCAGCGCCTGCGCTTCGCCATGGCACTCGTGAGCGACCCGGCACTGCTCATCCTCGATGAGCCGACCACAGGCATGGACGTCGAGGGGCGCCGCAGCTTCTGGGAGGCCATCCACGCCGACGCCGAGCGCGGGCGCACCATCGTCTTCGCCACGCACTACCTCGAGGAGGCCGACGCCTTCGCCGACCGGATCGTCCTGATGCGTCATGGGCGCATCATTGCCGACGGCACTGCTGCGGAGATCCGCGCCTCCGTGAGCGGCCGCTCCCTGCGAGCCACCCTGACCTGCGCTCCTGAGCGGCTGCGCGACGCCCTGGCCGATGCGCAGATCCGTGGGCAGGTCCACGACGTCGAGGTCCTGGGCAGCACGCTCACCCTGAGCTCGACCGACAGCGACGCCGTGGCCGCGCTCCTCCTCAGCAATCATCTGGCCAAGGACCTGGAGATCACCAGCCGGGGACTGGAGGACGCCTTCGTGGCCCTGACCAGCGACAGCGCCTCTGCCCCCAGTGCCGGAGCGTCAGCATGA","MSTATPRTSREATVTEDPRTDHVDAVRLTDLHKSFGDVTAVDGIDLTIRPGEVVALLGPNGAGKTTTIDMILGLSRPTNGDARVFGMSPRQAVDRGLVAAVMQTAGLLPDITVRETVQLTASLFSHRIDAEEAMHRAGVTDFASRIVKKCSGGQQQRLRFAMALVSDPALLILDEPTTGMDVEGRRSFWEAIHADAERGRTIVFATHYLEEADAFADRIVLMRHGRIIADGTAAEIRASVSGRSLRATLTCAPERLRDALADAQIRGQVHDVEVLGSTLTLSSTDSDAVAALLLSNHLAKDLEITSRGLEDAFVALTSDSASAPSAGASA$","ABC-2 type transport system ATP-binding protein","Cytoplasm, Membrane","ABC transporter ATP binding subunit","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[151-189]T$	Q6NFA4_CORDI_Q6NFA4;
PF00005	$\"[51-225]T$	ABC_tran
PS50893	$\"[26-249]T$	ABC_TRANSPORTER_2
PS00211	$\"[150-164]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[50-226]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[26-239]T$	no description
PTHR19222	$\"[26-245]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[26-245]T$	ABC TRANSPORTER

","No hits to the COGs database.","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3.5e-30. IPB013563A 40-74 IPB013563C 147-174 IPB013563D 201-253***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 7.1e-27. IPB005074C 40-87 IPB005074D 138-181***** IPB005116 (TOBE domain) with a combined E-value of 2.3e-12. IPB005116A 58-74 IPB005116C 150-163 IPB005116D 170-189 IPB005116E 203-216***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.5e-12. IPB010509B 51-76 IPB010509D 145-189***** IPB000897 (GTP-binding signal recognition particle (SRP54) G-domain) with a combined E-value of 1e-06. IPB000897A 53-68***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.7e-06. IPB010929K 38-82 IPB010929M 147-193 IPB010929A 50-69","Residues 4-220 are 45% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 11-143 are 47% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA187B6) which is seen in Q6A7G4_PROAC.Residues 18-133 are 48% similar to a (LIPOPROTEIN ATP-BINDING RELEASING SYSTEM LOLD) protein domain (PDA0I1Q0) which is seen in Q7UH39_RHOBA.Residues 18-241 are 45% similar to a (C24F3.5 ATP-BINDING) protein domain (PD574736) which is seen in Q21213_CAEEL.Residues 21-230 are 42% similar to a (SIMILAR ABC ATP-BINDING TRANSPORTER) protein domain (PDA0K5L4) which is seen in Q7N905_PHOLL.Residues 23-229 are 43% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 23-237 are 45% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 25-137 are 51% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 25-91 are 58% similar to a (MULTIDRUG ABC-TYPE ATP-BINDING) protein domain (PDA106P9) which is seen in Q7X353_BBBBB.Residues 25-145 are 55% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA188U2) which is seen in Q9RXA9_DEIRA.Residues 26-231 are 48% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 26-219 are 46% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD784156) which is seen in Q8ESY8_OCEIH.Residues 36-132 are 50% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J3M6) which is seen in Q98E05_RHILO.Residues 36-231 are 45% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 38-224 are 44% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 41-86 are 78% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q9F341_STRCO.Residues 41-220 are 45% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 43-181 are 53% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 44-207 are 47% similar to a (COMPONENT ATPASE ABC- TYPE ABC-TYPE PERMEASE MULTIDRUG/PROTEIN/LIPID TRANSPORTER ATP-BINDING SYSTEM) protein domain (PDA185P6) which is seen in Q8NRA4_CORGL.Residues 44-207 are 48% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 46-209 are 47% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 52-227 are 46% similar to a (ATP-BINDING CG1494-PA) protein domain (PD310846) which is seen in Q9VRG3_DROME.Residues 54-257 are 46% similar to a (CG1801-PA ATP-BINDING) protein domain (PDA101Z1) which is seen in Q9VRG5_DROME.Residues 101-255 are 48% similar to a (COMPONENT ABC-TYPE ATPASE TRANSPORTER) protein domain (PDA0J0G9) which is seen in Q6A7W5_PROAC.Residues 110-238 are 53% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 110-221 are 52% similar to a (AMV130) protein domain (PD706071) which is seen in Q9EMR9_AMEPV.Residues 129-316 are 44% similar to a (GLP_170_16420_13880 ATP-BINDING) protein domain (PDA0Z2E6) which is seen in Q7R6S2_EEEEE.Residues 130-208 are 55% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA182E2) which is seen in Q8KED6_CHLTE.Residues 131-230 are 53% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 131-227 are 56% similar to a (ATP-BINDING COMPONENT ABC POSSIBLE TRANSPORTER) protein domain (PDA0I2Z1) which is seen in Q7V225_PROMP.Residues 136-235 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I301) which is seen in Q92RI1_RHIME.Residues 136-255 are 49% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0J201) which is seen in Q73M59_TREDE.Residues 138-220 are 57% similar to a (ATP-BINDING TRANSPORTER ABC-TYPE ABC) protein domain (PD891090) which is seen in Q73Y59_MYCPA.Residues 138-230 are 58% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 138-218 are 57% similar to a (ATP-BINDING RV2326C/MT2388/MB2353C TRANSMEMBRANE ABC TRANSPORTER) protein domain (PD957860) which is seen in YN26_MYCTU.Residues 138-230 are 51% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.Residues 141-260 are 47% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 144-222 are 55% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA18641) which is seen in Q8EG59_SHEON.Residues 144-227 are 52% similar to a (ATP-BINDING SUGAR ABC TRANSPORTER) protein domain (PDA0I778) which is seen in Q98JJ1_RHILO.Residues 147-227 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K1H6) which is seen in Q73MA6_TREDE.Residues 147-249 are 57% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 149-265 are 48% similar to a (PROBABLE ATP-BINDING ABC TRANSPORTER ATP BINDING) protein domain (PD763654) which is seen in Q8G625_BIFLO.Residues 151-241 are 51% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z3) which is seen in Q72D80_DESVH.Residues 151-220 are 58% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA198U3) which is seen in Q72IT9_THET2.Residues 151-189 are 87% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6NFA4_CORDI.Residues 151-236 are 57% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 154-271 are 45% similar to a (ATP-BINDING PLASMID) protein domain (PD244274) which is seen in Q9WW89_LACLC.Residues 208-317 are 62% similar to a (ATP-BINDING ABC TRANSPORTER YVFR SYSTEM ATP SUBUNIT BINDING) protein domain (PD060250) which is seen in Q6AAQ3_PROAC.","","-53% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 3.4E_27);-52% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 2.9E_26);-52% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 2.9E_26);-50% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 6.4E_26);-49% similar to PDB:1G29 MALK (E_value = 1.4E_25);","Residues 51 to 225 (E_value = 2.4e-54) place ANA_1203 in the ABC_tran family which is described as ABC transporter.","","transporter ATP binding subunit (drra)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1204","1280905","1281792","888","10.71","13.34","31469","ATGAGCCGTTCCGCCCGCCCCAGCAACACCGTCACCCTTCCGCCCACTACCTGCACCGGAACCGCAATGTCCTCTTCTCAGTCTTCCTCGTCCTCCTCCGCCTCATCAGTGGTCACGCGCCTCGATCTGTCCTCCCGGACCGCGCCACCGTTGGGAGGGTTGAGCCTTCCGCTGCTGTCGCTCGAGGTTCGCCGGCGCCTGCGCAACCGTCGGTCCGTCATCTTCTCGATCGTTCTTCCGGTGGCCTTCTTCCTCATGTTCACCACGACTGACTACTCCGCCATGCCCTATGGCAACGGCAACGTCGTGGCGAACATGATGATCGGCATGGCCCTGTACGGCGCGCTCATGACCACCACCGGGGCAGGAGCGGCCGTGAGCACCGAGCGGGCCTCAGGATGGAGCCGCCAGCTGCGTCTGACCCCGCTCAAGCCCATCGCCTACATCACCGCCAAGGCAATCGTGGGGATGCTCATCAGCGCCTTGGCCATCGGCGCCGTCTACGCCTGCGGCCCCCTGCGTCACGCGCAGATGCCGGCGAAGGTCTGGATCTCCTCGGCTCTCATCATCTGGCTGGGCTCCCTGGTCTTCGTCGCCTTCGGACTGTTCGTCGGCTACCTCCTGCCCTCGGACAACGCCATGCAGGTGGTCGGCCCGCTCATGGCCCTGCTCGCCTTCCTCGGCGGCATGTTCATCCCGTTGACACCGGGCTCCACCATGGATCGCATCGGCAGCTTCACCCCCATGTACGGGCTGCACAACCTGGCGCTGTGGCCCATGGGCGCCGAGAGCTTCTCCTGGTGGTGGGTGGTCAACGTGCTGACCTGGCTCGCCGTCTTCCTGGGCGGGGCCGCCTGGAAGATGGGCCGAGACACCGCCCGAGTGTGA","MSRSARPSNTVTLPPTTCTGTAMSSSQSSSSSSASSVVTRLDLSSRTAPPLGGLSLPLLSLEVRRRLRNRRSVIFSIVLPVAFFLMFTTTDYSAMPYGNGNVVANMMIGMALYGALMTTTGAGAAVSTERASGWSRQLRLTPLKPIAYITAKAIVGMLISALAIGAVYACGPLRHAQMPAKVWISSALIIWLGSLVFVAFGLFVGYLLPSDNAMQVVGPLMALLAFLGGMFIPLTPGSTMDRIGSFTPMYGLHNLALWPMGAESFSWWWVVNVLTWLAVFLGGAAWKMGRDTARV$","ABC-2 type transport system permease protein","Membrane, Extracellular","membrane protein, putative","K01992 ABC-2 type transport system permease protein","ABC-2 type transporter","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[53-234]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
tmhmm	$\"[73-93]?$ $\"[107-127]?$ $\"[148-168]?$ $\"[187-207]?$ $\"[216-236]?$ $\"[265-285]?$	transmembrane_regions

","BeTs to 5 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","No significant hits to the Blocks database.","Residues 106-208 are 60% similar to a (ABC PERMEASE TRANSPORTER MEMBRANE ATP-BINDING TRANSPORTER TRANSMEMBRANE PROTEIN COMPONENT INTEGRAL) protein domain (PD115342) which is seen in Q6AAQ2_PROAC.Residues 126-211 are 56% similar to a (MEMBRANE ABC INTEGRAL TRANSPORTER) protein domain (PDA135X2) which is seen in Q9F340_STRCO.","","-44% similar to PDB:1Q90 Structure of the cytochrome b6f (plastohydroquinone : plastocyanin oxidoreductase) from Chlamydomonas reinhardtii (E_value = );-56% similar to PDB:1XL4 Intermediate gating structure 1 of the inwardly rectifying K+ channel KirBac3.1 (E_value = );-56% similar to PDB:1XL6 Intermediate gating structure 2 of the inwardly rectifying K+ channel KirBac3.1 (E_value = );","Residues 53 to 261 (E_value = 7.8e-05) place ANA_1204 in the ABC2_membrane family which is described as ABC-2 type transporter.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1205","1281953","1282972","1020","6.99","-0.04","36081","ATGTGGGGCGCTGTCAGCGCCATCGTCTCCTGCGCGTGCCTGTATGCCGCCTGCTCGCTCAGCGTGAGACGGGTGCGGCAAGGGCTGACCTGGCCCGGCCGCCTGAGTCTGTTGCTCATCGTGGTCGGCGCACTCACAGCGATCGGGGCCGCCCTCGGCGTGGGCCCTCAGAGCCTGCAGCTGGTGGTCTTCCTGGCCGTTGTCCTGGCCTTCTCCCTGCCCTGGCAGGCGTCCATCGGCCCTATCGCGATCCTCGCCGGCGCCCTCTTCCTCGTTCCCAGGATGATGCCATCATGGTCCGCAAGTGAAGGCGCATGGATCGCTCTACTCGGCGCGGGCGGCGCCTGCGTCTTCGGGCGTTACATCATGGAGCAGCGGCGGGCGGCCCGCATTCTGGAGCAGCGCACCCATGAGTTGGAGATCAACGAGGAGCGCAACCGCATGGCCCGGGACATGCACGACATCCTGGGGCACTCGCTGACAGTCATCGCCTTGAAGACCGAGCTCGCCACCAGACTCGTCGATGCCGCACCCGATCAGGCCAAGGCGGAGCTGACCGAGGTTCAATCCCTGGCGCGCTCCGCCCTGGCCGACGTGCGCGCCACCGTCAACAGCTACCGCGAGCTGAGCCTGGCCGGCGAGCTGGCGCGCGCCACCAACGTCCTGACCTCTGCCGGTGTCCGCGCCGACCTCCCGCTGACCGTCGAGATCGTCGATCCCGAGCTGCGCGAGCTCTTCGCCTGGGTGGTGCGCGAGGGCGTCACCAACATCGTGCGCCACGCCCACGCCTCGCACTGCAGGGTGGTGCTGAGCGCCGACTCCATTGAGGTGGCCGACGACGGTATCGGGCTGAACTCGGCCGGCACCGGAGACGGTCACGGCTTGGAGGGACTGCGCCAGCGCTGTCAGGACAACGGCGCCGACCTCACCATCGAGACGCCCTCGCATGGCAGCGGCACCGTCCTGAGGGTGCGCGCCCGCCACCTATCCTCACCTATGGCGCCCGACGCGAGCCGGTGA","MWGAVSAIVSCACLYAACSLSVRRVRQGLTWPGRLSLLLIVVGALTAIGAALGVGPQSLQLVVFLAVVLAFSLPWQASIGPIAILAGALFLVPRMMPSWSASEGAWIALLGAGGACVFGRYIMEQRRAARILEQRTHELEINEERNRMARDMHDILGHSLTVIALKTELATRLVDAAPDQAKAELTEVQSLARSALADVRATVNSYRELSLAGELARATNVLTSAGVRADLPLTVEIVDPELRELFAWVVREGVTNIVRHAHASHCRVVLSADSIEVADDGIGLNSAGTGDGHGLEGLRQRCQDNGADLTIETPSHGSGTVLRVRARHLSSPMAPDASR$","Two-component system sensor kinase","Membrane, Cytoplasm","two-component system sensor protein","two-component system sensor kinase","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[241-329]T$	HATPase_c
SM00387	$\"[241-330]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[144-211]T$	HisKA_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[37-71]?$ $\"[77-95]?$ $\"[105-123]?$	transmembrane_regions

","BeTs to 8 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 4.8e-20. IPB011712A 143-160 IPB011712B 246-266 IPB011712C 277-286","Residues 144-235 are similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM TRANSFERASE 2.7.3.- SENSORY TRANSDUCTION NITRATE/NITRITE) protein domain (PD288674) which is seen in Q9ZA46_STRVN.Residues 235-323 are 56% similar to a (KINASE REGULATOR HISTIDINE RESPONSE PROBABLE FAMILY GAF) protein domain (PD771047) which is seen in Q7VET1_MYCBO.Residues 249-324 are 57% similar to a (KINASE SENSOR HISTIDINE TWO-COMPONENT SYSTEM SENSORY TRANSFERASE TRANSDUCTION 2.7.3.- TWO) protein domain (PD005700) which is seen in Q9RPF0_CORDI.","","-47% similar to PDB:1ZHH Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ (E_value = );-62% similar to PDB:1ZVD Regulation of Smurf2 Ubiquitin Ligase Activity by Anchoring the E2 to the HECT domain (E_value = );-47% similar to PDB:2HJ9 Crystal structure of the Autoinducer-2-bound form of Vibrio harveyi LuxP complexed with the periplasmic domain of LuxQ (E_value = );-47% similar to PDB:2HJE Crystal structure of Vibrio harveyi LuxQ periplasmic domain (E_value = );","Residues 144 to 211 (E_value = 1.2e-25) place ANA_1205 in the HisKA_3 family which is described as Histidine kinase.Residues 241 to 329 (E_value = 8.5e-08) place ANA_1205 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","system sensor protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1207","1283050","1283661","612","6.04","-3.59","21319","ATGATCCGAGTGATGCTGGCCGATGACCAGGCCATGGTGCGCGGGGCACTGGCCGCACTGCTCGCCCTGGAGACCGATATCGAGGTCGTCGCACAGGTCGGGAACGGGAACGATGTTCTGCCCGTCGCGCTCGAGCACCGGCCCGACGTCGTCCTCATGGACGTCGATATGCCCGGCACCGACGGGCTGAGCGCGACCGCGAGTCTCCTGGAGCGGTTGCCGGCCACGAGGGTCCTCATCGTGACGACCTTCGGGCGTCCCGGATTCCTGCGGCGCGCCATTCAGTCCGGGGCGCACGGCTTCGTCGTCAAGGATGCCCCGGCCACCGAGCTCGCCGAGTCGGTGCGCCGGGTCCATGCCGGGCTGCGCGTCGTCGACCCGGCACTGGCCGCCGACTCGCTCATCTTCGGGGACTCCCCCTTGACCGCCAGGGAGACCGAGGTGCTCCAGGCGGCGGCCGACGGCGCCACCGTCTCCGAGGTCGCCCGGCGAGTCCATCTCTCGGAGGGAACCACCCGAAACCACCTGTCCCAGGCCATGGCCAAGACCGGAGCCCCCACCCGGGCCGCGGCGGTGCACATCGCCGCACAGAAGGGGTGGATCATCGAGTAA","MIRVMLADDQAMVRGALAALLALETDIEVVAQVGNGNDVLPVALEHRPDVVLMDVDMPGTDGLSATASLLERLPATRVLIVTTFGRPGFLRRAIQSGAHGFVVKDAPATELAESVRRVHAGLRVVDPALAADSLIFGDSPLTARETEVLQAAADGATVSEVARRVHLSEGTTRNHLSQAMAKTGAPTRAAAVHIAAQKGWIIE$","Two-component system response regulator","Cytoplasm, Membrane","luxR family two component system responseregulator","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[140-195]T$	Q9RKL0_STRCO_Q9RKL0;
PR00038	$\"[141-155]T$ $\"[155-171]T$ $\"[171-183]T$	HTHLUXR
PF00196	$\"[138-195]T$	GerE
SM00421	$\"[138-195]T$	HTH_LUXR
PS50043	$\"[134-199]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[3-118]T$	Q9L005_STRCO_Q9L005;
PF00072	$\"[2-116]T$	Response_reg
SM00448	$\"[2-115]T$	REC
PS50110	$\"[3-119]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[139-203]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[2-128]T$	no description
PTHR23283	$\"[3-119]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF47	$\"[3-119]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (DHKB)
signalp	$\"[1-31]?$	signal-peptide

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000673 (CheB methylesterase) with a combined E-value of 4.2e-18. IPB000673A 5-14 IPB000673B 21-74***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 1.5e-15. IPB000792 141-187***** IPB005143 (Autoinducer binding domain) with a combined E-value of 4.3e-13. IPB005143B 141-184***** IPB001789 (Response regulator receiver) with a combined E-value of 5.6e-08. IPB001789A 49-62 IPB001789B 97-107***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 8.2e-07. IPB001867A 49-62 IPB001867B 77-121","Residues 2-48 are 74% similar to a (DNA-BINDING SYSTEM TWO-COMPONENT TRANSCRIPTION REGULATOR PHOSPHORYLATION TRANSDUCTION SENSORY REGULATION RESPONSE) protein domain (PDA0J0I8) which is seen in Q82FV7_STRAW.Residues 3-129 are 46% similar to a (SYSTEM TRANSCRIPTION TRANSDUCTION DNA-BINDING TWO-COMPONENT REGULATOR PHOSPHORYLATION SENSORY REGULATION RESPONSE) protein domain (PD715337) which is seen in Q82HD7_STRAW.Residues 3-118 are similar to a (SENSORY TRANSDUCTION PHOSPHORYLATION REGULATOR DNA-BINDING TRANSCRIPTION REGULATION RESPONSE TWO-COMPONENT KINASE) protein domain (PD000039) which is seen in Q9L005_STRCO.Residues 49-137 are 52% similar to a (REGULATOR TRANSCRIPTION TRANSDUCTION DNA-BINDING PHOSPHORYLATION SENSORY REGULATION RESPONSE SYSTEM TWO-COMPONENT) protein domain (PD032914) which is seen in Q825F8_STRAW.Residues 140-195 are 75% similar to a (DNA-BINDING TRANSCRIPTION REGULATION REGULATOR SENSORY PHOSPHORYLATION TRANSDUCTION RESPONSE TRANSCRIPTIONAL TWO-COMPONENT) protein domain (PD000307) which is seen in Q9RKL0_STRCO.","","-52% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 3.7E_19);-52% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 3.7E_19);-60% similar to PDB:1S8N Crystal structure of Rv1626 from Mycobacterium tuberculosis (E_value = 6.2E_14);-60% similar to PDB:1SD5 Crystal structure of Rv1626 (E_value = 6.2E_14);-57% similar to PDB:1DZ3 DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A (E_value = 1.4E_13);","Residues 2 to 116 (E_value = 4.4e-26) place ANA_1207 in the Response_reg family which is described as Response regulator receiver domain.Residues 138 to 195 (E_value = 1.2e-11) place ANA_1207 in the GerE family which is described as Bacterial regulatory proteins, luxR family.Residues 141 to 185 (E_value = 0.0041) place ANA_1207 in the HTH_10 family which is described as HTH DNA binding domain.","","family two component system response regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1208","1284845","1283685","1161","4.67","-21.75","40262","ATGGAACCGATCCTCATCGTTCTCGGCATCATCCTGGTCATCGTCATCGGAGGAGGGCTGTGGCTCTACGCCGGCCGACGGCGGGGCCAGGTCTCTGACGAGATCAGCGCCCACCAGCCGATGTCCGTGGAGGACCTTCTGCCCTCGGAGGGCGAGGACACCGATGAGGATGCGGAAGGGGCGGGCGCCGCCAAGCCGGCTGCGACGCTGGAGTCCCCCGAGTCCATCCCGGGCCGCATGCAGCGCCTGCGCGCCCGTCTGGCCGGTGCCGGCGGCTTCGGCAAGGCGGTCCTGTCCGTCCTGTCCCGAGGAGACCTCACCGAGGAGGACTGGGAGGAGATCGAGGACACCCTGCTCACCTCCGACCTCGGTATCGAGGTGACCACCTCCCTCATGGACGAGCTGCGCACCCAGGCCAAGGTTCTGGGAACTTCCGACCCCGAGGCGGTCCGCACTGTCCTGCGCGCCGAGCTGCTCAAGCTCGTCGACCCCTCCCTGGACCGCTCCCTCAACCTGGAGCGCCCCACCCCGGCCGAAGGGGCCCAGGGCAAGCCCGCGGCAGCCATCCTCATGGTGGGGGTCAACGGCACCGGCAAGACCACCACCTGCGGCAAGCTCGCCCGCGTCCTGGTGGCTCAGGACAAGACCGTCGTCCTGGGAGCGGCCGACACCTTCCGCGCCGCGGCGGCCGAGCAGCTGAGCACCTGGGGCGAGCGCGTGGGCGTTGACGTCGTGCGCTCCGAGAAGGAGGGAGCCGACCCCGCCTCGGTCGCCTACGACGCAGCCCGTGAGGCCTCCGCCCAGGAGGCGGACGTCGTCGTCGTCGACACCGCCGGGCGCCTGCAGAACAAGGCCGGCCTCATGGATGAGCTGGGCAAGATCAAGCGCGTCATGGAGAAGATCGCCCCGGTCGGCGAGATCCTCCTGGTGCTGGACGCCACCACCGGCCAGAACGGCATGCGTCAGGCTCAGGTCTTCTCCGAGGCCGTGGGCGTCACCGGCATCGTGCTCACCAAGCTCGACGGCACCGCCAAGGGCGGCATCGTCGTCACTGTCCAGAAGGAGCTGGGCGTGCCCGTCAAGCTCGTGGGCCTGGGGGAGGGCGCCGACGACCTGGCCCCCTTCGATCCGGAGGGCTTCGTCGACGCGCTGCTGGGCTGA","MEPILIVLGIILVIVIGGGLWLYAGRRRGQVSDEISAHQPMSVEDLLPSEGEDTDEDAEGAGAAKPAATLESPESIPGRMQRLRARLAGAGGFGKAVLSVLSRGDLTEEDWEEIEDTLLTSDLGIEVTTSLMDELRTQAKVLGTSDPEAVRTVLRAELLKLVDPSLDRSLNLERPTPAEGAQGKPAAAILMVGVNGTGKTTTCGKLARVLVAQDKTVVLGAADTFRAAAAEQLSTWGERVGVDVVRSEKEGADPASVAYDAAREASAQEADVVVVDTAGRLQNKAGLMDELGKIKRVMEKIAPVGEILLVLDATTGQNGMRQAQVFSEAVGVTGIVLTKLDGTAKGGIVVTVQKELGVPVKLVGLGEGADDLAPFDPEGFVDALLG$","Signal recognition particle-docking protein FtsY","Cytoplasm","signal recognition particle receptor","signal recognition particle-docking protein FtsY","signal recognition particle-docking protein FtsY","","Poland B.W., Silva M.M., Serra M.A., Cho Y., Kim K.H., Harris E.M., Honzatko R.B. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 1993. 268(34):25334-25342. PMID: 8244965Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 2000. 296(2):569-577. PMID: 10669609","","","

InterPro
IPR000897
Domain

GTP-binding signal recognition particle SRP54, GTPase
PD000819	$\"[189-280]T$	Q8VVP9_BBBBB_Q8VVP9;
PF00448	$\"[185-386]T$	SRP54
PS00300	$\"[359-372]T$	SRP54

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[84-374]T$	no description

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[185-362]T$	AAA

InterPro
IPR004390
Family

Cell division transporter substrate-binding protein FtsY
TIGR00064	$\"[105-385]T$	ftsY: signal recognition particle-docking p

InterPro
IPR013822
Domain

GTP-binding signal recognition particle SRP54, helical bundle
G3DSA:1.20.120.140	$\"[84-167]T$	no description
PF02881	$\"[83-163]T$	SRP54_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[179-386]T$	no description
PTHR11564	$\"[150-385]T$	GTPASE CONTAINING FAMILY OF SIGNAL RECOGNITION PARTICLE PROTEINS
PTHR11564:SF6	$\"[150-385]T$	CELL DIVISION PROTEIN FTSY
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","BeTs to 25 clades of COG0552COG name: Signal recognition particle GTPaseFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0552 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000897 (GTP-binding signal recognition particle (SRP54) G-domain) with a combined E-value of 1.6e-44. IPB000897A 188-203 IPB000897B 219-234 IPB000897C 271-280 IPB000897D 304-346","Residues 106-158 are 75% similar to a (DIVISION CELL RECOGNITION SIGNAL FTSY PARTICLE RECEPTOR GTP-BINDING HOMOLOG PARTICLE-DOCKING) protein domain (PD005336) which is seen in Q8VVP9_BBBBB.Residues 189-280 are similar to a (SIGNAL RECOGNITION PARTICLE DIVISION CELL GTP-BINDING FTSY RNA-BINDING RECEPTOR HOMOLOG) protein domain (PD000819) which is seen in Q8VVP9_BBBBB.Residues 289-385 are similar to a (SIGNAL RECOGNITION PARTICLE DIVISION CELL GTP-BINDING FTSY RNA-BINDING RECEPTOR HOMOLOG) protein domain (PD589625) which is seen in Q8VVP9_BBBBB.","","-70% similar to PDB:1VMA Crystal structure of Cell division protein ftsY (TM0570) from Thermotoga maritima at 1.60 A resolution (E_value = 6.5E_73);-67% similar to PDB:1FTS SIGNAL RECOGNITION PARTICLE RECEPTOR FROM E. COLI (E_value = 7.7E_66);-63% similar to PDB:1OKK HOMO-HETERODIMERIC COMPLEX OF THE SRP GTPASES (E_value = 4.7E_63);-63% similar to PDB:2CNW GDPALF4 COMPLEX OF THE SRP GTPASES FFH AND FTSY (E_value = 1.0E_62);-63% similar to PDB:2IYL STRUCTURE OF AN FTSY:GDP COMPLEX (E_value = 1.0E_62);","Residues 83 to 163 (E_value = 4.3e-08) place ANA_1208 in the SRP54_N family which is described as SRP54-type protein, helical bundle domain.Residues 185 to 386 (E_value = 6.9e-107) place ANA_1208 in the SRP54 family which is described as SRP54-type protein, GTPase domain.","","recognition particle receptor","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1210","1285676","1285197","480","8.54","3.30","17025","ATGAGCCATTGTTGTGTCAGGAAGTTGTCAGGTTTTGTTGTTGATTGGACGACAAGTGCGTGCAAAGTCTGGTCAGATCGTAATTCGCAAGGCAGAATCCTAACTATGGGTGTCATGATTCTTCCCCTCGTTGTCGTGCTGGTTGCCGGCCTGCTTGTGCTCGGCATGGTTTGTGCTGAGCGCTTCCCGGTGCGCTCTTGGCCCTCACGCATTCGCAGCGTGGTCCGCAACTCCCAGGAGGTGCGCCTGGCGGAGCAGGACGTCGAGGTCGAGGTCGTGCCCCAGGAGGTCAGCCTGTCCGACCTCATGACCCGTGAGGGGCCGGCGGCCTACGCCGGCACCGAGGGCTTCGGAGGGCTGGTCGGCGTCGTCGGAAAGGCGATGGATGCTGCCGAGAGGACCCGTGGCTCCGCCGGCGCCCGGCGTCGCGCTCAGGCGCACGAGCCGGCAACCGGTGGTCTGTCGCAGTCTCAGAGTTGA","MSHCCVRKLSGFVVDWTTSACKVWSDRNSQGRILTMGVMILPLVVVLVAGLLVLGMVCAERFPVRSWPSRIRSVVRNSQEVRLAEQDVEVEVVPQEVSLSDLMTREGPAAYAGTEGFGGLVGVVGKAMDAAERTRGSAGARRRAQAHEPATGGLSQSQS$","Hypothetical protein","Membrane, Periplasm, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-59]?$	signal-peptide
tmhmm	$\"[38-58]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1211","1289539","1285733","3807","5.16","-44.30","134079","GTGCACCTCAAGACGTTGACGATCAAGGGATTCAAGTCCTTCGCGTCGTCGACCACCCTCCGCCTGGAGCCAGGCATCACCGCCGTGGTCGGACCCAACGGGTCCGGCAAGTCCAATGTCGTCGACGCCCTGACCTGGGTCATGGGGGAGCAGGGCGCCAAGAACCTGCGCGGCGGCTCCATGGCCGACGTCATCTTCGCCGGCGCCGGCTCCCGCCCGGCCCTCGGGCGTGCCGAGGTCTCCTTGACCATCGACAACACCGACGGCGCCCTGCCGATCGACTACACCGAGGTCACCATCTCGCGCACCCTGTTCCGTGGCGGCGGGTCGGAGTACCGCATCAACGGCAGCCCGTGCCGCCTCCTCGACGTCCAGGAGCTCCTCAGCGACACGGGCCTCGGGCGCCAGATGCACGTCATCGTCGGGCAGGGGCAGCTCGACGCGGTCCTGAGCGCCACGCCTGAGGACCGCCGCGGCTTCATCGAAGAGGCCGCCGGCGTCCTCAAACACCGCAAGCGCAAGGAACGCGCCCTTCGCAAACTGGAGTCCATGGCCGCCGACCTCGCCCGCGTCGCTGACCTCACCCAGGAGCTGCGTCGCCAGCTCGGCCCCCTGGCCCGACAGGCCGCCATCGCCCGGCGCGCCCGGAGCATCCAGGTCGAGGTCCGTGACGCCACCGCCCGGCTCCTGGCCGACGACGTCGTCCAGGCCCAGTCCCTCCTGGAGGCCGGTGACGAGGACAAGGAGGCCCTGGCCCGGCGTCGCAGCGCCGTCGAGGAGGCCGAGCGTGTCGCCAGGGCCCGCCTGAGCGAGTTGGCCGCCATCGAGATCACCTCCGCCCAGCGCCTCGCCCGCGCCGGCGGTATCTGGGAGGAGCTCACGGCCGCGGCCCAGTCCCTCGGGGCGCTCGCGGACGTGGCCGGCGAGCGGATCCGGCTCCTGGCCTCCGCCCCGGCCCCGAGTCACGGCACCGATCCTGAGGAGCTCGAGCGGCGGGCCGAGGCCGCGGCCCGTGAGGAGGCCGAGCTTGCCGACACCCTCGAGGCCGCCCGCACCTCGCTCAGTGACGCCACCCGCGTGCGTGCGGACGCGGAAACCGCCGAGAAGGCAGCCGACCAGGAGCTCTCAGCGGCTCAGCGTCGCGTCTCAGACAGACGTGAGACCATCGCCCGGGCCGGTGGGCGCGTCGCCTCGGCCCGTAGTCGCCACGAGGCCAGCCTGGCCGCCCTCGAGCAGGCGCGCAGCGCGCTGCGCGCCGCTGAGGCCCGCGAGGACAGTGCCCGGGCCGCCCTGGCCGAAGCCGGGGGAGAAGCGGAACCGGCGCAGGTGGCCGCCGGTGGTGCGCGGGACGCCGTCGTCCCAGCGCAGGTACCTGCCGAGGCCGGCGCGGCTGCCGACGCGGCGGTGCGGGCCGCCGCCGTGCACGACGAGGCCGCACGCCGCCTGGCCCAGGCCCGTGAAGCCGTCGCGGCCGCGACCGACGCCCGCCGGGAGGCGGCCTCCGACCGGGCCACCTGGACCGCCAGACGCGACACCCTGGCCATGTCCCTGCGTGGCCAGGACGGCACCGCCGCGCTGCTGCAAGCCGGTATCGACGGTCTCCTCGGACCGCTTGCCGAGCACCTCAATGTTGAGCGCGGCTGGGAGAACGCCGTCGCCGCCCTCCTGGGAACGCTCGCCGAGGCCGGCCTGGCCACAGATGCTGAGGCGGCCCTGGCCGGGCTGGATCATGCCCGAAGCCAGGACATCGGGGCGGTACGACTGGTGCTGGCCGACGACCCATCACTGACTGCCGAAGCCGACACGGATGAAGAGGCAGGGGCGGCTCCCGTTGACGGGGCCCTGGCGGCTCACGACCTCGTCGGTCCCGCGCAGCCGGGACGTCTCGAGCGGGTCCTCGACCGGCTGCTCAAGGACTCCTGGGTGGTGGAGGACCTTGAGGCAGCCAGGACCCTGCGTAGCGAGCTGCCCGATGCCATCGTGGCCACCCGCAGCGGAGACGTCCTGGCGCCCGGCTGGGTCGCCGGAGCCGGTCGAGGAGCCTCCTCAGTCCTTGAGCTCACTGCCGCCCACGAGGAGGCCGACACTGAAGCCGCCGCCGCTGCGCAGGCCGAGACTGAGGCCGACGCGGCCCTGGAGGAGGCCCGTCGCCAGGAGGATGCTGCTCGCCAGGCGCTCAGCGAGGCACTGTCCGCCCTGCGCCAGGCTGACGCCGAGGCCGCCCGGGCCGCCGAGGCGATGGCCCGCCTGACCTCCGCCGCCCACGCCGCCGCCGAGGAGACCGGGCGTGCTCGCCGGGTGCTGGAGCGTGCCGAGGCCGAGTCGGTCCAGCGCACCGCCGAGCTCGCCGCCGCCACTGCCGCCCTGGCCGAGGTGGAGGACGGGGTGGGTGACACCAGGGACGGTGACGGCGTCGGAGGTGCCGGTGGGGCGGGAGCGGCGGGCGCCTCGGGGAAGGGGAGTCCCGACAGCCTTGAGCGCGCCCTGGAGGTGGCCCGCCGGGAGCGTGAGGCCGCTGCGGACACCGCGCGCCAGGCCCGCGCCGCGGAGACCGACGCCAGGCTCGCCCTGCGCACCGCCGAGGAGCGCGAGCGCTCCAGCCGCGGGCGGGCCGACTCGCTGCGAGCGGCGGCGCGCCGTGAAAGGGACCAGCGTGCCGCCGCCGAGCGGGCCCAGCAGCGGCGCAGCGCCCAGCTGGCCGTCGCCACCCATGTGCGGGACCAGGCGCGCGCGGCCGCTGAGGCAGCACGCCTCAGTGTGCAGCAGGCGGCAGATGAGCGCGCCGCCATTGAGACTGAACGTGCCCAGGCCCTGGCCGCCACCAACGAGGTTCGCGAGGAGATCGACCGGCTGACCAAGGAGCTGGGCAGCCTCACCGACGCCGCCCACCGCGAGGAGGTGGCTCGGGCCGAGCAGCGCATGCGTCTGGAAGCCCTGGCGGAGCGCGCCATGAACGAGCTCGGCCTGGAGCTGGATCCCCTTGTGGAGGAGTACGGACCGCACATGCTCGTTCCCGAGCTCATTGAGGACGCCGAGGCTGCCGCCGATTCTGGCTCCGACTCCGCCGCGGTTCAGGAGACTGCTCAGGTGTCGGCCGGCGGCTCGGGCCACCTGGGCCGTCCCTACGTGCGCTCCGAGCAGGAGAAGCGCCTGGCCAAGGCCTCGCGCGACCTCGCCCGGCTCGGCAAGGTCAACCCGCTGGCCCTGGAGGAGCACGCGGCTCTGGAGCAGCGTCACCAGTTCCTGGCCGAGCAGCTGGCCGACCTCAAGCGCTCGCGGGACGACCTGCTGAGCATCGTCGAGGAGATCGACGCGCGAGTTCAGGAAGTCTTCGCCCAGGCCTACGAGGACACCGCCCGTCAGTTCGCCTCCGTCTTCGATCGGCTCTTCCCCGGCGGGGAGGGGCGGCTGGTGCTCACGGATCCCGATGACATGCTCACCACCGGCATCGAGATCGAGGCGCGCCCCGCCGGCAAGAAGGTCAAACGACTCTCCCTGCTCTCAGGAGGGGAACGCTCGCTGGCCGCCGTGGCACTCCTGGTGGCGATCTTCAAGGCACGGCCCTCGCCCTTCTATGTCATGGACGAGGTCGAGGCGGCCCTGGACGACACGAACCTGGGGCGGTTGCTGGAGATTTTCACCGAGCTGCGGCGCTCCAGCCAGCTCATCATCATCACCCACCAGAAACGGACCATGGAGGTGGCCGACGCCCTCTACGGCATCACGATGCGCGACGGGGTCACCAAGGCCGTCTCGCAGAGGCTGGCCCAGCCCGACCGCGGTACGGCTGTGACTCCTGATGTCTGA","VHLKTLTIKGFKSFASSTTLRLEPGITAVVGPNGSGKSNVVDALTWVMGEQGAKNLRGGSMADVIFAGAGSRPALGRAEVSLTIDNTDGALPIDYTEVTISRTLFRGGGSEYRINGSPCRLLDVQELLSDTGLGRQMHVIVGQGQLDAVLSATPEDRRGFIEEAAGVLKHRKRKERALRKLESMAADLARVADLTQELRRQLGPLARQAAIARRARSIQVEVRDATARLLADDVVQAQSLLEAGDEDKEALARRRSAVEEAERVARARLSELAAIEITSAQRLARAGGIWEELTAAAQSLGALADVAGERIRLLASAPAPSHGTDPEELERRAEAAAREEAELADTLEAARTSLSDATRVRADAETAEKAADQELSAAQRRVSDRRETIARAGGRVASARSRHEASLAALEQARSALRAAEAREDSARAALAEAGGEAEPAQVAAGGARDAVVPAQVPAEAGAAADAAVRAAAVHDEAARRLAQAREAVAAATDARREAASDRATWTARRDTLAMSLRGQDGTAALLQAGIDGLLGPLAEHLNVERGWENAVAALLGTLAEAGLATDAEAALAGLDHARSQDIGAVRLVLADDPSLTAEADTDEEAGAAPVDGALAAHDLVGPAQPGRLERVLDRLLKDSWVVEDLEAARTLRSELPDAIVATRSGDVLAPGWVAGAGRGASSVLELTAAHEEADTEAAAAAQAETEADAALEEARRQEDAARQALSEALSALRQADAEAARAAEAMARLTSAAHAAAEETGRARRVLERAEAESVQRTAELAAATAALAEVEDGVGDTRDGDGVGGAGGAGAAGASGKGSPDSLERALEVARREREAAADTARQARAAETDARLALRTAEERERSSRGRADSLRAAARRERDQRAAAERAQQRRSAQLAVATHVRDQARAAAEAARLSVQQAADERAAIETERAQALAATNEVREEIDRLTKELGSLTDAAHREEVARAEQRMRLEALAERAMNELGLELDPLVEEYGPHMLVPELIEDAEAAADSGSDSAAVQETAQVSAGGSGHLGRPYVRSEQEKRLAKASRDLARLGKVNPLALEEHAALEQRHQFLAEQLADLKRSRDDLLSIVEEIDARVQEVFAQAYEDTARQFASVFDRLFPGGEGRLVLTDPDDMLTTGIEIEARPAGKKVKRLSLLSGGERSLAAVALLVAIFKARPSPFYVMDEVEAALDDTNLGRLLEIFTELRRSSQLIIITHQKRTMEVADALYGITMRDGVTKAVSQRLAQPDRGTAVTPDV$","Chromosome segregation protein SMC","Cytoplasm","Chromosome partition protein smc","chromosome segregation protein SMC","chromosome segregation protein SMC","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003395
Domain

SMC protein, N-terminal
PF02463	$\"[2-1249]T$	SMC_N

InterPro
IPR003439
Domain

ABC transporter related
PS00211	$\"[1167-1181]?$	ABC_TRANSPORTER_1

InterPro
IPR010935
Domain

SMCs flexible hinge
PF06470	$\"[531-653]T$	SMC_hinge

InterPro
IPR011890
Family

Chromosome segregation protein SMC
TIGR02168	$\"[2-1255]T$	SMC_prok_B: chromosome segregation protein

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-248]T$ $\"[1104-1257]T$	no description
PTHR18937	$\"[22-433]T$ $\"[453-797]T$ $\"[828-1018]T$ $\"[1037-1263]T$	STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER
PTHR18937:SF10	$\"[22-433]T$ $\"[453-797]T$ $\"[828-1018]T$ $\"[1037-1263]T$	STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC, BACTERIAL

","No hits to the COGs database.","***** IPB010935 (SMCs flexible hinge) with a combined E-value of 1.6e-36. IPB010935A 26-44 IPB010935D 1167-1202","Residues 5-44 are 95% similar to a (DNA REPAIR ATP-BINDING REPLICATION CHROMOSOME RECF SOS DNA-BINDING DAMAGE RECOMBINATION) protein domain (PD000596) which is seen in SMC_MYCLE.Residues 63-150 are similar to a (CHROMOSOME SMC SEGREGATION ATP-BINDING PARTITION MAINTENANCE STRUCTURAL COIL COILED CELL) protein domain (PD002128) which is seen in Q6AE90_BBBBB.Residues 154-205 are 92% similar to a (CHROMOSOME SMC ATP-BINDING SEGREGATION PARTITION MAINTENANCE STRUCTURAL COIL COILED CELL) protein domain (PD754575) which is seen in SMC_MYCTU.Residues 927-1005 are 63% similar to a (CHROMOSOME SEGREGATION SMC PARTITION COILED COIL ATP-BINDING ATPASES PROBABLE ASSOCIATED) protein domain (PD110600) which is seen in SMC_MYCTU.Residues 1045-1104 are similar to a (CHROMOSOME SMC SEGREGATION ATP-BINDING PARTITION COILED COIL HOMOLOG PROTEIN MAINTENANCE) protein domain (PD328842) which is seen in Q82JU6_STRAW.Residues 1111-1161 are similar to a (CHROMOSOME SMC SEGREGATION ATP-BINDING PARTITION COILED COIL MAINTENANCE STRUCTURAL CONDENSATION) protein domain (PD536994) which is seen in Q82JU6_STRAW.Residues 1175-1224 are similar to a (ATP-BINDING CHROMOSOME SMC SEGREGATION PLASMID PARTITION ABC ATPASE PROTEIN TRANSPORTER) protein domain (PD137161) which is seen in Q6AE90_BBBBB.Residues 1176-1209 are 94% similar to a (CHROMOSOME ATP-BINDING STRUCTURAL MAINTENANCE SEGREGATION COIL COILED CELL CYCLE NUCLEAR) protein domain (PD989789) which is seen in Q8NNW5_CORGL.","","-63% similar to PDB:1E69 SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA (E_value = 6.5E_33);-63% similar to PDB:1XEW Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases. (E_value = 2.2E_28);-63% similar to PDB:1XEX Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases. (E_value = 4.8E_28);-47% similar to PDB:1W1W SC SMC1HD:SCC1-C COMPLEX, ATPGS (E_value = 5.2E_14);","Residues 2 to 1249 (E_value = 6.7e-119) place ANA_1211 in the SMC_N family which is described as RecF/RecN/SMC N terminal domain.Residues 531 to 653 (E_value = 1.7e-09) place ANA_1211 in the SMC_hinge family which is described as SMC proteins Flexible Hinge Domain.","","partition protein smc","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1212","1289706","1290653","948","5.56","-5.83","33672","ATGCTTGAACTGTCCGGCCTGTCCAAACGCTTCGGGAGCCTGCAGGCCCTGGACGATCTCTCCTTGTCCCTGGACCGCGGTGAGATTGTTGGCTTCGTCGGTGCGAACGGAGCGGGCAAGTCCACCACGATGCGCATCGTCATGGGGGTGCTCCACGCTGACGCCGGCACCGTGACCTGGAAGGGAACCCCCGTGGACGCCACCATCCGCCGCAGTATCGGCTATATGCCTGAGGAGCGCGGCCTCTACCCCCGAATGAAGGTGGCCGAGCAGCTCATCTACCTGGCCCGTCTCCACGGTCTGTCCGCCTCCGCTGCCAAGGCGGCCGCGAGCCAGTGGACCGAGCGCCTGGGCCTGGAGGAGCGCCGCGGCGACGAGGTGCAGAGCCTGTCGCTGGGCAACCAGCAGCGTGTCCAGCTGGCTGCCGCGCTGGTGAGCAGCCCCGAGCTGCTCATTCTCGATGAGCCCTTCTCCGGCCTGGATCCGGTGGCCGTGGACGTCATGAGCCAGGTCATCCTGGAGCGGGCGGCAGCAGGCGTGCCCACGCTGTTCTCCTCCCACCAGCTCGACGTCGTCGAGCGCCTGTGCGACCGGGTGGTCATCGTCCGCTCGGGCCGGCTCGTGGCCGATGGGACGATTCCCGATCTGCAGGCCACCGCGACGCCCCGTTGGCGGGCCGTTGTCGAGCCGGCCGCGGGGAGCGCACCAGTGCAGACCGCCTCCTTGAACCTGCCCGCCCCCACGCTCGTGGTCGATGACGCCGGCCGCCTGGTCATCACCGCGGCAGGAGCCGATGAGCAGGAGCTGCTGAGCACGGCCCAGCGCCTGGGGACGGTGCGCGAGCTCGGCCCGGTGCGCCACCGGCTCACCGAGATTTTCCGGGATGTGCTGACCACGCCCTCCCGTGAGGGAACCGCCGACACCAATGAGACGAAGGAGACGCACTGA","MLELSGLSKRFGSLQALDDLSLSLDRGEIVGFVGANGAGKSTTMRIVMGVLHADAGTVTWKGTPVDATIRRSIGYMPEERGLYPRMKVAEQLIYLARLHGLSASAAKAAASQWTERLGLEERRGDEVQSLSLGNQQRVQLAAALVSSPELLILDEPFSGLDPVAVDVMSQVILERAAAGVPTLFSSHQLDVVERLCDRVVIVRSGRLVADGTIPDLQATATPRWRAVVEPAAGSAPVQTASLNLPAPTLVVDDAGRLVITAAGADEQELLSTAQRLGTVRELGPVRHRLTEIFRDVLTTPSREGTADTNETKETH$","ABC-type multidrug transport system, ATPase component","Membrane, Cytoplasm","ABC transporter (ATP-binding protein) homologyhaQ","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[130-172]T$	Q6A986_PROAC_Q6A986;
PF00005	$\"[27-205]T$	ABC_tran
PS50893	$\"[2-229]T$	ABC_TRANSPORTER_2
PS00211	$\"[130-144]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[26-205]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-220]T$	no description
PTHR19222	$\"[2-236]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 16 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.3e-29. IPB013563A 16-50 IPB013563C 127-154 IPB013563D 181-233***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.1e-24. IPB005074C 16-63 IPB005074D 118-161***** IPB005116 (TOBE domain) with a combined E-value of 1.4e-14. IPB005116A 34-50 IPB005116B 71-88 IPB005116C 130-143 IPB005116D 150-169***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 8.9e-11. IPB010509B 27-52 IPB010509D 125-169***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.6e-08. IPB010929K 14-58 IPB010929L 60-112 IPB010929M 127-173","Residues 2-101 are 57% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA188U2) which is seen in Q9RXA9_DEIRA.Residues 26-101 are 59% similar to a (ATP-BINDING NATA ABC TRANSPORTER) protein domain (PD742287) which is seen in O83851_TREPA.Residues 26-101 are 53% similar to a (ATP-BINDING TRANSPORTER YTHP) protein domain (PDA188Y3) which is seen in O34977_BACSU.Residues 26-187 are 50% similar to a (BIOGENESIS ATP-BINDING CYTOCHROME MEMBRANE HYDROLASE MITOCHONDRION EXPORT C CCMA C-TYPE) protein domain (PD732591) which is seen in CCMA_RECAM.Residues 27-204 are 46% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 27-99 are 59% similar to a (ATP-BINDING NODULATION LONG 276AA) protein domain (PD247867) which is seen in Q9YAK6_AERPE.Residues 27-65 are 76% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q6A986_PROAC.Residues 27-99 are 58% similar to a (ATP-BINDING PHOSPHONATE ABC-TYPE PROTEIN) protein domain (PDA0J3O0) which is seen in Q6MPJ3_BDEBA.Residues 27-176 are 48% similar to a (LD11139P ATP-BINDING CG11069-PA) protein domain (PD694001) which is seen in Q8MRJ2_DROME.Residues 27-189 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 27-214 are 42% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 30-211 are 43% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD738128) which is seen in Q8G833_BIFLO.Residues 125-217 are 60% similar to a (MULTIDRUG COMPONENT ABC-TYPE SYSTEM ATPASE ATP-BINDING) protein domain (PD622343) which is seen in Q8RBM5_THETN.Residues 127-215 are 52% similar to a (ATP-BINDING SUGAR ABC TRANSPORTER) protein domain (PDA0I778) which is seen in Q98JJ1_RHILO.Residues 127-208 are 57% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 129-210 are 59% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 130-212 are 60% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PD957735) which is seen in Q73JF3_TREDE.Residues 130-211 are similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD729639) which is seen in Q828Y1_STRAW.Residues 130-172 are 86% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q6A986_PROAC.Residues 130-202 are 60% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ABC-TYPE MULTIDRUG LMO2240 LMO2769 ABC-NBD) protein domain (PD353124) which is seen in Q88VS9_LACPL.Residues 130-210 are 56% similar to a (ATP-BINDING) protein domain (PDA0K5N1) which is seen in Q73TI7_MYCPA.","","-51% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 7.1E_27);-47% similar to PDB:2ONK ABC transporter ModBC in complex with its binding protein ModA (E_value = 1.5E_16);-44% similar to PDB:1JI0 Crystal Structure Analysis of the ABC transporter from Thermotoga maritima (E_value = 7.3E_16);-44% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.1E_15);-44% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 2.1E_15);","Residues 27 to 205 (E_value = 5.4e-53) place ANA_1212 in the ABC_tran family which is described as ABC transporter.","","transporter (ATP-binding protein) homolog yhaQ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1214","1290653","1291897","1245","6.96","-0.10","43443","ATGAGCGACCGGACCATCCCTATTACTCGCCGTCAGGAGATCGCCCTGGTCACCGGCCGCGAGCTGCGGGCGCACCTGCTGAAGAAGTCGACCATCATCCTGACCCTGGTGCTGCTCATCGCCGCCGTCGGCGGCATCGTCGGCGTCAAGCTCTACACCTCGGGCCAGGACCAGGCCTACCGGATCGGGCTCAAGGGCATGTCCCTCTCCCAGGCCGCCGGCCTGGACAAGGCGGCCGCCTCCAACGGGGAGGCGATCGAGCTCGTCGACGTCTCCGCCCACCAGGCGAAGGACGTCCTGGCCGATGACGCCCCCGAGGGCACGCCGCACGTGGACATGGTCCTGGACGTCTCCGGCTCGACCCCCACCATCACTGTGGACAAGTCAGCCGACGACGCAGTCGTCTCAGGGGTCACTGCCTTCCTCCAGCAGTCGGCTCTGGGCCAGCAGATCGCGTCCCTGGGAGGCGACCCCGCCCAGGTGGCCTCTCAGCTCAGTGCCGCCAAGCCCGAGGTGACAGTGCTCCACGCCCCTCAACGCGATTCGGCCGACTTCGGCTCACGCTACGCGATCCTCATGACGATCGACATCCTGCTGCTGTTCGCCATCATGGGAGGCGGTCAGTTCATCGCCCAGGGAGTGGTGGAGGAGAAGTCGAGCCGGATCGTGGAGATCCTCCTGGCCTGCGTGCGGCCCAGCTCGCTGCTGGCCGGCAAGATCCTGGGGATCGGCATCGCCTCGGTCCTGACCACAGGACTCGTCGCCGTCGTCGGAGTCATCACCGCGAAGGCCACGGGAGTCATGCCGGAGATCAGCCTCAACCTGGACGGCGTGCTCGTCGCAATGATCGTGTGGATGATCGTGGGCTATGCAATCTTCTCGGTCGCCTTCGGGGCCGCGGCCTCGCTCGTGAGCCGCCAGGAGGACGTCAGCTCGGTGAGCATGCCCCTGGTCATGCTCTCGATGATCCCCTATGTCCTGAGCTTCATGATGGCCACCGGAGACACCAACAGCATGACCTTCCGAGTGCTGTCCTACCTGCCGCCCTTCTCCCCCTTCATGATGCCTGCGCGCCTGGTGCTGGGGGTCTCCTCCTGGACCGAGCAGTTGATCGCCCTGGGGCTCGCGCTCGTCTTCCTGCCACTGCTGGTGCGCGTGGCGGCGGCGATCTACACCCGGGCCGTCACCCGCACCGGCGCCCGAGTCCCCCTCAAGGAGGTCCTCAGGAGGGCCGAACGGGCCTGA","MSDRTIPITRRQEIALVTGRELRAHLLKKSTIILTLVLLIAAVGGIVGVKLYTSGQDQAYRIGLKGMSLSQAAGLDKAAASNGEAIELVDVSAHQAKDVLADDAPEGTPHVDMVLDVSGSTPTITVDKSADDAVVSGVTAFLQQSALGQQIASLGGDPAQVASQLSAAKPEVTVLHAPQRDSADFGSRYAILMTIDILLLFAIMGGGQFIAQGVVEEKSSRIVEILLACVRPSSLLAGKILGIGIASVLTTGLVAVVGVITAKATGVMPEISLNLDGVLVAMIVWMIVGYAIFSVAFGAAASLVSRQEDVSSVSMPLVMLSMIPYVLSFMMATGDTNSMTFRVLSYLPPFSPFMMPARLVLGVSSWTEQLIALGLALVFLPLLVRVAAAIYTRAVTRTGARVPLKEVLRRAERA$","ABC-type multidrug transport system, permease component","Membrane, Cytoplasm","hypothetical ABC transporter, putative","K01992 ABC-2 type transport system permease protein","ABC-type Na+ efflux pump permease component-like","","Saenz H.L., Augsburger V., Vuong C., Jack R.W., Gotz F, Otto M. Inducible expression and cellular location of AgrB, a protein involved in the maturation of the staphylococcal quorum-sensing pheromone. Arch. Microbiol. 2000. 174(6):452-455. PMID: 11195102Zhang L., Gray L., Novick R.P., Ji G. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 2002. 277(38):34736-34742. PMID: 12122003","","","

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[226-396]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-48]?$	signal-peptide
tmhmm	$\"[32-52]?$ $\"[240-262]?$ $\"[277-297]?$ $\"[311-329]?$ $\"[344-364]?$ $\"[370-390]?$	transmembrane_regions

","BeTs to 5 clades of COG1668COG name: ABC-type Na+ efflux pump, permease componentFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1668 is aom-kz--vd-lb-----s--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 200-294 are 58% similar to a (ABC PERMEASE TRANSPORTER MEMBRANE ATP-BINDING TRANSPORTER TRANSMEMBRANE PROTEIN COMPONENT INTEGRAL) protein domain (PD115342) which is seen in Q9RMQ7_MYCSM.","","-44% similar to PDB:2P4E Crystal Structure of PCSK9 (E_value = );-44% similar to PDB:2PMW The Crystal Structure of Proprotein convertase subtilisin kexin type 9 (PCSK9) (E_value = );-46% similar to PDB:1VI1 Crystal structure of a fatty acid/phospholipid synthesis protein (E_value = );","No significant hits to the Pfam 21.0 database.","","ABC transporter, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1215","1292461","1292021","441","5.30","-5.09","15702","ATGGCAAGCACTTCCCACGCCGGCCGCATCCTCATCCTCATCAAGCCCGACGCCGTTGAGCGGCGTCTCACCGGTGAGATCCTGCGTCGTATCGAGGCCAAGGGGTACGCCCTGACGGCCCTGAAGGTCCTCACCCCCACTGAGGAGATCCTCGCCCAGCACTACGCCGAGCACGTGGACAAGCCCTTCTATCCCGGTGTTGTGGAGTACATGACCTCCGGCAACGTGGTGGCTGCAGTTGCTGAGGGGCAGCGTGTCGTCGAGGGCGTGCGCAGCCTCATGGGTCCCACCGACCCCACCACGGCCGCGCCCGGCACCATCCGCGGAGACCTGGGACGTGACTGGGGCACCCCCGCCATCCTCAACCTCGTCCACGGCTCGGACAGCGACGAGTCCGCCGCCCGTGAGATCGCCATCTGGTTCCCCGAGCTGGCTGACTGA","MASTSHAGRILILIKPDAVERRLTGEILRRIEAKGYALTALKVLTPTEEILAQHYAEHVDKPFYPGVVEYMTSGNVVAAVAEGQRVVEGVRSLMGPTDPTTAAPGTIRGDLGRDWGTPAILNLVHGSDSDESAAREIAIWFPELAD$","Nucleoside diphosphate kinase","Cytoplasm","Nucleoside diphosphate kinase (NDK) (NDPkinase)(Nucleoside-2-P kinase)","nucleoside diphosphate kinase ","Nucleoside-diphosphate kinase","","Chakrabarty A.M. Nucleoside diphosphate kinase: role in bacterial growth, virulence, cell signalling and polysaccharide synthesis. Mol. Microbiol. 1998. 28(5):875-882. PMID: 9663675Gilles A.M., Presecan E., Vonica A., Lascu I. Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J. Biol. Chem. 1991. 266(14):8784-8789. PMID: 1851158Janin J., Dumas C., Morera S., Xu Y., Meyer P., Chiadmi M., Cherfils J. Three-dimensional structure of nucleoside diphosphate kinase. J. Bioenerg. Biomembr. 2000. 32(3):215-225. PMID: 11768305","","","

InterPro
IPR001564
Domain

Nucleoside diphosphate kinase
PD001018	$\"[11-141]T$	Q6AFY7_BBBBB_Q6AFY7;
PR01243	$\"[10-32]T$ $\"[54-73]T$ $\"[74-91]T$ $\"[122-141]T$	NUCDPKINASE
G3DSA:3.30.70.141	$\"[5-143]T$	no description
PF00334	$\"[9-144]T$	NDK
SM00562	$\"[7-146]T$	NDK

InterPro
IPR012005
Family

Nucleoside-diphosphate kinase
PIRSF000735	$\"[11-144]T$	Nucleoside diphosphate kinase

noIPR
unintegrated

unintegrated
PTHR11349	$\"[52-143]T$	NUCLEOSIDE DIPHOSPHATE KINASE

","BeTs to 24 clades of COG0105COG name: Nucleoside diphosphate kinaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0105 is aompkzyq-dr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001564 (Nucleoside diphosphate kinase) with a combined E-value of 5.3e-47. IPB001564A 8-42 IPB001564B 51-90 IPB001564C 99-141 IPB001564C 95-137***** IPB006602 (Protein of unknown function DM10) with a combined E-value of 3.9e-10. IPB006602D 27-75 IPB006602E 76-103 IPB006602F 105-131","Residues 11-141 are similar to a (KINASE DIPHOSPHATE NUCLEOSIDE TRANSFERASE NDP NDK ATP-BINDING NUCLEOSIDE-2-P I B) protein domain (PD001018) which is seen in Q6AFY7_BBBBB.","","-63% similar to PDB:1K44 Mycobacterium tuberculosis Nucleoside Diphosphate Kinase (E_value = 7.3E_30);-62% similar to PDB:1B99 3'-FLUORO-URIDINE DIPHOSPHATE BINDING TO NUCLEOSIDE DIPHOSPHATE KINASE (E_value = 8.1E_29);-62% similar to PDB:1BUX 3'-PHOSPHORYLATED NUCLEOTIDES BINDING TO NUCLEOSIDE DIPHOSPHATE KINASE (E_value = 8.1E_29);-62% similar to PDB:1F6T STRUCTURE OF THE NUCLEOSIDE DIPHOSPHATE KINASE/ALPHA-BORANO(RP)-TDP.MG COMPLEX (E_value = 8.1E_29);-62% similar to PDB:1HIY BINDING OF NUCLEOTIDES TO NDP KINASE (E_value = 8.1E_29);","Residues 9 to 144 (E_value = 4.4e-62) place ANA_1215 in the NDK family which is described as Nucleoside diphosphate kinase.","","diphosphate kinase (NDK) (NDP kinase)(Nucleoside-2-P kinase) (NDK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1216","1293229","1292549","681","5.20","-6.33","22969","ATGTCCTTAGACGCCGCCTGGGCCCTTGAGTGGGCCCGTCGCGCCGCCGAGCTGATCGCCGAGAACCGCGCGGAGCTGACCGAGCTGGACCGAGCCATCGGAGACGCCGACCACGGGGACAACCTGGAGCGCGGCATGAAGGCGGTGGTCTCCAAGCTCGATGCCGCTCAGCAGTCCGGAGGTGTCCTAGCAAGTCCCGGAGGGGTCCTCAAGCTCGTCGCCACCACGCTCATGGCCACCGTCGGTGGTGCCGGTGGGCCACTGCTGGGAACGGCCTTCCTCAAGGCCGCCCGCTCCAGTGAGGCTGCCGCTTGGGGGCCTGGGGACCTGGCTCGCGCCCTGGAGGAGGCCACCTCGGGTCTGGAGGCCAGAGGACATGCCATCAGCGGTGACAAGACCATGGCCGATGCCTGGCGGCCCGCGGCGATGGCCGCCAGGGAAGCCGCCGAGAGCGGGCAGGACGAGGTCGGTGTTCTCGCCGCAGCCGCGCAGGCCGCGGCCACGGGTGCCCAGAAGACCGAGCCTCTCCAGGCCCGTCGTGGTCGGGCCTCCTTCCTGGGGGAACGCTCCTGCGGCCACCGCGATCCCGGAGCCCAGTCCTCCGCACTCATCCTTCAGGCCGCCCTCGATGCCGCCCGCGACCGCGCCGCCGACCCGATCCTGGTCGTCGAGCAGGCCTGA","MSLDAAWALEWARRAAELIAENRAELTELDRAIGDADHGDNLERGMKAVVSKLDAAQQSGGVLASPGGVLKLVATTLMATVGGAGGPLLGTAFLKAARSSEAAAWGPGDLARALEEATSGLEARGHAISGDKTMADAWRPAAMAAREAAESGQDEVGVLAAAAQAAATGAQKTEPLQARRGRASFLGERSCGHRDPGAQSSALILQAALDAARDRAADPILVVEQA$","Dihydroxyacetone kinase","Cytoplasm","Dihydroxyacetone kinase","dihydroxyacetone kinase ","dihydroxyacetone kinase, L subunit","","","","","

InterPro
IPR004007
Domain

Dak phosphatase
PF02734	$\"[32-210]T$	Dak2

InterPro
IPR012737
Domain

Dihydroxyacetone kinase, subunit L
TIGR02365	$\"[8-210]T$	dha_L_ycgS: dihydroxyacetone kinase, L subu

","BeTs to 3 clades of COG2376COG name: Dihydroxyacetone kinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2376 is ------y--d-lb-e--h---j----Number of proteins in this genome belonging to this COG is 3","***** IPB004007 (Dak phosphatase domain) with a combined E-value of 5.8e-17. IPB004007A 33-49 IPB004007B 73-93 IPB004007C 117-142 IPB004007A 20-36","No significant hits to the ProDom database.","","-50% similar to PDB:2BTD CRYSTAL STRUCTURE OF DHAL FROM E. COLI (E_value = 6.6E_23);","Residues 32 to 210 (E_value = 3.6e-50) place ANA_1216 in the Dak2 family which is described as DAK2 domain.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1217","1295404","1293548","1857","4.58","-53.50","65541","TTGAGAGAGCCTCTGTCCAGCCCGTCACGTCGAGTAAAGGATGGCACAGTGCCCGTAGACGACGACTCCAAGCAGGTCAGGCCCGGCGCCGCCTTCGGCATCCCCGAAGGGGCCACGGGGGAGGAGGTCGTCGACGCCGTCTTCGGCCGGGCCGGCATCGACCCCGAGCTCCTGCCCTATCTGGAGGCCGCAGGCGCCCCCGACCTGGCCGAGGGCGAGGGGCTGACCGTCTCCGTCTCCGAGCTTCAGGAGGCCGGTGCTCAGCGACAGGCTGACGCTGAGGCCCAGGACCGCGAGGACCTCGAGGCTCTGCGCGAGCTCGTTGCCGCCAATATGATCCCCGGCGGTGACGCTGATCGCCTCGAGGAGATACTGGCTGAGGTGGAGGCCGACGACTCCGACGACTGGGAATCCTGGGAGCCCCAGCTCGCCGACGACTCCGAGGGTGAGCACCTGCGCGATCTGCGGGCCGCCGCCCGCGGCGTCGAGGTCGCCGCCCGCATGCGCGAGGTCGAGGCCGAGATCCTCGCGCGCGCCCCCGAGCACCAGGTCCAGCCCTCCCTGGAGCGGGTCGAGGCCGTCCTCGACCTCCTGGGCAACCCCGAGCGCACCTACCGCACCGTCCACATCACCGGCACCAACGGCAAGACCTCCACCGCCCGTATGACCGAGCGACTGCTGGCCGCCGGCGGCATGCGCACCGGCCGCTTCACCTCCCCGCACCTGGCCACCATCCGCGAGCGCATCAGCCTCGACGGTGAACCGATCAGTGAGGAGGGCTTCATCGCCGCCTGGGAGGACGTGGCCCCATACGTCGCCATGGTCGACGAGCGCTCCCAGACCGCAGGCGGGCCCCGCCTGTCCTTCTTCGAGGTCCTGGCCGTCATGGCTCTGGCCGCCTTCGCCGACTACCCCGTCGACGTCGCCGTCATCGAGGTGGGCCTGGGCGGACGGTGGGACGCCACGAACGTCATCGGCTCCGACGTCGCCGTCATCACCCCGATCGGGCGCGACCACGAGCGTTGGCTGGGCTCGTCGATCACCGAGATCGCCCATGAGAAGGCCGGCATCATCAAGGACGGTTCCACTGTCATCGTCGCCCACCAGGTCCCCGAGGCGGCCGCTGAGATCGAGCAGACCGCGGCCTCTCACCGGGCCATCGTGCGCCGGGAGCGGGACCCTCAGGAGGATCCCACCTCACCGGAGGCCGGCGTCCTGCAGGTCCTCGACCGTCAGCTCGCCGTCGGCGGTCAGATGGTCACCTTCGCCACGGCGGCGGCCGTCTATGAGGATGTCTTCGTTCCGCTGCACGGGGAGTACCAGGCCCACAATGCCCTGCTGGCCCTGGCGGCCGCCGAGGCGGTCCACGGCGGGCGCCGGCTGCCGGCACGCATCGTCGAGGACGGCTTTGCCTCCGTCACCAGCCCGGGCCGTCTGGAGGTGCTGCGCTCCTCGCCCACCGTCCTGGTCGACGCCGGGCACAACCCGCACGGCATCGAGGCCCTCACCGGAGCCATCGAGGAGGCCTTCGGCTTCCAGCACCTCGTCGCGGTCCTGGGCGTCATGGCCGATAAGGACGCCGAGGGCATCCTGGCGGGCCTGGAGCCCGTCACTGACGCCGTCGTGTGCGTCCCCATCGACTCGCCTCGGGCCATGGACGTCGAGGACCTCGGTGAGATCGCCCGGGAGGTCTACGGTGCCGACCGCGTCGTGGTGAGTCAGCAGCTCGGCGAGGGGGTGGAGCGGGCGGTCGCCCTGTCCGAGGGGTATGACGCCCCGCTAACCGCCTCGGGAATCCTCATCGTCGGCTCCGTGGTCCTGGCTGCCGAGGCTCGCGCTCTGTTCGGCAGGCCCTGA","LREPLSSPSRRVKDGTVPVDDDSKQVRPGAAFGIPEGATGEEVVDAVFGRAGIDPELLPYLEAAGAPDLAEGEGLTVSVSELQEAGAQRQADAEAQDREDLEALRELVAANMIPGGDADRLEEILAEVEADDSDDWESWEPQLADDSEGEHLRDLRAAARGVEVAARMREVEAEILARAPEHQVQPSLERVEAVLDLLGNPERTYRTVHITGTNGKTSTARMTERLLAAGGMRTGRFTSPHLATIRERISLDGEPISEEGFIAAWEDVAPYVAMVDERSQTAGGPRLSFFEVLAVMALAAFADYPVDVAVIEVGLGGRWDATNVIGSDVAVITPIGRDHERWLGSSITEIAHEKAGIIKDGSTVIVAHQVPEAAAEIEQTAASHRAIVRRERDPQEDPTSPEAGVLQVLDRQLAVGGQMVTFATAAAVYEDVFVPLHGEYQAHNALLALAAAEAVHGGRRLPARIVEDGFASVTSPGRLEVLRSSPTVLVDAGHNPHGIEALTGAIEEAFGFQHLVAVLGVMADKDAEGILAGLEPVTDAVVCVPIDSPRAMDVEDLGEIAREVYGADRVVVSQQLGEGVERAVALSEGYDAPLTASGILIVGSVVLAAEARALFGRP$","Folylpolyglutamate synthase","Cytoplasm","folylpolyglutamate synthase","putative folylpolyglutamate synthase ","FolC bifunctional protein","","Sun X., Bognar A.L., Baker E.N., Smith C.A. Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(12):6647-6652. PMID: 9618466","","","

InterPro
IPR001645
Family

Folylpolyglutamate synthetase
TIGR01499	$\"[188-615]T$	folC: FolC bifunctional protein
PS01011	$\"[208-231]?$	FOLYLPOLYGLU_SYNT_1
PS01012	$\"[310-325]T$	FOLYLPOLYGLU_SYNT_2

InterPro
IPR004101
Domain

Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875	$\"[475-559]T$	Mur_ligase_C

InterPro
IPR013188
Domain

Influenza matrix M1, C-terminal
SM00759	$\"[337-423]T$	no description

InterPro
IPR013221
Domain

Mur ligase, middle region
PF08245	$\"[208-452]T$	Mur_ligase_M

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.10	$\"[154-476]T$	no description
G3DSA:3.90.190.20	$\"[477-615]T$	no description
PTHR11136	$\"[192-397]T$ $\"[414-615]T$	FOLYLPOLYGLUTAMATE SYNTHASE-RELATED

","BeTs to 19 clades of COG0285COG name: Folylpolyglutamate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0285 is -o-p--yqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB001645 (Folylpolyglutamate synthetase) with a combined E-value of 1.6e-71. IPB001645A 207-249 IPB001645B 290-325 IPB001645C 330-363 IPB001645D 491-503 IPB001645E 599-614***** IPB000713 (Cytoplasmic peptidoglycan synthetases, N-terminal) with a combined E-value of 2.1e-12. IPB000713A 208-219 IPB000713B 331-341 IPB000713C 488-507***** IPB013221 (Mur ligase, middle region) with a combined E-value of 1.1e-11. IPB013221A 210-219 IPB013221B 330-341 IPB013221C 438-448 IPB013221C 441-451","Residues 175-517 are 62% similar to a (SYNTHASE FOLYLPOLYGLUTAMATE LIGASE) protein domain (PDA1C1N8) which is seen in Q6A9I9_PROAC.Residues 175-444 are 63% similar to a (SYNTHASE FOLYLPOLYGLUTAMATE) protein domain (PDA19057) which is seen in Q8G4M5_BIFLO.Residues 176-606 are 49% similar to a (3D-STRUCTURE FOLYLPOLY-GAMMA-GLUTAMATE SYNTHETASE METABOLISM FPGS ATP-BINDING ONE-CARBON SYNTHASE FOLYLPOLYGLUTAMATE LIGASE) protein domain (PD722577) which is seen in FOLC_LACCA.Residues 176-612 are 48% similar to a (SYNTHETASE FOLYLPOLYGLUTAMATE METABOLISM LIGASE ATP-BINDING ONE-CARBON) protein domain (PD760024) which is seen in O67833_AQUAE.Residues 177-383 are 52% similar to a (FOLC METABOLISM ATP-BINDING ONE-CARBON LIGASE) protein domain (PD435771) which is seen in Q9X7F5_METCH.Residues 184-427 are 53% similar to a (METABOLISM ATP-BINDING ONE-CARBON SYNTHASE FOLYLPOLYGLUTAMATE LIGASE) protein domain (PDA1B7D6) which is seen in Q7NLP7_GLOVI.Residues 184-371 are 55% similar to a (SYNTHASE FOLYLPOLYGLUTAMATE METABOLISM LIGASE ATP-BINDING ONE-CARBON) protein domain (PD996379) which is seen in Q6MAP9_PARUW.Residues 184-367 are 54% similar to a (SYNTHASE INCLUDES: FOLATE FOLYLPOLY-GAMMA-GLUTAMATE BIOSYNTHESIS DIHYDROFOLATE MULTIFUNC FOLC SYNTHETASE FOLYLPOLYGLUTAMATE) protein domain (PD996346) which is seen in FOLC_BUCBP.Residues 184-532 are 50% similar to a (FOLYL-POLYGLUTAMATE SYNTHETASE LIGASE) protein domain (PD996345) which is seen in Q9K8G9_BACHD.Residues 185-444 are 51% similar to a (SYNTHASE DIHYDROPTEROATE) protein domain (PD763344) which is seen in Q9HS44_HALN1.Residues 186-494 are 44% similar to a (FOLC SYNTHETASE METABOLISM ATP-BINDING ONE-CARBON FOLYLPOLYGLUTAMATE LIGASE) protein domain (PD170687) which is seen in O83360_TREPA.Residues 187-377 are 55% similar to a (SYNTHASE FOLC FOLYLPOLYGLUTAMATE METABOLISM LIGASE ATP-BINDING ONE-CARBON) protein domain (PD996347) which is seen in Q98CN4_RHILO.Residues 187-369 are 56% similar to a (METABOLISM ATP-BINDING ONE-CARBON SYNTHASE DIHIDROFOLATE LIGASE) protein domain (PDA1A698) which is seen in Q84FV7_METEX.Residues 188-408 are 52% similar to a (FOLYL-POLYGLUTAMATE SYNTHETASE METABOLISM ATP-BINDING ONE-CARBON LIGASE) protein domain (PD517901) which is seen in Q8XJ43_CLOPE.Residues 188-386 are 56% similar to a (METABOLISM ATP-BINDING ONE-CARBON SYNTHASE FOLYLPOLYGLUTAMATE LIGASE) protein domain (PDA190S3) which is seen in Q8RBN3_THETN.Residues 190-444 are 69% similar to a (LIGASE SYNTHASE ATP-BINDING METABOLISM ONE-CARBON FOLYLPOLYGLUTAMATE SYNTHETASE FOLC BIFUNCTIONAL DIHYDROFOLATE) protein domain (PD003937) which is seen in Q82CA2_STRAW.Residues 206-361 are 47% similar to a (RELATED SYNTHETASE FOLYLPOLYGLUTAMATE) protein domain (PDA1D494) which is seen in Q7SFD9_NEUCR.Residues 206-403 are 46% similar to a (SYNTHASE FOLYLPOLYGLUTAMATE) protein domain (PDA1B429) which is seen in Q7M927_WOLSU.Residues 476-515 are 72% similar to a (LIGASE SYNTHASE FOLYLPOLYGLUTAMATE METABOLISM ATP-BINDING ONE-CARBON SYNTHETASE FOLC FOLYL-POLYGLUTAMATE BIFUNCTIONAL) protein domain (PD122331) which is seen in Q8FN66_COREF.Residues 516-611 are 62% similar to a (SYNTHASE FOLYLPOLYGLUTAMATE LIGASE METABOLISM ATP-BINDING ONE-CARBON FOLC SYNTHETASE FPGS GLUTAMATE) protein domain (PD982878) which is seen in Q8NN38_CORGL.","","-53% similar to PDB:1O5Z Crystal structure of Folylpolyglutamate synthase (TM0166) from Thermotoga maritima at 2.10 A resolution (E_value = 1.3E_55);-48% similar to PDB:1FGS FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI (E_value = 1.3E_49);-48% similar to PDB:1JBV FPGS-AMPPCP complex (E_value = 1.3E_49);-48% similar to PDB:1JBW FPGS-AMPPCP-folate complex (E_value = 1.3E_49);-48% similar to PDB:2GC5 G51S mutant of L. casei FPGS (E_value = 1.8E_49);","Residues 208 to 452 (E_value = 1e-06) place ANA_1217 in the Mur_ligase_M family which is described as Mur ligase middle domain.Residues 475 to 559 (E_value = 3.9e-15) place ANA_1217 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain.","","synthase (FPGS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1218","1295718","1297040","1323","5.19","-12.45","46481","ATGCGTTTGTCAGTGATTGGTTGCGGATATCTCGGTGCTGTTCACGCTGCGTCAATGGCGGAGCTTGGACATGATGTGGTGGGCGTGGACGTCGATGCTCGCAAGGTAAATCTTCTGAGTAACGGCAGGGCGCCGTTCTTCGAGCCCGAACTGGAAGGGCTTCTGGCCCGTAACGTGAAGGCCGGACGCCTGACCTTCACTCAGGACTTCTCCGCCATTGAGGGAGCCCAGGTCCATTTCATCGGCGTGGGCACACCGCAGTCCGAGTCGGGGGCGGCGGACATGACGTACGTCGACGCAGCTGTGACCGCCATGCTCCCCCACCTGGGGCACTGCACCAGCGGCCCCGAGGTGGTCGCCGGCAAGTCCACGGTTCCCGTTGGCACCGCCGCCCGCCTGTCCCAGCTGATCGAGCCGACCGGGGCGCTGCTGCTGTGGAACCCGGAGTTCTTGCGGGAGGGCTTCGCCGTTCAGGACACGCTGCGTCCGGACCGGATGGTCTACGGCCTGCCGGAGAATCCCGACGCCGCCGGCCGCGCCCAGGAGACGATGGACGCGGTCTACGCGCAGATCCTGGCCGCTGGCACCCCGCGCCTGGTCATGGACTACGCCACCGCCGAGCTGGTCAAGATCAGTGCGAACGCCTTCCTGGCCACGAAGATCTCCTTCATCAACGCCATGTCCCAGGTCTGCGACGCCGCGGGCGCCAATGTGACGGCCCTCGCTGAGGCGATCGGCATGGATGACCGTATCGGGCGCCGGTTCCTGCGCGCCGGTATCGGCTTCGGCGGAGGCTGTCTGCCCAAGGACATCCGTGCCTTCCAGGCCCGCGCCGGCGAGCTCGGCGTCGGCGACGCCCTGGCCTTCCTCGCGGAGGTCGATCGCGTCAACGACACCATGCGTGCCGGCGTCATCCGCACAGTCGCTGAGCTCCTCGGCGAGCACACGTCGGCGGCCACGGTGACGGTCCTAGGGGCCGCCTTCAAACCGGACAGCGACGACATGCGCAACTCCCCCGCCCTGGATCTCGCCGTGGAGCTGTCGGGCATGGTCGAGCGAGTCGTCGTGCACGACCCGGCCGCCGGCCCGATCCTCGCTCAGAGGACGAACCGCCCCTACGAGGTCGCCGCCTCAGCGCAGTCCGCCCTGGAGGGAACCGACCTGGTCATCATCGGCACGGAGTGGCGCGAGTACCAGGATCTTGACCCCGCCGAGGCGGCCGGTCTGGCACGTAACCGCTACGTCATTGACGGACGCAACTGCCTGGATGCGCAGGCCTGGAAGGCGGCCGGTTGGAGCTACCGCGGCATCGGCCGGCGGTGA","MRLSVIGCGYLGAVHAASMAELGHDVVGVDVDARKVNLLSNGRAPFFEPELEGLLARNVKAGRLTFTQDFSAIEGAQVHFIGVGTPQSESGAADMTYVDAAVTAMLPHLGHCTSGPEVVAGKSTVPVGTAARLSQLIEPTGALLLWNPEFLREGFAVQDTLRPDRMVYGLPENPDAAGRAQETMDAVYAQILAAGTPRLVMDYATAELVKISANAFLATKISFINAMSQVCDAAGANVTALAEAIGMDDRIGRRFLRAGIGFGGGCLPKDIRAFQARAGELGVGDALAFLAEVDRVNDTMRAGVIRTVAELLGEHTSAATVTVLGAAFKPDSDDMRNSPALDLAVELSGMVERVVVHDPAAGPILAQRTNRPYEVAASAQSALEGTDLVIIGTEWREYQDLDPAEAAGLARNRYVIDGRNCLDAQAWKAAGWSYRGIGRR$","UDP-glucose 6-dehydrogenase","Cytoplasm","Predicted UDP-glucose 6-dehydrogenase","UDP-glucose 6-dehydrogenase ","UDP-glucose 6-dehydrogenase","","Roychoudhury S., May T.B., Gill J.F., Singh S.K., Feingold D.S., Chakrabarty A.M. Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa. J. Biol. Chem. 1989. 264(16):9380-9385. PMID: 2470755Campbell R.E., Sala R.F., van de Rijn I., Tanner M.E. Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol. J. Biol. Chem. 1997. 272(6):3416-3422. PMID: 9013585","","","

InterPro
IPR001732
Domain

UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03721	$\"[1-193]T$	UDPG_MGDP_dh_N

InterPro
IPR013328
Domain

Dehydrogenase, multihelical
G3DSA:1.10.1040.10	$\"[211-304]T$	no description

InterPro
IPR014026
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation
PF00984	$\"[203-300]T$	UDPG_MGDP_dh

InterPro
IPR014027
Domain

UDP-glucose/GDP-mannose dehydrogenase, C-terminal
PF03720	$\"[322-424]T$	UDPG_MGDP_dh_C

InterPro
IPR014028
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding
PTHR11374	$\"[155-439]T$	UDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC DEHYDROGENASE

InterPro
IPR014360
Family

UDP-glucose/GDP-mannose dehydrogenase
PIRSF000124	$\"[1-439]T$	UDP-glucose/GDP-mannose dehydrogenase

InterPro
IPR014685
Family

UDP-glucose 6-dehydrogenase, bacterial
PIRSF500134	$\"[1-440]T$	UDP-glucose 6-dehydrogenase, bacterial type

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1870	$\"[316-435]T$	no description
G3DSA:3.40.50.720	$\"[1-210]T$	no description
PTHR11374:SF3	$\"[155-439]T$	UDP-GLUCOSE 6-DEHYDROGENASE
signalp	$\"[1-16]?$	signal-peptide

","BeTs to 13 clades of COG1004COG name: Predicted UDP-glucose 6-dehydrogenaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1004 is aom-k--q--rlbcefghs-ujx---Number of proteins in this genome belonging to this COG is 2","***** IPB001732 (UDP-glucose/GDP-mannose dehydrogenase) with a combined E-value of 1.6e-88. IPB001732A 2-13 IPB001732B 26-55 IPB001732C 76-86 IPB001732D 118-128 IPB001732E 144-169 IPB001732F 201-252 IPB001732G 261-270 IPB001732H 321-359","Residues 1-56 are 82% similar to a (DEHYDROGENASE UDP-GLUCOSE OXIDOREDUCTASE 6-DEHYDROGENASE NAD 3-HYDROXYISOBUTYRATE BIOSYNTHESIS UDP-GLUCOSE/GDP-MANNOSE UDP-GLCDH UDPGDH) protein domain (PD398280) which is seen in Q6AGX8_BBBBB.Residues 2-298 are 38% similar to a (LMBL) protein domain (PD824343) which is seen in Q54365_STRLN.Residues 61-101 are 80% similar to a (DEHYDROGENASE UDP-GLUCOSE 6-DEHYDROGENASE OXIDOREDUCTASE NAD UDP-GLUCOSE/GDP-MANNOSE 1.1.1.- BIOSYNTHESIS UDP-GLCDH UDPGDH) protein domain (PD190504) which is seen in Q6AGX8_BBBBB.Residues 61-438 are 44% similar to a (DEHYDROGENASE UDP-GLUCOSE/GDP-MANNOSE FAMILY UDP-GLUCOSE-6-DEHYDROGENASE) protein domain (PD102173) which is seen in Q93N63_COXBU.Residues 213-297 are similar to a (UDP-GLUCOSE DEHYDROGENASE 6-DEHYDROGENASE OXIDOREDUCTASE NAD UDP-GLCDH UDPGDH UDP-GLC SUGAR NUCLEOTIDE) protein domain (PD001282) which is seen in Q82DF7_STRAW.Residues 251-401 are 45% similar to a (NDP-N-ACETYL-D-GALACTOSAMINURONIC OXIDOREDUCTASE DEHYDROGENASE ACID 1.1.1.-) protein domain (PDA0U115) which is seen in Q8PXR2_METMA.Residues 290-437 are 44% similar to a (UDP-GLUCOSE 6-DEHYDROGENASE) protein domain (PDA131E5) which is seen in Q6NEW8_CORDI.Residues 320-425 are 51% similar to a (UDP-GLUCOSE DEHYDROGENASE 6-DEHYDROGENASE OXIDOREDUCTASE NAD NUCLEOTIDE SUGAR UDP-GLCDH UDPGDH UDP-GLC) protein domain (PD005757) which is seen in Q8U172_PYRFU.","","-48% similar to PDB:2O3J Structure of Caenorhabditis Elegans UDP-Glucose Dehydrogenase (E_value = 2.3E_45);-52% similar to PDB:1MFZ Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa (E_value = 1.8E_42);-52% similar to PDB:1MUU 2.0 A crystal structure of GDP-mannose dehydrogenase (E_value = 1.8E_42);-52% similar to PDB:1MV8 1.55 A crystal structure of a ternary complex of GDP-mannose dehydrogenase from Psuedomonas aeruginosa (E_value = 1.8E_42);-46% similar to PDB:1DLI THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION (E_value = 5.7E_28);","Residues 1 to 193 (E_value = 8e-66) place ANA_1218 in the UDPG_MGDP_dh_N family which is described as UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain.Residues 203 to 300 (E_value = 8.6e-46) place ANA_1218 in the UDPG_MGDP_dh family which is described as UDP-glucose/GDP-mannose dehydrogenase family, central domain.Residues 322 to 424 (E_value = 8.2e-28) place ANA_1218 in the UDPG_MGDP_dh_C family which is described as UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain.","","UDP-glucose 6-dehydrogenase (UDPGDH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1219","1298467","1297064","1404","9.44","11.48","50117","ATGAGACTCCTGCTGGGTAACACCCTGGTCTTCGCGCTGGGGGGCCTGGCGGTCAAGGCGGTCTCGTTGGTCCTCATGCCGTTGTACACGACTGCTTTGACGGCTGGTGAGTACGGGACGGCCGAGCTGCTCAACAGCGCGATCGAGATTGTGCTGCCGCTGCTCTCGCTTGGTGTCGTGGAGGCCCTCTACCGGTTCTCCATTGACGATGACGTTCCCAAGGATGAGCTCTTCGCCGGCTCCCTGGTGGTCCTGGGGGGAGGCGTCGTCTGCACCGGGGTGGCGTGCGCCTTGGGCAGCGCCTTGTGGAACATGGAGCACGCGGCAGCGTTCTTCGTCCTGTTCTGCTCGGTGTGCGTCTTCAAGGCCACGACCCAGCTCGCCCGTGGGCTGGGGCACGTGCGCCGCTTCGTGCTCTACGGGCTCATCAATGCGCTCGCCATGGTGGTGTCGACCTACCTGCTCCTGGTCCGTGCGCATACAGGTATCGAGGGCTACCTGTGGTCGTACACCATCGGCTATCTGGTGGGTGGTCTTGTCGCCTTCCTGGGGTCGGCCGAGTACCGGCTCCTGGCCCCATTCAGGTTCGATCGGGCGCTGCTGCGCCGGATGCTCGTCTACAGCCTGCCGCTCGTGCCCAATCTGCTGTCGTGGTGGCTGGTCAGTGTCTCCGGCCGGTACGTGGTCCTGTGGGGCAGCGGCCTGGCGGCTGCCGGGCTCTTCACCGCAGCGAGCAAGATGCCCTCACTCATCAACATCGTGGCCTCCGTCTTCCAGCAGGCCTGGCAGTACTCCACCGCCCGCGAGATCGACTCACCCGACCGCGGCGCCTTCTTCGGCTCCGTCCTGCGGGGCTACTCGCTGGCCACTCTGTCGGCCGCCGGGCTGGTCATCGCCTTGAACCGGCCGATCTCCAGGGTGATGCTCCAGGCCGAGTTCGCCGAGGGGTGGCGCTACGTCCCCCTGCTCATGCTGGCGGCGACCTTCGGGGTCATGACCATCTTCTTCGGCACTTTCTACCAGGCACTCATGAACAGCCGCATGCTCATGGTCTCCACCATGATGGGGGCGATGGTCAACGTGATCCTCGGCGTGGCTCTCGTGCCGTTCATGGGACCGTGGGGCGCCGGCCTGGCCGGAGCGGTGGCCTACGCCCTCGTCCTGGTGGTGCGGGCACGAGACCTCAGGCGCCGCATCGACCTGCCCATGGATCGCTCGCGCCTGACCTACCAGCTCGCGCTGCTCAGCGTCATGGCCGTGTGCACGTCCTTCGACGGCGGCTCATGGCTGAACGGGGCGGTCTGGGTCTGCCTGATCCTCCTGGCGACCAGCGACATGTCAGTGCTGGGTGGCGGCGCTCGAGCCGTGGCCGCAGCGTTCGCCGGCAGGCTTGGGCGGCGCTGA","MRLLLGNTLVFALGGLAVKAVSLVLMPLYTTALTAGEYGTAELLNSAIEIVLPLLSLGVVEALYRFSIDDDVPKDELFAGSLVVLGGGVVCTGVACALGSALWNMEHAAAFFVLFCSVCVFKATTQLARGLGHVRRFVLYGLINALAMVVSTYLLLVRAHTGIEGYLWSYTIGYLVGGLVAFLGSAEYRLLAPFRFDRALLRRMLVYSLPLVPNLLSWWLVSVSGRYVVLWGSGLAAAGLFTAASKMPSLINIVASVFQQAWQYSTAREIDSPDRGAFFGSVLRGYSLATLSAAGLVIALNRPISRVMLQAEFAEGWRYVPLLMLAATFGVMTIFFGTFYQALMNSRMLMVSTMMGAMVNVILGVALVPFMGPWGAGLAGAVAYALVLVVRARDLRRRIDLPMDRSRLTYQLALLSVMAVCTSFDGGSWLNGAVWVCLILLATSDMSVLGGGARAVAAAFAGRLGRR$","Membrane protein involved in the export of O-antigen and teichoic acid","Membrane, Extracellular","hypothetical transmembrane protein possiblyinvolved in polysaccharide biosynthesis, putative","polysaccharide biosynthesis protein","polysaccharide biosynthesis protein","","Becker A., Kleickmann A., Kuster H., Keller M., Arnold W., Puhler A. Analysis of the Rhizobium meliloti genes exoU, exoV, exoW, exoT, and exoI involved in exopolysaccharide biosynthesis and nodule invasion: exoU and exoW probably encode glucosyltransferases. Mol. Plant Microbe Interact. 1993. 6(6):735-744. PMID: 8118055Yao Z., Valvano M.A. Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a. J. Bacteriol. 1994. 176(13):4133-4143. PMID: 7517390Popham D.L., Stragier P. Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis. J. Bacteriol. 1991. 173(24):7942-7949. PMID: 1744050","","","

InterPro
IPR002797
Family

Polysaccharide biosynthesis protein
PF01943	$\"[4-270]T$	Polysacc_synt

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[9-29]?$ $\"[43-63]?$ $\"[78-98]?$ $\"[108-128]?$ $\"[137-157]?$ $\"[167-185]?$ $\"[200-220]?$ $\"[226-244]?$ $\"[285-305]?$ $\"[319-339]?$ $\"[348-368]?$ $\"[372-390]?$ $\"[411-431]?$ $\"[437-457]?$	transmembrane_regions

","BeTs to 7 clades of COG2244COG name: Membrane protein involved in the export of O-antigen and teichoic acidFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2244 is aompk---vd-lb-efghsn-j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 4-77 are 66% similar to a (BIOSYNTHESIS POLYSACCHARIDE TRANSPORTER O-ANTIGEN MEMBRANE EXPORT TRANSMEMBRANE LIPOPOLYSACCHARIDE UNIT FLIPPASE) protein domain (PD583708) which is seen in Q8KQS7_STRTR.Residues 197-321 are similar to a (BIOSYNTHESIS POLYSACCHARIDE MEMBRANE TRANSMEMBRANE VIRULENCE MVIN FACTOR TRANSPORTER O-ANTIGEN EXPORT) protein domain (PD100135) which is seen in Q8KQS7_STRTR.","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 270 (E_value = 1.9e-05) place ANA_1219 in the Polysacc_synt family which is described as Polysaccharide biosynthesis protein.","","transmembrane protein possibly involved in polysaccharide biosynthesis, putative","","1","","","","","","","","","","","Tue Aug 14 12:36:30 2007","","Tue Aug 14 12:36:30 2007","","","Tue Aug 14 12:36:30 2007","","Tue Aug 14 12:36:30 2007","","Tue Aug 14 12:36:30 2007","Tue Aug 14 12:36:30 2007","","","","","yes","","" "ANA_1220","1299383","1298475","909","9.00","8.97","34334","ATGAACTGGCGCGAGCTGTTCTCCTCGAACTATGTCATGCGCCTGGCCACCCACACCCCGATGTACACGCCGACTCAGTATCTCCTGTCCAAGCGTCGGCTCAGCATCTTCAAAGGAGCCGACATCAAGCTCCTGTGCGGCACCAACGCCCTGTACACGAATATGCTGCGGCCCCTGCCGACATGGAACATCAACTACCTCAACTGCGGGATGGCCACAGGCACGGTATGTCTAGGGGTGGGCGCGGGTGCCAACTCCTCATCGGTCAACCTCTACACGCGGGCCCTCTACCGCAAGGTGCTGTCCCATGACCTGGTGCACTCGGTGCGTGACGAGCGCACCAAGCATCTCCTGCAGCGGGTGGGACTGCGGGCCTGGAACACCGGCTGCCCCACCCTGTGGGGACTGACCCCTGAGCACTGCGAGACCATTGCCCGCACCAAGGGCGACGAGGTGGTCTTCACGCTCACCTCCTACCACCCGAACCCGCGCAAGGACCGGGCAATGGTTGACGTGCTGCGCAGGAGCTATTCGCGACTGCACTTCTGGCCCCAGTCCATCGACGACCTGGACTACCTGCAGTCGCTGGGAGCGGCCGACGGCGTCGAGATCGTCACGCCGAGCCTGGCAGGTTTCCGGGAGGTGCTCGACCGGGGCGTCGACTACGTGGGAAACCGCCTGCATGGGGGTATCTTCGCCCTGCAGCGCAAGCGGCGCGCCATCATCGTGGCCATCGACTACCGCGCGCGGGAGATGGCCAAGGACTACTCCCTGCCGCTGGTGGAGCGCGACTCCATCGAGACCGATCTGGCCGACTTGATCGAGTCCTCCTGGCCGACCGCGATCCATGGCCTGGACTTCGACCGCATCGAGAAGTGGAAGGCTCAGTTCGATGTCGGCAAGCCATAA","MNWRELFSSNYVMRLATHTPMYTPTQYLLSKRRLSIFKGADIKLLCGTNALYTNMLRPLPTWNINYLNCGMATGTVCLGVGAGANSSSVNLYTRALYRKVLSHDLVHSVRDERTKHLLQRVGLRAWNTGCPTLWGLTPEHCETIARTKGDEVVFTLTSYHPNPRKDRAMVDVLRRSYSRLHFWPQSIDDLDYLQSLGAADGVEIVTPSLAGFREVLDRGVDYVGNRLHGGIFALQRKRRAIIVAIDYRAREMAKDYSLPLVERDSIETDLADLIESSWPTAIHGLDFDRIEKWKAQFDVGKP$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[64-84]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 5-267 are 50% similar to a (DOMAIN PLASMID) protein domain (PDA0D549) which is seen in Q72WL9_DESVH.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1222","1301147","1299708","1440","9.66","14.48","51436","ATGCCGGCGAGCTATAAGAACCGCATCGCATTCCTGCTGGGCAACACCCTGGTCTTCGCGCTGGGGGGCCTGGCGATCAAGGCCGTCTCCCTGGTCCTCATGCCGTTGTACACGACTGCGCTGACGGCTGGTGAGTACGGGACGGCCGAGCTGCTCAACAGCGCGATCGAGATTGTGCTGCCGCTACTGTCGGCGGGCGTGGTGGAGGCCCTCTACCGGTTCTCCATTGACGACGACGTTCCCAAGGATGAGCTCTTCGCCGGCTCCCTGGTGGTCCTGGGGGGAGGCGTCGTGTGCGCTGGGGTGGCGTGCGCCTTGGGGCGCGTCTTGTGGAACATGGAGCATGCGGGTTCCTTCTTCGTCCTGTTCTGCTCGGTGTGTGTCTTCAAGGCCACGACCCAGCTTGCCCGTGGGTTGGGGCACGTGCGCCGCTTCGTGGCCTATGGGCTTATCAATGCGCTCGCCATGGTGGTGTCCACCTACCTGCTCCTGGTCCGCGCGCACCTGGGCGTGGAGGGGTACCTGTGGTCCTTCACCATCGGCTATCTGGTGGGTGGTCTTGTCGCCTTCCTGGGGTCGGCCGAGTACCGGCTCCTGGCCCCATTCAGGTTTGATCGGGCGCTGCTGCGCCGGATGCTCGTCTACAGCTTGCCGCTCGTGCCCAATCTGCTGTCGTGGTGGCTGGTCAGTGTCTCCGGCCGGTACGTGGTCCTGTGGGGCAGCGGAGTCGTGGCCGCGGGGCTCTTCACGGCGGCGAGCAAGATGCCTGCGCTGGTTAACATCGTGGCCTCCGTGTTCCAGCAGGCCTGGCAGTACTCCACCGCCCGTGAGATTAACTCACCCGACCGAGGCGCCTTCTTCGGCGTCGTGATGAGGGGGTACTCGCTGGCGACCCTCACGGTTGCCGGGCTGGTCATCGCCTTGAACCGGCCGATCTCCAGGGTGATGCTCCAGGCCGAGTTCGCCGAGGGGTGGCGCTACGTCCCCCTGCTCATGCTGGTCGCCTCCTTCGGGGTCATCAGCATCTTCTTCGAGAGCTTCTACCAGGCCTTGAAGAACAGCGGCGTTCTCATGGCCTCGACTGCACTGGGCGCGGGGGTCAACGTGGTGCTCGGTGTGGCTCTTGTGCCGTTCATGGGGCCGTGGGGCGCCGGCCTGGCCGGAGCAGTGGCTTACATGCTCGTCCTGGTGGTGCGGGCACGAGACCTCAGGCGCCGCATCAACCTGCCGATAGACCGCCTTCGTCTCACCTACCAGCTCGCACTGCTCATCAGTATCACCGCATGTATGTCCTTCGATGGCGGCTCATGGCTGAACGGGGCAGTCTGGGCCTGCCTGGGGCTGCTGGCGACCAGCGACATCGCGGTTCTCACCAACAGTGCTCGAGCTGTGGCGGAGTCCCTGAGGCGCAGGAGCGGGGGACTGATGCGCCAGCTCTGA","MPASYKNRIAFLLGNTLVFALGGLAIKAVSLVLMPLYTTALTAGEYGTAELLNSAIEIVLPLLSAGVVEALYRFSIDDDVPKDELFAGSLVVLGGGVVCAGVACALGRVLWNMEHAGSFFVLFCSVCVFKATTQLARGLGHVRRFVAYGLINALAMVVSTYLLLVRAHLGVEGYLWSFTIGYLVGGLVAFLGSAEYRLLAPFRFDRALLRRMLVYSLPLVPNLLSWWLVSVSGRYVVLWGSGVVAAGLFTAASKMPALVNIVASVFQQAWQYSTAREINSPDRGAFFGVVMRGYSLATLTVAGLVIALNRPISRVMLQAEFAEGWRYVPLLMLVASFGVISIFFESFYQALKNSGVLMASTALGAGVNVVLGVALVPFMGPWGAGLAGAVAYMLVLVVRARDLRRRINLPIDRLRLTYQLALLISITACMSFDGGSWLNGAVWACLGLLATSDIAVLTNSARAVAESLRRRSGGLMRQL$","Membrane protein involved in the export of O-antigen and teichoic acid","Membrane, Cytoplasm","Polysaccharide biosynthesis protein domainprotein","hypothetical transmembrane protein possibly involved in polysaccharide biosynthesis","polysaccharide biosynthesis protein","","Becker A., Kleickmann A., Kuster H., Keller M., Arnold W., Puhler A. Analysis of the Rhizobium meliloti genes exoU, exoV, exoW, exoT, and exoI involved in exopolysaccharide biosynthesis and nodule invasion: exoU and exoW probably encode glucosyltransferases. Mol. Plant Microbe Interact. 1993. 6(6):735-744. PMID: 8118055Yao Z., Valvano M.A. Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a. J. Bacteriol. 1994. 176(13):4133-4143. PMID: 7517390Popham D.L., Stragier P. Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis. J. Bacteriol. 1991. 173(24):7942-7949. PMID: 1744050","","","

InterPro
IPR002797
Family

Polysaccharide biosynthesis protein
PF01943	$\"[12-278]T$	Polysacc_synt

noIPR
unintegrated

unintegrated
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[51-71]?$ $\"[86-106]?$ $\"[116-136]?$ $\"[145-165]?$ $\"[175-193]?$ $\"[208-228]?$ $\"[234-252]?$ $\"[285-307]?$ $\"[326-344]?$ $\"[354-374]?$ $\"[380-398]?$ $\"[419-439]?$ $\"[445-465]?$	transmembrane_regions

","BeTs to 3 clades of COG2244COG name: Membrane protein involved in the export of O-antigen and teichoic acidFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2244 is aompk---vd-lb-efghsn-j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 7-89 are 61% similar to a (BIOSYNTHESIS POLYSACCHARIDE TRANSPORTER O-ANTIGEN MEMBRANE EXPORT TRANSMEMBRANE LIPOPOLYSACCHARIDE UNIT FLIPPASE) protein domain (PD583708) which is seen in Q8KQS7_STRTR.Residues 205-329 are similar to a (BIOSYNTHESIS POLYSACCHARIDE MEMBRANE TRANSMEMBRANE VIRULENCE MVIN FACTOR TRANSPORTER O-ANTIGEN EXPORT) protein domain (PD100135) which is seen in Q8KQS7_STRTR.","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 278 (E_value = 9.3e-05) place ANA_1222 in the Polysacc_synt family which is described as Polysaccharide biosynthesis protein.","","biosynthesis protein domain protein","","1","","","","","","","","","","","Tue Aug 14 12:37:29 2007","","Tue Aug 14 12:37:29 2007","","","Tue Aug 14 12:37:29 2007","","Tue Aug 14 12:37:29 2007","","Tue Aug 14 12:37:29 2007","Tue Aug 14 12:37:29 2007","","","","","yes","","" "ANA_1223","1302362","1301256","1107","9.43","8.11","40919","ATGTGGATTCACTTCGCGCTCTTCGCCGCCCTTCTCCTGCCAGCAGCTCTCCTGGGGCTGCGGGGCAATGCCAGTCGGCGGGGCTCCCGGGTCATTCTGGTCGTGGCCTTCGTGGCCTTCGTGGCCTTCTCCTCCATGCGAGCCGTCAGCGTCGGCAACGACACGATTGAGTACCACCGGGTCTTCGAGGAGATCAAGGCGACGACCTCCCTCCAGGAGGCCTTCACCGTCAGCCGCTTCGAGTACGGCTATGTCGTACTCAACTACCTGGTCAGCCGCATCACGGACAGCTTCAACATCCTGCTGCTCATCATCTCGGTGTTCGTCTACGGATCAGCGGTGCTGTTCATCAAGCGGTACGCCGCCAACTACTCCCTGGCGGTCCTCCTCGCCTTCGGCATATCCGCCTTCTACGACTTCACACTCTTTACCCGACAGAGCGTTGCGGTGGCGATCTTCCTGCTGGCCGTCCCCGCGCTCATGGAGCGCAAGCTGTTGCGCTACGCCCTGCTCATCGCGCTCGCCTCCCAGTTCCATCTCAGCGCCCTGCTCCTGCTCGTCATCTACCTCGTCTCCGCCATGAGGCTGAGTACCTTCGGTGACTGGATCAAATGGGGCGCCCTCATCGGGACCAGCATGCTCTCACTGAGCTGGGTGATGAACTCCCTTGCGGCGTCCTCCGCCTACTACGGTCACTACCTCAACAGCGACTACGCCGACGGCGGGGTGCGCTCGGCCACCGTTCTGCTGATCGTAGTGCGCATCTTCCTCATACTTCTGGCCTCCACCTGCGGATGGGAGGCCGCCGTGGAGGAAGACCCCTCCGGGCGTACCCGCAGTCTCCTGGCACTGGCCGTTGCCGATATCGCCATGGTGACGGTGTCCCTGGGCTTCAACCTCGTCGATCGTCTCGAGATGTACCTGACCATGCCCTTCGTCGTCGGTCTGGTGAACCTCACCGTGCGGGGCCGCAGGCCCGAGCGCTCCTACATCGGCGCCCTCCTGGTCATCATCGCCTTCGCAGCCTCCACGATCTTCTTCCTGTACCGGCCCGAGTGGTACCACCTGTTCCCCTACCGAACCGTCTTCGAGAAAGGGATCCCGTGA","MWIHFALFAALLLPAALLGLRGNASRRGSRVILVVAFVAFVAFSSMRAVSVGNDTIEYHRVFEEIKATTSLQEAFTVSRFEYGYVVLNYLVSRITDSFNILLLIISVFVYGSAVLFIKRYAANYSLAVLLAFGISAFYDFTLFTRQSVAVAIFLLAVPALMERKLLRYALLIALASQFHLSALLLLVIYLVSAMRLSTFGDWIKWGALIGTSMLSLSWVMNSLAASSAYYGHYLNSDYADGGVRSATVLLIVVRIFLILLASTCGWEAAVEEDPSGRTRSLLALAVADIAMVTVSLGFNLVDRLEMYLTMPFVVGLVNLTVRGRRPERSYIGALLVIIAFAASTIFFLYRPEWYHLFPYRTVFEKGIP$","Polysaccharide polymerase","Membrane, Cytoplasm","EpsJ, putative","putative polysaccharide polymerase","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[31-51]?$ $\"[97-117]?$ $\"[119-137]?$ $\"[143-161]?$ $\"[171-191]?$ $\"[205-225]?$ $\"[246-266]?$ $\"[280-300]?$ $\"[329-349]?$	transmembrane_regions

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[195-312]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[18-382]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF41	$\"[18-382]T$	GLYCOSYLTRANSFERASE

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[17-175]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[15-235]T$	no description
PTHR22916	$\"[22-237]T$	GLYCOSYLTRANSFERASE

","BeTs to 22 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","***** IPB001173 (Glycosyl transferase, family 2) with a combined E-value of 2e-10. IPB001173A 45-57 IPB001173B 95-104","Residues 8-140 are 51% similar to a (O-ANTIGEN BIOSYNTHESIS) protein domain (PD813194) which is seen in Q8PL49_XANAC.Residues 11-129 are 54% similar to a (SLR1537) protein domain (PD119772) which is seen in P73422_SYNY3.Residues 17-112 are 51% similar to a (TLR2358) protein domain (PD809374) which is seen in Q8DGF9_SYNEL.Residues 22-157 are similar to a (TRANSFERASE GLYCOSYLTRANSFERASE GLYCOSYL FAMILY TRANSFERASE GROUP SYNTHASE BIOSYNTHESIS 2.4.1.- 2.-.-.-) protein domain (PD000196) which is seen in Q8EMC7_OCEIH.","","-54% similar to PDB:1H7L DTDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS (E_value = 6.9E_14);-54% similar to PDB:1H7Q DTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS (E_value = 6.9E_14);-54% similar to PDB:1QG8 NATIVE (MAGNESIUM-CONTAINING) SPSA FROM BACILLUS SUBTILIS (E_value = 6.9E_14);-54% similar to PDB:1QGQ UDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS (E_value = 6.9E_14);-54% similar to PDB:1QGS UDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS (E_value = 6.9E_14);","Residues 17 to 175 (E_value = 7.3e-45) place ANA_1225 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","(teichuronic acid biosynthesis)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1226","1305089","1304403","687","10.23","9.19","25800","ATGACGATGCCGCCATGGGAGGAGCTGCCGGCCTCCCTGCGTACCGAGGAGGTCCGCCCCTACTACGAGGCACTGGCCCGGCGCGGAGTCCAGCTGCGGCTCAAGCGCCTGCTCGACGTCGTCGGAGCGACGATTCTGATGGTGCTGCTCGGGTGGCTGTTCATCATCCTGGCGGCCCTCATCAAGCTGGACTCGCCCGGACCGGTGTTCTTTCGCCAACGGCGGGTCACCCAGTTCGGGCGCGAGTTCCGGATCGTCAAGTTCCGCACCATGACGCACCGGCCGGCAGACCCCGGCGACCAGATCACCCGGGGCAACGACCCCCGGGTCACCAAGGTCGGAGCGGTGCTGCGCCGCTACCGGCTCGATGAGATCAGTCAGCTCATCGACATCCTGCGCGGCACGATGAGCTTCGTAGGGACCAGGCCGGAGGTGCCCGAGTACGTCCAGCAGTACACCCCGCAGATGCGGGCCACCTTGCTGCTGCCCGCCGGAGTCACCTCCACAGCCTCCATCGAGTTCAAGGACGAGGCCGAGATCCTGGCGGCCGCCCCGCCGGGCCAGGACGCCTACCTCACTCAAGTCCTGCCGGCCAAGATGCGCCTCAACCTGCGTGACGTCCAGAACTTCAGCATCGGACGAGATCTGTCGATCGCGCTGAGGACCGTCCTGGCGGTGGCCAGGTGA","MTMPPWEELPASLRTEEVRPYYEALARRGVQLRLKRLLDVVGATILMVLLGWLFIILAALIKLDSPGPVFFRQRRVTQFGREFRIVKFRTMTHRPADPGDQITRGNDPRVTKVGAVLRRYRLDEISQLIDILRGTMSFVGTRPEVPEYVQQYTPQMRATLLLPAGVTSTASIEFKDEAEILAAAPPGQDAYLTQVLPAKMRLNLRDVQNFSIGRDLSIALRTVLAVAR$","Glycosyl transferase","Membrane, Cytoplasm","WlbG","probable sugar transferase","sugar transferase","","","","","

InterPro
IPR003362
Family

Bacterial sugar transferase
PF02397	$\"[35-228]T$	Bac_transf

noIPR
unintegrated

unintegrated
tmhmm	$\"[37-57]?$	transmembrane_regions

","BeTs to 12 clades of COG2148COG name: Sugar transferases involved in lipopolysaccharide synthesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG2148 is -o------vd--bcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB003362 (Bacterial sugar transferase) with a combined E-value of 3.3e-59. IPB003362A 33-63 IPB003362B 65-91 IPB003362C 105-143 IPB003362D 163-174 IPB003362E 199-228","Residues 61-109 are 69% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE BIOSYNTHESIS SUGAR POLYSACCHARIDE SYNTHESIS UNDECAPRENYL-PHOSPHATE CAPSULAR CARRIER EXOPOLYSACCHARIDE) protein domain (PD710582) which is seen in Q8VP01_BORAV.Residues 99-228 are 67% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE SUGAR BIOSYNTHESIS POLYSACCHARIDE SYNTHESIS UNDECAPRENYL-PHOSPHATE CAPSULAR CARRIER EXOPOLYSACCHARIDE) protein domain (PD001742) which is seen in Q9RFX2_STRSU.","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 228 (E_value = 5.7e-12) place ANA_1226 in the Bac_transf family which is described as Bacterial sugar transferase.","","(1996) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1227","1306297","1305086","1212","5.29","-12.84","43224","ATGCGTGTTGATTTCTCGCCTCCAGACATCACCGACGCCGAGTGCCAGGAAGTGGTGGATGCACTGCGCTCTGGCTGGATCACCACCGGACCGCGCACCAAGACCCTGGAGAAGCAGGTGGCGCAGCGCTGTGGAACCACCCGGGCCGCCTGTCTGAACTCCGCGACCGCCTCGCTGGAGCTGACCCTCCGGGTCCTGGGCATCGGTCCCGGAGACGAGGTCATCGTCCCGGCCTACACCTACACGGCCTCTGCCTCCCCGATCGTTCATGTGGGCGCCACCCCCGTGATCGTCGATGCCGGTGACGCTGACGGCGGCTACGGGCTGGACCCCGGCGCCCTGGAGGCCGCCATCACCCCGCGGACCAAGGCCGTCATCCCGGTCGACATCGGTGGTCGCATGTGCGACTACCCGGCGCTGCGCGCGGTCGTAGACAGCCACAGCCACCTGTTCACACCGGCAGGGGCAGTCCAGGAGGCGCTGGGACGTGTCGCCCTCGTCGCCGACGGCGCCCACAGCTTCGGTGCCCGGCGCGACGGCACGCCCTCGGGCAGCGCCGCCGACTTCACCACCTTCAGCTTCCACGCCGTGAAGAACCTGACCACCGCGGAGGGCGGTGCCGTCACGTGGAGGCCGGAGCTGGGCCTGGACGAGGAGCTCTACCGCCAGTACATGCTGCTGTCCTTGCACGGGCAGAGCAAGGACGCCCTGTCCAAGACCCGCCTGGGGGCCTGGGAGTACGACGTCGTCAGCCCCGCCTACAAGTGCAACATGACCGACGTGTGCGCCGCGATCGGCCTGGCGCAGATGACCCGCTACGACTCGATGCTCGAGCGTCGGCGCCAGATCATCACCCGCTACGACCAGGCCCTGGCGCCGGCGGGCGTGACATCGCTGCGGCACTACGAGGACGGGAGCGTCTCATCCGGGCACCTCTACCTGGCGAACCTGCCGGGCCTGGGGGAGGAGGCGCGCAACGAGTTCATCGAGCGCATGGCGCGCGCGGACGTGGCCTGCAACGTCCACTACAAGCCGCTGCCCCTGCTGAGCGCCTACCGCGACCTCGGCTTCTCCATTGAGGACTTCCCGCAGGCCTACGCCCTCTACGCCAGTGAGGTGAGTCTGCCTCTGCACACCTCACTGACCGACGAGCAGGTCGACTACGTCATCAGCTGCGCGCTCGAGACGCTCGCGGCGATGGGCCGCTCATGA","MRVDFSPPDITDAECQEVVDALRSGWITTGPRTKTLEKQVAQRCGTTRAACLNSATASLELTLRVLGIGPGDEVIVPAYTYTASASPIVHVGATPVIVDAGDADGGYGLDPGALEAAITPRTKAVIPVDIGGRMCDYPALRAVVDSHSHLFTPAGAVQEALGRVALVADGAHSFGARRDGTPSGSAADFTTFSFHAVKNLTTAEGGAVTWRPELGLDEELYRQYMLLSLHGQSKDALSKTRLGAWEYDVVSPAYKCNMTDVCAAIGLAQMTRYDSMLERRRQIITRYDQALAPAGVTSLRHYEDGSVSSGHLYLANLPGLGEEARNEFIERMARADVACNVHYKPLPLLSAYRDLGFSIEDFPQAYALYASEVSLPLHTSLTDEQVDYVISCALETLAAMGRS$","Capsular polysaccharide biosynthesis protein","Cytoplasm","UDP-bacillosamine synthetase","capsular polysaccharide biosynthesis protein; putative","DegT/DnrJ/EryC1/StrS aminotransferase","","Ahlert J., Distler J., Mansouri K., Piepersberg W. Identification of stsC, the gene encoding the L-glutamine:scyllo-inosose aminotransferase from streptomycin-producing Streptomycetes. Arch. Microbiol. 1997. 168(2):102-113. PMID: 9238101","","","

InterPro
IPR000653
Family

DegT/DnrJ/EryC1/StrS aminotransferase
PIRSF000390	$\"[2-401]T$	Predicted pyridoxal dependent aminotransferase, DegT/DnrJ/EryC1/StrS types
PF01041	$\"[8-394]T$	DegT_DnrJ_EryC1

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[3-272]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[273-395]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[55-126]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF35	$\"[55-126]T$	ASPARTATE AMINOTRANSFERASE

","BeTs to 15 clades of COG0399COG name: Predicted pyridoxal phosphate-dependent enzyme apparently involved in regulation of cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0399 is --m-k--qv-r-bcefgh-nuj--t-Number of proteins in this genome belonging to this COG is 2","***** IPB000653 (DegT/DnrJ/EryC1/StrS aminotransferase) with a combined E-value of 6.2e-24. IPB000653A 70-119 IPB000653B 150-184 IPB000653C 192-206","Residues 22-90 are similar to a (AMINOTRANSFERASE TRANSFERASE FAMILY BIOSYNTHESIS DEGT/DNRJ/ERYC1/STRS REGULATORY LIPOPOLYSACCHARIDE PLEIOTROPIC PEROSAMINE SYNTHETASE) protein domain (PD484596) which is seen in Q814Z4_BACCR.Residues 45-213 are 39% similar to a (AMINOTRANSFERASE PROBABLE TRANSFERASE) protein domain (PDA0E6B1) which is seen in Q7USA0_RHOBA.Residues 114-169 are 62% similar to a (AMINOTRANSFERASE TRANSFERASE SYNTHETASE 2.6.1.- BIOSYNTHESIS POLYSACCHARIDE CAPSULAR SUGAR AMINO SPR1654) protein domain (PDA143I4) which is seen in Q814Z4_BACCR.Residues 171-209 are 82% similar to a (AMINOTRANSFERASE TRANSFERASE BIOSYNTHESIS FAMILY DEGT/DNRJ/ERYC1/STRS REGULATORY LIPOPOLYSACCHARIDE PLEIOTROPIC PEROSAMINE SYNTHETASE) protein domain (PD406961) which is seen in Q9RFX1_STRSU.Residues 219-292 are similar to a (SUGAR AMINO SYNTHETASE) protein domain (PD971851) which is seen in Q93QV7_BACFR.Residues 220-296 are similar to a (AMINOTRANSFERASE TRANSFERASE BIOSYNTHESIS FAMILY DEGT/DNRJ/ERYC1/STRS REGULATORY LIPOPOLYSACCHARIDE PLEIOTROPIC PEROSAMINE SYNTHETASE) protein domain (PD685696) which is seen in Q8AA53_BACTN.Residues 311-378 are similar to a (AMINOTRANSFERASE TRANSFERASE BIOSYNTHESIS FAMILY DEGT/DNRJ/ERYC1/STRS REGULATORY LIPOPOLYSACCHARIDE PLEIOTROPIC POLYSACCHARIDE PEROSAMINE) protein domain (PD002530) which is seen in Q9RFX1_STRSU.","","-48% similar to PDB:1MDO Crystal structure of ArnB aminotransferase with pyridomine 5' phosphate (E_value = 4.8E_42);-48% similar to PDB:1MDX Crystal structure of ArnB transferase with pyridoxal 5' phosphate (E_value = 4.8E_42);-48% similar to PDB:1MDZ Crystal structure of ArnB aminotransferase with cycloserine and pyridoxal 5' phosphate (E_value = 4.8E_42);-44% similar to PDB:2FN6 Helicobacter pylori PseC, aminotransferase involved in the biosynthesis of pseudoaminic acid (E_value = 1.7E_31);-44% similar to PDB:2FNI PseC aminotransferase involved in pseudoaminic acid biosynthesis (E_value = 1.7E_31);","Residues 8 to 394 (E_value = 4.5e-101) place ANA_1227 in the DegT_DnrJ_EryC1 family which is described as DegT/DnrJ/EryC1/StrS aminotransferase family.Residues 34 to 126 (E_value = 2.5e-05) place ANA_1227 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.","","synthetase (1996)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1228","1308153","1306297","1857","7.04","0.28","67448","ATGGTCATCGACTTCCTGGCCACGTATATGGCGCTGTACTCCGCGGCCTGGGGGACCACGAAGTGGGCGACCGCCACGGGGGCGACCGGCGGCATCCTGGCCGTCGGGGTGCTCGGGATCGTCAACGTGGGCGTCTTCGCCACCTTCAAGATGTACAACAGCCTGTGGCGCTACGCCTCGATGGCGGAGGCGCTGAGGATTCTGTACGCGACCGTCGTCGGCTCGATCTGCGGCGACCTGCTCTTCTCCCTGGCCTTCGATGGTGGGCTGTCAGTGCGTTCCTACGTCATGGCCTGGGCGCTGCTCGTCATCATGACCGCGGGGACTCGCCTCGCCGCCCGGGCGCTGTGGCACAGCCGCGCCCAGCGCAGTGCTCGCACAGGTGAGCCGGGCTCCCGGCCCCGTACCCTCATCGTCGGAGCCGGGCAGACCGGTTCTCTGACCATCAAGCGCATGCACCTGGGGGACGAGGACATGTGCGGAGAACCGGTGGCCCTGGTCGATGACGACATCACCAAGCACGGTCGCCACGTCCACGGCGTCAAGGTCTACGGTGCGTGTGACGACATCCCCCGCATCGCCCAGGAGTGCCGGGCCGAGCAGATCGTCCTGGCCTGCCCCTCGGCGCTGGCCTCCGAGCGCCAGCGCATCCTGTCCATCTGCCTGACAACGGGCCTGAGGATCCTCACCCTCCCGAACGTACGGGACCTGGCTCAGCAGGATGACGGGCGGATCGCACTGCGGGAGGTCGAGATCTCCGAGCTGCTCTCCCGTGACGAGGTCGCCTTCGACTCCACGGGGATGGGGTACGTGCGCGACCAGGTCGTCCTGGTCACCGGCGGTGGTGGCTCCATCGGCTCTGAGCTGGTCCGTCAGCTCATCGAGGCCCGGCCTAGCCAGATCATCATCTTCGACGTCTACGAGAACACGGCCTACGAGCTGCTCCACGAGATGCAGCCCAAGGCGACCGAGCTGGGGGTGACGCTCTCGGTCGTCATCGGCTCGGTGACCAACGAGCGCATCGTCCGCGACTGCTTCCAGCGGTACCGGCCCAAGGTCGTCTTCCACGCGGCGGCCCACAAGCACGTGCCGCTCATGGAGGACAACGCCCGTGAGGCCGTGGAGAACAACGTGCTGGGCACCTGGGTCGTCTGCCGTCTGGCGGAGGAGCTCGGCTGCAGCCACTGCATCCTGGTCTCCACCGACAAGGCGGTCAACCCCACCAACGTCATGGGGGCCACCAAGCGGCTGTGCGAGCTGGAGATCCAGGCCCTGGCCCAGACCAGCCGCTCCACCGTCTTCGCCGCCGTGCGCTTCGGCAACGTGCTCGGCAGCCACGGCTCGGTCATCCCGCTGTTCAGGCGCCAGCTCAGATCAGGTGGGCCACTGACTGTCACCCACCCCGACATCACCCGCTACTTCATGACGATCCCCGAAGCGGCCCAGCTGGTCATCACCGCCGGCTCCATGGCCCAGGCCGGAGAGATCTTCATCTTGGAGATGGGCAAGCCCGTGCGGATCTACGACCTGGCCGTCAACCTCATCAAGCTCTCGGGCCTGCGGGTGGGGCGTGACATCGAGGTCGTCTTCACCGGGCTGCGTCCTGGCGAGAAGCTCTACGAGGAGCTGCAGATGCACGATGAGGATCTGCACCCCACGCAGAACCCCTCGATCCTCGTCTCCACGGCACCGCCTCCCACCAGGCTGGAGGTGGAGGACAAGATCGCTCGGCTCATGGCCTGTCTGCCCCAGGGCGGCGAGCAGATCAAGCGGGAGCTTGCTCGCGCGGTGCCCACCTATCACCCACGTTTTGACAACAGTACGAATCCGTCGCCAACAGTGAGGACAGCTGACTGA","MVIDFLATYMALYSAAWGTTKWATATGATGGILAVGVLGIVNVGVFATFKMYNSLWRYASMAEALRILYATVVGSICGDLLFSLAFDGGLSVRSYVMAWALLVIMTAGTRLAARALWHSRAQRSARTGEPGSRPRTLIVGAGQTGSLTIKRMHLGDEDMCGEPVALVDDDITKHGRHVHGVKVYGACDDIPRIAQECRAEQIVLACPSALASERQRILSICLTTGLRILTLPNVRDLAQQDDGRIALREVEISELLSRDEVAFDSTGMGYVRDQVVLVTGGGGSIGSELVRQLIEARPSQIIIFDVYENTAYELLHEMQPKATELGVTLSVVIGSVTNERIVRDCFQRYRPKVVFHAAAHKHVPLMEDNAREAVENNVLGTWVVCRLAEELGCSHCILVSTDKAVNPTNVMGATKRLCELEIQALAQTSRSTVFAAVRFGNVLGSHGSVIPLFRRQLRSGGPLTVTHPDITRYFMTIPEAAQLVITAGSMAQAGEIFILEMGKPVRIYDLAVNLIKLSGLRVGRDIEVVFTGLRPGEKLYEELQMHDEDLHPTQNPSILVSTAPPPTRLEVEDKIARLMACLPQGGEQIKRELARAVPTYHPRFDNSTNPSPTVRTAD$","Polysaccharide biosynthesis protein CapD","Membrane, Cytoplasm","capD protein","polysaccharide biosynthesis protein","polysaccharide biosynthesis protein CapD","","Lin W.S., Cunneen T., Lee C.Y. Sequence analysis and molecular characterization of genes required for the biosynthesis of type 1 capsular polysaccharide in Staphylococcus aureus. J. Bacteriol. 1994. 176(22):7005-7016. PMID: 7961465Fallarino A., Mavrangelos C., Stroeher U.H., Manning P.A. Identification of additional genes required for O-antigen biosynthesis in Vibrio cholerae O1. J. Bacteriol. 1997. 179(7):2147-2153. PMID: 9079898","","","

InterPro
IPR003869
Domain

Polysaccharide biosynthesis protein CapD
PF02719	$\"[276-563]T$	Polysacc_synt_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[270-520]T$	no description
PTHR10366	$\"[278-550]T$	NAD DEPENDENT EPIMERASE/DEHYDRATASE
PTHR10366:SF23	$\"[278-550]T$	CAPSULAR POLYSACCHARIDE BIOSYNTHESIS PROTEIN
signalp	$\"[1-16]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[31-49]?$ $\"[64-86]?$ $\"[92-112]?$	transmembrane_regions

","BeTs to 12 clades of COG1086COG name: Predicted nucleoside-diphosphate sugar epimerasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1086 is --m-----v---b--fghsnujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB003869 (Polysaccharide biosynthesis protein CapD) with a combined E-value of 2.5e-70. IPB003869A 401-414 IPB003869B 432-468 IPB003869C 469-501 IPB003869D 532-543***** IPB001509 (NAD-dependent epimerase/dehydratase) with a combined E-value of 2.2e-10. IPB001509A 277-288 IPB001509B 352-389***** IPB005913 (dTDP-4-dehydrorhamnose reductase) with a combined E-value of 5.6e-07. IPB005913B 342-381","Residues 137-233 are 56% similar to a (REPRESSOR DNA-BINDING REX TRANSCRIPTIONAL REDOX-SENSING TRANSCRIPTION REGULATION NAD BIOSYNTHESIS POLYSACCHARIDE) protein domain (PD584634) which is seen in Q6AS87_BBBBB.Residues 242-303 are 75% similar to a (POLYSACCHARIDE BIOSYNTHESIS SUGAR CAPSULAR EPIMERASE/DEHYDRATASE NUCLEOTIDE WBPM 46-DEHYDRATASE SYNTHESIS ENZYME) protein domain (PD005861) which is seen in Q891U6_CLOTE.Residues 305-369 are 72% similar to a (SUGAR BIOSYNTHESIS EPIMERASE/DEHYDRATASE POLYSACCHARIDE WBPM NUCLEOTIDE CAPSULAR LIPOPOLYSACCHARIDE 46-DEHYDRATASE DEHYDRATASE) protein domain (PDA1E2B9) which is seen in Q891U6_CLOTE.Residues 350-401 are 73% similar to a (REDUCTASE DTDP-4-DEHYDRORHAMNOSE OXIDOREDUCTASE DTDP-6-DEOXY-L-MANNOSE-DEHYDROGENASE DTDP-4-KETO-L-RHAMNOSE UBIQUINONE NADH-UBIQUINONE SYNTHASE BIOSYNTHESIS RHAMNOSE) protein domain (PD570627) which is seen in Q8XN75_CLOPE.Residues 405-487 are similar to a (POLYSACCHARIDE BIOSYNTHESIS CAPSULAR SUGAR EPIMERASE/DEHYDRATASE SYNTHESIS ENZYME CAPD 46-DEHYDRATASE NUCLEOTIDE) protein domain (PD659729) which is seen in O05349_VIBCH.Residues 412-520 are similar to a (REDUCTASE OXIDOREDUCTASE EPIMERASE/DEHYDRATASE TRANSFERASE SYNTHETASE NAD PEPTIDE ENZYME SYNTHASE PROBABLE) protein domain (PD344516) which is seen in Q9RMC4_ACILW.Residues 525-602 are 58% similar to a (BIOSYNTHESIS POLYSACCHARIDE SUGAR CAPSULAR EPIMERASE/DEHYDRATASE WBPM NUCLEOTIDE LIPOPOLYSACCHARIDE 46-DEHYDRATASE SYNTHESIS) protein domain (PD004112) which is seen in Q82WZ8_NITEU.","","-52% similar to PDB:2GN4 Crystal structure of UDP-GlcNAc inverting 4,6-dehydratase in complex with NADPH and UDP-GlcNAc (E_value = 1.7E_28);-52% similar to PDB:2GN6 Crystal structure of UDP-GlcNAc inverting 4,6-dehydratase in complex with NADP and UDP-GlcNAc (E_value = 1.7E_28);-52% similar to PDB:2GN8 Crystal structure of UDP-GlcNAc inverting 4,6-dehydratase in complex with NADP and UDP (E_value = 1.7E_28);-52% similar to PDB:2GN9 Crystal structure of UDP-GlcNAc inverting 4,6-dehydratase in complex with NADP and UDP-Glc (E_value = 1.7E_28);-52% similar to PDB:2GNA Crystal structure of UDP-GlcNAc inverting 4,6-dehydratase in complex with NADP and UDP-Gal (E_value = 1.7E_28);","Residues 274 to 426 (E_value = 2.5e-05) place ANA_1228 in the adh_short family which is described as short chain dehydrogenase.Residues 275 to 545 (E_value = 5.8e-05) place ANA_1228 in the RmlD_sub_bind family which is described as RmlD substrate binding domain.Residues 276 to 500 (E_value = 7.4e-10) place ANA_1228 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 276 to 563 (E_value = 4.8e-166) place ANA_1228 in the Polysacc_synt_2 family which is described as Polysaccharide biosynthesis protein.Residues 277 to 530 (E_value = 0.00026) place ANA_1228 in the 3Beta_HSD family which is described as 3-beta hydroxysteroid dehydrogenase/isomerase family.Residues 278 to 515 (E_value = 0.0015) place ANA_1228 in the NAD_binding_4 family which is described as Male sterility protein.","","protein (1996)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1229","1310259","1308916","1344","5.56","-9.67","46176","ATGACGCTCGAGGACCTTCTTCATCTAACTCGTCGACGTTTCGGATCTCTCGCGCTGGCGATCGTGATCTGCGTACTTTTGTCAGTAGTGTTCGCTTTCGTGACGCCGAGTTCCTACACGGCGACGGCTCAGGCCTACCTGCACGTGGAGGTGGGTGGAGACCCGGGGCTGAACACGCAGTCCCACTACAACGCGGCACAGCTTGCCGACTTGAAGGCCGAGGCCGCCGTTCCGGTCTTCACCTCGGAGGCGGTCGCCCAGCGCGTGATCGAGTCCCTCAAGCTGGATGTCGCCCCGGAGGACCTGGCCTCGTCAGTATCGGCGACACGGACGCCCGAGACCGTGTCGGTGCAGGTCTCCGTTGAGGCATCCACTGCGCGTCAGGCTCAGGTTCTGGCCGATGAGGTCGTCCGCCAGACGGCCGAAGAAATGACCGAGCTGGAGGGCAGTGACTCTCCGGTGAAGATCTCCCTGCTGTCCTCCGCCGAGCTGGTGAGTGCCACTCGGTCCCCCGCCCTGGTCACCTGCGTGGGCGTGGGGCTGCTGGCCGGACTGGTTCTGGGTTACGTGTGGATTCTCGTCCAGGAGCTGCTCGACAAGAGCCTCAGGGGACCGGAGGACGTGCGCAAGGCCCTGTCGACGCCCGTGCTCGGTGTACTGCCGAAGGATCCGTCGCCTCTGCGGCTGGGGCGTGGTGCGCAGACAGAGGTTGAGGAGCGGCTTCGGGCCGCTCGCACCAACGTGCTCCATGCCCTGTCTCACGGGGCTCGGCAGGTCGTGGTCGTCACCTCTGCTGGTCCGCGGGAGGGGGCCTCGACGACGGCTGCGGGTCTGGCACGGGTCCTGGCTCTGTCCGGTCATCGGGTCGTCCTGGTCGGAGGAGACCTGCGCTCGCCAAGTGCGGTCGGCGCCCCGGGTGCCCCAGGGCTCGCGGAGGTCCTCGTGGGGACGGCTCGTCTCAGTCAGGTCCTGGTCGAAGGCGAGGTGCCGGGCCTGGAGCTCCTGCCTGCCGGCGACATGCCCGGGAACCCCTCTGAGCTGCTCGGCGGTCGCAACATGAGCGACCTCCTGCACCATCTGGCCGCAGACCGCATCGTGATCATCGATGCGCCTCCGGTATGCCGCTTCACCGATGCAGTGGTGCTGGCCGAGTATGCCGGTGGCGTCCTCCTCGTGGCGCGAGCCGGGCGTACCTCCGCCGAAGAACTTCGCGAGGCCGCGCTGGCCGTGGGGCAGGGAGGCGGGCACATACTCGGCGTGGTGCTCACCAACGTGTCCGATCTCGGGCGCGGTAGTCGGAGTGCCCAGACCGCCGTCACTCATGCGGAGAGTGCCACCGTCTGA","MTLEDLLHLTRRRFGSLALAIVICVLLSVVFAFVTPSSYTATAQAYLHVEVGGDPGLNTQSHYNAAQLADLKAEAAVPVFTSEAVAQRVIESLKLDVAPEDLASSVSATRTPETVSVQVSVEASTARQAQVLADEVVRQTAEEMTELEGSDSPVKISLLSSAELVSATRSPALVTCVGVGLLAGLVLGYVWILVQELLDKSLRGPEDVRKALSTPVLGVLPKDPSPLRLGRGAQTEVEERLRAARTNVLHALSHGARQVVVVTSAGPREGASTTAAGLARVLALSGHRVVLVGGDLRSPSAVGAPGAPGLAEVLVGTARLSQVLVEGEVPGLELLPAGDMPGNPSELLGGRNMSDLLHHLAADRIVIIDAPPVCRFTDAVVLAEYAGGVLLVARAGRTSAEELREAALAVGQGGGHILGVVLTNVSDLGRGSRSAQTAVTHAESATV$","Etk-like tyrosine kinase involved in Eps biosynthesis","Membrane, Cytoplasm","possible Etk-like tyrosine kinase involved inEps biosynthesis, putative","lipopolysaccharide biosynthesis","Non-specific protein-tyrosine kinase","","Franco A.V., Liu D., Reeves P.R. The wzz (cld) protein in Escherichia coli: amino acid sequence variation determines O-antigen chain length specificity. J. Bacteriol. 1998. 180(10):2670-2675. PMID: 9573151Morona R., Van Den Bosch L., Daniels C. Evaluation of Wzz/MPA1/MPA2 proteins based on the presence of coiled-coil regions. Microbiology 2000. 146:1-4. PMID: 10658645","","","

InterPro
IPR003856
Domain

Lipopolysaccharide biosynthesis
PF02706	$\"[1-139]T$	Wzz

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[258-425]T$	no description
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[173-193]?$	transmembrane_regions

","BeTs to 8 clades of COG0489COG name: ATPases involved in chromosome partitioningFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0489 is aompkzyqvdr-bcefghsnujx---Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","Residues 303-395 are 55% similar to a (KINASE TYROSINE-PROTEIN EXOPOLYSACCHARIDE POLYSACCHARIDE BIOSYNTHESIS TRANSFERASE CAPSULAR SYNTHESIS TRANSMEMBRANE PHOSPHORYLATION) protein domain (PD793880) which is seen in Q6ADE8_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 139 (E_value = 0.00022) place ANA_1229 in the Wzz family which is described as Chain length determinant protein.","","Etk-like tyrosine kinase involved in Eps biosynthesis, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1230","1311458","1310517","942","8.71","7.47","35758","ATGAGTATCAAGGGTGCTGCAGAAGCAGTTCTTCCCCCGCCGGCTCAGGGATGGTTGAAGCAGGCGATCTACCACCGCAACTGTCACCTGTCGCCGCCCCAGTACCGCGCGGCCCTCAAACACTGGTACTGGCTCTTCAAGGGACGCCCCTGCCACCTGGAGGCGCCGCGCACCATGACTGAGAAGATCCACTGGCTCAAGCTCTATGACTCCACACCCCTCAAAGGGCGTCTGGCGGACAAGTTCCTGGTGCGCGAGTGGGTCGCCGACACGGTGGGGGAGGAGTACCTCGTACCTCTGCTGGGTGTGTGGGACTCGCCTGATGAGATCGACTTCGCCTCCCTGCCGACCAGCTTCGTCCTCAAGGCCACGCACGGCTCGGGGTGGAACATCCTCGTACCGAACAAGAGTGCTCTTGATGAGGAGTGGGCCCGTGGACGCCTCAAGGAGTGGCTCGGCCTGCGCCAGGCGATGAAGGGCGGCTTCGAACTGCACTACGAGTACTGTGAGCCGCGCATCGTGTGCGAGCGCTTCCTGCGTGACGGCACAGGGGGCCTGAGGGACTACAAGTTCATGGTGTTCGACGGCGTCGTCCAGTTCGCCTTCACTGTGGACAGGCGTGCGGGGCTCGCGATGCGGGGGACCTACCTACCGGACTGGACCCGAGCCCCCTTCGAGTACACCTGCGAGGCTGTCCGTGCCCCGGACGTTCCCCCGCCGAGCGGCCTGGAGACCATGCTCCGGCTCGCCAGCAGGCTCGGGAAGGGGTTCGCCTGCGCGCGCGTTGACTTCTACCAGGTGCGGGGACGTGTCTACTTCGGTGAGATCACCTTCACCGACGCCGATGGGTTGTCTGAATTTGCTCCCGCTCGCTACAACCGCATATTCGGTGATCGAATCGTCCTTCCTGAGAAGAAGTCGTTCAAGGGCGTCCTACTGTAA","MSIKGAAEAVLPPPAQGWLKQAIYHRNCHLSPPQYRAALKHWYWLFKGRPCHLEAPRTMTEKIHWLKLYDSTPLKGRLADKFLVREWVADTVGEEYLVPLLGVWDSPDEIDFASLPTSFVLKATHGSGWNILVPNKSALDEEWARGRLKEWLGLRQAMKGGFELHYEYCEPRIVCERFLRDGTGGLRDYKFMVFDGVVQFAFTVDRRAGLAMRGTYLPDWTRAPFEYTCEAVRAPDVPPPSGLETMLRLASRLGKGFACARVDFYQVRGRVYFGEITFTDADGLSEFAPARYNRIFGDRIVLPEKKSFKGVLL$","Hypothetical protein","Cytoplasm","glycosyltransferase","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 23-302 are 53% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE SUGAR EPS11Q ORF2 PROBABLE XAC0085 POSSIBLE 2.4.1.-) protein domain (PD340131) which is seen in Q8A829_BACTN.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1231","1315351","1311872","3480","5.13","-46.11","129375","GTGGTACCGCGGTGCGGCACCAGCCGGGCACCAGCCCCGGTCGGGAGCCGACGTCGTCCTCGTCAGGCCCCGGGCACCCGCCCGAGGCGGCAGGAACGAGTGAGACGAGAGCACACCGCGATGGCTGAGAAGATGGCTGACAGCACCACCGCCGACGGCAACGAGCCGGCCGGCGCCGCCTTCTACCCCCTGCACCGCCCGGGGGAGCAGATCGACCCCTCGCCCTCCTTCCCCGCCATTGAGGAGGACGTCCTGGCCTACTGGAAGGCCGACGGCACCTTCCAGGCCTCCATCGACAACCGCGCCGAGCCCTGCGACGAGTTCGTCTTCTACGACGGACCGCCCTTCGCCAACGGCCTGCCCCACTACGGCCACCTGCTGACCGGCTACGTCAAGGACGCCGTCGGGCGCTACCAGACCCAGCGCGGCAAGCGCGTCGAGCGCCGCTTCGGCTGGGACACCCACGGCCTGCCCGCCGAGCTCGAGGCCCAGCGTCTGCTCGGCATCGACGACGTCACCGAGATCACCCGCCCCGGCGGCATCGGCATCGAGAAGTTCAACGAGGAGTGCCGCAGCTCCGTCCTGCGCTACACCAAGGAGTGGGAGGACTACGTCACCCGCCAGGCCCGCTGGGTCGACTTCGACAACGACTACAAGACCCTCGACCCTGACTACATGGAGTCGGTGCTGTGGGCCTTCAAGCAGCTGTGGGACAAGGGTCTGGCCTACCAGGGCTACCGCGTCCTGCCCTACTGCTGGCACGACCGCACCCCCTTGAGCAACCACGAGCTCAAGATGGACGACGACGTCTACCAGGACCGCCAGGACAATACGGTCACGGTGGGCCTGCGCCTGGAGGAGCCCCTGCGCCAGGGCGCCGAGCGCCCCGAGCTGGTCCTCATTTGGACCACCACCCCCTGGACGCTGCCCTCCAACCTGGCCATCGCCGTGGGCCCTGACGTCGAGTACGTGACCGTCCACGTCGACGAGGACCTCGACTCGCCGGTGGCCGGCCAGGACGTCGTCATCGCGAAGGACCTGCTGGGCTCCTACGCCCGCGAGCTCGGTGAGGACCCGCAGGTGCTGGCCACCTGCACCGGGGCCGACCTGGTGGGGCGGCGCTACCACCCGATCTTCGACTACTTCGACGACGCCGCCCACCGTGCCGAGGGCGCCGCCCCGGGGCCGAATGCCTGGACGATCATCGCCGCCGACTTCGTGACCACCTCCGACGGAACCGGCCTGGTGCACATGGCCTCGGCCTTCGGTGAGGACGACATGATTGCCTGCTCCGAGGCCGGCATCGAGACAGTCGTGCCCGTCGACGACGGCGGCTGCCTGACCGAGGAGGTGAGTGACTACGCCGGGCTGCAGGTCTTCGAGGCCAACAAGCCCATCGTTGCCGACCTGCGCGACGGCACCGGCCCCCTGGCCCGCCGCGACGAGAGCCGGCGCGCCGTCCTGGTGCGCCAGGCCTCCTACGTGCACTCCTACCCGCACTGCTGGCGCTGCCGCAAGCCGCTCATCTACAAGGCCGTCTCCTCCTGGTTCGTGCGCGTCTCGGCGATCCGCGACCGCATGGTCGAGCTCAACCAGGACATCGACTGGTACCCCGGCCACATCAAGGACGGCATCTTCGGCAAGTGGCTGGCGAACGCGCGCGACTGGTCGATCTCCCGCAACCGTTTCTGGGGCGCGCCCATCCCGGTGTGGGTCAGCGACAACCCCGACTACCCGCGCACCGACGTCTACGGCTCCTACGCCGAGCTCGAGCGCGACTTCGGTGTCAAGGTCACCGACCTGCACCGCCCCTTCATCGACACCCTCGTGCGGCCCAACCCCGACGACCCCACGGGTAAGTCCATGATGCGCCGCATCCCCGACGTCCTGGACTGTTGGTTCGAGTCCGGCTCCATGCCCTTCGCCCAGGTGCACTACCCCTTCGAGAACGTCGAGTGGTTCGAGTCGCACTACCCGGGCGACTTCATCGTGGAGTACATCGGCCAGACCCGCGGCTGGTTCTACACCCTCCACGTCCTGGCCACCGCCCTGTTCGACCGGCCCGCCTTCACCTCTTGCGTCTCCCACGGCATCCTCCTGGGTAACGACGGGGCGAAGATGAGCAAGTCGCTGCGCAACTACCCGGACGTCTCCATGGTCTTCGACCGCGACGGGGCCGACGCCATGCGCTGGTTCCTGCTCTCGGCGCCGGTCATGCGCGGAGGCAACCTCGTGGTCACCGACAAGGCCATCCGCGACACCGTGCGCCAGGTGGTGCTGCCGCTGTGGAACACCTGGTACTTCTTCGCCCTCTACGCGGGCCAGGTGGGCCAGTCCGGCTACGTCACGAGCGGCGTCGACCTGGATGACGCGAGCCTGTTCGCCAAGCACGGCGGCCTGCACGTCATGGACCGCTACGTCCTGGCCCGCACCAAGGACCTGACCGAGACGGTGGCCGCCCAGATGGACGGCTACGACATCACCGGGGCCTGCGCCACGATCCGCGACTTCCTCGACGTGCTCACCAACTGGTACCTGCGCACCTCGCGCCAGCGTTTCACCGACGGCGAGACGACCGCCTTCGACACCCTGGCCACCGTGCTGCGGGTGCTCACCGAGGTCATGGCGCCGCTGGCGCCGCTGGTGAGCGAGGAGATCTGGCGGGGCCTGACCGGTGGGCGCTCCGTGCACCTGACCGACTGGCCCGCGCTGCCCGGGCATGTCGCCAATGCCGAGCTCGTGGCGGCCATGGATGAGGCCCGAGCCGCGGTCTCGGCCGCCCTGAGCCTGCGCAAGGCCGAGAAGCTGCGCGTGCGCCAGCCGCTTCGCAGCCTGACCGTCGCCACCGCTGACCCGGCCGGGCTGGCCCCCTTCCGCGAGCTCGTGGCCGAGGAGGTCAACGTCAAGGAGGTACGGGTCCTGGATGCCGAGTCCGCCGGCTACGAGGCCCGAACGGACCTGGCCCTCAACCCGCGCGCCTTCAGCCCCGAGGTCCGCAAGCTCACCTCCAAGCTCTTCGCCGCCGTCAAGGCGGGCCAGTGGGAGCTCACCGAGGACGGGGATGTGCGCTTCAACGACGTCCTGCTCGATGGCGCCCCCGTGGTCCTGGAGGCGGAGGACTCCGCCTTCACCCTGACCACCCGCATCGAGGTCGACGATGACTCCCTGGCCGCCACCATGCTGCCCTCGGGGGCCTTCGTGGTCCTGGAGACGGCCCTCGACGACGCCCTGGAGGCCGAGGGCTGGGCCCGCGACCTGGTGCGTCTGGTCCAGGACGAGCGCAAGGCCGTCGGCCTGCACGTGGGGGACCGGATTCGCCTGGAGCTGCGGGTCCCGCAGGACAAGGACGCCTGGACCGGTGCCCACCTGGACCTCATCAAGCGGGAGGTCGGCTGCGTGGACGCCTCCGTTGTGGCCGACCCGGCCGTGAAGGAGCCCACCGCCACGGTTGAGAAGGTCACCGAGGCGAGGGAGAGCTGA","VVPRCGTSRAPAPVGSRRRPRQAPGTRPRRQERVRREHTAMAEKMADSTTADGNEPAGAAFYPLHRPGEQIDPSPSFPAIEEDVLAYWKADGTFQASIDNRAEPCDEFVFYDGPPFANGLPHYGHLLTGYVKDAVGRYQTQRGKRVERRFGWDTHGLPAELEAQRLLGIDDVTEITRPGGIGIEKFNEECRSSVLRYTKEWEDYVTRQARWVDFDNDYKTLDPDYMESVLWAFKQLWDKGLAYQGYRVLPYCWHDRTPLSNHELKMDDDVYQDRQDNTVTVGLRLEEPLRQGAERPELVLIWTTTPWTLPSNLAIAVGPDVEYVTVHVDEDLDSPVAGQDVVIAKDLLGSYARELGEDPQVLATCTGADLVGRRYHPIFDYFDDAAHRAEGAAPGPNAWTIIAADFVTTSDGTGLVHMASAFGEDDMIACSEAGIETVVPVDDGGCLTEEVSDYAGLQVFEANKPIVADLRDGTGPLARRDESRRAVLVRQASYVHSYPHCWRCRKPLIYKAVSSWFVRVSAIRDRMVELNQDIDWYPGHIKDGIFGKWLANARDWSISRNRFWGAPIPVWVSDNPDYPRTDVYGSYAELERDFGVKVTDLHRPFIDTLVRPNPDDPTGKSMMRRIPDVLDCWFESGSMPFAQVHYPFENVEWFESHYPGDFIVEYIGQTRGWFYTLHVLATALFDRPAFTSCVSHGILLGNDGAKMSKSLRNYPDVSMVFDRDGADAMRWFLLSAPVMRGGNLVVTDKAIRDTVRQVVLPLWNTWYFFALYAGQVGQSGYVTSGVDLDDASLFAKHGGLHVMDRYVLARTKDLTETVAAQMDGYDITGACATIRDFLDVLTNWYLRTSRQRFTDGETTAFDTLATVLRVLTEVMAPLAPLVSEEIWRGLTGGRSVHLTDWPALPGHVANAELVAAMDEARAAVSAALSLRKAEKLRVRQPLRSLTVATADPAGLAPFRELVAEEVNVKEVRVLDAESAGYEARTDLALNPRAFSPEVRKLTSKLFAAVKAGQWELTEDGDVRFNDVLLDGAPVVLEAEDSAFTLTTRIEVDDDSLAATMLPSGAFVVLETALDDALEAEGWARDLVRLVQDERKAVGLHVGDRIRLELRVPQDKDAWTGAHLDLIKREVGCVDASVVADPAVKEPTATVEKVTEARES$","Isoleucyl-tRNA synthetase","Cytoplasm","isoleucyl-tRNA synthetase ileS","isoleucyl-tRNA synthetase ","isoleucyl-tRNA synthetase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[115-126]?$	AA_TRNA_LIGASE_I

InterPro
IPR002300
Domain

Aminoacyl-tRNA synthetase, class Ia
PF00133	$\"[83-745]T$	tRNA-synt_1

InterPro
IPR002301
Domain

Isoleucyl-tRNA synthetase, class Ia
PR00984	$\"[108-119]T$ $\"[300-323]T$ $\"[625-638]T$ $\"[665-674]T$	TRNASYNTHILE
TIGR00392	$\"[70-959]T$	ileS: isoleucyl-tRNA synthetase

InterPro
IPR013155
Domain

tRNA synthetase, valyl/leucyl, anticodon-binding
PF08264	$\"[804-947]T$	Anticodon_1

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[72-735]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.730.10	$\"[799-890]T$	no description
PTHR11946	$\"[76-383]T$ $\"[399-975]T$	ISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES
PTHR11946:SF9	$\"[76-383]T$ $\"[399-975]T$	ISOLEUCYL TRNA SYNTHETASE

","BeTs to 26 clades of COG0060COG name: Isoleucyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0060 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB013155 (tRNA synthetase, valyl/leucyl, anticodon-binding) with a combined E-value of 2.2e-90. IPB013155A 81-94 IPB013155B 114-156 IPB013155C 204-222 IPB013155D 240-264 IPB013155E 301-320 IPB013155F 400-436 IPB013155G 555-569 IPB013155H 704-730***** IPB002301 (Isoleucyl-tRNA synthetase signature) with a combined E-value of 6.2e-55. IPB002301A 108-119 IPB002301B 300-323 IPB002301C 496-511 IPB002301D 625-638 IPB002301E 665-674***** IPB002300 (Aminoacyl-tRNA synthetase, class Ia) with a combined E-value of 4.4e-15. IPB002300A 121-151 IPB002300B 556-569","Residues 18-101 are 48% similar to a (SYNTHETASE ISOLEUCYL-TRNA AMINOACYL-TRNA) protein domain (PD983480) which is seen in Q6AFZ0_BBBBB.Residues 88-186 are 74% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS LEUCYL-TRNA METHIONYL-TRNA ISOLEUCYL-TRNA VALYL-TRNA LEURS) protein domain (PD000389) which is seen in Q8G3I2_BIFLO.Residues 211-235 are 92% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE ISOLEUCYL-TRNA ISOLEUCINE--TRNA ILERS ATP-BINDING BIOSYNTHESIS METAL-BINDING ZINC) protein domain (PDA0R3Z1) which is seen in SYI_MYCLE.Residues 264-356 are 58% similar to a (SYNTHETASE ISOLEUCYL-TRNA AMINOACYL-TRNA) protein domain (PDA197Q8) which is seen in Q6AFZ0_BBBBB.Residues 268-384 are 43% similar to a (SYNTHETASE ISOLEUCYL-TRNA AMINOACYL-TRNA LIGASE) protein domain (PDA0M2D8) which is seen in Q73HW7_WOLPM.Residues 271-469 are 45% similar to a (SYNTHETASE ISOLEUCYL-TRNA AMINOACYL-TRNA) protein domain (PDA0M2B2) which is seen in Q7NF75_GLOVI.Residues 296-382 are 53% similar to a (GLP_609_31077_27580) protein domain (PDA0M2D5) which is seen in Q7QZU2_EEEEE.Residues 300-471 are 66% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA LEUCYL-TRNA VALYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD000939) which is seen in Q6NGD7_CORDI.Residues 300-381 are 52% similar to a (SYNTHETASE LIGASE ZINC ISOLEUCYL-TRNA ISOLEUCINE--TRNA METAL-BINDING BIOSYNTHESIS ILERS AMINOACYL-TRNA ATP-BINDING) protein domain (PDA0M2D0) which is seen in SYI_TREPA.Residues 338-466 are 53% similar to a (SYNTHETASE ISOLEUCYL-TRNA PROBABLE AMINOACYL-TRNA LIGASE) protein domain (PDA0M2D7) which is seen in Q7UNZ2_RHOBA.Residues 488-544 are 82% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA LEUCYL-TRNA ATP-BINDING BIOSYNTHESIS LEUCINE--TRNA LEURS ISOLEUCYL-TRNA VALYL-TRNA) protein domain (PD386284) which is seen in SYI_MYCTU.Residues 546-590 are 77% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA VALYL-TRNA LEUCYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD000647) which is seen in Q73HW7_WOLPM.Residues 576-618 are 65% similar to a (SYNTHETASE ISOLEUCYL-TRNA AMINOACYL-TRNA) protein domain (PD858199) which is seen in Q8G3I2_BIFLO.Residues 619-677 are 94% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE VALYL-TRNA ISOLEUCYL-TRNA ATP-BINDING BIOSYNTHESIS VALINE--TRNA VALRS ISOLEUCINE--TRNA) protein domain (PD002669) which is seen in SYI_MYCTU.Residues 677-727 are 78% similar to a (SYNTHETASE AMINOACYL-TRNA ISOLEUCYL-TRNA M I V TRNA I LIGASE CLASS) protein domain (PD924853) which is seen in Q83I16_TROW8.Residues 688-727 are 92% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA METAL-BINDING ZINC CYSTEINYL-TRNA VALYL-TRNA) protein domain (PD000476) which is seen in Q6AFZ0_BBBBB.Residues 728-777 are 90% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE ISOLEUCYL-TRNA ISOLEUCINE--TRNA ILERS ATP-BINDING BIOSYNTHESIS SYNTHETASE METAL-BINDING) protein domain (PD118352) which is seen in Q6AFZ0_BBBBB.Residues 803-1115 are 44% similar to a (SYNTHETASE ISOLEUCYL TRNA AMINOACYL-TRNA) protein domain (PD651492) which is seen in Q8SQV6_EEEEE.Residues 804-864 are 69% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE ISOLEUCYL-TRNA VALYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCINE--TRNA VALINE--TRNA VALRS) protein domain (PD259544) which is seen in Q83I16_TROW8.Residues 867-918 are 71% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS VALYL-TRNA LEUCYL-TRNA ISOLEUCYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD023651) which is seen in Q6AFZ0_BBBBB.Residues 936-1088 are 47% similar to a (SYNTHETASE AMINOACYL-TRNA ISOLEUCYL-TRNA M I V TRNA I LIGASE CLASS) protein domain (PD712683) which is seen in Q83I16_TROW8.Residues 947-1080 are 49% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ISOLEUCYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCINE--TRNA ILERS METAL-BINDING ZINC) protein domain (PD347709) which is seen in Q7VEZ0_MYCBO.","","-56% similar to PDB:1ILE ISOLEUCYL-TRNA SYNTHETASE (E_value = 1.0E_173);-56% similar to PDB:1JZQ Isoleucyl-tRNA synthetase Complexed with Isoleucyl-adenylate analogue (E_value = 1.0E_173);-56% similar to PDB:1JZS Isoleucyl-tRNA synthetase Complexed with mupirocin (E_value = 1.0E_173);-45% similar to PDB:1FFY INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN (E_value = 2.1E_78);-45% similar to PDB:1QU2 INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN (E_value = 2.1E_78);","Residues 83 to 745 (E_value = 2.1e-209) place ANA_1231 in the tRNA-synt_1 family which is described as tRNA synthetases class I (I, L, M and V).Residues 115 to 747 (E_value = 5.9e-06) place ANA_1231 in the tRNA-synt_1g family which is described as tRNA synthetases class I (M).Residues 804 to 947 (E_value = 4.7e-36) place ANA_1231 in the Anticodon_1 family which is described as Anticodon-binding domain.","","synthetase ileS (ileS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1233","1316729","1315782","948","5.39","-11.42","34479","ATGACTGACGCACACCCCCGCATGGCGCTGGGCACCATGCACTTCGGAACCCGCCTGCCTGCCACCCAGTCCCGTGAAATCCTCGACGCCTACCTGGATCTGGGCGGCCAGTGGATCGACACCGCGAACTGCTACGCCTTCTGGGGAGCCGAGTCCGGCCTCGGGGGCCAGAGCGAGACCGTCATCGGCCAGTGGCTCGCTGATCGCGGCGTGCGCGACCAAGTGAAAATCAGCACCAAGGTCGGTGCGGAGCCGACCCGCCCCCACGGCTTTCCGGGCGCCGTGGAAGGTCTCGGCAGGGAGACCGTCAACCAGGCCATCCGGGACAGTCTGGAGCGCCTGCAGACGGAGCGCGTCGACATGTACTGGGCCCATATGGAGGACCGGGAGCAGTCGGTCGCGGATGTTGCTGAGAGCTTCGGCGCCCTGGTTGACCAAGGGCTGACCGCACGGATCGGGCTGTCCAACCACCCGGCCTGGTACGCCGCCGCAGCCAACGTGCACGCCCAGCAGCGGGGCTCAGCCGGCTTCAGCGCCCTGCAGCTGCGGGAGTCGTACCTCCACCCGAGGCCGGATACCCCGGTAGAGGGCGAGGACCACCCCCACGGGATGATGACCAGCGAGAGCAAGGACTTCGCCGAGCGCTGCGGGCTGGACCTGTGGGCCTACACGCCGCTGCTGACCGGCGCCTACGAGCACCCAGAACGTCCGCTGCCTGAGGCATACAGGCACCCGGGGACTGACAAGCGGCTGACAGCGCTGCGCACGTGGTCGGAGCGTCTTGCCATGAAGCCGAGCCAGGTCGTCCTGGCCCTTCTCAACGCCCAGCAGCCGACGATCACCCCGATCGTGGGCGTCAGCAGTGTCGCCCAGCTCACTGACGCCATCGAGGCCACGCGCTTCAGCCTCCCTCAGGAGGCCGTCGAGGAGCTCAACGCAGCCGGCTAG","MTDAHPRMALGTMHFGTRLPATQSREILDAYLDLGGQWIDTANCYAFWGAESGLGGQSETVIGQWLADRGVRDQVKISTKVGAEPTRPHGFPGAVEGLGRETVNQAIRDSLERLQTERVDMYWAHMEDREQSVADVAESFGALVDQGLTARIGLSNHPAWYAAAANVHAQQRGSAGFSALQLRESYLHPRPDTPVEGEDHPHGMMTSESKDFAERCGLDLWAYTPLLTGAYEHPERPLPEAYRHPGTDKRLTALRTWSERLAMKPSQVVLALLNAQQPTITPIVGVSSVAQLTDAIEATRFSLPQEAVEELNAAG$","Aldo/keto reductase","Cytoplasm","putative oxidoreductase.","aldo/keto reductase","aldo/keto reductase","","Bohren K.M., Bullock B., Wermuth B., Gabbay K.H. The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 1989. 264(16):9547-9551. PMID: 2498333Schade S.Z., Early S.L., Williams T.R., Kezdy F.J., Heinrikson R.L., Grimshaw C.E., Doughty C.C. Sequence analysis of bovine lens aldose reductase. J. Biol. Chem. 1990. 265(7):3628-3635. PMID: 2105951Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A. An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 1992. 257(5066):81-84. PMID: 1621098Borhani D.W., Harter T.M., Petrash J.M. The crystal structure of the aldose reductase.NADPH binary complex. J. Biol. Chem. 1992. 267(34):24841-24847. PMID: 1447221Gulbis J.M., Zhou M., Mann S., MacKinnon R. Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. Science 2000. 289(5476):123-127. PMID: 10884227","","","

InterPro
IPR001395
Family

Aldo/keto reductase
PD000288	$\"[6-160]T$	Q9KZ45_STRCO_Q9KZ45;
PR00069	$\"[109-127]T$ $\"[140-157]T$	ALDKETRDTASE
G3DSA:3.20.20.100	$\"[6-314]T$	no description
PTHR11732	$\"[7-189]T$ $\"[206-287]T$	ALDO/KETO REDUCTASE
PF00248	$\"[1-315]T$	Aldo_ket_red

noIPR
unintegrated

unintegrated
PTHR11732:SF15	$\"[7-189]T$ $\"[206-287]T$	ALDO/KETO REDUCTASE

noIPR
unintegrated

unintegrated
tmhmm	$\"[148-168]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB000817 (Prion protein) with a combined E-value of 2.3e-10. IPB000817A 196-237 IPB000817A 187-228 IPB000817A 190-231 IPB000817A 172-213 IPB000817A 179-220 IPB000817A 184-225 IPB000817A 205-246 IPB000817A 181-222 IPB000817A 199-240 IPB000817A 195-236 IPB000817A 206-247 IPB000817A 188-229 IPB000817A 178-219 IPB000817A 200-241 IPB000817A 189-230 IPB000817A 203-244 IPB000817A 202-243 IPB000817A 193-234 IPB000817A 173-214 IPB000817A 201-242 IPB000817A 163-204 IPB000817A 222-263 IPB000817A 198-239 IPB000817A 214-255 IPB000817A 208-249 IPB000817A 177-218 IPB000817A 183-224 IPB000817A 186-227 IPB000817A 191-232 IPB000817A 204-245 IPB000817A 192-233 IPB000817A 194-235 IPB000817A 185-226 IPB000817A 211-252 IPB000817A 210-251 IPB000817A 236-277 IPB000817A 180-221 IPB000817A 209-250 IPB000817A 213-254 IPB000817A 221-262 IPB000817A 197-238 IPB000817A 182-223 IPB000817A 217-258 IPB000817A 176-217 IPB000817A 219-260 IPB000817A 166-207 IPB000817A 218-259 IPB000817A 240-281 IPB000817A 245-286 IPB000817A 170-211 IPB000817A 161-202 IPB000817A 239-280 IPB000817A 157-198 IPB000817A 215-256 IPB000817A 212-253 IPB000817A 229-270 IPB000817A 164-205 IPB000817A 165-206 IPB000817A 168-209 IPB000817A 175-216 IPB000817A 234-275 IPB000817A 220-261 IPB000817A 228-269 IPB000817A 162-203***** IPB001442 (Type 4 procollagen, C-terminal repeat) with a combined E-value of 6.4e-08. IPB001442B 197-243 IPB001442B 194-240 IPB001442B 191-237 IPB001442B 188-234 IPB001442B 206-252 IPB001442B 200-246 IPB001442B 203-249 IPB001442B 185-231 IPB001442B 209-255 IPB001442B 190-236 IPB001442B 193-239 IPB001442B 212-258 IPB001442B 184-230 IPB001442B 199-245 IPB001442B 179-225 IPB001442B 182-228 IPB001442B 205-251 IPB001442B 187-233 IPB001442B 181-227 IPB001442A 219-246 IPB001442A 210-237 IPB001442A 203-230 IPB001442A 225-252 IPB001442A 200-227 IPB001442A 198-225 IPB001442A 222-249 IPB001442A 204-231 IPB001442A 195-222 IPB001442A 213-240 IPB001442A 186-213 IPB001442A 228-255***** IPB001285 (Synaptophysin/synaptoporin) with a combined E-value of 5e-07. IPB001285F 187-231 IPB001285F 196-240 IPB001285F 191-235 IPB001285F 202-246 IPB001285F 194-238 IPB001285F 205-249 IPB001285F 184-228 IPB001285F 186-230 IPB001285F 178-222 IPB001285F 248-292 IPB001285F 180-224 IPB001285F 181-225 IPB001285F 193-237 IPB001285F 176-220 IPB001285F 206-250 IPB001285F 208-252 IPB001285F 197-241 IPB001285F 171-215***** IPB010465 (DRF autoregulatory) with a combined E-value of 7.6e-07. IPB010465D 187-222 IPB010465D 185-220 IPB010465D 193-228 IPB010465D 196-231 IPB010465D 190-225 IPB010465D 195-230 IPB010465D 191-226 IPB010465D 194-229 IPB010465D 192-227 IPB010465D 189-224 IPB010465D 197-232 IPB010465D 203-238 IPB010465D 202-237***** IPB000885 (Fibrillar collagen, C-terminal) with a combined E-value of 9.8e-07. IPB000885A 192-243 IPB000885A 189-240 IPB000885A 186-237 IPB000885A 201-252 IPB000885A 195-246 IPB000885A 204-255 IPB000885A 198-249 IPB000885A 183-234 IPB000885A 207-258 IPB000885A 206-257 IPB000885A 179-230***** IPB002486 (Nematode cuticle collagen, N-terminal) with a combined E-value of 1.2e-06. IPB002486 201-237 IPB002486 207-243 IPB002486 213-249 IPB002486 219-255 IPB002486 210-246 IPB002486 189-225 IPB002486 198-234 IPB002486 222-258 IPB002486 216-252 IPB002486 195-231 IPB002486 204-240 IPB002486 191-227 IPB002486 192-228 IPB002486 203-239 IPB002486 206-242 IPB002486 188-224 IPB002486 209-245 IPB002486 200-236 IPB002486 225-261***** IPB008161 (Collagen helix repeat) with a combined E-value of 8.6e-06. IPB008161 195-237 IPB008161 192-234 IPB008161 198-240 IPB008161 201-243 IPB008161 189-231 IPB008161 203-245 IPB008161 204-246 IPB008161 210-252","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1235","1318685","1317894","792","5.04","-9.88","27422","ATGAGCGAGAACCCGAAGAACGTCACCGTCGACTCCGCTGTCTCCGCGCCGGCCCGCCGCGCCCTGATCACCGGCGCCTCCACCGGTATCGGTGCCGCCACCGTTCGGCTCCTGCGCTCCCACGGGTGGGAGGTCGTCGCCACCGCGCGGCGGGTGGAGCGCCTTGAGGCGCTGGCCGCCGAGACCGGCTGCACGTGGGTGGCCGCCGACCTCCAGGAGCCCGGCGACGTTGAGCGCCTGGCCAGTGAGGTGCTGGCCGGCGGAGCTGTCGACGCCGTCGTCAACAATGCCGGTGGCGCGCTGGGGGTCGACCCGGTCGCCGAGGGCAGCGTCCAGGAGTGGGCGACCATGTACGAGCGCAACGCGCTCGCGGCCCTGCGCGTGAGCCAGGCCTTCCTGCCGGGGCTTCGGGAGCGGGGCGGGGACCTGGTCTTCCTCACCTCCACGGCGGCCCACGACACCTACCCCGGTGGGGGCGGATACGTGGCGGCCAAGCACGCCGAGCGGATCATCGCCAACACGCTGCGCCTGGAGCTGGTGGGCGAGCCGGTGCGCGTCATTGAGATCGCCCCCGGCATGGTGGCCACCGAGGAGTTCTCCCTCAACCGTCTCCATGGAGACGCCGAGGCCGCGGCGAAGGTATACGCCGGCGTGGCCGAACCGCTGAGCGCCGACGACGTCGCCGCCTGCATCGCCTGGACGCTGGAGCTGCCCGCTCACGTCAACATCGACTCCATGGTGGTGCGGCCGCGGGCCCAGGCCTCCAACACGCTGGTGGCCCGGGAGCAGTAG","MSENPKNVTVDSAVSAPARRALITGASTGIGAATVRLLRSHGWEVVATARRVERLEALAAETGCTWVAADLQEPGDVERLASEVLAGGAVDAVVNNAGGALGVDPVAEGSVQEWATMYERNALAALRVSQAFLPGLRERGGDLVFLTSTAAHDTYPGGGGYVAAKHAERIIANTLRLELVGEPVRVIEIAPGMVATEEFSLNRLHGDAEAAAKVYAGVAEPLSADDVAACIAWTLELPAHVNIDSMVVRPRAQASNTLVAREQ$","Short-chain dehydrogenase/reductase SDR","Cytoplasm","Short-chain dehydrogenases of various substratespecificities","short-chain dehydrogenase/reductase SDR","short-chain dehydrogenase/reductase SDR","","Peters C., Schmidt B., Rommerskirch W., Rupp K., Zuhlsdorf M., Vingron M., Meyer H.E., Pohlmann R., von Figura K. Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B. J. Biol. Chem. 1990. 265(6):3374-3381. PMID: 2303452Wilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J., Clements P.R., Hopwood J.J. Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA. Proc. Natl. Acad. Sci. U.S.A. 1990. 87(21):8531-8535. PMID: 2122463de Hostos E.L., Schilling J., Grossman A.R. Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii. Mol. Gen. Genet. 1989. 218(2):229-239. PMID: 2476654","","","

InterPro
IPR000917
Domain

Sulfatase
PS00523	$\"[13-25]?$	SULFATASE_1

InterPro
IPR002198
Family

Short-chain dehydrogenase/reductase SDR
PTHR19410	$\"[19-252]T$	SHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106	$\"[19-180]T$	adh_short

InterPro
IPR002347
Family

Glucose/ribitol dehydrogenase
PR00081	$\"[20-37]T$ $\"[88-99]T$ $\"[135-151]T$ $\"[161-180]T$ $\"[182-199]T$	GDHRDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[18-238]T$	no description
PTHR19410:SF42	$\"[19-252]T$	SHORT-CHAIN DEHYDROGENASE-RELATED

","BeTs to 9 clades of COG0300COG name: Short-chain dehydrogenases of various substrate specificitiesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0300 is -o----y---rlb-ef-hsnuj----Number of proteins in this genome belonging to this COG is 3","***** IPB002347 (Glucose/ribitol dehydrogenase family signature) with a combined E-value of 3.1e-21. IPB002347A 20-37 IPB002347B 88-99 IPB002347C 135-151 IPB002347D 161-180 IPB002347E 182-199***** IPB002198 (Short-chain dehydrogenase/reductase SDR) with a combined E-value of 6e-13. IPB002198A 90-99 IPB002198B 141-189***** IPB003560 (2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature) with a combined E-value of 3.3e-10. IPB003560A 25-42 IPB003560C 112-132 IPB003560D 176-199","Residues 123-249 are 48% similar to a (ALCOHOL CHAIN SHORT DEHYDROGENASE DEHYDROGENASE) protein domain (PD166723) which is seen in Q8U4K9_PYRFU.Residues 129-178 are 72% similar to a (OXIDOREDUCTASE DEHYDROGENASE REDUCTASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY CHAIN SHORT PROBABLE OXIDOREDUCTASE) protein domain (PD003795) which is seen in Q82E61_STRAW.Residues 221-262 are 78% similar to a (OXIDOREDUCTASE CHAIN DEHYDROGENASE/REDUCTASE SHORT OXIDOREDUCTASE SHORT-CHAIN DEHYDROGENASE FAMILY 1.-.-.- PROBABLE) protein domain (PD006579) which is seen in Q9X890_STRCO.","","-45% similar to PDB:2NWQ Short chain dehydrogenase from Pseudomonas aeruginosa (E_value = 1.3E_12);-35% similar to PDB:2JAH BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE CLAVULANIC ACID DEHYDEOGENASE (CAD) FROM STREPTOMYCES CLAVULIGERUS (E_value = 2.5E_11);-35% similar to PDB:2JAP CLAVULANIC ACID DEHYDROGENASE: STRUCTURAL AND BIOCHEMICAL ANALYSIS OF THE FINAL STEP IN THE BIOSYNTHESIS OF THE BETA-LACTAMASE INHIBITOR CLAVULANIC ACID (E_value = 2.5E_11);","Residues 19 to 180 (E_value = 3e-18) place ANA_1235 in the adh_short family which is described as short chain dehydrogenase.Residues 21 to 244 (E_value = 8.5e-05) place ANA_1235 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 22 to 183 (E_value = 0.00095) place ANA_1235 in the KR family which is described as KR domain.","","dehydrogenases of various substrate specificities (AB032242)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1237","1318803","1320170","1368","6.53","-2.20","47573","ATGAACGCCATCATCCTCGCCGTCCTGGTCATGCTCATCCTGGCGATGCTGCGCGTCCATGTGGTCCTGTCCCTGTTCGTCGGCGCGCTCGCGGGCGGGTTGAGTGCAGGCCTGGGCGTCAGCCGCACCATGGTCGCCTTCCAGGACGGACTGGCCGCCGGAGCCAAGATCGCCCTGTCCTATGCGCTGCTGGGGGCCTTCGCCATGGCGGTGGCGCACTCGGGCCTGCCCCAGCTGCTGGCGAACTGGCTCATCGGCCGCATCGAGAACAAGGACGAGTCCGTCTCCCGCAGGGCCGTGCGCACCACCACCATGCTGGTGCTGGGCGGGATCACGGCCATGGCTGTCATGAGTCAGAACCTCATCCCGGTTCACATCGCCTTCATCCCACTGGTGGTCCCGCCGCTGCTCATCGTCATGAGCCGTCTGCAGCTGGACCGTCGCGCCGTGGCCTGCGCCATCACCTTCGGGCTGGTCACCACCTACATGTTCCTGCCCCTGGGCTTCGGACGGGTCTTCCTCCATGACATCCTCTACGCCAACATCGAGGAGGCGGGCCTGGACGTCTCCCAGGTCCCGGCCACCCAGGCCATGGGGATTCCGGCGCTGGGTATGCTCGCGGGACTGCTCATCGCCGTGTTCGTCACCTACCGCAAGCCCCGCGTCTACCGGGTCGAGACCGGCAGCACCACCGGCTCGGGCGAGGAGGACTCCGGCCCGGTCGAGATCGACCGCCACAAGGTGGCGATCGCGCTGGTCGCCGTCGTCGCCTGCTTCATGGTCCAGACCTTCCTGACCTGGACGGAGTCCGAGGCCGACCCGCTCCTGGTCGGGGCCCTGATCGGCCTGCTGCTGTTCATGGCCACCCGGGTCGTCACCATCGCCGAGGCCGACGACGTCTTCACCGGAGGTATGCGGATGATGGCGCTCATCGGGCTCATCATGATCACGGCGCAGGGCTTCGCCAATGTCCTCAAGGAGACCAAGCAGATCGAGCCGCTGGTGACGTCGGCGACATCCTTGTTCGCGGGCTCCAAGCCCGCAGCCGCCTTCGTCATGCTGCTCGTGGGCCTCATCGTGACGATGGGTATCGGCTCGTCCTTCTCCACCCTGCCGATCATCTCCGCAATCTACGTGCCGTTGTGCGTCTCCCTGGGCTTCTCACCGGTCGCCACGGTCTCTCTCATCGGGACCGCCGGGGCCCTGGGGGATGCCGGCTCACCGGCGTCGGACTCCACGCTGGGGCCCACGGCCGGGCTCAACGCCGACGGGCAGCACGACCACATGCGCGACTCGGTCATCCCGACCTTCCTGCACTTCAACATTCCGCTGCTCATCGCCGGGTGGATCGCCGCCATGGTGCTCTGA","MNAIILAVLVMLILAMLRVHVVLSLFVGALAGGLSAGLGVSRTMVAFQDGLAAGAKIALSYALLGAFAMAVAHSGLPQLLANWLIGRIENKDESVSRRAVRTTTMLVLGGITAMAVMSQNLIPVHIAFIPLVVPPLLIVMSRLQLDRRAVACAITFGLVTTYMFLPLGFGRVFLHDILYANIEEAGLDVSQVPATQAMGIPALGMLAGLLIAVFVTYRKPRVYRVETGSTTGSGEEDSGPVEIDRHKVAIALVAVVACFMVQTFLTWTESEADPLLVGALIGLLLFMATRVVTIAEADDVFTGGMRMMALIGLIMITAQGFANVLKETKQIEPLVTSATSLFAGSKPAAAFVMLLVGLIVTMGIGSSFSTLPIISAIYVPLCVSLGFSPVATVSLIGTAGALGDAGSPASDSTLGPTAGLNADGQHDHMRDSVIPTFLHFNIPLLIAGWIAAMVL$","Na+/H+ antiporter","Membrane, Cytoplasm","Na+/H+ antiporter family protein","Na+/H+ antiporter family protein","Na+/H+ antiporter NhaC","","","","","

InterPro
IPR004770
Family

Na+/H+ antiporter NhaC
PF03553	$\"[153-449]T$	Na_H_antiporter

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[5-27]?$ $\"[57-77]?$ $\"[98-118]?$ $\"[124-139]?$ $\"[149-169]?$ $\"[197-217]?$ $\"[248-268]?$ $\"[274-292]?$ $\"[307-325]?$ $\"[348-368]?$ $\"[377-397]?$ $\"[433-453]?$	transmembrane_regions

","BeTs to 8 clades of COG2056COG name: Predicted permeaseFunctional Class: RThe phylogenetic pattern of COG2056 is ---------b-huj-------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 386-434 are 89% similar to a (PERMEASE GLUCONATE TRANSPORTER MEMBRANE TRANSMEMBRANE HIGH-AFFINITY FAMILY GNTP SUGAR SYSTEM) protein domain (PD005615) which is seen in Q6NG69_CORDI.Residues 449-521 are 83% similar to a (MEMBRANE PERMEASE INTEGRAL NA/H TRANSPORTER PROBABLE SIMILAR PROTEIN ANTIPORTER ANTIPORTER) protein domain (PD231247) which is seen in Q9KT98_VIBCH.Residues 519-689 are 66% similar to a (MEMBRANE PERMEASE INTEGRAL NA/H TRANSPORTER PROBABLE SIMILAR PROTEIN ANTIPORTER ANTIPORTER) protein domain (PD442276) which is seen in Q6NG69_CORDI.Residues 698-798 are similar to a (NA/H ANTIPORTER NHAC MEMBRANE TRANSPORTER INTEGRAL FAMILY PROBABLE TRANSMEMBRANE C4-DICARBOXYLATE) protein domain (PD007817) which is seen in Q9JXG2_NEIMB.","","No significant hits to the PDB database (E-value < E-10).","Residues 349 to 741 (E_value = 0.0024) place ANA_1237 in the CitMHS family which is described as Citrate transporter.Residues 351 to 797 (E_value = 0.0042) place ANA_1237 in the DctM family which is described as DctM-like transporters.Residues 496 to 792 (E_value = 1.1e-71) place ANA_1237 in the Na_H_antiporter family which is described as Na+/H+ antiporter family.","","antiporter family protein","","1","","","Thu Aug 2 17:44:53 2007","","Thu Aug 2 17:44:53 2007","","","Thu Aug 2 17:44:53 2007","Thu Aug 2 17:44:53 2007","Thu Aug 2 17:44:53 2007","","","","","","Thu Aug 2 17:44:53 2007","Thu Aug 2 17:44:53 2007","Thu Aug 2 17:44:53 2007","","Thu Aug 2 17:44:53 2007","Thu Aug 2 17:44:53 2007","","","","","yes","","" "ANA_1238","1320260","1321084","825","5.46","-5.12","28001","ATGCGTATCGGGTTCATCGGCGCCGGCAACATGGTCAGCGCCATTGTGCGAGGGGCCGTGGCTGCGGGAACACCGGCCGGGCACCTGCTGCTGACCAGCAAGCACGGCTCTGCCGAGCGTTTGGCCGAGCAGGTCGGGGCCGTCCACGTGCCCGACGCCGCCGAGCTGGTGTCACGCAGCGACGTCCTCATCCTGGGCCTCAAGCCCTACGTCATCCCCGATGTCCTGCCCCGGTTGTCGGAGGCCATCACCGACAGCCGCCCCCTGGTGGTCTCCATCGCGGCCGGTGTGCCCTTGGAGCGTTTGGAGTCGATGCTGCCGAGCGGCACCCGGGTGGTGCGCACCATGCCGAACATGGCCGCCTCCGTGGGCGAGTCGATGACCGCACTGGCCCCCGGCAGCAGTGCGAGCGCCGAGGACCTGGAGACGGTTCGCACCCTCATGGAGACCATCGGTCGCACCGTGGTCCTGGAGGAGAAGGACTTCTCCTCCTTCATCGGTCTGGCGGGCTCCTCCCCCGCCCTGGTGTGCGCCTTCATCGACGCCCTGGCTCGCGCCGGCGTCATGGGCGGCATCCCCAAGGCCCAGGCCGTCCAGATCGTGGCGCAGGCGGTGCTGGGAACCGCCCGTACCGTGCAGACCGAGGCTCAGCGCACCGCTGAGGGAGGCCACGGCCGCACCCCGGCCGACCTCATCGACGCGGTCTGCTCCCCCGGAGGGACAACAGTGGCGGGCATGGTGGCCCTGGAGCGGGCCGGTTTCTCCGACGCCGTCGTGCGCGCCTTCGAGGCCATTGCCGAGAGGGACCGCGAGCTGGGCGCCTGA","MRIGFIGAGNMVSAIVRGAVAAGTPAGHLLLTSKHGSAERLAEQVGAVHVPDAAELVSRSDVLILGLKPYVIPDVLPRLSEAITDSRPLVVSIAAGVPLERLESMLPSGTRVVRTMPNMAASVGESMTALAPGSSASAEDLETVRTLMETIGRTVVLEEKDFSSFIGLAGSSPALVCAFIDALARAGVMGGIPKAQAVQIVAQAVLGTARTVQTEAQRTAEGGHGRTPADLIDAVCSPGGTTVAGMVALERAGFSDAVVRAFEAIAERDRELGA$","Pyrroline-5-carboxylate reductase","Cytoplasm, Membrane","pyrroline-5-carboxylate reductase","pyrroline-5-carboxylate reductase ","pyrroline-5-carboxylate reductase","","Delauney A.J., Verma D.P. A soybean gene encoding delta 1-pyrroline-5-carboxylate reductase was isolated by functional complementation in Escherichia coli and is found to be osmoregulated. Mol. Gen. Genet. 1990. 221(3):299-305. PMID: 2199815Savioz A., Jeenes D.J., Kocher H.P., Haas D. Comparison of proC and other housekeeping genes of Pseudomonas aeruginosa with their counterparts in Escherichia coli. Gene 1990. 86(1):107-111. PMID: 2107123","","","

InterPro
IPR000304
Family

Delta 1-pyrroline-5-carboxylate reductase
PIRSF000193	$\"[1-274]T$	Pyrroline-5-carboxylate reductase
PTHR11645	$\"[1-274]T$	PYRROLINE-5-CARBOXYLATE REDUCTASE
TIGR00112	$\"[3-272]T$	proC: pyrroline-5-carboxylate reductase

InterPro
IPR004455
Family

NADP oxidoreductase, coenzyme F420-dependent
PF03807	$\"[2-257]T$	F420_oxidored

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[1-91]T$	no description
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 19 clades of COG0345COG name: Pyrroline-5-carboxylate reductaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0345 is --mp-zyqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB000304 (Delta 1-pyrroline-5-carboxylate reductase) with a combined E-value of 2.9e-55. IPB000304A 3-18 IPB000304B 60-70 IPB000304C 87-100 IPB000304D 111-121 IPB000304E 159-203 IPB000304F 227-255","Residues 90-249 are 65% similar to a (REDUCTASE OXIDOREDUCTASE PYRROLINE-5-CARBOXYLATE BIOSYNTHESIS NADP PROLINE P5CR P5C REDUCTASE PYRROLINE) protein domain (PD002555) which is seen in Q9A1S9_STRPY.","","-56% similar to PDB:2AHR Crystal Structures of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus pyogenes (E_value = 8.5E_42);-56% similar to PDB:2AMF Crystal structure of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus Pyogenes (E_value = 8.5E_42);-47% similar to PDB:2GER Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase (E_value = 7.7E_35);-47% similar to PDB:2GR9 Crystal structure of P5CR complexed with NADH (E_value = 7.7E_35);-47% similar to PDB:2GRA crystal structure of Human Pyrroline-5-carboxylate Reductase complexed with nadp (E_value = 7.7E_35);","Residues 1 to 145 (E_value = 0.00053) place ANA_1238 in the NAD_Gly3P_dh_N family which is described as NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus.Residues 2 to 257 (E_value = 4.2e-60) place ANA_1238 in the F420_oxidored family which is described as NADP oxidoreductase coenzyme F420-dependent.","","reductase (proC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1239","1321550","1323253","1704","5.79","-7.39","62455","ATGACCACCACCGTCACGCCACCCGCCCGCACCCTGCGCCCACCGCGCAAGGCCCGTTCCAACGGCCAGTGGGCCCTCGACGGGCGCAAGCCGCTCAATGACAACGAGGCCTTCAAGCAGGACGGGGACCCGCTGGCGGTGCGCGACCGGATCGTGAACATCTACGGTCCCGGCGGCTACGAGAGCATCGCACCCGATGACCTCAACGGCCGTTTCCGCTGGTGGGGTCTGTACACCCAGCGCAAGCAGGGGATCGACGGCGGCCGCACCGCCCAGCTGGACGCCTCCGAGCTCTCCGACCGCTACTTCATGCAGCGGGTGCGCCTGGACGGTGGGAGCCTGAGCCGTGAGCAGCTGCGGGTGCTCGGCTCGGTCTCCAACGACTTCGCCCGCGGCACCGCCGACATCACCGACCGGCAGAACATCCAGCTGCACTGGGTGGAGATCGACAATGTCCCAGAGCTGTGGCGGCGCCTGGAGTCAGTGGGGCTGACCACGATTGAGGGCTGTGGGGACACGCCTCGGGGATTCCTGGTCTCCCCGGTGGCCGGCATCGCCAAGGACGAGGTCATCGATCCGACCCCGCTGGCCCGTGACATCAAGGACACCTACCTGGGCGACCCCGAGCTGGCCAATCTTCCCCGCAAGTTCAAGACGGCCATCACCGGCTCCCCCAGCCTCGACATCCTCCACGAGATCAACGACATCTCCTTCGTGGGCGTCAACCACCCCGAGCTCGGTCCCGGCTACGACCTGTGGGTGGCCGGCGCCCTGTCCACCGCCCCGCGTCTGGGTCAGCGGCTAGGGGCCTTCGTCACCCCTGAGGACGCCCTGGACGTCTGGTACGCCGTCATCCGCATCTTCCGCGACTACGGCTACCGTCGCCTGCGCAACAAGGCCCGGTTGAAGTTCCTCATGGCCGAGTGGGGGCCGGAGAAGTTCCGCCAGGTCCTCCAGGACGACTACCTGGGGCGTGCCCTGCCCGACGGCCCGGCCCCTGAGGAGCCGAGCGGGGACTCCGACCACATCGGCGTCCACGAGCAGAAGGACGGCCGCTTCTGGGTGGGGGCCAAGCCGCCCGTCGGCAGGTTGAGCGGGGATGTCCTGCTGGGCCTGGCAGACCTGGCCGAGCGGGTCGGCTCGGACCGGGTGCGCACCACCCCGCTGCAGAACCTGCTACTCCTGGACGTGCCCGCCGAGAAGGTCGACGACGCCGTCGCCGGTCTGCGGGAGCTGGGGCTCGATCCCACCCCGGGCGCCTTCACCCGCTCGACCTTGGCCTGCACCGGGCTGGAGTTCTGCAAGTTCGCGATCGTGGAGACCAAGAAGTTGGCGGCGCGCGTCTCGGCCGAGCTCGACGCGCGCCTGGCCGACACCGACCTGGAGCGGCGCATCACCTTGACCGTCAACGGCTGCCCGAACTCCTGCGCCCGCATCCAGATCGCGGACATCGGCCTCAAGGGCCAGATCATCACGGTCGACGGCGAGCAGATGCCCGGCTTTCAGGTGCACCTGGGCGGCGGCCTGGCCACCGACGGACGCGCCGAGGCCGGCCTGGGCCGCACGGTGCGGGGCCTGAAGGTCCCCGCCTCCGGCCTGACCGACTACGTCGAGCGCCTGGTGCGCCGCTACCTGGATCAGCGCCTCCCTGAGGAGACCTTCGCCCAATGGGCGCACCGAGCCGATGAGGAGGCCCTGCAGTGA","MTTTVTPPARTLRPPRKARSNGQWALDGRKPLNDNEAFKQDGDPLAVRDRIVNIYGPGGYESIAPDDLNGRFRWWGLYTQRKQGIDGGRTAQLDASELSDRYFMQRVRLDGGSLSREQLRVLGSVSNDFARGTADITDRQNIQLHWVEIDNVPELWRRLESVGLTTIEGCGDTPRGFLVSPVAGIAKDEVIDPTPLARDIKDTYLGDPELANLPRKFKTAITGSPSLDILHEINDISFVGVNHPELGPGYDLWVAGALSTAPRLGQRLGAFVTPEDALDVWYAVIRIFRDYGYRRLRNKARLKFLMAEWGPEKFRQVLQDDYLGRALPDGPAPEEPSGDSDHIGVHEQKDGRFWVGAKPPVGRLSGDVLLGLADLAERVGSDRVRTTPLQNLLLLDVPAEKVDDAVAGLRELGLDPTPGAFTRSTLACTGLEFCKFAIVETKKLAARVSAELDARLADTDLERRITLTVNGCPNSCARIQIADIGLKGQIITVDGEQMPGFQVHLGGGLATDGRAEAGLGRTVRGLKVPASGLTDYVERLVRRYLDQRLPEETFAQWAHRADEEALQ$","Putative nitrite/sulphite reductase","Cytoplasm","nitrile/sulphite reductase","putative nitrite/sulphite reductase ","Sulfite reductase (ferredoxin)","","Zeghouf M., Fontecave M., Coves J. A simplifed functional version of the Escherichia coli sulfite reductase. J. Biol. Chem. 2000. 275(48):37651-37656. PMID: 10984484Crane B.R., Siegel L.M., Getzoff E.D. Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. Science 1995. 270(5233):59-67. PMID: 7569952","","","

InterPro
IPR005117
Domain

Nitrite/sulfite reductase, hemoprotein beta-component, ferrodoxin-like
PF03460	$\"[93-162]T$ $\"[343-412]T$	NIR_SIR_ferr

InterPro
IPR006066
Domain

Nitrite and sulfite reductase iron-sulfur/siroheme-binding site
PR00397	$\"[423-441]T$ $\"[470-488]T$	SIROHAEM
PS00365	$\"[470-486]T$	NIR_SIR

InterPro
IPR006067
Domain

Nitrite and sulphite reductase 4Fe-4S region
PF01077	$\"[170-327]T$ $\"[418-542]T$	NIR_SIR

InterPro
IPR008287
Family

Ferredoxin-nitrite reductase
PIRSF000244	$\"[36-567]T$	Sulfite/ferredoxin-nitrite reductase

noIPR
unintegrated

unintegrated
G3DSA:3.30.413.10	$\"[171-322]T$ $\"[419-562]T$	no description
PIRSF500146	$\"[1-567]T$	Ferredoxin--nitrite reductase

","BeTs to 12 clades of COG0155COG name: Sulfite reductase hemoprotein beta-componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0155 is a-----yq-dr-bcefg-sn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB011255 (Nitrite/sulfite reductase, flavoprotein alpha-component, domains 1 and 3) with a combined E-value of 2.2e-47. IPB011255B 136-147 IPB011255D 205-218 IPB011255F 283-319 IPB011255G 350-372 IPB011255H 426-441 IPB011255I 470-488 IPB011255J 540-560***** IPB005117 (Nitrite/sulfite reductase ferredoxin-like half domain) with a combined E-value of 6.6e-13. IPB005117A 427-441 IPB005117B 470-488","Residues 33-84 are 71% similar to a (REDUCTASE NITRITE OXIDOREDUCTASE FERREDOXIN--NITRITE FERREDOXIN-NITRITE FERREDOXIN IRON-SULFUR PEPTIDE NITRATE CHLOROPLAST) protein domain (PD011025) which is seen in Q82L84_STRAW.Residues 106-197 are 47% similar to a (BIOSYNTHESIS COBALAMIN OXIDOREDUCTASE PROBABLE PORPHYRIN SYNTHASE PRECORRIN-3B METAL-BINDING IRON AGR_C_5083P) protein domain (PD432427) which is seen in Q9HZU1_PSEAE.Residues 106-147 are 90% similar to a (REDUCTASE OXIDOREDUCTASE SULFITE NITRITE IRON-SULFUR 4FE-4S FERREDOXIN--NITRITE FERREDOXIN-NITRITE SUBUNIT HEMOPROTEIN) protein domain (PD126478) which is seen in Q82L84_STRAW.Residues 146-397 are 43% similar to a (REDUCTASE FERREDOXIN-NITRITE NIRA) protein domain (PD456422) which is seen in O30073_ARCFU.Residues 149-190 are 83% similar to a (REDUCTASE OXIDOREDUCTASE NITRITE SULFITE FERREDOXIN--NITRITE FERREDOXIN-NITRITE HEMOPROTEIN FERREDOXIN SUBUNIT PROBABLE) protein domain (PDA195L9) which is seen in Q700Z2_STRPE.Residues 191-248 are 77% similar to a (REDUCTASE OXIDOREDUCTASE NITRITE NITRITE/SULPHITE PROBABLE HEMOPROTEIN NIRA NITRILE/SULPHITE FERREDOXIN--NITRITE FERREDOXIN-DEPENDENT) protein domain (PDA04171) which is seen in Q82L84_STRAW.Residues 249-322 are similar to a (REDUCTASE OXIDOREDUCTASE SULFITE NITRITE SUBUNIT IRON-SULFUR 4FE-4S FLAVOPROTEIN FAD NADPH) protein domain (PD002535) which is seen in Q7WT38_BBBBB.Residues 348-423 are 63% similar to a (HEMOPROTEIN REDUCTASE SULFITE BETA-COMPONENT OXIDOREDUCTASE) protein domain (PDA1B850) which is seen in Q8NLW9_CORGL.Residues 362-420 are 69% similar to a (REDUCTASE OXIDOREDUCTASE NITRITE SULFITE FERREDOXIN--NITRITE FERREDOXIN-NITRITE FERREDOXIN SUBUNIT PROBABLE HEMOPROTEIN) protein domain (PD858437) which is seen in Q73YC1_MYCPA.Residues 427-486 are 73% similar to a (REDUCTASE OXIDOREDUCTASE SULFITE NITRITE IRON-SULFUR SUBUNIT 4FE-4S HEMOPROTEIN NADPH HEME) protein domain (PD000955) which is seen in Q9ADG1_STRCO.Residues 487-566 are 67% similar to a (REDUCTASE OXIDOREDUCTASE NITRITE PROBABLE HEMOPROTEIN NIRA NITRITE/SULPHITE BETA-COMPONENT NITRILE/SULPHITE FERREDOXIN--NITRITE) protein domain (PD993596) which is seen in Q82L84_STRAW.","","-69% similar to PDB:1ZJ8 Structure of Mycobacterium tuberculosis NirA protein (E_value = 7.4E_172);-69% similar to PDB:1ZJ9 Structure of Mycobacterium tuberculosis NirA protein (E_value = 7.4E_172);-50% similar to PDB:2AKJ Structure of spinach nitrite reductase (E_value = 1.2E_57);-42% similar to PDB:1AOP SULFITE REDUCTASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION (E_value = 6.1E_25);-42% similar to PDB:2AOP SULFITE REDUCTASE: REDUCED WITH CRII EDTA, SIROHEME FEII, [4FE-4S] +1, PHOSPHATE BOUND (E_value = 6.1E_25);","Residues 93 to 162 (E_value = 4.3e-20) place ANA_1239 in the NIR_SIR_ferr family which is described as Nitrite/Sulfite reductase ferredoxin-like half domain.Residues 170 to 327 (E_value = 8e-54) place ANA_1239 in the NIR_SIR family which is described as Nitrite and sulphite reductase 4Fe-4S domain.Residues 343 to 412 (E_value = 2.7e-16) place ANA_1239 in the NIR_SIR_ferr family which is described as Nitrite/Sulfite reductase ferredoxin-like half domain.Residues 418 to 566 (E_value = 6.4e-15) place ANA_1239 in the NIR_SIR family which is described as Nitrite and sulphite reductase 4Fe-4S domain.","","reductase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1240","1323250","1324041","792","5.15","-10.52","28058","GTGAGCGCCACAACCACTGACCGCACCCAGGCATCCCTGAACGTGGCGCACCGTGCTCCTGCCGCCTCGGGGTCTCGGGGAGCCGGCTCGGCCCCGCTGCGGTCCACGGAGGAGCTGCGCGCCCTGGCCGAGGCCGGTGCGCGCGAGCTCGGTGACGATGCCCCGGCCCTCGACGTCGCCCAGTGGGCGGCCCAGAACTTCCCCGACACGCTGGCCGTGGCTTGCTCCATGGCCGACGCCGTCCTGCCGCACGTGGTCTCCCGGGTCCTGCCCGGCGTCGACGTCCTCTTCCTGGACACCGGCTACCACTTCACCGAGACCGTGGGTACCCGCGACGCCGTGGCCGCCACCATGGACGTCACCGTCGTCGACGTGACTCCTGAGCTGAGCCTGGCCGAGCAGGACGAGCGCTACGGGCCGGACCTGTGGTCGCGGGACCCGGCCGCCTGCTGCCGTCTGCGCAAGGTCGAGCCGCTGGCGAGGGCCCTGAGCGGCTACGAGGCCTGGGCCACCGGGGTGCGCCGCGAGGACGCCCCCACCCGCACCCACACACCGTTGATCGGATGGGACGCCACCCACGAGATCGTCAAGATCAATCCCCTGGCCGCCTGGAGCATGGAGGAGCTGACCGGCTACGCCGACCAGCACGGAGTGCTCATCAACCCCCTCCTGTACGACGGCTACCCCTCGATCGGCTGCGCCCCGTGCACGGCGCGAGTCAAGCCCGGAGACGACCCCCGTTCCGGCCGCTGGGCCGGATTCACCAAGACAGAATGCGGAATCCACCTATGA","VSATTTDRTQASLNVAHRAPAASGSRGAGSAPLRSTEELRALAEAGARELGDDAPALDVAQWAAQNFPDTLAVACSMADAVLPHVVSRVLPGVDVLFLDTGYHFTETVGTRDAVAATMDVTVVDVTPELSLAEQDERYGPDLWSRDPAACCRLRKVEPLARALSGYEAWATGVRREDAPTRTHTPLIGWDATHEIVKINPLAAWSMEELTGYADQHGVLINPLLYDGYPSIGCAPCTARVKPGDDPRSGRWAGFTKTECGIHL$","Phosphoadenosine phosphosulfate reductase","Cytoplasm, Extracellular","phosophoadenylyl-sulfate reductase","phosphoadenosine phosphosulfate reductase ","phosphoadenosine phosphosulfate reductase","","Savage H., Montoya G., Svensson C., Schwenn J.D., Sinning I. Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure 1997. 5(7):895-906. PMID: 9261082Berendt U., Haverkamp T., Prior A., Schwenn J.D. Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 1995. 233(1):347-356. PMID: 7588765Schwedock J., Long S.R. ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti. Nature 1990. 348(6302):644-647. PMID: 2250719","","","

InterPro
IPR002500
Domain

Phosphoadenosine phosphosulfate reductase
PF01507	$\"[70-239]T$	PAPS_reduct

InterPro
IPR004511
Family

Phosphoadenosine phosphosulfate reductase CysH-type
TIGR00434	$\"[56-263]T$	cysH: phosophoadenylyl-sulfate reductase

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[25-233]T$	no description

","BeTs to 13 clades of COG0175COG name: 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase and related enzymesFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0175 is -ompkzy--drlbcefg-sn-j----Number of proteins in this genome belonging to this COG is 2","***** IPB002500 (Phosphoadenosine phosphosulfate reductase) with a combined E-value of 1.2e-27. IPB002500B 95-112 IPB002500C 168-178 IPB002500D 196-232 IPB002500E 256-263","Residues 61-111 are 76% similar to a (REDUCTASE TRANSFERASE SUBUNIT SULFATE PAPS PHOSPHOADENOSINE PHOSPHOSULFATE BIOSYNTHESIS NUCLEOTIDYLTRANSFERASE CYSTEINE) protein domain (PD002993) which is seen in Q9ADG3_STRCO.Residues 131-237 are similar to a (REDUCTASE TRANSFERASE PAPS SUBUNIT PHOSPHOADENOSINE PHOSPHOSULFATE SULFATE BIOSYNTHESIS CYSTEINE SULFOTRANSFERASE) protein domain (PD002340) which is seen in Q82L82_STRAW.","","-46% similar to PDB:2GOY Crystal structure of assimilatory adenosine 5'-phosphosulfate reductase with bound APS (E_value = 9.1E_22);-46% similar to PDB:2O8V PAPS reductase in a covalent complex with thioredoxin C35A (E_value = 9.4E_19);-46% similar to PDB:1SUR PHOSPHO-ADENYLYL-SULFATE REDUCTASE (E_value = 1.1E_14);-50% similar to PDB:1XDO Crystal Structure of Escherichia coli Polyphosphate Kinase (E_value = 1.1E_14);-50% similar to PDB:1XDP Crystal Structure of the E.coli Polyphosphate Kinase in complex with AMPPNP (E_value = 1.1E_14);","Residues 70 to 239 (E_value = 1.4e-53) place ANA_1240 in the PAPS_reduct family which is described as Phosphoadenosine phosphosulfate reductase family.","","reductase (cysH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1241","1324023","1325048","1026","5.53","-9.86","38467","ATGCGGAATCCACCTATGAGCATCACCCTGACCCACACCCGTCCGGCCCCAGCCCCCTCCTCCACCCCCCATCAGACGCCGGAGCTCGAACCGGCCGGCCTGGCCGACCTCTCCCGGGCCCCCGTCACCACTGAGGCCCTGGACATCCTTGACGTCCTGGAGGCCGAGGCCATCCTCGTCATCCGGGAGATCGCCGCCGAGTGCCGCCGCCCCGTGCTGCTGTTCTCCGGGGGCAAGGACTCCGTGGTCATGCTGCACCTGGCGCGCAAGGCCTTCTGGCCCGCTCCGATCCCCTTCCCCGTCCTGCACGTGGACACCGGCCACAACTTCCCCGAGTTGCTGGCCTACCGTGACCGGACGGTCGAGGAGCTCGGTCTGCGGCTCGTGGTGGCCCGCGTCCAGGACTACATCGACGACGGCCGTCTGCGCGAGCGCAACGACGGCACCCGTAACCCGCTCCAGACGATCCCGCTTCTCGACGCCATCGAAGAGGGCGGCTTCGACGGTGTCTTCGGCGGCGGGCGCCGCGACGAGGAGAAGGCCCGGGCCAAGGAGCGCATCGTCTCCCTGCGCGACGAGTTCGGCCAGTGGGACCCGCGCAACCAGCGCCCCGAGCTGTGGAACCTGCTCAACCCCCGCCACCGCCCCGGTGAGCACGTGCGGGTCTTCCCCTTGAGCAACTGGACCGAGCTGGACGTGTGGCGCTACATCGAGCGTGAGGACATCGCCCTGCCCGGCCTCTACTACGCCCATGAGCGTGAGGTCTTCCTGCGTGACGGGATGTGGCTGGCGGCCGGCGGCGTCAACCGGCTGCGCGACGGCGAGCAGGTGGTCACCCGCACCGTGCGCTACCGCACTGTGGGCGACATGTCCTGCACCGGCGCCGTCGAGTCCGAGGCTGCCACCAACCACGACATCGTTCTGGAGGTCGCCGCCTCCACCCTGACCGAGCGGGGAGCCACCCGCGCCGATGACCGCCTGAGCGAGGCGGCCATGGAGGACCGCAAGAAGGAGGGCTACTTCTGA","MRNPPMSITLTHTRPAPAPSSTPHQTPELEPAGLADLSRAPVTTEALDILDVLEAEAILVIREIAAECRRPVLLFSGGKDSVVMLHLARKAFWPAPIPFPVLHVDTGHNFPELLAYRDRTVEELGLRLVVARVQDYIDDGRLRERNDGTRNPLQTIPLLDAIEEGGFDGVFGGGRRDEEKARAKERIVSLRDEFGQWDPRNQRPELWNLLNPRHRPGEHVRVFPLSNWTELDVWRYIEREDIALPGLYYAHEREVFLRDGMWLAAGGVNRLRDGEQVVTRTVRYRTVGDMSCTGAVESEAATNHDIVLEVAASTLTERGATRADDRLSEAAMEDRKKEGYF$","Sulfate adenylyltransferase, small subunit","Cytoplasm","Sulfate adenylyltransferase subunit 2 (Sulfateadenylatetransferase) (SAT) (ATP-sulfurylase small","putative sulfate adenylyltransferase subunit 2 ","sulfate adenylyltransferase, small subunit","","Savage H., Montoya G., Svensson C., Schwenn J.D., Sinning I. Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure 1997. 5(7):895-906. PMID: 9261082Berendt U., Haverkamp T., Prior A., Schwenn J.D. Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 1995. 233(1):347-356. PMID: 7588765Schwedock J., Long S.R. ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti. Nature 1990. 348(6302):644-647. PMID: 2250719","","","

InterPro
IPR002500
Domain

Phosphoadenosine phosphosulfate reductase
PF01507	$\"[70-295]T$	PAPS_reduct

InterPro
IPR011784
Family

Sulfate adenylyltransferase, small subunit
TIGR02039	$\"[50-341]T$	CysD: sulfate adenylyltransferase, small su

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[54-248]T$	no description

","BeTs to 12 clades of COG0175COG name: 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase and related enzymesFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0175 is -ompkzy--drlbcefg-sn-j----Number of proteins in this genome belonging to this COG is 2","***** IPB002500 (Phosphoadenosine phosphosulfate reductase) with a combined E-value of 5.2e-37. IPB002500A 78-87 IPB002500B 101-118 IPB002500C 169-179 IPB002500D 220-256***** IPB011063 (PP-loop) with a combined E-value of 2.7e-06. IPB011063A 69-88","Residues 62-137 are similar to a (REDUCTASE TRANSFERASE SUBUNIT SULFATE PAPS PHOSPHOADENOSINE PHOSPHOSULFATE BIOSYNTHESIS NUCLEOTIDYLTRANSFERASE CYSTEINE) protein domain (PD002993) which is seen in MMCV_STRLA.Residues 149-248 are similar to a (REDUCTASE TRANSFERASE PAPS SUBUNIT PHOSPHOADENOSINE PHOSPHOSULFATE SULFATE BIOSYNTHESIS CYSTEINE SULFOTRANSFERASE) protein domain (PD002340) which is seen in Q8EYJ4_LEPIN.Residues 203-248 are 89% similar to a (TRANSFERASE SULFATE SUBUNIT NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE BIOSYNTHESIS ADENYLATE SMALL SAT ATP-SULFURYLASE) protein domain (PD972511) which is seen in Q842M1_BBBBB.Residues 249-341 are similar to a (TRANSFERASE SUBUNIT SULFATE NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE ADENYLATE SMALL SAT ATP-SULFURYLASE BIOSYNTHESIS) protein domain (PD006993) which is seen in MMCV_STRLA.","","-55% similar to PDB:1ZUN Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae (E_value = 7.1E_52);","Residues 70 to 295 (E_value = 7.8e-96) place ANA_1241 in the PAPS_reduct family which is described as Phosphoadenosine phosphosulfate reductase family.","","adenylyltransferase subunit 2 (Sulfate adenylatetransferase) (SAT) (ATP-sulfurylase small subunit) (Mitomycinbiosynthesis protein V)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1242","1325048","1326406","1359","5.09","-15.33","47538","ATGAGCACCCCCACCCTCACCGACATCCCCGCCGAGGCCGAGGCACGCGCCGCCGCCACCGGCTCGCTGCTGCGGCTGGCCACGGCCGGCAGCGTCGACGACGGCAAGTCCACGCTCGTGGGCCGCCTGCTGTTCGACTCCAAGTCCGTGCTGCGCGACCAGCTGGCCGCCGTCGAGCAGGTCAGCCTGGATCGGGGCCTGACCAGCGCCGACCTCGCGCTGCTGACCGACGGGCTGCGGGCTGAGCGGGAGCAGGGCATCACGATCGACGTCGCCTACCGCTACTTCGCCACCCCGCAGCGCTCCTTCATCCTGGCCGACTGCCCCGGGCACGTGCAGTACACCCGCAACACGGTCACCGGCTGCTCCACGGCCGACGTCGTCGTGCTGCTGGTGGACGCCCGCAATGGGGTCCTGGAGCAGACGCGCCGCCACCTGGCGGTCGCCGCCCTCCTGCGGGTCCCGCACGTCATCGTCGCGGTCAACAAGATCGACCTGGTGGACTTCTCCGCCGAGGTCTACGCGGCCATCGAGGCCGATATCCGCGCTGTGGCCGCCGAGCTGGGCGTGGCCGAGATCCATGTCCTGCCGACCTCCGCGCTCCTGGGGGACAACATCGTCGAGGCCTCGGCCAGCACGCCCTTCTACGAGGGGCCGACCCTGTTGGGGCTGCTGGAGTCCCTGCCCACCGCCCGTGAGGAGGGCGCCTTCCGCATGCCGGTCCAGCTGGTCATCCGCCCCCAGGGGGCGGCGCCGGCGCCTGAGCTGCGCGACTACCGGGGCTACGCCGGGCGGATCGCTTCGGGCACGGTGCGCGTCGGCGACCCCGTGGTGGTGCTGCCCTCGGGCAGGCACTCGCGCGTGGCCGGCATCGACCTGGGCGAGCGCAGCCTGGAGGAGGCCGTTGAGGGCCAGTCGGTGACGGTTCGCCTGACCGACGACATCGACGTCGCCCGCGGTGACACTCTGGCCGCGGCGGGGGACGCGCCCCAGGTGCTCACCGAGGTCGACGCCCGTGTGTCCTGGCTGAGCGAGGAGCCCCTGCGCCCCCGGGCGCGAGTACTGCTCAAGCACGGCGCCCAGACGGTCCAGGCGATCGTGCGCGCCATTGAGGGGCGCCTCGACCTCGATGACCTGACCACGGTGCCCGCTGACCGCCTGGAGCTCAACGACATCGGCCTGGTTCGGCTGCGTCTGGCCTCGCCGGTGCCCTTGGCCGACTACTCGGTCTCCCGGTCCGACGGCGCCTTCCTCCTCATCGACGCCCACGAGGGCGGCACGCTCGGGGCGGGCATGGTGCAGCTCGCAGGCGCAGGGCGCGGAGAACCGGCTGCGGCCGCCTCCTCAGGCAGGGGCTAA","MSTPTLTDIPAEAEARAAATGSLLRLATAGSVDDGKSTLVGRLLFDSKSVLRDQLAAVEQVSLDRGLTSADLALLTDGLRAEREQGITIDVAYRYFATPQRSFILADCPGHVQYTRNTVTGCSTADVVVLLVDARNGVLEQTRRHLAVAALLRVPHVIVAVNKIDLVDFSAEVYAAIEADIRAVAAELGVAEIHVLPTSALLGDNIVEASASTPFYEGPTLLGLLESLPTAREEGAFRMPVQLVIRPQGAAPAPELRDYRGYAGRIASGTVRVGDPVVVLPSGRHSRVAGIDLGERSLEEAVEGQSVTVRLTDDIDVARGDTLAAAGDAPQVLTEVDARVSWLSEEPLRPRARVLLKHGAQTVQAIVRAIEGRLDLDDLTTVPADRLELNDIGLVRLRLASPVPLADYSVSRSDGAFLLIDAHEGGTLGAGMVQLAGAGRGEPAAAASSGRG$","Sulfate adenylyltransferase, large subunit","Cytoplasm","sulfate adenylyltransferase subunit 1","sulfate adenylyltransferase; large subunit ","sulfate adenylyltransferase, large subunit","","Paduch M., JeleD F., Otlewski J. Structure of small G proteins and their regulators. Acta Biochim. Pol. 2001. 48(4):829-850. PMID: 11995995","","","

InterPro
IPR000795
Domain

Protein synthesis factor, GTP-binding
PR00315	$\"[25-38]T$ $\"[84-92]T$ $\"[104-114]T$ $\"[120-131]T$ $\"[157-166]T$	ELONGATNFCT
PF00009	$\"[21-232]T$	GTP_EFTU
PS00301	$\"[77-92]T$	EFACTOR_GTP

InterPro
IPR004161
Domain

Translation elongation factor EFTu/EF1A, domain 2
PF03144	$\"[264-324]T$	GTP_EFTU_D2

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[21-215]T$	small_GTP: small GTP-binding protein domain

InterPro
IPR011779
Domain

Sulfate adenylyltransferase, large subunit
TIGR02034	$\"[24-433]T$	CysN: sulfate adenylyltransferase, large su

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.10	$\"[232-366]T$	no description
G3DSA:3.40.50.300	$\"[14-216]T$	no description
PTHR23115	$\"[22-354]T$	TRANSLATION FACTOR
PTHR23115:SF34	$\"[22-354]T$	SULFATE ADENYLYLTRANSFERASE SUBUNIT 1

","BeTs to 6 clades of COG2895COG name: GTPases - Sulfate adenylate transferase subunit 1Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2895 is ----------r---efg-sn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB004160 (Elongation factor Tu, C-terminal) with a combined E-value of 1.1e-19. IPB004160A 23-43 IPB004160B 95-145***** IPB005517 (Elongation factor G, domain IV) with a combined E-value of 4.2e-09. IPB005517A 24-48 IPB005517C 103-142","Residues 23-66 are similar to a (GTP-BINDING SUBUNIT BIOSYNTHESIS TRANSFERASE SULFATE FACTOR NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE ADENYLATE KINASE) protein domain (PD000134) which is seen in Q73X26_MYCPA.Residues 30-225 are 40% similar to a (CHROMOSOME READING YOR076C CANDIDA K XV ORF GLABRATA STRAIN S.CEREVISIAE) protein domain (PD147587) which is seen in Q08491_YEAST.Residues 73-101 are identical to a (FACTOR GTP-BINDING ELONGATION BIOSYNTHESIS TU G EF-TU EF-G LEPA TRANSLATION) protein domain (PD012708) which is seen in Q9ADG6_STRCO.Residues 120-163 are similar to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS TU EF-TU TRANSLATION INITIATION SUBUNIT 1-ALPHA) protein domain (PD173400) which is seen in Q82L80_STRAW.Residues 164-262 are 54% similar to a (TRANSFERASE SULFATE SUBUNIT GTP-BINDING ADENYLYLTRANSFERASE ADENYLATE NUCLEOTIDYLTRANSFERASE KINASE SAT LARGE) protein domain (PD812628) which is seen in Q7WGW4_BORBR.Residues 164-244 are 63% similar to a (FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS TU EF-TU 1-ALPHA TRANSLATION SUBUNIT EF-1-ALPHA) protein domain (PD007358) which is seen in Q8FM67_COREF.Residues 264-332 are similar to a (GTP-BINDING BIOSYNTHESIS FACTOR SUBUNIT TRANSFERASE SULFATE ELONGATION NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE ADENYLATE) protein domain (PD245502) which is seen in CYSN_XYLFT.Residues 390-433 are 72% similar to a (SUBUNIT TRANSFERASE SULFATE GTP-BINDING NUCLEOTIDYLTRANSFERASE ADENYLYLTRANSFERASE ADENYLATE KINASE LARGE SAT) protein domain (PD007412) which is seen in Q82L79_STRAW.","","-63% similar to PDB:1ZUN Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae (E_value = 6.6E_96);-46% similar to PDB:1JNY Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in complex with GDP (E_value = 9.1E_45);-46% similar to PDB:1SKQ The crystal structure of Sulfolobus solfataricus elongation factor 1-alpha in complex with magnesium and GDP (E_value = 9.1E_45);-47% similar to PDB:1F60 CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA (E_value = 1.0E_32);-47% similar to PDB:1G7C YEAST EEF1A:EEF1BA IN COMPLEX WITH GDPNP (E_value = 1.0E_32);","Residues 21 to 232 (E_value = 1.8e-64) place ANA_1242 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain.Residues 259 to 324 (E_value = 7.5e-09) place ANA_1242 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2.","","adenylyltransferase subunit 1","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1244","1326410","1327201","792","5.64","-6.39","27281","ATGACGCACGACGTCTCTCCCCATGGACCCGACGGTTCCGCGGATGGCTGGGTGGCGCTGGTGGGCGGCGGCCCGGGCAGCAGCGGCCTCATCACCGCCCGAGGCCTGGAGCTACTGGGCCGGGCGGACGTGGTCGTCGTCGACGCGCTGGCGCCCCGAGACCTCCTGGAGGACCTTGACCCCAGCACGGAGGTCATCGACGCCTCCAAGCGTCGCGGCCGACACGTCATGAGTCAGGAGGAGATCGACACGCTCCTGGTCGACCTGGCCCGCCGCGGCAAGGGGGTGGTCCGTCTCAAGGGCGGCGACCCCTACGTGCTCGGACGCGGCGGGGAGGAGGCGGCCGCCTGCCGTGCAGCCGACGTGGCCGTCGAGGTCGTCCCGGGGATCACCAGCGCCATCGCCGTGCCCGCGGCGGCGGGGATCCCCGTCACCCACCGGGGGCTGTCGCGCGGCTTCTCGGTCATCACGGCTCATGCGGATCTGGGGGTGCTCCCCCAGCGCCGCGACCACACCCTCATCCTGCTCATGGGGGTCTCCCGGCTGCGGGACTCGGTCGCCTCCCTGCTGGAGGCCGGCAGCGATCCAGCCACACCGGCGGCGATCATCGAGCGCGGCTACCACCCCGACCAGCGCGTGACCACCACCGAGCTGCGATGTCTGGCCGACGTCGCCGCCCGGTACGGCGTGACCGCCCCCGCGGTCATCGTCATCGGCGACGTCGTCACCCTGAGCCCGTACTGGGCTGACCGAGTCGTCGAGGAGGCCCGGCCGGCGAGTCCCGCCGCGTGA","MTHDVSPHGPDGSADGWVALVGGGPGSSGLITARGLELLGRADVVVVDALAPRDLLEDLDPSTEVIDASKRRGRHVMSQEEIDTLLVDLARRGKGVVRLKGGDPYVLGRGGEEAAACRAADVAVEVVPGITSAIAVPAAAGIPVTHRGLSRGFSVITAHADLGVLPQRRDHTLILLMGVSRLRDSVASLLEAGSDPATPAAIIERGYHPDQRVTTTELRCLADVAARYGVTAPAVIVIGDVVTLSPYWADRVVEEARPASPAA$","Uroporphyrin-III C-methyltransferase","Cytoplasm","uroporphyrin-III C-methyltransferase","uroporphyrin-III C-methyltransferase ","uroporphyrin-III C-methyltransferase","","Raux E., Schubert H.L., Warren M.J. Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum. Cell. Mol. Life Sci. 2000. 57(13):1880-1893. PMID: 11215515","","","

InterPro
IPR000878
Domain

Tetrapyrrole methylase
PF00590	$\"[17-222]T$	TP_methylase

InterPro
IPR006366
Domain

Uroporphyrin-III C-methyltransferase, C-terminal
TIGR01469	$\"[16-246]T$	cobA_cysG_Cterm: uroporphyrin-III C-methylt

InterPro
IPR014776
Domain

Tetrapyrrole methylase, subdomain 2
G3DSA:3.30.950.10	$\"[131-244]T$	no description

InterPro
IPR014777
Domain

Tetrapyrrole methylase, subdomain 1
G3DSA:3.40.1010.10	$\"[2-130]T$	no description

noIPR
unintegrated

unintegrated
PTHR21091	$\"[70-257]T$	METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
PTHR21091:SF16	$\"[70-257]T$	UROPORPHYRIN-III METHYLTRANSFERASE

","BeTs to 17 clades of COG0007COG name: Uroporphyrinogen-III methylaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0007 is aomp-zyq-dr-bcefg-sn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB003043 (Uroporphiryn-III C-methyltransferase) with a combined E-value of 4.9e-44. IPB003043A 18-48 IPB003043B 93-132 IPB003043C 197-218","Residues 18-242 are 62% similar to a (METHYLTRANSFERASE TRANSFERASE METHYLASE UROPORPHYRIN-III C-METHYLTRANSFERASE III SYNTHASE BIOSYNTHESIS UROPORPHYRINOGEN SIROHEME) protein domain (PD001478) which is seen in Q9L1C9_STRCO.","","-45% similar to PDB:1S4D Crystal Structure Analysis of the S-adenosyl-L-methionine dependent uroporphyrinogen-III C-methyltransferase SUMT (E_value = 3.0E_25);-46% similar to PDB:1PJQ Structure and function of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis (E_value = 5.7E_24);-46% similar to PDB:1PJS The co-crystal structure of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis, in complex with it NAD cofactor (E_value = 5.7E_24);-46% similar to PDB:1PJT The structure of the Ser128Ala point-mutant variant of CysG, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis (E_value = 5.7E_24);-43% similar to PDB:1V9A Crystal structure of Uroporphyrin-III C-methyl transferase from Thermus thermophilus complexed with S-adenyl homocysteine (E_value = 3.2E_19);","Residues 17 to 222 (E_value = 7.6e-64) place ANA_1244 in the TP_methylase family which is described as Tetrapyrrole (Corrin/Porphyrin) Methylases.","","C-methyltransferase (cobA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1245","1327244","1328287","1044","10.09","5.87","34893","ATGCGCAAGCTTGTTCTTCTCGCCCTCGTCGGCCTGGCCGCCCAGCTGGTCGACGGATCCCTCGGGATGGGGTACGGCATGACCTCCTCCTCCCTGCTGCTTCTGGCCGGGCTGAGCCCGGCACTGGCCTCGGCCTCCGTGCACCTGGCCGAGATCGGCACGACCCTGGCCTCGGGGGCCTCCCACTGGAGGCTGGGCAACACCGATCCTCGCCTGGTGGTCCGGCTGGGGCTGCCCGGTGCGGTGGGGGCCTTCAGCGGCGCCGCGGTTCTGTCTCACCTGTCGACCCGCGCGGCGACCCCGGTGACGGCGAGCCTGCTGATACTGCTGGGGACCTATGTCCTGGGGCGCTTCGCACTGCGCCCGCCCAGCGGATCCGGTAGCCGGCGCTCGCCGCACGGCAGGCGGCTCCTGGTTCCCCTGGGACTGGTGGGCGGTTTCGTTGACGCCACCGGTGGTGGCGGCTGGGGGCCGGTCGTGACGACGACACTGCTCACGGGTGGTCGCACAGCGCCGCGCACCGTGGTCGGCTCGGTGGGGGCCTCGGAGTTCCTGGTGACGGTGGCGGCCTCAGCCGGATTCCTCACCGGACTGGGCACCGCGGGCATCAGCCTCGGGATCGTCCTGACCCTGCTGGCCGGCGGGCTCGTGGCCGCACCGATCTCCGCCTGGCTGGTCTCCCGCCTGCCCGGAGCGGTGCTGGGCACCGCCGTCGGCGGGCTGATCCTGGCCACGAACCTGCGGGTGCTACTGTCCTGGGCCGAGGCCTCGGCTCAAACTGGGGTCGTGTTGTACAGCGCGCTCGGGGTGATCTGGGCGGCCTTCCTGATCCTGGCGGTCCGCAAGGCACGCGCCGCTGCCACAGAGATTCGAGAGGAGACAGAGCAGGTGCTTGAGGAGGTCCACGCCGATCCTCCACGCGGCCACGAACCTGAGGCTACTGTCCTGGAGGAGGCGATCGCCGCCGGAGGTCCCGTCACCCCGAGGCCGGTCGAGCCGACTCGTCCTCACACGCACGCGGTTCTGGTGGTGGAGCCGGCATGA","MRKLVLLALVGLAAQLVDGSLGMGYGMTSSSLLLLAGLSPALASASVHLAEIGTTLASGASHWRLGNTDPRLVVRLGLPGAVGAFSGAAVLSHLSTRAATPVTASLLILLGTYVLGRFALRPPSGSGSRRSPHGRRLLVPLGLVGGFVDATGGGGWGPVVTTTLLTGGRTAPRTVVGSVGASEFLVTVAASAGFLTGLGTAGISLGIVLTLLAGGLVAAPISAWLVSRLPGAVLGTAVGGLILATNLRVLLSWAEASAQTGVVLYSALGVIWAAFLILAVRKARAAATEIREETEQVLEEVHADPPRGHEPEATVLEEAIAAGGPVTPRPVEPTRPHTHAVLVVEPA$","Permease","Membrane, Extracellular","Predicted permeases","hypothetical protein","protein of unknown function DUF81","","","","","

InterPro
IPR002781
Family

Protein of unknown function DUF81
PF01925	$\"[5-250]T$	DUF81

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[31-51]?$ $\"[72-92]?$ $\"[98-116]?$ $\"[137-157]?$ $\"[203-225]?$ $\"[234-254]?$ $\"[260-280]?$	transmembrane_regions

","BeTs to 4 clades of COG0730COG name: Predicted permeasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0730 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 18-96 are 78% similar to a (MEMBRANE PROTEIN TRANSMEMBRANE PERMEASE PREDICTED INTEGRAL PLASMID SPANNING PROBABLE PRECURSOR) protein domain (PD001246) which is seen in Q8NLX4_CORGL.","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 250 (E_value = 4.8e-07) place ANA_1245 in the DUF81 family which is described as Domain of unknown function DUF81.","","permeases ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1246","1328284","1328970","687","7.84","2.37","24028","ATGAGCACTCGTCCCCTGGTGCTGCTGGCCCACGGCTCGCGCCGGCCCGGGCCGTCCTCGGTCCTGTCGCGTACCGCTGAGCGCGTCGGCACGATCCTGCCGGGGGTGGAGGTGCGCACCGGCTACGTCGAGCTCCAGTCCCCGGACCCGGCCACGGCCCTGGAGGGGCTGGTGGATCCGGTGGTGCTGCCCTTCTTCCTGGCCCGCGGCTATCACGTCGTCCATGACGTACCGGCCGCAGTGGAACGACACGGGTCGGGGACGGTCACCGGGCACCTGGGGGTCGAGGAGCACTTGGTGGAGGCCGTCGCGCAGCGGCTCCGGGAGGCGTCCGCGCCTCTGGGCGGGCTGGCAAGACTCGACCACATCGTCCTGGGCGCGGCCGGGTCGCGCCAGGCGGTGGCGCTGGAGGAGGTTGAGACCATCACTCGCCTGCTCGAGGCGCGTCTGGGGCGCGAGGTGACGCCCGCCTACCTCTCGGCTGCGCGTCCCAGTGTCAGTGACGCGGTGAGCACGGCCCGGGCCCGGGGTGCCAGGCGGGTGGGCGTGGCCACCTACCTACTGGCGGAGGGGCGTTTCCACCGGGCCCTGCACTCCACGGGCGCCGACGTCGTGGCCGCCCCCATCGGCGACCACCCGGCGCTCGCCGAGCTGGTGGCCCTCCGCTACCGGGAACAGGTCGCCTAA","MSTRPLVLLAHGSRRPGPSSVLSRTAERVGTILPGVEVRTGYVELQSPDPATALEGLVDPVVLPFFLARGYHVVHDVPAAVERHGSGTVTGHLGVEEHLVEAVAQRLREASAPLGGLARLDHIVLGAAGSRQAVALEEVETITRLLEARLGREVTPAYLSAARPSVSDAVSTARARGARRVGVATYLLAEGRFHRALHSTGADVVAAPIGDHPALAELVALRYREQVA$","Cobalamin (vitamin B12) biosynthesis CbiX protein","Cytoplasm","chalcone/stilbene synthase family protein","hypothetical protein","cobalamin (vitamin B12) biosynthesis CbiX protein","","Rodionov D.A., Vitreschak A.G., Mironov A.A., Gelfand M.S. Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes. J. Biol. Chem. 2003. 278(42):41148-41159. PMID: 12869542","","","

InterPro
IPR002762
Domain

Cobalamin (vitamin B12) biosynthesis CbiX
PF01903	$\"[11-105]T$ $\"[128-221]T$	CbiX

InterPro
IPR014423
Family

Cobaltochelatase/ferrochelatase CbiX/SirB
PIRSF004877	$\"[3-228]T$	Cobaltochelatase/ferrochelatase CbiX/SirB

InterPro
IPR014696
Family

Cobaltochelatase/ferrochelatase, CbiX/SirB long form
PIRSF500174	$\"[3-228]T$	Cobaltochelatase/ferrochelatase, CbiX/SirB long form

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1400	$\"[2-120]T$	no description

","BeTs to 8 clades of COG2138COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2138 is aom------dr-bc------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","Residues 123-228 are 54% similar to a (BIOSYNTHESIS SIROHYDROCHLORIN LYASE COBALAMIN METAL-BINDING COBALTOCHELATASE COBALT CBIXS CBIX MA3471) protein domain (PD047021) which is seen in Q9L2E8_STRCO.Residues 121-224 are 57% similar to a (SYNTHASE SECRETED CHALCONE/STILBENE FAMILY MB0265C CBIX PLASMID) protein domain (PD038876) which is seen in Q73TL3_MYCPA.Residues 123-228 are 54% similar to a (BIOSYNTHESIS SIROHYDROCHLORIN LYASE COBALAMIN METAL-BINDING COBALTOCHELATASE COBALT CBIXS CBIX MA3471) protein domain (PD047021) which is seen in Q9L2E8_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 105 (E_value = 1.7e-18) place ANA_1246 in the CbiX family which is described as CbiX.Residues 128 to 221 (E_value = 8.2e-13) place ANA_1246 in the CbiX family which is described as CbiX.","","synthase family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1247","1329878","1329075","804","5.33","-6.31","28536","ATGACCGCCAGGAGCTCTGCCCGTGGGCCGAACAGTGACAGTGATGACTCCGGGGCCTCCGCCTCTGATGACATCAGGGAGGCGACGCGCGCCCTCAATGAGGCGATCACCGCCTTCTCCCGTGCGGTGGGAGCGGCCGGTCAGGGAGCGCGCCGGAGCAGCGAGAGTGCGATAGCGGCCTCCCTGGACCTCGCCTCCCGGAAGCTGGCCTCCGCCTCCACTGCAGTCAGCGGCGCCGCCCCGGGTCGGCGCGGCGGGCGCCGTCGGAGCGAGGAGACCAGGGCGCGGATTCTTGCTGCTGCCAGGGAGGTCTTCGCTGCCAAGGGCTACGAGGGGGCGTCGGTCAGTGACATCGCCTCGGCGGCCGGATTCACCAAGGGCGCCTTCTACTCCTCCTTCCCCTCCAAGGAGGCCCTGTTCCTGGAGGTCGTCACCTGTGGTGAGGAGAGCTCGGATGAGGCCGCTCGGGAGATGGCGAGCCCCGAGCAGTGGGGCGAGCAGCTCCAGGAGCTTCCCATGGAGGATGTTGTCCTGCACCTGGAGACCTGGCTCTACGCGATTCGTCATGAGGACTCCCGGGACCGGCTGGCCGGCAGTTGGCGCCGCTGGCTGAGAGAGACCTCCCTCCTGGTGGCCCGTTCCCATGGACGCCGTGAGCCGAGCCAGCAGGATGAGGAGACGGCCTTCGGACTTCTGGCGGTGGGCATCTTCGGCCGCGTGAGCGCCGCAGCCACCACCTCGCAAGAGGTCGAACCCATCATCCAGCGCCTGTCCGAGCGGCTCCTTGAGGACGGTGGCAACTGA","MTARSSARGPNSDSDDSGASASDDIREATRALNEAITAFSRAVGAAGQGARRSSESAIAASLDLASRKLASASTAVSGAAPGRRGGRRRSEETRARILAAAREVFAAKGYEGASVSDIASAAGFTKGAFYSSFPSKEALFLEVVTCGEESSDEAAREMASPEQWGEQLQELPMEDVVLHLETWLYAIRHEDSRDRLAGSWRRWLRETSLLVARSHGRREPSQQDEETAFGLLAVGIFGRVSAAATTSQEVEPIIQRLSERLLEDGGN$","Transcriptional regulator, TetR family","Cytoplasm, Periplasm","transcriptional regulator, TetR family domainprotein","transcriptional regulator; TetR family protein","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[97-110]T$ $\"[118-141]T$	HTHTETR
PF00440	$\"[97-143]T$	TetR_N
PS50977	$\"[91-151]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[75-143]T$	no description

","BeTs to 14 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 5.9e-21. IPB001647 97-139***** IPB013573 (Tetracycline transcriptional regulator YcdC-like, C-terminal) with a combined E-value of 2.5e-16. IPB013573A 75-117 IPB013573B 118-159***** IPB013571 (Tetracycline transcriptional regulator QacR-related, C-terminal) with a combined E-value of 7.7e-08. IPB013571A 91-141***** IPB013572 (Tetracycline transcriptional repressor MAATS-type, C-terminal) with a combined E-value of 1.2e-07. IPB013572A 82-102 IPB013572B 118-140","Residues 97-144 are similar to a (TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL FAMILY REGULATOR TETR REGULATOR TETR-FAMILY REGULATORY) protein domain (PD000384) which is seen in Q9JN89_STRCO.","","No significant hits to the PDB database (E-value < E-10).","Residues 97 to 143 (E_value = 6.2e-21) place ANA_1247 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator, TetR family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1248","1330794","1329985","810","8.04","1.60","28741","ATGCCTGCTCCAACCAGTGCCACTGCTGAAGCGGCCCCGGCCAGTGAGACTGTTCTTGAGGTCGCGTCCCAGAAGACTTCGCTCTGGCGTCAGCTCGGCCTGCTCATCCAGTGGCAGTTCCGTCGCAGCCTGCCCGTGCTTCCTCTCTTCATCATCGTCCAGACGCTGCTGTCCGTCTCCATGGTCCTGGGATACGGGCTCATTGCGGGCCACCCAGGCCGCGAGGCGAGTCTCTACCTGGCCGGCGGCGGCCCGGCGATCGCGCTCATCTCGCTGGGACTCATCATGACGCCTCAGTGGGTCTCCCAGTCCCGCACTGAGGGCAGCCTGGACTGGATGCGCACCCTGCCCGTCCCCAGGGTCGCCTTCCTCCTGGCAGACCTCGCGATCTGGACCGCTCTCGCACTGCCCGGCCTGGTTGTGGGCGTCCTCGTGGCCAACGTCCGCTTCGACGTCGACCTCGCCCCGCAGTGGTGGCTGGTGCCCGGCGCCGTACTGGTCGCTCTGACAGCGGCCTGCATCGGATACGCCATCGCCACGCTCCTGGCTCCGGCCCTGGCTCAGATCCTCTCCCAGGTACTTGCTTTCGGCATCATGCTGTTCTCGCCCGTCAGCTTCCCCGCCGACAGGCTCCCCGACTGGGCCCAGGAGATCCACCGCTGGTTGCCCTTCGAGCCCATGGCTCAGGTGGTGCGTGCGGGACTGTTCTCCCACGACGCCGCCATGCCCGCCCGTTCCTGGGGCCTCCTGGGCGGATGGTGCCTGGTGGCCGTCGCCGGAGCGTCATGGGCCCTGGGAAGGCGGCCCTGA","MPAPTSATAEAAPASETVLEVASQKTSLWRQLGLLIQWQFRRSLPVLPLFIIVQTLLSVSMVLGYGLIAGHPGREASLYLAGGGPAIALISLGLIMTPQWVSQSRTEGSLDWMRTLPVPRVAFLLADLAIWTALALPGLVVGVLVANVRFDVDLAPQWWLVPGAVLVALTAACIGYAIATLLAPALAQILSQVLAFGIMLFSPVSFPADRLPDWAQEIHRWLPFEPMAQVVRAGLFSHDAAMPARSWGLLGGWCLVAVAGASWALGRRP$","ABC-type multidrug transport system, permease component","Membrane, Cytoplasm","membrane protein, putative","K01992 ABC-2 type transport system permease protein","ABC-2 type transporter","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[30-236]T$	ABC2_membrane

noIPR
unintegrated

unintegrated
tmhmm	$\"[46-68]?$ $\"[82-102]?$ $\"[123-145]?$ $\"[159-179]?$ $\"[184-204]?$ $\"[246-266]?$	transmembrane_regions

","BeTs to 6 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 10","No significant hits to the Blocks database.","Residues 75-233 are similar to a (MEMBRANE PROTEIN) protein domain (PD823314) which is seen in Q835P4_ENTFA.","","No significant hits to the PDB database (E-value < E-10).","Residues 30 to 236 (E_value = 7.2e-05) place ANA_1248 in the ABC2_membrane family which is described as ABC-2 type transporter.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1250","1331866","1330913","954","6.81","-1.19","33554","ATGGCCGACGTACTCGCCATTGAGGACCTTCACAAGCACTTCGGAAGCGGGGCGCACACGGTGAGAGCCAACGCCGGTGTCACCATGCGGGTGGGTGCCGGTGAGGTGGTCGGGCTCCTTGGGCACAACGGCGCGGGCAAGACCACGCTGGTCAACCAGGTGGTGGGGCTCTTGCGCCCGACCTCCGGGAGCATCAGGCTCGAAGGTGTCGACGCCGTCGCCAACCCCGCTCTCGCCCGCCGCCTCACCAATGTCCAGGCACAGGCCAACGTTCCCATCACGGGACTGACGCCCTTGACGGCAATCGACCTCGTGGGGCGCATGCGAGGAGGGCGCCCGCGTCAGACACGCAGACGCGCCGAGGAGCTCATCGAGGCTCTCGACCTAGGGGAGTGGGCGAGGACTCCCGCGCAGAAGATCTCCGGAGGTGTTGCCCGTCTGACTGCCTTCGCCATGTGCGCCGTCATCCCCGGGCGCCTGGTCATCCTCGATGAGCCCACCAACGACGTCGACCCGGTGCGCCGGCGCCTGCTGTGGGACCAGATCCGTCTTCTGGCCGAGGCCGGCGCGGCGGTCCTCCTGGTGACCCACAACGTACGGGAGGCCGAGCGGGCGGTCGACCGGCTCACCATTCTGGACCACGGCCACGTCATCGCCGAGGGGACCCCTGCGGCACTCGTGGCCGGCCACGGATCCTCCTTCGTCCTGGAGATCAGCCGGGCCCCCGGGCAGCGGATCGAGCCGCCCGCTGGAATGAGCCTGACGCAGCACGACGCCGTGCGAGCATCCGTGGCGGTGGACTCTCACTGTGCGACCCAGGCCGTGGAGTGGGCCGCTCATGCCCTCAAGGACGGAGTGATCGAGCGCTACGAGCTGGCACCGATCTCACTGGAGGACGTCTACGTGGACCTGACTGGGAGTACCGGCGAGGAGGTGAGCCGTCATGCCGCCTGA","MADVLAIEDLHKHFGSGAHTVRANAGVTMRVGAGEVVGLLGHNGAGKTTLVNQVVGLLRPTSGSIRLEGVDAVANPALARRLTNVQAQANVPITGLTPLTAIDLVGRMRGGRPRQTRRRAEELIEALDLGEWARTPAQKISGGVARLTAFAMCAVIPGRLVILDEPTNDVDPVRRRLLWDQIRLLAEAGAAVLLVTHNVREAERAVDRLTILDHGHVIAEGTPAALVAGHGSSFVLEISRAPGQRIEPPAGMSLTQHDAVRASVAVDSHCATQAVEWAAHALKDGVIERYELAPISLEDVYVDLTGSTGEEVSRHAA$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Membrane","CalT5","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[140-179]T$	Q835P5_ENTFA_Q835P5;
PF00005	$\"[34-215]T$	ABC_tran
PS50893	$\"[5-239]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[33-216]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-230]T$	no description
PTHR19222	$\"[5-229]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 16 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.9e-17. IPB013563A 23-57 IPB013563C 137-164 IPB013563D 191-243***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.4e-16. IPB005074C 23-70 IPB005074D 128-171***** IPB005116 (TOBE domain) with a combined E-value of 4.6e-09. IPB005116A 41-57 IPB005116D 160-179 IPB005116E 193-206","Residues 1-69 are 60% similar to a (COBALT ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PDA0I1O9) which is seen in Q7NNW9_GLOVI.Residues 3-65 are 65% similar to a (ATP-BINDING NATA ABC TRANSPORTER) protein domain (PD742287) which is seen in O83851_TREPA.Residues 4-212 are 47% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 5-223 are 46% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 12-69 are 67% similar to a (ATP-BINDING COMPONENT ATP-TRANSPORTER PLASMID) protein domain (PDA0J3M3) which is seen in Q6QW96_AZOBR.Residues 22-221 are 46% similar to a (ATP-BINDING LONG 268AA ABC TRANSPORTER) protein domain (PD528472) which is seen in Q96ZV5_SULTO.Residues 27-71 are 80% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q89G68_BRAJA.Residues 34-217 are 45% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 37-228 are 42% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD738128) which is seen in Q8G833_BIFLO.Residues 96-275 are 50% similar to a (ATP-BINDING NODULATION I MEMBRANE NOD EXPORT FACTOR) protein domain (PD082119) which is seen in NODI_AZOCA.Residues 140-179 are 82% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q835P5_ENTFA.","","-43% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 1.8E_17);-43% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 6.3E_15);-44% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 3.8E_12);-44% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 3.8E_12);-41% similar to PDB:1G6H CRYSTAL STRUCTURE OF THE ADP CONFORMATION OF MJ1267, AN ATP-BINDING CASSETTE OF AN ABC TRANSPORTER (E_value = 5.5E_11);","Residues 34 to 215 (E_value = 2.7e-34) place ANA_1250 in the ABC_tran family which is described as ABC transporter.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1252","1333819","1332080","1740","6.91","-0.34","62086","ATGTGGAAGCTGCTGACGCGAGTCGTCAACGCCGCCGAGATGCGCACCATCATCGCCTGGTTCGTAGCCTCCGCCGTCCTCCAGGGCCTCACCCTGGCCCTCATGATCCCCTTCCTGCGAGCCCTCTACTCCCGCTCGCAGTTCCTGACCGCCTGGCTGATCGCCGTCGTAGTCATGGCAGTGAGCGCCGCGCTCGTCGAGACCATCGCCATGCACCGCTCCTACCGGGTCAGTGTCTTCGAGGTCTGCGACACCATGATCGACCGCGTCGCCGATCACGTCCTGACCCTGCCGCTGGGCTGGTTCAGCGCCGAGCGGGAGGCCGCCGTCGTCAACGCCACCTCCAAGGAGGTCAACACCCTCTCCCACCTGGCCTCCATGGTGATCCCCAACCTGTGCAACGCCTTCATCGTCCCGCTGGTCATGCTCGGGGCCACCGCCGTCGTCGAATGGCCCCTGGCGCTCATCATGGCCGCCGCCATCGTCCCGCTGGTCCTGACGTGGCGGCTCATGGGCGCCGCGACCACTCGCGCCAACGAGATGGAGGACCGCACCTCGAGCGCCGCGGCCGGACGCCTCGTGGAGTTCGCCCGACTCCAGCCCGTGCTGCGCGCCACCGGTGCCACCAAGACGGGCTGGGCGCCGGTGCAAGCCGCCCTGGAGGCCGACTCCGCCTCCACCCTGGACGGCCTACGGGTCAAGGGCAGGCCCGGGCAGTACTTCAACCTTATCGTCAACGTCGCCTTCGCCCTGGTCATGGCGATGGGGCTGGCACGGGTCAGTGGGCACCGGCTCGACGTCGTCGCATACCTGGCGATCATGGCCGTCACCGCGCGCACGCTCCTGCCACTGACCAAGGCCGCCATGTACGGATCCGAGGCCGACAACGCGAAGGTCGCCCTGCGGGCCGTGGGGGATATTCTCGACGCGCGTCCCCTGTCCGACCCCGAGCCCGGTCAGGAGATCGAGCCTCGGGGGACCACGATCGCCCTGAACGACGTCTCCTTCTCCTACGACGCCGGCCGCCCCGTCCTGGCGGGCGTCTCCTTGAGCGCACCGCAGGGGAGAGTGACCGCCCTGGTGGGCCCGTCAGGGGCGGGCAAGTCCACGATCCTGCGCCTGGCGGCCCGGTTCTGGGACGTCGACGACGGGACCGTCACCATTGGCGGCGCACCGGTTCGCTCCATGCGCGCCTCGACGATCATGGGCATGACCTCCATGGTCTTCCAGGACGTCTACCTGTTCGACACCACGATCCGGGAGAACCTGCGCATCGCCCGGCCCGAGGCCACCGACGCCGAGCTGGCCGAGGCCGCCCGGCGCGCCCGCCTGGACCGCGTCATCGAGGCGCTGCCGCACGGGTGGGACACGCAGGTCGGTCCCGGCGGGCTGAGCCTGTCCGGTGGGGAGCGTCAGCGTGTCGCCATTGCCCGGGCCTTCGTCAAGGACGCCCCCATCCTGCTGCTCGACGAGATCACCTCGGCCCTGGACGGGGAGAACGAGTCCGCCATCACCGAGGTGGTGCGCGAGCTCTCCGAGGGGCGCACCGTCATCGTGGTGGCCCACCGCCTGTCCACCGTCCGCCAGGCCGACGAGGTCGTCTTCCTCGAGCCGACTCAGGCCGGCGCCCGTGTGGCCCAGCGCGGTACGCCCCAGGAGCTGGCTGCCGTCGCCGGCCCCTTCCGCGAGTTCATCGAGGCCTCCACGGCCTCCTCGCGCTGGCACATCCGTCAGGGGTGA","MWKLLTRVVNAAEMRTIIAWFVASAVLQGLTLALMIPFLRALYSRSQFLTAWLIAVVVMAVSAALVETIAMHRSYRVSVFEVCDTMIDRVADHVLTLPLGWFSAEREAAVVNATSKEVNTLSHLASMVIPNLCNAFIVPLVMLGATAVVEWPLALIMAAAIVPLVLTWRLMGAATTRANEMEDRTSSAAAGRLVEFARLQPVLRATGATKTGWAPVQAALEADSASTLDGLRVKGRPGQYFNLIVNVAFALVMAMGLARVSGHRLDVVAYLAIMAVTARTLLPLTKAAMYGSEADNAKVALRAVGDILDARPLSDPEPGQEIEPRGTTIALNDVSFSYDAGRPVLAGVSLSAPQGRVTALVGPSGAGKSTILRLAARFWDVDDGTVTIGGAPVRSMRASTIMGMTSMVFQDVYLFDTTIRENLRIARPEATDAELAEAARRARLDRVIEALPHGWDTQVGPGGLSLSGGERQRVAIARAFVKDAPILLLDEITSALDGENESAITEVVRELSEGRTVIVVAHRLSTVRQADEVVFLEPTQAGARVAQRGTPQELAAVAGPFREFIEASTASSRWHIRQG$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","transporter","K06147 ATP-binding cassette; subfamily B; bacterial","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR000276
Family

Rhodopsin-like GPCR superfamily
PS00237	$\"[61-77]?$	G_PROTEIN_RECEP_F1_1

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[467-508]T$	Q89RL0_BRAJA_Q89RL0;
PF00005	$\"[355-539]T$	ABC_tran
PS50893	$\"[329-567]T$	ABC_TRANSPORTER_2
PS00211	$\"[466-480]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[354-571]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[17-296]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[313-565]T$	no description
PTHR19242	$\"[5-574]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF92	$\"[5-574]T$	HLYB/MSBA FAMILY ABC TRANSPORTER
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[20-40]?$ $\"[46-66]?$ $\"[128-148]?$ $\"[154-172]?$ $\"[240-258]?$	transmembrane_regions

","BeTs to 19 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 13","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.3e-49. IPB005074C 344-391 IPB005074D 454-497 IPB005074E 516-536***** IPB005116 (TOBE domain) with a combined E-value of 3.8e-20. IPB005116A 362-378 IPB005116C 466-479 IPB005116D 486-505***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 4.9e-19. IPB013563A 344-378 IPB013563C 463-490***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.4e-18. IPB010509B 355-380 IPB010509D 461-505***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.7e-10. IPB010929K 342-386 IPB010929M 463-509 IPB010929A 354-373","Residues 89-260 are 47% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER MULTIDRUG ATP-BINDING/PERMEASE TRANSMEMBRANE RESISTANCE PERMEASE MEMBRANE) protein domain (PD087348) which is seen in Q9ZB57_PROMI.Residues 94-423 are 40% similar to a (LANTIBIOTIC MEMBRANE SYSTEM ABC-TRANSPORT ATP-BINDING) protein domain (PDA0J3N6) which is seen in Q6NIL4_CORDI.Residues 136-534 are 41% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 173-309 are 51% similar to a (ATP-BINDING ABC TRANSPORTER PROBABLE COMPONENT PROTEIN PERMEASE/ATP-BINDING RV1349/MT1392/MB1384 TRANSMEMBRANE TRANSPORTER) protein domain (PD307473) which is seen in Q9EWN7_STRCO.Residues 194-536 are 41% similar to a (LANTIBIOTIC SYSTEM MERSACIDIN TRANSPORTER) protein domain (PDA0G5T2) which is seen in Q7UG09_RHOBA.Residues 264-423 are 48% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I309) which is seen in Q9AM85_RIEAN.Residues 269-425 are 46% similar to a (ATP-BINDING/PERMEASE FUSION ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I2L4) which is seen in Q7NX92_CHRVO.Residues 324-421 are 56% similar to a (TRANSPORTER ABC EXPORT) protein domain (PDA18411) which is seen in Q7P4Z0_BBBBB.Residues 329-558 are 44% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 341-545 are 49% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 344-537 are 45% similar to a (ATP-BINDING ABC PROTEIN TRANSPORTER) protein domain (PD995669) which is seen in Q73R06_TREDE.Residues 345-396 are 76% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q7NNT7_GLOVI.Residues 355-536 are 45% similar to a (ATP-BINDING SECRETION PROBABLE ABC TOXIN TRANSPORTER) protein domain (PDA0C7R3) which is seen in Q7UXT8_RHOBA.Residues 398-463 are 68% similar to a (ATP-BINDING TRANSPORTER ABC) protein domain (PDA1B4P3) which is seen in Q9EWN7_STRCO.Residues 414-537 are 54% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I0J1) which is seen in Q83A70_COXBU.Residues 451-528 are 60% similar to a (ATP-BINDING) protein domain (PD991504) which is seen in Q7SCP7_NEUCR.Residues 451-523 are 72% similar to a (ATP-BINDING TRANSPORTER ABC RESISTANCE TRANSMEMBRANE SIMILAR MULTIGENE POLYMORPHISM FAMILY GLYCOPROTEIN) protein domain (PD250423) which is seen in Y742_STRCO.Residues 451-523 are similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PDA0I0J5) which is seen in Q7P0D6_CHRVO.Residues 451-523 are 67% similar to a (ATP-BINDING LIN1097 LMO1131) protein domain (PD932075) which is seen in Q8Y7Y8_LISMO.Residues 465-522 are 71% similar to a (ATP-BINDING TRANSPORTER IRONIII ABC) protein domain (PD431760) which is seen in Q9WXT3_THEMA.Residues 467-508 are 88% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q89RL0_BRAJA.","","-58% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 7.1E_45);-58% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 7.1E_45);-56% similar to PDB:2GHI Crystal Structure of Plasmodium yoelii Multidrug Resistance Protein 2 (E_value = 1.4E_40);-53% similar to PDB:1MV5 Crystal structure of LmrA ATP-binding domain (E_value = 6.0E_36);-56% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 8.7E_35);","Residues 345 to 545 (E_value = 1.5e-07) place ANA_1252 in the SMC_N family which is described as RecF/RecN/SMC N terminal domain.Residues 355 to 539 (E_value = 2e-55) place ANA_1252 in the ABC_tran family which is described as ABC transporter.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1253","1335669","1333822","1848","5.94","-11.71","65431","ATGCCTAAGCAATCGATGCACCGGACGAGTCACCAGGAGGACGCAGGCGTCACCGTCGGCGAGCTCATCCGACCGGCGCGACCGGCCATGATCGCGACTGGGCTGCTGACCACCCTCGGAGCGCTGCTGTACATCGTCCCCTTCGAGGCCATGCGCAACCTGGCAGCCATCTGGCTGGGCGAGACCTCACCGCAGGGCTGGCGCGGCAGCCCGTGGACCTGGGCGGCCATCGCCGTCGGAGCGCTCTTCGCCTCCCAGGCCCTCTACCTGGCGGGCCTGGGGATCACACACCTGGCCGAGGCCCGGCTGCGCCACCACCTGCGCAGACAAGTCATCGAGGCCATCAGCGGCCTGCCCCTGGGGCGGGTCGCGCAGATCCCGCACGGCACCATCCGCAAGATGGTCTGCGACGACACCACCTCCATCCACACCCTCGTCGCCCACGTCCCCGGGGACGCCACCAACGCCGTCGTCATGGCGGCGGCGGGGACGGCCTACCTGCTGTGGGCCGACTGGCGCCTGGCCTGCGCGCTGGTGGGGCTGTGGGTCCTCGCCCTGGGAGCGATGCTCCTGACCATGTCTGGCCTGTCGGGCATCACCGAGCGCTTCGGCGCCGCTCAGACCGCGCTGGCCGCCGCGACCGTCGAGATGCTCGAGGGCATCAAGGAGATCAAGGGCTTCCAGGCCACCGACGCCTCCCGCACCCGCTTCAGCCAGGCGCGCGCCGAGTTCTCCAGCCTGTCCTACGAGTGGGTGAGCAGGTCCGGGAAGGCCATCAGCGCCATGACCGCCGTCCTGCGTCCCTCCACGGTCTTCGCCACGGTCGCGCTCCTGGCCGTCCTCTTCACCTCCCAGGGCTGGACGCCCCTGTCGGCCACCCTGCCGTTCTTCCTGGTGGCCCTCGGGCTGCCGGAGGGACTCATGACCCTCATCGGCCTCATGCAGCACATGTACGAGTCCAGGATGGCCGCCCAGGCCACCGCGGACCTGCTCTCCCTGCCACCGATGCCCGAGGGAACCCATGACGAGGGCGAGGGACTTGCGCCCGGGCGCGTCGACGTCGAGGACGTCACCTTCTCCTACGAGGCCGGCTCCCCGGTCCTGCACGGCGCCTCCTTCACCGCCGAGCCCGGAACCGTGACAGCGCTCGTCGGCCCCTCCGGCGGGGGCAAGTCGACCCTGGCCCGCCTCATCGCCCGCTTCTACGACGTCGACGACGGAGCCGTGCGCATCAGCGGCGTCGACGTGCGTGAGGCGACGTTCCCCTGGCTGCTCTCGCGCGTGGCGGTCGTGCTGCAGGACGTGGCCCTGGCCCACGAGTCCGTCCACGACAACATCGCCCTGGGACGCCCCGACGCCACCCGGGAACAGGTCGAGGCAGCTGCCCGCGCGGCCTGCATCCACGAGCGCATCGCACGTCTGCCCCATGGCTACGACACGATCCTGGGTGAGGAAGGCGGGTTCCTCTCCGGAGGGGAGCGCCAGCGCGTCACCCTGGCGCGCGCCTACCTCCAGGACGCCCCCATCCTCGTCCTGGACGAGGCCACCGCCCAGGCCGACCCGGCCTCCGAGCGCGACATCCACCAGGCCCTGTCCCGGCTCGCCGCCGGGCGGACCGTCATCATCATCGCCCACCGCCTGTCCACGATCCGCGACGCAGACCAGATCCTCGTCGTCGACGCCGGACGCATCACCGAGCGCGGCACGCACGACGAGCTGTTGGCCGCCGGCGGACGCTATGCCGCCATGTGGCGCAGTCAGGACCTGAGTGAGGAGACCGACGCCGCCGCACTGACCGCCCAGGGCGACCGACTGGGAGCCGAATCCGCCGGGCAGGAGGAGAAGTAA","MPKQSMHRTSHQEDAGVTVGELIRPARPAMIATGLLTTLGALLYIVPFEAMRNLAAIWLGETSPQGWRGSPWTWAAIAVGALFASQALYLAGLGITHLAEARLRHHLRRQVIEAISGLPLGRVAQIPHGTIRKMVCDDTTSIHTLVAHVPGDATNAVVMAAAGTAYLLWADWRLACALVGLWVLALGAMLLTMSGLSGITERFGAAQTALAAATVEMLEGIKEIKGFQATDASRTRFSQARAEFSSLSYEWVSRSGKAISAMTAVLRPSTVFATVALLAVLFTSQGWTPLSATLPFFLVALGLPEGLMTLIGLMQHMYESRMAAQATADLLSLPPMPEGTHDEGEGLAPGRVDVEDVTFSYEAGSPVLHGASFTAEPGTVTALVGPSGGGKSTLARLIARFYDVDDGAVRISGVDVREATFPWLLSRVAVVLQDVALAHESVHDNIALGRPDATREQVEAAARAACIHERIARLPHGYDTILGEEGGFLSGGERQRVTLARAYLQDAPILVLDEATAQADPASERDIHQALSRLAAGRTVIIIAHRLSTIRDADQILVVDAGRITERGTHDELLAAGGRYAAMWRSQDLSEETDAAALTAQGDRLGAESAGQEEK$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","ABC transporter, permease/ATP-binding protein","K06147 ATP-binding cassette; subfamily B; bacterial","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[75-244]T$	ABC_membrane

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[494-531]T$	Q7MVA1_PORGI_Q7MVA1;
PF00005	$\"[378-562]T$	ABC_tran
PS50893	$\"[352-586]T$	ABC_TRANSPORTER_2
PS00211	$\"[489-503]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[377-563]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[31-319]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[349-613]T$	no description
PTHR19242	$\"[21-592]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF92	$\"[21-592]T$	HLYB/MSBA FAMILY ABC TRANSPORTER
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[74-94]?$ $\"[174-194]?$ $\"[264-284]?$ $\"[294-314]?$	transmembrane_regions

","BeTs to 20 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 13","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 6.4e-54. IPB005074C 367-414 IPB005074D 477-520 IPB005074E 539-559***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3.9e-18. IPB013563A 367-401 IPB013563C 486-513***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1e-14. IPB010509B 378-403 IPB010509D 484-528***** IPB005116 (TOBE domain) with a combined E-value of 2.7e-12. IPB005116A 385-401 IPB005116C 489-502","Residues 76-449 are 39% similar to a (LANTIBIOTIC MEMBRANE SYSTEM ABC-TRANSPORT ATP-BINDING) protein domain (PDA0J3N6) which is seen in Q6NIL4_CORDI.Residues 266-580 are 43% similar to a (LANTIBIOTIC SYSTEM MERSACIDIN TRANSPORTER) protein domain (PDA0G5T2) which is seen in Q7UG09_RHOBA.Residues 276-467 are 46% similar to a (ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I309) which is seen in Q9AM85_RIEAN.Residues 307-464 are 46% similar to a (ATP-BINDING/PERMEASE FUSION ABC ATP-BINDING TRANSPORTER) protein domain (PDA0I2L4) which is seen in Q7NX92_CHRVO.Residues 339-559 are 44% similar to a (ATP-BINDING SECRETION PROBABLE ABC TOXIN TRANSPORTER) protein domain (PDA0C7R3) which is seen in Q7UXT8_RHOBA.Residues 352-444 are 65% similar to a (TRANSPORTER ABC EXPORT) protein domain (PDA18411) which is seen in Q7P4Z0_BBBBB.Residues 367-595 are 40% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 368-417 are 82% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q7NNT7_GLOVI.Residues 377-547 are 45% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 380-559 are 45% similar to a (COMPONENT TRANSPORTER ATP-BINDING ABC ATP BINDING) protein domain (PDA1D1M0) which is seen in Q7U9N7_SYNPX.Residues 423-480 are 68% similar to a (RESISTANCE ATP-BINDING MULTIDRUG P-GLYCOPROTEIN) protein domain (PDA1B2X6) which is seen in Q6YUU5_EEEEE.Residues 428-481 are 66% similar to a (ATP-BINDING TRANSPORTER ABC COMPONENT PROBABLE) protein domain (PD931592) which is seen in Q9HWG6_PSEAE.Residues 431-468 are 81% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER MULTIDRUG TRANSMEMBRANE RESISTANCE ATP-BINDING/PERMEASE P-GLYCOPROTEIN PERMEASE) protein domain (PD000101) which is seen in Q88JQ3_PSEPK.Residues 444-564 are 55% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I0J1) which is seen in Q83A70_COXBU.Residues 471-546 are 68% similar to a (ATP-BINDING MEMBRANE ABC TRANSPORTER) protein domain (PDA0I0J5) which is seen in Q7P0D6_CHRVO.Residues 473-573 are 56% similar to a (APRD ATP-BINDING) protein domain (PDA0I303) which is seen in Q89EV0_BRAJA.Residues 474-546 are 65% similar to a (ATP-BINDING TRANSPORTER ABC RESISTANCE TRANSMEMBRANE SIMILAR MULTIGENE POLYMORPHISM FAMILY GLYCOPROTEIN) protein domain (PD250423) which is seen in Q7N7D6_PHOLL.Residues 527-583 are 66% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD952632) which is seen in Q6A607_PROAC.Residues 538-610 are 56% similar to a (ABC-TRANSPORTER ATP-BINDING) protein domain (PD612243) which is seen in Q8RT51_PSEAE.Residues 543-584 are 85% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER MULTIDRUG TRANSMEMBRANE RESISTANCE ATP-BINDING/PERMEASE P-GLYCOPROTEIN MEMBRANE) protein domain (PD375591) which is seen in Q9F6W3_CHLAU.","","-52% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 3.2E_51);-52% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 3.2E_51);-61% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 2.1E_42);-61% similar to PDB:2FF7 The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state (E_value = 2.1E_42);-61% similar to PDB:2FFB The crystal structure of the HlyB-NBD E631Q mutant in complex with ADP (E_value = 4.6E_42);","Residues 75 to 244 (E_value = 1.3e-07) place ANA_1253 in the ABC_membrane family which is described as ABC transporter transmembrane region.Residues 378 to 562 (E_value = 2e-57) place ANA_1253 in the ABC_tran family which is described as ABC transporter.","","transporter, permease-ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1254","1338052","1335680","2373","6.28","-10.41","84605","GTGGAGCAGCCTCCGGAAGGGGTGGCAGAAGCGGCGCTGGTCAGCGTCGAGGGCCTGAGCGTCCACTACCTCGGACGCGAGAGCTGGGTCCTGGATGCCGTCGACCTGACCCACCTGCGCGCTCAGGTCACCGCCGTCATCGGTCCCTCGGGCTGCGGCAAGACCACCCTCGTGCGCGCGCTGTGCGGCCTCATCCCGCACTGCCTGCCCTCGGAATACGCCGGCAGCCTGAGACTGGCCGGCACCGAGGTCGCCGACGCCACCGTCCAGACCCTGGCCCAGACCGTCGCCTACGTCGGCCAGAGCCCCGATGCCGCCGTCGTCACCCGCACCGTCCACGACGATGTCGCCTTCCCGCTGCAGAACCTGTGCCTGGCCAGGTCGGAGATCACCGCGCGGGTCGAGCAGGCCCTGCGTGCGGTGGGACTCATCGAGCGCATCTGGGACGACCCCTGGACGCTCTCCGGCGGACAGCGTCAACGGCTCGCGCTCGCCGTCGCTTTGGCCATGCGCCCACAGCTCCTCGTGCTCGACGAGCCGACCAGCACCATCGATGCCACCGGCCGGGAGGAGTTCTACACCCTCATCTCCTCCCTGACCGCCTCCGGGACGGCGGTCGTCGTCATCGACCACGACCTCGACCCGGTACTGCCCATCGTCGACCAGGTCCTGGCCCTCAACGCCGACGGGCGGACCATCGCCGTCGGCTCGCCGCGTGAGGTCTTCATGAGCCACCGCCGCGAGCTGACCGACGCCGGAGTGTGGATGCCCCGAGCCCTGCGTGAGGCCGGCGACGACCTCCCCGCGGGGATGCAGGCCTCGGAGGCGGCGCTGACCTGCGCCGAGGCCGGAATCCGGGTGCCCCGGCTCGCCGACCTGTGCGCCGAGGGCGAGGTGCGCTACCTGGAGAAACAGGCGGCCGGCTCCGCTGAGAGCTGGCAGCAGGTCGAGGTCATCGACACCCGCGAGGTACTCGCCGGCCGCCCCCGGCCCGAGCCCAGAACCAGTGTGGAGCTGGTCGACCTCGAAGTGCCGGGGCGCTCACCTCGAGTGTCCCTGCGGCTGGGTGGCGGCGAGCTCGTGGCGCTGCTCGGCCCCAACGGCGCGGGCAAGTCCTCGATCCTGTCTGCCCTGGCCGGACTTGTGCGCTCCACAGCATCCAAGGCGGTGGTCGGTGGCCAGGATGTCGGCAAGGGCAGGCACCTGGTTGGATACGTCTTCCAGAATCCTGAGCACCAGTTCGTGGCCACCACCGTCGGGGCAGAGCTCGCCGTCGGAGGGACCTCGCCGGAGCGGGTCAGTGAGCTCCTCGAGCAGTTCCACCTGACCGCCCACCGGGACCACCATCCCCTGACCCTCTCGGGCGGCCAGGCCCGCAGGCTCTCAGTGGCCACCATGGTCAGCGAGGAGCGCGACGTCGTCGTCCTGGACGAGCCCACTTACGGGCAGGACTGGGACAACACCTGCGAGCTCATGGACTTCATCGACCAGCTGTGCCACCAGGGACGCACGGTCATCATGGCCACCCACGACCTCGAGCTCGCCCTGGAGCACTGCACCCATATCGTCGCCCTGCCCGGGGCGGCCGGAACCGGAGCAGCGGACTCGCGCGCCGGTCTGCCCGAGCCCGCCCCGGTGCCGCCCCAGCCTAGGCCCCGGCGAGGCCTGTTCACCTCGCTCAACCCCTTCACCCTCTTCGCCTCGGTCCTGCCGGTCATGGTGATGGTCTTCGCCCTGCGCAACCATCACCTCAACCTGGGCATCCTGCTGACATCCTCGGTCCTCATCGTCGCCGCCCGCGCCTCCCTGAGACGCACGGTGGCCTCGGTGGTCGCCCCCTGGGTGGTCGCTGCGCTCATGACCTGGATCTTCAGCAGCGGGGTCCACCACCAGGAGACGGCCGCGCGCCTCTACGACCTGGGTGACGCGGTGACGGGAGGCACCGGTATCGGCGCGCTCATCGCACTGGTCCTCGTCTCGGGCGTCTCCACCGACCCCGAGGCCCTCATCCGCACTCTGACCACCACCTTCCACATGCCCTACCGCCTCGGGGCGGCGGGGACCGCGGCCATCGCCTTCATCACCCGCTTCCACGGCGACTTCGTCCTCCTGCGCACCGCCAGGGCGCTGCGCGGGGTCGGCGGCCGCTGGGGGATGCTCGCGCCCGTGGTCCGCTGGATCGGCTCCATCCTGCCGCTGATGATCCTGGCCATCCAGCACGCCGAGCGCGTCGCCCTGTCCATGGACTCACGCGCCTTCGGCGCCCACCGACGGCGCACCGAGATGACCGACGAGCCCTGGAGAGGACGCGACTGGGGAGTTGTCGTTCTCACCTGGGCGCTGGCCCTCATCATCTGGAACACCCTCCGCTGA","VEQPPEGVAEAALVSVEGLSVHYLGRESWVLDAVDLTHLRAQVTAVIGPSGCGKTTLVRALCGLIPHCLPSEYAGSLRLAGTEVADATVQTLAQTVAYVGQSPDAAVVTRTVHDDVAFPLQNLCLARSEITARVEQALRAVGLIERIWDDPWTLSGGQRQRLALAVALAMRPQLLVLDEPTSTIDATGREEFYTLISSLTASGTAVVVIDHDLDPVLPIVDQVLALNADGRTIAVGSPREVFMSHRRELTDAGVWMPRALREAGDDLPAGMQASEAALTCAEAGIRVPRLADLCAEGEVRYLEKQAAGSAESWQQVEVIDTREVLAGRPRPEPRTSVELVDLEVPGRSPRVSLRLGGGELVALLGPNGAGKSSILSALAGLVRSTASKAVVGGQDVGKGRHLVGYVFQNPEHQFVATTVGAELAVGGTSPERVSELLEQFHLTAHRDHHPLTLSGGQARRLSVATMVSEERDVVVLDEPTYGQDWDNTCELMDFIDQLCHQGRTVIMATHDLELALEHCTHIVALPGAAGTGAADSRAGLPEPAPVPPQPRPRRGLFTSLNPFTLFASVLPVMVMVFALRNHHLNLGILLTSSVLIVAARASLRRTVASVVAPWVVAALMTWIFSSGVHHQETAARLYDLGDAVTGGTGIGALIALVLVSGVSTDPEALIRTLTTTFHMPYRLGAAGTAAIAFITRFHGDFVLLRTARALRGVGGRWGMLAPVVRWIGSILPLMILAIQHAERVALSMDSRAFGAHRRRTEMTDEPWRGRDWGVVVLTWALALIIWNTLR$","ABC-type cobalt transport system, ATPase component","Membrane, Cytoplasm, Extracellular","cobalt ABC transporter, ATP-binding protein","K02006 cobalt transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003339
Family

Cobalt transport protein
PF02361	$\"[552-762]T$	CbiQ

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[154-196]T$ $\"[452-495]T$	Q8ES39_OCEIH_Q8ES39;
PF00005	$\"[41-230]T$ $\"[358-530]T$	ABC_tran
PS50893	$\"[16-254]T$ $\"[316-552]T$	ABC_TRANSPORTER_2
PS00211	$\"[154-168]T$ $\"[453-467]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[40-230]T$ $\"[357-528]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[8-263]T$ $\"[350-543]T$	no description
PTHR19222	$\"[14-319]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
tmhmm	$\"[559-579]?$ $\"[584-604]?$ $\"[608-628]?$ $\"[643-663]?$ $\"[677-697]?$ $\"[718-738]?$ $\"[771-789]?$	transmembrane_regions

","BeTs to 11 clades of COG1122COG name: ABC-type cobalt transport system, ATPase componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1122 is aom-kz--vdrlbce-gh------twNumber of proteins in this genome belonging to this COG is 1","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1e-25. IPB013563A 30-64 IPB013563C 151-178 IPB013563A 347-381 IPB013563C 450-477***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.9e-22. IPB005074C 30-77 IPB005074D 142-185 IPB005074C 347-394 IPB005074D 441-484***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3.2e-20. IPB010509B 41-66 IPB010509D 149-193 IPB010509B 358-383 IPB010509D 448-492***** IPB005116 (TOBE domain) with a combined E-value of 2.3e-17. IPB005116A 48-64 IPB005116C 154-167 IPB005116D 174-193 IPB005116C 453-466***** IPB010929 (CDR ABC transporter) with a combined E-value of 3.7e-07. IPB010929K 28-72 IPB010929M 151-197 IPB010929A 357-376","Residues 25-209 are 40% similar to a (ATP-BINDING) protein domain (PD845659) which is seen in Q82AF2_STRAW.Residues 27-211 are 44% similar to a (ABC ATP ATP-BINDING TRANSPORTER BINDING) protein domain (PD736553) which is seen in Q8G819_BIFLO.Residues 338-512 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 42-224 are 47% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD737914) which is seen in Q835P3_ENTFA.Residues 360-513 are 45% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD738131) which is seen in Q830L1_ENTFA.Residues 45-227 are 50% similar to a (SUPERFAMILY ABC ATP-BINDING ATP_BIND) protein domain (PDA0K5L1) which is seen in Q6F7A3_ACIAD.Residues 130-233 are 55% similar to a (ATP-BINDING RBSA PLASMID RIBOSE) protein domain (PDA0I5K6) which is seen in Q6W1L5_RHISN.Residues 141-227 are 62% similar to a (ATP-BINDING LONG 471AA ABC TRANSPORTER) protein domain (PD586344) which is seen in Q972J5_SULTO.Residues 154-231 are 61% similar to a (ATP-BINDING SUGAR ABC TRANSPORTER) protein domain (PDA0I778) which is seen in Q98JJ1_RHILO.Residues 205-268 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA115H1) which is seen in Q6ACM0_BBBBB.Residues 336-525 are 45% similar to a (ATP-BINDING LONG ABC TRANSPORTER 492AA) protein domain (PD292101) which is seen in Q9YG38_AERPE.Residues 338-512 are 48% similar to a (ATP-BINDING TUNGSTATE) protein domain (PDA194Y1) which is seen in Q72GB4_THET2.Residues 351-499 are 41% similar to a (ATP-BINDING ABC SYSTEM) protein domain (PDA078N5) which is seen in Q6NED2_CORDI.Residues 351-512 are 47% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN) protein domain (PD626684) which is seen in Q8ZXM7_PYRAE.Residues 351-529 are 41% similar to a (ATP-BINDING) protein domain (PD620228) which is seen in Q8KJR6_BBBBB.Residues 351-396 are 76% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE SYSTEM MEMBRANE PROBABLE ACID) protein domain (PD000005) which is seen in Q92P94_RHIME.Residues 358-511 are 47% similar to a (ATP-BINDING TRANSPORTER ABC PROTEIN RIBOSE) protein domain (PD525719) which is seen in Q8ZUZ6_PYRAE.Residues 360-513 are 45% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PD738131) which is seen in Q830L1_ENTFA.Residues 399-515 are 47% similar to a (ATP-BINDING LONG 230AA ABC TRANSPORTER) protein domain (PD377145) which is seen in Q9Y979_AERPE.Residues 406-512 are 47% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0K1H6) which is seen in Q73MA6_TREDE.Residues 433-527 are 58% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA0I2Z5) which is seen in Q73R11_TREDE.Residues 437-512 are 56% similar to a (ATP-BINDING ABC TRANSPORTER) protein domain (PDA106Q1) which is seen in Q73R37_TREDE.Residues 442-525 are 60% similar to a (ATP-BINDING COBALT ABC TRANSPORTER) protein domain (PD167286) which is seen in O83255_TREPA.Residues 452-495 are 77% similar to a (ATP-BINDING ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE MEMBRANE SYSTEM PROBABLE ABC-TYPE) protein domain (PD000006) which is seen in Q8ES39_OCEIH.Residues 707-786 are 60% similar to a (COBALT PERMEASE ABC TRANSPORTER TRANSPORTER ABC-TYPE COMPONENT CBIQ FAMILY PROTEIN) protein domain (PD866009) which is seen in Q6ACL9_BBBBB.","","-49% similar to PDB:1G29 MALK (E_value = 6.6E_20);-50% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 3.3E_19);-49% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 4.3E_19);-48% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 4.7E_18);-48% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 4.7E_18);","Residues 41 to 230 (E_value = 7.4e-47) place ANA_1254 in the ABC_tran family which is described as ABC transporter.Residues 358 to 530 (E_value = 3.9e-41) place ANA_1254 in the ABC_tran family which is described as ABC transporter.Residues 552 to 762 (E_value = 0.0047) place ANA_1254 in the CbiQ family which is described as Cobalt transport protein.","","ABC transporter, ATP-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1255","1338719","1338084","636","11.06","8.10","21743","ATGAGCACCACCAACCGCACGCCGGCCGCCACCGAGCAGGACAGGCCATCGGTTCGCACCTCGTCCCGCTCAGGCCTGGCCGACTCCGCCCTGGGAACCCGCAACCTCATGATGATCGCCGCACTGGCGGTTGTCTGCATGATCCTCATGGTCCCCCTGAACTACCTGGCCCCGGCGGCGGGAGCCTCCCGGGACGCAGTTCTTCTGGGCTGCGCGATCATGGGACTGTGGCTCGTTCCGTTCCTGCTGCCCGCCACCGTCGTTCGCCGCCCCGGCGCTGTCATGATCGCGGCCCTTCTCATGGGGATCATGAGTGTCTTCACCACTCCGACGGGGCCCGCCGCCATCGTCGGCACCCTCATCGGCGGAGTCTTCGTCGAGGCGCCCCTGGCCATCCTGCTCTACCGGAAGTGGACCTGGTGGTCCTTCCTCATCTCAGCGGCAACGTTCGGCCTGCTCAACGGCATCATGTACGTCTCCGTCATGAGTGCCTCAGCGGGAATGGCCTCGGCGAGCGCCGGCGTCATCATCGCCGTGGTCTCGGCCCTGGTTGGCGGCGGCCTCACCATTGTCCTGACCCGACTGCTCAACCGCGCCGGCGTCGGCATCGATCACCGCACGGTCGGCCGTGCCTGA","MSTTNRTPAATEQDRPSVRTSSRSGLADSALGTRNLMMIAALAVVCMILMVPLNYLAPAAGASRDAVLLGCAIMGLWLVPFLLPATVVRRPGAVMIAALLMGIMSVFTTPTGPAAIVGTLIGGVFVEAPLAILLYRKWTWWSFLISAATFGLLNGIMYVSVMSASAGMASASAGVIIAVVSALVGGGLTIVLTRLLNRAGVGIDHRTVGRA$","Permease","Membrane, Cytoplasm","ABC-type transporter, permease components,putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[36-56]?$ $\"[66-86]?$ $\"[91-109]?$ $\"[115-135]?$ $\"[144-164]?$ $\"[170-192]?$	transmembrane_regions

","BeTs to 3 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","Residues 40-156 are 51% similar to a (MEMBRANE PERMEASE TRANSPORTER ABC-TYPE ABC MW0960 SA0929 COMPONENT SAG0836 SP0719) protein domain (PD107376) which is seen in Q6ACM1_BBBBB.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","transporter, permease components, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1256","1340667","1339123","1545","5.15","-22.29","54775","GTGAGCACCAGCGCCCCGGGGCCGCGCGTCACCGGCCTGGAGACCGAATTCGGCCTCCTGTGCGCCCCCGCGGGGCCGTCGGAAGCGACGAAGGAGGACCTGCCGGATGTCGAGCGGGCGGCGGCGCTCATCTTCCGTCACCGGCCGGTCGGCTACCGCAGCACCAACCTCTTCCTGCCCAACGGCGGGCGCCTCTACCTCGACATCGGTGCCCACCCCGAGTACGCCACCGCCGAGTGCGTGAGCGTGCGCGACCTCGTCGCCCAGGACCAGGCCGGCCGGGCGATCCTGGCCGACATGGCCACGCGTGCCGCCACGAGCCTCGCCCAGGAGGGGACCGCGGTCCGCTTCCACCTCCTGGCCAACAACACCGATTCGGCCGGCCACACCTACGGCTGCCACGAGAGCTACTCCGTGCCCCGAAGCCTGCTCGACCCCACCGACGACGCATCGGCCGCCAGCAGTGAGACCACCATGGCGGTCCTCACCTCCTTCCTGGCCACGCGTCCCGTCCTGGTCGGCTCCGGGCGCCCACTGGCAGGCGGCCCGACGGAGCCGAACGACGGCAGCCGCGGTGCGGGGGAGGAGGCCGCCTGGGGCCTGTCGCCGCGCGCCCCCCACCTGCAGGCCCTGACCTCGGCCGACACCACCGGGCAGCGCGCCCTGGTCAACACCCGCGACGAGCCCCACGCCGACGCCACCCGCCTGCGCCGCCTGCACGTCACCTGCGCCGACACCACCATGGCCGAGCCGACAACAGGCCTGCGCAGCGCCGTGACCCTGCTGCTCTTGGACGCCCTCGAGGCCGGCTGGGACTTCACCGACCTGACCCTGGCCGACCCCCTGGCCACGCTGTCCGCACTCGGGGAGAGCCCCTGGGGGGACGTGCCCGCCACCACCGTCCAGGGCCGGTGCCTGAGCGCCGTCGACATCCAGGAGGCTTTCCTGGAGCGGCTGACCTCCTACCTGGACCAGGCCGGAGTGCCGGACTTCCTGCGCGGCGCCGAGCACCTGCTCACCGACCTGGCGCCACGCGTCATCTCCGCGCTGCGCCACCACGACGACAGCGCCATCGACACCGAGATCGACTGGGCCATCAAGCGTCGCCTCATGCGCGCCCAGCGTGAGCGCCACCCCCAGCTGAGCGGCCAGTCCCTGGAGACCCTGCGCTCGCGGGTGGACCTGGCCTACCACGACCTCAACGCCGAGGCCGGGCTGGTGCCGCGCCTGGTCGCCGAGGGGGCCATGGTGAACCTGTGCGAACCGGAGGAGATCGAGCGTGCCCGCCACACGCCCCCGGCCACGCGCGCCGCCCTCCGGGGTGCCTTCGTGGCGGCCTGCCTGGAGGTGGGAGCTGACTTCTCCGTCTCCTGGGAGGGCTTGCGACTGGACTCTCCGCCCACTGCGCCCGTGGACCTGCCGGATCCGCTGGAGACGGTCCATGAGGCCGCCGAGTCCCTGACTCAGCGGGTGCTGGGCCTGCGTCCCGAGGACATGCACCGCATCGACCTCGTGGGACGCGGCGGCCTGGGTGCGCCGGGCTGA","VSTSAPGPRVTGLETEFGLLCAPAGPSEATKEDLPDVERAAALIFRHRPVGYRSTNLFLPNGGRLYLDIGAHPEYATAECVSVRDLVAQDQAGRAILADMATRAATSLAQEGTAVRFHLLANNTDSAGHTYGCHESYSVPRSLLDPTDDASAASSETTMAVLTSFLATRPVLVGSGRPLAGGPTEPNDGSRGAGEEAAWGLSPRAPHLQALTSADTTGQRALVNTRDEPHADATRLRRLHVTCADTTMAEPTTGLRSAVTLLLLDALEAGWDFTDLTLADPLATLSALGESPWGDVPATTVQGRCLSAVDIQEAFLERLTSYLDQAGVPDFLRGAEHLLTDLAPRVISALRHHDDSAIDTEIDWAIKRRLMRAQRERHPQLSGQSLETLRSRVDLAYHDLNAEAGLVPRLVAEGAMVNLCEPEEIERARHTPPATRAALRGAFVAACLEVGADFSVSWEGLRLDSPPTAPVDLPDPLETVHEAAESLTQRVLGLRPEDMHRIDLVGRGGLGAPG$","Putative proteasome component","Cytoplasm","Putative proteasome component family","hypothetical protein","protein of unknown function DUF245 domain protein","","Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R. The 20S proteasome of Streptomyces coelicolor. J. Bacteriol. 1998. 180(20):5448-5453. PMID: 9765579Pouch M.N., Cournoyer B., Baumeister W. Characterization of the 20S proteasome from the actinomycete Frankia. Mol. Microbiol. 2000. 35(2):368-377. PMID: 10652097Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., Tanaka K., De Mot R., Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr. Biol. 1995. 5(7):766-774. PMID: 7583123","","","

InterPro
IPR004347
Domain

Protein of unknown function DUF245, C-terminal
PF03136	$\"[150-491]T$	DUF245

InterPro
IPR004989
Domain

Protein of unknown function DUF275, N-terminal
PF03316	$\"[56-138]T$	DUF275

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 12-137 are 63% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD009688) which is seen in Q6NH95_CORDI.Residues 162-325 are 57% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD008464) which is seen in Q53081_RHOER.Residues 358-487 are 55% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 B2126_C3_265 SCO1640 ORF61 RHODOCOCCUS) protein domain (PD008229) which is seen in P72263_RHOER.","","No significant hits to the PDB database (E-value < E-10).","Residues 56 to 138 (E_value = 3.8e-17) place ANA_1256 in the DUF275 family which is described as Actinomycetales protein of unknown function, DUF275.Residues 150 to 491 (E_value = 2.5e-56) place ANA_1256 in the DUF245 family which is described as Putative proteasome component.","","proteasome component family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1257","1340852","1340664","189","4.26","-7.06","6553","ATGAGTGAGTTCGCCCAGCCGTCCCGCAGCCGTCAGGACGACCCCGCTCCCGACGACGACCCGACCCCCGCCCCCGCCGGCCCCGCCCGGGGCCAGGGCCTGGACTCGGTGCTGGACATGATCGACGACGTCCTGGCCGTTGACGCCCAGGAGTTCGTGCGCGGCTTCGTCCAGAAGGGCGGCCAGTGA","MSEFAQPSRSRQDDPAPDDDPTPAPAGPARGQGLDSVLDMIDDVLAVDAQEFVRGFVQKGGQ$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

InterPro
IPR008515
Family

Protein of unknown function DUF797
PF05639	$\"[3-62]T$	DUF797

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 62 (E_value = 1.7e-05) place ANA_1257 in the DUF797 family which is described as Protein of unknown function (DUF797).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1258","1342624","1340849","1776","5.68","-13.46","62817","GTGGCGCCGGCGAGCACCCATCGGATCCCCGGCCGTGAGGTCACGGTCATGGGCCTGGAGACCGAGTACGGCATCCTCGGGGCCGAGCCCGAGGACGTCGTGGCCGCCTGCCTGGACGCTGAGGGTGAGGTCGGGCGCAGCCGAGGCGTGCGCTGGGACTACTCCGGCGAGTACCCCCTGCGTGATGCCCGCGGATTCGAGATGGACCGCGCAGCGGCTGACCCCTCCATGCTCACCGACATCCCCGGAGCCGCCTCCGTCGAGGCCCCCGTCCCCGGGCGGGTACGTACCACCGCCGTCGTGCGCCTGACCGCCCAGGAGGAGGCCTGGCAGCGCGGCACCGCCACCTGCGTGGGCACCGGCGGGCGCCTCTACGTGGACCACGGCCACCCCGAGTACGCCACACCCGAGTGCACCGGTGCCGCGCAGGCCGTCCTGGCCGACCGGGCCGGGGACCTCCTGGTGGCCAGCGGGGCCGAGCGGCTGCGTCGCGGCGGCGTGAAGGCCCGGCTATTCAAGAACAACGTCGACGGCAAGGGCGCCACCTACGGCACTCACGAGAACTACCTCGTGCCTCGCGCCCTCGACTTCGACGACCTCGTTCAGGCCCTGGTCCCCCTGCTCGTGGTCCGCCCGCTCCTGGTGGGCTCGGGCCGGGTCGGCACCGGCGCTGTCACCCAGGGCGCCGACTTCCAGATCAGCCAGCGGGCCGACTACCTGGAGAGGATCGTCGGCCTGGGCACCACGGTGGACCGCCCCCTGGTCAACACTCGCGACGAGCCCCACGCCGACCCCCTGCGCTGGCGCCGTCTTCACCTGGTGGCGGGCGACGCCAACTGCTTCGACACCATCGCCTGGCTCAAGCTCGGCATGACCGCCCTCGTCCTCCAAGTGCTGGCCGACGGCGTCCCCGCCGCCTGGCGCCGCCTGCGCCTGGCAGACCCCGTGGCCCAGGCCCGGGAGGTCTCCCGTGACACCCGCCTTCAAGGCACGCTGGAGCTGGACGACGGGCGGCGCCTGAGCGCCCTGGAGATCCTGGAGCACTACCTGCAGGCGGTGCGCAGCCACCTGAAGGACCACGGCCGCCCCGCGCCGGCGCCGCAAGGCGACCCCCTGCGCCCGGACCTGGCCGCGCTGGCCGACGGCGCCGACACCGATGGCGCCGAGACCGGCGCGATCCTCGCCTTCTGGGAGGCCTCACTGGCCTCACTGCGCGAGCTGCAGGCCCAGTGCGCCGGTGGCCACGAGCCGGGGGAGTCGCAAGGAGCGGCCGGGCACCTGGAGTGGGTCGCCAAGAAGCAGCTCCTGGATGCCACCGCCCGCCGCCATCCCGGCGCCGGCGGACACGACGTCCTCCATGCCGTCGACCTGGCCTGGTCCGAGCTCTCCCCGGCCGGGAGGGGCCTGGCCGAGCGGGTGCCAGCCGGCGCCGACGCGCGAGGCGGGCTCAGTGACGAGGTGGTGGAGACGGCCCTCGCCAAGCCGCCCACCACGACCCGGGCCTGGCTGAGAGGTAGGCTCGTGAGCGACTTCCCCGGGCAGGTGGTCGCCGCCGGCTGGCACTCCATGGTCCTGGAAACCGGTGAGATGGCCCAGCGCCGCCTGCCCCTGACCGACCCCCTGGCCTTCACCCGCACCGCCACGGTGCCGGCCCTCAAGGACGCCGCCGATGTCGTCGAGGTCCTCTCTCGCCTCACGGGCGAACGCCCCGGCGACCCGGGGCGAGCCACCGAAGCAGTGACCACATCCGCCACCCTGTTAGGAGAGCAGACATGA","VAPASTHRIPGREVTVMGLETEYGILGAEPEDVVAACLDAEGEVGRSRGVRWDYSGEYPLRDARGFEMDRAAADPSMLTDIPGAASVEAPVPGRVRTTAVVRLTAQEEAWQRGTATCVGTGGRLYVDHGHPEYATPECTGAAQAVLADRAGDLLVASGAERLRRGGVKARLFKNNVDGKGATYGTHENYLVPRALDFDDLVQALVPLLVVRPLLVGSGRVGTGAVTQGADFQISQRADYLERIVGLGTTVDRPLVNTRDEPHADPLRWRRLHLVAGDANCFDTIAWLKLGMTALVLQVLADGVPAAWRRLRLADPVAQAREVSRDTRLQGTLELDDGRRLSALEILEHYLQAVRSHLKDHGRPAPAPQGDPLRPDLAALADGADTDGAETGAILAFWEASLASLRELQAQCAGGHEPGESQGAAGHLEWVAKKQLLDATARRHPGAGGHDVLHAVDLAWSELSPAGRGLAERVPAGADARGGLSDEVVETALAKPPTTTRAWLRGRLVSDFPGQVVAAGWHSMVLETGEMAQRRLPLTDPLAFTRTATVPALKDAADVVEVLSRLTGERPGDPGRATEAVTTSATLLGEQT$","Putative proteasome component","Cytoplasm","putative proteasome component","hypothetical protein","protein of unknown function DUF245 domain protein","","Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R. The 20S proteasome of Streptomyces coelicolor. J. Bacteriol. 1998. 180(20):5448-5453. PMID: 9765579Pouch M.N., Cournoyer B., Baumeister W. Characterization of the 20S proteasome from the actinomycete Frankia. Mol. Microbiol. 2000. 35(2):368-377. PMID: 10652097Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., Tanaka K., De Mot R., Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr. Biol. 1995. 5(7):766-774. PMID: 7583123","","","

InterPro
IPR004347
Domain

Protein of unknown function DUF245, C-terminal
PF03136	$\"[191-556]T$	DUF245

InterPro
IPR004989
Domain

Protein of unknown function DUF275, N-terminal
PF03316	$\"[17-190]T$	DUF275

","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 17-80 are 57% similar to a (PROTEASOME COMPONENT MLCB2533.17 SIMILAR CGL1496 ORF61 RHODOCOCCUS NI86/21 SCO1647 B2126_C1_172) protein domain (PD022888) which is seen in Q828J1_STRAW.Residues 121-190 are 72% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD009688) which is seen in Q7TZ11_MYCBO.Residues 221-359 are 66% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 SCO1640 ORF61 RHODOCOCCUS NI86/21) protein domain (PD008464) which is seen in Q9RAW9_BBBBB.Residues 427-545 are 55% similar to a (PROTEASOME COMPONENT PROTEASOME-ASSOCIATED MLCB2533.17 SIMILAR CGL1496 B2126_C3_265 SCO1640 ORF61 RHODOCOCCUS) protein domain (PD008229) which is seen in Q828J1_STRAW.","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 190 (E_value = 4.5e-31) place ANA_1258 in the DUF275 family which is described as Actinomycetales protein of unknown function, DUF275.Residues 191 to 556 (E_value = 9.3e-70) place ANA_1258 in the DUF245 family which is described as Putative proteasome component.","","proteasome component","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1259","1344279","1342630","1650","5.44","-18.11","59389","ATGGATGAGGAACCGGTGGAGCACAAGGATCCGGTGGCGCAGACGCTGACGGGCGCCTCCCGGGACCAGTCTGTGCAGGCCGGCAGCCAGTCCGGAGGGGACGTCACCGAGCGCCTGCGGGAGCTCAGCGAGCACGCCGGCGTGCTCAGCCGTAAGAACACCCACCTGGCCAACGCCCTCAGGGCGGCGCGCCAGGAGCTGGCGGTCCTGCACGAGGACGTCAAGGCCCTCCAGCTCCCGCCCCTGGCGCACGCCACCGTCCTGGCCGTGGACGCAGGCGCGCGCACCGCCGACGTCTCCATCGCCGGGCGGCGCCACCGGGTGGGCGTGGGGCCCGCCGTCGTGTCCTCCTCCCTCCACCCGGGTGACGACGTCGTCCTCAACGAGCATCTCGTCATCACCGCCACCTGCCCCTCACCGCGCTTCGGGGAGGTCGTCACCGTCAAGGAGACCTACGACGACGGCACCGTCCTGGTCCTGGCCCGCCACGACGAGGAGCAGGTCCTCAGCCTCTCGGATACCCTGAGCGACCACCGCCCCCGGGTCGGCGACGCCCTCGTGGCCGACCTGGCCGTGCGCATGGCACTGCGTCCCGTGGTGCGCTCCGAGGTCGAGGAGCTCGTCCTGGAGGAGGTGCCCGACGTCGGATACGGCGACATCGGGGGACTGGGTGAACAGATCGAGCTCATCCGCGACGCCGTCGAGCTGCCCTTCCTCCACCCCGACCTCTACCGCGAGCACCGGCTCACCCCGCCGCGCGGAGTGCTGCTCTACGGGCCGCCCGGATGCGGCAAGACCCTTATCGCCAAGGCGGTCGCCGCCTCCCTGGGGGCCGGCGGGCGCGGCGAGGCCTACTTCCTCAACATCAAGGGCCCCCAGTTGCTGGACAAGTACGTGGGGGAGACCGAGCGGCGCATCCGCGTCATCTTCGCCCGCGCCCGGGAGAAGGCGGCCACCGGCGTGCCCGTCGTCGTCTTCTTCGACGAGATGGACTCCCTGTTCCGCACCCGCGGATCCGGACGCTCCTCCGACGTGGAGACCACCGTCGTCCCGCAGATGCTCGCCGAGATCGACGGCGTCGACGAGCTCGACAACGTCGTGGTCATCGGTGCCACCAACCGCGAGGACATGATCGACCCGGCCATCCTGCGGCCGGGCCGCCTGGACGTCAAGATCCGCATCGGCCGGCCGGACCGGCGCGGCGCCGCCGAGATTCTGGCGACATACCTGGCCCCCGACCTCCCCATCAGCGAGGAGCTCCTGGCCGCGCACGGTGACGCGCAGGGCGCGGTGGACGCCCTCATCGAGCAGGTGATCGATGCCCTCTACACCCGCCGCCGCGCCACCGAGATGGTCGAGCTCACCCGCGCCGACGGGGAGATCGAGATCCTCCACGTCGCCGACCTCGTCAGCGGTGCCATGCTCGCCAACATCGTCGACCGCGCCAAGAAGGCAGCCGTCAAGGACCTGGTCACCAAGGGCAGGCGCGGCCTGACGTCCGAGCACCTGCGCCGTGCCGTCATCGAGGAGATCCTGGAGAACGAGGGCCTGCCCGCCACCGTCCACCCCGACGACTGGGCCCGCGTCAGCGGGAGGCGCGGCACGCCAGTGGTCTCCATGAGCGTGCTCCAGCGCTCGCGGGAGGAGTGA","MDEEPVEHKDPVAQTLTGASRDQSVQAGSQSGGDVTERLRELSEHAGVLSRKNTHLANALRAARQELAVLHEDVKALQLPPLAHATVLAVDAGARTADVSIAGRRHRVGVGPAVVSSSLHPGDDVVLNEHLVITATCPSPRFGEVVTVKETYDDGTVLVLARHDEEQVLSLSDTLSDHRPRVGDALVADLAVRMALRPVVRSEVEELVLEEVPDVGYGDIGGLGEQIELIRDAVELPFLHPDLYREHRLTPPRGVLLYGPPGCGKTLIAKAVAASLGAGGRGEAYFLNIKGPQLLDKYVGETERRIRVIFARAREKAATGVPVVVFFDEMDSLFRTRGSGRSSDVETTVVPQMLAEIDGVDELDNVVVIGATNREDMIDPAILRPGRLDVKIRIGRPDRRGAAEILATYLAPDLPISEELLAAHGDAQGAVDALIEQVIDALYTRRRATEMVELTRADGEIEILHVADLVSGAMLANIVDRAKKAAVKDLVTKGRRGLTSEHLRRAVIEEILENEGLPATVHPDDWARVSGRRGTPVVSMSVLQRSREE$","AAA+ ATPase","Cytoplasm, Membrane","AAA ATPase","vesicle-fusing ATPase ","AAA ATPase, central domain protein","","","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[251-398]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[254-444]T$	AAA

InterPro
IPR003960
Domain

AAA ATPase, subdomain
PS00674	$\"[366-384]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[203-394]T$	no description
PTHR23073	$\"[199-471]T$	26S PROTEASE REGULATORY SUBUNIT
PTHR23073:SF4	$\"[199-471]T$	AAA-FAMILY ATPASE

","BeTs to 10 clades of COG0464COG name: ATPases of the AAA+ classFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0464 is aompkzy--dr-bc-f----uj----Number of proteins in this genome belonging to this COG is 3","***** IPB003960 (AAA-protein subdomain) with a combined E-value of 7.6e-60. IPB003960A 217-232 IPB003960B 252-273 IPB003960C 302-337 IPB003960D 352-402 IPB003960E 472-488 IPB003960B 260-281***** IPB003338 (AAA ATPase VAT, N-terminal) with a combined E-value of 4e-52. IPB003338A 238-291 IPB003338B 311-338 IPB003338C 344-398 IPB003338D 453-492***** IPB000642 (Peptidase M41) with a combined E-value of 1.1e-39. IPB000642A 235-284 IPB000642B 292-334 IPB000642C 365-409 IPB000642D 463-488***** IPB004201 (Cell division protein 48, CDC48, domain 2) with a combined E-value of 4.7e-30. IPB004201B 289-341 IPB004201C 364-411 IPB004201E 316-353","Residues 37-223 are 55% similar to a (ATP-BINDING ATPASE AAA-FAMILY AAA ARC ATPASES AAA ML1316 H-TRANSPORTING PROBABLE) protein domain (PD023538) which is seen in Q828J2_STRAW.Residues 219-373 are 46% similar to a (ATPASE ATP-BINDING) protein domain (PDA043P0) which is seen in Q7WSR6_BBBBB.Residues 226-295 are 81% similar to a (ATP-BINDING PROTEASE CELL DIVISION DNA SUBUNIT HELICASE PROTEASOME HYDROLASE ATPASE) protein domain (PD337570) which is seen in Q6NH92_CORDI.Residues 253-313 are 62% similar to a (ATP-BINDING PEROXISOME ATPASE FACTOR-2 PEROXIN PEROXIN-6 MEMBRANE BIOGENESIS ASSEMBLY REPEAT) protein domain (PD010151) which is seen in Q9VK63_DROME.Residues 291-346 are 92% similar to a (ATP-BINDING CELL DIVISION PROTEASOME SUBUNIT ATPASE 26S PROTEASE REGULATORY FTSH) protein domain (PD000092) which is seen in Q9RJ58_STRCO.Residues 349-379 are 93% similar to a (ATP-BINDING CELL DIVISION PROTEASOME FTSH ATPASE PROTEASE HYDROLASE 3.4.24.- HOMOLOG) protein domain (PD186075) which is seen in Q828J2_STRAW.Residues 433-543 are similar to a (ATP-BINDING ATPASE AAA-FAMILY AAA ARC ATPASES AAA ML1316 H-TRANSPORTING PROBABLE) protein domain (PD022222) which is seen in YL15_MYCTU.","","-62% similar to PDB:1OZ4 VCP/p97 (E_value = 6.9E_42);-62% similar to PDB:1R7R The crystal structure of murine p97/VCP at 3.6A (E_value = 6.9E_42);-62% similar to PDB:1YPW Structure of p97/VCP in Complex in ADP/AMP-PNP (E_value = 6.9E_42);-62% similar to PDB:1YQ0 Structure of p97/VCP in complex with ADP/ADP.AlFx (E_value = 6.9E_42);-62% similar to PDB:1YQI VCP/p97 complexed with ADP (E_value = 6.9E_42);","Residues 254 to 444 (E_value = 1.7e-62) place ANA_1259 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).","","ATPase (cdc48)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1261","1344471","1347287","2817","5.04","-37.99","103052","ATGTCTGAGATCCCCACGAGCCACTCCGCTCCCCCGTCGTCATCCAGCCGTCTGCTGCCCTCCGAGCCCCACAGCCCGCGAGTGCCGGCCAAGGTGTCGACCGACGGCCTGGAGACCACCTGGGGCGAGCGCTGGGAGTCCGAGGGGACCTACGCCTTCGACCGCAGCGCCGAGCGCGCCGAGGTCTTCTCCATCGACACCCCGCCGCCGACGGTCTCCGGCTCCCTGCACGTGGGGCACGTCTTCTCCTACACCCACACCGACACCGTGGCTCGCTTCCAGCGCATGCGCGGCAAGGCGGTGTTCTACCCCATGGGCTGGGACGACAACGGCCTGCCCACTGAGCGCCGCGTCCAGAACTACTTCGGGGTGCGCTGCGACCCCTCCCTGCCTTACGACCCGGACTTCACTCCTCCGCACACCGGCGGGGAGGGTAAGTCGATCAAGGCCCGTGACCAGGTGCCGGTCTCGCGTCGCAACTTCGTCGAGCTGTGCGAGCGCCTCACGGTGGAGGACGAGAAGCAGTTCGAGGCCCTGTGGCGCAGGCTCGGCCTGAGCGTGGACTGGTCGCACACCTACCAGACCATTGGCGAGCGGGCCCGCAAGGTCGCCCAGACCGCCTTCCTGCACAACCTTGAGCGCGGGGAGGCCTACCAGGCGGCGGCGCCGGGTCTGTGGGACGTCACCTTCCAGACGGCGGTGGCCCAGGCCGAGCTGGAGTCGCGCGAGTACCCCGGCTTCTACCACCGCCTGGCCTTTCACATCGTCGATGAGGCCGCCGCCGCCAAGGCAGAGGCCGCCGGCGCCCCGGTGGAGAACGGCGTCGACGTGTGCATCGAGACCACCCGTCCCGAGCTGCTGCCTGCGTGCGTGGCCCTGGTGGCCCACCCCGACGACGAGCGCTACCAGCCCCTGTTCGGCACCACCGTGTCCTCGCCCGTCTTCGGCGTCGAGGTGCCGGTCCTGCCGCACCCGGCCGCGGAGAAGGACAAGGGCGCCGGCATCGCCATGTGCTGCACCTTCGGTGACACCACGGACATCGACTGGTGGCGCGACCTGCAGCTGCCGCTGCGAGCGATCCTGCGCAAGGACGGGCGCATCGAGACCGAGACCCCCGAGTGGATCACCTCCCCGGCCGGCCGCGAGATGTACGAGGCCATGGCCGGCAAGACCACCTTCTCGGCCCGTGAGGCCCTCGTGGCCCGCCTGGCCCAGACCGGTGAGATGCGCGGCGAGCCCGTCAAGACGGTGCGTCAGACCAACTTCTTCGAGAAGGGTGACAAGCCCCTGGAGATCGTCACCTCCCGCCAGTGGTACATCCGCAACGGCGGCAAGGAGTGGACGAACCCGGCCTCCGGTGCGGACCTGCGCGAGGAGCTGCTCGAGCGCGGCCGCCAGCTGGAGTTCCACCCCGACTTCATGCGCGTGCGCTACGAGAACTGGGTGCGCGGCCTCAACAACGACTGGCTGGTCTCACGCCAGCGCTTCTTCGGCGTCCCCTTCCCGCTGTGGTACCAGGTCGGGGCCGACGGCGAGGTCGACTACGACGCGATCCTGACGCCGGCCGAGTCCGAGCTGCCCGTGGACCCCTCCTCCGACGTCCCGGCCGGCTACACCGAGGACCAGCGTGGCGAGCCCGGTGGTTTCGTCGGTGAGCTCGACATCATGGACACCTGGGCCACCTCCTCCCTCTCGCCCCAGCTGGCCTCGGGCTGGCTGAGCGATGAGGACCTCTTCGGCCGGGTCTACCCGATGGACCTGCGCCCGCAGGGGCAGGACATCATCCGCACCTGGCTGTTCACCACAGTGGTGCGCGCGAACCTGGAGTTCGCGGCCCTGCCGTGGACGAATGCCGGCCTGTCGGGCTGGATCCTGGACTCCGACCACAAGAAGATGTCCAAGTCGAAGGGCAATGTCGTCACCCCCATGGGCCTGCTGGAGCAGTACGGCTCCGACGCCGTGCGCTACTGGGCCAGCTCGGCCCGCCTGGGCCTGGACGCGGCCTTCGAGGAGACCCAGATCAAGATCGGCCGTCGCCTGGCCATCAAGGTCCTCAACGCCTCCAAGTTCGCCCTGTCCATGGGGATCCCCTGGGACGCCGATGAGGCCACCGTGGCGGCGGCTCCTGCCCCCTGCCTGGACGCCTCGGTGGTCAGTGAGCCGATCGACCGTGCGGTCCTGGCGGCTCTGGCCGACGTCGTCGACGCCGCCACGGCGGCCTTCGAGGAGTTCGGTCACGCCCGGGCCCTGGAGGTCACCGAGTCCTTCTTCTGGACCTTCTGCGATGACTACATCGAGCTGGTCAAGGAACGGGCCAATGACTTCGACGGCTCTCACGACGCCGCTGCCGTCTGCTCGGCGCGGGCGACGCTGGCGATCGCCGTGGACACCTTCGTGCGCCTGTTGGCCCCCTTCCTGCCCTTCGCCACCGAGGAGGTGTGGAGCTGGTACCGCACCGGCTCGGTGCACCGGGCCGCCTGGCCGCAGTCCGAGGGTCTGCGGGAGGCCGCCGCGGGAGCCGACGCCGAGCTGGTGGCCCGTGCGGGAGTCGCCCTGGCGGCGCTGCGCAAGGTGAAGTCGGAGGCCAAGACGAGCCAGAAGACTCCGATCCTCTCGGTGACGCTGGCCGTTGCCGCCGACCGGCCCGAGTACGCCGAGGCCATCGAGGCGGTGCGTGCGGACCTGACGGAGGCCGCCAAGGTCACCGATGCCTTCAGCGTGGAGCAGGCCGCCCCGGCAGCCGACTCGGCTGAAGGCGCCTCCCCGGTGACCGTGACCGCCGCCGAGCTCGGCCAGGCCCCGGCCAAGAAGAAGTGA","MSEIPTSHSAPPSSSSRLLPSEPHSPRVPAKVSTDGLETTWGERWESEGTYAFDRSAERAEVFSIDTPPPTVSGSLHVGHVFSYTHTDTVARFQRMRGKAVFYPMGWDDNGLPTERRVQNYFGVRCDPSLPYDPDFTPPHTGGEGKSIKARDQVPVSRRNFVELCERLTVEDEKQFEALWRRLGLSVDWSHTYQTIGERARKVAQTAFLHNLERGEAYQAAAPGLWDVTFQTAVAQAELESREYPGFYHRLAFHIVDEAAAAKAEAAGAPVENGVDVCIETTRPELLPACVALVAHPDDERYQPLFGTTVSSPVFGVEVPVLPHPAAEKDKGAGIAMCCTFGDTTDIDWWRDLQLPLRAILRKDGRIETETPEWITSPAGREMYEAMAGKTTFSAREALVARLAQTGEMRGEPVKTVRQTNFFEKGDKPLEIVTSRQWYIRNGGKEWTNPASGADLREELLERGRQLEFHPDFMRVRYENWVRGLNNDWLVSRQRFFGVPFPLWYQVGADGEVDYDAILTPAESELPVDPSSDVPAGYTEDQRGEPGGFVGELDIMDTWATSSLSPQLASGWLSDEDLFGRVYPMDLRPQGQDIIRTWLFTTVVRANLEFAALPWTNAGLSGWILDSDHKKMSKSKGNVVTPMGLLEQYGSDAVRYWASSARLGLDAAFEETQIKIGRRLAIKVLNASKFALSMGIPWDADEATVAAAPAPCLDASVVSEPIDRAVLAALADVVDAATAAFEEFGHARALEVTESFFWTFCDDYIELVKERANDFDGSHDAAAVCSARATLAIAVDTFVRLLAPFLPFATEEVWSWYRTGSVHRAAWPQSEGLREAAAGADAELVARAGVALAALRKVKSEAKTSQKTPILSVTLAVAADRPEYAEAIEAVRADLTEAAKVTDAFSVEQAAPAADSAEGASPVTVTAAELGQAPAKKK$","Valyl-tRNA synthetase","Cytoplasm","valyl-tRNA synthetase","valyl-tRNA synthetase ","tRNA synthetase, valyl/leucyl, anticodon-binding","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[70-81]T$	AA_TRNA_LIGASE_I

InterPro
IPR002300
Domain

Aminoacyl-tRNA synthetase, class Ia
PF00133	$\"[40-670]T$	tRNA-synt_1

InterPro
IPR002303
Family

Valyl-tRNA synthetase, class Ia
PR00986	$\"[63-74]T$ $\"[296-313]T$ $\"[425-438]T$ $\"[552-573]T$ $\"[583-601]T$	TRNASYNTHVAL
PTHR11946:SF5	$\"[33-120]T$ $\"[139-912]T$	VALYL-TRNA SYNTHETASE

InterPro
IPR013155
Domain

tRNA synthetase, valyl/leucyl, anticodon-binding
PF08264	$\"[723-875]T$	Anticodon_1

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[29-669]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.730.10	$\"[719-815]T$	no description
PTHR11946	$\"[33-120]T$ $\"[139-912]T$	ISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES

","BeTs to 26 clades of COG0525COG name: Valyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0525 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB013155 (tRNA synthetase, valyl/leucyl, anticodon-binding) with a combined E-value of 2.8e-82. IPB013155A 38-51 IPB013155B 69-111 IPB013155C 179-197 IPB013155D 215-239 IPB013155E 279-298 IPB013155F 320-356 IPB013155G 488-502 IPB013155H 629-655***** IPB002303 (Valyl-tRNA synthetase signature) with a combined E-value of 2.4e-36. IPB002303A 63-74 IPB002303B 296-313 IPB002303C 425-438 IPB002303D 552-573 IPB002303E 583-601***** IPB002300 (Aminoacyl-tRNA synthetase, class Ia) with a combined E-value of 1.4e-19. IPB002300A 76-106 IPB002300B 489-502","Residues 45-118 are 84% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS LEUCYL-TRNA METHIONYL-TRNA ISOLEUCYL-TRNA VALYL-TRNA LEURS) protein domain (PD000389) which is seen in Q6A7F4_PROAC.Residues 119-179 are 86% similar to a (SYNTHETASE AMINOACYL-TRNA VALYL-TRNA LIGASE M I V TRNA I CLASS) protein domain (PDA1F0B3) which is seen in Q6AFZ2_BBBBB.Residues 186-242 are 84% similar to a (SYNTHETASE AMINOACYL-TRNA VALYL-TRNA LIGASE TRNA I V RELATED VALRS VAL) protein domain (PD868185) which is seen in Q8G777_BIFLO.Residues 243-407 are 73% similar to a (SYNTHETASE AMINOACYL-TRNA VALYL-TRNA) protein domain (PDA1D397) which is seen in Q8G777_BIFLO.Residues 279-407 are 82% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA LEUCYL-TRNA VALYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD000939) which is seen in Q6A7F4_PROAC.Residues 408-446 are 84% similar to a (SYNTHETASE AMINOACYL-TRNA VALYL-TRNA LIGASE) protein domain (PD930848) which is seen in Q8G777_BIFLO.Residues 474-538 are 81% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA VALYL-TRNA LEUCYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD000647) which is seen in Q8G777_BIFLO.Residues 546-598 are 73% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE VALYL-TRNA ISOLEUCYL-TRNA ATP-BINDING BIOSYNTHESIS VALINE--TRNA VALRS ISOLEUCINE--TRNA) protein domain (PD002669) which is seen in Q8G777_BIFLO.Residues 615-652 are 81% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCYL-TRNA METAL-BINDING ZINC CYSTEINYL-TRNA VALYL-TRNA) protein domain (PD000476) which is seen in Q8G777_BIFLO.Residues 653-692 are 92% similar to a (SYNTHETASE AMINOACYL-TRNA VALYL-TRNA LIGASE M I V TRNA I CLASS) protein domain (PD867391) which is seen in Q8G777_BIFLO.Residues 741-778 are 81% similar to a (SYNTHETASE AMINOACYL-TRNA LIGASE ISOLEUCYL-TRNA VALYL-TRNA ATP-BINDING BIOSYNTHESIS ISOLEUCINE--TRNA VALINE--TRNA VALRS) protein domain (PD259544) which is seen in Q6A7F4_PROAC.Residues 795-828 are 83% similar to a (SYNTHETASE LIGASE AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS VALYL-TRNA LEUCYL-TRNA ISOLEUCYL-TRNA LEUCINE--TRNA LEURS) protein domain (PD023651) which is seen in Q8G777_BIFLO.","","-39% similar to PDB:1GAX CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS VALYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(VAL) AND VALYL-ADENYLATE ANALOGUE (E_value = 3.0E_59);-39% similar to PDB:1IVS CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS VALYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(VAL) AND VALYL-ADENYLATE ANALOGUE (E_value = 3.0E_59);-39% similar to PDB:1IYW Preliminary Structure of Thermus thermophilus Ligand-Free Valyl-tRNA Synthetase (E_value = 3.0E_59);-36% similar to PDB:1ILE ISOLEUCYL-TRNA SYNTHETASE (E_value = 3.4E_23);-36% similar to PDB:1JZQ Isoleucyl-tRNA synthetase Complexed with Isoleucyl-adenylate analogue (E_value = 3.4E_23);","Residues 40 to 670 (E_value = 1.9e-19) place ANA_1261 in the tRNA-synt_1 family which is described as tRNA synthetases class I (I, L, M and V).Residues 63 to 680 (E_value = 5.4e-07) place ANA_1261 in the tRNA-synt_1g family which is described as tRNA synthetases class I (M).Residues 723 to 875 (E_value = 2.8e-35) place ANA_1261 in the Anticodon_1 family which is described as Anticodon-binding domain.","","synthetase (valS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1262","1347532","1347693","162","6.93","-0.15","6211","GTGACCCCTTACTTCGAGGTGCGCAACATCCACTTCTACGTCAACAAGTGCGGTTTCCACATCGTGGAGTTCTTCAATGAGCACCACCCCGCCCCCTCTGCCCCGGGCATGGACAAGGACCTCTCCTTCCGCTTCGTCAAGTATGTGGGGCTCCCGGAGTAG","VTPYFEVRNIHFYVNKCGFHIVEFFNEHHPAPSAPGMDKDLSFRFVKYVGLPE$","GCN5-related N-acetyltransferase","Cytoplasm, Extracellular","conserved hypothetical protein","GCN5-related N-acetyltransferase","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-27 are similar to a (TRANSFERASE GNAT FAMILY ACETYLTRANSFERASE ACETYLTRANSFERASE 2.3.1.- ACYLTRANSFERASE YRKN N-ACETYLTRANSFERASE GCN5-RELATED) protein domain (PD103665) which is seen in YRKN_BACSU.","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1263","1348733","1347720","1014","5.46","-7.64","35540","ATGGCGGCGACCCGCGCTGACGTGGCCCGGGCGGCGGGGGTGTCGCCCTCGACCGTCACCTACGTCCTGACCGGTCAGCGCTCGACGCGCTCGAGCACTCGGGAGCGGGTCATGCGGGCCGTGCGCGAGCTCGACTACCACCCCAACACCGCCGCCCGCTCACTGGCCTCACCGGTGCTGCGCACCGTGGGTGTCCTGTTCCGGCGCCAGCGCTCCATCATTGACGCCAACGACTTGGACTATGTCGACGGTGTGCGCCGCGCACTGGCGCCCAGCGGAATCCAGGTCGTCATCCCGGTCATGGCCGCCTCGACGCCGCTGATCGAGCTGCGCTCGCTCGTGCGCTCCGGCGCCCTGGGCGGGGTGGTTCTCATGGACGTGGCCGACGGTGATGACCGCGAGGCGATGCTGCTGGAGGACAAGGTCCCCACCGTCCTCATCGGCTCCTCGGATCGCGCCAGTGGGGCGCCCGGCATTGACGCGGACTTCGCCCAGATGGCCCGCGCCGGCGTGGAGCACCTGTCCGAACTCGGGCACCGTCGCATCGTCGCCCTCATGAGGGAGACCGCATCCGATGACGCTCACGCCCGCCAGGACCAGGCATATGAGCTCCTGCGTGCCGCGCAGGATCTGGAGGTGGAAGTCCTGGTGCGCCAGGTGCCCGAGGCGGCACTGGCCGGCGCCGAGATCGTGGGAGCCGGCGGCCTCATCGAGGGGTGCAGCGCAGTCCTGTCCAACAACCCCGCCGCCGTGGTGGGACTGGCCTGCGCGGCGCAGGCCCACGGGCTCTCTGTTCCCGCGGACCTGTCCGTGCTCACCCTCGGGATCTCGCAGGACAGCGGACGCCAGGAGGAGGCCTTCAGCGAGCTTAGCGTGGACCGTGAGGCCATGGGGGCCGAGGCGGGCTCACTCCTCCTGAGGTGCCTCTCAGGAGAACCGGACCCGGCCCAACGCCGCAGGCTCATGCCCGCCCTCCTCACCGACCGTGGTACCACGGCGCGCCATCAGGAATAG","MAATRADVARAAGVSPSTVTYVLTGQRSTRSSTRERVMRAVRELDYHPNTAARSLASPVLRTVGVLFRRQRSIIDANDLDYVDGVRRALAPSGIQVVIPVMAASTPLIELRSLVRSGALGGVVLMDVADGDDREAMLLEDKVPTVLIGSSDRASGAPGIDADFAQMARAGVEHLSELGHRRIVALMRETASDDAHARQDQAYELLRAAQDLEVEVLVRQVPEAALAGAEIVGAGGLIEGCSAVLSNNPAAVVGLACAAQAHGLSVPADLSVLTLGISQDSGRQEEAFSELSVDREAMGAEAGSLLLRCLSGEPDPAQRRRLMPALLTDRGTTARHQE$","Transcriptional regulator, LacI family","Cytoplasm","putative transcriptional regulator","LacI-family transcriptional regulator","regulatory protein, LacI","","Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 1992. 267(22):15869-15874. PMID: 1639817Vartak N.B., Reizer J., Reizer A., Gripp J.T., Groisman E.A., Wu L.F., Tomich J.M., Saier Jr M.H. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 1991. 142(9):951-963. PMID: 1805309","","","

InterPro
IPR000843
Domain

Bacterial regulatory protein, LacI
PF00356	$\"[3-28]T$	LacI
SM00354	$\"[2-72]T$	HTH_LACI
PS50932	$\"[3-57]T$	HTH_LACI_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[3-60]T$	no description
G3DSA:3.40.50.2300	$\"[61-201]T$	no description

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[28-444]T$	Alpha-amylase

InterPro
IPR006589
Domain

Glycosyl hydrolase, family 13, subfamily, catalytic region
SM00642	$\"[28-444]T$	Aamy

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[20-504]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[14-329]T$ $\"[346-363]T$ $\"[387-579]T$	AMYLASE
PTHR10357:SF11	$\"[14-329]T$ $\"[346-363]T$ $\"[387-579]T$	ALPHA-AMYLASE

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[75-282]T$	BPD_transp_1
PS50928	$\"[79-272]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[83-105]?$ $\"[114-134]?$ $\"[144-164]?$ $\"[195-215]?$ $\"[251-271]?$	transmembrane_regions

","BeTs to 13 clades of COG0395COG name: Sugar permeasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0395 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 75 to 282 (E_value = 4.3e-17) place ANA_1265 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter, permease components (AF175299)","","1","","","","","","","","","","","Tue Aug 14 12:47:47 2007","","Tue Aug 14 12:47:47 2007","","","Tue Aug 14 12:47:47 2007","","","","Tue Aug 14 12:47:47 2007","Tue Aug 14 12:47:47 2007","","","","","yes","","" "ANA_1266","1352581","1351544","1038","9.77","10.90","37747","ATGAGTACAACGACGCACTCCGAACAAGTCGTCAATCACCAGTCCAAGAGCTCCAAGGCCCAGGCCCGTCTGGCCTGGATACTCATCTCGCCCACGGTGCTGGTACTGACGATCGTCATCCTCATCCCCATCGCGCAGTCCCTCTACCAGTCGCTCTTCGGGCGGCCCCGGCTGGAGGACAACGGCTTCTTCTCCACCATCGAGCCCTTCGTGGGCCTGAAGAACTACACCGACATCTTCTCCAGCGCCGGTGAGCGGTTCTGGGTCGCCTTCTACAACACGACCCTCTTCGGCGTGGTCACCGTGGTCCTGGAGACCGTTCTGGGTGTGGCCATGGCGCTCATCATGCACAAGGCGATGAAGGGGCGCGGCATCGTGCGCGCCTCCATCCTCGTGCCCTGGGCGATTCCCACCGCCGTCTCCGCCATCCTGTGGGGCTGGATCTTCAACCAGAACGGCGTTGCCAACGCCATCCTGGGACGGCACGTCATGTGGGCCTCGGGGGACCTGAGTGCCAAGGCGGCCATCATCATCGCCGACGTGTGGAAGACGGCACCCTACATCGGGCTGCTCACCCTGGCCGGGCTCCAGCTCATCCCCGATGAGGTCTACGAGGCCGCCAAGATCGACGGCGCCAGCGCCTGGAAGCGGTTCACCTCCATCACCCTGCCACTGGTCAAGCCCGCGCTCGTCGTGGCCGTGGTCTTCCGCGCCCTGGACGCCCTGCGTATGTTCGACCTGCCCTACATCCTCATCGGCCCCAGAAAGGGCAGCGTGGAGACCCTCTCCATGCTGGTCCAGGACGAGAGCTCCAACTCGCGCTACGGCAGTGCCGCGGCCTATGCCCTCATCCTGTTCCTGTATGTCTTCGTCTTCGCGGTCGCGTTCTTGAAGATCACCAACACCGACATCAGCGGCAACGACGAGGCTCGGCGCAAGCGCAATGAGCGCAAGCTGCCGGTCAGCGCCTTCTTCAAGCGCTCCGGCTCCTCCACCCCGGCCTCCCAGACGGCTACTGAAAGGAGCCAGCAGGCATGA","MSTTTHSEQVVNHQSKSSKAQARLAWILISPTVLVLTIVILIPIAQSLYQSLFGRPRLEDNGFFSTIEPFVGLKNYTDIFSSAGERFWVAFYNTTLFGVVTVVLETVLGVAMALIMHKAMKGRGIVRASILVPWAIPTAVSAILWGWIFNQNGVANAILGRHVMWASGDLSAKAAIIIADVWKTAPYIGLLTLAGLQLIPDEVYEAAKIDGASAWKRFTSITLPLVKPALVVAVVFRALDALRMFDLPYILIGPRKGSVETLSMLVQDESSNSRYGSAAAYALILFLYVFVFAVAFLKITNTDISGNDEARRKRNERKLPVSAFFKRSGSSTPASQTATERSQQA$","ABC-type multiple sugar transport system, permease protein","Membrane, Cytoplasm","ABC-type transporter, permease components","K02025 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[87-304]T$	BPD_transp_1
PS50928	$\"[91-296]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-47]?$	signal-peptide
tmhmm	$\"[24-44]?$ $\"[95-115]?$ $\"[130-150]?$ $\"[277-297]?$	transmembrane_regions

","BeTs to 14 clades of COG1175COG name: ABC-type sugar transport systems, permease componentsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1175 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 87 to 304 (E_value = 2e-14) place ANA_1266 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter, permease components (AF175299)","","1","","","","","","","","","","","Tue Aug 14 12:48:08 2007","","Tue Aug 14 12:48:08 2007","","","Tue Aug 14 12:48:08 2007","","","","Tue Aug 14 12:48:08 2007","Tue Aug 14 12:48:08 2007","","","","","yes","","" "ANA_1267","1353964","1352672","1293","5.47","-7.92","47275","ATGACACCCTTACCCCGTCGTCAGTTCATCCAGGGCTCGGCCCTGGCTGCGGTGCTGGCCTCCGTCGGGGCCTGTTCCACCTCCCGCGGAGACGACGACGGTCCCGTCACCTTCGAAGGCACTGGACCAATCACCTGGGTCCAGGGCAAGGACAACTCGGGTGGCAAGGTGCAGGCCAGGCTCGATGAGTGGAACAAGGCCCATCCTGGTGAGGAGGTCAAGCTCATTGAGCTCTCCGCCGAGGCCGACCAGCAGCGCACCTCGTTCATCAATGCCGTCAGGATCAACTCCAACGCTTACGACGTCGTCTCCCTGGACAACGTCTGGGTCTCCGAGTTCGCCGCCAACCGGTGGGTGGTCGAGCTGCCCGAGGACGAGCTCAAGAACGACAACATCCTTGAACCCGTGTGGAAGACCGGGGTCTACAAGGACAAGGTCTTCGCGGTTCCCCATGCCACCGATGCGCCGGTGATGTTCTACCGCAAGGACTTCCTGGCTCAGGCCGGCGTCGAGGTCCCGACGACCTGGGACGAGGTCAAGGCTGCCATCGACAAGGTCCGGGCCCTTCCCGAGCACAAGAACATTGGTGGGTTCGGCGGTCAGTTCGCCAAGTATGAGGGCCTGACCTGCTGCGCCTCGGAGTTCATCCACACCGCCGGCGGTGGCTTCTACGACCCGGACAACCAGGTCATCGTTGACTCCACCGAGTCGGTCGCCGGCCTGCAGTGGCTCATCGACGGCTTCTCCCAGGGCTACATCCCCAAGGAGTCCCTGGAGTGGAAGGAGGAGGACGGTCGTAACGCCTTCGAGAAGGGCGACCTCCTCTTCTACCGTCAGTGGCCCTACCAGTACGCCAACAACAAGAAGTCCCTGGGGCCGGACAAGTTCGACGTCGCCGCCCTGCCGAGCATCGATGGCAAGCCATTCGTGCCGACCCTGGGTGGGCACAACTGCGCCATCACCAAGGGTTCCAAGAACAAGGCAACCGCCTTGAAGTTCCTCAAGTGGTGGATCGGCGAGGACTCCCAGCGCTATTCCCTCAAGGCCCAGGCGAACGCTCCGATCCTTGGATCCCTCTACGACGACCCCGAGCTCCTCAAGGAATTCCCCTACCTGCCGATTCTCAAGAAGAGCCTCGAGAACGCCAAGAGCCGTCCCCAGGCCGTCTACTACGGCGACGTCACCGCCAAGATTCAGGACAGCATCTACCCTGCGATCCAGCAGCCGGGGGGCAGGGCGGCCAAGGACGTCATCGCCGGCCTGAGCAGCAGCCTGAAGAAGCTGGAGGGCTAA","MTPLPRRQFIQGSALAAVLASVGACSTSRGDDDGPVTFEGTGPITWVQGKDNSGGKVQARLDEWNKAHPGEEVKLIELSAEADQQRTSFINAVRINSNAYDVVSLDNVWVSEFAANRWVVELPEDELKNDNILEPVWKTGVYKDKVFAVPHATDAPVMFYRKDFLAQAGVEVPTTWDEVKAAIDKVRALPEHKNIGGFGGQFAKYEGLTCCASEFIHTAGGGFYDPDNQVIVDSTESVAGLQWLIDGFSQGYIPKESLEWKEEDGRNAFEKGDLLFYRQWPYQYANNKKSLGPDKFDVAALPSIDGKPFVPTLGGHNCAITKGSKNKATALKFLKWWIGEDSQRYSLKAQANAPILGSLYDDPELLKEFPYLPILKKSLENAKSRPQAVYYGDVTAKIQDSIYPAIQQPGGRAAKDVIAGLSSSLKKLEG$","ABC-type multiple sugar transport system, substrate-binding protein","Extracellular, Periplasm, Cytoplasm","ABC-type transporter, periplasmic component","K02027 multiple sugar transport system substrate-binding protein","extracellular solute-binding protein, family 1","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[10-344]T$	SBP_bac_1

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[4-30]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[156-363]T$	no description
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 10 clades of COG1653COG name: Sugar-binding periplasmic proteins/domainsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1653 is -o-pkz--vdrlbcefghs--j--t-Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","-49% similar to PDB:1EU8 STRUCTURE OF TREHALOSE MALTOSE BINDING PROTEIN FROM THERMOCOCCUS LITORALIS (E_value = 2.7E_38);-40% similar to PDB:2OBG Crystal Structure of Monobody MBP-74/Maltose Binding Protein Fusion Complex (E_value = 3.1E_10);-43% similar to PDB:1MDQ REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN (E_value = 5.2E_10);-41% similar to PDB:1N3W Engineered High-Affinity Maltose-Binding Protein (E_value = 5.2E_10);-41% similar to PDB:1N3X Ligand-free High-Affinity Maltose-Binding Protein (E_value = 5.2E_10);","Residues 10 to 344 (E_value = 8e-28) place ANA_1267 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","transporter, periplasmic component (AF175299)","","1","","","","","","","","","","","Tue Aug 14 12:48:29 2007","","Tue Aug 14 12:48:29 2007","","","Tue Aug 14 12:48:29 2007","","","","Tue Aug 14 12:48:29 2007","Tue Aug 14 12:48:29 2007","","","","","yes","","" "ANA_1268","1354338","1356167","1830","7.12","0.82","65373","ATGGCCGGCGGGGTCTCCGGCACTGAAATCCCCTTCCAGCCCGAGGCGCACTGGTCGGTTCCGTGGCTGCTCGTCGACCGCATTGCGCGCAGCGGCGACCGGCCGCTCGTGGCCCGTAAGTCACCCCTGTCCGGGGACTGGCAGGAGGTCTCGGCCCGAGCCTTCGGCGAGGAGGTGGCCCACGTGGCCGCGGGTCTCATCGGCATGGGACTCGAGGCGGGCACCACCGTCGGCATCATGGCGCACACCTCCTACGACTGGTTCCTCCTGGACATGGCCATCGCCCGCGCGGGCCTCATCTCCGTGCCCATCTACGAGACGAGCTCAGCCGAGCAGGTCGAGTGGATCGTCACCGACTCCGACGTGCGTGTGGTCATCACCGAGAGCGGCACACTGGCCGAGCTCGTACGCGGCGCCGTCGCCGGTATCGAGCACACGGTGAGGATCCTCGCCCTGGACTCCGACGCGATCACCACCATCGTCCAGGCGGGCTCGGGCGTCAGCCCCTCCCAGGTCGACCAGCGCTCCAACGCCCTCACGGTCGACGACGTCTACTCCATCATTTACACCTCCGGCACCACGGGCCGCCCCAAGGGCGTCGAGCTCACCCATCGCAACGCCGTCGGCATCCCCTACCACGGGGTGCGCTACCTGCCCGGCGTCCTGTGGGGCACCAACGTGCGCCTGCTGCTCTTCCTGCCGCTGGCCCACGTCTACGCCCGATGCCTCCAGCTGCTGTCGCTGGCCGGCGAGGGTGTGCTGGGCCACACCCCCGACGCCAAGACTCTCCTGCCCGACCTGCAGTCCTTCGCCCCCTCCTACATCCTGGCCGTTCCACGCGTCCTGGAGAAGATCTACAACGCCGCCGACGCCAAGGCCGGCAGCGGCGCCAAGCTCAAGCTGTTCCGCTGGGCGGCCAAGGTCGCCATCGCCCACTCCCGTGCCCTGGACACCCCTCAGGGCCCCTCCCGCGGCCTGCGTCGGGCGCACGCCGTGGCCGACCGGCTCGTGTTCCGCAAGATCCGGGGACTCATGGGCCCCAACGCCCGCTTCATCATCTCCGGCGGAGGGCCGCTGGGACAGCGTCTGGGACACTTCTACCGCGGGCTGGGCCTGGTCATCCTGGAGGGTTACGGCCTGACCGAGACCATTGGCCCGGTCAGCGTCAACACCGACTGGCTCAACAAGATCGGCACCGTCGGCCCACCCGTCTGCGGCAACGAGATCCGCATCGGTGAGGATGACGAGATCCAGGTCCGCGGCATGGGAGTCTTCTCCACCTACCACAACAACCCCTCGGCCACCGCCGACGCCTTCACCGCCGACGGCTGGTTCCGCACCGGAGACATCGGCGCCCTCGATGATGACGGCTACCTGCGCATCACCGGACGCAAGAAGGAGCTCATCGTCACCGCCGGCGGCAAGAACGTCGCCCCCACCCAGCTCGAGGACCGCCTGCGCGGCCACCCGCTCATCAGCCAGGTGCTCGTCATCGGGGACGGGGAGCCCTTCATCTCCGCGCTCATCACCCTGGACAAGGAGATGCTCCCCCAGTGGCTGCGCAACCACGGGCTGCCGACCATGGACGTGGTCGAGGCCTCCTCCCACCCGCAGGTGCTCGCCGCCCTGGACCGGGCCGTGGCGCGCACGAACCGGGCGGTCTCCCGGGCCGAGTCGATCCGTACCTTCCGGGTACTGGCCACCGACTTCACCGAGGCCAACGGCCTGCTCACCCCGTCACTGAAGGTCAAGCGCGGCCCGGTCATGGAGGCCCACGCCGACGTCATCGCCGAGATCTACAGCTCCACGCGCAAAGGACCGCAGGAGTAA","MAGGVSGTEIPFQPEAHWSVPWLLVDRIARSGDRPLVARKSPLSGDWQEVSARAFGEEVAHVAAGLIGMGLEAGTTVGIMAHTSYDWFLLDMAIARAGLISVPIYETSSAEQVEWIVTDSDVRVVITESGTLAELVRGAVAGIEHTVRILALDSDAITTIVQAGSGVSPSQVDQRSNALTVDDVYSIIYTSGTTGRPKGVELTHRNAVGIPYHGVRYLPGVLWGTNVRLLLFLPLAHVYARCLQLLSLAGEGVLGHTPDAKTLLPDLQSFAPSYILAVPRVLEKIYNAADAKAGSGAKLKLFRWAAKVAIAHSRALDTPQGPSRGLRRAHAVADRLVFRKIRGLMGPNARFIISGGGPLGQRLGHFYRGLGLVILEGYGLTETIGPVSVNTDWLNKIGTVGPPVCGNEIRIGEDDEIQVRGMGVFSTYHNNPSATADAFTADGWFRTGDIGALDDDGYLRITGRKKELIVTAGGKNVAPTQLEDRLRGHPLISQVLVIGDGEPFISALITLDKEMLPQWLRNHGLPTMDVVEASSHPQVLAALDRAVARTNRAVSRAESIRTFRVLATDFTEANGLLTPSLKVKRGPVMEAHADVIAEIYSSTRKGPQE$","AMP-dependent synthetase and ligase","Cytoplasm","Long-chain acyl-CoA synthetases (AMP-forming)","AMP-dependent synthetase and ligase","AMP-dependent synthetase and ligase","","Smith D.J., Earl A.J., Turner G. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 1990. 9(9):2743-2750. PMID: 2118102Schroder J. Protein sequence homology between plant 4-coumarate:CoA ligase and firefly luciferase. Nucleic Acids Res. 1989. 17(1):460-460. PMID: 2911486Mallonee D.H., White W.B., Hylemon P.B. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 1990. 172(12):7011-7019. PMID: 2254270","","","

InterPro
IPR000873
Domain

AMP-dependent synthetase and ligase
PR00154	$\"[182-193]T$ $\"[194-202]T$	AMPBINDING
PF00501	$\"[51-497]T$	AMP-binding
PS00455	$\"[187-198]T$	AMP_BINDING

noIPR
unintegrated

unintegrated
G3DSA:2.30.38.10	$\"[397-462]T$	no description
G3DSA:3.40.50.980	$\"[15-205]T$	no description
PTHR11968	$\"[11-309]T$ $\"[350-519]T$ $\"[537-602]T$	ATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF10	$\"[11-309]T$ $\"[350-519]T$ $\"[537-602]T$	LONG-CHAIN-FATTY-ACID COA LIGASE

","BeTs to 12 clades of COG1022COG name: Long-chain acyl-CoA synthetases (AMP-forming)Functional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1022 is ao---zyq--r--c-fgh------t-Number of proteins in this genome belonging to this COG is 2","***** IPB000873 (AMP-binding signature) with a combined E-value of 5.3e-08. IPB000873A 182-193 IPB000873B 194-202","","","-40% similar to PDB:1ULT Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.3E_23);-40% similar to PDB:1V25 Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.3E_23);-40% similar to PDB:1V26 Crystal structure of tt0168 from Thermus thermophilus HB8 (E_value = 1.3E_23);-39% similar to PDB:2D1Q Crystal structure of the thermostable Japanese Firefly Luciferase complexed with MgATP (E_value = 3.3E_16);-39% similar to PDB:2D1R Crystal structure of the thermostable Japanese firefly Luciferase complexed with OXYLUCIFERIN and AMP (E_value = 3.3E_16);","Residues 51 to 497 (E_value = 1.8e-86) place ANA_1268 in the AMP-binding family which is described as AMP-binding enzyme.","","acyl-CoA synthetases (AMP-forming) (fadD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1269","1356308","1358116","1809","7.09","0.48","64501","ATGACGACTCCCTGGGCTCTGGCCGAGCGCGTGCGCCGCAGTCCCGACGGCGGGCTCATCGCCCGCAAGTCCCCCTTGGGGCGGCGTTGGCGGGAGATGAGCGCCAGTGCCTTCCGCACCCAGGTGCGTGAGGTGGCCGCGGGCCTGGTGGCCCGAGGACTTCAGCCCGGAGACGCCATCGGCATCATGTCGCACACGTCGTATGAGTGGACGCTGCTGGACTTCGCCGCCTGGGAGGCGGGCCTCGTCGTCGTCCCCGTCTACGAGACCTCCTCGGCCGAGCAGGCCCAGTGGATCCTCACCGACGCCGGCGTGAAGCTCATCGTCGTGGAGAACGAGGCCATGGCCGCCATGGTCGGCGCACTGACCTCCACCGTCCCCGAGCTGGAGAGCCTGCAGGTGCTGTGCATCGAGCGCGAGGACGTCCTGGGGCTCATCAGGGCCGGTCGAGGCGTGGACGCCGGCGAGCTCGACCGGCGCAGCACGGCCCTGACCTCTCAGTCCCTGGCCACCATCGTCTACACCTCCGGGACGACCGGGCGTCCCAAGGGTGTCGAGCTCAGCCACGGCAACCTCGTTCACCTATGCGTCAACGTCTGCCCGCACGTGCCCGAGGTCCTGGGCGGAGCCGAGGTCCGTTTCCTACTGTTCCTGCCCCTGGCCCACGTGCTTGGCCGGTTCGTGGAGATCGCGGTCGTCTGCTCGCGCTCGGGCGTACTGGGGCACGTGCCCGACGTGCGTAATCTCCTCAACGACCTGGGCTCCTTCCGCCCCACCGCGGTCCTGGCCGTCCCCCGGGTGTTCGAGAAGATCTATAACGCCGCCGATGCCAAGGCGACCGGCGCCAAGCAGAAGGTCTTCCGCCTGGCGGCCAAGACCGCGATCGCCTACTCGCGAGCCCTGGACACCCCTGAGGGCCCGTCGCGCCGCCTCAAGGCGCAGCGCGCCGCCTTCGACAAGCTCGTCTTCTCCACCCTGCGCTCCGTACTGGGCGGGCAGGTCACGCACGTGGTCTCCGGTGGCGGGCCTCTGGGCGAGCGCCTGGGGCACTTCTACCGCGGCGCCGGAGTCACCGTCCTGGAGGGCTACGGCCTGACCGAGACCATGGGGCCGTGCAGCGTCAACCTGCCCGAGGCCACCCGGATCGGGACCGTGGGTACCCCGCTGCCCGGCTGCTCGATCCGACTGGACGACGACGGGGAGATCCTGGTTCGGGGCATCGGCACCTTCACGGGCTACCACAACAACCCCGAGGCCACGGCCGAGGCCTTCACCGACGACGGCTGGCTGCGCACCGGGGACATCGGCTCCTTCGAAGGCGCCGAGGGTTTCCTGCGGATCACCGGTCGCAAGAAGGAGCTCATCGTCACCGCCGGGGGCAAGAACGTCGCCCCGGCCCCTCTGGAGGACCGCCTGCGGGGTCACCCGCTGGTCAGTCAGGTGCTCGTCGTCGGGGAGAACCGTCCCTGCATCGGTGCGCTCCTCACCCTGGATGCGGAGATGTTGCCTCTGTGGCTGTCCTCCCACGGGCTGGAGGAGATGACTGTCGTCGACGCCGCCCGGGACCCACGGGTGCGCGCCGCCCTGGAGAAGGCGGTGGCCCGGACCAACGAGGCGGTCTCACGGGCGGAGTCGATCCGCACCTTCGAGGTGCTGCCCACGGACTTCACCGTGGCCAACGGCTTGCTGACTCCCTCGCTCAAGGTACGCCGCGCCGAGGCGGAGAAGCGCTTCTCGGCCGAGATCGAGGCGCTCTACACGCGTACCCCGCTCATCCCCAGCACCACCGTCTCACCGTTGCAGGACTGA","MTTPWALAERVRRSPDGGLIARKSPLGRRWREMSASAFRTQVREVAAGLVARGLQPGDAIGIMSHTSYEWTLLDFAAWEAGLVVVPVYETSSAEQAQWILTDAGVKLIVVENEAMAAMVGALTSTVPELESLQVLCIEREDVLGLIRAGRGVDAGELDRRSTALTSQSLATIVYTSGTTGRPKGVELSHGNLVHLCVNVCPHVPEVLGGAEVRFLLFLPLAHVLGRFVEIAVVCSRSGVLGHVPDVRNLLNDLGSFRPTAVLAVPRVFEKIYNAADAKATGAKQKVFRLAAKTAIAYSRALDTPEGPSRRLKAQRAAFDKLVFSTLRSVLGGQVTHVVSGGGPLGERLGHFYRGAGVTVLEGYGLTETMGPCSVNLPEATRIGTVGTPLPGCSIRLDDDGEILVRGIGTFTGYHNNPEATAEAFTDDGWLRTGDIGSFEGAEGFLRITGRKKELIVTAGGKNVAPAPLEDRLRGHPLVSQVLVVGENRPCIGALLTLDAEMLPLWLSSHGLEEMTVVDAARDPRVRAALEKAVARTNEAVSRAESIRTFEVLPTDFTVANGLLTPSLKVRRAEAEKRFSAEIEALYTRTPLIPSTTVSPLQD$","AMP-dependent synthetase and ligase","Cytoplasm, Membrane","Long-chain acyl-CoA synthetases (AMP-forming)","AMP-dependent synthetase and ligase","AMP-dependent synthetase and ligase","","Smith D.J., Earl A.J., Turner G. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 1990. 9(9):2743-2750. PMID: 2118102Schroder J. Protein sequence homology between plant 4-coumarate:CoA ligase and firefly luciferase. Nucleic Acids Res. 1989. 17(1):460-460. PMID: 2911486Mallonee D.H., White W.B., Hylemon P.B. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 1990. 172(12):7011-7019. PMID: 2254270","","","

InterPro
IPR000873
Domain

AMP-dependent synthetase and ligase
PR00154	$\"[167-178]T$ $\"[179-187]T$	AMPBINDING
PF00501	$\"[34-483]T$	AMP-binding
PS00455	$\"[172-183]T$	AMP_BINDING

noIPR
unintegrated

unintegrated
G3DSA:2.30.38.10	$\"[382-447]T$	no description
G3DSA:3.40.50.980	$\"[1-189]T$ $\"[191-378]T$	no description
PTHR11968	$\"[7-271]T$ $\"[304-505]T$ $\"[523-588]T$	ATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF10	$\"[7-271]T$ $\"[304-505]T$ $\"[523-588]T$	LONG-CHAIN-FATTY-ACID COA LIGASE

InterPro
IPR002701
Domain

Chorismate mutase
PF01817	$\"[16-96]T$	CM_2
PS51168	$\"[6-97]T$	CHORISMATE_MUT_2

InterPro
IPR010951
Family

Chorismate mutase, bacteria
TIGR01795	$\"[8-101]T$	CM_mono_cladeE: chorismate mutase

noIPR
unintegrated

unintegrated
G3DSA:1.20.59.10	$\"[12-84]T$	no description

","BeTs to 12 clades of COG1605COG name: Chorismate mutaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1605 is aomp-zyqvdrlb-efghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002701 (Chorismate mutase) with a combined E-value of 1.1e-12. IPB002701 12-44","","","No significant hits to the PDB database (E-value < E-10).","Residues 16 to 96 (E_value = 5.9e-14) place ANA_1270 in the CM_2 family which is described as Chorismate mutase type II.","","mutase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1271","1359855","1358575","1281","5.25","-10.93","45833","GTGGATCTGCTCAAGTGCTCCTTCTGCGGCAAGAGCCAGAAGCAGGTCAAGAAGCTCATCGCCGGGCCCGGTGTTTACATCTGCGACGAGTGCATCGAGCTGTGCAACGAGATCGTTGACGAGGAGCTGAGTGATTCAGGCGCCGGTGTGCCTCTCGAGCTTCCTAAGCCCCAAGAGATCTTCGACTTCCTCAATCAGTACGTCATCGGTCAGGAGGCCGCCAAGCGCGCCATGAGCGTGGCGGTCTACAACCACTACAAGCGTGTCCAGGTCAAGGAGCGATCCGTGGCCGAGGGGGATGGCCTGGAGCTGGGCAAGTCCAACATCCTCCTGCTGGGGCCCACCGGAACCGGTAAGACTCACCTGGCCCGAACCCTCGCCCGCCTCCTGGACGTCCCCTTCGCCATTGTTGATGCCACGGCTCTGACCGAGGCGGGGTATGTCGGCGAGGATGTGGAGAACATCCTCCTCAAGCTCATCCAGGCCGCTGACGGTGACGTCAAGCGTGCTGAGAAGGGCATCATCTACATCGATGAGATCGACAAGATCGGTCGCAAGGCGGAGAACCCCTCGATCACCCGCGACGTCTCAGGTGAGGGCGTCCAGCAGGCACTGCTCAAGATTATCGAGGGGACAACGGCCTCCGTGCCGCCCGGCGGCGGGCGCAAGCACCCGCACCAGGAGTTCCTGGAGATCGATACCACCAATATTCTCTTCATTGCCGCAGGAGCCTTTGCCGGTATTGAGGAGATCGTGCGTCAGCGTCAGCGTAAGGAGTCCGGAGCCCAGATGGTGGGCTTTGGAGCGCAGTTGACCGGCAGCACGGCCTCACAGGACGTCTTCACCTCACCGGTGCGCCCCGAGGACCTTCACAAGTTCGGCCTCATCCCCGAGTTCATCGGCCGTCTTCCCGTCATCGCCACGGTTCAGGATCTGGGCGTACGTGAGCTCGTGCGCGTCATGACCGAGCCCAAGAACGCTCTGGTCTCCCAGTACCAGTACCTCTTCAGTCTCGACGGCGTCGAGCTCGAGCTGACCGATGCCGCTATTGAGGCGGTGGCCTCCCTCGCCCTGGAGCGCAAGACCGGTGCTCGGGGGCTGACCTCCATCGTCGAGGAGGTCCTGGGGCAGGCCATGTTCGAGGTTCCCTCCCTGCCTGAGGTCGGGCGCGTCGTCGTCGATGCCGATGCCGTCAGGGGTACCGGGAAGCCCAGTTACCAGTCCGGATCGGGGACGCTGCGCTCGACGAGCAAGATGGGGGAGCGGAGCCGGACCGCATGA","VDLLKCSFCGKSQKQVKKLIAGPGVYICDECIELCNEIVDEELSDSGAGVPLELPKPQEIFDFLNQYVIGQEAAKRAMSVAVYNHYKRVQVKERSVAEGDGLELGKSNILLLGPTGTGKTHLARTLARLLDVPFAIVDATALTEAGYVGEDVENILLKLIQAADGDVKRAEKGIIYIDEIDKIGRKAENPSITRDVSGEGVQQALLKIIEGTTASVPPGGGRKHPHQEFLEIDTTNILFIAAGAFAGIEEIVRQRQRKESGAQMVGFGAQLTGSTASQDVFTSPVRPEDLHKFGLIPEFIGRLPVIATVQDLGVRELVRVMTEPKNALVSQYQYLFSLDGVELELTDAAIEAVASLALERKTGARGLTSIVEEVLGQAMFEVPSLPEVGRVVVDADAVRGTGKPSYQSGSGTLRSTSKMGERSRTA$","ATP-dependent Clp protease, ATP-binding subunit ClpX","Cytoplasm","ATP-dependent Clp protease, ATP-binding subunitClpX","ATP-dependent Clp protease; ATP-binding subunit ClpX","ATP-dependent Clp protease, ATP-binding subunit ClpX","","Morett E., Segovia L. The sigma 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol. 1993. 175(19):6067-6074. PMID: 8407777Austin S., Kundrot C., Dixon R. Influence of a mutation in the putative nucleotide binding site of the nitrogen regulatory protein NTRC on its positive control function. Nucleic Acids Res. 1991. 19(9):2281-2287. PMID: 2041769Albright L.M., Huala E., Ausubel F.M. Prokaryotic signal transduction mediated by sensor and regulator protein pairs. Annu. Rev. Genet. 1989. 23:311-336. PMID: 2694934Austin S., Dixon R. The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent. EMBO J. 1992. 11(6):2219-2228. PMID: 1534752","","","

InterPro
IPR002078
Domain

RNA polymerase sigma factor 54, interaction
PS00676	$\"[165-180]T$	SIGMA54_INTERACT_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[105-328]T$	AAA

InterPro
IPR004487
Family

ClpX, ATPase regulatory subunit
PTHR11262:SF4	$\"[2-420]T$	ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX
TIGR00382	$\"[1-407]T$	clpX: ATP-dependent Clp protease, ATP-bindi

InterPro
IPR010603
Domain

Zinc finger, C4-type
PF06689	$\"[3-42]T$	zf-C4_ClpX

InterPro
IPR013093
Domain

ATPase AAA-2
PF07724	$\"[104-306]T$	AAA_2

InterPro
IPR013991
Domain

PhnA protein N-terminal, proteobacterial
SM00782	$\"[2-33]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.60	$\"[311-410]T$	no description
G3DSA:3.40.50.300	$\"[46-310]T$	no description
PTHR11262	$\"[2-420]T$	HSL AND CLP PROTEASE

","BeTs to 18 clades of COG1219COG name: ATP-dependent protease Clp, ATPase subunitFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1219 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB010603 (ClpX C4-type zinc finger) with a combined E-value of 1.2e-192. IPB010603A 6-39 IPB010603B 54-89 IPB010603C 103-151 IPB010603D 181-234 IPB010603E 287-316 IPB010603F 343-384***** IPB000641 (CbxX/CfqX superfamily signature) with a combined E-value of 5.6e-33. IPB000641A 64-78 IPB000641B 108-123 IPB000641C 144-158 IPB000641D 162-181 IPB000641E 198-210 IPB000641F 281-298 IPB000641G 298-317 IPB000641H 363-375***** IPB003960 (AAA-protein subdomain) with a combined E-value of 1.4e-08. IPB003960B 106-127 IPB003960C 152-187***** IPB000642 (Peptidase M41) with a combined E-value of 2.2e-08. IPB000642A 89-138 IPB000642B 146-188***** IPB013093 (ATPase AAA-2) with a combined E-value of 1.4e-07. IPB013093G 105-127 IPB013093B 106-127***** IPB000523 (Magnesium chelatase, ChlI subunit) with a combined E-value of 9.4e-07. IPB000523A 89-131","","","-69% similar to PDB:1UM8 Crystal structure of helicobacter pylori ClpX (E_value = 3.9E_90);-52% similar to PDB:1OFH ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE) (E_value = 2.2E_40);-52% similar to PDB:1OFI ASYMMETRIC COMPLEX BETWEEN HSLV AND I-DOMAIN DELETED HSLU (H. INFLUENZAE) (E_value = 2.2E_40);-60% similar to PDB:1G3I CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX (E_value = 3.3E_20);-60% similar to PDB:1G41 CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE (E_value = 3.3E_20);","Residues 3 to 42 (E_value = 1.7e-26) place ANA_1271 in the zf-C4_ClpX family which is described as ClpX C4-type zinc finger.Residues 104 to 306 (E_value = 9.3e-81) place ANA_1271 in the AAA_2 family which is described as ATPase family associated with various cellular activities (AAA).Residues 108 to 318 (E_value = 1.7e-06) place ANA_1271 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).Residues 108 to 137 (E_value = 1.5e-07) place ANA_1271 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).","","Clp protease, ATP-binding subunit ClpX (clpX)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1272","1360803","1360129","675","5.19","-7.10","24516","ATGTCCTCGACCCGTCCCTACTTCGAGGCCATCGCCCGTCAGGCAGGTGCCATGCCGCAGGCCCGCTACGTGCTGCCCCAGTTCGAGGAGCGCACCGCCTACGGCTTCAAGCGTCAGGACCCCTACGCCAAGCTCTTCGAGGACCGCATCGTCTTCATGGGCGTCCAGGTCGACGATGCCTCCGCCGATGACATCATGGCTCAGCTCCTGGTCCTGGAGTCCCAGGACCCCGATGGTCTCATCACCATGTACATCAACAGTCCCGGCGGCTCCTTCACGGCGCTGACGGCCATCTACGACACCATGCAGTACATCAAGCCGCAGGTGCAGACCGTCTGCCTGGGGCAGGCGGCCTCCGCCGCTGCCGTGCTCCTGGCCGCCGGAAGTGAGGGCAAGCGGCTGGCCCTGCCCAACGCGCGCGTTCTCATCCACCAGCCCGCTATGGAGGGAGTGCAGGGGCAGGCCAGCGACATCGAGATCGTCGCCAACGAGATCGACCGCATGCGCTCCTGGCTGGAGGACACCCTGGCCGCGCACACCGGCCGGGACCGCGAGAAGATCCACGCCGACCTCGAGCGAGACAAGATTCTCACGGCTGCAGATGCCAAGGAGTACGGGATCGTGGACCAGGTGCTCACTTCTCGTAAGGCCCCCGCCTCTCCGCACTCCTCCTGA","MSSTRPYFEAIARQAGAMPQARYVLPQFEERTAYGFKRQDPYAKLFEDRIVFMGVQVDDASADDIMAQLLVLESQDPDGLITMYINSPGGSFTALTAIYDTMQYIKPQVQTVCLGQAASAAAVLLAAGSEGKRLALPNARVLIHQPAMEGVQGQASDIEIVANEIDRMRSWLEDTLAAHTGRDREKIHADLERDKILTAADAKEYGIVDQVLTSRKAPASPHSS$","ATP-dependent Clp protease, proteolytic subunit ClpP","Cytoplasm","ATP-dependent Clp protease, proteolytic subunitClpP","ATP-dependent Clp protease proteolytic subunit ","Endopeptidase Clp","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 1990. 265(21):12536-12545. PMID: 2197275","","","

InterPro
IPR001907
Family

Peptidase S14, ClpP
PR00127	$\"[40-55]T$ $\"[80-100]T$ $\"[111-128]T$ $\"[132-151]T$ $\"[190-209]T$	CLPPROTEASEP
PTHR10381	$\"[77-215]T$	PROTEASE FAMILY S14 CLPP PROTEASE
PF00574	$\"[35-215]T$	CLP_protease
PS00381	$\"[111-122]T$	CLP_PROTEASE_SER
PS00382	$\"[133-146]T$	CLP_PROTEASE_HIS

noIPR
unintegrated

unintegrated
G3DSA:3.90.226.10	$\"[23-216]T$	no description

","BeTs to 17 clades of COG0740COG name: Protease subunit of ATP-dependent Clp proteasesFunctional Class: N [Cellular processes--Cell motility and secretion] Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0740 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001907 (Clp protease) with a combined E-value of 7.9e-81. IPB001907A 39-73 IPB001907B 75-111 IPB001907C 112-146 IPB001907D 168-211","","","-70% similar to PDB:1TYF THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS (E_value = 7.2E_46);-70% similar to PDB:1YG6 ClpP (E_value = 7.2E_46);-70% similar to PDB:2FZS Crystal structure of E. coli ClpP with a Peptide Chloromethyl Ketone Covalently Bound at the Active Site (E_value = 7.2E_46);-69% similar to PDB:1YG8 The structure of a V6A variant of ClpP. (E_value = 1.2E_45);-61% similar to PDB:1Y7O The structure of Streptococcus pneumoniae A153P ClpP (E_value = 3.6E_37);","Residues 35 to 215 (E_value = 2.8e-100) place ANA_1272 in the CLP_protease family which is described as Clp protease.","","Clp protease, proteolytic subunit ClpP (clpP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1273","1361443","1360805","639","5.02","-9.63","22607","GTGAGCGAGCTCTACACACCCGCTGCGGTCGCCCCTCCTCAGGCAGCCGACGCCGCAGGCGCGGGTCTGGGGTTGACCGACTCCATCTACAACCGCCTCCTCAAGGAGCGCATCATCTGGCTCGGCTCTGAGGTGCGTGACGACAACGCCAACGCCATCTGCGCTCAGATGCTGCTGCTGGCAGCCGAGGATCCCGAGCGGGACATCTACCTCTACATCAACAGCCCCGGCGGCTCGGTGACTGCCGGTATGGCCATCTATGACACCATGCAGTACGTCCAGCCCGACGTCGCCACCGTGGCCACGGGGCTGGCTGCGTCCATGGGGCAGCACCTGTTGTCGGCCGGCGCCAAGGGCAAGCGCTACCTCACTCCTCACGCCCGCGTGCTCATGCACCAGCCCTCCGGAGGTGCAGGGGGTTCAGCCACCGACATCCGCATCAATGCCGACCTCATCATCAAGATGAAGCAAGAGCTCGCGGAGATCACCGCGGCCAACACCGGGCACACGGTGGAGGAGATCATCGCCGACTCCGATCGCGACCACTGGTTCTCGGCCCAGGAGGCCCTGGAGTACGGCTTCGTCGACCACATCGTGCGCTCCAGCCGGGAGATCGGCAAGCAGAACGGAGACAACTGA","VSELYTPAAVAPPQAADAAGAGLGLTDSIYNRLLKERIIWLGSEVRDDNANAICAQMLLLAAEDPERDIYLYINSPGGSVTAGMAIYDTMQYVQPDVATVATGLAASMGQHLLSAGAKGKRYLTPHARVLMHQPSGGAGGSATDIRINADLIIKMKQELAEITAANTGHTVEEIIADSDRDHWFSAQEALEYGFVDHIVRSSREIGKQNGDN$","ATP-dependent Clp protease proteolytic subunit1","Cytoplasm","ATP-dependent Clp protease proteolytic subunit1","endopeptidase Clp ","Endopeptidase Clp","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 1990. 265(21):12536-12545. PMID: 2197275","","","

InterPro
IPR001907
Family

Peptidase S14, ClpP
PR00127	$\"[28-43]T$ $\"[68-88]T$ $\"[99-116]T$ $\"[120-139]T$ $\"[177-196]T$	CLPPROTEASEP
PTHR10381	$\"[65-205]T$	PROTEASE FAMILY S14 CLPP PROTEASE
PF00574	$\"[22-202]T$	CLP_protease
PS00382	$\"[121-134]T$	CLP_PROTEASE_HIS

noIPR
unintegrated

unintegrated
G3DSA:3.90.226.10	$\"[29-203]T$	no description

","BeTs to 17 clades of COG0740COG name: Protease subunits of ATP-dependent proteases, ClpP familyFunctional Class: OThe phylogenetic pattern of COG0740 is -----qvCebRhuj--OLINxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-75% similar to PDB:2C8T THE 3.0 A RESOLUTION STRUCTURE OF CASEINOLYTIC CLP PROTEASE 1 FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.5E_61);-75% similar to PDB:2CBY CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 5.9E_61);-75% similar to PDB:2CE3 CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 5.9E_61);-78% similar to PDB:1TYF THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS (E_value = 1.2E_53);-78% similar to PDB:1YG6 ClpP (E_value = 1.2E_53);","Residues 130 to 310 (E_value = 2.5e-106) place ANA_1273 in the CLP_protease family which is described as Clp protease.","","Clp protease proteolytic subunit 1","","1","","","Thu Aug 2 18:02:49 2007","","Thu Aug 2 18:02:49 2007","","","Thu Aug 2 18:02:49 2007","Thu Aug 2 18:02:49 2007","Thu Aug 2 18:02:49 2007","","","Thu Aug 2 18:02:49 2007","","","Thu Aug 2 18:02:49 2007","Thu Aug 2 18:02:49 2007","","","Thu Aug 2 18:02:49 2007","Thu Aug 2 18:02:49 2007","","","","","yes","","" "ANA_1274","1361755","1362123","369","4.87","-5.60","13063","ATGTCCCCCTCATCCAGCACCCCCTCCACCGAGTCCCTGTTCCGACTCGGCCTCAACGCCGCCCTGCCCATCTCCGAGGAGGCGACCACCTCACGGGTCGTCGTCAACAACGAGATTCTGCGCACCGTCGTCTTCACCTTCGACGCCGGTCAGGTCCTCACCGAGCACTCCTCCCCCAGGGCGGTGATCGTCACGCTCCTGGAGGGCGAGATGGACTTCTCCATCGGCGAGCGCACCGAGCGGATGGGCGCCGGGGACGTCATCTACCTGGCACCCGGTGACCGTCACGCGCTGACGGCCGTGACGCCGTGCCGCATGCAGCTGGTGATGGTCGACGTCGACAAGGCCGCAGCAGCGAACGAGAAGTAG","MSPSSSTPSTESLFRLGLNAALPISEEATTSRVVVNNEILRTVVFTFDAGQVLTEHSSPRAVIVTLLEGEMDFSIGERTERMGAGDVIYLAPGDRHALTAVTPCRMQLVMVDVDKAAAANEK$","Cupin 2 domain protein","Cytoplasm, Membrane","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","Cupin 2, conserved barrel domain protein","","Giraud M.F., Leonard G.A., Field R.A., Berlind C., Naismith J.H. RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase. Nat. Struct. Biol. 2000. 7(5):398-402. PMID: 10802738Woo E.J., Dunwell J.M., Goodenough P.W., Marvier A.C., Pickersgill R.W. Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat. Struct. Biol. 2000. 7(11):1036-1040. PMID: 11062559Woo E.J., Marshall J., Bauly J., Chen J.G., Venis M., Napier R.M., Pickersgill R.W. Crystal structure of auxin-binding protein 1 in complex with auxin. EMBO J. 2002. 21(12):2877-2885. PMID: 12065401Adachi M., Takenaka Y., Gidamis A.B., Mikami B., Utsumi S. Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 2001. 305(2):291-305. PMID: 11124907Pochapsky T.C., Pochapsky S.S., Ju T., Mo H., Al-mjeni F., Maroney M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 2002. 9(12):966-972. PMID: 12402029Fusetti F., Schroter K.H., Steiner R.A., Van noort P.I., Pijning T., Rozeboom H.J., Kalk K.H., Egmond M.R., Dijkstra B.W. Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus. Structure 2002. 10(2):259-268. PMID: 11839311Cleasby A., Wonacott A., Skarzynski T., Hubbard R.E., Davies G.J., Proudfoot A.E., Bernard A.R., Payton M.A., Wells T.N. The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution. Nat. Struct. Biol. 1996. 3(5):470-479. PMID: 8612079Titus G.P., Mueller H.A., Burgner J., Rodriguez de cordoba S., Penalva M.A., Timm D.E. Crystal structure of human homogentisate dioxygenase. Nat. Struct. Biol. 2000. 7(7):542-546. PMID: 10876237","","","

InterPro
IPR013096
Domain

Cupin 2, conserved barrel
PF07883	$\"[43-112]T$	Cupin_2

InterPro
IPR014710
Domain

RmlC-like jelly roll fold
G3DSA:2.60.120.10	$\"[35-111]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-53% similar to PDB:1YHF X-ray crystal structure of conserved hypothetical SPy1581 protein from Streptococcus pyogenes. (E_value = 1.6E_10);","Residues 43 to 112 (E_value = 1.5e-10) place ANA_1274 in the Cupin_2 family which is described as Cupin domain.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1276","1362698","1363831","1134","9.39","12.50","43200","ATGATCGTCATTACCCTGCTGGTGGGAATCCTGTTCTGGATCGGAATTGACATCTGGGCCGGCATTACCTCAAAGTGGTACAAAGCCGTGGAGCTGAATCCGAACATCACCTCGGACGACTTCAGCGTTCTGGTACCGATCTACGGCAACGTCAAGTACTTGCAGAACGCGGATTATCTGCACCCTTATGGAGATCGAGTAGTCCTGTGCACCACATCTGGTGAGTCCGAGGAGTTCTACCGCGACCTGGAGGACATCGCCATTCGCTACGGGTTCAGAATCTTCCGCAGCAACTACGTCCCACGGAAGGTAGGGCGCAAGCGGAGCACCTCGGGAATCACCCGGGACACGGTTGTCCGCGACGCACTGCTGGCCGCCCCCCTCAACTCCTACATCGTCTGCCTTGACGCCGATACTACGGCGCAGGAGCCGCTGACCCACATCATCGGCGCCCTGGTGGCCAACAAGGCCGACTTCGCCTCGGTCACCATCGTGCCTCAGAAGAAGGGGCCCTTCATCGTCCAGATGCAGCGCCACGAGTACGTGGTCTCGATGCGCGCACGCAGAATCATGCCGTGGCTGCTCAGCGGCGCCCTTCACATCGGCAAGACCGACGTCATGCGCCAGATCATGGCCCGCCACTCACTGTTCTTCCAGGGCAATGACATCGAGTCCGGGATTATCGGAGACGCACTGGGATACAAGGCCGTTCACATTCTTGCCCACGTCAACACCAACGCGCCGGACACCCTGTACTCCTGGTGGCGCCAGCGGATCGCCTGGAGCGGCGGTTCCTTCAGGCTCTTCATCATCAACTTCAGGTTCGTCTTCCAGCACCCCTTCCTGTGGCTGTACAGCGGTATCGTGGTCATCAGCATGTTTGTGCTCAGGTGGATAGCAGTCGTGAATCCCGGATGGACACTCCTGCTGGCACTGTTCATCTACTATGCCGCCATCGTGTGGCTTCACTGGGACCACGGCAACAAGTGGCTGATCTTCCAGCCCTTCTACTGCCTCTTCGTCAGCCTCATCGTGGTGCCCATCGGCGTTGCCTACTATTTCAAGATGGCCATTCCTGAGCACAACTTCGGAGTCATTCGTCCCAAGCGCAAGGAGCTTGTCACAGCGAACTGA","MIVITLLVGILFWIGIDIWAGITSKWYKAVELNPNITSDDFSVLVPIYGNVKYLQNADYLHPYGDRVVLCTTSGESEEFYRDLEDIAIRYGFRIFRSNYVPRKVGRKRSTSGITRDTVVRDALLAAPLNSYIVCLDADTTAQEPLTHIIGALVANKADFASVTIVPQKKGPFIVQMQRHEYVVSMRARRIMPWLLSGALHIGKTDVMRQIMARHSLFFQGNDIESGIIGDALGYKAVHILAHVNTNAPDTLYSWWRQRIAWSGGSFRLFIINFRFVFQHPFLWLYSGIVVISMFVLRWIAVVNPGWTLLLALFIYYAAIVWLHWDHGNKWLIFQPFYCLFVSLIVVPIGVAYYFKMAIPEHNFGVIRPKRKELVTAN$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[259-277]?$ $\"[281-301]?$ $\"[306-324]?$ $\"[334-354]?$	transmembrane_regions

InterPro
IPR001179
Domain

Peptidyl-prolyl cis-trans isomerase, FKBP-type
PF00254	$\"[158-218]T$	FKBP_C
PS50059	$\"[167-249]T$	FKBP_PPIASE

InterPro
IPR005215
Family

Trigger factor
PIRSF003095	$\"[1-431]T$	FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor)
TIGR00115	$\"[1-413]T$	tig: trigger factor

InterPro
IPR008880
Domain

Bacterial trigger factor, C-terminal
PF05698	$\"[239-400]T$	Trigger_C

InterPro
IPR008881
Domain

Bacterial trigger factor, N-terminal
PF05697	$\"[1-151]T$	Trigger_N

noIPR
unintegrated

unintegrated
G3DSA:3.10.50.40	$\"[150-249]T$	no description
G3DSA:3.30.70.1050	$\"[1-118]T$	no description

","BeTs to 18 clades of COG0544COG name: FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor)Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0544 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB008880 (Bacterial trigger factor, C-terminal) with a combined E-value of 1.1e-14. IPB008880A 40-59 IPB008880B 193-241","","","-47% similar to PDB:1T11 Trigger Factor (E_value = 2.9E_19);-45% similar to PDB:1W26 TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR CRADLE FOR NASCENT PROTEINS (E_value = 9.4E_18);","Residues 1 to 151 (E_value = 1.7e-50) place ANA_1277 in the Trigger_N family which is described as Bacterial trigger factor protein (TF).Residues 158 to 238 (E_value = 0.00011) place ANA_1277 in the FKBP_C family which is described as FKBP-type peptidyl-prolyl cis-trans isomerase.Residues 239 to 400 (E_value = 1.3e-24) place ANA_1277 in the Trigger_C family which is described as Bacterial trigger factor protein (TF) C-terminus.","","factor (tig)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1280","1366006","1365842","165","11.84","10.91","6379","ATGGCAGTGCCGAAGCGGAAGATGTCCCGCAGCAACACCCGCAACCGCCGCTCACAGTGGAAGGCGAAGCTCACCGAGCTCACCACCATCCGCGTCCAGGGCCGCGAGATCTCCGTCCCTCGCCGTCTGGCGCGGGCCTACAAGGAGGGCCTCATCGAGCAGTGA","MAVPKRKMSRSNTRNRRSQWKAKLTELTTIRVQGREISVPRRLARAYKEGLIEQ$","Ribosomal protein L32","Extracellular, Cytoplasm","ribosomal protein L32, putative","K02911 large subunit ribosomal protein L32","ribosomal protein L32","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Vilardell J., Warner J.R. Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA. Mol. Cell. Biol. 1997. 17(4):1959-1965. PMID: 9121443","","","

InterPro
IPR002677
Family

Ribosomal L32p protein
PF01783	$\"[2-54]T$	Ribosomal_L32p
TIGR01031	$\"[2-28]T$	rpmF_bact: ribosomal protein L32

","BeTs to 4 clades of COG0333COG name: Ribosomal protein L32Functional Class: JThe phylogenetic pattern of COG0333 is ----yqvceb-hujgpolinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 110 (E_value = 5.1e-07) place ANA_1280 in the Ribosomal_L32p family which is described as Ribosomal L32p protein family.","","protein L32, putative","","1","","","Thu Aug 2 18:12:40 2007","","Thu Aug 2 18:12:40 2007","","","Thu Aug 2 18:12:40 2007","Thu Aug 2 18:12:40 2007","Thu Aug 2 18:12:40 2007","","","Thu Aug 2 18:12:40 2007","","","Thu Aug 2 18:12:40 2007","Thu Aug 2 18:12:40 2007","","","Thu Aug 2 18:12:40 2007","Thu Aug 2 18:12:40 2007","","","","","yes","","" "ANA_1281","1366163","1366951","789","6.05","-5.71","27322","ATGGCCCCGCACGCCCCTCGCACACCATCGCACCAGCCGTCTCAGGAGCAGTCATCCCCCGGACTCATCACCCTGGCCCGCGGCGAGCAGCCCGAGATCGACCTGGAGATCAAGAAGTCCCACTTCCTGGCACGCGCCTGCCGCACGGACTCCATGGACGAGGCTCGGAGCTTCATTGCGGACGTGCGCTCCACCTACCCCGATGCGCGCCACCACTGCTCGGCGCTGACGCTCACCGATCTCTCCGACGGACACGCCCTGGCCGCTCCTGCCCCACCCACCGAGCGCTCCAACGACGACGGCGAGCCCTCCGGCACGGCCGGCCAGCCCATGCTCGACATCCTGAGGGGAACGGGACTGGCCAACACGACCGTCGTCGTCACCCGTTACTTCGGCGGAACGCTCCTGGGAACCGGCGGACTGGTGCGCGCCTACTCCGAGGCGACCGCTCAGGCACTGCAGGCGGCTGCACGGGTCACCCTGACCCGGCTTCATCTGTGGGACCTGCGGGTTCCGGTGGCCCAGGCCGGCAGGATCGAGGCGGAGCTGCGCTCCCGCAACCCCGCCGCGGCGTCGGGACCGACAGCGGAGGGCGGGACGGCCGCCACGGCACCGACCATTCACGTCGAGGAGACGATCTGGGGACCGACCCACGCGGTCCTCGTGCTGGCCACATCCTGCGCCGATCCCGAGCTCCTGCACGCCCCGCTGGCGGCCCTGACCCGCGGCGAGGGGGCAGCAGAACCGGCCGGCAGCCGACTGGTCGAGGTCCCCGTGCCACCGGCCTGA","MAPHAPRTPSHQPSQEQSSPGLITLARGEQPEIDLEIKKSHFLARACRTDSMDEARSFIADVRSTYPDARHHCSALTLTDLSDGHALAAPAPPTERSNDDGEPSGTAGQPMLDILRGTGLANTTVVVTRYFGGTLLGTGGLVRAYSEATAQALQAAARVTLTRLHLWDLRVPVAQAGRIEAELRSRNPAAASGPTAEGGTAATAPTIHVEETIWGPTHAVLVLATSCADPELLHAPLAALTRGEGAAEPAGSRLVEVPVPPA$","Uncharacterized conserved protein","Cytoplasm, Periplasm","Uncharacterized ACR","hypothetical protein","protein of unknown function UPF0029","","","","","

InterPro
IPR001498
Domain

Protein of unknown function UPF0029, N-terminal
PTHR16301	$\"[95-137]T$	IMPACT-RELATED
PF01205	$\"[37-154]T$	UPF0029
PS00910	$\"[108-137]T$	UPF0029

noIPR
unintegrated

unintegrated
G3DSA:3.30.230.30	$\"[24-162]T$	no description

","BeTs to 13 clades of COG1739COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1739 is -o----y-vd-lb-efgh-nu---twNumber of proteins in this genome belonging to this COG is 1","***** IPB001498 (Protein of unknown function UPF0029) with a combined E-value of 1.2e-30. IPB001498A 38-58 IPB001498B 107-149","","","-55% similar to PDB:1VI7 Crystal structure of an hypothetical protein (E_value = 1.8E_17);-45% similar to PDB:2CVE Crystal structure of a conserved hypothetical protein TT1547 from thermus thermophilus HB8 (E_value = 2.2E_12);","Residues 37 to 154 (E_value = 6.8e-44) place ANA_1281 in the UPF0029 family which is described as Uncharacterized protein family UPF0029.","","ACR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1283","1367401","1368435","1035","6.00","-3.05","36327","TTGTTCTCTCCCGAGCTCTTGCGGGCCCGACGTCGCCTCATCATGTGGCTCCGCCGGTCACCGTCACTACGGGGCTCACCCAACCCACATCCAAAGGACATCACTATGACGTACGCACCCGACGCAACCGCCCTGGTCGGCAACACTCCCCTGGTCCGCATCAACCGCGTCACCGACGGCGCCCCCGCCACCGTCCTGGCCAAGGTGGAGGCCTTCGAGCCGGCCGCCTCGGTCAAGGACCGCATCGCTCTGTCCATCGTGCGCGCCGCGGAGGCCTCCGGTGACCTCAAGCCCGGCGGCACCATCGTGGAAGCGACCTCCGGGAACACCGGCGTCGGCCTGGCCATGGTGGGAGCGGCCCTGGGGTACAAGGTCATCATCACCATGCCCGAGACCATGTCCAAGGAGCGCCGGGCCATCATGCGCGCCTTCGGTGCGGAGCTGGTGCTGACCACCGAGGGCGGCGTGGCCGGAGCGGTCAAGCGGGCTGAGGAGATCCAGGCCGCCACCCCCAACTCAATCCTCGCCTCCCAGTTCACCAACCCCGCCAACCCCAAGATCCACCGAGAGACCACGGCCCGGGAGATCCTGGAGCAGACCGGGGGCGACATCGACGTCTTCGTGGCCGGTATCGGCACCGGAGGCACGCTGACCGGCGTGGGCCAGGTACTGCGCCAGGAGAAGCCCGGGGTGAAGATCTACGGTGTCGAGCCCTCCGAGTCCCCGCTGCTGAGCGAGGGCCAGGCCGCTCCCCACAAGATCCAGGGCCTGGGCCCCAACGTGGTTCCCGAGATTCTCGACCAGGGCATCTGGGACGAGCTGCTCCACATCGAGTCCGACGTCGCCATCACCTACGCTCGCCGTGCCGCTGCGGAGGAGGGCCTCCTGGTGGGGATTTCCTCGGGCGCAGCTCTGGCCGCCGCCACCGAGCTGGCCAGGCGTCCCGAGTTCGAGGGCAAGACCATCGTCACCGTCCTGCCTGACACCGGTGAGCGTTACCTGTCCACGCCTCTGTTCAAGGACTTCCTCGACTGA","LFSPELLRARRRLIMWLRRSPSLRGSPNPHPKDITMTYAPDATALVGNTPLVRINRVTDGAPATVLAKVEAFEPAASVKDRIALSIVRAAEASGDLKPGGTIVEATSGNTGVGLAMVGAALGYKVIITMPETMSKERRAIMRAFGAELVLTTEGGVAGAVKRAEEIQAATPNSILASQFTNPANPKIHRETTAREILEQTGGDIDVFVAGIGTGGTLTGVGQVLRQEKPGVKIYGVEPSESPLLSEGQAAPHKIQGLGPNVVPEILDQGIWDELLHIESDVAITYARRAAAEEGLLVGISSGAALAAATELARRPEFEGKTIVTVLPDTGERYLSTPLFKDFLD$","Cysteine synthase A","Cytoplasm","cysteine synthase A","cysteine synthase ","cysteine synthase A","","Saito K., Kurosawa M., Murakoshi I. Determination of a functional lysine residue of a plant cysteine synthase by site-directed mutagenesis, and the molecular evolutionary implications. FEBS Lett. 1993. 328(1):111-114. PMID: 8344414Swaroop M., Bradley K., Ohura T., Tahara T., Roper M.D., Rosenberg L.E., Kraus J.P. Rat cystathionine beta-synthase. Gene organization and alternative splicing. J. Biol. Chem. 1992. 267(16):11455-11461. PMID: 1597473","","","

InterPro
IPR001216
Binding_site

Cysteine synthase/cystathionine beta-synthase P-phosphate-binding site
PS00901	$\"[68-86]T$	CYS_SYNTHASE

InterPro
IPR001926
Domain

Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291	$\"[42-329]T$	PALP

InterPro
IPR005856
Family

Cysteine synthase K/M
TIGR01136	$\"[42-339]T$	cysKM: cysteine synthases

InterPro
IPR005859
Family

Cysteine synthase A
TIGR01139	$\"[42-339]T$	cysK: cysteine synthase A

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1100	$\"[152-335]T$	no description
PTHR10314	$\"[57-341]T$	SER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF8	$\"[57-341]T$	CYSTEINE SYNTHASE

","BeTs to 19 clades of COG0031COG name: Cysteine synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0031 is -o-pkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001926 (Pyridoxal-5'-phosphate-dependent enzyme, beta family) with a combined E-value of 8.1e-17. IPB001926A 77-86 IPB001926B 104-129","","","-62% similar to PDB:1Z7W Crystal Structure of O-Acetylserine Sulfhydrylase from Arabidopsis thaliana (E_value = 3.3E_73);-62% similar to PDB:2ISQ Crystal Structure of O-Acetylserine Sulfhydrylase from Arabidopsis Thaliana in Complex with C-Terminal Peptide from Arabidopsis Serine Acetyltransferase (E_value = 3.3E_73);-62% similar to PDB:1Z7Y Crystal Structure of the Arabidopsis thaliana O-Acetylserine Sulfhydrylase K46A mutant (E_value = 1.6E_72);-60% similar to PDB:1FCJ CRYSTAL STRUCTURE OF OASS COMPLEXED WITH CHLORIDE AND SULFATE (E_value = 7.8E_59);-60% similar to PDB:1OAS O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM (E_value = 7.8E_59);","Residues 42 to 329 (E_value = 2.4e-109) place ANA_1283 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme.","","synthase A (cysK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1284","1368561","1369136","576","9.69","6.59","20385","ATGCACAACTCCCAGCGGTCCCTTCTGGACCTGGCCCGTGAGGACCTGGCGACGGCCCGCAAGCGCGACCCCGCCGCCCGCTCCAGCCTGGAGGTGGCCCTCCTCTATCCGGGCGTCCACGCCCTGTGGGCGCACCGGGCGGCTCACAAGCTGTGGCACAAGGGGCACCGCTTCGCAGCGCGTGCCCTGTCTCAGGCGGCCCGCAACTTCACCGGTATCGAGATCCACCCGGCCGCGACGATCGGTGAGCGCTTTTTCATCGACCACGGCATGGGCGTGGTTATCGGTGAGACCGCGGAGGTCGGCAACGACGTGTTGCTGTTCCACGGAGTGACTCTGGGCGGGGTGTCGATGAGTCCGGGTAAGCGCCACCCCACCATCGGTAACAATGTGCAGATCGGCGCCGGTGCCAAGGTCCTGGGGCCGGTCACCGTCGAGGACGGGGCCAAGGTGGGGGCCAACGCGGTCCTGGTGAAGAACCTCCCGCAGGGTCATGTTGCCGTGGGCGTACCCAGCCGGGCCCGCGACCCCCGCACCGACCCCGAGCTCATGATGGACCCGACCATCTACATCTGA","MHNSQRSLLDLAREDLATARKRDPAARSSLEVALLYPGVHALWAHRAAHKLWHKGHRFAARALSQAARNFTGIEIHPAATIGERFFIDHGMGVVIGETAEVGNDVLLFHGVTLGGVSMSPGKRHPTIGNNVQIGAGAKVLGPVTVEDGAKVGANAVLVKNLPQGHVAVGVPSRARDPRTDPELMMDPTIYI$","Serine O-acetyltransferase","Cytoplasm","serine O-acetyltransferase","serine O-acetyltransferase ","serine O-acetyltransferase","","Raetz C.R., Roderick S.L. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 1995. 270(5238):997-1000. PMID: 7481807Wang X.G., Olsen L.R., Roderick S.L. Structure of the lac operon galactoside acetyltransferase. Structure 2002. 10(4):581-588. PMID: 11937062Iverson T.M., Alber B.E., Kisker C., Ferry J.G., Rees D.C. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 2000. 39(31):9222-9231. PMID: 10924115Beaman T.W., Vogel K.W., Drueckhammer D.G., Blanchard J.S., Roderick S.L. Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. Protein Sci. 2002. 11(4):974-979. PMID: 11910040","","","

InterPro
IPR001451
Repeat

Bacterial transferase hexapeptide repeat
PF00132	$\"[72-89]T$ $\"[98-115]T$ $\"[124-141]T$ $\"[142-159]T$	Hexapep
PS00101	$\"[133-161]?$	HEXAPEP_TRANSFERASES

InterPro
IPR005881
Family

Serine O-acetyltransferase
TIGR01172	$\"[12-173]T$	cysE: serine O-acetyltransferase

noIPR
unintegrated

unintegrated
G3DSA:1.10.3130.10	$\"[1-73]T$	no description
G3DSA:2.160.10.10	$\"[74-185]T$	no description
PTHR23416	$\"[73-175]T$	SIALIC ACID SYNTHASE-RELATED
PTHR23416:SF2	$\"[73-175]T$	SERINE ACETYLTRANSFERASE

","BeTs to 12 clades of COG1045COG name: Serine acetyltransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1045 is -o------v-rlbcefgh-nuj----Number of proteins in this genome belonging to this COG is 1","***** IPB010493 (Serine acetyltransferase, N-terminal) with a combined E-value of 6e-51. IPB010493B 29-49 IPB010493C 51-84 IPB010493D 95-122 IPB010493E 123-175","","","-56% similar to PDB:1T3D Crystal structure of Serine Acetyltransferase from E.coli at 2.2A (E_value = 4.1E_33);-55% similar to PDB:1S80 Structure of Serine Acetyltranferase from Haemophilis influenzae Rd (E_value = 7.0E_33);-55% similar to PDB:1SSQ Serine Acetyltransferase- Complex with Cysteine (E_value = 7.0E_33);-55% similar to PDB:1SST Serine Acetyltransferase- Complex with CoA (E_value = 7.0E_33);-56% similar to PDB:1SSM Serine Acetyltransferase- Apoenzyme (truncated) (E_value = 9.2E_33);","Residues 72 to 89 (E_value = 89) place ANA_1284 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 98 to 115 (E_value = 115) place ANA_1284 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 124 to 141 (E_value = 141) place ANA_1284 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 142 to 159 (E_value = 159) place ANA_1284 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).","","O-acetyltransferase (cysE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1285","1370552","1369254","1299","5.44","-13.99","46887","ATGTCGAACGCCTCGCCCGCCCTGCACTCCTCGAGCTGGTCCTCCTCGACCACCGGCCTGCTGACCCGAGACCACCACCTGACCGTTCCCCTGGACCGCAGCGGGCAGGGGGACTCAGCCCCCGACGGGACGGAGTCCATCACCGTCTACGCCCGTGAGATCTCAGCCGTGGGCATCGACCCGGTCTCCCGGCCGCCACTGGTCTTCCTTCAGGGCGGGCCGGGCTGCGAGGCGCCCCGCCCCAGCGCTGACTCCGGGCTCGGCTGGATCGGTGAGATCCTCGAGCACCACCGACTCATCCTCGTCGACCAGCGCGGCACCGGAGCCTCCAGCCCGGTGGACCGGCCCGATGCCGCCGGCACCCCAGCAGACACCGCCCGGCTGCTCACTCACCTGCGCGCCGATGAGATCGTCGAGGACTGCGAGGACCTGCGCCGCGCTCTGGGTCTGGAGCGCTGGAGCCTGCTGGGCCAGTCCTTCGGAGGGTTCTGCGTCACCCGGTACCTCTCCGAGCACGCCCAGAGCCTGGAGAAGGTCTACATCACCGGTGGCCTGCCCGCCGTCGGGCACAGTATCGACGAGGTCTACGCCCTCAGCTACGAGGCGATGCGCCTCAAGAGCGAGGAGTACTACACCCGCTTCCCCCAGGACCGCGACCGCATGGCGTCCCTGGCGGAGAAAGCCGGTCGGGGCGAGCTGAGGACGGCCGGAGGGGATCTCGTAGGACCCGAGCGCCTGCGCTCGCTCGGCGCCCTGCTGGGCGGGGCCGGGGGAGCGGACACGATCCACTACCTCCTGGAGCGCGACCCCGACTCCTGGGCCTTCCGCTACGACCTGGGGCAGTGCCTGCCATTCGGCGGCAGGTTCCCGCTCTACGCCGTCATCCACGAGTCCTGCTGGGCCGACACCGGCACCACCGACTGGGCCGCCCAGCGGGTGCGCCCCGCAATCTTTGATGACGATCCCACCCTCCTGACAGGAGAGCACGTACGCCGCGAGGCCTTCGTCGAGGACGCCGGTCTGCGCCCATGGCTGGAGGTGGCCGACCTCCTGGCCGCACACGAGTGGCCGGCGCTCTACGACCCGGCCCGCCTGAGGGCCACGACGACCCCCGGGGCGGCCGCCGTCTACGCCCGCGACGTGTTCGTGCCGATGACCACCTCCCTGGAGACGGCCGCGCTCATCCCCGGCCTGCGCACCTGGATCACCAGCGAGTACGAGCATGACGGCTCACGCGCCTCCGGCGGTCGGGTCTTCAAGCGCCTGCGAGACCTGGCCGCCGGGGTAATCGCCCGCTGA","MSNASPALHSSSWSSSTTGLLTRDHHLTVPLDRSGQGDSAPDGTESITVYAREISAVGIDPVSRPPLVFLQGGPGCEAPRPSADSGLGWIGEILEHHRLILVDQRGTGASSPVDRPDAAGTPADTARLLTHLRADEIVEDCEDLRRALGLERWSLLGQSFGGFCVTRYLSEHAQSLEKVYITGGLPAVGHSIDEVYALSYEAMRLKSEEYYTRFPQDRDRMASLAEKAGRGELRTAGGDLVGPERLRSLGALLGGAGGADTIHYLLERDPDSWAFRYDLGQCLPFGGRFPLYAVIHESCWADTGTTDWAAQRVRPAIFDDDPTLLTGEHVRREAFVEDAGLRPWLEVADLLAAHEWPALYDPARLRATTTPGAAAVYARDVFVPMTTSLETAALIPGLRTWITSEYEHDGSRASGGRVFKRLRDLAAGVIAR$","Proline iminopeptidase","Cytoplasm, Extracellular","proline iminopeptidase","prolyl aminopeptidase","alpha/beta hydrolase fold","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[97-184]T$	Abhydrolase_1

InterPro
IPR002410
Family

Peptidase S33, prolyl aminopeptidase
PR00793	$\"[67-75]T$ $\"[99-110]T$ $\"[155-169]T$	PROAMNOPTASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[63-408]T$	no description
PTHR10992	$\"[53-223]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF12	$\"[53-223]T$	PROLINE IMINOPEPTIDASE

","BeTs to 11 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","***** IPB002410 (Prolyl aminopeptidase (S33) family signature) with a combined E-value of 1.2e-11. IPB002410A 67-75 IPB002410B 99-110 IPB002410C 155-169***** IPB003089 (Alpha/beta hydrolase fold signature) with a combined E-value of 7.5e-07. IPB003089A 96-111 IPB003089B 155-168","","","No significant hits to the PDB database (E-value < E-10).","Residues 97 to 424 (E_value = 7e-07) place ANA_1285 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","iminopeptidase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1286","1371593","1370592","1002","6.34","-4.49","36098","ATGCCGGAGGGGCACACCATCCACCGGCTCGCCGCCGCCCTTGACGAGCTCTACGGTGGTCAGAGTCTGCGCGTGCGCTCCCCGCAGGGGCGTTTCGCTGACGGGGCGAGCCGCCTGGACGGTCAGGTCCTCCTGGGCAGCCAGGCCCACGGCAAGCACCTCTTCCTGCCCTTCGGTCCCCGTGCCGACATGTCCCTTGACGACGACTCCGTCACCTGGCTGCGGATCCACCTGGGCCTCTACGGGGCATGGACCTTCGACGGCGACCGTGAGTTCACAGCGCCCCACGCCATCGGGGCGCCGCGTCGGCGCGTCGGGGAGCGCGGTGAGCACGCCCTCAAGGGTGGGGGAGGCTCGGCCCTGACCGGGCTGAACGGCGGAAGCCTCGAAGCCGAGGGGCAGGATGCAGCCACGCATGGGCCCGCCCCCGAGGAGTGGGAGCCGCCTGAGCCGCGCGGTGCGGTGCGGCTGCGGCTACTCGGCGAGCACGGGGTGGCCGACCTGACCGGACCGGCGGCCTGCGAGCTGCTGGACGCCGAGGGCGTGGCCGCCGTGCGCCGCCGCCTCGGCCCGGACCCGCTGCGCGCCGACGGCGACGTGGAGGCCTTCGTGGCCAAGGCGCGCTCGCGGCGTAAGAGCATCGGAGAGCTGCTCATGGACCAGGCCGTCATCTCCGGAGCCGGCAACATCTACCGTGCCGAGACGCTCTTCCGCGTCGGGGTCTCGCCCTTCCGCGCGGGCAACCGCACCAGCGAGGAGCGGTTGCGGGCCATCTGGGAGGACCTGCGCCCCCTCATGGAGTACGGGGTGGCCACCGGCTTCATCACCACCGTCGACCTCGACGACGTCCCCGACCCCCTGCCGCCAGACGACCCTGAGGCCGGCCGGTGGTACGTCTACCACCGCACCGGCCGCCCCTGCCTGCGCTGTGGGACCCCGGTGGCGGAGCGGGAGGTGGCGTCCCGCAGGCTCTTCTGGTGCCCGACCTGCCAGGCCCACTGA","MPEGHTIHRLAAALDELYGGQSLRVRSPQGRFADGASRLDGQVLLGSQAHGKHLFLPFGPRADMSLDDDSVTWLRIHLGLYGAWTFDGDREFTAPHAIGAPRRRVGERGEHALKGGGGSALTGLNGGSLEAEGQDAATHGPAPEEWEPPEPRGAVRLRLLGEHGVADLTGPAACELLDAEGVAAVRRRLGPDPLRADGDVEAFVAKARSRRKSIGELLMDQAVISGAGNIYRAETLFRVGVSPFRAGNRTSEERLRAIWEDLRPLMEYGVATGFITTVDLDDVPDPLPPDDPEAGRWYVYHRTGRPCLRCGTPVAEREVASRRLFWCPTCQAH$","Formamidopyrimidine-DNA glycolase","Cytoplasm, Extracellular","Formamidopyrimidine-DNA glycosylase","formamidopyrimidine-DNA glycolase","Formamidopyrimidine-DNA glycolase","","O. Connor T.R., Graves R.J., de Murcia G., Castaing B., Laval J. Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role. J. Biol. Chem. 1993. 268(12):9063-9070. PMID: 8473347Duwat P., de Oliveira R., Ehrlich S.D., Boiteux S. Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein. Microbiology 1995. 141:411-417. PMID: 7704272","","","

InterPro
IPR000191
Family

Formamidopyrimidine-DNA glycolase
PD003680	$\"[197-273]T$	Q8FLN4_COREF_Q8FLN4;
PF01149	$\"[2-164]T$	Fapy_DNA_glyco
PF06831	$\"[189-281]T$	H2TH

InterPro
IPR000214
Binding_site

Formamidopyrimidine-DNA glycolase, zinc-binding site
PS51066	$\"[298-332]T$	ZF_FPG_2

InterPro
IPR012319
Domain

Formamidopyrimidine-DNA glycosylase, catalytic
PS51068	$\"[2-99]T$	FPG_CAT

noIPR
unintegrated

unintegrated
PTHR22993	$\"[143-331]T$	FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE
PTHR22993:SF4	$\"[143-331]T$	FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE (FAPY-DNA GLYCOSYLASE)

","BeTs to 11 clades of COG0266COG name: Formamidopyrimidine-DNA glycosylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0266 is ---------drlbcefghsn-j---wNumber of proteins in this genome belonging to this COG is 2","***** IPB000191 (Formamidopyrimidine-DNA glycolase) with a combined E-value of 2.3e-44. IPB000191A 1-16 IPB000191B 49-58 IPB000191C 74-86 IPB000191E 188-203 IPB000191F 214-243 IPB000191G 299-331***** IPB010663 (FPG and IleRS zinc finger) with a combined E-value of 7.3e-23. IPB010663D 189-196 IPB010663E 218-237 IPB010663F 299-331","","","-47% similar to PDB:1EE8 CRYSTAL STRUCTURE OF MUTM (FPG) PROTEIN FROM THERMUS THERMOPHILUS HB8 (E_value = 3.8E_18);-48% similar to PDB:1L1T MutM (Fpg) Bound to Abasic-Site Containing DNA (E_value = 1.4E_17);-48% similar to PDB:1L1Z MutM (Fpg) Covalent-DNA Intermediate (E_value = 1.4E_17);-48% similar to PDB:1L2B MutM (Fpg) DNA End-Product Structure (E_value = 1.4E_17);-48% similar to PDB:1L2C MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex (E_value = 1.4E_17);","Residues 2 to 175 (E_value = 7.7e-08) place ANA_1286 in the Fapy_DNA_glyco family which is described as Formamidopyrimidine-DNA glycosylase N-terminal domain.Residues 189 to 281 (E_value = 9.1e-27) place ANA_1286 in the H2TH family which is described as Formamidopyrimidine-DNA glycosylase H2TH domain.","","glycosylase (fragment)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1287","1372096","1371596","501","5.65","-7.70","17305","ATGCGCATCCATATCGCCTCCGACCACGCCGGTTACGAGCTCAAGAGCGCCGTGATCGAGCACCTGAGGGAGCAGGGGCACGACGTCATCGACCACGGAGCCCACGCCTACGATCCGAATGATGACTACCCTGCCTTCTGTCTGGCCTGCGGGGAGGCCGTCGTGGCCGACGCCGGGAGCCTGGGCATTGTTCTCGGGGGTAGTGGCAACGGGGAGCAGATCGCCGCCAACAAGGTTGACGGGGTGCGAGCCGCCCTGGCCTGGTCGATCGAGACCGCCCGACTTGCCCGCCAGCACAACAACGCCAACGTCGTCGCACTGGGTGGTCGCATGCATGACCTGGGGGCGGGCCTGGCCATCATCGATGCTTTCCTCGCCGAGCCCTTCAGCGGGGACGAGCGCCACGTGCGTCGCATCGCGCAGCTCGCCGACTACGAGAGCCGCGTTCATGACGCCGCCGCTCCAGCGGCTGATCGCGCCGCTGCCGCCACCGGGGCCTGA","MRIHIASDHAGYELKSAVIEHLREQGHDVIDHGAHAYDPNDDYPAFCLACGEAVVADAGSLGIVLGGSGNGEQIAANKVDGVRAALAWSIETARLARQHNNANVVALGGRMHDLGAGLAIIDAFLAEPFSGDERHVRRIAQLADYESRVHDAAAPAADRAAAATGA$","Ribose 5-phosphate isomerase","Cytoplasm","Ribose 5-phosphate isomerase RpiB","ribose 5-phosphate isomerase RpiB ","ribose 5-phosphate isomerase","","Rosey E.L., Stewart G.C. Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans. J. Bacteriol. 1992. 174(19):6159-6170. PMID: 1400164","","","

InterPro
IPR003500
Family

Ribose/galactose isomerase
PIRSF005384	$\"[1-150]T$	Sugar-phosphate isomerase, RpiB/LacA/LacB types
PF02502	$\"[2-143]T$	LacAB_rpiB
TIGR00689	$\"[3-148]T$	rpiB_lacA_lacB: sugar-phosphate isomerases,

InterPro
IPR011860
Family

Ribose 5-phosphate isomerase, actinobacteria
TIGR02133	$\"[1-148]T$	RPI_actino: ribose 5-phosphate isomerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.1400.10	$\"[1-159]T$	no description

","BeTs to 10 clades of COG0698COG name: Ribose 5-phosphate isomerase RpiBFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0698 is -------qv-rlbce--h--ujx--wNumber of proteins in this genome belonging to this COG is 3","***** IPB003500 (Ribose/galactose isomerase) with a combined E-value of 4.3e-43. IPB003500A 1-31 IPB003500B 58-99","","","-77% similar to PDB:1USL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, COMPLEXED WITH PHOSPHATE. (E_value = 8.8E_52);-77% similar to PDB:2BES STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, IN COMPLEX WITH 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID. (E_value = 8.8E_52);-77% similar to PDB:2BET STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, IN COMPLEX WITH 4-PHOSPHO-D-ERYTHRONATE. (E_value = 8.8E_52);-65% similar to PDB:1O1X Crystal structure of ribose-5-phosphate isomerase RpiB (TM1080) from Thermotoga maritima at 1.90 A resolution (E_value = 3.1E_25);-54% similar to PDB:1NN4 Structural Genomics, RpiB/AlsB (E_value = 1.2E_19);","Residues 2 to 143 (E_value = 4.5e-72) place ANA_1287 in the LacAB_rpiB family which is described as Ribose/Galactose Isomerase.","","5-phosphate isomerase RpiB","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1289","1372193","1374376","2184","4.70","-50.91","79823","ATGACTGACGCCTGCGCGACCTCATCGACTCCCACCGGCCCTGCATCGGACTCACCGGCCCCCCACTCTCAGCCGACGGCTTCCCCCAGCCCCACCGCTGAGGCGGTCCTCGCCGGCGTGCTGGAGACGGCGCACACCGACACCTCCGTACGTCCCCAGGACGACCTGTTCCGCTTCGTCAACGGCCAGTGGCTCGCCACCGCTGAGATCCCGGCGGACCGCCCCAGTAGCGGCGCCTTCACCACCTTGCGCGACGAGGCGGAGGCCGCCTGCCGACAGATCGTTGAGGAGCTTGCCGAGCAGTTCTCCTCCGTGGCACCCGAGGTGGCCTCGGAGGTCCTGGCCACGAACCGGGGCCGGGTCGGCGCCCTCTACGAGGCATTCATGGACGAGGCCCACCTGGAGGAGCTCGGGGCCGAGCCGCTGGCTGAGGAGCTGGCGCCGGTGCTGGACGCCTCCTCCAAGGAGGAGCTGGCCCGTGCGCTGGGAGAGATGACTCCGATCGGCTTCATGGGCGTGGTCGGCGCGGATGTCGAGGTGGATATCAATGACCCGGAGCGCTACACGAGCTGGGTGGGGCAGTCGGGCCTGGGACTGCCGGACGAGTCCTACTACCGCGAGGAGGCTCAGGCACCGCTGCGCCAGGCCTACGTGGCGCACGTGGCCAGGATGCTGTCTCTTGCGGGGCTGACGGACTCCTTCGGCGCCTCGGGTGAGGAGCTCGCCGAGCGAGTCATGGCCGTGGAGACCGCCCTGGCCAAGGGGCACTGGGACCGCGTCACCTGCCGTGACGTGGAGAAGATGAACAATCCGATGTCCTGGCGGCAGATCGTGGACTCGGCCCCCGACCTGCCCTGGGACGAGTGGCGCGAGGGGATTCGCGCTGCCGCCCGGAGCGCCAGCATCGAGCAGACCGCCTTCCTCGAGGAGGCCATCGTCACTCAGCCCGACTACCTCCCCCACGCGGCCGGCATCTGGCAGGAGACCTCCCTGGAGGATCTCAAGGTCTGGGCCGCCTGGCATACCGTTCATGGACGCGCCACCCTGCTGTCGGGGGCCTTCGTGGAGGAGAACTTCGACTTCTACGGCCGCACGCTCCAGGGGACCGACGAGCTGCGGCCCCGTTGGAAGCGCGGCGTCGGCCTGGTGGAGTCCTGCCTGGGTGAGGCACTGGGTGAGATCTACGTGGAGCGGCACTTCCCGCCGTCGCACAAGTCGGCGATGGAGGCCCTGGTGGGCCGGCTCATCGAGGCCTACCACCAGTCCATCTCCTCGTTGGAGTGGATGAGTCCGGCCACGCGGGAGCGGGCCCTGGAGAAGCTGGCGCTGTTCACCCCCAAGATCGGCTACCCGGTGCGCTGGCGCGACTACTCCGACGTCGAGGTGGTCCCCGGCGACGTCCTGGCCTCGGTGCGCAGCGTGGAGCGGGCCGACATGGCCTACTCGCTGAACAAGCTGACCAAGCCGGTGGACCGCGACGAGTGGCACATGACCCCTCAGACGGTCAACGCCTACTACAACCCGACCATGAACGAGATCGTCTTCCCCGCCGCGATCCTTCAGCCTCCCTTCTTCGATCCGCAGGCCGACGACGCCGTGAACTATGCGGGCATCGGTGCTGTCATCGGTCACGAAATCGGCCACGGCTTCGATGACCAGGGCTCCACCTTCGACGGCACCGGAAAGGTCAGTGACTGGTGGACCCAGGAGGACCGGGAGGCCTTCACCGAGCGCACGAGGGCACTCATCAGCCAGTACGACGCCTACACGCCCGAGGTCGTCGCCGCCAAGCACCGGGACGCGGGTACGGAGCAGGCGGAGATCCCGCACGTCAACGGCGCTTTGACCATCGGGGAGAACATTGGTGACCTGGGCGGCCTGGGCATCGCTCTCAAGGCCTACTCCCTGGCCCTGGCCGACGTCGGTATCCCCTCAGTGGATGAGGCTCCTGTCATCGACGGGCTCACCGGCCTGCAGCGCTTCTTCTACTCCTGGGCGCGGATCTGGCGTTCCAAGAGCCGTCCTGACTATGCCGAGCTCCTTCTGACCGTCGACCCGCACTCGCCGGCGGAGTTCCGGTGTAACGGGATCGTGCGCAATGTGGACGCCTTCTACAAGGCCTTCGCGGTGGATTCCGACGACGCTTTGTGGTTGTCACCAAACGAACGGGTCTCTATTTGGTAA","MTDACATSSTPTGPASDSPAPHSQPTASPSPTAEAVLAGVLETAHTDTSVRPQDDLFRFVNGQWLATAEIPADRPSSGAFTTLRDEAEAACRQIVEELAEQFSSVAPEVASEVLATNRGRVGALYEAFMDEAHLEELGAEPLAEELAPVLDASSKEELARALGEMTPIGFMGVVGADVEVDINDPERYTSWVGQSGLGLPDESYYREEAQAPLRQAYVAHVARMLSLAGLTDSFGASGEELAERVMAVETALAKGHWDRVTCRDVEKMNNPMSWRQIVDSAPDLPWDEWREGIRAAARSASIEQTAFLEEAIVTQPDYLPHAAGIWQETSLEDLKVWAAWHTVHGRATLLSGAFVEENFDFYGRTLQGTDELRPRWKRGVGLVESCLGEALGEIYVERHFPPSHKSAMEALVGRLIEAYHQSISSLEWMSPATRERALEKLALFTPKIGYPVRWRDYSDVEVVPGDVLASVRSVERADMAYSLNKLTKPVDRDEWHMTPQTVNAYYNPTMNEIVFPAAILQPPFFDPQADDAVNYAGIGAVIGHEIGHGFDDQGSTFDGTGKVSDWWTQEDREAFTERTRALISQYDAYTPEVVAAKHRDAGTEQAEIPHVNGALTIGENIGDLGGLGIALKAYSLALADVGIPSVDEAPVIDGLTGLQRFFYSWARIWRSKSRPDYAELLLTVDPHSPAEFRCNGIVRNVDAFYKAFAVDSDDALWLSPNERVSIW$","Neprilysin","Cytoplasm, Extracellular","belongs to peptidase family M13","probable zinc metalloprotease ","Neprilysin","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Turner A.J., Isaac R.E., Coates D. The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function. Bioessays 2001. 23(3):261-269. PMID: 11223883Le Moual H., Roques B.P., Crine P., Boileau G. Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11. FEBS Lett. 1993. 324(2):196-200. PMID: 8099556Malfroy B., Schofield P.R., Kuang W.J., Seeburg P.H., Mason A.J., Henzel W.J. Molecular cloning and amino acid sequence of rat enkephalinase. Biochem. Biophys. Res. Commun. 1987. 144(1):59-66. PMID: 3555489","","","

InterPro
IPR000718
Family

Peptidase M13, neprilysin
PR00786	$\"[495-507]T$ $\"[513-525]T$ $\"[534-550]T$ $\"[619-630]T$	NEPRILYSIN
PTHR11733	$\"[34-727]T$	ZINC METALLOPROTEASE FAMILY M13 NEPRILYSIN-RELATED
PF01431	$\"[503-724]T$	Peptidase_M13

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[541-550]?$	ZINC_PROTEASE

InterPro
IPR008753
Domain

Peptidase M13
PF05649	$\"[51-451]T$	Peptidase_M13_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.390.10	$\"[383-727]T$	no description
PTHR11733:SF18	$\"[34-727]T$	ZINC METALLOPROTEASE (BACTERIA)

","BeTs to 3 clades of COG3590COG name: Predicted metalloendopeptidaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG3590 is ----------rl------s--j----Number of proteins in this genome belonging to this COG is 1","***** IPB008753 (Peptidase M13) with a combined E-value of 5.6e-143. IPB008753A 52-72 IPB008753B 117-151 IPB008753C 168-205 IPB008753D 334-368 IPB008753E 376-416 IPB008753F 428-454 IPB008753G 533-583 IPB008753H 611-637 IPB008753I 684-725***** IPB000718 (Neprilysin metalloprotease (M13) family signature) with a combined E-value of 2.1e-39. IPB000718A 495-507 IPB000718B 513-525 IPB000718C 534-550 IPB000718D 619-630","","","-44% similar to PDB:1DMT STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON (E_value = 3.3E_71);-44% similar to PDB:1R1H STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS (E_value = 3.3E_71);-44% similar to PDB:1R1I STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS (E_value = 3.3E_71);-44% similar to PDB:1R1J STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS (E_value = 3.3E_71);-44% similar to PDB:1Y8J Crystal Structure of human NEP complexed with an imidazo[4,5-c]pyridine inhibitor (E_value = 3.3E_71);","Residues 51 to 451 (E_value = 1.9e-122) place ANA_1289 in the Peptidase_M13_N family which is described as Peptidase family M13.Residues 503 to 724 (E_value = 1.2e-88) place ANA_1289 in the Peptidase_M13 family which is described as Peptidase family M13.","","to peptidase family M13","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1291","1374580","1375542","963","4.73","-14.59","32160","ATGCGTCTTGGACGCCCCCTGGCCGCCGCGAGCGTGATGGCCGCCGCCATCGGCGCCTCCCTCGCCGCCTCCCCCGCCCTGGCCGGCGACTCCCTCGCCTTCAAGATCGCCGATGACCAGCAGGTCATCGTCAACCCCTCGGACACCGCCTTCCCGGTGTCGGGCTCCGGCTGCACCGGCAAGGACGCGGCTGTCGGCGTCGCCCTCCACACCTCGAAGGGCGAGATGTCCACCATCGTGAAGGCCACCCCCGACGCCGAGGGCAACTGGTCCACCACCCTGAACATCCCCGAGCTGGTCAAGTCCACCGGCGCTGAGGCCAAGACCGACGGCTCGGACGACGGCTGGTCCATCGTGGCCGGCTGCGTCTCCTACGGTGAGGAGAAGGGCCAGGACCAGCAGGGTATCGCCTTCGACGACACCGACGTGGACGGCACCTACAAGATCACCACCGACGAGAACGGCGCTCAGAAGATCACGGTGGACGTCAAGGGCTTCTCCCCCAAGGAGAAGGTCACCCTCACCCTGGTCAGCAAGACCGACTCCTCCAAGACCTACCCCGTCGGCACGCTGGAGGCTGACGACAAGGGCAACGTCACGGGCGAGCTTCCGGCCCCCTCGAACGTGGATGACGGCGAGTACACGCTGACCATCGAGGGCGACCGTTACGGCGAGGGCGGCAGCAGCACCAAGACCGTCGTCGTCAAGGACCACCGCCTCGACCTCGTCGAGAACGACGGCAACGGCATCACCGACAACGGTGGCGCCACCGCCAACCCGACCGCTCCCGCCTCCAACGGCAGCGTGAACGTCCCGGCCAGCACCGACGCCACCCCGGCGGCCTCCACCTCCGGCAAGCCCCTGGCCCAGACCGGTGCCAACGGCCTGCTCTTCGGCGGCATTGCCGCGGCCCTCGTGGCCATCGGTGGCGGCGCCCTCGTCGTGCGTCGTCGTAAGGCCTGA","MRLGRPLAAASVMAAAIGASLAASPALAGDSLAFKIADDQQVIVNPSDTAFPVSGSGCTGKDAAVGVALHTSKGEMSTIVKATPDAEGNWSTTLNIPELVKSTGAEAKTDGSDDGWSIVAGCVSYGEEKGQDQQGIAFDDTDVDGTYKITTDENGAQKITVDVKGFSPKEKVTLTLVSKTDSSKTYPVGTLEADDKGNVTGELPAPSNVDDGEYTLTIEGDRYGEGGSSTKTVVVKDHRLDLVENDGNGITDNGGATANPTAPASNGSVNVPASTDATPAASTSGKPLAQTGANGLLFGGIAAALVAIGGGALVVRRRKA$","Gram positive anchor domain protein","Extracellular, Periplasm","Gram positive anchor domain protein","hypothetical protein predicted by Glimmer/Critica","LPXTG-motif cell wall anchor domain","","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
PF00746	$\"[290-319]T$	Gram_pos_anchor
TIGR01167	$\"[287-320]T$	LPXTG_anchor: LPXTG-motif cell wall anchor
PS50847	$\"[288-320]T$	GRAM_POS_ANCHORING

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[9-29]?$ $\"[295-315]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-65% similar to PDB:1TI2 Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici (E_value = );-65% similar to PDB:1TI4 Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with pyrogallol (E_value = );-65% similar to PDB:1TI6 Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with inhibitor 1,2,4,5-tetrahydroxy-benzene (E_value = );-65% similar to PDB:1VLD Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici (E_value = );-65% similar to PDB:1VLE Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with pyrogallol (E_value = );","Residues 290 to 319 (E_value = 1.3e-05) place ANA_1291 in the Gram_pos_anchor family which is described as Gram positive anchor.","","positive anchor domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1292","1375695","1376807","1113","8.07","2.85","38933","ATGGACTCCACCTCCCACGACGAGCACAGCGCAGCCCCCTCGGAGGCCTCGGAGGCCTCGGACGCCACCGGGGACCCCACCGATACCTCCTCCCCCCTGCCGCAGCGACGCCGCCAGGGCCGAGGCGGCACAGGCGTCAAGCGCTGGTCGAGGCGCCGCAAGATCGTCGTCGGCCTGAGCACCGCGGTCATGACGACCGCCCTGGCCCTGGGCGCGGATGTGGCGGTCCTGGCTCATCGCCCTGCACGCGTCGACATCGCCATGCCCACCACGTCCTCCCCGACGGCGGGCGAGACCTGGCTGATCCTGGGAACCGACTCACGCGCCACCGTGCCGGGAGACCAGAACCGTTACGGAACCACTCAGGAGGTGGAGGGTTCCCGCGCCGATGTCATCGCCCTGGTACGCCCCTCCCAGGAGGGAGTCACCATCATCAACCTGCCCCGGGACCTGACCATCAACAGCAAGGGCATGGAGCTGGACCGGCTGGCCACCACCTACGTTCCAGGACCTCAGAACACGGTCAACGCCCTGTGCACCGGGCTCGGAATCCCCACCACGCATCTGGTGACCATCGACATGGCTCAGTTCGCCACTATCATCGACTCCCTGGGTGGCATTGAGGTGGACGTGCCCGAGCCGGTTCGAGACGCCTACACCGGACTGAACCTCTCCTCCGCCGGCCGCCATCGACTCAGCGGGATCGACGCCCTAGCCCTTGTCCGCTCACGGCACCCGGAGATCCTGCGCGACGGCAGATGGGTGACCATGAGCCAGGCCGATGGCGCCCAACGCCGTAGCCAGTCCACGGCCACCGTGATGCAGGCCGTGCTGTCCGCCATCGGGCAGAAGGCCAGCAACCCCGTCTCACTCCATCAGCTGGCACACACCGTGGCCGGGAACATCACCCTGGACTCAGGTACTGGGCTCAGCGACCTGGCCGCACTGGGACGCAGCGCCTCGAAGGCCAGGCGGGCCGGGGCCACGACGATCATTGATCTTCCGACGGGACCACGGGACGAGTCGATCATCGTCTCCCCCAACCAGGAGTCGCGTGACCTGTTGGCCCGCTATGGGTACAGTCCCAAAACCTGTCGGCCAGCGGGCGCCTAG","MDSTSHDEHSAAPSEASEASDATGDPTDTSSPLPQRRRQGRGGTGVKRWSRRRKIVVGLSTAVMTTALALGADVAVLAHRPARVDIAMPTTSSPTAGETWLILGTDSRATVPGDQNRYGTTQEVEGSRADVIALVRPSQEGVTIINLPRDLTINSKGMELDRLATTYVPGPQNTVNALCTGLGIPTTHLVTIDMAQFATIIDSLGGIEVDVPEPVRDAYTGLNLSSAGRHRLSGIDALALVRSRHPEILRDGRWVTMSQADGAQRRSQSTATVMQAVLSAIGQKASNPVSLHQLAHTVAGNITLDSGTGLSDLAALGRSASKARRAGATTIIDLPTGPRDESIIVSPNQESRDLLARYGYSPKTCRPAGA$","Cell envelope-related function transcriptional attenuator, LytR/CpsA family","Periplasm, Membrane","putative membrane protein","transcriptional regulator","cell envelope-related function transcriptional attenuator, LytR/CpsA family","","","","","

InterPro
IPR004474
Domain

Cell envelope-related transcriptional attenuator
PF03816	$\"[128-287]T$	LytR_cpsA_psr
TIGR00350	$\"[127-283]T$	lytR_cpsA_psr: cell envelope-related functi

noIPR
unintegrated

unintegrated
tmhmm	$\"[55-75]?$	transmembrane_regions

","BeTs to 5 clades of COG1316COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1316 is --------vdrlbc----------t-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","-46% similar to PDB:1FXO THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TMP COMPLEX. (E_value = );-46% similar to PDB:1FZW THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). APO ENZYME. (E_value = );-46% similar to PDB:1G0R THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). THYMIDINE/GLUCOSE-1-PHOSPHATE COMPLEX. (E_value = );-46% similar to PDB:1G1L THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-GLUCOSE COMPLEX. (E_value = );-46% similar to PDB:1G23 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). GLUCOSE-1-PHOSPHATE COMPLEX. (E_value = );","Residues 128 to 287 (E_value = 1.4e-09) place ANA_1292 in the LytR_cpsA_psr family which is described as Cell envelope-related transcriptional attenuator domain.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1293","1378870","1377497","1374","5.50","-5.87","43501","TTGTCTCACCTTCTGATCGACACCGGCAGTGCCTGGAGCGTCGTACAACGGCTCCGGGGGACGACACGTCATGTGTCGTCCCCCGGAGCCGAGGCTGTTCCCTCAGCTTGGGGAACGTCAGCGGATCAGGTCAGATGCGGCTCAGGCCTTGTTGCGGCGACGCAGCACCAGGGCGGCGCCTCCAGCCACGACCAGGAACGCTGCGATCCCGCCGAAGAGCAGGCCGTTGGCACCGGTGTGGGCCAGGGAACCGTCGCTGTCCTTGGTCGTCTCACCGCCGGCCCGGTTCTCCGAGGAGGAGTCCTTGGCGTTCGAGCTCAGGTTGTTGCCCTTGTCAGCCCCGGCCTTGTTGTCGCCGGCGTTGGCCTGCTTGTCTCCACCAGCCTGCTTGTCGCTGCCGGCGTTGGCGTTGCTGTTGCTTCCGCCGTTGTTGCCGCCACCGCTGTTCTCGGTGGTCTTCTGCTCGCTGGCCTTCTGCTCGGTGGTCTTGTCGCCGCCGGCCTGCTTGTCGCTCCCACCGTTGTTCTCAGAAGCCGAGCGCTCAGTAGTGCTCTGCTCAGTGGTGTTCTGCTCAGTGGTCTGACGCTCGGAGGTCGAGCGCTGCTCCGTGGTGTTGTGCTCCGAGTTTTGACGCTCGGAGGTGGAACGCTCGGTGGTCTTCTGCTCGCTGGCCTTCTGCTCGGTGGTCTTGTCACCGCCGGCCTGCTTGTCGCCGCCGCCGTTGTTCTCGGTGGTCTTCTGCTCGGTGGTCTTGTCGCCACCGGCCTGCTTGTCGCCGCCGCCGTTGTTCTCGGTGGTCTTCTGCTCGGTGGTCTTGTCACCGCCGGCCTGCTTGTCGCCGCCGTTGTTGCCGCCGCCATTGTTCTCGGCGGTCTCGGTCTCGGTGGTGGAGCGCTCGGTGCTCTCGACGGTGAAGGTGTGCTGGGAGACCGTGGTGACGGTCTGGCTGGTGGCCGTCTCGCTGTGGTGGGAGCCGGTCAGGACCAGGACGTACTCCCCGTCGGGGGCGTCAGTGGGGGCGGGCAGGTTGCCCGTGAGGTTACCGTTGGCGTCAACCGTCAGCTCACCAAGGGTGTAGCAGATGCTGGAGTCGCTCTTGCTCTTGAGGAGGACAGTGACCTTCTCGCTGGCGTAGAAGCCCTGAGCGTTGAAGGTGAAGGTCTGGGACTGGCTCTCCGTGCGGGTGGAGACCTCGTAGGAGCCGGAGATACGCGTGTCGTCGAAGTAGATCTGCGTCTGCTGCTGCTTGGTGACCTGGGCCGTCTCGGTCTTGTCGCCGTAGGTCATGCAGCCGGCTCCGATGGTCCATCCGTCAGTAGTGGTGGCCGTGGTCGAGCCGATGGACTTGATGAGCGCCGCCAGGTCGAGGTCTGA","LSHLLIDTGSAWSVVQRLRGTTRHVSSPGAEAVPSAWGTSADQVRCGSGLVAATQHQGGASSHDQERCDPAEEQAVGTGVGQGTVAVLGRLTAGPVLRGGVLGVRAQVVALVSPGLVVAGVGLLVSTSLLVAAGVGVAVASAVVAATAVLGGLLLAGLLLGGLVAAGLLVAPTVVLRSRALSSALLSGVLLSGLTLGGRALLRGVVLRVLTLGGGTLGGLLLAGLLLGGLVTAGLLVAAAVVLGGLLLGGLVATGLLVAAAVVLGGLLLGGLVTAGLLVAAVVAAAIVLGGLGLGGGALGALDGEGVLGDRGDGLAGGRLAVVGAGQDQDVLPVGGVSGGGQVAREVTVGVNRQLTKGVADAGVALALEEDSDLLAGVEALSVEGEGLGLALRAGGDLVGAGDTRVVEVDLRLLLLGDLGRLGLVAVGHAAGSDGPSVSSGGRGRADGLDERRQVEV$","Hypothetical protein","Membrane, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Szecsi P.B. The aspartic proteases. Scand. J. Clin. Lab. Invest. Suppl. 1992. 210:5-22. PMID: 1455179","","","

InterPro
IPR001969
Active_site

Peptidase aspartic, active site
PS00141	$\"[4-15]?$	ASP_PROTEASE

noIPR
unintegrated

unintegrated
tmhmm	$\"[130-150]?$ $\"[152-172]?$ $\"[178-198]?$ $\"[207-227]?$ $\"[233-253]?$ $\"[255-275]?$ $\"[281-301]?$	transmembrane_regions

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
TIGR01167	$\"[531-565]T$	LPXTG_anchor: LPXTG-motif cell wall anchor
PS50847	$\"[532-565]T$	GRAM_POS_ANCHORING

noIPR
unintegrated

unintegrated
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[7-27]?$ $\"[539-559]?$	transmembrane_regions

InterPro
IPR001930
Family

Peptidase M1, membrane alanine aminopeptidase
PTHR11533	$\"[98-805]T$	PROTEASE M1 ZINC METALLOPROTEASE

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[305-314]?$	ZINC_PROTEASE

InterPro
IPR006172
Family

DNA-directed DNA polymerase B
PS00116	$\"[467-475]?$	DNA_POLYMERASE_B

InterPro
IPR012778
Family

Peptidase M1, aminopeptidase N actinomycete-type
PTHR11533:SF12	$\"[98-805]T$	AMINOPEPTIDASE N
TIGR02412	$\"[5-863]T$	pepN_strep_liv: aminopeptidase N

InterPro
IPR014782
Domain

Peptidase M1, membrane alanine aminopeptidase, N-terminal
PR00756	$\"[131-146]T$ $\"[271-281]T$ $\"[305-320]T$ $\"[324-336]T$	ALADIPTASE
PF01433	$\"[14-397]T$	Peptidase_M1

","BeTs to 11 clades of COG0308COG name: Aminopeptidase NFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0308 is ---p--y--drl-cefghsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB001930 (Membrane alanyl dipeptidase (M1) family signature) with a combined E-value of 5.7e-32. IPB001930A 131-146 IPB001930B 187-202 IPB001930C 271-281 IPB001930D 305-320 IPB001930E 324-336","","","-45% similar to PDB:1Z1W Crystal structures of the tricorn interacting facor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations (E_value = 1.2E_49);-45% similar to PDB:1Z5H Crystal structures of the Tricorn interacting Factor F3 from Thermoplasma acidophilum (E_value = 1.2E_49);-39% similar to PDB:2DQ6 Crystal Structure of Aminopeptidase N from Escherichia coli (E_value = 5.6E_20);-39% similar to PDB:2DQM Crystal Structure of Aminopeptidase N complexed with bestatin (E_value = 5.6E_20);-39% similar to PDB:2HPO Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site (E_value = 5.6E_20);","Residues 14 to 397 (E_value = 1.5e-55) place ANA_1295 in the Peptidase_M1 family which is described as Peptidase family M1.","","N (LYS-AP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1296","1383100","1381652","1449","9.12","9.27","50779","ATGTCAGACAAGAAGAAGACGGGCGGTGCCTTCGCCCTTGCTCAGCGTCTGGGGAGATCCCTGATGCTGCCCATTGCCACGCTCCCGGCAGCGGGCCTGCTGCTGCGTCTGGGGCAGGCGGACATGCTGGGGGCCGAGGGCCTCGCCGCGAAGGCGTCCTGGTTGCAGCCCGTCGCAGACATCTTCAGTGCGGCCGGTGGGGCGGTCTTCGACAACCTGCCCCTTATCTTCGCCGTCGGCGTCGCCGTGGGCTTCGCCAAGAAGGCTGACGGCTCTACCGGGGTGGCCGCGCTGTTCGGCTTCCTCGTCTACCGGGCAGTCACCTGGACCATGTCCCCCATCATCTTGGGCGAGCCCGCGCCCCTGAGCAAGGAGGCCCTGGACTGCCTCCACTCCTTCGATCCCGCCACGGGGAAGATCGCACAGGTCGGACCCTGGAACCAGGGAGTCAAGCTCTGTGACATCCCCACCCAGACTCCGATCAACTACGGGGTCCTCGGCGGTATCGTCATCGGCGTCGTCGCCGCCCTGCTGTGGCAGCGCTACTACCGCGTCAAGCTGCCCGACTGGCTGGCCTTCTTCGGCGGACGCCGCTTCGTCCCCATCGTCACCTCCGGTGCCGCGCTGGTCATCGCCCTGGTCATGTCGGCGCTCTACCCGGCCTTCAACTGGCTCATCAACGAGCAGCTCGGCGGCTGGCTCATCAACGCCGGAAACTCCAAGGGCATCGCCGGAGCCCTGGCGGTCTTCGTCTTCGGTACCGTCAACCGCCTGCTCATCCCCTTCGGCCTGCACCACCTGCTCAACTCCGTGCCCTGGTTCCAGCTCGGCTCCTGCCAGACGGCCTCTGGGGACACGGCGCACGGTGACATCACCTGTTTCTTCCAGGGTGTGGACGGCTCGAACTCCTGGACCGGGGGCTTCACGACCGGCTTCTTCCCGATCATGATGTTCGCGCTGCCCGCCGCCGCACTGGCCATCTGGCATACGGCCAAGCCTGCCAAGCGCAAGGCGACCGGTGCCCTCATGATCTCTGTGGCCCTGACCGCTTTCATCACCGGTATCACTGAGCCCCTCGAGTACGCCTTCGCCTACGTGGCCTTCCCGATCTACGCCGTCCACGCGGTGCTGACCGGCTCCTCCCTGGCCATCGCCAACCTCCTGGGCGCCAAGGACGGCTTCGCCTTCTCCGCCGGGGCGATCGACTACCTGCTCAACTTCGGCAAGTCCGCTGAGCTCTCCGGTGGTGTGGTCCGCGGACCGCTCATGATCATCGTCATGGGGCTGGTCTACGCCGTCATCTACTACTTCCTCTTCAGGTTCCTCATCGTCAAGTTCGACTTCAAGACCCCTGGGCGCGAGGACGACGACGTCGATGCCTTCGCTGCCGCGCAGGCCGCTGCCGCCAAGTCCACGGGCAAGAAGGCTGCGGAGTCAACCCGGCGCTGA","MSDKKKTGGAFALAQRLGRSLMLPIATLPAAGLLLRLGQADMLGAEGLAAKASWLQPVADIFSAAGGAVFDNLPLIFAVGVAVGFAKKADGSTGVAALFGFLVYRAVTWTMSPIILGEPAPLSKEALDCLHSFDPATGKIAQVGPWNQGVKLCDIPTQTPINYGVLGGIVIGVVAALLWQRYYRVKLPDWLAFFGGRRFVPIVTSGAALVIALVMSALYPAFNWLINEQLGGWLINAGNSKGIAGALAVFVFGTVNRLLIPFGLHHLLNSVPWFQLGSCQTASGDTAHGDITCFFQGVDGSNSWTGGFTTGFFPIMMFALPAAALAIWHTAKPAKRKATGALMISVALTAFITGITEPLEYAFAYVAFPIYAVHAVLTGSSLAIANLLGAKDGFAFSAGAIDYLLNFGKSAELSGGVVRGPLMIIVMGLVYAVIYYFLFRFLIVKFDFKTPGREDDDVDAFAAAQAAAAKSTGKKAAESTRR$","Phosphotransferase system IIC component, glucose/maltose/N-acetylglucosamine-specific","Membrane, Cytoplasm","PtsC2 protein","putative PTS transmembrane component ","Protein-N(pi)-phosphohistidine--sugar phosphotransferase","","Saier Jr M.H., Reizer J. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 1992. 174(5):1433-1438. PMID: 1537788","","","

InterPro
IPR003352
Domain

Phosphotransferase system, EIIC
PF02378	$\"[18-379]T$	PTS_EIIC

InterPro
IPR013013
Domain

Phosphotransferase system, EIIC component, type 1
PS51103	$\"[8-455]T$	PTS_EIIC_TYPE_1

noIPR
unintegrated

unintegrated
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[21-39]?$ $\"[63-85]?$ $\"[95-115]?$ $\"[159-179]?$ $\"[199-219]?$ $\"[233-253]?$ $\"[258-276]?$ $\"[308-328]?$ $\"[338-358]?$ $\"[364-384]?$ $\"[389-411]?$ $\"[417-439]?$	transmembrane_regions

","BeTs to 6 clades of COG1263COG name: Phosphotransferase system IIC components, glucose/maltose/N-acetylglucosamine-specificFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1263 is -----------lb-efgh---j--twNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 379 (E_value = 6.3e-79) place ANA_1296 in the PTS_EIIC family which is described as Phosphotransferase system, EIIC.","","protein (PTS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1297","1383361","1384110","750","6.23","-3.40","27682","ATGCCCAAGAACGCAGGTAAGAAGCCGGCAAAGTACGTCATCGTGCGCAATCACCTGCTGGACCTGGTCAGGAACGGGCTCGCCAACGGCAGTCCGGTGCCCTCTGAGCGCGAGCTGTGCGAGCAGTTTGAGGTCTCCCGCATGACCGTGCGTCAGGCCATCGACACCCTCGTCGTCGACGGCGTCCTGGAGCGCCACCAGGGCAAGGGAACCTTCGTGGCGCCTCCCAAGCTCGACCTGCAGGTTCGGCTGACCTCCTTCACTCAGGAGATGCGACGCCGCGGGATGGAACCCGGCGTCGTCATGCTGCAGGCCGAGACCATCGCCTCCGATGAGACCGTGGCGGAGGCACTCGAGCTCGAGACCGGGGTCGAGGTCCACCACCTGCGTCGCCTCCTGACCGCCAACGCCATCCCCATGGCGATCGAGGAGAACTGGATTCCCGCAGCACTCCTGCCCAACCTGCTGCGCACCAGCCCGAACTTCTCGGTCTACGCCGAGCTGACCCAGGCCGACCTGGCGCCGCAGTGGGGCGAAGACATGATCGAGGCCCATGCGGCCACGGCCCAGGAGGCAGCGCTGCTCTCCGTCCAGGAGGGCGCCCCGACCCTGGACATCACTCGGCGCACCTTCCATGAGCACTGCGCCATCGACTACTCGCGCACCCTGTTCCGAGCCGACCGTTACACCCTGTGGGTCCCGGTGGCCGCCCCCAAACCCGCCTTCCGCCCCGACCGCTCGTCGTCTTGA","MPKNAGKKPAKYVIVRNHLLDLVRNGLANGSPVPSERELCEQFEVSRMTVRQAIDTLVVDGVLERHQGKGTFVAPPKLDLQVRLTSFTQEMRRRGMEPGVVMLQAETIASDETVAEALELETGVEVHHLRRLLTANAIPMAIEENWIPAALLPNLLRTSPNFSVYAELTQADLAPQWGEDMIEAHAATAQEAALLSVQEGAPTLDITRRTFHEHCAIDYSRTLFRADRYTLWVPVAAPKPAFRPDRSSS$","Transcriptional regulator, GntR family","Cytoplasm","GntR-family transcriptional regulator","K03710 GntR family transcriptional regulator","UbiC transcription regulator-associated domain protein","","Haydon D.J., Guest J.R. A new family of bacterial regulatory proteins. FEMS Microbiol. Lett. 1991. 63(2):291-295. PMID: 2060763Van aalten D.M., Dirusso C.C., Knudsen J., Wierenga R.K. Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. EMBO J. 2000. 19(19):5167-5177. PMID: 11013219Rigali S., Derouaux A., Giannotta F., Dusart J. Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies. J. Biol. Chem. 2002. 277(15):12507-12515. PMID: 11756427","","","

InterPro
IPR000524
Domain

Bacterial regulatory protein GntR, HTH
PR00035	$\"[33-47]T$ $\"[47-63]T$	HTHGNTR
PF00392	$\"[11-73]T$	GntR
SM00345	$\"[15-73]T$	HTH_GNTR
PS50949	$\"[9-76]T$	HTH_GNTR

InterPro
IPR011663
Domain

UbiC transcription regulator-associated
PF07702	$\"[93-230]T$	UTRA

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[4-73]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[30-74]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF1	$\"[30-74]T$	TRANSCRIPTION REGULATOR AMINOTRANSFERASE GNTR-RELATED

","BeTs to 7 clades of COG2188COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2188 is ---------drlb-efg----j---wNumber of proteins in this genome belonging to this COG is 2","***** IPB011663 (UbiC transcription regulator-associated) with a combined E-value of 1.1e-26. IPB011663 33-73***** IPB000524 (Bacterial regulatory protein, GntR family) with a combined E-value of 2.2e-22. IPB000524 33-73***** IPB011711 (GntR, C-terminal) with a combined E-value of 5.8e-10. IPB011711A 30-60","","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 73 (E_value = 1.9e-20) place ANA_1297 in the GntR family which is described as Bacterial regulatory proteins, gntR family.Residues 93 to 230 (E_value = 4.4e-34) place ANA_1297 in the UTRA family which is described as UTRA domain.","","transcriptional regulator (PA3757)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1298","1384314","1384544","231","4.23","-9.88","7972","ATGTCTCAGGCACAGAGCATCGTCGACGCCCTCGGAGGATTCGACAACATCGTGGAGATCGAGCCCTGCATCACGCGGCTGCGCTGCGAGCTGGAGGACGGTTCCCTTGTGGACGAGGCCGCCCTGAAGGCCGCAGGAGCGCACGGGGTCGTCAAGCTCGGCGAGATCGTGCAGGTCGTGGTCGGTCCCAACGCGGACACGATCGCAGAGGACATCGAGGACCTGCGGTGA","MSQAQSIVDALGGFDNIVEIEPCITRLRCELEDGSLVDEAALKAAGAHGVVKLGEIVQVVVGPNADTIAEDIEDLR$","Phosphotransferase system PTS, EIIB protein","Membrane, Cytoplasm","Sugar Specific PTS family,n-acetylglucosamine-specific enzyme IIABC","phosphotransferase system; N-acetylglucosamine-specific IIBC component","phosphotransferase system PTS, EIIB protein","","Postma P.W., Lengeler J.W., Jacobson G.R. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 1993. 57(3):543-594. PMID: 8246840Meadow N.D., Fox D.K., Roseman S. The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Annu. Rev. Biochem. 1990. 59:497-542. PMID: 2197982Saier Jr M.H., Reizer J. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 1992. 174(5):1433-1438. PMID: 1537788","","","

InterPro
IPR001996
Domain

Phosphotransferase system, EIIB
PF00367	$\"[4-38]T$	PTS_EIIB
PS51098	$\"[1-76]T$	PTS_EIIB_TYPE_1

noIPR
unintegrated

unintegrated
G3DSA:3.30.1360.60	$\"[2-76]T$	no description

InterPro
IPR001127
Domain

Phosphotransferase system, sugar-specific permease EIIA 1 domain
PD002243	$\"[5-128]T$	Q6A9Y1_PROAC_Q6A9Y1;
PF00358	$\"[2-132]T$	PTS_EIIA_1
TIGR00830	$\"[5-128]T$	PTBA: PTS system, glucose subfamily, IIA co
PS51093	$\"[21-128]T$	PTS_EIIA_TYPE_1
PS00371	$\"[70-82]T$	PTS_EIIA_TYPE_1_HIS

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PS00687	$\"[113-120]?$	ALDEHYDE_DEHYDR_GLU

noIPR
unintegrated

unintegrated
G3DSA:2.70.70.10	$\"[2-150]T$	no description

","BeTs to 7 clades of COG2190COG name: Phosphotransferase system IIA componentsFunctional Class: GThe phylogenetic pattern of COG2190 is --------EB-h--gpo----Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-58% similar to PDB:1F3G THREE-DIMENSIONAL STRUCTURE OF THE ESCHERICHIA COLI PHOSPHOCARRIER PROTEIN III GLC (E_value = 2.4E_21);-58% similar to PDB:1F3Z IIAGLC-ZN COMPLEX (E_value = 2.4E_21);-58% similar to PDB:1GGR COMPLEX OF ENZYME IIAGLC AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE (E_value = 2.4E_21);-58% similar to PDB:1GLA STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE (E_value = 2.4E_21);-58% similar to PDB:1GLB STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE (E_value = 2.4E_21);","Residues 139 to 271 (E_value = 3.2e-29) place ANA_1299 in the PTS_EIIA_1 family which is described as phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1.","","system, N-acetylglucosamine-specific IIABC component STY0723 (PTS)","","1","","","Fri Aug 3 12:38:16 2007","","Fri Aug 3 12:38:16 2007","","","Fri Aug 3 12:38:16 2007","Fri Aug 3 12:38:16 2007","Fri Aug 3 12:38:16 2007","","","Fri Aug 3 12:36:46 2007","","","Fri Aug 3 12:36:46 2007","Fri Aug 3 12:36:46 2007","","","Fri Aug 3 12:36:46 2007","Fri Aug 3 12:36:46 2007","","","","","yes","","" "ANA_1300","1387552","1385144","2409","5.10","-35.34","88192","ATGTCAGGAGACACGGTGCGGTGGGTGCACAACCCTCAGCCGCTAGGGCACACTTGGACACTGCTAGTCCTGCTAGCGCCCGCATCTCGATCCGACCCATCCATCCCCAGGGGTGATGGCGGAGCGCAACCCTGCTCCACGCCCGCTCCATGGCGCTCCATCGCACATCTGCTCACGCAAGGCGGACCCACGCACATGAACGAGTTCAACGACGACCTGTTACCTGCTTCCGAGAGCCTCAAGCAACTGGCTGAGGCGTACGGTGTCTCCACCGAGTACTGGGACTATCACGGCAACCTTGCCTCACCCTCAAGCGCTACTCTCAGGGCCGTGCTGGCCGCATTAGGGGTGAGCATCAACTCCGAGGAGGAGATCGGGCGCGCTCTGCGAGAGGTCGAGGACGCCCCCTGGCGGCAGGCGCTTGCCCCCACGGTCGTCACGCGCGGCGGTGTGGAGTCGACCGTCCCCGTCTACGTGCCCGACGGCGCCAAGGTGCGGGTGCGCGTCGAGCTCGAGAACGGGGACGTCCGTGAGCTGACTCAGACTGAGGACTGGACCGTGCCCCGTGAGGTGGACGGCGTCAAGCGCGGCCGTGCGTCCTTCATCCTCGGAGCCGATCTGCCCCTGGGATGGCACCGGATCATCGCCGAGGTCAGCCCCGGCTCCACGGACCAGGCCGCCCCGCAGGGGGCTCATGCCGCGCCGCCCGCCGACAGCGAGGCGGAGACCATCACCGTGACCTCGGCGCTGGCGGTCACCCCCAACCATCTCAATCTGCCCGAGTCTCTCGGAGACCGGGGCTGGGGGGTCATGACCCAGCTGTACTCGACCCGCTCGCGCGGGTCGTGGGGGACCGGTGACACCGACGATCTCACTGAGCTCGCCGCCTTCCTGGGGGACCAGGGAGCCGACTTCCTGCTCATCAACCCCCTGCACGCGGCTGAGCCGGTGGCGCCGATGACCCACTCGCCCTACCTGCCGGTGACACGCCGCTTCGTCAACCCCCTCTACATCCGGCCGGAGAATATCCCCGAGGTGGCCCGTCTGTCCGGCCCTAAGCGCTCGCTGGTGCAGTGGGCCTTCGAAGAGGTCAAGGACAGTGACCTCAGCGCCGAGCCGATCGACCGCGACGCGGTGTGGAAGGCCAAGCGCGAGGCCCTCGAGGTCATCTTCGCCGCCGGTCGCTCCTACTCCCGTCAGCGAGACTTCGAGCGCTTCCGGGCCGAGCAGGGCGAGGGGCTGGAGCGCTTCGCCCTGTGGAGCGCGCTGGTGGAGAAGCACGGGCCCCTGGACACCTGGCCCGCCACGCTGCGGGAGGCGGACTCCGCTTACGTCGCCAACGAGGCGCACCAGCTGGCCGAGCGCATCGACTTCTTCGCCTGGCTGCAGTGGATCGTCGACGAGCAGCTGGCTCGTGCCCAGGCCGAGGCGTTGGCCTCGGGGATGGCCCTGGGCATCATGGACGACCTCGCTGTCGGAGTGCACTCGCAGGGAGCCGACGTGTGGTCCAACCCGGAGGCCTTCGCCTCCGGAGTCACCGTGGGGGCTCCGCCGGACATGTACAACCAGCAGGGCCAGAACTGGTCCCAGCCGCCGTGGAACCCCGAGTACCTGGCGCGCAGCGCCTACGCCCCTCTGCGTGACATGGTGCGCACGGTCCTGCGTCACGCCGGCGCACTGCGCGTGGACCACATCATCGGCCTATTCCGCCTGTGGTGGATCCCCGAGGGCATGGGGGCGGACCATGGCGCCTACGTGCGCTACGACCACGAGGCCATGCTCGGCGTCGTCCTGCTGGAGGCTCACCGGGCCGGTGCCGTCGTCATCGGTGAGGACCTGGGGACCGTGGAGCCCTGGGCGCGCGACTACCTGGCCAGCCGCGGTGTGCTGGGGACCAGCGTCCTGTGGTTCGAGAAGCAGCACGACGGCTGGCCACTCCAGCCCCAGGACTACCGCAGGCTCGCCCTGTCCACGGTCAACACCCACGATCTTCCTCCGACTGCCGGCTACCTGGCCGACGAGCACGTCGATCTGCGTGAGCGCCTGGGCCTGCTCACCGAGCCGGTCGAGCAGGTGCGCACCGAGGCGCGCATCGAGCGCGACCGGATGACCGCCCGCCTGCGCGAGCACGGCCTGCTGGGGGACGCCCCCACCGAGCGTCAGGTCGTCGAAGCCCTGCACCGCTACGTGGTGCGCACCCCCTCAGTCCTGGTCGGCGTCGCCCTGGTCGACGGCGTGGGGGAGCGGCGCGCTCAGAACCAGCCCGGCACCGACCAGGAGTACCCCAACTGGCGGATCCCCCTGGCCGACGGCGCGGGCGAGGTCGTGTTGGTGGACGACCTGCCCGAGAACGCACGCCTGAGCAGTCTGCTGAGTGTCGTGCGCGACGAGATGGCTTCTCAGGACTGA","MSGDTVRWVHNPQPLGHTWTLLVLLAPASRSDPSIPRGDGGAQPCSTPAPWRSIAHLLTQGGPTHMNEFNDDLLPASESLKQLAEAYGVSTEYWDYHGNLASPSSATLRAVLAALGVSINSEEEIGRALREVEDAPWRQALAPTVVTRGGVESTVPVYVPDGAKVRVRVELENGDVRELTQTEDWTVPREVDGVKRGRASFILGADLPLGWHRIIAEVSPGSTDQAAPQGAHAAPPADSEAETITVTSALAVTPNHLNLPESLGDRGWGVMTQLYSTRSRGSWGTGDTDDLTELAAFLGDQGADFLLINPLHAAEPVAPMTHSPYLPVTRRFVNPLYIRPENIPEVARLSGPKRSLVQWAFEEVKDSDLSAEPIDRDAVWKAKREALEVIFAAGRSYSRQRDFERFRAEQGEGLERFALWSALVEKHGPLDTWPATLREADSAYVANEAHQLAERIDFFAWLQWIVDEQLARAQAEALASGMALGIMDDLAVGVHSQGADVWSNPEAFASGVTVGAPPDMYNQQGQNWSQPPWNPEYLARSAYAPLRDMVRTVLRHAGALRVDHIIGLFRLWWIPEGMGADHGAYVRYDHEAMLGVVLLEAHRAGAVVIGEDLGTVEPWARDYLASRGVLGTSVLWFEKQHDGWPLQPQDYRRLALSTVNTHDLPPTAGYLADEHVDLRERLGLLTEPVEQVRTEARIERDRMTARLREHGLLGDAPTERQVVEALHRYVVRTPSVLVGVALVDGVGERRAQNQPGTDQEYPNWRIPLADGAGEVVLVDDLPENARLSSLLSVVRDEMASQD$","4-alpha-glucanotransferase","Cytoplasm","4-alpha-glucanotransferase(Amylomaltase)(Disproportionating enzyme) (D-enzyme)","4-alpha-glucanotransferase ","4-alpha-glucanotransferase","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR003385
Family

Glycoside hydrolase, family 77
PF02446	$\"[272-795]T$	Glyco_hydro_77
TIGR00217	$\"[234-790]T$	malQ: 4-alpha-glucanotransferase

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[265-769]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide

","BeTs to 9 clades of COG1640COG name: 4-alpha-glucanotransferaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1640 is -------q-drl-cefgh-----it-Number of proteins in this genome belonging to this COG is 1","***** IPB003385 (Glycoside hydrolase, family 77) with a combined E-value of 2.5e-70. IPB003385A 277-290 IPB003385B 323-345 IPB003385C 458-493 IPB003385D 515-544 IPB003385E 545-577 IPB003385F 753-765","","","-38% similar to PDB:2OWC Structure of a covalent intermediate in Thermus thermophilus amylomaltase (E_value = 1.2E_21);-38% similar to PDB:2OWW Covalent intermediate in amylomaltase in complex with the acceptor analog 4-deoxyglucose (E_value = 1.2E_21);-38% similar to PDB:2OWX THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6 (E_value = 1.2E_21);-39% similar to PDB:1FP8 STRUCTURE OF THE AMYLOMALTASE FROM THERMUS THERMOPHILUS HB8 IN SPACE GROUP P21212 (E_value = 1.7E_20);-39% similar to PDB:1FP9 STRUCTURE OF AMYLOMALTASE FROM THERMUS THERMOPHILUS HB8 IN SPACE GROUP C2 (E_value = 1.7E_20);","Residues 272 to 795 (E_value = 8.3e-134) place ANA_1300 in the Glyco_hydro_77 family which is described as 4-alpha-glucanotransferase.","","(Amylomaltase)(Disproportionating enzyme) (D-enzyme) (malQ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1301","1388050","1387790","261","4.53","-6.85","8856","TTGCACGAGGGAGGGAACCGGGAAGGAGAAGCCATGAGCACTGCATCAGACATCGTCGCCGGTCTCGGCGGCCAGGAGAACATCACCGACCTCGAGCCCTGCATCACGCGCCTGCGCGTCGAGGTGGCCGATCAGACGAAGGTTGACGAGGAGGCGCTGCGAGCGGCCGGCGCCTTCGGCGTGGTGCGTTCGGGCCGCGTCGTCCAGGTCGTCGTGGGGCCCACGGCGGACAACCTCGCCTCAGAGATCGCAGCTCTCTGA","LHEGGNREGEAMSTASDIVAGLGGQENITDLEPCITRLRVEVADQTKVDEEALRAAGAFGVVRSGRVVQVVVGPTADNLASEIAAL$","Phosphotransferase system PTS, EIIB protein","Membrane, Cytoplasm","PtsB protein","PTS system; glucose-specific IIAB fragment","phosphotransferase system PTS, EIIB protein","","Postma P.W., Lengeler J.W., Jacobson G.R. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 1993. 57(3):543-594. PMID: 8246840Meadow N.D., Fox D.K., Roseman S. The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Annu. Rev. Biochem. 1990. 59:497-542. PMID: 2197982Saier Jr M.H., Reizer J. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 1992. 174(5):1433-1438. PMID: 1537788","","","

InterPro
IPR001996
Domain

Phosphotransferase system, EIIB
PF00367	$\"[15-49]T$	PTS_EIIB
PS51098	$\"[12-86]T$	PTS_EIIB_TYPE_1
PS01035	$\"[27-44]T$	PTS_EIIB_TYPE_1_CYS

noIPR
unintegrated

unintegrated
G3DSA:3.30.1360.60	$\"[7-86]T$	no description

","BeTs to 6 clades of COG1264COG name: Phosphotransferase system IIB componentsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1264 is -----------lb-efgh---j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB001996 (Phosphotransferase system PTS, EIIB domain) with a combined E-value of 5.2e-21. IPB001996A 18-61 IPB001996B 64-73***** IPB011535 (Phosphotransferase system, glucose-like IIB component) with a combined E-value of 1.2e-18. IPB011535A 15-48 IPB011535B 64-76","","","No significant hits to the PDB database (E-value < E-10).","Residues 15 to 49 (E_value = 1e-15) place ANA_1301 in the PTS_EIIB family which is described as phosphotransferase system, EIIB.","","protein (EII-Glc)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1302","1388385","1390082","1698","4.79","-26.11","59078","ATGACAGCGTCCGATACCACCTCCACAACCCTGTCCGGCATCGGTGTGAGCCCTGGCCTTGTGGCCGGCCCCGTCGCCAGGATGGCACCTCCCATTCCTGAGCCCGAGATCGCGACCCTCGAACCCAGTCGCGACATCGAGAAGGAGTGCGAGCGCATCGCGCTGGCGGCCCAACAGGTCAAGAAGGGCTTGGAGCTGTCCGCGGCCGAGGCCAAGGCCGAGGCCCGTACCCTCCTTGAGACCACCGCGCAGATGGCGGCCGACCCCACCCTGACCTCGACGGCACAGGCCATGGTGCGCGAGAAGCGCCTGGTTCCGGAGCGCGCCGTGTGGGAGTCCGCGGGAACGCTGGCCTCCATGCTGGAATCCCTGGGCGGCTACATGGCCGAGCGCACCCGCGACATCCAGGACGTGCGCGACCGCATCGTCGCCGTCCTGACCGAGTCCCCAATGCCGGGGATTCCCCGTCTGCCCGAGCCCTTCGTGCTCGTGGCGGCCGACCTGGCCCCGGCCGACACCGCGCTGCTGGACCCCGAGAAGGTCATCGCCTTCATCACCTCCGAGGGCGGCCCCACCTCCCACACCGCGATCCTGGCGCGCGCACTGGGCATGCCGGCGATCGTCGGCACTGGCGAGAAGGTCACCGACGCGCTGGCCGAGGGCGACATCGTCCTGGTCGACGGCACCAAGGGAAGCATCACCCTCAACCCCTCCGAGGACGCCCTGCGCCGGGCGCGGGAGCTCGCCTCGCGCGTGCGTGTCTTCAACGGTGACGGAGCCACGAAGGACGGCCACGAGGTCCAGCTGCTGGCCAATGTCGGTGACGCGGCCGGCGCCCGTAGCGCCGCCGAGGCCGGGGCCATGGGCATCGGCCTGTTCCGCACCGAGTTCTGCTTCCTGGACCAGCCCGAAGAGCCCACGGTGGAGGCTCAGGTGGAGGCCTACCAGGGTGTCCTCGAGGCCTTCCCCGGCAAGAAGGTCGTGGTGCGCACCCTCGACGCCGGAGCGGACAAGCCGCTGCCCTTCCTGACCGACGCCACCGAGGCCAACCCGGCGCTGGGCGTGCGCGCCTACCGCACGACGCGCCGCGACCCCGAGGTCCTGGACCACCAGCTCGAGGCCCTGGCCAAGGCCGAGGCCGCCACCGAGGCGAAGGTGTGGGTCATGGCCCCGATGATCTCCACGGCCGAGGAGGCCGAGGCCTTCACGCAGAAGGCCCGCTCCTACGGCCTGAAGACGGCCGGGATGATGATCGAGGTGCCCTCGGCCGCGCTCATGGCCGACAAGCTCTTTGAGCACGCCGACTTCGCCTCGGTGGGCACCAACGACCTCACCCAGTACGTCATGGCGGCCGACCGCCTGCTGTCCTCGCTGGCGGATCTGTCCACGGCCTGGCAGCCGGCCGTCCTGCGTCTGATCGGCACCGCCTGCGAGGGTGCCTCACCCAAGGGACGTCCGGTGGGCGTGTGCGGTGAGGCCGCCGCGGACCCGGCGCTGGCCGCCGTGCTCGTGGGTCTGGGGGTCGCCTCCCTGTCGATGACGGCGCGCGCACTGCCGGACGTCGACGCCGTCCTGAAGTCCGTCACGCTCACCGAGTGCCAGGAGCTGGCGAGGATCGCCCTGGACGCGGCGACGGCTGAGGACGCGCGCTCGGCGGTGCGCGCCAAGCTGCCGATCCTGGAGGAGCTCGGTCTGTGA","MTASDTTSTTLSGIGVSPGLVAGPVARMAPPIPEPEIATLEPSRDIEKECERIALAAQQVKKGLELSAAEAKAEARTLLETTAQMAADPTLTSTAQAMVREKRLVPERAVWESAGTLASMLESLGGYMAERTRDIQDVRDRIVAVLTESPMPGIPRLPEPFVLVAADLAPADTALLDPEKVIAFITSEGGPTSHTAILARALGMPAIVGTGEKVTDALAEGDIVLVDGTKGSITLNPSEDALRRARELASRVRVFNGDGATKDGHEVQLLANVGDAAGARSAAEAGAMGIGLFRTEFCFLDQPEEPTVEAQVEAYQGVLEAFPGKKVVVRTLDAGADKPLPFLTDATEANPALGVRAYRTTRRDPEVLDHQLEALAKAEAATEAKVWVMAPMISTAEEAEAFTQKARSYGLKTAGMMIEVPSAALMADKLFEHADFASVGTNDLTQYVMAADRLLSSLADLSTAWQPAVLRLIGTACEGASPKGRPVGVCGEAAADPALAAVLVGLGVASLSMTARALPDVDAVLKSVTLTECQELARIALDAATAEDARSAVRAKLPILEELGL$","Phosphoenolpyruvate-protein phosphotransferase","Cytoplasm","phosphoenolpyruvate-protein phosphotransferase","phosphoenolpyruvate-protein phosphotransferase ","phosphoenolpyruvate-protein phosphotransferase","","Reizer J., Hoischen C., Reizer A., Pham T.N., Saier Jr M.H. Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Protein Sci. 1993. 2(4):506-521. PMID: 7686067Reizer J., Reizer A., Merrick M.J., Plunkett I.I.I. G., Rose D.J., Saier Jr M.H. Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue that possesses a putative sensory transduction domain. Gene 1996. 181(1):103-108. PMID: 8973315Pocalyko D.J., Carroll L.J., Martin B.M., Babbitt P.C., Dunaway-Mariano D. Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs. Biochemistry 1990. 29(48):10757-10765. PMID: 2176881Unternahrer S., Hinnen A. Temperature sensitivity of the cdc9-1 allele of Saccharomyces cerevisiae DNA ligase is dependent on specific combinations of amino acids in the primary structure of the expressed protein. Mol. Gen. Genet. 1992. 232(2):332-336. PMID: 1557039Cosenza L.W., Bringaud F., Baltz T., Vellieux F.M. The 3.0 A resolution crystal structure of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei. J. Mol. Biol. 2002. 318(5):1417-1432. PMID: 12083528","","","

InterPro
IPR000121
Domain

PEP-utilizing enzyme
PD000940	$\"[290-490]T$	Q6AHH4_BBBBB_Q6AHH4;
PF02896	$\"[261-530]T$	PEP-utilizers_C

InterPro
IPR006318
Domain

Phosphoenolpyruvate-protein phosphotransferase
PR01736	$\"[291-310]T$ $\"[435-450]T$ $\"[452-467]T$ $\"[488-500]T$	PHPHTRNFRASE
TIGR01417	$\"[11-554]T$	PTS_I_fam: phosphoenolpyruvate-protein phos

InterPro
IPR008279
Domain

PEP-utilising enzyme, mobile region
PF00391	$\"[150-231]T$	PEP-utilizers
PS00370	$\"[189-200]T$	PEP_ENZYMES_PHOS_SITE

InterPro
IPR008731
Domain

phosphotransferase system, PEP-utilising enzyme, N-terminal
PF05524	$\"[11-132]T$	PEP-utilisers_N

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.60	$\"[248-561]T$	no description
G3DSA:3.50.30.10	$\"[144-234]T$	no description
PTHR22931	$\"[11-555]T$	PHOSPHOENOLPYRUVATE DIKINASE-RELATED
PTHR22931:SF10	$\"[11-555]T$	PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE

","BeTs to 11 clades of COG1080COG name: Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria)Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1080 is ---------d-lb-efghsn-j-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB008731 (PEP-utilising enzyme, N-terminal) with a combined E-value of 1.4e-112. IPB008731A 127-143 IPB008731B 169-209 IPB008731C 286-315 IPB008731D 330-360 IPB008731E 373-398 IPB008731F 430-473 IPB008731G 484-514***** IPB002192 (Pyruvate phosphate dikinase, PEP/pyruvate-binding) with a combined E-value of 2.5e-33. IPB002192E 184-209 IPB002192G 268-299 IPB002192I 348-357 IPB002192J 388-398 IPB002192K 437-455 IPB002192L 486-495","","","-49% similar to PDB:2HRO Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus (E_value = 4.9E_59);-43% similar to PDB:2HWG Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system (E_value = 2.0E_52);-48% similar to PDB:2BG5 CRYSTAL STRUCTURE OF THE PHOSPHOENOLPYRUVATE-BINDING ENZYME I-DOMAIN FROM THE THERMOANAEROBACTER TENGCONGENSIS PEP: SUGAR PHOSPHOTRANSFERASE SYSTEM (PTS) (E_value = 6.5E_35);-44% similar to PDB:1EZA AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE (E_value = 2.3E_16);-44% similar to PDB:1EZB AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 17 STRUCTURES (E_value = 2.3E_16);","Residues 11 to 132 (E_value = 2.3e-11) place ANA_1302 in the PEP-utilisers_N family which is described as PEP-utilising enzyme, N-terminal.Residues 150 to 231 (E_value = 1.1e-27) place ANA_1302 in the PEP-utilizers family which is described as PEP-utilising enzyme, mobile domain.Residues 246 to 530 (E_value = 3e-84) place ANA_1302 in the PEP-utilizers_C family which is described as PEP-utilising enzyme, TIM barrel domain.","","phosphotransferase (ptsI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1303","1390079","1391059","981","5.79","-7.62","35438","GTGACAACCCCATACCCCGTCCCCGCCGCCACGGAGGAGCCCCTCGGGTCGGTGACTCGAATCCTCAGTCTGGCGGCGGGTGACGGGGAGGATGTCTTCTCCGGGGGATCCCTCCCCCAGCTCTCGGGCAGGGTCTACGGAGGTCAGGTGGTGGCCCAGGGCATGCTTGCCGCGGCCGCCACGGTCGAGGACGACGGTGACGGTGAGCGTCTGCCGCACTCGGTCCACGCCTTCTTCATGCGGGGCGGGCAGCCCGATACGCCGATCACCTTCGCCGTCGAGCGCCTGCACGACGGACGCTCCTTCTCCCAGCGGCGCACCGCCGCCTCCCAGGAGGGCACGCCGATCCTGACGATGCTCACCTCCTTCCAGGAGGAGCAGGAGGGGGCCGACCTCCACGTGGCAGCCCCCGAGGTTCCGCGCCCTGAGGACTTGACGAGCGCTCTGGAGATCTTCCGAACCATCGATCATCCGGTGGCGCGTTTCCTGGGGCGCACGGCGGCCTTCGACCTCAGGCACGTGGAGGGCAACCTCTACCTGCGCCCCGCCAAGGAGCGTGCCGGTCGCCAGCACCTGTGGATGCGCTCGCGCAGCCGCATCCCGGAGCAGACCTCCCAGACCGTGCACCGGGCACTGCTGGCCTACGTGTGCGACCAGGTGATGCTGGAGCCGGTGCTGCGAAGCCAGGGACTGTCCTGGCGCAGTGAGGGCATGAGCCTGGCGACCCTCGACCACGCCCAGTGGTTCCACCGCGACGTCGACATGGGCGACTGGCTGCTCTACGTGCAGGACTCCCCCTCCTCACAGGGCGGCCGGGGCATGGCTCGCGCTCAGGTCTTCGACTCATCCGGTCGGCTGGTGTCGACCATCGCCCAGGAGGGCATGGTCCGCATGCCCACCGCTTCCACGTCCGACGGCGGTTCGGGACGTTGGCGGATCCGCATGGGAGAGGGCGACGACGGCAGCGCCATCCCCGGCTGA","VTTPYPVPAATEEPLGSVTRILSLAAGDGEDVFSGGSLPQLSGRVYGGQVVAQGMLAAAATVEDDGDGERLPHSVHAFFMRGGQPDTPITFAVERLHDGRSFSQRRTAASQEGTPILTMLTSFQEEQEGADLHVAAPEVPRPEDLTSALEIFRTIDHPVARFLGRTAAFDLRHVEGNLYLRPAKERAGRQHLWMRSRSRIPEQTSQTVHRALLAYVCDQVMLEPVLRSQGLSWRSEGMSLATLDHAQWFHRDVDMGDWLLYVQDSPSSQGGRGMARAQVFDSSGRLVSTIAQEGMVRMPTASTSDGGSGRWRIRMGEGDDGSAIPG$","Acyl-CoA thioesterase II","Periplasm, Membrane, Cytoplasm, Extracellular","acyl-CoA thioesterase II","acyl-CoA thioesterase II ","acyl-CoA thioesterase","","Naggert J., Narasimhan M.L., Deveaux L., Cho H., Randhawa Z.I., Cronan J.E., Green B.N., Smith S. Cloning, sequencing, and characterization of Escherichia coli thioesterase II. J. Biol. Chem. 1991. 266(17):11044-11050. PMID: 1645722","","","

InterPro
IPR003703
Family

Acyl-CoA thioesterase
PIRSF004843	$\"[9-305]T$	Acyl-CoA thioesterase II, TesB type
PTHR11066	$\"[30-301]T$	ACYL-COA THIOESTERASE
PF02551	$\"[28-130]T$ $\"[162-295]T$	Acyl_CoA_thio

noIPR
unintegrated

unintegrated
G3DSA:3.10.129.10	$\"[12-131]T$ $\"[142-297]T$	no description
PTHR11066:SF10	$\"[30-301]T$	ACYL-COA THIOESTERASE II

","BeTs to 7 clades of COG1946COG name: Acyl-CoA thioesteraseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1946 is ------y---r---efghs--j----Number of proteins in this genome belonging to this COG is 1","***** IPB003703 (Acyl-CoA thioesterase) with a combined E-value of 1.2e-56. IPB003703A 46-74 IPB003703B 83-123 IPB003703C 131-143 IPB003703D 205-228 IPB003703E 241-284","","","-52% similar to PDB:1C8U CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME (E_value = 1.1E_41);","Residues 28 to 130 (E_value = 3e-16) place ANA_1303 in the Acyl_CoA_thio family which is described as Acyl-CoA thioesterase.Residues 162 to 295 (E_value = 2.2e-18) place ANA_1303 in the Acyl_CoA_thio family which is described as Acyl-CoA thioesterase.","","thioesterase II (PA3942)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1304","1392010","1391306","705","8.40","4.75","25322","ATGAGTAGGAATACCCCAGGACTCATCCCCGAAGGCGGTGTCATCGGGAAACTTCCGTTCGACGGGCAGTGGTTGACCGAGCGCAGCCCCACACACCGCGTTCCCAGCCATGGGACTCACCTGTTCGCCACCACCTACGCGTTTGACTTCGTCGTCGTCGACGACGATGGTCTCACGGCTCCAGCACGCAGCATACGTGCGCTCTTCACCCCCGAACCGCCAGAGCTCTTCCACGCCTTCGGTCGTCCCTTGCACTCGCCCGTTGCGGGAACCGTGGTCTCCGTTCACGACGGCGAGCCCGACCACGTGGCGCGCCGTTCCGTCCTGACTCGCATCCCGTACGGATTGAGTCAGCCCCAACGAATTCGGCAGGGACTTCCCGCCATCCCTGGAAACCACATCATCATCCAGGTTGCCGAGGGGCCTCATTGCGTGGGACTCGTGCACCTTCAGCGAGGCTCCGTCCAGGTGTCGCCCGGCGACCGGGTGAGCGCAGGCGATCAGATCGGTCGATGCGGCAACTCCGGCAACTCCACGCAGCCCCACCTTCACATCCAAGCGATGGACAGTCCAGATCTCCGTACCGCGAAGGGGGTTCCGCTCCGTTTTGAGGAGTTCCGGCAACGCAGCCCGCAGCAGGGTGCTCCCTGGGCGCTTCGGCGACAGTCATGCCCCGAGCAGGGGGCGGTCGTCGCTCAACCTTGA","MSRNTPGLIPEGGVIGKLPFDGQWLTERSPTHRVPSHGTHLFATTYAFDFVVVDDDGLTAPARSIRALFTPEPPELFHAFGRPLHSPVAGTVVSVHDGEPDHVARRSVLTRIPYGLSQPQRIRQGLPAIPGNHIIIQVAEGPHCVGLVHLQRGSVQVSPGDRVSAGDQIGRCGNSGNSTQPHLHIQAMDSPDLRTAKGVPLRFEEFRQRSPQQGAPWALRRQSCPEQGAVVAQP$","Peptidase M23B","Cytoplasm, Extracellular","possible secreted peptidase","secreted peptidase","peptidase M23B","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR002886
Family

Peptidase M23B
PTHR21666:SF7	$\"[131-184]T$	M23/M37 PEPTIDASE FAMILY MEMBER
PF01551	$\"[124-184]T$	Peptidase_M23

noIPR
unintegrated

unintegrated
PTHR21666	$\"[131-184]T$	PEPTIDASE-RELATED

","BeTs to 16 clades of COG0739COG name: Membrane proteins related to metalloendopeptidasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0739 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 4","***** IPB002886 (Peptidase M23/M37) with a combined E-value of 1.1e-06. IPB002886B 132-176","","","No significant hits to the PDB database (E-value < E-10).","Residues 86 to 203 (E_value = 2.6e-08) place ANA_1304 in the Peptidase_M23 family which is described as Peptidase family M23.","","secreted peptidase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1305","1391070","1391315","246","7.91","1.55","8994","TTGAAGACACGGATCGAGGACTGCGTTCTCCATCCAGGACGTACTTCTCCCCCATACGACTGCGGCCGGATCTCAGAGGTTTGCAGGAGAACGCAGTCCTCGCCGGAGAAGTACGTCCCCATTCAGGAGCTGCGCACTGCGCCGCAGGCCCATCCCCCGATTCTCGCCACGATCTGGTCGCAGCGCCCCGCGACCGATCAGCACGCCGGATCTGAGGCTCCTTCCATGACGCCATATCAAGGTTGA","LKTRIEDCVLHPGRTSPPYDCGRISEVCRRTQSSPEKYVPIQELRTAPQAHPPILATIWSQRPATDQHAGSEAPSMTPYQG$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1306","1393849","1392167","1683","5.18","-19.61","61764","GTGGCTGAGTACATCTACCAGATGATTAAGGCGCGCAAGGCCCACGGTGACAAGGTCATCCTCGATGACGTCACCATGGCCTTCCTCCCCGGAGCCAAGATCGGCATGGTCGGCCCCAACGGCGCCGGCAAGTCCTCCATCCTCAAGATCATGGCCGGCATCGACCAGCCCTCCAACGGCGAGGCCCGCCTGACCCCCGGCTACAGCGTCGGCATCCTCCTGCAGGAGCCCCCGCTCAACGAGGACAAGACGGTGCTCGGCAACGTCGAGGAGGGCGTTGCCGAGATCAAGTCCAAGCTGGACCGCTATAACGAGATCAGCGCCGCCATGGCGGACCCGGACGCCGACTTCGACGCCCTCATGGCGGAGATGGGCACCCTCCAGGACGCCCTGGACGCCGCCAACGCCTGGGACCTCGACTCCCAGCTCGAGCAGGCCATGGACGCCCTGCGCTGCCCCCCGCCGGACGCCGAGGTCAAGCACCTCTCCGGTGGTGAGCGCCGCCGCGTCGCCCTGTGCAAACTGCTTCTCGAGGCCCCCGACCTCCTCCTCCTGGACGAGCCCACCAACCACCTCGACGCCGAGTCCGTGCTCTGGCTCGAGCAGCACCTGGCCAGCTACCAGGGCGCCGTCATCGCCGTCACCCACGACCGCTACTTCCTTGACCACGTCGCCGAGTGGATCGCCGAGGTCGACCGCGGCCACCTCTACCCCTACGAGGGCAACTACTCCACCTACCTGGAGACCAAGGAGAAGCGCCTCGAGGTCCAGGGCAAGAAGGACGCCAAGCTCGCCAAGCGCCTCAAGGAGGAGCTCGAGTGGGTGCGCTCCTCGGCCAAGGGACGCCAGGCCAAGTCCAAGGCCCGTCTGGCCCGCTACGAGGAGATGGCCGCCGAGGCCGAGCGCACCCGCAAGCTCGACTTCGAGGAGATCCAGATCCCGCCGGGGCCCCGCCTGGGCAACCAGGTCCTGGAAGCCACCAACCTCAACAAGGGCTTCGACGGGCGCACCCTCATCGACGGGCTCTCCTTCACCCTGCCGCGCAACGGCATCGTCGGGGTCGTCGGCCCCAACGGCGTCGGCAAGTCCACCCTGTTCAAGACCATCGTGGGCCTGGAGCCGCTCGACGGCGGAGACCTCAAGATCGGTCAGACCGTCAAGCTCTCCTACGTCGACCAGTCCCGAGCCGGCATCGACCCCAAGAAGACCCTCTGGGAGGTCGTCTCTGACGGGCTGGACTACATCCAGGTCGGCAACGTGGAGATGCCCTCGCGCGCCTACGTCGCCTCCTTCGGCTTCAAGGGGGCCGACCAGCAGAAGCCGGCCGGCGTCCTCTCCGGCGGAGAGCGCAACCGCCTCAACCTGGCCCTGACCCTCAAGCAGGGCGGCAACCTCATCCTCCTGGACGAGCCCACCAACGACCTCGACGTCGAGACCCTGGGCTCCCTGGAGAACGCCCTGCTGGAGTTCCCCGGCTGCGCCGTGGTCATCACCCACGACCGCTGGTTCCTCGACCGCGTGGCCACCCACATCCTGGCCTGGGAGGGAACGGATGAGAACCCCGCCAGCTGGTACTGGTTCGAGGGGAACTTCGCCTCCTACGAGGAGAACAAGGTCGAGCGCCTTGGCCCCGAGGCGGCCCGCCCCCACCGGGTCACCTACCGGAAGCTGACTCGAGACTGA","VAEYIYQMIKARKAHGDKVILDDVTMAFLPGAKIGMVGPNGAGKSSILKIMAGIDQPSNGEARLTPGYSVGILLQEPPLNEDKTVLGNVEEGVAEIKSKLDRYNEISAAMADPDADFDALMAEMGTLQDALDAANAWDLDSQLEQAMDALRCPPPDAEVKHLSGGERRRVALCKLLLEAPDLLLLDEPTNHLDAESVLWLEQHLASYQGAVIAVTHDRYFLDHVAEWIAEVDRGHLYPYEGNYSTYLETKEKRLEVQGKKDAKLAKRLKEELEWVRSSAKGRQAKSKARLARYEEMAAEAERTRKLDFEEIQIPPGPRLGNQVLEATNLNKGFDGRTLIDGLSFTLPRNGIVGVVGPNGVGKSTLFKTIVGLEPLDGGDLKIGQTVKLSYVDQSRAGIDPKKTLWEVVSDGLDYIQVGNVEMPSRAYVASFGFKGADQQKPAGVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLGSLENALLEFPGCAVVITHDRWFLDRVATHILAWEGTDENPASWYWFEGNFASYEENKVERLGPEAARPHRVTYRKLTRD$","Macrolide-transport ATP-binding protein ABC transporter","Cytoplasm, Membrane","ATP binding protein of ABC transporter","probable macrolide-transport ATP-binding protein ABC transporter","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[161-204]T$ $\"[445-487]T$	Q9X7B1_MYCLE_Q9X7B1;
PF00005	$\"[31-234]T$ $\"[349-517]T$	ABC_tran
PS50893	$\"[6-258]T$ $\"[324-541]T$	ABC_TRANSPORTER_2
PS00211	$\"[162-176]?$ $\"[445-459]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[30-242]T$ $\"[348-518]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-281]T$ $\"[286-512]T$	no description
PTHR19211	$\"[134-541]T$	ATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19211:SF7	$\"[134-541]T$	ABC TRANSPORTER ABCF3, UUP

","BeTs to 16 clades of COG0488COG name: ATPase components of ABC transporters with duplicated ATPase domainsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0488 is ------y--drlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 4","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.4e-20. IPB005074C 338-385 IPB005074D 433-476***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 2.8e-13. IPB010509B 31-56 IPB010509D 157-201 IPB010509D 440-484***** IPB005116 (TOBE domain) with a combined E-value of 3.1e-13. IPB005116A 38-54 IPB005116C 162-175 IPB005116D 182-201 IPB005116D 465-484***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 6.2e-12. IPB013563A 338-372 IPB013563C 442-469***** IPB013283 (ABC transporter family E signature) with a combined E-value of 4.2e-07. IPB013283D 35-60 IPB013283D 353-378***** IPB010929 (CDR ABC transporter) with a combined E-value of 8.9e-07. IPB010929K 18-62 IPB010929M 159-205","","","-42% similar to PDB:2IW3 ELONGATION FACTOR 3 IN COMPLEX WITH ADP (E_value = 2.5E_10);-42% similar to PDB:2IWH STRUCTURE OF YEAST ELONGATION FACTOR 3 IN COMPLEX WITH ADPNP (E_value = 2.5E_10);-42% similar to PDB:2IX3 STRUCTURE OF YEAST ELONGATION FACTOR 3 (E_value = 2.5E_10);","Residues 31 to 234 (E_value = 1.7e-50) place ANA_1306 in the ABC_tran family which is described as ABC transporter.Residues 349 to 517 (E_value = 1.6e-40) place ANA_1306 in the ABC_tran family which is described as ABC transporter.","","binding protein of ABC transporter (ABC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1307","1394167","1396278","2112","7.87","6.66","76680","ATGCCGGATTTGGACAGCGAATCGCTGTATAGGGCCCTGTTGGCCAAGGACACCCGATTCGACGGACGGTTCTTCGTTGGGGTCGCAACGACCGGTGTCTATTGCCGCCCAGTGTGCCGGGCGCGGAAACCGCTTGCGGTCAACTGCTCCTTCTACGCCACGGCAGCCGAGGCCGAACAAGCGGGGTTCCGCCCCTGTCTGCTGTGCCGGCCCGAGCTGGCACCCGGGTACGCCCCCGTGGACTCTTCGGCATCACTGGCTCGCGCCGCAGCACGGTACATCGAGAGGAACTGTGGTGTTCAGGGAAGCCTGACGGATATCGCCCGTCATCTGGGCTGCTCCAACCGCCACCTGCGCCGTGTCTTCGAGGACGCTTATCACGTGCGTCCCGTGGAGTACCGCCAGACCTGCAGACTTCTGCTGGCCAAGAGTCTTTTGACCGACACGGACCTATCAGTGGTGGACGTGGCCTATGCGGCGGGGTTCGGCAGCCTGCGCCGCTTCAACGAGGTGTTCCGACGTCGCTACCGGCTGACGCCCACCGCTTTGCGCAGCCAAGCACGGCTCAACAGGGCCGACGGTGACACCGTCCAGCTCAGTCTGGGGTACCGTCCCCCATACCGTTGGGACCTCATACTGAAGTTCCTGGCACGCAGAGCCATCCCCGGCGTCGAGAAGGTAGAAGACGATCGTTACGCCAGGACGATCCGCCTGCGCTCCTCAGGACGTGATCTCACAGGCTGGGTGGCCGTGGGCAACGACTCCGAGCACAATCGGCTGGCGGTAACCGTCTCCGCCTCACTGCTATCCGCACTACCGGTGGTGCTGGACGGGATCAAAAATCTGTTCGATCTCCACTGCGAGCCCGATACCGTGGCTGGCGCACTCACAAGCATGGATGACTCCACGCTCGGACCATTCATCCCGGGCACACGTGTGCCCGGCTGCTTCGACGCCTTCGAAACCGCTGTCCTCGCGGTCCTGGGTCAGCAGGTCACGGTCCAGGCAGCCAGGACGCTGGCCGGTCGGCTCGTCCAGGCCCTCGGTTCACCCGTGGACACCGGAATCGACGGACTGACCACGACTTTCCCCACGGTTCAGGAGCTCCTCAACCTCGACGGTGCGATCGAGCAGCATCTAGGACCGCTCGGCATCATTGCTGCCCGGGCACGGGCTATTCACGGACTGGCCGCGATGATGAGTTCCGGCATCATCGACGCCTCCTGCTGCCCCGACCCTGAAGCCGCAGTTACTCGGTTCATGGAGATCCCGGGCATTGGAGCCTGGACCGCCAACTATATCGCCATGCGCTGCCTGGCTTGGCCCGATGCATTCCTCGCCACCGACCTGGAGGTCAGAAAGGCGCTGGGAAACCCGCCCACAGGGAAGATCCTCACCCTGGCCGAATGTTGGAAACCGTGGCGGGCCTACGCCGTCATGCACCTGTGGAACCGGGCAGAAGCAGAAGCAGCGTCCGAACACGCCACCAAGAGCAAGAAGCGGAACGAGAAGAAGGAAGAGATGCACTATCTCAGCCATTACGAGTCGCCCTTGGGAGCCATGACCATGGCCAGCGACGGCGAGCACCTGACAGGCCTGTGGTTCGATGGTCAGAAGTACGACCGCTCGACGATCGACGGCAACGCAGAGCTCAAGCCACATCTGCCCGTCTTCACGCAGACCGCCCAGTGGCTCGACGCCTACTTCGGGGGCACTGACCCGGGTTTCACTCCGCCGATCAGGGTTGAGGGCTCCGACTTCAAGAGGATGGTCTCCTCCATCATGCTCTCCATCCCCTTCGGCGCCACCAGCACCTATGCCCAGATCGCTGCCGAGGTGGCCCGGCGTACTGGCCGGAGGCACATGTCCGCCCAGGCCGTGGGCGGCGCGGTCGGACACAACCCGATCTCTCTTATCGTGCCGTGCCACCGCGTGCTCGCCTCCGACGGGGGCCTGCGCGGTTACGCCGGAGGAGTCGACCGTAAGGAATGGCTCCTGAAGATGGAGGCGTCAACATGTCTGGCCCGACAACCGCTGGCGACGGCGGTGGAAGGCGAGAATGAAAAGGCCGACCGCGGCCCAAATCACACCTTGGAGAATCCAGGTGATTGA","MPDLDSESLYRALLAKDTRFDGRFFVGVATTGVYCRPVCRARKPLAVNCSFYATAAEAEQAGFRPCLLCRPELAPGYAPVDSSASLARAAARYIERNCGVQGSLTDIARHLGCSNRHLRRVFEDAYHVRPVEYRQTCRLLLAKSLLTDTDLSVVDVAYAAGFGSLRRFNEVFRRRYRLTPTALRSQARLNRADGDTVQLSLGYRPPYRWDLILKFLARRAIPGVEKVEDDRYARTIRLRSSGRDLTGWVAVGNDSEHNRLAVTVSASLLSALPVVLDGIKNLFDLHCEPDTVAGALTSMDDSTLGPFIPGTRVPGCFDAFETAVLAVLGQQVTVQAARTLAGRLVQALGSPVDTGIDGLTTTFPTVQELLNLDGAIEQHLGPLGIIAARARAIHGLAAMMSSGIIDASCCPDPEAAVTRFMEIPGIGAWTANYIAMRCLAWPDAFLATDLEVRKALGNPPTGKILTLAECWKPWRAYAVMHLWNRAEAEAASEHATKSKKRNEKKEEMHYLSHYESPLGAMTMASDGEHLTGLWFDGQKYDRSTIDGNAELKPHLPVFTQTAQWLDAYFGGTDPGFTPPIRVEGSDFKRMVSSIMLSIPFGATSTYAQIAAEVARRTGRRHMSAQAVGGAVGHNPISLIVPCHRVLASDGGLRGYAGGVDRKEWLLKMEASTCLARQPLATAVEGENEKADRGPNHTLENPGD$","3-Methyladenine DNA glycosylase; transcriptional regulator, AraC family","Cytoplasm, Extracellular","DNA methylation and regulatory protein Ada or","transcriptional regulator; AraC family","methylated-DNA--protein-cysteine methyltransferase","","Tainer J.A., Thayer M.M., Cunningham R.P. DNA repair proteins. Curr. Opin. Struct. Biol. 1995. 5(1):20-26. PMID: 7773744Vassylyev D.G., Morikawa K. DNA-repair enzymes. Curr. Opin. Struct. Biol. 1997. 7(1):103-109. PMID: 9032058Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 1992. 174(20):6321-6325. PMID: 1328155Kuo C.F., McRee D.E., Fisher C.L., O. Handley S.F., Cunningham R.P., Tainer J.A. Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III. Science 1992. 258(5081):434-440. PMID: 1411536Guan Y., Manuel R.C., Arvai A.S., Parikh S.S., Mol C.D., Miller J.H., Lloyd S., Tainer J.A. MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily. Nat. Struct. Biol. 1998. 5(12):1058-1064. PMID: 9846876Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Chepanoske C.L., Golinelli M.P., Williams S.D., David S.S. Positively charged residues within the iron-sulfur cluster loop of E. coli MutY participate in damage recognition and removal. Arch. Biochem. Biophys. 2000. 380(1):11-19. PMID: 10900127","","","

InterPro
IPR000005
Domain

Helix-turn-helix, AraC type
PR00032	$\"[153-168]T$ $\"[168-184]T$	HTHARAC
PF00165	$\"[89-135]T$ $\"[141-185]T$	HTH_AraC
SM00342	$\"[101-184]T$	HTH_ARAC
PS01124	$\"[88-186]T$	HTH_ARAC_FAMILY_2
PS00041	$\"[138-180]T$	HTH_ARAC_FAMILY_1

InterPro
IPR001497
Active_site

Methylated-DNA-[protein]-cysteine S-methyltransferase, active site
PS00374	$\"[640-646]?$	MGMT

InterPro
IPR003265
Domain

HhH-GPD
PF00730	$\"[324-473]T$	HhH-GPD
SM00478	$\"[328-487]T$	ENDO3c

InterPro
IPR004026
Domain

Ada, metal-binding
PF02805	$\"[7-72]T$	Ada_Zn_binding

InterPro
IPR010316
Domain

AlkA, N-terminal
G3DSA:3.30.310.20	$\"[198-318]T$	no description
PF06029	$\"[198-318]T$	AlkA_N

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[584-669]T$	no description

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[139-191]T$	no description

InterPro
IPR014048
Domain

Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
PF01035	$\"[584-674]T$	DNA_binding_1
TIGR00589	$\"[585-669]T$	ogt: methylated-DNA-[protein]-cysteine S-me

noIPR
unintegrated

unintegrated
G3DSA:1.10.1670.10	$\"[442-493]T$	no description
G3DSA:1.10.340.30	$\"[319-441]T$	no description
G3DSA:3.40.10.10	$\"[4-89]T$	no description
PTHR10815	$\"[549-669]T$	METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE

","BeTs to 6 clades of COG0122COG name: 3-Methyladenine DNA glycosylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0122 is aom-kzy--dr-bcefg-s--j----Number of proteins in this genome belonging to this COG is 1","***** IPB004026 (Metal binding domain of Ada) with a combined E-value of 3.9e-46. IPB004026A 16-49 IPB004026B 52-71 IPB004026C 103-134 IPB004026E 153-182***** IPB001497 (Methylated-DNA-[protein]-cysteine S-methyltransferase) with a combined E-value of 2.1e-16. IPB001497 617-656***** IPB000005 (Helix-turn-helix, AraC type) with a combined E-value of 3.9e-09. IPB000005 153-184","","","-44% similar to PDB:1DIZ CRYSTAL STRUCTURE OF E. COLI 3-METHYLADENINE DNA GLYCOSYLASE (ALKA) COMPLEXED WITH DNA (E_value = 9.1E_34);-44% similar to PDB:1MPG 3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI (E_value = 9.1E_34);-44% similar to PDB:1PVS 3-methyladenine Glcosylase II(AlkA) Hypoxanthine complex (E_value = 9.1E_34);-52% similar to PDB:1ZGW NMR structure of E. Coli Ada protein in complex with DNA (E_value = 3.9E_16);-52% similar to PDB:1U8B Crystal structure of the methylated N-ADA/DNA complex (E_value = 6.6E_16);","Residues 7 to 72 (E_value = 2.4e-39) place ANA_1307 in the Ada_Zn_binding family which is described as Metal binding domain of Ada.Residues 89 to 135 (E_value = 5.7e-06) place ANA_1307 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, AraC family.Residues 141 to 185 (E_value = 1.1e-07) place ANA_1307 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, AraC family.Residues 198 to 318 (E_value = 4.2e-32) place ANA_1307 in the AlkA_N family which is described as AlkA N-terminal domain.Residues 324 to 473 (E_value = 0.00014) place ANA_1307 in the HhH-GPD family which is described as HhH-GPD superfamily base excision DNA repair protein.Residues 584 to 674 (E_value = 1e-27) place ANA_1307 in the DNA_binding_1 family which is described as 6-O-methylguanine DNA methyltransferase, DNA binding domain.","","methylation and regulatory protein Ada or","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1308","1398372","1397251","1122","4.67","-29.26","41111","GTGGCCACTGACTTCTCCGCTGAGATCGAACGACTCCGACACACCTACGCCTCCATTGCCGCGGTGACCGACCCCGAGGCCCTGCGCGCCCGGATCGCCGAGCTCTCCGAGCAGGCCTCCGCACCCGACCTGTGGGATGACCCCGACTCCGCCCAGGTGGTCACCTCCGCGCTGTCCCACGCCCAGGCCGACCTCAAGCGGGTCGAGAGCCTGGGGGAGCGCATCGAGGACCTCGAGGCGATGGTCGAGCTCGCCGGTGAGGAGGAGGGCGAGGACGCCGCCGAGATCCTCGCCGAGGCCGAGACGGACCTGGCGGCCATCAGCAAGGACCTCTCCGACCTGGAGATCCGCACGCTGCTCAGCGGCGAGTACGACCCCCGCGACGCCGTCATCACCATCCGCTCGGGCGCCGGCGGCGTGGACGCCGCCGACTTCGCCGAGATGCTCCTGCGCATGTACACCCGCTGGGCCGAGCGGCACGACTACCCCGTCAAGGTCCTCAACACCTCCTACGCCGAGGAGGCGGGCCTGAAGTCGGTCACCTTCGAGGTCCACGCCCCCTACGCCTACGGGACCCTGAGCGTCGAGGGCGGCACGCATCGCCTGGTGCGTATCAGCCCCTTCGACAACCAGGGCCGCCGCCAGACCTCCTTCGCCGCCGTCGAGGTCATCCCGCTCATCGAGTCCACCGACCACATCGACATCCCCGAGACCGACATCCGCATCGACGTCTTCCGCTCCTCGGGACCCGGCGGGCAGAGCGTCAACACCACCGACTCCGCCGTGCGCATCACCCACCTGCCCACGGGCCTGGTGGTCTCCATGCAGGACGAGAAGTCCCAGATCCAGAACCGCGCCGCCGCCATGCGCGTCCTCCAGTCGCGCCTGCTCCTGCTCAAGCAGCAGGAGGAGGACGCCAAGAAGAAGGAGCTCGCCGGGGACGTCAAGGCCTCCTGGGGGGACCAGATGCGCTCCTACGTTCTCAACCCCTATCAGATGGTCAAGGACCTGAGGACCAACTTCGAGGTCGGCAATCCTGATTCGGTGTTCGACGGCGACATCGACGGCTTCATCGACGCCGGCATCCGCTGGCGCAAGCAGCAGGAAACGGCCGAGGACTGA","VATDFSAEIERLRHTYASIAAVTDPEALRARIAELSEQASAPDLWDDPDSAQVVTSALSHAQADLKRVESLGERIEDLEAMVELAGEEEGEDAAEILAEAETDLAAISKDLSDLEIRTLLSGEYDPRDAVITIRSGAGGVDAADFAEMLLRMYTRWAERHDYPVKVLNTSYAEEAGLKSVTFEVHAPYAYGTLSVEGGTHRLVRISPFDNQGRRQTSFAAVEVIPLIESTDHIDIPETDIRIDVFRSSGPGGQSVNTTDSAVRITHLPTGLVVSMQDEKSQIQNRAAAMRVLQSRLLLLKQQEEDAKKKELAGDVKASWGDQMRSYVLNPYQMVKDLRTNFEVGNPDSVFDGDIDGFIDAGIRWRKQQETAED$","Peptide chain release factor 2","Cytoplasm","peptide chain release factor 2","peptide chain release factor 2","peptide chain release factor 2","","Tate W.P., Poole E.S., Mannering S.A. Hidden infidelities of the translational stop signal. Prog. Nucleic Acid Res. Mol. Biol. 1996. 52:293-335. PMID: 8821264Craigen W.J., Lee C.C., Caskey C.T. Recent advances in peptide chain termination. Mol. Microbiol. 1990. 4(6):861-865. PMID: 2215213Pel H.J., Rep M., Grivell L.A. Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure. Nucleic Acids Res. 1992. 20(17):4423-4428. PMID: 1408743","","","

InterPro
IPR000352
Domain

Class I peptide chain release factor
PF00472	$\"[226-338]T$	RF-1
PS00745	$\"[246-262]T$	RF_PROK_I

InterPro
IPR004374
Family

Peptide chain release factor 2
PIRSF500106	$\"[1-370]T$	Peptide chain release factor 2
PTHR11075:SF6	$\"[11-369]T$	PEPTIDE CHAIN RELEASE FACTOR 2
TIGR00020	$\"[1-366]T$	prfB: peptide chain release factor

InterPro
IPR005139
Domain

PCRF
PF03462	$\"[83-196]T$	PCRF

InterPro
IPR012086
Family

Protein chain release factor, RF-1/RF-2
PIRSF003056	$\"[21-373]T$	Protein chain release factor, RF-1/RF-2

noIPR
unintegrated

unintegrated
PTHR11075	$\"[11-369]T$	PEPTIDE CHAIN RELEASE FACTOR

","BeTs to 16 clades of COG1186COG name: Protein chain release factor BFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1186 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000352 (Class I peptide chain release factor domain) with a combined E-value of 5.2e-110. IPB000352A 119-168 IPB000352B 175-226 IPB000352C 239-284 IPB000352D 324-351","","","-57% similar to PDB:2IHR RF2 of Thermus thermophilus (E_value = 2.4E_64);-57% similar to PDB:2B9M 30S ribosomal subunit, tRNAs, mRNA and release factor RF2 from a crystal structure of the whole ribosomal complex. This file contains the 30S ribosomal subunit, tRNAs, mRNA and release factor RF2 from a crystal structure of the whole ribosomal complex\". The entire crystal structure contains one 70S ribosome, tRNAs, mRNA and release factor RF2 and is described in remark 400. (E_value = 6.9E_64);-60% similar to PDB:1ML5 Structure of the E. coli ribosomal termination complex with release factor 2 (E_value = 7.7E_63);-60% similar to PDB:1GQE POLYPEPTIDE CHAIN RELEASE FACTOR 2 (RF2) FROM ESCHERICHIA COLI (E_value = 1.7E_62);-60% similar to PDB:1MI6 Docking of the modified RF2 X-ray structure into the Low Resolution Cryo-EM map of RF2 E.coli 70S Ribosome (E_value = 1.7E_62);","Residues 83 to 196 (E_value = 3.3e-46) place ANA_1308 in the PCRF family which is described as PCRF domain.Residues 226 to 338 (E_value = 8.1e-62) place ANA_1308 in the RF-1 family which is described as Peptidyl-tRNA hydrolase domain.","","chain release factor 2 (prfB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1309","1399384","1398473","912","5.06","-10.85","32405","ATGCAGGTATTGCCCCAGAGGCTCTCGGTTCTATTGGCCGTCCATCGAGCCGGAGGAGTCGTCGCAGCGGCAGATTTCCTTCATATAACGCCGTCGGCGGTCTCCCAGCAGATTCGCCTCCTGGAGCGCGAGTGCGGCGCCCGGGTCCTGGATCGCACGCCCACCGGAGCCGTGCTCACGGCGGCCGGGAAGGTTCTGGCGGACGCGGCCGAGCGCATCGAGGACGAGCTGACCACCGTGCGCCGCGAGCTGGCGGACCTGGACGACTCCATCCCCTCCGGTGTGGTGCGTGTCGCGAGCTTCGCCTCCGCCGTCCGGGCGCTCCTGCTGCCCCTCCTCAGCTCGCTGGCGATGACCAGCCCCGAGCTGGAGGTGATCGTCGAGGAGGCCGAGGAGCGCAACGCCCTGCCCCGCCTGCGTCGCGGTGAGCTCGACCTGGTCCTCATCGAGCGTGACGAGCACACGCTGCCCGCGGCGCCTCGGGGCATGGTCGACATCCCACTGCTGGACGAGTCCTGGCTCGTCGTCGTGCCGGCTGAGCAGGCGGCCCCCTCGACCCTGGCGGACCTGGCGCGCGCCACCTGGATCGACCTGGCCCCGGGGACCGCGGGCGCCTTCGCCCTGGACCGTCTCGAGCGTCAGCTGGGGGTGCCGTTGACGACACGGCACGTCGCCTACGACTACGACGTCGTCCTGGCCATGGTCAGTCAGGGCCTGGGCTGCGCGCTTCTGCCCGAGCTGGCCGTCTACTCCGGGCTCGTCCCCGATGAGCTCAGTGTGGTGCGCCTACCCGGGCTGGGCGTGCGCCAGCTGGTGGTGCGCCACCGACAGACCCGCACCGAGCCGGGCCCGGCGACACGCGCGGTGCTCGAGGCGCTGCTGGCCCAGGCTCAGGGCATTGAGCTGGGGTGA","MQVLPQRLSVLLAVHRAGGVVAAADFLHITPSAVSQQIRLLERECGARVLDRTPTGAVLTAAGKVLADAAERIEDELTTVRRELADLDDSIPSGVVRVASFASAVRALLLPLLSSLAMTSPELEVIVEEAEERNALPRLRRGELDLVLIERDEHTLPAAPRGMVDIPLLDESWLVVVPAEQAAPSTLADLARATWIDLAPGTAGAFALDRLERQLGVPLTTRHVAYDYDVVLAMVSQGLGCALLPELAVYSGLVPDELSVVRLPGLGVRQLVVRHRQTRTEPGPATRAVLEALLAQAQGIELG$","Putative LysR-family transcriptional regulator","Cytoplasm","LysR family regulatory protein","putative LysR-family transcriptional regulator","LysR, substrate-binding","","Viale A.M., Kobayashi H., Akazawa T., Henikoff S. rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum. J. Bacteriol. 1991. 173(16):5224-5229. PMID: 1907267Sung Y.C., Fuchs J.A. The Escherichia coli K-12 cyn operon is positively regulated by a member of the lysR family. J. Bacteriol. 1992. 174(11):3645-3650. PMID: 1592818Kondorosi E., Pierre M., Cren M., Haumann U., Buire M., Hoffmann B., Schell J., Kondorosi A. Identification of NolR, a negative transacting factor controlling the nod regulon in Rhizobium meliloti. J. Mol. Biol. 1991. 222(4):885-896. PMID: 1840615Henikoff S., Haughn G.W., Calvo J.M., Wallace J.C. A large family of bacterial activator proteins. Proc. Natl. Acad. Sci. U.S.A. 1988. 85(18):6602-6606. PMID: 3413113Thony B., Hwang D.S., Fradkin L., Kornberg A. iciA, an Escherichia coli gene encoding a specific inhibitor of chromosomal initiation of replication in vitro. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(10):4066-4070. PMID: 2034653","","","

InterPro
IPR000847
Domain

Bacterial regulatory protein, LysR
PF00126	$\"[5-64]T$	HTH_1
PS50931	$\"[3-60]T$	HTH_LYSR

InterPro
IPR005119
Domain

LysR, substrate-binding
PF03466	$\"[89-298]T$	LysR_substrate

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[5-89]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[172-249]T$	no description
signalp	$\"[1-23]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[21-41]?$ $\"[72-92]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-52]?$	signal-peptide
tmhmm	$\"[30-50]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[58-78]?$	transmembrane_regions

InterPro
IPR012495
Family

TadE-like
PF07811	$\"[34-76]T$	TadE

noIPR
unintegrated

unintegrated
signalp	$\"[1-60]?$	signal-peptide
tmhmm	$\"[36-58]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 34 to 76 (E_value = 1.2e-05) place ANA_1314 in the TadE family which is described as TadE-like protein.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1315","1401647","1401417","231","9.98","3.37","8190","ATGAAGCGCCTCATCCCTCCCACATCCCACCGCCCTCACCCCGGTCCCCGATCGTGGTGTGCCACCAGTGCGACCCGGATCGATCTGCGCGATGAGCGCGGCGACGTCCCCGGCTGGGTCCTGGTGACCCTCATGACCGCGGGGCTCGTCGTGGCTCTGTGGACGGTGGCCGGCAGCACGCTGACCGAGGTCTTCCTCAACGCCATCGCGAAGGTGACCAGTGCGATCTGA","MKRLIPPTSHRPHPGPRSWCATSATRIDLRDERGDVPGWVLVTLMTAGLVVALWTVAGSTLTEVFLNAIAKVTSAI$","Membrane protein","Cytoplasm, Extracellular","putative membrane protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[36-56]?$	transmembrane_regions

InterPro
IPR001992
Family

Bacterial type II secretion system protein
PF00482	$\"[174-301]T$	GSPII_F

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[110-130]?$ $\"[136-156]?$ $\"[287-307]?$	transmembrane_regions

","BeTs to 4 clades of COG2064COG name: Predicted membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2064 is aompkz---------f-h---j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 174 to 301 (E_value = 1.6e-10) place ANA_1316 in the GSPII_F family which is described as Bacterial type II secretion system protein F domain.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1317","1403536","1402685","852","11.19","11.17","30530","ATGGGTGCCGTCGCCGGGCTCCTGGGCGGGGTGGGGCTGCTCCTGATCTGGATGGCCTGCACCTCCGAGCCGCCTCAGTGGCGCTCGAGACGCTCCCGTCTCCTGGCCGACATCCTGGTCCAGGCCGGCGCCGGCCGTACCAGTCCCACCATGTTCGTCCTGGGCTCGCTCGGGCTGGGGCTGCTCATCGGCCTGGTCTTCCTGGGAATGTCCCGAGCCTGGCCGGTGGCTCTCGCCTTCAGTGCCATCTTCACGGCCATCCCCTTCCTCATCATCTCCTCGCGGGCGCGCAACCGTCGCACCCGGCTGCGCGAGGTATGGCCCGAGGCCGTCGACACCCTCGTCTCCGGCGTCCGTGCGGGTATGAGCCTGCCGGAGGCGCTGACCAACCTCGGTGAGCGCGGCCCGGAGGCCGTTCGCCCCCAGTTCCGGGCCTTCGCCACCGACTATGCCGCCTCCGCCCGCTTCGACAGCTCCCTGGACCGGCTCAAGACCCGCTTCGCCGACCCAGTCGCCGACCGGATCGTTGAGGCCCTGCGCCTGGCCCACGAGGTAGGCGGCACCGACCTGGGGACGCTGCTGCGCTCCCTGTCGCAGATGCTGCGTGAGGACATGCGCACCCGAGGCGAGCTCGAGGCGCGCCAGTCCTGGACCGTCAACGGCGCCAAGGTCGCGGTCGCCGCCCCATGGCTGGTTCTGGCACTGCTGGCCACCCGGCCTCAGGCAGCAGCGGCCTACGCCACCACCGCCGGAGCTGTCGTTCTCCTGGTCGGAGCAGTCGTCTCGGTCATCGCCTACCGGCTCATGCTGCGCCTGGGGCGGCTCCCCGAGGAGGAAAGGACACTGCGATGA","MGAVAGLLGGVGLLLIWMACTSEPPQWRSRRSRLLADILVQAGAGRTSPTMFVLGSLGLGLLIGLVFLGMSRAWPVALAFSAIFTAIPFLIISSRARNRRTRLREVWPEAVDTLVSGVRAGMSLPEALTNLGERGPEAVRPQFRAFATDYAASARFDSSLDRLKTRFADPVADRIVEALRLAHEVGGTDLGTLLRSLSQMLREDMRTRGELEARQSWTVNGAKVAVAAPWLVLALLATRPQAAAAYATTAGAVVLLVGAVVSVIAYRLMLRLGRLPEEERTLR$","Type II secretion system protein","Membrane, Cytoplasm","conserved hypothetical protein","type II secretion system protein","type II secretion system protein","","Salmond G.P., Reeves P.J. Membrane traffic wardens and protein secretion in gram-negative bacteria. Trends Biochem. Sci. 1993. 18(1):7-12. PMID: 8438237","","","

InterPro
IPR001992
Family

Bacterial type II secretion system protein
PF00482	$\"[110-238]T$	GSPII_F

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[47-67]?$ $\"[73-93]?$ $\"[219-239]?$ $\"[245-265]?$	transmembrane_regions

","BeTs to 4 clades of COG2064COG name: Predicted membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2064 is aompkz---------f-h---j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 110 to 238 (E_value = 8.6e-09) place ANA_1317 in the GSPII_F family which is described as Bacterial type II secretion system protein F domain.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1318","1404744","1403536","1209","5.92","-5.41","43344","GTGCGCGCTCGCGGCATCGACCCCCTCAACGACGCCTCCGACCTGGAACAGCTCGTCACCCAGGCCGAGGAGGACTACCTGCGCCGCTCCGACGCCGGACTCGTCCCGCCGCTCATCGACCCTCCGGGCGCGCGCACCCGCGTGCTGGACGCCATGGCGGGGTTGGGGCCGCTCCAGGGCTACCTTGATGACGAGTCCATTGAGGAGATCTGGGTCAATGCCCCCGGCCGCGTCTTCGTCGCCCGTTCCGGGCGCCCCGAGCTGACCACCACGATCCTGGAGAGCGAGGACCTCACCGTCCTGGTCGAGCGGATGCTGCGGGCCTCCGGGCGCCGCCTGGACCTGTCCAGCCCCTTCGTCGACGCTCAGCTCGCCGGGGGACAGCGGCTCCACGTCGTCATCCCGCCCATCACCTCCCAGCACTGGGCGGTCAACATCCGCAAGCACACCTCGCGTGCCTCCCGCACCACCGACCTCGTGCGTATGGGATCGCTGACCAGCCAGGTCGCCGCCTTCCTGGACGCCTCCGTACAGGCCGGCCTCAACATCCTGGTCTCGGGCGCCACCCAGGCTGGCAAGACCACGATGGTCAGGGCACTGGCCGGAGCGATCCCGGGTTCCCAGCGGGTCATCTCCTGCGAAGAGGTCTTCGAGCTCGCCCTGCGCAACCGGGACTGTGTGTCCATGCAGACCCGGCCGCCCAACCTCGAGGGGGTCGGTGAGATCAGCCTGCGGCGCCTGGTCAAGGAGGCCTTGCGCATGCGCCCCGACCGCCTCCTCATCGGAGAGGTTCGCGAGGCCGAGGCCCTGGACCTGCTCATCGCCATGAACTCGGGCTTGCCCTCCATGTGCACCATCCATGCCAACTCTGCTCGGGAGGCCGTCATCAAGATCTGTACGCTCCCGCTTCTAGCGGGGGAGAATGTTTCCAGCGACTTCGTGGTCCCCACCGTCGCCAGCGCCATCGACCTGGTTGTCCATCTTGACCTGGATCGCAGTGGGCGCCGTACCGTGCGAGAGGTCGCGGCCCTGTCCGGCCGGGTTGAGAACGGCATCATCGAGCTCTCCGACGTCTTCCACCGCGACTCCGCCGGCAACCTCGTGCGGGGCGCCGGGGCGCCTGACGCCGCCGAGCGCTTCAACCGGGCCGGTCATGACCTCACCACCCTGCTCAACGCCCGCCCCACTAGTGCCCAGGAGGCCTACTGA","VRARGIDPLNDASDLEQLVTQAEEDYLRRSDAGLVPPLIDPPGARTRVLDAMAGLGPLQGYLDDESIEEIWVNAPGRVFVARSGRPELTTTILESEDLTVLVERMLRASGRRLDLSSPFVDAQLAGGQRLHVVIPPITSQHWAVNIRKHTSRASRTTDLVRMGSLTSQVAAFLDASVQAGLNILVSGATQAGKTTMVRALAGAIPGSQRVISCEEVFELALRNRDCVSMQTRPPNLEGVGEISLRRLVKEALRMRPDRLLIGEVREAEALDLLIAMNSGLPSMCTIHANSAREAVIKICTLPLLAGENVSSDFVVPTVASAIDLVVHLDLDRSGRRTVREVAALSGRVENGIIELSDVFHRDSAGNLVRGAGAPDAAERFNRAGHDLTTLLNARPTSAQEAY$","Type II secretion system protein E","Cytoplasm","TadA-like protein","type II secretion system protein E","type II secretion system protein E","","Salmond G.P., Reeves P.J. Membrane traffic wardens and protein secretion in gram-negative bacteria. Trends Biochem. Sci. 1993. 18(1):7-12. PMID: 8438237Hobbs M., Mattick J.S. Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes. Mol. Microbiol. 1993. 10(2):233-243. PMID: 7934814","","","

InterPro
IPR001482
Domain

Bacterial type II secretion system protein E
PD000739	$\"[158-257]T$	Q8Y1N8_RALSO_Q8Y1N8;
PF00437	$\"[44-332]T$	GSPII_E

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[145-342]T$	no description

","BeTs to 13 clades of COG0630COG name: Type IV secretory pathway, VirB11 components, and related ATPases involved in archaeal flagella biosynthesisFunctional Class: 1, ,NThe phylogenetic pattern of COG0630 is aompkz----r----f-hs-ujx---Number of proteins in this genome belonging to this COG is 3","***** IPB001482 (Bacterial type II secretion system protein E) with a combined E-value of 6e-26. IPB001482B 179-199 IPB001482C 209-219 IPB001482D 242-287","","","-54% similar to PDB:2OAP Crystal structure of the archaeal secretion ATPase GspE in complex with AMP-PNP (E_value = 1.2E_29);-54% similar to PDB:2OAQ Crystal structure of the archaeal secretion ATPase GspE in complex with phosphate (E_value = 1.2E_29);-50% similar to PDB:1G6O CRYSTAL STRUCTURE OF THE HELICOBACTER PYLORI ATPASE, HP0525, IN COMPLEX WITH ADP (E_value = 6.7E_20);-50% similar to PDB:1NLY Crystal structure of the traffic ATPase of the Helicobacter pylori type IV secretion system in complex with ATPgammaS (E_value = 6.7E_20);-50% similar to PDB:1NLZ Crystal structure of unliganded traffic ATPase of the type IV secretion system of helicobacter pylori (E_value = 6.7E_20);","Residues 44 to 332 (E_value = 4.1e-53) place ANA_1318 in the GSPII_E family which is described as Type II/IV secretion system protein.","","protein (AF229646)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1319","1405074","1406402","1329","4.80","-30.82","46811","ATGTCACAGCCTCCGCAGTCCCCGGACGCCCCCGGCACCACTGATGTCAACGGCGGTACCGACAGCCTCACCGACGAGGTGACCTCCGACGTCGAGCGCGCTGCGGCTCACGCTGCCGATGACCACGGCAAGCTCAGCGCTCTTCCCGGTGACCAGGACGCCAACGACACTGCCGATGACGACGACGCCGACGGCTATCGCGCCCCCGTTGTCGTCGCTCCGCTGCCCGGGGCGTCATCCGGCCCTGCACGGGGCGATAAGCGTGCCTCGACGCCCCAGGTCGCCGAGGCCCCCCGCCCCCGTCACTCGGCGCTCTCCCTGGCGGCGATGGCGAGCGTCGCCGTCGGCGGCCTCAACCCGGCTCGGCTGGCGCTGCCGCAGTCCGAGACGCCGGAGCGGCACATCGTCGGTGTCATCGACACCCAGGGCCGCCACTGGGAGATCCATGAGGCCCGCACCGATGCCGTGGGCGCTTCCTTGGAGGCTGAGGCCGAGGTGCTGCGCCGCATCGGCCGGGTCGTCGACGACGGACGGCTCTCCTTCGATGTTCCTCGCGTCGCCGGGTCCCTGCGTCAGAAGGACGCCCACATTCAGGTCCGCTCCCATGTGGAGGGCAAGCCGATCCCGGTGGAGACGCTCCGGCCAGGGCCGGGGATGTCAGCGGGCCTGGGCAAGGCGCTCGGTGAGATCCACGAGCTGTCCATGACGGTGATCTCCGAGGCTGGTATGCCGGTCTACGACGCCGAGGAGGTGCGTCAGCGCTGGCTGAGCCTGCTGGACGACACCGCCGCGACGGGCAGGACCCCACCGGCGCTGCTGGGGCGCTGGGAGCAGGCCCTGGAGGACACCGCCCTGTGGCGCTTCCGCCCCACCGTGGTTCACGGGGACCTCGCTGAGGAGAACGTCCTGGTGGCCGGTGGCACGGTGGTGGCGGTGCGGGGCTGGTCCCAGGCGCATGTGGGTGACCCGGCCGAGGACCTGGCCTGGGTGTACTCCTCAGCACCGGTGGACTGCCTGGACTCCATTGAGGACGCCTACGACATCGCCCGCTCCGAGGGCGTTGACCGCCACCTGCGTGAGCGGGCCGAGCTGGTCAGTGAGCTGAGCCTGGCGCGCTGGCTGCTACACGGGGTGCGGACCGGGGACAAGCCGGTCATCAATGACGCGGTGGCGATGCTGGAGGACCTGGCCGCCCAGGTGGGTGACGCCCCGCTGGTGGAGCCGGCCACGCCCCGGCTGGCACCGGTGCCCGGGGTTCGCGAGCCGGCTGAGCCTGACGCCATCACCAACCCGGTGGCGATGGTGCGCGTCGACGACGAGGAGAGCTGA","MSQPPQSPDAPGTTDVNGGTDSLTDEVTSDVERAAAHAADDHGKLSALPGDQDANDTADDDDADGYRAPVVVAPLPGASSGPARGDKRASTPQVAEAPRPRHSALSLAAMASVAVGGLNPARLALPQSETPERHIVGVIDTQGRHWEIHEARTDAVGASLEAEAEVLRRIGRVVDDGRLSFDVPRVAGSLRQKDAHIQVRSHVEGKPIPVETLRPGPGMSAGLGKALGEIHELSMTVISEAGMPVYDAEEVRQRWLSLLDDTAATGRTPPALLGRWEQALEDTALWRFRPTVVHGDLAEENVLVAGGTVVAVRGWSQAHVGDPAEDLAWVYSSAPVDCLDSIEDAYDIARSEGVDRHLRERAELVSELSLARWLLHGVRTGDKPVINDAVAMLEDLAAQVGDAPLVEPATPRLAPVPGVREPAEPDAITNPVAMVRVDDEES$","Aminoglycoside phosphotransferase","Cytoplasm","macrolide 2''''-phosphotransferase-like protein,putative","aminoglycoside phosphotransferase","aminoglycoside phosphotransferase","","Trower M.K., Clark K.G. PCR cloning of a streptomycin phosphotransferase (aphE) gene from Streptomyces griseus ATCC 12475. Nucleic Acids Res. 1990. 18(15):4615-4615. PMID: 2167474","","","

InterPro
IPR002575
Domain

Aminoglycoside phosphotransferase
PF01636	$\"[147-364]T$	APH

InterPro
IPR008266
Active_site

Tyrosine protein kinase, active site
PS00109	$\"[292-304]?$	PROTEIN_KINASE_TYR

noIPR
unintegrated

unintegrated
G3DSA:3.90.1200.10	$\"[101-349]T$	no description

","BeTs to 4 clades of COG3173COG name: Predicted aminoglycoside phosphotransferaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG3173 is -o-------dr-b--f-----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 147 to 364 (E_value = 2.4e-07) place ANA_1319 in the APH family which is described as Phosphotransferase enzyme family.","","2-phosphotransferase-like protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1320","1409862","1406425","3438","5.06","-46.08","122563","ATGACCCCCACCGGTCCACGCCGGCTCACCCCCCAGGCACTGGCAGAGGCGCTCGGCATCCACACCCCCACCCAGGAGCAGGCGCGCGTCATCGCCCACCGGCTGAGCCCCCTGCTGGTGGTCGCCGGAGCCGGCTCGGGCAAGACGGCCACCATGGCCCAGCGAGTCGTCTATCTGGTCGCCACCGGGCAGGTCCGTCCCGACCAGATCCTCGGACTGACCTTCACCCGCAAGGCCACCGCCGAGCTCGACCAGCGCGTCGCCTCCCGCCTGGCCGGCCTCAGCGCGGCCGGCCTGCTCCCGGCCACTGGGCCAGGGGCTGACGGAAAGGGCGGCTCTACTGCCGATTCCGCTGACGCCACCGACGTCGGCGAGCCGATGATCGCCACCTACAACTCCTTCGCAGGCGCCCTGGTGCGAGACCACGGACTGCGCATCGGCGTGGACCCCGACTCCACCCTCATCACCCAGGCCCGCTCCTGGCAGATCGTCACCTCCCTGCTTGAGGCCCGCACGCTCCCGCTGCCCAACGAGAGCCTCAGCCACAACGCGAGCGCCACCCTGGTCCTGGCCGACTCCCTGAGCCAGAACCTGCTGACCATCGAGGAGGCCGCCAAGGACCTGGCCGACCTGTCCGAGCAGTTCACCGCCCTGGCCGCCATCAAGGGCTGCAAGACCCTGGTCGGCAAGGCGCCCGCCGTCATGGCCGAGTGGGAGGCCCTGCTCGACGTCGTCGCCGAGCTGCATGCGCACAAACGTCACCACGGCCTGCTCGACTTCGGTGACCAGATCTCCCTGGCCTGCGCCATCGCCGAGTCCGTCCCCGAGGCCGCCGGCCAGGTGCGGGCCCAGTACCCTGCGGTTCTGCTCGACGAGTTCCAGGACACCTCGGTGGCCCAGGTCAGGCTCCTGTCGGCCCTCTTCGCCGACTCCGGGGTGACCGCTGTCGGCGACCCCCACCAGGCCATCTACGGCTGGCGAGGAGCCAGCGCAGCAGCCCTGGACACCTTCCACCAGCGGTTCAACCCCACCGGCACCGCCCTCCTGGACTCCGGGACCTTACCGGCTGAGGCCACCCCCGTCCTGGAGCTGTCGACCTCCTGGCGCAACGACTCCACCATCCTGGAGGTCGCCAACGTCGTCTCCGCGCCGCTGCGCTCCGGTGTCGTTGAGGACGGGGACCCGGTGGGCGAGCACCTCACCGTCGCCCCCTTGCGGGCCCGCCCCGCGGCCTTCGGCCTGGAGCCCGGGGCAGCGTTCGGGGCCTTCCTCCAGGACCCAGCCGAGGAGGCCCGCACGGTGGCCGCCTTCCTCGCCGAGCGCTGGTCGCCCGGTGCCGAGATGGCCGTCCTGTGCCGCACTCGGGCGCAGATGGAGCCCGTTGCCGCCGAGCTGGAGGCCGCCGGCCTGCCTTACACGATCATTGGCCTGGGCGGGATGCTCTACGTCCCCGAGGTCGCCGACGTTCGCGCCCTGCTGACCACGGCCTCGGACCCGGAGCGCGGGGACCGGGTGGTCAGGCTCCTGACCGGTTTCGGCATCGGTGCCCGCGACCTGCGGGTCCTGGCGGCGCTGGCCCGCGAGCTCACCCGCACCGCAACCGAAAGCGGCAAGGAGGGACCAGGGGCTCACGGCGACCGTGCCGAGGCCGACTCCCCACTGCTCAGCGAGGCCCTGGACGCCCTGCTGCGATGGCATGAGGACGGAGTGCAGGAAGAGCAGGAAGAGTCCGCGGCGGCCCGGGACCTGACCGAGGCCGGACGGGCTGTTGCCTTGCGCACCGCTCGAGCGATCCGACGCATCCGGGAGGCCGTCTCCCTTCCCCTGCCCGACCTCGTGGCCCTGGCCGAGCAGGTCCTCGACCTCGACATCGAGATCGCCGCCCGGGTCGGCCACCCCATGGGGCACCGTGCCCTCGACTCCTTCCACGAGACAGCCCGGGCCTTCGCCGCCGACACCGACGCCCCCACCCTCACCGGCTTCCTGGAATGGCTCGACGCCGCCGAGGAGCACGAGGACGCCATGAGCGCCCCCGAGGTCGAGCCCTCGCCCGGGGCGGTCCAGCTCCTCACCGTCCACGCCGCCAAGGGCCTGGAGTGGGACGTCGTCGCCGTCCCCGGCATGGACGAGCAGGTCTTCCCCTCCTACACCAGCGCCGTCAAGGACGACCTTCGTGTCGCGGAGACCGGCTGGATGGGCTCCACCTCCACCTTCCCCTTCCCGCTGCGGGCCGACGCCGGCGACCTGCCCCCCTTCACCGTGGGGGACCTCGACCCGGCTGTCACGGACAAGCCCCTCCTGACTGAGACGATGAGCGCCTACAAGGAGGCCCTCGGACGCCAGAGCCTGCGCGAGGAGCGCCGCCTGGCCTACGTGGCCTTCACACGGGCCCGCCACGAGCTCCTCCTGACCGGCTCCCATCTGTCCAAGACCGCTTCCAAGCCCCGCCGCCCCTCACGCTTCCTCACCGAGCTCCAGCGGCGCGACCTCCTCCGCCCCTACGCGGAGGGTTGGGTCGACTTCGATGAGTCCCGCCCCAACCCACTGACCGCCCTGACCCAGGTGGGCACCTGGCCCCCCGACGCCGATGCAGCAGAGAGCCTGGACAGCCAGGCCCCGGAGGCCAGGGGAGAGGACGCCCCGGTCACCGACCGGCTCGCCGATGTGCGCCGGGCCCGGTACGCGGCCGCCGCCCAGGTCACCGCCGCCATGGGCGGGACCGAGCCCGTCCAGGAGGCGTACGCTCAAGCCCAGCCCGATGACGAGACGGTGCGGCGGTGGAGACTTGAGGCGGGACTCCTCCTGGCCGAGCGCACCCGGGCCCTGTCCAGCGGGCCCGCCGTCCGCCTGCCCGAGCACCTGGCCGCCACCCGCCTGGACGACCTGCGTGCCGACCGCCACCAGTTCGCACTCGACCTGCGTCGCCCACTCCCACCCGAGCCCCGCGCCGCCGGCCGGCTCGGAACCGTCTTCCACGACGCCGTCGCCCAGCGCCTGAGCGCACGCGGCACCCTGTTCGACCTGGGGCAGGCGGGCGTGCCTGACAGCCTCGGGCCCCAGGACCGGGACCGCATCGAGCGCTGGCTGGAGACCGCCGAGAACCTGCCGCTCCTGGAGGACTACGTCCTGGCCGAGACCGAGACGGACCGGGAGATCACCATCGGCGCCACCACCCTGCGCTGCCGCATGGACGCCGTCTTCCAGCGCAAGGACGGTTCCGGGTGGCTCATCGTCGACTGGAAGACCGGGCGGCGACAGGTGCCCGTGGACCAGCTCAGCGTCTACGTCCATGCCTGGGCTGCCTCCCAAGGTGTGCCCACCGGGGCGGTACGGGCCGCCTACGTCTACGTCGACTACCCCGGAGGACGCGTCGATGAGCTCACCGCCGAGGGCCTGCTCAGCATCGAGCAGATCCAGGCGGCCCTGACAGTGGGCTGA","MTPTGPRRLTPQALAEALGIHTPTQEQARVIAHRLSPLLVVAGAGSGKTATMAQRVVYLVATGQVRPDQILGLTFTRKATAELDQRVASRLAGLSAAGLLPATGPGADGKGGSTADSADATDVGEPMIATYNSFAGALVRDHGLRIGVDPDSTLITQARSWQIVTSLLEARTLPLPNESLSHNASATLVLADSLSQNLLTIEEAAKDLADLSEQFTALAAIKGCKTLVGKAPAVMAEWEALLDVVAELHAHKRHHGLLDFGDQISLACAIAESVPEAAGQVRAQYPAVLLDEFQDTSVAQVRLLSALFADSGVTAVGDPHQAIYGWRGASAAALDTFHQRFNPTGTALLDSGTLPAEATPVLELSTSWRNDSTILEVANVVSAPLRSGVVEDGDPVGEHLTVAPLRARPAAFGLEPGAAFGAFLQDPAEEARTVAAFLAERWSPGAEMAVLCRTRAQMEPVAAELEAAGLPYTIIGLGGMLYVPEVADVRALLTTASDPERGDRVVRLLTGFGIGARDLRVLAALARELTRTATESGKEGPGAHGDRAEADSPLLSEALDALLRWHEDGVQEEQEESAAARDLTEAGRAVALRTARAIRRIREAVSLPLPDLVALAEQVLDLDIEIAARVGHPMGHRALDSFHETARAFAADTDAPTLTGFLEWLDAAEEHEDAMSAPEVEPSPGAVQLLTVHAAKGLEWDVVAVPGMDEQVFPSYTSAVKDDLRVAETGWMGSTSTFPFPLRADAGDLPPFTVGDLDPAVTDKPLLTETMSAYKEALGRQSLREERRLAYVAFTRARHELLLTGSHLSKTASKPRRPSRFLTELQRRDLLRPYAEGWVDFDESRPNPLTALTQVGTWPPDADAAESLDSQAPEARGEDAPVTDRLADVRRARYAAAAQVTAAMGGTEPVQEAYAQAQPDDETVRRWRLEAGLLLAERTRALSSGPAVRLPEHLAATRLDDLRADRHQFALDLRRPLPPEPRAAGRLGTVFHDAVAQRLSARGTLFDLGQAGVPDSLGPQDRDRIERWLETAENLPLLEDYVLAETETDREITIGATTLRCRMDAVFQRKDGSGWLIVDWKTGRRQVPVDQLSVYVHAWAASQGVPTGAVRAAYVYVDYPGGRVDELTAEGLLSIEQIQAALTVG$","UvrD/REP helicase","Cytoplasm","widely conserved ATP-dependent DNA helicase;Rep-like protein","UvrD/REP helicase","UvrD/REP helicase","","Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 1997. 90(4):635-647. PMID: 9288744","","","

InterPro
IPR000212
Family

UvrD/REP helicase
PTHR11070	$\"[34-92]T$ $\"[121-182]T$ $\"[212-342]T$ $\"[358-569]T$ $\"[621-721]T$ $\"[780-975]T$	UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580	$\"[23-568]T$	UvrD-helicase

InterPro
IPR014016
Domain

Helicase superfamily 1, UvrD-related
PS51198	$\"[21-371]T$	UVRD_HELICASE_ATP_BIND

InterPro
IPR014017
Domain

UvrD-like DNA helicase, C terminal
PS51217	$\"[372-697]T$	UVRD_HELICASE_CTER

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[20-347]T$ $\"[365-834]T$	no description

","BeTs to 22 clades of COG0210COG name: Superfamily I DNA and RNA helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0210 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 4","***** IPB000212 (UvrD/REP helicase) with a combined E-value of 1.1e-54. IPB000212A 42-52 IPB000212B 74-87 IPB000212C 248-263 IPB000212D 281-297 IPB000212E 316-329 IPB000212F 364-382 IPB000212G 689-705 IPB000212H 785-797","","","-38% similar to PDB:1PJR STRUCTURE OF DNA HELICASE (E_value = 4.2E_31);-38% similar to PDB:1QHG STRUCTURE OF DNA HELICASE MUTANT WITH ADPNP (E_value = 4.2E_31);-38% similar to PDB:3PJR HELICASE SUBSTRATE COMPLEX (E_value = 4.2E_31);-41% similar to PDB:2PJR HELICASE PRODUCT COMPLEX (E_value = 1.0E_24);-39% similar to PDB:1UAA E. COLI REP HELICASE/DNA COMPLEX (E_value = 5.3E_18);","Residues 23 to 568 (E_value = 1.3e-51) place ANA_1320 in the UvrD-helicase family which is described as UvrD/REP helicase.","","conserved ATP-dependent DNA helicase; Rep-like protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1321","1413107","1409859","3249","5.90","-16.03","113658","ATGGTCAGCACCGTCACCTGGCCAGGGCTCCCCGCCGAAGCCACCGGGTCGCGGGCCTTCCGCTCCGAGCTGCGCAACCTCCTGGCCCGTGCCGGAGAGCTCGGCATCAGCGCCGACGACCTGGCCGACCTGGGACACCGGCTCAATGTCCCCATCTGGGGGCCCGCGTCCCAGCTCCTGCGCACCTGGGATGCTCAGGGGCGGGCCAGCGCCGAGCGCAGGGCCCAGACCCGCAAGATGGACACGGCTCGCCTCCAGGACCGCGCCGTGGAGGCCCTGAGCTCCTGGGGCGCCGACGCCGTCACTGTCCGCCGCCCTGTGCCGGACCTCGTCGTCGTGGACGACTACCAGGACTGCACGGCCGCCACCGCCAGGCTCCTGACGGCCCTGGCGACCCCGGACCCCGACGGGCACCGGGCGCAGATCGTGGTGCTGGGGGACCCCGACGTCGCCGTGGAGACCTTCCGTGGCGGCACCCCCAGCCTGCTCATCGCAGCCGAGGACCACTCGGGGCTTGCAGCCAGCCGCCTGCGCCTGACCACTTGCTACCGAGGCAACCCGGCCATCGCGGCGGTGATCCGCGACCAGAGTGCCCGGGTCCCGGTGACCGGCACGACCGCCCACCGGCAGACGACCCTGGCGCCCCGGTCCTCAGTACGGTCCTCGGTAGGGCCTTCCTCCGGGGCGAATGACGCTGAGCACCCGCAGGCGGCGGCCGGCGTCGAGGTCATCCTGGCCTCCTCCATCTGGCAGGAGCACGCCCACGTCGCCCGGGCGCTCAGGCTCGAGCACGTGCACCACGGCACCGCCTGGTCACAGATGGCGGTCATCGTTCGCAGCGCCGCCGACGCCGAGACCCTCGCCAGGGACCTGCGCAGACGAGGCGTGCCCCTGGCCTCCCGCACGCCTGCGGTCCTGCTACGCGCAGAACCGGCCGCAGCCGCGCTCCTGGACATCGTGCGCGCCGCCATCCGCGACCAGCTGGGCGGGCACGGTGAACCGCCCCAGCGCGACGCCGCCATCAACCTCCTCACCAGCCCCCTGGTGGGACTGACCACCATGGACCTGCGCCGACTGCGCCGCAGGCTGCGCCAGAACCCGCCGGCTGCAACCCCGCACGCCAGTGCGCCCGAGCCCAGTGAGCCCAGGACCACCGCCCCCACAGCCGTTCCTGCTCCCGATCCCACTGCTGACCCCACAGCCGGGCCCGGGCCCCGAACCGGCGGCGACGCCGCCCTCCTGGCTCTGCTGGCCGACCCCGAGCGGGCCTCCGGCTTCGCCCGCTCCCTGGACGGGCAGCCGCTGAGCGCCCAGGCGGACCGACTCCTCACCGCAGCCAGGATCCTTGAGGCCCTGCGCGCCGCCATCGGGCAGACCCCGGCCGAGGCCCCGCTCGATGTCGAGGCCCTGCTGTGGGCTGCCTGGAACGCCTCCGAGCGGGCCGAGGCCTGGCGCGCCACCGCCTTGCTGCCCTCGGCAAGCTCGGTGCGAATGCTCCTGTCCGAGGCCGCCGAGCACGACCTCGACGTCGTCACCACCCTGTTTAAACGCGCCGAGGTCTGGGCTGAGCGCCACCCGGGCCAGGACGCCTCCAGCTTCCTGGCCGAGCTCGATGCCGAGGTCCTGCCCTCGGACTCCGTGGCCCCTCAGGGGCGGCGCCCGGAGGGCGTGGCCGTCATGACCCCGGCCGGTTGCGCGGGCCAGGAGTGGGAGCTTGTTGTGGTCGTCGGGCTGGAACGGGACCGCTGGCCGGACCTGCGCCTGAGGGACTCCCTGACCCGCACCGGCCTGCTCGTCGACGCCGTCACCGGCCGCCTGACCACAGACACCGTTGCACCGGGGGAAGGGACCAGCGGCACCGGCGCCGTGGCCGCTGCCCGGGCGCAGGTGCGCGCCGATGAGCGCCGCATGCTCATCATGGCCCTGTCCCGCGCCTCCAGGCGCCTCCTGCTGACCGCCACCGCCGACGCCGAGCACGCCCCCTCACCCTTCCTGACCGAGATCGCCCGCAGCGCCGGGATCGCCCTGACCGACGCCGACGGCGCCCCCCTCCTGACTCCCGACACCGGCGACCTCACCCTGCGCGGCCTGGTAGGGGAGCTGCGCCATGCCGCCATCTGCGGGAACCTTGAGACGGCCACCGACGCCGAGCGCCGCCGCGGCCGGGCCGCCGTCGACCTGTTGGCCGACCTCGCCCGCCAAGGCGTACCCGGCGCCGACCCCGCCACCTGGATCGGCGCGACCGGCCCCACCTCCAGCGCCCCCCTCATCGCCGCCGGCGAGCGGATACGGGTCAGCCCCTCCGATGTGGAGGGCCTGGCCGCCTGCCCCCTCAAGTGGTTCCTGACCCGCAGCGGCGGATCGGCCCCCGCCAGCGACGCCCAGGCCCTGGGCAGCCTTGTCCACGCCGTCGCCGAACGGGCGGAGAAGGAGCACCTGCGCGGTCCGGCCCTGCGCGAGGCCTTCGAGGAGCGATTGACCGGCCTCGGCTACCCCGCCACCTGGCAGGGAGGCCTGGCCGCAGACCGCGCCCGCGCCATGATCGAGCGCCTCGACGCCTACCTGGCTGACTGCGACGCCCTGGGCGTGCGCGCCGACGTCGAGCAGCCGGTGCGCACCGACGTCGACATCCCCCTGAGTGTCCTCAGCCCTGCGGTCCGCCAGCGGGCCGGTCTGCGGACACCGACGAAAGGCGGCAACGCCGTCCCGGTCACGATCTCCGGGCGCATCGATCGCCTCGAGCACCTCGGCGGCCTTTCGGGAGATGACCCGGAGGACTCCACCGAGCCCAACCGGAACGGCACGGTGCGGGTCATCGATCTCAAGACCGGGCAGCGCGTCCCCAAGGACGTCCAGCGTCACCCCCAGCTGGCCACCTACCGGCTGGCCCTGAGCTCGCAGGGCCTCGACGTCGTCGGAGGAGCCCTCGTGCTCCTGGGCAAGGAGCCCTCCAAACGCTCAGGAGACGGCTACGTCCTGGCCCCGCCGGGCGCCGCCCTCGACCCCAGCCCCGCCGCCCCGGAACCTGCGGAGAAGGCCGCGTGCGAGCCCGCTGAGGAACCGGGTGACGCGGAAGCGAACGGTGCTGCCGACAGCAGCGAGGAGTACTGGGCCGAGGACCTCGTGGCCGCCGCGGCCGTGGCCGGAGTAGGCCCGCAGATCGAGGCCCGCACCGGTGAGCACTGCCGTACCTGCCGGGTCAAGGACTCCTGCCCCGTGCAGGTCGAGGGAAGGAGAGTCGTCTCATGA","MVSTVTWPGLPAEATGSRAFRSELRNLLARAGELGISADDLADLGHRLNVPIWGPASQLLRTWDAQGRASAERRAQTRKMDTARLQDRAVEALSSWGADAVTVRRPVPDLVVVDDYQDCTAATARLLTALATPDPDGHRAQIVVLGDPDVAVETFRGGTPSLLIAAEDHSGLAASRLRLTTCYRGNPAIAAVIRDQSARVPVTGTTAHRQTTLAPRSSVRSSVGPSSGANDAEHPQAAAGVEVILASSIWQEHAHVARALRLEHVHHGTAWSQMAVIVRSAADAETLARDLRRRGVPLASRTPAVLLRAEPAAAALLDIVRAAIRDQLGGHGEPPQRDAAINLLTSPLVGLTTMDLRRLRRRLRQNPPAATPHASAPEPSEPRTTAPTAVPAPDPTADPTAGPGPRTGGDAALLALLADPERASGFARSLDGQPLSAQADRLLTAARILEALRAAIGQTPAEAPLDVEALLWAAWNASERAEAWRATALLPSASSVRMLLSEAAEHDLDVVTTLFKRAEVWAERHPGQDASSFLAELDAEVLPSDSVAPQGRRPEGVAVMTPAGCAGQEWELVVVVGLERDRWPDLRLRDSLTRTGLLVDAVTGRLTTDTVAPGEGTSGTGAVAAARAQVRADERRMLIMALSRASRRLLLTATADAEHAPSPFLTEIARSAGIALTDADGAPLLTPDTGDLTLRGLVGELRHAAICGNLETATDAERRRGRAAVDLLADLARQGVPGADPATWIGATGPTSSAPLIAAGERIRVSPSDVEGLAACPLKWFLTRSGGSAPASDAQALGSLVHAVAERAEKEHLRGPALREAFEERLTGLGYPATWQGGLAADRARAMIERLDAYLADCDALGVRADVEQPVRTDVDIPLSVLSPAVRQRAGLRTPTKGGNAVPVTISGRIDRLEHLGGLSGDDPEDSTEPNRNGTVRVIDLKTGQRVPKDVQRHPQLATYRLALSSQGLDVVGGALVLLGKEPSKRSGDGYVLAPPGAALDPSPAAPEPAEKAACEPAEEPGDAEANGAADSSEEYWAEDLVAAAAVAGVGPQIEARTGEHCRTCRVKDSCPVQVEGRRVVS$","UvrD/REP helicase","Cytoplasm, Membrane","POSSIBLE ATP-DEPENDENT DNA HELICASE","UvrD/REP helicase","Superfamily I DNA and RNA helicase-like","","Gorbalenya A.E., Koonin E.V., Donchenko A.P., Blinov V.M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989. 17(12):4713-4730. PMID: 2546125","","","

InterPro
IPR014017
Domain

UvrD-like DNA helicase, C terminal
PS51217	$\"[210-567]T$	UVRD_HELICASE_CTER

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[81-171]T$ $\"[241-668]T$	no description

","BeTs to 3 clades of COG2887COG name: RecB family exonucleaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2887 is --m--z----r---------ujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB000212 (UvrD/REP helicase) with a combined E-value of 1.1e-06. IPB000212D 104-120 IPB000212G 559-575 IPB000212H 633-645","","","-43% similar to PDB:2HG4 Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS. (E_value = );-62% similar to PDB:1UAA E. COLI REP HELICASE/DNA COMPLEX (E_value = );","No significant hits to the Pfam 21.0 database.","","ATP-DEPENDENT DNA HELICASE","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1323","1413760","1413975","216","5.37","-1.83","7553","ATGCAGGTCACGATCGGAATCAAGCACGCCAGCCGCGAGCTCTCCCTGGAGACCTCCGACTCTCAGGAGAAGGTGCTGGCCGCCGTGGCCGACGCCGAGACCAAGGCCGTCATCCTCAGCGACGACAAGGGCCGCAAGGTCTTCGTGCCGGCCGGCTCCCTGGCATACATCGAGCTCGGTGAGGCCGAGCCCCGCCGGGTTGGCTTTGGTATCTGA","MQVTIGIKHASRELSLETSDSQEKVLAAVADAETKAVILSDDKGRKVFVPAGSLAYIELGEAEPRRVGFGI$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","conserved hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","Fri Aug 3 12:45:39 2007","","Fri Aug 3 12:45:39 2007","","","Fri Aug 3 12:45:39 2007","Fri Aug 3 12:45:39 2007","Fri Aug 3 12:45:39 2007","","","","","","Fri Aug 3 12:45:39 2007","","","","Fri Aug 3 12:45:39 2007","Fri Aug 3 12:45:39 2007","","","","","yes","","" "ANA_1324","1415704","1414865","840","7.22","0.82","32862","ATGGACCGCTCCCTGTACGAGGCAGAGCTGCTGAGGCTGCAGGCGGAGCTGGTCGAGATGCAGGAGTGGGTCAGGGCCACTGGAGCCCGCGTCGTCGTCATCTTCGAGGGTCGTGACGCGGCCGGCAAGGGTGGGGCGATCAAACGTATCACCGAGTACCTCAACCCGCGTATCGCGCGCGTGGTCGCGCTTCCCGTGCCTACTGAGCGTGAGCGCACCCAGTGGTACTTCCAGCGCTACATTGCGCACCTGCCTGCCGCCGGCGAGATCTGCCTGTTCGACCGCTCCTGGTACAACCGCGGCGGCGTCGAGCACGTCATGGGTTACTGCACCCCGGAGGAGCACCGGCGCTTCCTCCAGCAGTGCCCGGTCTTCGAGAGGATGCTCGTCGACGACGGCATCCTGCTGCGCAAGTACTGGTTCTCCGTCCCTCAGAAGGAGCAGTACAAGCGCTTCAAGTCGCGCATGACCGACCCCATGCGGCGCTGGAAGCTCTCACCCACCGACCTGGAGGCCCTGCCCCGCTGGGAGGACTACTCGCGGGCCAAGGACGAGATGTTCGTCCACACGGACATCGACTCCGCCCGCTGGCACGTCGTGGAGTCGGCCGACAAGCGCAAGGCACGCCTCAACATGATCCACCACCTGCTGGAGTCCATTCCCTACGAGCACGTGGAGCGTCCTGAGATGACCTTCCCGAAGAAGTCCTCGTTGCCGTCGTCGGGCTACCGCCGCACGGACCGCTCCCTCCAGAGCGAGGTGCCCGACTACGCGGCCACCCTCAGTGAGTCCGACGCAACTGAGCGCTACGTGGACCTCGAGGATCAGGGGATCAGCTAG","MDRSLYEAELLRLQAELVEMQEWVRATGARVVVIFEGRDAAGKGGAIKRITEYLNPRIARVVALPVPTERERTQWYFQRYIAHLPAAGEICLFDRSWYNRGGVEHVMGYCTPEEHRRFLQQCPVFERMLVDDGILLRKYWFSVPQKEQYKRFKSRMTDPMRRWKLSPTDLEALPRWEDYSRAKDEMFVHTDIDSARWHVVESADKRKARLNMIHHLLESIPYEHVERPEMTFPKKSSLPSSGYRRTDRSLQSEVPDYAATLSESDATERYVDLEDQGIS$","Polyphosphate kinase 2","Cytoplasm","Uncharacterized BCR","hypothetical protein","protein of unknown function DUF344","","","","","

InterPro
IPR005660
Domain

Polyphosphate kinase 2
PF03976	$\"[1-228]T$	PPK2

","BeTs to 7 clades of COG2326COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2326 is ---------dr--c-fg---uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 228 (E_value = 5e-147) place ANA_1324 in the PPK2 family which is described as Polyphosphate kinase 2.","","BCR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1324.1","1416118","1415870","249","9.92","7.85","9656","GTGTTCTCACGTCAGGCACAGAAGGACGCGAAGAAACTCACCGCGGCGGGGCTCAAACTTAAAACCGAGAAGCTCCTCAACCTCATGCGGGAGAATCCCTTCGTCAAGCCGCCTCGTGATGCAAAGCTGGTTGGGGACCTATTGGGCTGCTACTCGCGGCGTATCACTATCCAGCATCGACTCGTCTACGAGGTGCACACCGACGAGAGGACCATCCACGTCCTGAGAATGTGGACCCACTACGAGTGA","VFSRQAQKDAKKLTAAGLKLKTEKLLNLMRENPFVKPPRDAKLVGDLLGCYSRRITIQHRLVYEVHTDERTIHVLRMWTHYE$","Toxin of toxin-antitoxin (TA) system","Cytoplasm","","","","","Anantharaman V, Aravind L.New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system.Genome Biol. 2003;4(12):R81.PMID: 14659018Roberts RC, Helinski DR.Definition of a minimal plasmid stabilization system from the broad-host-range plasmid RK2.J Bacteriol. 1992 Dec;174(24):8119-32.PMID: 1459960","","","

InterPro
IPR007712
Family

Plasmid stabilization system
PF05016	$\"[1-76]T$	Plasmid_stabil

InterPro
IPR009614
Family

Addiction module toxin, Txe/YoeB
TIGR02116	$\"[2-81]T$	toxin_Txe_YoeB: addiction module toxin, Txe

InterPro
IPR012753
Family

Addiction module toxin, RelE/StbE
TIGR02385	$\"[1-81]T$	RelE_StbE: addiction module toxin, RelE/Stb

","No hits to the COGs database.","***** IPB009614 (Addiction module toxin, Txe/YoeB) with a combined E-value of 1.9e-11. IPB009614B 30-57 IPB009614C 58-79","Residues 2-81 are similar to a (MW2380 SA2245) protein domain (PD451360) which is seen in Q82UW6_NITEU.","","","Residues 1 to 76 (E_value = 3.6e-05) place ANA_1324.1 in the Plasmid_stabil family which is described as Plasmid stabilisation system protein. Residues 2 to 81 (E_value = 3.4e-05) place ANA_1324.1 in the Plasmid_Txe family which is described as Plasmid encoded toxin Txe.","","","","1","","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:08:51 2007","Wed Aug 15 13:08:51 2007","Wed Aug 15 13:08:51 2007","Wed Aug 15 13:13:30 2007","","Mon Aug 20 18:15:42 2007","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:07:33 2007","Mon Aug 20 18:15:42 2007","Wed Aug 15 13:07:33 2007","Mon Aug 20 18:15:42 2007","Wed Aug 15 13:07:33 2007","Wed Aug 15 13:07:33 2007","Mon Aug 20 18:15:42 2007","","Wed Aug 15 13:07:33 2007","","Wed Aug 15 13:07:33 2007","yes","","" "ANA_1325","1414056","1414868","813","5.11","-12.23","29573","ATGACCGCTGCCGCCGCGCGCCACGCAGCTTCAACGCCCGGCGTTAGGGTGGAGTGCATGGATCGCCAGGACAGCCAGAGGGGCCTGCTCGCCCAGTGGATCGAAGAGTCCAGCCGCATCGTCTTCTTCGGCGGCGCCGGGGTCTCGACCGAGTCGGGGATCCCCGACTTCCGGGGTGCCAAGGGCTTCTACCACCAGGATCGGGAGATTCCCCTGGAGCAGGTGCTGTCCATCGACTTCTTCACCGTGCACCCGCAGGCCTACTGGGAGTGGTTTGCCCAGGAGAACGCCCGCGAGGGCGTGGCCCCCAACGACGCGCACAGGTTCGTGGCCGATCTCGAGCGGGCCGGGAAGCTGTCGGCCGTGGTCACGCAGAACATTGACGGCCTCCACCAGCGGGCCGGCTCCGAGCGGGTCCTCGAGCTGCACGGCAACTGGTCGCGCCTGACCTGCACCGGCTGCGGCGAGCACGTCACCCTGGACGACGCCGACGGCGCCCGCTCCGGCGAGGTCCCCCACTGCCTCGCGTGCGCCTCAGTGCTGCGCCCGGACATCGTGTTCTACGGGGAGATGCTGGACAGCGACGTCATGGAGGGGGCCGTGCGGGCCATCTCGGAGGCGGACCTGCTGATCGTGGCCGGCACGAGCCTGGTCGTCTACCCGGCGGCGGGCCTCATCGACTACTACGCCGGTGAGCGTCTGGTCCTCATGAACGCGACTCCCACGCCGTATGACTCCCGTGCCGACCTCATCATCCGTGAGCCGGTCGGGCAGGTCTTCGAGGAGCTGGGGCGCAGGAGCCGCCGGCCCTAG","MTAAAARHAASTPGVRVECMDRQDSQRGLLAQWIEESSRIVFFGGAGVSTESGIPDFRGAKGFYHQDREIPLEQVLSIDFFTVHPQAYWEWFAQENAREGVAPNDAHRFVADLERAGKLSAVVTQNIDGLHQRAGSERVLELHGNWSRLTCTGCGEHVTLDDADGARSGEVPHCLACASVLRPDIVFYGEMLDSDVMEGAVRAISEADLLIVAGTSLVVYPAAGLIDYYAGERLVLMNATPTPYDSRADLIIREPVGQVFEELGRRSRRP$","NAD-dependent protein deacetylase, SIR2 family","Cytoplasm","transcription regulatory protein, Sir2 family","transcriptional regulatory protein; Sir2 family ","Silent information regulator protein Sir2","","Gotta M., Strahl-Bolsinger S., Renauld H., Laroche T., Kennedy B.K., Grunstein M., Gasser S.M. Localization of Sir2p: the nucleolus as a compartment for silent information regulators. EMBO J. 1997. 16(11):3243-3255. PMID: 9214640Brachmann C.B., Sherman J.M., Devine S.E., Cameron E.E., Pillus L., Boeke J.D. The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev. 1995. 9(23):2888-2902. PMID: 7498786Frye R.A. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 1999. 260(1):273-279. PMID: 10381378Sherman J.M., Stone E.M., Freeman-Cook L.L., Brachmann C.B., Boeke J.D., Pillus L. The conserved core of a human SIR2 homologue functions in yeast silencing. Mol. Biol. Cell 1999. 10(9):3045-3059. PMID: 10473645Denu J.M. Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases. Trends Biochem. Sci. 2003. 28(1):41-48. PMID: 12517451","","","

InterPro
IPR003000
Family

Silent information regulator protein Sir2
PTHR11085	$\"[45-266]T$	CHROMATIN REGULATORY PROTEIN SIR2
PF02146	$\"[45-221]T$	SIR2
PS50305	$\"[28-270]T$	SIRTUIN

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1220	$\"[26-263]T$	no description

","BeTs to 14 clades of COG0846COG name: NAD-dependent protein deacetylases, SIR2 familyFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0846 is a---kzyqvdrlb-efgh--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB003000 (Silent information regulator protein Sir2) with a combined E-value of 7.8e-50. IPB003000A 39-62 IPB003000B 107-130 IPB003000C 139-154 IPB003000D 181-190 IPB003000E 208-221***** IPB007654 (Protein of unknown function DUF592) with a combined E-value of 1.5e-15. IPB007654D 45-72 IPB007654H 177-199 IPB007654I 200-238","","","-58% similar to PDB:1M2N Sir2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex (E_value = 4.0E_44);-58% similar to PDB:1ICI CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX (E_value = 1.2E_43);-58% similar to PDB:1M2G Sir2 homologue-ADP ribose complex (E_value = 1.2E_43);-58% similar to PDB:1M2H Sir2 homologue S24A mutant-ADP ribose complex (E_value = 2.6E_43);-59% similar to PDB:1YC5 Sir2-p53 peptide-nicotinamide (E_value = 2.6E_43);","Residues 45 to 221 (E_value = 1.1e-68) place ANA_1325 in the SIR2 family which is described as Sir2 family.","","regulatory protein, Sir2 family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1326","1416393","1416133","261","4.35","-8.12","9632","ATGACGTACGCTTGCTGTGTGTCTACGATTCCAGTGACGACCGCTCGTTCTCAGTTGTATCGGCTCATCGATCAGGTCAACGAAGACTCCGAGCCGCTGGTCATCACCGGCCAACGCGGCAATGCCGTCTTGGTGGGGGAGGAGGACTGGAGGGCGATCCAGGAGACGCTCTACCTGGAGTCCGTCCCGGGCATGATGGACTCGATCCGGAATGCCCGACGTGAAGGCATCGAGGCGGGCTCGGAAGAACTCGACTGGTGA","MTYACCVSTIPVTTARSQLYRLIDQVNEDSEPLVITGQRGNAVLVGEEDWRAIQETLYLESVPGMMDSIRNARREGIEAGSEELDW$","Prevent-host-death family protein","Cytoplasm","AviX2","hypothetical protein","prevent-host-death family protein","","","","","

InterPro
IPR003756
Family

Protein of unknown function DUF172
PF02604	$\"[7-80]T$	PhdYeFM

InterPro
IPR006442
Family

Prevent-host-death protein
TIGR01552	$\"[9-61]T$	phd_fam: prevent-host-death family protein

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-56% similar to PDB:1K1G STRUCTURAL BASIS FOR RECOGNITION OF THE INTRON BRANCH SITE RNA BY SPLICING FACTOR 1 (E_value = );-53% similar to PDB:1GVO STUCTURE OF PENTAERYTHRITOL TETRANIRATE REDUCTASE AND COMPLEXED WITH 2,4 DINITROPHENOL (E_value = );-53% similar to PDB:1GVQ STUCTURE OF PENTAERYTHRITOL TETRANIRATE REDUCTASE AND COMPLEXED WITH CYCLOHEXANONE (E_value = );-53% similar to PDB:1GVR STUCTURE OF PENTAERYTHRITOL TETRANIRATE REDUCTASE AND COMPLEXED WITH 2,4,6 TRINITROTOLUENE (E_value = );-53% similar to PDB:1GVS STUCTURE OF PENTAERYTHRITOL TETRANIRATE REDUCTASE AND COMPLEXED WITH PICRIC ACID (E_value = );","Residues 7 to 80 (E_value = 9.9e-16) place ANA_1326 in the PhdYeFM family which is described as Phd_YefM.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1328","1419774","1416691","3084","6.21","-5.53","110645","ATGGGCGGGGGAGGGCCCCGTCCTCCCCACGCGCCGCGCAGCAGGACGGGTGGTGGCCGTCCCGGTCCGCTGGCCATGACGATCTCGATCATCGTGGCCATCGCCGTGGCCATCGGCATCCTGTCGCAGGTGTGGACCGAGGTCCTCTGGTTCAGTCAGATCGGGTACGCCCGTGTGCTGTGGACGCAGTGGATCGCCCTCATCGTCCTCTTCCTGGCGGGATTCGCCATCATGTTCGGGGCCGTCTTCGTCTCGATGACCAGGGCCTACCGTGCCCGGGAGATCGGGATGCCCGACGACGAGGCCACGCGTAACCTCGAGGCCTACCGCTCCGTCATCGAACCCATGCGACGTCGGCTGACCTGGGCGGTTCCGGCAGTGCTGGCACTGTTCGGCTCGGCCTGGGAGCTGGCCCCCAGCTGGCGGGAGATTCTGCTGGCCTTGAACTCCCAGTCCTTCGGGGTCAAGGACCCCCAGTTCGGGATCGACATCTCCTTCTACGTCTTCATCCTGCCGGCGGTGCTGACGCTCGTGTCCTTCCTGGCCGGCGTCGTCCTGTTCTCCGGGGTGACGTCCATCGTCGTCCACTACCTGTACGGCGGTATCTCCGTGGTGCGCAAGCCCCACTTCACCAAGGCCGCCCGCATGCACCTGGCAGTCTTCCTGGCGCTGTACGCCGTCATCCGGGCCGTGGGCTACTGGCTGGGGCGTTACAGCGCCCTGTACGCCTCCAACTCCAAGTTCGACGGCGCCAACTACACCGACGTCAACGCGGTCATCCCCGCCAATGCGATCCTCGCGGCCATCGGACTGGCCGTGGCGATCCTCTTCATCGCCTCGGTGCGCTCCAGCTCCTGGCGCCTGCCGATCATCGGTGTGGCCGTCATGATCGTCTCCTCCCTGGTGGTGGGGACCGCCTACCCGCTGGTCATCCAGAAGTTCATCGTCGACCCCAACGCCCAGCGCCAGGAGGCCGAGTACATCCAGCGCAATATCAACGCCACCAAGGCCGCCTATGGCCTGGAGAACGTGGAGACCACCAACTACGACGCCACGACGAAGGCGGCGGCCGGCCAGCTGGAGAAGGACGCGGAGTCCACCACCTCGATCCGGCTCCTGGACCCCGGGCTCATCTCCCCGACCTTCCAGCAGGTCCAGCAGAACAAGCAGTACTACTCCTTCGCGAACCGGCTCAACGTGGACCGCTACAAGGTGGGCTCCTCCAGCCGGGACACGGTCATCGCGGTGCGTGAGCTCAACCTGTCCGGCCTGGGCGAGCAGCAGCAGACCTGGGTCAACGAGCACACCGTCTACACCCACGGCTACGGCGTCGTGAACGCCTACGGCAACACGGTGGCCACCCGCGGCTACCCCTCCTTCTGGGAGGGAGGCATCCCCTCCAAGGGGGACCTGGGCGAGTACGAGCCCCGGATCTACTTCGGTCAGTCCTCGCCGTCCTACTCCATCGTGGGCGGCAAGGACAACGGCTCGCCGCGCGAGCTGGACTACCCCGATGACGAGTCCAAAACCGGTCAGGTCAACACCACCTTCGCCGGCAACGGCGGGCCGAGCGTGTCCAACCCGTTCAACCGTCTGCTCTACGCCACCAAGTTCCGGGAGGCCAACATCCTCTTCTCCCAGGAGGTGCGCGAGGGCTCCCAGATCCTCTACGACCGGGACCCGGCCAAGCGAGTCGCCAAGGTGGCCCCCTGGCTGACCCTGGACAACAGTCCCTACCCGGCCGTCGTCGATCACGATGACAACCCGGCCACTCCCAAGCGGGTCGTGTGGATCGTCGACGGCTACACCACGACGAACAACTACCCCTACGCCCAGCACGAGTCCCTGGCCAAAGCGACGGCGACCGCCGACAACAAGGGCGGACTTCTGCGGGCGCCGGAGGAGTCCAACTACGTGCGCAACTCCGTCAAGGCCGTCGTGGACGCCTATGACGGGTCGGTCAAGCTCTACCAGTGGGATGACAAGGACCCGATCCTCAAGGCCTGGCAGAAGGTCTTCCCCGGGACGGTCACGCCCATGAGCCAGATGAGCGCCGACCTCATCGCCCACATGCGCTACCCCGAGGACCTGTTCAATGTCCAGCGCACCATGATGGCGACCTATCACGTCAACGACGCCGCGGAGTTCTACTCCGGTGGAGACTTCTGGAAGATCCCGGACGACCCGACCACGCCCGGTCAGGACCAGCAGGCCCCCTACTACCTGACCCTCAAGATGCCCGGGCAGGACCAGGCGAGCTTCTCCCTGTCCAGCGCCTACATCATCGGCGGAAACACCAACCGCAACGTGCTCACCGGCTTCCTCGCCGTGGACTCCGAGACCTCTCCCGGCACCGGGAAGAAGGGGGAACGCAGTCCGAGCTACGGCAAGCTGAGACTCCTGGAGCTGCCGCGTTCCTCGAACGTGGCCGGGCCGGGGCAGGTGCAGAACATCTTCGACTCCAACCCGGAGATCTCCAAGGAGCTCAACCTCCTGTCCCAGGAGGGATCCCAGGTCATCAAGGGCAACCTGCTGACGCTGCCCGTGGGAGGCGGACTGCTCTACGTCCAGCCCGTCTACGTGCAGTCGTCGTCGGGAACTCAGTACCCGCTGCTGCGCAAGGTGCTGGTCTCCTTCGGGGACAACGTCGGATTCGCCGACACCCTCTCGGGGGCGCTCGACCAGGTCTTCGGCGGTAACTCCGGGGCGACCACGGGTCAGGAGGCCATCGACGGCGATGCCGCCGCGGCCAATGACACCAATGAGACGACCGATGGCAAGGACCCGACGGCGGATGGCGGAGCCAAGGCGTCGGCGAGCCCGAGCGCCACGCCCACGGCTTCAGCCAGTGCGTCCCCCTCGGCCTCGGCCAGCGCGTCCTCCAGTTCCTCCGCCACCCTGTCGGCCTCGGGAACCTCGGATCCGAAGGCGGAGCTCAATCAGGCGCTCTCCGATGCTCAGACCGCGATGACTGACGCGGACAACGCCAGGAGCAAGGGCGACTGGTCGGCATACGGTGATGCGCAGAGGCGCCTCAACGAAGCCGTCAACCGGGCCGTTGAGGCCCAGAAGAAGGTGGGCTGA","MGGGGPRPPHAPRSRTGGGRPGPLAMTISIIVAIAVAIGILSQVWTEVLWFSQIGYARVLWTQWIALIVLFLAGFAIMFGAVFVSMTRAYRAREIGMPDDEATRNLEAYRSVIEPMRRRLTWAVPAVLALFGSAWELAPSWREILLALNSQSFGVKDPQFGIDISFYVFILPAVLTLVSFLAGVVLFSGVTSIVVHYLYGGISVVRKPHFTKAARMHLAVFLALYAVIRAVGYWLGRYSALYASNSKFDGANYTDVNAVIPANAILAAIGLAVAILFIASVRSSSWRLPIIGVAVMIVSSLVVGTAYPLVIQKFIVDPNAQRQEAEYIQRNINATKAAYGLENVETTNYDATTKAAAGQLEKDAESTTSIRLLDPGLISPTFQQVQQNKQYYSFANRLNVDRYKVGSSSRDTVIAVRELNLSGLGEQQQTWVNEHTVYTHGYGVVNAYGNTVATRGYPSFWEGGIPSKGDLGEYEPRIYFGQSSPSYSIVGGKDNGSPRELDYPDDESKTGQVNTTFAGNGGPSVSNPFNRLLYATKFREANILFSQEVREGSQILYDRDPAKRVAKVAPWLTLDNSPYPAVVDHDDNPATPKRVVWIVDGYTTTNNYPYAQHESLAKATATADNKGGLLRAPEESNYVRNSVKAVVDAYDGSVKLYQWDDKDPILKAWQKVFPGTVTPMSQMSADLIAHMRYPEDLFNVQRTMMATYHVNDAAEFYSGGDFWKIPDDPTTPGQDQQAPYYLTLKMPGQDQASFSLSSAYIIGGNTNRNVLTGFLAVDSETSPGTGKKGERSPSYGKLRLLELPRSSNVAGPGQVQNIFDSNPEISKELNLLSQEGSQVIKGNLLTLPVGGGLLYVQPVYVQSSSGTQYPLLRKVLVSFGDNVGFADTLSGALDQVFGGNSGATTGQEAIDGDAAAANDTNETTDGKDPTADGGAKASASPSATPTASASASPSASASASSSSSATLSASGTSDPKAELNQALSDAQTAMTDADNARSKGDWSAYGDAQRRLNEAVNRAVEAQKKVG$","Uncharacterized conserved protein","Membrane, Periplasm","Uncharacterised protein family (UPF0182) family","K09118 hypothetical protein","protein of unknown function UPF0182","","","","","

InterPro
IPR005372
Family

Protein of unknown function UPF0182
PF03699	$\"[12-832]T$	UPF0182

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[64-84]?$ $\"[120-138]?$ $\"[166-200]?$ $\"[221-241]?$ $\"[260-280]?$ $\"[290-310]?$	transmembrane_regions

","BeTs to 4 clades of COG1615COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1615 is a---------r--c------------Number of proteins in this genome belonging to this COG is 1","***** IPB005372 (Protein of unknown function UPF0182) with a combined E-value of 1.1e-137. IPB005372A 141-175 IPB005372B 248-258 IPB005372C 382-403 IPB005372D 431-452 IPB005372E 540-588 IPB005372F 597-611 IPB005372G 636-674 IPB005372H 682-728 IPB005372I 788-804","","","-41% similar to PDB:1OD2 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN (E_value = );-41% similar to PDB:1OD4 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN (E_value = );-41% similar to PDB:1W2X CRYSTAL STRUCTURE OF THE CARBOXYLTRANSFERASE DOMAIN OF ACETYL-COENZYME A CARBOXYLASE IN COMPLEX WITH CP-640186 (E_value = );-51% similar to PDB:2O62 Crystal structure of hypothetical protein (ZP_00105914.2) from Nostoc punctiforme PCC 73102 at 1.75 A resolution (E_value = );-45% similar to PDB:1ZDL Crystal Structure of Mouse Thioredoxin Reductase Type 2 (E_value = );","Residues 12 to 832 (E_value = 1.8e-281) place ANA_1328 in the UPF0182 family which is described as Uncharacterised protein family (UPF0182).","","protein family (UPF0182) family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1330","1420132","1420713","582","4.74","-16.12","20610","ATGCATGACGAGGCGACCATCCCGGGCTCGGGTCGAGCCGCGGCCTCCGCAGCACATGCGCTGGCCCGCGCGGTGACGGAGACCGAGACTCACGTGGCGGCCCACGGCTGGGACCAGCCGGTGCGCGTCTTCGCACTGGTGCGCACAGCCGAGGCTCTTGAGGCCGACCCGGACGTGGCCGGCCTCCTGGACACCGCCACCGTGGAGGAGGCCCGCACGAACCCCGAGCTGCTCATGGTGGTGGAGCAGGAGGGGCTGCCGCCCGCCGCGGACCTGGAGCACCTGCTGGCGCAGCTCGCCTGGCCCGACTCCGTCCACGGCGCCGCCATCAGCGTCGAGCGGCTGGTCCTTCCGCCCGCGGCCCAGGAGGAGGCCGAGGCCATCACCGATGCCGCTAAGCGTCTGGCCTTCCTCCAGGAGCGCCCGGACCGCGAGGACATCCGCATGGTGGTGGGGGTCCTGCGCGGCGGGCAGTCCTGGTGCGTACTGCGCTCACGCAGTCACGACGACGACGCCTCGCTCTACCAGGGCGAGCACCTGGTCCCCGGGCTGGTCGAGGCCCTGGCGGCGACCTTCCTGTAG","MHDEATIPGSGRAAASAAHALARAVTETETHVAAHGWDQPVRVFALVRTAEALEADPDVAGLLDTATVEEARTNPELLMVVEQEGLPPAADLEHLLAQLAWPDSVHGAAISVERLVLPPAAQEEAEAITDAAKRLAFLQERPDREDIRMVVGVLRGGQSWCVLRSRSHDDDASLYQGEHLVPGLVEALAATFL$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-50% similar to PDB:1QCY THE CRYSTAL STRUCTURE OF THE I-DOMAIN OF HUMAN INTEGRIN ALPHA1BETA1 (E_value = );-47% similar to PDB:1SB7 Crystal structure of the E.coli pseudouridine synthase TruD (E_value = );-47% similar to PDB:1SI7 Structure of E. coli tRNA psi 13 pseudouridine synthase TruD (E_value = );-47% similar to PDB:1SZW Crystal structure of E. coli tRNA pseudouridine synthase TruD (E_value = );-41% similar to PDB:1FFK CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI AT 2.4 ANGSTROM RESOLUTION (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1331","1422372","1420774","1599","4.46","-43.72","56717","ATGCCCAAGGACGACCCGGCGAGAGGAAACCCCGTGAGCGAGGACGCCTTCGACGAGCTCGAGAAGATGCTCGCATCTCTGTTCGGCGAGCAGATGGCCTCCGACGCCGTCGGCGCCCTGCGCTCATCCGGGGTGGATCCCAGTTCCATCGCCCAGATGCCGGGGGTGGGGGACATCTCTCAGCTCAGTCCCGCCCAGCTGCTGGCGATGCGCGCCCAGTTCCAGCAGATGTTCTCCGCCTCCACCACCGAGCCGGTCAACTGGCAGATGGGGCAGGAGCTGGCCCTTCAGCAGGCGCGCGGCGACGGCGACCCCACGGTGACCGCCGCGGTCGCCGAGTCCACGCGCCAGGCCCTTCAGGTGGCCGACCTGTGGCTCGACACCGCCACTGAATTCATGCCCGCCCCCGGGCAGCGGGAGGCCTGGAGCCGTGGCACCTGGGTCGAGCGCACGCTGCCGGTGTGGAAGGACGTGTGCGCCCCGGTGGCCGAGGCCGTCACCGCCGCCCTGGCCCGCACCCTGGAGAAGCAGATTCAGGACATGCCGGCTGAGATGGGGCAGGCCGCCCAGCAGATGGGGGCGCTCGGGTCCATCATGCGCACCATGGCCGGCACGGCCTTCGGCCTCCAGATCGGCCAGGCCATCGGTGAGCTCGCCAAAGAGGCGTTGGGGGCCACCGACACCGGCCTGCCCCTGACCCGTGAGCCCGGCACGGCACTGGTTCCCGTCAACGTGGCCGCCTTCGCTGAGGGGCTGGAGGTCGATGAGGACGAAGCCCGCATGTTCCTGGCTGTGCGGGAGGCCGCCACCGCCCGCCTTTACGCCCACGTGCCGTGGCTGCGCGGTCAGGTGCTTCAGGCAGTGGTCGCCTACGCCCGCGAGATCCGCATCGACACTGAGATGCTGGAGTCCGCTGTGGCCCAGGTGGATCCCAACGACCCCGACGCTCTGCGCGAGGCCCTTGAGAGTGGGCTGTTCGCACCCCAGGAGACGGCGGCCCAGCGCGAGGCCCTGGAGGACCTGGAGACGCTCCTGGCACTCGTTGAGGGCTGGGTCGAGGTGGTCACCGCCCGCGCCGCCGCACCGCACCTGCCCCACCTCATGGCACTGGCCGAGATGATGCGCCGGCGCCGGGCCCAGGGCGGCGCCGCCGAGCAGGTCTTCGCCCGCCTCATCGGGCTGACCTTCCGGCCCCGCCGGGCTCGGGAGGCCGCCGAGCTGTGGGCCCACCTGGGCGCCCAGGCCGGTGACGCCGAGCGCGACGCCTTCTGGAACCACCCCGACGTCATGCCCACGGCCTCCGAGCTCGCCAACCCCAAGGACTTCCTCACCATGCGGCGCATGGCCCAGGACATCGACGCCGAGATCGACGCCGACCTGGCCTCCCTGCTGGACGGGACCCTCGGGTACGCCGAGGGCGCCAAGGAGGCTGATGAGAACAGCCCCGAGGGGCTCGGGGACCGGAACCCCGCCTCCGCCGACGACGCGGCCTCCCAGGAGCCCAGCCAGTCAACGGGCCCCGTCTCGGCCGGCCCCGGGGACGAGGACTCGCCCGGAGAGCCCGACGAGCAGGACCCGACCGGCACGGACAAGGCCTGA","MPKDDPARGNPVSEDAFDELEKMLASLFGEQMASDAVGALRSSGVDPSSIAQMPGVGDISQLSPAQLLAMRAQFQQMFSASTTEPVNWQMGQELALQQARGDGDPTVTAAVAESTRQALQVADLWLDTATEFMPAPGQREAWSRGTWVERTLPVWKDVCAPVAEAVTAALARTLEKQIQDMPAEMGQAAQQMGALGSIMRTMAGTAFGLQIGQAIGELAKEALGATDTGLPLTREPGTALVPVNVAAFAEGLEVDEDEARMFLAVREAATARLYAHVPWLRGQVLQAVVAYAREIRIDTEMLESAVAQVDPNDPDALREALESGLFAPQETAAQREALEDLETLLALVEGWVEVVTARAAAPHLPHLMALAEMMRRRRAQGGAAEQVFARLIGLTFRPRRAREAAELWAHLGAQAGDAERDAFWNHPDVMPTASELANPKDFLTMRRMAQDIDAEIDADLASLLDGTLGYAEGAKEADENSPEGLGDRNPASADDAASQEPSQSTGPVSAGPGDEDSPGEPDEQDPTGTDKA$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","conserved hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1332","1422447","1423826","1380","5.22","-13.00","47947","ATGTTCCGTTCGCCGACGGCGTGCCCGCACCGCCCCGGAGAGGCTCAGGGCTTCTCCGTAGCGGCCCTGGGCCGGGTTCGTACCAGGTTCATGCTGGGTTCGTGTCGGTATGTGTCCGTCTTCCCCAGGATGATGTCGCATGATGAGCGCGTGACGCACCCAGACCAGCACGACGCCGCCGACACTGCGGACTCGACCTCCCCAGGCACCACCCAGCCGATGCGGGAGCATGAGAGCAATCCGCTCGACCAGGCCGGGCACGCCGAGGCCCCGGCCCCGCAGCCCTCCGCGCAGGACCGGCGTCGACGCAGGCTGCGACGCTCCGTGACGGTCGGGGCGGTCCTGGTGGTGGTGGCCCTCATCGTCGCCGTCTTCACGGTGCCGATCAACGTGGTCATCGAGGCCCCCGGCCCGACCTGGAACGTGCTGGACAACGGTTCGTCGTCGAGCCAGGACGTCCTGAAGGTCTCGGGAACTGAGACCTATCCGACCGAGGGCGCCCTGCGGATGACGACGGTCTCCGTATCGGGCTGCCCCGGCTACCCGGTGACCACCGCTGACCTCGTCACCGCCTGGTTCTCGGCGGACAAGCGGATCGTGGACCGCAACCAGGTGTGCCCGCAGGATCAGAGCGCCGAGCAGGTCGAGGAGACCGGTAAGGCCCAGATGACGGCCTCGCAGGACTCCGCCGTCATCGCCGCACTCGTGGAGACCGGTAAGGCCGGCGCCATGCACCTGACCGTCACTGAGGTGACCGAGCAGCAGACCTCGACGGAGATCCAGGCCGGGGACGTCCTGGAGACCATCACTCCTGAGGGCGGCCAGACGACGACCATCACCTCCTTCTCCCAGCTGCGAGAGCTCATGACCACCATTGCCGAAGGCACTCGGGTGACACTCGGGGTGCGCCGCGGCGAGCAGCAGGCGAGCGCCGCGCTCACCACGATCGCCCCGCAGGAGGGGACGACCGGTTCCCTGCTGGGGCTGAGCCTGAGGATCTCGGTGGACAGTCAGGTGGAGGCCACCTTCAGCCTGTCCGACGTCGGCGGCCCCAGTGCTGGCATGATGTTCGCGTTGGGGGTCGTTGACGAGATCACCCCGGGGGCCCTGACCGGAGGCAAGGACATCTCCGGGACCGGGACGATCGACATGACCGGGCAGGTCGGCCCCATCGGCGGGATCCAGCAGAAGATGGCGGGTGCCAGAGAGGCGGGCTCCGCGTTCTTCCTCGCCCCGACGAGCAACTGCGAGGAGGTCAAGGGTCATGAGCCCAAGGGCATGCAGGTCTTCGCCGTGAGCACCCTGCACGAGGCCGTCACCGCCACTCAGGCGATCGCGTCGGGTGACACCTCCGGCCTGGCCACGTGCTCGGCCAAGTGA","MFRSPTACPHRPGEAQGFSVAALGRVRTRFMLGSCRYVSVFPRMMSHDERVTHPDQHDAADTADSTSPGTTQPMREHESNPLDQAGHAEAPAPQPSAQDRRRRRLRRSVTVGAVLVVVALIVAVFTVPINVVIEAPGPTWNVLDNGSSSSQDVLKVSGTETYPTEGALRMTTVSVSGCPGYPVTTADLVTAWFSADKRIVDRNQVCPQDQSAEQVEETGKAQMTASQDSAVIAALVETGKAGAMHLTVTEVTEQQTSTEIQAGDVLETITPEGGQTTTITSFSQLRELMTTIAEGTRVTLGVRRGEQQASAALTTIAPQEGTTGSLLGLSLRISVDSQVEATFSLSDVGGPSAGMMFALGVVDEITPGALTGGKDISGTGTIDMTGQVGPIGGIQQKMAGAREAGSAFFLAPTSNCEEVKGHEPKGMQVFAVSTLHEAVTATQAIASGDTSGLATCSAK$","Secreted protein containing a PDZ domain","Membrane, Periplasm","Predicted secreted protein containing a PDZdomain","K07177 PDZ domain-containing protein","secreted protein containing a PDZ domain-like","","","","","

noIPR
unintegrated

unintegrated
PTHR10046	$\"[350-437]T$	ATP DEPENDENT LON PROTEASE FAMILY MEMBER
tmhmm	$\"[109-129]?$	transmembrane_regions

","BeTs to 3 clades of COG3480COG name: Predicted secreted protein containing a PDZ domainFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG3480 is ----------rlb-------------Number of proteins in this genome belonging to this COG is 1","***** IPB001984 (Peptidase family S16) with a combined E-value of 8.7e-07. IPB001984I 375-418","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","secreted protein containing a PDZ domain","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1333","1423995","1424975","981","6.54","-2.26","34855","ATGCGTGTACGAGGCGGGTGCGCCATCCTGTGGCGCCAGCAGGGCGTCAGCCAGATCGGGACAAGTCCCGAGCGCCGCACCATTGTCAGTGACCTGAGCCTGGCCGAGCAGCGCCTGCTCGATGAGTTCGCGCGCAACCTGGAGAGCGCAGGGGTCTACCGGGCCGCCCGGCGCAGCCGGGTGCCGGTGACGCGGGCGCGGCAGATTGTCGCGGACCTGGAGCGTCAGGGGGTGCTGGTGGCCTCGGCGACCAGCGAGCTCGGTGGGGCCGACGGCGTCTACTGGGACCGGCTGGGAGCTGACGCCAAGGGCCGTGGCGCGGTCCTGTCCCAGGCCGTCCTGGCTGTTCACGGCGTGAACGCCCTGGCTCAGGAGGCTGCTCTGTGGCTGGCGGAGGCGGGGGTGGGCACGATCCTGTCCACCCGGTCTCCGCAGGACGGGGGCCTGGCTCCGCTCCTGTCGGCGCGGTTCCCAGCCCTGAGGACGCGGGCGCCGTTGCGCACCCGTCCTGATGTCATGGTGACGGTGGACGCGCACGTGGTCGAGCCGCTGCTCGCGCGCCGACTCGTTCAGGAGGACGTGGTGCATCTGCCTGTCGTCGTCGGCGAGGCGGGAGTGCGCATCGGCCCGGTACTCAACGCTCAGGGCCCGTGCTCGACCTGCCTGGCCCTGTGGGAGAGGGACGCCGACCCGTGCTGGCCGGCGCTGGCCACGCAGATGCGCACCCTGCCGATGCCCGAGGTCGAGCACCTGGTCCTGCACGAGGCCGCGGCGTCAACGGCGCGGGCCGTCATCGACACGCTGGTGGGCCGGGCATCCGGGGCCGACGGCGCCGGGGACGAGGCTGAACCAAGCGGGGAGGCGAGCGAGGACTCGGCCGCGTGGTGGTCCACGCACTCGGTGGAGGTCACCGGCCGGGAGCCCCGGGGGCGGCACAGGGCCTGGGATCGTCACCCCGAGTGCCTGTGCTCGCAACTGTGA","MRVRGGCAILWRQQGVSQIGTSPERRTIVSDLSLAEQRLLDEFARNLESAGVYRAARRSRVPVTRARQIVADLERQGVLVASATSELGGADGVYWDRLGADAKGRGAVLSQAVLAVHGVNALAQEAALWLAEAGVGTILSTRSPQDGGLAPLLSARFPALRTRAPLRTRPDVMVTVDAHVVEPLLARRLVQEDVVHLPVVVGEAGVRIGPVLNAQGPCSTCLALWERDADPCWPALATQMRTLPMPEVEHLVLHEAAASTARAVIDTLVGRASGADGAGDEAEPSGEASEDSAAWWSTHSVEVTGREPRGRHRAWDRHPECLCSQL$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1334","1427096","1425009","2088","7.32","1.41","75283","ATGAGCCCGACCACCCCCCACCCCGCCCCTCTCGAGGTATCCAGGCTCCTGGAGGCCCTCGACCCCGACCAGCGCGAGGTCGCCGAGCACCTCGAAGGCCCCCTGTGTGTCCTGGCGGGCGCAGGCACCGGCAAGACCCGGGCCATCACCTATCGCATCGCCCACGGCGTGGCCACCGGCGCCTATCAGGCCACCCAGGTCCTGGCCGTCACCTTCACCGCCCGCGCCGCCGGCGAGATGCGCTCGCGCCTGGCCGACCTCGGCGTCCCCGGCGTCCAGGCCCGTACCTTCCACGCCGCCGCCCTGCGTCAGCTCACCTACTTCTGGCCCACCGCCATCGGCGGGCGCCGCCCCGATATCCAGGCCCATAAGGCGCCCCTGGTCGGCGCCGCCGCCCGTCGCCTGGGCCTGCCCACCGACCGGGCCACCGTGCGGGACCTGGCCGCCGAGGTCGAGTGGGCCAAGGTCACCATGACCCTGCCCGAGGACTACGCCCAGGCCGCCGTCGTCGCCGGTCGCACCGGCGTGGCCGGGCAGGAGGCGGCCACCGTCGCCCAGGTCCTGTCCCTCTACGAGGAGGCCAAGAGCGAGCGCGGCGTCATCGACTTCGAGGACGTGCTCCTGCTGACCATCGGGATCCTCCTGGACCGCGAGGACGTCGCCGCCCAGGTGCGCGGCCAGTACAAGCACTTCGTCGTCGATGAGTACCAGGACGTCTCCCCGCTCCAGCAGCGCCTGTTGGACCTGTGGCTGGGACGGCGCCGCCAGCTCTGCGTCGTGGGGGACGTCTCTCAGACCATCTATTCCTTCACCGGCGCCACGCCCGCCTTCCTCACCGGTTTCGCCACCCGCTACGAGGGGGCGCGCACCGTGCGCCTGAGCCGCGACTACCGCTCTACCCCGCAGGTCGTCTCCCTGGCCAACCGGGTCCTGTCCCGCTCGCGGCGTGGGGGCGGCGGTCTGCATCTGCCCGCCGGCGCCGTCGAGCTGGTCGCCCAGCGGCCCAGCGGCCCAGCCGTGCGTTTCGAGACCTACGACGATGACATCGCCGAGGCCGAGGGCGCCGTCGCTCAGGTGCGCCGGCTGCAGGCCGCCGGGGTCCCCCTGAGCGAGATCGCGATCCTGTACCGCACCAACTCCCAGTCCGAGGTCTTCGAACAGGCCCTGGCCGGAGCCCAGATCGGCTACCTCGTGCGCGGCGGCGAGCGTTTCTTCGAGCGCGAGGAGGTCAAACGCGCCATGGCCGTCGTCCTCGGGGCCGCCCGCACCGAGAAGGCCACCCTGACCGGAGACCTCGGCCAGGACGCGCGCACCGTCCTGGCCCGTGAGGGCTGGAGCGAGGAGCCGCCCGCACCGCGTGGAGCTGTGCGCGAGCGGTGGGACGCTCTCAACGCCCTGGTGGCCCTGGCCGATGAGATGGCCCAGACCCGCGGCGCCGACCTCGACGCCTTCCACACCGAGCTGCGTGAGCGCGCCGACGCCCAGAACGCCCCCACCGTCGAGGGCGTCACCCTGTCCTCCCTGCACGCCGCCAAGGGCCTGGAGTGGGACGCCGTCATCCTCGCAGGCGTCTGCGAGGGGCTGCTGCCGATCTCCTTGGCCGAGGGGCAGGCGGCCATCGAGGAGGAGCGGCGCCTGCTCTATGTGGGCGTCACCCGCGCGAGAGAGCACCTCATCATCTCCTACGCCCGTGCCCGCAACGCAGGCGGACGGGCCGCCCGCAAGCCCTCCCGCTTCCTGGACGGCCTGTGGCCCACCGGCGACGGTCTCAAAGACGCCTCCCGGCGCCAGGGCCGCCAAAGCGCCAAGGAACGCTCCCGGCAGTCCGCCGCCGACTTCGAGGCCAACAACGACCCGCGCACCATCGCCCTGTTCGAGGAGCTGCGGGCCTGGCGCTCCCAGGTCGCCAAGGAGAGGGGCAAGCCCGCCTTCACGGTCTTCGCCGACGCCACCCTGCGGGACATCGCCGTCGTCAAACCCACCAGCCTGCCCCAGCTCTCCCTCATCCGCGGCGTGGGCGCCACCAAGCTCCAGGACTATGGCGGGCCGGTCCTGGCCCTCCTGCGCGACTTCGAAGCGGAGAACTGA","MSPTTPHPAPLEVSRLLEALDPDQREVAEHLEGPLCVLAGAGTGKTRAITYRIAHGVATGAYQATQVLAVTFTARAAGEMRSRLADLGVPGVQARTFHAAALRQLTYFWPTAIGGRRPDIQAHKAPLVGAAARRLGLPTDRATVRDLAAEVEWAKVTMTLPEDYAQAAVVAGRTGVAGQEAATVAQVLSLYEEAKSERGVIDFEDVLLLTIGILLDREDVAAQVRGQYKHFVVDEYQDVSPLQQRLLDLWLGRRRQLCVVGDVSQTIYSFTGATPAFLTGFATRYEGARTVRLSRDYRSTPQVVSLANRVLSRSRRGGGGLHLPAGAVELVAQRPSGPAVRFETYDDDIAEAEGAVAQVRRLQAAGVPLSEIAILYRTNSQSEVFEQALAGAQIGYLVRGGERFFEREEVKRAMAVVLGAARTEKATLTGDLGQDARTVLAREGWSEEPPAPRGAVRERWDALNALVALADEMAQTRGADLDAFHTELRERADAQNAPTVEGVTLSSLHAAKGLEWDAVILAGVCEGLLPISLAEGQAAIEEERRLLYVGVTRAREHLIISYARARNAGGRAARKPSRFLDGLWPTGDGLKDASRRQGRQSAKERSRQSAADFEANNDPRTIALFEELRAWRSQVAKERGKPAFTVFADATLRDIAVVKPTSLPQLSLIRGVGATKLQDYGGPVLALLRDFEAEN$","ATP-dependent DNA helicase","Cytoplasm","Superfamily I DNA and RNA helicases","putative ATP-dependent DNA helicase ","UvrD/REP helicase","","Morozov V., Mushegian A.R., Koonin E.V., Bork P. A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases. Trends Biochem. Sci. 1997. 22(11):417-418. PMID: 9397680","","","

InterPro
IPR000212
Family

UvrD/REP helicase
PTHR11070	$\"[31-581]T$	UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580	$\"[20-494]T$	UvrD-helicase

InterPro
IPR002121
Domain

HRDC
PF00570	$\"[618-694]T$	HRDC
PS50967	$\"[618-695]T$	HRDC

InterPro
IPR014016
Domain

Helicase superfamily 1, UvrD-related
PS51198	$\"[18-300]T$	UVRD_HELICASE_ATP_BIND

InterPro
IPR014017
Domain

UvrD-like DNA helicase, C terminal
PS51217	$\"[301-556]T$	UVRD_HELICASE_CTER

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[9-293]T$ $\"[294-583]T$	no description

","BeTs to 22 clades of COG0210COG name: Superfamily I DNA and RNA helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0210 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 4","***** IPB000212 (UvrD/REP helicase) with a combined E-value of 4.5e-54. IPB000212A 39-49 IPB000212B 71-84 IPB000212C 191-206 IPB000212D 224-240 IPB000212E 260-273 IPB000212F 293-311 IPB000212G 505-521 IPB000212H 542-554","","","-41% similar to PDB:2IS1 Crystal structure of UvrD-DNA-SO4 complex (E_value = 1.9E_39);-41% similar to PDB:2IS2 Crystal structure of UvrD-DNA binary complex (E_value = 1.9E_39);-41% similar to PDB:2IS4 Crystal structure of UvrD-DNA-ADPNP ternary complex (E_value = 1.9E_39);-41% similar to PDB:2IS6 Crystal structure of UvrD-DNA-ADPMgF3 ternary complex (E_value = 1.9E_39);-41% similar to PDB:1PJR STRUCTURE OF DNA HELICASE (E_value = 4.7E_38);","Residues 20 to 494 (E_value = 1.4e-74) place ANA_1334 in the UvrD-helicase family which is described as UvrD/REP helicase.Residues 618 to 694 (E_value = 2e-16) place ANA_1334 in the HRDC family which is described as HRDC domain.Residues 618 to 695 (E_value = 3.1e-17) place ANA_1334 in the HRDC family which is described as HRDC domain.","","I DNA and RNA helicases (uvrD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1336","1428274","1427159","1116","5.01","-13.19","39350","ATGCGCACCTCCCAGCTCGCCCTCTCCCGCTCCGCCACCGACCGCGACGCCGAGCGACGCAGCGAGCCCGGGCTGCTGGAGCGCCTCGCCGCCGACCCCGACACCCGCCTGCTGCTGGTCGACGCCCGTGGCCGCGTCGCCCTGACCGGCCCCGCCATTCACCCCGACTTGCCCGACGACGGCCTCACCCCACCCAGCCTCATCGGCAGCCCCGGCGCCACCGCCTGGGAGGGCCCCGGCACCCGCAGCGGCTGGGGCCTGCCCGACCTGCGCGTCGGCTACCTCGGAGCCTCCGCCCCCACTCGCTGCCCCGACCTGACCGTCCTCTACATGGGCCGCGAACTCTCCGATGACGCAGCCTCCACCGGCCCCGCCTGGATCGCCGTCGTCGTGCCCCAGGCCCTCGAGGTCCCCGACGCCCCCGAGCCTCCCGCCACCGGCTCCGACGCCGAGGGCACCGCCGTCGACCACCCCGACCTGCGCCGCCTGCTGGAGCGCTACCCGCTCTCCGCCCTGCGAGCCATGGGCGCCCAGATGACGGCCCGCGACGCCGGCCTGGCCACCACGGCCACCGCCCTGGCCGCCTGGCACGCCCGCTCCGCCTACTGCCCGGGCTGCGGCGGACGCACCGAGATCATTGAGGCCGGCTGGGCCCGGCGCTGCTCCGACTGCGCCACCGTCCACTTCCCGCGCACCGACCCGGCCGTCATCATGGCGGTCACCGACACCTCCGACCGCCTCCTCCTCGTGCGCGGCGCCGCCTGGGCTCCCCGGCGCTACTCGGTCGTGGCCGGCTTCGTCGAGGCCGGCGAGTCCGTTGAGGCGGCCGTGGCCCGGGAGGTATGGGAAGAGGCCGGGCTGCGCGTGGCCGACGTCGAGTACGTCGCCTCCCAGCCCTGGCCCTTCCCACGCTCCCTCATGCTCGGCTGCCGTGCCCGCCTGGCCCCCGGCGAGGACCGGCCCCGCCCCGACGGCCAGGAGGTCGTTGAGGCCCGCCTGGTCTCCCGTGACGAGCTCACCGCGGCCGCCGACGACGGCAGCATCCTCCTGCCCGGCCCCACCTCCATCGCCAGACTCCTCATCGAGGACTGGTACGGCGGCCCCATCGTCAGCTGA","MRTSQLALSRSATDRDAERRSEPGLLERLAADPDTRLLLVDARGRVALTGPAIHPDLPDDGLTPPSLIGSPGATAWEGPGTRSGWGLPDLRVGYLGASAPTRCPDLTVLYMGRELSDDAASTGPAWIAVVVPQALEVPDAPEPPATGSDAEGTAVDHPDLRRLLERYPLSALRAMGAQMTARDAGLATTATALAAWHARSAYCPGCGGRTEIIEAGWARRCSDCATVHFPRTDPAVIMAVTDTSDRLLLVRGAAWAPRRYSVVAGFVEAGESVEAAVAREVWEEAGLRVADVEYVASQPWPFPRSLMLGCRARLAPGEDRPRPDGQEVVEARLVSRDELTAAADDGSILLPGPTSIARLLIEDWYGGPIVS$","NADH pyrophosphatase","Cytoplasm","NADH pyrophosphatase","NADH pyrophosphatase ","NUDIX hydrolase","","Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 1992. 174(20):6321-6325. PMID: 1328155Koonin E.V. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 1993. 21(20):4847-4847. PMID: 8233837Mejean V., Salles C., Bullions L.C., Bessman M.J., Claverys J.P. Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydrolases. Mol. Microbiol. 1994. 11(2):323-330. PMID: 8170394Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 1993. 268(31):23524-23530. PMID: 8226881McLennan A.G. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int. J. Mol. Med. 1999. 4(1):79-89. PMID: 10373642Bessman M.J., Frick D.N., O. Handley S.F. The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes. J. Biol. Chem. 1996. 271(41):25059-25062. PMID: 8810257","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[260-274]T$ $\"[274-289]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[221-341]T$	no description
PF00293	$\"[232-358]T$	NUDIX
PS00893	$\"[265-286]T$	NUDIX

InterPro
IPR015375
Domain

NADH pyrophosphatase-like, N-terminal
PF09296	$\"[35-196]T$	NUDIX-like

InterPro
IPR015376
Domain

Zinc ribbon, NADH pyrophosphatase
PF09297	$\"[198-229]T$	zf-NADH-PPase

noIPR
unintegrated

unintegrated
PTHR22769	$\"[236-339]T$	MUTT/NUDIX HYDROLASE

","BeTs to 7 clades of COG2816COG name: NTP pyrophosphohydrolases containing a Zn-finger, probably nucleic-acid-bindingFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2816 is ------y--dr---efgh---j----Number of proteins in this genome belonging to this COG is 1","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 7.7e-10. IPB000086 260-287","","","-43% similar to PDB:1VK6 Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli k12 at 2.20 A resolution (E_value = 1.8E_11);-43% similar to PDB:2GB5 Crystal structure of NADH pyrophosphatase (EC 3.6.1.22) (1790429) from Escherichia coli K12 at 2.30 A resolution (E_value = 1.8E_11);-48% similar to PDB:2DPN Crystal Structure of the glycerol kinase from Thermus thermophilus HB8 (E_value = 1.8E_11);","Residues 35 to 196 (E_value = 0.00056) place ANA_1336 in the NUDIX-like family which is described as NADH pyrophosphatase-like rudimentary NUDIX domain.Residues 198 to 229 (E_value = 2.5e-12) place ANA_1336 in the zf-NADH-PPase family which is described as NADH pyrophosphatase zinc ribbon domain.Residues 232 to 358 (E_value = 3.5e-27) place ANA_1336 in the NUDIX family which is described as NUDIX domain.","","pyrophosphatase (MutT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1337","1430587","1428575","2013","8.65","11.56","74008","ATGCGAACCCAAATGGACATCGCCGTCATCGGCTCCAACATGGTTGGCCTCATCTCCTACCCGCATCCTAAGCCCTGCCAAGCGAAGCCCCAGGATGCTGTTGACGTTCGTAGAGAATGTGAAGGAAAAAACACCAATGGCCTCCTCTCACCTGTTGATCTCCAGAATGTAGAAGAAGACATTGCCTCCTGTCGACTTATCGTCCTACAGGTCGAAACCCCCCTGAAGACTGCCCATGAGGCGATTGCCTTGGGGCGTAAGCACAACGTCCCTGTTCTGCTCAACCCTGCTCCTGCTGACCCTAATCTCGAGTTGGCGCGAATTCGCGGCTGTAGTTACATCGTTCTCAACAGCGCTGAACTATCTATGCTTACCCACATGCCGACAGGTACCTCTGAAGACGTTCGGAGTGCGGCCGCCAGAATATGTGAGAACGACATCGACAACGTCATTGTAGTCCTCGAAGGTCAGGGCGTGATGTGGGTTTCCAGCACCGGAGCGCGGCCACTGCTTGCAGCTCCCACCATCACACTCGATACCACCAGCGCTCGCGACGCCTTCATTGGCTCCTTCGGCCACCACCTGGTAAACACTGGCAACGTGGAGCGATCTCTAGAGTTGGCAATTGCTTCACAGGTTCCTCTAGCAGAAGAGGGCTCTGAGTCTTCTTCGCCGCCATTATCACGTTCGAAACCGTTGCTCGAGAAAAGCGGGCGCTTTAATGCCTCAAAGCGTTTACTCAGAGGGGGTGATGAAAGTAAGAGTGGGACGATACGAGTTCGGATTAGGCTATCTGAAGGCTATATTCTGTGGCAGTTCTTGACGATAATGTATGTAGTTGGGGTGGCCCTTGCTGTCTGGATGCTCGTTGATTACAGTAGAGTGTTTTCCTGGGTTAAAGAACTGCGGGGAAAAGAGAGGGCTTTCGCATTCTATAATTGGGGGAGTTCGTGGGGGCCCAGTGAATATCTTTCGAATTCAAGTCAGTTATTTGCCTTAGTCGGAGGAGTTCTTGCACTTACGGCGATAGCCGGGTCTCAGTTTGGTCCGATTGCCGATAGTCTAGGGCGTATTCTTACTGACCGCTGGAAGTCTTCGTTGGTGGCGCTTGCCATGGCTTTGTTGTGCTGCCTGGTTATTCTAGTTAATGTCATATGGTGGGTGGTTCCTCGCTCGTGGTCGGACCATGTCCTTGTGTTAGGCGGGATGTGTTTTAGTGTGCTCTGTGTGGCGTCTCCGTGGATGCTGATTGCGGTTGTTCATGAGCCTGTAGTAGAGAAAATTAACTCTCGCTTCAAGAGGAAGAAAAAAGAGCTTGATGTCTTGTGGGAAGAATATAGGAAACACTCCGAAAGCCGCGCCCCTGCGGTGGGTGGCGATGCTTTCGGTGAGGTTGCGGAACTATATCCAAGTCCGAATCGGAGTAAGCTGGTTGTTTGGGCGCATCGACTTATCGTAAGCATTCCACTGCTGTTCCTTGTGGTTGTTTATATTGTCGGGGTTTTGAGGGGTGGCCAGGGTCAGGTAAAGAGTCCTCCATCTTCATGGAATTTGATTGTCTCTGTAGCCGTGGCTGCAATACTGTCGGCGACTCTCGTGGTGTTTTGGCTATATTTTATGAGGATGGTGTATGCATTCTTCATGTTAAGCGAAAGGGTTGTTAAAGGTGATCGACGTAGGTGGGTGGATCACCTGTTTCGAGGGCTCTTTGCTGTGTTCACATTGATGTATGGCGTGCCGTTAGTTGCGGGATCGTGTATTTTTGTTTGGCATGAGGCTGTTGCTGTTGAGAAATCGTATGTCTGGGCCTGGGTGGTGTCGATGCTTTCGGCTGCATTGTCTCTAGGGATCTCCTTCTATTTTCTTGTATACTTTGCTGGTGATAAAAGGCGTTTATTTCGCCCAGTTTTGGTGTACCTTCCAAGAAAGTTGAGGGCTTGCGAGGTGGATGTTATGGAGTTGGGTGGGTATGTCGCCCTTGAATCCGAGACGACTCAGGGGGGGGTGAAATAG","MRTQMDIAVIGSNMVGLISYPHPKPCQAKPQDAVDVRRECEGKNTNGLLSPVDLQNVEEDIASCRLIVLQVETPLKTAHEAIALGRKHNVPVLLNPAPADPNLELARIRGCSYIVLNSAELSMLTHMPTGTSEDVRSAAARICENDIDNVIVVLEGQGVMWVSSTGARPLLAAPTITLDTTSARDAFIGSFGHHLVNTGNVERSLELAIASQVPLAEEGSESSSPPLSRSKPLLEKSGRFNASKRLLRGGDESKSGTIRVRIRLSEGYILWQFLTIMYVVGVALAVWMLVDYSRVFSWVKELRGKERAFAFYNWGSSWGPSEYLSNSSQLFALVGGVLALTAIAGSQFGPIADSLGRILTDRWKSSLVALAMALLCCLVILVNVIWWVVPRSWSDHVLVLGGMCFSVLCVASPWMLIAVVHEPVVEKINSRFKRKKKELDVLWEEYRKHSESRAPAVGGDAFGEVAELYPSPNRSKLVVWAHRLIVSIPLLFLVVVYIVGVLRGGQGQVKSPPSSWNLIVSVAVAAILSATLVVFWLYFMRMVYAFFMLSERVVKGDRRRWVDHLFRGLFAVFTLMYGVPLVAGSCIFVWHEAVAVEKSYVWAWVVSMLSAALSLGISFYFLVYFAGDKRRLFRPVLVYLPRKLRACEVDVMELGGYVALESETTQGGVK$","Ribokinase","Membrane, Cytoplasm","membrane protein, putative","putative carbohydrate kinase ","Sugar kinase ribokinase family-like","","Sigrell J.A., Cameron A.D., Jones T.A., Mowbray S.L. Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures. Structure 1998. 6(2):183-193. PMID: 9519409","","","

InterPro
IPR011611
Domain

PfkB
PF00294	$\"[61-208]T$	PfkB

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[46-238]T$	no description
PTHR10584	$\"[41-231]T$	SUGAR KINASE RELATED
PTHR10584:SF29	$\"[41-231]T$	RIBOKINASE
tmhmm	$\"[268-290]?$ $\"[367-387]?$ $\"[397-417]?$ $\"[484-504]?$ $\"[518-538]?$ $\"[568-590]?$ $\"[600-622]?$	transmembrane_regions

","BeTs to 11 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","-48% similar to PDB:2FV7 Crystal structure of human ribokinase (E_value = 1.2E_11);","Residues 61 to 208 (E_value = 1.2e-11) place ANA_1337 in the PfkB family which is described as pfkB family carbohydrate kinase.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1340","1430984","1432216","1233","5.98","-8.67","41938","GTGCGCACCTACCTCGATCATGCCGCCTCGTCCCCGGTCCGCCCCGAGGTCGCCCAGCAGGTCGCCCAGGACCTGGCCAGTGGGCTCGGGGGCTGGGCGAATCCGAGTGCGCAGCACACTGCGGGTCGACGGGTGGGGGCGCTGCTGGCACAGGCGCGTGCCCGCCTGGCCAGTGCCCTGGGGGTGGATGCGCATGAGGTGCTGCTGACCTCCGGTGGGACCGAGGCCGATGCCCTGGTGGTCTCAGGGCGGGCGCGAGCGGTGCCGGGCGGGCGGCTGGTCGTCTCTGCAATTGAGCACCCGGCGGTTCTGGACTCGGCGCGCACCGCCGTGGACCAGTTGGGGGCGGGGCTGAGCCTGCTGGAGGTTGACGGCGCCGGGCGGGTCGAGCTCGACTCGGTGGATCGGGCGGTGGCGCCGGCGGGCAGTACCGACCACTCCCCCGCGTCCCTGGTCTCGGTGATGACGGCGAACAATGAGACCGGCGTGGTGCAGGACATGGCGGCGCTGGTGGAGCGCGTGCGGGAGGCCAGTGGCAGCGGGCGTCCCGGCGAGGCCGGGTACGTGCCCGTCCACTCCGACGTGGTTGCGGCGCTGGGGAAGGTTCCGGTGGACTTCCATGGCTGGGGCCTGGATGCGATGAGCTTGAGCGGCCACAAGCTGGGGGCGCCGGTGGGCGTGGGGGCCCTGGTAGTTCGCCGCGACCTGACGTTGACGCCGGCCACGGGCGGGGGCCGTCAGGAGCGGGGGCTCCGCTCGGGTACTCAGGACGTGGTGGCGGCCCGGGCGCTGGCCCTGGCGGTGGAGCTGGCGGTCGCCGAGCGGGAGGAGCAGGAGGCCCGGCTGGCGGCGCTGCGACGTCGGATCCTGGAGGGGGCCGGGGCGCTTCCGGGCGTTCACGCCACGTTGCCGGAAGGTGCCGATCATGTGGCCTCCACGGCGCACCTGTGGTTCGAGGAGGCCGGCGTCGAGGCCCTGCTCATGGCCCTGGACCTGGCGGGGTTTGATGCGTCGGCGGGGTCGGCCTGCCACGCCGGGGTTACCCAGCCCAGTCATGTGCTCCTGGCGATGGGCTTTGAGGAGGGGCCGGCCCGCTCCACGCTGCGCTGCTCCTTGGGCCAGGAGACGAGCCCCGACGACGTCGAGCGCCTACTCGCCGCCCTGCCCGCCGCCCTGGAGGGGGCCAGGCGCGCCTGGAAGGTGACACACAAGACGGCCGAGACGCGCCTGTAG","VRTYLDHAASSPVRPEVAQQVAQDLASGLGGWANPSAQHTAGRRVGALLAQARARLASALGVDAHEVLLTSGGTEADALVVSGRARAVPGGRLVVSAIEHPAVLDSARTAVDQLGAGLSLLEVDGAGRVELDSVDRAVAPAGSTDHSPASLVSVMTANNETGVVQDMAALVERVREASGSGRPGEAGYVPVHSDVVAALGKVPVDFHGWGLDAMSLSGHKLGAPVGVGALVVRRDLTLTPATGGGRQERGLRSGTQDVVAARALALAVELAVAEREEQEARLAALRRRILEGAGALPGVHATLPEGADHVASTAHLWFEEAGVEALLMALDLAGFDASAGSACHAGVTQPSHVLLAMGFEEGPARSTLRCSLGQETSPDDVERLLAALPAALEGARRAWKVTHKTAETRL$","Cysteine desulfurase","Cytoplasm","iron-sulfur cofactor synthesis protein SC2A11.20[similarity]","cysteine desulfurase ","Cysteine desulfurase","","Ouzounis C., Sander C. Homology of the NifS family of proteins to a new class of pyridoxal phosphate-dependent enzymes. FEBS Lett. 1993. 322(2):159-164. PMID: 8482384","","","

InterPro
IPR000192
Family

Aminotransferase, class V
PF00266	$\"[3-384]T$	Aminotran_5
PS00595	$\"[211-230]?$	AA_TRANSFER_CLASS_5

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[3-274]T$	no description

noIPR
unintegrated

unintegrated
PTHR11601	$\"[2-397]T$	CYSTEINE DESULFURYLASE

","BeTs to 18 clades of COG1104COG name: Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1104 is a-----yqvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-45% similar to PDB:1P3W X-ray crystal structure of E. coli IscS (E_value = 4.3E_30);-40% similar to PDB:2HDY Structure of human selenocysteine lyase (E_value = 1.3E_21);-38% similar to PDB:1ECX NIFS-LIKE PROTEIN (E_value = 3.2E_17);-38% similar to PDB:1EG5 NIFS-LIKE PROTEIN (E_value = 3.2E_17);","Residues 3 to 384 (E_value = 6.9e-43) place ANA_1340 in the Aminotran_5 family which is described as Aminotransferase class-V.Residues 24 to 316 (E_value = 0.00098) place ANA_1340 in the Beta_elim_lyase family which is described as Beta-eliminating lyase.","","cofactor synthesis protein SC2A11.20 [similarity] (nifS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1341","1432252","1432617","366","9.13","3.13","13723","ATGCCCACCACCTCGAACAAGATGATCGGCGACTTCAGCGGCAAGCCGGCATCGAACGCCATGTATGCGGCAATCGAGTCCTACGCACTCTCGCTCGGCTCCGTCACCAAGCACCTGACGGCCCAGGTGAGCTTCTCCGTCAACCGGAAGTTCCTGTGGGTCTGGGCCTATGAGAGGACGGGCGACAGCACCCTGTTCCTCAACGTGAGGCTCGATCGTCCCGTGGAGGATCCGCACGTCCACCGCGTCGACCAGGTCAGTGCGAACAGGTGGAACCACCACGTCGTCGTCAAGACGATGGAGGCCGCACAGAGCGACTGGCTCAGGGACCTCATTCGCGCCGGTTACGAGTTCGCCGCCCGGTGA","MPTTSNKMIGDFSGKPASNAMYAAIESYALSLGSVTKHLTAQVSFSVNRKFLWVWAYERTGDSTLFLNVRLDRPVEDPHVHRVDQVSANRWNHHVVVKTMEAAQSDWLRDLIRAGYEFAAR$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1342","1433381","1434709","1329","6.05","-7.31","46208","ATGACATCTCCTCCCTCAGCGCCGTCCATGCCGGGCGCCACGAGGTCCTCCTGGGCTCTCCCGGTTGCCTGGCGGCCACCGACCTGCGGTAGCCTGCCACGGCCGTTGCATCATCTACCCGCCTGTCTGAAGGAGATCCTCGTGCGCGTCCTGGCTGCCCTGTCCGGTGGAGTCGACTCCGCCGTGGCCGCGGCGCGCGCCGTCGGCGCCGGTCATGAGGTCGTGGGCGTCCACATGGCCCTGACCCGCAACCGGGCCCAGACCCGCTCGGGCTCACGCGGCTGCTGCTCCATCGAGGACTCCGCCGACGCCCGCTGGGCCGCCCAGATCCTGGGCATCCCCTTCTACGTGTGGGACCTGTCTGAGGAGTTCGAGGAGCGCGTCGTGTCCGACTTCCTCGACGAGTACCGCGCCGGGCGCACCCCCAACCCCTGTGTGCGCTGCAACGAGCGCGTCAAGTTCGACGCCCTCCTGGAGCGGGCCCTGGCCCTGGGCTTCGACGCCGTCGCCACCGGCCACTACGCGCGACTTAGCGGCGGCGCCTCCTCCGGCCGCCCCGGGGACACCGAGGGCCTCATGCTGCGCCGCGCCGTCGACACCGCCAAGGACCAGTCCTATGTTCTGGCCGTCTCCGGCCGCGAGGGCCTGGCCCGAGCCCTCTTCCCCCTAGGGGACGCGCCCTCCAAGGCTCAGGTGCGCGCCGAGGCCGAGGCCCGGGGCCTGCCGGTGGCCTCCAAGCCGGACTCCTACGACATCTGCTTCGTGGCCGACGGCGACACCCGCGGTTTCCTGACCCGCTCGCTCGGCGCCCACGAGGGCGCCATGGTCTCCCCCGACGGCGAGATCCTGGGCACCCACCAGGGCTACTTCGGCTTCACCGTCGGCCAGCGCAAGGGCCTGGGCCTGTCCCACCCGGCCGAGGACGGCCGCCCCCGCTACGTCATCGAGACGCGCCCGGCCACCAACGAAGTCGTCGTCGGACCCGAGGAGCTGCTCAGCCGCACCGCGGTCGACGGCGACGGACTCGTTCTGCTCGCCGACCCCGAACCTCTCACCACCGGCCCCGACACCGGCACCACCGATTCTGACGACTCCCCCGCCGTCGGCTGGCATGAGGCCAGCGTCCAGGTGCGCGCCCACGGCCGCCCGGTCCCGGCAAGGGTCCGCGTCGATGCAGCACAGGGCCTCCTGCACGCCGAGCTGGCCACGCCCCTGCGTGGCGTGGCCGCCGGTCAGAGCCTGGTTATCTACGGCGGCGGCGACGGCGACCAAGTCCTGGCCCAAGCGACCGTCGCGTCCGCACCGGCCTCCAGCCACCCCGTCGCCTGA","MTSPPSAPSMPGATRSSWALPVAWRPPTCGSLPRPLHHLPACLKEILVRVLAALSGGVDSAVAAARAVGAGHEVVGVHMALTRNRAQTRSGSRGCCSIEDSADARWAAQILGIPFYVWDLSEEFEERVVSDFLDEYRAGRTPNPCVRCNERVKFDALLERALALGFDAVATGHYARLSGGASSGRPGDTEGLMLRRAVDTAKDQSYVLAVSGREGLARALFPLGDAPSKAQVRAEAEARGLPVASKPDSYDICFVADGDTRGFLTRSLGAHEGAMVSPDGEILGTHQGYFGFTVGQRKGLGLSHPAEDGRPRYVIETRPATNEVVVGPEELLSRTAVDGDGLVLLADPEPLTTGPDTGTTDSDDSPAVGWHEASVQVRAHGRPVPARVRVDAAQGLLHAELATPLRGVAAGQSLVIYGGGDGDQVLAQATVASAPASSHPVA$","tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase","Cytoplasm","tRNA(5-methylaminomethyl-2-thiouridylate)-methyltransferase","tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase ","tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase","","","","","

InterPro
IPR004506
Family

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
PTHR11933	$\"[63-426]T$	TRNA (5-METHYLAMINOMETHYL-2-THIOURIDYLATE)-METHYLTRANSFERASE
PF03054	$\"[48-431]T$	tRNA_Me_trans
TIGR00420	$\"[48-431]T$	trmU: tRNA (5-methylaminomethyl-2-thiouridy

","BeTs to 19 clades of COG0482COG name: Predicted tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the PP-loop ATPase domainFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0482 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB004506 (tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase) with a combined E-value of 3e-68. IPB004506A 49-79 IPB004506B 139-154 IPB004506C 165-174 IPB004506D 196-235 IPB004506E 243-258 IPB004506F 284-300 IPB004506G 407-417","","","-57% similar to PDB:2HMA The Crystal Structure of tRNA (5-Methylaminomethyl-2-Thiouridylate)-Methyltransferase TrmU from Streptococcus pneumoniae (E_value = 7.0E_42);-47% similar to PDB:2DER Cocrystal structure of an RNA sulfuration enzyme MnmA and tRNA-Glu in the initial tRNA binding state (E_value = 2.5E_39);-47% similar to PDB:2DET Cocrystal structure of an RNA sulfuration enzyme MnmA and tRNA-Glu in the pre-reaction state (E_value = 2.5E_39);-47% similar to PDB:2DEU Cocrystal structure of an RNA sulfuration enzyme MnmA and tRNA-Glu in the adenylated intermediate state (E_value = 2.5E_39);-46% similar to PDB:1J0A Crystal Structure Analysis of the ACC deaminase homologue (E_value = 2.5E_39);","Residues 48 to 431 (E_value = 1.4e-136) place ANA_1342 in the tRNA_Me_trans family which is described as tRNA methyl transferase.","","(5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1343","1435734","1434754","981","4.47","-20.37","32233","ATGCTCGATGCCCCCCTGCTCGTCCTCGTCGACCTTGAGACCACCGAGACCACCCCCACCGGCCCCAGCCTGGAGCTGCTTACCGCTGCCCGGGAGCTGACCGGCGGCGACGTCGTCGCCCTGGCCCTCCAGCCTCTGGGGCAGGCCGCCTCAGCGGCCCTGGCCGGCGCCGGAGCCACCCGCCTGCTGTCCGCCGACCTGGGTGAGGCCGCCCACCTGCCCGCCACCGCGGCCGACGCCGTCGTGGCGGCCGTCGGCGCCGTCCAGCCCGCCGCGGTCCTGGTCGTCTCCGACTACCGCGGCAAGGAGCTGGCCGGACGGGCCGCCGTTGTGCTCGGCTCGGCCTGCGTCTCCGACGTCACCGCCCTGGAGGCCGCCGGCACCGAGCTGCGTGCCTCCAAGCTGGTCCTGTCCGGCTCTTGGTCCACCACCGCCGGCGTCGCCTCGGGCGGCTCCGCACCGATCATCGCCGTGCGCCCCGGGATCGCCGAGGTCACCGCGACCGAGGGCGCGCCCCTGACGGCCGAGCCCCTCGAGGTTCCCGTCAGCGCCGAGGCCGCCGCTGTGCGCCTCGTCTCGCGCGAGGCCACCTCCGTGGCCTCCGGCCCCGCCCTGAGCGAGGCGCGCACCGTTGTCGTGGGTGGCCGCGGCGTGGACGGCGACTTCGACCTGGTCCGCTCCCTGGCCCAGCCGCTCGACGCTGCCGTCGGGGCCACCCGCGTGGCCTGCGACGAGGGCTGGATCGAGCGCAGCGCCCAGATCGGTCAGACCGGTGAGGCCATCTCCCCGCGCCTGTACATCGGCCTGGGCGTCTCCGGCGCTGTCCACCACACCAGCGGCATTCAGGGGGCCGGCACCGTCGTCGCCATCTGCGACGACTCCGAGGCTCCGATCTTCGAGATGGCCGACTTCGGCGTCGTCGGCGACGTCACCGAGGTCGTGCCCCAGCTCGTCGAGGAGCTCGCCAAGCTGCGCGGCTGA","MLDAPLLVLVDLETTETTPTGPSLELLTAARELTGGDVVALALQPLGQAASAALAGAGATRLLSADLGEAAHLPATAADAVVAAVGAVQPAAVLVVSDYRGKELAGRAAVVLGSACVSDVTALEAAGTELRASKLVLSGSWSTTAGVASGGSAPIIAVRPGIAEVTATEGAPLTAEPLEVPVSAEAAAVRLVSREATSVASGPALSEARTVVVGGRGVDGDFDLVRSLAQPLDAAVGATRVACDEGWIERSAQIGQTGEAISPRLYIGLGVSGAVHHTSGIQGAGTVVAICDDSEAPIFEMADFGVVGDVTEVVPQLVEELAKLRG$","Electron transfer flavoprotein, alpha subunit","Cytoplasm","flavoprotein reductase","electron transfer flavoprotein; alpha subunit","electron transfer flavoprotein, alpha subunit","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[8-191]T$	no description

InterPro
IPR014731
Domain

Electron transfer flavoprotein, alpha subunit, C-terminal
PF00766	$\"[202-285]T$	ETF_alpha

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1220	$\"[198-324]T$	no description
PTHR10909	$\"[8-322]T$	ELECTRON TRANSPORT OXIDOREDUCTASE
PTHR10909:SF4	$\"[8-322]T$	ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT

","BeTs to 13 clades of COG2025COG name: Electron transfer flavoprotein alpha-subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2025 is ao-p-zy-vdr-b-ef--sn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB001308 (Electron transfer flavoprotein, alpha subunit) with a combined E-value of 1.4e-38. IPB001308A 208-252 IPB001308B 258-298 IPB001308C 299-318***** IPB014731 (Electron transfer flavoprotein, alpha subunit, C-terminal) with a combined E-value of 9.3e-32. IPB014731B 201-224 IPB014731C 253-304","","","-51% similar to PDB:1EFV THREE-DIMENSIONAL STRUCTURE OF HUMAN ELECTRON TRANSFER FLAVOPROTEIN TO 2.1 A RESOLUTION (E_value = 1.8E_25);-51% similar to PDB:1T9G Structure of the human MCAD:ETF complex (E_value = 1.8E_25);-51% similar to PDB:2A1T Structure of the human MCAD:ETF E165betaA complex (E_value = 1.8E_25);-51% similar to PDB:2A1U Crystal structure of the human ETF E165betaA mutant (E_value = 1.8E_25);-48% similar to PDB:1EFP ELECTRON TRANSFER FLAVOPROTEIN (ETF) FROM PARACOCCUS DENITRIFICANS (E_value = 6.5E_23);","Residues 202 to 285 (E_value = 1.8e-29) place ANA_1343 in the ETF_alpha family which is described as Electron transfer flavoprotein FAD-binding domain.","","reductase (ETFLS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1344","1436626","1435832","795","4.62","-18.63","27897","GTGGCGAGATGCCGCTGTTATGGCAACCTTGAGCCCATGAGAATCGTGGTCTGCATCAAGCACGTTCCTGACGTCCAGTCCGAGCGTCGCATTGAGGACGGTCGCCTCGTGCGCGGCGAGGAGGACGTCCTCAACGAGCTCGACGAGAATGCCGTCGAGGCCGCTGTCTGTCTGGCCGAGGAGGCCGACGGCGAGGTCATCGCCCTGACCATGGGACCCGAAGACGCTGAGGACGGGGTGCGCCGCGCCCTGCAGATGGGGGCCGACTCCGGGGTCGTCGTGGCCGATGACGACCTGGCCGGCGCCGACGTCGTCACCACCGCCCGGGTCCTGGCCGCCGCCATCGAGCGCATCGGCAAGGTCGACCTGGTCGTCACCGGAATGGCCTCCCTGGACTCCATGACCTCTATGCTGCCCGGCGCCCTGGCCGCCGCCCTGCACCTTCCGGCCGTCACGCTGGCCAACCGGCTCGAGGTCGACGGCGGCGCCGTAACCGTTACCCGCACCGTGGGCACCGTCCGCGAGGTCCTCAGTGCGCCGCTGCCCGCGCTCGTCAGCGTCACCGACCAGGCCAACGAGCCCCGCTACCCCAACTTCGCCGCCATGCGCGCCGCGAAGAAGAAGCCCATCGACTTCTGGGATGTTTCCGAGCTCGGCCTTCAGATCGCCGAGCCGGCCGTCGCCGTCGTCGACGACGAGGCCCGACCCGCCCGTGAGGCCGGCATCATCCGCACCGACGCCGGAGAGGCGGGCCGTGAGCTCGCCGCCTGGCTCGTGGAGAACAAGCTCGTCTGA","VARCRCYGNLEPMRIVVCIKHVPDVQSERRIEDGRLVRGEEDVLNELDENAVEAAVCLAEEADGEVIALTMGPEDAEDGVRRALQMGADSGVVVADDDLAGADVVTTARVLAAAIERIGKVDLVVTGMASLDSMTSMLPGALAAALHLPAVTLANRLEVDGGAVTVTRTVGTVREVLSAPLPALVSVTDQANEPRYPNFAAMRAAKKKPIDFWDVSELGLQIAEPAVAVVDDEARPAREAGIIRTDAGEAGRELAAWLVENKLV$","Electron transfer flavoprotein, beta-subunit","Cytoplasm","flavoprotein reductase nonH","K03521 electron transfer flavoprotein beta subunit","electron transfer flavoprotein beta-subunit","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR000049
Domain

Electron transfer flavoprotein, beta-subunit, core
PD003528	$\"[175-218]T$	Q82N22_STRAW_Q82N22;

InterPro
IPR012255
Family

Electron transfer flavoprotein, beta subunit
PIRSF000090	$\"[13-264]T$	Electron transfer flavoprotein, beta subunit
PTHR21294	$\"[13-264]T$	ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[13-260]T$	no description

InterPro
IPR014730
Domain

Electron transfer flavoprotein, alpha/beta-subunit, N-terminal
PF01012	$\"[39-222]T$	ETF

","BeTs to 13 clades of COG2086COG name: Electron transfer flavoprotein beta-subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2086 is ao-p-zy-vdr-b-ef--sn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB000049 (Electron transfer flavoprotein beta-subunit) with a combined E-value of 9.9e-57. IPB000049A 13-24 IPB000049B 44-60 IPB000049C 65-90 IPB000049D 122-157 IPB000049E 167-210","","","No significant hits to the PDB database (E-value < E-10).","Residues 34 to 222 (E_value = 3.1e-31) place ANA_1344 in the ETF family which is described as Electron transfer flavoprotein domain.","","reductase nonH (etfB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1345","1436803","1439187","2385","5.48","-30.85","86394","ATGCCAGAGCCCGCTCCAGCACCGCGCGCCGAGCTGCCAGCAGCTCCCGACCACGGCCTGGGCGTCGCTCTCAACGGAGACGGCGCGGACTTCGCTGTCCACGCCCCGCATGCCACTGCCGTGGACCTGTGCCTGCTGACCCTGGGTGCCGACGGCGCCGTGGTGGAGGAGACCCGGATTGGGATGCACGGGCCCTCGCGGGGCCTGTGGAGCGCGCACGTCCCCGGCGTCGGCGTCGGTCAGCGCTACGGCTACCGCGCCCACGGCCCCTGGAACCCGCACGAGGGCCTGCTCTACAACCCCCGCAAGCTGCTGCTGGACCCCTACGCCCGGGCCCTGGACGGCCGCGTGGACCTGGGGCCGGCCGTCTACGCCCACGAGGTCACCGATGATCTGGTCCCTGCGGCCGAGCCGTGGAGGCCCTCACGCCTGGACTCGGCCGGCAGCACCGCCGTCGGCGTGGTCACCGGTGACACCTTCCCGGTGGTTCCGGGGCCGCGTGTGCCCCGCGAGCGCGCCGTCATCTACGAGGCCCATGTCAAGGGCCTGACCTACCAGCTGCCCGGGGTGCCCGAGGAGCTGCGCGGCACCTACGCGGGGCTGGCCCACTCGGTGACGGTTGAGCACCTCAAGGCCCTGGGGATCACCACGATCGAGCTGCTGCCGATCCACGCCTCCGTGAGCGAGCCCTTCCTGACCAAGCGGGGCCTGAGCAACTACTGGGGCTACTCCACGCTGAGCTACTTCGCACCCGAGCCCTCCTACGCCACAGCCGCGGCGCGTGCGGCCGGCCCGCAGGCGGTCCTGGACGAGGTGCGCGGCATGGTCTCCATGCTCCACGAGGCCGGCCTGGAGGTCGTGCTCGACGTCGTCTACAACCACACCTGCGAGGGCGGTGTCGACGGCCCCTCCTTGAGCCTGCGCGGCCTGGACAACCTGGACTACTACCTGCACGCCCCCTACCTGCCGGCGCAGTACATGGATGTCACCGGCACCGGCAACACAGTGGACTTCCGGGCCACGGGTGCGATCCGCCTGGTTCTGGACTCGCTGCGCTACTGGGTCGCTGAGGTCGGGGTCGACGGCTTCCGATTCGACCTGGCCACCACCCTGGGGCGCCACGCCGCGGAGTTCTCGCCACGTCACCCGCTGCTCACGGCCATCGCCACGGACCCGGTCCTCAGCACCGTCAAGCTCATCAGCGAGCCCTGGGACGTGGGACCCGGCGGCTGGCGCACCGGCCAGTTCCCCGAGCCCTTCCAGGACTGGAACGACCACTTCCGCGACACCACGCGCTCCTTCTGGCTACATGACGCCTCGGAGATCTCCAAGGGCCGTCTGGGCTCGGACCTGCGCGACCTGGCCACGCGCCTGTCGGGCAGCGCGGACCTGTTCAGCCACGGAGAGTTCCCCGGCGGCCGCGGCCCGCTGGGCTCGGTCAACTTCGTGGCAGCGCACGACGGCTTCACCCTGCGCGACCTGGTGGTCTACGACCACAAGCACAATCTGGCCAACAAGGAGGACAACCGCGACGGCAACTCCAACAACCGCTCCTGGAACCACGGTTTCGAGGGGGACGTCGTCGAGGGCATCAACGGCGGGCCGATCGAGGTGCTGCGCCGCCGGTCGATGCGCAACCTGCTGGCCACCGTGCTGCTGAGCGCCGGGACCCCCATGCTGGTGGCCGGCGACGAGATGGGACGCACCCAGCAGGGCAACAACAACTGCTACTGCCAGGACTCCGTGCTCTCCTGGGTGGACTGGAACCTGGAGGTCTGGCAGCGAGATCTGGTCGCCACGACGCGCTTCCTCATCCACCTGCGCCACACCCACCCGGTGGCACGTCCCTCGCGCTTCGCGACCGGACAGGTCCTGGACGGTGACACGATCGCGGACCTGGCCTGGTATCGGGCGGATGCCGCACCGATGGACGGGGACTCCTGGCACGACCCGCACACTCGCGTGGTCCAGATGCTGCGCTCGGGCCGCCTCTGGAACGACGACGACATGCTCGTGGTCATCAACGGCGCCTTGGACCAGGTCGACGTCGTCCTGCCCGAGGGGCGCGGCACCGACTGGCACCTGGCCTGGGACTCGACCTGGGCGGTCCCCCAGCCTCATACCGCGCCCTTCTCCCAGGCACGGCGCGTAAGCCGAAGCCCCCAGGACACTCCGGCTGACGTCATCATCGAGACCGACGACGCCGGCGAGGTCAAGGACGTCAAGACCGTGGCCAACGGCTCCGAGGTTCATGCCGCCGAGAGTCTCACGGACTGCCACCAGGACCGGCCGGGCGACACGACGATGCTGGAGGCGCTGTCCCTGCGGGTCTACTTCTCCGGCGAGCCGCTGGAGACCCTGATCCCGGGCGCCGAGGCGCACTGA","MPEPAPAPRAELPAAPDHGLGVALNGDGADFAVHAPHATAVDLCLLTLGADGAVVEETRIGMHGPSRGLWSAHVPGVGVGQRYGYRAHGPWNPHEGLLYNPRKLLLDPYARALDGRVDLGPAVYAHEVTDDLVPAAEPWRPSRLDSAGSTAVGVVTGDTFPVVPGPRVPRERAVIYEAHVKGLTYQLPGVPEELRGTYAGLAHSVTVEHLKALGITTIELLPIHASVSEPFLTKRGLSNYWGYSTLSYFAPEPSYATAAARAAGPQAVLDEVRGMVSMLHEAGLEVVLDVVYNHTCEGGVDGPSLSLRGLDNLDYYLHAPYLPAQYMDVTGTGNTVDFRATGAIRLVLDSLRYWVAEVGVDGFRFDLATTLGRHAAEFSPRHPLLTAIATDPVLSTVKLISEPWDVGPGGWRTGQFPEPFQDWNDHFRDTTRSFWLHDASEISKGRLGSDLRDLATRLSGSADLFSHGEFPGGRGPLGSVNFVAAHDGFTLRDLVVYDHKHNLANKEDNRDGNSNNRSWNHGFEGDVVEGINGGPIEVLRRRSMRNLLATVLLSAGTPMLVAGDEMGRTQQGNNNCYCQDSVLSWVDWNLEVWQRDLVATTRFLIHLRHTHPVARPSRFATGQVLDGDTIADLAWYRADAAPMDGDSWHDPHTRVVQMLRSGRLWNDDDMLVVINGALDQVDVVLPEGRGTDWHLAWDSTWAVPQPHTAPFSQARRVSRSPQDTPADVIIETDDAGEVKDVKTVANGSEVHAAESLTDCHQDRPGDTTMLEALSLRVYFSGEPLETLIPGAEAH$","Glycogen debranching enzyme GlgX","Cytoplasm, Extracellular","glycogen debranching enzyme","putative glycosyl hydrolase ","glycogen debranching enzyme GlgX","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR004193
Domain

Glycoside hydrolase, family 13, N-terminal
PF02922	$\"[19-110]T$	Isoamylase_N

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[191-368]T$	Alpha-amylase

InterPro
IPR011837
Family

Glycogen debranching enzyme GlgX
TIGR02100	$\"[14-726]T$	glgX_debranch: glycogen debranching enzyme

InterPro
IPR013779
Family

Isoamylase-type debranching enzyme
PIRSF003068	$\"[14-728]T$	Isoamylase-type debranching enzyme

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[166-618]T$	no description

InterPro
IPR013783
Domain

Immunoglobulin-like fold
G3DSA:2.60.40.10	$\"[14-156]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[166-680]T$	AMYLASE
PTHR10357:SF25	$\"[166-680]T$	GLYCOGEN DEBRANCHING ENZYME

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[50-59]T$	AA_TRNA_LIGASE_I

InterPro
IPR002305
Domain

Aminoacyl-tRNA synthetase, class Ib
PF00579	$\"[38-324]T$	tRNA-synt_1b

InterPro
IPR002306
Family

Tryptophanyl-tRNA synthetase, class Ib
PR01039	$\"[54-70]T$ $\"[105-124]T$ $\"[182-203]T$ $\"[238-248]T$	TRNASYNTHTRP
PTHR10055	$\"[47-366]T$	TRYPTOPHANYL-TRNA SYNTHETASE
TIGR00233	$\"[40-368]T$	trpS: tryptophanyl-tRNA synthetase

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[41-263]T$	no description

","BeTs to 24 clades of COG0180COG name: Tryptophanyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0180 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002305 (Aminoacyl-tRNA synthetase, class Ib) with a combined E-value of 6.5e-23. IPB002305A 47-61 IPB002305B 106-122 IPB002305C 184-205 IPB002305D 234-247","","","-55% similar to PDB:1YI8 Crystal structure of tryptophanyl trRNA synthetase II from Deinococcus radiodurans in complex with L-Trp (E_value = 4.9E_54);-55% similar to PDB:1YIA Crystal structure of tryptophanyl tRNA synthetase II from Deinococcus radiodurans in complex with 5-Hydroxy tryptophan. (E_value = 4.9E_54);-55% similar to PDB:1YID Crystal structure of tryptophanyl tRNA synthetase II from Deinococcus radiodurans in complex with ATP. (E_value = 4.9E_54);-56% similar to PDB:2A4M Structure of Trprs II bound to ATP (E_value = 9.3E_53);-53% similar to PDB:2G36 Crystal structure of Tryptophanyl-tRNA synthetase (EC 6.1.1.2) (Tryptophan-tRNA ligase)(TrpRS) (tm0492) from THERMOTOGA MARITIMA at 2.50 A resolution (E_value = 4.5E_47);","Residues 38 to 324 (E_value = 3.8e-56) place ANA_1346 in the tRNA-synt_1b family which is described as tRNA synthetases class I (W and Y).","","synthetase (trpS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1347","1440468","1442663","2196","5.51","-20.91","80186","GTGACTCAGATCGTTTCTCACCGTAGTCTTGGCCCTGTGACTCCGAACACGACGCCGAAGGCCGGCAAGAAGCAGTCCACCCGTCCCTCCAAGTCCTCTGCCGCTCCCACCGACGCACCCGCTCAGGGCACCGGGACGCAGACCGCGCCGTCGGGGTCGTCCGCGGCCTGCGCGGCACCGCAGCCGGCCCCGTTCTCGTTGATCGGCCGGATCCCGGTCACCGAGGTCTTCCCCGTCGTCGAGGACGGGCGCTGGCCGGCCAAGGCCGTCATCGGCGAGGTCATTCCGATCCGCGCCACCGTCTTCCGCGAGGGGCACGACCGCTTCGGCGCCACCGCGGTCCTGGTGCGTCCTGACGGCAGCGACGGCCCCAGCGCCCGCATGCACGACATCGCCCCGGGGCTGGACCGTTATGAGGCCTCCGTGGCGCCCGACGCCCCCGGGGACTGGCGCTTCCGCGTCGAGGGATGGTCGGACCCGTACGCCACCTGGAGCCACGACGCCGGTATCAAGGTGCCCGCCGGCATCGACGTCGAGCTCATGCTGGAGGAGGGCGCCCGGGTCCTGGACCGGGCGGCGGCCCTTGAGGGGCGCGACGAGGAGGGAGTCAAGGCCCTCAACAACGCCGTGTGGATCATGCGCGACCCCTCCAACCCCGTGGCCGACCGCCTGGCTGCGGGCCTGTCGGACTCGGTCCAGGCAGCCCTGGAGCGCCTGCCGCTGCGCGACCACGTCTCGCCCTCCGCCGAGTACCCGCTCCAGGTGGACCGCGAGCGCGCCCTGACCGGCTCCTGGTATGAGATCTTCCCGCGCTCGCTGGGCTCGGGAGCCGGCGAGGACGGCTCCTGGCACTCGGGGACACTGCGCAGCGCGACCGAGCGGCTGGACCGCATCGCGGCCATGGGCTTCGACGTCCTCTACCTCACGCCCATCTCCCCCATCGGCCTGACCAACCGCAAGGGCCGCAACAACACCCTGACGGCGCGTCCCGGCGACCCCGGCTCCCCTTACGGCATCGGCTCCCCCGACGGCGGCCACGACGCCATCCACCCCGACCTGGGCACCTTCGAGGACTTCGACGCCCTGGTGGCGCGCTCGCGCGAGCTGGGCATGGAGGTGGCCCTGGACCTGGCGCTCCAGTGCTCGCCGGACCACCCGTGGGTGGCCGAGCACCCCGAGTGGTTCACGGTCCTGGCCGACGGCTCGATCGCCTACGCCGAGAACCCGCCCAAGAAGTACCAGGACATCTACCCGCTCAACTTCGACAACGACCCCGAGGGCATCTACCAGGCGATCCTGGAGGTCGTGCGCACCTGGATCGCGCACGGGGTGACGATCTTCCGGGTGGATAACCCCCACACCAAGCCCCTGCCCTTCTGGCAGCGGCTCATCGCCGAGATCCACGCCGAGTCCCCCGACGTGCTGTTCCTGGCCGAGGCCTTCACCCGCCCCGCCATGATGCGCACCCTGGGCATGATCGGCTTCCACCAGTCCTACACCTACTTCGCCTGGCGCAACACCAAGGACGAGCTCATCGAGTACATGATGGAGCTCAGCAAGGACACCGCCCACCTGCTGCGCCCGGCATTCTGGCCCACGACGCACGACATCCTGACCCCCTTCATGACCAACGGGAAGGTGCCGGCCTTCAAGCTGCGCGCCGTCCTGGCGGCCACGCTCTCACCGACCTGGGGCATCTACTCGGGCTACGAGCTGGCCGAGTCCACACCGCGCCCGGGCTATGAGGAGCAGATCGACAACGAGAAGTACGAGTACAAGCCGCGCGACTTCGCCGCCGCTCGCCGCAACGGCATCGAGGACCTGCTCACGCGCCTCAACGCCGCCCGCACCGCCCACCCGGCACTGCGCCAGCTGCGGGACATCTACTTCCACCCCACGAGCGATGACCAGATCCTCGCCTACTCCAAGCGGGTGGACGCCTTCCACAGCCCCACGGGCAGGGACGACGTCATCCTCACGGTGGTCAACCTCGACCCGCACGGGGCGAGGGCCGGCGAGGTCTACCTCAACCTGGAGGCCCTGGGCCTGCCGGGCTGGGTGGACGCCTCTCGCCCGGTGGTGCGGGTGACCGACGCGCTCACCGGAGACTCCTACGAGTGGTCGGGGCAGAACTATGTGCGCCTCGACCCCTTCGCCGGGCAGGTCGCCCACGTCTTCTCCGTGGAGCCGCTGTGA","VTQIVSHRSLGPVTPNTTPKAGKKQSTRPSKSSAAPTDAPAQGTGTQTAPSGSSAACAAPQPAPFSLIGRIPVTEVFPVVEDGRWPAKAVIGEVIPIRATVFREGHDRFGATAVLVRPDGSDGPSARMHDIAPGLDRYEASVAPDAPGDWRFRVEGWSDPYATWSHDAGIKVPAGIDVELMLEEGARVLDRAAALEGRDEEGVKALNNAVWIMRDPSNPVADRLAAGLSDSVQAALERLPLRDHVSPSAEYPLQVDRERALTGSWYEIFPRSLGSGAGEDGSWHSGTLRSATERLDRIAAMGFDVLYLTPISPIGLTNRKGRNNTLTARPGDPGSPYGIGSPDGGHDAIHPDLGTFEDFDALVARSRELGMEVALDLALQCSPDHPWVAEHPEWFTVLADGSIAYAENPPKKYQDIYPLNFDNDPEGIYQAILEVVRTWIAHGVTIFRVDNPHTKPLPFWQRLIAEIHAESPDVLFLAEAFTRPAMMRTLGMIGFHQSYTYFAWRNTKDELIEYMMELSKDTAHLLRPAFWPTTHDILTPFMTNGKVPAFKLRAVLAATLSPTWGIYSGYELAESTPRPGYEEQIDNEKYEYKPRDFAAARRNGIEDLLTRLNAARTAHPALRQLRDIYFHPTSDDQILAYSKRVDAFHSPTGRDDVILTVVNLDPHGARAGEVYLNLEALGLPGWVDASRPVVRVTDALTGDSYEWSGQNYVRLDPFAGQVAHVFSVEPL$","Alpha amylase","Cytoplasm, Extracellular","pep1","alpha amylase; catalytic region","alpha amylase, catalytic region","","Schleicher M., Andre E., Hartmann H., Noegel A.A. Actin-binding proteins are conserved from slime molds to man. Dev. Genet. 1988. 9(4):521-530. PMID: 3243032Matsudaira P. Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 1991. 16(3):87-92. PMID: 2058002Dubreuil R.R. Structure and evolution of the actin crosslinking proteins. Bioessays 1991. 13(5):219-226. PMID: 1892474","","","

InterPro
IPR001589
Domain

Actin-binding, actinin-type
PS00019	$\"[497-506]?$	ACTININ_1

InterPro
IPR002345
Domain

Lipocalin
PS00213	$\"[256-268]?$	LIPOCALIN

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[267-606]T$	Alpha-amylase

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[263-619]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[262-314]T$ $\"[346-510]T$ $\"[529-678]T$	AMYLASE
PTHR10357:SF11	$\"[262-314]T$ $\"[346-510]T$ $\"[529-678]T$	ALPHA-AMYLASE

","BeTs to 9 clades of COG0366COG name: GlycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0366 is ---p--y-vdrlbcefg----j----Number of proteins in this genome belonging to this COG is 7","***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 3.3e-12. IPB006589A 293-310 IPB006589B 353-381 IPB006589C 443-454","","","No significant hits to the PDB database (E-value < E-10).","Residues 267 to 606 (E_value = 6.8e-05) place ANA_1347 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1348","1442660","1444597","1938","4.77","-41.80","71436","GTGAGCACCGATCCAATGAGTACTGCCCAGGTGCCCCCCGGCAGCGAGGCTCCAACCGCGGCGCCGGGTGGAGCCTTCGGCCCGCCCGCGGCGGGCGTTTCCGTCACGGCGCCCGTGGCGGCCCAGATGCCGGCGCTCCCCACCCCCAGCAGCGGGATCCCCATGCCGCTGGCGGTGGCCCCGCCGATCCCCGGGGTGCCGGCCCTGCCGGCCCAGGCCCGCCCCGGCCTGAGCCCGGACCCCGAGTGGTTCCGCACGGCGGTCTTCTACGAGGCACTGCTGCGTTCCTTCGCCGACTCCGACGGCGACGGCGTCGGAGACCTGCGCGGGCTCATCTCCCGCCTGGACTACCTGGCGTGGCTGGGCGTGGACTGCGTGTGGATCCCGCCGTTCTACCCCTCGCCCGTGCGCGACGGCGGCTACGACATCTCCGACTACACGGCCATCGACCCGCGCTACGGGACGATGGAGGACTTCCGCGAGCTGGTCCACCAGGCCCACCAGCGCGGAATCCGCATCATCATCGACATGGTCGTCAACCACACCTCAGACGCCCACCCCTGGTTCCAGGCCTCCCGCTCGGACCCCGAGGGGCCTTACGGGGACTTCTACGTGTGGGCCGACGACGACTCCGGTTACGACGACGCCCGCATCATCTTCGTGGACACCGAGGAGTCCAACTGGGCCTACGACGTCGAGCGCGGCCAGTTCTACTGGCACCGCTTCTTCTCCCACCAGCCCGACCTCAACTACCGCAACCCGGCGGTCATCGAGGCCATCCACGACGTCATCCGCTTCTGGGCGCGCACCGGGGTGGACGGTTTCCGCCTCGACGCCATCCCCTATCTGACCGAGTCGGAGGGCACCAACTGCGAGAATCTGGCCGGCACCCACGAGATCATCGCCGGGATCCGTCAGATGCTCGACCGGGAGTTCCCCGGCACCATCACGCTGGCCGAGGCCAACCAGTGGCCCGAGGACGTCGTGGAGTACTTCGGCACCGAGGAGGCCCCCGAGTGCACCATGTGCTTCCACTTCCCGGTCATGCCGCGCATCTTCTACGCGCTGCGGCAGGGCTCGGCCGAGGCCATCCGCTGGGTGCTGGAGAAGACCCCTGATATTCCCGCCCACGGGCAGTGGGGAACCTTCCTGCGCAATCACGACGAGCTGACCCTGGAGATGGTCACCGACGCCGAGCGCGACCAGATGTACGCCTGGTACGCCCCCGAGGAGCGCATGCGCGCCAACATCGGGATCCGACGCCGCCTGGCCCCACTCCTGGACGCCTCCCGCGCCGAGGTGGAGCTGGCCTACGCCCTGCTCCTGTCGCTGCCGGGCAGCCCCTGCCTCTACTACGGCGACGAGATCGGCATGGGCGAGAACATCTGGCTGGAGGACCGCGACGCCGTGCGCACCCCCATGCAGTGGGACGACTCCCCCAACATGGGCTTCTCCTCCGTGGTGGATCCCGGCGCCCTGACGCTTCCACTCATCCAGGCCCCCGGCTACGCGCACCTGACGGTGGCCACAGAGATGGCCCGACCCGACTCGCTGCTGCACTTCACCCGGCGGATCCTGCACCTGCGCCGCGCCCATCCCGTCCTGGGACGCGGGAGCTTCCTCCTGCGCTCCACCAGCGACGACGCCATCCTGGCGCACACGCGCTGCGACGAGTCGTCAATGGAGGGAGCGGAGACCCTCCTGTGCGTCGCCAACCTCTCGGCCACCCCCCGATCGGTGACGATCGAGGTTCCCGAGCTGGCGGGCAGGGGCACCACGGACCTGTTCGGCGGCTGCGCCTTCCCGCCCGTCGACGACCGCGGCCGCCTCACCCTGACGCTGGGAGCGCGCGGATACTACTGGCTGTCCGTTGACCGGACTGAGCCCGACAACGCCCCCCAGGGCGACCACGACAACCACCCGACCGAGGAAGTCTGA","VSTDPMSTAQVPPGSEAPTAAPGGAFGPPAAGVSVTAPVAAQMPALPTPSSGIPMPLAVAPPIPGVPALPAQARPGLSPDPEWFRTAVFYEALLRSFADSDGDGVGDLRGLISRLDYLAWLGVDCVWIPPFYPSPVRDGGYDISDYTAIDPRYGTMEDFRELVHQAHQRGIRIIIDMVVNHTSDAHPWFQASRSDPEGPYGDFYVWADDDSGYDDARIIFVDTEESNWAYDVERGQFYWHRFFSHQPDLNYRNPAVIEAIHDVIRFWARTGVDGFRLDAIPYLTESEGTNCENLAGTHEIIAGIRQMLDREFPGTITLAEANQWPEDVVEYFGTEEAPECTMCFHFPVMPRIFYALRQGSAEAIRWVLEKTPDIPAHGQWGTFLRNHDELTLEMVTDAERDQMYAWYAPEERMRANIGIRRRLAPLLDASRAEVELAYALLLSLPGSPCLYYGDEIGMGENIWLEDRDAVRTPMQWDDSPNMGFSSVVDPGALTLPLIQAPGYAHLTVATEMARPDSLLHFTRRILHLRRAHPVLGRGSFLLRSTSDDAILAHTRCDESSMEGAETLLCVANLSATPRSVTIEVPELAGRGTTDLFGGCAFPPVDDRGRLTLTLGARGYYWLSVDRTEPDNAPQGDHDNHPTEEV$","Trehalose synthase","Cytoplasm","Trehalose synthase (Maltosealpha-D-glucosyltransferase)","trehalose synthase","trehalose synthase","","Jarling M., Cauvet T., Grundmeier M., Kuhnert K., Pape H. Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase. J. Basic Microbiol. 2004. 44(5):360-373. PMID: 15378530","","","

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[91-505]T$	Alpha-amylase

InterPro
IPR006589
Domain

Glycosyl hydrolase, family 13, subfamily, catalytic region
SM00642	$\"[91-486]T$	Aamy

InterPro
IPR012810
Domain

Trehalose synthase/alpha-amylase, N-terminal
TIGR02456	$\"[82-625]T$	treS_nterm: trehalose synthase

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[79-538]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[79-622]T$	AMYLASE
PTHR10357:SF11	$\"[79-622]T$	ALPHA-AMYLASE

","BeTs to 10 clades of COG0366COG name: GlycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0366 is ---p--y-vdrlbcefg----j----Number of proteins in this genome belonging to this COG is 7","***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 8.2e-39. IPB006589A 113-130 IPB006589B 153-181 IPB006589C 271-282 IPB006589D 382-391***** IPB004185 (Glycoside hydrolase, family 13, N-terminal Ig-like domain) with a combined E-value of 1.5e-38. IPB004185B 102-135 IPB004185C 140-171 IPB004185D 172-211 IPB004185H 433-478***** IPB004193 (Glycoside hydrolase, family 13, N-terminal) with a combined E-value of 6.6e-11. IPB004193C 132-156 IPB004193D 167-181 IPB004193E 265-278***** IPB006048 (Alpha amylase, C-terminal all-beta domain) with a combined E-value of 9.3e-10. IPB006048B 154-182 IPB006048C 268-283***** IPB006046 (Alpha-amylase signature) with a combined E-value of 1.6e-08. IPB006046B 170-181 IPB006046C 272-283","","","-46% similar to PDB:1ZJA Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 (triclinic form) (E_value = 6.1E_69);-46% similar to PDB:1ZJB Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 (monoclinic form) (E_value = 6.1E_69);-47% similar to PDB:1UOK CRYSTAL STRUCTURE OF B. CEREUS OLIGO-1,6-GLUCOSIDASE (E_value = 2.2E_66);-46% similar to PDB:1M53 CRYSTAL STRUCTURE OF ISOMALTULOSE SYNTHASE (PALI) FROM KLEBSIELLA SP. LX3 (E_value = 9.1E_65);-45% similar to PDB:1WZA Crystal structure of alpha-amylase from H.orenii (E_value = 1.0E_55);","Residues 91 to 505 (E_value = 2.2e-80) place ANA_1348 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.","","synthase (Maltose alpha-D-glucosyltransferase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1350","1444786","1446204","1419","5.01","-24.45","50692","ATGATCGCCTCCTGGGAGCCGGAGGAGGGCGTGCGCGACCTCGTCATCGCCGCACTGCGGGGCAACCAGGCCGAGACCGGTCACCGCGACGGCATGGTGCTGCTGCACGTGCCGGTGGTCCTGGAGGCCGCCGAGGCGCTCGACTCCTTCGCCACCCCCGGTGAGGCCCCCGGCAACCACGGACTGCTGCTGACCACTGCCTCCGACGGGGCACCTGCGCAGGTGGCGCTCGTCGACGGCGCCCACCACCCGGCCTTCTGGCGGGCCTGGGCCCTGAGCGCCCTGGAGGCGGGCACCGTCCTGGGCGAGGCCGGAGCCCTGGCCATCGCCCAGCGGGCGCCGAGGCTGCGGGTGACCACCGGGGAGCAGTCCAACACCTCCGTCATCCTGCCGGCCCCCTCCGACCCCGCCGAGGCCCTCGGGGAGGAGGACGCCGCCACCGGTGACCTCATCGTCAAGCTCCTGCGGGTCCTGGAGCACGGACGCAACCCCGACGTGGAGCTGTCGGTAGCCCTTGCCCGCAGCGGCTGGGACCGGGTGCGCACACCGGTGGCCTGGTCCACCATGACCTGGACGCGCATGGGCGGCTGCGGCCAGCCCGCCCTGGAGGAGTCCACCGACTCGGCCGTGGCCTGCAGCTTCGTCCCCCGCGCCGACGACGGCTTCGAGCTGTTCTGCTCACTGGCCTCCACCGACGACGTCGACGGGCCGGTGCGGGCCCAGGCCGTGGAGCTGGCTCGGGATCTGGGACGTACGACCGCGCAGATGCACCACCACCTGGCCGCCTCCCTGGGCACGAGCCGACCGCCAACGCCGACCGAGCTCGCTGCCTCCCTGCGCAAGCGCGCCCGGTGGGCGCTGGAGGAGGTGCCCGAGCTCTCCGGGCACATCCGAGCCCTGGAGCTCAAGGTAGAGCAGACCATGGAGCGGCTTGAGGCGCTCCAGTCCCTGGAGCCGGCCACCCGCATCCACGGCGACTACCACCTCGGGCAAGTGCTTCACGAGATCGGCGGCCAGCAGCGCTGGTATGTCCTGGACTTCGAGGGCGAGCCCCTGCGCCCCCTGGCCCAGCGCTCCGACCCCGACCTGCCGGCCCGGGACGTAGCCGGCATGCTGCGCTCCTTCGACTACGCCGCCGCCGTCGGCAAGGCCCCCCACGCCGACTGGCTCCCCGCCGTGCGCTCCGCCTTCGAGGAGGGCTACCGCCTGGGGCGCCAGGAGACCGGCTCGCTCACCCCGTCGCCGGCGGCATCCGGCGACCAGGAGCAGGCCGAGGCCTCGTACCAGACTGTCCTGACCTGCCTGGAGCTCGACAAGGCCCTCTACGAGGCCGTCTACGAGGCCCGCAACCGCCCCGACTGGCTGGGCATCCCCATGGCGGGGATCGAGTCAGTCCTGTCCAAGCACACGGAGGGCTGA","MIASWEPEEGVRDLVIAALRGNQAETGHRDGMVLLHVPVVLEAAEALDSFATPGEAPGNHGLLLTTASDGAPAQVALVDGAHHPAFWRAWALSALEAGTVLGEAGALAIAQRAPRLRVTTGEQSNTSVILPAPSDPAEALGEEDAATGDLIVKLLRVLEHGRNPDVELSVALARSGWDRVRTPVAWSTMTWTRMGGCGQPALEESTDSAVACSFVPRADDGFELFCSLASTDDVDGPVRAQAVELARDLGRTTAQMHHHLAASLGTSRPPTPTELAASLRKRARWALEEVPELSGHIRALELKVEQTMERLEALQSLEPATRIHGDYHLGQVLHEIGGQQRWYVLDFEGEPLRPLAQRSDPDLPARDVAGMLRSFDYAAAVGKAPHADWLPAVRSAFEEGYRLGRQETGSLTPSPAASGDQEQAEASYQTVLTCLELDKALYEAVYEARNRPDWLGIPMAGIESVLSKHTEG$","Uncharacterized protein probably involved in trehalose biosynthesis","Cytoplasm","pep2","hypothetical protein","Uncharacterized protein probably involved in trehalose biosynthesis-like","","","","","No hits reported.","BeTs to 3 clades of COG3281COG name: Uncharacterized protein, probably involved in trehalose biosynthesisFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG3281 is -----z----r----f----------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1351","1446293","1448503","2211","4.98","-42.21","82323","ATGAGCGCCAACACACCTGAGAAGGACCTCGCCCCTGTCCCTGTGGACCCCTGGATCCTGGCCGACGTCGCCTACGCGCGCTACCACGACCCTCACGAGGTCCTGGGCGCCCACGTCGGCGAGAACGGAGTCACCATCCGCACCGTCCGTCACCTGGCCGACGACGTCGTCGTCGTCACCAAGGACGGCTCCCACCCGGCCACCCATGAGCAGGACGGCGTGTGGGTGGCGGTCCTGCCCGGCCAGGAGATCCCCGACTACCGCATCAAGGTCACCTACGGCGACGAGACCACCACCGTCGACGACCCCTACCGCTACATGCCGACCCTGGGTGAGATGGACACCTACCTCATCTCCGAGGGCCGCCACGAGGAGCTGTGGGAGGTCCTGGGCGCCCACGTCAAGCGCTACGACGGCCCCATGGGTGAGGTCGAGGGAACCGCCTTCGCCGTGTGGGCCCCCAACTCCCGCGCGGTGCGCGTCGTCGGCGACTTCAACTACTGGGACGGCACCGCCACCGCCATGCGCTCCCTGGGCTCATCGGGAGTGTGGGAGCTGTTCGTGCCCGGCGTCGGGGTCGGTGCGCGATACAAGTTCGAGCTCTGCTTCGCCGACGGCTCCTGGCACCAGAAGGCCGACCCGATGGCCCGCGCCACCGAGGTCCCCCCGGCCACCGCCTCGGTGGTCACCGACCAGTTCCACCAGTGGGAGGACCAGGAGTGGATGGCCAAGCGCGCCACCACCGACCCCCACAGCGGGCCGATGAGCATCTACGAGGTCCACGTCGGCTCGTGGCGCCAGGGACTGGGCTTCCGCGGCCTGGCTAAGGAGCTGGTCCCCTACGTCAAGGAGGCCGGCTTCACCCACGTGGAGTTCCTGCCGGTGGCCGAGCACCCCTTCGGCGGCTCCTGGGGCTACCAGGTCACCAGCTACTACGCGCCCACCTCGCGCTTCGGCACCCCGGACGACTTCCGCTACCTGGTGGACCAGCTCCACCAGGCCGGCATCGGCGTCATTCTGGACTGGGTGCCGGCCCACTTCCCCAAGGACGAGTGGGCCCTGGCCCGCTTCGACGGCACCCCCCTGTACGAGGACCCCGACCCGCAGCGCGGCGAGCACCCCGACTGGGGCACCTACGTGTTCAACTTCGGACGCAACGAGGTGCGCAACTTCCTGGTCGCCAACGCCCTGTACTGGCTCCAGGAGTTCCACGCCGACGGTCTGCGCGTCGACGCCGTGGCCTCCATGCTCTACCTGGACTACTCGCGCCAGGACGGCCAGTGGCATCCCAACCAGTTCGGCGGCCGCGAGAACCTGGAGGCCATCAGCTTCCTGCAGGAGGCCACCGCCACCGCCTACCGCAAGAACCCCGGCATCATCATGGCCGCCGAGGAGTCCACGGCGTGGCCGGGCGTCACCGCCCCCACCGAGTACGGCGGCCTGGGCTTCGGACTGAAGTGGAACATGGGGTGGATGAACGACACCCTGCGCTACCTGGCGGAGGACCCCGTCAACCGCCGCTACCACCACGGAGAGCTGACCTTCTCCCTCGTCTACGCCTTCTCCGAGCAGTTCATCCTGCCGCTGAGCCACGATGAGGTCGTCCACGGCAAGGGCTCCCTGCTGTCCAAGATGCCCGGCGACCCCTGGCAGGAGCTGGCGGGCCTGCGCGCCCTGTACGCCTACCAGTGGTCCCACCCCGGCAAGCAGCTGCTGTTCATGGGCCAGGAGTTCGGTCAGGGAACCGAGTGGAACGCCGATACCTCCCTGGACTGGTGGATCCTGGACGATCCCGGCCACCAGGGGCTGCTCGCCCTGGTCAGCGACCTCAACCGCCTCTACCTGAGCTCGCCGGCCCTGTGGTCGGAGGACTTCTCCCACCGCGGATTCGAGTGGATCGAGGCCGGCGACGGCGACCACAACGTCCTGTCCTACCTGCGCAAGGGGACCGACGCCGACGGGCGGGCCGACCTCATGGTCTGCATCATCAACTTCGCCGGCACCCCGCATGAGGGCTACCGGGTGGGCCTGCCCTTCGCCGGGGACTGGGAGGAGGTCCTCAACACCGACTCCGAGGACTACGGCGGCTCCGGTGTGGGCAACCTGGGCCGGGTCGAGGCCGAGGACCTGCCCTGGAACGGGCGCCCGGCCTCAGTGCGTCTGCGGGTCCCCCCGATGGGAGCGGTCTTCCTGCGTCCGGCTCAGGACTGA","MSANTPEKDLAPVPVDPWILADVAYARYHDPHEVLGAHVGENGVTIRTVRHLADDVVVVTKDGSHPATHEQDGVWVAVLPGQEIPDYRIKVTYGDETTTVDDPYRYMPTLGEMDTYLISEGRHEELWEVLGAHVKRYDGPMGEVEGTAFAVWAPNSRAVRVVGDFNYWDGTATAMRSLGSSGVWELFVPGVGVGARYKFELCFADGSWHQKADPMARATEVPPATASVVTDQFHQWEDQEWMAKRATTDPHSGPMSIYEVHVGSWRQGLGFRGLAKELVPYVKEAGFTHVEFLPVAEHPFGGSWGYQVTSYYAPTSRFGTPDDFRYLVDQLHQAGIGVILDWVPAHFPKDEWALARFDGTPLYEDPDPQRGEHPDWGTYVFNFGRNEVRNFLVANALYWLQEFHADGLRVDAVASMLYLDYSRQDGQWHPNQFGGRENLEAISFLQEATATAYRKNPGIIMAAEESTAWPGVTAPTEYGGLGFGLKWNMGWMNDTLRYLAEDPVNRRYHHGELTFSLVYAFSEQFILPLSHDEVVHGKGSLLSKMPGDPWQELAGLRALYAYQWSHPGKQLLFMGQEFGQGTEWNADTSLDWWILDDPGHQGLLALVSDLNRLYLSSPALWSEDFSHRGFEWIEAGDGDHNVLSYLRKGTDADGRADLMVCIINFAGTPHEGYRVGLPFAGDWEEVLNTDSEDYGGSGVGNLGRVEAEDLPWNGRPASVRLRVPPMGAVFLRPAQD$","1,4-alpha-glucan branching enzyme","Cytoplasm","1,4-alpha-glucan branching enzyme","1;4-alpha-glucan branching enzyme ","1,4-alpha-glucan branching enzyme","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR004193
Domain

Glycoside hydrolase, family 13, N-terminal
PF02922	$\"[34-105]T$ $\"[129-216]T$	Isoamylase_N

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[259-344]T$	Alpha-amylase

InterPro
IPR006048
Domain

Alpha-amylase, C-terminal all beta
PF02806	$\"[632-734]T$	Alpha-amylase_C

InterPro
IPR006407
Domain

1,4-alpha-glucan branching enzyme, core region
TIGR01515	$\"[114-732]T$	branching_enzym: 1,4-alpha-glucan branching

InterPro
IPR013780
Domain

Glycosyl hydrolase, family 13, all-beta
G3DSA:2.60.40.1180	$\"[627-736]T$	no description

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[236-616]T$	no description

InterPro
IPR013782
Family

1,4-alpha-glucan branching enzyme
PIRSF000463	$\"[22-736]T$	1,4-alpha-glucan branching enzyme

InterPro
IPR013783
Domain

Immunoglobulin-like fold
G3DSA:2.60.40.10	$\"[117-232]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[213-731]T$	AMYLASE
PTHR10357:SF13	$\"[213-731]T$	1,4-ALPHA-GLUCAN BRANCHING ENZYME

","BeTs to 11 clades of COG0296COG name: 1,4-alpha-glucan branching enzymeFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0296 is ------yq-dr-bcefgh---j-i--Number of proteins in this genome belonging to this COG is 2","***** IPB004193 (Glycoside hydrolase, family 13, N-terminal) with a combined E-value of 1.1e-48. IPB004193A 149-157 IPB004193B 253-268 IPB004193C 297-321 IPB004193D 332-346 IPB004193E 398-411 IPB004193F 480-489***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 8.8e-19. IPB006589A 277-294 IPB006589B 318-346 IPB006589C 404-415","","","-42% similar to PDB:2BHU CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE (E_value = 2.5E_29);-42% similar to PDB:2BHY CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH TREHALOSE (E_value = 2.5E_29);-42% similar to PDB:2BHZ CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX WITH MALTOSE (E_value = 2.5E_29);-42% similar to PDB:2BXY IS RADIATION DAMAGE DEPENDENT ON THE DOSE-RATE USED DURING MACROMOLECULAR CRYSTALLOGRAPHY DATA COLLECTION (E_value = 2.5E_29);-42% similar to PDB:2BXZ IS RADIATION DAMAGE DEPENDENT ON THE DOSE-RATE USED DURING MACROMOLECULAR CRYSTALLOGRAPHY DATA COLLECTION (E_value = 2.5E_29);","Residues 34 to 105 (E_value = 105) place ANA_1351 in the Isoamylase_N family which is described as Isoamylase N-terminal domain.Residues 129 to 216 (E_value = 2.6e-27) place ANA_1351 in the Isoamylase_N family which is described as Isoamylase N-terminal domain.Residues 259 to 607 (E_value = 3.3e-07) place ANA_1351 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.Residues 632 to 734 (E_value = 2.2e-39) place ANA_1351 in the Alpha-amylase_C family which is described as Alpha amylase, C-terminal all-beta domain.","","branching enzyme (glgB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1352","1448670","1451144","2475","5.16","-30.74","93372","ATGTTCCCTTGCGCGCTCCGGTCGGCCCGGCCCCGTCGATGTACGATGTTTCAGTCCGCTGCAAAACTCTTGCAGTCGGCGACCACGATGCCTGACAAGGGAAGAAGAATGACACAGAAGCTGGTCACGAGCGCCCCCGCGCAGGTGCGCGCCGTATCCGGTCGACCCGAGACCGCAGCCACCCTCATGGAGGTCTGGCAGGGCCTGTCCGCCGCCGTCGTCGACACCATCGCGGACGACTGGTACGCCACCGAGCAGAAGTACAGCGCAGGACGCCAGGAGCACTACTTCTCCGCCGAGTTCCTCATGGGCCGCGCCCTGCTCAACAACCTCTCCAACCTGGGGATGGTCGACGAGGCACGCGAGGCCGTCGGTTCCTTCGGCGTCAACCTCTCCGACGTCCTGGAGCAGGAGCCCGACGCCGCCCTGGGCAACGGTGGTCTGGGCCGCCTGGCCGCCTGCTTCCTCGACTCCTGCGCCACCCTCGACCTGCCGGTCAACGGCTTCGGCATCCTCTACCGCTATGGGCTGTTCAAGCAGCTCTTCGAGGACGGCTTCCAGACCGAGCACCCCGACCCTTGGATGGAGGAGGGCTACCCCTTCGTCATCCGCCACGAGGAGGCCCAGCGCCTGGTGCACTACCAGGACATGACCGTGCGCGCCATCCCCTACGACATGCCCATCACCGGCTACGGCACCAAGAACGTGGGGACCCTGCGCCTGTGGAAGGCCGAGCCACTCGAGGAGTTCGACTACGACGCCTTCAACTCCCAGCGCTTCACCGAGGCGATCGTCGAGCGCGAGCGCACCTCGGACATCTCCCGTGTCCTCTACCCCAACGACACCACCTACGAGGGCAAGGTCCTGCGGGTGCGCCAGCAGTACTTCTTCTGCTCCGCCTCCCTGCAGCAGATCGTTGAGAACTACGTCAGCCACCACGGTGAGGACCTGACCGGCTTCGCCGACTACAACGCCATCCAGCTCAACGACACCCACCCGGTGCTCGCCATCCCCGAGCTGATGCGCATCCTCCTGGACGAGCACCACCTGGGCTGGGAGGAGGCCTGGGAGGTGGTCACCAAGACCTTCGCCTACACCAACCACACGGTGCTGGCCGAGGCCCTGGAGACCTGGGAGATCTCCATCTTCGACCGCCTCTTCCCGCGCATCACCGAGATTGTTCGCGAGATCGACCGCCGCTTCCGCATGGAGATGGCCGAGCGCGGCCTGGAGCAGGGCACCATCGACTACATGGCCCCCATTTCCGGGGACAAGGTGCGCATGGCCTGGATCGCCTGCTACGCCTCCTACTCCATCAACGGCGTCGCCGCGCTGCACACAGAGATCATCAAGCGCGAGACCCTGGGCGAATGGCACGCCATCTGGCCCGAGCGCTTCAACAACAAGACCAACGGCGTCACCCCGCGCCGCTGGCTGCGCCAGTGCAACCCGCGCCTGTCGGCGCTCCTGGACGAGGTCACCGGCTCGGACACCTGGGTCAAGGACCTCTCCGTTCTGGCCGAGCACACCGACTCCGTGGACGAGTCCGTCTACGACCGCCTCGCGGAGATCAAGCACGCCAACAAGGTGGACTTCGCCGCCTGGATCGCCCAGCGCGAGGGGATCGAGATCGACCCGGAGGCCATCTTCGACGTCCAGATCAAGCGTCTCCACGAGTACAAGCGCCAGCTGCTCAACGCCATCTACATCCTGGACCTCTACTTCCGCATGAAGCAGGACCCGAGCCTGCAGGTCCCCAAGCGGGTCTTCATCTTCGGCGCCAAGGCCGCTCCCGGGTACATCCGGGCCAAGGCCATCATCAAGCTCATCAACGCCATCGCCGACCTGGTCAACAACGACCCCGTGGTCTCCCAGACCATCAAGGTCGTCTTCGTCCACAACTACAACGTCTCCCCGGCCGAGCACATCATCCCGGCCGCCGACGTCTCTGAGCAGATCTCGATGGCCGGCAAGGAGGCCTCGGGGACCTCCAACATGAAGTTCATGATGAACGGCGCCCTGACCCTGGGCACCCTCGACGGCGCCAACGTGGAGATCCTGGAGGCGGTTGGTGACGACAACGCCTACATCTTCGGCGCCACGGAGGACGAGCTGCCCGCCCTGCGTGAGAGCTACGACCCCGTGTGGCACTACGAGAACGTCCCCGGTCTCAAGCGCGTCCTGGACGCCTTCACCGACGGCACCCTGGACGACAACGGCTCGGGCTGGTTCGCCGACCTGCGCCGCAGCCTGCTGGAGGCCTCCTACGAGCCGGCCGACGTCTACTACGTCCTGGGCGACTTCGCCTCCTACCGCGAGACCAAGGACGCCATGGCGGCCGACTACGCCGACACCCGCGCCTGGCAGCGCAAGGCCTGGGTGAACATCACCCGCTCGGGCCGTTTCTCCTCCGACCGCACCATCAGCGACTACGCCCGCGAGGTCTGGAAGATCGACCCCGAGCCCATCGCCTGA","MFPCALRSARPRRCTMFQSAAKLLQSATTMPDKGRRMTQKLVTSAPAQVRAVSGRPETAATLMEVWQGLSAAVVDTIADDWYATEQKYSAGRQEHYFSAEFLMGRALLNNLSNLGMVDEAREAVGSFGVNLSDVLEQEPDAALGNGGLGRLAACFLDSCATLDLPVNGFGILYRYGLFKQLFEDGFQTEHPDPWMEEGYPFVIRHEEAQRLVHYQDMTVRAIPYDMPITGYGTKNVGTLRLWKAEPLEEFDYDAFNSQRFTEAIVERERTSDISRVLYPNDTTYEGKVLRVRQQYFFCSASLQQIVENYVSHHGEDLTGFADYNAIQLNDTHPVLAIPELMRILLDEHHLGWEEAWEVVTKTFAYTNHTVLAEALETWEISIFDRLFPRITEIVREIDRRFRMEMAERGLEQGTIDYMAPISGDKVRMAWIACYASYSINGVAALHTEIIKRETLGEWHAIWPERFNNKTNGVTPRRWLRQCNPRLSALLDEVTGSDTWVKDLSVLAEHTDSVDESVYDRLAEIKHANKVDFAAWIAQREGIEIDPEAIFDVQIKRLHEYKRQLLNAIYILDLYFRMKQDPSLQVPKRVFIFGAKAAPGYIRAKAIIKLINAIADLVNNDPVVSQTIKVVFVHNYNVSPAEHIIPAADVSEQISMAGKEASGTSNMKFMMNGALTLGTLDGANVEILEAVGDDNAYIFGATEDELPALRESYDPVWHYENVPGLKRVLDAFTDGTLDDNGSGWFADLRRSLLEASYEPADVYYVLGDFASYRETKDAMAADYADTRAWQRKAWVNITRSGRFSSDRTISDYAREVWKIDPEPIA$","Glucan phosphorylase","Cytoplasm","Glucan phosphorylase","glycogen phosphorylase ","glycogen/starch/alpha-glucan phosphorylase","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR000811
Family

Glycosyl transferase, family 35
PIRSF000460	$\"[39-823]T$	Glucan phosphorylase
PTHR11468	$\"[69-820]T$	GLYCOGEN PHOSPHORYLASE
PF00343	$\"[123-820]T$	Phosphorylase
PS00102	$\"[659-671]T$	PHOSPHORYLASE

InterPro
IPR011833
Family

Glycogen/starch/alpha-glucan phosphorylase
TIGR02093	$\"[38-818]T$	P_ylase: glycogen/starch/alpha-glucan phosp

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2000	$\"[38-502]T$	no description

","BeTs to 13 clades of COG0058COG name: Glucan phosphorylaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0058 is --m-k-yq-drlbcefgh---j-i--Number of proteins in this genome belonging to this COG is 1","***** IPB000811 (Glycosyl transferase, family 35) with a combined E-value of 3.6e-252. IPB000811A 75-113 IPB000811B 138-177 IPB000811C 180-218 IPB000811E 255-309 IPB000811F 352-398 IPB000811G 426-478 IPB000811H 544-578 IPB000811I 587-628 IPB000811J 644-698 IPB000811K 782-820","","","-77% similar to PDB:2C4M STARCH PHOSPHORYLASE: STRUCTURAL STUDIES EXPLAIN OXYANION-DEPENDENT KINETIC STABILITY AND REGULATORY CONTROL. (E_value = );-59% similar to PDB:1L5V Crystal Structure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate (E_value = 3.8E_172);-59% similar to PDB:1L5W Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose (E_value = 3.8E_172);-59% similar to PDB:1L6I Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose (E_value = 3.8E_172);-59% similar to PDB:2ASV X-Ray studies on protein complexes: Enzymatic catalysis in Crystals of E. coli Maltodextrin Phosphorylase (MalP) (E_value = 3.8E_172);","Residues 123 to 820 (E_value = 0) place ANA_1352 in the Phosphorylase family which is described as Carbohydrate phosphorylase.","","phosphorylase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1353","1452193","1451246","948","4.52","-22.78","32354","ATGAGCATGTTCGGCGCCGTCGACCTATCCAGTCTCGCCCCCGCCACCAAGCCGACCGGCTCTACCAGTGGGGCGAGCCCCACTACCGGGGACCGCCCCACCGGAGCTGCCGGTTCCGGTCTGCCGGTGCCGCTCGTCGTTGACGTCGACGCCTCCAACCTGCGCGACGTCGCCGAGGTCTCCACCCAGGTCCCTGTCATCGTCGTCCTGCACAGCCCGCGCAGCCAGGCCAGTGCCGACCTCGCCACCGTCCTGGAGCAGCTCGCCGATCAGTACGCCGGCCGCTTCCAGGTGGCGCGCGTCAACGTGGATACGGCCCCGGAGGTCGCTCAGGCCCTCCAGGCTCAGGCCGTCCCCACTGTGGTGGCCCTCATCGCGGGCCAGCCGGTGCCGATGTTCCAGGGGGCGGTGCCCCAGGAGCAGCTGCACTCCGTCATCGACCAGCTGCTGGAGGTGGCCGCCGCCAACGGTGTCAACGGCACCATCGCCGTCGACGGCGCAGCCGGTGCCGGCACTGCTGAGGCCGAGCCCGAGGAGACCGAGGTCGAGCGGGCCGCCCGCGAGGCCATCGAGGCCGGCGACTTCGCCGCCGCTGAGGAGGTCTACACCCACGCCATCGCCCAGAACCCGGGCGACGACGACCTCAAGGTGGCCCGCAACCAGGTGCGCCTCATGGCCCGGCTGGACGGCCAGGACCCCCACGAGCTCCTCACAGCCGCCGACGCCGCGCCCACGGATCTGGCCGCGGCCCTGGCCGGTGCTGACGCCGCCCTGGCCCTGGGGGATGTCAACGCGGCCCTCGGACGCGCCCTGGAGGCTGTACGCACCCACGCGGGGGAGGAGCGGGAGGAGGCCCGGCTGCGGCTGCTCGAGCTCTTCGAGGTCATCGGCTCCACCTCCCCGGAGGTCGCCCAGGCCCGCCGCCGACTGGCCACCATGCTTTACTGA","MSMFGAVDLSSLAPATKPTGSTSGASPTTGDRPTGAAGSGLPVPLVVDVDASNLRDVAEVSTQVPVIVVLHSPRSQASADLATVLEQLADQYAGRFQVARVNVDTAPEVAQALQAQAVPTVVALIAGQPVPMFQGAVPQEQLHSVIDQLLEVAAANGVNGTIAVDGAAGAGTAEAEPEETEVERAAREAIEAGDFAAAEEVYTHAIAQNPGDDDLKVARNQVRLMARLDGQDPHELLTAADAAPTDLAAALAGADAALALGDVNAALGRALEAVRTHAGEEREEARLRLLELFEVIGSTSPEVAQARRRLATMLY$","Thioredoxin","Cytoplasm, Extracellular","Thioredoxin domain-containing protein","K05838 putative thioredoxin","Thioredoxin domain","","Holmgren A. Thioredoxin. Annu. Rev. Biochem. 1985. 54:237-271. PMID: 3896121Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 1989. 264(24):13963-13966. PMID: 2668278Holmgren A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 1995. 3(3):239-243. PMID: 7788289Martin J.L. Thioredoxin--a fold for all reasons. Structure 1995. 3(3):245-250. PMID: 7788290Saarinen M., Gleason F.K., Eklund H. Crystal structure of thioredoxin-2 from Anabaena. Structure 1995. 3(10):1097-1108. PMID: 8590004","","","

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[43-151]T$	no description

InterPro
IPR013766
Domain

Thioredoxin domain
PF00085	$\"[81-149]T$	Thioredoxin

InterPro
IPR015467
Domain

Thioredoxin family
PTHR10438	$\"[84-150]T$	THIOREDOXIN-RELATED

noIPR
unintegrated

unintegrated
PTHR10438:SF13	$\"[84-150]T$	THIOREDOXIN M(MITOCHONDRIAL)-TYPE

","BeTs to 6 clades of COG3118COG name: Thioredoxin domain-containing proteinFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG3118 is ----------r---efghs--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 64 to 149 (E_value = 0.00015) place ANA_1353 in the Thioredoxin family which is described as Thioredoxin.","","domain-containing protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1354","1453405","1452359","1047","5.98","-3.09","35950","ATGTCCACCCGTCGAGCCTTTCTGAGCGCAGGCAGTGCCTCCGCCATCGCCCTGAGCCTGGCCGCCTGCTCGCGGTCTCAGCCCACGACCGCTGAGACCGTGGCCTCCGGTACGCCGATCGCCGAACCCGTCCTCAACGACAAGCAGCTCGAAGAGATTCTCCAGCGCGTCCAGACCGGCCTGGCAGCGGCGGACAAGGAGAAGAACGCGGACAAGCTCAAAGAGGTCATGTCCGGTCCGGCAGCGCGGATCCGCGCTGCCGAGTACGCCACCGCCTCCGCCAGCGGAAACGGCTCCGTCATTCACACCATGAACACCAAGATCCAGGGCGGGGGAGTGGGGCAGACCGTCGGCTTCCCCCGTAACGCAGCCGTCGCCTCGGAGAGCGACAAGAGCGTCTCGATCATCTCCCTGGAGCAGGGCTCGGCCCGGGACCAGTTCAAGGTGTGGGCCTGGGTGCAGGGGTTCGCCGCGCAGGCGAGCATTCCCGTGCTGACCAAGCAGTCGGCCCAGCACGCCAAGCAGGTGACGGCCGATTCCACCGGGCTGGTCGTCACCCCCAAGGCGGCTCTCGACGCCTACGTCGATGCGCTCAACCATCCTGACGGCGAGAACGGCAAGGCATTCCCTGACGACAACCTGCGTCAGAAGGTCCAGGACGCCCGAAAGACCGACCTGAGCAACTTGGGTGAGGTCACCGTCACGGCGGTCCCCGGTCAGGACGGGTTCCAGGGCCTCCAGCTGGAGGAGGGGGACGGCGGGGCGCTGGTCTTCACCACCCTGACCTACACGGTGGTCTACAAGCGCACCGTTGACGGCTCCGACCTCACCCTGCAGGGTGACATTGCCGCCCACATGGGTGGCAACCAGAAGATCGTCGGCACCGTCACCGCCACCTACGACTCCATGGTCGCCTTCTCCATCCCCAAGGAGGGAAGCGGCGGGAAGGTGACCGTTCTGGGAGCCGAGACGGCGCTGATGAAGGTGGACCGGGACGACTCCAAGACGCCGGCCCCCGCGGCATCGGCCTCGGCCAAGCCGTCCTGA","MSTRRAFLSAGSASAIALSLAACSRSQPTTAETVASGTPIAEPVLNDKQLEEILQRVQTGLAAADKEKNADKLKEVMSGPAARIRAAEYATASASGNGSVIHTMNTKIQGGGVGQTVGFPRNAAVASESDKSVSIISLEQGSARDQFKVWAWVQGFAAQASIPVLTKQSAQHAKQVTADSTGLVVTPKAALDAYVDALNHPDGENGKAFPDDNLRQKVQDARKTDLSNLGEVTVTAVPGQDGFQGLQLEEGDGGALVFTTLTYTVVYKRTVDGSDLTLQGDIAAHMGGNQKIVGTVTATYDSMVAFSIPKEGSGGKVTVLGAETALMKVDRDDSKTPAPAASASAKPS$","Hypothetical protein","Extracellular, Periplasm","lipoprotein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-26]?$	signal-peptide

noIPR
unintegrated

unintegrated
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[222-244]?$	transmembrane_regions

InterPro
IPR007793
Family

DivIVA
PF05103	$\"[199-268]T$	DivIVA

","BeTs to 3 clades of COG1390COG name: Archaeal/vacuolar-type H+-ATPase subunit EFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1390 is aompkzy--d-------------it-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 199 to 268 (E_value = 9.1e-06) place ANA_1359 in the DivIVA family which is described as DivIVA protein.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1360","1457277","1457768","492","7.29","0.21","18068","GTGACTGCCGACGACGCCGCCCAGTCCGAGACCGAGTCGACCAGCACCCGTGGTTCTGGTGACCGCGACTGGGCGGCGTCGCGTCGTCGTGCGGCCACACAGCGGGCCCGCATGCTTCAGGAGCGCCAGGAGGCCGAGCACGCTCGGGCTGCCCGCATCGTGGGGCTCTTCCTCGAGGTCGCCCGCGAAGAGGGCCTCCAGGACGTTCCTCTGCGGGTGCGTGGCTACGCGGGCGGCAGCGCCCGCACCCCGCTGCGCGGCTGGTACCTGAGGGCCGACGAGACGGTCGGCATCGACACGCAGGGGCGCTACTACGTCCTGTCGATGCCGCTGAGCCTGGCGCAGCGCCTACGCGGGGTCAGGCCCGAGAGCCAGCCAGTGCCGATGACCATCGGTGAGGGCGGACGCGACGGCGATATCGTGCCGCTGCGCTTCGCGCTGGACCGCCTGCTGCCGGGCTGGGAGGAGCGCTCCCCCGAGCCGCTCGTGTGA","VTADDAAQSETESTSTRGSGDRDWAASRRRAATQRARMLQERQEAEHARAARIVGLFLEVAREEGLQDVPLRVRGYAGGSARTPLRGWYLRADETVGIDTQGRYYVLSMPLSLAQRLRGVRPESQPVPMTIGEGGRDGDIVPLRFALDRLLPGWEERSPEPLV$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1361","1458094","1457804","291","10.71","9.27","10886","ATGGCACGTCGCAGATCCAAGCGCCCCTACGGGCAGGGGCACATCCCCTTGAGCATGGACCGTCTCGCCTCCGTGCCACGCACCCAGACCGGCCCCGGCGGCGCCGACTTCACCGTGCGACACCTGCGCGGCGGTGACAAGCCCTACACCTGTCCCGGTTGCCACCGCGTCATCCCGGCCGGCACCGCGCACGTGGTGGCCTGGAGCAACGAGTCCCTCTTCGGGGCGGACCGGGGCCTTGAGGAGCGCCGTCACTGGCACACCTCATGCTGGGAGCGCCGCCTCTGGTAG","MARRRSKRPYGQGHIPLSMDRLASVPRTQTGPGGADFTVRHLRGGDKPYTCPGCHRVIPAGTAHVVAWSNESLFGADRGLEERRHWHTSCWERRLW$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PD066851	$\"[47-94]T$	Q6NHS5_CORDI_Q6NHS5;

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[77-279]T$	BPD_transp_1
PS50928	$\"[77-269]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[80-102]?$ $\"[107-129]?$ $\"[148-168]?$ $\"[189-211]?$ $\"[217-237]?$ $\"[252-270]?$	transmembrane_regions

","BeTs to 15 clades of COG0395COG name: Sugar permeasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0395 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 77 to 279 (E_value = 2.8e-18) place ANA_1362 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter BH3847 (permease)","","1","","","","","","","","","","","Tue Aug 14 15:12:02 2007","","Tue Aug 14 14:53:17 2007","","","Tue Aug 14 14:53:17 2007","","","","Tue Aug 14 14:53:17 2007","Tue Aug 14 14:53:17 2007","","","","","yes","","" "ANA_1363","1459999","1459070","930","9.98","7.90","34035","GTGAGCACCAAGAGCGCCCCCGCGCGGCGCCGTCGAGCGAGCTGGAGGCAGTGGGGCCCCGGCCTCCTGCTCATCTCGCCCTCGATCATCCTCGTCGGCGTCTTCGTCTACGGGATGATCGGGATCAACATCAACACCTCCCTGCTGGACATGCACACCGCCGGCCAGGTCTCCGGACGCAGGGGGACCACCGTCGTCGGGCTGAGCAACTTCACGGCCCTGTTCGGTAACCCGGACTTCCGCCACTCCTTCATCAACCTCATCCTGTTCACCGTCACCTTCCTGGCCGGCACCCTCGTGGTCGGCTTCCTGTGGGCCTGGCTCCTGGACCGCCCCATCAAGGGGGAGGGGATCTTCCGCTCCATCTTCCTGTTCCCCATGGCCGTGTCCTTCGTGGCCTCGGGTGTGGTGTGGCGGTGGCTGCTGAACTCCGCGCAGGGCGAGAGCGCCTCGGGGCTCAACCGCCTGTTCGAGATGACCGGCCTGCGGTTCTTGGAGAACTCGTGGACCCAGAACACCACCTGGGGGATTCTGGCCATCGCGCTGCCGGCCGTGTGGCAGCTGGCCGGATACGTCATGGCGCTCTTCCTGGCCGGCTTCCGTGGCATTCCCGACGACCTGCGTGAGGCCGCCCGGGTCGACGGCGCCAGCGAGTGGCAGCTCTACAAGTCGATCATCTTCCCCCAGCTGACCCCGATCGCCCTGAGCGCCGTCATCATCATCGGGCACATGTCCCTAAAGTCCTTCGACCTCATCATGTCGATCACGGACCAGCGCACCTACTCCACCAAGGTCCCGGCCATCGACATGTTCAACTTCATGACCGACAACGACTACTCCAACGCCGCCGCCGTCGGCACGATCCTGCTGGTCCTGGTCGCCGTCGCCGTCATCCCCTACCTCATCCACGACGCCAAGGGCAGGAGGTGA","VSTKSAPARRRRASWRQWGPGLLLISPSIILVGVFVYGMIGININTSLLDMHTAGQVSGRRGTTVVGLSNFTALFGNPDFRHSFINLILFTVTFLAGTLVVGFLWAWLLDRPIKGEGIFRSIFLFPMAVSFVASGVVWRWLLNSAQGESASGLNRLFEMTGLRFLENSWTQNTTWGILAIALPAVWQLAGYVMALFLAGFRGIPDDLREAARVDGASEWQLYKSIIFPQLTPIALSAVIIIGHMSLKSFDLIMSITDQRTYSTKVPAIDMFNFMTDNDYSNAAAVGTILLVLVAVAVIPYLIHDAKGRR$","ABC-type multiple sugar transport system, permease component","Membrane, Cytoplasm","ABC transporter BH3846","K02025 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[80-309]T$	BPD_transp_1
PS50928	$\"[84-300]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[87-107]?$ $\"[122-142]?$ $\"[177-197]?$ $\"[225-245]?$ $\"[282-302]?$	transmembrane_regions

","BeTs to 14 clades of COG1175COG name: ABC-type sugar transport systems, permease componentsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1175 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 80 to 309 (E_value = 2.8e-12) place ANA_1363 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter BH3846 (permease)","","1","","","","","","","","","","","Tue Aug 14 15:12:28 2007","","Tue Aug 14 14:53:36 2007","","","Tue Aug 14 14:53:36 2007","","","","Tue Aug 14 14:53:36 2007","Tue Aug 14 14:53:36 2007","","","","","yes","","" "ANA_1364","1461462","1460143","1320","5.63","-7.36","46051","ATGCGTCCCACCCACTATCTCTCCCGCCGCGCCGTGCTGGCAGGGTTGGGAACCACTGCAGTCGCCGCCACCCTGGCCGCCTGTGCCACCTCCGGCAGCTCCGGCTCGAAGTCCGGTGGAGCCGCCGGTGAGGGGGACGCCAGCCAGGTCGACGTCGTCACCTGGTGGTCGGCCGGCTCGGAGAAGCTCGGTCTGGATGCCCTGGTCAAGGTCTTCAACCAGCAGTTCCCCAAGACGAAGTTCGAGAACAAGGCCGTCTCCGGCGGCGCCGGCAGCCAGGCCAAGCAGAAGCTTTCCGCGGACCTGGCCGCCAAGAACCCGCCGGACACCTACCAGGCCCACGCCGGCGCCGAGATCAAGGACCACATCGAGGCCGGCTACCTGCTGGACGTCTCCAACCTCTACGAGGAGTTCAAGCTCAACGAGGCATTCCCGGCCACCCTCATGGACCGCCTCAAGGACTCCGACGGCAAGATCTACTCGGTGCCCTCCAACATCCACCGGGCCAATGTCGTGTGGGCCTCGGTGTCTGCGCTCAAGGCCGCTGGGCTCGACCCGACCAAGCCCGCCACCACCATCGACGCCTGGATCGCCGACATGGAGAAGGTCAAGGCTGCCGGCCTGACCCCCATCACCATGGGCATGGCTTGGACCCAGCTCGAGCTGCTCGAGACCATTCTCATCGCCGACCTGGGCGTGGACGCCTACAACGGGCTCTTCGCAGGCAAGACCGACTGGGGCGGCGCCGAGGTCACCAAGGCGCTGGGGCACTACAAGACCATCGTGGGCTTCACCGACTCCTCCCTTTACACCGAGGACTGGGAGCCCGCCATGAAGCCCATCATGGACGGCAAGGCCGCCTTCAACGTCATGGGCGACTGGGCCGTGGCCGGCTTCGACGCTGCCGGCAAGAAGGCCGGCCAGGACTACGTCTACTTCCCAGTCCCGGGCACCGACGGCGTCTTCGACTTCCTGGCCGACTCCTTCACCCTGCCTGACGGCGCCAAGCACCCCGGCGGTGCCAAGAACTGGCTCAACACCATCTCCTCCAAGGACGGCCAGATCGCCTTCAACACGGTCAAGGGCTCCATCCCGGCCCGAGCCGACCTCACCGACGAGGAGAAGGGCAAGTTCTCCGAGTACCAGCGCGCGGCCATGGAGTCCTTCGCCAAGGACAAGATCGTCTCCTCCATCGCTCACGGCGCGGCCCTGCCGGCCAAGGCCACCAACGCGATGAACGACGCCCTGACCAAGTTCGCCCAGGGCGCCTCCGACGTCACCGCCCTGCAGGCCGACCTCAAGGCCGCTGCCGCCTCCTGA","MRPTHYLSRRAVLAGLGTTAVAATLAACATSGSSGSKSGGAAGEGDASQVDVVTWWSAGSEKLGLDALVKVFNQQFPKTKFENKAVSGGAGSQAKQKLSADLAAKNPPDTYQAHAGAEIKDHIEAGYLLDVSNLYEEFKLNEAFPATLMDRLKDSDGKIYSVPSNIHRANVVWASVSALKAAGLDPTKPATTIDAWIADMEKVKAAGLTPITMGMAWTQLELLETILIADLGVDAYNGLFAGKTDWGGAEVTKALGHYKTIVGFTDSSLYTEDWEPAMKPIMDGKAAFNVMGDWAVAGFDAAGKKAGQDYVYFPVPGTDGVFDFLADSFTLPDGAKHPGGAKNWLNTISSKDGQIAFNTVKGSIPARADLTDEEKGKFSEYQRAAMESFAKDKIVSSIAHGAALPAKATNAMNDALTKFAQGASDVTALQADLKAAAAS$","ABC-type multiple sugar transport system, substrate-binding component","Extracellular, Periplasm","Hypothetical ABC transporter extracellularbinding protein PH1214precursor, putative","K02027 multiple sugar transport system substrate-binding protein","extracellular solute-binding protein, family 1","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[13-355]T$	SBP_bac_1

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[7-35]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[52-375]T$	no description
PS51257	$\"[1-28]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[12-32]?$	transmembrane_regions

","BeTs to 7 clades of COG1653COG name: Sugar-binding periplasmic proteins/domainsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1653 is -o-pkz--vdrlbcefghs--j--t-Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","-56% similar to PDB:2B3B Thermus thermophilus Glucose/Galactose Binding Protein With Bound Glucose (E_value = 8.4E_64);-56% similar to PDB:2B3F Thermus thermophilus Glucose/Galactose Binding Protein Bound With Galactose (E_value = 8.4E_64);","Residues 13 to 355 (E_value = 5.9e-18) place ANA_1364 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","ABC transporter extracellular binding protein PH1214precursor, putative","","1","","","","","","","","","","","Tue Aug 14 15:12:49 2007","","Tue Aug 14 14:53:53 2007","","","Tue Aug 14 14:53:53 2007","","","","Tue Aug 14 14:53:53 2007","Tue Aug 14 14:53:53 2007","","","","","yes","","" "ANA_1365","1462833","1461847","987","4.90","-13.63","33947","ATGGCTAACGCTCCCGTCAACATCACCATCACCGGTGCTGCCGGCAACATCGGCTACGCCCTGCTGTTCCGCATCGCCTCCGGCGCCCTGCTCGGCCCGGACCAGCGCGTCAACCTCCGTCTGCTGGAGATCCCGCCGGCCGTCAAGGCCGCTGAGGGTACCGCGATGGAGCTGTTCGACTCCGCCTTCCCGACCCTGGGCAGTGTCGACATCTTCGACGACGCCAAGGCCGCTTTCGAGGGCGCCAACATCGCCTTCCTCGTCGGCTCCATGCCCCGCAAGGCCGGTATGGAGCGCGCCGACCTGCTCTCCGCCAACGGCGGCATCTTCGGTCCCCAGGGTGAGGCCCTCAACGCCGGTGCCGCCGAGGACATCAAGGTGCTCGTCGTGGGCAACCCCGCCAACACCAACGCCCTCATCGCGGCCTCGCACGCCCCCGACATCCCCTCCTCGCGCTTCACGGCCATGACCCGTCTGGACCACAACCGCGCCCTGGCCCAGCTGGCGACCAAGGCCGGCTGCCACGTCACCGACATCGACAAGGTCACCGTCTGGGGCAACCACTCCTCCACTCAGTACCCCGACCTGACCCAGGCCACCGTCAAGGGCTCGCCCATCACCGACATCCTGGCCGACCGGGCCTGGGTCGAGGACGACTTCATCCCGACCGTCGCCAAGCGCGGCGCCGCCATCATCGACGCTCGCGGCGCCTCCTCGGCGGCCTCGGCGGCCTCTGCGGCCATCGATCACGTGCACGACTGGGTGTTGGGCACCTCCGGGTCCTGGACCTCCTCCTCGGTCATGTCCGACGGCTCCTACGGCGTGCCCGAGGGCATCATCTCCTCCTTCCCCTGCACCTCGGAGAACGGGGAGTGGAAGATCGTCCAGGGTCTCGAGATCGACGACTTCTCCCGCGCCAAGATCGATGCCTCGGCGGCCGAGCTCGTCGAGGAGAAGAACGCCGTGGCCTCCATGGGGCTCATCTGA","MANAPVNITITGAAGNIGYALLFRIASGALLGPDQRVNLRLLEIPPAVKAAEGTAMELFDSAFPTLGSVDIFDDAKAAFEGANIAFLVGSMPRKAGMERADLLSANGGIFGPQGEALNAGAAEDIKVLVVGNPANTNALIAASHAPDIPSSRFTAMTRLDHNRALAQLATKAGCHVTDIDKVTVWGNHSSTQYPDLTQATVKGSPITDILADRAWVEDDFIPTVAKRGAAIIDARGASSAASAASAAIDHVHDWVLGTSGSWTSSSVMSDGSYGVPEGIISSFPCTSENGEWKIVQGLEIDDFSRAKIDASAAELVEEKNAVASMGLI$","Malate dehydrogenase","Cytoplasm","Malate dehydrogenase","malate dehydrogenase ","malate dehydrogenase","","Gietl C. Malate dehydrogenase isoenzymes: cellular locations and role in the flow of metabolites between the cytoplasm and cell organelles. Biochim. Biophys. Acta 1992. 1100(3):217-234. PMID: 1610875Birktoft J.J., Rhodes G., Banaszak L.J. Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution. Biochemistry 1989. 28(14):6065-6081. PMID: 2775751","","","

InterPro
IPR001236
Family

Lactate/malate dehydrogenase
G3DSA:3.90.110.10	$\"[156-328]T$	no description
PF00056	$\"[6-155]T$	Ldh_1_N
PF02866	$\"[157-326]T$	Ldh_1_C

InterPro
IPR001252
Active_site

Malate dehydrogenase, active site
PS00068	$\"[156-168]T$	MDH

InterPro
IPR001557
Family

L-lactate/malate dehydrogenase
PIRSF000102	$\"[7-326]T$	L-lactate/malate dehydrogenase

InterPro
IPR008267
Domain

Malate dehydrogenase
PD003052	$\"[273-319]T$	Q8GTZ6_EEEEE_Q8GTZ6;

InterPro
IPR010945
Family

Malate dehydrogenase, NAD or NADP
PTHR23382	$\"[98-326]T$	MALATE DEHYDROGENASE
TIGR01759	$\"[3-322]T$	MalateDH-SF1: malate dehydrogenase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[2-155]T$	no description
signalp	$\"[1-28]?$	signal-peptide

","BeTs to 16 clades of COG0039COG name: Malate/lactate dehydrogenasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0039 is aomp-zyqvdrlbce-ghs-ujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB008267 (Malate dehydrogenase) with a combined E-value of 7e-159. IPB008267A 6-45 IPB008267B 81-112 IPB008267C 113-131 IPB008267D 135-174 IPB008267E 175-201 IPB008267F 210-258 IPB008267G 269-290***** IPB001557 (L-lactate dehydrogenase) with a combined E-value of 4.4e-79. IPB001557A 7-47 IPB001557B 69-120 IPB001557C 132-186 IPB001557D 214-263 IPB001557E 277-322 IPB001557D 215-264 IPB001557D 213-262","","","-64% similar to PDB:1IZ9 Crystal Structure of Malate Dehydrogenase from Thermus thermophilus HB8 (E_value = 1.0E_84);-64% similar to PDB:1Y7T Crystal structure of NAD(H)-depenent malate dehydrogenase complexed with NADPH (E_value = 1.0E_84);-64% similar to PDB:2CVQ Crystal structure of NAD(H)-dependent malate dehydrogenase complexed with NADPH (E_value = 1.0E_84);-64% similar to PDB:1BMD DETERMINANTS OF PROTEIN THERMOSTABILITY OBSERVED IN THE 1.9 ANGSTROMS CRYSTAL STRUCTURE OF MALATE DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM THERMUS FLAVUS (E_value = 5.1E_84);-63% similar to PDB:1BDM THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A SINGLE SITE MUTANT (T189I) OF MALATE DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED ENZYMATIC ACTIVITY (E_value = 2.5E_83);","Residues 6 to 155 (E_value = 2.3e-39) place ANA_1365 in the Ldh_1_N family which is described as lactate/malate dehydrogenase, NAD binding domain.Residues 157 to 326 (E_value = 8.4e-50) place ANA_1365 in the Ldh_1_C family which is described as lactate/malate dehydrogenase, alpha/beta C-terminal domain.","","dehydrogenase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1366","1463087","1464898","1812","8.78","5.59","62539","ATGAGCTCACGCCGATCCCCCGCGCCCATCCTCGCGCCACTGCGCCGCGGCTCCCCGCCCCGCCCCACGGTCTCCTCACCGGCCGGGCGTCGCGCAGGCGCCCTCTCCTTCGGTCTGACGCTCCTGGGCGCCCTGGGAGCCGGGTGGTGCCTCATCTGCACCGGACGCGCCCTGGGCGCCCTGCTGAGCTCCTCGTCAGCGGCGGGCCTGCTCGCCCAGGCCCTGGCCGCGGCCGCCGTGAGCGCCACCTGCCAGCTGGTGGCCCAGCGGGTCGCCCGTTTCAGTGCGCTCACCGAGGAGGCGCACCTGCGCCGCCTCACCCTGGCTCACCTGCTGGGGCTGGGCCCGGCACGCGCCGCCGACATCCGCAGCGGTGCGACCGCCTCCCTGCTGACCGACGGCGCAGAGCGGGTGGCCCTCTACCGGCAGACCTTCCTGGCCCCCACACTGGCGGCCGCTGCGGCTCCCCTGCTGGTGCTCGTCGAGTTGGCCGCCTTCGTCGACGTCGTTCCCGCCCTGGTCCTGGCGGCGGCCGTCATCGTGGTACCGGCCTTCATCGCCTGGTGCCACTCGCGGCTGCGGGCCTCGTCCTCGAACTCCCGACGGGCGCGGATGCGTCTGGCCGCCGAGTACCTCGACGCGATCCAGGGACTGCGCACCCTCACCCTGGCCCGGGCCGCGGAGCGCACCAGTGCGCGCCTGCGCCTGGAGGGGGAGTCGAACCGACGCGCCGTCATGGGGCTGCTGGCGGGCAACCAGCTCGTCATCCTGCTCACCGACAGCCTGTTCTCGCTCTTCCTCATCTCCGTGGCCGCCGGTCTGGCCCTGGTACGCCTGTCCACCGGCGCCATCGACGTCAGTGACGCCTTGGCAATCGTCCTGACCTCCTACGTGCTCCTCGAGCCGCTGGACCACGTGGGCGCCTTCTTCTACGTGGGCATGGCCGGAATGGCCAACCAACGCGCCATCCGCAGGATCCTGTCGCGGCCCCTGCCCCGCTCAACCGCTCGTCCCGGGGCCACGGTCTCCTCCCCCATGGCCGCTCAGGCATCCATCGTGCTCGACGACGTCGAGGCCGCCTGGGACGCCGATCCGGTGCTGGAGGGCGTCAATCTGAGCGTGCGCCGTGGTGAGAGCCTGGCGGTGGTCGGCCCCTCAGGGGCGGGCAAATCGACGCTCATGGCGATGCTTGCCGGCAACCTGCTGCCCAGGGGCGGATCCGTACGCGTCGAGGGCACCGAGCTGAGCGCCGCGACGCAGGACGAGGTGCGTTCGGCCTCCGCGCTGGTGGCGCAGACGACCTGGCTGTTCACTGGGACGATTGCCGACAACCTGCGCCTGGCCCAGCCCTACGCGACGCCGTCGCAGATGTGGCAGGCCCTGGAGGTGGCCCGCCTCGACAAGGAGGTGGCGCTCATGCCCGAGGGGCTGGAGACCCAGGTCGGCGAGGCCGGCCTGGGACTGTCGGGAGGTCAGGCCCAGCGCCTGTCCCTGGCCCGCGCCTTCCTGGCCGACCGCCCCGTACTGCTCCTGGACGAACCCACCAGCCAGGTGGACCTGGCCAGCGAGGCGGCCATCGTGGAGTCCCTTGAGCAGCTGTCCCAGGGCCGCACGGTCGTCACCATCTCCCATCGCGTCGGAGCGCTGACGGCAGCGGACCGGACGGTGAGGGTTGATGCCGGTACGGTCCACGAGGTCGGTGAAGCCCGGACGCCCAAATCCGCCAGCGCGGCGCCCACTCAGGAAGCCACCGGGGCCGACGGGTCTTCCTCCAAGGTCTCCGACGGGGATCACCAGGAGGAGCGGGCATGA","MSSRRSPAPILAPLRRGSPPRPTVSSPAGRRAGALSFGLTLLGALGAGWCLICTGRALGALLSSSSAAGLLAQALAAAAVSATCQLVAQRVARFSALTEEAHLRRLTLAHLLGLGPARAADIRSGATASLLTDGAERVALYRQTFLAPTLAAAAAPLLVLVELAAFVDVVPALVLAAAVIVVPAFIAWCHSRLRASSSNSRRARMRLAAEYLDAIQGLRTLTLARAAERTSARLRLEGESNRRAVMGLLAGNQLVILLTDSLFSLFLISVAAGLALVRLSTGAIDVSDALAIVLTSYVLLEPLDHVGAFFYVGMAGMANQRAIRRILSRPLPRSTARPGATVSSPMAAQASIVLDDVEAAWDADPVLEGVNLSVRRGESLAVVGPSGAGKSTLMAMLAGNLLPRGGSVRVEGTELSAATQDEVRSASALVAQTTWLFTGTIADNLRLAQPYATPSQMWQALEVARLDKEVALMPEGLETQVGEAGLGLSGGQAQRLSLARAFLADRPVLLLDEPTSQVDLASEAAIVESLEQLSQGRTVVTISHRVGALTAADRTVRVDAGTVHEVGEARTPKSASAAPTQEATGADGSSSKVSDGDHQEERA$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","ATP binding transporter 1","K06147 ATP-binding cassette; subfamily B; bacterial","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[488-530]T$	Q9ZBY5_STRCO_Q9ZBY5;
PF00005	$\"[377-561]T$	ABC_tran
PS50893	$\"[352-585]T$	ABC_TRANSPORTER_2
PS00211	$\"[488-502]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[376-562]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[34-315]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[314-571]T$	no description
PTHR19242	$\"[71-568]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF55	$\"[71-568]T$	ABC TRANSPORTER (CYDD)
signalp	$\"[1-50]?$	signal-peptide
tmhmm	$\"[33-53]?$ $\"[67-87]?$ $\"[146-166]?$ $\"[172-190]?$ $\"[254-276]?$	transmembrane_regions

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[58-266]T$	ABC_membrane

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[408-592]T$	ABC_tran
PS50893	$\"[381-616]T$	ABC_TRANSPORTER_2
PS00211	$\"[519-533]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[407-593]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[69-348]T$	ABC_TM1F

InterPro
IPR014223
Family

ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC
TIGR02868	$\"[44-577]T$	CydC: ABC transporter, CydDC cysteine expor

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[345-614]T$	no description
PTHR19242	$\"[16-608]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91	$\"[16-608]T$	LIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA
tmhmm	$\"[70-90]?$ $\"[96-116]?$ $\"[172-192]?$ $\"[198-218]?$ $\"[294-314]?$	transmembrane_regions

InterPro
IPR001991
Family

Sodium:dicarboxylate symporter
PF00375	$\"[44-424]T$	SDF

InterPro
IPR006118
Family

Site-specific recombinase
PS00398	$\"[413-425]?$	RECOMBINASES_2

noIPR
unintegrated

unintegrated
PTHR11958	$\"[172-431]T$	SODIUM/DICARBOXYLATE SYMPORTER-RELATED
PTHR11958:SF6	$\"[172-431]T$	gb def: Na+/H+-dicarboxylate symporter
tmhmm	$\"[44-64]?$ $\"[83-105]?$ $\"[126-146]?$ $\"[173-191]?$ $\"[212-232]?$ $\"[242-262]?$ $\"[328-348]?$ $\"[354-385]?$	transmembrane_regions

","BeTs to 11 clades of COG1301COG name: Na+/H+-dicarboxylate symportersFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1301 is -o--kz-q-dr-b-efg-s-ujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001991 (Sodium:dicarboxylate symporter) with a combined E-value of 4.1e-31. IPB001991A 81-107 IPB001991E 259-300 IPB001991F 304-341 IPB001991G 387-421","","","No significant hits to the PDB database (E-value < E-10).","Residues 44 to 424 (E_value = 9e-08) place ANA_1368 in the SDF family which is described as Sodium:dicarboxylate symporter family.","","symporter ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1369","1468715","1468416","300","10.23","4.85","10652","GTGACTCATGACCCGCATCCCCAGCAGGCCGAGCACAAGGAGCCCTACCGCACCATTTGTGTCGTCCTCGTGGCCATTGGCCTGGCGGCTGTCCCAGCCATCGCCCTGCTGGGGCACCGCCGCATCGCCGTCCTGTGGGCGGCCGCCGGGATCCTCATGCTGGCCATCGTCCGCCTCCAGCGCCCCGACGGCACCTGGCTGGCGGCGCGCAGCCGCCTGTTCGACGTCGTCCTCGGCGTCGGCCTGGCCGCCGCCCTGCTTCTCCTGTCGCCATACGTCAACCTGCCCCGCATCGTGTGA","VTHDPHPQQAEHKEPYRTICVVLVAIGLAAVPAIALLGHRRIAVLWAAAGILMLAIVRLQRPDGTWLAARSRLFDVVLGVGLAAALLLLSPYVNLPRIV$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[19-37]?$ $\"[42-62]?$ $\"[76-96]?$	transmembrane_regions

InterPro
IPR002695
Family

AICARFT/IMPCHase bienzyme
PD004666	$\"[42-225]T$	PUR9_COREF_Q8FR29;
PTHR11692	$\"[31-223]T$ $\"[239-604]T$	BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN

InterPro
IPR011607
Domain

MGS-like
PF02142	$\"[47-161]T$	MGS

InterPro
IPR013982
Domain

AICARFT/IMPCHase bienzyme, formylation region
PF01808	$\"[166-498]T$	AICARFT_IMPCHas
SM00798	$\"[166-498]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.140.20	$\"[409-604]T$	no description
G3DSA:3.40.50.1380	$\"[31-217]T$	no description

","BeTs to 17 clades of COG0138COG name: AICAR transformylase/IMP cyclohydrolase PurH (only IMP cyclohydrolase domain in Aful)Functional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0138 is ao-p--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002695 (AICARFT/IMPCHase bienzyme) with a combined E-value of 1.2e-197. IPB002695A 41-85 IPB002695B 86-110 IPB002695C 150-182 IPB002695D 199-221 IPB002695E 261-274 IPB002695F 316-332 IPB002695G 340-369 IPB002695H 371-397 IPB002695I 456-494 IPB002695J 548-585 IPB002695K 586-604***** IPB011607 (MGS-like) with a combined E-value of 1.6e-14. IPB011607A 153-169 IPB011607B 545-558","","","-44% similar to PDB:1P4R Crystal Structure of Human ATIC in complex with folate-based inhibitor BW1540U88UD (E_value = 1.8E_54);-44% similar to PDB:1PKX Crystal Structure of human ATIC in complex with XMP (E_value = 1.8E_54);-44% similar to PDB:1PL0 Crystal structure of human ATIC in complex with folate-based inhibitor, BW2315U89UC (E_value = 1.8E_54);-43% similar to PDB:1G8M CRYSTAL STRUCTURE OF AVIAN ATIC, A BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME IN PURINE BIOSYNTHESIS AT 1.75 ANG. RESOLUTION (E_value = 1.3E_52);-43% similar to PDB:1M9N CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH AICAR AND XMP AT 1.93 ANGSTROMS. (E_value = 1.3E_52);","Residues 47 to 161 (E_value = 6.8e-55) place ANA_1371 in the MGS family which is described as MGS-like domain.Residues 166 to 498 (E_value = 1.2e-126) place ANA_1371 in the AICARFT_IMPCHas family which is described as AICARFT/IMPCHase bienzyme.","","purine biosynthesis protein purH [Includes:Phosphoribosylaminoimidazolecarboxamide formyltransferase(AICAR transformylase); IMP cyclohydrolase (EC 3.5.4.10) (Inosinicase)(IMP synthetase) (ATIC)]","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1373","1470912","1473407","2496","6.58","-2.17","88648","ATGACTGCGCCCATCAACATCGCAGCAACACCGGTATATCGGAGGACTCCCCCGGAGCAGTGGCAGGAGGCCGCCTCCGCCTACCGGCGCTGGTGGAGCCGCCACCCGGGATTGTCCAGTGCCCTGAACCTGGTGGTGCGCGGAGCCTACGTCCTGATGATCCCGCTGCTCATCGCCGCCCTAGTGATGGTCCCGAGGCTGGCCTACGCCGCCGTGCCGGCGGCCTTCATGGCCGTGTGCCTCATGGTGGTGGCCCTCCTGGCGCGCACACGCACCATCAGCTGGCGCTCGGTTCTGCTCATGTACGGTGTCGGCGCCGCCTGGTCGCTCGTCGTGGCCGCCATCATGAGCTCGGTGCGTACCCGCGCAGGCCTGTCCGTCATGGGCAACGGGATGAGTATCGCCCTGACCATTGCCCTGGAGGTTCTCAGCCCGCTGGTGCCCCTGGTGCTCGTGGTCTTCCTGGCGCCGGGGCGGATGCGCCGCCTGGCGGCCTCCGACTGGGCCCTGCTGGGTTTCGCGGCCGGAGCGGGCCTGACGGCCCTCAACGACGGCATTCGGGCCCTTGAGGAGAGCAGCCTGCTCTCCTTGGTCCTGGGCAACGGGCGCCTTCCCTTCTCCTTCAACCCGTGGACCTCGGGCTCGATGACCCAGGAGAACAGCAACGTCCTGGCCGTCAGCAACCAGGTGAGCACCGCGAACATCACGATGGCGGTGGCGCTGGCGATCACGCTGTGGCGCCTCAAGGACTCCCCGGCCTTCGAAGGGGCTAAGAACCTCGTGTGGCTGCGGATCGTGGCCTGGATCCTGCCGGCGGTGGTCATCCTGCAGTCGGTCAGTGACCACGCCACCTACATCGCCAGGATCGCCCAGCAGCTCGGCCAGAGCGACTCCGGCGGCGGGTTCCCGGCGCTGCTCATGTTCCTGTGGAAGGTCAACGGCGGAGGCCTGAGCGCCATCCCCCTGTCCGTCATTCTCATGGCCGCCTGCCTGCTCCTGGACGCCCACCGCCGCGCCTACGCGGGTGTGCACGGCTGGACGGTGGCCGGGGCGCCGGCTCCCCGCTACCCCAACCTCACCGAGGCGCCGCCCTTCGTGCGCGCCCTCATCGTCTCGGTGGTGGCCCTGGCGAACTTCACCTGGGGTGACCTGGCCGTCACCTGGGGCGCCTACGGGGATCTGCGCCAGGGACGGCTCTACGCCATGCGGGCGGGACGGGCCACGGCGGAGCAGGTGCGCGGCGTGCGAGCAGACGCCATGGAGGCCACGACGCCGGGTGCTGAGCCCAATGCCCGCCAGGGCTTCCGCCTGGGGATCCTGGTGGTCAGCGTCGTGCTGTTCCTCCTGTGCTGCATGTACGAGGTGCGCACCGTCTGGCAGCTGGCCCCCGAGCTCAAGGAGACCGAGGACGATCTGTTCCTCTCCGCCCTGCCACGCCTGTTCTCCCAGTGGTGGAGCGGGTTGAGTGGCACCCAGGGGCTCCTCTACGCGATCGGTGCGCTGGCGGCGGTGGCCATGAGTCTGTCCCTGGTCCTGACGCTGGGGGCCCCGGGGCGCCGCATCAGCACGGCGCCGTCGTCGAGCAGCCTCATCAGTCACCTGCTCACTCTCACGCCGGGGCAGGCGTGCCTGGCGCTGCTGGACTTCGCCATGACCTACATGCCGCGCTCGGCCCTGAGCGCCAGTCCCGCCGGTGGCGGAACCGACCTGGCCGCCGAGCTCTCCGTCAACCGGCGGATCCGGGGCGCCGAGAGCTTCTCCGAGAGTCAGGCGCTGTTCACGGCGCGTACCAAGCGGCAGGTGGCGGTCGAGTCTGATATTGCGCGCCTTCGCGAGCTCGCCGAGTCCCTGGGCGTCACCGACGTCGATGCCCTCGAGCCTAGCCGGATCGATGAGACCGTCGCCGATCTGGCCGCCTCCGGGGCCGACTCCCAGGTCGTCGGGCAGATGCGCGACCTGGCCGCCTCAGTATCGGAGCAGCAGTCGGAGATCCTGGACCTGACCCGCCGGCTCAACACCGGTAACGGCGAGCAGTTCGCCATTCTGGAGGGCTTGCGGATCAACGACGACTTCCGGGGTGAGGCCATCGACCAGCGGCCGGTGGACAGCCCCGTCCACGCCCTGGCGCTATCCCCGGCCGGGAACCAGCTGGTCGTCGTCGAGTACCAGGGGGCCGCCCCCACCATTGATGACGACGACGAGACCGACATTCCTCCCCGCAGGCTGCCGGGGCGGGCGGCGCACAAGTCGGCCGACAACGTTCTGGAGCACCTGGCCTCGGACGAGCGCGTCGCGCGGTTCTTCCGGGAGAACCCTGAGCTGTGGCAGGCCATCAAGGAGGGACGCGCACTCCTGGAGGCGAACGTCCTCTACACCCCCATCCCCGGGATGACCTACCGGGCCGGGACCGCGCTCCTGGCGGTGACGCCCGAACTGGTCGAGGGCGTGGATACGGCCGTCAGCTCCTTGAGCAGCGCGGGCACGGCGGCTCGCTGA","MTAPINIAATPVYRRTPPEQWQEAASAYRRWWSRHPGLSSALNLVVRGAYVLMIPLLIAALVMVPRLAYAAVPAAFMAVCLMVVALLARTRTISWRSVLLMYGVGAAWSLVVAAIMSSVRTRAGLSVMGNGMSIALTIALEVLSPLVPLVLVVFLAPGRMRRLAASDWALLGFAAGAGLTALNDGIRALEESSLLSLVLGNGRLPFSFNPWTSGSMTQENSNVLAVSNQVSTANITMAVALAITLWRLKDSPAFEGAKNLVWLRIVAWILPAVVILQSVSDHATYIARIAQQLGQSDSGGGFPALLMFLWKVNGGGLSAIPLSVILMAACLLLDAHRRAYAGVHGWTVAGAPAPRYPNLTEAPPFVRALIVSVVALANFTWGDLAVTWGAYGDLRQGRLYAMRAGRATAEQVRGVRADAMEATTPGAEPNARQGFRLGILVVSVVLFLLCCMYEVRTVWQLAPELKETEDDLFLSALPRLFSQWWSGLSGTQGLLYAIGALAAVAMSLSLVLTLGAPGRRISTAPSSSSLISHLLTLTPGQACLALLDFAMTYMPRSALSASPAGGGTDLAAELSVNRRIRGAESFSESQALFTARTKRQVAVESDIARLRELAESLGVTDVDALEPSRIDETVADLAASGADSQVVGQMRDLAASVSEQQSEILDLTRRLNTGNGEQFAILEGLRINDDFRGEAIDQRPVDSPVHALALSPAGNQLVVVEYQGAAPTIDDDDETDIPPRRLPGRAAHKSADNVLEHLASDERVARFFRENPELWQAIKEGRALLEANVLYTPIPGMTYRAGTALLAVTPELVEGVDTAVSSLSSAGTAAR$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

InterPro
IPR007449
Domain

ZipA, C-terminal FtsZ-binding region
SM00771	$\"[568-687]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-70]?$	signal-peptide
tmhmm	$\"[38-60]?$ $\"[66-88]?$ $\"[98-120]?$ $\"[134-156]?$ $\"[168-186]?$ $\"[225-245]?$ $\"[260-280]?$ $\"[312-332]?$ $\"[437-457]?$ $\"[494-514]?$ $\"[529-549]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-51% similar to PDB:1R66 Crystal Structure of DesIV (dTDP-glucose 4,6-dehydratase) from Streptomyces venezuelae with NAD and TYD bound (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1374","1474593","1473424","1170","9.16","6.51","40187","GTGGTGCTGGCGACGATCGCCGTGTCCAAGGCGGCCGCCAGCCTCAACGCCGCGGCCATTCTCAGTGCAGGCGACGCCCTGCACACCGGGACCGCCCTGTGGAGCCTCGGCTTCGGGGGCTCGACCGCGCTGACCTCCGAGGACGACGGTGTGCTCAGCCTGCCGCTGCTGGGACTCACCCTGGTACAGGCGGGCTGGACCTGGTTCTGCGTGCGGCGCGCCCACCCCTCCCGGCCGGCGGCCGGGGCGGCCATCGTCGCCGCCGCGACCGTCGTGGCGGCCCTGGCCTGCCTCACCGGCCCCGCCGGGCTGGACACCTGGCCCGCCGTCGTCGGTATCGCCCTGCTCACCGGCGTCATCGTCGCCATCCAGCTCATGCGCGCCGGCCACCACTGGTCGCCCCTGACCCGATGGTGGGACCGCCGACCACATTGGCTGGGGCCTTCCCTGTCGCTGGCCTACGGGGCCACGCGAGCCCTGAGCCTGCTGAGTCTGCTGGTGGTGGTCGCGGCTGTCGTCAACGGAGCCGGCCGGGTCTCGGTCCTGCACGACTCCCTGGCCGGGGACGGCTTCGTCGCGATGGCCGGCCTCATCCTGCTTCAGGCCGGCTGGGTGCCGACCCTGTTCATCTGGGCCTGCTCCTGGCTCATCGGAGCCGGCTTCTCCGTGGGCACGGGCACGGTCTTCGCCCCCGACCGGGTGGTGGCCGGGCCCGTCCCACGCCTGCCGCTGCTGGGGCTGGTGCCGTCGACGCCGCTGAGCAGCGTGGGCCTGTGGCTGCCCCTGGTGGTGACGGCCGGCGCCATGGTGGCCGCCTGGCGACGTCGAGCGGTGCTCAACGCCCTGCGGGTGCGCTACGCCCTCAGCGCCGCCGGTCTGGCCGCCCTCCTCGTGGCCGGTGGCGTGGGCCTGTTGTGCCTGGCTGCCTCCGGGTCCGTGGGGCCGAACCGGATGAGCAGTGTCGGTCCGCTGGTCCTCTACACCGTCATCCTCGTCTTCGTCGAGGTCGGTGTCGGCCTGGCGGCCATGGCCGTCCTGGCCCACCCCTACACACGCACTTGGGCCCGCAACACCCTGCCCGAGTCGGTCCTGCCGGCGGCCTACCGGCGCCAGGATGTGCGCGAGGACGCCGTCGATGAGACTGACTGGGAGAACGACCGCGAGAGGTGA","VVLATIAVSKAAASLNAAAILSAGDALHTGTALWSLGFGGSTALTSEDDGVLSLPLLGLTLVQAGWTWFCVRRAHPSRPAAGAAIVAAATVVAALACLTGPAGLDTWPAVVGIALLTGVIVAIQLMRAGHHWSPLTRWWDRRPHWLGPSLSLAYGATRALSLLSLLVVVAAVVNGAGRVSVLHDSLAGDGFVAMAGLILLQAGWVPTLFIWACSWLIGAGFSVGTGTVFAPDRVVAGPVPRLPLLGLVPSTPLSSVGLWLPLVVTAGAMVAAWRRRAVLNALRVRYALSAAGLAALLVAGGVGLLCLAASGSVGPNRMSSVGPLVLYTVILVFVEVGVGLAAMAVLAHPYTRTWARNTLPESVLPAAYRRQDVREDAVDETDWENDRER$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-17]?$	signal-peptide
tmhmm	$\"[15-37]?$ $\"[51-71]?$ $\"[81-103]?$ $\"[109-129]?$ $\"[150-172]?$ $\"[191-211]?$ $\"[216-236]?$ $\"[255-273]?$ $\"[288-308]?$ $\"[327-347]?$	transmembrane_regions

InterPro
IPR000169
Active_site

Peptidase, cysteine peptidase active site
PS00639	$\"[131-141]?$	THIOL_PROTEASE_HIS

InterPro
IPR003781
Domain

CoA-binding
PF02629	$\"[4-118]T$	CoA_binding

InterPro
IPR005810
Family

Succinyl-CoA ligase, alpha subunit
PR01798	$\"[100-117]T$ $\"[193-211]T$ $\"[224-237]T$ $\"[256-273]T$	SCOASYNTHASE
PIRSF001553	$\"[3-305]T$	Succinyl-CoA synthetase, alpha subunit
PTHR11117	$\"[1-49]T$ $\"[68-310]T$	SUCCINYL-COA SYNTHETASE-RELATED
TIGR01019	$\"[3-304]T$	sucCoAalpha: succinyl-CoA synthetase, alpha
PS00399	$\"[252-265]T$	SUCCINYL_COA_LIG_2
PS01216	$\"[170-197]?$	SUCCINYL_COA_LIG_1

InterPro
IPR005811
Domain

ATP-citrate lyase/succinyl-CoA ligase
PF00549	$\"[151-290]T$	Ligase_CoA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.261	$\"[142-305]T$	no description
G3DSA:3.40.50.720	$\"[2-141]T$	no description

","BeTs to 21 clades of COG0074COG name: Succinyl-CoA synthetase alpha subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0074 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB003781 (CoA Binding Domain) with a combined E-value of 3.4e-82. IPB003781A 5-59 IPB003781B 86-124 IPB003781C 137-149 IPB003781D 185-239 IPB003781E 244-275","","","-64% similar to PDB:1JKJ E. coli SCS (E_value = 2.4E_75);-64% similar to PDB:1JLL Crystal Structure Analysis of the E197betaA Mutant of E. coli SCS (E_value = 2.4E_75);-64% similar to PDB:1SCU THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION (E_value = 2.4E_75);-64% similar to PDB:2SCU A DETAILED DESCRIPTION OF THE STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI (E_value = 2.4E_75);-64% similar to PDB:1CQI CRYSTAL STRUCTURE OF THE COMPLEX OF ADP AND MG2+ WITH DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE (E_value = 3.1E_75);","Residues 4 to 118 (E_value = 5.6e-38) place ANA_1375 in the CoA_binding family which is described as CoA binding domain.Residues 151 to 290 (E_value = 1e-35) place ANA_1375 in the Ligase_CoA family which is described as CoA-ligase.","","synthetase alpha chain (sucD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1376","1476836","1475631","1206","4.75","-23.57","41733","ATGGATCTGTACGAATACCAGGCCAGGAACCTGTTCCGTCAGCACGGCGTCCCCGTGCTCGACGGCGCCGTGGCCACAACCCCTGAGGAGGCGCGCAGCGCCGCGCAGTCCCTCCTCGACGCGGGAAGCGAGCTGGTGGTCGTCAAGGCCCAGGTCAAGACCGGCGGCCGAGGCAAGGCCGGCGGCGTCAAGCTCGCCCGCACCGCTGAGGAGGCCGAGGCCCGCGCCCGCGACATCCTGGGCATGGACATCAAGGGCCACACAGTGCGCGCCGTCCTCATCTCCGACGGCGTCGACCTGGACGCCGAGTACTACTTCTCCATCCTCCTGGACCGCGCCGAGCGCCAGTACCTGGCGATGTGCTCGCGCGAGGGCGGCATGGACATCGAGACCCTCGCCGTCGAGCGCCCCGAGGCCCTGGCCCGCATCGGCATCGACCCGCTCGAGGGCATCACCCCGGCCGTCGCCCACCGGATCGTCGAGGCCGCGGGCTTCGAGGCCGGGCCTCTGGCCGACGAGGTCGCCGCCGTCATCGAACGCCTCTGGGAGGTCTTCACCGCCGAGGACGCCACCCTCGTGGAGGTCAATCCCCTGGTCAAGGCCACCGACGGCCGCATCATCGCCCTGGACGGCAAGGTCACCCTCGACGACAACTCCCGCTTCCGCCACCCCGCCCACGCCGAGCTCGTCGACAACGCCGCCACCGACCCCCTGGAGGCCCGCGCCCGCGAGGCCGGCCTCAACTACGTGCGCCTCGAGGGCGAGGTCGGGGTCCTGGGCAACGGCGCCGGCCTGGTCATGTCCACCCTCGACGTCGTCGCCGGCGCCGGCGAGCGCCACGGCGGCATGAAGCCCGCCAACTTCCTCGACCTGGGAGGCGGCTCATCGGCCGAGGTCATGGCCACCGGCCTGGAGGTCGTCGCCTCCGACCCCCAGGTGCGCGCAATCCTCGTCAACGTCTTCGGCGGCATCACCTCCTGCGACACCGTCGCCCAGGGCATCGTGACCGCCGTCGAGTCCCTGGGCGGGTTGCCCAAGCCCGTCGTCGTGCGCCTGGACGGCAATAACGCCGACACCGGTCGCGCCATCCTGGCCGACGCCGCCATCGAGGGCGTCACCGTCGTCGACACCATGGACGGGGCCGCCGACGTCGTCACCGCCATCGCCGAGAAGATCAGCGGCCGGCCCGCTGGCAAGGAGGCCTGA","MDLYEYQARNLFRQHGVPVLDGAVATTPEEARSAAQSLLDAGSELVVVKAQVKTGGRGKAGGVKLARTAEEAEARARDILGMDIKGHTVRAVLISDGVDLDAEYYFSILLDRAERQYLAMCSREGGMDIETLAVERPEALARIGIDPLEGITPAVAHRIVEAAGFEAGPLADEVAAVIERLWEVFTAEDATLVEVNPLVKATDGRIIALDGKVTLDDNSRFRHPAHAELVDNAATDPLEARAREAGLNYVRLEGEVGVLGNGAGLVMSTLDVVAGAGERHGGMKPANFLDLGGGSSAEVMATGLEVVASDPQVRAILVNVFGGITSCDTVAQGIVTAVESLGGLPKPVVVRLDGNNADTGRAILADAAIEGVTVVDTMDGAADVVTAIAEKISGRPAGKEA$","Succinyl-CoA synthetase, beta subunit","Cytoplasm","Succinyl-CoA synthetase beta chain (SCS-beta)","succinyl-CoA synthetase; beta subunit ","succinyl-CoA synthetase, beta subunit","","Galperin M.Y., Koonin E.V. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 1997. 6(12):2639-2643. PMID: 9416615Fan C., Moews P.C., Walsh C.T., Knox J.R. Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. Science 1994. 266(5184):439-443. PMID: 7939684Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Fan C., Moews P.C., Shi Y., Walsh C.T., Knox J.R. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(4):1172-1176. PMID: 7862655","","","

InterPro
IPR005809
Family

Succinyl-CoA synthetase, beta subunit
PIRSF001554	$\"[1-392]T$	Succinyl-CoA synthetase, beta subunit
PTHR11815	$\"[1-393]T$	SUCCINYL-COA SYNTHETASE BETA CHAIN
TIGR01016	$\"[1-389]T$	sucCoAbeta: succinyl-CoA synthetase, beta s
PS01217	$\"[254-278]T$	SUCCINYL_COA_LIG_3

InterPro
IPR005811
Domain

ATP-citrate lyase/succinyl-CoA ligase
PF00549	$\"[243-386]T$	Ligase_CoA

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[9-226]T$	ATP_GRASP

InterPro
IPR013650
Domain

ATP-grasp fold, succinyl-CoA synthetase-type
PF08442	$\"[2-200]T$	ATP-grasp_2

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[81-236]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.261	$\"[237-392]T$	no description

","BeTs to 21 clades of COG0045COG name: Succinyl-CoA synthetase beta subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0045 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB013650 (ATP-grasp fold, succinyl-CoA synthetase-type) with a combined E-value of 9.9e-110. IPB013650A 1-31 IPB013650B 47-62 IPB013650C 99-147 IPB013650D 181-221 IPB013650E 247-290 IPB013650F 302-355***** IPB005809 (Succinyl-CoA synthetase, beta subunit) with a combined E-value of 2.8e-81. IPB005809A 47-59 IPB005809B 102-130 IPB005809C 181-219 IPB005809D 249-285 IPB005809E 292-346","","","-57% similar to PDB:1JKJ E. coli SCS (E_value = 3.9E_76);-57% similar to PDB:1SCU THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION (E_value = 3.9E_76);-57% similar to PDB:2SCU A DETAILED DESCRIPTION OF THE STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI (E_value = 3.9E_76);-57% similar to PDB:1CQI CRYSTAL STRUCTURE OF THE COMPLEX OF ADP AND MG2+ WITH DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE (E_value = 6.6E_76);-57% similar to PDB:1CQJ CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE (E_value = 6.6E_76);","Residues 2 to 200 (E_value = 5e-93) place ANA_1376 in the ATP-grasp_2 family which is described as ATP-grasp domain.Residues 243 to 386 (E_value = 2.9e-37) place ANA_1376 in the Ligase_CoA family which is described as CoA-ligase.","","synthetase beta chain (SCS-beta) (SCS-BETA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1378","1476978","1477847","870","6.01","-5.23","31972","GTGGTCGCAGCGTCTCACGGCGGGGCGTGCGCACCGGGGCCTCCACCGGCCACGAGCGCCGTCCAGCCACGTAGGATGACGAGGGATGGGACACGTAGCATGAGCAAGGATCCCGAGAGTCTTCAGGGTGGGTCGACTGAGGTCACCAAGGTGGGCGGCAGAGTCCTTCGCGCTCGGCGCCAGGGCAGCACCAATGTTGAGTGGCTGCTCACCGTGCTGGAGCGCAGGGGGTTCAGGTACTCACCGAGATTTCTTGGTCTGTCCGACGACGACCGGCAGGTCCTCGAGTTCATTGAGGGCCAGGCCGGCGCCTACCCGCTGCCTGAGGAGCTGCGCCACGATGAGGCGCTCATCTCAGCGGCCCGGGCGCTGCGCTTACTGCACGAGGTGACCAGCGAACTGGCGACCGAGGTGCTGGATGGCTGGATGCTGGAGGCGGTTGAGCCTTACGAGGTCATCTGCCATGGGGACTTCGCGCCGTACAACTGCGTCTTCGACGGGAGCAGGCTGGTTGGCATCATCGACTTCGACACCGCGCACCCAGGTCCTCGCATCCGCGACATCGCCTACGCGATCTATCGCTTCGCCCCACTGACCGCACCAGAAAACGCCGCCGGATTCGGCTCTCTGGCCGAGCAGGCTCGGCGGGCTCGGCTGTTCTGCGACGAGTACGGGGAGGTGAATCGGTCTGAGATCATCGAGGCCGTGTGCCGACGGCTGCTCGATCTGGTCCGGTACATGCGTGCTCAGGCGGCGCAGGGCGACACTGCATTCCAATCCCATCTCGACGACGGCCACGACACCCTCTATCTGCGCGACATCCACTATCTGAGGACCAACGCGGCGGCACTCACCAGGGCTCTTATGTAA","VVAASHGGACAPGPPPATSAVQPRRMTRDGTRSMSKDPESLQGGSTEVTKVGGRVLRARRQGSTNVEWLLTVLERRGFRYSPRFLGLSDDDRQVLEFIEGQAGAYPLPEELRHDEALISAARALRLLHEVTSELATEVLDGWMLEAVEPYEVICHGDFAPYNCVFDGSRLVGIIDFDTAHPGPRIRDIAYAIYRFAPLTAPENAAGFGSLAEQARRARLFCDEYGEVNRSEIIEAVCRRLLDLVRYMRAQAAQGDTAFQSHLDDGHDTLYLRDIHYLRTNAAALTRALM$","Aminoglycoside phosphotransferase","Cytoplasm","Trifolitoxin immunity protein","hypothetical protein","aminoglycoside phosphotransferase","","Trower M.K., Clark K.G. PCR cloning of a streptomycin phosphotransferase (aphE) gene from Streptomyces griseus ATCC 12475. Nucleic Acids Res. 1990. 18(15):4615-4615. PMID: 2167474","","","

InterPro
IPR002575
Domain

Aminoglycoside phosphotransferase
PF01636	$\"[142-220]T$	APH

InterPro
IPR008266
Active_site

Tyrosine protein kinase, active site
PS00109	$\"[153-165]?$	PROTEIN_KINASE_TYR

noIPR
unintegrated

unintegrated
G3DSA:3.90.1200.10	$\"[97-195]T$	no description

","No hits to the COGs database.","***** IPB002575 (Aminoglycoside phosphotransferase) with a combined E-value of 1.6e-09. IPB002575B 155-164 IPB002575C 169-189","","","No significant hits to the PDB database (E-value < E-10).","Residues 55 to 220 (E_value = 6.5e-10) place ANA_1378 in the APH family which is described as Phosphotransferase enzyme family.","","immunity protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1379","1478457","1480832","2376","5.28","-24.03","84064","ATGCCAGCCGCCATGTCCTCAGACACCGCAGACACTGTCCCCTCCCCCACCGGCTCGTCGGCCGGCCCGCTGCTCGGCCTGGACGGCGAGCCCCTGCGCATCGGGGTCCTCACTTCCGGCGGTGACGCCCAGGGCATGAACGCGGCCGTGCGGGCCGTGGTCCGCACCGCCATCCGCCTGGGGGCCAGGCCCTACGCGGTCATGGAGGGCTGGGCCGGGGCCGTGGCCGGGGGTGACGGCATCCGTCCCCTGGAGTGGGACTCGGTGGGCTCCATCCTCCAGCGCGGCGGCACCATCATCGGCACCGCCCGCTCGGCCGAGTTCCGCGAGCGCGCCGGCCAGCTGGCGGCCGCTCGCAACCTGCTGGAGCACGGCATCGACCGACTCGTGGTCATCGGCGGCGACGGCTCTCTAACCGGCACCAACGAGTTCCGCAAGAACTGGCCCTCCCTGCTCGAGGAGCTCGTCGAGACCGGTGACATCAGTGCGGAGACGGCCGCCGCCCATCCCGTCCTCATGGTGACCGGCCTGGTGGGCAGCATCGACAACGACCTCGTGGGCGCCGACATGACCATCGGCACCGACTCCGCCCTCCACCGCATCCTGGAGGCCATCGACGACATCTCCTCAACGGCCGCCTCCCACCAGCGCACCTTCGTCGTGGAGGTCATGGGCCGCCACTGCGGCTACCTGGCCCTCATGGCGGCCGTGGCCGGGGGCTGTGACTACGTCCTGGTCCCTGAGCTCCCCCCGGGCAAGGACTGGGAGGAGGACATGTGCTCCAAGCTCAAGGCGGGCAGAGAGGCCGGGCGCCGCGAGTCCATGGTGATCGTCGCCGAGGGCGCCACCGACCGCGAGGGCAACCGCATCACCGCCGACGACGTCCGCCAGGTCATCGCCGACAAGCTGGGTGAGGCCGCCCGTGTCACCATCCTGGGGCACGTCCAGCGCGGTGGCCGCCCCAGCGCCTACGACCGCTGGATGTCCACGCTGTTGGGCTGCGCTGCCGCCCGTGAGGTGGTGTCCATGGAGCCGGGCAGCGAGCCGGTCATCATCGCCGAGCGCCACAACCGCATCCGCCGTCTGCCGATGATGGAGCAGATCGCGGCCACGCGCGCTGTCAAGGATCTCGTGGCCGCCCACGACTACCTCGGGGCGGTCCAGGCCCGCGGGGCGAGCTTCGGCAGGATGCTCGAGCTGTTCGAGACCATGTCCACGCCTCCCGCCGAGCCGGCCACTGACACGGGATCGACGCCGTCGACCTCCGACCGCCCCAAGCGGGTCGCCATCATCCACGCCGGCGGCCTGGCCCCGGGGATGAACACGGCGGCGCGTGCGGCCGTGCGCCTGGGCATCGACCACGACTTCACGATGCTGGGCGTCTACGGCGGCTTCCCCGGCCTGCTGGACGGCGACGTGCGCGAGCTGACCTGGGCCGACGTCGAGGGCTGGGTCGGTGATGGCGGCGCCCAGCTGGGCACGCGCCGCGAGGTGCCCACCATTGAGCAGCTCTACGCGCTGGGGCGGGCCATCGAGCTCCATGAGATCGACGCCCTGCTGGTCATCGGCGGCTACAACGCCTACCTGAGCGCCTACCGCCTGGTCACCGAGCGGGACCGCTACCCCGCCTTCCAGATCCCGATCGTGTGCGTGCCGGCCTCCATCGACAACAACCTGCCCGGCTCCGAGCTGAGCATCGGCACCGACACGGCCCTCAACAACGCGGTGGTGGCACTGGACTCCATCAAGCTCTCCGCGGCGGCCTCCCACCGCTGCTTCGTCGCCGAGGTCATGGGCCGCAAGTGCGGCTACCTGTCCCTGATGTCGGGCCTGGCCACCGGCGCGGAGAAGGTCTACCTCAACGAGGAGGGCATCACGCTGGCGGGCCTGGCAGCGGACTCCGAGCGGATGGTGGAGTCCTTCCGCTCGGGCCGCAGCCTCTACCTGGTGATCCGCAACGAGCGGGCCAGCGTCAACTACACCACCGACGTCCTGGCCCACATCTTCGCCGAGGAGGGCAAGGGCCTCTACGACGTGCGCGAGGCGATCCTGGGTCACCAGCAGCAGGGAGGCAGCCCCACGGCCTTCGACCGGATCATGGCGACCAAGCTAGTCGCCCACTCCCTGGAACTGCTGGCCTGCGCACTCAAGCGCGGTGAGCCGACGGCCTCCTACGTGGGCCTGATGGGGGGCAAGGTCTCCGACCAGCCCCTGGACCGCATGAACGACGACCTCGACCGCGACCACCGTCGCCCCCGCCACCAGTGGTGGCTGGGTCTGCGCCCCGCCGTGGGCCTGGTCAGCCAGGACATCGGGACCCTGACGCTTCAGGACGTGCCCGACTTCGGTGAGGCGGTCGACGACGCGGCCAGCTGA","MPAAMSSDTADTVPSPTGSSAGPLLGLDGEPLRIGVLTSGGDAQGMNAAVRAVVRTAIRLGARPYAVMEGWAGAVAGGDGIRPLEWDSVGSILQRGGTIIGTARSAEFRERAGQLAAARNLLEHGIDRLVVIGGDGSLTGTNEFRKNWPSLLEELVETGDISAETAAAHPVLMVTGLVGSIDNDLVGADMTIGTDSALHRILEAIDDISSTAASHQRTFVVEVMGRHCGYLALMAAVAGGCDYVLVPELPPGKDWEEDMCSKLKAGREAGRRESMVIVAEGATDREGNRITADDVRQVIADKLGEAARVTILGHVQRGGRPSAYDRWMSTLLGCAAAREVVSMEPGSEPVIIAERHNRIRRLPMMEQIAATRAVKDLVAAHDYLGAVQARGASFGRMLELFETMSTPPAEPATDTGSTPSTSDRPKRVAIIHAGGLAPGMNTAARAAVRLGIDHDFTMLGVYGGFPGLLDGDVRELTWADVEGWVGDGGAQLGTRREVPTIEQLYALGRAIELHEIDALLVIGGYNAYLSAYRLVTERDRYPAFQIPIVCVPASIDNNLPGSELSIGTDTALNNAVVALDSIKLSAAASHRCFVAEVMGRKCGYLSLMSGLATGAEKVYLNEEGITLAGLAADSERMVESFRSGRSLYLVIRNERASVNYTTDVLAHIFAEEGKGLYDVREAILGHQQQGGSPTAFDRIMATKLVAHSLELLACALKRGEPTASYVGLMGGKVSDQPLDRMNDDLDRDHRRPRHQWWLGLRPAVGLVSQDIGTLTLQDVPDFGEAVDDAAS$","6-phosphofructokinase","Cytoplasm","BcDNA.GH12192","phosphofructokinase; platelet ","6-phosphofructokinase","","Lorberg A., Kirchrath L., Ernst J.F., Heinisch J.J. Genetic and biochemical characterization of phosphofructokinase from the opportunistic pathogenic yeast Candida albicans. Eur. J. Biochem. 1999. 260(1):217-226. PMID: 10091602Elson A., Levanon D., Brandeis M., Dafni N., Bernstein Y., Danciger E., Groner Y. The structure of the human liver-type phosphofructokinase gene. Genomics 1990. 7(1):47-56. PMID: 2139864Ronimus R.S., Morgan H.W. The biochemical properties and phylogenies of phosphofructokinases from extremophiles. Extremophiles 2001. 5(6):357-373. PMID: 11778837Heinisch J., Kirchrath L., Liesen T., Vogelsang K., Hollenberg C.P. Molecular genetics of phosphofructokinase in the yeast Kluyveromyces lactis. Mol. Microbiol. 1993. 8(3):559-570. PMID: 8326866","","","

InterPro
IPR000023
Family

Phosphofructokinase
PD000707	$\"[174-232]T$ $\"[551-606]T$	Q6A5J4_PROAC_Q6A5J4;
PR00476	$\"[36-55]T$ $\"[61-74]T$ $\"[125-141]T$ $\"[175-192]T$ $\"[193-211]T$ $\"[213-229]T$ $\"[231-248]T$ $\"[270-282]T$ $\"[304-326]T$	PHFRCTKINASE
PTHR13697	$\"[172-762]T$	PHOSPHOFRUCTOKINASE
PF00365	$\"[33-342]T$ $\"[426-714]T$	PFK
PS00433	$\"[308-326]T$ $\"[680-698]T$	PHOSPHOFRUCTOKINASE

InterPro
IPR009161
Family

6-phosphofructokinase, eukaryotic type
PIRSF000533	$\"[1-790]T$	ATP-dependent phosphofructokinase, eukaryotic type
TIGR02478	$\"[32-772]T$	6PF1K_euk: 6-phosphofructokinase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.450	$\"[29-251]T$ $\"[423-626]T$	no description

","BeTs to 14 clades of COG0205COG name: 6-phosphofructokinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0205 is ------yqvdrlbce-ghs--j-itwNumber of proteins in this genome belonging to this COG is 3","***** IPB000023 (Phosphofructokinase) with a combined E-value of 1.9e-64. IPB000023A 34-55 IPB000023B 195-248 IPB000023C 306-337 IPB000023A 428-449 IPB000023C 678-709","","","-58% similar to PDB:6PFK PHOSPHOFRUCTOKINASE, INHIBITED T-STATE (E_value = 2.3E_57);-58% similar to PDB:1MTO X-ray Crystal structure of a Phosphofructokinase mutant from Bacillus stearothermophilus bound with frutose-6-phosphate (E_value = 4.0E_57);-57% similar to PDB:3PFK PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL (E_value = 4.0E_57);-57% similar to PDB:4PFK PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL (E_value = 4.0E_57);-55% similar to PDB:1PFK CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS (E_value = 2.1E_50);","Residues 33 to 342 (E_value = 1.4e-168) place ANA_1379 in the PFK family which is described as Phosphofructokinase.Residues 426 to 714 (E_value = 9.9e-53) place ANA_1379 in the PFK family which is described as Phosphofructokinase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1380","1480864","1482177","1314","11.66","18.08","43852","ATGGTGCCTGGCGTGCGCGCGCTGATACGACCCCGGTTCCTTCTGGCTGCCGCCATGGCGGGAGTGGCCGCGGGCCTCATCGGGATCGCGATGGCACTGCTCCTGGAACTCTTCGAGTCACTGTTCTACGGCGTCGCCCACGGCGGGCTCCTGGAACGCCTGGCCACCGCCCCGCCCTGGCGGCGCGCGCTCGCCCCGGCCCTGGGCGGCCTTGTCGCCGGCGGCTTGTGGTGGTGGCTGCGCGCCACCGGCGGGGTGGCGGACGTGGAGGCCGCGGTCGCGGACCGCAGTGGTCAGGCGGCTGCCCGGATGGGGCTGACGCGTCCCTTCCTCGACGCCGTCACCCAGGTCCTCACCGTCGGCGCGGGCAATTCGGTGGGCCGCGAGGGCGCCCCGCGTCTGGCCGCCGGGGCGGTGGCGGCCAGGCTCGCCATCCGCCTGGGGATCGGCAGGAGTGAGGGCGCGATCCTCATTGCCTCCGCCGCCGGGGCGGGACTGGCGGCCATGTACAACGCGCCGCTGGGAGGGGCCGCCTACGCCGTCGAGCTCATCATGGTCGCCGGGATGCGACGGCGCGGTGCCCTCGTGGCGGTACCGGTGTGCCTCATCGCCATGCTCGTCTCCTGGCTGCACTCCCACGGGCACCCCACCTTCGAGATCGCCTCGCCTGGGTTGTCGTCAGGGACCGCCCTCGGGCTGGTCCTGCTCGTGCCCGTGGCCGCAGCAGTCGGTGTGGGGGCGAGGCGACTGTGGTCGTGGATGCTGGCGCACCGGTTGCGCGTCCCCCGGTGGCTGCCTGCGGCGATCGGTGCGGCGGGACTGGTCACCGGGCTGGCGAGCCTGTGGGTCCCGCCGATCGTCGGCAATGGCCGTGACGCCATGGAGATGGCTCTGGGTACTGGCCTTCCCGGGGCCTCGAACAGCCCTGTGGGAGCGGGCCTAGTCCTGCTGGTGGGCATCGTGGTCCTTAAGCCGGTCCTCACCGGTCTCACGCTCGCAGCCGGTGCCACCGGCGGCAGGCTAGCCCCCTCCCTGGCCGCGGGCTCGAGCGCCGGAGCCGCCCTGGCGATCGCGCTCGACGCCTGTGGGGTGCAGGCCAGCGTGGCGGTCCTGGCACTGGCGGGGGCCGGCGCGGTGCTCGCCACCACTCAGAGGGCCCCCGTCTTCGGGATCGTCTTCACCTGGGAGCTGGCCCGAGCCGGTGCCTGGACGCTGGTGGCCCTGTTCGCCGTCGTCGTGGCGGTCACGCTGCTGACTTCCCCCGCCTGGCGGAACGCCGAGGTCTTGCGGCTGCGGACCTCACGGAGTCGGTAG","MVPGVRALIRPRFLLAAAMAGVAAGLIGIAMALLLELFESLFYGVAHGGLLERLATAPPWRRALAPALGGLVAGGLWWWLRATGGVADVEAAVADRSGQAAARMGLTRPFLDAVTQVLTVGAGNSVGREGAPRLAAGAVAARLAIRLGIGRSEGAILIASAAGAGLAAMYNAPLGGAAYAVELIMVAGMRRRGALVAVPVCLIAMLVSWLHSHGHPTFEIASPGLSSGTALGLVLLVPVAAAVGVGARRLWSWMLAHRLRVPRWLPAAIGAAGLVTGLASLWVPPIVGNGRDAMEMALGTGLPGASNSPVGAGLVLLVGIVVLKPVLTGLTLAAGATGGRLAPSLAAGSSAGAALAIALDACGVQASVAVLALAGAGAVLATTQRAPVFGIVFTWELARAGAWTLVALFAVVVAVTLLTSPAWRNAEVLRLRTSRSR$","Voltage-gated chloride channel","Membrane, Cytoplasm","Voltage gated chloride channel superfamily","hypothetical protein predicted by Glimmer/Critica","Cl- channel, voltage-gated family protein","","Jentsch T.J., Gunther W. Chloride channels: an emerging molecular picture. Bioessays 1997. 19(2):117-126. PMID: 9046241Jentsch T.J., Steinmeyer K., Schwarz G. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature 1990. 348(6301):510-514. PMID: 2174129Schmidt-Rose T., Jentsch T.J. Transmembrane topology of a CLC chloride channel. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(14):7633-7638. PMID: 9207144Lehmann-Horn F., Mailander V., Heine R., George A.L. Myotonia levior is a chloride channel disorder. Hum. Mol. Genet. 1995. 4(8):1397-1402. PMID: 7581380Lloyd S.E., Pearce S.H., Fisher S.E., Steinmeyer K., Schwappach B., Scheinman S.J., Harding B., Bolino A., Devoto M., Goodyer P., Rigden S.P., Wrong O., Jentsch T.J., Craig I.W., Thakker R.V. A common molecular basis for three inherited kidney stone diseases. Nature 1996. 379(6564):445-449. PMID: 8559248","","","

InterPro
IPR001807
Family

Chloride channel, voltage gated
PR00762	$\"[112-131]T$ $\"[163-182]T$ $\"[336-356]T$ $\"[369-385]T$	CLCHANNEL
PTHR11689	$\"[8-417]T$	CHLORIDE CHANNEL

InterPro
IPR014743
Domain

Chloride channel, core
PF00654	$\"[65-422]T$	Voltage_CLC

noIPR
unintegrated

unintegrated
G3DSA:1.10.3080.10	$\"[12-419]T$	no description
PTHR11689:SF14	$\"[8-417]T$	VOLTAGE-GATED CLC-TYPE CHLORIDE CHANNEL ERIC
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[60-80]?$ $\"[193-211]?$ $\"[225-245]?$ $\"[266-286]?$ $\"[305-323]?$ $\"[325-347]?$ $\"[353-371]?$ $\"[373-393]?$ $\"[399-419]?$	transmembrane_regions

","BeTs to 3 clades of COG0038COG name: Chloride channel protein EriCFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0038 is aompkzyq-drlbce-gh-n-j----Number of proteins in this genome belonging to this COG is 2","***** IPB001807 (Chloride channel signature) with a combined E-value of 1.1e-14. IPB001807B 112-131 IPB001807C 163-182 IPB001807D 336-356 IPB001807E 369-385","","","No significant hits to the PDB database (E-value < E-10).","Residues 65 to 422 (E_value = 2.4e-07) place ANA_1380 in the Voltage_CLC family which is described as Voltage gated chloride channel.","","gated chloride channel superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1381","1482278","1483141","864","10.30","8.10","30344","ATGGATCGTCTCCACGACGCCGCACCACCTCGTCACGCACTACAGCCCAGCGCGGCTGACGCCTACGCCTTCGAGATCGGACGGCCCGCAGCCTCTGAGGGCACCGCCCTTGCCGCCGTCGCCCTGCTGGCCGGCGCGCCGGCGCTGGGCACGGCCCTGGCGCTCCTGCGGGGGCCGTGGATTCTCATGCTCGTCCTCCTTCACGTCGGCGGGCTCGCCCTGTGGTTCGGACTGTCCGGCCGAGGCTGGCGCGATCTGCTGACCGGTGGCGGCATCCGCAGCAGAACCGTCCTGTTCGCCGCTGGCGCCCTGGGCGGAGTCGCCTTCGGCGGCCTGCACACCTGGATGGGGCCGACGGGTACCGGCCCGCTGTGGAAGCCGGAGATCACCGCCTCCACGGTGCTTCACGCACTGGTCTTCGCCCTGACAGTCGGCGTCGCCTACAACGCGATCCCCGAGGAGATCACCCTCAGGCGCACCCTGTTCTCACCGATACACGAGCGCTACGGGCCAGCGGCTGCTGTGCTGATGACGACGGCGTCCTTCACCGCCCTGCACCTGCCGACCTGGCTGACCTCCGACACCAGCCTCAAGGGCTACGCCTGGCAGATCCTCCACAAGGTGCTCTTCGGGCTGCTCGCCGGCTGGTCGGTGGTGCGGCTGCGGTCGATGTTCTTCGCCCTGGGCCTGCACGTCAGCGGAAACACGCTGGGACTGTTCATCGGCCAGCTCCAGAGCGAGAACCTGCCCGACTTCGAACTTTCGTGGCTCAACGCGGCGATCCTGCTCACCGGCGCAGCCGCGGTCGCCGCCCTCATCCTCCTCCTGGGCCGACGTAGAAGAGTGCCACCACCAGTCTTCTAA","MDRLHDAAPPRHALQPSAADAYAFEIGRPAASEGTALAAVALLAGAPALGTALALLRGPWILMLVLLHVGGLALWFGLSGRGWRDLLTGGGIRSRTVLFAAGALGGVAFGGLHTWMGPTGTGPLWKPEITASTVLHALVFALTVGVAYNAIPEEITLRRTLFSPIHERYGPAAAVLMTTASFTALHLPTWLTSDTSLKGYAWQILHKVLFGLLAGWSVVRLRSMFFALGLHVSGNTLGLFIGQLQSENLPDFELSWLNAAILLTGAAAVAALILLLGRRRRVPPPVF$","CAAX amino terminal protease","Membrane, Extracellular","CAAX amino terminal protease family family","hypothetical protein predicted by Glimmer/Critica","Abortive infection protein","","O'connor L., Coffey A., Daly C., Fitzgerald G.F. AbiG, a genotypically novel abortive infection mechanism encoded by plasmid pCI750 of Lactococcus lactis subsp. cremoris UC653. Appl. Environ. Microbiol. 1996. 62(9):3075-3082. PMID: 8795193Diep D.B., Havarstein L.S., Nes I.F. Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J. Bacteriol. 1996. 178(15):4472-4483. PMID: 8755874","","","

InterPro
IPR003675
Family

Abortive infection protein
PF02517	$\"[139-242]T$	Abi

noIPR
unintegrated

unintegrated
tmhmm	$\"[34-54]?$ $\"[60-80]?$ $\"[95-115]?$ $\"[134-152]?$ $\"[173-193]?$ $\"[199-219]?$ $\"[224-244]?$ $\"[254-276]?$	transmembrane_regions

","BeTs to 4 clades of COG1266COG name: Predicted metal-dependent membrane proteaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1266 is -om-kz-qvdrlbcefg----j-it-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 139 to 242 (E_value = 0.00056) place ANA_1381 in the Abi family which is described as CAAX amino terminal protease family.","","amino terminal protease family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1382","1483682","1483404","279","9.69","4.38","10549","GTGCGATTGGATGAGGTCATTGTTCACCCGCGTGTCCACGAGCGCCACCCCGAGGTGAGTGTCGAGGATGTGCTGTCCGCCTGGAAGCATGCGATCCGTTCTGCGCCTCGGGTGGACGACTCTCGCACATGGGTTTCAGTGGGAGTGGACGTCAAGGGGCGGTTGCTGGAGATGGTTGCTGTTCATAATGGGCGTGGAGACTGGCTTGTTTATCATGCTATGACGCCGCCCTCGAAAAAGACTCTCAAGGAACTATCTATCGACAGGAGGAGATCATGA","VRLDEVIVHPRVHERHPEVSVEDVLSAWKHAIRSAPRVDDSRTWVSVGVDVKGRLLEMVAVHNGRGDWLVYHAMTPPSKKTLKELSIDRRRS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1384","1485767","1483899","1869","5.04","-34.18","68601","GTGACCTCTCCCGCGCCCCTTGTTGTCTCTGCCCACCACGTCGGCGATGATCCGGACTGGTGGCGCCGCGCCGTCGTCTACCAGGTCTACCCCCGCTCCTTCGCCGACTCCGACGGCGACGGCGTCGGCGACATCCCCGGCATCACCGCCCGCCTCGACCACCTCGACGAGCTGGGCGTCGACGTCGTGTGGCTCAGCCCCGTCTACCGCTCCCCTCAGGACGACAACGGCTACGACATCTCCGACTACCAGGACATCGACCCCCTCTTCGGATCCCTGACCGACCTCGACGCCCTCATCGAGGGACTGCACTGTCGCGGCATGCGCCTGGTCATGGACCTCGTCGTCAACCACACCAGCGACGAGCACCCCTGGTTCACCGCCAGCCGCTCCTCCAAGGACGACCCCAAGCGCGACTGGTACATCTGGCGGCCCGCCCGGCAGGTTGACGGGCTCTCCCCCGGGCAGCCGGGCACCGAGCCCACCAACTGGGGATCGGCCTTTTCCGGGTCGGCCTGGGCCTGGGATGAGGAGAGCCAGGAGTTCTACCTGCACCTCTTCTCACCCAAGCAGCCCGACCTCAACTGGGAGAACCCGCAGGTGCGCCGCGCCATCCACGAGATGATGACCTGGTGGCTGGACCGCGGCGTCGACGGCTTCCGCATGGACGTCATCAACCTCATCTCCAAGACCTACCCGCTCACTGACGCACCCCAGGGCGAGGGCGACCTCTACGGCAACGCCTTCGCCGCCGTTGCCAACGGCCCCCGCATCCATGAGTTCCTGCACGAGATGAACCAGCAGGTCCTCGCACCGCGGTCCAGTCACGTCATCACCGTCGGGGAGATGCCCGGGGCCACGAGCGCCGAGGCCGCCCTCTACACCGACCCCGCCCGAGGTGAGCTCGACATGGTCTTCCAGTTCGAGCACGTCAGCCTCACCGACGGCCCCGGAGGCAAGTTCGACCCCCAGCCCCTCGAGCTCGTCACCCTCAAGCAGAACCTGGCCCACTGGCAGGCCGCCCTCGCTCCCGACACGACCCCCAACGGCGCCGTGAGCGCGGAGAAGGGATGGAACTCCGCCTACTGGGACAACCACGACCAGCCCCGCGCCGTCTCCCGTTTCGGCGATGACGACCCCGCCTGGCGCGTCCGCTCGGCCAAGACCCTCGCCACGATCCTCCACGCCCACCGCGGCACCCCCTACATCTACCAGGGCGAGGAGCTGGGCATGGCCAACACGGTCTTCCGCTCCATCGATGACTACCGGGACCTGGAGTCCGTCAACCACTTCCACGAGCGTGTCCGCGCCGGCGACGACCCGGCCGCCGTCCTGGCCGGCATCGCCCCCGTCTCCCGGGACAACGCCCGCACCCCCGTCCACTGGGACAGCAGCGAGAAGGCCGGGTTCACCACCGGCGAGCCCTGGATCGCCCTGGCCCCCGACCACGGCACCGTCAACGCCGCCGCCCAGGTGGGAGTACCTGGCAGCGTGTTCGAGCATTACCGTCGCCTCATCGCCCTGCGGCACGATGACGACGCCCTCGCCCTGGGCACCTTCCGGCTCCTGGCGGCCGACCACCCCACCGCCTGGGTCATCCTGCGTCAGTGGCGCGCCCCTGAGGCCCAGGGCGGCGGCATCGAGCAACTCCTGCTCATCGCCCAGTGCGCCCGTGAGGACTTGCCCCTGACCGGGCAGGGCGGCCTGCTGGCGGCGCTCGCGGCCGAGGGCCTGGAGCCAGGGGAGTGGAGCGGGGCCGAGCAGGTGCTGCGCGCCGCCGATCCGGACGTTCAGCCCGGCTCGACCCACGCGGGCCTGCCGGAGGCGCTACCGGGATGGGACTCGGTCCTGCTGCGCCGTCGTCGTTGA","VTSPAPLVVSAHHVGDDPDWWRRAVVYQVYPRSFADSDGDGVGDIPGITARLDHLDELGVDVVWLSPVYRSPQDDNGYDISDYQDIDPLFGSLTDLDALIEGLHCRGMRLVMDLVVNHTSDEHPWFTASRSSKDDPKRDWYIWRPARQVDGLSPGQPGTEPTNWGSAFSGSAWAWDEESQEFYLHLFSPKQPDLNWENPQVRRAIHEMMTWWLDRGVDGFRMDVINLISKTYPLTDAPQGEGDLYGNAFAAVANGPRIHEFLHEMNQQVLAPRSSHVITVGEMPGATSAEAALYTDPARGELDMVFQFEHVSLTDGPGGKFDPQPLELVTLKQNLAHWQAALAPDTTPNGAVSAEKGWNSAYWDNHDQPRAVSRFGDDDPAWRVRSAKTLATILHAHRGTPYIYQGEELGMANTVFRSIDDYRDLESVNHFHERVRAGDDPAAVLAGIAPVSRDNARTPVHWDSSEKAGFTTGEPWIALAPDHGTVNAAAQVGVPGSVFEHYRRLIALRHDDDALALGTFRLLAADHPTAWVILRQWRAPEAQGGGIEQLLLIAQCAREDLPLTGQGGLLAALAAEGLEPGEWSGAEQVLRAADPDVQPGSTHAGLPEALPGWDSVLLRRRR$","Alpha amylase","Cytoplasm","oligo-1,6-glucosidase","oligo-1;6-glucosidase ","alpha amylase, catalytic region","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[28-432]T$	Alpha-amylase

InterPro
IPR006589
Domain

Glycosyl hydrolase, family 13, subfamily, catalytic region
SM00642	$\"[28-457]T$	Aamy

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[16-518]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[17-317]T$ $\"[359-537]T$	AMYLASE
PTHR10357:SF11	$\"[17-317]T$ $\"[359-537]T$	ALPHA-AMYLASE

","BeTs to 10 clades of COG0366COG name: GlycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0366 is ---p--y-vdrlbcefg----j----Number of proteins in this genome belonging to this COG is 7","***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 5.9e-29. IPB006589A 50-67 IPB006589B 90-118 IPB006589C 216-227 IPB006589D 361-370***** IPB004185 (Glycoside hydrolase, family 13, N-terminal Ig-like domain) with a combined E-value of 1.7e-27. IPB004185B 39-72 IPB004185C 77-108 IPB004185D 109-148 IPB004185H 386-431 IPB004185A 18-50***** IPB005323 (Bacterial pullanase-associated domain) with a combined E-value of 6.4e-07. IPB005323B 107-119 IPB005323C 211-222***** IPB004193 (Glycoside hydrolase, family 13, N-terminal) with a combined E-value of 1.6e-06. IPB004193D 104-118 IPB004193E 210-223***** IPB006046 (Alpha-amylase signature) with a combined E-value of 2.7e-06. IPB006046B 107-118 IPB006046C 217-228","","","-69% similar to PDB:1UOK CRYSTAL STRUCTURE OF B. CEREUS OLIGO-1,6-GLUCOSIDASE (E_value = 9.7E_165);-62% similar to PDB:1ZJA Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 (triclinic form) (E_value = 1.5E_125);-62% similar to PDB:1ZJB Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 (monoclinic form) (E_value = 1.5E_125);-58% similar to PDB:1M53 CRYSTAL STRUCTURE OF ISOMALTULOSE SYNTHASE (PALI) FROM KLEBSIELLA SP. LX3 (E_value = 3.5E_114);-58% similar to PDB:1WZA Crystal structure of alpha-amylase from H.orenii (E_value = 6.3E_39);","Residues 28 to 432 (E_value = 2.1e-118) place ANA_1384 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.","","(1) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1385","1485921","1488533","2613","5.41","-32.23","95295","ATGAGTTCTCGCGCCTCACTCGGGGCGCCGCCTCTCCCACCGCTCCCCACGACGACTCCTGCTGTGAAAGGCCGACCGTTGGTTTCTCCTCTCCGCGATGCCCCTGACACTCCGCGTCCGGCCGCTGCCCGCCCTGAGGCGGTCATCGCCGGGACCTCGTCGGAGGAGTCCCGCTACCGGTTCACGGTGCTCACCTCTCGGCTCATCCGCATGGAGCACTCCCCCACGGGCGTCTTCACCGATGCCGCCACCCAGCTGGTCGTCAGCCGCGACCTGGGTGAGACGCCGTCGTTCCGGGTGGTGCACGGCCAGGACCGTCTGGAGATCATCACCGAGCACCTGCACCTGACCCATGTGCCTTCCCTGGGCTTCTCCCCCGCCGGGCTCAGCGTCAGGCTGCGCTCGACGGCGCTGCACGCCCATGGCGGCACCTGGCACCACGGCGACGTGTGGGATCCGGGCGAGACCTTCCCGACGAACCTGGGCGGCACCACCCGCACCCTTGATGAGGCCGACGGCGCCGTCGCCCTCGGTCCGGGCCTGCTGAGTCTCAACGGCATCACCGCCCTGGACGACTCGGCCTCGCTGCTGCTCACCCAGGACGAGTGGGTCCAGCCCCGTGAGCCCGGCAACCGCCTGTCCGACGGGGCGCAGGACCTCTACGTCTTCGGCTACGGCCAGGACTACCAGGAGGCACTGCGGGACTTCTTCGGCCTCACCGGGCCGAGCCCCCTCATCCCGCGGGCGCTGCTGGGCAACTGGTGGAGCCGCTACCACCCCTACAGCGACCAGGAGTACCTGGCGCTCATGGACCGCTTCGCCGCCGAGGAGCTGCCCTTCTCGGTGGCCGTCATCGACATGGACTGGCACGTCACCGACATCGACCCGGCGATCGGCACGGGATGGACCGGCTACACCTGGAACCGGGAGCTGTTCCCGGACCCGGCGGCCTTCCTGGCCGGCCTGCACGAGCGGGGCATGCTCACCACGCTCAACGTGCACCCGGCCCAGGGGGTGCGTCGCCACGAGGAGGCCTATGAGGAGGTCTGCGCCGACCTGGGCCTGGATGCGAGCACCGGGGAGGACGTGCCCTTCAACATCGCCGACCGGGACTTCGTGGGCTCCTACCTCTCGCGCCTCCACCATCCCCTGGAGGACGAGGGTGTGGACTTCTGGTGGCTGGACTGGCAGCAGGGCGGCTCCACGACGGTTCCCGGACTGGACCCGCTGTGGATGCTCAACCACGTCCACTACCTCGACTCGGGCCGCGAGCGCCCGGCGGCCGACGGTGGCGTGGAGCGGCGCCGCCCGGTGACCTTCTCGCGCTTCGCCGACGCCTCGAGCCACCGCACCCCGGTGGGCTTCTCCGGGGACACGATCATCAGCTGGGACTCCCTGCGCTTCCATCCGCGCTTCACGGCCACGGCCGCCAACATCGGCTACTTCTGGTGGTCCAACGACATCGGCGGGCACATGATGGGCGGCAGCGACGACGCGATGGCGGCCCGCTGGTTCCAGCTGGGCTGCTTCTCCCCCATCAACCGCCTGCACTCGTCGAACTCAGGCTTCACCTCGAAGGAGCCGTGGCGCTACTCGCGTGACGCGCGCGCCACGATGGAGGCGCACCTGCGGCTGCGTCACCGGCTGGTGCCCTACCTGTACACGTGGGCGCGCCGCTCGGCGGGTGAGGGCATCGCTCCGGTGCGCCCGGTGTACCACGACCACCCACGCGAGCTGGCCGCCTACGAGCACCGGGGCAGCTTCTGCTTCGGGGACCTGCTGGTGGTGCCCTTCACCTCCCCGCTCGATGCGACCACCGGCCTGGGGCGGGAGCTGACCTGGCTGCCCGACGGCGTCTGGTACGACCTGCCCACGGGGCGCCGCTATGAGGCCACCACCGGTGGGCGCGGTCGCATGCTGAGCCTGTCGCGCCCCCTGGACCGGATCGGGGTGCTGGCCCGGGCGGGCTCCGTGATCCCCCTGGCCGGGAACCTGACGGAGGCGGCCGGGGACAATCCGCGTGAGCTGGAGATCGTCGTCGTGCCCGGGGGCTCGGGGAGCTTCACCTTGGAGGAGGACGACGGCTCGGCCCAGCCCGGGCAGGACCAGATCGCCCGCACCCACATGGCGCTGACCTGGCCCGAGGCCGAGGAGGAGGACGGCGCCGACGTGGTGCTGCGCATCCGCCTGGAGGGGGCGGCCGAGGTCGTGCCGGCCTCGCGGCTGGTGACGGTGCGACTCCTGGCCGGCCAGGTGGCCGGAGCCTGGCTGGGGGTGGGTGAGCGGGCGCGCCGGCTGGCCACCGAGGAGGTCAGCGGTGACGGCTTCACCCTGGGGGCCGGGACGCTGGTGCACCTGGAGGAGCTCAGCCGCCAGGAGCTCATCGACGGCGTCCAGCTGGTCCTTCGCGGCACGAAGCACTCCCCAGCCGACTGGCGCGATGAGGTCCACGCAATCCTGGACGCCGCGCGTGTGGAGTACATGGCCAAGGACCTGGCTTGGGACGCGGTGCAGCGGGGCCTGAGCGGAACCGCCCTGCTGGGTGAGCTCGAGGCCCTGGGCCTGCCGGAGACGCTGCGGGCGGCCGTGTCCGAGGTGCTCCCCCACTCCTGA","MSSRASLGAPPLPPLPTTTPAVKGRPLVSPLRDAPDTPRPAAARPEAVIAGTSSEESRYRFTVLTSRLIRMEHSPTGVFTDAATQLVVSRDLGETPSFRVVHGQDRLEIITEHLHLTHVPSLGFSPAGLSVRLRSTALHAHGGTWHHGDVWDPGETFPTNLGGTTRTLDEADGAVALGPGLLSLNGITALDDSASLLLTQDEWVQPREPGNRLSDGAQDLYVFGYGQDYQEALRDFFGLTGPSPLIPRALLGNWWSRYHPYSDQEYLALMDRFAAEELPFSVAVIDMDWHVTDIDPAIGTGWTGYTWNRELFPDPAAFLAGLHERGMLTTLNVHPAQGVRRHEEAYEEVCADLGLDASTGEDVPFNIADRDFVGSYLSRLHHPLEDEGVDFWWLDWQQGGSTTVPGLDPLWMLNHVHYLDSGRERPAADGGVERRRPVTFSRFADASSHRTPVGFSGDTIISWDSLRFHPRFTATAANIGYFWWSNDIGGHMMGGSDDAMAARWFQLGCFSPINRLHSSNSGFTSKEPWRYSRDARATMEAHLRLRHRLVPYLYTWARRSAGEGIAPVRPVYHDHPRELAAYEHRGSFCFGDLLVVPFTSPLDATTGLGRELTWLPDGVWYDLPTGRRYEATTGGRGRMLSLSRPLDRIGVLARAGSVIPLAGNLTEAAGDNPRELEIVVVPGGSGSFTLEEDDGSAQPGQDQIARTHMALTWPEAEEEDGADVVLRIRLEGAAEVVPASRLVTVRLLAGQVAGAWLGVGERARRLATEEVSGDGFTLGAGTLVHLEELSRQELIDGVQLVLRGTKHSPADWRDEVHAILDAARVEYMAKDLAWDAVQRGLSGTALLGELEALGLPETLRAAVSEVLPHS$","Alpha-glucosidase","Cytoplasm, Extracellular","possible xylosidase or glucosidase","alpha-glucosidase; family 31 of glycosyl hydrolase","glycoside hydrolase, family 31","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR000322
Family

Glycoside hydrolase, family 31
PTHR22762	$\"[72-661]T$	ALPHA-GLUCOSIDASE
PF01055	$\"[221-659]T$	Glyco_hydro_31

noIPR
unintegrated

unintegrated
PTHR22762:SF3	$\"[72-661]T$	gb def: Hypothetical protein

","BeTs to 5 clades of COG1501COG name: Alpha-glucosidases, family 31 of glycosyl hydrolasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1501 is ---p--y-v--lb-e------j----Number of proteins in this genome belonging to this COG is 1","***** IPB000322 (Glycoside hydrolase, family 31) with a combined E-value of 1.7e-10. IPB000322B 235-260 IPB000322E 545-578","","","-39% similar to PDB:1WE5 Crystal Structure of Alpha-Xylosidase from Escherichia coli (E_value = 3.1E_18);-39% similar to PDB:1XSI Structure of a Family 31 alpha glycosidase (E_value = 3.1E_18);-39% similar to PDB:1XSJ Structure of a Family 31 alpha glycosidase (E_value = 3.1E_18);-39% similar to PDB:1XSK Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate (E_value = 3.1E_18);-39% similar to PDB:2F2H Structure of the YicI thiosugar Michaelis complex (E_value = 3.1E_18);","Residues 221 to 659 (E_value = 2.3e-84) place ANA_1385 in the Glyco_hydro_31 family which is described as Glycosyl hydrolases family 31.","","xylosidase or glucosidase (xylS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1386","1488613","1489278","666","4.83","-12.73","23743","ATGAGTGAGACCCCCGCCCCGCGCTTCCCGGAGGCCGAGCCCTACTTCGTGGGCGACGAGCGCACCAATCGCGAGCGCATGCTCGCCGGTGACTGGTACGTCGCCGACGACCCCGATAACGCCAGGATCGCCGCCCACGCCCGCACAATGCTCTACCGCTTCGAGCGGGCCTTCGCCGAGGGCGAGGAGGACTGTTGGGATCTGCTGCGCTCCGCGATCCCGGGGCTGGGCGACAAGGCTCACCTGCTGCCGCCGGTGCGCGTGGACTACGGGGACAACATCTCCGTGGGTGAGGGGACCTTCGTCAACTACGGGCTCGTGGCCCTCGACGTCGCCCAGATCAGTATCGGCGCGCACTGCCAGATCGGCCCGAACGTCCAGCTGCTCACACCGGTCCACCCCCTGGAGCCGACACCGCGCGCCTGCTCCCTGGAGGCGGCCGACCCCATCACGATCGGGGACAACGTGTGGCTGGGCGGCGGGGTCATCGTCTGCCCCGGCGTGACCATCGGGGACAACTGCGTCATCGGCGCGGGCTCGGTAGTCACCAAGGACATTCCCGCCAGCAGCCTGGCCGTGGGCAACCCGGCCCGGGTCCTGCGCCAGCTGGACGACTCCACCTTCGGCCCCCGCCATCAGCACCCGCCTCAGGAGACGCCGCAATGA","MSETPAPRFPEAEPYFVGDERTNRERMLAGDWYVADDPDNARIAAHARTMLYRFERAFAEGEEDCWDLLRSAIPGLGDKAHLLPPVRVDYGDNISVGEGTFVNYGLVALDVAQISIGAHCQIGPNVQLLTPVHPLEPTPRACSLEAADPITIGDNVWLGGGVIVCPGVTIGDNCVIGAGSVVTKDIPASSLAVGNPARVLRQLDDSTFGPRHQHPPQETPQ$","Maltose transacetylase","Cytoplasm, Extracellular","maltose transacetylase","maltose transacetylase ","transferase hexapeptide repeat containing protein","","Raetz C.R., Roderick S.L. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 1995. 270(5238):997-1000. PMID: 7481807Wang X.G., Olsen L.R., Roderick S.L. Structure of the lac operon galactoside acetyltransferase. Structure 2002. 10(4):581-588. PMID: 11937062Iverson T.M., Alber B.E., Kisker C., Ferry J.G., Rees D.C. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 2000. 39(31):9222-9231. PMID: 10924115Beaman T.W., Vogel K.W., Drueckhammer D.G., Blanchard J.S., Roderick S.L. Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. Protein Sci. 2002. 11(4):974-979. PMID: 11910040","","","

InterPro
IPR001451
Repeat

Bacterial transferase hexapeptide repeat
PF00132	$\"[113-130]T$ $\"[149-166]T$ $\"[167-184]T$	Hexapep

noIPR
unintegrated

unintegrated
G3DSA:2.160.10.10	$\"[65-205]T$	no description
PTHR23416	$\"[150-204]T$	SIALIC ACID SYNTHASE-RELATED
PTHR23416:SF7	$\"[150-204]T$	NEUD PROTEIN

","BeTs to 10 clades of COG0110COG name: Acetyltransferases (the isoleucine patch superfamily)Functional Class: RThe phylogenetic pattern of COG0110 is -Mt-y-vCEBR-------in-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-60% similar to PDB:2IC7 Crystal Structure of Maltose Transacetylase from Geobacillus kaustophilus (E_value = 7.3E_38);-60% similar to PDB:2P2O Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form (E_value = 7.3E_38);-62% similar to PDB:1OCX E. COLI MALTOSE-O-ACETYLTRANSFERASE (E_value = 3.6E_37);-59% similar to PDB:1KQA GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A (E_value = 8.6E_31);-59% similar to PDB:1KRR Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A (E_value = 8.6E_31);","Residues 163 to 180 (E_value = 180) place ANA_1386 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 199 to 216 (E_value = 216) place ANA_1386 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 217 to 234 (E_value = 0.0091) place ANA_1386 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).","","transacetylase ","","1","","","Mon Aug 6 10:22:30 2007","","Mon Aug 6 10:22:30 2007","","","Mon Aug 6 10:22:30 2007","Mon Aug 6 10:22:30 2007","Mon Aug 6 10:22:30 2007","","","Mon Aug 6 10:22:30 2007","","","Mon Aug 6 10:22:30 2007","Mon Aug 6 10:22:30 2007","","","Mon Aug 6 10:22:30 2007","Mon Aug 6 10:22:30 2007","","","","","yes","","" "ANA_1387","1489275","1489994","720","6.54","-1.65","26080","ATGAACCCCGAGACCTTTTCCGACCTGGCCGCTTCCCGGCACTCCGTGCGGGACTTCCGGGCTGATCCCGTACCACCTGAGGTCATCGAGGAGATCCTGGGGGATGCCCGCCAGGCACCGAGCTGGTCCAACACCCGCCCCTTCATGGTGGCGCTGGCCACCGGTGAGCAGGCGGACCGTCTGCGCGCGGCCTACGTCAAGGAGTTCGACGCCGCGCTCCCCCTCCAGCACAAGGAGCCTGGGGCGATGGCCCGCCTGGCCCTGAGCGGCAAGGCGCCCGACGGCGACTACCCGACCTGGGCGCCCTACCCCGCGGACCTGCTGCCCCACTCCCAGGCGGTCGGCGGCCGGCTGTACGCGCACATGGGTATCGGCCGCAAGGACCGCGAGGCCCGTGACGCGGCCGCCCGCCGCAACTGTGAGGCCTTCGGCGCCCCAGTCATCGGTTTCGTCCTGGTCCACGAGGGCCTCATGCCCTTCGCGGCGCTCGACGCCGGGATCATGCTGCAGACCCTGTTCCTGTCCGCCAAGGCCCACGGGGTCGACTCCTGTCCCCTGGGGGTCCTGGCCACGTGGCGCCGTCCCTTCGACGCCGAGTTCGAGGCGCCGTCGGACTACCGTCTCATCACGGGCTTCGCCCTGGGCTACGCCTCCGAGGCCCCCGTCAACGACTTCCGGGCCGAGCGGCGCCCCGTGCGCCTGGTGCCGAACCGCAGCTGA","MNPETFSDLAASRHSVRDFRADPVPPEVIEEILGDARQAPSWSNTRPFMVALATGEQADRLRAAYVKEFDAALPLQHKEPGAMARLALSGKAPDGDYPTWAPYPADLLPHSQAVGGRLYAHMGIGRKDREARDAAARRNCEAFGAPVIGFVLVHEGLMPFAALDAGIMLQTLFLSAKAHGVDSCPLGVLATWRRPFDAEFEAPSDYRLITGFALGYASEAPVNDFRAERRPVRLVPNRS$","Nitroreductase","Cytoplasm","nitroreductase family protein, putative","nitroreductase","nitroreductase","","","","","

InterPro
IPR000415
Family

Nitroreductase
PF00881	$\"[10-216]T$	Nitroreductase

noIPR
unintegrated

unintegrated
G3DSA:3.40.109.10	$\"[4-232]T$	no description

","BeTs to 11 clades of COG0778COG name: NitroreductaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0778 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000415 (Nitroreductase family) with a combined E-value of 4.1e-09. IPB000415A 39-62 IPB000415B 164-189","","","No significant hits to the PDB database (E-value < E-10).","Residues 10 to 216 (E_value = 6.3e-11) place ANA_1387 in the Nitroreductase family which is described as Nitroreductase family.","","family protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1388","1491143","1490142","1002","9.20","5.54","34906","ATGAACGCCCCGGCCTCCTTCCCGACTTCATCAGTGGAGCCGCGGGCTCCTCGCCTCCTGGACCGGCTCGTCCCGGCCAGTCCCCAGTGGCGCATTCCTCCGCGAAAGGCGGAGCGGCTCGGCTGGCTCCAGCTTCTTCTCGGAATTCCGATGATCTTCGTCGTTCAACTCGTCGCCGGGATTCTCGCAGTGATGACCGGATTCGCGCACCTGACGGCTAACGGTCGGCTTGATTCCCTGCCGGAAGCCTTATTCGTCATAGCTATCTTCGGTGCACCGCTGGCCCTGCTCGGGTACTGGCTGCTGGTGCACTTCGTCGGTGGCCGGCCCGTCATTGAGGTGGGCGGGCGTGGGGCAGCACTGCGCGAGTTCCTGGTCGGCCTGACCATAGGAGCGCTGCTCATGAGCGCCGTCATCGCGGTTCTGGCCCTGCTCGGTTCGTACCACGTGGTGGACGTCGGCTGGAGCACGGGGATCCTCGCCGGTCTAGGAGCCGGAGTCCTTGCCGGATTCACCGAGGAGATTCTGTTTCGAGGGATTCTGCTGCGCCTCATCGAGGGCTGGGTGGGGACCTGGTGGGCGCTGGCCATCACCTCGTTCCTCTTTGGAATCTCTCACCTGGGCAACGCTCATGCGACGGTCTTCGGTGCGGTGGCGATCGCGCTGGAGGCGGGCATCCTGCTGGGCGCCTGCTACCTGCTCACCCGTCGCCTGTGGCTGGCGATCGGGCTGCACGCCGCCTGGAACTTCGTCCAGGGCGGTATCTTCGGCTCCGACATCTCCGGCATCGGGTCGGGACGCGGACTCATCGAGGCCCGCTTCACCGGCCCCGACCTGCTCACCGGCGGAGTCATGGGAATCGAGGCCTCCGTCGTCGCGGTCGTGCTGTGCACGGCGGCCGGTCTGGCCATGCTGCTGGCGGTCCGCCGGCGCGGGCTCGTCGTCCCGCCCTGCTGGCACCGCCCGTCTCAGGCCGCACTGGACGGCACGCAGCCGGCCTAG","MNAPASFPTSSVEPRAPRLLDRLVPASPQWRIPPRKAERLGWLQLLLGIPMIFVVQLVAGILAVMTGFAHLTANGRLDSLPEALFVIAIFGAPLALLGYWLLVHFVGGRPVIEVGGRGAALREFLVGLTIGALLMSAVIAVLALLGSYHVVDVGWSTGILAGLGAGVLAGFTEEILFRGILLRLIEGWVGTWWALAITSFLFGISHLGNAHATVFGAVAIALEAGILLGACYLLTRRLWLAIGLHAAWNFVQGGIFGSDISGIGSGRGLIEARFTGPDLLTGGVMGIEASVVAVVLCTAAGLAMLLAVRRRGLVVPPCWHRPSQAALDGTQPA$","Abortive infection protein","Membrane, Cytoplasm","putative transmembrane protein","putative transmembrane protein","Abortive infection protein","","O'connor L., Coffey A., Daly C., Fitzgerald G.F. AbiG, a genotypically novel abortive infection mechanism encoded by plasmid pCI750 of Lactococcus lactis subsp. cremoris UC653. Appl. Environ. Microbiol. 1996. 62(9):3075-3082. PMID: 8795193Diep D.B., Havarstein L.S., Nes I.F. Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J. Bacteriol. 1996. 178(15):4472-4483. PMID: 8755874","","","

InterPro
IPR003675
Family

Abortive infection protein
PF02517	$\"[160-256]T$	Abi

noIPR
unintegrated

unintegrated
tmhmm	$\"[42-64]?$ $\"[83-103]?$ $\"[124-144]?$ $\"[154-172]?$ $\"[187-207]?$ $\"[213-233]?$ $\"[238-256]?$ $\"[286-308]?$	transmembrane_regions

","BeTs to 7 clades of COG1266COG name: Predicted metal-dependent membrane proteaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1266 is -om-kz-qvdrlbcefg----j-it-Number of proteins in this genome belonging to this COG is 2","***** IPB003675 (Abortive infection protein) with a combined E-value of 4.8e-08. IPB003675A 167-178 IPB003675B 196-216","","","No significant hits to the PDB database (E-value < E-10).","Residues 160 to 256 (E_value = 1.7e-20) place ANA_1388 in the Abi family which is described as CAAX amino terminal protease family.","","transmembrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1390","1494134","1491261","2874","5.31","-27.49","102697","ATGCCCGGCTCCGGCGGTGCGGCCACGCCGCCGCCCGAGGCCGCGCTGCCCGCCCTCATCCCCGCCGCAGGCTCCTTCGACGATGACTCCTGGGCCGACGTCGAGGCCCCGGAGGAGGACTGGGGGCCCGAGGACGCCCCACCGCCCGAGGACGAGTCCGCCGCAGCCCCCACCTGGGAGGAGCGTCAGGACGAGGTCTCCGCCCTGGTCGCCCGCGCCCAGGCCAATGCCGCCGCGGCCCGCGCCCGAGCCGACGGCGCCGCGCCCTCGGGCCAGCCCACCGGCCAGGCCTGGGGCGTGACGGTCTCAGACCCGGCCGAGCTCATCCGTGGCCTCAACCCCGCCCAGGAGTCCGCCGTCACCCACGCCGGCGCCCCCCTGCTCATCATCGCCGGCGCGGGCTCGGGCAAGACCCGGGTCCTGACCCACCGCATCGCCCACCTCATCGCCACCGGCCGCGCCCGCCCCGGCGAGATCCTGGCCATCACCTTCACCAACAAAGCCGCCGCCGAGATGCGCGAACGCGTCACCGCCCTGGTGGGCCCCGCCGGCGAGCGCATGTGGGTCTCCACCTTCCACTCCGCCTGCGTACGCATCCTGCGCCGCGAGCACGAGGCCGCCGGCCTGCGCTCCACCTTCTCCATCTACGATGCCGCCGACTCCACCCGCCTCATCACCCTCATCGTGCGTGAGCTGGGCATCGACCCCAAGCGCTTCACCCCCAAGACCTTCGCCCACCGCATCTCCGACCTCAAGAACGAGCTCATCACCCCGGCCCAGTTCGCCGAGCGGGCCGTCACCTCCAACCCCCTCGAGCGCCACCTCGCCGAGGTCTACCGCGCCTACGCCCAGCGCCTGAGCTCCGCCAACGCCCTGGACTTCGACGACATCATCATGCGCACCGTCGCCCTGCTCCAGACCCGCCCGGCCGTGGCCGAGATGTACCGGCGCCGCTTCCGCCACATCCTGGTCGACGAGTACCAGGACACCAACCACGCCCAGTACGTCCTCGTGCGCGAGCTCGTCGGCGGCCCCGGCACCTCCGGGGCAGGCTCGGCCCTGCCACCGGGCGAGCTCACCGTCGTCGGCGACTCCGACCAGTCCATCTACGCCTTCCGCGGCGCAACCATCCGCAACATCGAGGAGTTCGAGGAGGACTACCCCTCGGCCCGCACCATCCTGCTGGAGCAGAACTACCGCTCCACCCAGAACATCCTCTCGGCCGCGAACGCCGTCATCTCCCGCAACAGCGGCCGGCGCGAGAAGAACCTGTGGACCGCCGCCGGAGACGGCGCCCCCATCACCGGTTACGTCGCCGACTCCGAGCACGACGAGGCCCGCTGGATCAGCCAGGAGGTCGACCGCCTGGCCGACGAGCACGGCATACGCCCTCGCGACGTCGCCGTCTTCTACCGCACCAACGCCCAGTCCCGTGCCCTCGAAGAGGCCTTCATGCGCGCCGGCCAGCCCTACAAGGTCATCGGCGGCACCCGCTTCTACGACCGCCGCGAGATCAAGGACGCCATCGCCTACCTGCGCGCCGTCGACAACCCCGACGACGACGTCAACCTGCGCCGCATCCTCAACGTCCCCAAACGCGGCCTGGGTGACAAGGCCGAGGGCGCCCTGGCCGAGCACGCCGCCCGCTACGCCGTCTCCTTCGGGCAAGCCGTCGCCGACGCCGCCGGAGCCCCCCGTGAGGCTCAGACAGGCGAGACCGAGAACGCCGACGGACAGGCCTCCTCCTCCGGGGCCGGCGAGCCGCCCGAGGTCGAGGGCCTGACCACCCGGGCCCGCAACCAGGTGCGTGGCTTCCACGAGCTGCTCACCACCCTGCGTCACATGGTCACCGCCGGCGACGGCGTCGCCGATATCCTCGACTCCGCCCTGGACGCCTCGGGCTACCTCGCCGAGCTGCGCGCCAGCGACGACCCCCAGGACGCCACCCGCGTGGAGAACCTCGCCGAGCTCCACTCCGTGGCCAGCGACTTTCAGGCCGCCAACCCCGACGGCACCCTGGCCGACTTCCTCGAGCGCGTCTCACTCGTGGCCGACTCCGATCAGCTCCCGCCCAGCGCCGACTTGGAGGACGAGGATGCCCGGCAGGCCGAGGAGCAGGGCCAGATCACCCTCATGACCGTCCACACCGCCAAGGGCCTGGAGTTCCCGGTCGTCTTCGTCACCGGCATGGAGGACGGCACCTTCCCCCACAGCCGCTCCCTGGCCGAGGAGACCGAGCTCGCCGAGGAACGGCGCCTGGCCTACGTGGCCCTCACCCGTGCCCGCGAGCGCCTCTACCTCACCCGCGCCGCCGTGCGCTCGGCCTGGGGCGCCGCCAACGCCATGCCCGCCTCCCGCTTCCTCGACGACGTCCCGGATGAGACCATCGACTGGAAGCGCCTGGCCTCCTCCATGGAGGCGCTGCGCGGCGGCGGCACCGGCTGGGGCAGCAGCTGGGGCGAGGGCGGCTTCGGCTCGGGTGGGCGGCGCTCAGGCTCCTCCCGGCAGAGTACCTACTCCGACGACGATGACTTCGCCCCGCCCGTGGGCGCAGGAACCAAGCGCTCGGGCAGGCTGGGGCGCGTGGAGACCGCCCAGGACCGGGCTGCCAAGCGCACCTCCGCTCGCCTCGAGGCCCGCGGCAAGCAGAGCGCCTCCTCACCGGCCGGCGTTGCCGCCTCGGAGGATCTGCCGGCAGCCGTCGCCGGGCTGAGGACCGGCGACCAGGTGCGCCACGACTCCTACGGGGTGGGCACCGTCGTCGGCCTGGAGGGCAAGGGGAGGTCCCTGACCGCCCGCGTCGAGTTCGTCATCGACGGCGCCCCCACCACCAAGCGCCTCATCCTGCGCTACGCCCCCGTCGCCAAGATCTGA","MPGSGGAATPPPEAALPALIPAAGSFDDDSWADVEAPEEDWGPEDAPPPEDESAAAPTWEERQDEVSALVARAQANAAAARARADGAAPSGQPTGQAWGVTVSDPAELIRGLNPAQESAVTHAGAPLLIIAGAGSGKTRVLTHRIAHLIATGRARPGEILAITFTNKAAAEMRERVTALVGPAGERMWVSTFHSACVRILRREHEAAGLRSTFSIYDAADSTRLITLIVRELGIDPKRFTPKTFAHRISDLKNELITPAQFAERAVTSNPLERHLAEVYRAYAQRLSSANALDFDDIIMRTVALLQTRPAVAEMYRRRFRHILVDEYQDTNHAQYVLVRELVGGPGTSGAGSALPPGELTVVGDSDQSIYAFRGATIRNIEEFEEDYPSARTILLEQNYRSTQNILSAANAVISRNSGRREKNLWTAAGDGAPITGYVADSEHDEARWISQEVDRLADEHGIRPRDVAVFYRTNAQSRALEEAFMRAGQPYKVIGGTRFYDRREIKDAIAYLRAVDNPDDDVNLRRILNVPKRGLGDKAEGALAEHAARYAVSFGQAVADAAGAPREAQTGETENADGQASSSGAGEPPEVEGLTTRARNQVRGFHELLTTLRHMVTAGDGVADILDSALDASGYLAELRASDDPQDATRVENLAELHSVASDFQAANPDGTLADFLERVSLVADSDQLPPSADLEDEDARQAEEQGQITLMTVHTAKGLEFPVVFVTGMEDGTFPHSRSLAEETELAEERRLAYVALTRARERLYLTRAAVRSAWGAANAMPASRFLDDVPDETIDWKRLASSMEALRGGGTGWGSSWGEGGFGSGGRRSGSSRQSTYSDDDDFAPPVGAGTKRSGRLGRVETAQDRAAKRTSARLEARGKQSASSPAGVAASEDLPAAVAGLRTGDQVRHDSYGVGTVVGLEGKGRSLTARVEFVIDGAPTTKRLILRYAPVAKI$","ATP-dependent DNA helicase PcrA","Cytoplasm","ATP-dependent DNA helicase PcrA","ATP-dependent DNA helicase PcrA ","UvrD/REP helicase","","Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 1997. 90(4):635-647. PMID: 9288744","","","

InterPro
IPR000212
Family

UvrD/REP helicase
PTHR11070	$\"[123-588]T$ $\"[634-809]T$	UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580	$\"[112-557]T$	UvrD-helicase

InterPro
IPR014016
Domain

Helicase superfamily 1, UvrD-related
PS51198	$\"[110-402]T$	UVRD_HELICASE_ATP_BIND

InterPro
IPR014017
Domain

UvrD-like DNA helicase, C terminal
PS51217	$\"[403-719]T$	UVRD_HELICASE_CTER

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[109-393]T$ $\"[396-800]T$	no description

","BeTs to 22 clades of COG0210COG name: Superfamily I DNA and RNA helicasesFunctional Class: LThe phylogenetic pattern of COG0210 is --T-YqvCEBRHUJgPOLinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-59% similar to PDB:1PJR STRUCTURE OF DNA HELICASE (E_value = 1.1E_144);-59% similar to PDB:1QHG STRUCTURE OF DNA HELICASE MUTANT WITH ADPNP (E_value = 1.1E_144);-59% similar to PDB:3PJR HELICASE SUBSTRATE COMPLEX (E_value = 1.1E_144);-60% similar to PDB:2PJR HELICASE PRODUCT COMPLEX (E_value = 3.2E_123);-51% similar to PDB:2IS1 Crystal structure of UvrD-DNA-SO4 complex (E_value = 9.3E_115);","Residues 179 to 669 (E_value = 1.6e-189) place ANA_1390 in the UvrD-helicase family which is described as UvrD/REP helicase.","","DNA helicase PcrA","","1","","","Mon Aug 6 10:29:12 2007","","Mon Aug 6 10:29:12 2007","","","Mon Aug 6 10:29:12 2007","Mon Aug 6 10:29:12 2007","Mon Aug 6 10:29:12 2007","","","Mon Aug 6 10:29:12 2007","","","Mon Aug 6 10:29:12 2007","Mon Aug 6 10:29:12 2007","","","Mon Aug 6 10:29:12 2007","Mon Aug 6 10:29:12 2007","","","","","yes","","" "ANA_1392","1494301","1494936","636","5.11","-9.39","22557","ATGCGCACGATCGCCCTGTACACGACCGAGACCATGGCGGATTGGGAGTATGCCTACCTCACCACTCAGATCGCCGATGCAGAAGGGCTCAAGCCCGGACGCTTCCGACTGCTGCTCGTGGGTGATGGACTGGAGCCGGTGCACACACTGGGGAATCTCCCTCTTGCTCCGGAGGTCGACCTCGGCGCCCTGGATGCGCTGGCCGCCGACGGCTCACTCGCGGCCCTGGTCATTCCGGGAGGGAATCACTACGCGGCCGGGCACGAGCGGCTCATCAAGGCGGTCGGCCATCTCGTGGACAAGGAGATTCCGGTGGCGGCGATCTGCGGTGCCACGCTCCTGCTTGCCCGCGCTGGCTTCCTGGACGAGCGCCGTCACACCTCTAATGCCGCCTCGTACCTTGAGGCCAGTGGATACCGAGGCGGTGCGCACTACGTGGAGGCCCCGTTGGTCACCGACCGGGGCGTCACAACAGCCTCGGGCATCCACGCGATCCCCTTCACTGCGGAGGTCATGCGGATCACCAACCTTGTGCCCGATGCGATGGTCGACTCCTGGGAACAGGTCTTCCTCAACGGCAAGGAGAAGGACTACATGGCCCTGATGGAGGCGACCGTTGCCTGGCAGAACGCCTGA","MRTIALYTTETMADWEYAYLTTQIADAEGLKPGRFRLLLVGDGLEPVHTLGNLPLAPEVDLGALDALAADGSLAALVIPGGNHYAAGHERLIKAVGHLVDKEIPVAAICGATLLLARAGFLDERRHTSNAASYLEASGYRGGAHYVEAPLVTDRGVTTASGIHAIPFTAEVMRITNLVPDAMVDSWEQVFLNGKEKDYMALMEATVAWQNA$","ThiJ/PfpI family protein","Cytoplasm","DJ-1/PfpI family superfamily","ThiJ/PfpI family protein","ThiJ/PfpI domain protein","","Hod Y., Pentyala S.N., Whyard T.C., El-Maghrabi M.R. Identification and characterization of a novel protein that regulates RNA-protein interaction. J. Cell. Biochem. 1999. 72(3):435-444. PMID: 10022524Mizote T., Tsuda M., Nakazawa T., Nakayama H. The thiJ locus and its relation to phosphorylation of hydroxymethylpyrimidine in Escherichia coli. Microbiology 1996. 142:2969-2974. PMID: 8885414Halio S.B., Blumentals II., Short S.A., Merrill B.M., Kelly R.M. Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 1996. 178(9):2605-2612. PMID: 8626329","","","

InterPro
IPR002818
Domain

ThiJ/PfpI
PF01965	$\"[36-176]T$	DJ-1_PfpI

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[2-172]T$	no description
PTHR11019	$\"[40-166]T$	THIJ/PFPI

","BeTs to 10 clades of COG0693COG name: Putative intracellular protease/amidaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0693 is aompkzyq-dr-bcefghs-uj--twNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","-44% similar to PDB:2FEX The Crystal Structure of DJ-1 Superfamily Protein Atu0886 from Agrobacterium tumefaciens (E_value = 7.9E_12);","Residues 36 to 176 (E_value = 3e-05) place ANA_1392 in the DJ-1_PfpI family which is described as DJ-1/PfpI family.","","family superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1393","1495007","1495390","384","6.81","-0.33","14011","GTGATCACGGCCCCGCATGAGCTGACCCCGGCCCGGTGGCAGGTGCTGGGCGCCGTCCTGGAGGAACCGCTACCGGTGGCTGAGATCGCCCGACGGGTCGGACTAACGCGGCAAAGCGTGCAGCGGGTGGCCAATGATGTCGTCACGCAGGACTGGGCGCACTGGCAGCCCAATCCCGGGCGGCGCGGTCAGAACCTGCTCATCCTGACCGACAGGGGACGGCGAGCGATCGCGGCGCTCACCGCGGAGCAGCACGCCTGGGCCGACACCGTCGGCCAGGAGATCGGAGAGAAGGATCTGGAGGCCCTGGGGACACTGATCAGCAGGCTCACTGACGCATCGCGCCGCTACCGGCAAGCCGCCGGAGAGGAACCCTCGCCTTAA","VITAPHELTPARWQVLGAVLEEPLPVAEIARRVGLTRQSVQRVANDVVTQDWAHWQPNPGRRGQNLLILTDRGRRAIAALTAEQHAWADTVGQEIGEKDLEALGTLISRLTDASRRYRQAAGEEPSP$","Transcriptional regulator, MarR family","Cytoplasm","putative MarR-family transcriptional regulator","hypothetical protein","Resolvase helix-turn-helix domain protein","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR000835
Family

Bacterial regulatory protein, MarR
SM00347	$\"[1-100]T$	HTH_MARR
PS50995	$\"[1-112]T$	HTH_MARR_2

InterPro
IPR006120
Domain

Resolvase, helix-turn-helix region
PF02796	$\"[5-47]T$	HTH_7

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[8-80]T$	no description

","BeTs to 6 clades of COG1846COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1846 is aompkz--vdrlb-efg-sn-j----Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 47 (E_value = 0.0042) place ANA_1393 in the HTH_7 family which is described as Helix-turn-helix domain of resolvase.","","MarR-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1394","1495714","1496709","996","7.41","0.86","34773","ATGAGTCGAGCGATCGAGTACCGCACATTCGGCGGGCCAGAGGTCCTGGAGGAGGCCGAGCGCCCGCCGCAGGCACCCGGCGACGGAGAGGTGCGTATCGCGGTGCGCGACGTCGGGCTCAACCCCCTCGACTTCAAGACCTTCCGAGGCGATCTGCGAGGGCTTGAACGGGTTCAGCGCATCATTCATCCTCGACGCTGGTTTGAGGGCGCATCCGCTCGCTTCCCCAGGGGCGTGGCCCGCGACTTCGCGGGCGTCATTGACGCCGTCGGTGCAAACGTCACCGACCTCGCCGTGGGCGATGCCGTGCTGGGCACCTTGCGAAGTGCGCCCGGCCAGGCCGACACCCGCGGGGCACTCACCACCGAGTTGGTGGCACCCGCCGACGACGTCATCACGAAGCCGGCTCCACTGTCCTTCACACAGGCGGCCTGCCTTGGCGTAGCTGCGCAAACCGCGTGCGGCGCATTCAGGCAGCTGAATCTGCACGAAGGCGATGTCATTGTCATCAGTGCCGCCGCAGGCGGCGTGGGTTCGCTCGCCTCTCAGCTGGCCGTGAGCCGAGGCGCCACCGTCATCGGAATCGCCGGCGCCCGCAATATGGACTACCTCCGCTCCTTGGGCGCTATTCCAGTCACGTACGGTGAGAATCTGACCAGCCGGGTTCGCGACGCGGCTCCCTCCCCCGTCACCAAGCTCCTGGACTGCTACGGCGGTACCTACGTACGACTTGGCCGCGATCTCGGACTGACGGGCCGTTCCATCGGCACCTTGGTTCCCTCGCCCGCTGCAATCCTCAGGGGCGCGCAGTTCACCGGCTCACGGCACAGCAGTGGACGTGGCGACCTCGAGGAGGTGGCAGAGCTGGTGGCGGATGACGCCATCAAGGTCGAGGTCGCCCGCACCTACTCCTTCACGTTGGAGCAGATTCGCGCCGCCTACACCGAGCTGGCAAAGGGTCACGTCCGCGGCAAGCTCGTCATCGATCTATCCTGA","MSRAIEYRTFGGPEVLEEAERPPQAPGDGEVRIAVRDVGLNPLDFKTFRGDLRGLERVQRIIHPRRWFEGASARFPRGVARDFAGVIDAVGANVTDLAVGDAVLGTLRSAPGQADTRGALTTELVAPADDVITKPAPLSFTQAACLGVAAQTACGAFRQLNLHEGDVIVISAAAGGVGSLASQLAVSRGATVIGIAGARNMDYLRSLGAIPVTYGENLTSRVRDAAPSPVTKLLDCYGGTYVRLGRDLGLTGRSIGTLVPSPAAILRGAQFTGSRHSSGRGDLEEVAELVADDAIKVEVARTYSFTLEQIRAAYTELAKGHVRGKLVIDLS$","Zinc-containing alcohol dehydrogenase","Cytoplasm","quinone oxidoreductase","oxidoreductase","Alcohol dehydrogenase, zinc-binding domain protein","","Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Taneja B., Mande S.C. Conserved structural features and sequence patterns in the GroES fold family. Protein Eng. 1999. 12(10):815-818. PMID: 10556240","","","

InterPro
IPR002085
Family

Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695	$\"[15-55]T$ $\"[73-330]T$	ALCOHOL DEHYDROGENASE RELATED

InterPro
IPR013149
Domain

Alcohol dehydrogenase, zinc-binding
PF00107	$\"[164-292]T$	ADH_zinc_N

InterPro
IPR013154
Domain

Alcohol dehydrogenase GroES-like
PF08240	$\"[28-134]T$	ADH_N

noIPR
unintegrated

unintegrated
G3DSA:3.90.180.10	$\"[2-200]T$	no description
PTHR11695:SF34	$\"[15-55]T$ $\"[73-330]T$	ALCOHOL DEHYDROGENASE, ZINC-CONTAINING

","BeTs to 10 clades of COG0604COG name: NADPH:quinone reductase and related Zn-dependent oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0604 is -o-p-zyq-drlb-efghs--j----Number of proteins in this genome belonging to this COG is 4","***** IPB002364 (Quinone oxidoreductase/zeta-crystallin) with a combined E-value of 3.3e-23. IPB002364A 39-52 IPB002364B 75-95 IPB002364C 118-145 IPB002364D 163-186***** IPB011597 (GroES-related) with a combined E-value of 8.8e-17. IPB011597A 27-54 IPB011597B 76-103 IPB011597C 117-154 IPB011597D 166-210***** IPB002328 (Zinc-containing alcohol dehydrogenase) with a combined E-value of 7.2e-13. IPB002328A 15-46 IPB002328B 76-103 IPB002328D 118-156","","","No significant hits to the PDB database (E-value < E-10).","Residues 28 to 134 (E_value = 2.4e-06) place ANA_1394 in the ADH_N family which is described as Alcohol dehydrogenase GroES-like domain.Residues 164 to 292 (E_value = 5.7e-07) place ANA_1394 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase.","","oxidoreductase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1395","1496793","1497209","417","6.80","-0.33","14982","ATGAACAGCGAGCTCGCCGCCAGCAACCGCGCTGTCGCTGCGAAAACCGGGCTCAATGACAGCGATCTGGCGGTACTCGACGCCCTGCACCGCGACGGTCCGCAGACCCCCACTGCCCTCGCCCGCCGCACCCGGATGGGGACGACAACGATGACGAGTGTGCTGCGGCGACTCGTCCGCGATGGCTGGGTTGAGCGTCGTCCCAGTGAGACGGACCTGCGTTCCTTCACCATCCACGCCACGAGCGCTGATCGTCTTGCCGAGATATTCCTGCCCGCCAACCGGAAACTGACGGCACTGGTGGACGGCTGGCCCGAGAGCCAGGTCAATCAACTCATTGCGTTCCTGGAAGACGCCACGACAGTGATCCACGACTCGGCGGATCAGCTATCCTCCGCAGGCGGTCGTAACTCCTGA","MNSELAASNRAVAAKTGLNDSDLAVLDALHRDGPQTPTALARRTRMGTTTMTSVLRRLVRDGWVERRPSETDLRSFTIHATSADRLAEIFLPANRKLTALVDGWPESQVNQLIAFLEDATTVIHDSADQLSSAGGRNS$","Transcriptional regulator, MarR family","Cytoplasm, Periplasm","putative MarR-family transcriptional regulator","hypothetical protein predicted by Glimmer/Critica","regulatory protein, MarR","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR000835
Family

Bacterial regulatory protein, MarR
PF01047	$\"[18-79]T$	MarR
SM00347	$\"[11-109]T$	HTH_MARR
PS50995	$\"[1-121]T$	HTH_MARR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[18-85]T$	no description

","BeTs to 8 clades of COG1846COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1846 is aompkz--vdrlb-efg-sn-j----Number of proteins in this genome belonging to this COG is 6","***** IPB000835 (Bacterial regulatory protein, MarR family) with a combined E-value of 1.5e-07. IPB000835 51-84","","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 87 (E_value = 6.6e-11) place ANA_1395 in the MarR family which is described as MarR family.","","MarR-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1396","1498265","1497369","897","5.13","-11.47","30962","GTGGTTCCTGAGTTGTGTGGCGGCGCGCCGGCGGGCGCGGTGGACCGCTACGGGCTGCGGGCGCTGGTGCGTCAGGCGGCCGGTCGGCTGGCTGCGGCCGGCGTGACCAGCCCTCAGGTCGACGCCCGCATCCTGGCCGAGCACCTGCTGGGGCGGGCCCTGCTGCTGGCCGACGGCGCCGACGGCGACTTCCCGGCCGCCTATGACGCACTGGTGCTGCGCCGCGAGTGCCGCGAGCCGCTCCAGCACATCATCGGCCGCATGTGGCTGCGGGGCGCCGAGCTCATCAGCCGTCCCGGCGTGTTCATCGTGCGCCCGGAGACCGAGGTGGTGGCCGGGGCCGCCATTGAGGCGGCCCGCGAGGTCATGGACGGCGGCGGGGGAGTGGTCCTGACCGCTGACCTGTGCACCGGCTCGGGCGCGATCGCAGCCTGCGTCGCCAAGGAGGTGCCCGGGGCCCGGGTGGTCGCCGTCGAGATCAGTGAGACCGCTGCGTCTCTGGCCCGTGAGAACTGCGAGCGGCTGGTGCCCGGTCGGGTCGAGGTGATCCACGCCGACGCCACCGACCCGCTGGTCCTTCATGACCTCAACGGGCAGGTCGACGTCGTCGTCTCCAATCCGCCCTACGTCCCGGCCGGAGCCGTGGAGGACACTGAGACGGCCCAGCACGAGCCCACGGTGGCGCTCTACGGCGGTGGTCCGGACGGGCTGGAGATTCCGATTGACGTCCTGGTGCGCTCGGTCGCGCTGCTGCGCACCGGTGGGGTGCTCGTCATGGAGCACGACCACGAGCAGGGGGCGCTGCTGCGTGCGGCCGCGCTCGGGGCAGGGTTCAAGCAGGCCGAGACCGGCCAGGACCTCACCGGCCGCGACCGCTACCTGCGCGCCGTGCGGTAA","VVPELCGGAPAGAVDRYGLRALVRQAAGRLAAAGVTSPQVDARILAEHLLGRALLLADGADGDFPAAYDALVLRRECREPLQHIIGRMWLRGAELISRPGVFIVRPETEVVAGAAIEAAREVMDGGGGVVLTADLCTGSGAIAACVAKEVPGARVVAVEISETAASLARENCERLVPGRVEVIHADATDPLVLHDLNGQVDVVVSNPPYVPAGAVEDTETAQHEPTVALYGGGPDGLEIPIDVLVRSVALLRTGGVLVMEHDHEQGALLRAAALGAGFKQAETGQDLTGRDRYLRAVR$","Modification methylase, HemK family","Cytoplasm","possible methylase protein","modification methylase; HemK family","modification methylase, HemK family","","Nakayashiki T., Nishimura K., Inokuchi H. Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli. Gene 1995. 153(1):67-70. PMID: 7883187Le Guen L., Santos R., Camadro J.M. Functional analysis of the hemK gene product involvement in protoporphyrinogen oxidase activity in yeast. FEMS Microbiol. Lett. 1999. 173(1):175-182. PMID: 10220893","","","

InterPro
IPR002052
Domain

N-6 Adenine-specific DNA methylase
PS00092	$\"[203-209]?$	N6_MTASE

InterPro
IPR004556
Family

Modification methylase HemK
TIGR00536	$\"[17-298]T$	hemK_fam: methyltransferase, HemK family

InterPro
IPR013216
Domain

Methyltransferase type 11
PF08241	$\"[133-206]T$	Methyltransf_11

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[88-295]T$	no description
PTHR18895	$\"[106-298]T$	METHYLTRANSFERASE
PTHR18895:SF7	$\"[106-298]T$	HEMK METHYLTRANSFERASE FAMILY MEMBER

","BeTs to 23 clades of COG2890COG name: Predicted rRNA or tRNA methylaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG2890 is aompk-yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-50% similar to PDB:1NV8 N5-glutamine methyltransferase, HemK (E_value = 1.8E_16);-50% similar to PDB:1NV9 HemK, apo structure (E_value = 1.8E_16);-50% similar to PDB:1SG9 Crystal structure of hypothetical protein HEMK (E_value = 1.8E_16);-50% similar to PDB:1VQ1 Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution (E_value = 1.8E_16);-42% similar to PDB:1T43 Crystal Structure Analysis of E.coli Protein (N5)-Glutamine Methyltransferase (HemK) (E_value = 4.4E_15);","Residues 92 to 295 (E_value = 6.1e-08) place ANA_1396 in the MTS family which is described as Methyltransferase small domain.Residues 133 to 206 (E_value = 8.5e-07) place ANA_1396 in the Methyltransf_11 family which is described as Methyltransferase domain.","","methylase protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1397","1499367","1498255","1113","4.85","-21.50","39760","GTGAAGGAACCCGAGTCCATGAGTGAGGACTTCTCCGCCGCAGAGCCGCTCCTGGCCGAGTACGCGGATATCGAGGCCGAGATGGCCGGGCCCGCGGCCGCCGACCCCGGGGCCATGCGTCGGCTGGGGCGCCGCTACGCCGAGCTGGGCAGGGTCGTGGCCGCCTACCGGGCCTGGCAGGCGGCCAGTGCCGACCTGGCTGACGCCCGCGAGCTGGCCGCGGAGGACGAGGACTTCGCCGCCGAGGTGCCGACCCTGGAGGCCGCCGAGGCCGCTGCCGGAGAGCACCTGCGCGAGGTCCTCGTGCCCCGGGATCCCGATGACGCCCGCGACGTCATCATCGAGGTCAAGGCCGGTGAGGGCGGTGAGGAGTCGGCGCTGTTCGCCTCCGACCTGGCCCGCATGTACTCCCGCTACGCCGAGCGGCAGGGGTGGGCCGTGGAGGTCCTCGACGCCACTGACTCCGACCTGGGCGGTTACAAGGACGTGCGCCTGGCTATTAAGGCCCGCGGGCCTGTAGAGCCCCAGGACGGGGTGTGGGCGCACCTGAAGTACGAGGGCGGCGTCCACCGCGTCCAGCGCGTCCCGGTCACCGAGTCCCAGGGGCGCATCCACACCTCTGCGGCCGGCGTCCTGGTCATGCCGGAGGCTGACGACCCCGGCGAGCTCCAGATCGACGCCGCCGACCTGCGCATCGACGTCTTCCGCTCCTCGGGACCCGGGGGCCAGAGCGTCAACACCACGGACTCGGCCGTGCGCATCACGCACCTGCCCACAGGGATCGTCGTGTCCATGCAGAACGAGAAGTCCCAGCTGCAGAACAAGGAAGCGGCCATGCGGGTCCTGCGGGCCCGGCTCCTGGCCGAGCGCGCGGCGGCCGCCGCCGCCGAGGCGGCGCAGGCCCGTCGCAGCCAGGTGCGCACTGTGGACCGCTCCGAGCGCATCCGCACCTACAATTTCCCTGAGAACCGGATCGCCGACCACCGCACCGGCTTCAAGGCCTACAACCTCGACGCCGTTCTTGACGGTGATCTCGGCCCGGTGATCGCCTCGGCCATCGCCATGGACGAGGCCGAACGATTATCCCAGGTGGGTGAGGGCAGTGGTTCCTGA","VKEPESMSEDFSAAEPLLAEYADIEAEMAGPAAADPGAMRRLGRRYAELGRVVAAYRAWQAASADLADARELAAEDEDFAAEVPTLEAAEAAAGEHLREVLVPRDPDDARDVIIEVKAGEGGEESALFASDLARMYSRYAERQGWAVEVLDATDSDLGGYKDVRLAIKARGPVEPQDGVWAHLKYEGGVHRVQRVPVTESQGRIHTSAAGVLVMPEADDPGELQIDAADLRIDVFRSSGPGGQSVNTTDSAVRITHLPTGIVVSMQNEKSQLQNKEAAMRVLRARLLAERAAAAAAEAAQARRSQVRTVDRSERIRTYNFPENRIADHRTGFKAYNLDAVLDGDLGPVIASAIAMDEAERLSQVGEGSGS$","Peptide chain release factor 1","Cytoplasm","peptide chain release factor 1","peptide chain release factor 1","peptide chain release factor 1","","Tate W.P., Poole E.S., Mannering S.A. Hidden infidelities of the translational stop signal. Prog. Nucleic Acid Res. Mol. Biol. 1996. 52:293-335. PMID: 8821264Craigen W.J., Lee C.C., Caskey C.T. Recent advances in peptide chain termination. Mol. Microbiol. 1990. 4(6):861-865. PMID: 2215213Pel H.J., Rep M., Grivell L.A. Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure. Nucleic Acids Res. 1992. 20(17):4423-4428. PMID: 1408743","","","

InterPro
IPR000352
Domain

Class I peptide chain release factor
PF00472	$\"[216-329]T$	RF-1
PS00745	$\"[236-252]T$	RF_PROK_I

InterPro
IPR004373
Family

Peptide chain release factor 1
PTHR11075:SF9	$\"[15-366]T$	PEPTIDE CHAIN RELEASE FACTOR 1
TIGR00019	$\"[33-367]T$	prfA: peptide chain release factor

InterPro
IPR005139
Domain

PCRF
PF03462	$\"[71-186]T$	PCRF

InterPro
IPR012086
Family

Protein chain release factor, RF-1/RF-2
PIRSF003056	$\"[11-367]T$	Protein chain release factor, RF-1/RF-2

noIPR
unintegrated

unintegrated
PIRSF500105	$\"[10-367]T$	Peptide chain release factor 1
PTHR11075	$\"[15-366]T$	PEPTIDE CHAIN RELEASE FACTOR

","BeTs to 19 clades of COG0216COG name: Protein chain release factor AFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0216 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000352 (Class I peptide chain release factor domain) with a combined E-value of 4.3e-107. IPB000352A 102-151 IPB000352B 165-216 IPB000352C 229-274 IPB000352D 302-329 IPB000352D 315-342","","","-63% similar to PDB:2B3T Molecular basis for bacterial class 1 release factor methylation by PrmC (E_value = 6.6E_67);-58% similar to PDB:2B64 30S ribosomal subunit, tRNAs, mRNA and release factor RF1 from a crystal structure of the whole ribosomal complex. This file contains the 30S subunit, tRNAs, mRNA and release factor RF1 from a crystal structure of the whole ribosomal complex\". The entire crystal structure contains one 70S ribosome, tRNAs, mRNA and release factor RF1 and is described in remark 400. (E_value = 3.3E_66);-64% similar to PDB:1RQ0 Crystal structure of peptide releasing factor 1 (E_value = 1.4E_64);-64% similar to PDB:2FVO Docking of the modified RF1 X-ray structure into the Low Resolution Cryo-EM map of E.coli 70S Ribosome bound with RF1 (E_value = 1.4E_64);-63% similar to PDB:1ZBT Crystal structure of Peptide chain release factor 1 (RF-1) (SMU.1085) from Streptococcus mutans at 2.34 A resolution (E_value = 6.9E_64);","Residues 71 to 186 (E_value = 3.4e-42) place ANA_1397 in the PCRF family which is described as PCRF domain.Residues 216 to 329 (E_value = 1.3e-65) place ANA_1397 in the RF-1 family which is described as Peptidyl-tRNA hydrolase domain.","","chain release factor 1 (prfA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1398","1499681","1499469","213","9.09","5.27","7715","ATGAAGCAGGGCATCCACCCCGACTACGTGGCCACCACGGTCACGTGCACCTGTGGCAACACCTTCGAGACCCGCTCCACCGTCACCTCCGGTGAGATCCGCGTGGACGTGTGCTCGGCCTGCCACCCGTTCTACACCGGCAAGCAGAAGATCCTCGACACCGGTGGCCGCGTTGCCCGCTTCGAGGCCCGGTACGGCAAGCGCAGCAAGTAG","MKQGIHPDYVATTVTCTCGNTFETRSTVTSGEIRVDVCSACHPFYTGKQKILDTGGRVARFEARYGKRSK$","Ribosomal protein L31","Extracellular","ribosomal protein L31","50S ribosomal protein L31","ribosomal protein L31","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR002150
Family

Ribosomal protein L31
PR01249	$\"[2-19]T$ $\"[32-47]T$ $\"[47-65]T$	RIBOSOMALL31
PF01197	$\"[1-68]T$	Ribosomal_L31
TIGR00105	$\"[1-70]T$	L31: ribosomal protein L31
PS01143	$\"[36-57]T$	RIBOSOMAL_L31

","BeTs to 18 clades of COG0254COG name: Ribosomal protein L31Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0254 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB002150 (Ribosomal protein L31) with a combined E-value of 7.2e-39. IPB002150A 1-20 IPB002150B 27-65","","","-70% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 1.0E_17);-70% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 1.0E_17);-70% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 1.0E_17);-70% similar to PDB:2J01 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 2 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE I. (E_value = 1.0E_17);-70% similar to PDB:2J03 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 4 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE II. (E_value = 1.0E_17);","Residues 1 to 68 (E_value = 1.6e-41) place ANA_1398 in the Ribosomal_L31 family which is described as Ribosomal protein L31.","","protein L31 (rpmE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1399","1501933","1499822","2112","8.83","4.58","76376","GTGACCGAGACCTCCAGCGCCCAGCCCTCGCTTTCCACCATGCGTCTGGCCGAGCTTCAGTCGCTCGCCGGCTCCATGGGCCTCAAGGGCACCTCCCGTATGCGTAAGAGTGAGCTCGTCGCCGCCATCCGTGAGGCGCGCGGCTCCTCCGCCTCCACTCCCGACTCCCACAGCACGTCGAAGAGCTCGCCCGATGCTGGGGCGACCGACGTCGCCGACTCTTCATCCTCCACCTCCTCCACTTCTTCGACCGGTGAGTCCTCTTCGGAGCAGCCCCCGGTCGCGGCCTCCGGGCGCTCCCGACGCCGTCGTGCCACCGCTGCCTCCGGGGCCCCCGAGGAGCGCCAGCCCGCGCCGGTCCTCGACCTGGGGTTCGATCTGTCCGACCGCTCCGGCTCCTCCGGCAGCGACTCGGACAACGGCTCCGGCCGTGATGAGGAGCGCCCCGCACGCAGCCGGTGGCGCGAGCGCACCGAGCGCTCCGAGACCACTGAGGGCGATGACCGTGACTCCTACGGGCGCTCGGAGCGGGGCGCGCGCGCCTCACGCGATCAGTTCCGCCGTGGCCGCCGGCGCGCCCAGGCCTCCGCCGGCGCCCCCGAGAACCAGGAGCGCGCCTCACGCGAGACCCGCACCGACTCGCCCGAGGACCACGCCGACGCCAAGGCCGCTCTCATGCGGGACCTGGCTGACGCCACCGGGACCTCCGTCGTCGAGTCCCAGGAGCGTCCGCGCCGGGGCCGTGACGGCAGCGATGACTCCGACGGCTACGACGAGGAGCGCGGTGGGCGTCGTCGTCGGGGCCGCAAGCGCGGACGCGACCGCTTCGACCGCGATGAGCGCGACTCCGGCCGCGAGGGCCGGGACGGCTCCGCCGGGCGCGGCAACCGCAACCAGCCGCGTGAGGACGAGGTCCTCCTGCCGGTCGCCGGCATCCTGGACGTCACCGACAACCAGCATGCCTACCTGCGCACCTCCGGGTACCTGCCCGGCCCCAAGGACGTCTACGTCTCCAACCAGCTCATCAAGGACAACGGGCTGCGTGCCGGCGACGCCGTGACCGGCTGGGTCCGCGAGGGCGGAGAATCGTCCACGCCCCACCAGGGCGGGCGCAACAACCGCCGTCAGAACCGGGCCGGCCGGGTCAAGTACAACCCCATGGTCAGCGTCGAGACCGTCAACGGCATGGACGCCGAGCGTTCCAAGCGCCGCCCCGAGTTCGCCAAGCTCACCCCCCTCTACCCCCAGGAGCAGCTGCGCCTGGAGACCACGCCCAAGGCCGTCACCCCGCGGATCATTGATCTGGTCTCGCCCATCGGCAAGGGGCAGCGCGGGCTCATCGTCTCCCCGCCCAAGGCGGGTAAGACGATCGTCCTGCAGCAGATCGCCAACGCCATCAGCGTCAACAACCCCGAGGCCCACCTCATGGTCGTGCTCGTCGACGAGCGCCCTGAGGAGGTCACCGACATGCAGCGCACGGTCAAGGGCGAGGTCATCGCCTCCACCTTCGACCGCCCCGCCTCCGACCACACGATCGTGGCCGAACTGGCCATCGAGCGCGCCAAGCGCCTCGTGGAGCTGGGCCAGGACGTCGTCGTGCTGCTGGACTCCATCACCCGGCTCGGGCGCGCCTACAACCTGGCAGCCCCGGCCAGCGGCCGGATCCTCTCCGGTGGTGTGGACGCCTCCGCCCTCTACCCGCCCAAGCGCTTCTTCGGGGCGGCCCGCAACGTGGAGAACGGCGGCAGCCTGACCATCCTGGCCACGGCCCTGGTGGAGACCGGCTCCAAGATGGATGAGGTCATCTTCGAGGAGTTCAAGGGAACCGGAAACATGGAGCTGCGGCTGTCGCGCCAGCTCGCCGACAAGCGCATCTTCCCGGCTGTGGACGTGGCGGCCTCCGGCACCCGCCGCGAGGAGCTGCTCATCGACCCCGCCCAGCTCAAGATCATGTGGCGCCTGCGCCGCCTCTTCGCCGGGCTGGAGCAGCAGCAGGCCATCGAGCTGGTGCTCTCCAAGCTCAAGGACACCCAGTCCAACGCCGAGTTCCTCATGGTGCTGTCCAAGACCACCCCGGCCGGCACCTCCCTGGCCGACGGCGAGGACGAGTAA","VTETSSAQPSLSTMRLAELQSLAGSMGLKGTSRMRKSELVAAIREARGSSASTPDSHSTSKSSPDAGATDVADSSSSTSSTSSTGESSSEQPPVAASGRSRRRRATAASGAPEERQPAPVLDLGFDLSDRSGSSGSDSDNGSGRDEERPARSRWRERTERSETTEGDDRDSYGRSERGARASRDQFRRGRRRAQASAGAPENQERASRETRTDSPEDHADAKAALMRDLADATGTSVVESQERPRRGRDGSDDSDGYDEERGGRRRRGRKRGRDRFDRDERDSGREGRDGSAGRGNRNQPREDEVLLPVAGILDVTDNQHAYLRTSGYLPGPKDVYVSNQLIKDNGLRAGDAVTGWVREGGESSTPHQGGRNNRRQNRAGRVKYNPMVSVETVNGMDAERSKRRPEFAKLTPLYPQEQLRLETTPKAVTPRIIDLVSPIGKGQRGLIVSPPKAGKTIVLQQIANAISVNNPEAHLMVVLVDERPEEVTDMQRTVKGEVIASTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSITRLGRAYNLAAPASGRILSGGVDASALYPPKRFFGAARNVENGGSLTILATALVETGSKMDEVIFEEFKGTGNMELRLSRQLADKRIFPAVDVAASGTRREELLIDPAQLKIMWRLRRLFAGLEQQQAIELVLSKLKDTQSNAEFLMVLSKTTPAGTSLADGEDE$","Transcription termination factor Rho","Cytoplasm, Periplasm, Membrane","transcription termination factor Rho","transcription termination factor Rho","transcription termination factor Rho","","Novoseler M., Hershkovits G., Katcoff D.J. Functional domains of the yeast chromatin protein Sin1p/Spt2p can bind four-way junction and crossing DNA structures. J. Biol. Chem. 2005. 280(7):5169-5177. PMID: 15563464","","","

InterPro
IPR000194
Domain

ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding
PF00006	$\"[428-636]T$	ATP-synt_ab

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[441-626]T$	AAA

InterPro
IPR004665
Family

Transcription termination factor Rho
TIGR00767	$\"[6-689]T$	rho: transcription termination factor Rho

InterPro
IPR011112
Domain

Rho termination factor, N-terminal
PF07498	$\"[10-52]T$	Rho_N

InterPro
IPR011113
Domain

Rho termination factor, RNA-binding
PF07497	$\"[307-400]T$	Rho_RNA_bind

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[195-272]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[403-690]T$	no description
PTHR15184	$\"[301-364]T$ $\"[383-667]T$	ATP SYNTHASE
PTHR15184:SF2	$\"[301-364]T$ $\"[383-667]T$	TRANSCRIPTION TERMINATION FACTOR RHO

","BeTs to 16 clades of COG1158COG name: Transcription termination factorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1158 is -------qvdr-b-efghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB011113 (Rho termination factor, RNA-binding) with a combined E-value of 1.2e-196. IPB011113A 318-369 IPB011113B 388-422 IPB011113C 431-459 IPB011113D 460-501 IPB011113E 528-555 IPB011113F 556-585 IPB011113G 586-615 IPB011113H 616-655***** IPB011112 (Rho termination factor, N-terminal) with a combined E-value of 7.8e-192. IPB011112A 319-366 IPB011112B 388-422 IPB011112C 433-486 IPB011112D 502-556 IPB011112E 560-614 IPB011112F 654-684***** IPB000194 (H+-transporting two-sector ATPase, alpha/beta subunit, central region) with a combined E-value of 1.4e-32. IPB000194B 428-463 IPB000194D 528-577 IPB000194E 583-631***** IPB013223 (Ribonuclease B, OB region N-terminal) with a combined E-value of 2.1e-25. IPB013223C 482-505 IPB013223D 545-591 IPB013223E 598-608***** IPB013957 (Protein of unknown function DUF1777) with a combined E-value of 4.9e-06. IPB013957A 242-285 IPB013957A 254-297 IPB013957A 252-295 IPB013957A 260-303 IPB013957A 245-288 IPB013957A 246-289 IPB013957A 250-293 IPB013957A 256-299 IPB013957A 248-291 IPB013957A 247-290 IPB013957A 244-287 IPB013957A 258-301 IPB013957A 255-298 IPB013957A 150-193 IPB013957A 243-286 IPB013957A 249-292 IPB013957A 253-296 IPB013957A 239-282 IPB013957A 236-279 IPB013957A 238-281 IPB013957A 231-274 IPB013957A 240-283 IPB013957A 264-307 IPB013957A 262-305 IPB013957A 154-197 IPB013957A 148-191 IPB013957A 228-271 IPB013957A 141-184 IPB013957A 144-187 IPB013957A 169-212 IPB013957A 259-302 IPB013957A 155-198 IPB013957A 263-306 IPB013957A 152-195 IPB013957A 237-280 IPB013957A 234-277 IPB013957A 140-183 IPB013957A 232-275 IPB013957A 268-311 IPB013957A 261-304","","","-71% similar to PDB:1PV4 X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA (E_value = 2.8E_107);-71% similar to PDB:1PVO X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP (E_value = 2.8E_107);-71% similar to PDB:1XPO Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin (E_value = 2.8E_107);-71% similar to PDB:1XPR Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic 5a-formylbicyclomycin (FB) (E_value = 2.8E_107);-71% similar to PDB:1XPU Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic 5a-(3-formylphenylsulfanyl)-dihydrobicyclomycin (FPDB) (E_value = 2.8E_107);","Residues 10 to 52 (E_value = 9.2e-11) place ANA_1399 in the Rho_N family which is described as Rho termination factor, N-terminal domain.Residues 307 to 400 (E_value = 3.4e-07) place ANA_1399 in the Rho_RNA_bind family which is described as Rho termination factor, RNA-binding domain.Residues 428 to 636 (E_value = 1.1e-76) place ANA_1399 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain.","","termination factor Rho (rho)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1400","1502267","1502004","264","7.19","0.13","8751","GTGTCCGAGTCGATCATTCCGGTGGGGCTGATCGTGCGTACGGTCGGCCCCACCGGCGTCACGGCGACGGCGAGAAGTGTCATGGATGGAATAACGGCTGCATCCCCGGCGTTGCTCGCCAGTGTTCCGTTAGGTGCTGCTTCTCCGGGCTGCTATGATGACGCTGTCGGCCGCACGGATCGCACCACGCCGCTGACCGCACCAGCCCCGGACCTGAGGCTCAGGTCTCAGCAGAAGCCGGCAGTGCATGACCCACCCCCGTGA","VSESIIPVGLIVRTVGPTGVTATARSVMDGITAASPALLASVPLGAASPGCYDDAVGRTDRTTPLTAPAPDLRLRSQQKPAVHDPPP$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1401","1503045","1502311","735","5.95","-2.32","25479","ATGACCGCTCATACGACCGCGCCCGTCGCCCCTTCTGGGGGCACCCAGTCCCTGGCCGGATCGCCGACCTATGACGCCTACGCCAATACCCAGATGGGGCGTCTGAACCGGATCGTGGCTCTGCACGCCGGGGTCTCGGAGCCCTCGACCTCCCAGATGCTCGCCGAGCGGCTGGCCGAGTCGACTCGCAAGGCCCTGGAGGCCGACTCCCGCCTGGCCAGCATCGAGGTCATCGGGCTCAGGCCCCTGGTCAAGGACATCGCCCTGGCCAGTGTGGGTGGGCCGGTGTCCGCCGACCTGCAGAAGGTGATCGATGCCCTGTCCGCCGCCGACGGCGTCATCCTGGTCAGCCCGGTCTTTCAGGCCTCCTACTCCGGACTGTTCAAGTCCGCCATGGATGTGCTGCCGGCCGGCACGCTTGAGGGCGTCCCCGTCCTGCTGGGGGCGACGGCCGGCACTGCGCGGCACAGTCTTGTGACCGAGATGGCGCTGCGGCCGCTGGTGGTCTACATGAAGGCCCTGCCGACGCAGACCGCCGTCTTCGCGGCCAGTGAGGACTTCGGCGCGGCCTGGCAGAGGCCATCATCCTCCGAGCGGCCCGAGTCGCCCTTGAGCGAGCGCGTGGCTCGGGCGGGACGGGAGCTGGCCACGCTCATGGAGCGCTTCCCGCGCCAGGCGCCGGTTGACCCGCTGGCCGACTTCGCGCCCATGGAGACGCTCCTCGCAGGTCGCTGA","MTAHTTAPVAPSGGTQSLAGSPTYDAYANTQMGRLNRIVALHAGVSEPSTSQMLAERLAESTRKALEADSRLASIEVIGLRPLVKDIALASVGGPVSADLQKVIDALSAADGVILVSPVFQASYSGLFKSAMDVLPAGTLEGVPVLLGATAGTARHSLVTEMALRPLVVYMKALPTQTAVFAASEDFGAAWQRPSSSERPESPLSERVARAGRELATLMERFPRQAPVDPLADFAPMETLLAGR$","NADPH-dependent FMN reductase","Periplasm, Membrane","Predicted flavoprotein","putative oxidoreductase ","NADPH-dependent FMN reductase","","","","","

InterPro
IPR005025
Domain

NADPH-dependent FMN reductase
PF03358	$\"[37-133]T$	FMN_red

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[37-230]T$	no description

","BeTs to 4 clades of COG0431COG name: Predicted flavoproteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0431 is -o----y--drlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is 2","***** IPB005025 (NADPH-dependent FMN reductase) with a combined E-value of 6.3e-11. IPB005025A 110-133 IPB005025B 140-152","","","No significant hits to the PDB database (E-value < E-10).","Residues 36 to 213 (E_value = 1.2e-06) place ANA_1401 in the FMN_red family which is described as NADPH-dependent FMN reductase.","","flavoprotein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1403","1504246","1503098","1149","5.57","-11.11","42961","ATGCAGTTTGGAATCTTCACGGTTGGAGACATCACGACCGATCCGGCTACTGGTAAGGCTCCCAGCGAGCATCAGCGCATCAAGAACACAGTCGAGATGGCGGTCCTGGCTGAGCAGGCAGGTTTGGACTTCTTCGCTACCGGGGAGCACCACAACCCACCCTTCGCGCCGTCGTCACCCGCGACCCTGCTGGCCAACATCGCCGCCCGCACGGACAAGCTTCTCCTGAGCACTGCGACCACCCTCATCACGACCAATGACCCGGTGCGTCTGGCCGAGGAGTACGCCTACCTCCAGCACCTCTCCGACGGGCGCGTCGACCTCATGATGGGACGCGGCAACACCGGGCCGGTCTACCCCTGGTTCGGCAAGGACATCCGCAAGGGCATCTCGCTCGCGGTGGAGAACTATGACCTGCTGCGCCGCCTGTGGCGCGAGACCAATGTGGACTGGGAGGGTGAGTTCCGCACCGCGCTGCAGGACTTCACATCCATGCCCCGCCCACTCGACGGCGTCCCGCCCTTCGTGTGGCACGCCTCCATCCGCTCGCCCCAGATCGCCGAGCAGGCCGCCTATTACGGAGACGGGTACCTCCACAACAACATCTTCTGGCCCATCGACCACGTCAAGAAGATGGTCGATCTCTACCGAGAGCGCTTCGCCTTCTATGGTCATGGTCGGCCCGAGCAGGCGATCGTGGGCTTGGGTGGACAGATCTTCGCCGCCAGGAGTGAGACCGAGGCCATCGAGCGATACACCCCCTACTTCCGCAACACCTACGTCTACCAGGGGGCGTCGCTGGAAGAGATGACACAGCACACGCCTCTCGCGGTCGGCACGCCTGAGCAGATCGTGGAGAAGTACCTGACCTACCGGGACGCGATCGGCGACTACCAGCGTCAGGCCTTCAACCTGGACCTGGGCGGCGTCCCGCACAAGGAGATCATGAAGCAGATCGAGTACCTGGGTTCCGAGATCGTTCCGGCGCTGCGCGCCGAGCTGGAGTCCACCAGGCCCGAAGGGGTTCCCGACGCACCGCTCCACCCGCGCCACCGGGCCCTGCTGGAGGGGGCCGAGCCTCCGGCTGAGGAGCCCTTCTCCCTGTCCAACGAGTTCGACCCGCTCACGGGCCGGAAGGTGAGGATCTGA","MQFGIFTVGDITTDPATGKAPSEHQRIKNTVEMAVLAEQAGLDFFATGEHHNPPFAPSSPATLLANIAARTDKLLLSTATTLITTNDPVRLAEEYAYLQHLSDGRVDLMMGRGNTGPVYPWFGKDIRKGISLAVENYDLLRRLWRETNVDWEGEFRTALQDFTSMPRPLDGVPPFVWHASIRSPQIAEQAAYYGDGYLHNNIFWPIDHVKKMVDLYRERFAFYGHGRPEQAIVGLGGQIFAARSETEAIERYTPYFRNTYVYQGASLEEMTQHTPLAVGTPEQIVEKYLTYRDAIGDYQRQAFNLDLGGVPHKEIMKQIEYLGSEIVPALRAELESTRPEGVPDAPLHPRHRALLEGAEPPAEEPFSLSNEFDPLTGRKVRI$","Luciferase-like monooxygenase","Cytoplasm","oxidoreductase(N5,N10-methylenetetrahydromethanopterin reductase)","putative monooxygenase","luciferase family protein","","Fisher A.J., Thompson T.B., Thoden J.B., Baldwin T.O., Rayment I. The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 1996. 271(36):21956-21968. PMID: 8703001Moore S.A., James M.N. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 1995. 249(1):195-214. PMID: 7776372Eichhorn E., Davey C.A., Sargent D.F., Leisinger T., Richmond T.J. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J. Mol. Biol. 2002. 324(3):457-468. PMID: 12445781Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J. Mol. Biol. 2000. 300(4):935-950. PMID: 10891279","","","

InterPro
IPR011251
Family

Bacterial luciferase-like
G3DSA:3.20.20.30	$\"[1-334]T$	no description
PF00296	$\"[1-330]T$	Bac_luciferase

InterPro
IPR000870
Family

Homoserine kinase
PR00958	$\"[15-30]T$ $\"[98-113]T$ $\"[134-147]T$ $\"[176-193]T$ $\"[253-268]T$	HOMSERKINASE
PIRSF000676	$\"[8-299]T$	Homoserine kinase
TIGR00191	$\"[8-300]T$	thrB: homoserine kinase

InterPro
IPR006203
Domain

GHMP kinase, ATP-binding region
PS00627	$\"[91-102]?$	GHMP_KINASES_ATP

InterPro
IPR006204
Domain

GHMP kinase
PF00288	$\"[84-147]T$	GHMP_kinases_N

InterPro
IPR013750
Domain

GHMP kinase, C-terminal
PF08544	$\"[211-286]T$	GHMP_kinases_C

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[6-115]T$	no description

noIPR
unintegrated

unintegrated
PTHR20861	$\"[42-300]T$	HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE
PTHR20861:SF1	$\"[42-300]T$	HOMOSERINE KINASE

","BeTs to 18 clades of COG0083COG name: Homoserine kinaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0083 is -ompkzyqvdrlbce-ghs-uj----Number of proteins in this genome belonging to this COG is 1","***** IPB000870 (Homoserine kinase signature) with a combined E-value of 4.1e-34. IPB000870A 15-30 IPB000870B 98-113 IPB000870C 134-147 IPB000870D 176-193 IPB000870E 253-268***** IPB006203 (GHMP kinase, ATP-binding region) with a combined E-value of 5.3e-16. IPB006203A 12-27 IPB006203B 91-105 IPB006203C 138-147","","","-46% similar to PDB:1FWK CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP (E_value = 1.5E_15);-46% similar to PDB:1FWL CRYSTAL STRUCTURE OF HOMOSERINE KINASE (E_value = 1.5E_15);-46% similar to PDB:1H72 CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE (E_value = 1.5E_15);-46% similar to PDB:1H73 CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH THREONINE (E_value = 1.5E_15);-46% similar to PDB:1H74 CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE (E_value = 1.5E_15);","Residues 84 to 147 (E_value = 6.4e-15) place ANA_1404 in the GHMP_kinases_N family which is described as GHMP kinases N terminal domain.Residues 211 to 286 (E_value = 0.0017) place ANA_1404 in the GHMP_kinases_C family which is described as GHMP kinases C terminal.","","kinase (thrB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1405","1506707","1505379","1329","4.80","-25.11","45584","GTGGCTCAAGACCTCTCATCCGCCCAGCGCACACTGACCGTCGGCGTCCTCGGCGCCGGGACCGTCGGAAGCCAGGTCATTCGCCTCCTCACCGAGCAGGCCGACGACTTCGCCGCCCGCTCCGGCGCACGTCTTGAGATCACGGGCGTCGCCGTCCGCGACGTCAACGCGCCGCGCGACTTCGCCGTCCCCCAGGACCTCCTCACCGATGACGCCACCGCCGTCGCCACCGGCAACGACCTGGTCGTTGAGCTCATCGGCGGGATCGAGCCGGCCCGCACCCTCATCCTGGCCGCCTTCAAGGCCGGGGCCAGCGTCATTACCGGCAACAAGGCCCTCATCGCGGCCCACGGCCCCGAGCTCTACACCGCCGCCGCGGCCGCAGGCACCGACTTCTACTACGAGGCCGCTGTTGCCGGTGCCATCCCGGTGGTCTACGCGCTGCGCGAGTCCATGGCCGGTGACCGCGTCACCAGTGTGCTCGGCATCGTCAACGGCACCACTAACTACATCCTTGATGAGATGAGCACCAAGGGCCTGTCCTTCGAGACCGCCCTGGCCACCGCCCAGGAGCTCGGCTACGCCGAGGCCGACCCCACCGCCGACGTCGACGGCCTGGACGCCGCCGCCAAGGCCGCCATCATCGCCTCCCTCGCCTTCCACACCCGCGTGGGCCTCGACGACGTCTCCGTTGAGGGCATCCGCGAGGTCACCGCCGACGACATCCGCGAGGCCCACGCCTCGGGCTGCGAGCTCAAGCTCCTCGCCATCGCCCAGCGCCGCGACGACGAGCACGCGCAAGGCGTCTCCGTGCGCGTCCACCCAGCCCTCGTCCCCAACGACCACCCGCTGGCCAGCGTTCACGGCGCCTACAACGCCGTCCTGGTCGAGGCCGAGAGTGCCGGGCGCCTCATGTTCTACGGTCAGGGAGCCGGGGGAGCCCCGACGGCCTCCGCGGTCCTGTCCGACGTCGTCGCAGCCGCCGCCCACCGGGTCCACGGCGGCCAGGCCCCCCGCGAGTCCTCCTACGCGAGCCTTCCGGTCCTCGGCCCCGAGGCCGCCGTCACCCGCTACCAGATCCAGCTGCGCTCAGACGACGCCGTCGGCTCCCTGGCAGCGATGGCCTCCGTCTTCGCCGAGAACGAGGTCTCCATCAACTCGGTGCGCCAGAGCGCCTACGTCACCTCCGACGGCAGCCACGACCAGGCCGTCGTCACCTTCGTGACCCACCCTGCCCCCGTCTTCCACCTCGACGCCGCCGTCGAGGGCCTGCGGGACTCCGACCGGGTCGCCGAGGTCGTCTCCATCCAGCGCGTCGAAGGCGAGTGA","VAQDLSSAQRTLTVGVLGAGTVGSQVIRLLTEQADDFAARSGARLEITGVAVRDVNAPRDFAVPQDLLTDDATAVATGNDLVVELIGGIEPARTLILAAFKAGASVITGNKALIAAHGPELYTAAAAAGTDFYYEAAVAGAIPVVYALRESMAGDRVTSVLGIVNGTTNYILDEMSTKGLSFETALATAQELGYAEADPTADVDGLDAAAKAAIIASLAFHTRVGLDDVSVEGIREVTADDIREAHASGCELKLLAIAQRRDDEHAQGVSVRVHPALVPNDHPLASVHGAYNAVLVEAESAGRLMFYGQGAGGAPTASAVLSDVVAAAAHRVHGGQAPRESSYASLPVLGPEAAVTRYQIQLRSDDAVGSLAAMASVFAENEVSINSVRQSAYVTSDGSHDQAVVTFVTHPAPVFHLDAAVEGLRDSDRVAEVVSIQRVEGE$","Homoserine dehydrogenase","Cytoplasm","homoserine dehydrogenase","homoserine dehydrogenase ","Homoserine dehydrogenase","","Chipman D.M., Shaanan B. The ACT domain family. Curr. Opin. Struct. Biol. 2001. 11(6):694-700. PMID: 11751050","","","

InterPro
IPR001342
Domain

Homoserine dehydrogenase, catalytic
PF00742	$\"[143-325]T$	Homoserine_dh
PS01042	$\"[189-211]T$	HOMOSER_DHGENASE

InterPro
IPR002912
Domain

Amino acid-binding ACT
PF01842	$\"[358-426]T$	ACT

InterPro
IPR005106
Domain

Homoserine dehydrogenase, NAD-binding
PF03447	$\"[18-135]T$	NAD_binding_3

noIPR
unintegrated

unintegrated
G3DSA:3.30.360.10	$\"[153-310]T$	no description
PIRSF000098	$\"[10-442]T$	Homoserine dehydrogenase
PTHR21499	$\"[71-442]T$	ASPARTATE KINASE
PTHR21499:SF2	$\"[71-442]T$	HOMOSERINE DEHYDROGENASE

","BeTs to 22 clades of COG0460COG name: Homoserine dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0460 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001342 (Homoserine dehydrogenase) with a combined E-value of 1.6e-68. IPB001342A 12-32 IPB001342B 98-112 IPB001342C 134-145 IPB001342D 162-172 IPB001342E 189-217 IPB001342F 273-294 IPB001342G 308-324","","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 135 (E_value = 3.6e-31) place ANA_1405 in the NAD_binding_3 family which is described as Homoserine dehydrogenase, NAD binding domain.Residues 143 to 325 (E_value = 2e-92) place ANA_1405 in the Homoserine_dh family which is described as Homoserine dehydrogenase.Residues 358 to 426 (E_value = 1.3e-05) place ANA_1405 in the ACT family which is described as ACT domain.","","dehydrogenase (HdH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1409","1509225","1507402","1824","5.05","-12.34","63170","ATGAACACAATGTCCACGGGCGCCGCCTCTCGGCCGGCCCTCACGCGAGGGGCGGTGAGGGGGGCCGCTGCCATCCTCACTCTCTTCCTTGTCGCGATCTTGTCGCAGTTCGCCCCCCAGGCGAGCGCTGAGCAGAACAAGAGCGTCAACGTCACCAACCTGTCTCTGACACGGGTGGACGGTAACAACGTCGAGCAGGACGGACAGCTCAACACCTACGACCTCGCCCGTCTCAGCTTCGACTGGAGCGGTGTCGACGCCAACCTCAAGAGCGGCGACTCCTTCACGATCGGTCTGGGTGAGTACTTCACCAACCTGCAGAACAGCGAGACCCACCCCATGACCGTCGAGTACGGCGGCAAGGATGTCGAGGTCGGTACCTGCACCCTGACCGTCAAGGACGTCACCTGCACCTTCAACTCCAAGGTTGACGAGCTCAAGGCTGCCGGCTTCCACAACTTCAAGGGTTCCGGCTCCGCCCTGGTGTCCGTTGCCAAGGCCACCGACGTGCAGTCCGTTGACTTCACCGTCAACGGTGTCACCACCACCGTCACCCTGCCCGGTGGCGGCGGCATCGGCGGCCCCAAGGAGAGCGACTGGGAGCTCACCAAGTGGGCCTCCAGCTTCTACAACGACTACAAGGAGCTGACCTGGGGTGTGAACTTCGGGACCAACCAGACCACTGGTGACAAGCTCGGCAAGACCTTCGACGGCTCCCGTCAGAGCATCGTCTTCACCGACACCCTCGGTGGCGGCATGGCCTTCAACCAGGCTGACGCCACTCGCACGGTCCTCAACCTGCGTCCTGCGGACGGCAAGTCCATCCCGGTGACCAACGCCGCTGGCCAGGACGCCACCACCCAGTACGGTGACTACGACGTCAAGGCCACCTACTCCCAGGACGGCCGCACCGCCACCTACGAGGTGACCGGTCCGTTCAAGAACGGCACCAACTTCACCCTGGAGTACCCCGTCTCCTTCGTGGACGCCAACGGCAAGGCCGTCGCCGCCTCGCGGGGCACCTCCTACGAGAACACCGTCAACCTCAACGGCACGGACTTGACCAGCACTCAGCAGCAGTCCTACGTCCAGTACTTCGACATCTCGGTCCAGATGGAGCCCGGCTTCGGCAGCTTCAACGTGACCAAGGTCGTTGAGGGTGAGGCCGCCGCGAAGGCCGCCGGCTCCAGCTTCGTCGTTGACGTCGCCTACGAGCTGCCGGCCGCTGCCAGCTCCTACCCGGACTGGAAGGCTCCCGAGGGCCAGAAGGCCACTGGCGAGGGCCGTACCGGAACCTCCTCCGTCACGGTTAAGCCCGGTGAGCCGGTCGCCTTCGACGGCACCTTCCCCGTGGGCACCAAGGTCACGCTCTCCGAGGACACCTCCAAGGCCCAGCCCGCCGCCTCCGGCTTCAGCTGGGGTGAGCCGGTCTTCACCATCGACGGTCAGAAGACCAACACCTTCACCATCCGCGACCAGGAGCTCGTCAAGGTCTCTCTGACCAACACGACGACGACCACCTCGACGCCGCCGACGACCACGCAGACCCCGCCCACGGTGACCACTCCGCCGGCGACCCCGCCGACCACCACGCAGGCCCCGCCTACGGTCGACAACCCGCCGGCGACCCCGCCGACCACTACGCAGCAGCCGCCGAGCACCCCGGGTGCTCCGGTGCCGCCCACCTCCACCCCGAAGACGCCGAACGGTGGCACCCCGCCGCTGGCGCACACCGGTGCTAACGCCGTTGCGCTCGTGCTGCTCGCCGGCGCCGGCCTGGGTGGCGGTGCCCTGCTGGTGGCTCGTCGCCGCAACGCCTCCTGA","MNTMSTGAASRPALTRGAVRGAAAILTLFLVAILSQFAPQASAEQNKSVNVTNLSLTRVDGNNVEQDGQLNTYDLARLSFDWSGVDANLKSGDSFTIGLGEYFTNLQNSETHPMTVEYGGKDVEVGTCTLTVKDVTCTFNSKVDELKAAGFHNFKGSGSALVSVAKATDVQSVDFTVNGVTTTVTLPGGGGIGGPKESDWELTKWASSFYNDYKELTWGVNFGTNQTTGDKLGKTFDGSRQSIVFTDTLGGGMAFNQADATRTVLNLRPADGKSIPVTNAAGQDATTQYGDYDVKATYSQDGRTATYEVTGPFKNGTNFTLEYPVSFVDANGKAVAASRGTSYENTVNLNGTDLTSTQQQSYVQYFDISVQMEPGFGSFNVTKVVEGEAAAKAAGSSFVVDVAYELPAAASSYPDWKAPEGQKATGEGRTGTSSVTVKPGEPVAFDGTFPVGTKVTLSEDTSKAQPAASGFSWGEPVFTIDGQKTNTFTIRDQELVKVSLTNTTTTTSTPPTTTQTPPTVTTPPATPPTTTQAPPTVDNPPATPPTTTQQPPSTPGAPVPPTSTPKTPNGGTPPLAHTGANAVALVLLAGAGLGGGALLVARRRNAS$","LPXTG-motif cell wall anchor","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","LPXTG-motif cell wall anchor domain","","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
TIGR01167	$\"[574-606]T$	LPXTG_anchor: LPXTG-motif cell wall anchor

noIPR
unintegrated

unintegrated
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[21-39]?$ $\"[581-601]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB008883 (Tumour susceptibility gene 101) with a combined E-value of 5.3e-06. IPB008883C 534-574 IPB008883C 527-567 IPB008883C 520-560 IPB008883C 526-566 IPB008883C 517-557 IPB008883C 521-561 IPB008883C 509-549 IPB008883C 518-558 IPB008883C 510-550 IPB008883C 533-573 IPB008883C 516-556 IPB008883C 523-563 IPB008883C 503-543 IPB008883C 528-568 IPB008883C 524-564 IPB008883C 544-584 IPB008883C 525-565 IPB008883C 541-581 IPB008883C 522-562 IPB008883C 511-551 IPB008883C 538-578 IPB008883C 535-575 IPB008883C 530-570 IPB008883C 504-544 IPB008883C 508-548 IPB008883C 501-541 IPB008883C 513-553","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1410","1511173","1509713","1461","4.92","-27.48","51319","ATGACTGACCAGATTCCCGCCGGAGAGCCGCCCCTGGGGTCACTGGCCTGCCCCGAGCCCGAGGACCGTCCCGACCTGTGGCCCACCACGGCACGGCGCACGGCCGACGGTGAGCTCGCCCTGGGCGGGCTGACCGTCTCCGAGATCCTCACCGAGGCTCCCAGCCCCGTCTTCGTCCTGGATGAGGCCGACCTGCGCGGTCGCGCCGCCTCCTGGGCCGCCGCCATGCATGAGGAGTTCTGGCCCAGCTATGGCATGGCCGGGGGAGAGGCCTTCTACGCAGGGAAGGCCTTCCTGACCACCAAGGTCGCCCAGTGGGTCCTCGAGGAGGGTATGGGCATCGACACCGCCAGCCGCGGCGAGCTCGCCGTGTCCCTCGCCGCCCTGCAGGAGGTGGACGGGGAGGAGGCCACCACGGACGCCACCCGTCTGGGCCTGCACGGTAACGGCAAGACGCAGGCCGAGATCGCCGTCGCCCTCACCCACCACGTGGGCCACCTCGTCCTCGACTCCCTCGAGGAGGTCGACCTCGCCGTCCGCGCCGTGCGTGAGCTGCGTGCCAGTGGCGTCTACGGGCCCGAGGAGACCGGCAAGGTCATGGTGCGCCTGACCACCGGCGTGCACGCCGGTGGCCACGAGTACATCTCCACCGGTCATGAGGACCAGAAGTTCGGCCTCTCCGTCCACGGAGGCGCTGCCCGGTGCGCCATTGACGCGATCATCTCCGCCCCTGAGCTCGAGCTGCACGGGCTGCACTCCCACATCGGCTCCCAGATCCTGGACCTGGCCGGCTTCCGGGAGGCCGTCGGCATTGTCCTCACCCTGCGCCACGAGGTCGCCGTCGACACCGGGCACCTGTGCCCGGAGGTCGACCTGGGCGGTGGCTATGGCATCGCCTACACCGGGGCCGACCCGGTGCCGCCCAGTCCGGCACAGGTCGCCCGCACCCTGGCTGAGGCCGTGCGCGAGACCTGCGAGCGTCTTGGGGATGAGGTCCCCACCGTCTCCATCGAGCCCGGTCGCGCAGTAGCCGGCCCGACGACGGTCACCCTCTACACCGTCACCGGCCTCAAGCGTGTCGAGCTGGGGGAGGGGGCCTCGCGTCTCTACGTCAGCATCGACGGCGGCATGAGCGACAACATCCGCCCCGCCCTCTACGAGGCCGCCTACACGGCCCTGGTCGCCAACCGCCGCCCCGACCCGCAGGCCGGGCTGGTGCGCAGCCGGGTAGTGGGCAAGCACTGCGAGTCCGGCGACGTCGTCGTGCGCGACGTGGACCTGCCCGCCGACCTGGCCGTCGGTGACGTGCTGGCCGTGCCCGCCACCGGCGCCTACGGGCGCTCCATGGCCTCTAACTACAACCTCTTCACCCGCCCCGGCGTGCGCTGGGTGCGAGAGGGCGAGTCGGGCTGGGTCCTGCGCCCCGAGACCATCGAGGACCTCATTCGCCTCGAGGGCTGA","MTDQIPAGEPPLGSLACPEPEDRPDLWPTTARRTADGELALGGLTVSEILTEAPSPVFVLDEADLRGRAASWAAAMHEEFWPSYGMAGGEAFYAGKAFLTTKVAQWVLEEGMGIDTASRGELAVSLAALQEVDGEEATTDATRLGLHGNGKTQAEIAVALTHHVGHLVLDSLEEVDLAVRAVRELRASGVYGPEETGKVMVRLTTGVHAGGHEYISTGHEDQKFGLSVHGGAARCAIDAIISAPELELHGLHSHIGSQILDLAGFREAVGIVLTLRHEVAVDTGHLCPEVDLGGGYGIAYTGADPVPPSPAQVARTLAEAVRETCERLGDEVPTVSIEPGRAVAGPTTVTLYTVTGLKRVELGEGASRLYVSIDGGMSDNIRPALYEAAYTALVANRRPDPQAGLVRSRVVGKHCESGDVVVRDVDLPADLAVGDVLAVPATGAYGRSMASNYNLFTRPGVRWVREGESGWVLRPETIEDLIRLEG$","Diaminopimelate decarboxylase","Cytoplasm","diaminopimelate decarboxylase","diaminopimelate decarboxylase ","diaminopimelate decarboxylase","","Sandmeier E., Hale T.I., Christen P. Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 1994. 221(3):997-1002. PMID: 8181483Martin C., Cami B., Yeh P., Stragier P., Parsot C., Patte J.C. Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases. Mol. Biol. Evol. 1988. 5(5):549-559. PMID: 3143046Poulin R., Lu L., Ackermann B., Bey P., Pegg A.E. Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites. J. Biol. Chem. 1992. 267(1):150-158. PMID: 1730582Moore R.C., Boyle S.M. Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli. J. Bacteriol. 1990. 172(8):4631-4640. PMID: 2198270","","","

InterPro
IPR000183
Domain

Orn/DAP/Arg decarboxylase 2
PR01179	$\"[93-111]T$ $\"[113-125]T$ $\"[245-258]T$ $\"[335-354]T$ $\"[443-456]T$	ODADCRBXLASE
PF00278	$\"[349-464]T$	Orn_DAP_Arg_deC
PF02784	$\"[61-346]T$	Orn_Arg_deC_N
PS00878	$\"[93-111]T$	ODR_DC_2_1
PS00879	$\"[280-297]?$	ODR_DC_2_2

InterPro
IPR002986
Domain

Diaminopimelate decarboxylase
PR01181	$\"[111-128]T$ $\"[368-386]T$ $\"[453-475]T$	DAPDCRBXLASE
TIGR01048	$\"[31-486]T$	lysA: diaminopimelate decarboxylase

noIPR
unintegrated

unintegrated
G3DSA:2.40.37.10	$\"[302-485]T$	no description
PTHR11482	$\"[37-483]T$	ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE
PTHR11482:SF5	$\"[37-483]T$	DIAMINOPIMELATE DECARBOXYLASE

","BeTs to 19 clades of COG0019COG name: Diaminopimelate decarboxylaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0019 is a-mp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000183 (Orn/DAP/Arg decarboxylase, family 2) with a combined E-value of 3.3e-30. IPB000183B 113-122 IPB000183C 141-175 IPB000183D 248-259 IPB000183E 287-296 IPB000183F 338-358 IPB000183G 434-454***** IPB002986 (Diaminopimelate decarboxylase signature) with a combined E-value of 1.3e-23. IPB002986A 111-128 IPB002986B 217-226 IPB002986C 368-386 IPB002986D 453-475***** IPB002985 (Arginine decarboxylase signature) with a combined E-value of 2.7e-09. IPB002985D 168-189 IPB002985F 325-342 IPB002985I 443-464","","","-59% similar to PDB:1HKV MYCOBACTERIUM DIAMINOPIMELATE DICARBOXYLASE (LYSA) (E_value = 2.3E_94);-59% similar to PDB:1HKW MYCOBACTERIUM DIAMINOPIMELATE DICARBOXYLASE (LYSA) (E_value = 2.3E_94);-59% similar to PDB:2O0T The three dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation (E_value = 2.3E_94);-47% similar to PDB:1TUF Crystal structure of Diaminopimelate Decarboxylase from m. jannaschi (E_value = 4.3E_40);-47% similar to PDB:1TWI Crystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysine (E_value = 4.3E_40);","Residues 61 to 346 (E_value = 4.5e-44) place ANA_1410 in the Orn_Arg_deC_N family which is described as Pyridoxal-dependent decarboxylase, pyridoxal binding domain.Residues 349 to 464 (E_value = 6.9e-34) place ANA_1410 in the Orn_DAP_Arg_deC family which is described as Pyridoxal-dependent decarboxylase, C-terminal sheet domain.","","decarboxylase (lysA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1411","1512865","1511180","1686","5.16","-21.65","60246","GTGACCCCAGAAGAGCTTGCCGCAGCCATCCGCACCGTCCTGGAGGAGGCCTCCGCCGAGGGCTCCCTCGCCCTGCCCGCCGCGGAGATTCCCGCCCCCCGCGTCGAGCGCCCCCGCAACCGCGACCACGGTGACTGGTCCACCAACGTGGCCATGCAGCTGGCCAAGAAGGCCGGCACCAAGCCGCGCGATCTCGCCGAGCTCCTCGTCCCTCGTCTTGAGGCCCTCGACGGCATCGCCTCCGTGGAGGTCGCCGGCCCCGGCTTTCTCAACATCCGCCTCGACGCCGCCAGCGCCGGCGAGCTTGCCCGCTCCATCGTCGAGGCCGGTCAGGCCTACGGCCGCAACGACTCCCTGAGTGGCCAGCACATCAATCTCGAGTACGTCTCGGCCAACCCGACCGGGCCGGTCCACCTGGGTGGCGCCCGCTGGGCCGCCGTCGGCGACTCCCTGGCCCGAATCCTGTCCGCCTGCGGTGCCCAGGTCACCCGGGAGTATTACTTCAACGACCACGGCACCCAGATCGACCGCTTCGCCCGTTCCCTGCTGGCCTCCGCGCGCGGCCAGGAGACCCCCGAGGACGGCTACGGCGGTGCCTACATCAGTGAGATCGCCCAGCAGGTGACTGCCGACGAGCTCGCCGCCGGCCGCCCAGACCCGGCCACCCTGCCCGACGCCGAGGCCACCGAGGTCTTCCGCTCCCGCGGCGTCGATCTCATGTTCGCCGCCGTCAAGGCTGAGCTGCACGCCTTCCGCTCCGACTTCGATGTCTTCTTCCACGAGGACTCCCTGCACACCTCCGGTGCCGTCGAGCGCGCCATCGCCCGGCTGCGCGAGCGCGGTGTCATCGAGGAGCGCGACGGCGCCACCTGGCTGCGCACCACCGACTTCGGGGACGACAAGGACCGCGTCCTCATCAAGTCTGACGGCAACGCCGCCTACTTCGCCGCCGACCTCGCCTACTACCTGGACAAGCGCGAGCGTGGCGCCGACTGCGCGGTCTACCTGCTCGGGGCCGACCACCACGGCTACATCGGCCGCATGATGGCCATGTGTGCGGCCTTCGGGGACACCCCCGGCACCAACATGCAGATCCTCATCGGTCAGCTCGTCAACCTCGTGCGCAACGGCGTCCCGGTGCGCATGTCCAAGCGCGCCGGCACCATCGTCACCCTGGAGGACCTGGTCGACGCCGTCGGCGTGGACGCAGCCCGCTACGCCCTGGCCCGCTCCTCCATGGACTCCATGATCGACATCGACCTGGATTTGCTGGCCTCCTCCACCTCCGACAACCCCGTCTACTACGTCCAGTACGCCCACGCCCGCACCCGCAACGTGGCCCGCAACGCCGCCGAGCACGGCGTGAGCCGGGACCCGAACGAGGCGCCCTTCGAGCCCGGTGCCCTGGACGATCCTGCCGACGCCGCCTTGCTGGGGGTCCTGGCCCAGTTCCCCGCCACCGTGGCCCAGGCCGCGCAGCTGCGCGAACAGCACCGCGTGGCCCGCTACCTCGAGCAGCTCGCTGCCGCCTACCACGCCTGGTACGGCGCCACCCGCGTCACTCCCCGTGGGGACGACGCCGTGGACTCCGGGCACGTCGCCCGCCTGTGGCTCAACGACGCCGTCGGGCAGGTCCTGGCCAACGGGCTCGACCTGCTGGGTGTGAGCGCCCCCGAGAGGATGTGA","VTPEELAAAIRTVLEEASAEGSLALPAAEIPAPRVERPRNRDHGDWSTNVAMQLAKKAGTKPRDLAELLVPRLEALDGIASVEVAGPGFLNIRLDAASAGELARSIVEAGQAYGRNDSLSGQHINLEYVSANPTGPVHLGGARWAAVGDSLARILSACGAQVTREYYFNDHGTQIDRFARSLLASARGQETPEDGYGGAYISEIAQQVTADELAAGRPDPATLPDAEATEVFRSRGVDLMFAAVKAELHAFRSDFDVFFHEDSLHTSGAVERAIARLRERGVIEERDGATWLRTTDFGDDKDRVLIKSDGNAAYFAADLAYYLDKRERGADCAVYLLGADHHGYIGRMMAMCAAFGDTPGTNMQILIGQLVNLVRNGVPVRMSKRAGTIVTLEDLVDAVGVDAARYALARSSMDSMIDIDLDLLASSTSDNPVYYVQYAHARTRNVARNAAEHGVSRDPNEAPFEPGALDDPADAALLGVLAQFPATVAQAAQLREQHRVARYLEQLAAAYHAWYGATRVTPRGDDAVDSGHVARLWLNDAVGQVLANGLDLLGVSAPERM$","Arginyl-tRNA synthetase","Cytoplasm","arginyl-tRNA synthetase","arginyl-tRNA synthetase ","arginyl-tRNA synthetase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR001278
Family

Arginyl-tRNA synthetase, class Ic
PR01038	$\"[123-138]T$ $\"[138-154]T$ $\"[162-175]T$ $\"[304-325]T$	TRNASYNTHARG
PTHR11956	$\"[31-561]T$	ARGINYL-TRNA SYNTHETASE
PF00750	$\"[102-421]T$	tRNA-synt_1d
TIGR00456	$\"[10-561]T$	argS: arginyl-tRNA synthetase

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[133-142]T$	AA_TRNA_LIGASE_I

InterPro
IPR005148
Domain

Arginyl tRNA synthetase, N-terminal
PF03485	$\"[11-94]T$	Arg_tRNA_synt_N

InterPro
IPR008909
Domain

DALR anticodon binding
PF05746	$\"[436-561]T$	DALR_1

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[120-439]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.730.10	$\"[440-561]T$	no description
G3DSA:3.30.1360.70	$\"[5-115]T$	no description

","BeTs to 26 clades of COG0018COG name: Arginyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0018 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB005148 (Arginyl tRNA synthetase N-terminal domain) with a combined E-value of 1.2e-101. IPB005148A 44-64 IPB005148B 79-92 IPB005148C 124-178 IPB005148D 304-320 IPB005148E 382-398 IPB005148F 430-449 IPB005148G 497-516 IPB005148H 535-561***** IPB013155 (tRNA synthetase, valyl/leucyl, anticodon-binding) with a combined E-value of 2.4e-10. IPB013155B 130-172 IPB013155H 379-405","","","-35% similar to PDB:1BS2 YEAST ARGINYL-TRNA SYNTHETASE (E_value = 6.9E_13);-35% similar to PDB:1F7U CRYSTAL STRUCTURE OF THE ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNA(ARG) AND L-ARG (E_value = 6.9E_13);-35% similar to PDB:1F7V CRYSTAL STRUCTURE OF YEAST ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNAARG (E_value = 6.9E_13);-44% similar to PDB:1IQ0 THERMUS THERMOPHILUS ARGINYL-TRNA SYNTHETASE (E_value = 5.0E_11);","Residues 11 to 94 (E_value = 3.8e-28) place ANA_1411 in the Arg_tRNA_synt_N family which is described as Arginyl tRNA synthetase N terminal domain.Residues 102 to 421 (E_value = 3e-132) place ANA_1411 in the tRNA-synt_1d family which is described as tRNA synthetases class I (R).Residues 436 to 561 (E_value = 1.4e-39) place ANA_1411 in the DALR_1 family which is described as DALR anticodon binding domain.","","synthetase (argS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1413","1513961","1513206","756","6.44","-2.33","27625","GTGCCGCCTGCCGCGTCACGAACCCGCCGTCCTGCCGTCATCGCCCACCGCGGCGGCGGACGTGAGGTTCCCGAGAACACCTGGAGCGCCGTCGAGCACGTGGCCGCGCTCGGGCTGGAGTGGATGGAGACCGATCTGCGGCTGACCGCCGACGGCGTCGTCGTGCTCAGCCACGACGAGGACCTGCGGCGTACCGCGAACGATCCCCGCACCGTGGGGGAGGTCATGTGGGCCGAGCTGGCCGACCTCGACTCCGGCGACGGGCGCGGCTTCGTCCGGCTCGACGACGCCCTGCACGCCCAGCCGGCGATGAAGTTCAATATCGACCTCAAGGACTCCAGCGTCGTCCAGGCGGCCCTGCAGACGGTGCGTGACGCCCAGGCCCTCGAGCGAGTCCGGTTCGCCTCCTTCTCCGCCCGTCGGCTGGCCGTGCTGCGCCGCCAGGAGCCGCGGGCCATGACCTCACTGGGAGTCAGTGACGTGCTCGGACTCATGCTGCGCAGCGAGGCGGCCGTCCCCCTGCCCCAGACCCGCTGGGGCTGGACCCGCGGCAGGGTCGACGCCGTCCAGGTGCCGGAGAGCTACCACGGCGTCCCGGTGGTCACCCGCCGCTTCGTCGCCTCCGCGCACACCGCGGGCCTGGAGGTCCACGTCTGGACGGTGGACGACCCCGAGCGGATGCGCTACCTGGCCGACCTCAACGTGGACGCCATCATGACCGACGTCCCCAGCCTCGCCCTCAAGACACTCAGCTGA","VPPAASRTRRPAVIAHRGGGREVPENTWSAVEHVAALGLEWMETDLRLTADGVVVLSHDEDLRRTANDPRTVGEVMWAELADLDSGDGRGFVRLDDALHAQPAMKFNIDLKDSSVVQAALQTVRDAQALERVRFASFSARRLAVLRRQEPRAMTSLGVSDVLGLMLRSEAAVPLPQTRWGWTRGRVDAVQVPESYHGVPVVTRRFVASAHTAGLEVHVWTVDDPERMRYLADLNVDAIMTDVPSLALKTLS$","Glycerophosphoryl diester phosphodiesterase","Cytoplasm","glycerophosphoryl diester phosphodiesterase","glycerophosphoryl diester phosphodiesterase","glycerophosphoryl diester phosphodiesterase","","","","","

InterPro
IPR004129
Family

Glycerophosphoryl diester phosphodiesterase
PTHR23344	$\"[10-250]T$	GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE
PF03009	$\"[16-245]T$	GDPD

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.190	$\"[8-251]T$	no description

","BeTs to 15 clades of COG0584COG name: Glycerophosphoryl diester phosphodiesteraseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0584 is -o-pkzy-vdrlb-efgh---j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB004129 (Glycerophosphoryl diester phosphodiesterase) with a combined E-value of 3.5e-18. IPB004129A 11-20 IPB004129B 24-59","","","-44% similar to PDB:2OTD The crystal structure of the glycerophosphodiester phosphodiesterase from Shigella flexneri 2a (E_value = 2.7E_15);-43% similar to PDB:1ZCC Crystal structure of glycerophosphodiester phosphodiesterase from Agrobacterium tumefaciens str.C58 (E_value = 1.2E_12);-42% similar to PDB:2O55 Crystal Structure of a putative glycerophosphodiester phosphodiesterase from Galdieria sulphuraria (E_value = 6.2E_12);-41% similar to PDB:1V8E Crystal Structure of Glycerophosphoryl Diester Phosphodiesterase from Thermus thermophilus HB8 (E_value = 1.8E_11);-41% similar to PDB:1VD6 Crystal Structure of Glycerophosphoryl Diester Phosphodiesterase complexed with Glycerol (E_value = 1.8E_11);","Residues 16 to 245 (E_value = 5.5e-42) place ANA_1413 in the GDPD family which is described as Glycerophosphoryl diester phosphodiesterase family.","","diester phosphodiesterase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1414","1516412","1513974","2439","9.46","18.90","84621","GTGCTGGTTCTCCTGGCAAGACCCACAGGAGACCGCTACTGTTTTAACCGAGTACAACCCAGGCTGTCGCTCTGGCAGCCGCCACATCGTGAACGCCGGGGCGCCGGCAGCAACGATTTCCCTATGACATTCAGCCACCTGGAGGCTTCCCACGTGACCCCGCAGCCCATGAGTCGACGCCAGCGTCGCGAGGCGGAACGTGCTGCCGAAGCCGCTCGCCACGTCGCTGAGGCGCAGGCCGGAACTGCCCCGTCGTCACCGTCGGCGACGCACACCACCCACGTCGCCGGAGCCACTCGCCGCTCACGTCGCGACCTTCACGCTCACCGTGCCGAGAACGGCGCCGCCTCCAGCCCCGTCACTGCTCCGAGCCCATCGGCTCTCCCCGACGTCCCGGTCGCCCCGCAGAAGCAGAACCATCCGCAGCGGCCCGTGGCGCCGGCAACGCCTGCGACAGCGGTTTCAGGCACGCGGAGGGGAGCGCGCTCAGGGGGCGGTTCAGCGCCGTCGGTCACCGTAGACCCGGCGCCGTCGCAGCCCGTTGCACCGATGAGCCGGATGGCCCGCCGGCGTCAGAATGCCAGTGCACAGCCCGAGCAGCCGCAGGCCTCGGCGCCTCAGGCGCTCAGCGCCGCATCTGCGGCCCCATCGGTCTCCTCCTCATCCTCCTCAGCGCAGGTCGCCGGCGACACTCGCCCCACTCGACGCTCTCGGAAGGACCTGCGCACCGCCCAGGTCTTCGAGGACCCCGAGCAGACGAGGGAGAACCCCGCCGTCGAGGGCGCTGCGCAGCCCGAGGCTCACCGTCCCGAGAGCCACTCCGAGCGCCGCCACGGCCAGCACCGTTCTCATCGCGGCCACCAGGCTGTGCCCGCCGCGGCACCATCAACGCCCTCGGCGCTGTCGCCCCTGGTCGCAGCCTCACTGGCCGAGTCCACCTCAGGGCTCGAGCCGGCAGACACTCACCCCGCCGGTGCCGCGCCGTGGTGGGCCGCTAGTGGCACGGCTCCTGCTTCGCCTGGTGACACACAGGGTGACGGTCATCGGCACGCAGCCGCGCAGACCGCCCCCGCCGAGCCGGAGGTCGGGGTGACCTCCGAGCCCGCCTCCCGATCCGCGGGCCGTCGCCGGCAACGCGCCTCCGCCGCAGCCCCAGCCTCGACCGCCTCGGCCAAGCCCGTCGTCGCCTCCACGCCCCACCACACCGCCACCTTCGACGTCGCCGGCACGCAGGCGGACCACCCCGCCGTCCAGACGCCGCAGGCTGAGCCGTCGGCGCTCGCGGAGCAGGCTCCCTCCGCTCCCGAGACGCCCCACGAGATTCGGTTCTCGCAGCGGATTACGGACTTCCGAGGTGCCGAGACCATCGAGGTCCCCGAGGTTCGCAAGATCATGGCTGCCCGCAAGGCCGGGGTGCCGCTCGCGGACGAGGAGACCATCCGCGCCATCAAGGCCGCCCGGAGCACTAGGAAGACCAAGTCCGAGAAGTCAGCCGCCCAGGCCAAGCGAGGCGAGGCGGCCGATGAGGCCAGCTCCCCGGCGTCGTCGGCCAAGGCCAAAGCGGCATCGAAGCCGGACACCCACCGCGACTCCTCGACCGGACCTGCCCCCGCCCGTCCCATCCGGCGCCGCACCGGCTCCGGGATTCTGGGGCGCACCGCCGTCCTGTCGGTTCTGGCTATGGCCACGGTGCTCGCCCCCTTGTCCAGCCACCTCGACAACACCCCGCTGGCCTCGGCCGCCATGAAGATGCACTCCAACGGCTCCGCCACGCAGAGCCCGGCCGCCGGCGGCACGAAGGCCTCCTCCGTGGCCAGCGCCGTGCTCGGCAGCGACGACCTGGACGACGACTCCGACACCCAGCTGTCCAACGTGCCCGACGCCGCCACCCGGGCCCGGATCCGTGAGGCCTTCCAGAACGCCGCCAAGACCTGCTCCTCGGCCACAGGAGCCTCCGGCGACACCACCGCCTTCAGCACCAAGCCGCAGCTGTTCTACCCGATGCTTCCGGGCACCTACGAGATCTCCTCCGAGTACGGGTACCGCACTCACCCCACCCTCGGCTACCGCAAGCTGCACGCCGGGCAGGACATGGCCGCCCCCGTGGGGACGCCCATCTACGCGGCCGCCGCCGGCACCGTCACCACCGCCGGTATGGTCGACGGCACCGGAACCATCACCATCAAGCACGAGATCGACGGCCAGGTCTGGTACACCAGCTACCTGCACATGTACGAGGACGGCATCCACGTCAAGGTCGGTGACACCGTCACGGCCGGTCAGATGATCGCCGGCGTGGGTAACACGGGCCGGTCCTCCGGTTCTCACCTGCACTTCGAGGTGCGCACCAAGGACGACACCGCCGACGAGTCCACCGTGGAGCCGTGGGGCTGGCTCAAGCAGCACAACGCCGTCGAGCTCACCACCAACTGCAGCTGA","VLVLLARPTGDRYCFNRVQPRLSLWQPPHRERRGAGSNDFPMTFSHLEASHVTPQPMSRRQRREAERAAEAARHVAEAQAGTAPSSPSATHTTHVAGATRRSRRDLHAHRAENGAASSPVTAPSPSALPDVPVAPQKQNHPQRPVAPATPATAVSGTRRGARSGGGSAPSVTVDPAPSQPVAPMSRMARRRQNASAQPEQPQASAPQALSAASAAPSVSSSSSSAQVAGDTRPTRRSRKDLRTAQVFEDPEQTRENPAVEGAAQPEAHRPESHSERRHGQHRSHRGHQAVPAAAPSTPSALSPLVAASLAESTSGLEPADTHPAGAAPWWAASGTAPASPGDTQGDGHRHAAAQTAPAEPEVGVTSEPASRSAGRRRQRASAAAPASTASAKPVVASTPHHTATFDVAGTQADHPAVQTPQAEPSALAEQAPSAPETPHEIRFSQRITDFRGAETIEVPEVRKIMAARKAGVPLADEETIRAIKAARSTRKTKSEKSAAQAKRGEAADEASSPASSAKAKAASKPDTHRDSSTGPAPARPIRRRTGSGILGRTAVLSVLAMATVLAPLSSHLDNTPLASAAMKMHSNGSATQSPAAGGTKASSVASAVLGSDDLDDDSDTQLSNVPDAATRARIREAFQNAAKTCSSATGASGDTTAFSTKPQLFYPMLPGTYEISSEYGYRTHPTLGYRKLHAGQDMAAPVGTPIYAAAAGTVTTAGMVDGTGTITIKHEIDGQVWYTSYLHMYEDGIHVKVGDTVTAGQMIAGVGNTGRSSGSHLHFEVRTKDDTADESTVEPWGWLKQHNAVELTTNCS$","Membrane protein related to metalloendopeptidase","Extracellular","M23/M37 peptidase domain protein protein","hypothetical protein","peptidase M23B","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR002886
Family

Peptidase M23B
PTHR21666:SF7	$\"[673-796]T$	M23/M37 PEPTIDASE FAMILY MEMBER
PF01551	$\"[691-795]T$	Peptidase_M23

noIPR
unintegrated

unintegrated
PTHR21666	$\"[673-796]T$	PEPTIDASE-RELATED

","BeTs to 16 clades of COG0739COG name: Membrane proteins related to metalloendopeptidasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0739 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 4","***** IPB002886 (Peptidase M23/M37) with a combined E-value of 4e-15. IPB002886A 703-712 IPB002886B 726-770","","","-42% similar to PDB:2GU1 Crystal structure of a zinc containing peptidase from vibrio cholerae (E_value = 1.3E_10);","Residues 691 to 795 (E_value = 7.3e-30) place ANA_1414 in the Peptidase_M23 family which is described as Peptidase family M23.","","peptidase domain protein protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1415","1517682","1516603","1080","4.66","-23.15","37789","ATGAGCACTCCGCTCGCCCTCCTGATCACCATCATCCTCCTGGCCGGCAACGCCTTCTTCGTCGGCGCCGAGTTCGCCGTCACCTCCTCACGCCGCAGCCAGCTCGAGCCACTGGCCGAGGCAGGCGACGCTCGCGCCGCCACCGCCCTGTGGGCCCTGCAGAACGTCTCGCGCATGCTGGCCACCGCCCAGCTCGGCGTCACCCTGTGCTCCACCGGCCTGGGCGTCGTCGCCGAGCCGGCCATCGCCCACGCCCTGGAGCCCCTGCTCGCGGCCGTCGGTGTCGGGCACGCCGGCTCCCATGCCGTCGCCGTCGTCATCGCCCTGGTCATCGTCGTGGGCCTGCACGTCGTCGCCGGGGAGATGGTGCCCAAGAACATCTCCATCGCCTCCCCGGAGAAGGCCGTGCGCTGGCTCGCCTCGCCCCTGGTGTGGTGCTCGCGCGTCTTCAGCCCCGTGGTCAACGCTCTCAACGGCTTCGCCAACGGGGTCCTGAGGGTCCTGGGCATTGAGGCCAAGGAGGAGATCGCCGCGGCCTTCAACGCCGAGGAGGTCGCCTCCATCGTCGAGCGCTCCACCGCCGAAGGAGTCCTGGAGGACTCCACCGGCCTGCTCAGCGGCGCCTTGGAGTTCTCCGAGGAGACCGCCGGCAGCGTCATGGTGCCCCTGAGCGAGCTCGTCACCCTGCCCCAGGACTGCACCCCGGAGGACGTGGAGCGGGCCGTGGCCTCCACCGGCTTCTCCCGCTTCCCGCTGGTGGCCGACCCGGCCGCAGTTGAAGAGGGGGAGGAGCCCGTCATCACCGGCTACCTGCACCTCAAGGACATCCTCTACGCCGACGGCGCTGAGCGCACCGAACCGGTACCTGCCTGGCGCGCTCGCGCGCTCGTGCCCGTCGGCTACGACGACGAGGTCGAGGAGGCGCTGGCGGCCATGCAGCGCTCGGGGGCTCACCTCGGGCACGTGCGCAACGCGCAGGGGCGCTTCGTCGGGGTCCTCTTCCTGGAGGATATCCTCGAAGAGCTCGTCGGCGAGGTCAACGACGCCATGCAGCGCGAAGAGCACCAGCGCCGTGATTAA","MSTPLALLITIILLAGNAFFVGAEFAVTSSRRSQLEPLAEAGDARAATALWALQNVSRMLATAQLGVTLCSTGLGVVAEPAIAHALEPLLAAVGVGHAGSHAVAVVIALVIVVGLHVVAGEMVPKNISIASPEKAVRWLASPLVWCSRVFSPVVNALNGFANGVLRVLGIEAKEEIAAAFNAEEVASIVERSTAEGVLEDSTGLLSGALEFSEETAGSVMVPLSELVTLPQDCTPEDVERAVASTGFSRFPLVADPAAVEEGEEPVITGYLHLKDILYADGAERTEPVPAWRARALVPVGYDDEVEEALAAMQRSGAHLGHVRNAQGRFVGVLFLEDILEELVGEVNDAMQREEHQRRD$","Uncharacterized CBS domain-containing protein","Membrane, Cytoplasm, Extracellular","Uncharacterized CBS domain-containing proteins","integral membrane protein","protein of unknown function DUF21","","Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 2004. 113(2):274-284. PMID: 14722619Carr G., Simmons N., Sayer J. A role for CBS domain 2 in trafficking of chloride channel CLC-5. Biochem. Biophys. Res. Commun. 2003. 310(2):600-605. PMID: 14521953Hebeisen S., Biela A., Giese B., Muller-Newen G., Hidalgo P., Fahlke C. The role of the carboxyl terminus in ClC chloride channel function. J. Biol. Chem. 2004. 279(13):13140-13147. PMID: 14718533","","","

InterPro
IPR000644
Domain

Cystathionine-beta-synthase
PF00571	$\"[220-343]T$	CBS

InterPro
IPR002550
Domain

Protein of unknown function DUF21
PF01595	$\"[5-202]T$	DUF21

noIPR
unintegrated

unintegrated
PTHR22777	$\"[39-354]T$	HEMOLYSIN-RELATED
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[5-27]?$	transmembrane_regions

","BeTs to 20 clades of COG1253COG name: Hemolysins and related proteins containing CBS domainsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1253 is -o----yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB005170 (Transporter associated domain) with a combined E-value of 3e-14. IPB005170A 204-226 IPB005170C 312-351***** IPB002550 (CBS) with a combined E-value of 9.3e-07. IPB002550 318-349","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 202 (E_value = 3.4e-74) place ANA_1415 in the DUF21 family which is described as Domain of unknown function DUF21.Residues 220 to 343 (E_value = 6.5e-14) place ANA_1415 in the CBS family which is described as CBS domain pair.","","CBS domain-containing proteins","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1416","1519022","1517679","1344","5.32","-14.08","46914","ATGACCGACTGGCTCATGATCGCCGTCGGCGTGGTCCTTACCGTGGGCACCGCCCTGTTCGTGGCCGGTGAGTTCTCCCTGGTGGCCCTCGACCCCTCCACCGTCGAGACCCGTGCTGCCACCGGTGACAAGCGCGCCACCACCGTTCAGCGGGCCCTGGGGCGACTGTCCACCCTCCTGTCCGGCGCCCAGGTCGGCATCACCCTGACCACCGTGCTCTTGGGCTACACCATGCAGGCGGCCCTGGCGAACCTGCTCACCGGCCTCATGAGCCACTGGCTGGCCGTCTCCGTGGCCACTGGCGCCGCAGTCGTCATCGCCCTCATCGTCGTCAACGCCTTCTCCATGGTCATCGGCGAGCTCATCCCCAAGAACGCCACCCTGGCCGACCCCATGCGCGCCGCCGGCCTCGTGGCCCCCTTCCTCATGGGCTTCACCACCCTGCTCAAGCCCCTCATCGTCCTGCTCAACGGCGCCGCCAACGCCGTCCTGCACGCCATGGGCATCGAGCCCGCCGAGGAGCTCAGCGGCACCCGCAGCGCCGGCGAGCTCGCCTCCCTCGTGCGCCACAGCGCCGAGGAAGGCACCCTCGACGCCTCCACCGCCACCCTGCTCACCCGCTCCATCGGACTGGGGGCCCTCACCGCCGTCGACGTCATGACCGACCGCGGCCGCCTCCACACCCTCGAGGCCGACGACTCCGCAGAGGACGTCGTGCACCTGGCCCGCGCCACCGGCCACTCCCGCTTCCCCGTCATCGGCCGCGACATCGATGACGTCATGGGCATCGTCCACCTGCGCCGCGCCATCGGCGTCCCCTACGAGCGGCGCGCCGACGTCCCCGTCGCCTCCACCTCCCTCATGACGCCCGCGCCCCGCGTCCCCGAGACCATGCCGCTGGCCAACCTGCTCGTCGAGCTGCGCGCCCAGGGCTCCCAGATGGCGATCGTCGTCGACGAGTACGGCGGCACCGCCGGCGTCGTTACCCTTGAGGACGCCGTCGAGGAGGTCGTCGGGGACGTCGCCGACGAGCACGACCGCCGCCGCGCCGGCGCCCACCTCGACCCCTCGGGCCACTGGGTCGTCCCCGGGTGGATGCGCCCCGACGAGCTCGCCACCCGTGCCGCCATCCAGGTGCCCGACGACGGCCCCTACGAGACCCTCGGTGGCCTGGTCATGACCGAGCTCGGCCGCATCCCCGCCGTCGGCGACGTCGTCGACCTGCCCCACGCCTCACTGACCGTCGACGCCATGGACGGGCGTCGCGTCACCCGCCTCCACGTGCGCCCCAAGGACCCCGAGGCCGCCCCCGGAAGCCGAGGACCAGAGGGGGAGCGCCGATGA","MTDWLMIAVGVVLTVGTALFVAGEFSLVALDPSTVETRAATGDKRATTVQRALGRLSTLLSGAQVGITLTTVLLGYTMQAALANLLTGLMSHWLAVSVATGAAVVIALIVVNAFSMVIGELIPKNATLADPMRAAGLVAPFLMGFTTLLKPLIVLLNGAANAVLHAMGIEPAEELSGTRSAGELASLVRHSAEEGTLDASTATLLTRSIGLGALTAVDVMTDRGRLHTLEADDSAEDVVHLARATGHSRFPVIGRDIDDVMGIVHLRRAIGVPYERRADVPVASTSLMTPAPRVPETMPLANLLVELRAQGSQMAIVVDEYGGTAGVVTLEDAVEEVVGDVADEHDRRRAGAHLDPSGHWVVPGWMRPDELATRAAIQVPDDGPYETLGGLVMTELGRIPAVGDVVDLPHASLTVDAMDGRRVTRLHVRPKDPEAAPGSRGPEGERR$","Hemolysin containing CBS domain protein","Membrane, Cytoplasm, Extracellular","CBS domain protein","hypothetical protein","protein of unknown function DUF21","","Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 2004. 113(2):274-284. PMID: 14722619Carr G., Simmons N., Sayer J. A role for CBS domain 2 in trafficking of chloride channel CLC-5. Biochem. Biophys. Res. Commun. 2003. 310(2):600-605. PMID: 14521953Hebeisen S., Biela A., Giese B., Muller-Newen G., Hidalgo P., Fahlke C. The role of the carboxyl terminus in ClC chloride channel function. J. Biol. Chem. 2004. 279(13):13140-13147. PMID: 14718533","","","

InterPro
IPR000644
Domain

Cystathionine-beta-synthase
PF00571	$\"[220-338]T$	CBS
SM00116	$\"[225-274]T$ $\"[290-338]T$	CBS

InterPro
IPR002550
Domain

Protein of unknown function DUF21
PF01595	$\"[5-201]T$	DUF21

InterPro
IPR005170
Domain

Transporter-associated region
PF03471	$\"[353-432]T$	CorC_HlyC

noIPR
unintegrated

unintegrated
PTHR22777	$\"[39-447]T$	HEMOLYSIN-RELATED
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[58-92]?$ $\"[98-118]?$ $\"[139-159]?$	transmembrane_regions

","BeTs to 20 clades of COG1253COG name: Hemolysins and related proteins containing CBS domainsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1253 is -o----yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB005170 (Transporter associated domain) with a combined E-value of 3.5e-39. IPB005170A 204-226 IPB005170B 258-270 IPB005170C 307-346 IPB005170D 382-400***** IPB002550 (CBS) with a combined E-value of 8.7e-18. IPB002550 313-344","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 201 (E_value = 2e-52) place ANA_1416 in the DUF21 family which is described as Domain of unknown function DUF21.Residues 220 to 338 (E_value = 7.1e-21) place ANA_1416 in the CBS family which is described as CBS domain pair.Residues 353 to 432 (E_value = 1.3e-20) place ANA_1416 in the CorC_HlyC family which is described as Transporter associated domain.","","domain protein (AF212041)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1417","1519450","1520100","651","7.74","2.69","24980","ATGCCATCGGAATGCCATCGGAGGACTAACCGTCCCGACACCTCAGTTCCGCGAGCGGATCTCAGCAGGCTTCGCGTTCGAGGACGGCTGGAGGACGTCGAGGGTAACCTGAGGATGCTGCTGCGAAAGAAGACGGAAATGGGAAGTTCGATCTTTATCCAGGTCCAATTTGTTGCGACTCCAGAGAATCGTTCCAAGGTCGAGCTCTTCGAGTCCCACTGGCTTGCAGAGCCAGGAGTCGACCAGGTCGTGCTCCGCCACGAACGGACACATGCGGAACAGACGGTCCGGCATGACCAGTGTCAGAATCGGGAAGAGTTGCGGCAACCTTGCAGGTATCGGCGGGAGAGCGTTGTAATTATGCAGGACGGCACCGCGGTGCCCTGCTGCAAAGATTTCGACACGAAGGCACCACCGGGTAACGCTTTCGAGCAGGATCTGGGTGAGATATGGAATGGAGATGTTGTGCAGTCGATGCACCGCTCGCACATTGACACTAATTATGACGCCATCTCATTATGCGCAAATTGTTCGGGATGGCAGGGAGAGCCAGTGTTCCCCGCGAAGGAAACTAAGGAACGAGTTCGTGGATTCGCGCAGTTAAAGAGTTCATTCCGCGACGAGCCACGACACATAAGGGCACGGGAATGA","MPSECHRRTNRPDTSVPRADLSRLRVRGRLEDVEGNLRMLLRKKTEMGSSIFIQVQFVATPENRSKVELFESHWLAEPGVDQVVLRHERTHAEQTVRHDQCQNREELRQPCRYRRESVVIMQDGTAVPCCKDFDTKAPPGNAFEQDLGEIWNGDVVQSMHRSHIDTNYDAISLCANCSGWQGEPVFPAKETKERVRGFAQLKSSFRDEPRHIRARE$","Radical SAM, fragment","Cytoplasm, Extracellular","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 111-179 are 55% similar to a (DOMAIN SAM RADICAL COFACTOR MODIFYING SIMILAR ENZYME CJ1618C OXIDOREDUCTASES BIOSYNTHESIS) protein domain (PD858867) which is seen in Q83DA2_COXBU.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:06:17 2007","Mon Aug 6 11:06:17 2007","Mon Aug 6 11:06:17 2007","Mon Aug 6 11:05:33 2007","","","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","Mon Aug 6 11:05:33 2007","","Mon Aug 6 11:05:33 2007","","Mon Aug 6 11:05:33 2007","yes","","" "ANA_1418","1521288","1521713","426","5.27","-7.46","15388","ATCGCCGCAGGCCCGCTTCCCACTTACCACTTCGGGGTATATGCGCGCATTGTGCGGGACGGCCGGCTGTTGTGCGTGAAAAAGACACGCGGCCCCTACACTGGTCTGCTCGACCTCCCCGGCGGGCAACCCGAATTCGCTGAGAACTGGGAAGATGCCCTCCGACGCGAGTTGACCGAGGAGGTGGGTGCCGAGTCCGTGTCCATCTCTAGTTGTGCTCGGTTCTCGCTACATGTCGAATTTAACGCCGCTGGCGAGAATATCGACTTCCACCACCATGGAGCCGTCGCAGATGTGCACCTGTGGAGCGCGCTTCCTGAACACGGAATGTCGTCATCGGACACGAATGGATGGGAGTGGTTCGATCTCGGATCAGGTGACCGATTGTGTCTCAGCCCCCTAGCACGATCGGTTCTAGATGGATGA","IAAGPLPTYHFGVYARIVRDGRLLCVKKTRGPYTGLLDLPGGQPEFAENWEDALRRELTEEVGAESVSISSCARFSLHVEFNAAGENIDFHHHGAVADVHLWSALPEHGMSSSDTNGWEWFDLGSGDRLCLSPLARSVLDG$","MutT/NUDIX family protein","Cytoplasm","NUDIX domain protein","MutT/NUDIX family protein","NUDIX hydrolase","","Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 1992. 174(20):6321-6325. PMID: 1328155Koonin E.V. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 1993. 21(20):4847-4847. PMID: 8233837Mejean V., Salles C., Bullions L.C., Bessman M.J., Claverys J.P. Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydrolases. Mol. Microbiol. 1994. 11(2):323-330. PMID: 8170394Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 1993. 268(31):23524-23530. PMID: 8226881McLennan A.G. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int. J. Mol. Med. 1999. 4(1):79-89. PMID: 10373642Bessman M.J., Frick D.N., O. Handley S.F. The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes. J. Biol. Chem. 1996. 271(41):25059-25062. PMID: 8810257","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[37-51]T$ $\"[51-66]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[12-123]T$	no description
PF00293	$\"[9-140]T$	NUDIX
PS00893	$\"[42-63]T$	NUDIX

noIPR
unintegrated

unintegrated
PTHR22769	$\"[13-65]T$	MUTT/NUDIX HYDROLASE

","BeTs to 15 clades of COG0494COG name: NTP pyrophosphohydrolases (MutT family) including oxidative damage repair enzymesFunctional Class: L,RThe phylogenetic pattern of COG0494 is a-T-YqvCEBRHuj---linxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 405 to 536 (E_value = 1.9e-05) place ANA_1418 in the NUDIX family which is described as NUDIX domain.","","domain protein","","1","","","Mon Aug 6 10:46:40 2007","","Mon Aug 6 10:46:40 2007","","","Mon Aug 6 10:46:40 2007","Mon Aug 6 10:46:40 2007","Mon Aug 6 10:46:40 2007","","","Mon Aug 6 10:46:40 2007","","","Mon Aug 6 10:46:40 2007","Mon Aug 6 10:46:40 2007","","","Mon Aug 6 10:46:40 2007","Mon Aug 6 10:46:40 2007","","","","","yes","","" "ANA_1419","1522163","1525990","3828","5.91","-22.99","139124","GTGCCCACGCAGGACCAGATCAGCCCAGGCTTCGGTGCCAACGAGTGGATGGTGGAGGAGATGCGGGCCGCCTGGTCGGCGGATCCGTCCTCCGTGAGTCCGCAGTGGCGCGAGCTCTTCGAGACCGATCCGGGTGCCGGTCTGCACCAGCCTGGTCCAGCCTCCTCCAACGGTTCTGCCTCGTCGGCCGCCGGCGGGCCGCGCCGGGCCACTATCACGCCCCAGGCCGCCTCCACCCTGCGCCGCTCCTCCGCCGTCCAGGACGTCACGCGCTCCGACCTGCCGCCGGCCCCGCCGTCGGACACCGCACCCCCGACCTCCCCCTACGCCCAGCGCCAGGCCGCCCACCCCGCTCACGACCAGGACGGTGACGCCTACGAGGACCGCGTTACCAGGCTCAAGGGTGCGGCGGCCCGCACCGCTAAGAACATGGACGATTCCCTGTCCATGCCCACTGCCACCTCCGCCCGGGCCGTGCCCGCCAAGGTCCTCATTGAGAACCGGGCCGTCATCAACACCCACCTGGCCCGCACCCGCGGCGGCAAGGTCTCCTTCACCCACCTCATCGGCTGGGCGGTCGTCGAGTCCCTGACCGAGATGCCCTCGATGAACGTCTCCTACGGGGTCGATGAGGCAGGCAAGCCGGTCCTGCACGAGCCCGCCCACGTGGCCTTCGGCCTGGCCATCGACGTGCCCGGCTCCGACGGGCAGCGCCGCCTGCTGGTGCCCTCCATCAAGCAGGCCGACCTCATGGACCTGTCCCAGTTCGTGAAGGCCTACGAGGCCCTCGTGGCCAAGGCCCGCGAGAACAAGCTGGACCTTGACGACTTCCGGGGTACCACCGTGACCCTGACCAACCCCGGCATGATCGGCACCCTGCACTCGGTGCCGCGCCTCATGCCCGGTCAGGGGCTCATCGTCGGGGTCGGCGCCATGGACTACCCGGCCGCCTTCGCCGGTGCCAGCCCCGATACCCTAGCCCGCCAGGCCATCGGCAAGGTCGTCACCCTGACCTCCACCTACGACCACCGCGTCATCCAGGGCGCCGCCTCCGGCGAGTTCCTGCGCCTGGTGGAGCGCAAGCTCCTGGGACTGGACGGCTTCTGGAACCGGGCCTTCGAGTCCCTGCGCATCCCCCTCGAGCCGGTCAAGTGGGTGCGCGACACCACCTACGACCCCGAGCTGGAGACCGGCAAGCCGGCGCGCGTGGCCGAGCTCATCCACGCCTACCGCCAGCGCGGCCACCTGGCGGCCGACAACGACCCGCTCACCTACCGCCTGCGCCGCCACCCCGACCTGGACATCACCTCCTACGGGCTGAGCCTGTGGGACCTGGACCGCTCCTTCCCCACCCGGGGCCTGGGCGGGCGCGACCGGGCAACCCTGCGCGAGATCCTCAGGATGCTGCGCGACGCCTACTGCCGCACCGTGGGCGTGGAGTACATGCACATCCAGGACCCGGCCCAGCGCGCCTGGTGGCAGGAGCGCCTCGAGCGCGACTGGGAGGACATCGCCGACGAGGAGCGCCGTCGGATCCTCACCAAGCTGGAGCAGGCCGAGGCCTTCGAGACCTTCCTGCAGACCAAGTACGTGGGCCAGAAGCGCTTCAGCCTCGAGGGCGGGGAGTCCCTCATCGTGGCCCTGGACCGCCTGCTCGACGCCGCCGCCCACGACGGCCTCGACGAGGTCGTCATCGGCATGGCCCACCGCGGCCGCCTCAACGTGCTCACCAACATCGCCGGCAAGTCCTACGGCCAGGTCTTCGACGAGTTCGAGGGCAACGGCGTCATCGAGGGCGCCGGCACCGGGGACGTCAAGTACCACCTGGGCACCGTGGGCGTCTTCTCCGGGACCGACGGCGTCTCCACCCGCGTCTCCCTGGCCGCCAACCCCTCCCACCTGGAGACGGTCGACGGCGTCGTCGAGGGCATCGTGCGCGCCAAGCAGGACCGCATCGGCCTGGGCGAGAAGGGCTACACGGTCATGCCGGTCCTCGTCCACGGTGACGCCGCCTTCGCCGGCCAGGGCGTGGTCTACGAGACCCTCAACATGAGCCAGCTGCCCGCCTACCGCACCGGCGGCACCGTCCACATCGTCGTCAACAACCAGATCGGCTTCACCACCGGCTCGGCTTCGGCCCGCTCCACCATCTACGCCACCGACCTGGCCAAGGGCCTGCAGGTGCCGATCTTCCACGTCAACGCCGACGACCCCGAGACGGTGGCCCGCACCGCCCGCCACGCCTACGAGTACCGACGCACCTTCCACAAGGACGTCATCATCGACCTCATCTGCTACCGGCGGCGCGGCCACAACGAGGGCGACGACCCCTCGATGACCCAGCCGCTCATGTACCGGCTCATCGACTCGCTGGACTCCACGCGCGGCGTCTACACCGCCGCCCTCGTGGGGCGCGGCGACATCACCCCGCAGGAGGCCCAGGAGATCGCCAAGAGCTACCAGGACGAGCTGGAGAGGGTCTTCACCGAGGCCCGCATCCAGGTCACCGGGGGCACGGGCTCCGACGGCGCCGGGGACGCCGCCGACACCTCCACACAGGATCTGTCGGACCCCACGAAGGTGGGCGTGCCCCTGTCCTCCCTGGAGATCCCCTACTCCCAGCGGGCGGGCACCGGCATGATGCTCGGCTGGACCTCGGCCGTGCCGCGCGACGTCGTCGAGCGCATCGGCGACGCCCAGGTCGCCTGGCCCGAGTCCTTCACCGTCCACCCCAAGCTCCAGGCCATGCTCTCCAAGCGCCGCGAGGCCACCCGCGAGGGCGGCATCGACTGGGGACTCGGGGAGCTCATCGCCCTGGGGAGCCTGCTCATGGAGGGCGTGCCGATCCGCCTGGCCGGTGAGGACGCCCGCCGCGCCACCTTCGCCCAGCGCCACGCCGTCCTGCACGACCACACCTCCGGGCAGGAGTGGACGCCCCTGAGCTTCCTGACCCCGGACCAGGCGCCCCTGGAGATCTACGACTCCCTGCTCAGTGAGTACGCCGCCCTGGCCTTCGAGTACGGCTACTCCGTGGAGCGCCCTGAGGGACTGACCATGTGGGAGGCCCAGTTCGGCGACTTCGCCAACGGCGCCCAGTCCGTCATCGATGAGTACGTCACCTCCGCCGCCCAGAAGTGGGGGCAGCGATCCGGCCTGGTCATGCTGCTCCCCCACGGCCAGGAGGGGCAGGGACCCGACCACTCCTCGGCCCGCATCGAGCGCTACCTGCAGATGTGCGCCCAGGACAACATGCTGGTGGCTCAGCCCTCCACGCCCGCCAGCTACTTCCACCTGCTGCGCGAGCACACCTACACCCGCCCGCGCCGCCCGCTCATCGTCTTCACCCCCAAGCAACTGCTGCGTCTGAAGGCCGCCTGCTCCCCGGTGGAGGCCTTCACCTCCGGCACCTTCCAGCCGGTCATCGGGGAGACCGACGACGCCGTCCTGGCCTCGGCGCAGAAACAGGGCGTGGACCGGGTGCTGCTGTGCTCGGGTCGCGTCTACTACGACCTGCTGGCCCACCGGACCAAGACCGGGGACACGAGAACGGCCATCGTCCGCCTCGAGCAGCTCTACCCGCTGGAGAGCTCGGCCATCGCCGAGGCACTGGCCCCCTTCAGCGGGGCCGAGCTCGTGTGGGTCCAGGACGAGCCCGCCAACCAGGGCATGTGGCCCTACCTGGCGCTCAACCTGCCGACCGACCTGACCGGCGGCGTCCTGCCCACGCTGATCTCCCGGCCCGAGGCCGCCGCCCCAGCGGTGGGCACCGCCGGTCTCCACCGCGCCCAGCAGGAGGAGATCCTCCGCCAGGCCTTCGCCCGCCGCTGA","VPTQDQISPGFGANEWMVEEMRAAWSADPSSVSPQWRELFETDPGAGLHQPGPASSNGSASSAAGGPRRATITPQAASTLRRSSAVQDVTRSDLPPAPPSDTAPPTSPYAQRQAAHPAHDQDGDAYEDRVTRLKGAAARTAKNMDDSLSMPTATSARAVPAKVLIENRAVINTHLARTRGGKVSFTHLIGWAVVESLTEMPSMNVSYGVDEAGKPVLHEPAHVAFGLAIDVPGSDGQRRLLVPSIKQADLMDLSQFVKAYEALVAKARENKLDLDDFRGTTVTLTNPGMIGTLHSVPRLMPGQGLIVGVGAMDYPAAFAGASPDTLARQAIGKVVTLTSTYDHRVIQGAASGEFLRLVERKLLGLDGFWNRAFESLRIPLEPVKWVRDTTYDPELETGKPARVAELIHAYRQRGHLAADNDPLTYRLRRHPDLDITSYGLSLWDLDRSFPTRGLGGRDRATLREILRMLRDAYCRTVGVEYMHIQDPAQRAWWQERLERDWEDIADEERRRILTKLEQAEAFETFLQTKYVGQKRFSLEGGESLIVALDRLLDAAAHDGLDEVVIGMAHRGRLNVLTNIAGKSYGQVFDEFEGNGVIEGAGTGDVKYHLGTVGVFSGTDGVSTRVSLAANPSHLETVDGVVEGIVRAKQDRIGLGEKGYTVMPVLVHGDAAFAGQGVVYETLNMSQLPAYRTGGTVHIVVNNQIGFTTGSASARSTIYATDLAKGLQVPIFHVNADDPETVARTARHAYEYRRTFHKDVIIDLICYRRRGHNEGDDPSMTQPLMYRLIDSLDSTRGVYTAALVGRGDITPQEAQEIAKSYQDELERVFTEARIQVTGGTGSDGAGDAADTSTQDLSDPTKVGVPLSSLEIPYSQRAGTGMMLGWTSAVPRDVVERIGDAQVAWPESFTVHPKLQAMLSKRREATREGGIDWGLGELIALGSLLMEGVPIRLAGEDARRATFAQRHAVLHDHTSGQEWTPLSFLTPDQAPLEIYDSLLSEYAALAFEYGYSVERPEGLTMWEAQFGDFANGAQSVIDEYVTSAAQKWGQRSGLVMLLPHGQEGQGPDHSSARIERYLQMCAQDNMLVAQPSTPASYFHLLREHTYTRPRRPLIVFTPKQLLRLKAACSPVEAFTSGTFQPVIGETDDAVLASAQKQGVDRVLLCSGRVYYDLLAHRTKTGDTRTAIVRLEQLYPLESSAIAEALAPFSGAELVWVQDEPANQGMWPYLALNLPTDLTGGVLPTLISRPEAAAPAVGTAGLHRAQQEEILRQAFARR$","2-oxoglutarate dehydrogenase E1 component","Cytoplasm","2-oxoglutarate dehydrogenase E1 component","2-oxoglutarate dehydrogenase; E1 component ","2-oxoglutarate dehydrogenase, E1 subunit","","Mattevi A., Obmolova G., Kalk K.H., Westphal A.H., de Kok A., Hol W.G. Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 A resolution. J. Mol. Biol. 1993. 230(4):1183-1199. PMID: 8487300","","","

InterPro
IPR001017
Domain

Dehydrogenase, E1 component
PF00676	$\"[514-840]T$	E1_dh

InterPro
IPR001078
Domain

Catalytic domain of components of various dehydrogenase complexes
PD001115	$\"[285-362]T$	Q7U0A6_MYCBO_Q7U0A6;
PF00198	$\"[125-365]T$	2-oxoacid_dh

InterPro
IPR005475
Domain

Transketolase, central region
PF02779	$\"[927-1123]T$	Transket_pyr

InterPro
IPR011603
Family

2-oxoglutarate dehydrogenase, E1 component
PIRSF000157	$\"[7-1275]T$	2-oxoglutarate dehydrogenase, E1 component
PTHR23152	$\"[657-832]T$ $\"[849-1272]T$	2-OXOGLUTARATE DEHYDROGENASE
TIGR00239	$\"[325-1272]T$	2oxo_dh_E1: 2-oxoglutarate dehydrogenase, E

noIPR
unintegrated

unintegrated
G3DSA:3.30.559.10	$\"[125-362]T$	no description
G3DSA:3.40.50.970	$\"[503-832]T$	no description

","BeTs to 12 clades of COG0567COG name: Pyruvate and 2-oxoglutarate dehydrogenases, E1 componentFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0567 is ------y--dr-b-efghsn-jxi--Number of proteins in this genome belonging to this COG is 1","***** IPB001078 (Catalytic domain of components of various dehydrogenase complexes) with a combined E-value of 7.9e-27. IPB001078B 229-268 IPB001078C 279-309 IPB001078D 334-370***** IPB004167 (E3 binding domain) with a combined E-value of 2.3e-21. IPB004167C 182-206 IPB004167E 267-309 IPB004167F 337-349***** IPB001017 (Dehydrogenase, E1 component) with a combined E-value of 1.3e-14. IPB001017D 668-705 IPB001017F 757-776***** IPB005475 (Transketolase, central region) with a combined E-value of 1e-06. IPB005475C 1062-1091","","","-46% similar to PDB:1C4T CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E_value = 2.1E_15);-46% similar to PDB:1E2O CATALYTIC DOMAIN FROM DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E_value = 2.1E_15);-46% similar to PDB:1SCZ Improved structural model for the catalytic domain of E.coli dihydrolipoamide succinyltransferase (E_value = 2.1E_15);-45% similar to PDB:1B5S DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS (E_value = 2.4E_11);-44% similar to PDB:2IHW Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), apo form (E_value = 1.2E_10);","Residues 125 to 365 (E_value = 1.2e-21) place ANA_1419 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain).Residues 514 to 840 (E_value = 1.2e-42) place ANA_1419 in the E1_dh family which is described as Dehydrogenase E1 component.Residues 927 to 1123 (E_value = 1.4e-50) place ANA_1419 in the Transket_pyr family which is described as Transketolase, pyrimidine binding domain.","","dehydrogenase E1 component (sucA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1421","1526121","1526714","594","5.56","-5.65","21358","ATGCGTGAGACGAGGCTGAGCTTCATCGGTGACGAGCTGGTGGCCGGTCATGGTGACGGGCGCGCCCTGGGATGGACGGGCCGGGTCATGGCCCGTACACCCCGGGACGCCGACATCCTGTGGACCTCCCTGGCGGTTCCCGGTGAGACGACCGCGCAGATGTCCGACCGCTGGGGGCCCGAGGTGGCCCGGCGCTCCACGCACACCGGCATCAACCGGCTCGTCGTGGGACTGGGCGTGGCCGACGTGCTCGCCGGCATCTCCTACGCCCGCTCCCGCCTGGCCCTGGCCAACATCCTCGACACGGCCGCCTCCGACCACCGCGAGTGCTTCGTCGTCGGGCCCCCTCCCCTGCCCGAGGCCGACCCCGACGCCACCGCCCAGCTGTCCCAGGCCGCCGAGGAGGTGTGCCTGCGGCGCAACGTGCCCTACGTGGACGCCTTCGAGCCGCTGCGCAACCACGAGCAGTGGACGGCCGACGTCGCCGCCGCCGGCGGCACGCACCCGGGCCAGGCCGGCTACGGTCTGCTGGCCTGGCTGGTGCTGCACCGCGGCTGGTACGAGTGGCTCGGCGTCGAGCGCCCCGAGTCCTGA","MRETRLSFIGDELVAGHGDGRALGWTGRVMARTPRDADILWTSLAVPGETTAQMSDRWGPEVARRSTHTGINRLVVGLGVADVLAGISYARSRLALANILDTAASDHRECFVVGPPPLPEADPDATAQLSQAAEEVCLRRNVPYVDAFEPLRNHEQWTADVAAAGGTHPGQAGYGLLAWLVLHRGWYEWLGVERPES$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","Upton C., Buckley J.T. A new family of lipolytic enzymes?. Trends Biochem. Sci. 1995. 20(5):178-179. PMID: 7610479","","","

InterPro
IPR001087
Family

Lipolytic enzyme, G-D-S-L
PF00657	$\"[74-181]T$	Lipase_GDSL

InterPro
IPR013831
Domain

Esterase, SGNH hydrolase-type, subgroup
G3DSA:3.40.50.1110	$\"[3-191]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:1VJG Crystal structure of putative lipase from the G-D-S-L family from Nostoc sp. at 2.01 A resolution (E_value = 5.3E_15);-43% similar to PDB:1Z8H Crystal structure of Putative lipase from the G-D-S-L family (17135349) from NOSTOC SP. PCC 7120 at 2.02 A resolution (E_value = 5.3E_15);","Residues 74 to 181 (E_value = 8.6e-05) place ANA_1421 in the Lipase_GDSL family which is described as GDSL-like Lipase/Acylhydrolase.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1422","1527512","1526733","780","7.37","0.96","28359","GTGGGTATGGCCTTGCCGGCTCCTCCTCAACGACGGCGGTGTGACATGAACCTGAAGAACCTGACAGCACCAGACCAGTGGACACTCTCTGACAACTCGCTCCTGCGGCGCATCCTCGTGTGCTTCCTGGGGGAGGTGATCACGGCGGTCGGGATCGCGATCTGCCTGGAGGGCAAGAGCGGCGTCGACCCGTTCACCGCCTTCCTCCAAGGCATCTCCCACGTCTCTGGGATCTCCTTCGCGGCGATCGTCCCGATCGTCAACATCATCATGCTGATCCTCGTCTTCCCCTTCGACCGGTCCATCTTCGGCCTGGGGACAGTCATCAACTTCACCGTCGTGGGTGTCCTCGTGGACTACTTCCGCCCGATCTACCGCAGCTTCTTCCATGTCGAGTACTCCTTCGGCAGCATGCTGCTCCACCTGGCGATCGGGCTGCCGCTGTTCTGCCTGGGAGTCTCCATGTACATCACCTGCGACCTGGGCCAGTGCCCTTATGACGGGATCGCGCCCTCGCTCAGGCGGCACTTCCCGCGCTACAGCTACCGCGTCTACCGGCTGGTTCAGGACATCGTCACAATCTTCCTGGCCCTGCTCCTGATCAGGTTCGACCTCTCGCTGGGCATCGTCGCCCTGGGTACGGTCATCATGGGCTTCTTCATCGGCCCCATCGTCGGTTTCTTCAACAACCACGTCTCCAACCGCCTGGTGGGGATCAGCGGTGACATCTTCGCCGTCTCCGAGTCGTCGTCTGACGAAGGCTCCCCGGCGCCTGCCTGA","VGMALPAPPQRRRCDMNLKNLTAPDQWTLSDNSLLRRILVCFLGEVITAVGIAICLEGKSGVDPFTAFLQGISHVSGISFAAIVPIVNIIMLILVFPFDRSIFGLGTVINFTVVGVLVDYFRPIYRSFFHVEYSFGSMLLHLAIGLPLFCLGVSMYITCDLGQCPYDGIAPSLRRHFPRYSYRVYRLVQDIVTIFLALLLIRFDLSLGIVALGTVIMGFFIGPIVGFFNNHVSNRLVGISGDIFAVSESSSDEGSPAPA$","Uncharacterized membrane protein","Membrane, Cytoplasm","Uncharacterized BCR, YitT family COG1284subfamily, putative","hypothetical protein","protein of unknown function DUF161","","","","","

InterPro
IPR003740
Family

Protein of unknown function DUF161
PF02588	$\"[37-118]T$	DUF161

noIPR
unintegrated

unintegrated
tmhmm	$\"[38-56]?$ $\"[75-97]?$ $\"[102-122]?$ $\"[141-161]?$ $\"[182-202]?$ $\"[208-228]?$	transmembrane_regions

","BeTs to 4 clades of COG2364COG name: Uncharacterized membrane proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2364 is ---------d--b----h--------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 37 to 118 (E_value = 1.6e-06) place ANA_1422 in the DUF161 family which is described as Uncharacterized BCR, YitT family COG1284.","","BCR, YitT family COG1284 subfamily, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1423","1528429","1527992","438","7.37","0.98","15795","ATGACAGACCGCATGGAATCGGGAACCCACGGTGACAACAGCGCCGAGCCCACCAAGAACCCCAAGACGGCGGATGGCTCCCAGGACTGCTCCTGCGCCGAGGCCCGCGCCCACCTGGAGGCCTTCCTCGATCGCGAGTGCACCGCCGACCTGGCCGAGCGCCTCGCCCAGCACGTGGCCACCTGCTCGCACTGCTCCCGCCTCGCTGACGCCGAGACCCACTTGCGGGAGATCCTGCGCTCGCGGTGCGCCGAGCAGGCCCCTCCCGAGCTGCGCGCCCGGGTCCTGGGGCGCCTGTCGGCCCTGCGCGCCACTGCGGTGAGCGTGACGACGACGTCGACCACGACTCGGACCCAGGCCTCCGCCTCCGGGCGGGTCGTGCGCGTCGTGGAGTCCCGGGTCGAGTCCTCCCGGACCGTCCGCTTCGAGCGCGACTGA","MTDRMESGTHGDNSAEPTKNPKTADGSQDCSCAEARAHLEAFLDRECTADLAERLAQHVATCSHCSRLADAETHLREILRSRCAEQAPPELRARVLGRLSALRATAVSVTTTSTTTRTQASASGRVVRVVESRVESSRTVRFERD$","Hypothetical protein","Cytoplasm, Periplasm","putative membrane protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

InterPro
IPR014295
Family

Anti-sigma factor RshA
TIGR02949	$\"[24-106]T$	anti_SigH_actin: anti-sigma factor, TIGR029

InterPro
IPR000838
Domain

RNA polymerase sigma factor 70, ECF
PS01063	$\"[92-123]?$	SIGMA70_ECF

InterPro
IPR007627
Domain

RNA polymerase sigma-70 region 2
PF04542	$\"[70-138]T$	Sigma70_r2

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[175-225]T$	no description

InterPro
IPR013249
Domain

RNA polymerase sigma factor 70, region 4 type 2
PF08281	$\"[176-229]T$	Sigma70_r4_2

InterPro
IPR014284
Domain

RNA polymerase sigma-70
TIGR02937	$\"[65-233]T$	sigma70-ECF: RNA polymerase sigma factor, s

InterPro
IPR014293
Family

RNA polymerase sigma-70, actinobacteria
TIGR02947	$\"[55-247]T$	SigH_actino: RNA polymerase sigma-70 factor

noIPR
unintegrated

unintegrated
G3DSA:1.10.1740.10	$\"[54-140]T$	no description

","BeTs to 12 clades of COG1595COG name: DNA-directed RNA polymerase specialized sigma subunits, sigma24 homologsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1595 is --------vdrlbcefghsn-j--t-Number of proteins in this genome belonging to this COG is 3","***** IPB000838 (Sigma factor, ECF subfamily) with a combined E-value of 2.1e-45. IPB000838A 94-130 IPB000838B 183-229***** IPB007630 (Sigma-70 region 4) with a combined E-value of 1.2e-17. IPB007630A 88-121 IPB007630B 203-230 IPB007630A 94-127","","","-91% similar to PDB:1H3L N-TERMINAL FRAGMENT OF SIGR FROM STREPTOMYCES COELICOLOR (E_value = 2.7E_28);-52% similar to PDB:1OR7 Crystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseA (E_value = 7.3E_18);","Residues 70 to 138 (E_value = 2.8e-20) place ANA_1424 in the Sigma70_r2 family which is described as Sigma-70 region 2.Residues 176 to 229 (E_value = 2.2e-18) place ANA_1424 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 182 to 231 (E_value = 1.5e-15) place ANA_1424 in the Sigma70_r4 family which is described as Sigma-70, region 4.","","polymerase sigma-70 factor, ECF subfamily (RPOE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1425","1529283","1529963","681","11.73","17.60","23553","GTGCGCCCCGCCGGCGGGCGGTCCGGCTCGACGGCGACACGATCGAGTGCTGGATGCTCATGTCCCGGCCAACGCGATGGCGCCCTGATTTCATTCCCCGTCCGCCCTGAGCGAGGCACGCACCACCTTCGAGCAGCGATATCGCTGGCCCGAGCCGCCCGCGTAGGCCAGGATGGGGGCATGAACATTCTGCGCTCCTTCGCCCGCCCCATGCTCGCCGCGCCCTTCATCGTCGATGGACTCGATGCCCTGGTGCGCCCCTCGCGCCACGTGGAGAAGTTCGAGAAGGTCGCCCCGACGCTGGAGCGGGTCGGTCTGCCGCCCGTGCTGGCCTCCGACGCCCGGCTGCTCACCCGCGCCTCGGGTGCCGTGAGCCTCGTGGCCGGGCTGGGGCTGGCCACCGGCCGGGCACCCCGCACGAACGCCACCATCCTGGCGGCCCTCAATGTGCCCCTCACCGTGGTCAACAACCCCGTCTGGGCGGTCAAGGGGACGCAGGCCCGCAAGGAGGCCCTCTCCGGGCTGCTGCGCGGGGCCGCCCTGGGGGCCGGGCTCGCGCTGGCCGCCGTCGACCGTCAGGGCAGGCCGTCCCTGGCCTGGCAGGTGCGCAACGCCCGTCAGCAGCGCGAGGCGATGCAGGCCGCCAACGAGGCCGTTCAGCAGCGCTACGTGACTGCCTGA","VRPAGGRSGSTATRSSAGCSCPGQRDGALISFPVRPERGTHHLRAAISLARAARVGQDGGMNILRSFARPMLAAPFIVDGLDALVRPSRHVEKFEKVAPTLERVGLPPVLASDARLLTRASGAVSLVAGLGLATGRAPRTNATILAALNVPLTVVNNPVWAVKGTQARKEALSGLLRGAALGAGLALAAVDRQGRPSLAWQVRNARQQREAMQAANEAVQQRYVTA$","DoxX family protein","Membrane, Extracellular","conserved hypothetical protein","hypothetical protein","DoxX family protein","","Reeves J.E., Fried M. The surf-4 gene encodes a novel 30 kDa integral membrane protein. Mol. Membr. Biol. 1995. 12(2):201-208. PMID: 7540914","","","

InterPro
IPR011592
Domain

Surfeit locus 4-related
PD010195	$\"[69-170]T$	Q6A993_PROAC_Q6A993;

InterPro
IPR011637
Family

DoxX
PF07681	$\"[64-157]T$	DoxX

","No hits to the COGs database.","***** IPB011592 (Surfeit locus 4-related) with a combined E-value of 5.3e-09. IPB011592A 68-77 IPB011592B 130-160 IPB011592C 172-200","","","No significant hits to the PDB database (E-value < E-10).","Residues 64 to 157 (E_value = 0.0012) place ANA_1425 in the DoxX family which is described as DoxX.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1426","1530186","1532462","2277","4.94","-35.60","80436","ATGACCGTCCAGTCCGCCCAACCGGCCCAGGCAAGCCAGTCGTCCCAGTCGCAGCAGGCCGCCCAGCCCGACATCATCTACACCTGGACCGATGAGGCCCCGATGCTGGCGACGCACTCCTTCCTGCCGATCGTGCGCGGCTTCGCCCAGCGGGCGGGCGTGAGCGTGGGCACGGCGGACATCTCGTTGGCGGGACGCATCCTGGCGGCTTTCTCCCTGGCCGACGACGACCTGGCCCGCCTGGGTGAGCTCACCCAGTCCCCGGCGGCCACGATCATCAAGCTGCCCAACATCTCGGCCTCCCTGCCCCAGCTCAAGGCCGCCATCGCCGAGCTCCAGGCCCTGGGCCACGAGATCCCCGACTACCCCGACTCCCCGGCCACGCCCGCCGAGCACGAGGCACGCGCCGCCTACGACGCCGTCAAGGGCAGCGCCGTCAACCCCGTCCTGCGCGAGGGCAACTCGGACCGGCGCGCCCCGGCGGCCGTCAAGGCCTACGCCCGCTCCCACCCGCACTCGATGGGGGCCTGGTCACCCCAGTCGCGCACCCGCGTGGCCACGATGGGATCAGGCGACTTCCGGCGCAACGAGCGCAGCGTCGTCGTGCCCGAGGCCGGCACCCTGCAGATCCGGTTGCGCCCGGCCGACGGCGGCGAGCCGATCGTCCTGCGGCAGTCACTGCCGGTGACGGCCGGGGAGGTCGTGGACGCCACCTTCATGAGCGCCGCCGCCCTGGATGAGTTCCTCGCCCAGCAGGTGAACGCCGCCAAGGACGAGGACCTGCTGCTGTCGGTGCACCTCAAGGCCACGATGATGAAGGTCTCCGACCCGATCATCTTCGGTCACGCGGTGCGCGCCGCCCTGCCGGGGGTCTTCTCCACCTACGGGAGGGTCCTGGCCGAGGCGGGTCTGCGGGCCGAGGACGGGCTGGCCTCGATCCTGGCGGGACTGGACTCGCTGCCCCAGGGCGAGGAGATCCGAGCTGCCATCGAGTCCGAGCTGGCCGCCGGACCGCGCCTGTCCATGGTGGACTCCGACCGCGGCATCACGAACCTGCACGTGCCCAGTGACGTCATCATCGACGCCTCTATGCCCGCCATGATCCGGGCCGGCGGCCACTTGTGGGGGCCGGACGGCCAGACCGCGGACACGCTCGCCGTCATCCCGGACTCCTCCTACGCCGGGGTCTACCAGGCCGTCATCGATGACTGCCGCGCCCACGGGGCTCTGGATCCGGCCACGATGGGCTCGGTGCCCAATGTGGGTCTCATGGCCCGCAAGGCCGAGGAGTACGGCAGCCACGACAAGACCTTCCTCATCCCGGCCGACGGCACCGTCGAGGTCGTCGCGGTCGAGGGGGCGGGGGCCGAGCCCGGTGCGGTGCTGCTGTCCCACGAGGTGGCCACCGGCGACATCTGGCGGGCCTGCACCACCCAGGACGCCCCCGTGCGCGACTGGGTGCACCTGGCGGTGACGCGGGCCCGGGCCACCGGCGCCCCGGCCGTCTTCTGGCTGGACCCCGAGCGCGGGCACGACGCCGTCCTCATCGACCTGGTGAACCGTTACCTGGCCGATGAGGACACCGAGGGCCTGGACATCCGCGTGCTGGACCCGGTGGCGGCCACGCGCCTGTCCCTGGAGCGCGCCCGCCGCGGCGAGGACACGATCTCGGTGACCGGCAACGTGCTGCGCGACTACAACACGGACCTCTTCCCCATCCTCGAGCTGGGCACGAGCGCCAAGATGCTCTCGGTGGTGCCGCTGATGAATGGCGGCGGCCTCTATGAGACCGGTGCCGGGGGCTCGGCCCCCAAGCACGTGCGCCAGCTCCTCGAGGAGGACTACCTTCGCTGGGACTCCCTGGGTGAGTTCCTGGCCCTGGCGGAGGCCTTCCACCACGTGGCCCAGGTCAGCGGCAACGAGCGCGCCGAGGTCCTGGCCGACGCACTGGAGGCCGCCACGGCCCGGCTGCTGGAGGAGAACCGCTCCCCGGCGCGCCGCCTGGGGCAGATCGACAACCGCGGCTCGCACGCCTGGCTGGCCCTGTACTGGGCCCGCGAGCTGGCCGCGCAGGAGACCAGCCCCGAGCTCGCCGCCGTCTTCTCCCCGATCGCCCAGCAGCTCGAGGCCTTCAATGACACGATCCAGGCCGAGCTGCTGGCCGTCCAGGGCTCACCGGTGGACATCGGCGGCTACTACCGTCCCGATGAGGCCCTGACCGACGCCGCCATGCGACCCTCAACCACCCTCAACGCGGTCATCGAGGCCCTGGCATGA","MTVQSAQPAQASQSSQSQQAAQPDIIYTWTDEAPMLATHSFLPIVRGFAQRAGVSVGTADISLAGRILAAFSLADDDLARLGELTQSPAATIIKLPNISASLPQLKAAIAELQALGHEIPDYPDSPATPAEHEARAAYDAVKGSAVNPVLREGNSDRRAPAAVKAYARSHPHSMGAWSPQSRTRVATMGSGDFRRNERSVVVPEAGTLQIRLRPADGGEPIVLRQSLPVTAGEVVDATFMSAAALDEFLAQQVNAAKDEDLLLSVHLKATMMKVSDPIIFGHAVRAALPGVFSTYGRVLAEAGLRAEDGLASILAGLDSLPQGEEIRAAIESELAAGPRLSMVDSDRGITNLHVPSDVIIDASMPAMIRAGGHLWGPDGQTADTLAVIPDSSYAGVYQAVIDDCRAHGALDPATMGSVPNVGLMARKAEEYGSHDKTFLIPADGTVEVVAVEGAGAEPGAVLLSHEVATGDIWRACTTQDAPVRDWVHLAVTRARATGAPAVFWLDPERGHDAVLIDLVNRYLADEDTEGLDIRVLDPVAATRLSLERARRGEDTISVTGNVLRDYNTDLFPILELGTSAKMLSVVPLMNGGGLYETGAGGSAPKHVRQLLEEDYLRWDSLGEFLALAEAFHHVAQVSGNERAEVLADALEAATARLLEENRSPARRLGQIDNRGSHAWLALYWARELAAQETSPELAAVFSPIAQQLEAFNDTIQAELLAVQGSPVDIGGYYRPDEALTDAAMRPSTTLNAVIEALA$","Isocitrate dehydrogenase, NADP-dependent","Cytoplasm","isocitrate dehydrogenase, NADP-dependent","isocitrate dehydrogenase; NADP-dependent ","isocitrate dehydrogenase, NADP-dependent","","Eikmanns B.J., Rittmann D., Sahm H. Cloning, sequence analysis, expression, and inactivation of the Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and biochemical characterization of the enzyme. J. Bacteriol. 1995. 177(3):774-782. PMID: 7836312Yasutake Y., Watanabe S., Yao M., Takada Y., Fukunaga N., Tanaka I. Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication. Structure 2002. 10(12):1637-1648. PMID: 12467571","","","

InterPro
IPR004436
Family

Isocitrate dehydrogenase NADP-dependent, monomeric type
PF03971	$\"[24-756]T$	IDH
TIGR00178	$\"[18-758]T$	monomer_idh: isocitrate dehydrogenase, NADP

","BeTs to 7 clades of COG2838COG name: Monomeric isocitrate dehydrogenaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2838 is ----------r----fg-snu-----Number of proteins in this genome belonging to this COG is 1","***** IPB004436 (Isocitrate dehydrogenase NADP-dependent, monomeric type) with a combined E-value of 0. IPB004436B 44-92 IPB004436C 93-118 IPB004436D 119-166 IPB004436E 174-223 IPB004436F 233-284 IPB004436G 338-378 IPB004436H 379-406 IPB004436I 407-438 IPB004436L 526-559 IPB004436M 560-599 IPB004436N 600-633 IPB004436O 640-680 IPB004436P 688-728 IPB004436Q 729-757","","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 756 (E_value = 0) place ANA_1426 in the IDH family which is described as Monomeric isocitrate dehydrogenase.","","dehydrogenase, NADP-dependent","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1427","1532459","1533925","1467","5.19","-17.62","49242","ATGACCGATGCCCCCGGCCCTGGCGTCCCTGCGGCCCTTTCGGCTGCCTCGGCAGGATCGGCCGAGCCGTGGCGGGCGCCGGTGGCGGCGGGGGCGCTCGAGGCCGTCGTAGAGCTGCCGGGGTCGAAGTCGCTGAGCGCGCGGGCCCTGCTGCTGGCCGCCATCGCCGATGCGCCGACGACGCTCACCGGGCTCCTGCGCTCGCGCGACACCGAACTCATGCTCGCCGCCCTGAGCGTGCTCGGCGCCCGCTTCGAGGACCTCGACGAGACCGGCACGCACCTGCGCGTCACACCGGCCCCCCTGCCGCTGCACGTGCAGGCCGGACCCGACGGACTCGGACGCATCGACGTCGGCCTGGCCGGGACCGTCATGCGCTTCGTTCCCGCCCTGGCCGCGCTGGCCGACGCCCCGGTCATCTTCGACGGGGACGAGTCCGCCCGGCGCCGCCCCATGGCGCCGCTGCTCGACGCGCTGGCAGCCCTGGGCGCGGAGGTCACCCACCTCGGTGAGCCCGGCTTCCTACCCTTCCGTGTCGGCCCCGGCGACGGCGCCCTCCTGCGAGCCGAGGGCGCCCGGGTGGCGGTCGATGGCTCGGCCTCCTCCCAGTTCGTCTCCGCCCTCCTGCTCCTGGGTGCCCTCCTGCCCGGCGGCCTGGAGCTCACCCCCACCGGGCCGGTGCCCTCACTGACACACGTGGCCATGACGGTGGCGACGTTGCGCGAGCGGGGCATCGCCGTGGACGAGCCCGCCCCCGGGGCCGGCGACGGCGAGCGCACCTGGCGGGTCCACCCCGGTCGCCCCCGCGGCGGGGAGGTCGTGATCGAGCCGGACCTGTCCAACGCCGGCCCCTTCCTGGCGGCCGCCCTCGTGGCCGGGGGCCGAGTCAGCGTCCCCCACTGGCCGGCGGCCACGACCCAGGCCGGCGACGCCTGGCGAGAGCTCCTCCCCCGCCTGGGCGGGGAGGCGAGGCTCACCGACGGGCTGCTCACGGCTCACGGCTCCGGGCGGCTGACCGGGATCCACGCGGACCTGTCCGACGTCGGCGAGCTGGCCCCCACGGTGGCGGCCCTGGCCACTCTCGCCGGAGCCCAGGGCCACACCAGCACCCTCACCGGCATCGCGCACCTGCGCGGGCACGAGACCGACCGCCTGGCGGCCCTGGCCACCCAGATCCGCCTCCTGGGCGGGGACGCCGAGGAGAGCGACGACGGGCTCATCATTCGCCCCGCCCCACTGCACGGCGCCGCCCTGCGCTCCTACGCCGACCACCGGATGGCGACCTTCGCCGCCGTCATCGGCCTGAGCGTGGAGGGGGTGAGCCTGGACGACGTCGAGTGCACCTCCAAGACGCTGCCCGGCTTCACGGACCTGTGGGCCGCCATGCTGGCCACCTCCGGTGGGGGCGGTACCGGGCCCGCCACCGCCTCGCATCGCGAGCCGGAGACCCCCGGAGATGGTGTCTGA","MTDAPGPGVPAALSAASAGSAEPWRAPVAAGALEAVVELPGSKSLSARALLLAAIADAPTTLTGLLRSRDTELMLAALSVLGARFEDLDETGTHLRVTPAPLPLHVQAGPDGLGRIDVGLAGTVMRFVPALAALADAPVIFDGDESARRRPMAPLLDALAALGAEVTHLGEPGFLPFRVGPGDGALLRAEGARVAVDGSASSQFVSALLLLGALLPGGLELTPTGPVPSLTHVAMTVATLRERGIAVDEPAPGAGDGERTWRVHPGRPRGGEVVIEPDLSNAGPFLAAALVAGGRVSVPHWPAATTQAGDAWRELLPRLGGEARLTDGLLTAHGSGRLTGIHADLSDVGELAPTVAALATLAGAQGHTSTLTGIAHLRGHETDRLAALATQIRLLGGDAEESDDGLIIRPAPLHGAALRSYADHRMATFAAVIGLSVEGVSLDDVECTSKTLPGFTDLWAAMLATSGGGGTGPATASHREPETPGDGV$","3-phosphoshikimate 1-carboxyvinyltransferase","Cytoplasm, Membrane","3-phosphoshikimate 1-carboxyvinyltransferase","3-phosphoshikimate 1-carboxyvinyltransferase ","3-phosphoshikimate 1-carboxyvinyltransferase","","Stallings W.C., Abdel-Meguid S.S., Lim L.W., Shieh H.S., Dayringer H.E., Leimgruber N.K., Stegeman R.A., Anderson K.S., Sikorski J.A., Padgette S.R., Kishore G.M. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(11):5046-5050. PMID: 11607190Padgette S.R., Re D.B., Gasser C.S., Eichholtz D.A., Frazier R.B., Hironaka C.M., Levine E.B., Shah D.M., Fraley R.T., Kishore G.M. Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site. J. Biol. Chem. 1991. 266(33):22364-22369. PMID: 1939260","","","

InterPro
IPR001986
Domain

3-phosphoshikimate 1-carboxyvinyltransferase
PD001867	$\"[66-439]T$	ARA2_STRCO_Q9K4A7;
G3DSA:3.65.10.10	$\"[41-250]T$ $\"[259-462]T$	no description
PF00275	$\"[28-459]T$	EPSP_synthase
PS00104	$\"[116-130]T$	EPSP_SYNTHASE_1
PS00885	$\"[378-396]?$	EPSP_SYNTHASE_2

InterPro
IPR006264
Domain

3-phosphoshikimate 1-carboxyvinyltransferase, subgroup
TIGR01356	$\"[35-465]T$	aroA: 3-phosphoshikimate 1-carboxyvinyltran

noIPR
unintegrated

unintegrated
PIRSF000505	$\"[24-469]T$	3-phosphoshikimate 1-carboxyvinyltransferase
PTHR21090	$\"[24-402]T$	AROM/DEHYDROQUINATE SYNTHASE
PTHR21090:SF5	$\"[24-402]T$	3-PHOSPHOSHIKIMATE 1-CARBOXYVINYLTRANSFERASE

","BeTs to 22 clades of COG0128COG name: 5-enolpyruvylshikimate-3-phosphate synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0128 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB001986 (EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)) with a combined E-value of 8.1e-60. IPB001986A 35-66 IPB001986B 116-134 IPB001986C 140-166 IPB001986E 358-408 IPB001986F 418-435","","","-49% similar to PDB:2BJB MYCOBACTERIUM TUBERCULOSIS EPSP SYNTHASE IN UNLIGANDED STATE (E_value = 5.2E_62);-42% similar to PDB:1G6S STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE (E_value = 1.6E_23);-42% similar to PDB:1G6T STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE (E_value = 1.6E_23);-42% similar to PDB:1X8R EPSPS liganded with the (S)-phosphonate analog of the tetrahedral reaction intermediate (E_value = 1.6E_23);-42% similar to PDB:1X8T EPSPS liganded with the (R)-phosphonate analog of the tetrahedral reaction intermediate (E_value = 1.6E_23);","Residues 28 to 459 (E_value = 1.8e-109) place ANA_1427 in the EPSP_synthase family which is described as EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase).","","1-carboxyvinyltransferase (aroA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1428","1533925","1535043","1119","7.83","2.80","39393","ATGGCCCGCCGCGACATCGGCACCGACGACCCGCGCGTGAGGGTCCGCCCCGGCCGGGGCTCGCGCCCGCGCACCAAGCAGCGCCCCAGTCACGCCGACGCAGCCCTGGGCATGGTCACCCGCATCGACCGCGGCCACTACCGGATCCGCCTGGACGACCCCAGCCTCACTGAGGACTCCAGCGGCAACATCACCGCCATGAAGGCCCGCGAGCTGGGGCGGGGCAAGGTCGTCGTCGGGGACCGGGTCGCCGTCGTCGGGGACACCAGCGGCCGCAAGGGCACCCTGGCGCGCATGGTCCGCATCGAGGAGCGCACCACCCTGCTGCGCCGCAGCGCCGAGGACGGGGACGGAGCCGGCACCGAGAGGGCGATCGTCGCCAACGCCGGCAAGCTCGTCATCGTCACCGCCGTGGCCGACCCCGAGCCGCGCCCACGCATGATCGACCGCTACCTCGTGGCCGCCTACGACGCCGGCATGGAGCCGCTCATCGTGCTCACCAAGACCGACCTGGCCGACGCCGCCCCGCTGAAGGGCCTCTACAGCCCCCTGGGTGTGCGCTGCCTGGCCACGCGACTGCGCCCCCACGGCCCCGAGGCCGGGCCCTCACAGGCCTGCGGCGAGCGGCCCGACGACGGTGTCGAAGCGGTCCGCCAAGCGCTTGACGGTGCCGTCTCGGTCCTCGTGGGCCACTCCGGGGTCGGCAAGTCCACGCTCATCAACGCGCTCGTGCCCGGGGCCGACCGCGCCACCGGGCACGTCAACGAGGTCACCGGCCGGGGCCGCCACACCTCCACCAGTCTTCAGGCCCTCGAGCTGCCCGGGGGCGGCTGGGTCATCGACACCCCCGGCGTGCGTTCTTTCGGGGTTTCTCACGTCGGCAGCGCCGACGTTCTGAGGGGCTTTCCGGACCTGGCCCGCGTGGCCGAGGACTGTCCGCGGGGCTGCACCCATGAGGAGGGCGTCGTCGACTGCGCCCTGGATGAGTGGGCGAGCACGGCGGACGGGCCGGACGCCTCGGGAGCCTCGGCTGCCCGCGAGGAGCGGCGCGCGAGGGTGGAGTCCTTCCGCCGGCTGCTGGCCCCCTCACTGGAGGCCGAGGACCCCACCCGGCCCTGA","MARRDIGTDDPRVRVRPGRGSRPRTKQRPSHADAALGMVTRIDRGHYRIRLDDPSLTEDSSGNITAMKARELGRGKVVVGDRVAVVGDTSGRKGTLARMVRIEERTTLLRRSAEDGDGAGTERAIVANAGKLVIVTAVADPEPRPRMIDRYLVAAYDAGMEPLIVLTKTDLADAAPLKGLYSPLGVRCLATRLRPHGPEAGPSQACGERPDDGVEAVRQALDGAVSVLVGHSGVGKSTLINALVPGADRATGHVNEVTGRGRHTSTSLQALELPGGGWVIDTPGVRSFGVSHVGSADVLRGFPDLARVAEDCPRGCTHEEGVVDCALDEWASTADGPDASGASAAREERRARVESFRRLLAPSLEAEDPTRP$","GTPase EngC","Cytoplasm, Extracellular","Predicted GTPases","hypothetical protein ","GTPase EngC","","Daigle D.M., Rossi L., Berghuis A.M., Aravind L., Koonin E.V., Brown E.D. YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics. Biochemistry 2002. 41(37):11109-11117. PMID: 12220175Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 2002. 317(1):41-72. PMID: 11916378","","","

InterPro
IPR004881
Family

GTPase EngC
PF03193	$\"[36-361]T$	DUF258

InterPro
IPR010914
Domain

EngC GTPase
PS50936	$\"[127-286]T$	ENGC_GTPASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[117-290]T$	no description

","BeTs to 13 clades of COG1162COG name: Predicted GTPasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1162 is -------qv-rlbcefghsn-j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB004881 (Protein of unknown function DUF258) with a combined E-value of 2.1e-32. IPB004881B 76-86 IPB004881C 97-110 IPB004881D 123-135 IPB004881E 164-172 IPB004881F 230-241 IPB004881G 275-284 IPB004881H 312-327","","","-53% similar to PDB:1U0L Crystal structure of YjeQ from Thermotoga maritima (E_value = 6.1E_20);-46% similar to PDB:1T9H The crystal structure of YloQ, a circularly permuted GTPase. (E_value = 1.8E_16);","Residues 36 to 361 (E_value = 7e-78) place ANA_1428 in the DUF258 family which is described as Protein of unknown function, DUF258.","","GTPases (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1429","1535305","1536036","732","5.96","-5.19","26124","ATGCACAACCGTCCGACCCCTTCGCTTCCACGTCCCGCCCTGGGCGACCTGTCCGCACGCGCCAACCTCTCTGCGGCGCGCCGGCGCGTCCTGGAGGTCGTGGAGGCTTCTAACGACGCGATGACGGCCGTTCAGGTCGCCAGCGCACTCAACCTGCACCACAACACCGTCCGTGAGCACCTCGACGCCCTGGTTGACGCCGGGTTCGTCACGGTGTCCACCAAGCCGACGGGCAAGCGGGGCCGCCCGGCCCTGCGCTACGCCTCAACGGCCCCCGACCCTCAGCAGATGGTCGACGCCTACCTGCTGCTGCTCGACGCGATCGCCGACACCCTGGGCGAGGGCGAGGACGCCCGCGCCACGGCCCTGGAGATCGGTCGCCGCTGGGCCGAGCTGACCCCCGGCACCATTGCTGAGCCCACGGTCGACGGCGAGCAGGTGGACCGGGTCACCGCCCTCATCCCCTACCTCGCGGTCATGGGCTTCGCCCCAGAGGTCTCCGGAGACACCGTCGTCCTGCGCTCCTGCCCGCTCATCACCCGCAACCACCGGCCGCGTGACCTGGTGTGCACCATGCACGAGGGTTTCCTCCGGGCCGTCGTCGGCCCCGACCCGGCCGCATATGAGCGGCTCAAGTTCCTGCCCAACGGGCCTGACGGATGCCAGATCAGCTCGGCTCAGCCCGTCCACGAGGAGCCGGACCTCAAGATCGTCCACGCCGACGTCGCCTGA","MHNRPTPSLPRPALGDLSARANLSAARRRVLEVVEASNDAMTAVQVASALNLHHNTVREHLDALVDAGFVTVSTKPTGKRGRPALRYASTAPDPQQMVDAYLLLLDAIADTLGEGEDARATALEIGRRWAELTPGTIAEPTVDGEQVDRVTALIPYLAVMGFAPEVSGDTVVLRSCPLITRNHRPRDLVCTMHEGFLRAVVGPDPAAYERLKFLPNGPDGCQISSAQPVHEEPDLKIVHADVA$","Sugar-specific transcriptional regulator TrmB","Cytoplasm","conserved hypothetical protein","hypothetical protein","transcriptional regulator TrmB","","Lee S.J., Engelmann A., Horlacher R., Qu Q., Vierke G., Hebbeln C., Thomm M., Boos W. TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 2003. 278(2):983-990. PMID: 12426307","","","

InterPro
IPR002831
Family

Transcriptional regulator TrmB
PF01978	$\"[37-93]T$	TrmB

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 93 (E_value = 0.00042) place ANA_1429 in the TrmB family which is described as Sugar-specific transcriptional regulator TrmB.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1430","1537863","1536166","1698","6.10","-11.03","57802","ATGACGAAGACGCCCGACGCACAGGCACCATCCCCTGATGAGGCCGCCGCTCCTGAGACTGCTGGCTCCGAGAACGTCCCTTCTCAGGACGCTGCCTCCCAGGAGACCGAGCGCAGCGGCGCCGACAGTGCGGTTCAGGCCCCCGGCGACACTGCTGGGCGCGCGGCGACGGGCGCCGGTAAGCCCGAGGGCGCCCACCGTCGAGCGGTGACGGCCGGTACCGCCCCCGCCATCGACCGCAACCGCCGCCCCCTGACCGGCGGGGCCGGCCCGACGGCGGGAGACGGGACCGCCGCCTCGTCCTCGGGCGGCCTGCTCCAGTCCGCCGACCGCCGCGGTGTCCTCATGGGGCTGCTCACCGCCGGAGCGGCCGTCGTCGTCGGCAGCGTCATCGGCAACCGGGGTCAGGGCGGAACCACCCAGGACGTCACGCCCACCGGCAACACCGTCAACGCCACCATCACGGTGGAGGGCTTGCGGTTCGTGCCGGACACGGTCGATGTCACCCCCGGCGACCGGCTCGTCATCACCCTGGACAACACCGCCGACCAGGTCCACGACCTCGTCCTGGCCACCGGCCAGACCACCGGGCGCATCGCCGCCAGAGCCAAGGGCACCCTCGACGCCGGCATCGTCGCGGGTCCGATCGAGGGCTGGTGCTCCATCGCCGGCCACCGCGCCCAGGGCATGGTCTTCCACGTCACCGCGGGCGGGGCGGCCGCCGCCGGCCACCAGCACGGCGATCACCAGCACAGCGGTGGCCAGAGCAATCAGGCCGGCTCCGGCAAGGACGCGGTTCCCGACTATGCGGCCCAGCTGCCCGCAGGCTTCAAGGCCTTCGACGCCGCCCTGCCACCGGCCCCTACCAGTCCCGACGGCGGTCCCATGACCCACCGGCACACCTTCACCGTCAAGGAGCAGGTCATGCCGGTCGGCGCCGGTGTCACCCAGCGGCGCCTGACCTTCAACGGGCAGGTTCCCGGCCCCGTCCTGCGCGGCAAGGTGGGGGACACCTTCGAGATCACCCTGGTCAACGATGGCACGATGAGCCACTCCCTGGACTTCCACGCCGGGATCACCCCGCCCGATCAGGCGATGCGCTCGATCAACCCCGGGGAGTCCCTCGTCTACACCTTCACGGCCCAGCACTCGGGGATCTGGCTCTACCACTGCTCCACCTCGCCGATGAGCCTGCACCTGGCCGCCGGCATGCATGGGGCCGTCATCATCGATCCACCGGGGCTGCCGGCCGTGGACCGCGAGTACGTCATCGTCGCCTCTGAGGTCTACCTCGGTCCCGAGGGCGGCGAGCCTAACACGGACAAGATCGCCGCCAAGACCCCCGACCTCATGACCTTCAACGGGGTGGCCTTCCAGTACCACCAGCAGCCGCTCAAGGCCAAGGTCGGCGAGCGCGTGCGCTTCTGGGTCATGGCCGCCGGCCCCTCACTTCCGACGTCGTTCCACACCGTCGGACTGCAGTTCGATCAGGTCTTCTTCGAGGGGGCCTGGACCCTGGGTGGTCCGAACCGGATCGGGGCCGCCTGGTCCGGCGGCTCCCAGGCCCTCGGCCTGCAGCCGGCTCAGGGCGGATTCGTCGAGTGCGTGGCCTCCGAGCCGGGCCACTACGTGTTCGTGACGCACTCCTTCGCCGACATGGAGAAGGGAGCTCACGGCGTCCTGGAGGTCAGCGCCTGA","MTKTPDAQAPSPDEAAAPETAGSENVPSQDAASQETERSGADSAVQAPGDTAGRAATGAGKPEGAHRRAVTAGTAPAIDRNRRPLTGGAGPTAGDGTAASSSGGLLQSADRRGVLMGLLTAGAAVVVGSVIGNRGQGGTTQDVTPTGNTVNATITVEGLRFVPDTVDVTPGDRLVITLDNTADQVHDLVLATGQTTGRIAARAKGTLDAGIVAGPIEGWCSIAGHRAQGMVFHVTAGGAAAAGHQHGDHQHSGGQSNQAGSGKDAVPDYAAQLPAGFKAFDAALPPAPTSPDGGPMTHRHTFTVKEQVMPVGAGVTQRRLTFNGQVPGPVLRGKVGDTFEITLVNDGTMSHSLDFHAGITPPDQAMRSINPGESLVYTFTAQHSGIWLYHCSTSPMSLHLAAGMHGAVIIDPPGLPAVDREYVIVASEVYLGPEGGEPNTDKIAAKTPDLMTFNGVAFQYHQQPLKAKVGERVRFWVMAAGPSLPTSFHTVGLQFDQVFFEGAWTLGGPNRIGAAWSGGSQALGLQPAQGGFVECVASEPGHYVFVTHSFADMEKGAHGVLEVSA$","Multicopper oxidase, type 3","Extracellular, Periplasm, Cytoplasm","putative major outer membrane protein","mulitcopper oxidase domain protein ","multicopper oxidase, type 3","","Messerschmidt A., Huber R. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur. J. Biochem. 1990. 187(2):341-352. PMID: 2404764Ouzounis C., Sander C. A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins. FEBS Lett. 1991. 279(1):73-78. PMID: 1995346Roberts S.A., Weichsel A., Grass G., Thakali K., Hazzard J.T., Tollin G., Rensing C., Montfort W.R. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 2002. 99(5):2766-2771. PMID: 11867755","","","

InterPro
IPR001287
Family

Copper-containing nitrite reductase
PR00695	$\"[321-337]T$ $\"[378-393]T$ $\"[395-411]T$	CUNO2RDTASE

InterPro
IPR011572
Domain

Blue (type 1) copper subtype
PD001235	$\"[336-410]T$	Q82VX5_NITEU_Q82VX5;

InterPro
IPR011707
Domain

Multicopper oxidase, type 3
PF07732	$\"[303-415]T$	Cu-oxidase_3

noIPR
unintegrated

unintegrated
G3DSA:2.60.40.420	$\"[288-412]T$ $\"[416-563]T$	no description
PTHR11709	$\"[349-496]T$	MULTI-COPPER OXIDASE
PTHR11709:SF1	$\"[349-496]T$	MULTICOPPER OXIDASE

","BeTs to 9 clades of COG2132COG name: Putative multicopper oxidasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG2132 is -o----yq--r-b-ef-hsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB001287 (Copper containing nitrite reductase signature) with a combined E-value of 3.1e-35. IPB001287B 321-337 IPB001287C 337-354 IPB001287D 354-373 IPB001287E 378-393 IPB001287F 395-411","","","-44% similar to PDB:2DV6 Crystal structure of nitrite reductase from Hyphomicrobium denitrificans (E_value = 2.3E_40);-51% similar to PDB:1KBV NITRITE-SOAKED CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE (E_value = 5.1E_40);-51% similar to PDB:1KBW CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE (E_value = 5.1E_40);-45% similar to PDB:1NDT NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS (E_value = 3.3E_23);-45% similar to PDB:1WA1 CRYSTAL STRUCTURE OF H313Q MUTANT OF ALCALIGENES XYLOSOXIDANS NITRITE REDUCTASE (E_value = 3.3E_23);","Residues 288 to 414 (E_value = 0.0006) place ANA_1430 in the Cu-oxidase_2 family which is described as Multicopper oxidase.Residues 303 to 415 (E_value = 4e-11) place ANA_1430 in the Cu-oxidase_3 family which is described as Multicopper oxidase.","","major outer membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1431","1539254","1537860","1395","11.45","27.96","47824","ATGAGCCTGTCCATCGGTTCTCCCGGTACCGGGTCCGCCCCCCGGCCCGGCTCGCTTCCCGGCCCCGGACGAGCAAGCGGCCCGGGCCGCCCCGCCAAGAAGCCCTCCCGGCGCACCACCCAGGTACGTCGCAACGCCCTGGTCATGGCCTGGCTGCTCATCGCCGCGGTCCTGGCGGCCCTGACCATCGTGGGCCCGCTGGTCTCCTGGGGCACCTGGCTGCCCCTGCACGCCCTGCTCCTGGGCGGGATCGGCAGCGCCATCACCATCTGGTCCGCCCACTTCGCCGACACCCTCCTGCACCGCCCGGCTCTGGGTGGTGCGGCCCTCCTGGACGCGCGCCTCTACGCCCACAGCCTCGGCACCGCCGTCGTGCTCACCGGCATCACCATGGGACAGCAGGCGGTGGCGCTCATCGGGGCGGGTATCGTCATGGCCCAGGCCATTGCGGGCGTCGTGGCCATCACCGTGCAGTACCGCAGGGCCATCGCCCCGCGCCTGGCCTCCCTGGCCCTCCACTACGCCGTCGCCCTGGTCCTGCTGGCCACCGGTGCGCTCCTGGGCTTCCTCATCTCCTGGTCCAACGCCCACGGGCGCTCCGCCCTGGCCGACGGCTTCTACCTGGCCCACACGACCACCATGCTGCTGGGCTTCGTGGGCACCACGGTCCTGGGCACGCTCACGGTCCTGTGGCCCACGATGCTGCGCACCCCCATGGAGCCGGTCGCACCGCGCTGGACCACTCGCGGCCTGCCCTACCTCGTGGGAGGCACCGCGCTGGTGGCCGCCTGCGGGCTGTGGCCGCCCCTGGCGGGTCTGGGCACCCTGGTCTACCTCGGCGGCGCCTGCGCAGTCCTCGTGCCCGCCTACCGCACCGCCCGCCGGGTCCCGCCAACCTCCTTCGCCACGGCCTCCGCCACGGCCTCGGTGGCCTGGTTCGTCGGCTGCGTCGCCGTCCTGGGGGCCCGCATGGCACTGGCCGACGACGCCGCTGCCTCCCGCCAGGTCATCCACTCCCTGCGCCTGCCCCTGGCGGCGGGCTTCGCCCTGCAGATCCTCGTGGCGGCCCTGAGCTACCTCACCCCGGTGATGCTCGGCGGCGGCCCCGCGGCCACCCGGGCCACCAACGCGATCATGGACCGCTTCGCCGCCTACCGGGTCACCGCAGCCAACGCCTGCCTCCTGCTGGCGCTCTACCCGGGGGCGCCCTGGCAGGTGCGCGTCGTCGCCGGCGCCCTGGCCGCGCTGGTGACCTCCTACCTGCTGGCGGGCATGATGCTCAGCCTGCGCGAGGTCTCCCAGCGCAAGCGCCCGCCGCGTACTCCGGCCGACGCCGACCCCACCTCCGACCCCGCGGGCCACCGGTCCGCCCAGCCCCGAAGGGGAACCCGATGA","MSLSIGSPGTGSAPRPGSLPGPGRASGPGRPAKKPSRRTTQVRRNALVMAWLLIAAVLAALTIVGPLVSWGTWLPLHALLLGGIGSAITIWSAHFADTLLHRPALGGAALLDARLYAHSLGTAVVLTGITMGQQAVALIGAGIVMAQAIAGVVAITVQYRRAIAPRLASLALHYAVALVLLATGALLGFLISWSNAHGRSALADGFYLAHTTTMLLGFVGTTVLGTLTVLWPTMLRTPMEPVAPRWTTRGLPYLVGGTALVAACGLWPPLAGLGTLVYLGGACAVLVPAYRTARRVPPTSFATASATASVAWFVGCVAVLGARMALADDAAASRQVIHSLRLPLAAGFALQILVAALSYLTPVMLGGGPAATRATNAIMDRFAAYRVTAANACLLLALYPGAPWQVRVVAGALAALVTSYLLAGMMLSLREVSQRKRPPRTPADADPTSDPAGHRSAQPRRGTR$","Hypothetical protein","Membrane, Extracellular","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-60]?$	signal-peptide
tmhmm	$\"[47-69]?$ $\"[75-95]?$ $\"[115-133]?$ $\"[139-159]?$ $\"[174-196]?$ $\"[215-235]?$ $\"[250-269]?$ $\"[275-290]?$ $\"[300-322]?$ $\"[341-361]?$ $\"[382-402]?$ $\"[408-428]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","Mon Aug 6 15:45:26 2007","","Mon Aug 6 15:45:26 2007","","","Mon Aug 6 15:45:26 2007","Mon Aug 6 15:45:26 2007","Mon Aug 6 15:45:26 2007","","","","","","Mon Aug 6 15:45:26 2007","","","","Mon Aug 6 15:45:26 2007","Mon Aug 6 15:45:26 2007","","","","","yes","","" "ANA_1432","1540345","1539251","1095","9.73","9.74","37447","ATGGGACTCAACGCCGCCCTCCTGCGCCTCAGCCTGCCGGCCCCCGTCAACGGGGCCGAGCTGGCGGCGCTCCACGGCCCCCTCATGCTCGTCGGCTTCCTGGGGGCCGTCATCGCCCTGGAACGGGCGGTCGCCGCACGCACCCCCTGGGCCTTCCTCGCCCCCCTGGGAAGTGCCGCGGGCTGCCTGGCCCTCCTGGCCGGTGCCCCCGACGTCGTCGGCCGGGGACTCATGACCGGCGCCGCCGGCATCCTATGCGCCATCTACCTGCGGGTTCACCGCCGCGCCCCCAGCGCTGCCGTCGACGTCGAGGCCATGGGCGGGGCCGCCCTCCTGCTGGGGGACGTCCTGTGGCTGGGTGGGCGCGGCATGGAGGATGTCGTCCCGCTGTGGCTGCTCTTCCCCACGCTCACCATCATCGGCGAGCGCCTGGAGCTGGCCCGCATCGCCTTCCTCGACGAGATGGTGGAGACCGTCGTCGAGGCGCTCGCCGGCGCGGCGGTCCTGGGTGCCTGCCTGTTGCTCATCGCACCGGGCTCCCACCTCGTGGTTGGCCCGGCCCTGCTGGGACTGGCCGTCGTCATGGCCTACTACGACGTCGCCCGACGCACGATCCGTCTGCGCGGCGGGGCGCGCTTCATGGCGGCCTCCATGCTCGCCGGCTACGTGTGGCTCGCCGTCGCCGGGGCAGTCTGGTCGCTGTGGGGCCTGCAGGGCCTGAACGGGGCCGCCTACGAGATCGTCATCCACTGCATCACGGTGGGCTTCGCCTTCTCCATGATCCTGGCCCACGCCCCGGTCATCATCCCCGCGATCGTCCACCGGGCCCTGCCCTACCACCGACTCATGTGGCTGCCCTACGTTCTGCTGCACGCCGGCCTGGTGGTACGAGTCGTCGGTCTGCTGGCGGAGGCCTCCGCGGCCTGGAAGGTCGGCGGTGCCGTGGGAGTGGCGGCGATCCTCGTCTTCATGGTCCTCACCCTGGGGCGCGTCCTGACCTCCGGCAGCATCCGCAAGCCGGTGAGGGCAAGACCGCCGGCTACGGCCGCGGCATCCGGATCGACGACGTCGCAGGCGACAGGGGGCCGCGCATGA","MGLNAALLRLSLPAPVNGAELAALHGPLMLVGFLGAVIALERAVAARTPWAFLAPLGSAAGCLALLAGAPDVVGRGLMTGAAGILCAIYLRVHRRAPSAAVDVEAMGGAALLLGDVLWLGGRGMEDVVPLWLLFPTLTIIGERLELARIAFLDEMVETVVEALAGAAVLGACLLLIAPGSHLVVGPALLGLAVVMAYYDVARRTIRLRGGARFMAASMLAGYVWLAVAGAVWSLWGLQGLNGAAYEIVIHCITVGFAFSMILAHAPVIIPAIVHRALPYHRLMWLPYVLLHAGLVVRVVGLLAEASAAWKVGGAVGVAAILVFMVLTLGRVLTSGSIRKPVRARPPATAAASGSTTSQATGGRA$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[22-40]?$ $\"[50-70]?$ $\"[127-147]?$ $\"[162-177]?$ $\"[183-201]?$ $\"[216-236]?$ $\"[246-268]?$ $\"[283-303]?$ $\"[309-329]?$	transmembrane_regions

InterPro
IPR000385
Domain

MoaA/nifB/pqqE, iron-sulphur binding
PS01305	$\"[44-55]T$	MOAA_NIFB_PQQE

InterPro
IPR006638
Domain

Elongator protein 3/MiaB/NifB
SM00729	$\"[38-247]T$	Elp3

InterPro
IPR007197
Domain

Radical SAM
PF04055	$\"[42-209]T$	Radical_SAM

InterPro
IPR010505
Domain

Molybdenum cofactor synthesis C-terminal
PF06463	$\"[214-350]T$	Mob_synth_C

InterPro
IPR013483
Family

Molybdenum cofactor biosynthesis protein A
TIGR02666	$\"[29-372]T$	moaA: molybdenum cofactor biosynthesis prot

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[45-184]T$	no description

noIPR
unintegrated

unintegrated
PTHR22960	$\"[170-372]T$	MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A

","BeTs to 18 clades of COG2896COG name: Molybdenum cofactor biosynthesis enzymeFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG2896 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB000385 (MoaA/nifB/pqqE family) with a combined E-value of 1.8e-52. IPB000385A 40-55 IPB000385B 90-104 IPB000385C 124-156 IPB000385D 187-199 IPB000385E 293-313","","","-53% similar to PDB:1TV7 Structure of the S-adenosylmethionine dependent Enzyme MoaA (E_value = 1.2E_39);-53% similar to PDB:1TV8 Structure of MoaA in complex with S-adenosylmethionine (E_value = 1.2E_39);-53% similar to PDB:2FB3 Structure of MoaA in complex with 5'-GTP (E_value = 1.2E_39);-52% similar to PDB:2FB2 Structure of the MoaA Arg17/266/268/Ala triple mutant (E_value = 1.5E_37);-47% similar to PDB:1RQP Crystal structure and mechanism of a bacterial fluorinating enzyme (E_value = 1.5E_37);","Residues 42 to 209 (E_value = 2.3e-34) place ANA_1436 in the Radical_SAM family which is described as Radical SAM superfamily.Residues 214 to 350 (E_value = 1.9e-37) place ANA_1436 in the Mob_synth_C family which is described as Molybdenum Cofactor Synthesis C.","","cofactor biosynthesis protein A (CNX2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1438","1542316","1542627","312","4.55","-5.85","10584","ATGACGAACCCCTCCCCCGAGCTGTCGCCCCAGGCGGACGCGCACGCCGGTCAGGCGCAGATCTCTGTGACCCTGCGCTACTTCGCCGCGGCCACTGAGGCCGCCGGGCGCCCCGAGGAGCGCCTGGACCTGCCCGCCGGCACGACACTGGCGGCTCTGCGCGAGCAGCTCTCCGGTCGAGGCCTGGAGATGGCGCGGGTCATCCCGATCTGCAGCTTCCTCGTCAACTCGGTCTCCACCCCGGCGGACTCGCTCACGCCCCTGGCCGACGGCGACGCCGTCGACGTGCTCCCGCCCTTCGCTGGCGGGTGA","MTNPSPELSPQADAHAGQAQISVTLRYFAAATEAAGRPEERLDLPAGTTLAALREQLSGRGLEMARVIPICSFLVNSVSTPADSLTPLADGDAVDVLPPFAGG$","Molybdopterin converting factor, small subunit","Periplasm, Cytoplasm","probable moaD2 protein","ThiS family protein","thiamineS protein","","Lauhon C.T., Kambampati R. The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD. J. Biol. Chem. 2000. 275(26):20096-20103. PMID: 10781607","","","

InterPro
IPR003749
Family

ThiamineS
PF02597	$\"[25-103]T$	ThiS

InterPro
IPR012675
Domain

Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30	$\"[22-103]T$	no description

","BeTs to 11 clades of COG1977COG name: Molybdopterin converting factor, small subunitFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1977 is ao-pk--q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 25 to 103 (E_value = 1.4e-14) place ANA_1438 in the ThiS family which is described as ThiS family.","","moaD2 protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1439","1543272","1542715","558","6.92","-0.17","19725","ATGCCCGTTCAGCCGGTGAAGCCCACATGGGTATGCTCGCGGCCGACCATCCGATCACGCCCAGCCCGCCGCCCCGATCGAGGAGACCCCGTGACGCCCAGTCCCGACCAGCCCAGCCGGCCGCTCCCGGCTCCCACGGCCCGCGTGGTCCGTGCCGAGGTCACCGAGTCACCCATCAGCGTCACCGAACTCGCCGACGCCGTCCAGGACGCTGCCGCCGGCGCCGTCGTCACTTTCGAGGGCGTGGTCCGCAACCACGACGCCGAGCGCGCCGTCACCGGCATCGGCTACTCCTGCCACCCCACGGCCGGCCAGGTCGTCGAGCAGATCGCCCAGGACGTGGCTCAGCAGGGGCGGGTGCGGGCCCTGGGCGTCGTCCACCGCGTCGGCGACCTGGGCGTCGGGGAGGCAGCGCTCGCGGTCGCCGTCAGCTCCGACCACCGCGCCGAGGCCTTCGCCGTGTGCAGCCAGATCGTCGAGGAGGTCAAGGAGCGCCTGCCCGTGTGGAAGCGCCAGACCTTCACCGACGGCTCGAGCCAGTGGAGCAACATCGCCTGA","MPVQPVKPTWVCSRPTIRSRPARRPDRGDPVTPSPDQPSRPLPAPTARVVRAEVTESPISVTELADAVQDAAAGAVVTFEGVVRNHDAERAVTGIGYSCHPTAGQVVEQIAQDVAQQGRVRALGVVHRVGDLGVGEAALAVAVSSDHRAEAFAVCSQIVEEVKERLPVWKRQTFTDGSSQWSNIA$","Molybdopterin converting factor, large subunit","Cytoplasm, Extracellular","moaE-like protein","molybdopterin biosynthesis MoaE","molybdopterin biosynthesis MoaE protein","","Pitterle D.M., Rajagopalan K.V. The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor. J. Biol. Chem. 1993. 268(18):13499-13505. PMID: 8514782","","","

InterPro
IPR003448
Family

Molybdopterin biosynthesis MoaE
PF02391	$\"[51-166]T$	MoaE

noIPR
unintegrated

unintegrated
G3DSA:3.90.1170.40	$\"[47-182]T$	no description
PTHR23404	$\"[97-181]T$	MOLYBDOPTERIN SYNTHASE RELATED
PTHR23404:SF2	$\"[97-181]T$	MOLYBDOPTERIN SYNTHASE LARGE SUBUNIT 2

","BeTs to 14 clades of COG0314COG name: Molybdopterin converting factor, large subunitFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0314 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB003448 (Molybdopterin biosynthesis MoaE) with a combined E-value of 5.5e-35. IPB003448A 74-100 IPB003448B 125-172","","","No significant hits to the PDB database (E-value < E-10).","Residues 51 to 166 (E_value = 6e-37) place ANA_1439 in the MoaE family which is described as MoaE protein.","","protein (MPT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1440","1543271","1544779","1509","5.33","-12.65","50721","ATGATAGGCCCCGGACGTTCGGGCACCGGCCCCGCGACCGCCCGCCCTGAGGTCGCAGCCCGCAGGGTACCCGCCGAAGGAAGGACCGCTATGGCGCAGATGATCCCCCTGGAGGACTACGTCTCCCAGGTGCTGGAGACCCTCTCACCCCTGGAGGACGGTCGCCTGGAGCTGGGGCGGACGCACGGCCGGGTGCTGGCCAAGGACGTGACCGCCGCCGTCCCGGTGCCGCCGTGGACGAACTCGGCGATGGACGGCTACGCGGTGCGCGCGAAGGACACGACCGGCGCCTGCCCGCTCACGCCCGTGGTTCTGCCGGTGAGCGGGGACGTTCCGGCCGGCGCCGCACCGCGGCCCCTCGCGGAGGGAACCGCCCAGCGGATCATGACTGGGGCGATGCTGCCTGAGGGCGCGGACGCCGTGGTCAAGGTGGAAGACACCGACCAGGCTCCCGGCCCGCACCCGATTCCCGAGCACGTCGAGATCCGCGCGGCAGCGACCCCGGGCCTCAGCGTGCGCCGCGCCGGGGAGGACGTGGCCGCGGGTGATCCGGTCATGGCGGCGGGGACGAGGCTGTCGGCGGCGGCCATCTCCGCCCTGGCCTCCGTGGGGCTCGGCTCGGTGCTGGTGCGGCCGCAGGTGCGCGTGGCGGTGGTGTCCACCGGGGCCGAGCTGCGTGACGCCGGCCAGGCGCTGGAGCCCGGGACGATTCCCGACTCCAACTCCCTGCTGCTCGCCGGGCTGGTCACCGAGCACGGGGCCGTGTGCACGAGCGTGGCCCGCAGCGGCGACACGGCCGAGGCCCTGGCTGAGGTCCTACAGCAGGCCGCGGCCGGCGCCGACCTCATCGTCACCTCCGGGGGCGTGTCCGCGGGAGCCTTCGATCCTCTAACGATGCTGGCTCAGGCGCAGCGGGGCGAGGAGGCCCCAGTGCACCTGGACTTCGTCAAGGTGGCCATGCAGCCGGGCAAGCCCCAGGGGCACGGCTGGGTGCTGGCCGACGACGGCCGGCGGGTGCCGATCATCTGCCTGCCGGGCAATCCGGTGAGTGTCCTGGTCTCCTTCACCACGATCGTGGCGCCGGCGCTGGCCCGTCTGGCCGGGCAGGACGCAGAGGATGGCGGCGCAGAGCCGCTTCCGGGGCGGCCTGTCATGACGGCGCACGCGGCGGTGGGTTGGCGAACCCCGCCGGGGCGGCGCCAGCACGTGCCGGTGCGCTTCACCGAGGCCCCCACCGGCTTAGGAGCCAGTTCCGACGTCGGTGACGGTGCGGGCCTGCCCTGGGTGACACCCACCCACCGGCTGGGCTCAGGCTCGCACCTGGTGGCCTCGCTGCCCGCCGCGCAGGCGCTGGCGGTGGTGGACGCCGAGGTCGAGGCGGTCGAGGTCGGCGACGAGCTGGCCCTCATTCCGCTGTCCGCCTCATCGAGCTCGGCGACCGCCGCCCCTGCAGGTCGCCGTCAAGAGCCCCGGACTGCGCCCACAGGGCGCGACCCCGTATCCCAGTGA","MIGPGRSGTGPATARPEVAARRVPAEGRTAMAQMIPLEDYVSQVLETLSPLEDGRLELGRTHGRVLAKDVTAAVPVPPWTNSAMDGYAVRAKDTTGACPLTPVVLPVSGDVPAGAAPRPLAEGTAQRIMTGAMLPEGADAVVKVEDTDQAPGPHPIPEHVEIRAAATPGLSVRRAGEDVAAGDPVMAAGTRLSAAAISALASVGLGSVLVRPQVRVAVVSTGAELRDAGQALEPGTIPDSNSLLLAGLVTEHGAVCTSVARSGDTAEALAEVLQQAAAGADLIVTSGGVSAGAFDPLTMLAQAQRGEEAPVHLDFVKVAMQPGKPQGHGWVLADDGRRVPIICLPGNPVSVLVSFTTIVAPALARLAGQDAEDGGAEPLPGRPVMTAHAAVGWRTPPGRRQHVPVRFTEAPTGLGASSDVGDGAGLPWVTPTHRLGSGSHLVASLPAAQALAVVDAEVEAVEVGDELALIPLSASSSSATAAPAGRRQEPRTAPTGRDPVSQ$","Molybdopterin biosynthesis protein MoeA","Cytoplasm","molybdopterin biosynthesis protein.","molybdopterin biosynthesis protein MoeA","molybdenum cofactor synthesis domain","","Kamdar K.P., Shelton M.E., Finnerty V. The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin. Genetics 1994. 137(3):791-801. PMID: 8088525","","","

InterPro
IPR001453
Domain

Molybdopterin binding domain
PD002460	$\"[222-368]T$	Q73SZ0_MYCPA_Q73SZ0;
PF00994	$\"[217-365]T$	MoCF_biosynth
TIGR00177	$\"[213-361]T$	molyb_syn: molybdenum cofactor synthesis do

InterPro
IPR005110
Domain

MoeA, N-terminal, domain I and II
PF03453	$\"[34-204]T$	MoeA_N

InterPro
IPR005111
Domain

MoeA, C-terminal, domain IV
PF03454	$\"[386-473]T$	MoeA_C

noIPR
unintegrated

unintegrated
G3DSA:2.170.190.11	$\"[77-178]T$	no description
G3DSA:3.40.980.10	$\"[186-370]T$	no description
PTHR10192	$\"[1-490]T$	MOLYBDOPTERIN BIOSYNTHESIS PROTEIN

","BeTs to 18 clades of COG0303COG name: Molybdopterin biosynthesis enzymeFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0303 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 2","***** IPB001453 (Molybdenum cofactor biosynthesis protein) with a combined E-value of 3.9e-90. IPB001453A 66-107 IPB001453B 128-150 IPB001453C 195-246 IPB001453D 281-302 IPB001453E 313-329 IPB001453F 342-366 IPB001453G 395-413 IPB001453H 431-455***** IPB008284 (Molybdenum cofactor biosynthesis protein, N-terminal) with a combined E-value of 2.7e-12. IPB008284A 177-189 IPB008284B 282-312 IPB008284C 326-358","","","-45% similar to PDB:1UZ5 THE CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN FROM PYROCOCCUS HORIKOSII (E_value = 1.5E_35);-45% similar to PDB:2NRO MoeA K279Q (E_value = 9.7E_35);-45% similar to PDB:1FC5 CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN (E_value = 2.8E_34);-45% similar to PDB:1G8L CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA (E_value = 2.8E_34);-45% similar to PDB:1G8R MOEA (E_value = 2.8E_34);","Residues 34 to 204 (E_value = 1.1e-59) place ANA_1440 in the MoeA_N family which is described as MoeA N-terminal region (domain I and II).Residues 217 to 365 (E_value = 4.1e-34) place ANA_1440 in the MoCF_biosynth family which is described as Probable molybdopterin binding domain.Residues 386 to 473 (E_value = 1.4e-07) place ANA_1440 in the MoeA_C family which is described as MoeA C-terminal region (domain IV).","","biosynthesis protein. (moeA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1441","1544791","1545303","513","6.35","-1.35","17563","ATGACGACCCGCCCCGAGATCACCCTCACCCACCTGGACGAGGCGGGCGCCGCCTACATGGTGGACGTCACCGCCAAGACCCCCACCGTGCGCGAGGCCCGCGCCACCGCCTTCGTGGCCTGCTCGGAGGCGATCGTGGACGCCCTGCGCGGCGGCTCTGTCCCCAAGGGCGACGTGCTCGCCGTGGCCCGCGTGGCCGGGATCGCGGCGACGAAGAAGGTGCCCGAGCTCCTCCCCCTGGCGCATGTCATCGGCGTGCATGGGGCGCGCGTGGACCTGGAGATCGTCGACGGCGGCGTGCGCATCGAGACCACGGTGCGCACGGCCGACCGCACGGGCGTGGAGATGGAGGCCCTCACCGCCGCCACCGTGGCGGGACTGGCGATCGTCGACATGGTCAAGGGAGTGGACCGGGGCGTCGAGCTGCGCGAGGCCAAGGTGGTCGCCAAGTCCGGGGGACGCTCAGGGGACTGGGTGCGCGGTGACCGCGGTGACCGCGGTGACGCTGCCTGA","MTTRPEITLTHLDEAGAAYMVDVTAKTPTVREARATAFVACSEAIVDALRGGSVPKGDVLAVARVAGIAATKKVPELLPLAHVIGVHGARVDLEIVDGGVRIETTVRTADRTGVEMEALTAATVAGLAIVDMVKGVDRGVELREAKVVAKSGGRSGDWVRGDRGDRGDAA$","Molybdopterin cofactor biosynthesis protein MoaC","Cytoplasm, Extracellular","molybdenum cofactor biosynthesis protein C","K03637 molybdenum cofactor biosynthesis protein C","molybdenum cofactor biosynthesis protein C","","Gray T.A., Nicholls R.D. Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames. RNA 2000. 6(7):928-936. PMID: 10917590Solomon P.S., Shaw A.L., Lane I., Hanson G.R., Palmer T., McEwan A.G. Characterization of a molybdenum cofactor biosynthetic gene cluster in Rhodobacter capsulatus which is specific for the biogenesis of dimethylsulfoxide reductase. Microbiology 1999. 145:1421-1429. PMID: 10411269Rieder C., Eisenreich W., O'brien J., Richter G., Gotze E., Boyle P., Blanchard S., Bacher A., Simon H. Rearrangement reactions in the biosynthesis of molybdopterin--an NMR study with multiply 13C/15N labelled precursors. Eur. J. Biochem. 1998. 255(1):24-36. PMID: 9692897Wuebbens M.M., Liu M.T., Rajagopalan K., Schindelin H. Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC. Structure 2000. 8(7):709-718. PMID: 10903949Rivers S.L., Mcnairn E., Blasco F., Giordano G., Boxer D.H. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Mol. Microbiol. 1993. 8(6):1071-1081. PMID: 8361352Wuebbens M.M., Rajagopalan K.V. Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies. J. Biol. Chem. 1995. 270(3):1082-1087. PMID: 7836363","","","

InterPro
IPR002820
Domain

Molybdopterin cofactor biosynthesis MoaC region
PD003575	$\"[24-151]T$	Q6AAG5_PROAC_Q6AAG5;
G3DSA:3.30.70.640	$\"[6-164]T$	no description
PF01967	$\"[20-153]T$	MoaC
TIGR00581	$\"[9-155]T$	moaC: molybdenum cofactor biosynthesis prot

InterPro
IPR012087
Family

Molybdenum cofactor precursor Z biosynthesis MoaC
PIRSF003315	$\"[8-162]T$	Molybdenum cofactor precursor Z biosynthesis protein MoaC

noIPR
unintegrated

unintegrated
PTHR22960	$\"[9-167]T$	MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A

","BeTs to 18 clades of COG0315COG name: Molybdenum cofactor biosynthesis enzymeFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0315 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB002820 (Molybdopterin cofactor biosynthesis protein MoaC) with a combined E-value of 2.2e-50. IPB002820A 10-49 IPB002820B 56-84 IPB002820C 110-138","","","-63% similar to PDB:1EKR MOAC PROTEIN FROM E. COLI (E_value = 5.5E_28);-62% similar to PDB:1EKS ASP128ALA VARIANT OF MOAC PROTEIN FROM E. COLI (E_value = 4.6E_27);-44% similar to PDB:1WE3 Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus (E_value = 4.6E_27);-44% similar to PDB:1WF4 Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus (E_value = 4.6E_27);","Residues 20 to 153 (E_value = 6.3e-51) place ANA_1441 in the MoaC family which is described as MoaC family.","","cofactor biosynthesis protein C (moaC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1442","1545272","1545982","711","5.20","-7.91","24311","GTGACCGCGGTGACCGCGGTGACGCTGCCTGAGCAGACGGTCGGCGCCATCGTGAGCACCGCGGATGCGGTCGAAGTCGCCGAGGCCCCCGATGGCGCCGAGACCGCCGATGTCATTGTGCTGGCCGGCGGGACCGGGGCTCGGCTGGACGGAGCCTCCAAGCCCGACGTCGTCGCCCGGGGGCTGCGCCTGCTCGACCACGTGCTGGCCGGTCTGGAGCATCTACGGACGCAGGGTCTTCCGCTCGGGCGCGTGTGCGTTGTCGCCCCGGCGGAGGTCGCTCTGCCCGATGGCGTCCTACGGGCATTGGAGGACCCTCCCCTGGGAGGGCCCGTCGCCGGGATCGCGGCCGGGCTGGATGTCCTAGGACGGAGCGACCCGGTTGCGGGACTGGCCGGGATCCTCACCTGCGACGCGCCCTTGTCCTGGAGGGCGCTGCCGGCCCTGCACCGGGCGCTGGCGCAGACCGAGCCGGAGCTGGACGGGGTCTGCGCCCGCGACGGCGAGCACACCCAGTACCTGCTGGGCCTCTACCGCCGCCGAGCACTGGCCGCGGCCGTCGCCCCGGACGGCGCGCCTCTGCGGGACACGGCTGTGCGCCGGTCACTCGGGACGCTCCGCGTCAGGGCCATCCCCACGGCTCGCGATGTCGTGCGGGATCTGGACACCTGGGCCGAGGTCCATTCCTGGGACTCGGGCCGCTCCGAGTAG","VTAVTAVTLPEQTVGAIVSTADAVEVAEAPDGAETADVIVLAGGTGARLDGASKPDVVARGLRLLDHVLAGLEHLRTQGLPLGRVCVVAPAEVALPDGVLRALEDPPLGGPVAGIAAGLDVLGRSDPVAGLAGILTCDAPLSWRALPALHRALAQTEPELDGVCARDGEHTQYLLGLYRRRALAAAVAPDGAPLRDTAVRRSLGTLRVRAIPTARDVVRDLDTWAEVHSWDSGRSE$","Molybdopterin-guanine dinucleotide biosynthesis protein A","Cytoplasm","Molybdopterin-guanine dinucleotide biosynthesisprotein A","hypothetical protein; putative molybdopterin-guanine dinucleotide biosynthesis protein A","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[38-231]T$	no description

","BeTs to 4 clades of COG2266COG name: GTP:adenosylcobinamide-phosphate guanylyltransferaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG2266 is aompkz--------------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-52% similar to PDB:1GZ9 HIGH-RESOLUTION CRYSTAL STRUCTURE OF ERYTHRINA CRISTAGALLI LECTIN IN COMPLEX WITH 2'-ALPHA-L-FUCOSYLLACTOSE (E_value = );-52% similar to PDB:1GZC HIGH-RESOLUTION CRYSTAL STRUCTURE OF ERYTHRINA CRISTAGALLI LECTIN IN COMPLEX WITH LACTOSE (E_value = );-56% similar to PDB:1YT5 Crystal structure of NAD kinase from Thermotoga maritima (E_value = );-36% similar to PDB:2J9I LENGSIN IS A SURVIVOR OF AN ANCIENT FAMILY OF CLASS I GLUTAMINE SYNTHETASES IN EUKARYOTES THAT HAS UNDERGONE EVOLUTIONARY RE-ENGINEERING FOR A TISSUE-SPECIFIC ROLE IN THE VERTEBRATE EYE LENS. (E_value = );","No significant hits to the Pfam 21.0 database.","","dinucleotide biosynthesis protein A","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1443","1546559","1546026","534","6.20","-2.11","18181","ATGAGTGAGACCCCCATCGTCCAGAAGGGCCTGGCGGCCCTGCCCGAGCCCGTCAAGGGCGCTGTCATCACCGTCTCCGACCGCTGCGTCAGCGGTGAGAGACAGGACCTCTCCGGCCCGCTGGCCCAGCGTCTCCTGGCCGAGCACGACATCGTCGTCGAGAAGGTGGACCTCGTGCCCGACGGCATCGAGCCGGTGCGCAAGGCGATCAGGCGGGCGGTGGCCGACGGCGCCCGGGTGGTCCTGACCACCGGCGGTACCGGGGTGACCCCTCGGGACCTCACCCCGGAGGCGACGGCACCACTGCTGGAGACCCGCATCGAGGGCATCGAGGCGCAGATCCGCGCCCACGGGCTGACCAAGACACCGCTGGCGGGACTGTCCCGCGGGCTGGTAGGCGTGACCTCTCGCGGCGACGACGGCGCCCTGGTCATCAACGCCCCCGGCTCGCGCGGTGGGGTCAAGGACACCGTTGCCGTCGTCGGCCCCCTGGTGCCCCATGTCCTGGAGCAGCTCGGCGGCGGCGACCACTGA","MSETPIVQKGLAALPEPVKGAVITVSDRCVSGERQDLSGPLAQRLLAEHDIVVEKVDLVPDGIEPVRKAIRRAVADGARVVLTTGGTGVTPRDLTPEATAPLLETRIEGIEAQIRAHGLTKTPLAGLSRGLVGVTSRGDDGALVINAPGSRGGVKDTVAVVGPLVPHVLEQLGGGDH$","Molybdenum cofactor biosynthesis protein","Cytoplasm","Molybdopterin biosynthesis enzymes","putative molybdenum cofactor biosynthesis protein","molybdenum cofactor synthesis domain","","Kamdar K.P., Shelton M.E., Finnerty V. The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin. Genetics 1994. 137(3):791-801. PMID: 8088525","","","

InterPro
IPR001453
Domain

Molybdopterin binding domain
PF00994	$\"[21-167]T$	MoCF_biosynth
TIGR00177	$\"[17-163]T$	molyb_syn: molybdenum cofactor synthesis do

InterPro
IPR008284
Family

Molybdenum cofactor biosynthesis protein
PS01078	$\"[80-93]T$	MOCF_BIOSYNTHESIS_1

InterPro
IPR012119
Family

Molybdenum cofactor molybdenum incorporation protein MogA
PIRSF036627	$\"[18-177]T$	Molybdenum cofactor molybdenum incorporation protein MogA

noIPR
unintegrated

unintegrated
G3DSA:3.40.980.10	$\"[13-177]T$	no description
PTHR10192	$\"[1-177]T$	MOLYBDOPTERIN BIOSYNTHESIS PROTEIN

","BeTs to 13 clades of COG0521COG name: Molybdopterin biosynthesis enzymesFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0521 is aompkz-q-dr-b-efgh--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB008284 (Molybdenum cofactor biosynthesis protein, N-terminal) with a combined E-value of 8e-20. IPB008284B 80-110 IPB008284C 129-161","","","-63% similar to PDB:2G2C Putative molybdenum cofactor biosynthesis protein from Corynebacterium diphtheriae. (E_value = 6.8E_32);-51% similar to PDB:2G4R anomalous substructure of MogA (E_value = 1.9E_21);-47% similar to PDB:1IHC X-ray Structure of Gephyrin N-terminal Domain (E_value = 6.0E_12);-47% similar to PDB:1JLJ 1.6 Angstrom crystal structure of the human neuroreceptor anchoring and molybdenum cofactor biosynthesis protein gephyrin (E_value = 6.0E_12);-47% similar to PDB:1O8N THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSYNTHETIC PROTEIN DOMAIN CNX1G (E_value = 7.8E_12);","Residues 21 to 167 (E_value = 9.4e-35) place ANA_1443 in the MoCF_biosynth family which is described as Probable molybdopterin binding domain.","","biosynthesis enzymes (PCD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1444","1546885","1548216","1332","8.67","6.67","47864","ATGTCCACGCTTGACACCTCCGGTCGCGTCCTCACAGGGTGGAACCCTGAAGAGCCGGAGAACTGGTCGGCGAAGATCGCCTGGACCACTCTGATCGTCTCGACCTACTCGATGATCCTGGCCTTCTGCGTCTGGTTCCTTCCCAGCGCGATCGCCCCCAAGCTCACCGAGATCGGCTTCAATCTCACCGAGAGCCAGCTGTACTGGCTCGCCGCCATGCCCGGCCTGTCCTGCGGCCTGATCCGCCTCATCTACATGTTCCTGCCGCCGATCATCGGTACTCGCAAGCTCGTCGCATGGTCGTCCCTGCTCTACGCTCTGCCGATGCTCGGCTGGTTCTTCGCGGTGCAGAGCACCGAGACGAGCTTCGGGACACTGCTCGCCCTGGCCTTCGCCTGCGGGATCGGGGGCGGCTCGTTCTCCGGCTACATGCCCTCGACCGGTTACTTCTTCCCCAAGCGGCTGACCGGTACCGCCCTGGGGATCCAGGCGGGCGTCGGGAACATGGGAATGAGTATCATCCAGTTGCTGAGCCCCTGGCTCATGGGTTTCGGTCTGCTGGGCATCACCTGGATCGCCCCCCAGCACGCCGGCAGCGGCCAAGTGTGGGTCCACAACGTGGCCGTCTTCTTCATCCCGTGGACCATCGTGGCCGCGGTCCTCGCCTTCGCCCTGCTCAAGGACGTCCCGGTCAAGGCTAACATCCGCCAGCAGATCGACATCTTCACCAACCCCGACACCTGGTACATGACGCTCATGTACGTGGCGACCTTCGGCCTGTTCTCCGGGTTCGCTGCACAGTTCGGACTCCTCATCAAGAACACCTACGGGCCTGGCTCGCCCCTGGTCGAGCACTTCGACAAGTCCCTTCTGCCCCTGGGCGCGACCTACGCCTTCCTCGGGCCACTGATCGGGTCGGTGGTCCGAATGCTGTGGGGGCCCCTGTGCGACCGCTTCGGCGGGGCCATCTGGACCTTCATCTCCATCGTCGGGATGGGTGCCACGCTGGCCGTCACCACCTTCTACCTCCACCCGACCGATCCGGCGCAGTTCCCCGGCTTCCTGTGGTCCATGCTGGCGATGTTCTTCTTCTCCGGCCTGGGCAACGCCGGCACCTTCAAGCAGATGCCGATGATCATGCCCAAGCGGCAGGCCGGCGGCGCCATCGGCTTCACGGCTGCCGTTGCCAGCCTGGGCCCCTTCATCGTCGGCGTCGCCATCGCCTCCCTGGGCACCACCGCCTGGTTCTGGATCTCGGTCGCCTACTGCGCCGTGTGCGCGGTCATCTGCTGGCTGCGCTACGCGCGACCGGGAGCCCCGTTCCCGGGCTGA","MSTLDTSGRVLTGWNPEEPENWSAKIAWTTLIVSTYSMILAFCVWFLPSAIAPKLTEIGFNLTESQLYWLAAMPGLSCGLIRLIYMFLPPIIGTRKLVAWSSLLYALPMLGWFFAVQSTETSFGTLLALAFACGIGGGSFSGYMPSTGYFFPKRLTGTALGIQAGVGNMGMSIIQLLSPWLMGFGLLGITWIAPQHAGSGQVWVHNVAVFFIPWTIVAAVLAFALLKDVPVKANIRQQIDIFTNPDTWYMTLMYVATFGLFSGFAAQFGLLIKNTYGPGSPLVEHFDKSLLPLGATYAFLGPLIGSVVRMLWGPLCDRFGGAIWTFISIVGMGATLAVTTFYLHPTDPAQFPGFLWSMLAMFFFSGLGNAGTFKQMPMIMPKRQAGGAIGFTAAVASLGPFIVGVAIASLGTTAWFWISVAYCAVCAVICWLRYARPGAPFPG$","Nitrate/nitrite transporter","Membrane, Extracellular","Nitrate/nitrite transporter","K02575 MFS transporter; NNP family; nitrate transporter","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[33-412]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[14-183]T$ $\"[201-437]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF2	$\"[14-183]T$ $\"[201-437]T$	NITRATE TRANSPORTER
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[67-87]?$ $\"[97-115]?$ $\"[121-143]?$ $\"[173-193]?$ $\"[207-227]?$ $\"[248-268]?$ $\"[293-313]?$ $\"[323-343]?$ $\"[353-373]?$ $\"[388-408]?$ $\"[414-432]?$	transmembrane_regions

","BeTs to 5 clades of COG2223COG name: Nitrate/nitrite transporterFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2223 is -------q--r-b-ef-----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 33 to 412 (E_value = 3.7e-12) place ANA_1444 in the MFS_1 family which is described as Major Facilitator Superfamily.","","transporter (narK2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1445","1548430","1552206","3777","6.09","-21.65","138157","ATGAGCACCACCGGCTCCCAGACCACCGGCCCCGGGATCGTTCCTGGACCCGACCAGCAGGTCGAGAACGCCCCCGGACTGCTCACGCTGGGCTCGTACCTGCGTCGAGGACAAGCCTCTGCCGACGCCCGCCGCCTGTTCCTGACCGGAGGGCGCGAGGCCGACACCTTCTACCGCCACCGGTGGAGCCACGACAAGATGGTCCACTCCACCCACGGGGTCAACTGCACCGGGTCGTGCGCCTGGGAGGTCTACGTCTCCGACGGCATCATCACCTGGGAGAAGCAGATCACCGACTACCCCACCACGGGGCCGGACATGCCCGAGTACGAACCCCGCGGCTGCCCGCGCGGTGCGGCCTTCTCCTGGTACACCTACTCCCCCACGCGCATCCGCTACCCCTACGTGCGCTCGGTCCTGCTGGACGCCTTCCGCGCTGCGAAAGCCGACAACGACGGCGACCCGGTCGCCGCCTGGGCGCAGGTCACCGGTGACCCCGCCACCGCCAAGGCCTACAAGTCCGCCCGAGGCAAGGGCGGCATGGTCCGCGTGGGCTGGGACGAGGCCATGGAGATCGTCGCGGCCGCCTACGTCCACACCATCCGCGCCTGGGGCCCGGACCGGATCGCCGGCTTCAGCGTCATCCCAGCCATGTCCCAGGTCTCCTACGGAGCCGGAGGCCGCCTCCACGAGCTCATCGGCGGCACGATGCTCTCCTTCTACGACTGGTACGCCGACCTGCCCCCGGCCTCACCCCAGGTCTTCGGGGACCAGACCGACGTCCCCGAGGCCGGCGACTGGTACAACTCCCAGTACCTCATGATGTGGGGCTCCAACCTGCCGCTGACCCGTACCCCGGACGCCCACTTCATGACCGAGGCCCGCTACCACGGGCAGAAGGTCGTGGCCGTCTCCCCCGACTACGCCGACAACACCAAGTTCGCCGACCAGTGGCTGCGCGTGGCCCCGGGCACCGACGGCGCCCTCGCCCAGGCGATGGGTCACGTCATCCTCTCGGAGTTCCACGTCAAGCGCGAGGAGTCCTTCTTCCTGGACTACATGCGCCGTCACACCGACTCCCCCTTCCTCATCAGTCTGGACCCCTCCCCCGACGGCACCGGCTACGTGCCCGGGCGCTTCGTGACGGCCTCCGACGTCAACGGCGTCGCCACCGGCGCCCCGAAGAACGAGTTCCGCCCCCTCGTGTGGGACCGCGAGCGCGGCCCGGCCGACCCCGGCGGCACCCTGGCCGACCGCTTCACCCCCGAGGGTGAGGGCAAGTGGAACCTGCTCATGGAGGGTGTCGACCCGGTCATGAGCATCCTGGACCTGCACGGCGAGGGCCCCCAGGTCCAGGCCGCCGAGGTCCTCCTGCCCCGCTTCGACCTGCCCGGCTCCTCCACCCCCGAGGGCTCCGTGGGCGGCGGCGTCGTGCGCCGCGGCGTGCCGGTCACCCGCATCGGGGACCGCATGGTCACCACCGTCTACGACCTGCTCCTGGCCCAGTACGCCGTCGAGCGCCCGTCCATGCCGGGCGAGTGGCCCGCGGACTACCAGGACGCCACTGTCCCAGGCACTCCCGCCTGGGCCAGCGAGATCACCGGCGTTCCCGGCCCCGCCATCATCCAGGTGGCGCGCGACTTCGCTCTCAACGCCGTGGAGTCCGGCGGCCGCTCCCAGATCGTCATGGGCGCGGGCATCAACCACTACTACCACGCCGACCAGATCTACCGGACGATCCTGGCGCTGACCTCCATGTGCGCCACCCAGGGCGTCAACGGCGGCGGCTGGGCCCACTACGTGGGTCAGGAGAAGGTCCGCCCGCTCAGCGGCTTCCAGCAGTACGCCTTCGCCCTGGACTGGCACCGCCCGGCCCGGCAGATGATCTCCACCGGCTTCTGGTACCTCACCACCGACCAGTGGCGCTACGACACCACCTCCGCCGAGCGCCTGGCCTCCCCGCTGGGGCCCGGCACCCTGGCGGGCAAGACCACGACCGACGCCATGGTCGAGGCCATGAAGCGCGGGTGGACGCCGTCCTACCCGACCTTCAACCGCAGCCCGCTGCTCCTGGGCCAGCAGGCCGCCGAGGCGGGCATGGACCCCAAGGACTACATCGTCGAGCAGCTGCGCTCCGGTGAGCTGCGCTTCGCCTGCGAGGACCCCGACGCCCCCGAGAACTTCCCGCGCATCCTGTGCTCGTGGCGCACGAACCTGCTGGGCAGCTCGGCCAAGGGCACGGAGTTCTTCCTGCGCCACATGGTGGGTGCGGATAACGACGTCAACGCCGTCGAGACCCCGGCCGAGCAGCGGCCCGCCTCGGTGACCTGGCGCGACGAGGCCCCCGTGGGCAAGCTCGACCTCATGTGGACCGCGGACTTCCGCAACACCTCCACCACCCTGCACTCCGACGTCGTCCTGCCGGCGGCCACCTGGTACGAGAAGCACGACATCTCCTCGACCGACATGCACCCCTTCGTGCACTCCTTCAACGCGGCCATCGACCCGCCCTGGGAGGCGCGCACCGACTTCCAGGTCTTCCAGACCCTGGCCGGGCTCATCTCCGCCTGGGCGCCGCGCTACCTGGGCACCCAGACCGACGTCGTCGCCGCGCCCCTGACGCACGACACCCCCGACGCCATGACAATGGCGCACGGTGACGTGTCCTCCCTGCCCCAGGAGTGGGTGCCGGGAGTGACGATGCCCAAGCTGGTGCCCACCGAGCGCGACTACACCCAGATCCGGGCCAAGTTCGACGCCCTGGGCCCCCTGGCCGAGAAGCTGGGGATTCCCTGCAAGGGCATCATGCTCAAGCCGGGTCCGGAGGTGGAGCGCCTGGCCCGCAACCACGGGGTCTCCTCCGACGGCGTGGCCGCCGGCCGGCCGCTGCTCGACACCGACATCCGTGCCGCCGACGCCATCTTCACGCTGTCGGGCACCACCAATGGGCGCATCGCCACCGAGGGCTGGGACACGCTGTCCAAGCGCACCGGAACCACGCTGGTCGAGCTCAGCGAGGAGGAGGCAGGCAAGCACATCTCCTTCGCCGACACCCAGGTCAAGCCCCAGGGAGTCATCACCTCCCCGGAGTGGTCCGGCTCCGAGCACGGCGGACGGCGCTACTCGGCCTTCGTGGTCAACGTGGAGCACGCCAAGCCCTGGCACACCCTGACCGGGCGCATGCACTACTACCTCGACCACGACTGGATGCGAGACATGGGCGAGTCCCTGCCGGTCTTCCGGCCGCCACTGGACTTCCACGCCCTGTACGGGGAGGCCGCGCCGGGCTCGGTGTCCACGAGCCAGGCGGGCACAGCGGAGGTCGCGGTGCGCTACATCACCGCGCACAACAAGTGGGCGATCCACTCGCAGTACTTCGACAACCTGCACATGCTCACGCTGGGACGTGGAGGCCAGACCATCTGGATGAGCCCCCAGGACGCCGACAAGATCGGCGTCAAGGACAACGAGTGGGTCGAGGCCTACAACCGCAACGGCATCGTGGCGGCGCGCGCCATTGTCTCCCACCGCATTCCCGAGGGCATGGTCTTCATGCACCACGCCCAGGAGCGCACCATGAACACCCCGCTGACCGAGTCCAGCGGCAGGCGCGGCGGGACGCACAACTCCCTGACGCGGATCGTGCTCAAGCCCAGCCACTTCGCAGGCGGCTACGGGCAGCTGTCCTACGCCTTCAACTACATCGGCCCCACGGGCAACAACCGCGACGAGGTCACGCTTATCCGTCGCCGCAGCAACCAGGAGGTGACTTTCTGA","MSTTGSQTTGPGIVPGPDQQVENAPGLLTLGSYLRRGQASADARRLFLTGGREADTFYRHRWSHDKMVHSTHGVNCTGSCAWEVYVSDGIITWEKQITDYPTTGPDMPEYEPRGCPRGAAFSWYTYSPTRIRYPYVRSVLLDAFRAAKADNDGDPVAAWAQVTGDPATAKAYKSARGKGGMVRVGWDEAMEIVAAAYVHTIRAWGPDRIAGFSVIPAMSQVSYGAGGRLHELIGGTMLSFYDWYADLPPASPQVFGDQTDVPEAGDWYNSQYLMMWGSNLPLTRTPDAHFMTEARYHGQKVVAVSPDYADNTKFADQWLRVAPGTDGALAQAMGHVILSEFHVKREESFFLDYMRRHTDSPFLISLDPSPDGTGYVPGRFVTASDVNGVATGAPKNEFRPLVWDRERGPADPGGTLADRFTPEGEGKWNLLMEGVDPVMSILDLHGEGPQVQAAEVLLPRFDLPGSSTPEGSVGGGVVRRGVPVTRIGDRMVTTVYDLLLAQYAVERPSMPGEWPADYQDATVPGTPAWASEITGVPGPAIIQVARDFALNAVESGGRSQIVMGAGINHYYHADQIYRTILALTSMCATQGVNGGGWAHYVGQEKVRPLSGFQQYAFALDWHRPARQMISTGFWYLTTDQWRYDTTSAERLASPLGPGTLAGKTTTDAMVEAMKRGWTPSYPTFNRSPLLLGQQAAEAGMDPKDYIVEQLRSGELRFACEDPDAPENFPRILCSWRTNLLGSSAKGTEFFLRHMVGADNDVNAVETPAEQRPASVTWRDEAPVGKLDLMWTADFRNTSTTLHSDVVLPAATWYEKHDISSTDMHPFVHSFNAAIDPPWEARTDFQVFQTLAGLISAWAPRYLGTQTDVVAAPLTHDTPDAMTMAHGDVSSLPQEWVPGVTMPKLVPTERDYTQIRAKFDALGPLAEKLGIPCKGIMLKPGPEVERLARNHGVSSDGVAAGRPLLDTDIRAADAIFTLSGTTNGRIATEGWDTLSKRTGTTLVELSEEEAGKHISFADTQVKPQGVITSPEWSGSEHGGRRYSAFVVNVEHAKPWHTLTGRMHYYLDHDWMRDMGESLPVFRPPLDFHALYGEAAPGSVSTSQAGTAEVAVRYITAHNKWAIHSQYFDNLHMLTLGRGGQTIWMSPQDADKIGVKDNEWVEAYNRNGIVAARAIVSHRIPEGMVFMHHAQERTMNTPLTESSGRRGGTHNSLTRIVLKPSHFAGGYGQLSYAFNYIGPTGNNRDEVTLIRRRSNQEVTF$","Nitrate reductase, alpha subunit","Periplasm, Extracellular","nitrate reductase, alpha subunit","nitrate reductase; alpha subunit ","nitrate reductase, alpha subunit","","Schneider F., Lowe J., Huber R., Schindelin H., Kisker C., Knablein J. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution. J. Mol. Biol. 1996. 263(1):53-69. PMID: 8890912","","","

InterPro
IPR002052
Domain

N-6 Adenine-specific DNA methylase
PS00092	$\"[832-838]?$	N6_MTASE

InterPro
IPR006468
Family

Nitrate reductase, alpha subunit
TIGR01580	$\"[25-1255]T$	narG: nitrate reductase, alpha subunit

InterPro
IPR006655
Family

Prokaryotic molybdopterin oxidoreductase
PS00490	$\"[797-814]T$	MOLYBDOPTERIN_PROK_2
PS00551	$\"[70-88]T$	MOLYBDOPTERIN_PROK_1

InterPro
IPR006656
Domain

Molybdopterin oxidoreductase
PF00384	$\"[130-853]T$	Molybdopterin

InterPro
IPR006657
Domain

Molydopterin dinucleotide-binding region
PF01568	$\"[1110-1230]T$	Molydop_binding

noIPR
unintegrated

unintegrated
G3DSA:2.40.40.20	$\"[1071-1212]T$	no description
G3DSA:3.40.228.10	$\"[239-606]T$	no description
G3DSA:3.40.50.740	$\"[785-854]T$	no description
G3DSA:3.90.55.10	$\"[57-153]T$	no description
PTHR11615	$\"[115-365]T$ $\"[508-644]T$ $\"[747-917]T$ $\"[1099-1248]T$	NITRATE, FROMATE, IRON DEHYDROGENASE
PTHR11615:SF35	$\"[115-365]T$ $\"[508-644]T$ $\"[747-917]T$ $\"[1099-1248]T$	NITRATE REDUCTASE ALPHA CHAIN

","BeTs to 17 clades of COG0243COG name: Anaerobic dehydrogenases, typically selenocysteine-containingFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0243 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB006655 (Prokaryotic molybdopterin oxidoreductase) with a combined E-value of 1e-33. IPB006655A 125-137 IPB006655B 176-200 IPB006655C 322-352 IPB006655E 1143-1166***** IPB006657 (Molydopterin dinucleotide binding domain) with a combined E-value of 6.2e-20. IPB006657A 115-134 IPB006657B 185-205 IPB006657C 1143-1166 IPB006657C 585-608***** IPB006963 (Molybdopterin oxidoreductase Fe4S4 domain) with a combined E-value of 4e-09. IPB006963B 110-137 IPB006963C 179-191","","","-41% similar to PDB:2IVF ETHYLBENZENE DEHYDROGENASE FROM AROMATOLEUM AROMATICUM (E_value = 1.1E_27);","Residues 130 to 853 (E_value = 1.3e-88) place ANA_1445 in the Molybdopterin family which is described as Molybdopterin oxidoreductase.Residues 1110 to 1230 (E_value = 1.5e-26) place ANA_1445 in the Molydop_binding family which is described as Molydopterin dinucleotide binding domain.","","reductase, alpha subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1446","1552206","1553900","1695","5.45","-11.53","61857","ATGAAGGTCATGGCCCAGATCGCAATGGTGATGAACCTCGACAAGTGCATCGGCTGCCACACCTGTTCAGTGACCTGCAAGCAGGCCTGGACCAACCGCGAGGGCACCGAGTACATGTGGTTCAACAACGTCGAGACCCGCCCTGGTGTCGGCTACCCCAAGGGCTGGGAGGACCAGGACACCTGGCGCGGTGGCTGGGAGCGCACGGCCTCGGGCCGCCTGCGGCCCCGCTCGGGCGGGCGCCTGCGCCGCCTGGTCAACATCTTCGCCAACCCCGAGATGCCCACGGTCGAGGACTACTACGAGCCGTGGACCTACGAGTACGACAAGCTGCTCTCGGCCCCCAAGGACTCCCCGGCGATTCCGGTGGCGCGCGCCAAGAGCCAGCTGACCGGCGAGTACATGCCCACCATCAAGTGGGGTCCCAACTGGGATGACGACCTGGGCGGCTCCATGGAGACCCTCCAGCAGGACCCGATCATCGAGGCGATGAGCACGAAGGTGCGCACCGACATCGAGTCGGCCTTCATGTTCTACCTGCCGCGCATCTGCGAGCACTGCCTCAACCCCACCTGCGTGTCCGCCTGCCCGTCGGGCGCCATGTACAAGCGCACTGAGGACGGCATCGTCCTGGTGGACCAGGACGCCTGCCGCGGCTGGCGCATGTGTGTGTCCTCCTGCCCTTACAAGAAGGTCTACTTCAACCACGCCACCGGCAAGGCCGAGAAGTGCACCCTGTGCTACCCGCGCCTGGAGATCGGCCAGCCCACTGTGTGCTCGGAGACCTGCGTGGGCCGCCTGCGCTACCTGGGCGTCCTCCTCTACGACGCCGATCGCGTCTCGCAGGCCGCCGCCGTCAAGGACCCGCAGGACCTGTACATGGCCCAGCGCGAGATCCTCCTCAACCCCCACGACCCCGAGGTCGTGGCGGGCGCGCGCGCCGAGGGCGTGCCGGACAACTGGATCGAGGCGGCCCAGGCCTCCCCCATCTGGGACCTCATCGACACCTATGAGGTGGCCCTGCCCCTGCACCCCGAGTACCGCACCATGCCGATGGTCTGGTACATCCCGCCGCTCTCCCCGGTCGTCGACGAGGTCGCGGCCGCCGGACTGGACGGTGAGAACTACAAGGTGCTGCTCACGGCCGTCTCCGACATGCGCATTCCGTTGGAGTACCTGGCGGGCCTGTTCACGGCCGGTGACACCAACACGGTCGAGCTCGTGCTGCGGCGCCTGGCCGCGATGCGCTCCCACATGCGCGACGTGCGCCTGGGCCGCGAGCCCGACCCGGCCATCGCCGCCGCCGTGGGCCTGGACGGCAAGAAGCTGGAGGCCATGTACCGGCTGCTGGCCATCGCCAAGTACGACGACCGCTACGTCATCCCCACCGCCAAGCCCGAGGTCCCCCGCGGCATGGAGTCCATGGGCAACGACGTCATGACCCTCCTGGGTGAGGGGGCCCCGGCCGGGTGCCACCCCGACGTCGCCTCCTTCCACGGCCAGGGCGGCGGCGCCATGAACGGCGGCCCGGTGAGCCTGCCGCTGCCGACCGTGCGCCGCGAGCCGGTGCCGGCCGCCGGCCCGGGCATGCCGCAGGTCGGTGTTCCTGAGCCGGTGGGGCAGGCCCAGGCGGCCGACTCCTCGGCCCGGGCCACCTCGAGCGGCCCGGCGGCTGCGGCCCCCAGGGACCTCTGA","MKVMAQIAMVMNLDKCIGCHTCSVTCKQAWTNREGTEYMWFNNVETRPGVGYPKGWEDQDTWRGGWERTASGRLRPRSGGRLRRLVNIFANPEMPTVEDYYEPWTYEYDKLLSAPKDSPAIPVARAKSQLTGEYMPTIKWGPNWDDDLGGSMETLQQDPIIEAMSTKVRTDIESAFMFYLPRICEHCLNPTCVSACPSGAMYKRTEDGIVLVDQDACRGWRMCVSSCPYKKVYFNHATGKAEKCTLCYPRLEIGQPTVCSETCVGRLRYLGVLLYDADRVSQAAAVKDPQDLYMAQREILLNPHDPEVVAGARAEGVPDNWIEAAQASPIWDLIDTYEVALPLHPEYRTMPMVWYIPPLSPVVDEVAAAGLDGENYKVLLTAVSDMRIPLEYLAGLFTAGDTNTVELVLRRLAAMRSHMRDVRLGREPDPAIAAAVGLDGKKLEAMYRLLAIAKYDDRYVIPTAKPEVPRGMESMGNDVMTLLGEGAPAGCHPDVASFHGQGGGAMNGGPVSLPLPTVRREPVPAAGPGMPQVGVPEPVGQAQAADSSARATSSGPAAAAPRDL$","Nitrate reductase, beta subunit","Cytoplasm, Periplasm","nitrate reductase, beta subunit","nitrate reductase beta chain ","nitrate reductase, beta subunit","","George D.G., Hunt L.T., Yeh L.S., Barker W.C. New perspectives on bacterial ferredoxin evolution. J. Mol. Evol. 1985. 22(1):20-31. PMID: 3932661Otaka E., Ooi T. Examination of protein sequence homologies: V. New perspectives on evolution between bacterial and chloroplast-type ferredoxins inferred from sequence evidence. J. Mol. Evol. 1989. 29(3):246-254. PMID: 2506358Fukuyama K., Matsubara H., Tsukihara T., Katsube Y. Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 A resolution. Structural comparisons of bacterial ferredoxins. J. Mol. Biol. 1989. 210(2):383-398. PMID: 2600971Duee E.D., Fanchon E., Vicat J., Sieker L.C., Meyer J., Moulis J.M. Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution. J. Mol. Biol. 1994. 243(4):683-695. PMID: 7966291","","","

InterPro
IPR001450
Domain

4Fe-4S ferredoxin, iron-sulfur binding
PR00353	$\"[9-20]T$ $\"[191-202]T$	4FE4SFRDOXIN

InterPro
IPR006547
Family

Nitrate reductase, beta subunit
TIGR01660	$\"[1-498]T$	narH: nitrate reductase, beta subunit

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.20	$\"[4-46]T$ $\"[156-246]T$	no description
PTHR11938	$\"[10-467]T$	FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF8	$\"[10-467]T$	NITRATE REDUCTASE BETA CHAIN

","BeTs to 5 clades of COG1140COG name: Nitrate reductase beta chainFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1140 is -----z----r-b-ef----------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-68% similar to PDB:1Q16 Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli (E_value = 9.6E_156);-68% similar to PDB:1R27 Crystal Structure of NarGH complex (E_value = 9.6E_156);-68% similar to PDB:1SIW Crystal structure of the apomolybdo-NarGHI (E_value = 9.6E_156);-68% similar to PDB:1Y5I The crystal structure of the NarGHI mutant NarI-K86A (E_value = 9.6E_156);-68% similar to PDB:1Y5L The crystal structure of the NarGHI mutant NarI-H66Y (E_value = 9.6E_156);","No significant hits to the Pfam 21.0 database.","","reductase, beta subunit (narH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1447","1553902","1554663","762","5.21","-8.64","27007","ATGGTCTCCTTCGTCCGCGCCCCCCGGGTTCTTCAGGAACCCGCCGAGGTGCACCTGACGCCCTCCCAGCGAGCCACCGTGCACATGGCGGCCTCGCTGCTGTTGGACTACCCGGCCGAGGGGACTCTGGAGACGCATCTGAACGCCGTCGAGGCCGAGCTGGCCACACTGCCGGCGGAGGTGGCCGTCCTCCTGGAGGAGTTCATCGCTCAGGCGCGGCGCCGCGGTGAGCGGGCCATGGCCGAGCACTACGTGGAGGTCTTCGACCGACGTCGGCGCTGCTGCCTGTACCTGACGTACTACACGGTGGGCGACACCCGGCATCGGGGCGCCGCGCTGCTGGCCTTCAAACAGGCACTGGCGGCGGCCGGCTACGAGATGGCCGCCGACGAGCTGCCCGACTACCTGCCGGTGGTCCTCGAGCTGTCCGCGCGCAGCGGCGACGAGGTGGCCAGTGCGCTCCTGTCCTCCCACCGGGAGGGCATAGAGGTGCTGCGCAGCGCCCTGGCCGACGCCGCCTCCCCCTACGCGGGGCTGGTGGAGGCCGTCTCGATGACTCTGCCGCAGATCGACGAGGCCACCGCCGAGCGCGTACGCGCCCTCGTGGCGGCCGGGCCGCCCACCGAGACCGTCGGTGTCACCGACACCCTGCCCTTCCCGACCATTCCCGTGCGCAACCCGAGCCTGTCCGGTGTAACCGCCGTGCCGGGCTCGGCACCAGTCGCCGATCCTTCCCCTTCACAAGCAGCCAGGAGAGCATGA","MVSFVRAPRVLQEPAEVHLTPSQRATVHMAASLLLDYPAEGTLETHLNAVEAELATLPAEVAVLLEEFIAQARRRGERAMAEHYVEVFDRRRRCCLYLTYYTVGDTRHRGAALLAFKQALAAAGYEMAADELPDYLPVVLELSARSGDEVASALLSSHREGIEVLRSALADAASPYAGLVEAVSMTLPQIDEATAERVRALVAAGPPTETVGVTDTLPFPTIPVRNPSLSGVTAVPGSAPVADPSPSQAARRA$","Nitrate reductase, delta subunit","Cytoplasm","Nitrate reductase delta subunit","nitrate reductase delta chain ","nitrate reductase molybdenum cofactor assembly chaperone","","Pantel I., Lindgren P.E., Neubauer H., Gotz F Identification and characterization of the Staphylococcus carnosus nitrate reductase operon. Mol. Gen. Genet. 1998. 259(1):105-114. PMID: 9738886","","","

InterPro
IPR003765
Family

Nitrate reductase, delta subunit
PF02613	$\"[27-188]T$	Nitrate_red_del
TIGR00684	$\"[32-183]T$	narJ: nitrate reductase molybdenum cofactor

","BeTs to 4 clades of COG2180COG name: Nitrate reductase delta subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2180 is a----z----r-b-ef----------Number of proteins in this genome belonging to this COG is 1","***** IPB003765 (Nitrate reductase, delta subunit) with a combined E-value of 9.6e-21. IPB003765A 31-45 IPB003765C 88-141 IPB003765D 142-184","","","No significant hits to the PDB database (E-value < E-10).","Residues 27 to 188 (E_value = 2.1e-39) place ANA_1447 in the Nitrate_red_del family which is described as Nitrate reductase delta subunit.","","reductase delta subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1448","1554665","1555453","789","10.05","10.58","29028","ATGAGCCCGATTCAGCAGAACCTCATGTGGGTGGCCCTGCCCTACGCCAGCCTGGTGCTGCTGGTGGCAGGCATGATCTGGCGGTGGCGCACCGACCAGTTCGGCTGGACCTCCCGCTCCTCGCAGTGGAACGAGTCCCGCATCCTGCGCCTGGCCTCCCCCCTGTTCCACCTGGGCTTCCTCATGGTGATGGGCGGTCACGTCGTCGGGCTCCTGGTGCCCAAGGACGTCACCGAGATGCTGGGCGTCTCCCAGCACATGTACCACCTGGGCGCCACCTACCTGGGAACCTTGGCGGCCATCCTGACGATCGTGGGCCTGGTCGGGCTCATCTACCGGCGCATCATCGTCAAGAGCGTGCGCCTGGCCACCACCCGCAACGACCTGGTCATGTACTGCTTCCTCATCGTGCCGATCCTGCTGGGAACGGCGGCCACGGTCCTCAACCAGCTCGCCGACGCCCACGGCTACGACTACCGCGAGACGATCAGCCCCTGGCTGCGCTCGGTACTGGTGCTCCAGCCGCGCCCCGAGCTCATGGCCGACGTGCCGGTCTCCTTCAAGCTCCACGTCATCGCAGGCTTCCTGCTCCTGGCGATCTGGCCCTTCACCCGTCTGGTCCACGTGGTCTCCGCACCCGTGGGCTACGTGACCCGCCCCTACGTGGTCTACCGTTCCCGCGAGGGCGCCACCTCCACCGCTCAGACCTCACGCGGCTGGACCCCGGTGCGGACCCAGGGCACCGGCAACCAGGGGGCCAACGACGTCACTCCCTCCCAGGGAGCCTGA","MSPIQQNLMWVALPYASLVLLVAGMIWRWRTDQFGWTSRSSQWNESRILRLASPLFHLGFLMVMGGHVVGLLVPKDVTEMLGVSQHMYHLGATYLGTLAAILTIVGLVGLIYRRIIVKSVRLATTRNDLVMYCFLIVPILLGTAATVLNQLADAHGYDYRETISPWLRSVLVLQPRPELMADVPVSFKLHVIAGFLLLAIWPFTRLVHVVSAPVGYVTRPYVVYRSREGATSTAQTSRGWTPVRTQGTGNQGANDVTPSQGA$","Nitrate reductase, gamma subunit","Membrane, Cytoplasm, Extracellular","respiratory nitrate reductase, gamma subunit","nitrate reductase gamma subunit ","respiratory nitrate reductase, gamma subunit","","Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M. Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon. Mol. Gen. Genet. 1990. 222(1):104-111. PMID: 2233673Pantel I., Lindgren P.E., Neubauer H., Gotz F Identification and characterization of the Staphylococcus carnosus nitrate reductase operon. Mol. Gen. Genet. 1998. 259(1):105-114. PMID: 9738886","","","

InterPro
IPR003816
Family

Nitrate reductase, gamma subunit
PF02665	$\"[4-228]T$	Nitrate_red_gam
TIGR00351	$\"[2-228]T$	narI: respiratory nitrate reductase, gamma

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[51-73]?$ $\"[92-112]?$ $\"[132-152]?$ $\"[183-203]?$	transmembrane_regions

","BeTs to 5 clades of COG2181COG name: Nitrate reductase gamma subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2181 is a---------r-b-ef----------Number of proteins in this genome belonging to this COG is 1","***** IPB003816 (Nitrate reductase, gamma subunit) with a combined E-value of 1.8e-62. IPB003816A 7-20 IPB003816B 28-78 IPB003816C 113-135 IPB003816D 180-227","","","-47% similar to PDB:1Y5I The crystal structure of the NarGHI mutant NarI-K86A (E_value = 2.3E_17);-47% similar to PDB:1Y5N The crystal structure of the NarGHI mutant NarI-K86A in complex with pentachlorophenol (E_value = 2.3E_17);-47% similar to PDB:1Q16 Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli (E_value = 3.0E_17);-47% similar to PDB:1SIW Crystal structure of the apomolybdo-NarGHI (E_value = 3.0E_17);-47% similar to PDB:1Y4Z The crystal structure of Nitrate Reductase A, NarGHI, in complex with the Q-site inhibitor pentachlorophenol (E_value = 3.0E_17);","Residues 4 to 228 (E_value = 2.3e-69) place ANA_1448 in the Nitrate_red_gam family which is described as Nitrate reductase gamma subunit.","","nitrate reductase, gamma subunit (narI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1449","1555488","1556408","921","5.12","-6.68","30138","ATGAGTATCACTCGTCGCGCGGCCATCGCCGCTGTCAGTCTGCTCTCCGCCGTCTGTCTGGCCGCGTGCGGCGGCTCCGCCTCCAACAGCGCCACCGGCGCCGCTTCCGCAGGCACCTCGGGTGGCGCGGGGAAGGCGACCGGCAAGGTCACGGTCCTGGCCGCGGCCTCCCTCCAGGGGGCCTTCGAGGAGATCGAGAAGACCGTGGAGAAGGACAACCCCGGCCTGGACGTCACCTTCGACTTCCAGGGCTCCCAGGACCTGGTGGCCTCCCTGGCGGGTGGCGACAGCGCCGACGTCCTGGCCACGGCCAACAACTCCACGATGAAGACCGCTGCGGACCAGAAGCTGGTCGGGAGCCAGACCGAGTTCGCCACCAACGTCCTGACCCTCATCGTCCCCAAGGGCAACCCCAAGAAGATCACCGGGCTGGACTCGTCGCTGGATGGCGCCAACCTGGTCATCTGCGCCCCCGAGGTGCCCTGCGGTGAGGCCACCAAGAAGCTCGCCCAGGCCCAGGGAATCACCCTCAAGCCGGTCTCCGAGGAGCAGAAGGTGACCGACGTGCGCGGCAAGGTCGAGTCCGGTGAGGCCGACGCCGGCATCGTCTACACCACCGACGCGGCGGCCGCCAAGGACAAGGCGGACAAGATCGACATCCCCGACGGCGGCGTCGTCAACCACTACCCGATCGCCCAGACCGCCAAGCCCGAGAACCCCGCGGGCGCGCAGGCCTTCATCGAGGCCGTCACCGGCAAGACCGGCCAGGAGATCCTGGCCAAGCACGGCTTCGGCAAGCCCGGCAGCACCGCTGCCGGGGCGAGTGCTGGGGCCAGCGCTGCCCCGTCCCAGGCCGCGACCACTGAGGGGTCCTCCGCCCCGGAGGCGAACAAGCCCACCGCGCAGACTACGGCTCCGTGA","MSITRRAAIAAVSLLSAVCLAACGGSASNSATGAASAGTSGGAGKATGKVTVLAAASLQGAFEEIEKTVEKDNPGLDVTFDFQGSQDLVASLAGGDSADVLATANNSTMKTAADQKLVGSQTEFATNVLTLIVPKGNPKKITGLDSSLDGANLVICAPEVPCGEATKKLAQAQGITLKPVSEEQKVTDVRGKVESGEADAGIVYTTDAAAAKDKADKIDIPDGGVVNHYPIAQTAKPENPAGAQAFIEAVTGKTGQEILAKHGFGKPGSTAAGASAGASAAPSQAATTEGSSAPEANKPTAQTTAP$","ABC-type molybdate transport system, periplasmic component","Extracellular, Periplasm","molybdenum ABC transporter, periplasmicmolybdate-binding protein, putative","molybdate ABC transporter; periplasmic molybdate-binding protein","molybdenum ABC transporter, periplasmic molybdate-binding protein","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR005950
Family

Molybdenum ABC transporter, periplasmic binding protein
TIGR01256	$\"[55-263]T$	modA: molybdate ABC transporter, periplasmi

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[9-257]T$	SBP_bac_1

InterPro
IPR011587
Domain

Prokaryotic extracellular metal-binding protein
PD008688	$\"[186-265]T$	Q8GAG9_ARTNI_Q8GAG9;

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[46-165]T$	no description
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[7-27]?$	transmembrane_regions

","BeTs to 10 clades of COG0725COG name: ABC-type molybdate transport system, periplasmic componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0725 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-45% similar to PDB:1AMF CRYSTAL STRUCTURE OF MODA, A MOLYBDATE TRANSPORT PROTEIN, COMPLEXED WITH MOLYBDATE (E_value = 3.2E_16);-45% similar to PDB:1WOD CRYSTAL STRUCTURE OF MODA, A MOLYBDATE PROTEIN, COMPLEXED WITH TUNGSTATE (E_value = 3.2E_16);","Residues 9 to 257 (E_value = 5.5e-08) place ANA_1449 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","ABC transporter, periplasmic molybdate-binding protein, putative","","1","","","","","","","","","","","Tue Aug 14 15:16:43 2007","","Tue Aug 14 15:16:43 2007","","","Tue Aug 14 15:16:43 2007","","","","Tue Aug 14 15:16:43 2007","Tue Aug 14 15:16:43 2007","","","","","yes","","" "ANA_1450","1556613","1558577","1965","9.60","12.24","68396","ATGGGGACGCGCGTGTCCTGGGGGCAGCTCCCCCAGCTGCTGGCAACGCCGTCGGCGCAAGCCGCCCTGTGGCTCTCGATCCGCACCTGTCTGAGTTCCACGGTCATCTGTGTGGCGCTGGGCGTGCCACTGGCGCTGCTGCTCGCCCGCAGCTGGCCGGGGGTGAGGATCGCGCGGATCCTCGCGGTGCTGCCGATGACGATGCCGCCGGTGGTGGCCGGTATCGCACTGCTGTCCACCTTGGGCAACCGCGGCCTGCTGGGGGCGCACCTGAAGGAGTGGGGGGTACCCATTGCCTTCTCCACCACCGCGGTGGTCATCGCCCAGGTGTTCGTCTCCATGCCTTTCCTGGTGGTCACTCTGGAGGCGACACTGCGCAGCCGCGACAAGCGGGCCGAAGTCACCGCCCGAAGCCTCGGGGCCGGCCCGTGGCGGGTTCTGGCGCAGGTGACGCTGCCGTTGGCAACGCCTGCTCTGGCTCGGGGCACGGCCCTGGCTCTGGGCCGGAGCCTGGGCGAGTTCGGGGCGACCATCGCCTTCGCCGGCTCCAAGGAGGGCGTCACCCGCACGATGCCGCTGGCCATCTACCTGGAGCGGGAGAAGGACACGGCCACCTCCCTGGCCCTGGCCGCTGTGCTCATTGGCCTGTCCTTCATCATCGTCGGGGCGACCAATATCGACTGGGGCAGGGTGGCCTCCCGCCTCCTGCCCCGCCGCGGGCTCCGGGGGCGCCAGGACCACGACGCCGCTGCGTCGGAGCCCCGAGGCGCGCAGGTCTCCACCCAAGGCGGGGACGAGCGGATTCCCGAGTCACCTCGGGACGGCGGACGCGGCCAGGACCTGCAGGTGGCCTTTGAGCTGCCTGAGCGTGACGTCGTCATCGACCTGGAGGTGGAGGCGGGGCGCACGACGGCACTCATCGGTCCCAATGGCTCGGGCAAGTCGACGGTCTGCTCTGTGGTGGCCGGCCTGCTCGACGCCGAGAACGGTCAGGTCGTGCTGGGCGGGCGAGTCCTGGACGGCACCGGGGGCTTCGTGCGGGCGGGGCGGCGCCGGGTAGCGCTGCTCAGCCAGGAGCCGGGCGTCTTCGCCCACATGTCCGTGCTGGGCAACGTGGTCTTCGCGCTGCGCTGCCAGGGGGTGAGCCGGGCGGAGGCGACGCGTCGGGCCCGCGCCGAGCTGGCCGCCGTCGGTGCCGATCACCTGGCATCCCGCCCGGGAGGAGCGCTCTCAGGAGGGCAGGCTGCCCGGGTGGCCTTGGCCCGGGCGCTGGCGACAGGGCCCCGTCTGCTGGTCCTGGACGAGCCGATGGCCGCCCTGGACGTGACCGCCCGCCAGGAGATGCGCCGCCTGGTGGCGCGCCGGTGCGCCGAGGAGGGGCTGACACTGCTCCTGGTGACCCATGACGTCCTGGACCTGACGGCGCTGGCCGAGGACGTCGTCGTCCTGGACCGGGGCCGAGTGGTGGAGCAGGGGCCGACGGCGAGGATCCTGTCCGCGCCCCGTTCGGACTTCGTCGCCCACCTGACCGGGACGGCTGTGCTCACCGGGGTCGTCGACGGCGACGCCGAGGCGCCGGGACTGCGGCTGCCGTCGGGGCAGGTCATTCATGGCCGCCCCCGGGAGGACTCCACTGACGGGCATGTCGGCGAGCAAGGCCACCGGGACGACCGCAACGAGGTGCCCCGGCCCGGAGCACCGGGGATCGCGCTGGTGCCGCCCGACGCCGTCGCCCTCTACCGGCAGGCGCCGCACGGCAGTCCCCGCAACGTCCTGACCGGCCGGGTGACGGGGCTGGAGCGCTCGGGGGCGCTGGTGAGTGTGCGCCTGGAGCTCGAGGAGGGGCAGCGGCTGTCAGCGGCGGTCACCGCGGGTGCCGTGGCTGAGCTCGGCATCACCGAGGGCCGGGAGGTCTGCTGCGTCATCAAGGCGGTGCAGGTGCGTATCCTGACCCGCCGGGGTTGA","MGTRVSWGQLPQLLATPSAQAALWLSIRTCLSSTVICVALGVPLALLLARSWPGVRIARILAVLPMTMPPVVAGIALLSTLGNRGLLGAHLKEWGVPIAFSTTAVVIAQVFVSMPFLVVTLEATLRSRDKRAEVTARSLGAGPWRVLAQVTLPLATPALARGTALALGRSLGEFGATIAFAGSKEGVTRTMPLAIYLEREKDTATSLALAAVLIGLSFIIVGATNIDWGRVASRLLPRRGLRGRQDHDAAASEPRGAQVSTQGGDERIPESPRDGGRGQDLQVAFELPERDVVIDLEVEAGRTTALIGPNGSGKSTVCSVVAGLLDAENGQVVLGGRVLDGTGGFVRAGRRRVALLSQEPGVFAHMSVLGNVVFALRCQGVSRAEATRRARAELAAVGADHLASRPGGALSGGQAARVALARALATGPRLLVLDEPMAALDVTARQEMRRLVARRCAEEGLTLLLVTHDVLDLTALAEDVVVLDRGRVVEQGPTARILSAPRSDFVAHLTGTAVLTGVVDGDAEAPGLRLPSGQVIHGRPREDSTDGHVGEQGHRDDRNEVPRPGAPGIALVPPDAVALYRQAPHGSPRNVLTGRVTGLERSGALVSVRLELEEGQRLSAAVTAGAVAELGITEGREVCCVIKAVQVRILTRRG$","ABC-type sulfate/molybdate transport system, permease component","Membrane, Cytoplasm","Molybdenum transport system permease proteinmodB","ABC transporter related","NifC-like ABC-type porter","","Wang S.Z., Chen J.S., Johnson J.L. A nitrogen-fixation gene (nifC) in Clostridium pasteurianum with sequence similarity to chlJ of Escherichia coli. Biochem. Biophys. Res. Commun. 1990. 169(3):1122-1128. PMID: 2194453","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[23-233]T$	BPD_transp_1
PS50928	$\"[23-222]T$	ABC_TM1

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[410-452]T$	Q8GAG7_ARTNI_Q8GAG7;
PF00005	$\"[301-486]T$	ABC_tran
PS50893	$\"[276-510]T$	ABC_TRANSPORTER_2
PS00211	$\"[410-424]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[300-487]T$	AAA

InterPro
IPR004606
Domain

Molybdenum-pterin binding
TIGR00638	$\"[584-653]T$	Mop: molybdenum-pterin binding domain

InterPro
IPR005116
Domain

TOBE
PF03459	$\"[586-649]T$	TOBE

InterPro
IPR006469
Family

NifC-like ABC-type porter
TIGR01581	$\"[1-221]T$	Mo_ABC_porter: NifC-like ABC-type porter

InterPro
IPR011867
Family

Molybdate ABC transporter, permease protein
TIGR02141	$\"[24-230]T$	modB_ABC: molybdate ABC transporter, permea

noIPR
unintegrated

unintegrated
G3DSA:2.40.50.100	$\"[573-653]T$	no description
G3DSA:3.40.50.300	$\"[277-513]T$	no description
PTHR19222	$\"[279-560]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[30-48]?$ $\"[60-80]?$ $\"[99-119]?$ $\"[209-229]?$	transmembrane_regions

","BeTs to 10 clades of COG0555COG name: ABC-type sulfate/molybdate transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0555 is aompkz-q-dr-bcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB005116 (TOBE domain) with a combined E-value of 3.3e-30. IPB005116A 308-324 IPB005116B 351-368 IPB005116C 410-423 IPB005116D 430-449 IPB005116E 464-477***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.5e-29. IPB013563A 290-324 IPB013563C 407-434 IPB013563D 462-514***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 4.7e-24. IPB005074C 290-337 IPB005074D 398-441***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 6.9e-13. IPB010509B 301-326 IPB010509D 405-449***** IPB003725 (Molybdenum-binding protein, N-terminal) with a combined E-value of 8.6e-08. IPB003725C 618-649","","","-42% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 3.8E_18);-42% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 3.2E_17);-42% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 3.2E_17);-42% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 3.2E_17);-42% similar to PDB:2AWN Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg) (E_value = 3.2E_17);","Residues 23 to 233 (E_value = 1.7e-21) place ANA_1450 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.Residues 301 to 486 (E_value = 5e-58) place ANA_1450 in the ABC_tran family which is described as ABC transporter.Residues 586 to 649 (E_value = 1.6e-16) place ANA_1450 in the TOBE family which is described as TOBE domain.","","transport system permease protein modB (AF077856)","","1","","","","","","","","","","","Tue Aug 14 15:17:11 2007","","Tue Aug 14 15:17:11 2007","","","Tue Aug 14 15:17:11 2007","Tue Aug 14 15:17:11 2007","","","Tue Aug 14 15:17:11 2007","Tue Aug 14 15:17:11 2007","","","","","yes","","" "ANA_1452","1558679","1559485","807","6.43","-2.46","27708","GTGATCACCGAGGAGCGTCTACGACCGCTGAGGCGCGATGAGCTGGAGCGCTACCACCGCAATGCGCTCGTGCCGCAGGTGGGGCTCGTGGGGCAGCAGCGCATCCGCGCGTCCCGGGTCCTGCTCATCGGTGCCGGCGGGCTCGGGGCGCCGGCGGCCCTGTACCTGGCGGCCGCCGGAGTGGGGACGATCGGGCTCATTGACGACGACAATGTCGACGTGTCCAACCTGCAACGCCAGGTCATCCACGCCACGGCGGCCGTGGGGCGCCCCAAGGTGGACTCGGCGGCCGAGGCGATCAGGGCGCTCAATCCTGACGTTGAGGTCGTTGCCCACCGGACGCGGTTGACGGCCGATAACGCCCAGGGCCTTCTGGGCGGCTGGGACGTGGTCATTGACGGCACGGACAACTTCCCCACGCGGTACCTGGTCAATGACGCCACCGTCATGCTGGGGCTGCCGCTGGTGCACGGGGCGGTACTGGGGTTCAACGGGCAGGTGGGGGTTTTCGACGCGCGCCGGGGCCCGTGCTACCGGTGCCTGCATCCCACCCCGCCGCCCGCAGGTTCGGTGCCCTCCTGCGCGGAGGCCGGGGTGCTGGGGGTGCTGCCCGGCATCATCGGGACGATGCAGGCCGCTGAGGCGCTCAAGCTGGTGATCGGTGGCGGGCAGCCGCTGCTGGGGAGGTTGGCGTTGCTCGACGCCTGGGGGGGGGGCGCACCTGCGGGAGATTCCGGTGGCAAAGAACCCGGCCTGCCCAGTGTGCGGGGAGAACCCGAGTATCACCGCACTGGTCACGGAGGCTGA","VITEERLRPLRRDELERYHRNALVPQVGLVGQQRIRASRVLLIGAGGLGAPAALYLAAAGVGTIGLIDDDNVDVSNLQRQVIHATAAVGRPKVDSAAEAIRALNPDVEVVAHRTRLTADNAQGLLGGWDVVIDGTDNFPTRYLVNDATVMLGLPLVHGAVLGFNGQVGVFDARRGPCYRCLHPTPPPAGSVPSCAEAGVLGVLPGIIGTMQAAEALKLVIGGGQPLLGRLALLDAWGGGAPAGDSGGKEPGLPSVRGEPEYHRTGHGG$","UBA/ThiF-type NAD/FAD binding protein","Cytoplasm","molybdopterin biosynthesis protein MoeB","UBA/ThiF-type NAD/FAD binding protein","UBA/THIF-type NAD/FAD binding protein","","Jentsch S., Seufert W., Hauser H.P. Genetic analysis of the ubiquitin system. Biochim. Biophys. Acta 1991. 1089(2):127-139. PMID: 1647207Hershko A. The ubiquitin pathway for protein degradation. Trends Biochem. Sci. 1991. 16(7):265-268. PMID: 1656558","","","

InterPro
IPR000594
Domain

UBA/THIF-type NAD/FAD binding fold
PF00899	$\"[56-190]T$	ThiF

InterPro
IPR007901
Domain

MoeZ/MoeB
PF05237	$\"[193-258]T$	MoeZ_MoeB

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[27-257]T$	no description
PTHR10953	$\"[33-252]T$	UBIQUITIN-ACTIVATING ENZYME E1

","BeTs to 20 clades of COG0476COG name: Dinucleotide-utilizing enzymes involved in molybdopterin and thiamine biosynthesis family 2Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0476 is aompkzyq-dr-bcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB007901 (MoeZ/MoeB) with a combined E-value of 1.1e-68. IPB007901A 40-82 IPB007901B 144-188 IPB007901C 218-251***** IPB000011 (Ubiquitin-activating enzyme) with a combined E-value of 5.7e-12. IPB000011H 35-68 IPB000011I 95-125 IPB000011J 153-194***** IPB000594 (UBA/THIF-type NAD/FAD binding fold) with a combined E-value of 1e-10. IPB000594 59-81","","","-54% similar to PDB:1ZFN Structural Analysis of Escherichia coli ThiF (E_value = 2.1E_30);-54% similar to PDB:1ZKM Structural Analysis of Escherichia Coli ThiF (E_value = 2.1E_30);-54% similar to PDB:1ZUD Structure of ThiS-ThiF protein complex (E_value = 2.1E_30);-53% similar to PDB:1JW9 Structure of the Native MoeB-MoaD Protein Complex (E_value = 4.3E_28);-53% similar to PDB:1JWA Structure of the ATP-bound MoeB-MoaD Protein Complex (E_value = 4.3E_28);","Residues 56 to 190 (E_value = 1.8e-66) place ANA_1452 in the ThiF family which is described as ThiF family.Residues 193 to 266 (E_value = 1.4e-25) place ANA_1452 in the MoeZ_MoeB family which is described as MoeZ/MoeB domain.","","biosynthesis protein MoeB (MOCS3)","","1","","","Mon Aug 6 16:01:27 2007","","Mon Aug 6 16:01:27 2007","","","Mon Aug 6 16:01:27 2007","Mon Aug 6 16:01:27 2007","Mon Aug 6 16:01:27 2007","","","Mon Aug 6 16:00:42 2007","","","Mon Aug 6 16:00:42 2007","Mon Aug 6 16:00:42 2007","","","Mon Aug 6 16:00:42 2007","Mon Aug 6 16:00:42 2007","","","","","yes","","" "ANA_1453","1559415","1559942","528","4.51","-12.70","17568","GTGGCAAAGAACCCGGCCTGCCCAGTGTGCGGGGAGAACCCGAGTATCACCGCACTGGTCACGGAGGCTGATACCTGCGTGGTTCCCCGGACTCCCGAGGCCGACACACAGCCGCAGGAGCCCGGATCCGGGGGTGAGTCCTGTCAGCAGGTCGGAGGCTCTGAGTCCGGCCCCGCCGCGTCCGCCCAGGCTCAAGGGGCTGGTGAGGCCCTGGGGGCGGGAGTGGGGGTTGTCTCTGCGGCCGAGCTGAGGAGGCTCCTGGAGGGCGATGTGCCGCCGGCGCTGCTGGATGTTCGTGAGGACATCGAGGTGGCGCTCGAGCCGATGGAAGGAGCGCTGCACATTCCGTTGCGTGAGGTGACGGCACACATGGACGAGCTCGACCCGGGCCGGCTGACGGTGGTGGTGTGCGCCGCTGGGGTGCGCTCGGCCCGCGCCATCGAGGCACTGAAGGCTGCGGGCTACCCCGGCCGGCTCCTCAGCCTCGAGGGCGGTATGAAGGCCTGGGCGGCTGGAGCGGCCGACTGA","VAKNPACPVCGENPSITALVTEADTCVVPRTPEADTQPQEPGSGGESCQQVGGSESGPAASAQAQGAGEALGAGVGVVSAAELRRLLEGDVPPALLDVREDIEVALEPMEGALHIPLREVTAHMDELDPGRLTVVVCAAGVRSARAIEALKAAGYPGRLLSLEGGMKAWAAGAAD$","UBA/ThiF-type NAD/FAD binding protein","Cytoplasm","ThiF family protein","UBA/ThiF-type NAD/FAD binding protein","Rhodanese domain protein","","Hofmann K., Bucher P., Kajava A.V. A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. J. Mol. Biol. 1998. 282(1):195-208. PMID: 9733650Gliubich F., Gazerro M., Zanotti G., Delbono S., Bombieri G., Berni R. Active site structural features for chemically modified forms of rhodanese. J. Biol. Chem. 1996. 271(35):21054-21061. PMID: 8702871","","","

InterPro
IPR001763
Domain

Rhodanese-like
SM00450	$\"[79-175]T$	RHOD
PS50206	$\"[89-174]T$	RHODANESE_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.250.10	$\"[73-171]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[34-54]?$	transmembrane_regions

InterPro
IPR000620
Domain

Protein of unknown function DUF6, transmembrane
PF00892	$\"[57-121]T$ $\"[140-260]T$	DUF6

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[19-41]?$ $\"[50-68]?$ $\"[74-92]?$ $\"[104-122]?$ $\"[128-148]?$ $\"[157-177]?$ $\"[187-207]?$ $\"[217-237]?$ $\"[243-263]?$	transmembrane_regions

","BeTs to 13 clades of COG0697COG name: Permeases of the drug/metabolite transporter (DMT) superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],RThe phylogenetic pattern of COG0697 is aompkzyqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 121 (E_value = 0.00015) place ANA_1456 in the DUF6 family which is described as Integral membrane protein DUF6.Residues 140 to 260 (E_value = 3.2e-06) place ANA_1456 in the DUF6 family which is described as Integral membrane protein DUF6.","","membrane protein domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1456.1","1563680","1564081","402","5.09","-3.96","14496","ATGGGGGAGAGCCCGCCAATTGTCAAGTGTGCTGCGGTCGTTCTCCGCGGGAATAGCATGCTGCTTGTCCGCAAGCGTGGTACGACCGACCTCATTTCTCCTGGAGGCAAGCTGGAGAGAGGGGAGTCGCATATCGCCTGCCTCGGCCGCGAGCTTGATGAGGAGCTCGGGGTCTCGTTGGTGTCGGCCACTTACTTCGGTACCTATGAAGATGTCTCCATCTTCGACCGGAGCCGGATGATCACCCTATTCGTCTACATGTGCGATATTGTGGGCGACCCGGTCCCTCGCTCTGAGATCGAGGCCGTAGAATGGGTCCCCGTGACCTGCTCGCCAGGTGATGGGTCAACCTTTCAGAGCAGAGTGATTCCTGATATTGCAAGGATGCGTGGCCAATGCTGA","MGESPPIVKCAAVVLRGNSMLLVRKRGTTDLISPGGKLERGESHIACLGRELDEELGVSLVSATYFGTYEDVSIFDRSRMITLFVYMCDIVGDPVPRSEIEAVEWVPVTCSPGDGSTFQSRVIPDIARMRGQC$","NUDIX hydrolase","Cytoplasm","","","","","Koonin EV.A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses.Nucleic Acids Res. 1993 Oct;21(20):4847.PMID: 8233837","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[31-45]T$ $\"[45-60]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[11-109]T$	no description
PF00293	$\"[6-108]T$	NUDIX
PS00893	$\"[36-57]T$	NUDIX

","BeTs to 19 clades of COG0494COG name: NTP pyrophosphohydrolases (MutT family) including oxidative damage repair enzymesFunctional Class: L,RThe phylogenetic pattern of COG0494 is a-T-YqvCEBRHuj---linxNumber of proteins in this genome belonging to this COG is","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 1.2e-08. IPB000086 31-58","Residues 7-124 are 61% similar to a (HYDROLASE YCFB) protein domain (PD622371) which is seen in Q9FCX1_ERWAM.","","","Residues 6 to 129 (E_value = 4.1e-11) place ANA_1456.1 in the NUDIX family which is described as NUDIX domain.","","","","1","","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:46:17 2007","Wed Aug 15 13:46:17 2007","Wed Aug 15 13:46:17 2007","Wed Aug 15 13:44:24 2007","","Mon Aug 20 18:18:24 2007","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:44:24 2007","Mon Aug 20 18:18:24 2007","Wed Aug 15 13:44:24 2007","Mon Aug 20 18:18:24 2007","Wed Aug 15 13:44:24 2007","Wed Aug 15 13:44:24 2007","Mon Aug 20 18:18:24 2007","","Wed Aug 15 13:44:24 2007","","Wed Aug 15 13:44:24 2007","yes","","" "ANA_1457","1564075","1565169","1095","5.61","-7.48","38258","ATGCTGAACAGCCCGGTGGGCGTGGTGACAGACCTGGACGGGACCGTCGTCTTCGGCGGAGTCGCCGATCCCCGACTGGCCCCCTTTCTCAGGCGGGCCGCGGGACGTGAGGACATATCGGTCATCGTGGCGACCTCACGTGCGCCCCGAGGAATGGCCGAGGTACTGGGAGATGCCGTGACCTGCCTGGAAGGCTCGGTCTGCCTCAACGGGGCTCTCTTGCGCCTAGGAGACAAGGAGAGGCGCTACCCCATGAGGGCGGATCACGTCCGCGCCGTCGTGGACGCCGCCTTCCGCGCGGGCATGCCTCTCTACGTGGACCAGGGCAGCTCTTTCACTGCACTGGCGGGCCATGACCCCGCCGCAGATCCGTGGTCGGGGGAAGTGTCTGAAGCGGTCTCAGATTTCGCTGAGTCCCCAGAGACAGGGGTGAAGAAGAAGTCCCGGCGAAGGGACAGCCAAGATTCCGGGACGGCACAGGGCCTCTGGGACGGCCTGGAGCACATGCGGGACTACCCGGATGGCACATGGTGCACCGACCCGGCGCAGGTACCGACTGAGGATGTGCTCAAGGTGACGGTCGTCAGCAAAAGGTGCCGGGGCCGTGCGGGGCAGGACAGCATCAGGCAGAGCATTACTGATCCGCTACAAGGAACGGCTGGTCCGGGTACGAGGGCTGCCGACTCGCAGGAGACGGGCGGCCCGGAGCCCGCGAGCACTCTCCAGGACTTGCTGGGGCTACGCCTCGACGGCGTCGTCGCCTACCCGCACGAGGACGGCGTGGTCGATATCTGCGCGGCAGGGGTGGACAAGAGCGTCTGCATGAGGCTGCCGGCCGCCTCGGGAGGTGCGGGTACCGTGGGAGGGACAGCCATCATGGGGCAGTCACCGGCCCTTCGCCATCGCCCCGTCTCCACGTGGGTCGCGGTAGGCAACGACGCCAACGACGTGGAGATGATCCGCGCGGCAGACATCGGTGTCATTGTCGGGGACGGGCTGAAAGAGGTCAGAGCAAGGAGGCAGACGGTCCGCGTCCCCTCACGCCCTGGCGCGGTGGTGTCCATTCTGGAGCAGCTGCTTGAGCTGCACCACTGA","MLNSPVGVVTDLDGTVVFGGVADPRLAPFLRRAAGREDISVIVATSRAPRGMAEVLGDAVTCLEGSVCLNGALLRLGDKERRYPMRADHVRAVVDAAFRAGMPLYVDQGSSFTALAGHDPAADPWSGEVSEAVSDFAESPETGVKKKSRRRDSQDSGTAQGLWDGLEHMRDYPDGTWCTDPAQVPTEDVLKVTVVSKRCRGRAGQDSIRQSITDPLQGTAGPGTRAADSQETGGPEPASTLQDLLGLRLDGVVAYPHEDGVVDICAAGVDKSVCMRLPAASGGAGTVGGTAIMGQSPALRHRPVSTWVAVGNDANDVEMIRAADIGVIVGDGLKEVRARRQTVRVPSRPGAVVSILEQLLELHH$","HAD superfamily hydrolase, type 3","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","Haloacid dehalogenase domain protein hydrolase, type 3","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317","","","

InterPro
IPR013200
Domain

HAD superfamily hydrolase-like, type 3
PF08282	$\"[8-356]T$	Hydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[8-360]T$	no description

","BeTs to 7 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0561 is aompkzy-vdrlbce-gh-n-j-itwNumber of proteins in this genome belonging to this COG is 6","***** IPB000150 (Cof protein) with a combined E-value of 2e-09. IPB000150A 8-17 IPB000150B 38-47 IPB000150E 301-332","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 356 (E_value = 0.00036) place ANA_1457 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1458","1566759","1565644","1116","11.06","13.36","37835","GTGAAGCGGGTTCGGGACGTGGCCGGTAGCTCGGAGTCGGAGACCGAAGGGCCCCGCCTCGGGGCCCCGGCCTCTCAGCTGCGATGCCCCGTTGGACGTCGCAGGGCCTTCCTCGTCCACCGGCGGGCCGCTGTGGTGACGATGCTGGCGCTTGCTGCGGCGCTGGCCGTGGTGGCTGTCTCGGTGCTGTTCGGTGCCTATAACATCTCCGGGACCGACGCGCTGCACACACTGCTGACGGGCTCTGGAAGCAGGATGGATCGCTTCTTCGTGCTCAACCAGCGGCTTCCGCGTGCGGTCGCGGCGGTGCTGGTGGGGGCGATGCTGGCGCTGTCGGGTGCGGTCTTCCAGAGCCTGTCACGAAATCCCCTGGGCAGCCCCGACATTGTGGGGTTCACAACTGGAGCCTCCAGTGGTGGGTTGTTCATGCTTCTGCTGGTGGCGTCGGCGAGTGATCTCCAGGTCTCGGTGGGGGCGGTCCTCGGAGGCTTTGCGACCGCGGCGGTGGTTGCTCTTGTGTCGCGGCGCGGTGGCGTGGGCGGCGACAACCTGATCCTGACCGGGGTCGCCATCTCCGAGATGCTCTCGGCGGCCAACAGCTACCTCATCTCCCAAGCCAGTCTGCCTAGTGCCGAGACGGCCAAGGCCTGGCAGTACGGTTCCTTCAACGCGATTTCCTGGGGGCAGGTCAAGCCCCTGGCTCTGGCAGCCGCGGTGCTGCTGATTCAGGTGGTGTGGCTCGTGCGGCCTGCGAGTCTGCTGGAGATGGGCGACGACGCCGCAACCGGCCTGGGACTGCGGGTTCGCACAGTGCGCGGCGCGATGCTCGGCTACGGCGTCATGCTGGCGGCGATCTGCGTGGCAACGGCTGGACCGATCGGTTTCATCGCCCTGGCCGCACCGCAGCTGGCGCGCCGGCTGAGCAGATCGGCTGGGATGACGATGATCGCCTCGGCGGCCATGGGGGCGCTCTTGCTGGGAGGGGCTGATTTTCTGGCGCAACGGCTGCTTAGCCCCTTCCAGATCCCGGTGGGTCTGGTCAGTGCGGCGCTGGGCGGGCTCTACCTCGTCTGGCTGCTCATGGCTCCCCTGGGGCGTGCGGAGCGGGCCGGCTGA","VKRVRDVAGSSESETEGPRLGAPASQLRCPVGRRRAFLVHRRAAVVTMLALAAALAVVAVSVLFGAYNISGTDALHTLLTGSGSRMDRFFVLNQRLPRAVAAVLVGAMLALSGAVFQSLSRNPLGSPDIVGFTTGASSGGLFMLLLVASASDLQVSVGAVLGGFATAAVVALVSRRGGVGGDNLILTGVAISEMLSAANSYLISQASLPSAETAKAWQYGSFNAISWGQVKPLALAAAVLLIQVVWLVRPASLLEMGDDAATGLGLRVRTVRGAMLGYGVMLAAICVATAGPIGFIALAAPQLARRLSRSAGMTMIASAAMGALLLGGADFLAQRLLSPFQIPVGLVSAALGGLYLVWLLMAPLGRAERAG$","ABC-type cobalamin/Fe3+-siderophores transport system, permease component","Membrane, Extracellular","ABC-type transporter, permease components","K02015 iron complex transport system permease protein","transport system permease protein","","","","","

InterPro
IPR000522
Family

Bacterial transport system permease protein
PF01032	$\"[53-362]T$	FecCD

noIPR
unintegrated

unintegrated
signalp	$\"[1-59]?$	signal-peptide
tmhmm	$\"[43-65]?$ $\"[99-119]?$ $\"[129-149]?$ $\"[155-173]?$ $\"[233-253]?$ $\"[280-300]?$ $\"[310-332]?$ $\"[342-362]?$	transmembrane_regions

","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 7","***** IPB000522 (FecCD transport family) with a combined E-value of 2.7e-45. IPB000522A 95-136 IPB000522B 217-227 IPB000522C 287-305 IPB000522D 339-362","","","-41% similar to PDB:1L7V Bacterial ABC Transporter Involved in B12 Uptake (E_value = 1.8E_16);-42% similar to PDB:2NQ2 An inward-facing conformation of a putative metal-chelate type ABC transporter. (E_value = 1.1E_13);-44% similar to PDB:1KPL Crystal Structure of the ClC Chloride Channel from S. typhimurium (E_value = 1.1E_13);-57% similar to PDB:1NAS SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN (E_value = 1.1E_13);-57% similar to PDB:1OAA MOUSE SEPIAPTERIN REDUCTASE COMPLEXED WITH NADP AND OXALOACETATE (E_value = 1.1E_13);","Residues 53 to 362 (E_value = 1e-79) place ANA_1458 in the FecCD family which is described as FecCD transport family.","","transporter, permease components (III)","","1","","","","","","","","","","","Tue Aug 14 15:21:43 2007","","","","","Tue Aug 14 15:21:43 2007","Tue Aug 14 15:21:43 2007","","","Tue Aug 14 15:21:43 2007","Tue Aug 14 15:21:43 2007","","","","","yes","","" "ANA_1459","1567823","1566756","1068","9.58","4.37","36359","GTGATCGCCCGGTGGTGGGAGCGCCGCCGTGGCTCTGGTGAGGAGTCTGCCGGGACGTCCGCCCCTACGTCAGTGGGGGTCCCGGTGGGTGGGACCGTCCTTGTTCTCGGGGTGCTGTCGGTGCTCCTGTGCCTGGTGAGCCTGGCCGTTGGGTCGCACAGTCTGACGCTGGAGGAAGTGGCCGGTGCCTTCGTGCCGGGGAGGACAACAGTCGCCTCGGTCATTGTCTGGCAGCTGCGGATGCCGCGGACCGTCCTGGCGGTCATGGTGGGAGCCTCGCTGGCCGTGGCGGGGGTCGTCATGCAGGGGCTGACCCGCAATCCCCTGGCCGAGCCGGGCATTCTCGGCATCAATGCCGGAGCGTCGCTGTCGGTGGTCCTGTCGATGTCTCTGTTGGGGCTGACAGATGTGAGTGACTTCCTCTGGTTCGCCTTCGCGGGGGCCGCCCTGGCCGCCTTCCTCGTCCATCTCATGTCGGTGCGCAGTGCCGACGCCGGCCCCGCCAGACTCGTGCTGGCCGGGGTGGCCCTGGGGGCGAGTCTGCGGTCGATCACCGGGACCATCACGATGTATGACTCCGTCACCTTCGACTCCTATCGTTTCTGGGTTCTGGGATCGTTGGCGGACCGGGATGCGGTGCTGCTGGTGTGGGTGGCGCCCTTCCTCGTCGTCGGGCTGGTGCTGGCTCTGGCCTCGGGGCTCACGCTCAACGCCTTGGTGTTGGGGGAGGAGCAGGCCAAGGCGCTGGGTGTCAGCCCGAGGCGCGCTCGGGCGCTGGCACTGATCTCGATCACTCTGCTGTGTGGGGCGTCGACGGCGGCGGTCGGGCCGATCTCCTTCGTTGGGCTGGTGGTCCCGCAGGTGCTGCGGCTGGCCCTGGGGGCTGACCAGCGCAGGCTGCTGGCGGTCTCCCTCGTCGCCGGACCGGTCCTGCTGCTGGCCGCCGACGTCGTCGGGCGGGTCATCCTGGACTCCGGCGAGATGGAGGCGGGGGTCGTGACCGCATTCATCGGAGGTCCGGTGCTGCTGCTCATGGTCATCCAGCGGATGGGGGTGAAAGGGCGGTGA","VIARWWERRRGSGEESAGTSAPTSVGVPVGGTVLVLGVLSVLLCLVSLAVGSHSLTLEEVAGAFVPGRTTVASVIVWQLRMPRTVLAVMVGASLAVAGVVMQGLTRNPLAEPGILGINAGASLSVVLSMSLLGLTDVSDFLWFAFAGAALAAFLVHLMSVRSADAGPARLVLAGVALGASLRSITGTITMYDSVTFDSYRFWVLGSLADRDAVLLVWVAPFLVVGLVLALASGLTLNALVLGEEQAKALGVSPRRARALALISITLLCGASTAAVGPISFVGLVVPQVLRLALGADQRRLLAVSLVAGPVLLLAADVVGRVILDSGEMEAGVVTAFIGGPVLLLMVIQRMGVKGR$","ABC-type cobalamin/Fe3+-siderophores transport system, permease component","Membrane, Cytoplasm","ABC-type transporter, permease components","K02015 iron complex transport system permease protein","transport system permease protein","","","","","

InterPro
IPR000522
Family

Bacterial transport system permease protein
PF01032	$\"[39-348]T$	FecCD

noIPR
unintegrated

unintegrated
signalp	$\"[1-51]?$	signal-peptide
tmhmm	$\"[25-47]?$ $\"[84-104]?$ $\"[114-134]?$ $\"[140-160]?$ $\"[212-232]?$ $\"[263-285]?$ $\"[300-320]?$ $\"[330-348]?$	transmembrane_regions

","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 7","***** IPB000522 (FecCD transport family) with a combined E-value of 7.1e-48. IPB000522A 80-121 IPB000522C 272-290 IPB000522D 325-348","","","-43% similar to PDB:1L7V Bacterial ABC Transporter Involved in B12 Uptake (E_value = 1.2E_25);-50% similar to PDB:2NQ2 An inward-facing conformation of a putative metal-chelate type ABC transporter. (E_value = 1.2E_12);-43% similar to PDB:1U5H Structure of Citrate Lyase beta subunit from Mycobacterium tuberculosis (E_value = 1.2E_12);-43% similar to PDB:1U5V Structure of CitE complexed with triphosphate group of ATP form Mycobacterium tuberculosis (E_value = 1.2E_12);-43% similar to PDB:1Z6K Citrate lyase beta subunit complexed with oxaloacetate and magnesium from M. tuberculosis (E_value = 1.2E_12);","Residues 39 to 348 (E_value = 5.3e-95) place ANA_1459 in the FecCD family which is described as FecCD transport family.","","transporter, permease components (III)","","1","","","","","","","","","","","Tue Aug 14 15:21:17 2007","","","","","Tue Aug 14 15:21:17 2007","Tue Aug 14 15:21:17 2007","","","Tue Aug 14 15:21:17 2007","Tue Aug 14 15:21:17 2007","","","","","yes","","" "ANA_1460","1567928","1568995","1068","8.92","5.66","37450","ATGACATCCCACTACAGCCGCCGCAGCGCTCTCGTCTTCGCAGGGTTGGCCACCGCCATCCCCGTCCTCGCCGCTTGCTCCGGTAAGAAGACGGACTCCAGCGCCTCCTCGACTGCCAAGGCCAAGCCCACCTCATCGGTGCCCACCGGCATGCCCGAGGGCAAGGGCTCGGGCAAGGCCGACGACGTCTTCCCCCGCAAGGTCGTCCACTTCAAGGGCACCACCGAGATCAAGAAGGCCCCCACCAAGGTCGTCATCCTGTCCACCGGTCAGCTCGACGTCGCCCTGACCCTGGGCATCGTGCCGATCGGCTCGACCAAGGGCGACGGCGCCGCAACGGTCCCGGAGTACCTCAAGAAGGCCTTCCCCAAGCAGGCCGACAAGCTGGGCGCGATCAAGGATGTCGGCTCTCGCAAGTCCCCCAGCGTCGAGGACATCGGCAACCTGTCCCCGGACCTCATCCTCGTCAACCAGGCGGGCAAGGACGATATCGACACCCTCTACAAGTCCCTGTCCGAGGTGGCGCCCACCGTCGTCACCCAGGGCAAGAGCGAGGCGTGGAAGCAGGACTTCCTCCTCGTGGCCGACGCCCTGGGCAAGCCGGAGACCGCCAAGAAGTGGATGGAGACCTACCAGGTCGACGCCGCCAAGGCCGGCGAGGCCATCGACGGCAACCCCACCGTCTCCCTGCTGCGTAAGACCAGCGACAAGCTTCGTCTCTTCGGGGCGGTCTCGCTGGCCGGCTCGGTCCTGTCCGATATGGGCGTCGCACGCCCCAGCACCCAGACCTTCACCGACAACGGCAACAAGGACATCAGCTCCGAGACGCTGGCTGAGGCCGAGGCCGACTGGATCCTCTACGGGGCGCAGAAGACCCCGAAGGACGAGAAGGACAAGGACAAGAACAACACCGAGCTGACCGCCATGCCCCTGTGGGCGGGGCTCAAGGCCGTCAACGACAAGCACGCCGTGCGCGTTGACGACGACGCCTTCTTCCTCAACGCCGGCCCCACCGCGGCACGGCTCGTCATGACCACGGTGGCGGACACGCTGCCGAAGAAGAAGTAG","MTSHYSRRSALVFAGLATAIPVLAACSGKKTDSSASSTAKAKPTSSVPTGMPEGKGSGKADDVFPRKVVHFKGTTEIKKAPTKVVILSTGQLDVALTLGIVPIGSTKGDGAATVPEYLKKAFPKQADKLGAIKDVGSRKSPSVEDIGNLSPDLILVNQAGKDDIDTLYKSLSEVAPTVVTQGKSEAWKQDFLLVADALGKPETAKKWMETYQVDAAKAGEAIDGNPTVSLLRKTSDKLRLFGAVSLAGSVLSDMGVARPSTQTFTDNGNKDISSETLAEAEADWILYGAQKTPKDEKDKDKNNTELTAMPLWAGLKAVNDKHAVRVDDDAFFLNAGPTAARLVMTTVADTLPKKK$","ABC-type cobalamin/Fe3+-siderophores transport system, periplasmic component","Membrane, Periplasm, Extracellular","ABC-type Fe3+-siderophores transport systems,periplasmic components","K02016 iron complex transport system substrate-binding protein","periplasmic binding protein","","Mahe B., Masclaux C., Rauscher L., Enard C., Expert D. Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: characterization of a novel ferrisiderophore permease of the ABC transporter family. Mol. Microbiol. 1995. 18(1):33-43. PMID: 8596459Borths E.L., Locher K.P., Lee A.T., Rees D.C. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proc. Natl. Acad. Sci. U.S.A. 2002. 99(26):16642-16647. PMID: 12475936","","","

InterPro
IPR002491
Family

Periplasmic binding protein
PF01497	$\"[81-330]T$	Peripla_BP_2
PS50983	$\"[83-355]T$	FE_B12_PBP

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1980	$\"[77-180]T$	no description
PS51257	$\"[1-26]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[10-28]?$	transmembrane_regions

","BeTs to 13 clades of COG0614COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, periplasmic componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0614 is aompkz--vdrlbcefgh-nuj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","-42% similar to PDB:2CHU CEUE IN COMPLEX WITH MECAM (E_value = 5.4E_10);","Residues 81 to 330 (E_value = 2.7e-39) place ANA_1460 in the Peripla_BP_2 family which is described as Periplasmic binding protein.","","Fe3+-siderophores transport systems, periplasmic components (III)","","1","","","","","","","","","","","Tue Aug 14 15:20:43 2007","","Tue Aug 14 15:20:43 2007","","","Tue Aug 14 15:20:43 2007","","","","Tue Aug 14 15:20:43 2007","Tue Aug 14 15:20:43 2007","","","","","yes","","" "ANA_1461","1568999","1569865","867","6.65","-1.44","30518","GTGCCCGCTCCGGTCTCATCGCAGGCTCCTTCAGACGCCCAGGTCCCCACTGCGGGCCTGGGCGTCCGGGGCATCCGCCTGGCCTACCACCCCAGCCATCCGGTCATCGAGGACCTGAGCACGGCCATCACCCCGGGCGCGGTGACAATGATCGTGGGCCCCAATGCCTGCGGGAAGTCCACACTGCTGCGCGCCATGAGCCGGGTCCTCTCCCCGGGCTCCGGGCAGGTGGTCCTCGACGGCCGCGACATCGCCACCCTGGCCCCCAAGAAGCTAGCCCGGCGAGTGGGCATGCTGGCCCAGTCCTCCATCGCCCCGCCCGGGATCACCGTCCACGAGCTGGTGGCGCGCGGGCGCTACCCGTATCAGTCGCTCCTGCGTCAGTGGTCGGCCGACGACGACGCGGCCGTCACCGAGGCCATGGAGCGCACCGACGTCGTTGGCCTGGCCAACCGGCACGTGTCCGCACTCTCCGGCGGGCAGCGTCAGCGGGTGTGGGTGGCGATGGCCCTAGCCCAGCGCACCGACATCCTCCTGCTCGACGAGCCGACCACCTACCTAGACCTGGCCCACCAGGTGGACCTCCTCGAGCTGTGCCGGGACCTGAACGCCGAGCTGGGCACCACCATCGTGGCGGTGCTCCACGACCTCAACCAGGCCTGCCGTTACGGGGACGAGGTGATCGCCATGCGCGCCGGCAGCATCCTGGCCCACGGCCGCCCCGAGGAGGTCGTCACCGCTGAGATGGTTGAGGAGGTCTTCGGCCTGAAGGTCCAGGTCATTGCCGACCCACTCACCGGGACCCCGCTGGTTCTGCCTCTTCCACGCAAGACCCGGGACACGGCGTCGGGCAGCAAGGCCGGGTAG","VPAPVSSQAPSDAQVPTAGLGVRGIRLAYHPSHPVIEDLSTAITPGAVTMIVGPNACGKSTLLRAMSRVLSPGSGQVVLDGRDIATLAPKKLARRVGMLAQSSIAPPGITVHELVARGRYPYQSLLRQWSADDDAAVTEAMERTDVVGLANRHVSALSGGQRQRVWVAMALAQRTDILLLDEPTTYLDLAHQVDLLELCRDLNAELGTTIVAVLHDLNQACRYGDEVIAMRAGSILAHGRPEEVVTAEMVEEVFGLKVQVIADPLTGTPLVLPLPRKTRDTASGSKAG$","ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component","Cytoplasm, Membrane","FepC","putative iron-siderophore uptake system ATP-binding component","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[157-199]T$	Q8UK08_AGRT5_Q8UK08;
PF00005	$\"[46-233]T$	ABC_tran
PS50893	$\"[20-257]T$	ABC_TRANSPORTER_2
PS00211	$\"[157-171]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[45-242]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[20-255]T$	no description
PTHR19222	$\"[20-271]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31	$\"[20-271]T$	METAL ABC TRANSPORTER

InterPro
IPR002085
Family

Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695	$\"[11-85]T$ $\"[107-340]T$	ALCOHOL DEHYDROGENASE RELATED

InterPro
IPR002328
Domain

Alcohol dehydrogenase, zinc-containing
PS00059	$\"[58-72]T$	ADH_ZINC

InterPro
IPR006140
Domain

D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PS00065	$\"[168-196]?$	D_2_HYDROXYACID_DH_1

InterPro
IPR013149
Domain

Alcohol dehydrogenase, zinc-binding
PF00107	$\"[164-303]T$	ADH_zinc_N

InterPro
IPR013154
Domain

Alcohol dehydrogenase GroES-like
PF08240	$\"[25-129]T$	ADH_N

noIPR
unintegrated

unintegrated
G3DSA:3.90.180.10	$\"[1-210]T$	no description
PTHR11695:SF38	$\"[11-85]T$ $\"[107-340]T$	ZINC-TYPE ALCOHOL DEHYDROGENASE-RELATED

","BeTs to 16 clades of COG1063COG name: Threonine dehydrogenase and related Zn-dependent dehydrogenasesFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG1063 is ao-pkzy-vdrlb-efghsn-j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB011597 (GroES-related) with a combined E-value of 2.4e-47. IPB011597A 24-51 IPB011597B 54-81 IPB011597D 165-209 IPB011597E 233-265***** IPB002328 (Zinc-containing alcohol dehydrogenase) with a combined E-value of 3.8e-23. IPB002328A 12-43 IPB002328B 54-81 IPB002328C 89-103","","","-41% similar to PDB:1KOL Crystal structure of formaldehyde dehydrogenase (E_value = 1.3E_21);-43% similar to PDB:1Y9A Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate (E_value = 1.6E_19);-44% similar to PDB:1LLU THE TERNARY COMPLEX OF PSEUDOMONAS AERUGINOSA ALCOHOL DEHYDROGENASE WITH ITS COENZYME AND WEAK SUBSTRATE (E_value = 2.7E_19);-41% similar to PDB:1KEV STRUCTURE OF NADP-DEPENDENT ALCOHOL DEHYDROGENASE (E_value = 1.9E_17);-41% similar to PDB:1PED BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM) (E_value = 1.9E_17);","Residues 25 to 129 (E_value = 4.9e-33) place ANA_1462 in the ADH_N family which is described as Alcohol dehydrogenase GroES-like domain.Residues 164 to 303 (E_value = 8.7e-35) place ANA_1462 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase.","","alcohol dehydrogenase (Zn-dependent)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1463","1571218","1571769","552","4.80","-7.58","20094","ATGAAGACCCTCGTTCTCGTCTTCCACCCCGACATGTCCGCCTCGCGCGCCAACCGGCCCCTGGCGGCCAAGGCCGAGACCCTCGGCAACGACGTCACCGTGCGCTACATGTACGACCTCTACCCCGACCAGAAGGTCGACGTCGCCGCCGAGCAGACCGCCCTGGAGGCCGCCGACCGGGTCGTCCTCCAGTTCCCCATGTACTGGTACTCCACCCCCGCCCTGCTCAAGCAATGGCTCGACGACGTGCTCCTCTACGGCTGGGCCTACGGATCGACCGGCAAGGCCCTGGCCGGCAAGGAGCTGCTGGTGGCTGTGAGCACCGGTGGCCCCGGCGACGCCTACAGCCACGAGTCCTCTTACGGCTACACGCTCACCGAGCTGCTGCGGCCCCTCCAGGCGACGGCGAACATGGTCCAGATGACCTATCTCGAGCCCTTTACCACCACGGGGACCCTCACCATCACCGATGAGGCCCTGGCTCAGCGGGCCGAGGACTACGCCGCCACCCTGCAGTCCACGAACCTGCCGGTTCTGGACCTCCGCGGCTGA","MKTLVLVFHPDMSASRANRPLAAKAETLGNDVTVRYMYDLYPDQKVDVAAEQTALEAADRVVLQFPMYWYSTPALLKQWLDDVLLYGWAYGSTGKALAGKELLVAVSTGGPGDAYSHESSYGYTLTELLRPLQATANMVQMTYLEPFTTTGTLTITDEALAQRAEDYAATLQSTNLPVLDLRG$","NAD(P)H oxidoreductase","Periplasm, Extracellular","General stress protein 14 (GSP14)","similar to NAD(P)H oxidoreductase ","NAD(P)H dehydrogenase (quinone)","","Fischl A.S., Kennedy E.P. Isolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli. J. Bacteriol. 1990. 172(9):5445-5449. PMID: 2168383Li R., Bianchet M.A., Talalay P., Amzel L.M. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(19):8846-8850. PMID: 7568029","","","

InterPro
IPR003680
Family

Flavodoxin-like fold
PF02525	$\"[1-172]T$	Flavodoxin_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[2-173]T$	no description

","BeTs to 9 clades of COG2249COG name: Putative NADPH-quinone reductase (modulator of drug activity B)Functional Class: R [General function prediction only]The phylogenetic pattern of COG2249 is ------------b-efgh-nuj---wNumber of proteins in this genome belonging to this COG is 3","***** IPB003680 (NAD(P)H dehydrogenase (quinone)) with a combined E-value of 3.4e-24. IPB003680 54-99","","","-62% similar to PDB:1QRD QUINONE REDUCTASE/FAD/CIBACRON BLUE/DUROQUINONE COMPLEX (E_value = 3.9E_14);-59% similar to PDB:1DXQ CRYSTAL STRUCTURE OF MOUSE NAD[P]H-QUINONE OXIDOREDUCTASE (E_value = 9.7E_13);-56% similar to PDB:1QR2 HUMAN QUINONE REDUCTASE TYPE 2 (E_value = 3.7E_12);-56% similar to PDB:1SG0 Crystal structure analysis of QR2 in complex with resveratrol (E_value = 3.7E_12);-56% similar to PDB:1XI2 Quinone Reductase 2 in Complex with Cancer Prodrug CB1954 (E_value = 3.7E_12);","Residues 1 to 176 (E_value = 1e-48) place ANA_1463 in the Flavodoxin_2 family which is described as Flavodoxin-like fold.","","stress protein 14 (GSP14) (QUINONE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1464","1572346","1571852","495","5.10","-7.11","18496","ATGGTTGAGATCGTTGCGTACCGGCCGGAGCAGCGTCAGGCGCTGCTGGACCTGTCCCTGCGCGCCTGGGCTCCAGTCTTCCCACTCATGGAGCAGGACGTGCCCGCCTTCGTCTACCGCTCCTTCTACCCCGAGGGCTGGCGGCAGCGACAGTTCTCCGATCTCGCCGAGGTCCTCGACGGCGAGCCCGACGGCGTCGACGTCGCCGTCCTCGACGGTCGCCCGGTGGGCTGGGTGTGCACCCGTCTGCATCCCGAGGACAGGATGGGGGAGGTCTATATCGTCGTCGTCGACCCCGACTACCAGCGTCACGGCATTGGCCGTGCCCTCATGAGCCACTCCATGGAGCGGGCCCGGGCCGCCGGGATGGCCATGGTGATGGTGGAGACCGGCGGGGACCTGGGGCACGCCCCGGCCCGCGCCACCTACGAGGGACTCGGCTTCCAGCGCTGGCCGGTGGCGCGCTACTTCAAGGACCTGGCCGACGGCGACTGA","MVEIVAYRPEQRQALLDLSLRAWAPVFPLMEQDVPAFVYRSFYPEGWRQRQFSDLAEVLDGEPDGVDVAVLDGRPVGWVCTRLHPEDRMGEVYIVVVDPDYQRHGIGRALMSHSMERARAAGMAMVMVETGGDLGHAPARATYEGLGFQRWPVARYFKDLADGD$","GCN5-related N-acetyltransferase","Cytoplasm","acetyltransferase, GNAT family family","hypothetical protein","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[67-149]T$	Acetyltransf_1
PS51186	$\"[2-164]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[2-153]T$	no description
PTHR23091	$\"[29-129]T$	N-TERMINAL ACETYLTRANSFERASE
PTHR23091:SF1	$\"[29-129]T$	RIBOSOMAL-PROTEIN-ALANINE ACETYLTRANSFERASE

","BeTs to 8 clades of COG0454COG name: Histone acetyltransferase HPA2 and related acetyltransferasesFunctional Class: K [Information storage and processing--Transcription] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0454 is aompkzyqvdrlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 67 to 149 (E_value = 2.3e-17) place ANA_1464 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","GNAT family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1466","1573762","1572440","1323","5.49","-10.64","47480","ATGCAGCATAATGCCGGTTTTACCAGGGATGACGTCGTCACAGCGGCCCTTGAGATCGGTGTGGACCGGTTCACGATGGGCAAGGTGGCGCGTCGGCTCGGGGTGAGTGCGGCTGATCTGGGACGCACCGTCAGCTCTCGTGACGACCTGCTCGTGGCTTGCCTGGAGCGTGTGTCCGCCGACGCCACACTGCCCCCCACCGGCCTGAGCTGGCAGGACTACCTGCGCCGGCTCTCCGACTCGCTGTGGGACGTGCTCGACGCCCATCCCGGCCTGGACCACACCCTCATCAACCTGGCCTGGGCCTACGTGCCCTTCATGTCGGTGGCCAAGCGCGCCCACAACGCCCTCGTCTCCGGGGGCCTGCGCAGCGAGGACGCCTACCTGGCGCTTAACTACACCCTCTCGACGGTTCTGACCGCCCACCAGCAGGCGGTCGCCATGGCCGAGACCGTCGAGTCCGACCGTCAGCCGGGCCGGAGTGAGCGCGGCATCGACGTCGCCGCCCGCATGTGGGACGAGCGCTTCGGCGACTCGAACGCCGCCCTGGGCATGCGTGGGCCCAATGAGCTGCACAGTGGCGACGACGCCGACCGCGTCCCCTTCCGCCCCAAGGAGTCCTGGCTGGACCGCGGTGCGATGGCCCCCAAGCTGGAGGTCATCATCGGCGGCTTCTCCAGCCTGAGCGACGTCCTGTCCGGCGCCGGGAGCCCCGGCGCCTCACGGGGGCCATCCCCCGCCTCACAGTCCAACGACACCAGGGAGTCCTCCGTGAACACTCTCGTACTCGTCTTCCACCCCAACATCTCCGAGTCCCGGGTCAACAAGGCCCTCGGGGCTGCGGCGGAGTCGCTCGGTGGCAACATCACCGTGCGCTACATGTACGACATCTACCCCGACTTCAACATCGATGTGGCCACCGAGCAGGCGGCTCTGCTGGGCGCCGACCGCATCGTGCTGCAGTACCCCATGTACTGGCTCTCCTGCCCGCCCCTGCTCAAGAAGTGGCTCGACGACGTCCTCACCTTCGGCTGGGCCTACGGCTCGACCGGCACGGCCCTGCACGGCAAGGAGCTGCTCCTGGCCGTCAGCGTCGGCGGCGCCGGCAGCGCCTACGGCCGCGAGGGCGCGCACATCTACACGATCCACGAGTTCCTGCGGCCCATGCAGGGAACCTCGCGAGTCATCGGCACCAAGTACGCGGTGCCCTTCCTGTCGGTGGGCGCCCTGGAGATCACCGATGAGGCCATCGCCCGCCGGGCGCAGGACTACGCCGCGGTCCTCCAGACCCCCGAGCTCCCGCTGCTCGACATCTTCGGCTGA","MQHNAGFTRDDVVTAALEIGVDRFTMGKVARRLGVSAADLGRTVSSRDDLLVACLERVSADATLPPTGLSWQDYLRRLSDSLWDVLDAHPGLDHTLINLAWAYVPFMSVAKRAHNALVSGGLRSEDAYLALNYTLSTVLTAHQQAVAMAETVESDRQPGRSERGIDVAARMWDERFGDSNAALGMRGPNELHSGDDADRVPFRPKESWLDRGAMAPKLEVIIGGFSSLSDVLSGAGSPGASRGPSPASQSNDTRESSVNTLVLVFHPNISESRVNKALGAAAESLGGNITVRYMYDIYPDFNIDVATEQAALLGADRIVLQYPMYWLSCPPLLKKWLDDVLTFGWAYGSTGTALHGKELLLAVSVGGAGSAYGREGAHIYTIHEFLRPMQGTSRVIGTKYAVPFLSVGALEITDEAIARRAQDYAAVLQTPELPLLDIFG$","NAD(P)H oxidoreductase","Cytoplasm","General stress protein 14 (GSP14)","similar to NAD(P)H oxidoreductase ","NAD(P)H dehydrogenase (quinone)","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR003680
Family

Flavodoxin-like fold
PF02525	$\"[258-433]T$	Flavodoxin_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[5-65]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[259-430]T$	no description

","BeTs to 9 clades of COG2249COG name: Putative NADPH-quinone reductase (modulator of drug activity B)Functional Class: R [General function prediction only]The phylogenetic pattern of COG2249 is ------------b-efgh-nuj---wNumber of proteins in this genome belonging to this COG is 3","***** IPB003680 (NAD(P)H dehydrogenase (quinone)) with a combined E-value of 2.6e-22. IPB003680 311-356***** IPB003012 (Tetracycline repressor protein signature) with a combined E-value of 1.7e-06. IPB003012A 20-43 IPB003012B 71-90","","","No significant hits to the PDB database (E-value < E-10).","Residues 258 to 433 (E_value = 7.1e-42) place ANA_1466 in the Flavodoxin_2 family which is described as Flavodoxin-like fold.","","stress protein 14 (GSP14)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1467","1574033","1574926","894","6.09","-3.63","31962","ATGAGCGAGACTCCCCGCCCACAGCGCCCAGTCTTTCCGGAACCGCCCGCGGCGCCCTCACCGGCAGCGGCGCCCCCCGCGCCGACGGCACCCCCGGCCAAGCAGCGGCGCTGGCGCGATGACCTGCACCTGGCGCACACGATCGCCAACAAGGTGGACAGCCTCACCCTGGCCCGTTTCGATGCCGGCAACTTCACCGTGGAGACCAAGTCGGACCTCACGCCGGTCACCGAGGCCGACAAGGAGGCCGAGCGCGTCATCCGCGAACAGCTGGGGCGGGCGCGCGGGCGAGACTCCGTCCTGGGTGAGGAGCTGCCCACCACCGGGCACTCCTCGCGTCAGTGGGTCATCGACCCGATCGACGGGACCAAGAACTTCGTGCGGGGCGTGCCGGTGTGGGCCACGCTCATCGGCCTCATCGAGGATGGCCAGTGCGTCGTCGGGCTGGTCTCGGCCCCCGCGCTGGGGAGGCGCTGGTGGGCCGTGTCCGGCGGCGGGGCCTGGACCGGGCGCTCCCTGAGCTCGGCGCGGCGGCTGTCGGTGTCCGGCGTCGACGACCTCTCCCGGGCCTCGATGTCCTACTCCTCGCTGTCGGGGTGGGCGCAGACCAGGCGGCTGCGCGGGATGCTGGGGCTCATGCAGTCGTGCTGGCGCACCCGCGCCTACGGGGACTTCTGGTCCTACATGCTCGTGGCCGAGGGCGCCGTGGACCTGGCCGCCGAGCCAGAGCTCGAACTCTACGACATGGCGGCGCTCGTGCCCGTGGTCACCGAGGCGGGCGGGCGCTTCACATCCCTGGACGGCGAGCCCGGACCCTTCGGGGGCAATGCCGTGGCCACGAACTCGCTGCTGCACGACGTCGCCCTGCACCACCTGAGCGCCGAGACGGACTGA","MSETPRPQRPVFPEPPAAPSPAAAPPAPTAPPAKQRRWRDDLHLAHTIANKVDSLTLARFDAGNFTVETKSDLTPVTEADKEAERVIREQLGRARGRDSVLGEELPTTGHSSRQWVIDPIDGTKNFVRGVPVWATLIGLIEDGQCVVGLVSAPALGRRWWAVSGGGAWTGRSLSSARRLSVSGVDDLSRASMSYSSLSGWAQTRRLRGMLGLMQSCWRTRAYGDFWSYMLVAEGAVDLAAEPELELYDMAALVPVVTEAGGRFTSLDGEPGPFGGNAVATNSLLHDVALHHLSAETD$","Histidinol-phosphate phosphatase","Periplasm, Membrane","inositol monophosphatase family protein","putative monophosphatase","histidinol-phosphate phosphatase, putative","","Neuwald A.F., York J.D., Majerus P.W. Diverse proteins homologous to inositol monophosphatase. FEBS Lett. 1991. 294(1):16-18. PMID: 1660408York J.D., Ponder J.W., Majerus P.W. Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(11):5149-5153. PMID: 7761465Berridge M.J., Downes C.P., Hanley M.R. Neural and developmental actions of lithium: a unifying hypothesis. Cell 1989. 59(3):411-419. PMID: 2553271","","","

InterPro
IPR000760
Family

Inositol monophosphatase
PD023420	$\"[75-130]T$	Q9K4B1_STRCO_Q9K4B1;
PR00378	$\"[110-129]T$ $\"[226-241]T$ $\"[243-261]T$	INOSPHPHTASE
PTHR20854	$\"[71-297]T$	INOSITOL MONOPHOSPHATASE
PF00459	$\"[37-289]T$	Inositol_P
PS00629	$\"[115-128]T$	IMP_1

InterPro
IPR011809
Family

Histidinol-phosphate phosphatase, putative, inositol monophosphatase
TIGR02067	$\"[41-293]T$	his_9_proposed: histidinol-phosphate phosph

noIPR
unintegrated

unintegrated
G3DSA:3.30.540.10	$\"[36-170]T$	no description
G3DSA:3.40.190.80	$\"[180-292]T$	no description
PTHR20854:SF4	$\"[71-297]T$	MYO INOSITOL MONOPHOSPHATASE

","BeTs to 18 clades of COG0483COG name: Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase familyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0483 is aom-kzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB000146 (Inositol phosphatase/fructose-1,6-bisphosphatase) with a combined E-value of 6.5e-27. IPB000146A 64-106 IPB000146B 111-134 IPB000146D 227-280","","","-47% similar to PDB:2P3N Thermotoga maritima IMPase TM1415 (E_value = 3.6E_17);-47% similar to PDB:2P3V Thermotoga maritima IMPase TM1415 (E_value = 3.6E_17);-40% similar to PDB:1AWB HUMAN MYO-INOSITOL MONOPHOSPHATASE IN COMPLEX WITH D-INOSITOL-1-PHOSPHATE AND CALCIUM (E_value = 7.3E_10);-40% similar to PDB:1IMA STRUCTURAL ANALYSIS OF INOSITOL MONOPHOSPHATASE COMPLEXES WITH SUBSTRATES (E_value = 7.3E_10);-40% similar to PDB:1IMB STRUCTURAL ANALYSIS OF INOSITOL MONOPHOSPHATASE COMPLEXES WITH SUBSTRATES (E_value = 7.3E_10);","Residues 37 to 289 (E_value = 1.7e-65) place ANA_1467 in the Inositol_P family which is described as Inositol monophosphatase family.","","monophosphatase family protein (PAPS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1468","1575192","1576145","954","5.84","-6.17","34501","ATGCTCACCGCTCTGGGAGACTCGGCACGAGAGCGCGGCTGGGTGGTCGTTGATGAGACCGCACGCGAGGGGCTCATGGACCGACTCGCCGCCGAGTTCACTCGCCAGGTGTCGCAGCTCGCCAGCAAGGAGCGCTCACGGTTGACCTCCTTGAGCCTGAGCACACCGCTTGGTGGCGGTAGCGCAACACTCGAGCACGCACCCACCCCTGAGCCCTCCTGGCGGCAGAAGGCGCGAGCACTGACCCAGTGGCTCGCGGAACACGGCACCGGTCTGCTGCTCACGATCGACGAAGTACATGCCATTCCGCGCGAGGAGCTGCGAGCACTGTCCGCAGAGGTACAGCACCTCATTCGCGAGGGGGCTCCTATCGGCCTGCTCATGGCAGGCCTCCCCAAGGCCGTTGAGGAGCTCCTCAATGACGACATCACCACCTTCCTGCGCCGGGCCGAGCGGATCGAGCTCGGCGAGGTGGCCATCGACGACGTCTGTAACGCCTTGAAGTCAACCTTCAACGCGGGCGAGAAAGCGCTGAGCAACGACCTGGCTCAGGAGTGCGCGAATGCGACCGGCGGCTACCCATTCATGATCCAGCTCGTGGGGTATCAGGTGTGGAAACACAGCGGCGATGGCCCAGTGACCCAGCCAGCAGTCGCCGCGGGAACGACCGCCGCCCGCCTGCGCCTCGGCAACCTGGTGCACGCTCCGGCGCTGCGCGACCTGTCCGACGTCGACCGCACGATGCTCGTGTGCATGGCCAAGGACGACGGCCCGTCACAGATCGCTGACATCGCCGAACGCATGGACCGCCCCGTCAACTACGTGTCGGTCTACCGCAACCGGCTGCTCGCCGCCGGAATCATCAAGACTGCCGGCTATGGCAAGGTCGACTTCGCCGCCCCCTATCTGCGCGAGTACCTGCGCGAGCACGCAGCACACCTCGTCATGGAGTGA","MLTALGDSARERGWVVVDETAREGLMDRLAAEFTRQVSQLASKERSRLTSLSLSTPLGGGSATLEHAPTPEPSWRQKARALTQWLAEHGTGLLLTIDEVHAIPREELRALSAEVQHLIREGAPIGLLMAGLPKAVEELLNDDITTFLRRAERIELGEVAIDDVCNALKSTFNAGEKALSNDLAQECANATGGYPFMIQLVGYQVWKHSGDGPVTQPAVAAGTTAARLRLGNLVHAPALRDLSDVDRTMLVCMAKDDGPSQIADIAERMDRPVNYVSVYRNRLLAAGIIKTAGYGKVDFAAPYLREYLREHAAHLVME$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","Walsby A.E., Hayes P.K. Gas vesicle proteins. Biochem. J. 1989. 264(2):313-322. PMID: 2513809Jones J.G., Young D.C., DasSarma S. Structure and organization of the gas vesicle gene cluster on the Halobacterium halobium plasmid pNRC100. Gene 1991. 102(1):117-122. PMID: 1864501","","","

InterPro
IPR000638
Family

Gas vesicle protein GvpA
PS00669	$\"[281-294]?$	GAS_VESICLE_A_2

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-63% similar to PDB:2CXX Crystal structure of a probable GTP-binding protein engB (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1470","1576393","1577229","837","8.96","2.41","29643","TTGAACTGGCTGCACGCCATCCTCCTCGGCATCGTCGAGGGCATCACCGAGTTCCTCCCGGTGTCCTCCACCGGGCACCTCAACATCGTCGAGAAGCTCCTCGGCTACGAGATCAACTCCGCAGGCATGACCGCCTTCACCGCCGTCATCCAGGTCGGTGCGATCATCGCCGCCATCATCTACTTCTGGGCCGACATCGTCCGCATCGTCACCGCCTGGTTCAGGGGACTGAGCAACCAGCAGGCCCGCCAGGACCCCGACTACACGCTCGGCTGGGGCATCATCCTGGGATCGATCCCGGTGGCCGCCGTCGGACTGCTGTTCAAGGACTTCATCGAGGGACCGGTCCGCTCCCTGTGGGTGATCGCCGGCGCCCTCATCATCTGGTCGGGGGCCATGTGGCTGGCCGACCGCCAGCAGAACCTCACCAAGGGCATGAAGGACGTGACCGTCAAGGACGCCCTCATCATCGGTGCGTTCCAGGCCCTGGCCCCGGTGTTCCCCGGTATCTCCCGCTCCGGGGCGACGATCTCCGCCGGCCTGTTCCTCAAGTTCGACCGGGTGACGGCCACGCGCCTGTCCTTCTACATGGGCATCCCGTCCCTGGTCGCAGCCGGACTGCTGGAGGCCGCAACGGAGGCCAGCACCATCAGCAACACCGTGGGCTGGACGCCCACCATTGTCGCGACCGTCGTCTCCGGCGTCGTCGCCTACGCGACCATCGCCTGGCTGCTGCGCTTCGTGTCCTCCAACAAGTTCACGTCCTTCCTCGTCTACCGCGTGCTGCTGGGCCTCATCATCATCGCCCTGGTCTCCGCCGGCACCATCGCCGCCTGA","LNWLHAILLGIVEGITEFLPVSSTGHLNIVEKLLGYEINSAGMTAFTAVIQVGAIIAAIIYFWADIVRIVTAWFRGLSNQQARQDPDYTLGWGIILGSIPVAAVGLLFKDFIEGPVRSLWVIAGALIIWSGAMWLADRQQNLTKGMKDVTVKDALIIGAFQALAPVFPGISRSGATISAGLFLKFDRVTATRLSFYMGIPSLVAAGLLEAATEASTISNTVGWTPTIVATVVSGVVAYATIAWLLRFVSSNKFTSFLVYRVLLGLIIIALVSAGTIAA$","Undecaprenol kinase","Membrane, Cytoplasm, Extracellular","undecaprenol kinase, putative","undecaprenyl-diphosphatase ","putative undecaprenol kinase","","Cain B.D., Norton P.J., Eubanks W., Nick H.S., Allen C.M. Amplification of the bacA gene confers bacitracin resistance to Escherichia coli. J. Bacteriol. 1993. 175(12):3784-3789. PMID: 8389741","","","

InterPro
IPR003824
Family

Bacitracin resistance protein BacA
PF02673	$\"[5-267]T$	BacA
TIGR00753	$\"[6-264]T$	undec_kin_bacA: undecaprenol kinase, putati

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide
tmhmm	$\"[47-67]?$ $\"[88-108]?$ $\"[114-136]?$ $\"[198-218]?$ $\"[224-244]?$ $\"[256-276]?$	transmembrane_regions

","BeTs to 14 clades of COG1968COG name: Uncharacterized ACR, bacitracin resistance proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG1968 is --m----qvdrlbcefg-snuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB003824 (Bacitracin resistance protein BacA) with a combined E-value of 7.1e-71. IPB003824A 8-26 IPB003824B 46-62 IPB003824C 94-112 IPB003824D 158-199 IPB003824E 228-264","","","-59% similar to PDB:1MJ0 SANK E3_5: an artificial Ankyrin repeat protein (E_value = );","Residues 5 to 267 (E_value = 1.4e-103) place ANA_1470 in the BacA family which is described as Bacitracin resistance protein BacA.","","kinase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1471","1577469","1579895","2427","5.61","-22.19","88766","ATGACCGCACGCCACCCATCCGCTTCTCCTACGCCAATTCGCTTCGGAAGTCGTCCGATGATCGCCGCAGGTTTCGTCAAGCGGCAGGGACAGGATGAGCTCTTCGACGCCATCTTCGCTCACTCCGAGCCTCGCACGGTGCTGACGGGGATGCGGGGAAGCGGCAAGACTCAGCTGGCCGCTGCGGTTGCGACCAGGTGCGAGGAGGAGGGCTGGCCCCTTGTCGCCTGGATTCATGCGGCCTCACGTAAGGAGATCCTTGCCGGTCTCTACGAGTTCGCACTGCGGATCGGTATCGACGCGCCGAAGAACATCCCTCTGGAGGTCATTGTTCAGCGCCTCCTGGATCGGCTGCGCTCAGCAGAGGCGGCGGACCGTCTCTTCGTTTTCGACAATGTGGAGAATCCGGACGACCTGAGAGACCTCATTCCCGAGGGTGCTGGAGTTCGGACCCTCGTCACCACCCCGCGTCACTTCGACTGGGACGGCCCGGGGTGGCTGCGGTTGGCGGTGGGCGCCTTCGATCGGGAGCAGTCGATCGCCCTCCTGTGCGAGCACACCGGTGACACTCACCGCGAAGCTGCTGACCGGATCGCGGATGCGCTGGGCGACGTGCCTGTCGCCATTACCCAAGCCGCCGCGACAGCACAACAGGGTGGATACGCCTTATCCGGCTACCTTGACAGGCTGAGTCGTCACCCGCTCGAGTCAAGCATGAGTCGCCTCGAGGGTACCCACTACCCCGACGCCGTCGGCATCGTACTATTCATGGCCTATGAACAGGTCTTGGAGCAGCTCAGATCCAAGCATCCTCAGCAGGAGAGGATCGCCGTATCGCTCCTCGGCGCACTGTCTCTCCTGGCTGCTTCCGGAGTGCCGACTCCCTGGCTCTTGAGGCTCGACGCCGACTCCGACGCGGTACGAGACACCCTGTCTTTCCTGAAGAGTGCCGCTATCTTCCAAGAATCCAGCGACGGCGACAAGACCATTATTCCCTGGCTCCAGGGACACGTGTACCGGGAAACCTACCTGAATGACCAGAAGAAGCTCGGTGAGGCGCGCGAGTGCGCCACGTCAGTTCTCAGCGGGATCGACGTAGATCGCCTAGAGAATGTTGAACAGCGGCGAGACGAGACTCACCGTCTCATCGAGCAGCTACTCTCAGTCACATCACAGGACTATTCTCATTCATTGTTTTCTGAGCCACAGGTGTCTTCAAAGCTCGCCGAGACATTGCACGACGCGACCAGCCTGGGGATGTCGCAGCTAGCCCTTGGCCTCACTGACTCCGTGACCCGGGCCTGCGACGCCTTGGGCCCCCACCACCCCGACACCCTGGCTTCACGCAACAACCTCGCCGGCGCCTACCGGGCGAGCGGCCGGCTCGACAAGGCCATCGCCCTGTACGAGCAGACCCTTGAGGACTCCATCCGCTTCCTGGGCCCCGACCATCCCAGCACCCTGACCTCACGTTTCAACCTCGCCGGCACCTACAGAGCGAGCGGCAGGCTCGACAAAGCCATCACCCTGTACGAACAGGTCTTCAGCGGCCGTAGCCGCGTCTTGGGCCCCGATGACCGCAGTACCCTCACCGCGCGTGACCATTTCGCCGACACCTACTGGGAAGCGGGCCGATTCGACGAGGCCATCGCCCTGAAAAAGCAGATCCTCGCAGACGCCATGCGCATCATGGGTGCCGACAGCTCCGGCGCCTCGGCCGCACGTCTCAACCTCGCCGCTACCTACCGGGATGCGGGCAGGCTCGACGAAGCCATCCCCCTTTACCAGGAGAACCTCGACGATGTCAGCCGCGTCCTGGGCCTCAACCATTCCGAAACGTTGGCATCACGCCACCGCCTCGCCGGCGCCTACCGGGACGCGGGCAGACTGGACGAGGCCATCACCCTGAACCAGGAGAACCTCGAGGAATTCACCCGTCTCGCAGGTCCCGACCACCCACACACCCTCAGCGCACGCAATCAACTCGCCGGCATCTACCGGGAAGCGGGCAGGCTCGACGAAGCCATCTCCCTCTTGGAGCAGAACCTCGACGACGTCACCCGCACCCTGGGCCTCGACCACCCTGAAACCTTGGCCTCACGCCACAGTCTCGCCGGTGCCTACCGGGATACGGGCAGGCTGGATGAGGCAATCGCCCTGTTCGAGCAGAACCTCACCGACTTCATCCGCATTCTGGGTCCCGACCGCCCCGACACCTTCACCTCGCGTAGCACCCTCGCCGGCGCCTACCGGGATGCCGGCAGGCTCGACGAGGCCATCCCCCTGTTCGAGCAGAACCTCGACGACCGCACCCGCACCCTGGGACCTGCTCACCCTGTCACTCTCACCTCGCGCAACAACCTCGCCGGCGCCTATCGCGCCGCTGGAAGAATGGAGGATGCGGAGAAGCTCTTCGGGACGCCGTAA","MTARHPSASPTPIRFGSRPMIAAGFVKRQGQDELFDAIFAHSEPRTVLTGMRGSGKTQLAAAVATRCEEEGWPLVAWIHAASRKEILAGLYEFALRIGIDAPKNIPLEVIVQRLLDRLRSAEAADRLFVFDNVENPDDLRDLIPEGAGVRTLVTTPRHFDWDGPGWLRLAVGAFDREQSIALLCEHTGDTHREAADRIADALGDVPVAITQAAATAQQGGYALSGYLDRLSRHPLESSMSRLEGTHYPDAVGIVLFMAYEQVLEQLRSKHPQQERIAVSLLGALSLLAASGVPTPWLLRLDADSDAVRDTLSFLKSAAIFQESSDGDKTIIPWLQGHVYRETYLNDQKKLGEARECATSVLSGIDVDRLENVEQRRDETHRLIEQLLSVTSQDYSHSLFSEPQVSSKLAETLHDATSLGMSQLALGLTDSVTRACDALGPHHPDTLASRNNLAGAYRASGRLDKAIALYEQTLEDSIRFLGPDHPSTLTSRFNLAGTYRASGRLDKAITLYEQVFSGRSRVLGPDDRSTLTARDHFADTYWEAGRFDEAIALKKQILADAMRIMGADSSGASAARLNLAATYRDAGRLDEAIPLYQENLDDVSRVLGLNHSETLASRHRLAGAYRDAGRLDEAITLNQENLEEFTRLAGPDHPHTLSARNQLAGIYREAGRLDEAISLLEQNLDDVTRTLGLDHPETLASRHSLAGAYRDTGRLDEAIALFEQNLTDFIRILGPDRPDTFTSRSTLAGAYRDAGRLDEAIPLFEQNLDDRTRTLGPAHPVTLTSRNNLAGAYRAAGRMEDAEKLFGTP$","TPR-repeat-containing protein","Cytoplasm","putative ATP","putative ATP/GTP binding protein (partial match)","Tetratricopeptide TPR_4","","Lamb J.R., Tugendreich S., Hieter P. Tetratrico peptide repeat interactions: to TPR or not to TPR?. Trends Biochem. Sci. 1995. 20(7):257-259. PMID: 7667876Das A.K., Cohen P.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 1998. 17(5):1192-1199. PMID: 9482716Goebl M., Yanagida M. The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Trends Biochem. Sci. 1991. 16(5):173-177. PMID: 1882418D'andrea L.D., Regan L. TPR proteins: the versatile helix. Trends Biochem. Sci. 2003. 28(12):655-662. PMID: 14659697","","","

InterPro
IPR001440
Repeat

Tetratricopeptide TPR_1
PF00515	$\"[488-514]T$	TPR_1

InterPro
IPR011717
Repeat

Tetratricopeptide TPR_4
PF07721	$\"[446-471]T$ $\"[572-597]T$ $\"[656-681]T$ $\"[698-723]T$	TPR_4

InterPro
IPR011990
Domain

Tetratricopeptide-like helical
G3DSA:1.25.40.10	$\"[418-597]T$ $\"[615-805]T$	no description

InterPro
IPR013026
Domain

Tetratricopeptide region
SM00028	$\"[446-479]T$ $\"[572-605]T$	TPR
PS50293	$\"[446-773]T$	TPR_REGION

noIPR
unintegrated

unintegrated
PTHR19959	$\"[443-804]T$	KINESIN LIGHT CHAIN
PTHR19959:SF21	$\"[443-804]T$	NEPHROCYSTIN 3

","BeTs to 12 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 5","***** IPB002151 (Kinesin light chain) with a combined E-value of 8.7e-10. IPB002151C 691-727 IPB002151D 759-803 IPB002151C 649-685 IPB002151C 733-769 IPB002151C 523-559 IPB002151C 565-601 IPB002151C 607-643 IPB002151C 481-517 IPB002151D 717-761 IPB002151D 549-593 IPB002151D 591-635 IPB002151D 507-551 IPB002151F 522-575 IPB002151F 438-491 IPB002151F 648-701 IPB002151F 480-533","","","-42% similar to PDB:1W3B THE SUPERHELICAL TPR DOMAIN OF O-LINKED GLCNAC TRANSFERASE REVEALS STRUCTURAL SIMILARITIES TO IMPORTIN ALPHA. (E_value = 4.4E_11);","Residues 446 to 471 (E_value = 471) place ANA_1471 in the TPR_4 family which is described as Tetratricopeptide repeat.Residues 446 to 474 (E_value = 0.0068) place ANA_1471 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 572 to 597 (E_value = 0.02) place ANA_1471 in the TPR_4 family which is described as Tetratricopeptide repeat.Residues 572 to 597 (E_value = 0.0029) place ANA_1471 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 656 to 681 (E_value = 681) place ANA_1471 in the TPR_4 family which is described as Tetratricopeptide repeat.Residues 698 to 723 (E_value = 0.018) place ANA_1471 in the TPR_4 family which is described as Tetratricopeptide repeat.","","ATP ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1472","1580160","1582931","2772","5.22","-43.49","101983","GTGGATGACGCCAGCGAAAGGTATGAACTGGCCGGAGTCGCCCAATCCGCCCTGGCTGGAGCCATCACCGAGATGGAGGTGGCACTCAGGGATCTCAGCGGGGACGACGCCGCAGTCCTGGAGGCGGTGCGGTTCCCGGATCACTTCGAGAGGTACCTCCGACGGCGTGCGGCGGGTCGCCGCCAGAACGTCGAGGCGGCAGCTGAGTCCTTCTTCGATGACCTGACCCGCATCGTCGCCGACGAGTTCACCTATCGAGCACCGGGTTCACGGGCCTTCGACATCGCCGCATTCAAGCAGCTACTCGCAGTCCATGAGCAACTAGTTGCCGGGCAGGAGCAACTGCTGGAGGGGCAGGCAGAGACTCACGAACTGCTGGGGACGATGGCGACGGACATTAAGGAGATCCATAGCGCGATCCCGCAGAGCCAACTTGCCTCACCCACGCGGATTCGCTTCGGTAGCCGCCCCAGGGTCGCCGCAGGCTTCGTCAAGCGAGAAGGGCAGGATGAGCTCTTCGATGCCATCTTCACTCACGCCGAGCCTCGTACGGTGCTGACGGGGATGCGAGGATGCGGCAAGACTCAACTGGCCGCTGCGGTTGCGACCAGGTGCGAGGAGGAATGGCTCCTAGTCGCCTGGATCAACGCGGCCACACGTAAGGAGCTTATTGCCGACCTCTACGAAATCGCACTGCGCATCGGTATCGATGCACCGAAGGATGTCCCTCCGGAGACTATTATTCGGCGATTCCTGGATCAGCTGCGCTCAACGGATGAGACCAACCGCCTCTTCGTCTTCGACAACGTGGAGAACCCCGACGACCTGAGAGACCTCATCCCCGAGGGCAGCGGAGTCCGGGTCATCATCACTACCACGCGCCACCTTGACTGGAATAGTTTTGGATGGTTACCGATAACGGTCGGCGTCTTCGATCGCAAACAGTCGATTACTCTCCTCTGCGAGCGCACCGGCGACACCAACAGTGACGCAGCCGACCAAATCGCTGACGCGCTTGGTGATCTCCCGGTCGCAGTTGCCCAAGCGGCCGCAACAGCTAAGTCAGGGCGATACTCTCTGTCTATCTATCTTGAGAGGCTGAGCAATCACTCACTCGAGGCAAGCATCAGCCGCCTCGAGGGCGATGACTACCCAGACGCCGTCGGTGTTGCACTGTTCATGGCGTACGAGCAGTTCTTAGATCAACTCAGAAAGGAACACCCTCAGCAGGAAAAGATCGCTATATCGCTCCTTGACACACTGTCCCTCCTGGCCACTTCCGGAGTACCGACTCACTGGCTCCTCAAGCTCCACGATGACTCCGACGCAGTCCGAGACACCCTGTCTTTTCTGAAGAGATCGTCCATTATTCAGGAATCCGCGGACGGCGACAAGACCATCATTCACCGCCTCCAGGGGCAAGTTTACCGCGAAACCTACTTAAGCGACCGCAAGAAAATTATCGAGGCGAGCACACATGCCATATCAACCCTCAACAGAGTCAACATCAAACAGGTGATTGGTTTTGAACAGAAAAGCCAGGAAATACGAAATCTCGTCGAACAAATACGCTCAATCACTTCACAAGAACACTCTCGCCCATTACTATCTGACCCAAACTTCACTTTAGGGATCGCAACAACACTATTCTATGCAGCTATTCTTGGAATGCCTCAGTTGGCACTTGCCCTCGCTGAGTCTGCCGCCCTGGCAGCCGATACCTTGGGCCCCGATCATCCTTACGCCCTGGGATCACGTAACAACCTCGCTAACGCTTACCAGGACGTAGGCAGGCTCGACGAGGCCATCACCTTGCACAAGCAGACCCTCGACGCTCGCACCCACACCCTGGGACCCAACCACCCCGACACCCTGGGATCAGGCGATAATCTCGCCTGCGCTTACCGGGAAGCAGGCAGGCTCGACGAGGCCATCACCTTGCACAAGCAGACCCTCGACGCTCGCACCCACATCCTCGGCCCCAACCACCCCGACACCCTGGACTCACGCCACAACCTCGCCGTCGCCTACCGGGATGCGGGCAGACTCGACCAAGCCATTGAGTTGCACCAGCAAACCCTCAAAGACACCGAAGGCCTCCTGGGACCCAACCACCCCGACACCCTGACCTCGCGCAACAACCTCGCCGTTGCCTACCGGGATGCGGGCAAACTCGACCAAGCCATCACCCTGTTCAAGCAGACCCTCGACGCTCGCACCCACATCCTCGGCCCCGACCACCCCGGCACTTTGGGCTCGCGCAACAACCTCGCCAACGTCTACCGGGATGCGGGCAAACTCGACCAAGCCATTGAGTTGCACCAGCAAACCCTCGAAGATACCGAAGTCCTCCTGGGCCCCGACCACCCCGACACCCTGACCTCGTCCAACAACCTCGCCGTCACCTACCGGGATGCGGGCAGACTCGACGAAGCCATTGAGTTGCATGAGCAGACCCTCGACGATCGCACCCACATCCTGGGCCCCGACCACCCCGACACTTTGGGCTCGCGCAACAACCTCGCCTACGCCTACCAGGATGCAGGCAGACTCCACGAGGCCATCACTCTGTACGAGCAGACCCTCGAGGACCGCACCCGCATCCTGGGACCCCACCACCCCCACACCCTCGCCTCGCGCAACAACCTCGCCAGCGCCTATCGCGCCGCAGGTCGAGTTGAAGAGGCGGAGAAGCTCTTCGAGACACCGTCGGACTCAGAGGATGAGCAGGATGGCACCGAGGACGACCCGGACCAGGAAGCCGGTCACTGA","VDDASERYELAGVAQSALAGAITEMEVALRDLSGDDAAVLEAVRFPDHFERYLRRRAAGRRQNVEAAAESFFDDLTRIVADEFTYRAPGSRAFDIAAFKQLLAVHEQLVAGQEQLLEGQAETHELLGTMATDIKEIHSAIPQSQLASPTRIRFGSRPRVAAGFVKREGQDELFDAIFTHAEPRTVLTGMRGCGKTQLAAAVATRCEEEWLLVAWINAATRKELIADLYEIALRIGIDAPKDVPPETIIRRFLDQLRSTDETNRLFVFDNVENPDDLRDLIPEGSGVRVIITTTRHLDWNSFGWLPITVGVFDRKQSITLLCERTGDTNSDAADQIADALGDLPVAVAQAAATAKSGRYSLSIYLERLSNHSLEASISRLEGDDYPDAVGVALFMAYEQFLDQLRKEHPQQEKIAISLLDTLSLLATSGVPTHWLLKLHDDSDAVRDTLSFLKRSSIIQESADGDKTIIHRLQGQVYRETYLSDRKKIIEASTHAISTLNRVNIKQVIGFEQKSQEIRNLVEQIRSITSQEHSRPLLSDPNFTLGIATTLFYAAILGMPQLALALAESAALAADTLGPDHPYALGSRNNLANAYQDVGRLDEAITLHKQTLDARTHTLGPNHPDTLGSGDNLACAYREAGRLDEAITLHKQTLDARTHILGPNHPDTLDSRHNLAVAYRDAGRLDQAIELHQQTLKDTEGLLGPNHPDTLTSRNNLAVAYRDAGKLDQAITLFKQTLDARTHILGPDHPGTLGSRNNLANVYRDAGKLDQAIELHQQTLEDTEVLLGPDHPDTLTSSNNLAVTYRDAGRLDEAIELHEQTLDDRTHILGPDHPDTLGSRNNLAYAYQDAGRLHEAITLYEQTLEDRTRILGPHHPHTLASRNNLASAYRAAGRVEEAEKLFETPSDSEDEQDGTEDDPDQEAGH$","TPR-repeat-containing protein","Cytoplasm","putative ATP","hypothetical protein","TPR repeat-containing protein","","Poland B.W., Silva M.M., Serra M.A., Cho Y., Kim K.H., Harris E.M., Honzatko R.B. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 1993. 268(34):25334-25342. PMID: 8244965Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 2000. 296(2):569-577. PMID: 10669609","","","

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[335-468]T$	no description

InterPro
IPR001440
Repeat

Tetratricopeptide TPR_1
PF00515	$\"[587-611]T$ $\"[667-705]T$ $\"[709-742]T$ $\"[755-779]T$ $\"[797-821]T$	TPR_1

InterPro
IPR002151
Family

Kinesin light chain
PR00381	$\"[660-679]T$ $\"[682-700]T$ $\"[747-764]T$ $\"[791-811]T$ $\"[826-847]T$	KINESINLIGHT

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[180-330]T$	AAA

InterPro
IPR011717
Repeat

Tetratricopeptide TPR_4
PF07721	$\"[835-860]T$ $\"[877-902]T$	TPR_4

InterPro
IPR011990
Domain

Tetratricopeptide-like helical
G3DSA:1.25.40.10	$\"[554-695]T$ $\"[705-901]T$	no description

InterPro
IPR013026
Domain

Tetratricopeptide region
SM00028	$\"[583-616]T$ $\"[667-700]T$ $\"[709-742]T$ $\"[751-784]T$ $\"[793-825]T$ $\"[835-868]T$	TPR
PS50293	$\"[583-910]T$	TPR_REGION

noIPR
unintegrated

unintegrated
PTHR19959	$\"[580-884]T$	KINESIN LIGHT CHAIN
PTHR19959:SF21	$\"[580-884]T$	NEPHROCYSTIN 3

","BeTs to 12 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 5","***** IPB002151 (Kinesin light chain) with a combined E-value of 1.3e-10. IPB002151C 786-822 IPB002151D 854-898 IPB002151C 618-654 IPB002151C 744-780 IPB002151C 576-612 IPB002151C 702-738 IPB002151E 648-683 IPB002151E 606-641 IPB002151E 858-893 IPB002151F 827-880 IPB002151F 617-670 IPB002151F 659-712 IPB002151F 785-838","","","-47% similar to PDB:1W3B THE SUPERHELICAL TPR DOMAIN OF O-LINKED GLCNAC TRANSFERASE REVEALS STRUCTURAL SIMILARITIES TO IMPORTIN ALPHA. (E_value = 1.0E_16);","Residues 587 to 611 (E_value = 611) place ANA_1472 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 667 to 705 (E_value = 705) place ANA_1472 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 709 to 742 (E_value = 742) place ANA_1472 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 755 to 779 (E_value = 0.0076) place ANA_1472 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 797 to 821 (E_value = 821) place ANA_1472 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 835 to 860 (E_value = 860) place ANA_1472 in the TPR_4 family which is described as Tetratricopeptide repeat.Residues 839 to 863 (E_value = 0.039) place ANA_1472 in the TPR_1 family which is described as Tetratricopeptide repeat.Residues 877 to 902 (E_value = 902) place ANA_1472 in the TPR_4 family which is described as Tetratricopeptide repeat.Residues 877 to 901 (E_value = 901) place ANA_1472 in the TPR_1 family which is described as Tetratricopeptide repeat.","","ATP ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1474","1582983","1584308","1326","5.71","-11.64","47464","ATGCGGATCCTCCACACCTCCGACTGGCACCTGGGGCGCACCTTCCACGGGCGCGTGCTCGATGACGCGCACGCCGCCTTCGCCGACCACCTCGTCGAGCTCGTCGCCGCCGAGTCGGTCGATGCCGTCCTCGTCGCCGGGGACGTCTACGACCGCGCCATCCCACCCAACGACGCCGTCGCCCTCCTCGATGAGACGCTGCGCCGCCTGACCGAGCGCACCCGGGTGGTCCTGACCCCCGGCAACCACGACTCCGCCCGGCGCCTCGGCTTCGCCGCCGACCTCATGCGCGAGGGCCTCATCATCCGAGCCCGCACCGCCGGCCTCGACCGCGGCATCATCCTCCCCGACGCCGACGGCAACGAGGCCGCCATCGTCCACGCCCTGCCCTACCTCGACCCCGACGCCGCACGCGAGATCCTCCCGCCCCTCCTCGCCGAACGCCTCGGCGAGGAGACCCCCGTGAAGCACACGGTGAGAGAGGAGAGCAACGAGGGTGAGGGCACCGCATCTCAATCCGGTGAGCTGGAGCGCCCGCGCCTGCCCCGCTCCCACGAGGCCGTCGTCTCCGCCGCCCTGCGCCTCGTGGCCGCGGACCTGGACCGCCTGCGTACCGGCCGCAGTCAGCGCCTGCCGAGCCTGCTCATGGCCCACGCCTTCGTCGTCGGCGGCGAGGCCTGCGAGTCCGAGCGGGACATTCGCGTCGGCGGCGTCGACTCCGTGCCCTCCGGGGTCTTCACCACCCTGGGCGGCTCACCCCTGGCCGAGCGCAGCGGCGGCCTGGACTACGTGGCCCTCGGCCACCTGCACCGGCCCCAAGAGCTCACCCGGCCCACCGGCCCGCGCCTGGTCTACTCCGGCTCGCCCCTGCCCTTCTCCTTCGACGAGGCCGAAGGCGCCCGCAACAGCGCCACCAAGTCCTCCGTCCTACTGGATCTCAGCGCCGACGGCGTCTCCGGGCTGGAGCGAATCCCCACCCCGGTCTTGCACCAGGTGCGCACACTGACCGGCACCATGCCCGAGCTCCTCTCCCCCGCCTTCGACGACGTCACCGGCGCCTGGGTGCGCGTCATCCTCCAGGGCGAGCGGCCACCCGGCGCCCTGGCCACCCTCAAGGAGCGCTTCGGCAGCCTCCTGGCCTTCCAGCACGAGGCCCCCACGCGCACTGCCCGCGAGCGCATCACCGTCACCGCCGCAGCAGACCCGCTGCGCATCACGGAGGACTTCTTCGACGACGTCTGCGGGCGCGCCCCCGGCCCCTCCGAGCGCGGCGTCCTGCGCAGTGCGTACGAGTCCGCCCTGGCGAGCGCGAGGAGCGAGCGATGA","MRILHTSDWHLGRTFHGRVLDDAHAAFADHLVELVAAESVDAVLVAGDVYDRAIPPNDAVALLDETLRRLTERTRVVLTPGNHDSARRLGFAADLMREGLIIRARTAGLDRGIILPDADGNEAAIVHALPYLDPDAAREILPPLLAERLGEETPVKHTVREESNEGEGTASQSGELERPRLPRSHEAVVSAALRLVAADLDRLRTGRSQRLPSLLMAHAFVVGGEACESERDIRVGGVDSVPSGVFTTLGGSPLAERSGGLDYVALGHLHRPQELTRPTGPRLVYSGSPLPFSFDEAEGARNSATKSSVLLDLSADGVSGLERIPTPVLHQVRTLTGTMPELLSPAFDDVTGAWVRVILQGERPPGALATLKERFGSLLAFQHEAPTRTARERITVTAAADPLRITEDFFDDVCGRAPGPSERGVLRSAYESALASARSER$","Exonuclease, SbcD","Cytoplasm, Extracellular","ATP-dependent double stranded DNA exonuclease","putative exonuclease","nuclease SbcCD, D subunit","","Stone S.R., Hofsteenge J., Hemmings B.A. Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A. Biochemistry 1987. 26(23):7215-7220. PMID: 2827745MacKintosh R.W., Haycox G., Hardie D.G., Cohen P.T. Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A. FEBS Lett. 1990. 276(1):156-160. PMID: 2176161","","","

InterPro
IPR004593
Family

Exonuclease SbcD
PIRSF000975	$\"[1-440]T$	Exonuclease, SbcD type
TIGR00619	$\"[1-302]T$	sbcd: nuclease SbcCD, D subunit

InterPro
IPR004843
Domain

Metallophosphoesterase
PF00149	$\"[1-272]T$	Metallophos

noIPR
unintegrated

unintegrated
G3DSA:3.60.21.10	$\"[1-363]T$	no description

","BeTs to 13 clades of COG0420COG name: DNA repair exonucleaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0420 is aompkzyqvdrlbcefg-------t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 272 (E_value = 3.1e-21) place ANA_1474 in the Metallophos family which is described as Calcineurin-like phosphoesterase.","","double stranded DNA exonuclease (sbcD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1476","1584305","1587577","3273","5.19","-40.35","115690","ATGAGGATCCACTCCCTGACCATGACCGGCATCGGCCCCTACGCGGGGCGGGAGCACATCGACTTCGACGCCGTGGGCGCCTCGGGCCGCTTCCTGCTCACCGGCCCCACCGGCTCGGGCAAGACCACCATCATCGACGCGATCGTCTTCGCCCTCTACGGGGACGTGGCCGACTCGGCCGACTCTTCCAAGGAGCGCATCCGCTCCACCCTCGTGGGCCCGCACACCGAGAGCGTCATCGAGCTCGTCTTCTCCACCGGCGCAGGCGTCTACCGGGTGCGCCGCACCCCCACCTACGAGCGGGCCAAGCGGCGCGGCCAGGGCACCACCACCCAGAACGGCACCGTCAAGCTCTGGCACCTGGCCAAGGTCGGCGGGGAGCCGCTCGACGAGCCCGTCACCCGCGTGGGCGACGCCGACGCGGAGATCGCGCGCGCCGTGGGCTTAAGCCGGGAGCAGTTCACGCAGACAGTCGTCCTGCCGCAGGGCAAGTTTGCCCGGTTCCTGCGCGCCGACTCCTCCGAGCGCCAGCACCTCCTCAAGGACGTCTTCGGCACCGGCATCTACGACGCCATCCAGGACGCCCTCATCCAGGCCTCCCGGGACGGGGCCCGGCGGGTCGAGCAGGCCGCAGCCGACCTGAGCGGCCAGGTCACCTCCCTGGGACGGCACCCCCTCCTCACTGAGGCCCCCGCCCAGGCACCGGCCCAGGCCTTGGAGGCGGCGATGGCGGGTGCCACCCCGGACCTGGTGGCTCTTCGCCGCATCGGCGCTGAGGTTCTGGATGCCTCCAGCAACCGGGTCGCGTTGGCCGAGGCTCGGGCTGAAGCCGCGGGGGCGGCCCTCACCCGGGCCCAGTCGGCGCGCGAGGAGGCCCAGAGCCTCCACGACCTCCTGGAGCGACGCCGGACACTGATCGAGGAGAAGGAGCGGCTGGCTGAGCGCGCCGAGCAGGAGGCCGACGACGCCCGGCGTCTCCAGGACGCCGAACGAGCCTCCCGGGTGCGGCCCTACCTGGTCGCCGAGCAGGCCGCCCGTCGCCGCGCCCAGCAGGCCGTCGCTGCACTGGCCGCCCGTGCCGACCAGAGCGGACTGGCCCACTTGGCCGAACAGGCCGGCGTCACCAGTGCCGGCAGCGTGGAGGAGGCCACCGGCAGCGCGGCTCACAGTCATGGTGCCGCGGTGACGCCCACCGCCCTCGTCGAGCCCCTGGTCCGTGAGGCGCAGCGCCAGCTCGCCGCCCTCGAGGATGAACCCAGCGAGGCGAAGGCCGGCGCTACCGAAGTAGGCACGGCCCCGCAGGACTCGGACGCGGCAGAGACCCCTGTGGCGGCCGATGAATCGGAGTCGGACTACGCCGAGGCACTGAGCCCCCACGACCTCGACGACCTGGCGCACCACTGCCGTCGCGAGCACGGGCAGCTCGAGACCCTGGTGGACCTCGAGGCCGGCCTCCCCGGGCGCAAAAGCGCCTTGCAGCAGCGGGAGGCGGAGCTGCAGCAGGCCGCCGCCCAGCTGGAGCAGCGCGCGGAGAAGCTCGCCGAGCGCCCCGCGCAGCGCACCGCCCTGGTGGACACGCTGGAGGCGGCGCGCGCGGCCCACGAGCGCCTCGACGGCCTTCAAGACCGCCGTACCCGGGCCGAGGAACGTCACCGGGCGGCCCTGGCCGTCGAGCAGCTCAGTGCCCAGCTCGCCCAGCGGGACAATGCCTGCGCTCAGGCGGCGACGCTCACGCGGGAGGCGACCGAACAGGTTCGTGCCACCCGTCTGGCCTGGATCTCCGGGACCGCCGGGGCTCTCGCCGGTGAGCTCACCGAGGGCGAGCCCTGCCCCGTGTGCGGCTCGACCACGCACCCCTCCCCCGCCTCCGCGGGCACCGACGGCGCCACCCGCCAGCAGGTCGAGGCCGCTGAGGAGCAGCAGCGGCAGGCCGACGAGGCACTCAGCAGCGCCCTCCGGCAGCGAGACACCTGTGCCACCCGGCTTGAGGAGGCCCAGCGCGCCAGTGACGGCATGGATGCCCCCGCCGCCAAGGAGGCACTGGAGGCGGCCGCCACCGCCCTGGCCACGGCGCGGGCCGCAGCCGACGGCGTCGAGGAGCTGGTGGAGCGCCTCGAGGCCTTCGATGCCGGCACCGAGCAGGAGCGCGCCGCACTCGATGCCGCCCGCACCGCCCAGGAGTCCGCCCGCAGCCGCCTGGAGGCCGAGCGCGAGGCCCTCACCCAGGACCAGCGGCGCTGCCTGGAGGCGCGCGGGACCTGGCCGAGCGTCACCGCCCGCGCCGCCGCGCTCCTCGTGCGGGCCAAGGAGGCCGAGGACGCCTCCCAGGACATCGACACAGCCCGCACCGCCCTGGCCCAGGCCCGCAGCGCCCTGGCGGACCTGGCCTCCGCGCTGAAGGAGGAGGGCTTCACCGGTGCGACCCAGGCAACGGCGGCCCTCATGGAGCGCGGCGCCATCGAGGCCCTGACGGCCAGCGTGCGCGCCGCCGCCACCGCCCGGGAGCGGGTCCACCTGGGCCTGGAGGACCCGCAGATCGCCGCCCTGAGCGGCCAGGAGGAAGACCGCCTCGAGGCCGCCACCGCCGAACTCGCCCAGGCGGACGCCGCCGCCCGGCAGGCCGCCTCCACTCAGGCGCGCGCCGCCGAGTCCCACGAGCACCTGCGCCGGGCCGTCGACGGCGTCGAGCAGGCGGCCACCGCCTATGAGGAGGCGGCCGGCTCCAGCGCCGACCTCATCCGGGTGGCGAACCTCGCCCGCGGGGAGAACGAGACCGGCACGCCCCTGGCCACCTGGGTACTGCAGGCCCGCTTCGAGGAGGTCCTCGTCTTCGCCAACGAACGCCTGTCCCAGATGTCCTCCGGGCGCTACGAGCTCATCCGGGTCGCCGAGGAGACCAGCCAACGCAAGCGCCGCAAAGGACTGGGCCTGGCCGTCGTCGACCACCTCGGAGACGAGCGCACCCGCGACCCCCGGACCCTCTCGGGCGGGGAGACCTTCTACGTCTCCCTGTCACTGGCCCTCGCCCTGGCCGACGTCGTCTCGGCCGAGTCCGGGGGCGTGAGCCTGGAGACCCTCTTCATCGACGAGGGCTTCGGCACCCTGGACGCCGACACCCTCCAGGCGGTCATGGCCCAGATCGACCACCTGCGCGCCGGCGGGCGCACCGTCGGCATCGTCTCCCACGTGGCCGAGCTGCGCGACCAGATCGCCGAGCGCATCGCAGTGCGGCGCGTCGCCTCGGGCGGCTCCACCCTGAAGGTGACCGCCTGA","MRIHSLTMTGIGPYAGREHIDFDAVGASGRFLLTGPTGSGKTTIIDAIVFALYGDVADSADSSKERIRSTLVGPHTESVIELVFSTGAGVYRVRRTPTYERAKRRGQGTTTQNGTVKLWHLAKVGGEPLDEPVTRVGDADAEIARAVGLSREQFTQTVVLPQGKFARFLRADSSERQHLLKDVFGTGIYDAIQDALIQASRDGARRVEQAAADLSGQVTSLGRHPLLTEAPAQAPAQALEAAMAGATPDLVALRRIGAEVLDASSNRVALAEARAEAAGAALTRAQSAREEAQSLHDLLERRRTLIEEKERLAERAEQEADDARRLQDAERASRVRPYLVAEQAARRRAQQAVAALAARADQSGLAHLAEQAGVTSAGSVEEATGSAAHSHGAAVTPTALVEPLVREAQRQLAALEDEPSEAKAGATEVGTAPQDSDAAETPVAADESESDYAEALSPHDLDDLAHHCRREHGQLETLVDLEAGLPGRKSALQQREAELQQAAAQLEQRAEKLAERPAQRTALVDTLEAARAAHERLDGLQDRRTRAEERHRAALAVEQLSAQLAQRDNACAQAATLTREATEQVRATRLAWISGTAGALAGELTEGEPCPVCGSTTHPSPASAGTDGATRQQVEAAEEQQRQADEALSSALRQRDTCATRLEEAQRASDGMDAPAAKEALEAAATALATARAAADGVEELVERLEAFDAGTEQERAALDAARTAQESARSRLEAEREALTQDQRRCLEARGTWPSVTARAAALLVRAKEAEDASQDIDTARTALAQARSALADLASALKEEGFTGATQATAALMERGAIEALTASVRAAATARERVHLGLEDPQIAALSGQEEDRLEAATAELAQADAAARQAASTQARAAESHEHLRRAVDGVEQAATAYEEAAGSSADLIRVANLARGENETGTPLATWVLQARFEEVLVFANERLSQMSSGRYELIRVAEETSQRKRRKGLGLAVVDHLGDERTRDPRTLSGGETFYVSLSLALALADVVSAESGGVSLETLFIDEGFGTLDADTLQAVMAQIDHLRAGGRTVGIVSHVAELRDQIAERIAVRRVASGGSTLKVTA$","Exonuclease, SbcC","Cytoplasm, Extracellular","putative exonuclease","SMC domain protein","ATPase involved in DNA repair-like","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-198]T$ $\"[981-1076]T$	no description

","BeTs to 13 clades of COG0419COG name: ATPase involved in DNA repairFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0419 is aompkz-qvd-lbcefg-------t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","exonuclease (sbcC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1477","1590301","1587644","2658","8.32","3.39","90731","GTGCCGCCTCCGCCGAGTGCCCCCGTACCCGAGGCGTACAGCGCGACCGAGGTCCCTGTGCCCCCGGTCGCCGCAGGCACCGCTCCTGCAGCGCCGGCGCCACAGGCTCAAGGCGGATTCGTGCAGCCCGGGCAGGCCGCTCAGCCTTCGCCCCTGGCGCAGACCTTCACCGCCTGGTTCCGCGGCCCGGGCCTGACCTCCACGGCCCTGAGCCTGGCGATCGTGCTCGGATCCGCAGCCATCAGCGCGATTCTCACGCTGGTGGCCATGTCGACCATGGACTCGACGAAGATGTTCCCGACGACCTTCTCCACGCTGCCGCTGCTCATGGGCTGGAGCCTGGGCGGGCAGTTCGTCATGTCAGGGTCGAACTCTTACGAGACCGTCACCCTGACCTTCACGCTGCTGCCCATGGGGGCGCTGACCGCCGCCGGCATCGGGGTCTTCTGGCTGGCGCGCCGCCGGGCCGCGGTTGACGGGTCGGCAGCCCCGCTGGTCCCGACCCTGGCGCGGGCCGGAGCCGAGGCTCTGGCTGTGGCCCTGGTGGCCTGCTTGGTGACGGCACCGTTCTCCATGACCGCCACGATGATGGGGCTGAAGGTCATGACGGTCTCCTCCTCCGCGCTGATGACGATCCTGTTGGTGACTGTGGTGGTCTTCGTGGCGCTGGTGGTGGCTCGCAGCGGCGGGTCGCTGCTCGAGCGCCTGCCGAGCCCGGTGGTGCAGGTCAGCCGTGAGCTGGGCGCCTTGAGCACCGCACTGGGCGTGGTCCTGGGGATCTTCATCATTGTCGCCTACATCGCTGCGGTACTGATCCAGGGGTCGGGTTTCGCCTCGATTCTTCTGCTGCCGGTGCTCCTGCCGAACCTGGTGCTGCTTGCCCTGGGCATGGGATCCCTGGGAGGTATCACCCTGGACAAGAGTGAGGCCGCAGCGGCCCTGGCCTACTTCCTGCCGTCCTTGGGCGGCAAGGACGGCGGCGACGCCTACGCCTGGACCTGGTTCGGCAGCTGGTCGATCCTGCTGTTCGCGGCCATGATCGTGGCCATCGTGGCGGCGGCGCTGCGCGTGGGCGTCAGGCGTTCCCGCACGGGGCGGACCGAGTGGCAGCGCGTCTGGCAGCTTCCGCTCGTGGCGCTGGCCCTGGGTGCGATCGTCTTCTACGGGCTGCTTCCGTTGCGTTTCTCAGGCGCTGACACCCCGGTGCGTTCCTCGGGCGGTGGATCCGGCCACTACATGTCTGTGAGCCTGCAGCCCAACGCCCTGACCTTCCTCCTGGTTGGGATCGTCGCGGCGATCATCTCGGTGCTGGCGGAGATGCTCCCCCTGTGGGCCTACTCCTCCTTCCCGGCAGTGCTGCAGCTGGCCGGTGGGAAGAAGGCCAGTGCGGCCTGGCGTGCGGGCACCTCCGGCGTGGCTCCGACGTCGTCGGCCCAGCAGTGGGCGTACAGCACCGACCCGGCCACCGGGGCCAGCATTGCCACGGACCCGGCCACCGGTGCCGTCTTCTCCATGGACCCGGCGACCGGCCAGTGGGTGGAGACCACGCCGGCCTCACAGGCCCCGGCTCCCGGCTTCGGCGGTGCGGCTGCAGGCGCGCCTGCTTCGGGCCAGCTGTCCGAGCCCGCCCCGATGAGTGCGGCCTCGCGCAAGAAGGTCATTCTGGGACTGTCCGCTTTCGGAGTCGTGGTGGCACTGGTGGTGGCCGGCGTCGTCGCGCTCAACGTCGTCAACGGCATGCGTGGCCCTGAGAAGGCGGTCGAGAGCTACCTGACGCTCCTGTCGGAGGGGAAGGCCGCTGAGGCCACCAAGATGGTGGACCCCGGTGTCCCCAATGATCAGCGCAAGCTGTTGACCGACGACGCCCTCAAGTCCGCCAAGGCGAGGATCAAGGTCACTAAGATCGAGGAGCCCACCATCTCTGGTGACACCGCCACGATCAAGGCTCACCTGTCCCTGGATGGGAAGGCTTTCAAGTACGACTTCACCGCCTCGAAGACGTCGGGCTCTTTCGGGCTGGACAGCTGGAAGGTGGATAAGCCCCTCGTGGTCTCCGCGGACTTCAGCTCCTCCGCGCTTCCGGGGCTGAAGGTCGCAGGGGTTGCCATCGACATGGCCAAGGATAAAGACGGGTTGAGTGGGTATCGCTCGACCCAGGTCGCCTACCCCGGTGTCTACCCGGTGGCGGCGCCGGACTCTGTCAGCAAGTACCTCACTGCCAAGGAGACGTCCTTCACGCTGATTCCTACGGGTGAGGGTGCGAGCGCGGAGGCGGAGTCGGTGGGCACCCAGACGGTGAATGCCACTCCCACTGACGAGCTCAAGACCAAGGCGTTGGCGAAGGTCAAGGAGCAGACGAAGACCTGCGCGACCGTCCCGACGAACTCGGACAAGCCCTGCCCCTTCCAGCTCACCACGGACATGACCTCGTTGTCGGTGGAGAAGGACGCCACGAAGGTGGAGTTCTCCAAGGACATCAACAATGACCTGTCCTTCACCTCCGACGAGATCAGCATCTCCGGGTCTCCTAAGCCGACGACCTTCGACAAGAACCCCAGCCCCCGCAAGGCGAAGTTCACCTTCTCCGGGAAGGTGGAGCTGCCGGAGGGCGGCGGCGATCCCACCATCACCATCGAGTCCAGCAGCAGCGTCTTCTAG","VPPPPSAPVPEAYSATEVPVPPVAAGTAPAAPAPQAQGGFVQPGQAAQPSPLAQTFTAWFRGPGLTSTALSLAIVLGSAAISAILTLVAMSTMDSTKMFPTTFSTLPLLMGWSLGGQFVMSGSNSYETVTLTFTLLPMGALTAAGIGVFWLARRRAAVDGSAAPLVPTLARAGAEALAVALVACLVTAPFSMTATMMGLKVMTVSSSALMTILLVTVVVFVALVVARSGGSLLERLPSPVVQVSRELGALSTALGVVLGIFIIVAYIAAVLIQGSGFASILLLPVLLPNLVLLALGMGSLGGITLDKSEAAAALAYFLPSLGGKDGGDAYAWTWFGSWSILLFAAMIVAIVAAALRVGVRRSRTGRTEWQRVWQLPLVALALGAIVFYGLLPLRFSGADTPVRSSGGGSGHYMSVSLQPNALTFLLVGIVAAIISVLAEMLPLWAYSSFPAVLQLAGGKKASAAWRAGTSGVAPTSSAQQWAYSTDPATGASIATDPATGAVFSMDPATGQWVETTPASQAPAPGFGGAAAGAPASGQLSEPAPMSAASRKKVILGLSAFGVVVALVVAGVVALNVVNGMRGPEKAVESYLTLLSEGKAAEATKMVDPGVPNDQRKLLTDDALKSAKARIKVTKIEEPTISGDTATIKAHLSLDGKAFKYDFTASKTSGSFGLDSWKVDKPLVVSADFSSSALPGLKVAGVAIDMAKDKDGLSGYRSTQVAYPGVYPVAAPDSVSKYLTAKETSFTLIPTGEGASAEAESVGTQTVNATPTDELKTKALAKVKEQTKTCATVPTNSDKPCPFQLTTDMTSLSVEKDATKVEFSKDINNDLSFTSDEISISGSPKPTTFDKNPSPRKAKFTFSGKVELPEGGGDPTITIESSSSVF$","Membrane protein","Membrane, Periplasm, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Kota J., Ljungdahl P.O. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J. Cell Biol. 2005. 168(1):79-88. PMID: 15623581","","","

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[370-627]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[69-89]?$ $\"[104-124]?$ $\"[130-152]?$ $\"[172-192]?$ $\"[206-226]?$ $\"[247-269]?$ $\"[275-295]?$ $\"[300-318]?$ $\"[337-357]?$ $\"[372-392]?$ $\"[421-441]?$ $\"[553-573]?$	transmembrane_regions

InterPro
IPR001030
Domain

Aconitate hydratase, N-terminal
PS01244	$\"[311-324]?$	ACONITASE_2

noIPR
unintegrated

unintegrated
tmhmm	$\"[394-412]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1481","1593845","1592922","924","4.98","-10.17","31896","ATGCCTGACATCCTCGCGAGTGGGCAGTGGAAGGAGTTCTCGGTGAGCAACCGGGGTGCTCTGGAGATCGGCCTGGTCGCTCCCGTGCCCGCCACCCTGGAGGTTGTGGGGACCTCGAGCGCTCCGAAGTATCTCGGGGCTTCGCGCGATGCCGTCGCGTTTCCCGGAAGAGCGGTGTCGGCTGAGCGGCCCGTCATCGTTCGTGCCAACGTGTCATCCCAGGAGGCCTTCCCCGGCGACTGCGTCGTCGACCTGTCCTTCGACGCCGCCGGGGGAGAGCACGCCTACCTCATCAGGGCAATCCCGGTGGCGGGCCAGGCCAGCGCCCCGCTCCTCCAGCTCACGTTGGAGGATGACGTGATTCGTGTCCGTCCAGGTGAGGGAGGTGTGGCGACGCTCGGGCTGGGGGGCTGGTGCGCCAAGCGCAGGCAGGAGTCCGGGGCGTCCTTGATGCCAACGGTCACAGAGGTCATCCTCGACGCCTCCGCATCCATGGCGCAGCACCGGCCCCGCGTGGAGTCGTTCCTGGACTTTGTTGCCGACTTGTACGCGACTCTGGGCATCCCTGCACCTCACGTGCGTTCCCTCAGCGTCGGTGGCTCAGTCGATGCGTCTTCAAGGGGGATGGGCGGGGTCGGCTCAGTGCAGGTGGACCCCGATGCCCGGGGCAGGCGCATCGTCGTCACTGACATTCCCTTGGAGACGGGACGCTGCGAGTGCCTTGTCCTGGGCAGCCCGGAGATCGTTCGTGCGCTGGCCCCCCACAGCGGGGCGCCCTACTTCGTGCCCAATGGTGATGCGTGGAACGAGCTCTTGCGGGAGGATGCGGCCTTCACCTCGCAGACTCTCGCCACCATGGACCCCCTTCTGGACTGGCTCGCTCAGCCCGCTTCATCTAATGCGTCGATTGGAACGTCATCATGA","MPDILASGQWKEFSVSNRGALEIGLVAPVPATLEVVGTSSAPKYLGASRDAVAFPGRAVSAERPVIVRANVSSQEAFPGDCVVDLSFDAAGGEHAYLIRAIPVAGQASAPLLQLTLEDDVIRVRPGEGGVATLGLGGWCAKRRQESGASLMPTVTEVILDASASMAQHRPRVESFLDFVADLYATLGIPAPHVRSLSVGGSVDASSRGMGGVGSVQVDPDARGRRIVVTDIPLETGRCECLVLGSPEIVRALAPHSGAPYFVPNGDAWNELLREDAAFTSQTLATMDPLLDWLAQPASSNASIGTSS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1482","1596635","1593876","2760","5.49","-22.39","100414","ATGTCGGGATGCGAGCAGCTTCTCTACACCAATGTCGACCATGTCGTTGACGGGGTAGAACGCTCGGGGTGGCAGACGATGACGCAGACTGCCGGCCTGAGTGACGGTGATGCAAGCACGCTCTACGCGTTGATCGACCCCACCCTCAACCCCGTCACGCCCCTGTCCGGATTCCCCACGGAACAGGAGGTGGCGGCAGCTGATCGACGCCTGGCACAGTTCTGGACGGACGAGGGCCTGGTACTCGTCCACACCGCTCCGGCGGGGAACGACACAACGGGACGGCCCAACACCATGACCCATGTGGTGCTTGCCAAGCACCACGAACCGGCGCCCGACCTACGAACCATTGACCTGTGGCGATCACCCGGCTGGGTGACTCCCTTCGGGCCCGAGCAGGTGAGGCAGGCGGAGCTTCCCGACCCGGCGTCGCTGCGACCCGGCGCCAGCGTCGACGACGACACGGTGGCCGAGTTCCTGGCCGACGGCTCGCGGAGCCCGGCCCTGGTTGCCATGGCCGACGCTCTCGAGCCGGGGCTGCTCCAGACGATCCGCGCCCAATGGGATGGCGTGCCGTCTGACCAGGCACGCAGGAGGAACACTGTGGTCCTCGCAGTGTCCTCGACCGATGAAGCCGCCCTGTGGATCGGAGCGCTGCTGCGCACCTGCGCCCCGGCCACCGGACGGTACCTGAGCTACTCCGTCCTCCAAAGGATCCTGACGCCCTCGGACGTCGAGATGCTCCTACAGTCTCGTATCGACGTGGCCTGCGTTCCGAGACAGGACCTGACGAACATGGGGGAGTCTCGACCGGGCCTGGTCGTCATCGACCCCCACGAGAGCGGCGCTGTCGAGCCGGCGCCGACGACGTCGTGGGGACGCCTGGTGGCGTTGATGAGTCAGGACCTGGGAGCGTGGGTCGCCGCCTACGAAGGAATGAAGGACGTCCTCAGCCTCCTGCCCGATCATTCCGATCTCAGCCCGGGGTGGCCGCTGGCCGCGGCCGAGGCCTGCGATCCTGGGCTCCTCGAGCCTCAGCAGGGGGAGACGCCGAGCTCTTCACAGGACGAGGAGGCGCGCGCACAGGATGAGGCGGAGCTCATCGAGGTGGAGCTCGTGTCGTGCTATCCGAGGTCGATGGTCGGTAATGACTACCTCGCAGCGGTGGTGACTGATCGCGTACTCGGCTCAGCGACGCAGAGTCCCGCCGCCTGGTATGCGCGCCTGTCTCGGATTCCCCGGTGGGCACCAGTGAGTGGACTCGTCAGTGGGCTCTGCGAACGCTACCTCGATGCCGCGTGCCGCGAGGTCCGGTGGATGACCGACCTCGAACGCCCCGTCTCCGAGCAGGCCAACCGTTGCCTGCGTCAGTGGAGCGGGATGCCGGAGCATCGGTCCACGGTCGATGCAGCACTCGCGCAGGCCAAAGAGCGTGTCGAGGCCGAGCAGCCGGGCACTGCGGGGGGCCTGCGCGTCTTGGACCGTATGCTCCGAGAGCACGTCAGCGTCTCGACCCGGACATGCGATGTCCTCCTGCAGGGATACGCCGACATGATGCAGCCGGCCGCCTACGGTTCTCGTGAGCAGCGTGAGATTCTTGCTGTGCCTGCGACATCGCTCAGCCGTAGCCTGCTGGCCGACCGGGTGAGCTGGCAGCTCGATAGCGAGGAGCACTCTGGGCGACTGAGGGTCCTGCCCAGTCTCAGTCGTGAGGTCCTGGACTGGTTGAGCCAGGACAACGAGCCCGGGAATCGAGTACAGATCGAAGCGCAGGTCGCTTTGACGCAGCTCGCCGCTGGTGGGAAGGACACCGGCAGGGCATGCCGCGCGCTGGGGCGCCTGGGGGGACTCTTCAGTCTTCAACCCACGGTGGTCGAGGTGCTGTCGCAGCAGGCGACGCCCGATATGTTGCAGTACCTCCCTCATGGCTGTCAGAACTTCCACGAGATCTTCTCCGAGGTCTTGGCCAGGAGGTATGACTCGGAGAATGCGGATAAGGTGGCCCGGACCTACCTCGACAGTCACGGACTCACTGATCGCTCCCTGACTATCGGCATAAATCACCGTTTCTCCCCATCTGCTGCCATGAGCCTGGTCGTGCTCAGCCGAGGGATGCCTCTGATGAGCCGTCGTAGCGACGTTGAGGTCCTGCACTATGCTGGCAACGTGCTGAGCGCCATCTGTGCACTGGCAGCTCACCATCACGACCTCGGCCGCGATCCGGTGCGTCAGGCAATGGTCAAGGCCCTGGCGGTGATGCTGGCCGGAGTCTGGAGCGGCAAGCGCATTCTTCTTGAGCGCGTCGTCTGGAAAGGGAACGGCCCCGAGGTTCGGTCGGTGAATCAGAAGCTGGAGCAGGTGATGGCGGAGCTTCCCGATATTCTCCAACGGCACCCGGAGTACCTGCTCTCCGATGATGACAACGGGCCGGGTGTGCTGATGCAGCCCTTGGTCCGGAACCTCTATTTCAGCAGTGGCGTTCGCATGTCAGAAAGCATGGCGGCCCGCGTTGATGAGCAGGTGAGTCAGCTGAGGCAGGGTGAAATGGAGTCCTCCCGCCTGTTCTCAGGTAAGTATGATGCGGCTTTAGCGACAGCTCGTGCTGTCATCGCTCGCGGCGGGGCTGGGGCGGTCGAGCTGTGGCGACCGATTCTTTATGACCTGTTTCATCAGGATGCCGGGGCCCGCCGCTGGGTCGATAAGACCCTGCTGTCTGCTGCGAGTCGTGGTTCCGGAAGCCGTCGGAGGATACTGAGATGA","MSGCEQLLYTNVDHVVDGVERSGWQTMTQTAGLSDGDASTLYALIDPTLNPVTPLSGFPTEQEVAAADRRLAQFWTDEGLVLVHTAPAGNDTTGRPNTMTHVVLAKHHEPAPDLRTIDLWRSPGWVTPFGPEQVRQAELPDPASLRPGASVDDDTVAEFLADGSRSPALVAMADALEPGLLQTIRAQWDGVPSDQARRRNTVVLAVSSTDEAALWIGALLRTCAPATGRYLSYSVLQRILTPSDVEMLLQSRIDVACVPRQDLTNMGESRPGLVVIDPHESGAVEPAPTTSWGRLVALMSQDLGAWVAAYEGMKDVLSLLPDHSDLSPGWPLAAAEACDPGLLEPQQGETPSSSQDEEARAQDEAELIEVELVSCYPRSMVGNDYLAAVVTDRVLGSATQSPAAWYARLSRIPRWAPVSGLVSGLCERYLDAACREVRWMTDLERPVSEQANRCLRQWSGMPEHRSTVDAALAQAKERVEAEQPGTAGGLRVLDRMLREHVSVSTRTCDVLLQGYADMMQPAAYGSREQREILAVPATSLSRSLLADRVSWQLDSEEHSGRLRVLPSLSREVLDWLSQDNEPGNRVQIEAQVALTQLAAGGKDTGRACRALGRLGGLFSLQPTVVEVLSQQATPDMLQYLPHGCQNFHEIFSEVLARRYDSENADKVARTYLDSHGLTDRSLTIGINHRFSPSAAMSLVVLSRGMPLMSRRSDVEVLHYAGNVLSAICALAAHHHDLGRDPVRQAMVKALAVMLAGVWSGKRILLERVVWKGNGPEVRSVNQKLEQVMAELPDILQRHPEYLLSDDDNGPGVLMQPLVRNLYFSSGVRMSESMAARVDEQVSQLRQGEMESSRLFSGKYDAALATARAVIARGGAGAVELWRPILYDLFHQDAGARRWVDKTLLSAASRGSGSRRRILR$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1483","1598683","1596674","2010","4.86","-33.66","72907","ATGACCGTGGCCCTGCCGGTTGCGCTCATGCTCAACAGGAGGTTCGGTCCCAAGGAGGGGGTCAGCGTCCAGCCGGGGGAGCAGGGATCCGACGCCGGCGAGACTCCGTCCGGGAACGCCCCCTCACCTGACGTTCCCGTCGCGCAGGAGGACACCCACGAGGAGCCGACGCCGGAGCCGGACCAGGCGCCGCAGGCCCCTTCCGATGAGGAGACGATCGAGTGGATCTTTCCCGCCTACGACTATTCGCGTGAGGATCTTGACCGACCTGAGGAGGGAGGGCGAGTCTCGGTCACCGTCAGTGACGTCGGAGGCAGCCTGCGCTACACCTGGCCCGATGCGAAACAGTCCGAGGTCTATCGGGTGGTCATCTCAGACCTGGAGGACCCCTACAGCCCGGATGACTTCGACGAGGTGGCTGTCACTGAGGGGCTGAATGCACTGGACTCGGCCCCGTGGACAACGGCCGTGCGCTTCGTCACCGTATGGGGCTACGAGCGCCTCGGCGATGACGAGAAGTATCTGGGGCAGTGCCGGCGAGTCGCCAGTCGCGTCGTCGTTCACCCCGTGGCGCAGTGGTCCCTGAGCTTCAACTCCGAGTCCCGGTGCGTTGACGCCTCCTGGGAACCTCCGGTGGCTCCCCCCGGGGCCACGGTGAAGGTGCGCACCGCCCGCCTTCCTCTGGAGCAATCGGTCGGGCGCTATCTGCGCGGGAGTGCCTGGCTCAGCTGCGAGATCCCGAACAACGGAGCAGGATTTCAGGATTCTGAGAATCTCGTGGGGGGAAAGCAGTACAACTACGTTGCCGCCGTCGAGGCCCAGATCTCCGGGGAGACCTACACCTCCACGCCGATGCGCCAGCAGATCACTCCCGAGGTGGAACGCGAGAAGATCGTCGACCTGGGCATTGCTGACGACGAAGGGAGTGACCCGGCACGCGGGTCGGCTCTGCGACTCACGTGGACCCAGCTGTCTCAGTCCTCCGTGACGGTCTACCGCACCCAGAGGCCCGTGGACCCGGCGGCATCCGATCGAGCCACGGTTCCCGAGGAGGCACTGGCGAACGCGGGCCTTCCCCAGGACGCGGCCATCACTGCGGCCGCAGGCATCGAGCAGCTCGACACCTCGGCCCGGCAGCTGCGCACGATCTCTGCGGTTCCATGGCCGGACGGGCATGAGTGGGACACCATCTACTTCACCCCGGTGACCTTCCACGGTGATGGGGAGGTGACGATCGGCACGACCGTCCAGCGCAAACGTGCCACCAGCATCGAGAACGTCACGCTGACTCGCCGTCTGAACTGGGATCTGGTGACATTCACCTGGCCGGGCGATGCGACTCTTGTCGAGCTGCGCATGACGGCTCTGGACGATCCGTTCGATGCCTCGGCAGCGCCTTTCATGTCCGTGACCCATGAGGACTACCAGGCTGATGGTGGCTGCGTCATCAAGAACGGCCTGCCCGCTCCCGGCGGGCGCCTCCACCTCAATGCGATCACCTACATGTCCGGCACCCAGATCTCCTCACCGCCCGTGAGCATTGAGGTTCCCTCCTTGTGGACCTACCAGTACTCTCTCAAGTGGCCGGGCGACGTGAAGGTCATGGGCGGTTTCATGCGTCAAGCGGTGGCGCGTTTCGGGCACACCGTCGTGGAGATCACCGTTGAGGCCCTCAGGGGGGTTCCGGATCAGTCGGGAGCCATCGGACTGGCGTTGCTTCACAACCCCTCGCACCTTCCTCTCCACGCCGCTGACGGGCAGAGAGTCGGCTTGTTCCTGGAGCGCCCCACCAAGGACAACCACCCGCAGGCTGAAACGTCTGTCCAGGTGCCGCCTAACGGACAGCCGCTGTCACTATGGTTCGATCACTCGAAATTCCCTGCCGGATACTTCCGGCTGGTTATCGACTCCTATCCACTGAGCGCCATTGACGAGAAGGCTCGGCATCTGGCGCTCGAGCACTTCGGTCTGGTTGATCCTTCCCTGTCTGCTCTCATCAAGAAGGGGTGA","MTVALPVALMLNRRFGPKEGVSVQPGEQGSDAGETPSGNAPSPDVPVAQEDTHEEPTPEPDQAPQAPSDEETIEWIFPAYDYSREDLDRPEEGGRVSVTVSDVGGSLRYTWPDAKQSEVYRVVISDLEDPYSPDDFDEVAVTEGLNALDSAPWTTAVRFVTVWGYERLGDDEKYLGQCRRVASRVVVHPVAQWSLSFNSESRCVDASWEPPVAPPGATVKVRTARLPLEQSVGRYLRGSAWLSCEIPNNGAGFQDSENLVGGKQYNYVAAVEAQISGETYTSTPMRQQITPEVEREKIVDLGIADDEGSDPARGSALRLTWTQLSQSSVTVYRTQRPVDPAASDRATVPEEALANAGLPQDAAITAAAGIEQLDTSARQLRTISAVPWPDGHEWDTIYFTPVTFHGDGEVTIGTTVQRKRATSIENVTLTRRLNWDLVTFTWPGDATLVELRMTALDDPFDASAAPFMSVTHEDYQADGGCVIKNGLPAPGGRLHLNAITYMSGTQISSPPVSIEVPSLWTYQYSLKWPGDVKVMGGFMRQAVARFGHTVVEITVEALRGVPDQSGAIGLALLHNPSHLPLHAADGQRVGLFLERPTKDNHPQAETSVQVPPNGQPLSLWFDHSKFPAGYFRLVIDSYPLSAIDEKARHLALEHFGLVDPSLSALIKKG$","Hypothetical protein","Periplasm, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1484","1601700","1598971","2730","5.98","-10.39","98140","ATGGAATCATCAGGGCCTGCCGAGTCCCGGTCTGTCTCGGTCTTCGTTGCTCCGCCGAGCCAACGGCCTGTTCTGTCCGCGCTTGTCGACCTGTCCGCCGCTGGGCTGCTCGCTCCCTTCGCCTGGATCGAGAGCGACAGCGAGCCGGACAAGGCTGCGGACCGCTACGACCCCGTCGCCGTGTGGGTCGATCACGGGCAGGTGACAGTGAGCACCTTCTCCCGGATCGTCAACCGCCATGACCTGGAAACGGTCCGGCTGCTCGTCGTCGTTCCTGTGGGGCATCCCGCTCAGGACGCCCTGCCCGCCAGCGCGGAGCAGTTCTATCAGCTCCTTGGGGTGCCGCAGCACGTGCGCCGGGAGAGCCTGCGCGTTATCGTTCCCTACTCCGCGCAGCCGCTGGCCGCCGAGCTGGGGCGCATCGGTTGGCGCAAGATCATGCTCTCCCCGGAGTCCACCTCCGATCCGGCCTACAGCGCCATCCCGTGGTGGACCAGGCCGGAGACGGTACCGGGATCAGCCGCGGTCGGTCTGGCGGTGCAGGCCGGTCTGTGCGGGGCCGTCAATGCGGCGCCGCATGACGGACAGCGTGAAGACGTCTCCTACGACATCAACGTCGTGCGCAGCTTCGTGCGTATCGTTGACGCCCACAGCGTGGAGGACCAGCTGCGCCGTCAGGTCACTGAGGTCGGAGAGAGCTTCCCGCAACCCACCCGCGCCGATACCGGTGTCCGGGTCCCGGCGTATGCGGATCCTGAGGCCAGGGTCGCCGCCGTGGCACAGGCCTGGCAGGAGCGCCACATCCACTCGTTGAGGCGTCCTCAGGTGCCGATGCCCGAACGCGCCGGTGCGCGCCGCATGGGGGCTCTCGAGGCGCTTAAGCTCTTCTTCTCCTTCCTGGTCAAGGCGCTCATCGGAGCTCCCGGTGAATGGCTCCGCAGCCGTGTGCGGGCCGCCAAGGCCTCCATCGCCTCTGGAGTGGCGTCGGCGGTCTTCGGTGAAGGATCCGCGGTACAGGTCGTCGTCGGAGGCGTGGACTCCAACGGGCGGACCGTCGGCTGGAACGAGCTGACCGATGCCGCCAAGCGCGCCAGCGACACGTTGCCCGCGGACTTCCCACGGTCGGGTCAACCCGTCCAACGGGATTTCGGGGCCTTGTGGCAGGACCTGGTCTCAGGAACGATCGCCCTGCTGGACGGCTCGGCCCACTCGTCGCTGGGCATCCAGGCCTACGAGGGGTACCTGCCGCGGCGTGATGCCATCGCCGCGCCTCCCGGCCCGAGGAGTCGCATCGAGATCACCGAGCCACTGGGCGACCTGCCGGCCGGCACCGTGCTCCACTCCTGGGACCAGCTCGAGATCGACCGCGTCCGCACCTATCTGCAGCAGCTCTCCCAGTCCCAGCACTCCCAGGGCCCAGAGGCGGCACGCCAGCTGGCGGAGATAGACCGGTGGCGAGCCGACAACAGCCGTCGCCTTCTGCCGCGCCTGGGCGCCGTTCTCTCCAACTGCTTCACCTCCACCAGGAACGACGTCGCCGCGCTGTCCCACGAGCTCCAGTCGCTTCTCGGGCAGGAGCCCGGCGGGGAGCTGGAGCAGCGCCAGCGCAGGCTGGCCAGGATCCTGCGTCTGTTCCTGCTGGTCCTCGTGATCGTCCTGGCGGTCCTGGTGGTGAGTAAGACCATGGGCCGTATTAGCTGGCTGTACTTCGCGCTCCTTGCGGTCGTGGCAGTGATCGGGTGGCTGGCCGTCTCGATATCAACCTTCGTCTCGCAGCAGCGTGAGGTCTTCCGCATTCTGTTCAGGATCGAGGAACGAGACCAACGCATCCCCCTGCTCACCGCGAACCTTCGGCTGGCGGTGGAGGATCTCGCCGCCCAGGGGGCCGCCTACTCACAGTTCAGGCGCTGGGCGACGATCGTCTCGGCCTTCTTGGAGGACCCGCTCGGGGCCCGTGACACAGGACCCGACCGGAGCTCGCAGAAGGTTGCGCTCCCTGATGCCATCCAGCGGGTCGAGGCAGAAGCCTCGCCCGAACACCTCGCCGACGCCGCTGCCTCCTTGCGCACGAGTGTCTTCACCGTGGGCTGGCTCACCCAGGCCTGGGAGACGATGCGTGCCGGTATTGGCGTGGACCTGGACCCTGAGCAGCGCAACCGTCTTGCGACCCGGCAGCTGGTGCTGACGGCGGAGTCCGGTGAGGCGGGAAGCGCCTTGAGCAACTGGGCGCAGGGTCTGCAGACCAAGGGGGTGCGCTCGGCCCAGGCGAGTCAGATCTGGCAGCAGTGTCTGGCGATCCTCTCGGGGGATCAGGGCCCCGACCCCCGGCTCACGGTGATGACGCCCTCGGGGGAGCGGCGTCAGGTCTCCGCCTACTGCCATGATCTGACGACCGGGGGCTCACGATCAGTGGTGCTCGATGTTCTCGGGCCGGTGGCCCGTTCGGGTCCGCAGTCCCTGACAGTGCCCGACCAGGCCTGGCTCAGCCAGTGGAACGACGGGTTGTCTCCCACGATGGTGCTGGTCGAAACCACGAACCCGATTGCGCCGGCTGACTTCATCTACCCGGATCACGACCAGAGCCCGAGCGGCCCGCTCGCCGGGATGGACTACTTCAACGTCGGACGGGACCAGACGGCGCCTCCTGGCAGCGCCGGTTCCTCCTCCAACGGGGCTCCGGGCGATACGCCCGCAGGGCCGGAACCCTTGTCCGGTCCTCTCGAGTACTAG","MESSGPAESRSVSVFVAPPSQRPVLSALVDLSAAGLLAPFAWIESDSEPDKAADRYDPVAVWVDHGQVTVSTFSRIVNRHDLETVRLLVVVPVGHPAQDALPASAEQFYQLLGVPQHVRRESLRVIVPYSAQPLAAELGRIGWRKIMLSPESTSDPAYSAIPWWTRPETVPGSAAVGLAVQAGLCGAVNAAPHDGQREDVSYDINVVRSFVRIVDAHSVEDQLRRQVTEVGESFPQPTRADTGVRVPAYADPEARVAAVAQAWQERHIHSLRRPQVPMPERAGARRMGALEALKLFFSFLVKALIGAPGEWLRSRVRAAKASIASGVASAVFGEGSAVQVVVGGVDSNGRTVGWNELTDAAKRASDTLPADFPRSGQPVQRDFGALWQDLVSGTIALLDGSAHSSLGIQAYEGYLPRRDAIAAPPGPRSRIEITEPLGDLPAGTVLHSWDQLEIDRVRTYLQQLSQSQHSQGPEAARQLAEIDRWRADNSRRLLPRLGAVLSNCFTSTRNDVAALSHELQSLLGQEPGGELEQRQRRLARILRLFLLVLVIVLAVLVVSKTMGRISWLYFALLAVVAVIGWLAVSISTFVSQQREVFRILFRIEERDQRIPLLTANLRLAVEDLAAQGAAYSQFRRWATIVSAFLEDPLGARDTGPDRSSQKVALPDAIQRVEAEASPEHLADAAASLRTSVFTVGWLTQAWETMRAGIGVDLDPEQRNRLATRQLVLTAESGEAGSALSNWAQGLQTKGVRSAQASQIWQQCLAILSGDQGPDPRLTVMTPSGERRQVSAYCHDLTTGGSRSVVLDVLGPVARSGPQSLTVPDQAWLSQWNDGLSPTMVLVETTNPIAPADFIYPDHDQSPSGPLAGMDYFNVGRDQTAPPGSAGSSSNGAPGDTPAGPEPLSGPLEY$","Hypothetical protein","Membrane, Periplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[541-559]?$ $\"[569-589]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1485","1605226","1601702","3525","5.41","-26.89","126674","ATGCTGGACCAGCTGCACGCGGACCTGGCGGTCCACGGGATCGATGAGGTGCCGGGCTGCTGGCAGTTCCTCAACGTCGACACCCCCCTTCAGGAGGAGCAGGGCGAGGCGGTGGCCTCGGTGAGCCGCCAAGGGGGCTCCTATGTGGCATGCGGCGTCGCCAACGGTGAGTACCGCGTCGTCGACGAGGCTCTGACTCAGTCGGTTCAACGTAACGGCAGTCAGGGGCTGCGACAGCTGGCCACCTGGATGCCTCGCCGCCCCAAGGACGTCGCCTTCCCCGTGACAGTGGGTGCCGGACAGTTCCGGGGGATCGGTCGCCTGCTCGTTCTGACGAGGCTGCGTGACATCTCGCAGGCCGTGCAGTCGGCTCTCGCGCGCATGGTGAGCCCCAAGGCTCAGGAGCAGGCGGCCCTGGTCTCGCAGGCGGTTCCCGGAGCCGGTGCCGCCCCCGACACCACGGCTCCGCCTCTGGTGCTCGTCGTCTCCTCGATGGCTGGAGGGTCTGGGGCGTCCATGACCCTCGATGTGTGTCGCCTCATCGCAGGAGTCAACTCGACGCCGGCGATCGACCCCCAGCTCATCTCGGTGTTCCTCTACACCGCCGAGGCCTTCGCCTCGGTACCGGCACACATGCGCTCGGGCATGCCGGGCAACACCCTGGCCATGCTGGGGGAGATCGTGGCCGCCCAGGCGGGGGCCGACGGCGCCGCGGCCGAGCTCGACCAGCGGCTCTACGAGACGCTCGGACTGACGAATCGGGCGGGGCGGGCCTTCAAGCGAGTCACCCCGATCGGCCTGCGCGCCGGCGGCTCCGGCGCGGTCTTCGGGGACGGCACCACCGAGGGAGTCTTCCGGGGAATGGGGCGCGGCCTGGCGCGCTACATCTCGTCGTCGGCCTTCGACGACTATGTCTCCTACGACATCGCCAACCAGGTCTCCATTCCGGGACGGGACATGACCAGCTGGGGCGTGGATCCCACGGACACGGCGTGGGGCTCCTTCGGCTACGCGTCGCTGAGCACCGGGCGGGACCGGTATGCCGAGTACGCCGCCCAACGCATTGCTCGGCGTTCCGTCGACCACAGCCTGGACGGATTCCGTTTGGTGGGTGACACCACCGGTGACACTCAGCGACTTGCCGACCTGTGGGCGCATCGTCAGGACAGTGAGCTGAGCAGCCTGGGACTTCCCACCTCCTCCGGCTCCCCGGTCCTGGCGGGAAGCTCGGCGGTGGACCAGGCCACGATCGACTGGTTCCTGAGCGATACGGTCTCCTCAACCGTCAACAAGTCCGTCCTGGGGGGCCACGCCAAGGACGCGGTCAAGGCCGTGCTGGCTCAACGGCCCCAGGCCGAGGGAATGCCGGTGACCGAATGGGCTGACGGGATGAACCGGTGGCTGACCACGTCCAAGGAGTCGGCCTTCATGTCCGAGCTCGAGCGCGCCAGCCTCAACTACGCGCTCAAACGAGTCGATGAGATGGCTGACCGCCTCGTGGCCACCACCCGGCAGGCGATCGCCGACCTCGGACTTCCTTACGCCCTGTATCTGTTGGGGCGGCTGCGCCAGCCCGGGGGCGTCCTGGACACGCTCATTCCCCGGGTCGCGGCGATGGAGCATCTGGCGCCCCAGCACCCCCTGTCCTTCCCCGACTCCCTCCTGAACCAGCTGCGCGGCATGGGCAAGGCCGTTCTGGGCGGAGCAGGGCTCGGGGAAGTGACCGGCAAGCTCGAGTCCGAGCTGCAGCAGTCGGCATTCCACTGGCTCAGCGCGCGAACTGCCGCTCATCTCGCCACAGCGATGCGCGACATGATGACCTCAGCCGTCAAGCCCTTGGAAGACGTCCTGGACGATGCCCGCAAGGTCCTCGTGGACGCGCGAGCGGTCCGCGCCAGCCAGCAGGGCATCGCCGACGTCACCACGGACGTCTACAGCGCATGGCCCCAGGAGCCTCAGCCCGGCCAGGCCGACGGCAGCATCGTGCCGCAGCGGTTCGCCACCGCCCACAACGAGGTCGTCCTCATGCCGGTGGAACAGTATCCCGGACGGTTCGAGGAGCACATCTCCGACGCCGTCGGCGGTGAGCGCGACTTCCACCAGGCGTACTCCCGTACTGTCCAGGAGGTCCTCTCCGGGACCTGGGAGCAGGGGGCGGGGGACAAGCCCCCGGAGGATCTGCTTACCGTGACGACCGCGTGGGTCCCCGCAGGCCTCCAGGGCGCCACCGGAAGCGCCCTTCCCACACCGGCCCGGTACGAGCTGCGTCTGCGCCCCTCGGAGGTCCTGGGCCGCGCCCGAGCGTTCGTCGCACGGCGCGGTGAGGCCTTCGAGGTCTTCTGCAGCCAGTCCCTGCGAAGCTTCCTCACCGACGAGACGGTGGGCGAGCACGAGCGGTCTCAGCGGTCGCAGGCCGTTCTCACCGGCCTGAAACGGACACTGGAGATGGCACGGCCCCTGGTGGAGATCAGCACCGAGACCTACCGCTCTCTTCACAACGGTGACACGCCTGCGCTGGCATACACCTTCTCGCCCATCCCCCTGCGCAATCAGAGCGTCGCCCAGGACTTCCTCGACTACCTCGACCAGGAGTCGACCATCGATCGTGAGCTGGTGCACGACCGAGTCGACAAGGCCCTGGGGGACGAGGACGTCGCCCGCATTGACGTCTTCGGCTCCTACCCCCGTACCCTGCCCGTGGCCTACTCCGGCCTGCTGCGCTCCGTGCGCGAGTCCTGGGACCGGGCCCACGGCTCGGCGGGAGCCCGGGACGCGTTCTGGCGGTTCCGGCGAGCACGTCCCCTCAGCGGTGGACTGCCCTTCGGTGACGCGGAGCGCCTCACCATGGTGCGTGGCTGGTGGACGGCCACCCTGGCCGGCGGGATCGAACGGGCGCCGTGGGGCGGCCACTCCGACACCCAGCCGGTACGTGTCTGGGACACCGAGGAGCAGGAGTGGGTGGCCTTCCCCGCTCCCATGCTCACTCCGCCGTCACGAATGATCACCGCCAACGCCTGGTTGCCCGCGGTGCTGGAATCATCCCTTCTGGCGTATCTGCGCGTGGGCGAGGACGGTCTGCAGGCCTTCAGGCCCTGGCGGGTGCTGCGCCGATGGGCTGATGCCTCCGTCAACGAGCCGCAGATCGCCTTCGGGGTGACGACTCCGGTCGACGAGGCCGTATCAACGCTCCTGGGACGGGGACAGGTCGACGGTCTCACTCCGGCCGCCGGAATCGATCAGCTCACGGATCCTGAGCTTCGCCGCGAAAAGCTCTTGAGCTACTGCGACGTGATCCTCGGCGACCTGGAGCAGAACTACCTGCCTGGCCCTGGAAAGGCCGATGAACCCGGGCACTTCACCAACTACCGCAGACGTTCCCTGGTGGAGACGACACCTTTGACCATCGATCTCGCCCAGGACATGCACGACGAGCTCAGTCACGTTCGTGGCGTTGTCGCCTCAGCTCCGCCCGCCTCGGATCTGGGCGCCTCGCCGACATCATTCGGATCCGGAATCGAGTACTGA","MLDQLHADLAVHGIDEVPGCWQFLNVDTPLQEEQGEAVASVSRQGGSYVACGVANGEYRVVDEALTQSVQRNGSQGLRQLATWMPRRPKDVAFPVTVGAGQFRGIGRLLVLTRLRDISQAVQSALARMVSPKAQEQAALVSQAVPGAGAAPDTTAPPLVLVVSSMAGGSGASMTLDVCRLIAGVNSTPAIDPQLISVFLYTAEAFASVPAHMRSGMPGNTLAMLGEIVAAQAGADGAAAELDQRLYETLGLTNRAGRAFKRVTPIGLRAGGSGAVFGDGTTEGVFRGMGRGLARYISSSAFDDYVSYDIANQVSIPGRDMTSWGVDPTDTAWGSFGYASLSTGRDRYAEYAAQRIARRSVDHSLDGFRLVGDTTGDTQRLADLWAHRQDSELSSLGLPTSSGSPVLAGSSAVDQATIDWFLSDTVSSTVNKSVLGGHAKDAVKAVLAQRPQAEGMPVTEWADGMNRWLTTSKESAFMSELERASLNYALKRVDEMADRLVATTRQAIADLGLPYALYLLGRLRQPGGVLDTLIPRVAAMEHLAPQHPLSFPDSLLNQLRGMGKAVLGGAGLGEVTGKLESELQQSAFHWLSARTAAHLATAMRDMMTSAVKPLEDVLDDARKVLVDARAVRASQQGIADVTTDVYSAWPQEPQPGQADGSIVPQRFATAHNEVVLMPVEQYPGRFEEHISDAVGGERDFHQAYSRTVQEVLSGTWEQGAGDKPPEDLLTVTTAWVPAGLQGATGSALPTPARYELRLRPSEVLGRARAFVARRGEAFEVFCSQSLRSFLTDETVGEHERSQRSQAVLTGLKRTLEMARPLVEISTETYRSLHNGDTPALAYTFSPIPLRNQSVAQDFLDYLDQESTIDRELVHDRVDKALGDEDVARIDVFGSYPRTLPVAYSGLLRSVRESWDRAHGSAGARDAFWRFRRARPLSGGLPFGDAERLTMVRGWWTATLAGGIERAPWGGHSDTQPVRVWDTEEQEWVAFPAPMLTPPSRMITANAWLPAVLESSLLAYLRVGEDGLQAFRPWRVLRRWADASVNEPQIAFGVTTPVDEAVSTLLGRGQVDGLTPAAGIDQLTDPELRREKLLSYCDVILGDLEQNYLPGPGKADEPGHFTNYRRRSLVETTPLTIDLAQDMHDELSHVRGVVASAPPASDLGASPTSFGSGIEY$","Hypothetical protein","Periplasm, Membrane, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1486","1608243","1605409","2835","5.41","-17.31","97979","ATGACCCGGCGTCACAGTTACTGTGAACTGATCCATCGATTGAGGCGGTTGGCCGTCAACGTCCTGGCAGTTCTGGGCGTCACGATCCTCCTGCTCGCAGGGGGTGCGCTGCCCGCTGCCCCTCAGGCTCTCGCCGCGCCCCAGAAGGATCAGTCCTCCGGGCCTCTCAGCTCATTCGGGGCCTGCCTCTCAGGTAAGGGCGAGGGGTCGTTGGTCCTCCTAATGGACCAGTCGGGTTCCCTGAGGCAGTCGGATCCGGAGAAGGCGAGAGTCAAGGCGAGCCAGTACCTTGCGCAGCGTCTCGCGGCCTTCGCCGACTCCTCCAAGGCCACGTTGAAGGTGAGGGTCGCGGGATTCGCCTCCGACTATCACGCGCTGGGCGATTGGGTGACGATCAACTCAGGTTCCCTGGCTGAGGTCGGCAAGCAGATCACCGCAGCCGGGGACGATCTCAAGGACTACGACACGGACTACTGGACCGCTCTGGAGGGAGCGCGCCAGGACCTGGCGGGACATGACCGCTCAGAGTGCCGGGCGGTGGCATGGTTCTCGGACGGCGCCTACGACCTCGATGTGCGGGACTCTGAGCAGTCCCAGCAGGATTTCGGCACCACCAAACCCTATGCTCCTGGCTCCGCCTTGACTGACGAGTCGGGCGTGAAGACGGCCGAGTCCGCAGGAAAGCAGGACATCTGCCGGCCCACCGGACTCGCTGACCAGCTGCGTTCCTCCCACATCACGTTGCTGGGCATTGGACTGAGCAGCGGAGACTCCAACTTCGATTTCATGAAGAGAATCACGCTCGGTGGAGGGGCGAATGCCGCTAAAAACTCAGTCGAGTCGTGCGGCAATGTCTCCGATCCACCGGGTGGATTCTATCCGGTGACGGATATCGACTCACTGCTCATGGCGTTCGACTCTATCTCCGCCCCGGGGCGCTCGGTCTCCAGCAGCACGACCAAGATCTGTCAGGGCGACGTGTGCTCCGACGGAGAGACCAGCTTCGTCCTGGATCGTTCGCTGCGCAGCGTACATATTCTGGCCTCGTCGGATACGCAGGGACTGGAGGCCGACCTCTACGCCCCTGGTTCTCAGACGCCCATCGCGATGACATCGGACTCCAGCGGCCCGCAGAACAAGCAAGGCGTCTCATACGAGTGGATGACGGGTCGGACGCTACGAATCGACCTTGACTCCGCCAACGCCGCCGCATGGAACGGGCAGTGGCGCCTGGTCTTCGTGGACAGGCGGTCAGCCTCAGCAGGACATGAGGTTCATGTCAACCTTCACCTCAGCTCGCCGTTGTCAATGGCCTGGAAGAACTTGGGACAGACGACCCTGCGCCAGGGGGAGGCGGTGCCGAACGCCGACCTGAAGCTGGTTGACGGCGTCGGAGGCCCGGAGGTTCCTGCGTCGGATCTCACCGGTCCAGTCTCCCTGAACATGTCGCTGAAGGATGCGAAGGGAAAAGAGCACACCCTCTTCACGAGCACCGACCCGGCCTCTCTGTCCACGCCGCAACGGATCACGATCCCCAAGGACGCTGCTCTCGGCAGCGGCACCCTGACCACCAGCCTCACCCTGACAACGGGTGACGCCACCAGTGCCAGCGGCTCACCCGTCAAAGGCACCACGCTCTCGCCATCGCTGGCCTCGACCGCGGTGACTGTCTCCCCGCCGTCGAACTACCCGACCCTGGGTGACCAGATCGACTTCGGTCGCATGGATGGTCAGACCGCGGCCAGCGCCGACCTCAAGGTCACCGGGCCGGGCTGCGTCTGGATCGGGGACGGTCAGACCACGCTCACCGGATCCCCGAAGGAAGCCGGAACCGTCACGCTCTCGGCTCAGGCGTCGTCGAAGGACACGTGCGTCAAGGTCGAGGAGGGGAAGACGGGAACCGTACCGGTCAAGCTGGCGGCTCAGGAGCACGCCAACGGCGCGGTGACAGGAACCGTGACCGTTACGGTGGCTCCGCTGAACAACCAGGGAGAGCCCCAAAGCGTCGCCGTCCCCTTCAAAGCCGATATGCGCCGCCCGCTCAACGTCGGCACCGCATGGACGGCATTCATCATCGCGCTGCTGTGCGGAGTGCTGATCCCGATCGGAGTCCTCTACCTCCTCAAGTACCTCTCGGCAGTGATCCCCTCGGGCTCGCTGGTCGCGGGCACGACTGTCGTGGACGTTCCCCGTGACGGAACCTCTCCCAGGATCGAGCTGCCCTCCCAACGGATGAGGATGTACTCCCTGCGGGGCCGTACGCGCACGTTTGAGATGGACGGCTACCGTCTACGCGCCATCATGGGACTGTCGCCTACTGCGGTCCCCCGGGTCGAGCTCGTCGAGCCGGACGTTCCATCAGTCTCCGGGGCGACTCCCGGATCACGCGGTGGGCGGGCGGTCGTGCCCCTGGGAGTCCGGGGCCAGTGGATCGCGGTTGCCGACCAGCCGTCGCAGTCGGACGACGTGCGGCGGGTGACCCTGATCGTGCTGGCAGCCTCACTGGACGACGCCGTCCTGGCCAAGGTGGTGGACGATGCCCGCGCCCATCTTGCCTCTCGCGTTGACTCGATCCTTCCTGCTGAGCCGGCCGGGGCGTCGACCTCAGCAGCAGAGGGGCGAATCGGGACTCTGCCCACAGCGGGGACATCGATGGCGGAGGCCGGGGGCGGCTTCGGCTCCCTCAATCCGGTCGACGACAGTCCTTTCGCCGGCTTCCCGACCAGCTCGGGGACGCCGTCGCCACAGGTGTCCAGCCCTGAGGTAGAGGCAGACGAGCGTCCCTCGTCCAACTCCGATCCTCAGGACCCTCCGGCCGCCCTGCCCACGTTATAG","MTRRHSYCELIHRLRRLAVNVLAVLGVTILLLAGGALPAAPQALAAPQKDQSSGPLSSFGACLSGKGEGSLVLLMDQSGSLRQSDPEKARVKASQYLAQRLAAFADSSKATLKVRVAGFASDYHALGDWVTINSGSLAEVGKQITAAGDDLKDYDTDYWTALEGARQDLAGHDRSECRAVAWFSDGAYDLDVRDSEQSQQDFGTTKPYAPGSALTDESGVKTAESAGKQDICRPTGLADQLRSSHITLLGIGLSSGDSNFDFMKRITLGGGANAAKNSVESCGNVSDPPGGFYPVTDIDSLLMAFDSISAPGRSVSSSTTKICQGDVCSDGETSFVLDRSLRSVHILASSDTQGLEADLYAPGSQTPIAMTSDSSGPQNKQGVSYEWMTGRTLRIDLDSANAAAWNGQWRLVFVDRRSASAGHEVHVNLHLSSPLSMAWKNLGQTTLRQGEAVPNADLKLVDGVGGPEVPASDLTGPVSLNMSLKDAKGKEHTLFTSTDPASLSTPQRITIPKDAALGSGTLTTSLTLTTGDATSASGSPVKGTTLSPSLASTAVTVSPPSNYPTLGDQIDFGRMDGQTAASADLKVTGPGCVWIGDGQTTLTGSPKEAGTVTLSAQASSKDTCVKVEEGKTGTVPVKLAAQEHANGAVTGTVTVTVAPLNNQGEPQSVAVPFKADMRRPLNVGTAWTAFIIALLCGVLIPIGVLYLLKYLSAVIPSGSLVAGTTVVDVPRDGTSPRIELPSQRMRMYSLRGRTRTFEMDGYRLRAIMGLSPTAVPRVELVEPDVPSVSGATPGSRGGRAVVPLGVRGQWIAVADQPSQSDDVRRVTLIVLAASLDDAVLAKVVDDARAHLASRVDSILPAEPAGASTSAAEGRIGTLPTAGTSMAEAGGGFGSLNPVDDSPFAGFPTSSGTPSPQVSSPEVEADERPSSNSDPQDPPAALPTL$","Von Willebrand factor, type A domain containing protein","Membrane, Periplasm, Extracellular","Hypothetical membrane protein, putative","hypothetical membrane protein","hypothetical protein","","Ruggeri Z.M., Ware J. von Willebrand factor. FASEB J. 1993. 7(2):308-316. PMID: 8440408Colombatti A., Bonaldo P., Doliana R. Type A modules: interacting domains found in several non-fibrillar collagens and in other extracellular matrix proteins. Matrix 1993. 13(4):297-306. PMID: 8412987Perkins S.J., Smith K.F., Williams S.C., Haris P.I., Chapman D., Sim R.B. The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. Its occurrence in collagen types VI, VII, XII and XIV, the integrins and other proteins by averaged structure predictions. J. Mol. Biol. 1994. 238(1):104-119. PMID: 8145250Bork P. Shuffled domains in extracellular proteins. FEBS Lett. 1991. 286(1):47-54. PMID: 1864378Edwards Y.J., Perkins S.J. The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted beta-sheet flanked by alpha-helices found in human ras-p21. FEBS Lett. 1995. 358(3):283-286. PMID: 7843416Lee J.O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 1995. 80(4):631-638. PMID: 7867070Qu A., Leahy D.J. Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(22):10277-10281. PMID: 7479767","","","

InterPro
IPR002035
Domain

von Willebrand factor, type A
SM00327	$\"[68-294]T$	VWA
PS50234	$\"[70-308]T$	VWFA

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[686-708]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[80-98]?$ $\"[104-124]?$ $\"[144-166]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[44-66]?$ $\"[75-95]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[114-134]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[57-77]?$ $\"[87-107]?$ $\"[137-157]?$	transmembrane_regions

InterPro
IPR003476
Family

Glycoside hydrolase, family 42
PIRSF001084	$\"[18-736]T$	Beta-galactosidase, BgaH type

InterPro
IPR013529
Domain

Glycoside hydrolase, family 42, N-terminal
PF02449	$\"[29-398]T$	Glyco_hydro_42

InterPro
IPR013738
Domain

Beta-galactosidase trimerisation
PF08532	$\"[408-673]T$	Glyco_hydro_42M

InterPro
IPR013739
Domain

Beta-galactosidase C-terminal
PF08533	$\"[682-734]T$	Glyco_hydro_42C

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[25-402]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[405-677]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-49% similar to PDB:1KWG Crystal structure of Thermus thermophilus A4 beta-galactosidase (E_value = 6.7E_75);-49% similar to PDB:1KWK Crystal structure of Thermus thermophilus A4 beta-galactosidase in complex with galactose (E_value = 6.7E_75);","Residues 29 to 398 (E_value = 2.9e-205) place ANA_1492 in the Glyco_hydro_42 family which is described as Beta-galactosidase.Residues 408 to 673 (E_value = 6.7e-23) place ANA_1492 in the Glyco_hydro_42M family which is described as Beta-galactosidase trimerisation domain.Residues 682 to 734 (E_value = 1.2e-05) place ANA_1492 in the Glyco_hydro_42C family which is described as Beta-galactosidase C-terminal domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1493","1616026","1613471","2556","5.05","-35.64","89488","GTGCTACAGTGCGCGATACGTCAGACATCATATGACTGGATGTGCGGTGGCGCACCGTCGCGCACGGCACTGCCGGTCGTTCAACGCCGGCGGGCAGCCGCTACCGCCACGAAGGACCTCCCCATGCTCTTCGATCTCACCGCATCCGACACCTCCCCCCTGAGCCTCAGCGAGGAAAATGTCGCTGCCCTGGCCGCCTGCGGGCGCGGCACGATCCTTCTCGATGTCGCCGCCCGCGCCGACGCCACCCTCATTGCGTTCACCGGTACCAACGGACGGATCACCCTGTCGCTGCGCGCCGGCCGCCTCGACGGCGAGCAGGTCCTCGGCGCAGTCGGCCGTCCGGAGGGGTCCTCCGGAGCCGGGAGTGAGAGCGGCATTCAGCACCGTGTCCTCGACGCCGAGGACGCCCTGGGCCTGGACGACGGCCGCCCCCACACCATCGCCGTCACCGTCAACGAGACCGGCACCCACCTCTACGCCGACGGCTACGAGTGCTTCTCCACGACGCTGACCGCCTTCCTCGCCCAGATCGGGTTGACCGATGTGCGTATCGACCCCGACGGGATCGCCGCGGTCACCCGCCTGGCCGCGTGGGACGAGCCGCTCAGCGACCGCGCCGTCATGGCCCAGTCCCTGCCCGCCACCCCACTGGTCCAGTTCGCGGCCAGTGAGCTCTCCGCCCGTGACGCCCGCCGTACCGGCGCCCTGGCCACCGGCTCCATCCGGGCGCTGCTGCGCACCCGCGGCCGCGGCCAGGCGGGCACCATCGTCGCCGCGAGCGGCCAGGGCGGCACCCTGCACCTCGACATCGATGCGGGAGGTCTGAGCTACCGGGTGCTCCCCGGCGAGGACTCGCCGGAGACCGAGCCCCTCATCGAGGTGCGAGCCCCGGGCCACTGGGACGACGGGACCTGGCACGACGTCGTGGTCACCTCGGGGCGCGGCGCGGTGGAGATCCATGTCGACGGCTACCAGGTGGCCCTCGTCCCCGGCGGTGCCTTCCTGGCCGACATCGCGCCGGTGACGCGTGTCGTCGTGGGCGCCGACCTGGACGGCAGGCGCCTTTTCGGTGAGGCGCAGACCGCCATGATCTACGACGCCGCCCTCACCGACGCCCAGGTCAAGCGCCTGGCCGGGGCCGCCCCGCTGCCCACGCGCGCCCTGTTCGACACCGGCTACCACGGCGCCCGGTCCTACCGGATCCCCTCCCTGCTCACCCTGGACAGTGGCGTCATCCTGGCTGGCGCCGACCAACGCGTCTCCATCCCCAACGACGCCCCCAATGACATCAACCTCGTCATGCGTCGCAGCCTCGACGGTGGGGCCACCTGGGAGGAGATGCACACCCTGCTCAGCCTCCCGGGCACCGGGGCACTGGGCGCCAGCCTCATCGACTCCGTCCTGGTCCAGGACCGCTCCACCGGACGCGTCATCTGCCTGGTCGACCAGTTCCCCGGCGGCATCGGTCAGCCCAACGCGGCCGTCGGCACCGGTTTCGATGAGCAGGGGCGTCGCGTGCTCCACAACCGCGCCGGCGAGCTTTTCGCCGTCGAGCCCGACGGCAGTGTCGTCACGCAGACCGGCGAGGCCACCGACTACCGCGTCATCCTCAGTGGCGATGACGCCGCCGGGGTGCGCGCCGGTGACGTGCTCCTGGGCGGCCGGGAGGCCGGCAGCATCTACCTCGCCCACGAGCAGGCTCCCGAGGACTGCCTCTTCCAGCACCGCGGCTCCCACCTGCTCATGATCACCTCCGACGACGACGGCGCCACCTGGTCCGAGCCGATCGACATCACCGCCCAGGTCAAGGTCGACTGGATGTGCTTCCTGGGAACCGGCCCCGGCAACGCCATCCAGCTGACCGCACCGGAGCACGCCGGACGCATCCTCGCACCCGTTTACTACAGCCACGAGGCCGGCGGCACCGCCTACCTGTCCTGCGCCGCCATCTACTCCGACGACGGCGGGACCACCTGGACCCTGGGCGCCTCACCCAATGACGGACGCGAGGTGCTGGGCGCCGTCGTCCACTCCCGGGACCTCACCGACGAGCGGGCCAGCCTCTACGAGTCCGTCCTCGTCGAAGGGAACGACGGAGCCGTGCACGTGTGGGCTCGCAACCAGCACCCCTCGGGGAGGGTCGCCCACGCCGTCTCCCACGACGGGGGCGTCACCTGGGGCGAGGTCGACTATGACGAGCAGCTTCCCGAGATCTTCTCCCAGCCCAACGCCATCGCCATCACCGGCCTGGAGGGCGCAGCGGCAGCCGGGGACGGCGACGGCGTCAAGGGTGCGGTCGGCCGGGGGATCGTCTTCGCCAATGCCTCCCGGATGCTGCCCTTCCGCGGCTGCGGCGTCCTGCGCCTGAGCTACGACGACGGCGCCACCTGGCCCCACAACCGGGTCATCAACCCGCGCCACTACGTCTACCAGTGCATGGCCCAGCTGCCCAGCGGCGACATCGCCCTACTGTGGGAGCGCGAGTGGCAGGGGCTGTTCCTGACCACCGTGCCGCTGGCCTGGCTGACGAGCTCGCACTCGACCATCAGCTGA","VLQCAIRQTSYDWMCGGAPSRTALPVVQRRRAAATATKDLPMLFDLTASDTSPLSLSEENVAALAACGRGTILLDVAARADATLIAFTGTNGRITLSLRAGRLDGEQVLGAVGRPEGSSGAGSESGIQHRVLDAEDALGLDDGRPHTIAVTVNETGTHLYADGYECFSTTLTAFLAQIGLTDVRIDPDGIAAVTRLAAWDEPLSDRAVMAQSLPATPLVQFAASELSARDARRTGALATGSIRALLRTRGRGQAGTIVAASGQGGTLHLDIDAGGLSYRVLPGEDSPETEPLIEVRAPGHWDDGTWHDVVVTSGRGAVEIHVDGYQVALVPGGAFLADIAPVTRVVVGADLDGRRLFGEAQTAMIYDAALTDAQVKRLAGAAPLPTRALFDTGYHGARSYRIPSLLTLDSGVILAGADQRVSIPNDAPNDINLVMRRSLDGGATWEEMHTLLSLPGTGALGASLIDSVLVQDRSTGRVICLVDQFPGGIGQPNAAVGTGFDEQGRRVLHNRAGELFAVEPDGSVVTQTGEATDYRVILSGDDAAGVRAGDVLLGGREAGSIYLAHEQAPEDCLFQHRGSHLLMITSDDDGATWSEPIDITAQVKVDWMCFLGTGPGNAIQLTAPEHAGRILAPVYYSHEAGGTAYLSCAAIYSDDGGTTWTLGASPNDGREVLGAVVHSRDLTDERASLYESVLVEGNDGAVHVWARNQHPSGRVAHAVSHDGGVTWGEVDYDEQLPEIFSQPNAIAITGLEGAAAAGDGDGVKGAVGRGIVFANASRMLPFRGCGVLRLSYDDGATWPHNRVINPRHYVYQCMAQLPSGDIALLWEREWQGLFLTTVPLAWLTSSHSTIS$","Exo-alpha-sialidase","Cytoplasm, Extracellular","exo-alpha-sialidase","exo-alpha-sialidase ","Neuraminidase (sialidase)-like","","Sasaki T., Fassler R., Hohenester E. Laminin: the crux of basement membrane assembly. J. Cell Biol. 2004. 164(7):959-963. PMID: 15037599Tisi D., Talts J.F., Timpl R., Hohenester E. Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin. EMBO J. 2000. 19(7):1432-1440. PMID: 10747011Ichikawa N., Kasai S., Suzuki N., Nishi N., Oishi S., Fujii N., Kadoya Y., Hatori K., Mizuno Y., Nomizu M., Arikawa-hirasawa E. Identification of Neurite Outgrowth Active Sites on the Laminin alpha4 Chain G Domain. Biochemistry 2005. 44(15):5755-5762. PMID: 15823034Beckmann G., Hanke J., Bork P., Reich J.G. Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins. J. Mol. Biol. 1998. 275(5):725-730. PMID: 9480764","","","

InterPro
IPR001791
Domain

Laminin G
SM00282	$\"[238-368]T$	LamG

InterPro
IPR002860
Repeat

Glycoside hydrolase, BNR repeat
PF02012	$\"[436-447]T$ $\"[584-595]T$ $\"[651-662]T$ $\"[718-729]T$ $\"[789-800]T$	BNR

InterPro
IPR012680
Domain

Laminin G, subdomain 2
PF02210	$\"[246-348]T$	Laminin_G_2

noIPR
unintegrated

unintegrated
G3DSA:2.120.10.10	$\"[380-834]T$	no description
PTHR10628	$\"[580-724]T$	SIALIDASE
PTHR10628:SF5	$\"[580-724]T$	SECRETED NEURAMINIDASE

","No hits to the COGs database.","***** IPB004124 (Glycoside hydrolase, family 33, N-terminal) with a combined E-value of 4.1e-21. IPB004124A 398-426 IPB004124B 449-488 IPB004124E 652-664 IPB004124F 712-741","","","-51% similar to PDB:2BF6 ATOMIC RESOLUTION STRUCTURE OF THE BACTERIAL SIALIDASE NANI FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH ALPHA-SIALIC ACID (NEU5AC). (E_value = 3.7E_61);-41% similar to PDB:1SLI LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH DANA (E_value = 8.6E_34);-41% similar to PDB:1SLL SIALIDASE L FROM LEECH MACROBDELLA DECORA (E_value = 8.6E_34);-41% similar to PDB:2SLI LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC, THE REACTION PRODUCT (E_value = 8.6E_34);-41% similar to PDB:3SLI LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC PREPARED BY SOAKING WITH 3'-SIALYLLACTOSE (E_value = 8.6E_34);","Residues 246 to 348 (E_value = 4.2e-07) place ANA_1493 in the Laminin_G_2 family which is described as Laminin G domain.Residues 436 to 447 (E_value = 447) place ANA_1493 in the BNR family which is described as BNR/Asp-box repeat.Residues 584 to 595 (E_value = 595) place ANA_1493 in the BNR family which is described as BNR/Asp-box repeat.Residues 651 to 662 (E_value = 662) place ANA_1493 in the BNR family which is described as BNR/Asp-box repeat.Residues 718 to 729 (E_value = 729) place ANA_1493 in the BNR family which is described as BNR/Asp-box repeat.Residues 789 to 800 (E_value = 800) place ANA_1493 in the BNR family which is described as BNR/Asp-box repeat.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1495","1616052","1617008","957","4.67","-24.66","33976","ATGTCCGCCACCTCAGAGAATCGGACTGACACGCCCGCCCAGCCCCGCACCGTGCCCTTCGTCGTCGGCGCCTACCCCATGCTTCCGCCCGACGACGAGGACCGCAGCGGTGCCGCCGCCCTGTACGCCGCGCTGGCCGACCTCGGCTGGGTCGACGGCATCGAGCTGCCCTTCCGGGAGGCCCTGGACGCCCCGGAGCCGTGGCTGGCCGAGCAGCTGGCCGGGCGCTTCGACCAGTGCGTCATCACGGCGATCCCGGGCACCATGGGGCGCGCCGGAGCCGACCCCGTCTTCGGACTGGCCTCCCCCGACGATGGCGGACGCGCTCAGGCACTGGCCTACACCCGCTCGCTGCTGGAGGCCGTCGACCGCCTGCACGAGGCTGCGGGCGAGCGGCTCGTCACCCGGGTGGAGCTGCACTCGGCGCCGCACCACCAGGCCACCCCCGAGGCCTTCCACGCCTCCTTGAGCGAGCTGAGCGAGGACTTCGCCTCCCGCGGCCTGGGGATGATCGTGGAGCACTGCGATGCCGAGGGCGGCGTGGGCCCCTCGGAAAAAGCCTTCCTGACGCTGACCCAGGAGATCGACGCCTGCCGGGACACCGCGGCACTCATCACCGTCAACTGGGGGCGCTCCGTCATCGAGACCCATGACCCGTCCACCCCGGAGAGCCACGTGCGCGAGCTCGTGGAGGCGGGAGTGCTGGGCGGCGTCATGATCTCGGGCGCCGGACCGGAGGAGACGCAGTGGGCCTGGGTGTGGGCCGACGCGCACCTGCCGCTGGCCGAGCACGAGCCGACCAGCTGGCTCACCCCGGAGAGGGTGGCCGCCACAATGCGGGCCGCCGACGGCGCCCAGGTCTACGAGGGCCTCAAGATCAACACTCCGGCGAGCGCCTCCCTGGAGGACAAGCTCGCCTGGGTCAGCCGTGTCCGCGAGACCATGCTCAGTGCCTGA","MSATSENRTDTPAQPRTVPFVVGAYPMLPPDDEDRSGAAALYAALADLGWVDGIELPFREALDAPEPWLAEQLAGRFDQCVITAIPGTMGRAGADPVFGLASPDDGGRAQALAYTRSLLEAVDRLHEAAGERLVTRVELHSAPHHQATPEAFHASLSELSEDFASRGLGMIVEHCDAEGGVGPSEKAFLTLTQEIDACRDTAALITVNWGRSVIETHDPSTPESHVRELVEAGVLGGVMISGAGPEETQWAWVWADAHLPLAEHEPTSWLTPERVAATMRAADGAQVYEGLKINTPASASLEDKLAWVSRVRETMLSA$","Hypothetical protein","Cytoplasm","YiaX1, putative","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1496","1621156","1617134","4023","5.54","-27.23","148568","ATGGAACAACGACGACGGAACGCCCCCAGACCACCACCTGATGAGATTTCACCATCGGAAGTAGGAACTGTGCTCGACGCCAACGTGTTCGACAGGATCCAGCTCGGCCTCGCCACCGCGGAGGACATTCGCTCGTGGTCCCACGGCGAGGTCAAGAAGCCCGAGACCATCAACTACCGCACCCTCAAGCCCGAGAAGGACGGCCTCTTCTGCGAGAAGATCTTCGGCCCCACCCGGGACTGGGAGTGCGCCTGCGGCAAGTACAAGCGCGTGCGCTACAAGGGGATCGTCTGCGAGCGCTGCGGAGTCGAGGTCACTCGCTCCAAGGTGCGTCGCGAGCGCATGGCCCACATCAAGCTCGCCGCGCCGGTCACCCACATCTGGTACTTCAAGGGCGTGCCCTCGCGCCTGGGCTACCTGCTCAACCTCGCGCCCAAGGACCTGGAGAAGGTCATCTACTTCGCGGCCTACATGGTCACCGAGGTGGATGAGGAGGGTCGTCACGACGACCTGCCCTCGCTGCGCAACGAGCTGGAGGTCAAGAAGAAGCACCTCGAGGAGTCCGGCCAGGCCGAGGTCGAGGCGCGCCAGCAGCGCCTCGAGGAGGACCTCGCCCAGCTCGAGTCCGAGGGCGCCGAGGCCTCCCAGCGCGACAAGCTCCGCAAGACCGCCGAGCGCGAGATCACGGCCATGCGCCGCCGCAACCAGCGCGCCCTGGAGCACATGGACAAGGTGTGGGACCGCTTCGTGAGCCTCAAGGTCGGTGACCTGGAGGGTGACGAGGTCCTCTACCGCGACATGGTCGCCGACTACGGCATCTACTTCAAGGGCTCCATGGGTGCCGAGGCCATCCAGGCCCGCCTGCGCAGCTTCGACCTCGAGGCCGAGGCCTCCGCCCTGGCCGAGATCGTCGAGAACGGCACCGGCCAGCGCAAGACCCGCGCCATCAAGCGCCTCAAGGTCGTCAACGCCTTCCGCATGACCGGCACCGCCCCGGAGTCGATGGTCCTGGACAACATTCCGGTCATCCCGCCGGACCTGCGCCCCATGGTCCAGCTCGACGGTGGCCGCTTCGCCACGAGTGACCTCAACGACCTCTACCGCCGCGTCATCAACCGCAACAACCGCCTCAAGCGGCTCATGGACCTGGGCGCCCCGACGATCATCGTCAACAACGAGAAGCGCATGCTTCAGGACGCCGTCGACGCCCTGTTCGACAACGGCCGCCGCGGCCGCCCGGTCACCGGCGTGGGCAACCGTCCGCTGAAGTCCCTGTCCGACATGCTCAAGGGCAAGCAGGGCCGCTTCCGCCAGAACCTCCTGGGCAAGCGCGTGGACTACTCCGGCCGTAGCGTCATCGTCGTCGGCCCCCAGCTCAAGCTCCACCAGTGCGGTCTGCCCAGCCAGATGGCCCTGGAGCTGTTCAAGCCCTTCGTCATGAAGCGGCTCGTCGAGCTCAAGGAGGCCCAGAACGTCAAGGCCGCCAAGCGCATGGTCGAGCGCGCCAACCCCAAGGTCTGGGACGTCCTGGCCGAGGTCATCCGCGAGCACCCCGTGCTGCTCAACCGCGCCCCCACCCTGCACCGCCTGGGCATCCAGGCCTTCGAGCCCCAGCTCATCGAGGGCAAGGCCATCCAGCTGCACCCGCTCGTGTGCGGCGCCTTCAACGCCGACTTCGACGGCGACCAGATGGCCGTCCACCTCCCGCTGGGCGCCGAGGCGCAGGCCGAGGCCCGCATCCTCATGCTGTCCTCGAACAACATCCTCAAGCCCTCCGACGGGCGCCCCGTGACCATGCCCAGTCAGGACATGATCATCGGCACCTACTACCTCACCTCCGACCCCGACCCGGCGGTCGAGGTCGAGCGCGACGCCGAGGGCAACGAGATCGTCCCGGCCTTCTCCTCCTTCGCGGAGGCGGTCATGGCCTACGACTTCGGCAAGCTCCACGTCAACGCCGCCTGCGACATCCGCTTCGAGGAGGGCATCGCCGCTCCCGAGGGCTGGCAGCCGCCCGAGGGCTGGAGTGAGGGCGACCCGATCACCCTGCGCACCTCGCTGGGCCGGGCCCTGTTCAACACCTCGCTGCCCGAGACCTTCCCCTACGTCAACTACATCGTTGACAAGAAGCAGCTGGGCAACATCGTCAACGCCCTGGCGGAGAACTACTCGCGCGTCGAGGTCGCCGCCTCCCTGGACGCCCTCAAGGCCAACGGCTTCTACTGGTCCACCTGGTCCGGTATCACCGTCGCCTTCGCCGACGTCGTCTCCCCGGAGGCCAAGCAGGAGATCCTGGTTCGCTACGAGAACGAGGCCGCTGAAATCGAGGAGCAGTTCGAGCTCGGTGCCCTCACCGAGGACGACCGCTACGCCTCCCTCATCGACATCTGGACCAAGGCCACCGCCGAGGTCGCCGAGGCGATGCGCGAGAACTTCCCGCAGCGCAACACCGTCTACCAGATGGTGGTCTCCGGGGCCCGAGGCAACTGGGACCAGATCCGCCAGCTCGCCGGTATGCGCGGCCTGGTGGCCGACCCCAAGCAGCGCCTCATCGAGCGCCCGATCAAGTCGAACTACCGCGAGGGCCTGAGCGTCCTGGAGTACTTCATCGCCACCCACGGCGCCCGTAAGGGCCTGGCTGACACGGCGCTGCGTACCGCCGACTCCGGCTACCTCACCCGTCGTCTGGTCGACGTCTCCCAGGACGTCATCGTCCGCGAGGAGGACTGCGGCACCCGCAAGGGCCTGACCAAGCGGATCTTCTCCTGGATCGACGCCGGCGACGAGCGCATCAAGGAGCCCTCGGAGATCCTGGGCACCACCGTGTTCGGCACCACCCTGGCGCGCGACGCCATCGACGCCGAGGGCAACCTCATCATCGAGGCCGGCGCTGACCTGGGTGACGCCGAGATTCAGGCCGCCATCGACGCGGGCATCGAGGAGATCACGGTGCGCTCCGTGCTCACCTGCGACTCCAACGTCGGCACCTGCGCCGCCTGCTACGGCCGCTCGCTGGCCACCGGTAAGCGCGTGGACATCGGTGAGGCCGTCGGCATCATCGCCGCCCAGTCCATCGGTGAGCCCGGAACGCAGCTGACCATGCGTACCTTCCACACCGGTGGTGCGGCCGGCGCCGCCGACATCACCCAGGGTCTGCCCCGTGTGCAGGAACTCTTCGAGGCCCGCACCCCCAAGGGCGAGGCCGCCGTGGCCGAGGCCGCCGGCACCCTCAAGATCGAGGACGACGCCGACGGCAAGCGCCTGGTCATCACCCGCGACGACGGTGAGGAGGACGTCATCGTCCCGGTCTCGCGCCGTCAGCGCCTGCTGGTGAACGACGGGGACCACGTCGAGCCCGGCCAGGCCCTCACCGAGGGTCCGGTCGACCCCAAGAAGGTCCTGCGTCTGCGCTCGGTGGCCGCCACCCAGCGCCACCTCGTCGAGGAGGTCCAGGAGGTCTACCGCTCCCAGGGCGTGGACATCCACTCCAAGCACATCGAGGTCATCGTGCGTCAGATGCTGCGCCGCGTGACCGTGCTGGACTCCGGGGACACCCGCCTCCTCCAGGGCGACCTCGTGGACGTCATGCACTACCGCGCCGAGAACCGCCGGGTCATGGCCGAGGGCGGCAAGACCGCCACCGGCCGTACCGAGCTCATGGGAATCACCAAGGCCTCGCTGGCCACGGACTCCTGGCTGAGCGCCGCCTCCTTCCAGGAGACCACCCGCGTGCTCACCGAGGCCGCCATGAACGGCAAGTCCGACCCGCTGCTGGGCCTCAAGGAGAACGTCATCCTCGGTAAGCTCATCCCCGCCGGTACGGGCCTGGCCCGCTACTCGGACATCGAGGTCGAGCCCACCGAGGAGGTCAAGGCGGAGGTCTTCTCCCGCGTGGACCTGGGAGACGGCGTCTTCGGCGAGTCCGTCGCCCTGGACGACTTCCACTTCGGCGGGGACCTGCGTGCGGACTTCTCCGACGACTTCCGCACCGGCTTCTCCAGCAGCGAGGACGTCGAGTTCTGA","MEQRRRNAPRPPPDEISPSEVGTVLDANVFDRIQLGLATAEDIRSWSHGEVKKPETINYRTLKPEKDGLFCEKIFGPTRDWECACGKYKRVRYKGIVCERCGVEVTRSKVRRERMAHIKLAAPVTHIWYFKGVPSRLGYLLNLAPKDLEKVIYFAAYMVTEVDEEGRHDDLPSLRNELEVKKKHLEESGQAEVEARQQRLEEDLAQLESEGAEASQRDKLRKTAEREITAMRRRNQRALEHMDKVWDRFVSLKVGDLEGDEVLYRDMVADYGIYFKGSMGAEAIQARLRSFDLEAEASALAEIVENGTGQRKTRAIKRLKVVNAFRMTGTAPESMVLDNIPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLMDLGAPTIIVNNEKRMLQDAVDALFDNGRRGRPVTGVGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPQLKLHQCGLPSQMALELFKPFVMKRLVELKEAQNVKAAKRMVERANPKVWDVLAEVIREHPVLLNRAPTLHRLGIQAFEPQLIEGKAIQLHPLVCGAFNADFDGDQMAVHLPLGAEAQAEARILMLSSNNILKPSDGRPVTMPSQDMIIGTYYLTSDPDPAVEVERDAEGNEIVPAFSSFAEAVMAYDFGKLHVNAACDIRFEEGIAAPEGWQPPEGWSEGDPITLRTSLGRALFNTSLPETFPYVNYIVDKKQLGNIVNALAENYSRVEVAASLDALKANGFYWSTWSGITVAFADVVSPEAKQEILVRYENEAAEIEEQFELGALTEDDRYASLIDIWTKATAEVAEAMRENFPQRNTVYQMVVSGARGNWDQIRQLAGMRGLVADPKQRLIERPIKSNYREGLSVLEYFIATHGARKGLADTALRTADSGYLTRRLVDVSQDVIVREEDCGTRKGLTKRIFSWIDAGDERIKEPSEILGTTVFGTTLARDAIDAEGNLIIEAGADLGDAEIQAAIDAGIEEITVRSVLTCDSNVGTCAACYGRSLATGKRVDIGEAVGIIAAQSIGEPGTQLTMRTFHTGGAAGAADITQGLPRVQELFEARTPKGEAAVAEAAGTLKIEDDADGKRLVITRDDGEEDVIVPVSRRQRLLVNDGDHVEPGQALTEGPVDPKKVLRLRSVAATQRHLVEEVQEVYRSQGVDIHSKHIEVIVRQMLRRVTVLDSGDTRLLQGDLVDVMHYRAENRRVMAEGGKTATGRTELMGITKASLATDSWLSAASFQETTRVLTEAAMNGKSDPLLGLKENVILGKLIPAGTGLARYSDIEVEPTEEVKAEVFSRVDLGDGVFGESVALDDFHFGGDLRADFSDDFRTGFSSSEDVEF$","DNA-directed RNA polymerase, beta' subunit","Cytoplasm","DNA-directed RNA polymerase, beta' subunit","DNA-directed RNA polymerase; beta' subunit ","DNA-directed RNA polymerase, beta' subunit","","Severinov K., Mustaev A., Kukarin A., Muzzin O., Bass I., Darst S.A., Goldfarb A. Structural modules of the large subunits of RNA polymerase. Introducing archaebacterial and chloroplast split sites in the beta and beta' subunits of Escherichia coli RNA polymerase. J. Biol. Chem. 1996. 271(44):27969-27974. PMID: 8910400Cramer P., Bushnell D.A., Kornberg R.D. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 2001. 292(5523):1863-1876. PMID: 11313498","","","

InterPro
IPR000722
Domain

RNA polymerase, alpha subunit
G3DSA:2.40.40.30	$\"[444-586]T$	no description
PF00623	$\"[442-584]T$	RNA_pol_Rpb1_2

InterPro
IPR006592
Domain

RNA polymerase, N-terminal
SM00663	$\"[333-612]T$	RPOLA_N

InterPro
IPR007066
Domain

RNA polymerase Rpb1, domain 3
PF04983	$\"[587-755]T$	RNA_pol_Rpb1_3

InterPro
IPR007080
Domain

RNA polymerase Rpb1, domain 1
G3DSA:3.90.1120.10	$\"[26-443]T$	no description
PF04997	$\"[27-440]T$	RNA_pol_Rpb1_1

InterPro
IPR007081
Domain

RNA polymerase Rpb1, domain 5
PF04998	$\"[862-1235]T$	RNA_pol_Rpb1_5

InterPro
IPR007083
Domain

RNA polymerase Rpb1, domain 4
PF05000	$\"[784-860]T$	RNA_pol_Rpb1_4

InterPro
IPR012754
Family

DNA-directed RNA polymerase, subunit beta-prime
TIGR02386	$\"[32-1281]T$	rpoC_TIGR: DNA-directed RNA polymerase, bet

InterPro
IPR013222
Domain

Glycosyl hydrolase family 98, putative carbohydrate-binding module
SM00776	$\"[1007-1125]T$	no description

noIPR
unintegrated

unintegrated
PTHR19376	$\"[27-142]T$ $\"[231-1289]T$	DNA-DIRECTED RNA POLYMERASE
PTHR19376:SF4	$\"[27-142]T$ $\"[231-1289]T$	DNA-DIRECTED RNA POLYMERASE BETA CHAIN

","BeTs to 26 clades of COG0086COG name: DNA-directed RNA polymerase beta' subunit/160 kD subunit (split gene in archaea and Syn)Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0086 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB007083 (RNA polymerase Rpb1, domain 4) with a combined E-value of 2.7e-128. IPB007083A 101-127 IPB007083B 332-349 IPB007083C 421-453 IPB007083D 519-537 IPB007083E 555-567 IPB007083F 816-843 IPB007083G 867-905 IPB007083H 1014-1041***** IPB006592 (RNA polymerase I subunit A, N-terminal) with a combined E-value of 6.2e-111. IPB006592A 64-86 IPB006592B 114-129 IPB006592C 332-349 IPB006592D 420-474 IPB006592E 543-582***** IPB007075 (RNA polymerase Rpb1, domain 6) with a combined E-value of 2.5e-28. IPB007075A 848-886 IPB007075B 887-911 IPB007075E 1003-1057 IPB007075I 1247-1282***** IPB000684 (Eukaryotic RNA polymerase II heptapeptide repeat) with a combined E-value of 3.5e-12. IPB000684A 850-904 IPB000684B 1013-1059","","","No significant hits to the PDB database (E-value < E-10).","Residues 27 to 440 (E_value = 7.4e-122) place ANA_1496 in the RNA_pol_Rpb1_1 family which is described as RNA polymerase Rpb1, domain 1.Residues 442 to 584 (E_value = 6.7e-81) place ANA_1496 in the RNA_pol_Rpb1_2 family which is described as RNA polymerase Rpb1, domain 2.Residues 587 to 755 (E_value = 3e-23) place ANA_1496 in the RNA_pol_Rpb1_3 family which is described as RNA polymerase Rpb1, domain 3.Residues 784 to 860 (E_value = 2.8e-22) place ANA_1496 in the RNA_pol_Rpb1_4 family which is described as RNA polymerase Rpb1, domain 4.Residues 862 to 1235 (E_value = 2e-81) place ANA_1496 in the RNA_pol_Rpb1_5 family which is described as RNA polymerase Rpb1, domain 5.","","RNA polymerase, beta subunit (rpoC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1497","1624789","1621268","3522","5.01","-52.59","129017","TTGGCTGCCTCGCGCACCTCCGCACCCACTGCTGCTGACATCGCCGCTCGTACCGCGTCGCGTCGTATCAACTTTGCCAAGATCGCCGAGCCCATGCAGGCTCCGAATCTGCTTGCCCTCCAGACCGAGAGCTTCGACTGGCTCGTCGGTAACGAGAGGTGGCGCGAGCGGATGACCGCCGCCAACAAGGCGCACCCGGGCTCCCTGCCCGAGACCTCCGGTCTGGAGGAGATCTTCGACGAGATCTCCCCGATCGAGGACTTCGGCGAGACCATGGCCCTGTCCTTCCACGACCACCGCTTCGAGGAGCCGAAGTACACGGCCGAGGAGTGCCAGGAGAAGGATCTCACCTACTCCGCCCCGCTCTACGTGGTGGCGGACTTCGAGAACTTCTCCACCGGTGAGATCAAGTCCCAGACCGTCTTCATGGGCGACTTCCCGCTCATGACCGACAAGGGCACCTTCATCGTCAACGGCTCCGAGCGCGTCGTCGTCTCCCAGCTCGTGCGCTCGCCGGGTGTGTACTTCGAGCGCACCACCGAGAAGGCCACGGACAAGTACGTCTACAACGTCAAGTTCATCCCCTCGCGCGGTGCCTGGCTCGAGTTCGAGATCGACAAGTCCGACCGTGTCGCGGTGCGCATCGACCGCAAGCGCAAGCAGGACGTCACCGTCTTTCTGCTGGCCCTGGGCATGGACGAGTCCGAGATCCGCAAGGAGTTCGCCGACTTCCCGGCCCTGACCTCCGCCCTGGACGAGGACCGCAAGATCACCACCCAGGACGAGGCGCTCCTGGACATCTACAAGAAGATCCGCCCCGGTGAGCCGCCGAGCGTCGAGGCCGGTCGCACCCTGCTGGAGAACTTCTACTTCAACCCCAAGCGCTACGACCTGGCCAAGGTCGGCCGCTACAAGATCAACAAGAAGCTGGGCCTGGCCTCGGATCTGACCGAGTCCACCCTACGCATCGAGGACATCGTCGCCGCTCTGCGCTACCTGCTGGCCCTGCACTCCGGCGCCGAGACCGTCGAGGGCGTGCGCGACGGCGAGATCACCGAGATCGCCGTCGAGTACGACGACATCGACCACCTGGGCAACCGCCGCATCCGCGCGGTGGGCGAGCTCATCCAGGCGCAGGTGCGCACCGGTATGAGCCGTATGGAGCGTCAGGTGCGCGAACGCATGACCACCCAGGACGTCGAGGCCATCACGCCGAACACCCTCATCAACATCCGGCCCGTGACGGCCGCGATCAAGGAGTTCTTCGGCACCTCCCAGCTCAGCCAGTTCATGGACCAGAACAACCCGCTGGCGGGCCTGACCCACAAGCGCCGCCTGAGCGCCCTGGGCCCCGGCGGTCTGTCCCGTGAGCGCGCCTCCATGGAGGTCCGCGACGTCCACACCTCGCACTACGGGCGCATGTGCCCCATCGAGTCCCCCGAGGGCCCCAACATCGGCCTCATCGGCTCGCTGGCGACCTTCGGGCGCATCAACCCCTTCGGCTTCGTCGAGACCCCCTACCGCGTCGTCGTCGACGGCCAGGTCACCGACGAGACGCACTACCTGACGGCCGACGACGAGGACCGCCACGTCATCGCCCAGGCCAACGTCGCCCTCACCGAGGACGGCCACTTCGCCGAGGACCACGTCCTGTGCCGCGTCACCGGCGGTGAGCCGGCCCTCGTGCCCTCCTCGCAGGTGGACCTCATGGACGTCTCCCCGCGCCAGATGGTGTCGGTGGGTACCTCCCTCATCCCCTTCCTCGAGCACGACGACGCCAACCGCGCCCTCATGGGCGCCAACATGCAGCGCCAGGCCGTGCCGCTCATCCGCCCCGACGCCCCGCTGGTGGGCACGGGCATGGAGCGGCGCACCGCCGTCGACGCCGGTGACGTCCTCGTGGCCGACAAGGCCGGTGTCGTCACCGAGGTCTGCGCGGACTTCGTGCGCGTGGCCAACGACGACGGCACCGAGATCGTCTACAAGGTCGCCAAGTTCCGCCGCTCCAACCAGGGCAACTGCTACAACCAGCGGGTCGTGGCCACCGAGGGCGAGCGCGTCGAGGTCGGCACGGTCCTGGCCGACGGCCCCGCCACCAACGAGGGCGACCTGGCCCTGGGCCAGAACCTCCTGGTCGCCTTCATGACCTGGGAGGGCCTCAACTACGAGGACGCCATCATCATCTCCCAGCGCGTGGTCGCCGAGGACATGCTCACCTCGATCCACATCGAGGAGCACGAGGTCGACGCCCGCGACACCAAGCTGGGCGCCGAGGAGATCACCCGCGACATCCCCAACGTCAGCGAGGAGACCCTGGCCAACCTCGACGAGCGCGGCATCATCCGCATCGGCGCCGAGGTCCGCAGCGGCGACATCCTCGTGGGCAAGGTGACCCCCAAGGGGGAGACCGAGCTGACCAGCGAGGAGCGCCTCCTGCGCGCCATCTTCGGTGAGAAGGCCCGCGAGGTGCGCGACACCTCCCTGCGCGTGCCCCACGGCGAGTACGGCATCGTCACCGGCGTGCGTGAGATCGACGCCGCCTCCGACGACGCCGAGCTGCCTGCGGGCGTCAACCGCATGGTGCGCGTCTACATCGCCCAGCGCCGCAAGATCACCGTCGGTGACAAGCTCTCCGGCCGTCACGGCAACAAGGGCGTCATCTCCAAGATCCTGCCCGTGGAGGACATGCCCTTCCTGGCCGACGGCACCCCGGTCGACGTCATCCTCAACCCGCTGGGCGTGCCCAGCCGTATGAACGTCGGACAGGTCCTCGAGCTGCACCTGGGATGGGTCGCCTCCCGCGGCTGGGACGCCACCGCCGCCCGCGAGGCCGGCGAGGCCTGGACCGCCAACCTGCCCGAGAACGGCATCAAGGCCGAGCCCCGCACGCCCGTGGCCACGCCCGTCTTCGACGGCGTGCGGGACAACGAGCTCATGGGGCTGCTGGGCTCCACGCTGCCGACCTCCGACGGCCTGCAGCTGGTCGAGCCCAACGGCAAGGCCCGCCTGTTCGACGGCCGCTCCGGTGAGCCCTTCCCGTACCCCATCTCGGTGGGCTACATGTACATCCTCAAGCTCCACCACCTCGTGGACGACAAGATCCACGCCCGCTCCACGGGTCCGTACTCCATGATCACCCAGCAGCCGCTGGGTGGTAAGGCCCAGTTCGGTGGTCAGCGCTTCGGTGAGATGGAGGTGTGGGCCATGGAGGCGTACGGCGCCGCCCACGCCCTCCAGGAGCTCCTCACCGTCAAGTCCGACGACGTCAACGGCCGCGTCAAGGTCTACGAGGCCATCGTCAAGGGCGAGGACATCCCCGAGCCCGGCATCCCCGAGTCCTTCAAGGTGCTCATGAAGGAGATGCAGTCGCTGTGCCTGAACGTCGAGGCCCTGGACGCCGAGGGCGTCGCCATCGCCCTGGACGACACCGACGACGACGGCTCGCGCGCCGCCGATGAGCTCGGCTTCGACCTGGGCCGGCGTCCGGGCGGGGCCATGGCCTCCACGGTTGACGAGATCTGA","LAASRTSAPTAADIAARTASRRINFAKIAEPMQAPNLLALQTESFDWLVGNERWRERMTAANKAHPGSLPETSGLEEIFDEISPIEDFGETMALSFHDHRFEEPKYTAEECQEKDLTYSAPLYVVADFENFSTGEIKSQTVFMGDFPLMTDKGTFIVNGSERVVVSQLVRSPGVYFERTTEKATDKYVYNVKFIPSRGAWLEFEIDKSDRVAVRIDRKRKQDVTVFLLALGMDESEIRKEFADFPALTSALDEDRKITTQDEALLDIYKKIRPGEPPSVEAGRTLLENFYFNPKRYDLAKVGRYKINKKLGLASDLTESTLRIEDIVAALRYLLALHSGAETVEGVRDGEITEIAVEYDDIDHLGNRRIRAVGELIQAQVRTGMSRMERQVRERMTTQDVEAITPNTLINIRPVTAAIKEFFGTSQLSQFMDQNNPLAGLTHKRRLSALGPGGLSRERASMEVRDVHTSHYGRMCPIESPEGPNIGLIGSLATFGRINPFGFVETPYRVVVDGQVTDETHYLTADDEDRHVIAQANVALTEDGHFAEDHVLCRVTGGEPALVPSSQVDLMDVSPRQMVSVGTSLIPFLEHDDANRALMGANMQRQAVPLIRPDAPLVGTGMERRTAVDAGDVLVADKAGVVTEVCADFVRVANDDGTEIVYKVAKFRRSNQGNCYNQRVVATEGERVEVGTVLADGPATNEGDLALGQNLLVAFMTWEGLNYEDAIIISQRVVAEDMLTSIHIEEHEVDARDTKLGAEEITRDIPNVSEETLANLDERGIIRIGAEVRSGDILVGKVTPKGETELTSEERLLRAIFGEKAREVRDTSLRVPHGEYGIVTGVREIDAASDDAELPAGVNRMVRVYIAQRRKITVGDKLSGRHGNKGVISKILPVEDMPFLADGTPVDVILNPLGVPSRMNVGQVLELHLGWVASRGWDATAAREAGEAWTANLPENGIKAEPRTPVATPVFDGVRDNELMGLLGSTLPTSDGLQLVEPNGKARLFDGRSGEPFPYPISVGYMYILKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMEVWAMEAYGAAHALQELLTVKSDDVNGRVKVYEAIVKGEDIPEPGIPESFKVLMKEMQSLCLNVEALDAEGVAIALDDTDDDGSRAADELGFDLGRRPGGAMASTVDEI$","DNA-directed RNA polymerase, beta subunit","Cytoplasm","DNA-directed RNA polymerase, beta subunit","DNA-directed RNA polymerase beta chain ","DNA-directed RNA polymerase, beta subunit","","Falkenburg D., Dworniczak B., Faust D.M., Bautz E.K. RNA polymerase II of Drosophila. Relation of its 140,000 Mr subunit to the beta subunit of Escherichia coli RNA polymerase. J. Mol. Biol. 1987. 195(4):929-937. PMID: 3116266","","","

InterPro
IPR007120
Domain

RNA polymerase Rpb2, domain 6
PF00562	$\"[632-1055]T$	RNA_pol_Rpb2_6

InterPro
IPR007121
Family

RNA polymerase, beta subunit
PS01166	$\"[874-886]T$	RNA_POL_BETA

InterPro
IPR007641
Domain

RNA polymerase Rpb2, domain 7
PF04560	$\"[1057-1133]T$	RNA_pol_Rpb2_7

InterPro
IPR007642
Domain

RNA polymerase Rpb2, domain 2
PF04561	$\"[170-355]T$ $\"[359-370]T$	RNA_pol_Rpb2_2

InterPro
IPR007644
Domain

RNA polymerase beta subunit
PF04563	$\"[36-425]T$	RNA_pol_Rpb2_1

InterPro
IPR007645
Domain

RNA polymerase Rpb2, domain 3
PF04565	$\"[429-498]T$	RNA_pol_Rpb2_3

InterPro
IPR010243
Family

DNA-directed RNA polymerase, beta subunit
TIGR02013	$\"[18-1130]T$	rpoB: DNA-directed RNA polymerase, beta sub

noIPR
unintegrated

unintegrated
G3DSA:2.40.270.10	$\"[699-1041]T$	no description
G3DSA:2.40.50.100	$\"[632-696]T$	no description
G3DSA:3.90.1100.10	$\"[20-631]T$	no description
PTHR20856	$\"[405-964]T$ $\"[987-1152]T$	DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2
PTHR20856:SF3	$\"[405-964]T$ $\"[987-1152]T$	DNA-DIRECTED RNA POLYMERASE BETA CHAIN

","BeTs to 26 clades of COG0085COG name: DNA-directed RNA polymerase beta subunit/140 kD subunit (split gene in Mjan, Mthe, Aful)Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0085 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB007120 (RNA polymerase Rpb2, domain 6) with a combined E-value of 2.7e-243. IPB007120A 149-176 IPB007120B 359-379 IPB007120C 420-459 IPB007120D 464-488 IPB007120E 579-608 IPB007120F 668-679 IPB007120G 702-733 IPB007120H 790-800 IPB007120I 874-915 IPB007120J 1040-1087***** IPB007121 (RNA polymerase, beta subunit) with a combined E-value of 7.5e-240. IPB007121A 149-176 IPB007121B 359-379 IPB007121C 421-454 IPB007121D 464-488 IPB007121E 582-608 IPB007121F 668-679 IPB007121G 702-733 IPB007121H 790-800 IPB007121I 874-915 IPB007121J 1040-1087***** IPB007646 (RNA polymerase Rpb2, domain 4) with a combined E-value of 1.7e-47. IPB007646C 705-736 IPB007646D 772-799 IPB007646E 893-925 IPB007646F 1032-1082***** IPB007647 (RNA polymerase Rpb2, domain 5) with a combined E-value of 7.9e-47. IPB007647B 464-482 IPB007647C 571-625 IPB007647D 705-736 IPB007647E 895-925 IPB007647F 1016-1070***** IPB009674 (RNA polymerase I, Rpa2 specific) with a combined E-value of 1.3e-36. IPB009674N 706-744 IPB009674O 772-798 IPB009674P 866-902 IPB009674Q 903-948 IPB009674S 1017-1051 IPB009674T 1052-1102","","","No significant hits to the PDB database (E-value < E-10).","Residues 36 to 425 (E_value = 2.2e-40) place ANA_1497 in the RNA_pol_Rpb2_1 family which is described as RNA polymerase beta subunit.Residues 170 to 355 (E_value = 8.4e-25) place ANA_1497 in the RNA_pol_Rpb2_2 family which is described as RNA polymerase Rpb2, domain 2.Residues 359 to 370 (E_value = 5.1e-05) place ANA_1497 in the RNA_pol_Rpb2_2 family which is described as RNA polymerase Rpb2, domain 2.Residues 429 to 498 (E_value = 2.5e-38) place ANA_1497 in the RNA_pol_Rpb2_3 family which is described as RNA polymerase Rpb2, domain 3.Residues 632 to 1055 (E_value = 2.5e-190) place ANA_1497 in the RNA_pol_Rpb2_6 family which is described as RNA polymerase Rpb2, domain 6.Residues 1057 to 1133 (E_value = 1.3e-50) place ANA_1497 in the RNA_pol_Rpb2_7 family which is described as RNA polymerase Rpb2, domain 7.","","RNA polymerase, beta subunit (rpoB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1499","1625424","1624870","555","9.49","8.94","18966","GTGGACGGGACCCGGTCGTGTTCCGGGGGCCTGGTGCTGTCCGGCCTCTGTGCGCTTCGACGTCGTCGGGCTCGGGGCGGTGGGGGATCGGGGACGTACATATGCGCCGAGGACTGCGATGTCCTCCAGGTCACTGAGGTCCGTCCCCAGTGGTCTGGAGGAGAACGCAGTCGCCGATCGGAAAGTACGTTCCCGACGCCGTCGGCCGGACAGGATCGGGTGGGCGCAGAGGCTGCGGGGCCGAGGACGTGCAGGGCTGTGGGGCCAGGGGAGTGGGTGGCTGGGCGGCAGCGCGCGGGGGCTGGGTGTGCCGGGCGCGAGCCGGCCGGCACCCCTCAGTCGATGGGCCGCACCGAGGGACTCAGGTCACGCGACGGCCACGGGTGGGGCAGTATGCGCGACTGTGGTGGGAATCGCAAGGAACCAGTGGGTATCGGCGTGGAGTCCTTGACGTCGGCCGTGTACGCTAGCGCTTTGCGTGCATTGTGTGTATTGGTGAGAGGAGTATCTGCCCTCCGCGCGGGTCCCGGCCCGTCGGAACCCTGGCGGGCGTGA","VDGTRSCSGGLVLSGLCALRRRRARGGGGSGTYICAEDCDVLQVTEVRPQWSGGERSRRSESTFPTPSAGQDRVGAEAAGPRTCRAVGPGEWVAGRQRAGAGCAGREPAGTPQSMGRTEGLRSRDGHGWGSMRDCGGNRKEPVGIGVESLTSAVYASALRALCVLVRGVSALRAGPGPSEPWRA$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1500","1625896","1625507","390","4.54","-11.04","13423","ATGGCGAAGCTGACCACCGAAGAGCTCATCGAGCAGTTCAAGGAGCTCACCCTCATCGAGCTGTCCGAGTTCGTCAAGGCCTTCGAGGAGACCTTCGACGTTACCGCCGCCGCTCCGGCCGCCGTGGCCGTTGCCGCCGCCCCCGGCGCTGCCGGTGGCGACGCCGCCGCCGAGGAGAAGGACGAGTTCGACGTCATTCTCGAGGCCGCCGGCGACAAGAAGATCCAGGTCATCAAGGAGGTGCGCGCCCTGACCTCCCTCGGCCTGAAGGAGGCCAAGGAGCTCGTTGACGGCGCTCCCAAGCCCGTCCTCGAGGGCGCCAACAAGGAGGCCGCCGAGAAGGCCAAGGAGCAGCTCGAGGGCGCCGGCGCCACCGTCACCCTCAAGTGA","MAKLTTEELIEQFKELTLIELSEFVKAFEETFDVTAAAPAAVAVAAAPGAAGGDAAAEEKDEFDVILEAAGDKKIQVIKEVRALTSLGLKEAKELVDGAPKPVLEGANKEAAEKAKEQLEGAGATVTLK$","Ribosomal protein L7/L12","Cytoplasm","ribosomal protein L7/L12","K02935 large subunit ribosomal protein L7/L12","ribosomal protein L7/L12","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Uchiumi T., Hori K., Nomura T., Hachimori A. Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding. J. Biol. Chem. 1999. 274(39):27578-27582. PMID: 10488095","","","

InterPro
IPR000206
Family

Ribosomal protein L7/L12
TIGR00855	$\"[1-129]T$	L12: ribosomal protein L7/L12

InterPro
IPR013823
Domain

Ribosomal protein L7/L12, C-terminal
PD001326	$\"[70-129]T$	Q6A6K5_PROAC_Q6A6K5;
PF00542	$\"[62-129]T$	Ribosomal_L12

InterPro
IPR014719
Domain

Ribosomal protein L7/L12, C-terminal/adaptor protein ClpS-like
G3DSA:3.30.1390.10	$\"[56-129]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.20.5.710	$\"[3-54]T$	no description
PTHR11809	$\"[7-129]T$	RIBOSOMAL PROTEIN L7/L12

","BeTs to 19 clades of COG0222COG name: Ribosomal protein L7/L12Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0222 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000206 (Ribosomal protein L7/L12) with a combined E-value of 1e-53. IPB000206A 7-38 IPB000206B 58-67 IPB000206C 73-113","","","-59% similar to PDB:1DD3 CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 FROM THERMOTOGA MARITIMA (E_value = 8.4E_15);-59% similar to PDB:1DD4 Crystal structure of ribosomal protein l12 from thermotoga maritim (E_value = 8.4E_15);-59% similar to PDB:1GIY CRYSTAL STRUCTURE OF THE RIBOSOME AT 5.5 A RESOLUTION. THIS FILE, 1GIY, CONTAINS THE 50S RIBOSOME SUBUNIT. THE 30S RIBOSOME SUBUNIT, THREE TRNA, AND MRNA MOLECULES ARE IN THE FILE 1GIX (E_value = 8.4E_15);-59% similar to PDB:1YL3 Crystal structure of 70S ribosome with thrS operator and tRNAs. Large subunit. The coordinates for the small subunit are in the pdb entry 1YL4. (E_value = 8.4E_15);-57% similar to PDB:1RQU NMR structure of L7 dimer from E.coli (E_value = 1.0E_12);","Residues 62 to 129 (E_value = 8.4e-38) place ANA_1500 in the Ribosomal_L12 family which is described as Ribosomal protein L7/L12 C-terminal domain.","","protein L7-L12 (rplL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1501","1626481","1625960","522","6.85","-0.05","18116","ATGGCACGGCCTGACAAGGAAGCAGCCGTTGCTGCGCTGGCGGACAAGTTCCGCCAGGCTGACGCGGTCCTGCTGACTGAGTACCGGGGACTGAGCGTCGCCCAGCTCAAGGAGCTGCGTCGTTCCCTCGCCGGTAACGCCGAGTACACCGTGGTGAAGAACACGCTTGCTGCGATCGCCGCCCGCCAGGTCGGGCTCGAGGACTTCGCCGACGACCTCACGGGCCCCTCCGCCCTGACGTTCGTCACCGGTGAGCCGGTCGAGGCCGCCAAGGCTCTGCGTGACTTCGCCAAGGACAACCAGCAGCTCGTCATCAAGGGCGGTGTCATGGACGGCGCCGTGCTGTCCGCCGACGGCGTTGACAAGCTTGCCTCTCTCGAGTCCCGCGAGGTGCTGCTCGCCAAGACCGCGGGCGCCATCAAGGCGTCCCTGTCCAAGGCTGCGTACCTCTTCGCCGCACCGGCCTCCAAGGCCGTGCGCACCGTCGACGCCCTGCGCGAGAAGCAGGAGACCGCGGCCTGA","MARPDKEAAVAALADKFRQADAVLLTEYRGLSVAQLKELRRSLAGNAEYTVVKNTLAAIAARQVGLEDFADDLTGPSALTFVTGEPVEAAKALRDFAKDNQQLVIKGGVMDGAVLSADGVDKLASLESREVLLAKTAGAIKASLSKAAYLFAAPASKAVRTVDALREKQETAA$","Ribosomal protein L10","Periplasm, Cytoplasm","50S ribosomal protein","50S ribosomal protein L10","ribosomal protein L10","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR001790
Family

Ribosomal protein L10
PF00466	$\"[1-98]T$	Ribosomal_L10

InterPro
IPR002363
Family

Eubacterial ribosomal protein L10
PS01109	$\"[6-40]T$	RIBOSOMAL_L10

","BeTs to 20 clades of COG0244COG name: Ribosomal protein L10Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0244 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002363 (Eubacterial ribosomal protein L10) with a combined E-value of 2.6e-26. IPB002363A 20-58 IPB002363B 95-112 IPB002363C 123-136","","","-56% similar to PDB:1ZAV Ribosomal Protein L10-L12(NTD) Complex, Space Group P21 (E_value = 2.3E_21);-56% similar to PDB:1ZAW Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form A (E_value = 2.3E_21);-56% similar to PDB:1ZAX Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B (E_value = 2.3E_21);","Residues 1 to 98 (E_value = 5.2e-32) place ANA_1501 in the Ribosomal_L10 family which is described as Ribosomal protein L10.","","ribosomal protein (rplJ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1503","1627235","1626753","483","4.16","-23.32","16789","ATGCGCATCTACCTGCCCGCCACCGCCGCCCACCTGCGCGCAAGCGTCCTGGGCTCCTCGCACCAGCCGCTCACGGCTCACGCCGCCACTCCCGCTCTTGCTCAGGCCCTGCCCGAGGAGGATGAGGAGGGCCTGGAGGTCTCCGCCTCACTGTGCGCCGCCGACGCCTCCGTCGTCCTGCTGGCCGAGCCCGAGGCCACGGGACTGGCCGACCGGCGCATCGTCATCGCGGCCGACGTCGAGGCCGAGAACGTGCGCGAGCTTCCCGTGGAGGGCGATGTGCTGCCCGGCACGATCGAGGTCACCGGCGAGATCTCCTGGGAGGACGTGGCCGCCCTGCTCGTGGACGCGCCCGAGGCTCAGGCCGACGTGCGGGCCGCCCGGCTCGGAGACGAGGACGCCTTCGAGCGCGCCGCCGAGGCCGATCTGCTCTGGTACGACGTCACGGAGCGGGAGGCACTGGCCGAGAGCCTCGGTGTCTGA","MRIYLPATAAHLRASVLGSSHQPLTAHAATPALAQALPEEDEEGLEVSASLCAADASVVLLAEPEATGLADRRIVIAADVEAENVRELPVEGDVLPGTIEVTGEISWEDVAALLVDAPEAQADVRAARLGDEDAFERAAEADLLWYDVTEREALAESLGV$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1504","1629323","1627320","2004","5.79","-7.43","69518","GTGAACGCCCCGGGGGCCGGACTCCTCCTGGCTCTCAGTGGCGACGACGCCGACATCCTGCGGGCGCTGAGCCAGGCGGGAAGCGGGCTGTGCGTCGTGCGCCGATGCGCCGACCTGCCCGAGCTGCTCTCAGCGGGGATGGCCGGACTGGCGAGCTTCGCCCTGCTGGACACCGGATTCGACGAGATCGACCGCACCGTCCTGGATCGCCTCGCGCGCGCTGGCCTGAGCGGTCTGCTCCTGGTGGAGAGCCACGAGGAGGAGCGCTGGCGCAGTGCGGGATGGCCGGTTCTCAGACGCGACACGGAGCCTGGCCGCATCTGCTCGGCGCTGCAGGACCTCGTGCGTCGCGGCGGAGCCTCCAGCACGGTCTCCGCCGGGCCGGAGGACACGAGCACCGACTGGCTGAGCGCCACCACCCCCGCTTCGACGGACTCGAACGCCGCCGCTCAGGAGGCCGCCTGGCTCGAAGAGCTGTGGCGTCAGTCGCCCGACTCCCCGGAGGGTGGAACCGCGTTCTCGCAGCCGCCCCCGACCTCCCCTGAGACCGCAGGCGGGCAGGGCCCGAGGCAGAGCCCGCGGCGCGACCGGGAGCCGGCAGCCATGGATATGCCGGAGCCCGCCTTCCCGGATGTGATGAGTCGGGCGGATGATGAGCCTGACGGGAGGATCGTCCTGGTGTGGGGGCCGCATGGCGCTCCCGGGCGCTCGACGGTCTCCGCCTCCCTCGCCCACGGCCTGGCCGCCTGTGGCGGTGCGATTCTCGTGGATGCCGATGTCGAGGCTCCCAGCCTCGTCCAGCTCCTCGGCATGCCGGAGGACTCCTCGGCCCTGGCCGGAGCGGCCCGCCTGGCCACCCACGGCCGTCTCGACGCCGAGAGCTTCCGACGGGTCCTGGCGCCGGTGGGCGACGAGCTCTTCCTGCTGGGCGGTCTGGGGAGGTCCGGGCGCTGGCGTGAGCTGCCACCGGCCTCGATGACCGAGGTATGGGCGCAGTGCCGTCGGGCCGCGGCCTGGACCGTCGTCGACGTCGCCGGCGGGCCCGTCGATAACGACGTCGATGACTTCACCCTCGAGCCCGGGCGTGGGGCCGTGACGGCCGACCTGGTATCGCACGCTGACGTCATCCTGGTCGTCGGCGGGGCCGACCCCGTCGGGGTGCGCCGCCTGCTCCAGCTCCTCGATGAGATGGGGGCCTCCATGAACCCCGCCGGCCGGGTCGAGGTCGTCATCAACCGGGTGCGGGCCTCGGCCGCAGGGCCCTCTCCCCAGCAGGCTCTGCGAGAGGCGCTGGCGCGCTTCGGTGGACTGGAGGACATTGTGCTCCTGCCCGACGACGCGGCGACGGCCGATGCCTGTCTGCTCCAGGGCTGCACTGTCCTGGAACAGGCTCCCGCCAGCGCACTGGGCAAGGCCCTCAGCGTACTGGTCGACCGTATCGATCCGAGGGTGGCTGCGGCCCGCAGGACTCGCTCCCCGCGTCGTTCCCTGTTGCGGCGCTCCAAGAGGCGCGGTGGGCGTCGGGAGCGCGGGGACTCCGAGGCTCGGGCCACAACCGCCAGAAGCAGGAGTCGCTCACGTACGGGCCGTGCGGCGGCCAGGAACCGCCGAGGCGGGGACGGGGGGCAGCCGGTTGGTCAACGAGTGCCGGCTGCCCAGGCGCCTAGTGGACCCACTCAGGTTCCGCCGCAGTTCCCTCCGGGCCTGCCGCCGTCGATCCAGCCCATGAATCAGCAGGTGAACCAGCTGCCGGGGCGGCCGCCGGAACCGCCTCCGAGCAGCCCGCTGGCTCAGACGCCGCCACCGGAGCAGGGGCCGGCCCCCGGCTCGCCGCACCGGCCGTGGGTGGCGCCTTGGCCGGGTGCGGCAACGGCGTCGGACGCAGCAACGCCCCCGGGGCAGGTGCGAGGCCCGGATGACGGCCGCGACCAGGCCGGGAGGAACGATGAGGGTACGGGCGGCCCTCCACCGGTGCCGCCGGGGACCGGGCGACACCGCTACTGA","VNAPGAGLLLALSGDDADILRALSQAGSGLCVVRRCADLPELLSAGMAGLASFALLDTGFDEIDRTVLDRLARAGLSGLLLVESHEEERWRSAGWPVLRRDTEPGRICSALQDLVRRGGASSTVSAGPEDTSTDWLSATTPASTDSNAAAQEAAWLEELWRQSPDSPEGGTAFSQPPPTSPETAGGQGPRQSPRRDREPAAMDMPEPAFPDVMSRADDEPDGRIVLVWGPHGAPGRSTVSASLAHGLAACGGAILVDADVEAPSLVQLLGMPEDSSALAGAARLATHGRLDAESFRRVLAPVGDELFLLGGLGRSGRWRELPPASMTEVWAQCRRAAAWTVVDVAGGPVDNDVDDFTLEPGRGAVTADLVSHADVILVVGGADPVGVRRLLQLLDEMGASMNPAGRVEVVINRVRASAAGPSPQQALREALARFGGLEDIVLLPDDAATADACLLQGCTVLEQAPASALGKALSVLVDRIDPRVAAARRTRSPRRSLLRRSKRRGGRRERGDSEARATTARSRSRSRTGRAAARNRRGGDGGQPVGQRVPAAQAPSGPTQVPPQFPPGLPPSIQPMNQQVNQLPGRPPEPPPSSPLAQTPPPEQGPAPGSPHRPWVAPWPGAATASDAATPPGQVRGPDDGRDQAGRNDEGTGGPPPVPPGTGRHRY$","Hypothetical protein","Extracellular, Membrane","hypothetical protein","ATPases involved in chromosome partitioning-like","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[223-480]T$	no description

","BeTs to 15 clades of COG0489COG name: ATPases involved in chromosome partitioningFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0489 is aompkzyqvdr-bcefghsnujx---Number of proteins in this genome belonging to this COG is 3","***** IPB001359 (Synapsin) with a combined E-value of 2.7e-07. IPB001359H 588-638 IPB001359H 558-608 IPB001359H 562-612","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1505","1630087","1629320","768","6.07","-1.55","25687","ATGTCATCTCGCCGCAGCCGTTCCCTGACCGCTCCCGAGCGTCCCCGCGGCGGTCGTTGGCGCCGTCCTGCCTGGAAGGACCCGCGCATGGCCGGGGGAGTGGTGCTGGTGGCCGCTGCCGTGGCCATGGGGGCCTGGGCGGTCGACGCGGCCGCCGACACCACTCGCGTCTATGTGCTCTCCCAGGATGTCGCTCCCGGGGCAGACCTCACTGCCGACGGCGTTCTCACGGTGGTCGAGGCCCATCCCGGCACCGACGCCTATGTCGAGGCCGGGCACCTGCCGGACGGTGCCGTGTCCACGCGCTCCATGCGCAAGGGGGAGCTGCTGGCCGCGGCGGCCGTCAACAGCGGTCGGGAGCAGGACCTGCGGCCGGTGGTCCTCAATGTCGCCTCCAACCTGCCGGCCTCGACCAAGGTCGGCGACTATGTCGATCTGTGGGTTGTGCCCAAGGAGGGCGTGGCGGGCCGCCCCGCGGCCCAGGCGTCCGCCACCGCGCAGGCAGGACAGGACGGACAGAGTGCTCAGAGCAGTCCAGGAGACCAGTCGGGACAGGCCGAGGGGACCGGAGCCCGCCGCGTGGCCACAGGGCTGGTGATCGCCTCGGTCGGTGAGACCAGTAGGGGGCTGATCTCCGGGCCCGGCACCGGGGTGGAGGTCAAGGTCCCCGAGGCCTCCCTCGCCGCCGTCCTCAGCGCCGTCGGGCAGGAGGGGGCGCTCGTCCTGGTTCCCACCGGCCAGGAAGCACCGGCGGAGAAGGCCTCGTGA","MSSRRSRSLTAPERPRGGRWRRPAWKDPRMAGGVVLVAAAVAMGAWAVDAAADTTRVYVLSQDVAPGADLTADGVLTVVEAHPGTDAYVEAGHLPDGAVSTRSMRKGELLAAAAVNSGREQDLRPVVLNVASNLPASTKVGDYVDLWVVPKEGVAGRPAAQASATAQAGQDGQSAQSSPGDQSGQAEGTGARRVATGLVIASVGETSRGLISGPGTGVEVKVPEASLAAVLSAVGQEGALVLVPTGQEAPAEKAS$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[30-50]?$	transmembrane_regions

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PF00376	$\"[7-44]T$	MerR

InterPro
IPR010093
Domain

Excisionase/Xis, DNA-binding
TIGR01764	$\"[5-55]T$	excise: DNA binding domain, excisionase fam

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 48 to 85 (E_value = 0.0072) place ANA_1506 in the MerR family which is described as MerR family regulatory protein.","","binding domain, excisionase family protein","","1","","","Mon Aug 6 17:05:26 2007","","Mon Aug 6 17:05:26 2007","","","Mon Aug 6 17:05:26 2007","Mon Aug 6 17:05:26 2007","Mon Aug 6 17:05:26 2007","","","Mon Aug 6 17:05:26 2007","","","Mon Aug 6 17:05:26 2007","","","","Mon Aug 6 17:05:26 2007","Mon Aug 6 17:05:26 2007","","","","","yes","","" "ANA_1508","1630845","1631156","312","11.03","7.58","11393","GTGGATGAGTCGGCCCACCGAGCCTCGCAAGCGGTCGACGACCGCGATGGAGGCCTGCTCCGCCTCCGCCAGCTCGGCACTCTGCGCCACCAGGTCCGCACGGCGCTCAGCATCGAAGCTGCTCTCCAGGTCGGCAATCATCGCGTCCCAGTCCATGAACCCACCTCACCACAGTCCGCCCGCCGAGGAAAGCACTCCGAGGCGGCTCACGCCGCGCTCCGCCAGCACCAGAGACCTCCACTACCACGATTCAGGGCCAAGACATGTCTCATCGTCACTATTGACATCATCACATCACAGGCGTACACCTAA","VDESAHRASQAVDDRDGGLLRLRQLGTLRHQVRTALSIEAALQVGNHRVPVHEPTSPQSARRGKHSEAAHAALRQHQRPPLPRFRAKTCLIVTIDIITSQAYT$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1509","1631193","1632023","831","5.26","-6.70","27217","ATGGGGGCTCGTCAACGGCTGACACTCCTGGCCTGCGCGTCAGGAGCTGTCCTGATCCTTCTGGGACGCACGGCTCACAGCGCGGCGGAGCAGCTCGCGACGGTCCCACCGCAGTCCTGGGGGCTGAGCGAGCTGTCCGACGCCGTCGTCGCCGGGACCTGTGCATGCGGGACCCTGGGCGCCCTGTGGCACGTGGTCTCCGCTCTCGTGGCCCTTATGGCGCTTGCCGGGGAGAAGGGGCCCGGCCCCCATGGTCTTGGCGGCACCTCCACGCTGGCGGCCAGAGTCCTGGCGACCTGGGGAGCGCCTGCAGTCAGACGCATCACCGCCTCAGCGCTGCTCGTCTCCCTGTCCTCGGCGCCCGCGCTGGCCACTCAAGAGACCGGCGGCGGGGACGATCTGGGATGGCGCCCCACCAGCTCGGCGCCCGCCTCACCGTCGTCGCAGTCCTCGACGCCGTCGCCGCCTGAGCAGTCCCCGTCGAGCGCTTCGACCGGTTCTGGCGACTCGGAGGACGCAAGCCAGTCAGCGGACTCGACGCCGCCGGGCAGCCAGACGCCGCAGCCCCCTACCGGCCCCGACGCCCCACCCTCCTCGAGCCCCACTCATACCGTCACGCCCGGCGAGAGCCTGTGGTCGATCACTGCCCACCTACTGCCCGCCGGCTCCAGCCCAGCCCGGATCGCACAGGCCTGGCCGGCCCTGTATCACGCCAACTCCGAGGAGATCGGCACCGACCCGGCCTTGATCCGCCCCGGCGCGGTCCTGAGCGTCCCGGACTCCCTGTCCGCACCGGACACGACGACAGGAGGTCAGGCGCCATCACGATGA","MGARQRLTLLACASGAVLILLGRTAHSAAEQLATVPPQSWGLSELSDAVVAGTCACGTLGALWHVVSALVALMALAGEKGPGPHGLGGTSTLAARVLATWGAPAVRRITASALLVSLSSAPALATQETGGGDDLGWRPTSSAPASPSSQSSTPSPPEQSPSSASTGSGDSEDASQSADSTPPGSQTPQPPTGPDAPPSSSPTHTVTPGESLWSITAHLLPAGSSPARIAQAWPALYHANSEEIGTDPALIRPGAVLSVPDSLSAPDTTTGGQAPSR$","Hypothetical protein","Extracellular, Periplasm, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Joris B., Englebert S., Chu C.P., Kariyama R., Daneo-Moore L., Shockman G.D., Ghuysen J.M. Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin. FEMS Microbiol. Lett. 1992. 70(3):257-264. PMID: 1352512","","","

InterPro
IPR002482
Domain

Peptidoglycan-binding LysM
PF01476	$\"[203-214]T$	LysM

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 203 to 214 (E_value = 0.0076) place ANA_1509 in the LysM family which is described as LysM domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1510","1632132","1632647","516","11.84","16.63","18454","ATGACCGCGACCACCACCGCCCAAGCCATCCGCCCCGCACGCCGCAAGACCGGCGCTCAACGTCGCAGCCGCCCCTCACCGAGTCACCCGACGCCGACTCGGGCGGTTCCGCACAAGCCCTCCAAGCCCGTGAACGGCTCCGAAGCCCTCGCACGGGAAACCTCCCTGACACGACGGTCCGCCGCCGGAGCCGACGCCTCACGCACGGCCGCGATCGTGGTGACTGCCGCCAGCGAGGTCCTGGCCGGGCTTCGCCCCGTGGACCACCTGGTGCGCTGGACCAGCCCCTCCCTATTCGAGGCCCTCGCCCGCCGGGCGGGCCTGGCCGCCCGGATCCTGGGACGCCAGACGAGCCCGCGGCGGCCACGCATCCGCAGCGTGCGCACCGAGCTGACGATGTCGGGGGCCTGCGAGGCCACGGTCCTGCTGGAGGAAGGTGACCGGGTCCGGGCCGCTGCGGCCCGGCTGGAGCTGCTGCGCGAGCGCTGGATCCTCACCGGTCTGGAGATGGCATGA","MTATTTAQAIRPARRKTGAQRRSRPSPSHPTPTRAVPHKPSKPVNGSEALARETSLTRRSAAGADASRTAAIVVTAASEVLAGLRPVDHLVRWTSPSLFEALARRAGLAARILGRQTSPRRPRIRSVRTELTMSGACEATVLLEEGDRVRAAAARLELLRERWILTGLEMA$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1511","1635553","1632719","2835","5.06","-41.75","104544","GTGTCGATCGTGGACCGGATCCTTCGCATTGGCGAGGGCCGCACCCTGAAGAAGCTTGATGCCATCGCCGATCAGGTGGAGGCTCTCGCCGACGAGTACAGCGAGCTCTCCGACGCCGAGCTGCGCGAGATGACTGATGAGCTCAAGGAGCGCTACCAGGACGGCGGGGAGAGCCTCGACGACCTGCTTCCCGAGGCCTTCGCTACGGTGGTGGAGGCGGCCGACCGCGTCCTGGGCATGCGCCCCTACCATGTCCAGATCATGGGCGGGGCCGCCCTCCACCGCGGCAACATCGCCGAGATGAAGACCGGTGAGGGCAAGACCCTTGTGGCCACGATGCCCTCCTACCTGCGGGCCCTGACCGGCAAGGGCGTCCACGTCGTGACTGTCAACGACTATCTCGCCGAGTACCAGTCCGACCTCATGGGGCGCGTTCACCGCTTCCTGGGGCTGACCACCGGCTGCATCCTCGTGGGCCAGACCCCCGCCGAGCGCCGTGAGCAGTACGCCTGCGACATCACCTACGGCACCAACAACGAGTTCGGCTTCGACTACCTGCGCGACAACATGGCCCAGCGCCCCGAGGACCTGGTCCAGCGCGGCCACGCCTTCGTCATCGTTGACGAGGTCGACTCCATCCTCATCGACGAGGCCCGCACCCCGCTCATCATCTCCGGCCCGGCCAGCGGCGACGTCAACAAGTGGTACAAGGAGTTCGCCACGATCTCCGAGCGCCTGCGCGCGGGCAAGGACTACGAGGTCGACGAGAAGAAGCGCACCGTGGGTGTGCTCTCCGCCGGCATCGAGCGGGTGGAGGACTACCTCGGGGTGGACAACCTCTACGAGTCGGAGAACACCCCCCTGATCGGCTTCCTCAACAACGCCATCAAGGCCAAGGAGCTCTTCCACCGGGACAAGGACTACATCGTGCGCGACGGCGAGGTCCTCATCGTCGACGAGCACACCGGCCGCGTCCTGCCCGGCCGCCGCTACAACGAGGGCATGCACCAGGCCATCGAGGCCAAGGAGCGCGTGGAGATCAAGGCCGAGAACCAGACCCTGGCCACCATCACCCTCCAGAACTACTTCCGCCTCTACCCCGAGGGCTCACGCTCGGGCATGACCGGTACCGCCGAGACCGAGGCCGCCGAGTTCGCCGGCACCTACAAGATCGGTGTCGTCCCGATCCCCACCAACAAGCCCATGATCCGCCAGGACCAGCCCGACCTCGTCTACACCACCGTCGAGGCCAAGCTCGACGCCGTCGTCGACGACATCGCTGAGCGTCACGAGCTCGGCCAGCCGGTCCTGGTAGGCACCACCAGCGTGGAGAAGTCGGAGATCCTCTCCGAGCGTCTGCGCGAGCAGGGCATCCCCCACGAGGTCCTCAACGCCAAGCAGCACGCCCGCGAGGCCGCCGTCGTGGCCATGGCCGGGCGCAAGGGCGCCGTCACCGTGGCCACCAACATGGCCGGACGCGGAACCGACATCATGCTGGGCGGTAACGCCGAGCACATCGCGGTCACCGCCCTCAAGGAGGCCGGCCTGGACCCCGAAGAGAACGCCGAGGAGTACGAGAAGGCCTGGCCGCAGGCCCTCGCCGCCGCCAAGGAGTCCTGCCGGGCCGAGCACGACGAGGTCGTCGAGCTCGGCGGCCTCTACGTGCTGGGCACCGAGCGCCACGAGTCGCGACGCATCGACAACCAGCTGCGCGGTCGCTCCGGCCGTCAGGGGGACCCGGGCGAGTCCCGCTTCTACCTGTCCATGGAGGACGACCTCATGCGCATGTTCGCCTCCGGGCTCGCTCAGCGCATCATGTCCTCGGGCGCCTACCCCGACGACGTGCCCCTGGAGTCCAAGATGGTCACTCGTGGCATTGCCGGGGCTCAGCGTCAGGTGGAGTCGCGCAACTACGAGATCCGCAAGAACGTCCTCAAGTACGACGACGTCATGACCGAGCAGCGTGAGAAGGTCTACTCCGAGCGCCGCCGCGTCCTGGACGGCGAGGACCTCGAGCCTCAGATCGAGGTCTTCCGGAACCAGGCCGTCACCTCCATCATCGAGGCCGGTACTGCCGAGGGGCGCCCCGACGAGTGGGACCTGGACGCCCTGTGGGGCGAGCTCGGCCGCCTCTACCCGGTCGGCCTGACCCAGGACGAGATCGTCGAGGCGCTGGGCGGCAAGGACGCGCTGACCTCGGAGCGCCTCATCGAGGAGCTCAGTGAGGATATCGCCGTGGCCTACGAGGACGCCGAGGCCCGCATCGAGGCCAACGCCCTGGCCCATGTCCAGCTCGGTGAGGAGCCCATGCGCACCCTGGAGCGCCGCATCCTGCTGGCCGTGGTGGACAAGCGCTGGCGGGAGCACCTCTACGAGATGGACTACCTCAAGGAGGGCATCGGTCTGCGGGCCATGGCCCAGCGCGACCCGCTCGTGGAGTACGCCAACGAGGGTGCCCGCATGTTCAGGGCGATGATGGAGGGGATCCGCGAGGAGACCGTCGAGCAGATCTTCGCCAACGTCACCCGTTTCGACGCCGCCGCCCAGCGCGCCGCCGAGGACGGCACCGTCGAGGCCGCCCAGGCCGTCGCCAAGGCCAACGCCACTGCCGCGGCAGGCATCCGTGTGGGCCAGGCCGGTGGTCAGGGCCGCGGCACGGTTCTGGGGGACACCGGGCAGGCCTCCATGGAGCAGCGGGTCACCTACTCCGGCCCCAGCGAGTCCGGTGAGGAGGAGACCTCAGGGGCCTCCTCGCGCAGGGCATCCCGTTCCGGCGCCAACTCGGGCGGCAACCGGGCCGAGCGCCGTCGCTCCAAGAAGAAGCGCCGGCACTGA","VSIVDRILRIGEGRTLKKLDAIADQVEALADEYSELSDAELREMTDELKERYQDGGESLDDLLPEAFATVVEAADRVLGMRPYHVQIMGGAALHRGNIAEMKTGEGKTLVATMPSYLRALTGKGVHVVTVNDYLAEYQSDLMGRVHRFLGLTTGCILVGQTPAERREQYACDITYGTNNEFGFDYLRDNMAQRPEDLVQRGHAFVIVDEVDSILIDEARTPLIISGPASGDVNKWYKEFATISERLRAGKDYEVDEKKRTVGVLSAGIERVEDYLGVDNLYESENTPLIGFLNNAIKAKELFHRDKDYIVRDGEVLIVDEHTGRVLPGRRYNEGMHQAIEAKERVEIKAENQTLATITLQNYFRLYPEGSRSGMTGTAETEAAEFAGTYKIGVVPIPTNKPMIRQDQPDLVYTTVEAKLDAVVDDIAERHELGQPVLVGTTSVEKSEILSERLREQGIPHEVLNAKQHAREAAVVAMAGRKGAVTVATNMAGRGTDIMLGGNAEHIAVTALKEAGLDPEENAEEYEKAWPQALAAAKESCRAEHDEVVELGGLYVLGTERHESRRIDNQLRGRSGRQGDPGESRFYLSMEDDLMRMFASGLAQRIMSSGAYPDDVPLESKMVTRGIAGAQRQVESRNYEIRKNVLKYDDVMTEQREKVYSERRRVLDGEDLEPQIEVFRNQAVTSIIEAGTAEGRPDEWDLDALWGELGRLYPVGLTQDEIVEALGGKDALTSERLIEELSEDIAVAYEDAEARIEANALAHVQLGEEPMRTLERRILLAVVDKRWREHLYEMDYLKEGIGLRAMAQRDPLVEYANEGARMFRAMMEGIREETVEQIFANVTRFDAAAQRAAEDGTVEAAQAVAKANATAAAGIRVGQAGGQGRGTVLGDTGQASMEQRVTYSGPSESGEEETSGASSRRASRSGANSGGNRAERRRSKKKRRH$","Preprotein translocase, SecA subunit","Cytoplasm, Membrane","preprotein translocase, SecA subunit","preprotein translocase; SecA subunit","preprotein translocase, SecA subunit","","Mori H., Sugiyama H., Yamanaka M., Sato K., Tagaya M., Mizushima S. Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. J. Biochem. 1998. 124(1):122-129. PMID: 9644254Lill R., Cunningham K., Brundage L.A., Ito K., Oliver D., Wickner W. SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli. EMBO J. 1989. 8(3):961-966. PMID: 2542029","","","

InterPro
IPR000185
Family

SecA protein
PR00906	$\"[62-86]T$ $\"[100-114]T$ $\"[116-126]T$ $\"[169-189]T$ $\"[321-343]T$ $\"[358-375]T$ $\"[397-410]T$	SECA
TIGR00963	$\"[26-829]T$	secA: preprotein translocase, SecA subunit
PS01312	$\"[484-499]T$	SECA

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[452-578]T$	Helicase_C
PS51194	$\"[418-623]T$	HELICASE_CTER

InterPro
IPR011115
Domain

SecA DEAD-like
PF07517	$\"[4-386]T$	SecA_DEAD

InterPro
IPR011116
Domain

SecA Wing and Scaffold
PF07516	$\"[616-842]T$	SecA_SW

InterPro
IPR011130
Domain

SecA preprotein cross-linking region
PF01043	$\"[227-340]T$	SecA_PP_bind

InterPro
IPR014018
Domain

SecA motor DEAD
PS51196	$\"[1-618]T$	SECA_MOTOR_DEAD

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[88-246]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.3060.10	$\"[647-838]T$	no description
G3DSA:3.40.50.300	$\"[408-497]T$	no description

","BeTs to 18 clades of COG0653COG name: Preprotein translocase subunit SecA (ATPase, RNA helicase)Functional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0653 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000185 (SecA protein) with a combined E-value of 0. IPB000185A 63-103 IPB000185B 104-154 IPB000185C 164-213 IPB000185D 305-352 IPB000185E 370-420 IPB000185F 421-463 IPB000185G 464-502 IPB000185H 547-595 IPB000185I 629-667 IPB000185J 778-822","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 386 (E_value = 1.5e-189) place ANA_1511 in the SecA_DEAD family which is described as SecA DEAD-like domain.Residues 227 to 340 (E_value = 5.3e-64) place ANA_1511 in the SecA_PP_bind family which is described as SecA preprotein cross-linking domain.Residues 452 to 578 (E_value = 0.0027) place ANA_1511 in the Helicase_C family which is described as Helicase conserved C-terminal domain.Residues 616 to 842 (E_value = 1.3e-76) place ANA_1511 in the SecA_SW family which is described as SecA Wing and Scaffold domain.","","translocase, SecA subunit (secA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1512","1635978","1636820","843","8.35","4.94","29483","CTGTCCCTGGGGCTGCCGAACAGCTGTGCGGGCTGCGGACGCTGGGAGACGGCGCTGTGCCCGCAGTGCCGGGAGCTGCTCGAGGCCGATCCCTTCGCCGTGGAGCACGCTGACGCCGCCGGAGACCTGGACATCTGGGCCCTGGCCTCCTACACCGGGCCGGTGCGCACTATGGTGCTGGGGTGGAAGAACGGCGCTCGGGAGGACCTGTCGGAGGCGATGGCCCGCTCCGGTCGGCGCCTGGGGCGCTGGTGGGCGCTGAGACACCCGCCGGAGGAGGTCTGGGCCGACTCGCCTCAGGGCGCGCGGGCGCTGCTCGTGGTCCCGGCGCCCTCCGGGATCGTGCGCCGTCTACGCGGCCGCCTGGTGGCGGCCCGCCTGGCCGATGCTCTCACCCGCGGGATCTGCGCGCAGTGGGCCGAGCAGTGTCCCGCGGCGCTCGTGCTGAGCACGGACCTGCTGCGCCGTCGGGGCGGCGGGGCGCACCAGGCGGGCCGATCCGCCCGTCAGCGGCGGGGTAACCGCGCCGAGGCTCCGCGCCTGCTGGCCGCCGTCACCGGCCTGCCGATCCTGCTGGTCGACGACGTCGTGACCACCGGGGCCACTCTGGGCGCCTGCGCCCGGGCGCTACGGGCGGGCGGCGGACGGGTTCTGGGTGCGCTGACGCTCAGTGCCGCCCCACCCCCGGCACATGCGCGTATCTCGGTACCGACCGGCCCCTCCCGCCAACCACGAGACGACACTGCATCTGCGTTGACCATGGATCCGGAAGATCTGGATTTGTCCGCCTGCGGCGATCAGGAGGCTTCTTCCGGGCGTGGCACGCACGAAAGGGAGGCGTGA","LSLGLPNSCAGCGRWETALCPQCRELLEADPFAVEHADAAGDLDIWALASYTGPVRTMVLGWKNGAREDLSEAMARSGRRLGRWWALRHPPEEVWADSPQGARALLVVPAPSGIVRRLRGRLVAARLADALTRGICAQWAEQCPAALVLSTDLLRRRGGGAHQAGRSARQRRGNRAEAPRLLAAVTGLPILLVDDVVTTGATLGACARALRAGGGRVLGALTLSAAPPPAHARISVPTGPSRQPRDDTASALTMDPEDLDLSACGDQEASSGRGTHEREA$","Phosphoribosyltransferase","Cytoplasm, Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","amidophosphoribosyltransferase-like","","Hershey H.V., Taylor M.W. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene 1986. 43(3):287-293. PMID: 3527873","","","

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[190-223]T$	Pribosyltran

InterPro
IPR002375
Family

Purine/pyrimidine phosphoribosyl transferase
PS00103	$\"[190-202]T$	PUR_PYR_PR_TRANSFER

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 353 to 386 (E_value = 2.4e-06) place ANA_1512 in the Pribosyltran family which is described as Phosphoribosyl transferase domain.","","protein ","","1","","","Mon Aug 6 17:13:21 2007","","Mon Aug 6 17:13:21 2007","","","Mon Aug 6 17:13:21 2007","Mon Aug 6 17:13:21 2007","Mon Aug 6 17:13:21 2007","","","Mon Aug 6 17:13:21 2007","","","Mon Aug 6 17:13:21 2007","","","","Mon Aug 6 17:13:21 2007","Mon Aug 6 17:13:21 2007","","","","","yes","","" "ANA_1513","1636965","1637687","723","6.81","-0.91","26763","GTGAGATGTGGCGGGTACTTGTCGCACACGGCCCGTCAGGGCCGGCCCACGAGCCCAGAAAGAGGTTCCACCATGGATATCACCGTCGTCGGTCGTAACGCCGAGATCAGCTCTCGCCTGCGCGACTACGTCGAGGACAAGGCCGTCAAGGTTGAGCAGTTCGACCCCCGGGTCCAGCGCGTCGAGGTGGAGGTCACCCACGAGCGCAACCCGCGCCAGGCCGACACCGCTGAGAGAGTGGAGATCACTGTCGTCTCCAAGGGCCCGATCATCCGGGCGGAGGCATCCTCATCGGACCGCTTCGCCGCTTTTGATATCGCCATGGGCAAGCTGACCGAGCGCCTTCGCCGGGCCAGGGACCGCAAGAAGGACCACCACCGCCGCCACACCGTGGCCGCACCGAATGAGGACCTCCAGGCAGCTCCCGGCGTGGAGGAGGCCCTCCTCCCCGACACCGGTGACGCACCGATCGAGGACTCCCCCTCTGCGCCCACTGAGCCGGGTGTCGCCGTTGAGGCGCAGCTCGGCGACTCCCCGGTGATCGTGCGTCAGAAGCTGCACGAGGCCAAGCCGATGACCGTTGACGAGGCCCTCTACCAGATGGAGCTCGTGGGACACCCCTTCTACCTGTTCATCGAGAAGTCCTCCAAGCAGCCCTGCGCCGTCTATCACCGTCACGGGTGGACCTACGGCGTCATCCGCCTGGACGCCCAGGTGCTGTAG","VRCGGYLSHTARQGRPTSPERGSTMDITVVGRNAEISSRLRDYVEDKAVKVEQFDPRVQRVEVEVTHERNPRQADTAERVEITVVSKGPIIRAEASSSDRFAAFDIAMGKLTERLRRARDRKKDHHRRHTVAAPNEDLQAAPGVEEALLPDTGDAPIEDSPSAPTEPGVAVEAQLGDSPVIVRQKLHEAKPMTVDEALYQMELVGHPFYLFIEKSSKQPCAVYHRHGWTYGVIRLDAQVL$","Sigma 54 modulation protein/ribosomal protein S30EA","Cytoplasm","S30AE family protein","sigma 54 modulation protein/ribosomal protein S30EA","ribosomal subunit interface protein","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Tan X., Varughese M., Widger W.R. A light-repressed transcript found in Synechococcus PCC 7002 is similar to a chloroplast-specific small subunit ribosomal protein and to a transcription modulator protein associated with sigma 54. J. Biol. Chem. 1994. 269(33):20905-20912. PMID: 8063707","","","

InterPro
IPR003489
Domain

Sigma 54 modulation protein/ribosomal protein S30EA
PF02482	$\"[26-125]T$	Ribosomal_S30AE
TIGR00741	$\"[25-129]T$	yfiA: ribosomal subunit interface protein

noIPR
unintegrated

unintegrated
G3DSA:3.30.160.100	$\"[25-137]T$	no description

","BeTs to 10 clades of COG1544COG name: Ribosome-associated protein Y (PSrp-1)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1544 is -------qvdrlbcefghs--jxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003489 (Sigma 54 modulation protein/ribosomal protein S30EA) with a combined E-value of 7.9e-21. IPB003489A 25-50 IPB003489B 81-121","","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 125 (E_value = 4.9e-19) place ANA_1513 in the Ribosomal_S30AE family which is described as Sigma 54 modulation protein / S30EA ribosomal protein.","","family protein (PSrp)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1514","1639625","1637829","1797","5.24","-10.12","61155","ATGACGCAGCCGATGAACCGTGACGCGTTCACCCAGGGGTGCGGGCCCGCCGAGACCACCGAGACCGCCGCGCCCACCGACTCCATCGGGGCCCTGAGGGTGGCCCCGTCCCGTCTGTCGCGACGTGGCGCGCTGGGACTGCTCTCGGCCACGGCCGCCGGAGTGCTGGCCGGCTGCACGGCGCTCCCGAGCTCCAGCGGCGTCACCCGCTCCGGGGTGGCCGCCTCTGACACCAATGCCCTCATCGAGACCGCGCCCGGACCGGGTGAGGGGGACTCGGCCGAGGACATTGTCAACGGCTTCCTGCGTGCCGCCATCGCGGGGTTCTCCGACGACTTCGCCACCGCCAAGCAGTTCCTCAGCGATCACGCCGTCGCGCAGTGGAAGCCCCTGGAGACGGTGAGCGCCTACAGCGGGTCGACTGAGCCGCAGGTCTCGGTGGCGGCCAACGGCTCCTTCACGGTGACCTCCGGGCAGGTGGGGGTGCTCAACTCCCTGGGTGTCTTCACCCCCGCCCCGGAGGGGAGCACCTATGCCGGCGAGTTCTCCCTGGCCACCAACTCCACCGGGCAGTGGCGCATCGTCGGACTGCCCCAGGGCATCCTGCTGCCCTTCTCCCGACTCATGCAGAACTTCGCCGTCAGCTCCCTGGCCTTCCTATCCAGGGACCGGTCCCGGTTCGTTCCCGAGCTGAGGTGGTACCCGCGCAGCTCGCAGGCCGACTCCCTGGTCTCCGGGCTGCTGGCCGGCCCCTCGGACTGGCTGGCGAAGGGCGCCTCCAGTCTCATCCCGCGCAATGCCGAGCGGGCGGGGCGGGGGGTCGTCGTCGAGGGCGGCACCGCCACCGTCCACCTGAGCGCGGACTCCGACCCCGCCTCGGAGGACGCCCGTGGGCTCATGGTGGCCCAGATCGAGCAGAGCCTCGTCCAGATCAGCGGTATCGACCACGTGCGAGTGCTCGCCGGCACCGTCGATCTCGGCGCCCCCGCCCAGCTGACGCCCATGGCCCCCGAGGTCGGAGGCATCGTGGGCATGTCGGAGGGCTCCGTCGTGCGCGGCACAGGGGCCAGACGCATCACCCTGGCCAGTGACCGGGTCCTGGGGACCAGTGATGCCCGCAGCCCAAGCCTGGGGGCCGACGGGGCCGTCTACGCGTTGTCGGCCTCCAGCCTGCTGCGCCTACCCCGAGGGCAGGAGTCCGCCAGCGTCATCCTCTCGGTGGGGGATCCCTCCGCGGGTGCCGGCGGGCTGGGGGCGCCGATGGGTGACCGGCACGGCTGGGCCTGGTTGCTGGCCGAGGGACGTCTGACCGCCGTCAACGGCTCGGGGCAGCGGGCCACTCTGGAGTCCTCCTGGCTGCAGGACGGCGCGGTCACGGCCTTCGACCTGTCCGTGGAGTCCGAGCGGATCGCCGTGCGGCGAACCGACGGACGGGTCGCCGTCGCCGTCATCATCAGAGACCAGGACGGCCGTCCTACCGGGCTGGGGCCGGCGCTGGAGATGCCCCGCGCCAGTGGGGCGGGCACGAGCGGACTGTCCTGGTGCGCCCCCAACGCCGTGTGCGTCCTGGCCACTGCCGGCACCGAGGGCGGGGGCGTGCCGGAGGTGCGTCTGGTCCAGGTCGGCGGGGCGGTCAACACGCTGGTCGGGGTGCGCGGGGCCCGCTCGGTCATCTCCGACCGCTCCGAGGAGTCCCTCCTCATCATCGACGAGGGCGGGCAGACCTGGCAGCGTCGTGGGGCGATGTGGCGGGTGCTCACCTCCGAGGTCTCCGACCCCTCCTTCCCCCTGCCCTGA","MTQPMNRDAFTQGCGPAETTETAAPTDSIGALRVAPSRLSRRGALGLLSATAAGVLAGCTALPSSSGVTRSGVAASDTNALIETAPGPGEGDSAEDIVNGFLRAAIAGFSDDFATAKQFLSDHAVAQWKPLETVSAYSGSTEPQVSVAANGSFTVTSGQVGVLNSLGVFTPAPEGSTYAGEFSLATNSTGQWRIVGLPQGILLPFSRLMQNFAVSSLAFLSRDRSRFVPELRWYPRSSQADSLVSGLLAGPSDWLAKGASSLIPRNAERAGRGVVVEGGTATVHLSADSDPASEDARGLMVAQIEQSLVQISGIDHVRVLAGTVDLGAPAQLTPMAPEVGGIVGMSEGSVVRGTGARRITLASDRVLGTSDARSPSLGADGAVYALSASSLLRLPRGQESASVILSVGDPSAGAGGLGAPMGDRHGWAWLLAEGRLTAVNGSGQRATLESSWLQDGAVTAFDLSVESERIAVRRTDGRVAVAVIIRDQDGRPTGLGPALEMPRASGAGTSGLSWCAPNAVCVLATAGTEGGGVPEVRLVQVGGAVNTLVGVRGARSVISDRSEESLLIIDEGGQTWQRRGAMWRVLTSEVSDPSFPLP$","Hypothetical protein","Membrane, Extracellular","putative lipoprotein","hypothetical protein","hypothetical protein","","Berks B.C. A common export pathway for proteins binding complex redox cofactors?. Mol. Microbiol. 1996. 22(3):393-404. PMID: 8939424Berks B.C., Sargent F., Palmer T. The Tat protein export pathway. Mol. Microbiol. 2000. 35(2):260-274. PMID: 10652088","","","

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[39-66]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
tmhmm	$\"[43-63]?$	transmembrane_regions

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[365-522]T$	no description
PF02518	$\"[405-515]T$	HATPase_c
SM00387	$\"[405-516]T$	HATPase_c

InterPro
IPR003660
Domain

Histidine kinase, HAMP region
PF00672	$\"[211-280]T$	HAMP
SM00304	$\"[231-283]T$	HAMP
PS50885	$\"[231-283]T$	HAMP

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[291-359]T$	HisKA
SM00388	$\"[291-359]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[441-455]T$ $\"[459-469]T$ $\"[476-494]T$ $\"[500-513]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[298-516]T$	HIS_KIN

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.240	$\"[281-355]T$	no description
PTHR23283	$\"[6-47]T$ $\"[183-514]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23	$\"[6-47]T$ $\"[183-514]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
signalp	$\"[1-55]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[211-229]?$	transmembrane_regions

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[4-118]T$	Q9KYW8_STRCO_Q9KYW8;
PF00072	$\"[3-114]T$	Response_reg
SM00448	$\"[3-113]T$	REC
PS50110	$\"[4-117]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[131-211]T$	Q6AGI7_BBBBB_Q6AGI7;
PF00486	$\"[145-222]T$	Trans_reg_C

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[120-222]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[4-120]T$	no description
PTHR23283	$\"[1-119]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[1-119]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 1.8e-39. IPB001867A 48-61 IPB001867B 75-119 IPB001867C 212-222***** IPB001789 (Response regulator receiver) with a combined E-value of 1.3e-13. IPB001789A 48-61 IPB001789B 95-105***** IPB000673 (CheB methylesterase) with a combined E-value of 8.8e-13. IPB000673B 20-73 IPB000673C 73-103","","","-72% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 3.5E_64);-53% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 1.2E_29);-53% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 1.2E_29);-53% similar to PDB:1KGS Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima (E_value = 2.6E_27);-50% similar to PDB:1P2F Crystal Structure Analysis of Response Regulator DrrB, a Thermotoga maritima OmpR/PhoB Homolog (E_value = 8.4E_26);","Residues 3 to 114 (E_value = 1.5e-36) place ANA_1516 in the Response_reg family which is described as Response regulator receiver domain.Residues 145 to 222 (E_value = 6e-23) place ANA_1516 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","response regulator mtrA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1517","1642500","1643834","1335","5.29","-4.59","45713","ATGAGTACCGAGTTCCCCCCTGACGGCAGCGGTCCGAGCGACGTTCCGGGCCGCGAGGCCCCCGCCACCTCCGGCAGCCCCGGCACCGGAGGCGCTCAGGATGGGTGGCAGGCCCCCGACGCCGGAGCCTTCACCGAGGCTCCCTCCTACCCGGCACCGGGCTCAGCACCGGGCTCAGCACCAAGCTCCCAGTACCCCGCCGGCTACGGCGGCTACCACACGCCACCGGTGGGCCAGCCGGGCTACCCAGGCTCCTCGGGCCCCGGCAACACTCCCTACCCCAGCACCTCGGGAGACCCCGGGTACCCCGGAGCCCCTGGATACCCGGGCTACGGCGGCTACACGTCAGTCCTGGCCCCCAAGCCCTCGATCATTCCGCTACGGCCACTGTCCATCGGGGAGATCCTCGGGGGAGCCTTCGAGTCCCTGCGCGCCAACCCCAAGGCGATGTTCATACCCTCACTGGTAGTGATGGGCATTACAGGACTCTTGTCCGCCGGGAGCGTCGCCCTGTTCATGTCCCGGCTCGGCCTGACGGACCTGACATCCGGAAAGGTTGAGTTCTCCGAGACCGACCTGGACAGCATCGGGTCATCGTTGGTGGGTCTGCTCATCCAGCTCGGCGTGACCGGCGTGCTGAGCATGCTGGCCACCTCGATCATCATCGGCCTGATCATCGTGACCGTCTCACGCACCATTCTTGGCCGTAAGGCGTCCTTGAGCGACGTGTGGCGGCGCACCCGGCCGAGAATGTGGGCGCTCATCGGCCAGACGCTCCTCATCGAGCTCATCCTCGCCGTCATCACCGCCGTCGTCACAGCGATCGCCTTCGGCATCGGCTGGGCTCTCCTGGGGAACATCATCGCCTACGGGGCCGATGAGGACTCCGCCGGGACCATCATCCTCGCCATCCTGGCGATTCTGGCGGTGATCGCCGTGCTCGGGCTGTTGACCTTCGCCCTGATATGCAAGCTGTCCCTGGCACCGGCGGCACTGGTCCTGGAGAACATCGGCGTCCTTGAGGGGATATCCCGCTCCTGGACCCTCACACGGGGCTACTTCTGGCGGATCGTCGGCATCCGCCTGCTCTCCTTCATCATCGTCTTCTTCGCCGTCCAGATCGTGTCTCAGGGCGTGTCCCTCGTCATGCAGGGGCTCGTCTACGCCGCCCCGAACATGACCATCGCGATCTTGGTGGCATCGACGCTGCTCAACAGCCTCATCCAGGCCGCGATCCAGCCCTTCGACTCCGCCGTGGTCGCGCTCATGTACACCGACCTGCGGATGCGCTCCGAGGGCCTGGACGTCGAGCTGCGTCACGCCGCCGGGGTATGA","MSTEFPPDGSGPSDVPGREAPATSGSPGTGGAQDGWQAPDAGAFTEAPSYPAPGSAPGSAPSSQYPAGYGGYHTPPVGQPGYPGSSGPGNTPYPSTSGDPGYPGAPGYPGYGGYTSVLAPKPSIIPLRPLSIGEILGGAFESLRANPKAMFIPSLVVMGITGLLSAGSVALFMSRLGLTDLTSGKVEFSETDLDSIGSSLVGLLIQLGVTGVLSMLATSIIIGLIIVTVSRTILGRKASLSDVWRRTRPRMWALIGQTLLIELILAVITAVVTAIAFGIGWALLGNIIAYGADEDSAGTIILAILAILAVIAVLGLLTFALICKLSLAPAALVLENIGVLEGISRSWTLTRGYFWRIVGIRLLSFIIVFFAVQIVSQGVSLVMQGLVYAAPNMTIAILVASTLLNSLIQAAIQPFDSAVVALMYTDLRMRSEGLDVELRHAAGV$","Integral membrane protein","Membrane, Cytoplasm, Extracellular","putative integral membrane protein","integral membrane protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[152-172]?$ $\"[210-230]?$ $\"[251-285]?$ $\"[299-321]?$ $\"[354-374]?$ $\"[388-408]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB010515 (Collagenase NC10 and endostatin) with a combined E-value of 4e-07. IPB010515K 78-128 IPB010515G 88-113 IPB010515H 80-116 IPB010515H 77-113 IPB010515J 86-122 IPB010515K 81-131 IPB010515K 75-125 IPB010515K 64-114 IPB010515K 58-108 IPB010515K 61-111 IPB010515K 84-134 IPB010515K 55-105 IPB010515K 44-94 IPB010515K 72-122","","","-52% similar to PDB:2CN2 CRYSTAL STRUCTURES OF CLOSTRIDIUM THERMOCELLUM XYLOGLUCANASE (E_value = );-52% similar to PDB:2CN3 CRYSTAL STRUCTURES OF CLOSTRIDIUM THERMOCELLUM XYLOGLUCANASE (E_value = );","No significant hits to the Pfam 21.0 database.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1518","1643842","1644528","687","6.05","-3.59","24634","GTGATACCTCTCAGGACGATCAGCGCGCAGACCCCGGCGACCCCCGACGCCGACGAGGCGCGGCGCGCCGCGGGCAGGGAGCTCTCCCGACCGATCTACCACGATCATCACGATCTGTGGGACCGGCTCTGGAGCTGGATCAGGGGGCTCTTCGATACCGACGGCATGGTCCCCGGGGCTCCTCCCTGGGTGTCGACGCTCATCGTGGTCCTCGTCGTCGCCGCCGGCATCGCGCTGCTGATCCTCCTGCTGACCAGGCTCTCCTCGGCACGCCGAGTGGTGACGCCGCCGTCGTTGTCGGTGCTCACCGACGACCGCGATGCCGACACCCTGACCCGAGCCGCGGACGCTGCGGCCGTACAGGCCGATTTCGCCACCGCCGTCGTCGAACGCTTCCGCGCCATCATCCGTTCCCTCGACGAACGCGGGATCATCGACGAGTACCCGGGCATGACGGCGCTGGAGGCGGCCACGCTCACCCACCGGGCCCTCGGTGAGCACCGGGTGGTGTCCCCGCTGTACGAGGCCGCCCACCTGTTCGATGCCGTCCTCTACGGTCGGGTCGTCTCCACCAGCACCCAGGACCAGCAGATGCGCGAGCTCGCCGATCAGATGGCCAGGGTCTCCCTCACCTCCGGACGCGCCCTCGTCGGCGCCTCGGCCCAGGCCCCGGGGACACCGGCATGA","VIPLRTISAQTPATPDADEARRAAGRELSRPIYHDHHDLWDRLWSWIRGLFDTDGMVPGAPPWVSTLIVVLVVAAGIALLILLLTRLSSARRVVTPPSLSVLTDDRDADTLTRAADAAAVQADFATAVVERFRAIIRSLDERGIIDEYPGMTALEAATLTHRALGEHRVVSPLYEAAHLFDAVLYGRVVSTSTQDQQMRELADQMARVSLTSGRALVGASAQAPGTPA$","Integral membrane protein","Membrane, Cytoplasm","putative integral membrane protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-90]?$	signal-peptide
tmhmm	$\"[63-83]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-67% similar to PDB:1WU4 Crystal structure of reducing-end-xylose releasing exo-oligoxylanase (E_value = );-67% similar to PDB:1WU5 Crystal structure of reducing-end-xylose releasing exo-oligoxylanase complexed with xylose (E_value = );-67% similar to PDB:1WU6 Crystal structure of reducing-end-xylose releasing exo-oligoxylanase E70A mutant complexed with xylobiose (E_value = );-67% similar to PDB:2DRO Crystal structure of reducing-end-xylose releasing exo-oligoxylanase D263C mutant (E_value = );-67% similar to PDB:2DRQ Crystal structure of reducing-end-xylose releasing exo-oligoxylanase D263G mutant (E_value = );","No significant hits to the Pfam 21.0 database.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1520","1644663","1645736","1074","6.44","-2.39","36732","ATGCTCATCCCCGTCCTGGTGACTGTGTGGACTCGGACCGTCACCTCCACCACGCCCCTGGCCATCGACAACCCCAAGGACCGGGGAACCATGGCGCTCGCCGAGCTGCTGCGCCACGAGGGGATCTCCGTGAGCAAGGCGGGCAGCCTCTCCGAGGCCGTGGACGCCAGCCGCCAGGGCGCGACCATCGCCGTGGTCAACGCCGACCGGCTCAGCGACCAGGACAGGCGGGCCCTGGCCGAGGCGGGCGGCGACGTCGTTGTCATCGGCGCCAAGGGCGGCAGCGACGCTCTGAAAGGGCTGACGGGCATGACCGCCAAGGGCACCGCGGCGGCGGATTCCTCCACCCTGGCGCCGCAGTGCGACGACGCCGACGCCCAGGCCGCCCGGGGCCTTGCCGGCACGCGCGCCTCCGTATCCCTGCAGGGTGATGGCGACGCCGTCGGCTGCTTCCCGGTGAGCAAGGACCGTTACGCCTATGCCACCGACTCCCTGCCCAGCGGTGCCACGTTGCGAGTCCTGCCTGATCCCGCACCAGTGACCAACGCACACCTGGCCCAGGAGGGGCACGCGGCCTTGGGAGTACGCGCGCTGGGCCACCACAGCCGCGTGCTGTGGTTGGACGCGGAGCACATGGAGTCCCCCTCCGTGTGGAACTCCCCCTCCACTCCCCCTTGGCTTCCGGTCCTCATCTTCCAGCTCCTTGTCACCGCCGGCGTGCTGGCGATCGTTCAGGGTCGTCGCTTCGGCGGCATCGTGAGCGAGGACCTGCCCGTCATCGTGCGCTCCACCGAGACCACGGTGGCCCGCGGGCGGCTCTACCGTCAGGGCTCGGACCGGCCCCGGGCGGCTCAAGCCCTGCGCTCGGGTGCCGCGCTGCGCCTGGGCGCCACTCTGGGCCTGCCCCCCGGGACCTCGCGCCGTGACGTCATCACCGCCGTCTCCCTGGCCTCCGGCGTCGCCCCGGGCACGGTGGACTCTCTTCTCTACGGTCCGCCCCCATCCAGCGACAGTGCCCTGGCCACCCTGGCAGTTCAGCTCGACCAACTCGAGAGCGAGGTTCACTCCACATGA","MLIPVLVTVWTRTVTSTTPLAIDNPKDRGTMALAELLRHEGISVSKAGSLSEAVDASRQGATIAVVNADRLSDQDRRALAEAGGDVVVIGAKGGSDALKGLTGMTAKGTAAADSSTLAPQCDDADAQAARGLAGTRASVSLQGDGDAVGCFPVSKDRYAYATDSLPSGATLRVLPDPAPVTNAHLAQEGHAALGVRALGHHSRVLWLDAEHMESPSVWNSPSTPPWLPVLIFQLLVTAGVLAIVQGRRFGGIVSEDLPVIVRSTETTVARGRLYRQGSDRPRAAQALRSGAALRLGATLGLPPGTSRRDVITAVSLASGVAPGTVDSLLYGPPPSSDSALATLAVQLDQLESEVHST$","Hypothetical protein","Periplasm, Membrane","putative secreted protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[86-227]T$	AAA

InterPro
IPR011703
Domain

ATPase associated with various cellular activities, AAA-3
PF07726	$\"[89-219]T$	AAA_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[69-224]T$	no description

","BeTs to 19 clades of COG0714COG name: MoxR-like ATPasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0714 is aompkzyqvdr-bcefg-s--j--t-Number of proteins in this genome belonging to this COG is 3","***** IPB011703 (ATPase associated with various cellular activities, AAA_3) with a combined E-value of 6.6e-106. IPB011703A 94-128 IPB011703B 160-208 IPB011703C 209-220 IPB011703D 297-320 IPB011703E 324-367 IPB011703B 161-209***** IPB000523 (Magnesium chelatase, ChlI subunit) with a combined E-value of 9.4e-21. IPB000523A 70-112 IPB000523C 165-216 IPB000523E 301-345","","","No significant hits to the PDB database (E-value < E-10).","Residues 68 to 240 (E_value = 0.00044) place ANA_1522 in the Mg_chelatase family which is described as Magnesium chelatase, subunit ChlI.Residues 89 to 219 (E_value = 3e-84) place ANA_1522 in the AAA_3 family which is described as ATPase family associated with various cellular activities (AAA).Residues 89 to 225 (E_value = 5.7e-14) place ANA_1522 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).","","protein (moxr)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1523","1646932","1648194","1263","10.59","10.16","45389","ATGCTTGCGGGGATCGCCCTGGTCCTCATCGTCCCGCGCCCGACCACCGTGCTGGCCTGGGCCGGCGTGGTCACGGTCCTCGTCGTGATCGACGTGGTGAGCGCCCCCTCGCCGGCGGTGCTGCGGGCCTCGCGCTCCGTGAGCCACGGAGTGCGGCTGGGTGAGTCGATCACCGCGACACTGACGCTCACCAACACCGGTCGGCGCACGGCCCGCCTCCTGCTGCGCGATGCCTGGCCCCCCAGCGCCGGAGCGACCCACGAGCGCGGGGCGATGACCCTCCCACCGGCCCAGCGCCGTCGTCATTCCACAGTGCTCACGCCCCGGCGCCGGGGGGAGCGCCGGGCGGGACCGTTGACCGTCAGGGTCATCGGTCCCCTGGGCATCGCGGGGCGGCAGGCGTCATTGGACGTCCCTGCCTCCGTCCGGGTCCTGCCGGCCTTCCGCTCGCGCCGCCACCTGCACTCACGCCTGGCCCGGCTGCGGGAGATGGACGGGCGCAGCTCCGTCATGGTGCGCGGGGAGGGGACCGAGTTCGACTCCCTGCGCGAGTACGTCGTCGGAGACGACGTGCGCTCCATCGACTGGCGCTCCACCGCTCGCCGGGGCGAGGTGCTGGTACGCACCTGGCGCCCGGAGCGCGATCGGAGGGTTCTCATCATCATCGACTCCGGCCGCCTGTCCGCCGCCCGGCTGGGGGACGCCCCCAGGCTCGACGCCCAGATCGAGGCCACGCTGCTGCTGGCGGCCCTGGCCTCCCGCGCCGGCGACCGGGTCGACGTGCTGGCCATGGACGACGCCGTGCGCGCGCAGGTGCGGGGCAGTGCCGGACCGGTGCTCATGACCGAGCTGGCCGAGCACCTGACCAATGTGGAGCCGCGTCTGACCGAGCTCGACTGGACCCTCGTGGCCTCCCTGGTGCGCACCACGCTCTCGCAGCGCGCACTGGTGGTGGTCATCTCCGCCCTGGACGGCAGTGCCGGGGACGCGACGATGATTCGGACGCTGGCGGCTCTGGCCCAGGAGCACACGGTCATTCTCGCCTCGGCCCTGGACCCCGAGCTGGAGGAGCTCAGATCGACGCATGACGACACCGACTCGGTGTACGTGGCCGCCTCCGCGGAGAAGGACCTGGTGGAGATGCACGCCGTGCGCCGCCGCCTGAGCCGCGGCGGGGTGGAGGTCGTGGAGGCGCCCGACCAGGGACTCGCCCCGGCACTGGCCGACTGCTACCTGGACCTCAAGGCTGCGGGGCGGCTATGA","MLAGIALVLIVPRPTTVLAWAGVVTVLVVIDVVSAPSPAVLRASRSVSHGVRLGESITATLTLTNTGRRTARLLLRDAWPPSAGATHERGAMTLPPAQRRRHSTVLTPRRRGERRAGPLTVRVIGPLGIAGRQASLDVPASVRVLPAFRSRRHLHSRLARLREMDGRSSVMVRGEGTEFDSLREYVVGDDVRSIDWRSTARRGEVLVRTWRPERDRRVLIIIDSGRLSAARLGDAPRLDAQIEATLLLAALASRAGDRVDVLAMDDAVRAQVRGSAGPVLMTELAEHLTNVEPRLTELDWTLVASLVRTTLSQRALVVVISALDGSAGDATMIRTLAALAQEHTVILASALDPELEELRSTHDDTDSVYVAASAEKDLVEMHAVRRRLSRGGVEVVEAPDQGLAPALADCYLDLKAAGRL$","Uncharacterized conserved protein","Membrane, Cytoplasm, Extracellular","Protein of unknown function family","hypothetical protein","protein of unknown function DUF58","","Ruggeri Z.M., Ware J. von Willebrand factor. FASEB J. 1993. 7(2):308-316. PMID: 8440408Colombatti A., Bonaldo P., Doliana R. Type A modules: interacting domains found in several non-fibrillar collagens and in other extracellular matrix proteins. Matrix 1993. 13(4):297-306. PMID: 8412987Perkins S.J., Smith K.F., Williams S.C., Haris P.I., Chapman D., Sim R.B. The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. Its occurrence in collagen types VI, VII, XII and XIV, the integrins and other proteins by averaged structure predictions. J. Mol. Biol. 1994. 238(1):104-119. PMID: 8145250Bork P. Shuffled domains in extracellular proteins. FEBS Lett. 1991. 286(1):47-54. PMID: 1864378Edwards Y.J., Perkins S.J. The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted beta-sheet flanked by alpha-helices found in human ras-p21. FEBS Lett. 1995. 358(3):283-286. PMID: 7843416Lee J.O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 1995. 80(4):631-638. PMID: 7867070Qu A., Leahy D.J. Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(22):10277-10281. PMID: 7479767","","","

InterPro
IPR002035
Domain

von Willebrand factor, type A
SM00327	$\"[215-383]T$	VWA

InterPro
IPR002881
Domain

Protein of unknown function DUF58
PF01882	$\"[109-213]T$	DUF58

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide

","BeTs to 14 clades of COG1721COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1721 is ao-pkz-qvdr-bc-fg----j--t-Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 109 to 213 (E_value = 7.1e-33) place ANA_1523 in the DUF58 family which is described as Protein of unknown function DUF58.","","of unknown function family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1524","1649213","1648218","996","6.87","-0.47","35214","GTGGATCTTGATGCCTTTTCCGCGGCGCACCGCGATCAGTGGGAACGTCTCGATGTCCTCGTGGGGCGTGGCCACCTCAGCGGGGCCGAGACTGATGAGCTCGTGGTTCTCTACCGCACCTGTGCCCGCCATCTGTCGCGGGTGCGTTCGGCCGCGCCGGATCCGCAGCTCATCGCCGAGCTGTCCTCCCGAGTGGCCGCGGCTCGCGGTCGCCTGACCGGAACGCGGGAGGTGAGGAGCCACTCGGTGCGTCGTTTCGTTCTCCAGTCCGTGCCTGCGGCCCTGTACCGCATCCGGTGGTGGACCTGCGGGGTCATGGTTGTCGAGATCGCCCTGGCGCTGGTGGTGGGGATGTGGACCCTGCGCAGTCCTGAGGCCATGGCCGCTCTGGGCAGCCCCGAGAAGCTGGACGCCTACGCCCACGAGGCCTTCGAGTCCTACTACTCCACGTACTCCGCCCCCGACTTCGCCGCTGCGGTGTGGACGAATAACGCCCGTATCGCAGCGATCTGCGTGGCCGGAGGGATCACGGGGTTCCTGCCGCTCTACATGCTGTACCAGAATGCCGTCGCCGTGGGACGGGCCGGGGCCATCATGACCGACCACGACATGCTCGGCGTGTTCCTCTCGCTCATCTCGCCTCACGGCCTGCTGGAGCTGACCTGCATCTTCATCGCCGGTGCGGCCGGACTCAAGCTCTTCTGGACCATGCTGGTCCCCGGCCGACGCAGCCGCGCCGCCGCCCTGGCCGCCGAGGGGCGCGCGCTCATCACGGTGGCTGTGGGTCTGACCGCCGCCCTGGCGGTGGCCGGACTCATTGAGGCCTTCGTGACTCCGGCCCCCATTGCCTGGCCGGTCAAGATCACCATTGGAGCCGGCGCGCTGGCACTGCTGTGGGCCTACACCCTCATCCTGGGACGCTCCGCCGTCGCCGTAGGAGCCACGGGTGACCTCGAGGAGGACGAGGCCGGGTACGTCCAGCCCGAGGTCGGCTGA","VDLDAFSAAHRDQWERLDVLVGRGHLSGAETDELVVLYRTCARHLSRVRSAAPDPQLIAELSSRVAAARGRLTGTREVRSHSVRRFVLQSVPAALYRIRWWTCGVMVVEIALALVVGMWTLRSPEAMAALGSPEKLDAYAHEAFESYYSTYSAPDFAAAVWTNNARIAAICVAGGITGFLPLYMLYQNAVAVGRAGAIMTDHDMLGVFLSLISPHGLLELTCIFIAGAAGLKLFWTMLVPGRRSRAAALAAEGRALITVAVGLTAALAVAGLIEAFVTPAPIAWPVKITIGAGALALLWAYTLILGRSAVAVGATGDLEEDEAGYVQPEVG$","Uncharacterized membrane protein","Membrane, Cytoplasm","putative integral membrane protein","hypothetical protein","protein of unknown function DUF95, transmembrane","","","","","

InterPro
IPR002798
Family

Protein of unknown function DUF95, transmembrane
PF01944	$\"[105-280]T$	DUF95

noIPR
unintegrated

unintegrated
tmhmm	$\"[101-121]?$ $\"[166-186]?$ $\"[196-214]?$ $\"[220-240]?$ $\"[255-277]?$ $\"[283-303]?$	transmembrane_regions

","BeTs to 9 clades of COG1300COG name: Uncharacterized membrane proteinFunctional Class: M, ,SThe phylogenetic pattern of COG1300 is a-m-kz----r-bc-f-----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 105 to 280 (E_value = 2.9e-50) place ANA_1524 in the DUF95 family which is described as Integral membrane protein DUF95.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1526","1649228","1650112","885","9.88","8.35","31743","ATGACGGCCGCATCCCCCACATCCTCCGAGCGAATGATCGAGCCCGAGCTGCTCATCACCGGCGAGGCAGTCGCCCTGGAGATCACCCCGGCAACGGTCGCCAACCGCATCGCTTCGGGGCTCATCGACTACACCGTCTACGCCCTGGGGGCAGCACTGTCCGTGTTCGCGGTGCTGGGACTGGTCATCGGCGACGGCTCAGCCCTCAAGGAGGACCTCGCCCTCCTCAAGGCGCTGCTGTCCCTGGTGGCCCTGGCCTGGCTGGTCGTCATCCCCCTGCTCGTCGAGCTCTTCAGCAGGGGCCGGAGCCTAGGCCGCATGGTGACGGGGGCCCGGGTGGTGCGCGACGACGGCGGCACCGTCAGGCTGCGCCACTGCCTGGTGCGCACTCTGCTGGCCGTCGTCGAGATCTGGGGCACCTGGGCCGTGCCGGCCCTATGCGCCAGCATCATCTCCAAGCGGGGGAAGAGGTTCGGGGACATGCTGGCCGGCACCTACGTGGTTCGAGAGCATCACCGCTCCCACGCGGCACCACCGCTGCTGATGCCCCCCGAGCTGGTCCAGTGGGCGGCAGGCACGGACCTGCGCTCCCTGCCCGGGGGCCTGAGCCTGACGGCGCGCACCTTCCTGCAGCGCGCCTCCTCCCTCATGCCCTCCTCCCGCCACCAGCTGGGGCTCGACCTGGCCTCTCAGGTCCAGGGATACGTCTCTCCCCCGCCTCCCGCCGGCACGCACCCCGAGCGGTTCCTCGCCGCGGTCCTCACCGAGCGGCGCAACCGGGAGCTGGTGCTGGAGAGCCGTAACCGCCGGCTGGAGGAGGACGTGCTGCGAGACATGGCCCGCCCGCCCTATGGGGTGGGCGGTGGTGAGACCCGACGGCGTTGA","MTAASPTSSERMIEPELLITGEAVALEITPATVANRIASGLIDYTVYALGAALSVFAVLGLVIGDGSALKEDLALLKALLSLVALAWLVVIPLLVELFSRGRSLGRMVTGARVVRDDGGTVRLRHCLVRTLLAVVEIWGTWAVPALCASIISKRGKRFGDMLAGTYVVREHHRSHAAPPLLMPPELVQWAAGTDLRSLPGGLSLTARTFLQRASSLMPSSRHQLGLDLASQVQGYVSPPPPAGTHPERFLAAVLTERRNRELVLESRNRRLEEDVLRDMARPPYGVGGGETRRR$","RDD domain containing protein","Membrane, Cytoplasm","conserved hypothetical protein","possible conserved membrane protein","RDD domain containing protein","","","","","

InterPro
IPR010432
Domain

RDD
PF06271	$\"[30-169]T$	RDD

noIPR
unintegrated

unintegrated
tmhmm	$\"[44-64]?$ $\"[78-98]?$ $\"[131-151]?$	transmembrane_regions

","BeTs to 5 clades of COG1714COG name: Uncharacterized membrane protein/domainFunctional Class: S [Function unknown]The phylogenetic pattern of COG1714 is --m-------r-bc-fgh-nujx---Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 30 to 169 (E_value = 2.3e-23) place ANA_1526 in the RDD family which is described as RDD family.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1527","1650413","1650171","243","5.05","-2.85","8319","ATGAACCGGCCAGACACCGCACCCGCGCCTGAGCAGCGGGCTGTCCTTCCCTCCGAGCTGAGGTCCGCCCTGCGCTGTCCGCTGAGCGGCGACGAGCTCGTTGACGGCCTTGACGAGGCCGGTCGCCCCGCACTCGTCTCCCGGAGCGCGGGCCTGGCCTACCCGGTGCGCGACGGCGTGCCGATCCTCCTGGTCCACGAGGCATCACGCGTGCCCGCTCCCGGTTCCGACCCTCAGGGCTGA","MNRPDTAPAPEQRAVLPSELRSALRCPLSGDELVDGLDEAGRPALVSRSAGLAYPVRDGVPILLVHEASRVPAPGSDPQG$","Uncharacterized conserved protein","Cytoplasm","50kD proline rich protein","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF343","","","","","

InterPro
IPR005651
Family

Protein of unknown function DUF343
PF03966	$\"[17-59]T$	Trm112p

","BeTs to 6 clades of COG2835COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2835 is -o---z----r---efghsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB005651 (Protein of unknown function DUF343) with a combined E-value of 8.4e-09. IPB005651A 16-38 IPB005651B 50-67","","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 59 (E_value = 0.0072) place ANA_1527 in the Trm112p family which is described as Trm112p-like protein.","","proline rich protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1528","1650844","1650410","435","7.42","0.82","15560","GTGAGAAGAGTCCGACACTGCCGCAAGCCCGGCTGCGAGCGCCCAGCCGTCGCCACCCTGACTTCCGTCTACGCGGACTCCACGATCGTGCTGGGGCCACTGGCCACCGAGGCCCAGCCCGAGGCCTATGACCTGTGCGATAAGCACGTCTCCTCCTTTACGGCCCCTCGCGGCTGGCAGATCATCCGCCTGGCCACCGAGTTCGAGCCGGCGCCCCCCAGCGAGGACGACCTCCTGGCCCTGGCCGACGCCGTTCGTGAGGCCTCCCGCGCTCCGCGCCCGGTCGCCGCGCCGGCTGAGCACCGGCCCCGCCCCGGCGGGATCATGCCGGCCTCCCTGACTGCCCCGCTGCCGCCCCCTCCGGAGATCGCCGAGGACGAGATCCTGCGGCGCGGGCACCTGCGGGTCCTGCGCGGACAGAAGGGGGACGCATGA","VRRVRHCRKPGCERPAVATLTSVYADSTIVLGPLATEAQPEAYDLCDKHVSSFTAPRGWQIIRLATEFEPAPPSEDDLLALADAVREASRAPRPVAAPAEHRPRPGGIMPASLTAPLPPPPEIAEDEILRRGHLRVLRGQKGDA$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1529","1650905","1651381","477","10.72","3.44","17473","GTGACCGACCTGTTCCCCTTCTCGCCCGGGCAGATTCCTCCGCGTTCCACCGCGGCCCCGGGGCGACGCCCGAGCAGTCGTCGCGACCGGCACGGCCGGGGACTGCGCGGCCCGCTTCTGCCACCGAACCTGCCGGCCTGGCGCACCCGCGCCGAGCGCTTCGACGAGCTCGTCGTGGACGCGGCCCAGGACCTGGCCAGACGCTGGCCGTCGGTGGATCAGATCCAGTTCGCCGTCGAGGAGGTCCCGCCCTCGGATCCGGCGCCCTGGGAGCGCTCGGTGGTGCTGGGACGGGGCTTCACCGCTGAGCCCCGTGCTGGACTGCCGGCACGCGTCGTCATCTACCGCCGGCCGGTGGCCTCCCGGGCCACGAACGACGCCGAGCTGGCCGACCTGGTGCACCGTGTCGTCGTCGAGCAGGTGGCCCTCATGCTGGGACGCCGACCCGAGGAGATCGATCCCGGCTCGGCCCTGTGA","VTDLFPFSPGQIPPRSTAAPGRRPSSRRDRHGRGLRGPLLPPNLPAWRTRAERFDELVVDAAQDLARRWPSVDQIQFAVEEVPPSDPAPWERSVVLGRGFTAEPRAGLPARVVIYRRPVASRATNDAELADLVHRVVVEQVALMLGRRPEEIDPGSAL$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","Mon Aug 6 17:33:38 2007","","Mon Aug 6 17:33:38 2007","","","Mon Aug 6 17:33:38 2007","Mon Aug 6 17:33:38 2007","Mon Aug 6 17:33:38 2007","","","","","","Mon Aug 6 17:33:38 2007","","","","Mon Aug 6 17:33:38 2007","Mon Aug 6 17:33:38 2007","","","","","yes","","" "ANA_1530","1653345","1651414","1932","4.62","-36.05","64333","ATGACGCAGCACCGTCAGGACGACACCGACAGCCAGCCGGAGTCACCGAAGAAGCCCGAGCCCCAGACCCTGCAGCATGAGTCGATGAGCCCGGACCCGCAGCCGGTCGACGACGAGGCCGTCTCCGTGGACAAGACCGACGACGAGACCACGGATGAGATCGTGGACGAGGAGCCGGAGGAGGGTGCGGACAGTCCTGCCGGTCAGGACCAGGATCCAGGCAGCGACTCCCCCCACGAGGACGCTGACGAGGTCCCCCACACCGATGCCGAGGATGCTGCCAACACCGACGCCGAGGCGTCGGATGACACCGATGCTGAGAAGGTGGATGAGACTGGCACCCCCTCCACCACCCCCTCCGCGAGGCGTCGGAGGAGCCCCGCCAGCACCAGGCGGCACCGCCGGTCACTGGGGCGGACGGTTGCCCGCGGCGTCGGCGTCCTGACCTCTCTCGCGCTGGCCGCAGCCGTCGGAGGCGTCACCTGGTGGGGGCACGCCGCACCGACCACACCGACCCCGCAGCTGCAGGCCCTGAGCCTGGCTCAGCCCGGGGGCCCCACCACCTACGTCTGCCCGCACGCGCCCACCAATACGTTGCGGGGCACCGACGTCGGCGCCATGGAGTCCACCACCGCCATCGTCCCGGCCAAGGGGGCTGGTAGTGCCGAGTCGGCCACTTACGCGGGTCGGAGCATCCCCACTGATACCGCCACCTCCACGAGTACCGCCGAGGGCGGCATCCTCACCCTCGCGCCCGCGGACGGCCGGGTGGCCAACGCCGTCGGGGCGGTGACGACCTTGACCAAGAGCGGTGACCTGCGGGGGCTCACTGCTGCCCCCTGCACCCAGCCGTCCGCCATGTCCTGGATCGTGGGCGGCTCCATCGCGGCGGGCTCCTCGGCCGAGCTGCGACTGGTCAACCCCGGCGTCACCCCCGCCACCGCGAAGGTCACCCTCTACGGTTCCATCGGCCGGCTCAGCCTGCCCAGCAACGGGGAGATCACCGTGCCCGCGGGCGGCTCCTCCTCCCTGGCCCTGGAGACGAAGGGCAGCCAGGATCCGCGCATCGCCGTATCCGTTGAGGCCGACGGCGGTTCCGTGGTTCCCACTCTCGTCACCGAGTCCCTCGACGGGGAGACCCCCGCCGGCACTGACGTCATCACTCCGGGAGCCGCACCGGCCACCGATCTGGTGATCCCCGGAGTGGAGATCATCGAGCCGGCCGCACAGGGCGAGGTTCCCGACGCCAAGACCGGTGCCGACTCCTCCGACACCCCGGCCGTGCGCATCGTTAACCCCGGAGCGGACCCGGCAACTGTGTCGGTGACCATGCTCGGCAAGGACGGGGCCCGCCCGCTGAGCGGGGCGCAGTCCGTGACCATCGATGCCGGCTCCGTCTTCGACATCCAGCTGGCTGGTGTGCCCGCCGGCACCTACGGCGTGCAGGTCACCTCGAGTGCGCCGGTGGGAGCCGCCGCCCGCTTGGTGCGCAGCGGTGGTGAGTACCCTGCGCGCTCCAAGGCCCTCGTCCATGACCAGGCGTGGGCGCAGGCCGCATTGCCGGGAGCCGCGGACTCCGGCCTGCTGGCGGTGCCGCGCGCGGCCTCCCTGAGCTCAGCGGTCACCGTGGCCAACAGCGGTGAGACCACCTCGGTGACCCTGTCCTCCCTCGACGGCTCCTGGAAGCAGGACGTCAAGGTCGCCAAGGGCGCTTCCGTCGTCGTCGAGGTGCCGGCCGAGGTCTCCGCCCTCCGCCTGAACGCGGCCGGCCAGGAGAGCTCGTCGGGGACCTCACGCACCTCCAGCGGCCTGGCCGCCGCCGCCATCGTGACCGCGCAGGCCGGCGGAGACCTGGCCGGCACGCTCATCTCCACCGTGCCGGCTCAGCCCGACGCCACCGTTCAGGCCCAGCGCCGCATCCTGCTGGACTGA","MTQHRQDDTDSQPESPKKPEPQTLQHESMSPDPQPVDDEAVSVDKTDDETTDEIVDEEPEEGADSPAGQDQDPGSDSPHEDADEVPHTDAEDAANTDAEASDDTDAEKVDETGTPSTTPSARRRRSPASTRRHRRSLGRTVARGVGVLTSLALAAAVGGVTWWGHAAPTTPTPQLQALSLAQPGGPTTYVCPHAPTNTLRGTDVGAMESTTAIVPAKGAGSAESATYAGRSIPTDTATSTSTAEGGILTLAPADGRVANAVGAVTTLTKSGDLRGLTAAPCTQPSAMSWIVGGSIAAGSSAELRLVNPGVTPATAKVTLYGSIGRLSLPSNGEITVPAGGSSSLALETKGSQDPRIAVSVEADGGSVVPTLVTESLDGETPAGTDVITPGAAPATDLVIPGVEIIEPAAQGEVPDAKTGADSSDTPAVRIVNPGADPATVSVTMLGKDGARPLSGAQSVTIDAGSVFDIQLAGVPAGTYGVQVTSSAPVGAAARLVRSGGEYPARSKALVHDQAWAQAALPGAADSGLLAVPRAASLSSAVTVANSGETTSVTLSSLDGSWKQDVKVAKGASVVVEVPAEVSALRLNAAGQESSSGTSRTSSGLAAAAIVTAQAGGDLAGTLISTVPAQPDATVQAQRRILLD$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[144-164]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[50-70]?$ $\"[76-96]?$ $\"[106-126]?$ $\"[272-306]?$ $\"[316-334]?$ $\"[386-406]?$ $\"[416-436]?$ $\"[459-479]?$ $\"[520-542]?$ $\"[819-839]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[201-221]?$	transmembrane_regions

","BeTs to 5 clades of COG1216COG name: Predicted glycosyltransferasesFunctional Class: RThe phylogenetic pattern of COG1216 is A-Tk----e-R----------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","Mon Aug 6 17:40:16 2007","","Mon Aug 6 17:40:16 2007","","","Mon Aug 6 17:40:16 2007","Mon Aug 6 17:40:16 2007","Mon Aug 6 17:40:16 2007","","","","","","Mon Aug 6 17:40:16 2007","","","","Mon Aug 6 17:40:16 2007","Mon Aug 6 17:40:16 2007","","","","","yes","","" "ANA_1535","1657667","1657347","321","4.83","-6.92","11893","ATGTGGAACATCCTCGGCGACGGCCCACTGAAGCACCCAGAGGAGCCTGACGCGGAGGTACTGTCGCTCCTCTTCGGTGGCGGTGACGACGTCGATGAAGGTCCTCTGGCGTGGCAGGAGCGCGCTCTGTGCGCGCAGACGGACCCAGAGGCCTTCTTCCCTGAGAAGGGTGGTTCCACACGCGAGGCCAAGCGAGTCTGTGCGACTTGCGAGGTTCGTGAGGAGTGCCTCGAGTACGCCCTCGCCAACGACGAGCGCTTCGGTATCTGGGGCGGCATGTCGGAGCGCGAGCGGCGCAAGCTCAAGCGTCGCGCAGTATGA","MWNILGDGPLKHPEEPDAEVLSLLFGGGDDVDEGPLAWQERALCAQTDPEAFFPEKGGSTREAKRVCATCEVREECLEYALANDERFGIWGGMSERERRKLKRRAV$","Transcription factor WhiB","Cytoplasm","regulatory protein whiB","transcription factor WhiB","transcription factor WhiB","","","","","

InterPro
IPR003482
Family

Transcription factor WhiB
PF02467	$\"[38-101]T$	Whib

","No hits to the COGs database.","***** IPB003482 (Transcription factor WhiB) with a combined E-value of 1.4e-14. IPB003482A 51-61 IPB003482B 76-92 IPB003482C 98-105","","","No significant hits to the PDB database (E-value < E-10).","Residues 38 to 101 (E_value = 1.9e-38) place ANA_1535 in the Whib family which is described as Transcription factor WhiB.","","protein whiB","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1536","1657997","1658800","804","4.76","-13.90","27957","ATGCGTGATCCCTTGCTGCCGCTGCTCCCCGGCCCTCAGGATGCCGACAGACCGTGGCTCATTTGTTATGGAATCGACGAACGAGTCGAGCTGACCGGGCACGTCCTGTCCATGTGGCTGGCCAAGATCGCGGGATTCGTCACATCAGAGTCGGTGCCCGGTGACGGAGTCCATGTGGCCCTCCCCCCGCACTGGCGGAGCGTCGCCTGGGCCTGCGGTACATGGCTGGCGGGGCGCAGTGTGCTCCTGGGGAGCAACGAGGAGATCCGTACCGCCGGCCTCATCCCGGAGCTGAGTGTGGCCTTCACCCCGGAGAGCCTCTACGACGAGGCCGAGGCACAGGCGCTGGTACCTCCCGCCTCGCTGGCGCTGCGCTGGCCGGACGAGCTGCCCGCCCTCGTGCTCGACGGCGCCGCCGACCTCATGCACTACCCCGACCGCTTCACACCGGTGAGCACCGCTGCTGATTCGGTGTGCCTGACAGACCTCACCTCCGAGGCCGCTGCGCCTGCGGCTCCGGGTGCTCCTGGGGGCACTGCCCCGTCGGATGGGAGGCTCACCGTGCTGACGCGCGCCCAGCTGGCGGCCCGGGTCGAGGCGGCCGACGCCCCCACAGGAAGCGGCAGACACTCCGCCTCGCGTGCCGTCCTGGTGCGCAGCCCCGACACGGCCCAGATGCTCCAGGAGGTTCTGGTCGCCTGGCGCACCGGGCGCACGGCGGTGGTCCTCACCCCCGAGGCGGGTGACGACGTCGCCGCGGCCGCCATCCGGCAGGAGGGCATCCAGGAGGGCATCACCGCGTGA","MRDPLLPLLPGPQDADRPWLICYGIDERVELTGHVLSMWLAKIAGFVTSESVPGDGVHVALPPHWRSVAWACGTWLAGRSVLLGSNEEIRTAGLIPELSVAFTPESLYDEAEAQALVPPASLALRWPDELPALVLDGAADLMHYPDRFTPVSTAADSVCLTDLTSEAAAPAAPGAPGGTAPSDGRLTVLTRAQLAARVEAADAPTGSGRHSASRAVLVRSPDTAQMLQEVLVAWRTGRTAVVLTPEAGDDVAAAAIRQEGIQEGITA$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1537","1660046","1658856","1191","5.17","-11.60","42551","ATGAGACGACTTGAGCCGGCGCGCCAGCGGTACGCCTGGGGGTCGACTTCCGCCATCCCCGCCCTCCTGGGCAGGGACGACGACGGCGAGCCCTGGGCTGAGGCCTGGTACGGGTCTCACCCGGCCGGTCCCGCTCAGGTCGCCGAGGGCGGCGTGCTGTCCGAGCTCATCGAGGCCGAGCCGGAGCGTCTCTTAGGTGAGGACATCATCTGGCGCTTCGGGCGCAGGCTTCCCTTCCTGCTCAAGCTCATCGCTCCTGAGCAGCCCCTGTCCCTCCAGGTCCACCCCAGTCAGGCCCAGGCCGCTGAGGGCTACGCCCTCGAGGACGAGGCGGGCATCGCCCTGGACCACCCCTGTCGCAACTACAAGGACACGAACCACAAGCCGGAGATGGTCCTGGCCCTCACCCGCTTCCAGGCGGTCGCCGGCTTCCGGGCCCCGCGCCGTGCCGTCGAGGTCCTGGCCGGTCTGGACAGCCCCCTGGCTCGCCGGATGCGCCGCACCCTGCGTCTGAACCCCACCCGCTACGGCATCCGGCAGGTCTTCTCCGACGTCGTCTCATCCGCAACCCGTCCCAGCCCCCAGGAGATCGACGCCCTCGTCACCGAGATCGCCGACAGGTTCGAGGCCGGTACGTCCCCGTCGCTGCGGGTGGACTCCAATGTCGTGAAAATGGCCGGCACCTTCCCCGGGGACCCCGGCATCGCCGCCGCGCTCCTGCTCAACCCCGTCACCCTGCAGCCCGGAGAGGCGCTGTTCGTGCCCGCGGGAAGCGTGCACGCCTACATCTCCGGTCTGGGCGTGGAGGTCATGGCCTCCTCGGACAACGTGCTGCGCGCCGGACTGAGTGCCAAGCACATCGACGTCCCCGAGATGCTGGCCTGCGTCGACTACGTGGCGGCGCCGCCGGTGCGCCCCGCCCCCGAGTACCTCTCTCGCGCCACCCGCGCCTACTACGCGCCGGTGGACGACTTCGAGCTCATGGTCACCACCGTGGTGACCGCTGACGGGCGCCTGCCAGTCCCCGGACGGGGGCCACGCATCCTCCTGGCCGTCGAGGGCGCCGTGACCCTGGTGACCCAGACCGACTCCCAGACGCTCGCCCAGGGCGAGGCCGTCTTCGTCGGAGCCGACGAGCGCAGCCTGTCCGTCGAGGGGGAGGGCACCCTCGTTCAGGCCGACGTCCCCTGA","MRRLEPARQRYAWGSTSAIPALLGRDDDGEPWAEAWYGSHPAGPAQVAEGGVLSELIEAEPERLLGEDIIWRFGRRLPFLLKLIAPEQPLSLQVHPSQAQAAEGYALEDEAGIALDHPCRNYKDTNHKPEMVLALTRFQAVAGFRAPRRAVEVLAGLDSPLARRMRRTLRLNPTRYGIRQVFSDVVSSATRPSPQEIDALVTEIADRFEAGTSPSLRVDSNVVKMAGTFPGDPGIAAALLLNPVTLQPGEALFVPAGSVHAYISGLGVEVMASSDNVLRAGLSAKHIDVPEMLACVDYVAAPPVRPAPEYLSRATRAYYAPVDDFELMVTTVVTADGRLPVPGRGPRILLAVEGAVTLVTQTDSQTLAQGEAVFVGADERSLSVEGEGTLVQADVP$","Mannose-6-phosphate isomerase, class I","Cytoplasm","mannose-6-phosphate isomerase, class I","mannose-6-phosphate isomerase ","mannose-6-phosphate isomerase, class I","","Giraud M.F., Leonard G.A., Field R.A., Berlind C., Naismith J.H. RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase. Nat. Struct. Biol. 2000. 7(5):398-402. PMID: 10802738Woo E.J., Dunwell J.M., Goodenough P.W., Marvier A.C., Pickersgill R.W. Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat. Struct. Biol. 2000. 7(11):1036-1040. PMID: 11062559Woo E.J., Marshall J., Bauly J., Chen J.G., Venis M., Napier R.M., Pickersgill R.W. Crystal structure of auxin-binding protein 1 in complex with auxin. EMBO J. 2002. 21(12):2877-2885. PMID: 12065401Adachi M., Takenaka Y., Gidamis A.B., Mikami B., Utsumi S. Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 2001. 305(2):291-305. PMID: 11124907Pochapsky T.C., Pochapsky S.S., Ju T., Mo H., Al-mjeni F., Maroney M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 2002. 9(12):966-972. PMID: 12402029Fusetti F., Schroter K.H., Steiner R.A., Van noort P.I., Pijning T., Rozeboom H.J., Kalk K.H., Egmond M.R., Dijkstra B.W. Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus. Structure 2002. 10(2):259-268. PMID: 11839311Cleasby A., Wonacott A., Skarzynski T., Hubbard R.E., Davies G.J., Proudfoot A.E., Bernard A.R., Payton M.A., Wells T.N. The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution. Nat. Struct. Biol. 1996. 3(5):470-479. PMID: 8612079Titus G.P., Mueller H.A., Burgner J., Rodriguez de cordoba S., Penalva M.A., Timm D.E. Crystal structure of human homogentisate dioxygenase. Nat. Struct. Biol. 2000. 7(7):542-546. PMID: 10876237","","","

InterPro
IPR001250
Family

Mannose-6-phosphate isomerase, type I
PR00714	$\"[4-22]T$ $\"[31-46]T$ $\"[77-98]T$ $\"[122-145]T$ $\"[225-240]T$ $\"[241-260]T$ $\"[260-279]T$ $\"[279-298]T$	MAN6PISMRASE
PF01238	$\"[1-363]T$	PMI_typeI
TIGR00218	$\"[1-394]T$	manA: mannose-6-phosphate isomerase, class
PS00965	$\"[122-130]T$	PMI_I_1

InterPro
IPR014710
Domain

RmlC-like jelly roll fold
G3DSA:2.60.120.10	$\"[1-280]T$	no description

noIPR
unintegrated

unintegrated
PTHR10309	$\"[6-379]T$	MANNOSE-6-PHOSPHATE ISOMERASE

","BeTs to 9 clades of COG1482COG name: Phosphomannose isomeraseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1482 is a-----y-vdrlb-e-gh------t-Number of proteins in this genome belonging to this COG is 1","***** IPB001250 (Mannose-6-phosphate isomerase, type I) with a combined E-value of 3.4e-70. IPB001250A 6-18 IPB001250B 30-41 IPB001250C 75-96 IPB001250D 119-150 IPB001250E 220-254 IPB001250F 261-297","","","-47% similar to PDB:1PMI HUMAN RANTES (E_value = 2.7E_37);","Residues 1 to 363 (E_value = 4e-59) place ANA_1537 in the PMI_typeI family which is described as Phosphomannose isomerase type I.","","isomerase, class I (manA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1538","1660660","1660079","582","4.87","-9.11","21236","ATGGGGCAGATCGAGCTGGGCAAGCCGCTTGCCGTCGAGGAGACGCCGATTCCGGGATTCCTGCGGATCGACCTGACTGTTCACGGGGACAACCGCGGCTGGTTCAAGGAGAACTGGCAGCGGGAGAAGATGCTGGCCCTGGGGCTGCCCGACTTCGGTCCGGTTCAGAACAACATCTCCTTCAACAACGAGGTCGGGGTCACCCGCGGTATCCACGCCGAGCCCTGGGACAAGTTCGTCTCGGTGGCCACCGGCCGCGTCTTCGGCGCCTGGGTGGACCTGCGTGAGGGGCCGTCTTTCGGAGCCGTCTACACCTGCGAGATCGACCCGTCGGTGGCGGTGTTCGTGCCTCGGGGCGTGGGCAACTCCTACCAGACGCTGGAGCCCAATACCGCCTACACCTACCTGGTCAACGACCACTGGTCGGCCGATGCCCAGTACACCTTCCTCAACCTGGCCGATGAGACGGTGAACGTGCCCTGGCCGATCGCACTGAGTGAGGCCATCCTCTCCGACAAGGACAAGGCGCACCCCCGCCTGGCCGACGTCACCCCTTTCCCGGCTCCCGGGGCCCAGGCCTAG","MGQIELGKPLAVEETPIPGFLRIDLTVHGDNRGWFKENWQREKMLALGLPDFGPVQNNISFNNEVGVTRGIHAEPWDKFVSVATGRVFGAWVDLREGPSFGAVYTCEIDPSVAVFVPRGVGNSYQTLEPNTAYTYLVNDHWSADAQYTFLNLADETVNVPWPIALSEAILSDKDKAHPRLADVTPFPAPGAQA$","DTDP-4-dehydrorhamnose reductase","Cytoplasm, Periplasm","possible fused dTDP-4-keto-L-rhamnose reductaseand dTDP-4-keto-6-deoxyglucose-3,5-epimerase enzyme","dTDP-4-keto-L-rhamnose reductase ","dTDP-4-dehydrorhamnose 3,5-epimerase related","","Giraud M.F., Leonard G.A., Field R.A., Berlind C., Naismith J.H. RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase. Nat. Struct. Biol. 2000. 7(5):398-402. PMID: 10802738Woo E.J., Dunwell J.M., Goodenough P.W., Marvier A.C., Pickersgill R.W. Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat. Struct. Biol. 2000. 7(11):1036-1040. PMID: 11062559Woo E.J., Marshall J., Bauly J., Chen J.G., Venis M., Napier R.M., Pickersgill R.W. Crystal structure of auxin-binding protein 1 in complex with auxin. EMBO J. 2002. 21(12):2877-2885. PMID: 12065401Adachi M., Takenaka Y., Gidamis A.B., Mikami B., Utsumi S. Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 2001. 305(2):291-305. PMID: 11124907Pochapsky T.C., Pochapsky S.S., Ju T., Mo H., Al-mjeni F., Maroney M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 2002. 9(12):966-972. PMID: 12402029Fusetti F., Schroter K.H., Steiner R.A., Van noort P.I., Pijning T., Rozeboom H.J., Kalk K.H., Egmond M.R., Dijkstra B.W. Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus. Structure 2002. 10(2):259-268. PMID: 11839311Cleasby A., Wonacott A., Skarzynski T., Hubbard R.E., Davies G.J., Proudfoot A.E., Bernard A.R., Payton M.A., Wells T.N. The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution. Nat. Struct. Biol. 1996. 3(5):470-479. PMID: 8612079Titus G.P., Mueller H.A., Burgner J., Rodriguez de cordoba S., Penalva M.A., Timm D.E. Crystal structure of human homogentisate dioxygenase. Nat. Struct. Biol. 2000. 7(7):542-546. PMID: 10876237","","","

InterPro
IPR000888
Family

dTDP-4-dehydrorhamnose 3,5-epimerase related
PD001462	$\"[14-185]T$	Q8G7M7_BIFLO_Q8G7M7;
PF00908	$\"[12-183]T$	dTDP_sugar_isom

InterPro
IPR014710
Domain

RmlC-like jelly roll fold
G3DSA:2.60.120.10	$\"[17-191]T$	no description

noIPR
unintegrated

unintegrated
PTHR21047	$\"[4-190]T$	DTDP-6-DEOXY-D-GLUCOSE-3,5 EPIMERASE

","BeTs to 9 clades of COG1898COG name: dTDP-4-dehydrorhamnose 3,5-epimerase and related enzymesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1898 is a-mpkz---drlbcef-hsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000888 (dTDP-4-dehydrorhamnose 3,5-epimerase related) with a combined E-value of 2.4e-34. IPB000888A 17-41 IPB000888B 57-73 IPB000888C 76-122 IPB000888D 147-162 IPB000888E 168-174","","","-68% similar to PDB:1NXM The high resolution structures of RmlC from Streptococcus suis (E_value = 4.2E_49);-68% similar to PDB:1NYW The high resolution structures of RmlC from Streptoccus suis in complex with dTDP-D-glucose (E_value = 4.2E_49);-68% similar to PDB:1NZC The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose (E_value = 4.2E_49);-68% similar to PDB:2IXL RMLC S. SUIS WITH DTDP-RHAMNOSE (E_value = 4.2E_49);-46% similar to PDB:1UPI MYCOBACTERIUM TUBERCULOSIS RMLC EPIMERASE (RV3465) (E_value = 9.7E_14);","Residues 12 to 183 (E_value = 3e-20) place ANA_1538 in the dTDP_sugar_isom family which is described as dTDP-4-dehydrorhamnose 3,5-epimerase.","","fused dTDP-4-keto-L-rhamnose reductase and dTDP-4-keto-6-deoxyglucose-3,5-epimerase enzyme involved in rhamnose biosynthesis","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1539","1660847","1661737","891","5.04","-9.83","32178","ATGGGCCATGCTTGGAGCATGCGAGGAATCATTCTGGCCGGAGGCTCCGGCACGCGACTCAACCCGATCACCCTGGGGACCTCCAAGCAGCTGGTCCCCGTCTACGACAAGCCGATGATCTACTACCCGCTGAGCACCCTCATGCTCGCCGGGATCCAGGACGTCCTGGTCATCACCACCCCCCACGACGCCCCCTCCTTCCACCGCCTCCTGGGCGATGGCTCCCAGCTGGGCGTCAACCTGTCCTACACGGTTCAGCAGGAGCCCAACGGCCTGGCTCAGGCCTTCGTGCTGGGCGCCGACTTCATCGGCTCCGACAGCGCCGCCCTGGTCCTGGGCGACAACATCTTCTACGGCCCTGGCATGGGCACGCAGCTGCGCCGCCACACCAGCCCCGACGGCGGCGTCGTCTACGCCTACCAGGTCGCCGACCCGACGGCCTACGGCGTGGTCGAGTTCGACGAGACCTTCAAGGCGATCTCCATCGAGGAGAAGCCGGCCCAGCCCCGCTCCAACTACGCCGTTCCCGGCCTGTACTTCTATGACAACGACGTCGTCGAGATCGCACGGAACCTCAAGCCCTCCGCCCGCGGCGAGTACGAGATCACCGACGTCAACCGCACCTACCTGGAGGCCGGCAGGCTCACCGTGGAGGTCCTGCCCCGCGGCACCGCCTGGCTCGACACCGGCACCTTCGACTCACTGGCCGACGCCACCAGCTTCATCCGTACCGTCCAGCACCGTCAGGGCCTCAATATCGGCGCCCCCGAGGAGGTCGCCTGGCGCATGGGCTTCATCGACGACGAGGGCCTGCGCCAGCGCGCCGAGCCCCTGGTGAAGTCCGGGTACGGCGCCTACCTCCTGGGCCTGCTGGACAACCAGCAGGCCTGA","MGHAWSMRGIILAGGSGTRLNPITLGTSKQLVPVYDKPMIYYPLSTLMLAGIQDVLVITTPHDAPSFHRLLGDGSQLGVNLSYTVQQEPNGLAQAFVLGADFIGSDSAALVLGDNIFYGPGMGTQLRRHTSPDGGVVYAYQVADPTAYGVVEFDETFKAISIEEKPAQPRSNYAVPGLYFYDNDVVEIARNLKPSARGEYEITDVNRTYLEAGRLTVEVLPRGTAWLDTGTFDSLADATSFIRTVQHRQGLNIGAPEEVAWRMGFIDDEGLRQRAEPLVKSGYGAYLLGLLDNQQA$","Glucose-1-phosphate thymidylyltransferase","Cytoplasm","glucose-1-phosphate thymidylyltransferase","glucose-1-phosphate thymidylyltransferase ","glucose-1-phosphate thymidylyltransferase","","","","","

InterPro
IPR005835
Domain

Nucleotidyl transferase
PF00483	$\"[8-245]T$	NTP_transferase

InterPro
IPR005907
Family

Glucose-1-phosphate thymidylyltransferase, long form
TIGR01207	$\"[8-292]T$	rmlA: glucose-1-phosphate thymidylyltransfe

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[5-296]T$	no description
PTHR22572	$\"[15-291]T$	SUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF13	$\"[15-291]T$	GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE
signalp	$\"[1-20]?$	signal-peptide

","BeTs to 14 clades of COG1209COG name: dTDP-glucose pyrophosphorylaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1209 is aompkz--vdrlbcef--sn-j----Number of proteins in this genome belonging to this COG is 2","***** IPB005835 (Nucleotidyl transferase) with a combined E-value of 1.3e-11. IPB005835A 10-24 IPB005835B 154-166 IPB005835C 222-231","","","-79% similar to PDB:1H5S THYMIDYLYLTRANSFERASE COMPLEXED WITH TMP (E_value = 1.1E_103);-79% similar to PDB:1H5R THYMIDYLYLTRANSFERASE COMPLEXED WITH THIMIDINE AND GLUCOSE-1-PHOSPATE (E_value = 1.5E_103);-79% similar to PDB:1H5T THYMIDYLYLTRANSFERASE COMPLEXED WITH THYMIDYLYLDIPHOSPHATE-GLUCOSE (E_value = 1.5E_103);-78% similar to PDB:1MC3 CRYSTAL STRUCTURE OF RFFH (E_value = 3.6E_102);-78% similar to PDB:1IIM thymidylyltransferase complexed with TTP (E_value = 3.4E_100);","Residues 8 to 245 (E_value = 8.2e-103) place ANA_1539 in the NTP_transferase family which is described as Nucleotidyl transferase.","","thymidylyltransferase (rfbA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1540","1663411","1661843","1569","8.95","12.33","57384","ATGCGACGTGAGCTCATCAAGTACTTACGACTGCCGACCCTGGACCGCTCACGGGCCGGGGCGGTAGCGTCGCGGCGTCCGGCACTGCTTGGTGGGCTCCTCCTGGTTCTCATGCTGCTGACCGGACTCGGGTGGGCGGTGTCCTCACCAGTGGAGTCGTCCCCTGATGAGGACTTCCACCTGGGGAGCATCTGGTGTCCTCGCCCGGTGGGGGAGTACTGTCAGACCAGCGTTGTCAACGGTCGACCGGTGGCTCGGGTCCCGGTGGCGGTGTCGGACGACTCCATGAAGTGCTACAACTTCCAGCCGGACAGATCGGCGGGGTGTGCTCTCGGTTACAACGACTCGGAGATGGCCTGGACCAAACGCTTTGATCATAGCGGGGCGTACCCGGTCGGCTACTACCACTTTCACCACCTCTTCGTCGGCAAGGACGTGCAGACCTCGGTCCTGGTGATGCGCGCCGTCAACGTGCTCATCGCTGTGGCGCTACTGGGGGTGGTCGGCTTCGCTGCGCCACAGCGCTTGAGGCGGCCATTCGTGGCTGCGATCGCCGCCTCCTGGGTGCCGATGGGTATCTACTTCATTGCTTCCAACAATCCCACCTCGTGGGCCGTGTCCGGGTTGATGGCCTACTCCGCGGCGACATATATGGCCGCGCAGCAGAAGGGGCGTCGGCGTATCGCCCTGGTGATCTGCGCAGTGATCGGTGCCGTGATGTGTCTGACGTCCCGATACGACTCCGCCTTCTTCCTCCTCGTCGTCGGCCTCGCCCTGCTCTTCGTGGTGCCATGGAAACGTGGAGGATGGGTGGGGCTGGCGGCCCTGGGCGCAGTGGCCCTCCTTGGGGTCGGCACTTTCATGGCCTCGTCCCAGGTGTCGAAGGTCGCTTACTTCTTGCGTCTTTTCGAGGCGTCTGATCCCGCGAATTCCGCCAACAAGCAGTCATTCTTCGAGAAGCTCCTCATTGGGCTGGAGACAGCGCCGAAGTATCTTGGTGGATTCTGGGGACACACATGGACCCCGGGGTGGCACGACGTTCCTCTGGGAGATCGCGCGCCCTATGTGCTCACCATTATGACGGCCGGGGCTTTCGTGGCCATCGCCTTACGCCGTGGCGGGTGGCGGAAGTGGACCTCCATGGCGGTCCTCGTGGGGGCGATGGTCCTCCTTCCGGCCGTGTTCTATGCGAACGGGGCCATGGAGCACATCGAGCTCTACCAGGCGCGGTACATCTTCCCGCTGCTGGCACCCACCTTCTTCCTCATGCTGGCCGTTGACCAGGATGAGGACTCGTGGTTCACGGTTCCGCAGGCCGTGTGGGTCACAGTCTGCGCTTCGCTGTGTCAGGCAATCACTCTCCATACGCTGCTGCTGCGATTCGTTCAGGGAGTTCACAAGCGATGGGAGCTCAACCTCGACAAGCACATCGAGTGGTGGTGGAGCGTGCCGGTCTCGCCCATGATGGTCTGGTTCCTCACGACATGCGTCGCCACCGCGGCTGTGGGGGTCGCCATGGCGATGCTGACGCGTGCGCCTCAGGGGCAAGAGGAGCCACAGGAGTCGTAA","MRRELIKYLRLPTLDRSRAGAVASRRPALLGGLLLVLMLLTGLGWAVSSPVESSPDEDFHLGSIWCPRPVGEYCQTSVVNGRPVARVPVAVSDDSMKCYNFQPDRSAGCALGYNDSEMAWTKRFDHSGAYPVGYYHFHHLFVGKDVQTSVLVMRAVNVLIAVALLGVVGFAAPQRLRRPFVAAIAASWVPMGIYFIASNNPTSWAVSGLMAYSAATYMAAQQKGRRRIALVICAVIGAVMCLTSRYDSAFFLLVVGLALLFVVPWKRGGWVGLAALGAVALLGVGTFMASSQVSKVAYFLRLFEASDPANSANKQSFFEKLLIGLETAPKYLGGFWGHTWTPGWHDVPLGDRAPYVLTIMTAGAFVAIALRRGGWRKWTSMAVLVGAMVLLPAVFYANGAMEHIELYQARYIFPLLAPTFFLMLAVDQDEDSWFTVPQAVWVTVCASLCQAITLHTLLLRFVQGVHKRWELNLDKHIEWWWSVPVSPMMVWFLTTCVATAAVGVAMAMLTRAPQGQEEPQES$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-46]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[150-170]?$ $\"[180-198]?$ $\"[204-219]?$ $\"[228-246]?$ $\"[250-265]?$ $\"[270-290]?$ $\"[352-370]?$ $\"[380-400]?$ $\"[439-459]?$ $\"[489-509]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-47% similar to PDB:1KIT VIBRIO CHOLERAE NEURAMINIDASE (E_value = );-47% similar to PDB:1W0O VIBRIO CHOLERAE SIALIDASE (E_value = );-47% similar to PDB:1W0P VIBRIO CHOLERAE SIALIDASE WITH ALPHA-2,6-SIALYLLACTOSE (E_value = );-58% similar to PDB:2C0N CRYSTAL STRUCTURE OF A197 FROM STIV (E_value = );-59% similar to PDB:2DMC Solution structure of the 18th Filamin domain from human Filamin-B (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1541","1664470","1663466","1005","5.41","-8.36","35554","GTGTTCATCGACAGGCTGATGGCTCATGGTGAGACGTCAGCAGGACGACGTTCTGCGGGAAGGAAGAGACGGCCAGTGAAAGAGACCATACCCCTGCAGACCGAGGGAACCTCCCTCCCTCGTGCCGGGCGCGACGAAGGGGAGACGCGCGGACGTGTTCTCGTCACCGGCGCCAACGGTCAGCTGGGGCGTGCTCTCATGGCCCTGCTGCCGCAGGCGGGATTCGATCCCATCGGCGTCGACCTGCCTGAGGTGGACATTTCGGATGCGGCCGCCATGTCCTCCTGGGACTGGACTGGCTACGACATCATCATCAATGCCGCGGCCTGGACCAACGTGGACGGGGCGGAGACCCCTGAGGGGCGCCGTCTGTCCTGGCGGGCCAACACGGTCGGCCCGGTCAACCTGGCCCGGGCGGCCGTCCAGCACGGCCTGACCCTGGTGCACCTGTCCACCGAGTACACCTTCGACGGCGTGACGGCTGTCCACACCGAGGAGGAGACCCCCTCACCGCTGGGCGTCTACGGTCAGTCCAAGGCGGCAGGGGATGCCGCCGTCAGCGTCTGCCCTCGGCACTACCTGGTGCGCACCTCCTGGGTGGTCGGCGATGGCAAGAACTTCGTCAAGACGATGCTCTCCCTGGCCGAGCGCGGTATCAGCCCACAGGTTGTGGCCGACCAGACCGGGCGTCTCACCTTCGCCTCCGATCTGGCAGCCGGCATCATCCACCTCATTACCTCGGGCGCCGAGTTCGGCACCTACAACCTCTCCGGTGACGGCCCGATCCTCTCCTGGGCCGATATCGCCAAGCGGGTCTACGAGAGTGCAGGCCACAGCCCCGATGAGGTCACTCCCGTCACCACTGAGGAGTACTACGCCGGTCAGGAGGGGATTGCGCCGCGGCCACTGAGCTCGGCCCTGGACCTGGCGAGGATCAAGGCCACAGGCTTCACCCCGGCTGACTCCACGGAGCGCCTGGACGTCTATCTTCAGGGCCTCCTGTAG","VFIDRLMAHGETSAGRRSAGRKRRPVKETIPLQTEGTSLPRAGRDEGETRGRVLVTGANGQLGRALMALLPQAGFDPIGVDLPEVDISDAAAMSSWDWTGYDIIINAAAWTNVDGAETPEGRRLSWRANTVGPVNLARAAVQHGLTLVHLSTEYTFDGVTAVHTEEETPSPLGVYGQSKAAGDAAVSVCPRHYLVRTSWVVGDGKNFVKTMLSLAERGISPQVVADQTGRLTFASDLAAGIIHLITSGAEFGTYNLSGDGPILSWADIAKRVYESAGHSPDEVTPVTTEEYYAGQEGIAPRPLSSALDLARIKATGFTPADSTERLDVYLQGLL$","DTDP-4-dehydrorhamnose reductase","Cytoplasm, Extracellular","possible fused dTDP-4-keto-L-rhamnose reductaseand dTDP-4-keto-6-deoxyglucose-3,5-epimerase enzyme","dTDP-4-dehydrorhamnose reductase ","dTDP-4-dehydrorhamnose reductase","","","","","

InterPro
IPR005913
Family

dTDP-4-dehydrorhamnose reductase
PF04321	$\"[52-334]T$	RmlD_sub_bind

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[52-247]T$	no description
PTHR10491	$\"[52-334]T$	DTDP-DEHYDRORHAMNOSE DEHYDROGENASE

","BeTs to 13 clades of COG1091COG name: dTDP-4-dehydrorhamnose reductaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1091 is aompkz-q-drlbcef--sn-jx---Number of proteins in this genome belonging to this COG is 1","***** IPB005913 (dTDP-4-dehydrorhamnose reductase) with a combined E-value of 1.8e-47. IPB005913A 51-62 IPB005913B 92-131 IPB005913C 134-172 IPB005913D 193-239 IPB005913E 252-272 IPB005913F 286-324","","","-58% similar to PDB:1VL0 Crystal structure of DTDP-4-dehydrorhamnose reductase, rfbD ortholog (CAC2315) from Clostridium acetobutylicum at 2.05 A resolution (E_value = 4.1E_36);-54% similar to PDB:1KBZ Crystal Structure of apo-dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) from Salmonella enterica serovar Typhimurium (E_value = 1.5E_22);-54% similar to PDB:1KC1 Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH (E_value = 1.5E_22);-54% similar to PDB:1KC3 Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose (E_value = 1.5E_22);-54% similar to PDB:1N2S CRYSTAL STRUCTURE OF DTDP-6-DEOXY-L-LYXO-4-HEXULOSE REDUCTASE (RMLD) IN COMPLEX WITH NADH (E_value = 1.5E_22);","Residues 52 to 334 (E_value = 7e-72) place ANA_1541 in the RmlD_sub_bind family which is described as RmlD substrate binding domain.Residues 53 to 257 (E_value = 1.2e-11) place ANA_1541 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 54 to 286 (E_value = 1.6e-05) place ANA_1541 in the 3Beta_HSD family which is described as 3-beta hydroxysteroid dehydrogenase/isomerase family.Residues 55 to 241 (E_value = 9e-06) place ANA_1541 in the NAD_binding_4 family which is described as Male sterility protein.","","fused dTDP-4-keto-L-rhamnose reductase and dTDP-4-keto-6-deoxyglucose-3,5-epimerase enzyme involved in rhamnose biosynthesis","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1542","1665668","1664547","1122","6.58","-3.55","40382","ATGAAGGTTCTTCTTGATGCGACGGCGATCCCGGCTGATCTCGGAGGCGTGGGGCGCTATGTCGACGACCTGGTCCCCGAGCTCATCGCCTGCGGCGTCAACCTGGCCATGGCCGTCCAGCAGCGGGACGTGGCGCACTTCTCCGCCAAGGTGCCCCGGGCTCACCTCTTCCCGGTCTCGCAGTCCATGGAGTCGCGCGGCGCCCGGATGGCCTGGGAGCAGACGGGGCTGCCGGCACTCATTCACCGGCTCCGTCCCGATGTCCTGCACTCGCCCCACTACACCTTCCCGGCCCTGCACCAGGTGCCCGTGGTCGTCACCCTCCACGACGCCACGTTCTTCTCCCACCCGCAGGCGCACTCGCCCCTCAAGCAGAAGTTCTTCACCAACGCCATCCGCCGAGCCGTGCGGCGGGCCGACGCACTGGTCGTCCCCTCACAGGCCACTCGCGACGAGACCATCAAGTACGTCGGTGGCGACCCCGAGCGCTTCCACGTCGCCTACCACGGAGTGGACACCTCCGTGTTCCACCCGGTCGACGACGCCGAGCGGGCCCGCGTGGCCGCCTCCCTCGGACTGGAGGGCCGGCGCTACATCGGTTTCCTGGGGACCCTGGAGCCTCGCAAGAACGTCCCCAACCTGGTGCGCGCCTGGGCCAGCGTCTTCCGCGACTGCGAGGACGCCCCGGCCCTCGTCCTGGCCGGCGGACCCGGCTGGGACGAGGACATTGAGCCCGCCCTGGCGCAGGTGCCCCGGCACCTGAGCGTCCTGCGGCCCGGCTACCTGCCCCTGGAGGACCTGCCCGGATTCCTGTCCGGCTGCGAGATCCTGGCCTATCCCTCCATCGGCGAGGGCTTCGGCCTGCCGGTCCTGGAGGCCATGGCCTGCGGGGCCGCCGTGCTCACCACCCGCGAGCTGAGCCTGCCGGAGGTCGGGGGCGACGCCGTCGCCTACTGCGGATCGGATGCGCAGGCCATCGCCCGGGGCCTCGTGGTCCTGGACGCCCAGCCCGAGCGGCGCCGGGAGCTGGGGGCCGCCGCCCTGGAGCGGGCCGCCGAGTTCACCTGGAGGGCCTCGGCTCAGGCGCACGTCGAGGCCTACCACGCCGCCATGGCGCGCTAG","MKVLLDATAIPADLGGVGRYVDDLVPELIACGVNLAMAVQQRDVAHFSAKVPRAHLFPVSQSMESRGARMAWEQTGLPALIHRLRPDVLHSPHYTFPALHQVPVVVTLHDATFFSHPQAHSPLKQKFFTNAIRRAVRRADALVVPSQATRDETIKYVGGDPERFHVAYHGVDTSVFHPVDDAERARVAASLGLEGRRYIGFLGTLEPRKNVPNLVRAWASVFRDCEDAPALVLAGGPGWDEDIEPALAQVPRHLSVLRPGYLPLEDLPGFLSGCEILAYPSIGEGFGLPVLEAMACGAAVLTTRELSLPEVGGDAVAYCGSDAQAIARGLVVLDAQPERRRELGAAALERAAEFTWRASAQAHVEAYHAAMAR$","Glycosyl transferase, group 1","Cytoplasm","mannosyltransferase B, putative","glycosyl transferase; group 1","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[184-350]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-372]T$	GLYCOSYLTRANSFERASE

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[178-349]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[104-365]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF29	$\"[104-365]T$	MANNOSYLTRANSFERASE

","BeTs to 21 clades of COG0438COG name: Glycosyltransferases IFunctional Class: MThe phylogenetic pattern of COG0438 is AMTKYQVCEBRhUj--o---XNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-42% similar to PDB:2GEJ Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man (E_value = 1.3E_10);-42% similar to PDB:2GEK Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP (E_value = 1.3E_10);","Residues 216 to 387 (E_value = 1.4e-27) place ANA_1543 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","WbpY PA5448","","1","","","Mon Aug 6 17:46:13 2007","","Mon Aug 6 17:46:13 2007","","","Mon Aug 6 17:46:13 2007","Mon Aug 6 17:46:13 2007","Mon Aug 6 17:46:13 2007","","","Mon Aug 6 17:46:13 2007","","","Mon Aug 6 17:46:13 2007","Mon Aug 6 17:46:13 2007","","","Mon Aug 6 17:46:13 2007","Mon Aug 6 17:46:13 2007","","","","","yes","","" "ANA_1545","1666939","1667937","999","9.04","3.90","35779","GTGACCCAGCCCGTCAGGCGTCCCTCAGCCCGCGTCGTCATCGTCAACTGGCGCCAGGCCGAACTCACGATCCGGGCGGCCCGCTCCATCCGTGAGCAGCTGGGAGACCGGGACGGGCTCGTCATCGTGGACAACGCCTCCGGTGACGGCTCAGCCGAGCGTCTGCGCCGGGAGGGACTCACCGTGGTCGAGTCGAGCGAGAACCGGGGCTTCGGTGCCGGCGTCAACCTCGGGGCCCTTGGCATGGAGGAGGAGGTCCTCGTCCTGCTCAACAATGACGCGGTGGCCGAGCCCGGCTTCCTCGAGGCGCTCCTGGCCGCCCTAAGCGACCCGCCGTCCGCAGTGGCTCCGGCTGCGGCGACGGCACGGATCCTGCTGGCCGGCCGCTGGAAGCCGGCGGCCCCGGGGCAGCCGGACGCACTCGTCTCCCCCCGCACCGGGCGGTGGACCCGACTCGATGACCAGGCCGCTGCCCGCGGCGAGGGGGAGGTCCTGGTCAACTCCACGGGCAACCTGGTGGATGCCTCTGGCAACGGCTACGACCGGGACTGGCTGGTGCCCGCTGGGCAGGAGCACTCCCCCAGTGAGGTCTTCGGCCTGTGCGGGGGCGCCTGCGCGATCCGACGTGAGGCGTGGCAGGCCCTGGGGGGCTTTCGCGAGGACCTGTTCATGTACTACGAGGACACGGATCTGTCCTGGCGCCTACGTGAGCGCGGCTGGCGAGTCCTCTACGTGCGCGAGGCCGTGGCGCGCCACGATCACGCCTCCTCCTCGGGCACGGACTCACCGATGTTCATCCGGGTCAACGCCCGCAACCGGATTCTGACGGCAGCCGCTCACAGTCCGGCCCCGGTGGTGATGCAGGCGCTGGCCCGTACGCTGGTGCGCACCGTGCGAGGACCGCAGCGCGGCCCGGTGATGACCGGGCTGGCCCAGGCGGTCCTCGGCCTGCCGCGCGAGCTGCGTCGACGGGCGAGGGGATCGTCGAGTAGCCAGTGA","VTQPVRRPSARVVIVNWRQAELTIRAARSIREQLGDRDGLVIVDNASGDGSAERLRREGLTVVESSENRGFGAGVNLGALGMEEEVLVLLNNDAVAEPGFLEALLAALSDPPSAVAPAAATARILLAGRWKPAAPGQPDALVSPRTGRWTRLDDQAAARGEGEVLVNSTGNLVDASGNGYDRDWLVPAGQEHSPSEVFGLCGGACAIRREAWQALGGFREDLFMYYEDTDLSWRLRERGWRVLYVREAVARHDHASSSGTDSPMFIRVNARNRILTAAAHSPAPVVMQALARTLVRTVRGPQRGPVMTGLAQAVLGLPRELRRRARGSSSSQ$","Glycosyl transferase, family 2","Cytoplasm","AprG1","glycosyl transferase; family 2","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[11-216]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[8-257]T$	no description

","BeTs to 8 clades of COG1216COG name: Predicted glycosyltransferasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1216 is a-m-kz---dr--cef--s--j----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 216 (E_value = 1.1e-12) place ANA_1545 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","(AF187550) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1546","1668069","1669169","1101","5.49","-14.48","40784","ATGGCTGGACCCGCCACACAATCCCCACGGGTCACCGTGGTGACCCGGACCCGCAACCGTCCCCTGATGCTCAGGCGAGCGGTCCAGTCGGTCGGGGCGCAGTCCTTCCAGGACCTCGAGCTCGTCATCGTCAATGACGCCGGAAGCACCGAGCCCGTGGAGAGTGCTCTGGAGAGTGCCCCCCAGTGGCTCAAGGGGCGCACCCGGGTGGTCACCAATGAGACCTCTCACGGACGCGAGGCCGCCCTGGAGGATGGTCTGGCCGCCTCCTCCTGCGAGTTCTTCGCGATCCATGACGACGACGACTCCTGGGAGCCCGGCTTCCTGGCCGCCTGCGTGGCCCACCTCGATGAGCACCCCGAGCACGGCGCCGTGGCGGCGCGCTGCGACCTGATCGATGAGATAGTCACGGAGGAGGGACTGACTGAGCGCTGCCGGGGGCCTTTGGCCCAGGACAAGGAGAGCTGGACCCTCATCGACACGATGGTGGCCAACTACGTCCCACCGATCTCACAGCTCATCCGCCGTGAGGTGGCCGACCGCATCGGCCACTGGGACGGGACCCTGCTGACCCAGGCCGACTGGGACTTCAACCTGCGTCTGCTGGCGACCTCCCCGGTGGGCTTCATCGACGGGGAGCCGCTGGCGCACTGGCACCACCGCGACTCCACCGACGGAACGATGGGTAACTCCGTCGTCGTCGACGCCGTCCACCACCGCACCGACAACCTCGCCATCCGGGACCGCTACGCCCGCCTGTCCCTGGAGGGCACCGAGGCCGCGGCCGCCGCTCCACGGAGTGTACCGGTGGACTCCGAGAACCTGGGTCTCCTGTTGGTCTCCGCGGAGTACTACCACCGTCTCCAGGAGAGACTGGAGAAGCAGGACAAGGAGATCGAGCATCTCAAGGGGACCATGCACGAGCTGGGCTCGGGCATCGACCAACTGCGCAATGAGGTGCGCGACGAGCTCCGTAGCACGACGCAGCAGGTCCTGAATCAGACCTACGACATCAGTGCGAAGATCGATCGCGTTGAGGCCACGGTCAAGCCCTTCTTCCGCACCGTGGCTCAGCACATCAAGAGGATTCGGCGAGGCTGA","MAGPATQSPRVTVVTRTRNRPLMLRRAVQSVGAQSFQDLELVIVNDAGSTEPVESALESAPQWLKGRTRVVTNETSHGREAALEDGLAASSCEFFAIHDDDDSWEPGFLAACVAHLDEHPEHGAVAARCDLIDEIVTEEGLTERCRGPLAQDKESWTLIDTMVANYVPPISQLIRREVADRIGHWDGTLLTQADWDFNLRLLATSPVGFIDGEPLAHWHHRDSTDGTMGNSVVVDAVHHRTDNLAIRDRYARLSLEGTEAAAAAPRSVPVDSENLGLLLVSAEYYHRLQERLEKQDKEIEHLKGTMHELGSGIDQLRNEVRDELRSTTQQVLNQTYDISAKIDRVEATVKPFFRTVAQHIKRIRRG$","Glycosyl transferase, family 2","Cytoplasm","glycosyl transferase, group 2 family proteindomain protein","glycosyl transferase; family 2","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[12-183]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[9-259]T$	no description
PTHR22916	$\"[17-203]T$	GLYCOSYLTRANSFERASE

","BeTs to 11 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 183 (E_value = 4.9e-19) place ANA_1546 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","transferase, group 2 family protein domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1547","1670487","1669198","1290","6.30","-5.25","46988","ATGACTGCAACCACCGGATCGTCCGCATCATCAACGTCGTCGGCGCAGAGCACCTCGGTAGCATCCCCGGCCGTGCGCATTGAGGACGTCTCCAAGCGCTTCCGGATCTACCACCACCGCAACCAGTCCCTCAAAGGCGCCATTCTGCAGCGCAGCCGTGGCGTCTACGAGGACTTCTGGGCACTCAAGGACATCACCTTCGACATCCCCGAGGGCAAGACCTTCGGGCTCATGGGGCACAACGGCTCGGGTAAGTCCACTCTGCTCAAGTGCATCGCCAAGATTCTGGCTCCCGACTCGGGCTCCATCACCGCCCGGGGGCGCATGGCCGCCATGCTGGAGGTCGGCTCGGGCTTCCACCCCGAGCTCTCCGGGCGGGAGAACATCTTCCTCAACGGTGCCATCCTGGGGATGAGCCGTCGTGAGATCGAAGCCAAGTTCGATGACATCGTGGACTTCTCCGGAGTGGGTGAGTTCATCGACCAACCGGTGAAGAACTACTCCTCGGGCATGTACGTGCGCCTGGGCTTCTCGGTGTCCATTCACGTCGAGCCGGAGATCCTCCTGGTTGACGAGGTCCTGGCCGTCGGTGACATGGAGTTCCAGGAACGGTGCATGGACAAGTTCGCCGAGTTCCGCGAGGACGGTCGCACCGTCGTCGTCGTCTCTCACGGCCTGGCGCAGATGCGCACCTTCTGCGATGAGGTCGCCTGGCTCGACCACGGCCGGCTCAAGGAGGTCGGGCCGGCCCCCGAGGTCATCGACAAGTACTCCGATATCACCCACGGCGCCAAGAAGGTCAAGGACGGCATCGGCACCCGCTTCGGCAGCGGTGAGGCCCAGATCAGCCGCATCGAGCTGCTGGACCGCACGGGCCGGCCGGTGAACTCCCTGCGTACCGGGGACGAGGCCACTATTCGCCTTCACTACCGCTGTGAGGAGACGATTGAGAAGCCCGTCTTCGGCTGCTCCATCGACACCCGGGAGGGCATCTTCGCCTGGGGACTTCACGGCCTCGACGACGGCTTCCAGCCCGAGAGGATCGAGCCGGGCGAGGGGGCCGTGGACGTCTCCATACCCGCCATGATGCTGCGGCCGGGGGCCTACCTCATCTCCGGCTCCATCCAGCCCTGGCAGCTCTCCAGCGTCATCGACGCCTACCAGAAGGCCACCTCCTTCGACATCGTCCCCGGACCGCGCATGGAATCCGGGGGCCTGGTGGCCCTGGGGGCCCACTACGAGCGGATCACCCCGCCGCGCCCCATGGTCAAGCACACCAAGAACAGCTGA","MTATTGSSASSTSSAQSTSVASPAVRIEDVSKRFRIYHHRNQSLKGAILQRSRGVYEDFWALKDITFDIPEGKTFGLMGHNGSGKSTLLKCIAKILAPDSGSITARGRMAAMLEVGSGFHPELSGRENIFLNGAILGMSRREIEAKFDDIVDFSGVGEFIDQPVKNYSSGMYVRLGFSVSIHVEPEILLVDEVLAVGDMEFQERCMDKFAEFREDGRTVVVVSHGLAQMRTFCDEVAWLDHGRLKEVGPAPEVIDKYSDITHGAKKVKDGIGTRFGSGEAQISRIELLDRTGRPVNSLRTGDEATIRLHYRCEETIEKPVFGCSIDTREGIFAWGLHGLDDGFQPERIEPGEGAVDVSIPAMMLRPGAYLISGSIQPWQLSSVIDAYQKATSFDIVPGPRMESGGLVALGAHYERITPPRPMVKHTKNS$","ABC-type polysaccharide/polyol phosphate transport system, ATPase component","Cytoplasm, Membrane","ABC transporter, ATP-binding protein","ABC transporter related","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[166-205]T$	O29951_ARCFU_O29951;
PF00005	$\"[72-242]T$	ABC_tran
PS50893	$\"[25-266]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[71-242]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[52-258]T$	no description
PTHR19222	$\"[25-34]T$ $\"[57-257]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF2	$\"[25-34]T$ $\"[57-257]T$	SIALIC ACID ABC TRANSPORTER

InterPro
IPR000412
Family

ABC-2
PS51012	$\"[36-280]T$	ABC_TM2

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[17-249]T$	ABC2_membrane

InterPro
IPR013526
Family

ABC-2 transporter
PR00164	$\"[38-59]T$ $\"[152-176]T$ $\"[189-208]T$	ABC2TRNSPORT

noIPR
unintegrated

unintegrated
tmhmm	$\"[40-60]?$ $\"[74-96]?$ $\"[117-146]?$ $\"[152-172]?$ $\"[193-211]?$ $\"[256-276]?$	transmembrane_regions

","BeTs to 12 clades of COG1682COG name: ABC-type polysaccharide/polyol phosphate export systems, permease componentFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1682 is a------q--rlbc-fghsnujx---Number of proteins in this genome belonging to this COG is 2","***** IPB000412 (ABC transporter, family 2) with a combined E-value of 4.5e-07. IPB000412A 31-54 IPB000412C 210-250","","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 249 (E_value = 5.7e-12) place ANA_1548 in the ABC2_membrane family which is described as ABC-2 type transporter.","","subunit of A-band LPS efflux transporter PA5451 , putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1549","1672457","1671363","1095","5.33","-10.99","39124","GTGACCCGTACCTGCCTTGTCACAGGTGGTGCCGGATTCATCGGCTGCGCGATCTCGCGTGACCTGGCCGACGCCTTCGACCGCGTCGTGGCCCTGGACAACATGCACCCGCAGATCCACCCCTCCCAGGCTCGCCCTGCCGAGCTCGACGAGCGTGTGGAGCTGCGCCGCCTGGACGTGTCGCTCGCCGAGGACTGGGACGCGCTCCTGGCCGAGGTCGCACCGGACGTCATCGTCCACCTGGCCGCGGAGACCGGGACCGGTCAGTCCCTCACCGAGGCCTCCCGGCACGCGAATGTCAACGTCGTCGGCACCACCCAGATGCTCGACGCCCTCGTGCGCCACGAGAGCCGTCCCAACAAGATCGTCCTGGCCTCTTCCCGGGCCGTCTACGGTGAAGGGAAATGGATCGATGCCGAAGGGCGCCCCTCCTACCCCGGGCAGCGCACCCACGCGATGCTCGAGGCCGGCCAGTGGGACTTCGCCGGCCTGACCCCCTCGGTGCAGTCCTCAACCGAGGTCAAGGCATCCCCGGCCAATGTCTACGCCGCCACCAAGTTCTGCCAAGAGAACCTCGTGACCTCCTGGTGCGGCTCCTTCGGCGTCACCCCGGTGCTCTATCGGCTTCAGAACGTCTATGGCCCCGGCCAGTCCCTCATCAACCCCTACACCGGCATCGTCTCCCTCTTCGCCCGCCTGGCCAAGCAGGGAAAGTCCATCCCGGTCTACGAGGACGGCCAGATCGTGCGGGACTTCGTCTTCATTGACGACGTCGCCTCCGCCATCGTGGCCGGCGTCCTGCACTCGCCGGCCGCCGCCCTGCCCTACGACATCGGCCTGGGGGAGCGGACCACCATCATGCAGGTCGCTCAGGCCATCGCCGAGCACTATGGAGCGCCGGCCCCGCACGTCACCGGACAGTTCCGCGACGGAGATGTGCGCGCAGCCTGGGCGGACACCGCGCGTGCCCGCCAGGCGCTGGACTGGGAGCCCCGGGTCGGTGTCACCGAGGGCATCAACCGGCTGTGCGACTGGATCGATGCCCAGGAGGGGGCGGTTGCCCCCACGCCCACCAGAACTGCGACGGAGGTGTGA","VTRTCLVTGGAGFIGCAISRDLADAFDRVVALDNMHPQIHPSQARPAELDERVELRRLDVSLAEDWDALLAEVAPDVIVHLAAETGTGQSLTEASRHANVNVVGTTQMLDALVRHESRPNKIVLASSRAVYGEGKWIDAEGRPSYPGQRTHAMLEAGQWDFAGLTPSVQSSTEVKASPANVYAATKFCQENLVTSWCGSFGVTPVLYRLQNVYGPGQSLINPYTGIVSLFARLAKQGKSIPVYEDGQIVRDFVFIDDVASAIVAGVLHSPAAALPYDIGLGERTTIMQVAQAIAEHYGAPAPHVTGQFRDGDVRAAWADTARARQALDWEPRVGVTEGINRLCDWIDAQEGAVAPTPTRTATEV$","Sugar nucleotide epimerase/dehydratase","Cytoplasm","sugar nucleotide epimerase/dehydratase","putative sugar nucleotide epimerase/dehydratase","NAD-dependent epimerase/dehydratase","","Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 1997. 36(21):6294-6304. PMID: 9174344","","","

InterPro
IPR001509
Family

NAD-dependent epimerase/dehydratase
PF01370	$\"[5-279]T$	Epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[3-307]T$	no description
PTHR10366	$\"[7-148]T$ $\"[178-349]T$	NAD DEPENDENT EPIMERASE/DEHYDRATASE

","BeTs to 13 clades of COG0451COG name: Nucleoside-diphosphate-sugar epimerasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0451 is aompk-yqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB001509 (NAD-dependent epimerase/dehydratase) with a combined E-value of 1.2e-35. IPB001509A 6-17 IPB001509B 76-113 IPB001509C 178-187 IPB001509D 277-298 IPB001509E 309-349***** IPB008089 (Nucleotide sugar epimerase signature) with a combined E-value of 8.5e-14. IPB008089B 250-265 IPB008089C 273-288 IPB008089D 312-329***** IPB002225 (3-beta hydroxysteroid dehydrogenase/isomerase) with a combined E-value of 5.1e-10. IPB002225A 2-40 IPB002225E 307-353","","","-43% similar to PDB:1BXK DTDP-GLUCOSE 4,6-DEHYDRATASE FROM E. COLI (E_value = 9.2E_21);-43% similar to PDB:2HUN Crystal structure of hypothetical protein PH0414 from Pyrococcus horikoshii OT3 (E_value = 5.9E_20);-41% similar to PDB:2P5U Crystal structure of Thermus thermophilus HB8 UDP-glucose 4-epimerase complex with NAD (E_value = 7.8E_20);-41% similar to PDB:2P5Y Crystal structure of Thermus thermophilus HB8 UDP-glucose 4-epimerase complex with NAD (E_value = 7.8E_20);-41% similar to PDB:1R6D Crystal Structure of DesIV double mutant (dTDP-glucose 4,6-dehydratase) from Streptomyces venezuelae with NAD and DAU bound (E_value = 1.1E_18);","Residues 3 to 142 (E_value = 1.9e-05) place ANA_1549 in the adh_short family which is described as short chain dehydrogenase.Residues 4 to 344 (E_value = 2.1e-05) place ANA_1549 in the RmlD_sub_bind family which is described as RmlD substrate binding domain.Residues 5 to 279 (E_value = 3.5e-41) place ANA_1549 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 6 to 309 (E_value = 1.5e-06) place ANA_1549 in the 3Beta_HSD family which is described as 3-beta hydroxysteroid dehydrogenase/isomerase family.Residues 7 to 262 (E_value = 1e-07) place ANA_1549 in the NAD_binding_4 family which is described as Male sterility protein.","","nucleotide epimerase-dehydratase (AF143772)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1550","1673694","1672603","1092","9.72","13.58","40772","GTGGCGGATACGGCGATATCGAGCCGGCGGACGGCCAGGAGACCCAGGGTTTTCTACCTGGACCTCATCCGGGCGCTGGCCGCTGTACTCATCGTCCTCACCCACTTCAACTATCACCTGCGCGAGCACGGAGGCGGCTACGTCCTAACCTTCCAGCCCTTCGGTGTCTATGTGGGCGCCCTGGGCGTCTCCCTGTTCCTCATCATCTCTGGTGCCGCCCTGACCCTGACCTACCGGCGGCCCATCAACCTCAAACGCTTCTACTGGAAGCGGTTCGTCAACATCTACCCGATGTTCTGGACCGCCTGGGTGCTGGGGACTCTCTACTACTTCCTCATCTTCAACGGGCGGCCTCCCAACGCCGCTCCGGCGAAGTCCTTCATCTTCACGCTTCTGGGAGTCGACGGCCTCGCCGCAGCCTTCGGCTGGCCCACGATGTATCTGCTGGGGGAGTGGTTCCTCGGCTTCATCCTCCTGTACTACCTCGTCTTCCCGGCGCTGCTGTGGGCCATCGACCGCTTCCCGGTCGTCACCGGCGTCGTGCTGCTGGCGGCCTATGCCGCCACGGTGTTCATCATGCAGCACTACTTCGGGGGCTACCGCTCGGCCATGATTCTCACTACCAGGCTCCCCGAGCTGGCCTTCGGCAGCTATTTCGTCCGCTATGTCCGCCGGGTCCACGGGGCCACCGTCATCCCGGCAGCTGCGGTCCTGGCTGTCTGTGCGATGCTCCCCGAGGAGATTCCCGAGGACGTGGGCACCACCATCGTGGGCATCTCGGCCTTCCTCATCCTCGTGGTCGTCGGTCGCTATGTGGCGATCCAGCCGGTTCGCGCCCTCGTCAGCCTCATCGCCCGGTACTCCTACCCGATCTTCCTCGTCCACCACGTGGTGATCCTGCTGGTCCTGCAGAAGGTTGACGTCTACGGCTTCTACCCCCTTCAGCGCTACATGCTGCTGGCAGCCGAGTTCGTCCTCATTTTCGCCCTGTCAGTGGGGCTGGAGAAGGTCTCCGGCATCGTCGTCGACTTCGTCACCACCGCCTTCAAGGGCATGAGCTGGCGCCCCGAGGTGTCCGAGGCTGAGCGCTGA","VADTAISSRRTARRPRVFYLDLIRALAAVLIVLTHFNYHLREHGGGYVLTFQPFGVYVGALGVSLFLIISGAALTLTYRRPINLKRFYWKRFVNIYPMFWTAWVLGTLYYFLIFNGRPPNAAPAKSFIFTLLGVDGLAAAFGWPTMYLLGEWFLGFILLYYLVFPALLWAIDRFPVVTGVVLLAAYAATVFIMQHYFGGYRSAMILTTRLPELAFGSYFVRYVRRVHGATVIPAAAVLAVCAMLPEEIPEDVGTTIVGISAFLILVVVGRYVAIQPVRALVSLIARYSYPIFLVHHVVILLVLQKVDVYGFYPLQRYMLLAAEFVLIFALSVGLEKVSGIVVDFVTTAFKGMSWRPEVSEAER$","Acyltransferase 3","Membrane, Cytoplasm, Extracellular","Acyltransferase family, putative","hypothetical protein predicted by Glimmer/Critica","acyltransferase 3","","","","","

InterPro
IPR002656
Domain

Acyltransferase 3
PF01757	$\"[17-349]T$	Acyl_transf_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[20-38]?$ $\"[57-77]?$ $\"[92-112]?$ $\"[126-144]?$ $\"[146-166]?$ $\"[172-192]?$ $\"[226-244]?$ $\"[254-274]?$ $\"[289-311]?$ $\"[325-345]?$	transmembrane_regions

","BeTs to 6 clades of COG1835COG name: Predicted acyltransferasesFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1835 is ----------rlb-ef-hsn-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 349 (E_value = 9.7e-10) place ANA_1550 in the Acyl_transf_3 family which is described as Acyltransferase family.","","family, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1551","1675577","1673697","1881","5.81","-14.55","71901","ATGGCAACGCTTGGTGAGGACCCGAAGCGACTCGGCATCTTCTTCTTCTTCGACGCTCAAGGGGTCGCGGACTCCTACGTCGAGGCCCTCCTCGCCGACATGGTCAAGAACCTCTCCGAGCTGGTCATTGTCGTCAACGGCGAACTGACCGCCACGAGCTACGCCAAGCTGAGCGCCTTCACGGACAACATCATTCTGCGTGAGAACAAGGGGCTGGACGCCTGGGCCTACAAGACGGCCCTGGAGAGCTACGGCTGGGACAGGCTCGTCGAGTTCGACGAAGTCATCCTGTTCAACGCCACCATCATGGGGCCGGTGTACCCCTTCGAGGAGATGTTCACCGAGATGGCCGGCCGGGACATCGACTTCTGGGGCATCACCTGGTTCCATAAGGTGCCCTATGACCCCTTCGGGCATGCGGCCGAGGGGTATCTTCCGCGCCACCTCCAGTCCCACTTCCATGCCTACCGGCGCTCCCTGGTCTCCTCCAAGGCATTCCAGGACTACTGGGACAACCTTCCTCAGATGAGCTCCTACGAGGACTCGGTGGGGCTTCACGAGGCTCCTTTCACCCAGCGCTTCGAGCGGCTCGGCTTCACCTCCGACGTCTACGTCAACACCGAGGACCTGGAGGGGTACACCTTCTCCCCGGTGCTCTTCGCCCCCAAGCGACTCATTGAGGAGAAGCGCTGCCCGATCTTCAAGCGCCGTTCCTTCTTCCACGACTACCAGGACCTGGTTCGCCAGTCCGTCGGCAACACCTCCCTCGAGCTCTACGAGTACCTGCGAGACCACACCGACTTCGACACGAACCTCATCTGGGACAACGCCCTGCGCTCGATGAACATGGCGGACCTGGTCAAGAATCTCCATCTCACCTACGTTCTGCCCACGCAGGCGGTGGTCCACGAACCCAAGCCGCAGAAAATCGCCCTCATCGCGCACCTGTACTACATGGACCTCCTCGAGCCCACGTTGGCCTACGTCAAGTCCATGCCGGAGGGGACGGACCTCATCCTCACCGTCGGCTCCCAGGAGAAGGCGGAGCTGGTGGAGGAGGCCTGCAAGGATCTTCCGTACAACGTGACCGTGCGCCTCATCGAGAACCGGGGGCGGGACGTCAGCGCGCTCCTGGTGGGCTGCAAGGACATCATTCACGACTACGACCTGGTCTGCTTCACCCACGACAAGAAGGTCACCCAGGTCAAGCCCTACTCGGTGGGGGACGGGTTCGCGATCAAGTGCTTTGAGAACCTGCTGGCCACGCGCGACTTCGTCAAGAATGTCATCGCTACCTTCGACGCCGAGCCGCGTCTGGGGCTCCTCGCTCCCACCCCGCCCAACCACGGAGACTACTTCCCGGTCTTCTCCATGGGGTGGGGGCCGAACTTCGAGCGCACCAAGACCCTCCTGGAGAAGGAGCTGAACCTGAGTGTCCCGATCGATGAGAGCAGAGCTCCCATCGCCCCGCTGGGCACCATGTTCTGGTTCCGTCCTGCCGCTCTGAAACCGCTGTTCGACCACGACTGGCAGTGGGAGGACTTCCCGCCTGAGCCGAATAATATTGACGGAACCATTCTCCACGCCATCGAGCGCGCCTACGGTTACGTCGCTCAGGCATCCGGCTACTTCTGCGGCTGGCTCTTCTCGGACTCCTTCGCCCGTATCGAGATCACCAGCCTGTCGCACTATGTTCAGGACTTCACTCATGCCGTCGCTGAGAACGGCATTCTCGGCTACGAGGATGACATGGTGAACAACCTCCGCAAGCGGGGCGCTGAACGCAAACGGATCAAGAAGCAGGTCGCGCGCTGGGTCCCGGCCCCCCTGCACAGGCCGCTTGTGAGGGCGTACCGGCGGGCCCGGAGGATCGGGAGGTGA","MATLGEDPKRLGIFFFFDAQGVADSYVEALLADMVKNLSELVIVVNGELTATSYAKLSAFTDNIILRENKGLDAWAYKTALESYGWDRLVEFDEVILFNATIMGPVYPFEEMFTEMAGRDIDFWGITWFHKVPYDPFGHAAEGYLPRHLQSHFHAYRRSLVSSKAFQDYWDNLPQMSSYEDSVGLHEAPFTQRFERLGFTSDVYVNTEDLEGYTFSPVLFAPKRLIEEKRCPIFKRRSFFHDYQDLVRQSVGNTSLELYEYLRDHTDFDTNLIWDNALRSMNMADLVKNLHLTYVLPTQAVVHEPKPQKIALIAHLYYMDLLEPTLAYVKSMPEGTDLILTVGSQEKAELVEEACKDLPYNVTVRLIENRGRDVSALLVGCKDIIHDYDLVCFTHDKKVTQVKPYSVGDGFAIKCFENLLATRDFVKNVIATFDAEPRLGLLAPTPPNHGDYFPVFSMGWGPNFERTKTLLEKELNLSVPIDESRAPIAPLGTMFWFRPAALKPLFDHDWQWEDFPPEPNNIDGTILHAIERAYGYVAQASGYFCGWLFSDSFARIEITSLSHYVQDFTHAVAENGILGYEDDMVNNLRKRGAERKRIKKQVARWVPAPLHRPLVRAYRRARRIGR$","Rhamnosyltransferase","Cytoplasm","conserved hypothetical protein","polysaccharide biosynthesis protein","Rhamnan synthesis F","","Shibata Y., Yamashita Y., Ozaki K., Nakano Y., Koga T. Expression and characterization of streptococcal rgp genes required for rhamnan synthesis in Escherichia coli. Infect. Immun. 2002. 70(6):2891-2898. PMID: 12010977","","","

InterPro
IPR007739
Family

Rhamnan synthesis F
PF05045	$\"[41-543]T$	RgpF

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-59% similar to PDB:1DOF THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY (E_value = );-58% similar to PDB:2I54 Phosphomannomutase from Leishmania mexicana (E_value = );-58% similar to PDB:2I55 Complex of glucose-1,6-bisphosphate with phosphomannomutase from Leishmania mexicana (E_value = );","Residues 83 to 585 (E_value = 2.8e-147) place ANA_1551 in the RgpF family which is described as Rhamnan synthesis protein F.","","hypothetical protein","","1","","","Mon Aug 6 17:53:09 2007","","Mon Aug 6 17:53:09 2007","","","Mon Aug 6 17:53:09 2007","Mon Aug 6 17:53:09 2007","Mon Aug 6 17:53:09 2007","","","Mon Aug 6 17:53:09 2007","","","Mon Aug 6 17:53:09 2007","","","","Mon Aug 6 17:53:09 2007","Mon Aug 6 17:53:09 2007","","","","","yes","","" "ANA_1552","1676494","1675652","843","5.51","-8.92","30681","ATGGCAAAGACAGTTCTCGTCACTGGAGCCGGCGGCTACATCGGTCGCCACGTCGTCACTGCTCTCCTGGAGCGCGGCCTGGATGTCAAGGCCCTCGACCTGCGACTCGACGGCGTCGACGAGCGGGCGGAGAAGGTCTCCCTGGACCTGTTCTCCGGGGACGCCGACATCTACGACCAGATGGGGCGCCCCGACGTCGTCCTGCACATGGCCTGGCGCGACGGCTTCAAGCACGCCTCGTCCGCCCACATGGACGACCTGGCCAAGCACGTTCACCTCATCGAGAACCTCTACGCGGGCGGCCTCAAGCACCTCGCGGTCATGGGGACGATGCATGAGGTCGGCTACTGGGAGGGGGCCATCGACGAGAACTCGCCGTGCAACCCCGCCTCGCTCTACGGCATCGCCAAGAACGCGCTGCGGGAGACCACCTTCCTGTCGGCCAAGACGCACGACACCGTCGCCCAGTGGATCCGCGCCTACTACATCGTGGGTGACGACAAGTTCGGCAACTCGATCTTCTCCAAGCTCCTGGCCGCCGCAGAGGAAGGGCGCACCACCTTCCCCTTCACCACGGGTAAGAACCGCTACGACTTCATCTCCGTGGACGAGCTGGCCAGGCAGATCGCAGCGATCGTGGACCAGACCGAGGTCAACGGCGTCATCAACGCCTGCACCGGTGAGCCCATGAGCCTGGCCGAGCGCGTCGAGGCCTACATCCGCGACAACGGCCTGAACATCACCCTGGAGTACGGGGCCTTCCCGGATCGGCCCTACGACTCGCCGGGTGTGTGGGGCGATCCCACCAAGATCCGCCGTATCCTCGCCTCAAGCGCGAGCTGA","MAKTVLVTGAGGYIGRHVVTALLERGLDVKALDLRLDGVDERAEKVSLDLFSGDADIYDQMGRPDVVLHMAWRDGFKHASSAHMDDLAKHVHLIENLYAGGLKHLAVMGTMHEVGYWEGAIDENSPCNPASLYGIAKNALRETTFLSAKTHDTVAQWIRAYYIVGDDKFGNSIFSKLLAAAEEGRTTFPFTTGKNRYDFISVDELARQIAAIVDQTEVNGVINACTGEPMSLAERVEAYIRDNGLNITLEYGAFPDRPYDSPGVWGDPTKIRRILASSAS$","NAD-dependent epimerase/dehydratase","Cytoplasm","Eps11I","NAD-dependent epimerase/dehydratase","NAD-dependent epimerase/dehydratase","","Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 1997. 36(21):6294-6304. PMID: 9174344","","","

InterPro
IPR001509
Family

NAD-dependent epimerase/dehydratase
PF01370	$\"[5-225]T$	Epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[2-245]T$	no description
PTHR10366	$\"[7-273]T$	NAD DEPENDENT EPIMERASE/DEHYDRATASE

","BeTs to 8 clades of COG1087COG name: UDP-glucose 4-epimeraseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1087 is --m---yq-d-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 2","***** IPB002225 (3-beta hydroxysteroid dehydrogenase/isomerase) with a combined E-value of 2e-09. IPB002225A 2-40***** IPB001509 (NAD-dependent epimerase/dehydratase) with a combined E-value of 1e-06. IPB001509A 6-17 IPB001509C 129-138***** IPB013549 (Domain of unknown function DUF1731) with a combined E-value of 5.8e-06. IPB013549A 5-29","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 225 (E_value = 2e-17) place ANA_1552 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 5 to 32 (E_value = 2.1e-07) place ANA_1552 in the NmrA family which is described as NmrA-like family.Residues 6 to 251 (E_value = 0.00016) place ANA_1552 in the 3Beta_HSD family which is described as 3-beta hydroxysteroid dehydrogenase/isomerase family.Residues 7 to 30 (E_value = 0.00029) place ANA_1552 in the NAD_binding_4 family which is described as Male sterility protein.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1553","1678557","1676530","2028","9.05","9.78","74126","ATGAACAGGCAGGCTCCCGTGTCCGGTAAGTCCGCGAAGAACAGTACGGATCAGGTCAAGAACAACGACGCCGAGAAAGCCGATCACGACTCCACGCCGCAGACCCTCTCCGCCGCCGGCCTCACCGCACGGATGCGCGCGCTCACCGACGCGATGAGCGATCAGGGACGCCGGCTGGTCGAGCGCGTGGTGGACAGCCGCCTGGGCTCCTGGTGGAGCAGTACCGAGCGCCCCGGCCTCGTGGACTGGGCATTGCTGGGCGTCATCCTGCTCGGCGCCTACGCCTTCTTCCTCTACGGGGACGTGCGAGCCACCTTCGAGCACTCCTTCAACTTCCTGGACTCGGTGTTCCAGGGGCGGGTGGGAGACTTCTACCAGATCGCGATCGAGCACACCTCGACCGGTCACCCCGCGGTCTACGACATTCCGCTCTACCTGCTCTTCGGACTGTGGAACCTGCCGACGTACATCATCTACCGGATCACCGGCTTCCACTACCTGCTGTCAACGCCGGCGCAGCTGTGGCTCAAGACCATGATGGTGCTCGCCGCACTCCTGGCTGCCAAGGTGCTGGTGGACATCGCACGCGATCTGGGAGTCGGCCGGCAGCGCAGCAAGTGGGTCGCCTTCTTCTTCCTGTCCTCGATGACGCTGTTCGTCCCAGTCTTCGTCATCGTCCAGTACGACATCATCATGATCGTCTTCATCCTGCTGGGGCTGCGCGCCTACCTGCGCGGCCGGCTGGGCAGGTTCCTGCTGTGGTTCGCGATCGCCAACACCTTCAAGCTCTTCGCCATCTTCATCTTCGTGCCGCTCCTGCTGCTGCGGGAGAAGCGACTGCGTGTGGTGGCCCTTCAGTTCGGCGTCGGACTCATTGGCCTGGTGGCTTGCCGGGCCATTTACCACGGCAACGTGGCCTACAAGGCGTCCACCGGCGGGTTCATGAGCAGTATGCTTCAGAGGCTCACGGCCGTGGGGGTGCCGTGGCAGAGCAGCATGATTCCGATCTTCGTGGTGTTCATGGTCGGGATCGTCATCTTCGCCTACCTGCGCCGCCCTCAGGGGACGAAGGCCTTGGCGGCCGACGCGGTCTACATCTGCATGGCCATCTACCTCGTCTTCGCCACGATCGTCCCGCTCAACCCCTACTGGGCCGTCATGGTCTCACCTTTCGCGGTGCTCATCATCTTCCTCAACCCGCGCCACGTGCTGCTCAACTCGGCTCTTGAGACGGGCGTGGGAACCGCCTTGTTCCTCCTGTACGCCTTCACCGGCTACTCCATGTACAACCGGTCGATCCTCGATCAGCTGCTCCTGCCGCACCTGGTCGCCCCGACGGCGCAGCCCCGGTACGAGACCCCAGCACATTTCCTCGAGGCCATGGGGGTCACTCGGCAGGGGGCCTTCATCGTCGGCTTCATGATTGCTTGTGCCCTGGCGATCCTGGTCGTCAACTTCCCGCGTGCCGCGATGGTGGAGAGCCTGGGCCAGGGGGAGCGCATCCCGCGCTCGGTGGCCTGGGTGCGTCTTCTCATGCCGGCAGGCTTCAGTGCGCTCGTGCTGATCCCCTACTTCGTACCCGCCGTTCCAGTGGTGTACTCGGCCTCCACTGACGCCCCCCGGGCGGGGAGTGCCAACATTCTCGAGGACGGGGCCAGCATCGCTGAGACGATCACCCTGCCGTCCACCGTGGAGGCCAGCTCCCTCAACATCGCCTTCCTGGCCGAAGAGGTGCAGTGGCTGGACTCCTCAGTGGTCAGCGTCGAGGTCACAGATGCCTCGGGTGCCCGGGTCTTCAGAACCGAGGCCCCGGCGAACTCCCTCCACGACGGCCTGCACAGCTTCCCCGCCGACGGGCTCGTCCTGCGCGGTGGAGAGAAGTACACCGTAACGATCACCAGCAGGATGACCGAGGGCGGATATGCCCGCGTCATGATCAACCCCGCAGTGGACCAGTTCCCGACCACGGAGAACGGGACCACCGTCCACGGTGACCTCCTCATGACCATTGCCGGCAGAACCAAGTGA","MNRQAPVSGKSAKNSTDQVKNNDAEKADHDSTPQTLSAAGLTARMRALTDAMSDQGRRLVERVVDSRLGSWWSSTERPGLVDWALLGVILLGAYAFFLYGDVRATFEHSFNFLDSVFQGRVGDFYQIAIEHTSTGHPAVYDIPLYLLFGLWNLPTYIIYRITGFHYLLSTPAQLWLKTMMVLAALLAAKVLVDIARDLGVGRQRSKWVAFFFLSSMTLFVPVFVIVQYDIIMIVFILLGLRAYLRGRLGRFLLWFAIANTFKLFAIFIFVPLLLLREKRLRVVALQFGVGLIGLVACRAIYHGNVAYKASTGGFMSSMLQRLTAVGVPWQSSMIPIFVVFMVGIVIFAYLRRPQGTKALAADAVYICMAIYLVFATIVPLNPYWAVMVSPFAVLIIFLNPRHVLLNSALETGVGTALFLLYAFTGYSMYNRSILDQLLLPHLVAPTAQPRYETPAHFLEAMGVTRQGAFIVGFMIACALAILVVNFPRAAMVESLGQGERIPRSVAWVRLLMPAGFSALVLIPYFVPAVPVVYSASTDAPRAGSANILEDGASIAETITLPSTVEASSLNIAFLAEEVQWLDSSVVSVEVTDASGARVFRTEAPANSLHDGLHSFPADGLVLRGGEKYTVTITSRMTEGGYARVMINPAVDQFPTTENGTTVHGDLLMTIAGRTK$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[80-100]?$ $\"[172-192]?$ $\"[207-241]?$ $\"[251-273]?$ $\"[282-302]?$ $\"[328-348]?$ $\"[358-376]?$ $\"[380-398]?$ $\"[403-423]?$ $\"[466-486]?$ $\"[507-527]?$	transmembrane_regions

InterPro
IPR007267
Family

GtrA-like protein
PF04138	$\"[17-132]T$	GtrA

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[15-37]?$ $\"[43-61]?$ $\"[82-102]?$ $\"[108-126]?$	transmembrane_regions

","BeTs to 8 clades of COG2246COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2246 is ao-pkz----r-bce------j----Number of proteins in this genome belonging to this COG is 3","***** IPB007267 (GtrA-like protein) with a combined E-value of 1.2e-12. IPB007267A 18-44 IPB007267B 44-75 IPB007267C 55-68","","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 132 (E_value = 7.3e-26) place ANA_1554 in the GtrA family which is described as GtrA-like protein.","","conserved hypothetical membrane protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1555","1680078","1678993","1086","7.93","1.63","40049","ATGAAGAAGATCAGCGTCGTCATCCCCAGTTACAATGAGGAAAAAAGCGTCAGGTTGATGTATGACCGACTGAACTCGGTATTTCGCACCCATCTTCCTCAGTACGACTACGAGATCATCTTCGTCGATGACTACTCGACGGACGGCACCCGCGGCGCGATCCGCGCCCTGGCGGGTGAGGACAAGCGGGTGAAGGCCGTCTTCAACGCCCGTAACTTCGGTTTTCACCGGAATGTCTTCTCGGCGCTCACCTACGGCTCGGGGGATGCGACCTTCATGCTCTTCGGCGACCTTCAGGATCCCCCTGAGAACCTCCCGGAGTTCGTGGCCCGTTGGGAGGCGGGGGCCAAGGTCGTCATCGGGCAGAGGAGATCCTCTGACGAGGGCTTCATCATGACGGGATGCCGTCACCTCTACTACAAGCTCATCGACTGGTTCGCAGACACCCCTCAGATCGCGCGCTTCACCGGGTACGGGCTCTATGACGTCGAGTTCATCGATGTTCTGCGGCAGATCGGCGATATTCAGCCCTATTTCAAGACGGTTGTCGCCGAGTACGGAATCGGGCTCGAGATCGTCCAGTACGATCAGGCCCAGTCCTCCCGGGGGAAGTCGAACTTCAACTTCCTGCGCAACTATGACTTCGCCATGCAGGGGATCACCAGCTCCACCAAGCTGCTGATGCGCATGGCCACCTTCGTGGCCACCTTCGTCGGCATCATCTGCCTGGGTCTGGCCACCTTCGTCCTGGTCAAGAAGCTCATCGACTGGAACGCCTATCCGGTGGGTGAGGCCTCGCGTACCGTGGGCCTGTTCTTCCTCGGCTCCATTCAGCTGTTCTTCATCGGAATCCTGGGTGAGTACATTCTCAGCATCAACGGGCGCGTTGTCAGCAAGCCCCGCGTGGTCATCGGTGAGCGCCTCAACTTCGGGCCCTCCGAGGGGCCGTCGAGCTTCGGGCTCAGTCGTGGCGTGACACGCTCGAGCGGAAGCGCTGCGGAGGATGTGAGCCGCAGCGAGCCGGCCGGCCCGTCGTCGCAGACGGGGCCCTCCGTGCAGGAACGTCCCGGCGGGAACGCCTCTTGA","MKKISVVIPSYNEEKSVRLMYDRLNSVFRTHLPQYDYEIIFVDDYSTDGTRGAIRALAGEDKRVKAVFNARNFGFHRNVFSALTYGSGDATFMLFGDLQDPPENLPEFVARWEAGAKVVIGQRRSSDEGFIMTGCRHLYYKLIDWFADTPQIARFTGYGLYDVEFIDVLRQIGDIQPYFKTVVAEYGIGLEIVQYDQAQSSRGKSNFNFLRNYDFAMQGITSSTKLLMRMATFVATFVGIICLGLATFVLVKKLIDWNAYPVGEASRTVGLFFLGSIQLFFIGILGEYILSINGRVVSKPRVVIGERLNFGPSEGPSSFGLSRGVTRSSGSAAEDVSRSEPAGPSSQTGPSVQERPGGNAS$","Glycosyl transferase, family 2","Membrane, Cytoplasm","Glycosyl transferase, family 2","glycosyl transferase; family 2","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[5-187]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[3-146]T$	no description
PTHR10859	$\"[10-310]T$	GLYCOSYLTRANSFERASE RELATED
tmhmm	$\"[231-251]?$ $\"[270-292]?$	transmembrane_regions

","BeTs to 24 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 187 (E_value = 7e-24) place ANA_1555 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","transferase, family 2","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1556","1682250","1680208","2043","6.41","-11.20","74213","ATGAACCGAGGACTCGTCTACTTCCACTTCGATCCTCATCATCAGGTCCGCGACTACGTCCTGGCTGCGCTCAGCTCCCTGCGGCCCCACGCTGACCACGTCCTGCTGGTCTCCAACTCACCCATCGGCGAGGCCGATCGCGTCCGGCTGGAGACCTGCTGCGATGAGATCCTCCAGCGCCCCAATGAGGGACTTGACGCCGGCGCCTACCGGGCCGGCCTGGAGCACCTGGGCTGGGACCGGCTCGCCGACTTCGACGAGCTCATCCTGACCAACCACACCTACTACGCGCCGCTGCGGCCCTGGGAGGAGGTCCTCACCCGCGCCGAGGACTGGGGCGACATCTCCTTCTGGGGCATGACCGAGCACGCCGCCATGCGTCCCCACCCCTTCCTGGCCAAGCGCGAGCTGCCCCGCCACCTCCAGTCCCACTGGATCGTGGTGCGCCGCAGGCTCCTGAGGGACCCGGCCTTCCGTGAGTACTGGGAGCAGATGCCGCAGGTCTCCTCCTACCGCGACTCCATCCAGTGGCACGAGTCGCGCTTCACCGGCCACTTCGCCGAGCTCGGCCACACCTGGGAGGTCGCCTTCCCCGTGGACCGCTACCGCTCGGAGAACCCGGCCATCGAGGAGGCCCCGGCGCTGCTGGCCGACGGCTGCCCCCTGCTCAAGCGCCGCGCCCTCTTCCACGATCCGCTTCACCAGGACCGTCAGGCCGTCGTCGGTGGGGAGCTGCTGGAGGCCGCCGTGGCCGCCGGCTACAGCGAGGACCTCATCCTGTCCGACGTCGTCCACACCGCGGCCGCCCGCGACCTCATCGTCAACGCCGGCCTCACCGAGGTCGTGACCGGGTGTGTCCCCGGGGCCGCGGGGGCCGCTGCCGAGACGAGCCCGCCCGAGCGGCGGCACTCGGGCTGCGTCGTCGTCCACGTCCCGGCCGGGAGGGAGGCCGTGGAGCGAGCCGAGGCCAATGGCCTGGCCCGACGCCTGGCGAGCGCGCCGGCGCACTGGCGGGTCGTGGTCACCTCGCCCACGCACCTGGATGCCGCCGACCTGGAGCGGGTCACCGGCCGCCGTCCGTCACCGGAGGACTCGGCGCACGGGGAGGGGGACGTGTCTTTCCGCCCGGTGCGTGACCTCGATCCGCGCGGCACGATCGCCTTCCTCACCCAGTGCGACGACCTCTGGGATCCCGGGTGCGCTGCCGACGGTGACGACGGCGATGAGGATGACGGCGGTGACCCCCTGGTCCTGCGGGTCACCGTGGGGCCCACCTCCGGCCCCGGTACGCGGGCCGACGACGTCGCCCACCGGCAGGCGCTCGACTGCCTGCTGGACTCGCCGGGGTATGTGGCCGGCCTCATCGACCTCTTCGCGCGGCACCCCGGCCTCGGCGTGGCCATGCCCGCCGCCGGCCACATCGGTCAGGCTCATGGAGGGGCGACATGGGACGGGTTGGCAGGTGCCGCCACGGCGCTGTCCCGGCGGCTCGGCCTGACCGTGGAGCTCGATCCGCTCGCTCCCGTGGTCCCGGTCGGCGCGATGTTCCTGGCCCGCCCCGCAGCACTGCGCACCCTGAGTGAGGGTGCCAAGGAGCTCGTGCGGCTGACCGAGCAGGCGGCCCCCAGCGCTGAGCAGTCGGTGGAGCGCCTCAAGCGCGCCCGCGCCGCTGAGGTGCTTGAGCTGCTGACCGTCTACGCGGCCATGTCCAGCGGCTACCACCCCCGCGAGGTCCTCACCCCCACCTGGGCCGGGCGCCTTTACGGTGCTCTGGCCCACAAGCATCGCGTCGTCACTGCGGACCTTCCGGCCCACACCGACGAGCAGGTCAGGTTCCTCCAGGCCCGGTTCGGGCCCCGGGCCGGAGTCGGTGCCCGGGTGCGCACCTACGTCGATGTCCATCACCCCGACATGGGCAGTGCGCTCAAACCCGCTTACCGCTATCTGACCGGTGGGGCCTCAGACCTGGCGCGCACCGTGACGAGTGCCGGCAGGCGTCTGCGTGACGTCGGCCGTCATCGGGGGAAGGACAAGGGGGAATGA","MNRGLVYFHFDPHHQVRDYVLAALSSLRPHADHVLLVSNSPIGEADRVRLETCCDEILQRPNEGLDAGAYRAGLEHLGWDRLADFDELILTNHTYYAPLRPWEEVLTRAEDWGDISFWGMTEHAAMRPHPFLAKRELPRHLQSHWIVVRRRLLRDPAFREYWEQMPQVSSYRDSIQWHESRFTGHFAELGHTWEVAFPVDRYRSENPAIEEAPALLADGCPLLKRRALFHDPLHQDRQAVVGGELLEAAVAAGYSEDLILSDVVHTAAARDLIVNAGLTEVVTGCVPGAAGAAAETSPPERRHSGCVVVHVPAGREAVERAEANGLARRLASAPAHWRVVVTSPTHLDAADLERVTGRRPSPEDSAHGEGDVSFRPVRDLDPRGTIAFLTQCDDLWDPGCAADGDDGDEDDGGDPLVLRVTVGPTSGPGTRADDVAHRQALDCLLDSPGYVAGLIDLFARHPGLGVAMPAAGHIGQAHGGATWDGLAGAATALSRRLGLTVELDPLAPVVPVGAMFLARPAALRTLSEGAKELVRLTEQAAPSAEQSVERLKRARAAEVLELLTVYAAMSSGYHPREVLTPTWAGRLYGALAHKHRVVTADLPAHTDEQVRFLQARFGPRAGVGARVRTYVDVHHPDMGSALKPAYRYLTGGASDLARTVTSAGRRLRDVGRHRGKDKGE$","Rhamnosyltransferase","Cytoplasm","conserved hypothetical protein","K07272 polysaccharide biosynthesis protein","Rhamnan synthesis F","","Tougu K., Peng H., Marians K.J. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 1994. 269(6):4675-4682. PMID: 8308039","","","

InterPro
IPR007739
Family

Rhamnan synthesis F
PF05045	$\"[34-573]T$	RgpF

InterPro
IPR013173
Domain

DNA primase DnaG, DnaB-binding
SM00766	$\"[436-563]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 597 (E_value = 1.3e-43) place ANA_1556 in the RgpF family which is described as Rhamnan synthesis protein F.","","hypothetical protein","","1","","","Mon Aug 6 18:00:31 2007","","Mon Aug 6 18:00:31 2007","","","Mon Aug 6 18:00:31 2007","Mon Aug 6 18:00:31 2007","Mon Aug 6 18:00:31 2007","","","Mon Aug 6 18:00:31 2007","","","Mon Aug 6 18:00:31 2007","","","","Mon Aug 6 18:00:31 2007","Mon Aug 6 18:00:31 2007","","","","","yes","","" "ANA_1557","1684887","1682374","2514","6.81","-1.71","85286","ATGGTGAGGCCTGATGGACGCCCGTCGGTATCACCTCAAAGGAACCCCATGAACGTCCCTCGCGCTCTTGGCCGCATCGCCCCTCTCGGTGGCCATCGCCTCAGCGGCCATGCCGGTGGTCTCAGCACCCGTGCACGGGTGTGTCGGTCCGCCGGGCTCATCGCCCTGTCCGCACTGCTCCTGTCCAGCCTGGTGCCCGTGGCCGGTGCCGCTCCAGGCGCCGGCGACTCCGGTGGTCAGGGCGAGGCCCCCGCTCCGGTGCAGATCCTCGACCTGACCACCGCTAGTGGGCAGGCCACCGAGGTGGCGCAGTCGGGGCTCGACGACGTCCAGGCCTCGCCGGGGCAGGGCTCCGGCTCGGGGTCGCGCGATGGGGCGGGCGCCCAGACGCCAAGGCCGTCGACCGAGGAGGCCAGTGGCTCCGATAACGCCGCCTCGGTGAGTGCGACGCCGGTGCGCAGCGCAAGTGCTGCCGTGCCCGCTCTCGCTCAGGCCACGGGCGCAGCCGACGCGCCGGCCCCGTCGATCCTGCCGGTGGCTACGGACCCGCAGGCGGACGCCACCCTGCTGACCGACCCACTCGAGGTCGACCGCTTCTTCGTCGCCGGCTTCACCTGGGCCGGCAGCGCCGAGCTGCCCGAAGGCGTGCGTATCTACCTGCGTGTGCGGGAGAACGGGACCTGGTCACCCTGGTACCTCAATGAGGCGGCCGACGCCGGCCGCGACGACCGCGCCACCTCCGGCACGGGGGAGTTCGTCACCGGCGGGGCCGACGCGATCCAGGCCTCCGTCGTCGGCAGCTCGCTTCCCGCCGGACTCAAGCTGGCCCTGGTTCCCTCCCGCCCACAGGGCGAGGAGGTCCTCGATGCCGAGGATCTCACGGCCACCCAGGCCGCACCGACCCCCGTCATTGAGGATGCCTCCGCCACTGAGGACCATGGCGCCCAGGTGGAGCCGGCTGCCATGGCGCCATCTGCGAGCCCGGCGTGGGCCACTCAACCGGCCGCTGTATCAGCCGCACCAGCAGCCGCGCCCGCCCTCGCACCGGCTGCGACAACCGCCAACGGCCTGCCTGTCGCGGTGACCACCCGAGCCGAGTGGGGGGCCAATGCCTCCTACATGAGCTGGGATCCCGAGTACGCCAGCGCCGGCCACGTCGTCGTCCACCACACCGCAGGCACCAACAGCTACTCCGCAGGCCAGTCCGCCTCCATCGTGCGGGGCATCTACTACTACCACGCGGTCACCCTGGACTGGGGCGACATCGGCTACAACTTCCTCGTCGACAAGTTCGGCACCGTCTTCGAGGGGCGCTCCGGTTCCGTGGCAGCACCGGCCGGCAAGATGAGCATCGGGGCGCACGCCCGAGGCGTCAACACCGGCACCATGGGCATCTCCATGATGGGGGACTACAGTGCGGTGTCCCCCTCGGACGCCCAGCTGAGCTCCGTGGGCAAGATGGCCGGATGGTTTCTCAAGCGCGCCGGTATCTCCGATGTCACCGGCTGGGCGGGCCTGCACGTGTGGACCACCGAGCGCTACCAGGCCGGCTCCACCATCTCCATGCCCCGCATCCTCGGGCACCGCGACGTCGGCTACACCACCTGCCCCGGCAACGTCGGCTACTCCAAGCTCGGCGCCATCCGCGCCATCGCGAAGGCACAGGGCTCCGCCCCGCAGGGTGGAAGCAGCAACGCGCCGTCGACCGTGGCCCAGGACCATCCGGGAGCCGTCGCCCTGCGCAGCGCCCTGGGCGTCAACGGCTGGATCGGAGTGGCCACCACTGGTGTCTACGCCTCCTCCAAGGGTGGGGTCTTCCAGCGCTTCGAGCACGGGGTGGGCTACTGGAGCCCGGCGACCGGTGCGCAGTTCGTGGGCGAGCCGGTGCTCAGCGCCTGGGGCGCGTACGGGTACCAGACCGGGTCCATGGGTTACCCGCGCAGTGGTGGCGTGGTGGGAATCGGCGGCAGCCGTCACCAGATCTTCGAAGGCGGCATCGCCTACTGGCGCCCCGGGGGCCGGGTCAGCTTCATTCACGGCTCGATCCTGAATGGCTGGGCCGCCTCGGGCTGGGAACGCTCCTGGCTGGGACTTCCCACCTCTAACGAGACTGCCTCCACCAAGGGTGGGGTGTTCCAGCGCTTCGAGCACGGGGTGGGCTACTGGAGCCCGGCGACCGGTGCGCAGTTCGTGGGCGAGCCGGTGCTCAGCGCCTGGGGCGCGTACGGGTACCAGACCGGGTCCATGGGTTACCCGCGCAGTGGTGGCGTGGTGGGGATCGACGGTAGCCGTCACCAGATCTTCGAGGGCGGCATCGCCTACTGGCGCCCCGGGGGCCGGGTCAGCTTCATCCACGGCTCGATCCTCAGCGCCTGGGCGGACTCGGGCTGGGAGCGCTCCAAGGTGGGGCTGCCTACCGGGCACGCAGTCCGCCAGGCCAACGGCACCATGATCCAGACCTTCGAGAAGGGCAGCATCTCCGTGGCGCCCAACGGGAAGGTGACCATCCGCTGA","MVRPDGRPSVSPQRNPMNVPRALGRIAPLGGHRLSGHAGGLSTRARVCRSAGLIALSALLLSSLVPVAGAAPGAGDSGGQGEAPAPVQILDLTTASGQATEVAQSGLDDVQASPGQGSGSGSRDGAGAQTPRPSTEEASGSDNAASVSATPVRSASAAVPALAQATGAADAPAPSILPVATDPQADATLLTDPLEVDRFFVAGFTWAGSAELPEGVRIYLRVRENGTWSPWYLNEAADAGRDDRATSGTGEFVTGGADAIQASVVGSSLPAGLKLALVPSRPQGEEVLDAEDLTATQAAPTPVIEDASATEDHGAQVEPAAMAPSASPAWATQPAAVSAAPAAAPALAPAATTANGLPVAVTTRAEWGANASYMSWDPEYASAGHVVVHHTAGTNSYSAGQSASIVRGIYYYHAVTLDWGDIGYNFLVDKFGTVFEGRSGSVAAPAGKMSIGAHARGVNTGTMGISMMGDYSAVSPSDAQLSSVGKMAGWFLKRAGISDVTGWAGLHVWTTERYQAGSTISMPRILGHRDVGYTTCPGNVGYSKLGAIRAIAKAQGSAPQGGSSNAPSTVAQDHPGAVALRSALGVNGWIGVATTGVYASSKGGVFQRFEHGVGYWSPATGAQFVGEPVLSAWGAYGYQTGSMGYPRSGGVVGIGGSRHQIFEGGIAYWRPGGRVSFIHGSILNGWAASGWERSWLGLPTSNETASTKGGVFQRFEHGVGYWSPATGAQFVGEPVLSAWGAYGYQTGSMGYPRSGGVVGIDGSRHQIFEGGIAYWRPGGRVSFIHGSILSAWADSGWERSKVGLPTGHAVRQANGTMIQTFEKGSISVAPNGKVTIR$","N-acetylmuramoyl-L-alanine amidase","Extracellular","probable csp protein","hypothetical protein","LGFP repeat protein","","Kang D., Liu G., Lundstrom A., Gelius E., Steiner H. A peptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(17):10078-10082. PMID: 9707603Kiselev S.L., Kustikova O.S., Korobko E.V., Prokhortchouk E.B., Kabishev A.A., Lukanidin E.M., Georgiev G.P. Molecular cloning and characterization of the mouse tag7 gene encoding a novel cytokine. J. Biol. Chem. 1998. 273(29):18633-18639. PMID: 9660837","","","

InterPro
IPR002502
Domain

N-acetylmuramoyl-L-alanine amidase, family 2
PF01510	$\"[372-548]T$	Amidase_2

InterPro
IPR013207
Repeat

LGFP
PF08310	$\"[590-642]T$ $\"[696-748]T$	LGFP

InterPro
IPR015510
Domain

peptidoglycan recognition proteins
PTHR11022	$\"[386-556]T$	PEPTIDOGLYCAN RECOGNITION PROTEIN

noIPR
unintegrated

unintegrated
G3DSA:3.40.80.10	$\"[347-561]T$	no description
PTHR11022:SF5	$\"[386-556]T$	UNCHARACTERIZED

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:2F2L Crystal structure of tracheal cytotoxin (TCT) bound to the ectodomain complex of peptidoglycan recognition proteins LCa (PGRP-LCa) and LCx (PGRP-LCx) (E_value = 4.8E_13);-44% similar to PDB:1YCK Crystal structure of human peptidoglycan recognition protein (PGRP-S) (E_value = 7.0E_12);-41% similar to PDB:1OHT PEPTIDOGLYCAN RECOGNITION PROTEIN-LB (E_value = 2.2E_10);-46% similar to PDB:1S2J Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA (E_value = 8.5E_10);-46% similar to PDB:1SXR Drosophila Peptidoglycan Recognition Protein (PGRP)-SA (E_value = 8.5E_10);","Residues 372 to 548 (E_value = 3e-06) place ANA_1557 in the Amidase_2 family which is described as N-acetylmuramoyl-L-alanine amidase.Residues 590 to 642 (E_value = 4.8e-08) place ANA_1557 in the LGFP family which is described as LGFP repeat.Residues 696 to 748 (E_value = 2.7e-16) place ANA_1557 in the LGFP family which is described as LGFP repeat.","","csp protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1558","1685040","1686236","1197","6.28","-6.54","43968","TTGAGGCTCCGCGGTTTAACCGCTTCACGACGCAAATATTGCAATCCAGTCTCACCGCCCCGGAGCCCTCAGTCCGGCTGCGCCTGCCCAGCGGCCACGCCCCACGGCCTCCCGTGGGCTCGAGCGAGCTCCTGTGGCATGATGGCGTCGGCCATGATGGGCGCTCAGCGCCCCCAGTTCCCACGTATCGGAGCGAGTTCTATGCACGTCCTCATCACCGGAGGCGCCGGCTTCATCGGCGCCAACTTCGTCCACCAGACCCTGGTACGCCACCCCGATGCCACCGTCACCGTCCTGGACAAGCTCACCTACGCCGGGAACAAGGGCTCGCTGGCAGACCTGGATGACCGTGTCACGCTCGTCGTCGGAGACATCGCCGACGCCGACGTCGTCGACCCGCTCGTGGCCCAGGCCGACGTCGTCGTCCACTTCGCGGCCGAGTCTCACAACGACAACTCGCTGCGCGACCCCTCCCCCTTCATCCAGACCAACCTCGTGGGCACCTTCACCCTCCTGGAGGCGGTGCGCCGCCACAAGGTGCGCTTCCACCACATCTCCACCGACGAGGTCTACGGGGACCTGGAGCTGGACGACCCGGCGAAGTTCGAGCCGACGACGCCCTACAACCCCTCCTCCCCCTACTCCTCATCCAAGGCCGGAAGCGACCTGCTCGTGCGCGCCTGGGTGCGCTCCTTCGGCGTGGAGGCCACCATCTCCAACTGCTCGAACAACTACGGGCCCTACCAGCACATCGAGAAGTTCATCCCGCGTCAGATCACCAACCTCATCGACGGCGTGCGCCCCAAGCTCTACGGCGCCGGCGAGAACGTGCGCGACTGGATCCATGTCCTGGACCACAACGACGCCGTGTGGGACATCATCGAGAAGGGCCGCATTGGCGAGACCTACCTCATCGGCGCCGACGGCGAGAAGAACAACAAGGAGGTCGTCGAGCTGATCCTGGAGCTCATGGGCCACGCTCCCGACGACTACGAGCACGTCGCCGACCGCCCCGGTCACGACATGCGCTACGCCATCGACAACTCCAAGCTGGTCCAGGAGCTCGGCTGGGCGCCGAGGTTCACCGACTTCCGCTCCGGCCTGCAGGCCACCATCGACTGGTACCGGGACAACGAGGCCTGGTGGCGCCCGCTCAAGGCCGAGGTCGAGGCCAAGTACGCCGCCCAGGGGCAGTGA","LRLRGLTASRRKYCNPVSPPRSPQSGCACPAATPHGLPWARASSCGMMASAMMGAQRPQFPRIGASSMHVLITGGAGFIGANFVHQTLVRHPDATVTVLDKLTYAGNKGSLADLDDRVTLVVGDIADADVVDPLVAQADVVVHFAAESHNDNSLRDPSPFIQTNLVGTFTLLEAVRRHKVRFHHISTDEVYGDLELDDPAKFEPTTPYNPSSPYSSSKAGSDLLVRAWVRSFGVEATISNCSNNYGPYQHIEKFIPRQITNLIDGVRPKLYGAGENVRDWIHVLDHNDAVWDIIEKGRIGETYLIGADGEKNNKEVVELILELMGHAPDDYEHVADRPGHDMRYAIDNSKLVQELGWAPRFTDFRSGLQATIDWYRDNEAWWRPLKAEVEAKYAAQGQ$","DTDP-glucose 4,6-dehydratase","Cytoplasm","dTDP-D-glucose 4,6-dehydratase","dTDP-glucose 4;6-dehydratase ","dTDP-glucose 4,6-dehydratase","","Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 1997. 36(21):6294-6304. PMID: 9174344","","","

InterPro
IPR001509
Family

NAD-dependent epimerase/dehydratase
PF01370	$\"[70-306]T$	Epimerase

InterPro
IPR005888
Family

dTDP-glucose 4,6-dehydratase
TIGR01181	$\"[69-385]T$	dTDP_gluc_dehyt: dTDP-glucose 4,6-dehydrata

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[70-334]T$	no description
PTHR10366	$\"[72-383]T$	NAD DEPENDENT EPIMERASE/DEHYDRATASE
PTHR10366:SF41	$\"[72-383]T$	DTDP-GLUCOSE 4,6-DEHYDRATASE

","BeTs to 13 clades of COG1088COG name: dTDP-D-glucose 4,6-dehydrataseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1088 is a-mpkz---drlbcef-hsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB001509 (NAD-dependent epimerase/dehydratase) with a combined E-value of 2.9e-39. IPB001509A 71-82 IPB001509B 139-176 IPB001509C 210-219 IPB001509D 244-265 IPB001509E 337-377 IPB001509D 304-325***** IPB002225 (3-beta hydroxysteroid dehydrogenase/isomerase) with a combined E-value of 4.8e-13. IPB002225A 67-105 IPB002225B 117-167","","","-73% similar to PDB:1KEP The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with dTDP-xylose bound (E_value = 4.6E_122);-73% similar to PDB:1KER The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with dTDP-D-glucose bound (E_value = 4.6E_122);-73% similar to PDB:1KET The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with thymidine diphosphate bound (E_value = 4.6E_122);-73% similar to PDB:1OC2 THE STRUCTURE OF NADH IN THE DTDP-D-GLUCOSE DEHYDRATASE (RMLB) ENZYME (E_value = 4.6E_122);-61% similar to PDB:2HUN Crystal structure of hypothetical protein PH0414 from Pyrococcus horikoshii OT3 (E_value = 7.7E_77);","Residues 68 to 233 (E_value = 0.0012) place ANA_1558 in the adh_short family which is described as short chain dehydrogenase.Residues 69 to 377 (E_value = 3.4e-06) place ANA_1558 in the RmlD_sub_bind family which is described as RmlD substrate binding domain.Residues 70 to 306 (E_value = 1.4e-73) place ANA_1558 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 70 to 356 (E_value = 0.00031) place ANA_1558 in the Polysacc_synt_2 family which is described as Polysaccharide biosynthesis protein.Residues 71 to 331 (E_value = 4.4e-07) place ANA_1558 in the 3Beta_HSD family which is described as 3-beta hydroxysteroid dehydrogenase/isomerase family.Residues 72 to 294 (E_value = 5.1e-09) place ANA_1558 in the NAD_binding_4 family which is described as Male sterility protein.","","4,6-dehydratase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1559","1686279","1686629","351","12.13","16.31","12763","GTGTGGGGTCCCCGCGGGGACCCCACACGCGTTCCCGTCCTGCGTCCAACCTCCCGCCCCGGTCGCCGGCGACGTCGGGCGGTGACGACATGCCTGTTCGCATCCGCGTTCGCGGCGGTGGACACCGTCTCGCACCTGGTCAGCCGAGTCCAGAGGACCACCGGAATGCTTCTGGAGGGGTCCTTCAACCCGGTGCGGCTGCTGATCACCCTGGCTGTCAGCGGTGCCGTGTGCTGGGGCTTCCTGACCCTGGTGGATCTGTCCGCGCGGCGCAGAAGCACCGGATCGCAGCAGCGCGGTGATCGCCACCGCGCGCGGCGAGCGTGTCTGTCATCACCTATTGCGCGCTGA","VWGPRGDPTRVPVLRPTSRPGRRRRRAVTTCLFASAFAAVDTVSHLVSRVQRTTGMLLEGSFNPVRLLITLAVSGAVCWGFLTLVDLSARRRSTGSQQRGDRHRARRACLSSPIAR$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[28-48]?$ $\"[67-85]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-58% similar to PDB:1F9T CRYSTAL STRUCTURES OF KINESIN MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE MOTOR ATPASE (E_value = );-58% similar to PDB:1F9U CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE (E_value = );-58% similar to PDB:1F9V CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE (E_value = );-58% similar to PDB:3KAR THE MOTOR DOMAIN OF KINESIN-LIKE PROTEIN KAR3, A SACCHAROMYCES CEREVISIAE KINESIN-RELATED PROTEIN (E_value = );-58% similar to PDB:1F9W CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1560","1686776","1687780","1005","9.55","9.48","35978","GTGGTCCTGGCGGGCTTCGCGCTCATGCGCAGTAACGCCCTGCCGGTGGTCCTGGTCATCCTGGCGCTGGTGGTGTGGTGGTCGAGGGCGCGCCTGCGCCGAGCGCTGGCGGTCGGCGCAGTGGTCCTGATCGTCGTGGTCGCCCCTTCAGCACTGACGGCTCGCTCCCAGCACGCCGAGGAGGCCGTGGGCATCCCGTTGCAGACGGTCGGCTACACCCTGACCCACGACGCCGACTGCCTGCCGCCGGCCAGTCGGCAGGTCTTCGACAACGTCCTGGCCCCTGAGACCTGGAGACAGGTCTACCGACCTTCCAGTGTCGACCCGGTCAAGGACTCGCCGGCCTTCAACGGGGCCTACCTCGATGCGCACCGCGGCCAGTTCCTCTCCGCGTGGGGGCGGGCCCTGGTGGCGTGCCCCCGACCATTCGTCACCGGCTTCCTCATCCATACCGCCAACCTGTGGCGCTTCGACGCCGACCCGGTGGGCACCGACGGTCAGTCCCGTTTCATCTCCGTGGTCTCGAATCACCCGGCCGACCGTGATGAGCTGATCCGCACCTACGCCCGTGCCGGCGTCGTCAACCACTCACTCCTGCCAGGGCCCCTGCGCCCGGTGGCGGGCGCCGCCGTGCGGGCCATGGAGGCAACGCCGGGCCCGGGAACCTGGATGTGGGTAGTGGCTCTGAGCGTGGTCGGCTTCGTCTATGCCGGGAGGCGTGAGTGGGTGGCGATCTACGCCCCTGTCATCCTGGTGTGGGCGACGCTCATGGTTGCGGCCCCCACCGTCACGCCGTTCCGTTACATGGCCCCCATCATCATGGTCGCGCCGCTCGGACTCGCGGTCCTGCTAGGCACCGACCAAGCCGCCTGGAACCCCTCTTCTCGAGGAACAACCACAAGCGACGATACTATATGTGGTACCATCCTGAAATGCCAAGCGTCGCGAAGATCCTCGCCAAGATGCAGGACAACCCACGCGGAATCGCTTACACAGAACTCATGA","VVLAGFALMRSNALPVVLVILALVVWWSRARLRRALAVGAVVLIVVVAPSALTARSQHAEEAVGIPLQTVGYTLTHDADCLPPASRQVFDNVLAPETWRQVYRPSSVDPVKDSPAFNGAYLDAHRGQFLSAWGRALVACPRPFVTGFLIHTANLWRFDADPVGTDGQSRFISVVSNHPADRDELIRTYARAGVVNHSLLPGPLRPVAGAAVRAMEATPGPGTWMWVVALSVVGFVYAGRREWVAIYAPVILVWATLMVAAPTVTPFRYMAPIIMVAPLGLAVLLGTDQAAWNPSSRGTTTSDDTICGTILKCQASRRSSPRCRTTHAESLTQNS$","Membrane protein","Membrane, Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[35-53]?$ $\"[219-237]?$ $\"[242-260]?$ $\"[266-286]?$	transmembrane_regions

InterPro
IPR008651
Family

HicB
PF05534	$\"[59-109]T$	HicB

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-50% similar to PDB:2NAP DISSIMILATORY NITRATE REDUCTASE (NAP) FROM DESULFOVIBRIO DESULFURICANS (E_value = );-54% similar to PDB:1DDR MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE AND UREA (E_value = );-54% similar to PDB:1DDS MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE (E_value = );-54% similar to PDB:1DHI LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUTANT DIHYDROFOLATE REDUCTASE (E_value = );-54% similar to PDB:1DHJ LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUTANT DIHYDROFOLATE REDUCTASE (E_value = );","Residues 59 to 109 (E_value = 3.4e-22) place ANA_1561 in the HicB family which is described as HicB family.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1562","1690401","1688335","2067","10.68","23.52","70727","ATGGCTGCGAGCATGGCAGCGGGGCTGAACGCAGACTCCGGCTGGAGCCTGGCGGCCGCCACGCTCGTCATAGCCGGACTGCTGCTCGTACCCGGCTGGGTCATCGGACGATCTGCCCGCCTGGGGGCGCTGCCGTCCCTGGCGGTGGCCCCGGCCATCGGTTCGGCGCTCATCGGGGCGGCGGAGATCCTCACCCATGCCCTGGCGCTGACGTGGCGTCCCTGGGGCTGGGCGGTCATCGCCGCCCTGAGCGTCGGATCAACCCTCCTCATGCGCCTGGTGGCCGGCCCTGCAGCGGGGCCAGGGCGTCAGGGGATGCCGTGGAGCCGGGCCGAGCGGATGATCCTGGCCGGTGGTCTGAGCGTGGCCGTCGTCGTGCCGGCCGGGGTGATCCTGTCCTGTCTGCCGAGCCCCGGCTACCCCGCGCAGGCCTTTGACGCGACCTTCCACCTCAACGCGGTGGCAGCCATCCGAGAAGGGGGCAACGCCTCCATGCTGGGAGGCCTGTCGTCCCTCTACTCGGGTCGCGCCATCTACTACCCCACCGTGTGGCACGGGGCTGTGGCATTGGCGCCGGGCGGTCCGGTCCCGGCCAGTACTGCCGGGATCCTGGCTCTGACTGCCGTGATCTGGCCGCTGAGCCTTCTGGGGCTACTCGCCCGGGTCACCGGACTCGACTCCGCCTCCGACTCGGTCGGCGACGGTGCCGAGCGGCGCCAACAGGTGTGTGCGCTCGCCTCGGTGCTCGCGCTCAGCGCTGGGCTCGTGGGTTTCCCCTTGCTGCTCATGACCTCGCTGGCGGTGTGGCCCTATGCTCTGAGCGTCCTGGGGCTCCCCGGCGCCCTCGTGCTCTACGACCAGCTGCGTGAAGGCGCCGTATCGAGGCGCCTTCACCTGACATGGGTCCTTCTCATGCTGGCCGTCGCCGGAGGCGTGGTGGCCGCGCACGGCACCGGTCTGTTCAACCTGGCGATCCTCACCCTGCCTTTCCTGACCGACGCCGTCGCCTCCTGGTGGCGCCGCAGCGCCGGCCGGAGGGGCGGTCGAGCCCTCCTGGCGGTCGGAGCGGCCGGGGTCATGCTGGCCCTGGCCACGGGGGGCTGGCTCATGCGCGGCTCCCTGGCCTCCGTCCTGGGCTACGAGCGTCCTGCCGGCGGAGTGGCCGGCGCCGTGGCGACCCTGGGCCAGGCACTCATCGACCTCCCGATGTACGGGGCGGTTCCCGGCGCCACCGTGCCCATCGGGATCGTGTATGGCCTGCTCACCCTGGGGGCGGTATGGTCGGCACGCTCGCGGCGGGACCAGCGCCCCTGGCTCGTCATGTGGCTGCTGGCGCTGACTCTCCTGGTCCTGACAGGGGGGCCGCAGTGGGCGGGGCGGCAACTCGGCTCGCCCTGGTACCTGCAGAAGGCCCGAATCCTCCCCCTGGCCATCCTGCCGTCTCTGATCCTCCTGGCCCAGGGTGGTGCCGGGCAGCCCGGGCAACGACTGTGGGCGCTGCTGCGCCGGGCGGCCTCGGGACTGGGCGGAGCGCGGCCGAGGCGGATGGCGGCCGCCATGCTGGTCGCGATCGTGCTCCTGCCGGTGGCGGTGCGAGTCCCCGTGGAGCGGGCCCTCGTCACCTCCGTCTACGATCCGCAGCGCATTCAGTACGGGACCCTGCTCACTAAGGACGCCATCACACTCATTCAGCGCTCCCGGAGCAGGCTGCCCGACGACGCCGTCGTCCTGGGGGCGCCGTCGAGGGGGGCTGCCCACCTGTGGTCCCTGGGCGGGGTGCATGTCGTCTACCCGATGCGCGCCGCAGCTGCGCCGGGCACCCCGGAGGCCGCGCTGGCCTCAGCCTGGCCCGCCCTGGGGCAGAAGGGCTCCCAGACCTGCGCACTTCTCAACCAGCTGGGAGTGCGCTACTTCTACAGCAGCTCGGATGCGACGGCCTCGGGCTCGGTCACCGGCGCCGCCCCCTTGCGCTGGGACGCGCGCCTGACTCAGGTCCCCACCGAGGGGCTCGAGCTCATCGACTCCCAGGGAAGCGCCGCCCTGTGGCGCATCACCGCCTGCGACTGA","MAASMAAGLNADSGWSLAAATLVIAGLLLVPGWVIGRSARLGALPSLAVAPAIGSALIGAAEILTHALALTWRPWGWAVIAALSVGSTLLMRLVAGPAAGPGRQGMPWSRAERMILAGGLSVAVVVPAGVILSCLPSPGYPAQAFDATFHLNAVAAIREGGNASMLGGLSSLYSGRAIYYPTVWHGAVALAPGGPVPASTAGILALTAVIWPLSLLGLLARVTGLDSASDSVGDGAERRQQVCALASVLALSAGLVGFPLLLMTSLAVWPYALSVLGLPGALVLYDQLREGAVSRRLHLTWVLLMLAVAGGVVAAHGTGLFNLAILTLPFLTDAVASWWRRSAGRRGGRALLAVGAAGVMLALATGGWLMRGSLASVLGYERPAGGVAGAVATLGQALIDLPMYGAVPGATVPIGIVYGLLTLGAVWSARSRRDQRPWLVMWLLALTLLVLTGGPQWAGRQLGSPWYLQKARILPLAILPSLILLAQGGAGQPGQRLWALLRRAASGLGGARPRRMAAAMLVAIVLLPVAVRVPVERALVTSVYDPQRIQYGTLLTKDAITLIQRSRSRLPDDAVVLGAPSRGAAHLWSLGGVHVVYPMRAAAAPGTPEAALASAWPALGQKGSQTCALLNQLGVRYFYSSSDATASGSVTGAAPLRWDARLTQVPTEGLELIDSQGSAALWRITACD$","Hypothetical protein","Membrane, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[49-69]?$ $\"[75-95]?$ $\"[116-136]?$ $\"[200-220]?$ $\"[241-259]?$ $\"[265-285]?$ $\"[297-315]?$ $\"[321-340]?$ $\"[350-370]?$ $\"[409-429]?$ $\"[439-459]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:2J9I LENGSIN IS A SURVIVOR OF AN ANCIENT FAMILY OF CLASS I GLUTAMINE SYNTHETASES IN EUKARYOTES THAT HAS UNDERGONE EVOLUTIONARY RE-ENGINEERING FOR A TISSUE-SPECIFIC ROLE IN THE VERTEBRATE EYE LENS. (E_value = );-37% similar to PDB:1W1O NATIVE CYTOKININ DEHYDROGENASE (E_value = );-37% similar to PDB:1W1Q PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH ISOPENTENYLADENINE (E_value = );-37% similar to PDB:1W1R PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH TRANS-ZEATIN (E_value = );-37% similar to PDB:1W1S PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH BENZYLAMINOPURINE (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1563","1691737","1690433","1305","4.92","-21.62","46673","ATGCGCATCGCCGTCGTCGCCCTGGGCAAGATCGGACTGCCCCTGGCCGTCCAGTACGCAGACAAAGGCCACGAGGTCATCGGGGTCGACGTCAACCCCGCCGTCGTCGAGGCCGTCAACGCCGGGACCGAGCCCTTCCCCGGCGAGGCCCACCTGGCCGAGAAGCTCGCCGCCCTGAGCCCCGCCACCGGCAACGGCGCCCTGCGCGCCACCACCGACTATGCCGAGGCCATCCCCGAGGCCGACGCGATCGTGCTGGTTGTGCCGCTCTTCGTCAACGACGCCACCTGGGAGCCGGACTTCGCCTGGATGGACGACGCCACCCGCTCCCTGGCCGCCCACCTGACCCCCAACACCCTCATCTCCTATGAGACCACCCTGCCCGTGGGCACGCTGCGGGATCGCTTCAAGCCCATGATCGAGGAGATCAGCGGCCTGAAGGAGGGGACGGACTTCCACCTGGTCTTCAGTCCCGAGCGAGTCCTCACCGGCCGTGTCTTCGCCGACCTGCGCCGCTACCCCAAGCTGGTGGGCGGTCTGGACGAGGCCGGTACCCAGGCCGGCATCGCCTTCTACGAGTCCGTCCTCGACTTCGACGAGCGCGATGACCTGCCCCGCCCCAACGGCGTGTGGGACATGGGAACTGCCGAGGCTGCTGAGATGGCCAAGCTCGCCGAGACCACCTACCGCGACGTCAACATCGGCCTGGCCAACCAGTTCGCCGTCTACGCCGACAAGGCCGGCTTCGACATCGAGCGCGTCATCGAGGCCTGCAACTCCCAGCCCTACTCCCATATCCACCGCCCCGGTATCGCGGTGGGCGGGCACTGCATCCCGGTCTACCCGCGCCTGTACCTGTCCACCGACCCCGACGCCTCCGTGGTGCGTACCGCCCGCACCTTCAACGCCACGATGCCCGCCTACGTAGTGGGCCGAGCCACCGAGGTGCTCGGTTCGCTCAAGGGCCTGCGCGTCGTCGTGCTGGGAGCCTCCTACCGCGGCAAGGTCAAGGAGACTGCCTTCTCCGGCGTCTTCCCCACCGTGGAGGCCCTGCGCGAGGCCGGAGCCGAGGTCCTCGTCCACGACCCCATGTACACCGACGAGGAGCTGGCCGGCTTCGGTTGGACCCCCTACCACCTGGGGGAGCAGGTCGACGTCGCCATCGTCCAGGCCGACCACCCCGAGTACGGCGAGCTCTCGGCCGCCGACCTGCCCGGGCTGCGTCTCCTGCTGGACGGCCGCCGCGCCACGGACGCCGCCAAGTGGACCGGTGTCCCGCGCCTGACCATCGGCGGAGGCGAGTGA","MRIAVVALGKIGLPLAVQYADKGHEVIGVDVNPAVVEAVNAGTEPFPGEAHLAEKLAALSPATGNGALRATTDYAEAIPEADAIVLVVPLFVNDATWEPDFAWMDDATRSLAAHLTPNTLISYETTLPVGTLRDRFKPMIEEISGLKEGTDFHLVFSPERVLTGRVFADLRRYPKLVGGLDEAGTQAGIAFYESVLDFDERDDLPRPNGVWDMGTAEAAEMAKLAETTYRDVNIGLANQFAVYADKAGFDIERVIEACNSQPYSHIHRPGIAVGGHCIPVYPRLYLSTDPDASVVRTARTFNATMPAYVVGRATEVLGSLKGLRVVVLGASYRGKVKETAFSGVFPTVEALREAGAEVLVHDPMYTDEELAGFGWTPYHLGEQVDVAIVQADHPEYGELSAADLPGLRLLLDGRRATDAAKWTGVPRLTIGGGE$","UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase","Cytoplasm","udp-n-acetyl-d-mannosaminuronic aciddehydrogenase","UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase ","UDP-glucose/GDP-mannose dehydrogenase","","Roychoudhury S., May T.B., Gill J.F., Singh S.K., Feingold D.S., Chakrabarty A.M. Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa. J. Biol. Chem. 1989. 264(16):9380-9385. PMID: 2470755Campbell R.E., Sala R.F., van de Rijn I., Tanner M.E. Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol. J. Biol. Chem. 1997. 272(6):3416-3422. PMID: 9013585","","","

InterPro
IPR001732
Domain

UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03721	$\"[1-197]T$	UDPG_MGDP_dh_N

InterPro
IPR014026
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation
PF00984	$\"[216-280]T$	UDPG_MGDP_dh

InterPro
IPR014027
Domain

UDP-glucose/GDP-mannose dehydrogenase, C-terminal
PF03720	$\"[326-419]T$	UDPG_MGDP_dh_C

InterPro
IPR014028
Domain

UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding
PTHR11374	$\"[165-363]T$	UDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC DEHYDROGENASE

InterPro
IPR014360
Family

UDP-glucose/GDP-mannose dehydrogenase
PIRSF000124	$\"[1-427]T$	UDP-glucose/GDP-mannose dehydrogenase

InterPro
IPR014687
Family

UDP-N-acetyl-D-mannosaminuronate dehydrogenase
PIRSF500136	$\"[1-433]T$	UDP-N-acetyl-D-mannosaminuronate dehydrogenase

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.220	$\"[216-280]T$	no description
G3DSA:3.40.50.1870	$\"[307-430]T$	no description
G3DSA:3.40.50.720	$\"[1-195]T$	no description
PTHR11374:SF4	$\"[165-363]T$	UDP-N-ACETYL-D-MANNOSAMINURONIC ACID DEHYDROGENASE
signalp	$\"[1-16]?$	signal-peptide

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[42-62]?$ $\"[68-90]?$ $\"[111-131]?$ $\"[195-215]?$ $\"[225-243]?$ $\"[249-269]?$ $\"[281-299]?$ $\"[305-325]?$ $\"[335-355]?$ $\"[395-413]?$ $\"[422-442]?$ $\"[452-472]?$ $\"[487-507]?$	transmembrane_regions

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[198-370]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[13-357]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF44	$\"[13-357]T$	GLYCOSYLTRANSFERASE

","BeTs to 15 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 198 to 370 (E_value = 3e-07) place ANA_1565 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","transferase, group 1 family protein domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1566","1695094","1696467","1374","5.73","-19.60","48211","ATGTTGTCAGCCATGGTCGCGCTCCTTCACGGGTTGGTGCCTCGCCGGCACTCCAGGCGATCCGGCGAGCTCCTCAGCCACCTGGCGAGCCCTGGCCTGCCAGGTCTGACTCGGTACGACCTGGCGCATACGCCGGCGCACCGCCTCGATCTCCTCAGGCGTCTCACGCAGGTGACGCAGCAGTGCGCTGAGGGCTTCGACGTCGTACTCGAGCACCCACCCGATCCCCATCTCCTGGACGAGACGCCCGGTCTGGGTGCCGCGCACGGCGATGACGGGCAGCTCGTGGGCCAGGTACTCGTAGAGTTTGTAGGGGACGGCGAAGTCCCAGTACGGGTTCGGTTCGGTGAACAGCACCCCGAGGTCGGCGCGCTCGTAGAGCGGAAGGAGCTCACTGCCGGAGCGGTGGACGACGTCGGCCCGCCCGACGGGCAGGAGCGGGGCGTAGTGTTCGCGGGTCTCCTCCCAGGTCTCCTGGCGCACGCACAGTGTCACGCGCGTTCCAGGAGTCTGGCTGACAGCTTTCAGGCAGGCGTCGAGTCGGTAGTTGTCCTGCAGGACCCCGACGAACAGGAGGTCCAGCTCCGCTTTGTCCCGGGACTCGCCGACCGGGCGGCCCACGTCCCCGGCCTCGACGACCGGGGCGCCGGGGGGCAGGGCGCTCGCCCGATCCGGAGTGAGGAAAGGAACATGGCGGCCCATGGCCCGACTGGGCAGGAAGAGGTGGATGCCCAGGCGCCGGTAGACCAGAAGCTCACCGCGGTAGGTCGCCTGGAGACCGGCCTCCAGGATCGGGTTGATCCCTTGCCGGAACTGGCGGAAACGCCAGTAGATGTCCCTGTAGAAGATGCCCACGGGAGCCCCGGCGCGCTGGCAGTCGCGGAAGAAGGCCAGGTCCAGCAGCGGGTGCGGCGGCAGATGACGGGGCTCGGTCAGGGCGTTGGGGATGGTGGCGTTCTCGCCGTAGACGAAGGCGGGCACGTCACCGGCAGCGATCGCCGCTCGCACCCGGCGCATGGCCTGACGCCGCTCAGCGGCGTATCCGCTGACCTCCATGACCCGGTAGCCGATGTCGGTGAAGGCCTGACGCATCGCAAGGGGCCGCAGGATGGAGGCCGCGAGGCGGCCCGACTGGAGGGGGAAGGGAGTATGGAAGACCATGAGCCTGCCAGCCCCGCCTCCACCATCCATGCTGCTTGCGCTCACGAGGTCACCTCTTGTCTTGTGCCTTGGTCCCGCATGCGGACAATCCGCCCCGCGGGATGCCCAGAAAGCATCTCACACCTGACCGAACCGACGAGACACATGTCTGTTGCCAGCCACCACAGCATGTCGCTGGTGCCCGCCGGGCGTCAACCGCGTCACGTGTCATAA","MLSAMVALLHGLVPRRHSRRSGELLSHLASPGLPGLTRYDLAHTPAHRLDLLRRLTQVTQQCAEGFDVVLEHPPDPHLLDETPGLGAAHGDDGQLVGQVLVEFVGDGEVPVRVRFGEQHPEVGALVERKELTAGAVDDVGPPDGQERGVVFAGLLPGLLAHAQCHARSRSLADSFQAGVESVVVLQDPDEQEVQLRFVPGLADRAAHVPGLDDRGAGGQGARPIRSEERNMAAHGPTGQEEVDAQAPVDQKLTAVGRLETGLQDRVDPLPELAETPVDVPVEDAHGSPGALAVAEEGQVQQRVRRQMTGLGQGVGDGGVLAVDEGGHVTGSDRRSHPAHGLTPLSGVSADLHDPVADVGEGLTHRKGPQDGGREAARLEGEGSMEDHEPASPASTIHAACAHEVTSCLVPWSRMRTIRPAGCPESISHLTEPTRHMSVASHHSMSLVPAGRQPRHVS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide

InterPro
IPR001962
Domain

Asparagine synthase
PF00733	$\"[149-246]T$	Asn_synthase

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[139-403]T$	no description

","BeTs to 5 clades of COG0367COG name: Asparagine synthase (glutamine-hydrolyzing)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0367 is aompkzy---rlb-efg-s--j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 149 to 246 (E_value = 0.00073) place ANA_1567 in the Asn_synthase family which is described as Asparagine synthase.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1568","1700630","1699371","1260","8.37","5.06","45915","GTGCACGTTGTCTTCACTCCCTCGTGGTACCCGGACCGGAACCGCCCCCACAACGGTTCCTTCTTCCGCGACCAGGCGCGCATGCTTCAGCGCAGCGGGATGCGAGTGGGCGTCATCGCCCTGGAGCCGGTCTCCTTCTGGCAGGCACGCCGCGAGCTGACGGTGGATGTCGAGGAGGGGATCGTCGTCGTGCGCGGCACGGTGCCCACGATCCCCAAGGGCGTTCTGCCCGGGGACCGGATGGTGGCTCGCGCGGTGGCCGCCCGAGCGGTACGGCTCTATGAGGAGACGATTCGCAGCCTGCCTGAATCCTCCAGCAGCGGTGGGGGAGAGTCGGTTCCCGACGTCGTTCACGCCCACTCGGTGTTCACCGGCATCCACGTCGGCCGCTACGCCGCCGAGCGCTGGGGCGCCGCACTGGCCATCACCGAGCACCGTCCCAGCTCGACGGACCGCAGTGTGCATGGGTGGCGGTACCGGGCTCTGCGGCGCGACCTGCGACGTGCCCCAGGGCGCGCCGTTGTCTCCACCCCCTTTGCGGAGGTCCTGAGGGACTACTGGCGGCTCGGGGAGTGGAGGAGCATTGCCCTTCCGGTCAACGACGAGGTCTTCGATGTCCCCAGGCCAGCCAACCAGGATCGGCATGGCGACAACGCCAGGGCCCTGACCGTCTGCCACGTCTCCCACCTGGGGCGTAACAAGCGCCCCGAGGAGACCATCCGCGCCGTCGCCCGGCTGGCCCGCGCCGATGTCGCCGCCGGGCGCGAGCCCACACGCCTGCTCCTCGTCGGAGGGGAGGCCCACGAGATCGAGCCCCTGCGAGAACTGGCTCGGGCCGAGGGCATCGAGCAGACCTCCACCTTCACCGGCCGGGTGCCCCACGACGAAGTCAGCGGACTCATGGCTTCCAGCGACGTCTTCGTCCTGGCCAGCGAGGTCGAGGCCGGGGGCACCGTCCTGGCCGAGGCCCAGGCTTTGGGGCTGGTTTGCGTGGCCACGCCCACCTGGGCGGGACGATTCATGGTCGAGCCCGAGACCGGCGTCGTCCTGCCCGCCGCGGCCCAGGTCAGCGACGACGCCGTCGTGTCCGCCCTGACCGAGGCGCTCACCCACGTGACTGACTCCATCCGCGCTGGGGGCTACCGCCCCGAGACCATCCGGGCCCGCGCCCGCCAGCGGTTCGGGGAGGCCACCTTCGTCAGGGCCTGCCGAGAGCTCTACGAGCAGGCGCGCGGCGAGATCACCGGGAGTGCACGCTGA","VHVVFTPSWYPDRNRPHNGSFFRDQARMLQRSGMRVGVIALEPVSFWQARRELTVDVEEGIVVVRGTVPTIPKGVLPGDRMVARAVAARAVRLYEETIRSLPESSSSGGGESVPDVVHAHSVFTGIHVGRYAAERWGAALAITEHRPSSTDRSVHGWRYRALRRDLRRAPGRAVVSTPFAEVLRDYWRLGEWRSIALPVNDEVFDVPRPANQDRHGDNARALTVCHVSHLGRNKRPEETIRAVARLARADVAAGREPTRLLLVGGEAHEIEPLRELARAEGIEQTSTFTGRVPHDEVSGLMASSDVFVLASEVEAGGTVLAEAQALGLVCVATPTWAGRFMVEPETGVVLPAAAQVSDDAVVSALTEALTHVTDSIRAGGYRPETIRARARQRFGEATFVRACRELYEQARGEITGSAR$","Glycosyl transferase, group 1 family","Cytoplasm","putative glycosyltransferase","RfaG protein","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[208-334]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[114-407]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF41	$\"[114-407]T$	GLYCOSYLTRANSFERASE

","BeTs to 20 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 208 to 393 (E_value = 9.7e-14) place ANA_1568 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","glycosyltransferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1569","1698278","1699390","1113","6.77","-1.69","39715","ATGCGTGTCACCATCGTCAGCACCTGGTTCCCCACAGAGGTCTCCGCAGGACTGGGCATCTTCGTCGCCCGGCACGCCGCCTCGATGGCCGCCGCCGGACACGACATCCGGGTCGTCCACCTCGTCGCCGCTCACGTCGATGACGGCACGAGACGTACTCGCGTCATGGGTGTGCCGGTCGTGCGGCTGCCCATGACGCCCTCGCGCCCTCATGAGGTGCTGGCCGCCAGACGGGCACTGGGAACGCTGACCGCGGGCAGCGACATCGTCCACACCCACGCCATCTCCACACTCATGCCCTATGCCCTGAGGCGGCCGCGCGAGCCGTGGCTCCACACCGAGCACTGGTCGGGACTGGCCAATGGCGGGGCCGCTCTCGGCACGATCTCGCGCGCAGGGGCCCAGGTGGTGCTGCGTCTGGAACGCAGGCCCGACGTCGTCACCACCGTCTCCGACCAACTCGCCGCCGACCTGAGGGCCTACCGCCCTCACGGCGAGATCCTGACCGTTCCCAATGAAGTGACTCGTCCCAGCAGGCCCGCCGAGCGTCGGGCCGTCCAGCTGGGGCGGGACGTCCTGCAGATCGTGGGAGTCGGGGGACTGATCGAGCGAAAGCGTCCGGACCTGGCGGTCAGAACAGTCGCGGCGCTGGCGGAGCTGGGTGTCCCCGCCCGGCTGACCTGGGTGGGCGACGGCCCCCTGGCCGAGCACTGCACCGCTCTTGCCCAGAGCCTGAACGTCGATCTGGAGCTGACCGGTCAGCTCCCCGATGACCTCGTCGGGGAGGTTCTGTCCGTCAACGACCTCTTCCTCGTGCCGACGATGGCAGAGACCTTCTTCCTGGGGGCCGCCGAGGCGCTCGCGGCGGGTCGGCCGGTGGTCACCAGCGACCGCGGCGCGCATACGAGCTTCCTGGACCCCTCCGTCACTGAGATCGTCAGCCAGGACGACCCTCTCACGTGGGCCAGGGCCGTCATCGACGTCATGCACCGTTGCGAGGGACTGACGGCCCAGGACATCCAGGACACGCTGCCGCGGGCCTTCTCCCCCGAGGAGGTGGCGGGCGCCTACGGACGCGCCTACGAGGCCGCCATCAGCGTGCACTCCCGGTGA","MRVTIVSTWFPTEVSAGLGIFVARHAASMAAAGHDIRVVHLVAAHVDDGTRRTRVMGVPVVRLPMTPSRPHEVLAARRALGTLTAGSDIVHTHAISTLMPYALRRPREPWLHTEHWSGLANGGAALGTISRAGAQVVLRLERRPDVVTTVSDQLAADLRAYRPHGEILTVPNEVTRPSRPAERRAVQLGRDVLQIVGVGGLIERKRPDLAVRTVAALAELGVPARLTWVGDGPLAEHCTALAQSLNVDLELTGQLPDDLVGEVLSVNDLFLVPTMAETFFLGAAEALAAGRPVVTSDRGAHTSFLDPSVTEIVSQDDPLTWARAVIDVMHRCEGLTAQDIQDTLPRAFSPEEVAGAYGRAYEAAISVHSR$","Glycosyl transferase, group 1 family","Cytoplasm, Membrane","NanG6","hypothetical protein predicted by Glimmer/Critica","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[179-330]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[2-366]T$	GLYCOSYLTRANSFERASE
signalp	$\"[1-16]?$	signal-peptide

","BeTs to 14 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 179 to 342 (E_value = 1.8e-08) place ANA_1569 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1570","1702093","1700702","1392","9.98","14.81","50120","GTGAGTGGCTCCGCCAAGGGCGCCGCAGGCGATCCTGCGGCGCCCACCTCAGGCGGCTTGATCGGGCGGGTTCGCCGGCGCGTGTCGGCGCTTCTGGAGTCCTCGCCGTTGCTGGGGCACGTGCTGACCCTCATCACCGGGACGGCTGTGGCCCAGGTGGTCAGTTTCGGCATGTCGATCGTGCTGGCGCGCATCTACACGCCTCGCGACCTGGGACTGATGGCGATCTACACCTCTGTCGCGGGAATCCTCGTCGCGGTGGCGGCACTGCGCTACGACATGACGATCATGCTCCCCAAGAAGGAGCCCGAGGCCCTGAGCGTGGCCCGCTTGGGACTGGTGTGCATCGCCGTCGTCTCGCTGCTGGCGACGGTGGCGGCCTTCCCCCTGCACGGTCTGGTCACCCGGTGGTGGGGGCATGAGGTCGCCTTGTGGATGCCCTTAGTGGGTCTGACCACCTTCCTCATGTCGGGGGTGGAGCTGTTCAAGTTCTGGTTCAACCGCTCCAGCAACTACCGCGCCATCGCCATCAACCAGGCCGAGCAGCAGATCGGCGTCAACGTCGGCCAGGTCGGCCTCGGCCTCGCGGGAATGGGGGGGATGGCCGGCCTGATGCTGGGCTTCACCGCCGGCCAGGTCTTCGCCTTCGGAAATCTGGGACGCCAGGCCAAGGAGCTGTGGCGCCCACTGCCCCAGGAGGCGCCGTCCCTGAGGTGGGTGGCCCGCCGCTACCGGCGCATGCCGCTGCTCAACGGCCCCAACGCCCTGGCGGACGCCCTGCGCCTCAACGGCATCCAGCTGCTCATCGCGAGCTACTCGGCCTCCGCGCTGGGCCAGTTCCAGATGGCCTGGCGCTACCTGGACGCACCACTCATCCTCATCAACGGCGCGGTGGCCAAGGTCTTCTTCCAGAAGCTCTCCACGATCGAACCCGGTCAGATGAGGCCGTTGGTGCGGGTCACCATCAAGCGGGCGGTCCTGATCGGCATCGTCCCCTTCGCACTCATCTACGTGCTCTCGCCATGGCTCTTCCCGCTGCTCCTCGGCGCCACATGGACCGACTCCGGGAGCTTCGCGAGGGCCCTGACCCCGTGGCTGTTCATGCTGCTCATCACCTCGCCGATCTCCAACCTGTTCGTCGTCACCGAGCACCAGGACTGGATGCTGGGCTTCGCCCTGCTCTACACCGCCGCGCCCCTGGCCTGGCTGCACTGGTCACCGCTGGAGGTCATGCCCACCTGCTACGTGCTGGGTCTCATGATGGCGGGTCTGCTGGTGCTCAACACGCTGCTGGCCGACTACGCGGCCAAGCAGTTCGACGCGCACGGGTCCGTCCGGACCGGAAGGAGGCGCGGACATGACTCCCACGAAGCCGATGTCTCAGACGCCTGA","VSGSAKGAAGDPAAPTSGGLIGRVRRRVSALLESSPLLGHVLTLITGTAVAQVVSFGMSIVLARIYTPRDLGLMAIYTSVAGILVAVAALRYDMTIMLPKKEPEALSVARLGLVCIAVVSLLATVAAFPLHGLVTRWWGHEVALWMPLVGLTTFLMSGVELFKFWFNRSSNYRAIAINQAEQQIGVNVGQVGLGLAGMGGMAGLMLGFTAGQVFAFGNLGRQAKELWRPLPQEAPSLRWVARRYRRMPLLNGPNALADALRLNGIQLLIASYSASALGQFQMAWRYLDAPLILINGAVAKVFFQKLSTIEPGQMRPLVRVTIKRAVLIGIVPFALIYVLSPWLFPLLLGATWTDSGSFARALTPWLFMLLITSPISNLFVVTEHQDWMLGFALLYTAAPLAWLHWSPLEVMPTCYVLGLMMAGLLVLNTLLADYAAKQFDAHGSVRTGRRRGHDSHEADVSDA$","O-antigen translocase","Membrane, Cytoplasm","O-antigen translocase, putative","O-antigen translocase","polysaccharide biosynthesis protein","","Kota J., Ljungdahl P.O. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J. Cell Biol. 2005. 168(1):79-88. PMID: 15623581","","","

InterPro
IPR002797
Family

Polysaccharide biosynthesis protein
PF01943	$\"[37-310]T$	Polysacc_synt

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[316-463]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[41-63]?$ $\"[73-93]?$ $\"[112-132]?$ $\"[142-162]?$ $\"[199-219]?$ $\"[325-345]?$ $\"[361-381]?$ $\"[386-406]?$ $\"[412-432]?$	transmembrane_regions

","BeTs to 3 clades of COG2244COG name: Membrane protein involved in the export of O-antigen and teichoic acidFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2244 is aompk---vd-lb-efghsn-j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 37 to 310 (E_value = 0.0034) place ANA_1570 in the Polysacc_synt family which is described as Polysaccharide biosynthesis protein.","","translocase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1571","1703157","1702090","1068","5.64","-10.14","37599","ATGAGCGAGAACGTCGCCCTCGACGGGCAGGCCACCACCGCGCTGCCCGAGGTCCACTACCTCACCGACAAGGGCACGGCGGACAACCCGTTGCGCGTGGGCCTCATCGGCCTGGGCTCCATGGGACGCCACCACGCCCGGGTCATCCGTGCCACCGAGGGCATGGAGCTCGTGGCCGTGGCCGACCCCGGCGGCGACCGCTTCGGTGTGGCCGGCGAGCTGCCGGTCCTGCCCGATATCCACGCCCTCATCGACGCCGGGCTGGACGCCGCCATGGTGGCCGTCCCCACCGTCTACCACGAGGACGTCGCCCTGGCCCTGGCCGAGGCGGGCGTGCACACCATGGTGGAGAAGCCCATCGCCCACGACGCCGCAGCGGGCCGCCGCGTGGCCGCCGCCTTCGCCGAGCGGGGCCTGGTGGGCGCCGTCGGCTACGTGGAGCGCTGCAACCCCGCCCTGCGGGCCCTGCGCGAGCGCCTCGACGCCGGCGAGCTCGGTGCGGTCTACCAGGTCCTCACCCGCCGCCAGGGCCCCTTCCCGGCCCGTATCAGCGACGTCGGCGTCGTCAAGGACCTGGCCACCCACGACATCGACCTCACCGCCTGGGTCGCCGGCGCCCGCTACACCTCCGTGGCCGCGCAGGTCACGCACCGCTCCGGCCGCCAGAACGAGGACATGATGGTGGCCACCGGTCTGCTGGAGGGCGGCATCGTCGTCAGCCACCAGGTCAACTGGCTCACACCCTTCAAGGAGCGCGTCACGATCGTCACCGGGGAGAAGGGCGCCTTCGTGGCGGACACCCTCACCGGGGACCTCACCTTCCACGCCAACGGCACCGTGGCCTCCACCTGGGACCAGGTCGCCGCCTTCCGGGGGGTCAGCGAGGGTGACGTCATCCGCTACGCGATCCCCAAGCGCGAGCCGCTGGCCCTGGAGCAGGAGAACTTCCGCGACGCCGTGCGCGGCGTGGCCCAGCGCCACGTCACCATGGCCGAGGGCGTGGCCACGCTCGACGTCGTCGAGGCGGTCCTGACCTCGGCGAGCGAGAATCGGACGGTCACTTTGTGA","MSENVALDGQATTALPEVHYLTDKGTADNPLRVGLIGLGSMGRHHARVIRATEGMELVAVADPGGDRFGVAGELPVLPDIHALIDAGLDAAMVAVPTVYHEDVALALAEAGVHTMVEKPIAHDAAAGRRVAAAFAERGLVGAVGYVERCNPALRALRERLDAGELGAVYQVLTRRQGPFPARISDVGVVKDLATHDIDLTAWVAGARYTSVAAQVTHRSGRQNEDMMVATGLLEGGIVVSHQVNWLTPFKERVTIVTGEKGAFVADTLTGDLTFHANGTVASTWDQVAAFRGVSEGDVIRYAIPKREPLALEQENFRDAVRGVAQRHVTMAEGVATLDVVEAVLTSASENRTVTL$","Oxidoreductase","Cytoplasm","Predicted dehydrogenase","oxidoreductase-like","oxidoreductase domain protein","","","","","

InterPro
IPR000683
Domain

Oxidoreductase, N-terminal
PF01408	$\"[31-145]T$	GFO_IDH_MocA

InterPro
IPR004104
Domain

Oxidoreductase, C-terminal
PF02894	$\"[157-256]T$	GFO_IDH_MocA_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[21-180]T$	no description
PTHR22604	$\"[78-351]T$	OXIDOREDUCTASES

InterPro
IPR000653
Family

DegT/DnrJ/EryC1/StrS aminotransferase
PIRSF000390	$\"[5-377]T$	Predicted pyridoxal dependent aminotransferase, DegT/DnrJ/EryC1/StrS types
PF01041	$\"[11-370]T$	DegT_DnrJ_EryC1

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[5-245]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[248-370]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[81-131]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF35	$\"[81-131]T$	ASPARTATE AMINOTRANSFERASE

InterPro
IPR001451
Repeat

Bacterial transferase hexapeptide repeat
PF00132	$\"[14-31]T$ $\"[32-49]T$ $\"[50-67]T$ $\"[68-85]T$ $\"[108-122]T$ $\"[126-143]T$	Hexapep

noIPR
unintegrated

unintegrated
G3DSA:2.160.10.10	$\"[5-160]T$	no description
PTHR22572	$\"[110-162]T$	SUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF17	$\"[110-162]T$	UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE-RELATED

","BeTs to 5 clades of COG0110COG name: Acetyltransferases (the isoleucine patch superfamily)Functional Class: RThe phylogenetic pattern of COG0110 is -Mt-y-vCEBR-------in-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 62 to 79 (E_value = 79) place ANA_1573 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 80 to 97 (E_value = 97) place ANA_1573 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 98 to 115 (E_value = 115) place ANA_1573 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 116 to 133 (E_value = 133) place ANA_1573 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 156 to 170 (E_value = 170) place ANA_1573 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).Residues 174 to 191 (E_value = 191) place ANA_1573 in the Hexapep family which is described as Bacterial transferase hexapeptide (three repeats).","","(1996) ","","1","","","Mon Aug 6 18:05:50 2007","","Mon Aug 6 18:05:50 2007","","","Mon Aug 6 18:05:50 2007","Mon Aug 6 18:05:50 2007","Mon Aug 6 18:05:50 2007","","","Mon Aug 6 18:05:50 2007","","","Mon Aug 6 18:05:50 2007","Mon Aug 6 18:05:50 2007","","","Mon Aug 6 18:05:50 2007","Mon Aug 6 18:05:50 2007","","","","","yes","","" "ANA_1574","1705243","1705917","675","6.54","-1.60","24384","GTGTCCCCGGTCACCGACACCTGGCTCGTCATCCCCTTGTACAACGAGGCGACCGTCGTGCGCGAGGTCATCTCCCAGGCTCGCACCATCTTCCCCTATGTCGTCGTCGTCGATGACGGCTCCAAGGACGCCTCGGCCCGGGAGGCCGCGGCCGCGGGGGCCGTCGTGGTGCGCCACCCGATCAACCTCGGCCAGGGCGCAGCGCTGCAGACGGGCTTCTCCTACGTCCTGGAGAAGACGAATGCCGACTACGTCGTCACCTTCGACGCCGACGGCCAGCACTCCCCCACCGATGCCGCCGCCATGGTCGCCGCGGCGCGCGACGAGGATCTCGCCGTCGTCCTGGGCTCACGCTTCCTCGAGGGCCCGTCCCCGGTGGGCTGGCTCAAGCGACTCGTCCTGCGCACAGCGGCGGCCGTCAGCTCGCACACCTCCGGCATGCGCCTGACCGACGCCCACAACGGCCTGCGGGTGATCCGCCGCGACGTCCTGGAGCAGCTCGACCTCAAGCAGAACCGGATGGCGCACGCCAGCGAGATCATTCGCATGATCGGTGCCACCGGCATGCCCTGGCGCGAGTTCCCGGTGCACATCGTCTATACCGAGTACTCCCGCTCCAAGGGCCAGTCCCTGTGGAACTCGGTCAACATCCTGGTCGACCTGCTCTTCTCCTGA","VSPVTDTWLVIPLYNEATVVREVISQARTIFPYVVVVDDGSKDASAREAAAAGAVVVRHPINLGQGAALQTGFSYVLEKTNADYVVTFDADGQHSPTDAAAMVAAARDEDLAVVLGSRFLEGPSPVGWLKRLVLRTAAAVSSHTSGMRLTDAHNGLRVIRRDVLEQLDLKQNRMAHASEIIRMIGATGMPWREFPVHIVYTEYSRSKGQSLWNSVNILVDLLFS$","Glycosyl transferase, family 2","Membrane, Cytoplasm","Glycosyltransferases involved in cell wallbiogenesis","glycosyl transferase","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[8-168]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[9-167]T$	no description
PTHR10859	$\"[14-223]T$	GLYCOSYLTRANSFERASE RELATED

","BeTs to 16 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","***** IPB001173 (Glycosyl transferase, family 2) with a combined E-value of 1.5e-06. IPB001173A 33-45 IPB001173B 82-91","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 168 (E_value = 2.8e-26) place ANA_1574 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","involved in cell wall biogenesis (Ppm1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1575","1705941","1706354","414","11.49","7.13","15152","ATGATTCATCAGTTCGCCGCCCAGGTCACCCCGATCACGAACCACCAGCTCTACATCCAGGCCGCCCTGATCCTGGCCGTGATCGCCGTCGGCTGGATGATGCTGCGCACCCCCGGCGGGGCCCGCCACATGGCCGCCCGCAGGCTGGTCACCCTGGCCTTCGTGGCCTTCGCCGTCTTCAACATCACCTTCCCCTGGGTGATGAGCTCGATCGCGCACCGGATGGGAGTCGGGCGAGGCACTGACTTCCTGCTCTACGCCCTGGTCATTGCCTTCCTGGCGCAGATCCTCTCCTCCTTCCGGCGCAACAGCGCCAGAGAGCGCCAGATCACTCACCTGGCTCGACGCATCGCCCTGGACAATGCCCCCGAGCCCCCCGCTGCCGCACGGCTCACTACTGAGGCCGACGACTGA","MIHQFAAQVTPITNHQLYIQAALILAVIAVGWMMLRTPGGARHMAARRLVTLAFVAFAVFNITFPWVMSSIAHRMGVGRGTDFLLYALVIAFLAQILSSFRRNSARERQITHLARRIALDNAPEPPAAARLTTEADD$","Hypothetical protein","Membrane, Cytoplasm","Hypothetical membrane protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PD020696	$\"[57-119]T$	YF80_METJA_Q58975;
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[16-34]?$ $\"[49-69]?$ $\"[83-101]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","membrane protein","","1","","","Mon Aug 6 18:10:34 2007","","Mon Aug 6 18:10:34 2007","","","Mon Aug 6 18:10:34 2007","Mon Aug 6 18:10:34 2007","Mon Aug 6 18:10:34 2007","","","","","","Mon Aug 6 18:10:34 2007","","","","Mon Aug 6 18:10:34 2007","Mon Aug 6 18:10:34 2007","","","","","yes","","" "ANA_1576","1707237","1706398","840","6.54","-2.16","30010","GTGCGAGTGGTGACGGTCGCCTTCAACCCGGGAGAGGAGCTGGAGCGCTTCCTGGCCTCCTTGGCCACGGCGACGGCGCGCAGACTCGTCGTCGTCATCGCGGACAACGGCACCGAGCACGACGTCGTCACTGCTGCTGCTCAGCGCCACGGGGCGCGCGTCGTCGGGGACGGCACCAACCTCGGTTACGGGGCGGGCGCCAACCTTGCGGCCGCGGATCTGGAGGAGGACTGGATCGTGGTGGCCAATCCCGATCTCGTCTGGAGGCCCGGGAGCCTGGACGTCCTCATCGATGCGGGCCGGGCCAACCCGGCGGCCGGCTGCCTGGGCCCCCTCCTGCTCAATCCCGACGGCACCGTCTACCCCTCCGGGCGCGCCCTGCCCTCCCTGGTCAAGGGCGCCGGGCACGCCGTCCTGGGCAGAATCTGGCCGGACAACCCCTTCTCGGCCGCCTATCACACCGCCGGACAGGGGACTTCTGAGCAGACCCGAACGGTGGGATGGCTCTCCGGGGCCTGCCTGCTGCTGCCCGCTGCCGCCTGGAGGCGCCTGGAGGGCTTCGACGACGAGTACTTCATGTTCTTCGAGGACGTGGACTTAGGGGAGCGGGTCGGGCGGGCCGGCTGGCTCAACGTGCAGGTGCCGGGCTCCGTCGTCGTCCACGAGCAGGGGGCCAGCTGGAAGGCCCGCCCCGAGAAGATGATCCGGGCGCACCACGCTTCGGCCCGGCACTACCTCAGGGGCGTCTACGACGCCCCGTGGCAGGCGCCGGTGCGCTGGCTGCTGACTGGCGGTCTGCGCCTGCGTGAGGAGCTCGAGGTTCGCGCCTCCCGATCCTGA","VRVVTVAFNPGEELERFLASLATATARRLVVVIADNGTEHDVVTAAAQRHGARVVGDGTNLGYGAGANLAAADLEEDWIVVANPDLVWRPGSLDVLIDAGRANPAAGCLGPLLLNPDGTVYPSGRALPSLVKGAGHAVLGRIWPDNPFSAAYHTAGQGTSEQTRTVGWLSGACLLLPAAAWRRLEGFDDEYFMFFEDVDLGERVGRAGWLNVQVPGSVVVHEQGASWKARPEKMIRAHHASARHYLRGVYDAPWQAPVRWLLTGGLRLREELEVRASRS$","Glycosyl transferase, family 2","Cytoplasm","dTDP-Rha:a-D-GlcNAc-diphosphoryl polyprenol,a-3-L-rhamnosyl transferase","dTDP-RhA:a-D-GlcNAc-diphosphoryl polyprenol; A-3-L-rhamnosyl transferase","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[2-99]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[1-262]T$	no description

","BeTs to 7 clades of COG1216COG name: Predicted glycosyltransferasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1216 is a-m-kz---dr--cef--s--j----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 191 (E_value = 4e-06) place ANA_1576 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","polyprenol, a-3-L-rhamnosyl transferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1577","1707459","1708745","1287","5.04","-14.66","45063","ATGATCGCTCCCGTGCCTCAGTTCAGTAAGCCGCACGCGCGGCACTCCTCCAAGGAACTCGGACGCCGTCTGGCCCGCCGAGTAGGACTCAGCCTGCTCGCGGTGACGATCTTCGTCGTCTCCGCCGCGGGCTTCGCGTGGCACAACATCCAGTCACGGATCACCTGGTTCAACATCGACAGCCTCCTGTCCGAGGAGGACCGGCCCGGCACCAAGCCGCCGGACAGCTACGAGGGTCGTGCCGTCAACCTCCTGATCCTGGGCACCGACTCTCGGGCGGGGAGCAACAACGTCGACGGCTCTCAAGGCGATGATGAGGTCTCCGTGGCCCGCTCCGATACGGCACTGGTCATGCACATCTCGGCCGACCGCAAGCGCGTCGATGCCGTGTCCATCCCTCGCGACACGCTGGTCGATATCCCCGAGTGCACCACCCTCGATGGCGGGAAGACCGAGGCCAGCGAGGACGCACCGTTCAACTCCGCCTTCGCCAAGGGAGCCGGCAGCAGCAGTGACGACAAGAAGGCCGTGGCCTCTGGAGCCGCCTGCACCCTCAAGACGGTGGAGACGCTGACGAACGTGCGCATCGACGACTTCATCGTCGTTGACTTCACCGGTCTGTCCAAGGTGGTCGACTCCCTCGGCGGCGTCCACGTGCAGGTCGATGAGGCCATTGACGACTCCGAGTACACCGGTTTCAAGCTCGCTGAGGGTTGCCAGAAGCTGGACGGCGAGAACGCCCTGCAGTACGCCCGTGTCCGGCACGGGGTGAGCGACGGCTCGGATCTCTCCCGCATCACCCGTCAGCAGAACCTCATGAGAGCGATGGCCTCCAAGGCGCTGTCCTCCAGCCTCCTGACGCAGTCCGGCTTCCTCACCAGCACCCTGGAGACCCTCACCACGTCTGAGCGCATCGGTCAGATCGGCAACCTGTCGGGTCTGGCCTACTCCATCCAGGGCGTGGGCATCGACAAGATCAACTTCGTCACTATGCCGAACGAGCCCGCAGCTGACCCGAACCAGGTGGTCCCCTCTGAGGGCGCCAAGAAGGTCTGGAAGGCCCTCGAGGAGGACAAGCCCGTCCCCTCCGACACCTCGGCCCCGGCCTCGTCGGACTCGAGCGCCACCACGAACGACTCCTCCTCGCAGAGCACTGACGAGTCGGCCGAGACCTCCGACCCCTCCCAGGCCACCCCGACGCCGGCGCCGACCACTCAGGCCCCCAATGCGAGTACCCCTCAGCAGCAACCCGCCGCGAAGCCGACCACCCCTGCCTGCCCCGCCTGA","MIAPVPQFSKPHARHSSKELGRRLARRVGLSLLAVTIFVVSAAGFAWHNIQSRITWFNIDSLLSEEDRPGTKPPDSYEGRAVNLLILGTDSRAGSNNVDGSQGDDEVSVARSDTALVMHISADRKRVDAVSIPRDTLVDIPECTTLDGGKTEASEDAPFNSAFAKGAGSSSDDKKAVASGAACTLKTVETLTNVRIDDFIVVDFTGLSKVVDSLGGVHVQVDEAIDDSEYTGFKLAEGCQKLDGENALQYARVRHGVSDGSDLSRITRQQNLMRAMASKALSSSLLTQSGFLTSTLETLTTSERIGQIGNLSGLAYSIQGVGIDKINFVTMPNEPAADPNQVVPSEGAKKVWKALEEDKPVPSDTSAPASSDSSATTNDSSSQSTDESAETSDPSQATPTPAPTTQAPNASTPQQQPAAKPTTPACPA$","Cell envelope-related function transcriptional attenuator, LytR/CpsA family","Periplasm, Extracellular","FrnA","transcriptional regulator","cell envelope-related function transcriptional attenuator, LytR/CpsA family","","","","","

InterPro
IPR004474
Domain

Cell envelope-related transcriptional attenuator
PF03816	$\"[111-282]T$	LytR_cpsA_psr
TIGR00350	$\"[110-282]T$	lytR_cpsA_psr: cell envelope-related functi

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[28-48]?$	transmembrane_regions

","BeTs to 5 clades of COG1316COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1316 is --------vdrlbc----------t-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 111 to 282 (E_value = 3.3e-61) place ANA_1577 in the LytR_cpsA_psr family which is described as Cell envelope-related transcriptional attenuator domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1578","1708761","1710248","1488","8.41","3.16","52086","GTGACTCCGACAGACGACTCACTCCCGCCCTCGATCACCCCGGGCTCCGGTGGAGGCAGACCTCAACGCAGGCAGCGCCCCATTGATGCTGTCAACCAGCGCAGCCGCGAGCGCGGGGAGGCGTCCGGCGGCGAGGCCGTCGCCCAGCCCACTGACGTTGCCGGCGGTTCCCCGCGCCGCCCGTCATCGCCGACCGCCCGCCGCCCTCAGCGGCACTCGGTCCTGGGCCGCAACGACAGTGACCGGCCGGCCTCGGCTCAGTCCGCCTCCGTGCGGGAGGGCCAGCAGCCGCCCTCAGTCCAGCCGCGTCGCTCCTCCGCGCCGTCTCAGCGAGGCAGCCACGCCCGGGCCGGGTCGAGCGCCATCCCCTTGGAGCCGGATGCCGGCGTCGGCAACGGCGCGTCCGAGCCGGAGCGCACTCAGGCGATGCCCGCGCGGCGCGGCACCTACCCCGTGGGCTCCTCGGCCCCGCGCGAGCCCGCTGCGGGTGGGCCGTCGCTCAGGCCCGAGCGTCCGCGGCGACCGCAGCGCTCCCGTCCGAGGTGGCGCCGGATCGTGGGCTGGACAGTCGTCGTCATCGTTGTCGCCCTGGCTCTCATCGCAGCGCGGATCGCCTGGCTGTGGAACGACGTCTCCTCCCAGCTCCACCGCGTCGATGCCCTGTCCGGGGCGGCAGACACTCCCGGCGAGACCTGGCTCATCGTGGGATCGGATGCACGTGGAGGCGCCGTTCAGGACGAGACCGAGGGGGCGCGCGCCGACTCGGTCATGCTGCTGCACAAGGCGGACAACGGGCAGACGAGCCTGACCTCCCTGCCGCGCGACACCTACGTAGACATCCCCGAGTACGGGGAGAACAAGATCAACGCCGCCTACTCCTTCGGCGGCCCCAAGCTGCTGGTCCAGACCGTGGAGAAGCTCTCCGGGCTGACCGTGGACCACTATGTGGAGGTCGGCATGACCGGGGTGTCCCAGATGGTCGACGCCGTCGGCGGGGTCAACGTCTGCCTGGACTACGACGTCGCCGATGAGGACTCCGGCCTGGTCTGGAACACCTCTCAGGGCACGTGTCAGACGGTGGACGGGACGAAGGCGCTGGCCTACTCCCGGATGCGCAAGTCGGACCCGAACGGTGACGTGGGTCGCGGTCAGCGCCAGCGCGCCGTCATCTCCGCAGTGGTCTCCAAGGCGGCAGCGCCGTCCACCGCCTTCTCCTTCTCCCGGCAGGACGCGCTGGTCGACGCCGGTACGAACGCGCTCACGGTGGATCGCAGCGCCGGCACCATGAGCATCGCCCAGATGGTGCTGGCCTTCCGCTCCGCCTCCGGCAGCGGTCTGACCGGCGCCCCGCCCATTGAGGACCCCGCCTACTCCCCCGAGGACGCCAACATCGGCGAGACGGTACTGCTGCAGGACACCACCGCCCCGAACTTCTTCTCGAAGCTGCGCGACGGGAAGCTGACGGCCGCGGACTTCAACCAGTCCTGA","VTPTDDSLPPSITPGSGGGRPQRRQRPIDAVNQRSRERGEASGGEAVAQPTDVAGGSPRRPSSPTARRPQRHSVLGRNDSDRPASAQSASVREGQQPPSVQPRRSSAPSQRGSHARAGSSAIPLEPDAGVGNGASEPERTQAMPARRGTYPVGSSAPREPAAGGPSLRPERPRRPQRSRPRWRRIVGWTVVVIVVALALIAARIAWLWNDVSSQLHRVDALSGAADTPGETWLIVGSDARGGAVQDETEGARADSVMLLHKADNGQTSLTSLPRDTYVDIPEYGENKINAAYSFGGPKLLVQTVEKLSGLTVDHYVEVGMTGVSQMVDAVGGVNVCLDYDVADEDSGLVWNTSQGTCQTVDGTKALAYSRMRKSDPNGDVGRGQRQRAVISAVVSKAAAPSTAFSFSRQDALVDAGTNALTVDRSAGTMSIAQMVLAFRSASGSGLTGAPPIEDPAYSPEDANIGETVLLQDTTAPNFFSKLRDGKLTAADFNQS$","Cell envelope-related function transcriptional attenuator, LytR/CpsA family","Membrane, Extracellular","Transcriptional regulator","hypothetical protein","cell envelope-related function transcriptional attenuator, LytR/CpsA family","","","","","

InterPro
IPR004474
Domain

Cell envelope-related transcriptional attenuator
PF03816	$\"[252-399]T$	LytR_cpsA_psr
TIGR00350	$\"[251-399]T$	lytR_cpsA_psr: cell envelope-related functi

noIPR
unintegrated

unintegrated
tmhmm	$\"[185-207]?$	transmembrane_regions

InterPro
IPR001509
Family

NAD-dependent epimerase/dehydratase
PF01370	$\"[3-252]T$	Epimerase

InterPro
IPR005886
Family

UDP-glucose 4-epimerase
PTHR10366:SF39	$\"[5-314]T$	UDP-GLUCOSE 4-EPIMERASE
TIGR01179	$\"[2-327]T$	galE: UDP-glucose 4-epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[3-280]T$	no description
PTHR10366	$\"[5-314]T$	NAD DEPENDENT EPIMERASE/DEHYDRATASE

","BeTs to 14 clades of COG1087COG name: UDP-glucose 4-epimeraseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1087 is --m---yq-d-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 2","***** IPB001509 (NAD-dependent epimerase/dehydratase) with a combined E-value of 1.9e-36. IPB001509A 4-15 IPB001509B 70-107 IPB001509C 139-148 IPB001509D 250-271 IPB001509E 282-322***** IPB002225 (3-beta hydroxysteroid dehydrogenase/isomerase) with a combined E-value of 9.6e-18. IPB002225A 0-38 IPB002225C 118-172 IPB002225D 220-259***** IPB008089 (Nucleotide sugar epimerase signature) with a combined E-value of 3.5e-13. IPB008089B 219-234 IPB008089C 246-261 IPB008089D 285-302***** IPB013549 (Domain of unknown function DUF1731) with a combined E-value of 2.4e-06. IPB013549A 3-27","","","-51% similar to PDB:1GY8 TRYPANOSOMA BRUCEI UDP-GALACTOSE 4' EPIMERASE (E_value = 2.1E_53);-51% similar to PDB:2CNB TRYPANOSOMA BRUCEI UDP-GALACTOSE-4-EPIMERASE IN TERNARY COMPLEX WITH NAD AND THE SUBSTRATE ANALOGUE UDP-4-DEOXY-4-FLUORO-ALPHA-D-GALACTOSE (E_value = 2.1E_53);-54% similar to PDB:2C20 CRYSTAL STRUCTURE OF UDP-GLUCOSE 4-EPIMERASE (E_value = 6.8E_52);-52% similar to PDB:1LRJ Crystal Structure of E. coli UDP-Galactose 4-Epimerase Complexed with UDP-N-Acetylglucosamine (E_value = 4.2E_46);-52% similar to PDB:1LRK Crystal Structure of Escherichia coli UDP-Galactose 4-Epimerase Mutant Y299C Complexed with UDP-N-acetylglucosamine (E_value = 4.2E_46);","Residues 2 to 317 (E_value = 2e-05) place ANA_1579 in the RmlD_sub_bind family which is described as RmlD substrate binding domain.Residues 3 to 252 (E_value = 3.7e-63) place ANA_1579 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 3 to 271 (E_value = 0.0019) place ANA_1579 in the Polysacc_synt_2 family which is described as Polysaccharide biosynthesis protein.Residues 3 to 24 (E_value = 1.7e-05) place ANA_1579 in the NmrA family which is described as NmrA-like family.Residues 4 to 281 (E_value = 9.4e-08) place ANA_1579 in the 3Beta_HSD family which is described as 3-beta hydroxysteroid dehydrogenase/isomerase family.Residues 5 to 221 (E_value = 6.7e-05) place ANA_1579 in the NAD_binding_4 family which is described as Male sterility protein.","","4-epimerase (galE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1580","1711440","1712444","1005","9.49","12.06","38957","ATGAATCCTCCAGGTCAACGTTACAACAAACCAGCACTCGACGAGAACGAGCTCATTGAGCGCTACATTGAACGCGGACTCATCATCAAAGACCGGAATCGCGCCGCCAGATACCTCCGACACATCGGATACTATCGGCTCTCTCCCTACACAATCCCCTTCCAAGCCGACCGAACCACCCACTCCTTCAAGTCGGGCACCACCTTCGACGACATCCTCTATATCTACGTGTTCGATCGCCAGCTGCGCCTCATGACAATGGACGCCCTTGAACGCGTCGAGGTCGCGGTGCGCGCCGCAGTGTCCAACACAATGTCAATACACGGCGAAGGCGGAGCCTTCTGGTACCAAAACGCCTCCAACTATAAAAGCCGAAAAGGATACTCCACAACGATTGAACGCATCGAGCACCTCACAGAACGCGAACGACAGCGCACTCCTTCAGGTCGCGGCGAACAGGCGGATCACCTCCACTACCCTGATGCCCTCTCGCACTACCTCGCCACCTACTCGTCTCCAGAGACACCACCGTCTTGGCTGGTCATCGAGCTGCTCACCGCCGGCGAGCTTCATCACCTTTACACCAACCTGACCCTCAGGTACCGCAAGACAATTGCAAGAGAGCTCAACCTCCCTGATCAGGTACTGCAGTCCTGGCTCAAGACCTACGTGAGGGTGCGCAACATCTGCGCCCACCACGGACGTCTCTGGAACAGGTTCCTCGGCGTATATCCAGCGATCCCCAGAAGCCCGACCGTCCGCTGGCTCACCGATCGCAGCACCTTTGATACCGGCAATCCAAGAGCTCTAGAACGAAAGAGACTCTACCCCGTTCTCGTCTCTCTTCAGTCGATCTTGTTCACCATCAGCCCGCACTCGACGTGGGCTCTGAGGCTGCACTCTCTTTTAGGCGAATATCAACGCATCCCACTGAATGCCCTGGGAATGAAAGCCGACTGGGACGCCGATGAGTTCTGGCAAGAGGCCTTCAAGGCCGGCTCCTGA","MNPPGQRYNKPALDENELIERYIERGLIIKDRNRAARYLRHIGYYRLSPYTIPFQADRTTHSFKSGTTFDDILYIYVFDRQLRLMTMDALERVEVAVRAAVSNTMSIHGEGGAFWYQNASNYKSRKGYSTTIERIEHLTERERQRTPSGRGEQADHLHYPDALSHYLATYSSPETPPSWLVIELLTAGELHHLYTNLTLRYRKTIARELNLPDQVLQSWLKTYVRVRNICAHHGRLWNRFLGVYPAIPRSPTVRWLTDRSTFDTGNPRALERKRLYPVLVSLQSILFTISPHSTWALRLHSLLGEYQRIPLNALGMKADWDADEFWQEAFKAGS$","Abortive infection bacteriophage resistance protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","Abi family protein","","Garvey P., Fitzgerald G.F., Hill C. Cloning and DNA sequence analysis of two abortive infection phage resistance determinants from the lactococcal plasmid pNP40. Appl. Environ. Microbiol. 1995. 61(12):4321-4328. PMID: 8534099Anba J., Bidnenko E., Hillier A., Ehrlich D., Chopin M.C. Characterization of the lactococcal abiD1 gene coding for phage abortive infection. J. Bacteriol. 1995. 177(13):3818-3823. PMID: 7601848Bidnenko E., Ehrlich D., Chopin M.C. Phage operon involved in sensitivity to the Lactococcus lactis abortive infection mechanism AbiD1. J. Bacteriol. 1995. 177(13):3824-3829. PMID: 7601849","","","

InterPro
IPR011664
Family

Abortive infection bacteriophage resistance related
PF07751	$\"[10-236]T$	Abi_2

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 10 to 236 (E_value = 9.3e-43) place ANA_1580 in the Abi_2 family which is described as Abi-like protein.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1581","1713039","1712488","552","5.02","-6.32","18832","ATGAACGAGGTCAGCGCAACGACGGCGGACATGCAGGACGCGGGACGACCGGTGGTCGGCATCGTCATGGGGTCGGACTCGGACTGGCCGGTCATGGGGGCCGCAGCCGAGGTCCTCGACGAGTTCAAGGTGGCCTATGAGGCCGACGTCGTCTCCGCCCACCGCATGCCTACCGAGATGATCGACTACGGGCGCACCGCCGCTGAGCGGGGGCTGCGCGTCATCATCGCCGGCGCCGGGGGAGCGGCCCACCTTCCCGGAATGCTGGCGGCCGTCACCGAGCTGCCGGTCATCGGGGTGCCGGTGCCGCTGAAATACCTCGACGGCATGGACTCCCTCCTGTCCATCGTGCAGATGCCCGCCGGGGTCCCGGTGGCCACCGTCTCCATCGGCGGGGCCCGCAACGCCGGGCTACTGGCGGTGCGTATCCTCGCCTCCGGTCAGGGGCCGGAGGCCGCTCGCCTGGGGGCTGCGATGCGGGCCTTCCAGATGGACCTCAGCGAGGTCGCCCACGCCAAGGGTGCCGCCCTGCGCGAGAGGCTGCAGGATTGA","MNEVSATTADMQDAGRPVVGIVMGSDSDWPVMGAAAEVLDEFKVAYEADVVSAHRMPTEMIDYGRTAAERGLRVIIAGAGGAAHLPGMLAAVTELPVIGVPVPLKYLDGMDSLLSIVQMPAGVPVATVSIGGARNAGLLAVRILASGQGPEAARLGAAMRAFQMDLSEVAHAKGAALRERLQD$","Phosphoribosylaminoimidazole carboxylase, catalytic subunit","Cytoplasm","phosphoribosylaminoimidazole carboxylase,catalytic subunit","putative phosphoribosylaminoimidazole carboxylase catalytic subunit ","phosphoribosylaminoimidazole carboxylase, catalytic subunit","","Meyer E., Kappock T.J., Osuji C., Stubbe J. Evidence for the direct transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase. Biochemistry 1999. 38(10):3012-3018. PMID: 10074353Mathews I.I., Kappock T.J., Stubbe J., Ealick S.E. Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway. Structure 1999. 7(11):1395-1406. PMID: 10574791","","","

InterPro
IPR000031
Domain

1-(5-Phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR) carboxylase
PD002193	$\"[24-162]T$	Q82DG0_STRAW_Q82DG0;
G3DSA:3.40.50.7700	$\"[10-176]T$	no description
PF00731	$\"[17-173]T$	AIRC
TIGR01162	$\"[19-178]T$	purE: phosphoribosylaminoimidazole carboxyl

noIPR
unintegrated

unintegrated
PTHR23046	$\"[8-183]T$	PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT

","BeTs to 20 clades of COG0041COG name: Phosphoribosylcarboxyaminoimidazole (NCAIR) mutaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0041 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000031 (1-(5-Phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR) carboxylase) with a combined E-value of 3.8e-30. IPB000031 74-116","","","-77% similar to PDB:1O4V Crystal structure of phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77 A resolution (E_value = 3.6E_44);-70% similar to PDB:1XMP Crystal Structure of PurE (BA0288) from Bacillus anthracis at 1.8 Resolution (E_value = 1.4E_43);-72% similar to PDB:1U11 PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase) from the acidophile Acetobacter aceti (E_value = 1.5E_42);-72% similar to PDB:2FW1 Structure of PurE (N5-carboxyaminoimidazole ribonucleotide mutase) from the acidophilic bacterium Acetobacter aceti, at pH 8.5 (E_value = 1.5E_42);-72% similar to PDB:2FWJ Structure of PurE (N5-carboxyaminoimidazole ribonucleotide mutase) from the acidophilic bacterium Acetobacter aceti, complexed with AIR (5-aminoimidazole ribonucleotide) (E_value = 1.5E_42);","Residues 17 to 173 (E_value = 9.6e-78) place ANA_1581 in the AIRC family which is described as AIR carboxylase.","","carboxylase, catalytic subunit (purE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1582","1714409","1713114","1296","5.06","-17.36","44550","GTGAGCGCACCCATCGTCGCCGTGATCGGAGGCGGGCAGCTGGCCCGCATGATGCAGGAGGAGGCCAGTGCTCTGGGGATTCACCTCAGAGCACTGGTGGAGGCCGCGGACGGGTCCACCGGACAGGTGACCCCGGACGCCCCCGTCGGGGCCGCAGACGACGAGGCTGCCGTGCGCGCCGTCGTCACCGGGGACGGGACTGACGGGCCCGCAGGGGGGCCTGCCTCGGTTCTCACCTTCGAGCACGAGCACCAGGACTCGGCCCTTCTGGAGAGGCTCCAGGCCGAGGGAGTCAGTGTCCAGCCCACCCCGCAGGCCCTGACCCTGGCGCGCGACAAGCTCGCCATGCGGAGGATGATGAGCGGGGCCGGGCTCCCGCAGCCCGCCTGGGCGGAGATCGGCGGGCCGCAGCAGGAGAGCACCGAGCAGATGGTCGATGCCATTGAGGCCTTCGCCGCCGAGCACGGCTGGCCCGTGGTCCTCAAGACGCCGCGTGGAGGCTATGACGGCCACGGGGTGCTGCTGGTGCGCAGCGCCGAGTCCCTGCGCCAGGGCGAGGCGGCCGAGTGGGTCGCCTCGGTGGCGCGCGTCCGAGCGGGCCAGGGCGACGGCCGCGGGGCCGGAGGGGGAGGCAGCCTCGGAGGAGCAGCGGTGACCAGTCTCCTGGTGGAGCAGGCGATCCCCTTCACTCGCGAGCTCGCCGTCCTGCTGGCCCGCACCCCCAGCGGGCAGGTCGCGGTGTGGCCGGTTGCCCAGACGGTCCAGGAGGACGGCATGTGCGCCGAGGTCCTGGCGCCGGCGCCCGGTCTCGACTCGGCCGCCGTCGAGGAGGCCGAGCTCATCGGCCGCACGGTCGCCGAGCGCGCCGGGGTGACCGGGGTGCTCGCCGTCGAGCTCTTCGCCGTGGAGGCCTTCGGGGAGCCCACGCGTCTGTACGTCAACGAGCTGGCGATGCGTCCCCACAACTCCGGTCACTGGACCCAGGACGGGGCCGTCACCAGCCAGTTCGCCCAGCACCTGCGGGCGGTTCTCGACCTGCCGCTGGGGGCCACGGAGGCCACAGCGCCCACCACCGTCATGGTCAACCTCATTGGCGGCCGTCGCGAGCCGGGAACCGATGCCCTGGCCCGGGCCATGGCCGCGCACCCCGAGGCCCGCATCCACCTCTACGGCAAGCAATGGCGAACGGGACGTAAGCTCGGGCACGTCACCATGACGGTCAGCCCGGACCAGGAGGTCGCCGACGTCGTCGAGCAGGCGCGCGGGGCCGTCGCCATCCTGCGCGGGGACGCCTGA","VSAPIVAVIGGGQLARMMQEEASALGIHLRALVEAADGSTGQVTPDAPVGAADDEAAVRAVVTGDGTDGPAGGPASVLTFEHEHQDSALLERLQAEGVSVQPTPQALTLARDKLAMRRMMSGAGLPQPAWAEIGGPQQESTEQMVDAIEAFAAEHGWPVVLKTPRGGYDGHGVLLVRSAESLRQGEAAEWVASVARVRAGQGDGRGAGGGGSLGGAAVTSLLVEQAIPFTRELAVLLARTPSGQVAVWPVAQTVQEDGMCAEVLAPAPGLDSAAVEEAELIGRTVAERAGVTGVLAVELFAVEAFGEPTRLYVNELAMRPHNSGHWTQDGAVTSQFAQHLRAVLDLPLGATEATAPTTVMVNLIGGRREPGTDALARAMAAHPEARIHLYGKQWRTGRKLGHVTMTVSPDQEVADVVEQARGAVAILRGDA$","Phosphoribosylaminoimidazole carboxylase, ATPase subunit","Cytoplasm","Phosphoribosylaminoimidazole carboxylase ATPasesubunit(AIR carboxylase) (AIRC)","phosphoribosylaminoimidazole carboxylase; ATPase subunit ","Phosphoribosylaminoimidazole carboxylase","","Galperin M.Y., Koonin E.V. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 1997. 6(12):2639-2643. PMID: 9416615Fan C., Moews P.C., Walsh C.T., Knox J.R. Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. Science 1994. 266(5184):439-443. PMID: 7939684Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Fan C., Moews P.C., Shi Y., Walsh C.T., Knox J.R. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(4):1172-1176. PMID: 7862655","","","

InterPro
IPR003135
Domain

ATP-grasp fold, ATP-dependent carboxylate-amine ligase-type
PF02222	$\"[112-331]T$	ATP-grasp

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[117-344]T$	ATP_GRASP

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[204-420]T$	no description

InterPro
IPR013817
Domain

Pre-ATP-grasp fold
G3DSA:3.40.50.20	$\"[6-121]T$	no description

noIPR
unintegrated

unintegrated
PTHR23047	$\"[75-188]T$ $\"[213-425]T$	PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE ATPASE-SUBUNIT
PTHR23047:SF1	$\"[75-188]T$ $\"[213-425]T$	PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE ATPASE-SUBUNIT

","BeTs to 15 clades of COG0026COG name: Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase)Functional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0026 is -o-p--yqvdrlbcefghsn-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-41% similar to PDB:1B6R N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE FROM E. COLI (E_value = 2.3E_26);-41% similar to PDB:1B6S STRUCTURE OF N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE (E_value = 3.1E_26);-40% similar to PDB:1EYZ STRUCTURE OF ESCHERICHIA COLI PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE COMPLEXED WITH MG AND AMPPNP (E_value = 4.6E_14);-40% similar to PDB:1EZ1 STRUCTURE OF ESCHERICHIA COLI PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE COMPLEXED WITH MG, AMPPNP, AND GAR (E_value = 4.6E_14);-40% similar to PDB:1KJ8 Crystal Structure of PurT-Encoded Glycinamide Ribonucleotide Transformylase in Complex with Mg-ATP and GAR (E_value = 4.6E_14);","Residues 112 to 331 (E_value = 1.1e-52) place ANA_1582 in the ATP-grasp family which is described as ATP-grasp domain.","","carboxylase ATPase subunit(AIR carboxylase) (AIRC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1585","1714475","1715746","1272","9.22","7.97","45351","GTGACCCCACCCGTCTCAGAGTCCTCCGCGTCCTCCACCTCCCGCCAGGCCCTGCCCTCGTTTTCGACGCACGGCGCTGCCTCGGGGCCGCGCCGTTGGCTCCAGGTCCTGACGGTCTGGGCGGTGGCGAGCACCCTGACCTTCATCATTCTGCGGCTGGGCGCCCAGGACACGCCCGTCACCCCGTGGGCTGGGGCCGCGCCGTCCTGGGAGGAGCACCTGCGCTTCTGGGACGCCGGCTGGTACAACCGGATCGTTGAGGAGGGCTACCCGGAGCGGCTGCCCGTCGGCGACGACGGACGAGTGGCCCAGAACACGTGGGCCTTCATGCCACTGCTGAGCGCTGTGGCCTCCCTGCTGGGCTGGACCGGCTGGTCCTTCTACGTGCGCGCCGCCCTCGTGTCGGTCCTGGCCTCGGCGTCGGCGGCGATCGTCATGGACCGCTGGCTCTCACCACTGACGGGCGGCCGGGCCTCCCTGTGGGCGGTGGCTCTGGTCTGGTCCTCGCCGTGCGCCGCGGTTCTCCAGGTGCCTTACGCCGAGCCCCTGGGGCTGGTCCTGGTAGGGCTGACGCTGTGGCTGGTGAGCCGTGGGCGGGCACTGGCCGCTATCCCCGTGGCGCTGGCGGCCTGCTTCGCCCGCCCCATCGGTGTCCCGCTGGGGGCGGCGCTGGGGCTGTGGTGGGTCTGGGAGGTGGCCTGCGCCCGGGGCTGGGTTCCACCCACCTGGTTCTCCCGTCTTCTGCCGGGTCACGCCCCTCAGGCGCCGGGTGCGCGTCTGCGACTGCTGGCGCTGGCCCTGCTCACCTGCTCGGCGGCCCTGAGCTGGCCGGTCATCGCCTGGTTGGTCACAGGCCGACAGGACGCCTACACCGCCACCGAGACCTCCTGGCGTGGGGCGGACCTGGCGCCCGTCGTGCAGTGGGCGGTCCGCCTGGGCGACTGGGTGGGTCCGCACCTGGGTCCGGCGCTGCTGGTCGTCGTGCTTGTCGCCGTGGGCCTGCTCCTGAGCGCCCCGAGCCTGCGGGCCCTGGGGCCCGCGGCCTGGTTCTGGTGCCTGGGTTACCTGCTCTACCTCCTGGTCTTCTTCGATCCGACGACGTCGGTGCTGCGTCTCCTGCTGCCCCTGGCCCCGGTGGGCTGGGCGCTGGCCGCGGCGGCCGGCACCATCCGCCGACGGTTGGCCCTGCTGGCGGCATGCGTCGCCGGCCAGCTGCTGTGGGTCTCGTGGGTGTGGGACCTGGGCAGCGTCAGTGTTCACTGGGTGCCGTGA","VTPPVSESSASSTSRQALPSFSTHGAASGPRRWLQVLTVWAVASTLTFIILRLGAQDTPVTPWAGAAPSWEEHLRFWDAGWYNRIVEEGYPERLPVGDDGRVAQNTWAFMPLLSAVASLLGWTGWSFYVRAALVSVLASASAAIVMDRWLSPLTGGRASLWAVALVWSSPCAAVLQVPYAEPLGLVLVGLTLWLVSRGRALAAIPVALAACFARPIGVPLGAALGLWWVWEVACARGWVPPTWFSRLLPGHAPQAPGARLRLLALALLTCSAALSWPVIAWLVTGRQDAYTATETSWRGADLAPVVQWAVRLGDWVGPHLGPALLVVVLVAVGLLLSAPSLRALGPAAWFWCLGYLLYLLVFFDPTTSVLRLLLPLAPVGWALAAAAGTIRRRLALLAACVAGQLLWVSWVWDLGSVSVHWVP$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","integral membrane protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-55]?$	signal-peptide
tmhmm	$\"[33-53]?$ $\"[106-126]?$ $\"[131-151]?$ $\"[175-195]?$ $\"[200-218]?$ $\"[224-242]?$ $\"[263-283]?$ $\"[318-338]?$ $\"[343-363]?$ $\"[369-389]?$ $\"[394-414]?$	transmembrane_regions

InterPro
IPR007267
Family

GtrA-like protein
PF04138	$\"[14-139]T$	GtrA

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[15-33]?$ $\"[47-67]?$ $\"[82-102]?$ $\"[116-138]?$	transmembrane_regions

","BeTs to 4 clades of COG2246COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2246 is ao-pkz----r-bce------j----Number of proteins in this genome belonging to this COG is 3","***** IPB007267 (GtrA-like protein) with a combined E-value of 1.9e-09. IPB007267B 46-77 IPB007267C 127-140","","","No significant hits to the PDB database (E-value < E-10).","Residues 14 to 139 (E_value = 2.4e-17) place ANA_1586 in the GtrA family which is described as GtrA-like protein.","","protein family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1587","1716467","1717198","732","9.52","4.65","26567","GTGACTGCCCTGACTACCTTGGCACCGGCGCTGAACCTGCCCACCGCCCTCCCCTTCGTCCACGCACCGATGCTCGGCCCCGAGTGGCTCGACGCCACCTTCATCATCAAAGCCTTCGTCGGCTGGATCGGCCCCTGGGCCATCCTCGGCGTCATGCTCGTCATCTTCGCCGAGACCGGCCTGCTCATCGGCTTCTTCCTGCCCGGTGACTCACTGCTGTTCACCCTGGGGATGTTCGTGGCCATCGGCGAGACCAACCCGGCCGAAGGAGTTCCCGTCCCCATCTGGGTGGCGGCCCCCCTCGTGTGGCTCGCGGCCGTCGCCGGCAACCAGACCGGCTACCTCATCGGGCGCAAGGCGGGGCCGGCGATCTTCAACAAGCCGGATTCCCGTCTGTTCAAGCGGGAGTACGTGGAGCGCACCTCTGAGTTCTTCGAGCGCCACGGCGGCAAGGCCGTCACCCTGGCCCAGTTCGTGCCGATCGTGCGCACCTTCACGCCCGTCATCGCGGGCGTTGGCAAGATGAACTACCGCCACTTCATCACCTTCAACATCCTGGGCGCCACCTTCTGGGCCTTCGGCATCACCTGGCTGGGCTACTTCCTGGGAACGATCACGTGGATCCAGGACAACATCGACGCCATGATCCTGGTGATCGTCTTCATCTCAGTGGCGCCGATGCTCATCTCCGGCATCTCGCAGCTCATCAAGTCCCGCCGCCAGAAGTCCTGA","VTALTTLAPALNLPTALPFVHAPMLGPEWLDATFIIKAFVGWIGPWAILGVMLVIFAETGLLIGFFLPGDSLLFTLGMFVAIGETNPAEGVPVPIWVAAPLVWLAAVAGNQTGYLIGRKAGPAIFNKPDSRLFKREYVERTSEFFERHGGKAVTLAQFVPIVRTFTPVIAGVGKMNYRHFITFNILGATFWAFGITWLGYFLGTITWIQDNIDAMILVIVFISVAPMLISGISQLIKSRRQKS$","Uncharacterized membrane-associated protein","Membrane, Cytoplasm","DedA family protein","hypothetical protein","Uncharacterized membrane-associated protein-like","","","","","

InterPro
IPR015414
Domain

SNARE associated Golgi protein
PF09335	$\"[91-201]T$	SNARE_assoc

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-23]?$ $\"[29-49]?$ $\"[59-81]?$ $\"[87-107]?$ $\"[180-200]?$ $\"[214-236]?$	transmembrane_regions

","BeTs to 12 clades of COG0586COG name: Uncharacterized membrane-associated proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG0586 is ---p-----drlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 91 to 201 (E_value = 1.1e-06) place ANA_1587 in the SNARE_assoc family which is described as SNARE associated Golgi protein.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1588","1718327","1717251","1077","5.88","-5.34","37980","ATGCGGCGTTACGCCATGACGATGACGATGTCGGCGGTGTCCGTGGCCGTCGTCCTGCTGGGACTGCCGCTGGGTGGCGCCTGGATCGTCAGCGCGTTGCGCTCCGCCGGAAGCGGTGACCGGGTCATCATCATCGGCACGGTCATCCTCACGGTTCTGGTGCTCACCGGTACCGCGCTCACGGCGGCCTCCGTTGTGGCCTCCCGGGTCTCCAGGCGCATCTCGGCCCCGCTCATCTACCTGGCTGCTGAGGCCGAGCAGCTCGGCAGCGGTCAGGTCCGCCCGAGGCTGCGCTCCTCGGGGATCGAGGAGATCGACCTGGTCCAGGCCGAGCTTGTGCGCTCGGCCGAGCGCGTGGCCGGGCGCATCGCCGCTGAGCGACAGTTCGCCTCCGATGCCTCCCACCAGCTGCGCACGCCGCTGACCAGCTTGTCACTGCGCCTGGAGGAGATCGAGCTGCTCGCGGGTGAGGAGGAGGTGCGGGCGGAGGCCCACGCCTGCCTGGAGCAGGTTGAGAGGCTCACCGGCGTTGTTGAGGACCTGCTCAAGGTCTCGCGCCGTTCCGGGGGCGGGACCACGGAGGCGCTTCACCTCAAGGACATCTTCGCTCAGCAGCGCGAGGAGTGGGAGCCGGCCTTCGAGCAGGCCGGGCGCACCATCACCTTCTCCGATGAGATCAGCCACCCGGTGCTGGCCACGCCCGGGTCCCTGGCCCAGGTGCTGGCCACCGTCATTGAGAACTCCCTGCGCTACGGGGCCGGGACGACCTCGGTGAGTGTGCGCGGGGCCAACGGCGGTCATGCGGTCTTCATCGACATCGCCGATGAAGGAGAGGGCGTGGCCGAGGACATCGCACCGCACGTCTTCGAGCGGCATGTCTCCGGCTACGGCTCCACCGGTGTCGGGCTGGCCCTGGCCAAGGACCTCATCGAGGCCGACGGCGGCCGCATCGAGTTGTCGCAGCGCAGCCCGGCCGTCTTCTCCATCCTGCTCAACGCCGTCCCCAAGTCCCTGGACCCCAACAACGTCCTCCCGCAGGGCGCGCTGGTCTCGGTGGGGCGTCGTCGTCGTTTCTGA","MRRYAMTMTMSAVSVAVVLLGLPLGGAWIVSALRSAGSGDRVIIIGTVILTVLVLTGTALTAASVVASRVSRRISAPLIYLAAEAEQLGSGQVRPRLRSSGIEEIDLVQAELVRSAERVAGRIAAERQFASDASHQLRTPLTSLSLRLEEIELLAGEEEVRAEAHACLEQVERLTGVVEDLLKVSRRSGGGTTEALHLKDIFAQQREEWEPAFEQAGRTITFSDEISHPVLATPGSLAQVLATVIENSLRYGAGTTSVSVRGANGGHAVFIDIADEGEGVAEDIAPHVFERHVSGYGSTGVGLALAKDLIEADGGRIELSQRSPAVFSILLNAVPKSLDPNNVLPQGALVSVGRRRRF$","Two-component system sensor kinase","Membrane, Cytoplasm","Sensor protein afsQ2","two-component system sensor kinase","ATP-binding region, ATPase domain protein domain protein","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[193-331]T$	no description
PF02518	$\"[232-334]T$	HATPase_c
SM00387	$\"[232-335]T$	HATPase_c

InterPro
IPR003660
Domain

Histidine kinase, HAMP region
PF00672	$\"[52-121]T$	HAMP
SM00304	$\"[72-124]T$	HAMP
PS50885	$\"[72-124]T$	HAMP

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[125-190]T$	HisKA
SM00388	$\"[125-190]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[269-283]T$ $\"[297-315]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[132-335]T$	HIS_KIN

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.240	$\"[115-186]T$	no description
PTHR23283	$\"[42-333]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23	$\"[42-333]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[12-32]?$ $\"[42-64]?$	transmembrane_regions

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[29-127]T$	Q82HM7_STRAW_Q82HM7;
PF00072	$\"[27-137]T$	Response_reg
SM00448	$\"[27-136]T$	REC
PS50110	$\"[28-140]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[157-233]T$	Q82HM7_STRAW_Q82HM7;
PF00486	$\"[170-245]T$	Trans_reg_C

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[144-245]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[28-144]T$	no description
PTHR23283	$\"[28-142]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[28-142]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 2.1e-37. IPB001867A 70-83 IPB001867B 98-142***** IPB001789 (Response regulator receiver) with a combined E-value of 1.2e-11. IPB001789A 70-83 IPB001789B 118-128***** IPB000673 (CheB methylesterase) with a combined E-value of 4.1e-07. IPB000673B 42-95 IPB000673C 96-126","","","-49% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 6.4E_22);-45% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 1.2E_20);-45% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 1.2E_20);-53% similar to PDB:1KGS Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima (E_value = 6.2E_17);-44% similar to PDB:1P2F Crystal Structure Analysis of Response Regulator DrrB, a Thermotoga maritima OmpR/PhoB Homolog (E_value = 5.8E_15);","Residues 27 to 137 (E_value = 1.3e-38) place ANA_1590 in the Response_reg family which is described as Response regulator receiver domain.Residues 170 to 245 (E_value = 3e-16) place ANA_1590 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","transduction protein regX3","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1591","1720338","1719304","1035","4.96","-14.04","37437","GTGGACTCTGCTGAGAGAGCCACCCTGGCGGGACACGAGAGTCTGCTGCTGGGGGAGTCCCCCACCCTTACCCTGACCGAGCTGGCTCAGCGAGCCGGAACCAGTGTGGAGGTGGCGCAGAAGTTCTGGCGCGCCATGGGCTTCGCCGATGTCCAACCCGATGAGGTCCGCTTCACTGCCCAGGATGTCGCCGCACTTCAAGACACCGTGGCGCTGCTGGATGAGACCAGCGATTCCTCCCTGGCCTCGGCCAGCGTGCTCGAGCTCCTCAGGGCCCAGTCCTACACCATGGACCGCCTGGTCCTGTGGGAGTTGGAGACCTTCGTCACGGACCTCAGTGAGCGTCTCGGGCTGGATGACACCGCCGCACGGCTGGTGGCCCTCGATCGCATCGACGGCCTCGTGGAGCTCCTGTCGCGCCAGCTGACTTACGTGTGGCGCCGCCACATGGCCTCCATCCTGGGGCGCACCGATGCTGAGGTGTCGACCCGGGGCAGGGAGGACACCGGCCCCGACCTCTACCCGCTCATCCGCTCCCTGGGCTTCGTCGACATCGTCTCCTTCACTCAGCGGGCCCAGGGCATGAGCAAGGCCGCACTGACCCACATGCTCGAGGACTTCGAGAACACCGCCCGGGACGTCATCACCTCCCGAGGGGCGCGGGTGGTCAAGACGATCGGGGACGCTGTCATGTACATCTCCGACGACCTTCTCATCGCCGCCGACGTCGTCACCGCCCTGGTCGATGAGCTCCAGAAGGGGCCGGACGCCATCCGGGTGAGGGCCAGCCTCGTCGAGGGGCGGGTCATCTCCCGCTCCGGGGACGTCTTCGGCCCCACCGTCAACCTGGCCTCCCGGCTCGTGGACGCGGCTGAACCCGGCGGTATCCGCCTGGACGAGTCCACTGCTATGGCCATCCTCCGCTCGCCGGAGGCGGCACGGTACCGGGTGGGGCAGTGCCATGAGGTGGTGGCCAAGGGGCTGGGGCAGATCGTGCCCTGGTCGCTGGAGAGGACCTCGCCGACCCGCCCCTGA","VDSAERATLAGHESLLLGESPTLTLTELAQRAGTSVEVAQKFWRAMGFADVQPDEVRFTAQDVAALQDTVALLDETSDSSLASASVLELLRAQSYTMDRLVLWELETFVTDLSERLGLDDTAARLVALDRIDGLVELLSRQLTYVWRRHMASILGRTDAEVSTRGREDTGPDLYPLIRSLGFVDIVSFTQRAQGMSKAALTHMLEDFENTARDVITSRGARVVKTIGDAVMYISDDLLIAADVVTALVDELQKGPDAIRVRASLVEGRVISRSGDVFGPTVNLASRLVDAAEPGGIRLDESTAMAILRSPEAARYRVGQCHEVVAKGLGQIVPWSLERTSPTRP$","Adenylate cyclase, family 3","Cytoplasm","Adenylate cyclase (ATP pyrophosphate-lyase)(Adenylylcyclase)","hypothetical protein","adenylyl cyclase class-3/4/guanylyl cyclase","","Yuen P.S., Garbers D.L. Guanylyl cyclase-linked receptors. Annu. Rev. Neurosci. 1992. 15:193-225. PMID: 1349465Garbers D.L. Guanylyl cyclase receptors and their endocrine, paracrine, and autocrine ligands. Cell 1992. 71(1):1-4. PMID: 1356629Koesling D., Bohme E., Schultz G. Guanylyl cyclases, a growing family of signal-transducing enzymes. FASEB J. 1991. 5(13):2785-2791. PMID: 1680765Garbers D.L. The guanylyl cyclase receptor family. New Biol. 1990. 2(6):499-504. PMID: 1982420","","","

InterPro
IPR001054
Domain

Adenylyl cyclase class-3/4/guanylyl cyclase
PF00211	$\"[172-338]T$	Guanylate_cyc
SM00044	$\"[129-317]T$	CYCc
PS50125	$\"[179-288]T$	GUANYLATE_CYCLASE_2

InterPro
IPR013173
Domain

DNA primase DnaG, DnaB-binding
SM00766	$\"[42-154]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.1230	$\"[179-334]T$	no description
PTHR11920	$\"[182-302]T$	ADENYLATE AND GUANYLATE CYCLASES
PTHR11920:SF33	$\"[182-302]T$	ADENYLATE CYCLASE

","BeTs to 5 clades of COG2114COG name: Adenylate cyclase, family 3 (some proteins contain HAMP domain)Functional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG2114 is ------y---r--c-f-----j--t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-45% similar to PDB:1Y10 Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state (E_value = 1.6E_19);-45% similar to PDB:1Y11 Mycobacterial adenylyl cyclase Rv1264, holoenzyme, active state (E_value = 1.6E_19);","Residues 172 to 338 (E_value = 2.2e-08) place ANA_1591 in the Guanylate_cyc family which is described as Adenylate and Guanylate cyclase catalytic domain.","","cyclase (ATP pyrophosphate-lyase) (Adenylylcyclase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1592","1721458","1720541","918","4.87","-11.28","31163","ATGACCTCAGGCGGCAGCCCCTTTTCGCGTCTCGACACCGTTCCCGTCACCGGATCCACCCAGGACGACCTGCGCACGGCCCTCACAGGGCCCGAGCAAGAGTCCTGGCCGCACCTGTCGGCGCTGCGAGCACTTGCTCAGACCGCGGGCAGGGGGCGCTCCGGGCGCGCCTGGGTCACCCCCGACGACGGAGGTGCCCTCCTGGTCTCCGTGGTGCTGCGGCCCCTCGTCCCCGTCGACCGCCTGGCCTGGCTGCCGCTGCTGGGCGGCCTGGCCGTCCGCGACGCGCTGGCCCCCCTCGTCGAGGGCCTGCCCTGGCGTGTGGGGACCAAGTGGCCCAACGACGTCGTCGCCCTGCCTGATGACCCGGCGGCCGTGCCCGCAGTGCCCGGCTGGGCCGGCACGCGCAAGATCGCCGGCGTCCTCAGCGAGCTCGTCACGCCAGAAGCTGCTCAAGGGACTGCAGCTCACGGGCTCGCGTCCGACGTGGTTCCCGCCGACCGTGACGAGGCCCCCATGGTCATCCTCGGGATTGGCGTCAACATCGGGCAGGCGGCCGAGGAGCTGCCGGTTCCCTGGGCCGGCTCCCTGCGCACGCTGGGGGCGGTCGGTGCGGGACGCGGACCGGCGCTGACAGACGCAGCGGAGAGCGTCCTCACGGCGATCGGCCACCAGCTGGCTCGGCTCGTCGGGCAGTGGGAGGATGTCGGTGGCGACGTTGATGCCGCAGACGGCGCGCTCGGGCGCCGTCTGCGCTCAGCGCTGACCACCCTGGGGGAGCGGGTCAGTGTCCAGGCTCCTGATGGTGAGATCGGTGGGCTGGCTGTCGACGTCACCCCCGCCCTCGTGCTGCGCACCCAGGCCGGTGATACTGAGGTCCGTGCCGGCGACGTGACCCTCGTGCGCGTGGAGAGCTGA","MTSGGSPFSRLDTVPVTGSTQDDLRTALTGPEQESWPHLSALRALAQTAGRGRSGRAWVTPDDGGALLVSVVLRPLVPVDRLAWLPLLGGLAVRDALAPLVEGLPWRVGTKWPNDVVALPDDPAAVPAVPGWAGTRKIAGVLSELVTPEAAQGTAAHGLASDVVPADRDEAPMVILGIGVNIGQAAEELPVPWAGSLRTLGAVGAGRGPALTDAAESVLTAIGHQLARLVGQWEDVGGDVDAADGALGRRLRSALTTLGERVSVQAPDGEIGGLAVDVTPALVLRTQAGDTEVRAGDVTLVRVES$","Biotin acetyl-CoA carboxylase ligase","Cytoplasm, Membrane","POSSIBLE BIFUNCTIONAL PROTEIN BIRA: BIOTINOPERON REPRESSOR + BIOTIN--[ACETYL-COA-CARBOXYLASE]","biotin acetyl-CoA carboxylase ligase ","biotin/lipoate A/B protein ligase","","Hempel J., Harper K., Lindahl R. Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. Biochemistry 1989. 28(3):1160-1167. PMID: 2713359","","","

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PS00687	$\"[269-276]?$	ALDEHYDE_DEHYDR_GLU

InterPro
IPR004143
Domain

Biotin/lipoate A/B protein ligase
PF03099	$\"[47-119]T$	BPL_LipA_LipB

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[10-238]T$	no description
PTHR12835	$\"[14-119]T$ $\"[135-144]T$ $\"[165-194]T$	BIOTIN PROTEIN LIGASE

","BeTs to 14 clades of COG0340COG name: Biotin-(acetyl-CoA carboxylase) ligaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0340 is aom-k-yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003142 (Biotin protein ligase, C-terminal) with a combined E-value of 5.5e-09. IPB003142A 43-63 IPB003142B 107-118","","","-39% similar to PDB:2CGH CRYSTAL STRUCTURE OF BIOTIN LIGASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 7.6E_18);","Residues 29 to 119 (E_value = 1e-06) place ANA_1592 in the BPL_LipA_LipB family which is described as Biotin/lipoate A/B protein ligase family.","","BIFUNCTIONAL PROTEIN BIRA: BIOTIN OPERON REPRESSOR + BIOTIN--[ACETYL-COA-CARBOXYLASE] SYNTHETASE (BIOTIN--PROTEIN LIGASE) (AF201721)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1593","1721493","1722158","666","4.85","-11.12","22926","GTGATTCTCCTGGCATCGAAGTCATCCGGCCGCCTGGCCACACTGCGAGCCGCCGGCATCGAGCCGTTGGTCCGAGTCTCCGACGTCGATGAGGGGGCCGTACTCGAGGAACTGAGCCGCAGGCGTCGCGAGGCCGGGCTAGCGGCCCCGAGCGCCGCTGAGCAGGTCCAGGCCCTGGCTCGAGCCAAGGCCCTCGACGTCGCGGCCTCCACAGACCCGCAGGAGGCCGAGGTGGTTGTGGGCTGCGACTCCATGCTGGAGATCGGCAGCCAGGTCGTCGGAAAGCCCGCCGACGCCGCCGACGCCCGCGAGCGCTGGCGAACCATGAGCGGGAGCACCGGCACCCTGCACACGGGGCACTTCCTGGTGCGCACTGCCGACGGCGCCATCGCCGAGGGGGTCAGCTCGGCCACCATCCGTTTCGGCTCCCCGTCCCAGACCGAGATCGAGGCTTACGTCGCCAGCGGGGAACCGCTGTGGTGCGCCGGAGCCTTCACCATCGACGGCCTGGGCGGGGCCTTCATTGAGGGGATCGACGGCGACCCCCACGGAGTCGTCGGCATCTCCCTGCCGTTGCTACGCCGGCTCCTGGCGGACCTGGACGTGGTCTGGACAGACCTATGGGCGCCGCCACCGGTGACGAAACCGGCTGACGACGCCCACTGA","VILLASKSSGRLATLRAAGIEPLVRVSDVDEGAVLEELSRRRREAGLAAPSAAEQVQALARAKALDVAASTDPQEAEVVVGCDSMLEIGSQVVGKPADAADARERWRTMSGSTGTLHTGHFLVRTADGAIAEGVSSATIRFGSPSQTEIEAYVASGEPLWCAGAFTIDGLGGAFIEGIDGDPHGVVGISLPLLRRLLADLDVVWTDLWAPPPVTKPADDAH$","Septum formation protein","Cytoplasm","maf protein","K06287 septum formation protein","maf protein","","Butler Y.X., Abhayawardhane Y., Stewart G.C. Amplification of the Bacillus subtilis maf gene results in arrested septum formation. J. Bacteriol. 1993. 175(10):3139-3145. PMID: 8387996","","","

InterPro
IPR003697
Family

Maf-like protein
PF02545	$\"[1-208]T$	Maf
TIGR00172	$\"[2-198]T$	maf: septum formation protein Maf

noIPR
unintegrated

unintegrated
G3DSA:3.90.950.10	$\"[2-204]T$	no description

","BeTs to 15 clades of COG0424COG name: Nucleotide-binding protein implicated in inhibition of septum formationFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0424 is ----k-yqvdr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB003697 (Maf-like protein) with a combined E-value of 2.3e-40. IPB003697A 2-15 IPB003697B 79-122 IPB003697C 139-175 IPB003697D 180-190","","","-51% similar to PDB:2P5X Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like protein (E_value = 8.6E_12);-54% similar to PDB:1EX2 CRYSTAL STRUCTURE OF BACILLUS SUBTILIS MAF PROTEIN (E_value = 1.6E_10);-54% similar to PDB:1EXC CRYSTAL STRUCTURE OF B. SUBTILIS MAF PROTEIN COMPLEXED WITH D-(UTP) (E_value = 1.6E_10);","Residues 1 to 208 (E_value = 4.2e-52) place ANA_1593 in the Maf family which is described as Maf-like protein.","","protein (maf)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1594","1722822","1722172","651","4.97","-11.75","23523","ATGGTGGAACCGACGGCCTGCGTCGAGGATGTCGAGATGACGTGGACTCAGAGCGATCAGGAAGCCGTTGAGGCCACCTATGGCCAAGAACTGGCCGGGGCTGCGGGATCTCCCGAGGACGGTCTGGAGCCGGCCGGTGGCTGCGGCCAGAGCGACTCCTTGGAGCAGAAGGGCTTCCGTCGGCTCGATGAGATCGAGATGGATGCCTGGCGCTCCTTCCTGGCGGCCTCCACCTCCGTCACCGCCCGTCTCAATCGTGAGCTCGAGGCCGGGTGCGGCATCTCCATGCACGAGTACGAGATTCTGGTGCGCCTGTCCGAGGCTCCCGACCAGACTCTGCGCATGTCCACTCTCGCCGAGCACGTCTCGCACTCCCGCTCACGGCTGACTCACACGGTCCGGCGTCTGGAGAACGTGGGTTACGTCGAGCGCAGCTCCTGCGACTCCGACCGTCGCGGTGTCAACTGCACGCTGACGCCGCAGGGTCTCAGCTTCCTGCGCGAGGCTGCTCCGGTGCACCTTGACGGCGTGCGCCGCCATGTCGTCGACCGTCTCAGCCGTGAGCAGCAGGTCGCCATGGCTGAGCTCATGAAGGTCATCGCCCAGGCCCCGGACTCCTCCTGCGGGCTCTCGGCGGCCTCGGCCTCCTGA","MVEPTACVEDVEMTWTQSDQEAVEATYGQELAGAAGSPEDGLEPAGGCGQSDSLEQKGFRRLDEIEMDAWRSFLAASTSVTARLNRELEAGCGISMHEYEILVRLSEAPDQTLRMSTLAEHVSHSRSRLTHTVRRLENVGYVERSSCDSDRRGVNCTLTPQGLSFLREAAPVHLDGVRRHVVDRLSREQQVAMAELMKVIAQAPDSSCGLSAASAS$","Transcriptional regulator; MarR family","Cytoplasm, Periplasm","MmcW","transcriptional regulator; MarR family","regulatory protein, MarR","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR000835
Family

Bacterial regulatory protein, MarR
PR00598	$\"[113-129]T$ $\"[130-145]T$ $\"[149-165]T$ $\"[180-200]T$	HTHMARR
PF01047	$\"[94-165]T$	MarR
SM00347	$\"[87-190]T$	HTH_MARR
PS50995	$\"[66-202]T$	HTH_MARR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[94-169]T$	no description

","BeTs to 12 clades of COG1846COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1846 is aompkz--vdrlb-efg-sn-j----Number of proteins in this genome belonging to this COG is 6","***** IPB000835 (Bacterial regulatory protein, MarR family) with a combined E-value of 2.6e-09. IPB000835 129-162","","","No significant hits to the PDB database (E-value < E-10).","Residues 94 to 165 (E_value = 1.3e-12) place ANA_1594 in the MarR family which is described as MarR family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1595","1724012","1723350","663","7.90","2.52","23473","GTGCATGCCCTGCACCGGATCCAAAGCCGGCTGCGGGACTGCCGGGGAGAGGCTGCCTGGGATGGCCTGGTGCACCGCCGTTGCCGTATGAATGCGAGCCCCACGGGTGGCGGCGTCGCCCCGGGGCCGGCCGCGGCCGATGGGGGCTCGATCCGGCAGGTCGAGCGCGCAGGGTGGGAGCTCCTTCAGGCGACGGCCGAGGTTGCGGTGGCGGGGTGGTGCTGGACGGTGACCCACGAGCTCGCTCGCCGTACCCTGCCGCCACGGCAGAACACCGTCGACAAGCGGAAACTCACGGCTCTGGAGGCCAGATTTGATACGCCGTCCGACTCCGTGTTCTACCGGCTCACTGACACTGATGTGGACTCCTGGGCACAGGCCAGCGGAGACCGGAACCCCATCCATCTGCTGCCCGGAAGAGCGGCTGCGGCGGGGCTGTCGGCCGGCTCCCATGAGGTCGTTGCTCACGGCCTGCTGCTCGGAGCGATCAGTCTCGCACTCGTCCAGTCTTCGCCTTTGCGGCAGATTGGCCTGGTATTCATTGGTTCTGCTGATGTTCCGGCCTCCGAGTGCGGCGCGGAGGAGTCGTGGGCGATGCTCGCCGTCGATCCTGTCAGCGGAGACATCACTCAGGGCCGGCGTCCCGTCCTGCGCCGCCAGTGA","VHALHRIQSRLRDCRGEAAWDGLVHRRCRMNASPTGGGVAPGPAAADGGSIRQVERAGWELLQATAEVAVAGWCWTVTHELARRTLPPRQNTVDKRKLTALEARFDTPSDSVFYRLTDTDVDSWAQASGDRNPIHLLPGRAAAAGLSAGSHEVVAHGLLLGAISLALVQSSPLRQIGLVFIGSADVPASECGAEESWAMLAVDPVSGDITQGRRPVLRRQ$","MaoC domain protein dehydratase","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","MaoC domain protein dehydratase","","Si K., Maitra U. The Saccharomyces cerevisiae homologue of mammalian translation initiation factor 6 does not function as a translation initiation factor. Mol. Cell. Biol. 1999. 19(2):1416-1426. PMID: 9891075Sugino H., Sasaki M., Azakami H., Yamashita M., Murooka Y. A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene. J. Bacteriol. 1992. 174(8):2485-2492. PMID: 1556068","","","

InterPro
IPR002539
Domain

MaoC-like dehydratase
PF01575	$\"[114-168]T$	MaoC_dehydratas

noIPR
unintegrated

unintegrated
G3DSA:3.10.129.10	$\"[101-182]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 100 to 209 (E_value = 0.00082) place ANA_1595 in the MaoC_dehydratas family which is described as MaoC like domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1596","1724430","1724260","171","10.66","13.52","6458","GTGGCCAGCAAGTCCGCCGACGTTCGCCCCAAGATCACTCTGGCCTGCTCGGAGTGCAAGGAGCGCAACTACATCACCAAGAAGAACCGTCGGAACACCCCCGACCGTCTCAGCATCGCCAAGTTCTGCGCTCGCTGCGGCAAGCACACCGAGCACCGCGAGACCCGCTGA","VASKSADVRPKITLACSECKERNYITKKNRRNTPDRLSIAKFCARCGKHTEHRETR$","Ribosomal protein L33","Periplasm, Extracellular","50S ribosomal protein L33-related protein","50S ribosomal protein L33","ribosomal protein L33","","Ziegelin G., Scherzinger E., Lurz R., Lanka E. Phage P4 alpha protein is multifunctional with origin recognition, helicase and primase activities. EMBO J. 1993. 12(9):3703-3708. PMID: 8253092","","","

InterPro
IPR001705
Family

Ribosomal protein L33
PD002595	$\"[40-87]T$	Q6A6J5_PROAC_Q6A6J5;
PF00471	$\"[40-87]T$	Ribosomal_L33
TIGR01023	$\"[33-87]T$	rpmG_bact: ribosomal protein L33
PS00582	$\"[55-74]T$	RIBOSOMAL_L33

InterPro
IPR013237
Domain

Phage P4 alpha, zinc-binding
SM00778	$\"[61-83]T$	no description

","BeTs to 17 clades of COG0267COG name: Ribosomal protein L33Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0267 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001705 (Ribosomal protein L33) with a combined E-value of 3.7e-18. IPB001705 55-87","","","-77% similar to PDB:2HGJ Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA E and P codons. This entry 2HGJ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGI. (E_value = 2.0E_13);-77% similar to PDB:2HGQ Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex. This entry 2HGQ contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGP. (E_value = 2.0E_13);-77% similar to PDB:2HGU 70S T.Th. ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. This entry 2HGU contains 50S ribosomal subunit. The 30S ribosomal subunit can be found in PDB entry 2HGR. (E_value = 2.0E_13);-77% similar to PDB:2J01 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 2 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE I. (E_value = 2.0E_13);-77% similar to PDB:2J03 STRUCTURE OF THE THERMUS THERMOPHILUS 70S RIBOSOME COMPLEXED WITH MRNA, TRNA AND PAROMOMYCIN (PART 4 OF 4). THIS FILE CONTAINS THE 50S SUBUNIT FROM MOLECULE II. (E_value = 2.0E_13);","Residues 40 to 87 (E_value = 4.3e-19) place ANA_1596 in the Ribosomal_L33 family which is described as Ribosomal protein L33.","","ribosomal protein L33-related protein","","1","","","Mon Aug 6 18:24:09 2007","","Mon Aug 6 18:24:09 2007","","","Mon Aug 6 18:24:09 2007","Mon Aug 6 18:24:09 2007","Mon Aug 6 18:24:09 2007","","","Mon Aug 6 18:24:09 2007","","","Mon Aug 6 18:24:09 2007","Mon Aug 6 18:24:09 2007","","","Mon Aug 6 18:24:09 2007","Mon Aug 6 18:24:09 2007","","","","","yes","","" "ANA_1596.1","1725026","1725523","498","6.79","-0.10","18237","ATGGCCAATGACTCCTCCTTCGACGTCGTCTCCCGCCTCGACCGTCAGGAGGTGGACAACGCCGTCAACCAGTGCGCCAAGGAGATCTCCCAGCGCTACGACTTCCGCGGCGTTGACGCCTCCGTGAGCCTGTCAGGCGACACCATCACCCTGGAGGCCAACACGGCCGAGCGGGTCCTGGCGATCCTGGACGTCCTGGAGTCCAAGCTCTTCCGCCGCGGCGTCTCCCTCAAGGCCCTGGATCTGGGGGACAAGGAGCCGCGCCCCTCGGGCAAGATCTACCGCCTGGCCTGCCCGCTGCGCGAGGGACTCACCCAGGAGGTGGCCAAGAAGATCACCAAGGCGATCCGTGACGAGGGCCCCAAGAGCGTCAAGGCCACGATCCAGGGCGACGAGGTGCGCGTGACCTCCAAGTCCCGCGACGACCTCCAGACGGTGATCGCCCTGCTGAAGAACCTCGACGTCGACGCCGCCCTCCAGTTCGTCAACTACCGCTGA","MANDSSFDVVSRLDRQEVDNAVNQCAKEISQRYDFRGVDASVSLSGDTITLEANTAERVLAILDVLESKLFRRGVSLKALDLGDKEPRPSGKIYRLACPLREGLTQEVAKKITKAIRDEGPKSVKATIQGDEVRVTSKSRDDLQTVIALLKNLDVDAALQFVNYR$","Nucleotide-binding protein","Cytoplasm, Periplasm","","","","","","","","

InterPro
IPR007551
Family

Protein of unknown function DUF520
PF04461	$\"[4-165]T$	DUF520

noIPR
unintegrated

unintegrated
PD016517	$\"[17-165]T$	YAB4_STRCO_Q9F2U7;
G3DSA:3.30.70.860	$\"[95-165]T$	no description

","BeTs to 7 clades of COG1666COG name: Uncharacterized BCR, YajQ familyFunctional Class: SThe phylogenetic pattern of COG1666 is --------ebrh---------Number of proteins in this genome belonging to this COG is","***** IPB007551 (Protein of unknown function DUF520) with a combined E-value of 6.2e-09. IPB007551 6-22","Residues 17-165 are 81% similar to a (UPF0234 YAJQ VV1636 EF1165 ALL4662 RSC2549 LA3406 PP1352 BH2387 PM1656) protein domain (PD016517) which is seen in YAB4_STRCO.","","","Residues 4 to 165 (E_value = 5.3e-90) place ANA_1596.1 in the DUF520 family which is described as Protein of unknown function (DUF520).","","","","1","","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:25:34 2007","Wed Aug 15 14:25:34 2007","Wed Aug 15 14:25:34 2007","Wed Aug 15 14:24:36 2007","","","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","Wed Aug 15 14:24:36 2007","","Wed Aug 15 14:24:36 2007","","Wed Aug 15 14:24:36 2007","yes","","" "ANA_1600","1726188","1725544","645","5.65","-4.82","22830","GTGCGCGTTCTGATCGCTGACGACTCCGTCCTCCTGCGCGAGGGACTGGCACTCATCCTGGCCGACGGCGGCCACGAGGTCGTCGGGGGAGTGGGGGACGGTGAGGCCCTCGTGAGCGAGGCCCTGCGGCTGCGGCCCGACGTCGTCGTCGCCGACATCCGCATGCCGCCCTCCCACACCGACGAGGGACTGCGGGCCACCACCCGCATCCGCGCCCAGTGGCCGGGTGCACCCATCCTGCTGCTGAGCCAGTACGTCGTCGCCGGCTACCTGCCCGAGCTCCTGGCCGACGGCGGCGGCGCCCTGGGCTACCTCCTCAAGGACCGGGTCGGCGACATCGACGCCTTCCTCGGCGCGGTCGAGCGGGTGGCGCGCGGCGAGCTCGTCCTGGACCCCGACGTCGTCTCCCAGGTCCTCCAGCGAGGCCGGCGCGACGACCCGCTCACCGAGCTCACTCCCCGCGAGCGGGAGGTTCTGGCCCTCATGGCCGAGGGCCATACCAATGCCGGCATTGCCAAGATCATGGTGGTCACCGAGGGGGCCGTGGAGAAGCACACCCAGCGGATCTTCGCCAAGCTCGGCCTGCTGCCCGACGCCGCCGTCCACCGCCGCGTCAAGGCCGTCCTGACACTGCTGTCGGCCTAG","VRVLIADDSVLLREGLALILADGGHEVVGGVGDGEALVSEALRLRPDVVVADIRMPPSHTDEGLRATTRIRAQWPGAPILLLSQYVVAGYLPELLADGGGALGYLLKDRVGDIDAFLGAVERVARGELVLDPDVVSQVLQRGRRDDPLTELTPREREVLALMAEGHTNAGIAKIMVVTEGAVEKHTQRIFAKLGLLPDAAVHRRVKAVLTLLSA$","Two-component system response regulator","Cytoplasm","DNA-binding response regulator","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[151-212]T$	Q82BF8_STRAW_Q82BF8;
PR00038	$\"[151-165]T$ $\"[165-181]T$ $\"[181-193]T$	HTHLUXR
PF00196	$\"[148-195]T$	GerE
SM00421	$\"[148-211]T$	HTH_LUXR
PS50043	$\"[144-214]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[5-124]T$	Q9KY32_STRCO_Q9KY32;
PF00072	$\"[1-121]T$	Response_reg
SM00448	$\"[1-120]T$	REC
PS50110	$\"[2-83]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[140-213]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[2-126]T$	no description

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[331-420]T$	HATPase_c
SM00387	$\"[331-421]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[232-299]T$	HisKA_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[20-40]?$ $\"[46-68]?$ $\"[111-131]?$ $\"[137-157]?$ $\"[172-194]?$	transmembrane_regions

","BeTs to 6 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 6.1e-13. IPB011712A 231-248 IPB011712B 336-356","","","No significant hits to the PDB database (E-value < E-10).","Residues 232 to 299 (E_value = 5.4e-13) place ANA_1601 in the HisKA_3 family which is described as Histidine kinase.Residues 331 to 420 (E_value = 1e-08) place ANA_1601 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","two-component system sensor kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1602","1728541","1727537","1005","6.20","-4.10","36588","GTGAACACTCCACCTCCCACAGGAACCGACGACGACATCGCCCCACGCATCAGGGCCGCCGTCGACGCCGGCGAACTGCGCGGCGTGACGGGCGGGCCGGTCGAGCGGCTGGGGACCGGCGAGAGCTACACCGCCTGGCGAGTCGGCTCCGGGGAGCAGGCCCGGGTCCTGCGCCTTCCACGACGCCCGCCCCATGACCTGCCCCGCTCCATGCAGGCCGAGTTCGAGGTCCTCAGACGCGTCCCACCCGAGCTGGGAACCAGCGCCGTCGCCCTGGAGACCGGCAGCGACAACCCGCTCGGCACCCCCTACATGGTGACCACCCACGTCCCCGGTCGGGCCCTGCGCGCCACCGACTGGAACCCGCGGCTCGCCACCGCCCTCGCCCACCAGATCGCCCGCCTGCACGAGGCACTCGCCACCGCCACCGCCACCGCGCCGTCGGCCGCCTTCGTGCCTAGCGCCGACGAACAGGGGGAGGAGCTGGTGACCTGGTGGGGAGAGCATCATCCGCAGACCCTTACCGACCCCCGCGTCCGCCCGCTCCTGCCCGCCTGGCGCCGTGAGCTCGACCGCCTCGCCCCGGCCTTCGAGGCGGTCCCCACCCACCGACTCATCCACGGCGACGCCGTCGCCCCCAATGTCATCCTCGGCCCCGACGGCCTGTCGCGACTCATCGACTTCGAGTGGTCCGGGCCCGGCGACACCGCCAAGGACCTGGCCCTCATCGGGGGCCGGGTGACCGGCGGGCCCTGGTACCTGCCCATGACGCCCGACGACGTCACCGCCTTCGTCACTGAGTACGCGCGGTACCCGCGGCGCTCGCGGCTCGCGCAGGACACCGGTGCCACCGACCCGCAACGGCTGCTGGAGCGCCGCGAGGCCTACGAGCTCCTCGACCGCCTGGGCAACCTCCTGTACTGCCTCAGCCGCCCCGGCGAGGTTCGCTACGGCAAATGGGCCGACGAGCTCGCCCGCAGCCTGACCGCCCGGCTTGTGGACTGA","VNTPPPTGTDDDIAPRIRAAVDAGELRGVTGGPVERLGTGESYTAWRVGSGEQARVLRLPRRPPHDLPRSMQAEFEVLRRVPPELGTSAVALETGSDNPLGTPYMVTTHVPGRALRATDWNPRLATALAHQIARLHEALATATATAPSAAFVPSADEQGEELVTWWGEHHPQTLTDPRVRPLLPAWRRELDRLAPAFEAVPTHRLIHGDAVAPNVILGPDGLSRLIDFEWSGPGDTAKDLALIGGRVTGGPWYLPMTPDDVTAFVTEYARYPRRSRLAQDTGATDPQRLLERREAYELLDRLGNLLYCLSRPGEVRYGKWADELARSLTARLVD$","Aminoglycoside phosphotransferase","Cytoplasm","Phosphotransferase enzyme family, putative","hypothetical protein predicted by Glimmer/Critica","aminoglycoside phosphotransferase","","Trower M.K., Clark K.G. PCR cloning of a streptomycin phosphotransferase (aphE) gene from Streptomyces griseus ATCC 12475. Nucleic Acids Res. 1990. 18(15):4615-4615. PMID: 2167474","","","

InterPro
IPR002575
Domain

Aminoglycoside phosphotransferase
PF01636	$\"[33-296]T$	APH

noIPR
unintegrated

unintegrated
G3DSA:3.90.1200.10	$\"[41-243]T$	no description

","BeTs to 3 clades of COG0515COG name: Serine/threonine protein kinasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0515 is -o-p-zyq-drlbcefghs--j-i-wNumber of proteins in this genome belonging to this COG is 10","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 33 to 296 (E_value = 1.6e-17) place ANA_1602 in the APH family which is described as Phosphotransferase enzyme family.","","enzyme family, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1603","1729092","1728556","537","5.24","-3.89","19044","ATGTCCCTGACCGTCGTCGGCGGGCTGCCGGCGGTCGGTAAGACCGCTGTGTGCCGGGAGATCCTGCGCCTGCGCGCTGGGTCGCAGGCCGGACCGCCGACCTGGCTGCGCATCGACTCCATCGAGCAGGCCCTGCGGGACACTGGCGAGATGCTCCCCGGCATGCCCGCGGGCGCCGGATACTACGTGGCCGCCGCTGTGGCCCGGGACGTTCTGGCCTCGGGCGGGGACGTTCTGGTCGAGTGTGTCAACCCGCTGCCCATCACCCGCCGCCTGTGGGAGGAGACGGCCTCGGCCGCGGGCGCCCGGTTTCTCTCCGTCGAGCTCATCTGCTCCGATGCTGCCGAGCACCGGCGCCGCGCCCAACAGCGGGGCAGCGATATCGAGGGCCTCGAGCTGCCGGGGTGGCAGGAGATCGCCCGTCGCGATTACGCCCCCTGGCCCGAGGCCGACCTCCGCCTCGACACCGCCCGGCTCACCGTCACCGAGGCCGCCCGGGCCATCGTCGACCTCGGCCTCGCGGATGGAACCCGATGA","MSLTVVGGLPAVGKTAVCREILRLRAGSQAGPPTWLRIDSIEQALRDTGEMLPGMPAGAGYYVAAAVARDVLASGGDVLVECVNPLPITRRLWEETASAAGARFLSVELICSDAAEHRRRAQQRGSDIEGLELPGWQEIARRDYAPWPEADLRLDTARLTVTEAARAIVDLGLADGTR$","Hypothetical protein","Cytoplasm","Shy8","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1605","1729965","1729096","870","8.49","3.57","30945","ATGACAAGGACTCACCACTACAACGGTCTCAAGACCGCCGTCCTCCTGGGCGGCATGTGGAGCCTGCTTCTCCTGCTCGGCTACGTGCTGGCCCGGGGGACCGGCTCCGCCATCTGGCTGGTCATCGCGCCGGTCATCGGCCTGGTGCAGACCGCCCTCGGCTTATGGAACTCCGACAAGATCGCCGTGCGCTCCATGGGCGCCATCGAGGTCACCGAGGCCCAGCAGCCCCAGATGTACGCCATCGTGCGTGAGCTCTCCGCCGCTGCCGGCCAGCCCATGCCGCGCCTCTACGTGGCCCCCACGATGAGCCCCAACGCATTCGCCACCGGCCGCAGCCCCTCGCACGCCGCCGTGTGCTGCACGCAGGGCATTCTCCAGCTCCTCAACGAGCGTGAGCTGCGCGGCGTCCTGGGCCACGAGCTCTCCCACGTCTACAACCGCGACATCCTCACCTCCTCGGTGGCCGCGGGCATCGCCGGCGTCATCTCCTCCATGGTCACCATGGCCATGTGGTTCGGCGGCGGCAACCGGCGCGACCGGGACGGCGGCAACATCATCGCCGTCCTGCTGCTCTCCCTCCTGGCGCCCCTGGCCGCCGCCATCACCCAGTTCGCCATCTCCCGGACCCGCGAGTACGACGCCGACCACGACGGCGCCGAGCTCACACAGGACCCGCTCGCCCTGGCCAGCGCGCTCAGCAAGCTCGAGTCCGGAATCTCGCGCGTGCCCATGGGGCAGGACCCGCGCCTCGAACCGGTCTCCTCCATGATGATCGCCAACCCCTTCGGGAGCCTGCGCAACCTCTTCGCCACCCACCCGCCCATGGACAAGCGCATCGCCCGCCTCGAGCAGATGGCCGGGTACTGA","MTRTHHYNGLKTAVLLGGMWSLLLLLGYVLARGTGSAIWLVIAPVIGLVQTALGLWNSDKIAVRSMGAIEVTEAQQPQMYAIVRELSAAAGQPMPRLYVAPTMSPNAFATGRSPSHAAVCCTQGILQLLNERELRGVLGHELSHVYNRDILTSSVAAGIAGVISSMVTMAMWFGGGNRRDRDGGNIIAVLLLSLLAPLAAAITQFAISRTREYDADHDGAELTQDPLALASALSKLESGISRVPMGQDPRLEPVSSMMIANPFGSLRNLFATHPPMDKRIARLEQMAGY$","Zn-dependent protease with chaperone function","Membrane, Cytoplasm, Extracellular","proteinase htpX","putative peptidase ","peptidase M48, Ste24p","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 1989. 242(2):211-214. PMID: 2914602Murphy G.J., Murphy G., Reynolds J.J. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett. 1991. 289(1):4-7. PMID: 1894005","","","

InterPro
IPR001915
Family

Peptidase M48, Ste24p
PF01435	$\"[79-288]T$	Peptidase_M48

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[137-146]?$	ZINC_PROTEASE

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[12-30]?$ $\"[36-56]?$ $\"[153-173]?$ $\"[187-207]?$	transmembrane_regions

","BeTs to 20 clades of COG0501COG name: Zn-dependent protease with chaperone functionFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0501 is aompkzyq-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB009481 (HtpX, N-terminal) with a combined E-value of 5e-30. IPB009481C 76-118 IPB009481D 119-145 IPB009481E 185-236 IPB009481G 269-283 IPB009481B 38-78","","","No significant hits to the PDB database (E-value < E-10).","Residues 79 to 288 (E_value = 8.8e-19) place ANA_1605 in the Peptidase_M48 family which is described as Peptidase family M48.","","htpX (htpX)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1606","1730583","1729999","585","9.50","5.36","22308","ATGAGAACCCGCCGCATCCGCTTCGCCAGCGGAACTAACCGCTGGGCGCGTGACCTCTACCTGCGTGCCTTCCCCGAGGATGAGCGCATTCCCTGGGCGCTCATCCACGTGCTCAGCCTGCGCCGCGGCGTCGACCTCGTCGCCTGGTGGGACCAGCCCGCCGGACCGACCCGTGCGGCCCGCCCGGACCCTGTGGCCCTGACCTGGACCGTGCGTCGCCCCGGCTCCCGCCTGCTCTTCCTCTTCTACCTCGCCGTCGACGACGCCGCACGCGGCCGCGGGGTGGGCACCCGCCTCCTGGCCGAGCTCGAGCGCCGTCACCCCGGCTGCACCATCGTCCTGGACATCGAGCCCGTCATCGCTGAGGCCGACAACGCCGAGCAGCGACGCCGTCGGTTCTCCTTCTACGAGCGCTCCGGCTTCCGCGACACCGGGTACGCGGTCCAGGACTCGACGGGGGAGTACTGGACCCTCGCGCGTGAGGCGCCGGGAACCACCTTCGATCCCGACGACTTCCGCGATGCCCTGAGCTGCCTGGATTGCAGCCTCATCACCGCGCGAGTGGTCCGGCGCCAGCAGACATAG","MRTRRIRFASGTNRWARDLYLRAFPEDERIPWALIHVLSLRRGVDLVAWWDQPAGPTRAARPDPVALTWTVRRPGSRLLFLFYLAVDDAARGRGVGTRLLAELERRHPGCTIVLDIEPVIAEADNAEQRRRRFSFYERSGFRDTGYAVQDSTGEYWTLAREAPGTTFDPDDFRDALSCLDCSLITARVVRRQQT$","Acetyltransferase, GNAT family family","Cytoplasm","acetyltransferase, GNAT family family","hypothetical protein","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[46-142]T$	Acetyltransf_1
PS51186	$\"[19-161]T$	GNAT

","BeTs to 7 clades of COG0454COG name: Histone acetyltransferase HPA2 and related acetyltransferasesFunctional Class: K [Information storage and processing--Transcription] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0454 is aompkzyqvdrlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 46 to 142 (E_value = 0.00099) place ANA_1606 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","GNAT family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1607","1732185","1730698","1488","4.88","-30.38","53461","GTGAACGCACGTCCTCTCAATGTCGCCGTCATCGGAGCAGGCCCCGCAGGCATCTACGCCTCGGACATCCTCTCGAAGTCGGGCATGGAGGTCTGTATCGACCTGTTCGAGCGGCTTCCTGCGCCCTACGGGCTGGTGCGCTACGGCGTCGCCCCCGACCACCCGCGCATCAAGCAGATCATCGTGGCCCTCTACAAGATCCTCCAGCGCGGGGACATTCGGCTCATCGGCAACGTCGAGGTCGGCCGTGACATCTCGGTGGCCGAGCTCCAGGAGCACTATGACGCCATCATCTTCTCCACCGGAGCCGACACCGACGCCCCCCTCGACATTCCCGGCGTCGACGCCCCTGAGTGCTACGGCGGCGCCGACTTCGTCTCGTGGTACGACGGTCACCCCGACCACCCGCGTACCTGGGACCTGAGTGCCAAGGAGGTCGCCGTCATCGGCGTCGGCAACGTCGCGCTGGACATCGCCCGCGTCCTGGCCAAGCACGCCGACGACCTCATGACCACCGAGATCCCCGCGAACGTGGCCGCCACGCTCCAGCAGTCCCCGGTCACCGACGTGCACGTCTTCGGTCGCCGCGGTCCGGCTCAGGTGAAGTTCACCCCGCTGGAGCTGCGCGAGCTCGGCAAGCAGGCCGACGTCGACGTCCTCGTCGACGAGGAGGACTTCGAGTACGACGAGGGCTCGCAGGCGGCCCTGGCCTCCTCCAACCAGCAGCGCCAGGTCGTCAAGGCCCTTGAGGGGTACGCGATGCAGGAGCCGGAGGACCTCACCGCCTCCCACCGCATCCACATCCACCTCTTCTCGGCGCCCCACGAGGTCCTCACCGACGACGACGGCCACGTCGTCGGCCTGCGCACCGAGCGCACCCGCCTGACCGGCGACGGCAACGTCACCGGCACCGGCGAGTACCGCGACTGGCCCGTCCAGGCCGTCTACCGCGCTGTCGGATATGCCTCCAGCGCCATCGAGGGCCTGCCCTTCGACGCCGAGCGGCACGTCGTCCCCAACGAGGGCGGCCGCGTCCTCGGCGAGGACGGCAAGCCTCTGACCGGCCTGTACGCCACCGGCTGGATCCGTCGCGGCCCCGTGGGCCTCATCGGCTCCACCAAGTCCGACGCGCAGGAGACCATCACCAACCTCGTGGCCGACGCCAACGCCGGCCTGCTGCACGCCGAGACCAGCGACGAGGCCCAGGTCGGTCACGACGCCATCATCGCCCTGCTGGAGTCCCGCGGCATCCCCTTCACCAACTGGGAGGGCTGGGAGCTGCTGGACGCCTATGAGCGCGAGCTCGGTGAGGGCTACGGTGAGGTCGTTGTCACCGGAGGGGCCTCCAAGCCGCGCGAGCGCGTTAAGGTCGTCTCCCGCGATGCCATGACCGCGATCTCCCGCTCCACCGAGGTTCCCGAGGACCTCATCGGCCAGCCCGAGACGGGTCGCGTCCCCGAGCGCGTCGCCCACCGCCTGGCCGACTGA","VNARPLNVAVIGAGPAGIYASDILSKSGMEVCIDLFERLPAPYGLVRYGVAPDHPRIKQIIVALYKILQRGDIRLIGNVEVGRDISVAELQEHYDAIIFSTGADTDAPLDIPGVDAPECYGGADFVSWYDGHPDHPRTWDLSAKEVAVIGVGNVALDIARVLAKHADDLMTTEIPANVAATLQQSPVTDVHVFGRRGPAQVKFTPLELRELGKQADVDVLVDEEDFEYDEGSQAALASSNQQRQVVKALEGYAMQEPEDLTASHRIHIHLFSAPHEVLTDDDGHVVGLRTERTRLTGDGNVTGTGEYRDWPVQAVYRAVGYASSAIEGLPFDAERHVVPNEGGRVLGEDGKPLTGLYATGWIRRGPVGLIGSTKSDAQETITNLVADANAGLLHAETSDEAQVGHDAIIALLESRGIPFTNWEGWELLDAYERELGEGYGEVVVTGGASKPRERVKVVSRDAMTAISRSTEVPEDLIGQPETGRVPERVAHRLAD$","Ferredoxin--NADP(+) reductase","Cytoplasm, Extracellular","NADP adrenodoxin-like ferredoxin reductase","FAD-dependent pyridine nucleotide-disulphide oxidoreductase","Ferredoxin--NADP(+) reductase","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Russel M., Model P. Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 1988. 263(18):9015-9019. PMID: 3288628Cohen G., Argaman A., Schreiber R., Mislovati M., Aharonowitz Y. The thioredoxin system of Penicillium chrysogenum and its possible role in penicillin biosynthesis. J. Bacteriol. 1994. 176(4):973-984. PMID: 8106340Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N. Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 1990. 265(18):10535-10540. PMID: 2191951Xu X.M., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T. Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1. J. Biochem. 1991. 109(5):678-683. PMID: 1917890Mathieu I., Meyer J., Moulis J.M. Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum. Biochem. J. 1992. 285:255-262. PMID: 1637309Waksman G., Krishna T.S., Williams Jr C.H., Kuriyan J. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. J. Mol. Biol. 1994. 236(3):800-816. PMID: 8114095McKie J.H., Douglas K.T. Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett. 1991. 279(1):5-8. PMID: 1995341","","","

InterPro
IPR000103
Domain

Pyridine nucleotide-disulphide oxidoreductase, class-II
PR00469	$\"[7-29]T$ $\"[95-103]T$ $\"[141-165]T$	PNDRDTASEII

InterPro
IPR000759
Family

Adrenodoxin reductase
PR00419	$\"[7-29]T$ $\"[32-45]T$ $\"[75-85]T$ $\"[146-160]T$	ADXRDTASE

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368	$\"[7-29]T$ $\"[145-170]T$	FADPNR
PF07992	$\"[7-367]T$	Pyr_redox_2

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[90-321]T$	no description
PTHR11938	$\"[4-440]T$	FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF4	$\"[4-440]T$	FERREDOXIN/FERREDOXIN--NADP REDUCTASE-RELATED

","BeTs to 17 clades of COG0493COG name: NADPH-dependent glutamate synthase beta chain and related oxidoreductasesFunctional Class: E,RThe phylogenetic pattern of COG0493 is ---KYqVcEbR------l--xNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-50% similar to PDB:1LQT A covalent modification of NADP+ revealed by the atomic resolution structure of FprA, a Mycobacterium tuberculosis oxidoreductase (E_value = 1.8E_70);-50% similar to PDB:1LQU Mycobacterium tuberculosis FprA in complex with NADPH (E_value = 1.8E_70);-50% similar to PDB:2C7G FPRA FROM MYCOBACTERIUM TUBERCULOSIS: HIS57GLN MUTANT (E_value = 1.5E_69);-53% similar to PDB:1CJC STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS (E_value = 9.2E_67);-53% similar to PDB:1E1K ADRENODOXIN REDUCTASE IN COMPLEX WITH NADP+ OBTAINED BY A SOAKING EXPERIMENT (E_value = 9.2E_67);","Residues 120 to 480 (E_value = 0.0019) place ANA_1607 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.","","adrenodoxin-like ferredoxin reductase","","1","","","Mon Aug 6 18:31:15 2007","","Mon Aug 6 18:31:15 2007","","","Mon Aug 6 18:31:15 2007","Mon Aug 6 18:31:15 2007","Mon Aug 6 18:31:15 2007","","","Mon Aug 6 18:31:15 2007","","","Mon Aug 6 18:31:15 2007","Mon Aug 6 18:31:15 2007","","","Mon Aug 6 18:31:15 2007","Mon Aug 6 18:31:15 2007","","","","","yes","","" "ANA_1608","1732643","1735159","2517","6.22","-10.31","84981","ATGTTCGAAGGCGGTGTGCTTCCTCGTGTCCCGGCCGGTGGTGCGGCCGAGGTGCTGGCCGCGCCCGCCGGGGACGCGTCGGCGGGGGCTGTGACCTGCACTGAGGACGTGGTGGGTCTGCTGGGGTCCTTGGCCGGCGGTGGAGCGCTGGCCGGTGTGGTCGAGGGGCTGCTGTCCCGGCTGCTGGTGGCCGCCCAGAACCCCAACGACGACGGCGATGGCGGTGGCGGCGGCGTCGGTGGTGAGAGCTCTGACGCTGAGAGCGCCGGCAGTGCTGATGGTGAGGGCTTGTTCGCAGGCGATTCGGACGCTGACGCGACGCTGGTGGCCGCTGCTGATGGACACAGGGTCGTGTCCGTGGAGGAGGTCGGTGCTACTGGGCTGCTTGGCCTGGGAGCACGGGGTCTGGGGGAGCTGGCCGCGGCCTGTCACCGGCTGGCGGCGTGGGCCGCGTGGGGCGAGGCCCTGGCGGCGGCGTGCCTGACCGCCTGTGGTGAGCTGTCGAGTCATCCGGATCAGTGGGGCCCAGACGGTGCGGTCTCACCGGTGGTGGGGTTTGAGGAGCGGCGGTTCAACACCACCTGCCTGCTGTCGGCCCGCCTGGGGCTGTCTCGAACTCAGGCCGGGCAGGTCGTGGACCACGGTAGCGCGCTGATGGACGTCGGTTTCGGGCCCACCGAGGCCATGGAGCGGTGCGGGGTGCTGGATGCAGCCAAGGCGTCCTTGGTGACTCGTCGCCTGGAGGGCGTGCCGGCCCCGGTGGCCCTGGCGGTTCAGGAGCGGGTGCTGCCTCAGGCACCTAGGCGCAGCGTGTCCCAGGTGGGACGCGACATTGAGCGGGCCCTGATGGAGGTCGACCCCGCCGGGCATGCTGAGCGGGTGCGGGTCAATGTCTCCCGGCGGTGCGTGACGCGCCCCAGGCCCGCCGGCGAGGGCATGTCCCAGGTCTGCCTGCTGCTACCGACCATGGACGCGCTGCTGCTGGACGCCACTCTGGACGCGATCGCCGCCAGCGCGCGGGCCTGCGGTGAGCAGCGCACCCCAGCCCAGCTGCGCGCCGACGCCATCACCGCCATGACCCTGTCCACACTACGCACCAGCCAGCAGACCGCCTACCACAGACCCACGCAAGCCCCCGACGACGACACCAGTGGCGGCACTGGCGGTGGTGGCGGTCTCGGCAGCAGCACTGGAGACTTTGGCGGTGTGAGTGAGCTGGGTTCAGTGCCTGCCTCGTTCTCTCCTCCCAGGCGTTCTGCCTCCCTGGGTCGTCTGCTGCCTGACGGGGTGCCTTTGGAAGGGCTTCTGGGGGCCTTGAGCTCCCTGGTGGGGTCCGCCAGCCCGTGTTGGACCCCCTCAGGCACCGGACACCTCCCCCTCCCCAAGAACATCCACATCGACGTCCAGGTCACCGTTCCCCTCACCAGCCTGGCTGGTCTGGCTCCGCCCGACGACGGCCCCACCGGCAGCGACGATCCAGGAGACGGAGGCCCCGGCAAGAGCGCCGCCGCCACGCCTGATCCTCTCAGCGGTGCAGCATCCCCAGGCGGCAGGAGAAGCCTGCCCACCGCCGGCGGGAGGAGTCTGCCCACCGCTGACGGGAGGAGTCTGCCCGGTTCCAGCGGGAGGAGTCTGCCCGAACCCACCCCGGCCACTCCCGCCTTCCAGCCCGCCGCCTCGCGCTCTGCTGCTCACGACTCCTCGCCCGCCGCGTCGTGCTCTGCTGCTCCCAACGCCCAGCCCGCCGTTCAGCCTGCTGTCTCGTTGTCCGCCGCGGCTACCGGGGTTGCTCAGGTGCGGGTTGGGGCGCGCAGTGTGGCGGTGCCGGCCCTGACTGCCTGGGCCCTGGCCGCCGGCGGGACCTGGAGGCGCCTGGTCACCGACCCAGCAAGCGGAGTCGTGATCGACGTCGGCCGCACCAGGTACCGTCCCCCGGCCGGCCTGGCCGACCTGGTGCGCGCCCGCGACCGGGCCTGTGTCTTCCCCACCTGCCAGACCCCCGCCGAGCGGTGCGACATCGACCACCTCACCGCCTGGAGCCAGGGCGGGACCACCAGCCTGGACAACCTCGTCACCCTGTGCGAGGCCCACCACCGCCTCAAGCACACCCCCGGATGGGCCCTCACCCGAGACCAGGCCAGCGGGATCCTGTCCTGGCACACCCCCGACAAGACTGTCTACCAGCGCCACCCAGACGGCACCATCACCCGCCTACCCAAGAGGATCGGGCCCCACCAGCACCACGTCCCCGGCGCCGTCGTACTAACGGACCTGAGCAAGCAGATCAGCCCCGACCTCATCGACCGCCTCAACCGGGCCCTTGACAGAGCACTCGACGACCAGGTCCACGACCACACCGGCCTCGGCACCAACACCAACGGCAGCAGCAGGGCCCGGCTCGAGACTCGCGGCCCCCGCCCCGGCCAGAGAGCCGGAGCCTACGAGCCCACCCCCTACCCCAAAGCCGCCCACACCCTCCAACTCGCACCCCTCATCGACCAAGCCCCACCCTTCTAA","MFEGGVLPRVPAGGAAEVLAAPAGDASAGAVTCTEDVVGLLGSLAGGGALAGVVEGLLSRLLVAAQNPNDDGDGGGGGVGGESSDAESAGSADGEGLFAGDSDADATLVAAADGHRVVSVEEVGATGLLGLGARGLGELAAACHRLAAWAAWGEALAAACLTACGELSSHPDQWGPDGAVSPVVGFEERRFNTTCLLSARLGLSRTQAGQVVDHGSALMDVGFGPTEAMERCGVLDAAKASLVTRRLEGVPAPVALAVQERVLPQAPRRSVSQVGRDIERALMEVDPAGHAERVRVNVSRRCVTRPRPAGEGMSQVCLLLPTMDALLLDATLDAIAASARACGEQRTPAQLRADAITAMTLSTLRTSQQTAYHRPTQAPDDDTSGGTGGGGGLGSSTGDFGGVSELGSVPASFSPPRRSASLGRLLPDGVPLEGLLGALSSLVGSASPCWTPSGTGHLPLPKNIHIDVQVTVPLTSLAGLAPPDDGPTGSDDPGDGGPGKSAAATPDPLSGAASPGGRRSLPTAGGRSLPTADGRSLPGSSGRSLPEPTPATPAFQPAASRSAAHDSSPAASCSAAPNAQPAVQPAVSLSAAATGVAQVRVGARSVAVPALTAWALAAGGTWRRLVTDPASGVVIDVGRTRYRPPAGLADLVRARDRACVFPTCQTPAERCDIDHLTAWSQGGTTSLDNLVTLCEAHHRLKHTPGWALTRDQASGILSWHTPDKTVYQRHPDGTITRLPKRIGPHQHHVPGAVVLTDLSKQISPDLIDRLNRALDRALDDQVHDHTGLGTNTNGSSRARLETRGPRPGQRAGAYEPTPYPKAAHTLQLAPLIDQAPPF$","HNH endonuclease","Extracellular, Membrane, Cytoplasm","HNH endonuclease domain protein","HNH nuclease","HNH endonuclease","","Dalgaard J.Z., Klar A.J., Moser M.J., Holley W.R., Chatterjee A., Mian I.S. Statistical modeling and analysis of the LAGLIDADG family of site-specific endonucleases and identification of an intein that encodes a site-specific endonuclease of the HNH family. Nucleic Acids Res. 1997. 25(22):4626-4638. PMID: 9358175Gorbalenya A.E. Self-splicing group I and group II introns encode homologous (putative) DNA endonucleases of a new family. Protein Sci. 1994. 3(7):1117-1120. PMID: 7920259Shub D.A., Goodrich-Blair H., Eddy S.R. Amino acid sequence motif of group I intron endonucleases is conserved in open reading frames of group II introns. Trends Biochem. Sci. 1994. 19(10):402-404. PMID: 7817395","","","

InterPro
IPR002711
Domain

HNH endonuclease
PF01844	$\"[659-705]T$	HNH

InterPro
IPR003615
Domain

HNH nuclease
SM00507	$\"[647-699]T$	HNHc

","No hits to the COGs database.","***** IPB003870 (Protein of unknown function DUF222) with a combined E-value of 3e-18. IPB003870F 639-679","","","No significant hits to the PDB database (E-value < E-10).","Residues 659 to 705 (E_value = 6.2e-07) place ANA_1608 in the HNH family which is described as HNH endonuclease.","","endonuclease domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1609","1736647","1735172","1476","4.96","-21.06","51700","ATGCTCAAGAAAGGCGATACCGCCTCCTCTGGGAAGAGCTCGGGTGCCGCGTCCCCACGTGCGGTCGCGACCGCGACTGGTCCCCACGGTGGGGTGATGCTGGAGGCGGAGTGGAAAGGGGCTCCGCTCTCGGTTGAGGTGGGGCCTGCCGCAGTCAACGACAAGTACGCTGTCGTGCGCTTGGTGTTCACAACGACCTCGGATGAGAATGTGAGCCTGTCTCAGCCGTTCGGCTTCGTGGATCATTCGGGGACGATGCTTGCGATCAGAATGCTCTCTTTGGATAAGGGCTTGGTGTATCGCGAACTCGACGAAGAAACACGTCATTTATATGATGGTGTTGAAAAGGGTAAACCCTTGGAAGTATTTCCAGTATTTCATGCGCCGCCCGAGGGTGTTGGCATCGTGGAGCTGCTCCTTCCTAACGTGGGTATTGCTGCAGGTGTTCCGGTTTTGAAGGATACCGAGGTTGATTTCTCAGTGGATGATGTGCTGTCAAAGGCGAAGCTCGATGAGTCGGAGGCGGGGCCGTTCAAGATCGAGACGATGTCGCTGGCTGCTGATGATTCGGCGGATATGAAGCAGGATGAGAAGTCGACGACGGTGACGGTGGCTGGTGATGTCACGTTTGCGACTGACTCCGATCAGCTGTCGGCTCAGGCTGACAGTGTGTTGGCGAGTGTGGTGGAGCAGATCAAGAAGTTTCCCTCTGGTGGGGATCTGACGATCACGGGGCATACCGATGATGTGGCTGATGATGCGCATAACCAGGAGCTGTCGGAGCGGCGGGCCAAGGCGGTGTCGGAGCGGCTCAAGAGGCTGACGGATCTGTCTAAGTGGAAGGAGTCGGTCTCTGGTAAGGGGGAGTCCTCGCCGCGAGTATCGAATGACTCCGATGAGCACCGGCAGGCTAACCGTCGTGTGGAGATCACGCTGACGCCCTCGAAACCCGCCGAATCCAGTGCGTCACCAAGTGCGAGTGCGGCACCGTCGTCAACCTCGATGCCTAAGGCTGCCGGTCCTGCGGGCAAGGGACCTGAGGGTGTTGATGTGAAGATCGACGGTAAGACCGTGCGCATGGTGATCGACCATGTGGTTCGAGCCGGTGGCTACTTGGCTGGAACAGTGGTGGTCACCTCCAGCGAGAAGGTCAGCATGCCGGTTGCTCCCTTCTCCTTGCCTGGAAATATGATGGATATGCGTGACCTCGGAGTTTTTGGTGTGAGTGGTATAACTATCCTCAGTGGTGGGTTGAGATATCTGGAGGCCGACTACACGTATTCCGATGGAAGTAGACTTCCGTTAGCGAATAGTTTTGTGTGCGATCTTGAGCCTGAGGCTTCCCAGTCCCTCCCGGTGGTGTGGCCGGATGTCGGTGGGAGCAGTGTCACGATTGATATGCCGGCAGGTGAATATATTTATACGAAAGAGCGAGTCGTCGCTCGCCTCACGGATATCCCGGTCGTCAGCGCGTAG","MLKKGDTASSGKSSGAASPRAVATATGPHGGVMLEAEWKGAPLSVEVGPAAVNDKYAVVRLVFTTTSDENVSLSQPFGFVDHSGTMLAIRMLSLDKGLVYRELDEETRHLYDGVEKGKPLEVFPVFHAPPEGVGIVELLLPNVGIAAGVPVLKDTEVDFSVDDVLSKAKLDESEAGPFKIETMSLAADDSADMKQDEKSTTVTVAGDVTFATDSDQLSAQADSVLASVVEQIKKFPSGGDLTITGHTDDVADDAHNQELSERRAKAVSERLKRLTDLSKWKESVSGKGESSPRVSNDSDEHRQANRRVEITLTPSKPAESSASPSASAAPSSTSMPKAAGPAGKGPEGVDVKIDGKTVRMVIDHVVRAGGYLAGTVVVTSSEKVSMPVAPFSLPGNMMDMRDLGVFGVSGITILSGGLRYLEADYTYSDGSRLPLANSFVCDLEPEASQSLPVVWPDVGGSSVTIDMPAGEYIYTKERVVARLTDIPVVSA$","OmpA family domain protein","Cytoplasm, Periplasm, Extracellular","OmpA family domain protein","probable outer membrane protein precursor","OmpA/MotB domain protein","","Freudl R., Klose M., Henning U. Export and sorting of the Escherichia coli outer membrane protein OmpA. J. Bioenerg. Biomembr. 1990. 22(3):441-449. PMID: 2202726Bouveret E., Benedetti H., Rigal A., Loret E., Lazdunski C. In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J. Bacteriol. 1999. 181(20):6306-6311. PMID: 10515919De Mot R., Proost P., Van Damme J., Vanderleyden J. Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. aeruginosa and P. syringae. Mol. Gen. Genet. 1992. 231(3):489-493. PMID: 1538702","","","

InterPro
IPR006664
Domain

Bacterial outer membrane protein
PR01021	$\"[210-232]T$ $\"[241-256]T$ $\"[256-272]T$	OMPADOMAIN

InterPro
IPR006665
Domain

OmpA/MotB
PD000930	$\"[207-267]T$	Q9I4T3_PSEAE_Q9I4T3;
PF00691	$\"[209-306]T$	OmpA
PS51123	$\"[197-316]T$	OMPA_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.60	$\"[192-316]T$	no description

","BeTs to 11 clades of COG2885COG name: Outer membrane protein and related peptidoglycan-associated (lipo)proteinsFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG2885 is -------q--r---efghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB000498 (OmpA-like transmembrane domain) with a combined E-value of 5e-20. IPB000498E 194-222 IPB000498F 235-282 IPB000498G 283-314***** IPB006690 (OmpA-like domain) with a combined E-value of 7.9e-18. IPB006690A 208-233 IPB006690B 241-292 IPB006690C 303-312***** IPB001035 (Sodium-type flagellar protein MotY precursor signature) with a combined E-value of 2.9e-08. IPB001035K 256-273 IPB001035M 295-315","","","No significant hits to the PDB database (E-value < E-10).","Residues 209 to 306 (E_value = 9.7e-16) place ANA_1609 in the OmpA family which is described as OmpA family.","","family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1610","1738027","1736921","1107","4.76","-23.07","38830","GTGATCGGATCACTGCCGCTGAGCGCCCCCGAGCTGGAGTCGCGCATCATCCCCGCCCTCCAGACCATTGAGGACCGCCTCATGGAGGTGGTCACCAGCGCCGACGAGACCATCAATCCGCCGACCTCGCACCTGGCCGAGGCCGGGGGCAAGCGCCTGCGCCCGGTCCTGGCCCTGCTGACCGCCCAGCTCGGCGACCCGGCCCTGGCCACCGGTGAGGAGATCCGCGACGCCGGGGTGGCCGTGGAGCTGACCCACATCGCCACCCTCTATCACGACGACGTCATGGACGAGGCCCCGCTGCGCCGCGGCGCCCCGAGCGCCCAGACCGTGTGGGGCAACTCCGCCGCCATCCTCACCGGCGACGTCCTCGTGGCCCGGGCCTCCCAGCTGATGGCGGCCCTCGGCCCGGAGGCCGTCATGGCCCACGCCAAGACCTTCGAGCGCCTGTGCATGGGTCAGCTCCACGAGACCCTGCCACGCCCGGCAGGTACCGATCCGGTCGACCACTACATCCAGGTTCTGGCGGACAAGACCGGTTCCCTCATCGCAGTGTCCGCGCGCTACGGGGCGATGCTCACCGGTGCCGGGACGCACACCGAGCAGATCGTGGAGGAGTTCGGCGAGCGGATCGGTGTGGCCTTCCAGCTGGCCGACGACGTCATCGACCTCATGAGCGACTCGGCCACCACCGGTAAGACCCCCGGCACCGACCTGCGCGAGGGAGTGGACACCATGCCGGTCCTCCTCCTGCGCAAGGCCCTGGCGGCCGGCGAGCTCGACGCCGCCGGCCAGGCCATCCTCTCGCGCCTGTCCAGCGGCGACCTCTCCGATGACGCCTTCCTGTCCGACGTCGTCGCTCGCCTGCGCGAGCACCCCGTCCTGGCCCGTACCCGCGAGATGGCCATGGACTGGGCGGCTCAGGCAGTGGAGGGCCTGGAGGGCCTGGAGGAGGCCGTCCTTGACGGAACCCGGCAGCGCCTGGCCCAGGCTGGCATCGAGGGCGAGGCCGCCGCGGCGGCTATGACTGATGCCGGTGAGCGGGTGAGGCAGGTGCGTGCGGCCATGGAGGACTTCGCCCGCATCCTCGTGGACCGGGCCGCCTGA","VIGSLPLSAPELESRIIPALQTIEDRLMEVVTSADETINPPTSHLAEAGGKRLRPVLALLTAQLGDPALATGEEIRDAGVAVELTHIATLYHDDVMDEAPLRRGAPSAQTVWGNSAAILTGDVLVARASQLMAALGPEAVMAHAKTFERLCMGQLHETLPRPAGTDPVDHYIQVLADKTGSLIAVSARYGAMLTGAGTHTEQIVEEFGERIGVAFQLADDVIDLMSDSATTGKTPGTDLREGVDTMPVLLLRKALAAGELDAAGQAILSRLSSGDLSDDAFLSDVVARLREHPVLARTREMAMDWAAQAVEGLEGLEEAVLDGTRQRLAQAGIEGEAAAAAMTDAGERVRQVRAAMEDFARILVDRAA$","Trans-hexaprenyltranstransferase","Cytoplasm","Geranylgeranyl pyrophosphate synthase","trans-hexaprenyltranstransferase ","Polyprenyl synthetase","","Ashby M.N., Edwards P.A. Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase. J. Biol. Chem. 1990. 265(22):13157-13164. PMID: 2198286Fujisaki S., Hara H., Nishimura Y., Horiuchi K., Nishino T. Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli. J. Biochem. 1990. 108(6):995-1000. PMID: 2089044Carattoli A., Romano N., Ballario P., Morelli G., Macino G. The Neurospora crassa carotenoid biosynthetic gene (albino 3) reveals highly conserved regions among prenyltransferases. J. Biol. Chem. 1991. 266(9):5854-5859. PMID: 1826006Kuntz M., Romer S., Suire C., Hugueney P., Weil J.H., Schantz R., Camara B. Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: correlative increase in enzyme activity and transcript level during fruit ripening. Plant J. 1992. 2(1):25-34. PMID: 1303794Math S.K., Hearst J.E., Poulter C.D. The crtE gene in Erwinia herbicola encodes geranylgeranyl diphosphate synthase. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(15):6761-6764. PMID: 1495965","","","

InterPro
IPR000092
Family

Polyprenyl synthetase
PTHR12001	$\"[23-335]T$	GERANYLGERANYL PYROPHOSPHATE SYNTHASE
PF00348	$\"[37-288]T$	polyprenyl_synt
PS00444	$\"[211-223]T$	POLYPRENYL_SYNTHET_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.600.10	$\"[11-320]T$	no description
PTHR12001:SF15	$\"[23-335]T$	POLYPRENYL-DIPHOSPHATE SYNTHASE

","BeTs to 25 clades of COG0142COG name: Geranylgeranyl pyrophosphate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0142 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB000092 (Polyprenyl synthetase) with a combined E-value of 7.2e-20. IPB000092A 49-58 IPB000092B 94-107 IPB000092D 211-233","","","-54% similar to PDB:1WY0 Crystal structure of geranylgeranyl pyrophosphate synthetase from Pyrococcus horikoshii Ot3 (E_value = 1.2E_31);-51% similar to PDB:2FOR Crystal Structure of the Shigella flexneri Farnesyl Pyrophosphate Synthase Complex with an Isopentenyl Pyrophosphate (E_value = 1.5E_23);-51% similar to PDB:1RQI Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate (E_value = 2.0E_23);-51% similar to PDB:1RQJ Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Risedronate (E_value = 2.0E_23);-49% similar to PDB:2H8O The 1.6A crystal structure of the geranyltransferase from Agrobacterium tumefaciens (E_value = 3.4E_23);","Residues 37 to 288 (E_value = 1.2e-38) place ANA_1610 in the polyprenyl_synt family which is described as Polyprenyl synthetase.","","pyrophosphate synthase (AB006850)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1611","1739637","1738024","1614","6.70","-0.86","55837","GTGAGCCCCTCAGCCACTGCCCCGATCGTCAACTGGGACGCCCTGACGCCGGTCCTCATCATCCTGGGCGCCGGTGTCCTGGGTGTCCTCGTGGAGGCCTTCATCGCTCGTCCTGCCCGTCTGGCCATCCAGTCCACGCTGAGCTTCCTGGCCATCCTGGCCTCCGGGGTCTCCCTGTTCCTGCGCTGGGGCGAGGTCAAGGCCGCCGGGGCCGCCGCCGCGGCCATACCCCAGTTCCAGCTCCCCAAGGGTTTCCTGCCGGGCGCCCGCATGTCCGCGGGCCTGACCGAGGACCCCTTCTCCATCGCCGCCCAGGGCATCCTCCTGGTCATCGGTCTGCTGGCCGTCCTGGTGATGGCCGACCGCACCTCCGTCGGCGACGGGGCCTTCGCGGCCCAGGCCGCCGACCGGCCCGGCAGCGCGGAGGAGAGCGAGTCCATCCTGGCCGGCTGGACTACGACCGAGATCTTCCCCCTGACCCTGTTCTCACTGGGCGGCATGATGCTCTTCGGGGCCAGCAGTGACCTCATCACGCTGTTCGTCATTCTGGAGATGATCTCCCTGCCGCTGTACATCCTGGCGGCCACCGCCCGCCACCGCCGGCTCCTCAGCCAGGAGGCGGCGCTGAAGTACTTCGTGCTGGGGGCCTTCGCCTCCGCCTTCCTCCTCATGGGCTCGGCCCTGCTCTACGGGGTGGCCGGCGCCGTCGACTACAAGACCCTGGGCGAGGCCGTGAGCAGCGCGGCGGGGCAGGACTGGCTCATCCTGGCCGGCCTCATGCTGGTGATCGTCGGCCTGCTGTTCAAGGTGGCGGCCGTGCCCTTCCACGCCTGGAGCCCGGACGTCTACCAGGGTGCCCCCACCCCGGTCACCGGGTTCATGGCCGCCGGCGTCAAGGCCGCCGCCTTCCTGGCCCTGGTGCGCTTCTACTACCTGATCGCCGGCGCCATGGGCTGGGACCTGGCCCCCGCCCTGTGGGCCGTGGCGGCACTGACCATGCTCCTGGGCACCGTCGTCGGGGTGGTTCAGCGCGACGTCAAGCGCATGCTCGCCTACTCGGCCATCGCCCACGCCGGCTTCATGCTCATCGGGATCGGGGCCTACTCCAAGGCGGCGATCTCCGCGCTCAGCTTCTACGCCCTGACCTACGGGATCGCCACCGTGGGGGCCTTCGGCATCGTCACCCTGGTGCGCTCCCACCGCGACGGCTCCGTGGGCGGCGAGGACGGCGACCTGGATGCCTTCAAGGGCCTGGGACGCCGCAGCCCCTGGGCGGCCGGTGCCATGACCGTCTTCCTGCTGTCCTTCGCCGGAGTGCCCCTGACGGCCGGCTTCATGGCCAAGTTCCGGCTCTTCGCCACCGGCCTGAGCGGCAACGGGACGCCCTTCGTCATCCTCGCCGTCGTCTGCTCGGCCGTGACCGCCTTCTTCTACATGAGGCTCATCGTGCTCATGTTCTTCCATGAGCCCGACGGCGAGCGCGCCGTGGTCGTGGACAGCCGCGGCCCGATCATCCTGGCAGTCAGCGTTGCGGTGATGGCCACAATCGGGTTGGGCATTTTGCCGCAGACCGCCTTCGACCTGTTCGACCAGACGGCTATGCTCCTTCCGTGA","VSPSATAPIVNWDALTPVLIILGAGVLGVLVEAFIARPARLAIQSTLSFLAILASGVSLFLRWGEVKAAGAAAAAIPQFQLPKGFLPGARMSAGLTEDPFSIAAQGILLVIGLLAVLVMADRTSVGDGAFAAQAADRPGSAEESESILAGWTTTEIFPLTLFSLGGMMLFGASSDLITLFVILEMISLPLYILAATARHRRLLSQEAALKYFVLGAFASAFLLMGSALLYGVAGAVDYKTLGEAVSSAAGQDWLILAGLMLVIVGLLFKVAAVPFHAWSPDVYQGAPTPVTGFMAAGVKAAAFLALVRFYYLIAGAMGWDLAPALWAVAALTMLLGTVVGVVQRDVKRMLAYSAIAHAGFMLIGIGAYSKAAISALSFYALTYGIATVGAFGIVTLVRSHRDGSVGGEDGDLDAFKGLGRRSPWAAGAMTVFLLSFAGVPLTAGFMAKFRLFATGLSGNGTPFVILAVVCSAVTAFFYMRLIVLMFFHEPDGERAVVVDSRGPIILAVSVAVMATIGLGILPQTAFDLFDQTAMLLP$","NADH dehydrogenase I chain N","Membrane, Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain 2[similarity]","proton-translocating NADH-quinone oxidoreductase; chain N ","proton-translocating NADH-quinone oxidoreductase, chain N","","Walker J.E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 1992. 25(3):253-324. PMID: 1470679Johns D.R., Berman J. Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem. Biophys. Res. Commun. 1991. 174(3):1324-1330. PMID: 1900003Brown M.D., Voljavec A.S., Lott M.T., Torroni A., Yang C.C., Wallace D.C. Mitochondrial DNA complex I and III mutations associated with Leber's hereditary optic neuropathy. Genetics 1992. 130(1):163-173. PMID: 1732158Wallace D.C., Singh G., Lott M.T., Hodge J.A., Schurr T.G., Lezza A.M., Elsas L.J., Nikoskelainen E.K. Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy. Science 1988. 242(4884):1427-1430. PMID: 3201231","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PS00622	$\"[171-198]?$	HTH_LUXR_1

InterPro
IPR001750
Domain

NADH/Ubiquinone/plastoquinone (complex I)
PF00361	$\"[173-455]T$	Oxidored_q1

InterPro
IPR003916
Family

NADH-ubiquinone oxidoreductase, chain 5
PR01434	$\"[265-286]T$ $\"[357-369]T$ $\"[467-486]T$	NADHDHGNASE5

InterPro
IPR010096
Family

Proton-translocating NADH-quinone oxidoreductase, chain N
TIGR01770	$\"[12-526]T$	NDH_I_N: proton-translocating NADH-quinone

noIPR
unintegrated

unintegrated
PTHR22773	$\"[155-527]T$	NADH DEHYDROGENASE
PTHR22773:SF41	$\"[155-527]T$	NADH DEHYDROGENASE SUBUNIT 2
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[14-36]?$ $\"[41-61]?$ $\"[100-120]?$ $\"[150-170]?$ $\"[176-196]?$ $\"[211-233]?$ $\"[255-275]?$ $\"[296-316]?$ $\"[322-342]?$ $\"[349-369]?$ $\"[379-397]?$ $\"[424-444]?$ $\"[463-483]?$ $\"[504-526]?$	transmembrane_regions

","BeTs to 15 clades of COG1007COG name: NADH:ubiquinone oxidoreductase subunit 2 (chain N)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1007 is ao-p-z-q-dr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003918 (NADH-ubiquinone oxidoreductase subunit 4 signature) with a combined E-value of 8e-11. IPB003918B 211-235 IPB003918C 284-308 IPB003918E 430-456***** IPB003916 (NADH-ubiquinone oxidoreductase chain 5 signature) with a combined E-value of 1.2e-10. IPB003916D 265-286 IPB003916E 288-314***** IPB002128 (NADH dehydrogenase (ubiquinone), chloroplast chain 5, C-terminal) with a combined E-value of 6.6e-10. IPB002128C 163-214 IPB002128D 263-317 IPB002128E 331-385","","","No significant hits to the PDB database (E-value < E-10).","Residues 173 to 455 (E_value = 1.1e-56) place ANA_1611 in the Oxidored_q1 family which is described as NADH-Ubiquinone/plastoquinone (complex I), various chains.","","dehydrogenase (ubiquinone) chain 2 [similarity] (420)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1612","1741235","1739634","1602","6.53","-2.18","55323","ATGCCGACTCTTCCCGCATCGCTGCCCGTCCTGACCGTCATGGCGGTCACGCCGCTGGCCGGGGCGCTCTTGCTGTGGCTGGTCCCGCCGCTGCGCCGGCTCCACGCCCGCGCCGTGGGCCTCGTGTTCTCCCTGGCGGTCCTCGCCCTGGGCCTGTGGGCGCTGAGCGCCTTCGATCTGGCTCAAGCCGGCACCGTCCAGCTGACCGACACCCACTCCTGGATCCCCGCCATCGGCGCCTCCTGGGCGCTGGGCGTCAACGGCCTGGGCCTGTCCATGGTGCTGCTGGGCGCCTTCGTCACGCCCTTGGTGCTGCTCGCCTCCTGGGGTGAGGTCCCCGCCGACCGACAGGGCCTGTTCACCGGGCTCGTCCTGACGCTGGAGTTCTTCATCGTCGTCATCTTCTCGGCCCGGGACCTGCTCCTGTTCTACCTGTGCTTCGAGGCGATGCTCATCCCGGTGTACTTCCTCATCGGCTGCTTCGGCGGGCAGAATCGCCAGCGCGCCGCCCTGAAGTTCCTCCTGTACTCCCTGGCCGGCGGGCTCATCATGCTCATCGGCGTCATTGCCGTCTCCCTGCACTCCGCCACGAACGGTGTCCCCAGCTTCCTCATCGACTCGGTGGCCGCAAACCTGCACGTGTCCACCTCCGCCGGTCACTGGATCTTCCTGACCTTCTTTATCGCCTTCGCCATCAAGGCGCCGCTGGTCCCGGTCCACACCTGGCTGCCCGACACCGCCGAGCAGGCCACCCCGGGCACCTCGGTGCTGCTCATCGGCATCCTCGACAAGATCGGCACCTTCGGGATGATTACCCTGGTCCTGCCGATCTTCCCGGAGGCCTCCCGCTGGGCCGCCCCGGTGATCCTGGTCCTGGCGGTCGTCTCCATCATCTACGGGGGCCTGGCCGCCATCGCCCAGGACAACCTCTACCGCCTCATCTCCTACACCTCCGTGAGTCACTTCGGCTTCATGGTCCTGGGGATCTTCATCGGCAACCAGGTGGCCGTCAACGGCGCCATGGTCTACATGGTGGCCCACGGGCTGTCCATTGCCGGCCTCTACCTGGTTACCGGCTTCATGGCCCGGCGCACCGGGACGGTCGCCATCAGCGAGCTCGGCGGCATCGCCCGGGTCATGCCGCTGGTGGCCGGCACCTTCCTGGTCAGCGGGCTGGCCTCCATCGCCCTGCCGGGCCTGAGCGGGTTCGTGCCCGAGTGGATGGTGCTCACCGGCACCTTCTCGGTCTCGCTGGCCCTGGGCGGTGCAGCCGTCGTCGGCGTCGTCATCGCCGCCGTCTACATGCTGCTGCCCTACCAGCGGGTCTTCACCGGGGCGCCCGCCCCCGAGCGCGTGGGCAGCCCCGACCTCGACGGGCGCGAGCGCCTCGTCGTCGTCCCCATCATCGCCGCGATGCTCGCGCTCGGACTGGCCCCGGGCGTCTTGACGTCCGCCTTCGACGACGTCGCCCGGCAGGCCGCGCTCACGGTCACCAGCTCCTCGCAGGCTGAGGCCTCAGCCCGCGGCGCCGGTGACAGCCCCGATGCCGGCGGGACTGACGCTCCCGCCGCCTCCACCGCTACGGAAGGGAACACCAAGTGA","MPTLPASLPVLTVMAVTPLAGALLLWLVPPLRRLHARAVGLVFSLAVLALGLWALSAFDLAQAGTVQLTDTHSWIPAIGASWALGVNGLGLSMVLLGAFVTPLVLLASWGEVPADRQGLFTGLVLTLEFFIVVIFSARDLLLFYLCFEAMLIPVYFLIGCFGGQNRQRAALKFLLYSLAGGLIMLIGVIAVSLHSATNGVPSFLIDSVAANLHVSTSAGHWIFLTFFIAFAIKAPLVPVHTWLPDTAEQATPGTSVLLIGILDKIGTFGMITLVLPIFPEASRWAAPVILVLAVVSIIYGGLAAIAQDNLYRLISYTSVSHFGFMVLGIFIGNQVAVNGAMVYMVAHGLSIAGLYLVTGFMARRTGTVAISELGGIARVMPLVAGTFLVSGLASIALPGLSGFVPEWMVLTGTFSVSLALGGAAVVGVVIAAVYMLLPYQRVFTGAPAPERVGSPDLDGRERLVVVPIIAAMLALGLAPGVLTSAFDDVARQAALTVTSSSQAEASARGAGDSPDAGGTDAPAASTATEGNTK$","NADH dehydrogenase I chain M","Membrane, Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain 4[similarity]","NADH dehydrogenase I chain M ","proton-translocating NADH-quinone oxidoreductase, chain M","","Walker J.E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 1992. 25(3):253-324. PMID: 1470679Wallace D.C., Singh G., Lott M.T., Hodge J.A., Schurr T.G., Lezza A.M., Elsas L.J., Nikoskelainen E.K. Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy. Science 1988. 242(4884):1427-1430. PMID: 3201231","","","

InterPro
IPR001750
Domain

NADH/Ubiquinone/plastoquinone (complex I)
PF00361	$\"[137-413]T$	Oxidored_q1

InterPro
IPR003918
Family

NADH-ubiquinone oxidoreductase, chain 4
PR01437	$\"[143-162]T$ $\"[173-197]T$ $\"[248-272]T$ $\"[336-355]T$ $\"[388-414]T$	NUOXDRDTASE4

InterPro
IPR010227
Family

Proton-translocating NADH-quinone oxidoreductase, chain M
TIGR01972	$\"[11-497]T$	NDH_I_M: proton-translocating NADH-quinone

noIPR
unintegrated

unintegrated
PTHR22773	$\"[106-484]T$	NADH DEHYDROGENASE
PTHR22773:SF40	$\"[106-484]T$	NADH DEHYDROGENASE SUBUNIT 4
signalp	$\"[1-63]?$	signal-peptide
tmhmm	$\"[10-28]?$ $\"[38-58]?$ $\"[89-109]?$ $\"[119-137]?$ $\"[143-163]?$ $\"[173-193]?$ $\"[221-239]?$ $\"[260-278]?$ $\"[284-304]?$ $\"[313-333]?$ $\"[339-359]?$ $\"[380-400]?$ $\"[414-434]?$ $\"[463-483]?$	transmembrane_regions

","BeTs to 13 clades of COG1008COG name: NADH:ubiquinone oxidoreductase subunit 4 (chain M)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1008 is -o-p---q-dr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003918 (NADH-ubiquinone oxidoreductase subunit 4 signature) with a combined E-value of 1.7e-39. IPB003918A 143-162 IPB003918B 173-197 IPB003918C 248-272 IPB003918D 336-355 IPB003918E 388-414***** IPB003916 (NADH-ubiquinone oxidoreductase chain 5 signature) with a combined E-value of 1.4e-08. IPB003916A 87-112 IPB003916D 229-250","","","-40% similar to PDB:2FYN Crystal Structure Analysis of the double mutant Rhodobacter Sphaeroides bc1 complex (E_value = );-66% similar to PDB:1Z98 Crystal structure of the spinach aquaporin SoPIP2;1 in a closed conformation (E_value = );-66% similar to PDB:2B5F Crystal structure of the spinach aquaporin SoPIP2;1 in an open conformation to 3.9 resolution (E_value = );-44% similar to PDB:1Z9J Photosynthetic Reaction Center from Rhodobacter sphaeroides (E_value = );","Residues 137 to 413 (E_value = 3.2e-59) place ANA_1612 in the Oxidored_q1 family which is described as NADH-Ubiquinone/plastoquinone (complex I), various chains.","","dehydrogenase (ubiquinone) chain 4 [similarity]","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1613","1743243","1741249","1995","7.18","1.01","70190","ATGCTTCCCGCTCCTGTCACCGCCGTCGTGACGCCCCTGACCGAGGCCACCGGCCTGGCCTCCTGGGCCTGGCTGCTCATCGCCGTCCCCGCGGCCTCCGCCGCCTTCCTGCTGCTGGCCGGCCGCCGCTCCAACGCCTGGGGCCACTGGCTGGGCCTGGCCGCCTCCTTCGCCGCCGCCTGCCTGGGCGTGGGCATCCTCGTGCAGGTCCTGGGCCTGCCCGCCGAGGAACGCGTCATCGGCCTGCCCCTCTACCACTGGTTCTCCGCCGGGAACCTGAGCGTCGACGTCGGCCTGCGCCTGGACCCGCTGTCGCTGACCTTCGTCACACTGGTCACCTGCGTCGGCTTCCTCATCCACCTGTACTCGGTGGCCTACATGGCCCACGACCGCGACCGGCGCCGCTTCTTCGCCTACCTCAACCTCTTCATCGCCGCGATGCTCACCCTGGTCCTGGGTGACTCCTACATCGTGCTCTTCGTCGGCTGGGAGGGCGTGGGCCTGGCCTCCTACCTGCTCATCGGCTTCTGGAACACCGCCGACGCCGACGCCCCCCAGGGCGAGCAGGCCACCAGCCGCGAGAACGCCGCCGCCGCCAAGAAGGCCTTCATCATGAACCGTGTGGGCGATGTCGGCCTCCTGCTGGCCATGATGACGATGGTCGGCCAAGTCGGCTCGGTCTCCTTCGACGCCGTCTCCGCCGCCTCCCTCGACGGCTCGGTGAGCACCGGCTGGCTCACTGCCATCGGCTTCTTCCTGCTCCTGGCGGCCTGCGGTAAGTCCGCCCAGTTCCCTCTCCAGGCCTGGCTGGGTGACGCCATGGCCGGCCCCACGCCGGTCTCGGCCCTCATCCACGCCGCCACCATGGTCACCGCGGGCGTCTACCTCATGGTCCGCTCCGCAGCGGTCTTCGAGGGTGCCCCGAGCGCCCAGACGGCCGTGGCTGTCATCGGCGCCATCACCCTGCTGCTGGGGGCCGTCATCGGAAGCGCCAAGGACGACATGAAGAAGGTCCTGGCCGCTTCCACCATGAGCCAGATCGGCTACATGATGCTGGGAGCGGGCCTGGGCCCGGTCGGCTACGCCTTCGCCATCTTCCACCTGCTCACCCACGGCTTCTTCAAGGCCCAGCTCTTCCTGGGGGCCGGCTCGGTCATGCACGCCATGGGCGACCAGGTCAACATGCGCCGCTTCGGTGGCCTGCGTGGCGCCATGGCGATCACCTGGGCCACCATGGGCATCGGCTGGCTCGCCATCCTGGGGGTGCCGCCCTTCTCCGGGTTCTGGTCCAAGGACCGCCTCATTGAGGCCGCCTTCGTCGGCGAGGGCGCCAAGCCCTGGATCCTGGGAACCATCGCCCTGCTGGGTGCGGGCCTGACCGCCTTCTACATGTCCCGCCTGTTCTTCATGATCTTCCACGGCAAGCAGCGCTGGACCACCAAGGACGACCTGGAGGGCGAGGTCCACCCCCACGAGTCCGGCTGGCTCATGACGCTGCCCCTGATTGTCCTGTCCGTGTTCTCCGCGGGCCTGGGCGGGCTGCTGACCTACAACAACATGTTCGTCACCTGGCTGGAGCCGGTCACCGGTCACGCCGAGCACGGCGAGCCGGTCCTGCCGGCCACCGTCATCATGGGCGCCACCCTCGCGCTGGTCGTCGTCGGGGTTCTCGTGGCCTGGTGGATGTACGTGCGCCGCCCGGTGCCCGTCGTCCTGCAGCCGGCCAACCCCCTGGTGGAGGCCGCCCGCAAGGACATGTACCAGGACGCCATCAACGAGGCCCTGGCCATGCGCACCGGCCAGGGACTGGTCCTGGCCACCGACGCCGTCGAGCGCTACGTCGTCGACGGCGCCATCGAGGGTGCCGCCGCGGGCACCGGCGCCCTGGGCCGCCTGACCCGCCGCACCGAGTCCGGGTACGTGCGCTCCTACGCCGGCTACATGCTGGCCGGAACGGTCCTCGTACTCATCGCCGTCCTGGCCGCCAGGTTCTGA","MLPAPVTAVVTPLTEATGLASWAWLLIAVPAASAAFLLLAGRRSNAWGHWLGLAASFAAACLGVGILVQVLGLPAEERVIGLPLYHWFSAGNLSVDVGLRLDPLSLTFVTLVTCVGFLIHLYSVAYMAHDRDRRRFFAYLNLFIAAMLTLVLGDSYIVLFVGWEGVGLASYLLIGFWNTADADAPQGEQATSRENAAAAKKAFIMNRVGDVGLLLAMMTMVGQVGSVSFDAVSAASLDGSVSTGWLTAIGFFLLLAACGKSAQFPLQAWLGDAMAGPTPVSALIHAATMVTAGVYLMVRSAAVFEGAPSAQTAVAVIGAITLLLGAVIGSAKDDMKKVLAASTMSQIGYMMLGAGLGPVGYAFAIFHLLTHGFFKAQLFLGAGSVMHAMGDQVNMRRFGGLRGAMAITWATMGIGWLAILGVPPFSGFWSKDRLIEAAFVGEGAKPWILGTIALLGAGLTAFYMSRLFFMIFHGKQRWTTKDDLEGEVHPHESGWLMTLPLIVLSVFSAGLGGLLTYNNMFVTWLEPVTGHAEHGEPVLPATVIMGATLALVVVGVLVAWWMYVRRPVPVVLQPANPLVEAARKDMYQDAINEALAMRTGQGLVLATDAVERYVVDGAIEGAAAGTGALGRLTRRTESGYVRSYAGYMLAGTVLVLIAVLAARF$","NADH dehydrogenase I chain L","Membrane, Cytoplasm","NADH-quinone oxidoreductase chain L (NADHdehydrogenaseI, chain L) (NDH-1, chain L)","proton-translocating NADH-quinone oxidoreductase; chain L ","proton-translocating NADH-quinone oxidoreductase, chain L","","Walker J.E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 1992. 25(3):253-324. PMID: 1470679Johns D.R., Berman J. Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem. Biophys. Res. Commun. 1991. 174(3):1324-1330. PMID: 1900003Brown M.D., Voljavec A.S., Lott M.T., Torroni A., Yang C.C., Wallace D.C. Mitochondrial DNA complex I and III mutations associated with Leber's hereditary optic neuropathy. Genetics 1992. 130(1):163-173. PMID: 1732158Wallace D.C., Singh G., Lott M.T., Hodge J.A., Schurr T.G., Lezza A.M., Elsas L.J., Nikoskelainen E.K. Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy. Science 1988. 242(4884):1427-1430. PMID: 3201231","","","

InterPro
IPR001516
Domain

NADH-Ubiquinone oxidoreductase (complex I), chain 5/L, N-terminal
PF00662	$\"[81-142]T$	Oxidored_q1_N

InterPro
IPR001750
Domain

NADH/Ubiquinone/plastoquinone (complex I)
PF00361	$\"[153-438]T$	Oxidored_q1

InterPro
IPR003916
Family

NADH-ubiquinone oxidoreductase, chain 5
PR01434	$\"[102-127]T$ $\"[130-150]T$ $\"[256-277]T$ $\"[278-304]T$ $\"[346-358]T$ $\"[453-472]T$	NADHDHGNASE5

InterPro
IPR003945
Family

NADH-plastoquinone oxidoreductase, chain 5
PR01435	$\"[104-124]T$ $\"[296-318]T$ $\"[452-474]T$ $\"[535-556]T$	NPOXDRDTASE5
TIGR01974	$\"[21-660]T$	NDH_I_L: proton-translocating NADH-quinone

noIPR
unintegrated

unintegrated
PTHR22773	$\"[85-659]T$	NADH DEHYDROGENASE
PTHR22773:SF39	$\"[85-659]T$	NADH DEHYDROGENASE SUBUNIT 5
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[19-41]?$ $\"[51-73]?$ $\"[104-124]?$ $\"[136-154]?$ $\"[160-180]?$ $\"[209-229]?$ $\"[235-257]?$ $\"[278-298]?$ $\"[312-332]?$ $\"[347-367]?$ $\"[373-391]?$ $\"[406-428]?$ $\"[447-469]?$ $\"[499-519]?$ $\"[538-558]?$ $\"[644-662]?$	transmembrane_regions

","BeTs to 17 clades of COG1009COG name: NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunitFunctional Class: C [Metabolism--Energy production and conversion] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1009 is ao-pkz-q-dr-bcefg-snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003916 (NADH-ubiquinone oxidoreductase chain 5 signature) with a combined E-value of 7.7e-66. IPB003916A 102-127 IPB003916B 130-150 IPB003916C 189-210 IPB003916D 256-277 IPB003916E 278-304 IPB003916F 346-358 IPB003916G 453-472***** IPB002128 (NADH dehydrogenase (ubiquinone), chloroplast chain 5, C-terminal) with a combined E-value of 1.5e-60. IPB002128B 86-140 IPB002128C 143-194 IPB002128D 254-308 IPB002128E 320-374 IPB002128H 489-520 IPB002128G 438-492***** IPB003918 (NADH-ubiquinone oxidoreductase subunit 4 signature) with a combined E-value of 3.9e-31. IPB003918A 159-178 IPB003918B 202-226 IPB003918C 275-299 IPB003918D 360-379 IPB003918E 413-439","","","No significant hits to the PDB database (E-value < E-10).","Residues 81 to 142 (E_value = 7.5e-21) place ANA_1613 in the Oxidored_q1_N family which is described as NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus.Residues 153 to 438 (E_value = 1.7e-82) place ANA_1613 in the Oxidored_q1 family which is described as NADH-Ubiquinone/plastoquinone (complex I), various chains.","","oxidoreductase chain L (NADH dehydrogenaseI, chain L) (NDH-1, chain L) (NQO12)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1614","1743566","1743261","306","8.84","1.16","10957","GTGAGTCTCCCCATCACCGTCTACCTCATCCTGGCCGGGGTGCTGTTCACCCTGGGGGCGCTCACGGTGCTGCTGCGCCGCAACGCCATCATCGAGCTCATGGGCGTTGAGCTCATGCTCAACTCCGTCAACCTCGTCCTGGTGACCTTCTCCCGGATCCACGGCAACCTCACCGGTCAGGTCTTCGCCTTCTTCGTCATGGTGGTGGCCGCCGCCGAGGTCGTGGTGGGTCTGAGCATCGTCGTATCCATCTTCCGCACCCGCAGGTCCACGTCGGTCGACGACGAGAACCTGCTCAAGAACTGA","VSLPITVYLILAGVLFTLGALTVLLRRNAIIELMGVELMLNSVNLVLVTFSRIHGNLTGQVFAFFVMVVAAAEVVVGLSIVVSIFRTRRSTSVDDENLLKN$","NADH dehydrogenase I chain K","Membrane, Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain 4L","NADH dehydrogenase I chain K ","NADH-ubiquinone oxidoreductase, chain 4L","","","","","

InterPro
IPR001133
Family

NADH-ubiquinone oxidoreductase, chain 4L
PF00420	$\"[7-101]T$	Oxidored_q2

InterPro
IPR003214
Domain

Mitochodrial NADH-ubiquinone oxidoreductase, chain 4L
PD000359	$\"[14-59]T$	Q6MGN5_BDEBA_Q6MGN5;

InterPro
IPR003215
Domain

NADH dehydrogenase (ubiquinone), type 1
PD002107	$\"[77-100]T$	Q6A6G8_PROAC_Q6A6G8;

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[62-82]?$	transmembrane_regions

","BeTs to 13 clades of COG0713COG name: NADH:ubiquinone oxidoreductase subunit 11 or 4L (chain K)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0713 is -o-p-z-q-dr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003215 (NADH dehydrogenase (ubiquinone), type 1) with a combined E-value of 3.7e-35. IPB003215A 15-51 IPB003215B 59-88***** IPB003214 (Mitochodrial NADH-ubiquinone oxidoreductase, chain 4L) with a combined E-value of 6.1e-26. IPB003214A 14-45 IPB003214B 63-101","","","-59% similar to PDB:1VA8 Solution structure of the PDZ domain of Pals1 protein (E_value = );","Residues 7 to 101 (E_value = 3.1e-30) place ANA_1614 in the Oxidored_q2 family which is described as NADH-ubiquinone/plastoquinone oxidoreductase chain 4L.","","dehydrogenase (ubiquinone) chain 4L (420)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1615","1744573","1743563","1011","8.17","2.13","34173","ATGAGCACCCTGCTGATGACCGGCGCCCCCGCCGTCGCTCCGACCGCCCTGACTCAGGATGGTCACCTGGGGCTGGGCGAGGCCATCGTCTTCGGCGTCGTCGCCCTGGTCACCGTGGCCTGCGGCATCGGCGTCCTGACCGCCAAGCGCGCTGTGAACGCCGCCATCAACATGATCGGCATCATGATCTCGCTGGCCGTCCTCTACATCGTCAACGAGTCGCCCTTCATGGGCATCACCCAGGTCGTGGTCTACACCGGCGCCGTCATGACCCTCGTCCTGTTCGTCATCATGCTCGTGGGCGTCGGCGGTGACGAGCCGGTGGGAGCCGCCGGCACCGTCATGAGGCGCCCGGTCCTTATCCTCCTGGGACTGGGGCTGGCCGGTGCCCTGACCGCCGTCGTGTGGCGCTCCACCCTACCGACGCCGGCCGGCCTCAAGGACGGTGCCAAGGCCGCCCCCGACCTGCTGGCCGTCACGCTCTACCACGACCACGTCGTCACCATGGAGCTGACCGCCATCCTGCTCATCGTCGCCGCCGTCGGCGCCCTGACCCTCACCCACCGCCAGCGCATCCGGGCCCGGCTCAGCCAGCGCGGAGTCGCCGCGAGCAAGATGCAGGACTACGCCGCCAAGGGTGCCCACCCGGGCCAGAAGCCGATGCCCGGCGTCTACGCCTCCACCAACTCCGCCGCCGCCCCGGCCCTGGACGCCCAGGGCGAGGCCGTCGAGGAGTCCGTGCCCCGGGTCCTGCGGGCCCGCGGCCAGGGCCTGGAGCTGTCGGACGTCTCCCCGGAGATGGGACTGGCCCAGCGCTCGGGCACGATCGTCTCCCGCCTGGCCGGTGCCGACCAGGCCGGCGCAGGCGACAGTACCCGGGGCCCCCGGGACGCCCGCCGCTCCGGGATGCCCTCCATGCCCGGCGCCGCCGCCCCCGCCGTCAAGCAGCCCGTCCTCAGCGATGACGGGGCAGCCGACTCGGCCGCCCCGGAGCAGAAGGAGGAGAAGTGA","MSTLLMTGAPAVAPTALTQDGHLGLGEAIVFGVVALVTVACGIGVLTAKRAVNAAINMIGIMISLAVLYIVNESPFMGITQVVVYTGAVMTLVLFVIMLVGVGGDEPVGAAGTVMRRPVLILLGLGLAGALTAVVWRSTLPTPAGLKDGAKAAPDLLAVTLYHDHVVTMELTAILLIVAAVGALTLTHRQRIRARLSQRGVAASKMQDYAAKGAHPGQKPMPGVYASTNSAAAPALDAQGEAVEESVPRVLRARGQGLELSDVSPEMGLAQRSGTIVSRLAGADQAGAGDSTRGPRDARRSGMPSMPGAAAPAVKQPVLSDDGAADSAAPEQKEEK$","NADH dehydrogenase I chain J","Membrane, Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain nuoJ","NADH dehydrogenase I chain J ","NADH-ubiquinone/plastoquinone oxidoreductase, chain 6","","","","","

InterPro
IPR001457
Family

NADH-ubiquinone/plastoquinone oxidoreductase, chain 6
PF00499	$\"[37-187]T$	Oxidored_q3

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[28-46]?$ $\"[51-71]?$ $\"[81-103]?$ $\"[118-138]?$ $\"[166-186]?$	transmembrane_regions

","BeTs to 14 clades of COG0839COG name: NADH:ubiquinone oxidoreductase subunit 6 (chain J)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0839 is ao-p-z-q-dr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB001457 (NADH-ubiquinone/plastoquinone oxidoreductase, chain 6) with a combined E-value of 2.3e-08. IPB001457 66-106","","","-44% similar to PDB:2NPG An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance (E_value = );-44% similar to PDB:2NPJ An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance (E_value = );-44% similar to PDB:2NPE An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance (E_value = );-44% similar to PDB:2NPK An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance (E_value = );","Residues 37 to 187 (E_value = 6.2e-17) place ANA_1615 in the Oxidored_q3 family which is described as NADH-ubiquinone/plastoquinone oxidoreductase chain 6.","","dehydrogenase (ubiquinone) chain nuoJ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1616","1745280","1744570","711","6.42","-2.59","26092","ATGACTGATCGCCCCCACCGTTCCCGGGGCTCGCAGCACGATAAGTGGCTGCGTGACGCTCCCTCCGCCCTGGCCCGCGCCTTCGCGCCCGTGGCCGGCTACGGGGTCACCATCTCCTCGATGTTCCGCCCCGTGGTCACCGAGCAGTACCCCTTCGAGCCGCCGCAGGTGATGCCCCGCTACCATGGTCGCCACCAGCTCAACCGCTACGACGACGGCCTGGAGAAGTGCATCGGTTGCGAGCTGTGCGCCTGGGCCTGCCCCGCCGACGCGATCTACGTCGAGGCCGCCTCCAACGAGCCCGGCGCCCAGTACTCGCCCGGCGAGCGCTACGGGCGCGTCTACCAGATCAACTACCTGCGCTGCATCTTCTGCGGCATGTGCATCGAGGCCTGCCCCACCCGGGCCCTGACCATGTCCACCGACTTCGATGAGCTCGTCGGCCCCGGCCGCGAGGGCCTCATCTATGAGAAGGAGGACCTGCTGGCCCCCGTGCCCGAGGGCGCCGTGTCCGCGCCCCACCCCATGGTCGAGGGCACCGAGGACGGCGACTACTACCGCGGGAAGGTCGTTGGCTCTACCCAGGCCCAGATCGACTGGGTGCGGAGCCACCGCCCCGAGGACCCCAGCCTGGAGTCCGCCCGAGCCAAGGCCGCCCCCACCGCCTCCGACCGGGGCAGCCGCCACACCGTGAAGGGAGCCCTGCGATGA","MTDRPHRSRGSQHDKWLRDAPSALARAFAPVAGYGVTISSMFRPVVTEQYPFEPPQVMPRYHGRHQLNRYDDGLEKCIGCELCAWACPADAIYVEAASNEPGAQYSPGERYGRVYQINYLRCIFCGMCIEACPTRALTMSTDFDELVGPGREGLIYEKEDLLAPVPEGAVSAPHPMVEGTEDGDYYRGKVVGSTQAQIDWVRSHRPEDPSLESARAKAAPTASDRGSRHTVKGALR$","NADH dehydrogenase I chain I","Cytoplasm, Extracellular","NADH-quinone oxidoreductase chain I (NADHdehydrogenaseI, chain I) (NDH-1, chain I)","NADH dehydrogenase I chain I ","NADH-quinone oxidoreductase, chain I","","George D.G., Hunt L.T., Yeh L.S., Barker W.C. New perspectives on bacterial ferredoxin evolution. J. Mol. Evol. 1985. 22(1):20-31. PMID: 3932661Otaka E., Ooi T. Examination of protein sequence homologies: V. New perspectives on evolution between bacterial and chloroplast-type ferredoxins inferred from sequence evidence. J. Mol. Evol. 1989. 29(3):246-254. PMID: 2506358Fukuyama K., Matsubara H., Tsukihara T., Katsube Y. Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 A resolution. Structural comparisons of bacterial ferredoxins. J. Mol. Biol. 1989. 210(2):383-398. PMID: 2600971Duee E.D., Fanchon E., Vicat J., Sieker L.C., Meyer J., Moulis J.M. Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution. J. Mol. Biol. 1994. 243(4):683-695. PMID: 7966291","","","

InterPro
IPR001450
Domain

4Fe-4S ferredoxin, iron-sulfur binding
PR00353	$\"[115-126]T$ $\"[127-138]T$	4FE4SFRDOXIN
PF00037	$\"[70-93]T$ $\"[115-138]T$	Fer4
PS00198	$\"[77-88]T$ $\"[122-133]T$	4FE4S_FERREDOXIN

InterPro
IPR010226
Family

NADH-quinone oxidoreductase, chain I
TIGR01971	$\"[33-161]T$	NuoI: NADH-quinone oxidoreductase, chain I

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.20	$\"[56-142]T$	no description
PTHR10849	$\"[33-162]T$	NADH-UBIQUINONE OXIDOREDUCTASE 1, CHAIN 1

","BeTs to 17 clades of COG1143COG name: Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1143 is aompkz-qvdr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB000813 (7Fe ferredoxin signature) with a combined E-value of 1.4e-09. IPB000813B 85-95 IPB000813C 117-134","","","-67% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 6.5E_37);","Residues 70 to 93 (E_value = 5.5e-06) place ANA_1616 in the Fer4 family which is described as 4Fe-4S binding domain.Residues 115 to 138 (E_value = 7.2e-09) place ANA_1616 in the Fer4 family which is described as 4Fe-4S binding domain.","","oxidoreductase chain I (NADH dehydrogenaseI, chain I) (NDH-1, chain I) (nuoI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1617","1746916","1745273","1644","4.45","-34.81","59041","GTGAACCCGATCTACGCGGCTCAGGCCGCTGCCGACGACGCCCTGCCCAACGGGGGCGTGACCGCCGACTTCTCCGCCGAGACCTGGTGGCTGACCCTCATCAAGGCCGGCTTCATCGTCGCCTTCCTCATCGTCAGCGTCATGATGGCGCTGTGGGTGGAGCGGCGCGGCCTGGCCCGCATGCAGACCCGCCTGGGCCCCAACGTCAACGGCCCCCTCGGCCTGCTCCAGGCAGTCGCCGACGCCGGCAAGCTCATCATGAAGGAGGACTTCTGGCTCAAGGGGGCCGAGAAGGTCATCTACCTCCTGGCGCCGCTCATCGCCGCCTTCAGCGCCTTCATGGTCTACGCGGTCATCCCCTTCGGGCCGCAGGTGAGCATCTTCGGCCACTCCACGCCCCTGCAGCTGACCGACTTCCCGGTGGCGGTCCTCTACATCCTGGCCATCACCGCCTTCGGCGTCTACGGGATCATCCTGGGCGGCTGGTCCACGCACTCCACCTACCCGCTCTTCGGTGCCGTGCGCAGCGCCGCTCAGGTCATCTCCTACGAGCTGAGCATGAGCCTGTCCATCCTCACGGTCTTCCTGGCCTCGGGGACCATGTCCACCTCCGGGATCGTGACCGCCCAGGAGCGCATCTGGTGGGCCGTGGCGATGCTGCCCAGCTTCGTCATCTACGTCATCTCCATGGTCGGTGAGGTCAACCGCCTCCCCTTCGACCTGCCCGAGGCAGAGGGCGAGCTCGTCGCCGGCCACATGGTCGAGTACTCCTCGATGAAGTTCGCCTGGTACTTCCTGGCCGAGTACATCAACATGTTCAACGTCTCGGCCGTGTGCGTCACCCTGTTCCTGGGCGGCTGGCGCTCGGCGATCCTCAGCCTGTTCTGGGAGGGCGCCAACTCCGGCTGGTGGCCGATGCTGTGGTTCGTCGCCAAGGTCTGGGCCGTCATGTTCTTCATGATCTGGACCCGCGGAACCCTCGTGCGCATCCGCTACGACCACTTCATGAAGCTGGGCTGGAAGGTCCTCATCCCGATCTCCCTGGTCTGGTTCGTGCTGGTGGCCGTGGTGCGCGCCTTCCGCACCTTCTCGGGCGCCTCCGTGCAGGCCCTGCTGCTGCCGATGGCCGTCGTGTTCTGCGTCATCATGTTCATCCTCTTCCTCATCCCCGACAAGGAGGAAGAGGAGGAGCTCTACGAGGACTATGAGGACTACGACGACGAGGATGCGGACGACGAGGACGTCGAGATCCTGGACGCCGAGGACGACCACGTCGCCTTCCTCGAGGGCTTCCCGGTCCCGCCGCCTCCGGGCAGCTCCCTGCCGCCCTCACCGCGCGCCCGCCGCGCCGCCCTGGCGGCGCAGGCGACCGACGCGGCCGGTGACTCCGAGACCGGGGCGGCCACCGCCGTCGGCCTCCTGGAGGACACCGACGTCGAGGATGACGACGCGGCCGGTTCCGCGGACTCCGCCGCCTCCGCCGGGTCCCCCGACTCGGCCGGTGTAGCCGGCACGGCAGTCCCGGCCGGTAAGGACGCCGCCACCGCCCTGCCCACCTTCACCCTTGACGTCAAGGCCGACCCGGCCGGCGGCAAGGACACAGACACGGCCGCTGAGGCACCCCAGGAGGGAAAAGATGACTGA","VNPIYAAQAAADDALPNGGVTADFSAETWWLTLIKAGFIVAFLIVSVMMALWVERRGLARMQTRLGPNVNGPLGLLQAVADAGKLIMKEDFWLKGAEKVIYLLAPLIAAFSAFMVYAVIPFGPQVSIFGHSTPLQLTDFPVAVLYILAITAFGVYGIILGGWSTHSTYPLFGAVRSAAQVISYELSMSLSILTVFLASGTMSTSGIVTAQERIWWAVAMLPSFVIYVISMVGEVNRLPFDLPEAEGELVAGHMVEYSSMKFAWYFLAEYINMFNVSAVCVTLFLGGWRSAILSLFWEGANSGWWPMLWFVAKVWAVMFFMIWTRGTLVRIRYDHFMKLGWKVLIPISLVWFVLVAVVRAFRTFSGASVQALLLPMAVVFCVIMFILFLIPDKEEEEELYEDYEDYDDEDADDEDVEILDAEDDHVAFLEGFPVPPPPGSSLPPSPRARRAALAAQATDAAGDSETGAATAVGLLEDTDVEDDDAAGSADSAASAGSPDSAGVAGTAVPAGKDAATALPTFTLDVKADPAGGKDTDTAAEAPQEGKDD$","NADH dehydrogenase I chain H","Membrane, Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain 1SC10A7.14c [similarity]","NADH dehydrogenase I chain H ","NADH dehydrogenase (quinone)","","","","","

InterPro
IPR001694
Family

Respiratory-chain NADH dehydrogenase, subunit 1
PTHR11432	$\"[62-357]T$	NADH DEHYDROGENASE SUBUNIT 1
PF00146	$\"[31-359]T$	NADHdh
PS00668	$\"[238-251]T$	COMPLEX1_ND1_2

noIPR
unintegrated

unintegrated
signalp	$\"[1-50]?$	signal-peptide
tmhmm	$\"[33-53]?$ $\"[100-120]?$ $\"[139-159]?$ $\"[180-198]?$ $\"[212-232]?$ $\"[269-291]?$ $\"[301-321]?$ $\"[342-360]?$ $\"[370-390]?$	transmembrane_regions

","BeTs to 15 clades of COG1005COG name: NADH:ubiquinone oxidoreductase subunit 1 (chain H)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1005 is ao-p-z-q-dr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB001694 (Respiratory-chain NADH dehydrogenase, subunit 1) with a combined E-value of 9.4e-84. IPB001694A 46-92 IPB001694B 145-199 IPB001694C 214-263 IPB001694D 320-348","","","No significant hits to the PDB database (E-value < E-10).","Residues 31 to 359 (E_value = 3.1e-114) place ANA_1617 in the NADHdh family which is described as NADH dehydrogenase.","","dehydrogenase (ubiquinone) chain 1 SC10A7.14c [similarity] (nuoH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1618","1749663","1746913","2751","5.29","-28.23","96446","ATGACTGCTGAGACGACCACCAAGAGCTCCGCACCCGCGGCGCCGCCGGCCCCCGAGATGGTCCACATGACCATTGACGGGCTGCCCGTCGAGGTCGAGAAGGGGACCCTCCTCATCCGTGCCGCTGAGCAGGTCGGCGTGCGCATCCCGCGCTTCTGCGACCACCCGCTGCTCGCGCCGTCGGCCAACTGCCGCCAGTGCCTGGTGGAGGTGGCCATGCCGGGGCGCGACGGCGTCGTGCGGCCCATGCCCAAGCCCCAGCCCTCCTGCGCCATGACCGCCATGGAGGGTATGGAGATCTCCACCCAGGCCACCAGCGAGGTCGCCGCCAAGGCCCAGGCCGGCACCATGGAGTTCCTCCTCATCAACCACCCGCTGGACTGCCCGGTGTGCGACAAGGGCGGCGAGTGCCCCCTGCAGAACCAGGCCCTGGAGCTCATGGCCTCCGGCGCCCAGTCCGCCACCCGCTTCACCGACGTCAAGCGCACCTTCCCCAAGCCGCTGCGCCTGACCAGCAACATCCTGCTGGACCGCGACCGCTGCATCCTGTGCCAGCGCTGCGTGCGCTTCGCCGACCAGATCCCCGGCGACCCCTTCATCGCCCTCCAGGGCCGTGGCGGCGGGCACCCCTCCTTCGACATGGACGGCGAGCCCGAGCACACCGGGGGCCTGTACTCCGAGCAGATCGGGCGCTTCGACGCCCGCGTCCTGGACTTCCACACCGAGGCGCCCCAGGAGGGGCTCGACGACGACCTCCAGACGATCCGTGGCGTGCCCTCCCTGAGCGCCCTGGGAGACCTGACCGGCCCCGGCGGCGAGCCCGGCGCCTCCGACGGCACCGACTACGGCCCCGACCTCGGCGCCGGCCGCGAGGACCTGGACGCCTCCGGGCGCCCCTTCGCCTCCTACTTCTCGGGCAACATCATCCAGATCTGCCCCGTGGGCGCCCTGACCTCCGCGAAGTACCGCTTCCGGGCCCGCCCCATGGACCTGGTCTCCACCGACTCCGTCACCGAGCACGACGCCTCCGGATCCGCCATCCGCGTCGACATGCGCCGCGGCGTCGTCCTGCGTCACCTCGCGGGCAACGACCCCGAGGTCAACGAGGAGTGGATCACCGACAAGGACCGCTTCGCCTTCACCTGGTCCTCCCAGCCCGACCGCCTCACCGTCCCGCTCGTGCGCGACGAGGAGACCGGCGAGCTCGTCACCACCTCCTGGTCCGATGCTCTGGACGTAGCCGCCCAGGGGCTGGCCCGTGCCGCCGCAGACGGGGGAGTGGGGCTCCTGCCCGGAGGCCGCCTCACCCTGGAGGACGCCTGGGCCTGGTCCCGCTTCGCCCGCACCGCCCTGGGCACCAACGACATCGACCAGCGCGTGCGCAGCCACAGCCAGGAGGAGGACTCCTTCCTGGCCGCCCGCGTGGCCGGCACCGGACTGGGCGCCGTCACCTACCGCCACCTGGAGCGGGCCGGACAGGTCCTGCTCCTGGGCCTGGAGCCCGAGGACGAGTGCGGCTCCCTGTTCCTGCGCCTGCGCAAGGGCGTGCGCGCCGGCGGCGTCAAGGTGGCCACCGTGACCACCTGCCTGAGCGCCGGCAGCCGCAAGCTCTCCGCCCAGGCCGTCCTCACCCCGCCCGGTGAGGAGGCCCGCGTCGTCGCCCACCTCAGCCAGACCCACCCCGAGCTCGTCGAGGCCCTGCGCTCCGACGGCGCCACCATCCTCATCGGTGAGCGCGCCGTCCGCGTCCCCGGCCTGCTGAGCGTCGCCGACGCCCTGGCCACCGCCACCGGCGCCCACCTGGCCTGGGTGCCGCGCCGCAGCGGCGAGCGCGGCGGCATCGAGGCGGGCCTGCTGCCCGGCCTCCTGCCCGGCGGTCGTCCCGTGGCCGACCCCGAGGCCCGCGCCCAGGTCGAGCAGGCCTGGAACCTGGGCCCCGAGCACCTCCTGCCCGCGACACCGGGCCGCGACGTCACCGCCATCCTCTCGGCGCTCCTGGAGGGGAGCCTGGGCGGCGCGGTTGTCGGCGGCATCGACCTGCGCGACTTCCCCGACCCGGGTCTGGCCCGCGCGGCCCTGGCCGCCAGTGGCTTCACCGTCCAGCTCGAGGTGCGCCGCAGCGAGGTCAGCGAGCACGCCGACGTCGTCCTGCCCGTGGCCCCGGCCGTGGAGAAGAACGGCACCTTCGTCAACTGGGAGGGGCGCGTGCGCCCCTTCGGCCAGGCCCACGTCTCGCGCTCGCGCACCGACCGCCAGGTCCTGGGCATGCTCGCCGACGAGATGGGGATGGACCTGCAGGTCGACGACCTGGTCGTCCTGCACGAGCAGCTCGCCGACCTGGGCCTGTGGCGCGGGCAGCGCCCGTCGGTCGCCTTCGGGCCCGCCCCGGCGGTCTGCGCCGGCGCCCCCGCCTCCGCCGACGACGGCGTCGAGGCCCGACTGACCACTCACAAGCCCATGCTCGACGCCGGGCGCCTCCAGGACGGTGAGCCCTTCCTGGCCGCCACCGCCCTGCGCCCCGTCGCCCGGGTGGGCGCCGACCTCGCCCAGCGCCTGTCGCTGGCAGCCGGCCAGGAGGTGACCGTGGCGACCGCCGCCGGATCCATCACCCTGCCGGCCGTCGTCGGCGGCGTCAGCGACGGCACCGTGTGGCTGCCCGAGTGCTCGGCCGGCTCCACCGTCCACCAGACCCTGGGCGCCGGGCACGGCTCCCAGGTCACCGTGACCCATGCAGCGGAGGTACTGAGGTGA","MTAETTTKSSAPAAPPAPEMVHMTIDGLPVEVEKGTLLIRAAEQVGVRIPRFCDHPLLAPSANCRQCLVEVAMPGRDGVVRPMPKPQPSCAMTAMEGMEISTQATSEVAAKAQAGTMEFLLINHPLDCPVCDKGGECPLQNQALELMASGAQSATRFTDVKRTFPKPLRLTSNILLDRDRCILCQRCVRFADQIPGDPFIALQGRGGGHPSFDMDGEPEHTGGLYSEQIGRFDARVLDFHTEAPQEGLDDDLQTIRGVPSLSALGDLTGPGGEPGASDGTDYGPDLGAGREDLDASGRPFASYFSGNIIQICPVGALTSAKYRFRARPMDLVSTDSVTEHDASGSAIRVDMRRGVVLRHLAGNDPEVNEEWITDKDRFAFTWSSQPDRLTVPLVRDEETGELVTTSWSDALDVAAQGLARAAADGGVGLLPGGRLTLEDAWAWSRFARTALGTNDIDQRVRSHSQEEDSFLAARVAGTGLGAVTYRHLERAGQVLLLGLEPEDECGSLFLRLRKGVRAGGVKVATVTTCLSAGSRKLSAQAVLTPPGEEARVVAHLSQTHPELVEALRSDGATILIGERAVRVPGLLSVADALATATGAHLAWVPRRSGERGGIEAGLLPGLLPGGRPVADPEARAQVEQAWNLGPEHLLPATPGRDVTAILSALLEGSLGGAVVGGIDLRDFPDPGLARAALAASGFTVQLEVRRSEVSEHADVVLPVAPAVEKNGTFVNWEGRVRPFGQAHVSRSRTDRQVLGMLADEMGMDLQVDDLVVLHEQLADLGLWRGQRPSVAFGPAPAVCAGAPASADDGVEARLTTHKPMLDAGRLQDGEPFLAATALRPVARVGADLAQRLSLAAGQEVTVATAAGSITLPAVVGGVSDGTVWLPECSAGSTVHQTLGAGHGSQVTVTHAAEVLR$","NADH dehydrogenase I chain G","Cytoplasm","NADH-quinone oxidoreductase, chain G","NADH-quinone oxidoreductase; chain G","NADH-quinone oxidoreductase, chain G","","Weiss H., Friedrich T., Hofhaus G., Preis D. The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 1991. 197(3):563-576. PMID: 2029890Guinebaut V., Vincentelli R., Mills D., Weiss H., Leonard K.R. Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction. J. Mol. Biol. 1997. 265(4):409-418. PMID: 9034360","","","

InterPro
IPR000283
Domain

Respiratory-chain NADH dehydrogenase 75 kDa subunit
PS00641	$\"[50-67]T$	COMPLEX1_75K_1
PS00642	$\"[128-140]T$	COMPLEX1_75K_2
PS00643	$\"[180-190]T$	COMPLEX1_75K_3

InterPro
IPR001041
Domain

Ferredoxin
PF00111	$\"[23-71]T$	Fer2

InterPro
IPR006656
Domain

Molybdopterin oxidoreductase
PF00384	$\"[388-426]T$ $\"[711-736]T$	Molybdopterin

InterPro
IPR006657
Domain

Molydopterin dinucleotide-binding region
PF01568	$\"[831-886]T$	Molydop_binding

InterPro
IPR010228
Family

NADH-quinone oxidoreductase, chain G
TIGR01973	$\"[23-757]T$	NuoG: NADH-quinone oxidoreductase, chain G

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.740	$\"[388-519]T$ $\"[612-780]T$	no description
PTHR11615	$\"[34-195]T$ $\"[278-532]T$ $\"[659-889]T$	NITRATE, FROMATE, IRON DEHYDROGENASE
PTHR11615:SF10	$\"[34-195]T$ $\"[278-532]T$ $\"[659-889]T$	NADH-UBIQUINONE OXIDOREDUCTASE

","BeTs to 12 clades of COG1034COG name: NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1034 is -------qvdr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB000283 (Respiratory-chain NADH dehydrogenase 75 kDa subunit) with a combined E-value of 4e-100. IPB000283A 25-64 IPB000283B 111-137 IPB000283C 170-196 IPB000283D 302-329 IPB000283E 341-387 IPB000283F 713-737***** IPB006655 (Prokaryotic molybdopterin oxidoreductase) with a combined E-value of 8.1e-09. IPB006655A 383-395 IPB006655B 397-421 IPB006655E 844-867","","","-53% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 1.5E_31);","Residues 23 to 96 (E_value = 4.3e-08) place ANA_1618 in the Fer2 family which is described as 2Fe-2S iron-sulfur cluster binding domain.Residues 388 to 760 (E_value = 3e-10) place ANA_1618 in the Molybdopterin family which is described as Molybdopterin oxidoreductase.Residues 831 to 886 (E_value = 4.2e-05) place ANA_1618 in the Molydop_binding family which is described as Molydopterin dinucleotide binding domain.","","oxidoreductase, chain G","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1619","1750998","1749667","1332","5.72","-8.80","47731","GTGAGTGACACCGCCACCTACACCGCGCCGGGGACCCTCACCCCGGTCCTGAGCGACCTGTGGGACCAGGAGCGCTCCTGGACCCTGCAGGCCTACCTCGACCACGGCGGCTACGAGGGCCTCAAGAAGGCCAAGACCCTCAGCTGCGAGGACCTCATCAGCCTCATCAAGGACTCCGGTCTGCGAGGACGCGGCGGCGCCGGCTTCCCCACGGGACTCAAGTGGTCCTTCCTGCCCCCGGTCGACGGCGGCCCGCGCTACCTCGTGGTCAACGCCGACGAGTCCGAGCCGGGCACCTGCAAGGACATCCCCACGATCATGTCCAACCCGCAGGCCCTCATCGAGGGCATCGCCATCACCTCGCGCGCCATCGGCGGCGACCACGCCTTCGTCTACCTGCGCGGCGAGGTCCCCCACGTCTACCGCCGCCTGCTCAGCGCCGTGCGCGAGGCCACCGAGTCCGGCCTGCTGGACACCGGCTTCGGGCTCGACGGCCAGCAGCGGCTGCGCATCACTGCCCACGCCGGTGCCGGCGCCTACATCTGCGGTGAGGAGACCGCCCTGCTGGACTCCCTGGAGGGCCGCCGCGGCCACCCCCGCCTCAAGCCGCCCTTCCCCGCCGTCGCTGGCCTCTACGCCCGGCCCACGGTGGTCAACAACGTCGAGACCATCGCCTCGGTCCCGGCGATCCTGGCCCGCGGCGCCCAGTGGTACTCCACCATGGGCACCGAGAAGTCCAAGGGCCACGGCATCTTCTCCGTCTCCGGCCACGTGGCCCACCCCGGCCAGTATGAGGCCCCCTTCGGCATCACCATGCGCGAGCTCATCGAGCTCTCCGGCGGCATCCGTCCCGGCCACGAGCTGAAGTTCTGGGTGCCGGGAGGCTCCTCGACGCCGATCTTCGGCCCCGATGAGCTCGACGTCCCCTTGGACTACGAGTCCGTGGCCGAGGCCGGCTCCATGCTGGGCACCCGCGCCCTGCAGGTCTTCGACGAGACCGTCTCCGTGGTGCGCGTGGTCACCCGCTGGACCGAGTTCTACCAGCACGAGTCCTGCGGCAAGTGCACCCCCTGCCGCGAGGGCACCTACTGGATGCGCCAGATCATGCTGCGTCTGGAGGCTGGTCGCGGTCTGCCCGGCGACGTCGAGAAGCTCGAGTCCATCGCCTCCAACATCGCCGGACGTTCCTTCTGCGCCCTGGGCGACGCCTCCGCCACCCCGGTCCTGACCGGCATCAAGCGGTTCCGCGAGGAGTTCGAGGCCGGCTACACCGCCGCCGCCGACGAGCTCTTCCCCTACGCCGCCTCCTCCGTCTTCGAAAGTGCACGGTGA","VSDTATYTAPGTLTPVLSDLWDQERSWTLQAYLDHGGYEGLKKAKTLSCEDLISLIKDSGLRGRGGAGFPTGLKWSFLPPVDGGPRYLVVNADESEPGTCKDIPTIMSNPQALIEGIAITSRAIGGDHAFVYLRGEVPHVYRRLLSAVREATESGLLDTGFGLDGQQRLRITAHAGAGAYICGEETALLDSLEGRRGHPRLKPPFPAVAGLYARPTVVNNVETIASVPAILARGAQWYSTMGTEKSKGHGIFSVSGHVAHPGQYEAPFGITMRELIELSGGIRPGHELKFWVPGGSSTPIFGPDELDVPLDYESVAEAGSMLGTRALQVFDETVSVVRVVTRWTEFYQHESCGKCTPCREGTYWMRQIMLRLEAGRGLPGDVEKLESIASNIAGRSFCALGDASATPVLTGIKRFREEFEAGYTAAADELFPYAASSVFESAR$","NADH dehydrogenase I chain F","Cytoplasm","NADH-quinone oxidoreductase, F subunit","NADH-quinone oxidoreductase; F subunit ","NADH-quinone oxidoreductase, F subunit","","Weiss H., Friedrich T., Hofhaus G., Preis D. The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 1991. 197(3):563-576. PMID: 2029890","","","

InterPro
IPR000209
Domain

Peptidase S8 and S53, subtilisin, kexin, sedolisin
PS00136	$\"[154-164]?$	SUBTILASE_ASP

InterPro
IPR001949
Family

Respiratory-chain NADH dehydrogenase, 51 kDa subunit
PS00644	$\"[176-191]T$	COMPLEX1_51K_1
PS00645	$\"[350-361]T$	COMPLEX1_51K_2

InterPro
IPR011537
Family

NADH-quinone oxidoreductase, F subunit
TIGR01959	$\"[16-423]T$	nuoF_fam: NADH-quinone oxidoreductase, F su

InterPro
IPR011538
Domain

Respiratory-chain NADH dehydrogenase domain, 51 kDa subunit
PF01512	$\"[36-296]T$	Complex1_51K

noIPR
unintegrated

unintegrated
PTHR11780	$\"[25-429]T$	NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 (NDUFV1)

","BeTs to 11 clades of COG1894COG name: NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1894 is --m----qvdr--cef--sn-jx---Number of proteins in this genome belonging to this COG is 1","***** IPB001949 (Respiratory-chain NADH dehydrogenase, 51 kDa subunit) with a combined E-value of 1.5e-147. IPB001949A 49-78 IPB001949B 87-120 IPB001949C 176-219 IPB001949D 230-282 IPB001949E 287-303 IPB001949F 323-364 IPB001949G 394-418","","","-62% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 1.3E_101);-41% similar to PDB:1UVQ CRYSTAL STRUCTURE OF HLA-DQ0602 IN COMPLEX WITH A HYPOCRETIN PEPTIDE (E_value = 1.3E_101);","Residues 36 to 296 (E_value = 3e-131) place ANA_1619 in the Complex1_51K family which is described as Respiratory-chain NADH dehydrogenase 51 Kd subunit.","","oxidoreductase, F subunit (nuoF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1620","1751765","1750995","771","4.75","-14.20","27268","ATGAGCACCACCGAGAACACAGTCAACCCGGCCGTCGAGACCATCGCCACCGTCAGTGCGGTCGGCCCGGTGGGCACCGTCGCGCAAGCCGCCGTGGCCGCCGGCTACAGCTCAGAGGTCGCCCAGAGCCTGCAGGTCGACATCGAGCGGATCATCGCCCGCTACCCGGCGGGCAAGGAGCGCAGCGCCCTCATCCCGATGCTCCACCTCATTCAGTCCGTGGACGGCTATGTCTCGCCGGCCGGCATCGCCCTGTGCGCCGCCCGGCTCGGTCTGGAGCGGGCCGAGGTCAGCGCCGTGGCCACCTTCTACAGTCAGTTCCGCCGCCACCCGGTGGGCACGTACCACGTGGGCGTGTGCACCAACGCCCTGTGCGCCGTCATGGGTGGGGACGAGATCTGGAAGGCGGTCACCGAGCACACCGGCCTGGGCGCCGAGGAGACCAGCGAGGACGGCACCATCAGCCTCGAGCGCGTCGAGTGCAACGCCGCCTGCGACTACGCCCCCGTCGTCATGGTCAACTGGGAGTTCTTCGACAACCAGACCCCCGACTCCGCCGTCGCCATGATCAAGGCCCTCGAGCGCGGCGAGGACGTCGCCCCCACCCGCGGCCCCGAGACCGTCCCCACCTTCCGCGAGAACGAGCGCCTGCTGGCCGGCTTCGAGGACGGCCGCACCGACGAGGGGCGCGGCCCCGGCGAGCCGACCCTGCGCGGCCTGAGCATCGCCCGTGAGCAGGGCTGGACCGCGCCGAAGGAGGAGACCAAGTGA","MSTTENTVNPAVETIATVSAVGPVGTVAQAAVAAGYSSEVAQSLQVDIERIIARYPAGKERSALIPMLHLIQSVDGYVSPAGIALCAARLGLERAEVSAVATFYSQFRRHPVGTYHVGVCTNALCAVMGGDEIWKAVTEHTGLGAEETSEDGTISLERVECNAACDYAPVVMVNWEFFDNQTPDSAVAMIKALERGEDVAPTRGPETVPTFRENERLLAGFEDGRTDEGRGPGEPTLRGLSIAREQGWTAPKEETK$","NADH dehydrogenase I chain E","Cytoplasm","NADH-quinone oxidoreductase chain E (NADHdehydrogenaseI, chain E) (NDH-1, chain E)","NADH-quinone oxidoreductase chain E ","NADH-quinone oxidoreductase, E subunit","","","","","

InterPro
IPR002023
Family

NADH dehydrogenase (ubiquinone), 24 kDa subunit
PD003859	$\"[49-105]T$	NUOE_MYCTU_P95177;
PTHR10371	$\"[48-243]T$	NADH-UBIQUINONE OXIDOREDUCTASE 24 KDA SUBUNIT
PF01257	$\"[39-194]T$	Complex1_24kDa
TIGR01958	$\"[47-194]T$	nuoE_fam: NADH-quinone oxidoreductase, E su

","BeTs to 11 clades of COG1905COG name: NADH:ubiquinone oxidoreductase 24 kD subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1905 is --m----qvdr--cef--sn-jx---Number of proteins in this genome belonging to this COG is 1","***** IPB002023 (NADH dehydrogenase (ubiquinone), 24 kDa subunit) with a combined E-value of 3.5e-47. IPB002023A 60-71 IPB002023B 72-120 IPB002023C 141-183","","","-56% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 1.2E_23);","Residues 39 to 194 (E_value = 7.9e-38) place ANA_1620 in the Complex1_24kDa family which is described as Respiratory-chain NADH dehydrogenase 24 Kd subunit.","","oxidoreductase chain E (NADH dehydrogenaseI, chain E) (NDH-1, chain E) (Nuo)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1621","1753153","1751765","1389","5.45","-13.23","50784","ATGAGCACCGCACGCACCTTCCGCGCCTCCGGCCCCGCCACGGACGAGCTGTCCGCCGGCGCCGAGCAGTTCACCGTCAGCGGCGGGGACTGGGACGACGTCGTCGCCCAGATCGCCGAGCGCGACGAGGCCGACCGCCTGCGCAACGACCGGATCGTCCTCAACATGGGTCCGGTCCACCCCTCCACCCACGGCGTGCTGCGCCTGGTCCTGGAGGCCGACGGCGAGGTCGTCACCGAGGTCCGCGTCGGAACCGGCTACCTGCACACCGGTATCGAGAAGAACATGGAGTACCGCACCTGGGTGCAGGGCGAGACCTTCGTGACCCGCATGGACTACGTGGCCCCCTTCTTCCAGGAAGTCGCCTACGCGCTCGCCGTCGAGAAGCTCCTGGGCATCACCGACGACATCCCGGAGAAGGCCACCGTCACCCGTGTGCTGCTCATGGAGCTCAACCGCATCGCCTCCCACGTCGTGGCCGTGGGCACCGGGGGCAACGAGATGGGCGGCACCACGCTCATGACCATCGCCTTCCGCTGCCGCGAGAACATCCTCAAGGCCTTCGAGATGGTCTCCGGGCTGCGCATGAACCACGCTTACATCCGTCCCGGGGGCCTGGCCCAGGACATCCCCGAGGGCTTCACCGAGTTCGTGCGCTCGGTCATGCCGGACATGAAGAAGGACATCCACGAGCTCGAGCTGCTGCTCCTGGAGAACCCGATCCTCAAGTCCCGCTTCATCGGCGTGGGGGAGATCAGCCTGGCCGGCGGGCTCGCCCTGGGCCTGACCGGGCCCTGCCTGCGCGCGGCCGGCTACCCGCTGGACCTGCGACGCACCAACCCATACTGCGGCTACGAGACCTACGACTTCCGGGTCCCCACCTACCGGGTCTCCGACTGCTACAACCGCCTGCGGATCCGCCTGGACGAGGCCTACGAGTCCCTCAAGATCGTCTCCCAGTGCCTGGACCGCCTCGAGGAGATCGCCGCCCGCGGCGACGACCCCTCCAACACCACGATGGTGGCCGACCCGACCATCGCCTGGCCCGCCCGCATGTCCATCGCCACCGACGGCCAGGGCCAGTCCCTGGAGCACGTGCGCGAGATCATGGGCAGCTCCATGGAGTCCCTCATCCACCACTTCAAGCTGGTGACTCAGGGCTTCCGAGTCCCGGCCGGGCAGGTCTACCAGACCGTTGAGCACGCCAAGGGGATCCTGGGCGTCCACGCCGTCTCCGACGGCGGCACCCGCCCCTACCGGGTCCACTTCCGCGACCCCTCCTTCTCCAACCTGCAGTCGCTGGCCATGATGGGGGAGGGCGGCATGATTGCCGACCTCGTGCCCACCCTGGCCTCCATCGACCCCGTCCTGGGAGGCGTGGACCGCTGA","MSTARTFRASGPATDELSAGAEQFTVSGGDWDDVVAQIAERDEADRLRNDRIVLNMGPVHPSTHGVLRLVLEADGEVVTEVRVGTGYLHTGIEKNMEYRTWVQGETFVTRMDYVAPFFQEVAYALAVEKLLGITDDIPEKATVTRVLLMELNRIASHVVAVGTGGNEMGGTTLMTIAFRCRENILKAFEMVSGLRMNHAYIRPGGLAQDIPEGFTEFVRSVMPDMKKDIHELELLLLENPILKSRFIGVGEISLAGGLALGLTGPCLRAAGYPLDLRRTNPYCGYETYDFRVPTYRVSDCYNRLRIRLDEAYESLKIVSQCLDRLEEIAARGDDPSNTTMVADPTIAWPARMSIATDGQGQSLEHVREIMGSSMESLIHHFKLVTQGFRVPAGQVYQTVEHAKGILGVHAVSDGGTRPYRVHFRDPSFSNLQSLAMMGEGGMIADLVPTLASIDPVLGGVDR$","NADH dehydrogenase I chain D","Cytoplasm","NADH dehydrogenase I, D subunit","NADH dehydrogenase I; D subunit ","NADH dehydrogenase I, D subunit","","Fearnley I.M., Walker J.E. Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim. Biophys. Acta 1992. 1140(2):105-134. PMID: 1445936Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J. Mol. Biol. 1993. 233(1):109-122. PMID: 7690854","","","

InterPro
IPR001135
Domain

NADH-ubiquinone oxidoreductase, chain 49kDa
PF00346	$\"[167-462]T$	Complex1_49kDa

InterPro
IPR010219
Domain

NADH dehydrogenase I, D subunit
TIGR01962	$\"[50-462]T$	NuoD: NADH dehydrogenase I, D subunit

InterPro
IPR014029
Domain

NADH-ubiquinone oxidoreductase, chain 49kDa, conserved region
PS00535	$\"[88-99]?$	COMPLEX1_49K

InterPro
IPR014363
Family

[NiFe]-hydrogenase-3-type complex, chloroplast NADPH-quinone oxidoreductase NuoD
PIRSF000230	$\"[52-462]T$	[NiFe]-hydrogenase-3-type complex, large subunit/NADH:quinone oxidoreductase (complex I), subunit 49K/NdhH/NuoD

noIPR
unintegrated

unintegrated
G3DSA:1.10.645.10	$\"[65-455]T$	no description
PIRSF500036	$\"[21-462]T$	NADH:quinone oxidoreductase (complex I), subunit 49kD/NdhH/NuoD
PTHR11993	$\"[48-353]T$ $\"[370-462]T$	NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT

","BeTs to 17 clades of COG0649COG name: NADH:ubiquinone oxidoreductase 49 kD subunit 7Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0649 is ao-pkz-qvdr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB014029 (NADH-ubiquinone oxidoreductase, chain 49kDa, conserved region) with a combined E-value of 6.9e-123. IPB014029A 54-107 IPB014029B 115-169 IPB014029C 182-213 IPB014029D 242-293 IPB014029E 373-387 IPB014029F 412-462***** IPB001135 (NADH-ubiquinone oxidoreductase, chain 49kDa) with a combined E-value of 2.2e-99. IPB001135A 66-114 IPB001135B 130-182 IPB001135C 245-292 IPB001135D 298-328 IPB001135E 396-430 IPB001135F 443-462","","","-57% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 2.1E_84);-46% similar to PDB:1FRV CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE (E_value = 2.1E_84);-46% similar to PDB:1YQ9 Structure of the unready oxidized form of [NiFe] hydrogenase (E_value = 2.1E_84);-46% similar to PDB:2FRV CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE (E_value = 2.1E_84);","Residues 167 to 462 (E_value = 7.3e-77) place ANA_1621 in the Complex1_49kDa family which is described as Respiratory-chain NADH dehydrogenase, 49 Kd subunit.","","dehydrogenase I, D subunit (nuoD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1622","1753929","1753153","777","5.11","-15.97","28192","ATGAGTGAGAAGAACACCCCGGCACACGACTCAGGCTCCGAGGCCCTGACCGAGACTCCCGAGGCCCCCGCCGTCCCCGAGGTCGCCGGCACCCCCGTGCGCCCCGAGCTGCGCCTGGAGGTCATCACCGCTCCCACCGGCCAGTTCGGCGCCTCCGACGCAGGCGACACCACCGGCTACGGCGAGCACCGCAGCGTCGTCACCCTCGCCCCCGCCGCCGCGCGCCCCTACGGCGGCTGGTTCGACGACGTCGTCGACGCCCTCATCGAGGATCTCCAGGAGGCCGGCATCGACCCGGCCGCCGCCATCGAGAAGGTCGTCATCGAGCACGGCGAGCTCACCCTGTTCATCGCCCGCGAGCACCTACTCCACGTCGCCCGCCCCCTGCGCGACGACCAGGACCTGCGCTTCGAGCTGTGCCTGGGCGTCAGCGGCGTCCACTACCCCGAGCTGGCCGGGCGCGAGCTGCACGCCTGCATCCAGCTCATGAGCCTGACCCACGGCGGACGCCAGCTGCGCCTGCAGGTCGCCTGCCCCGAGAGTGACCCGCACGTGCCCTCCCTCGTCTCGCTCTACCCCGGCAACGACTGGCACGAGCGCGAGACCTGGGACCTCATGGGCATCGTCTTCGACGGCCACCCCCACCTGACCCGCACCGCCATGCCCGACGACTGGGTGGGCCACCCCCAGCGCAAGGACTACCCGCTGGGCGGCATCCCCGTCGAGTACAAGGGCGCCCAGACCCCGCCCGCCGACACCCGGAGGTCCTACCGCTGA","MSEKNTPAHDSGSEALTETPEAPAVPEVAGTPVRPELRLEVITAPTGQFGASDAGDTTGYGEHRSVVTLAPAAARPYGGWFDDVVDALIEDLQEAGIDPAAAIEKVVIEHGELTLFIAREHLLHVARPLRDDQDLRFELCLGVSGVHYPELAGRELHACIQLMSLTHGGRQLRLQVACPESDPHVPSLVSLYPGNDWHERETWDLMGIVFDGHPHLTRTAMPDDWVGHPQRKDYPLGGIPVEYKGAQTPPADTRRSYR$","NADH dehydrogenase I chain C","Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain nuoC","NADH dehydrogenase I chain C ","NADH (or F420H2) dehydrogenase, subunit C","","","","","

InterPro
IPR001268
Domain

NADH dehydrogenase (ubiquinone), 30 kDa subunit
PD001581	$\"[192-238]T$	NUOC_MYCTU_P95179;
PF00329	$\"[174-242]T$	Complex1_30kDa

InterPro
IPR010218
Domain

NADH (or F420H2) dehydrogenase, subunit C
TIGR01961	$\"[113-238]T$	NuoC_fam: NADH (or F420H2) dehydrogenase, s

noIPR
unintegrated

unintegrated
PTHR10884	$\"[96-240]T$	NADH-UBIQUINONE OXIDOREDUCTASE-RELATED
PTHR10884:SF4	$\"[96-240]T$	NADH-UBIQUINONE OXIDOREDUCTASE-RELATED

","BeTs to 15 clades of COG0852COG name: NADH:ubiquinone oxidoreductase 27 kD subunitFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0852 is ao-pkz-qvdr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB001268 (NADH dehydrogenase (ubiquinone), 30 kDa subunit) with a combined E-value of 1.2e-30. IPB001268 185-234","","","-55% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 4.3E_16);","Residues 174 to 242 (E_value = 1.2e-33) place ANA_1622 in the Complex1_30kDa family which is described as Respiratory-chain NADH dehydrogenase, 30 Kd subunit.","","dehydrogenase (ubiquinone) chain nuoC","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1623","1754519","1753926","594","7.78","1.99","21399","ATGGCGTCCATCCCGTCCAAGCGGAATGACCCCTACGCCGCCGCTGCCGCCGAGGTGGACAGCCCGGGCTTCCTGCTGACCACCGTCGAGAAGCTCGCGGGCCTGGCCCAGGCCCGCTCCATGTGGCCCGTCACCATGGGCCTGGCCTGCTGCGCCATCGAGATGATGGCCGCCGGCACCCCCCGCTTCGACATGGCCCGCTTCGGTTGGGAGGTCTTCCGCGCCTCCCCGCGCCACGCCGACGTCATGATCGTCTCGGGCCGCGTCTCCCACAAGATGGCCCCCATCGTGCGCAACGTCTACGACTCCATGCCCGAGCCCAAGTGGGTCATCTCCATGGGGGCCTGCGCCTCCTCAGGAGGCATCTTCAACAACTACGCCGTCGTCCAGGGCTGCGACCACATCGTCCCGGTGGACATCTACCTGCCGGGCTGCCCGCCGCGCCCCGAGATGCTCCTCAACGCCATGCTCGAGCTCACCCGCCAGATCGAGAAGAAGCCGCTGTTCAAGCACCGCGAGGAGATCGCCCGCGCCGTCGAGGCCGCCGCGCTGTCGGCCACCCCCACCCATGAGATGAAGGGCCTGCTGGCATGA","MASIPSKRNDPYAAAAAEVDSPGFLLTTVEKLAGLAQARSMWPVTMGLACCAIEMMAAGTPRFDMARFGWEVFRASPRHADVMIVSGRVSHKMAPIVRNVYDSMPEPKWVISMGACASSGGIFNNYAVVQGCDHIVPVDIYLPGCPPRPEMLLNAMLELTRQIEKKPLFKHREEIARAVEAAALSATPTHEMKGLLA$","NADH dehydrogenase I chain B","Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain nuoB","NADH dehydrogenase I chain B ","NADH-quinone oxidoreductase, B subunit","","Arizmendi J.M., Runswick M.J., Skehel J.M., Walker J.E. NADH: ubiquinone oxidoreductase from bovine heart mitochondria. A fourth nuclear encoded subunit with a homologue encoded in chloroplast genomes. FEBS Lett. 1992. 301(3):237-242. PMID: 1577158","","","

InterPro
IPR006137
Domain

NADH ubiquinone oxidoreductase, 20 kDa subunit
PF01058	$\"[53-160]T$	Oxidored_q6

InterPro
IPR006138
Family

NADH dehydrogenase (ubiquinone), 20 kDa subunit
TIGR01957	$\"[23-166]T$	nuoB_fam: NADH-quinone oxidoreductase, B su
PS01150	$\"[131-147]T$	COMPLEX1_20K

InterPro
IPR014406
Family

[NiFe]-hydrogenase-3-type complex, small subunit/NADH:quinone oxidoreductase, subunit PSST/NdhK/NuoB
PIRSF002913	$\"[26-191]T$	[NiFe]-hydrogenase-3-type complex, small subunit/NADH:quinone oxidoreductase (complex I), subunit PSST/NdhK/NuoB
PTHR11995	$\"[24-177]T$	NADH DEHYDROGENASE

InterPro
IPR014659
Family

NADH:quinone oxidoreductase, subunit PSST/NdhK/NuoB
PIRSF500035	$\"[24-194]T$	NADH:quinone oxidoreductase (complex I), subunit PSST/NdhK/NuoB

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.700	$\"[32-170]T$	no description
PTHR11995:SF2	$\"[24-177]T$	NADH-PLASTOQUINONE OXIDOREDUCTASE

","BeTs to 16 clades of COG0377COG name: NADH:ubiquinone oxidoreductase 20 kD subunit and related Fe-S oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0377 is ao-pkz-qvdr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB006138 (NADH dehydrogenase (ubiquinone), 20 kDa subunit) with a combined E-value of 9.1e-79. IPB006138A 35-85 IPB006138B 91-117 IPB006138C 118-163 IPB006138A 36-86","","","-79% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = 2.0E_54);","Residues 53 to 160 (E_value = 7.6e-58) place ANA_1623 in the Oxidored_q6 family which is described as NADH ubiquinone oxidoreductase, 20 Kd subunit.","","dehydrogenase (ubiquinone) chain nuoB (NQO6)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1624","1754962","1754603","360","7.18","0.13","13027","ATGAACCCCTACGCCTCCCTGCTCATCATGGCCGCGCTGGCCCTCCTGGTGGCCGTCGGCGGTCTGGCCATGAGCGCCATCATCAGCCCCGCCCGGCGCAACCGGGTCAAGGTCGCCAACTACGAGTGCGGCATCGACCCCACCCCCGCCAACACCGAGCACGGGCGCTTCCCCGTCTCCTTCTACCTGGTGGGCATGACCTTCATCATCTTCGATGTCGAGGTGGTCTTCCTCTACCCCTGGGCCACAGCCTTCGGGCGCCTGGGCTTCTTCGGGCTGGGGGCGGCCGTCCTGTTCATCGGCCTCATCACCGTGCCCTACATCCTCGAGTGGCGTCGCGGCGGACTGGACTGGGACTGA","MNPYASLLIMAALALLVAVGGLAMSAIISPARRNRVKVANYECGIDPTPANTEHGRFPVSFYLVGMTFIIFDVEVVFLYPWATAFGRLGFFGLGAAVLFIGLITVPYILEWRRGGLDWD$","NADH dehydrogenase I chain A","Membrane, Cytoplasm","NADH2 dehydrogenase (ubiquinone) chain 3[similarity]","putative NADH dehydrogenase chain A ","NADH-ubiquinone/plastoquinone oxidoreductase, chain 3","","","","","

InterPro
IPR000440
Family

NADH-ubiquinone/plastoquinone oxidoreductase, chain 3
PTHR11058	$\"[10-119]T$	NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3
PF00507	$\"[16-118]T$	Oxidored_q4

noIPR
unintegrated

unintegrated
PTHR11058:SF4	$\"[10-119]T$	NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3 (PROKARYOTIC AND PLANT)
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[59-79]?$ $\"[89-109]?$	transmembrane_regions

","BeTs to 13 clades of COG0838COG name: NADH:ubiquinone oxidoreductase subunit 3 (chain A)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0838 is -o-p---q-dr--cef--snujx---Number of proteins in this genome belonging to this COG is 1","***** IPB000440 (NADH-ubiquinone/plastoquinone oxidoreductase, chain 3) with a combined E-value of 4.7e-18. IPB000440A 38-78 IPB000440B 99-118","","","No significant hits to the PDB database (E-value < E-10).","Residues 16 to 118 (E_value = 1.7e-30) place ANA_1624 in the Oxidored_q4 family which is described as NADH-ubiquinone/plastoquinone oxidoreductase, chain 3.","","dehydrogenase (ubiquinone) chain 3 [similarity] (nuoA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1625","1756260","1754959","1302","9.58","10.60","46020","GTGACCCAGGCAGCCGCCCAGTCCAGCGCCTCCGCCTCTGCCGACGTCATCGTCGTCGGGGCCGGCCCGGCCGGATCCTCGGCGGCCTACCACATGGCCACACTCGGTCTCGACGTCATCCTTCTGGAGAAGCAGGAGCTCGGCCGGGACAAGGTCTGTGGGGACGGCCTGACCCCCTCGGCCGTGCGCGAGCTGGTCTCCATGGGTATGGACACCACCGGCTGGCAGCGCAACCGCGGCCTGCGTGTCATCGGCGGCGGGCACCTCCTTCACTTCCCCTGGCCCGAGCAGGCCTCCTTCCCCTCCTACGGGATGGCCCGACCCCGCGCCCTGCTCGACCGTGACCTGGCTGAGCACGCCGCCGCGGCCGGCGCCCGTCTGCTCACCGGCGTCACCGTCACCGCCCCCGTCACCTCACCCACCGGCCGGGTCACCGGCGTCGAGGCCCGCCCCACCAACCGGGTCGCCTACCCCGGCATCGAGGGGCCCACCACCTTCACCGCCCCGTTGGTCGTCGACGCCGGAGGTGTCTCGGCCCGCCTGGCCACCGCCGTCGGGCGTACCAAGAACGAGCGCCGCCCCATGGGCGTGGCCGTGCGCGCCTACTTCCGCTCCCCGCGCGCCAAGGACGCCTGGATGGAGTCGCGCCTCGAGCTGTGGGACGGCACTCCCGGCAAGTCCGACCTCCTGCCCGGCTACGGCTGGATCTGGTCCGTGGGGGAGGGGCTGGTCAACGTCGGACTCGGCTCGGTCTCCTCGCGCGCCCAGGCCACCGCCATCGACTACCGCGCCGTGTTCAACCGCTGGATGGACAACGTCCCGGCCTCCTGGGGCTTCACCAAGGAGAACCAGGTCGGCGGCCTGGTCAGCGCCGCCCTGCCCATGGCCTTCAACCGCAAGCCGCACTACGCCGACGGCCTCATGCTGCTGGGCGACGCAGGCGGCATGGTCTCGCCCTTCAACGGCGAGGGCATCGCCCAGGCCCTCATGTCCGGCCGCCTGGCCGCCCAGGCCGCCGCCCAGGCATCCGCCCGCACGACCACCTCCGGCCGTGAGCAGGTCCTGGCCCAGTACCCCAAGGCCCTCAGCTCCGAGATGGGCGGCTACTACACGCTCGGCCGTGTCTTCGTCGCCCTCATCGAGCACCCCGAGGTCATGCGCCTGTGCACCCGCTACGGGCTGCCGCGCAAGCGCCTCATGAAGCTCGTCACCAAGCTCCTGTCCGACGGGTGGGAGCGCCGCGGCGGCGACGGAATCGACCACTTCATCCAGCTCCTGACAAGGATGGTGCCGGAAGCATGA","VTQAAAQSSASASADVIVVGAGPAGSSAAYHMATLGLDVILLEKQELGRDKVCGDGLTPSAVRELVSMGMDTTGWQRNRGLRVIGGGHLLHFPWPEQASFPSYGMARPRALLDRDLAEHAAAAGARLLTGVTVTAPVTSPTGRVTGVEARPTNRVAYPGIEGPTTFTAPLVVDAGGVSARLATAVGRTKNERRPMGVAVRAYFRSPRAKDAWMESRLELWDGTPGKSDLLPGYGWIWSVGEGLVNVGLGSVSSRAQATAIDYRAVFNRWMDNVPASWGFTKENQVGGLVSAALPMAFNRKPHYADGLMLLGDAGGMVSPFNGEGIAQALMSGRLAAQAAAQASARTTTSGREQVLAQYPKALSSEMGGYYTLGRVFVALIEHPEVMRLCTRYGLPRKRLMKLVTKLLSDGWERRGGDGIDHFIQLLTRMVPEA$","Geranylgeranyl reductase","Membrane, Cytoplasm, Extracellular","bacteriochlorophyll synthase","geranylgeranyl reductase","geranylgeranyl reductase","","Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S. The primary structure of the flavoprotein D-aspartate oxidase from beef kidney. J. Biol. Chem. 1992. 267(17):11865-11871. PMID: 1601857Miyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M., Miyake Y. Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization. J. Biochem. 1991. 109(1):171-177. PMID: 1673125","","","

InterPro
IPR003042
Family

Aromatic-ring hydroxylase
PR00420	$\"[15-37]T$ $\"[304-319]T$	RNGMNOXGNASE

InterPro
IPR006076
Family

FAD dependent oxidoreductase
PF01266	$\"[15-48]T$	DAO

InterPro
IPR011777
Family

Geranylgeranyl reductase, plantal and prokaryotic
TIGR02032	$\"[14-339]T$	GG-red-SF: geranylgeranyl reductase family

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[15-332]T$	no description
PTHR10617	$\"[49-380]T$	FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE
PTHR10617:SF9	$\"[49-380]T$	GERANYLGERANYL HYDROGENASE

","BeTs to 5 clades of COG0644COG name: Dehydrogenases (flavoproteins)Functional Class: CThe phylogenetic pattern of COG0644 is AMTKyQvCE-R----------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 79 to 111 (E_value = 7.6e-08) place ANA_1625 in the Thi4 family which is described as Thi4 family.Residues 80 to 410 (E_value = 0.00015) place ANA_1625 in the FAD_binding_3 family which is described as FAD binding domain.Residues 81 to 111 (E_value = 5.5e-05) place ANA_1625 in the HI0933_like family which is described as HI0933-like protein.Residues 82 to 405 (E_value = 1.8e-06) place ANA_1625 in the DAO family which is described as FAD dependent oxidoreductase.Residues 82 to 111 (E_value = 6.6e-09) place ANA_1625 in the FAD_binding_2 family which is described as FAD binding domain.Residues 82 to 110 (E_value = 4.7e-09) place ANA_1625 in the GIDA family which is described as Glucose inhibited division protein A.Residues 82 to 110 (E_value = 8e-07) place ANA_1625 in the Lycopene_cycl family which is described as Lycopene cyclase protein.Residues 82 to 115 (E_value = 2.6e-08) place ANA_1625 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.","","synthase ","","1","","","Tue Aug 7 10:01:27 2007","","Tue Aug 7 10:01:27 2007","","","Tue Aug 7 10:01:27 2007","Tue Aug 7 10:01:27 2007","Tue Aug 7 10:01:27 2007","","","Tue Aug 7 10:01:27 2007","","","Tue Aug 7 10:01:27 2007","Tue Aug 7 10:01:27 2007","","","Tue Aug 7 10:01:27 2007","Tue Aug 7 10:01:27 2007","","","","","yes","","" "ANA_1626","1756604","1757362","759","6.94","-0.13","27165","GTGACCGCGGCCGGGATTTGCGATGATGACCCCATGAGCCGATCCCCCCTGCGAGCCAGCCTCGCCAAGGACCCGCGCGAGGTCGCCGGGATGTTCGACGCTGTCGCGCGCCGCTACGACCTGTCCAATGACGTGATGAGCCTGTTCCAGGTTCACATGTGGCGCCGGGTGACGCGCGCGGCCGTCGCCGCGAGGCCGGGGATGCGCGTCCTGGATCTGGCCGCGGGGACCGGCACCTCCTCGGTGGAGTACGCCGCTGACGGCGCCGAGGTCGTGGCCTGCGACTTCTCCACCGGCATGGTGGCCGAGGGTAAGCGCCGCCACCCCGAGATCGCCTTCGTGGCCGGGGACGCCACGGCGCTGCCCTTCGCCGACGCGAGCTTCGACGTCGTCACCATCTCCTACGGGCTGCGCAACGTGCAAGACACGGCGCGGGCACTGTCGGAGATGCGCCGGGTGACGGTACCAGGCGGGCAGATCGTCATCGCGGAGTTCTCTACCCCGACCTGGCCGCCCTTCCGCCACCTATACCGCTTCTACCTGGGCAGCGCCCTGCCGGCCGCCGCCCGCCTGGTCTCGTCGAACACCGAGGCCTACGACTATCTGGGCGAGTCGATCCTGGCCTGGCCGGACCAGCGGGAGCTGGCCGGCCTCATGCAGCAGGCCGGCTGGCGGGGCGTGGGCTACAAGAACCTCTCCGGCGGAATCGTCGCGGTTCACCGGGCCACGCGGCCCGTGCCCGCCCAGGGCGAGCAGTGA","VTAAGICDDDPMSRSPLRASLAKDPREVAGMFDAVARRYDLSNDVMSLFQVHMWRRVTRAAVAARPGMRVLDLAAGTGTSSVEYAADGAEVVACDFSTGMVAEGKRRHPEIAFVAGDATALPFADASFDVVTISYGLRNVQDTARALSEMRRVTVPGGQIVIAEFSTPTWPPFRHLYRFYLGSALPAAARLVSSNTEAYDYLGESILAWPDQRELAGLMQQAGWRGVGYKNLSGGIVAVHRATRPVPAQGEQ$","Ubiquinone/menaquinone biosynthesis methyltransferase","Cytoplasm","Methylase involved in ubiquinone/menaquinonebiosynthesis","putative ubiquinone/menaquinone methyltransferase ","ubiquinone/menaquinone biosynthesis methyltransferase","","Lee P.T., Hsu A.Y., Ha H.T., Clarke C.F. A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J. Bacteriol. 1997. 179(5):1748-1754. PMID: 9045837","","","

InterPro
IPR004033
Family

UbiE/COQ5 methyltransferase
PTHR10108:SF24	$\"[20-245]T$	UBIQUINONE/MENAQUINONE BIOSYNTHESIS METHYLTRANSFERASE
PF01209	$\"[19-244]T$	Ubie_methyltran
TIGR01934	$\"[28-244]T$	MenG_MenH_UbiE: ubiquinone/menaquinone bios

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[46-229]T$	no description
PTHR10108	$\"[20-245]T$	METHYLTRANSFERASE

","BeTs to 17 clades of COG2226COG name: Methylase involved in ubiquinone/menaquinone biosynthesisFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG2226 is ---p--yqvdr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB004033 (UbiE/COQ5 methyltransferase) with a combined E-value of 1.1e-68. IPB004033A 28-55 IPB004033B 95-107 IPB004033C 121-144 IPB004033D 145-177 IPB004033E 185-237","","","-51% similar to PDB:2GS9 Crystal structure of TT1324 from Thermus thermophilis HB8 (E_value = 9.0E_11);","Residues 19 to 244 (E_value = 1.5e-63) place ANA_1626 in the Ubie_methyltran family which is described as ubiE/COQ5 methyltransferase family.Residues 71 to 162 (E_value = 1.6e-29) place ANA_1626 in the Methyltransf_11 family which is described as Methyltransferase domain.Residues 71 to 160 (E_value = 8.1e-14) place ANA_1626 in the Methyltransf_12 family which is described as Methyltransferase domain.","","involved in ubiquinone-menaquinone biosynthesis (UBIE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1627","1757582","1758781","1200","5.18","-13.20","41911","GTGATCGAGGCCCACAGGGCGGATCGCATTGAGACACTGCGGGCCGCGTGGCGGGCCGTGGTCGGCGCAGCCTGGTGGCGTGATGCGCTGGTCCGCCCCGGGACCGGGCCGGTGGCGCTGGGCGCGATCACCTTCTCCCCCAGCTCCGAGCAGTCCTCGGTTCTGGTGGTTCCCGAGGTCCTCGTTGGGCTGGATGACTCCGGTGCTTGGCTGACGACCGTGGTGTCCGGGACTGACGACGGGACGGAGCCGGAGCACCCGGATCCCGGCTCGCTCCTGAAGGCGCTGGTGGCCGATGCTCGTGCAGCGGTCGACCGGGAGCAGGCCGGCACCGACAGGGACTCCGGGGACTCCGGCGGCACCACCGCCGTTGAGGCCGGGGCGCTCAGCGAGGAGCAGTGGTGCCGGGCGGTCTGCGCCACGCAGGAGCGGATGCGTGCGGGGCAGGCCCGCAAGGTGGTCCTGGCCCGCGACGTGCTGGCCTACCCGGGCGGGCCGCTGGCCACCGGTACGGTCCTGCGGCGCCTGGCCAGCGACTACCCCTCCACCTGGGTCTTCGCCGTCGACCAGATGGTGGGCGCCAGTCCTGAGCTGCTGCTGCGCCTGCGGGATCGACGCCTCATGAGCAGGGTGCTGGCCGGTACGGCCCGCCGGCACGCCGGCGAGGACGCTCTGGCGACGGCGCGCCTGGCTTCCTGGCTGGAGGGCTCGGAGAAGAACAACCGGGAGCATGAGCTGGCCCGGGACTCGGCGATCACGGCGCTGGAGCCGCTGTGCTCGGTGGTGGAGGCCCCCGCCCGCTTTGTCCTGACGCTGCCGAATGTGCTGCATCTGGCCAGTGATGTCACCGGGGTCGTTGCCGGGGACACCGGGGCACTGGCTCTGGTGGATGCGCTGCACCCGACGGCGGCCGTGTGCGGGACACCGACTCAGGCGGCGGCGCACCTCATTGAGGAGGCCGAGTCCATGGACCGGGGGCGTTACGCCGGGCCCGTGGGCTGGGTGGACTGGCACGGCGAGGGCGAGTGGTGCATCGCTCTGCGCAGTGCCCAGCTGCCCGCGGCGGGCCTCGGACCGCAGTCGCCCGCGAGAGTGTTCGGGGGCGGCGGCATCATGCCGGACTCCGAGCCGGTCGACGAGCTGGCGGAGACGACCGCCAAGATGCGCCCCATGCTGGGAGCACTCGGCGTGCGTCTCTGA","VIEAHRADRIETLRAAWRAVVGAAWWRDALVRPGTGPVALGAITFSPSSEQSSVLVVPEVLVGLDDSGAWLTTVVSGTDDGTEPEHPDPGSLLKALVADARAAVDREQAGTDRDSGDSGGTTAVEAGALSEEQWCRAVCATQERMRAGQARKVVLARDVLAYPGGPLATGTVLRRLASDYPSTWVFAVDQMVGASPELLLRLRDRRLMSRVLAGTARRHAGEDALATARLASWLEGSEKNNREHELARDSAITALEPLCSVVEAPARFVLTLPNVLHLASDVTGVVAGDTGALALVDALHPTAAVCGTPTQAAAHLIEEAESMDRGRYAGPVGWVDWHGEGEWCIALRSAQLPAAGLGPQSPARVFGGGGIMPDSEPVDELAETTAKMRPMLGALGVRL$","Isochorismate synthase","Cytoplasm, Membrane","Unknown","isochorismate synthase ","isochorismate synthase","","Liu J., Quinn N., Berchtold G.A., Walsh C.T. Overexpression, purification, and characterization of isochorismate synthase (EntC), the first enzyme involved in the biosynthesis of enterobactin from chorismate. Biochemistry 1990. 29(6):1417-1425. PMID: 2139795Barghouthi S., Payne S.M., Arceneaux J.E., Byers B.R. Cloning, mutagenesis, and nucleotide sequence of a siderophore biosynthetic gene (amoA) from Aeromonas hydrophila. J. Bacteriol. 1991. 173(16):5121-5128. PMID: 1830579Serino L., Reimmann C., Baur H., Beyeler M., Visca P., Haas D. Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa. Mol. Gen. Genet. 1995. 249(2):217-228. PMID: 7500944Martinez J.S., Zhang G.P., Holt P.D., Jung H.T., Carrano C.J., Haygood M.G., Butler A. Self-assembling amphiphilic siderophores from marine bacteria. Science 2000. 287(5456):1245-1247. PMID: 10678827Wildermuth M.C., Dewdney J., Wu G., Ausubel F.M. Isochorismate synthase is required to synthesize salicylic acid for plant defence. Nature 2001. 414(6863):562-565. PMID: 11734859","","","

InterPro
IPR004561
Family

Isochorismate synthase
PIRSF001502	$\"[1-399]T$	Isochorismate synthase
PTHR11236:SF3	$\"[129-396]T$	ISOCHORISMATE SYNTHASE
TIGR00543	$\"[37-395]T$	isochor_syn: isochorismate synthases

InterPro
IPR005801
Domain

Anthranilate synthase component I and chorismate binding protein
PD000779	$\"[125-384]T$	PCHA_PSEAE_Q51508;
PF00425	$\"[130-395]T$	Chorismate_bind

noIPR
unintegrated

unintegrated
G3DSA:3.60.120.10	$\"[129-395]T$	no description
PTHR11236	$\"[129-396]T$	AMINOBENZOATE/ANTHRANILATE SYNTHASE

","BeTs to 8 clades of COG1169COG name: Isochorismate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism] Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1169 is -o--------rlbcefgh--------Number of proteins in this genome belonging to this COG is 1","***** IPB006805 (Anthranilate synthase component I, N-terminal) with a combined E-value of 1.2e-21. IPB006805C 195-222 IPB006805E 294-334 IPB006805F 365-395***** IPB005801 (Anthranilate synthase component I signature) with a combined E-value of 1.3e-12. IPB005801A 232-245 IPB005801C 323-337 IPB005801D 338-352","","","-46% similar to PDB:1QDL THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS (E_value = 2.9E_23);-41% similar to PDB:1I1Q STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM (E_value = 4.5E_16);-42% similar to PDB:2EUA Structure and Mechanism of MenF, the Menaquinone-Specific Isochorismate Synthase from Escherichia Coli (E_value = 2.1E_13);-39% similar to PDB:1I7Q ANTHRANILATE SYNTHASE FROM S. MARCESCENS (E_value = 3.0E_12);-39% similar to PDB:1I7S ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN (E_value = 3.0E_12);","Residues 130 to 395 (E_value = 6e-46) place ANA_1627 in the Chorismate_bind family which is described as chorismate binding enzyme.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1628","1760544","1758805","1740","4.97","-17.31","58665","ATGAGCGGATACGACGAGACGAACCCGGAGGCATACTGGCCCACTGAGCCCGAGGCGGCGGCGGACGGCGCTCACTCCGGTGTCGACTCCTGGTCCGCCAGCAGCCAGGCCAGCCCGGCAACGGCGTCTTCCGTCAGTGAGGGCGCGAGCGTGACCGAGGACCACGGCGGCTACGCGGATCTCTCCCAGGCCTACACCGCCGACGCCTCCCACTCCGAGCCGGTCCTGCCGCAGGGAGCGGGCGTGCGGCGCTGGGACGAGACCCGGCAGCTGCCCGCCGAGCCGCCGACCTCGCAGATGCCCGCTGAGCAGTCCGCGTCGCCATACGCGCAGTCCGCCCAGGGGCAGTACCAGCCCCAGCAGCCGTCCTACCAGCCGCAGCAGCAGCCTCAGGGGCAGTACCCCGCCCCTCAGGTGCAGCAGGCGGCGCCGTCCAGTTACTCATCCGCCCAGCAGCCCTACCAGGGGCAGCAGACGCACCTCGGCTCGCCCTACACGAGCGTCCCGACGACGCCCGGTGGCTACGCGCCGGCCGGCGCCCCCACCGGGGAGTCCTTCTATGCGGCCTCGAAGGCCACAGGCGCTGACAGCGGCACCACGAGGCGCCGGCGGGGGCCGGGCTGGTTCGCCCTGGTCGCCTCCGTGCTGGTCGCCTCTCTGCTGGGGGCCGGCGGTGCCGTAGGAGCGATCAAGGCTCTCGACGCCCGGGATGGCGGCGCGTCACAGCGCTCCACGGCCGCCCCCACCGCCATCGCCACCGGGAGTACGACTCAGACCGTTAACAGCGCCGGCCAGGCCCCCGACTGGGAGGCCGTCTCGGCAGCCGTGTCCAACGCCGTCGTCTCCATCGCCGTCGCCACGGACAAGGGCAATGCCCTGGGCTCCGGAGTCATCTTCGACAAGGAGGGGCACATCATCACGAACAACCACGTGGTGGCGGGGGCCTCGCAGATCCAGGTGACGCTGGCCGACGGCCGCGTCTATGACGCCGAGACCACCGGTACCGACCCCGCCACCGACCTGGCGGTCATCCAGCTCAAGGACGCCCCCGACAACCTCACCGTTGCCCAGCTCGGAGACTCCGACAAGCTGGCCACCGGTCAGGACGTCATGGCGATCGGCAACCCGCTGGGTCTGTCCTCCACCGTCACCACCGGCATCATCTCCGCCCTCAACAGGCCCGTCGTCAACTCCCAGAATGAGGACGGCTCGGGTGATTCGGCGGTCTACACCAACGCCATCCAGATCGACGCCGCCATCAACCCCGGCAACTCCGGCGGCCCTCTCTTCGACGAGAAGGGGCGGGTCATTGGGATCACCAGCTCCATCGCCACCATGGGCCGCTCCGGCGGCGGCGAAGGAGGCTCGGGGAGCATCGGCATCGGTTTCGCCATTCCCGTCAAGCTGGCGGACAAGGTCGCCAAGCAGCTCATCAAGTCCGGTGCCGCCACGCACGCCTACCTGGGAGTCACCCTCGACACCGATGGCGCCACGGCCGACGGCGAGAAGCGCGCCGGCGCCAAGATCACCTCGGTTGAAAGCGGTTCGCCGGCTGACAAGGCCGGACTGAAGACGAACGACGTCGTCGTCGCCATTGATGGGAAGACCACCGCCCAGGGGTCGGCTCTCACCGGTTACGTGCGTCAGTACTCCGCCAACGACAAGGTCAAGCTCACGGTCATCCGCAACTCCAAGAAGCAGGACATCGACGTGACCCTGGCCGAGCGCAAGGACTCCTGA","MSGYDETNPEAYWPTEPEAAADGAHSGVDSWSASSQASPATASSVSEGASVTEDHGGYADLSQAYTADASHSEPVLPQGAGVRRWDETRQLPAEPPTSQMPAEQSASPYAQSAQGQYQPQQPSYQPQQQPQGQYPAPQVQQAAPSSYSSAQQPYQGQQTHLGSPYTSVPTTPGGYAPAGAPTGESFYAASKATGADSGTTRRRRGPGWFALVASVLVASLLGAGGAVGAIKALDARDGGASQRSTAAPTAIATGSTTQTVNSAGQAPDWEAVSAAVSNAVVSIAVATDKGNALGSGVIFDKEGHIITNNHVVAGASQIQVTLADGRVYDAETTGTDPATDLAVIQLKDAPDNLTVAQLGDSDKLATGQDVMAIGNPLGLSSTVTTGIISALNRPVVNSQNEDGSGDSAVYTNAIQIDAAINPGNSGGPLFDEKGRVIGITSSIATMGRSGGGEGGSGSIGIGFAIPVKLADKVAKQLIKSGAATHAYLGVTLDTDGATADGEKRAGAKITSVESGSPADKAGLKTNDVVVAIDGKTTAQGSALTGYVRQYSANDKVKLTVIRNSKKQDIDVTLAERKDS$","Trypsin-like serine protease","Extracellular","possible DO serine protease","trypsin-like serine proteases typically periplasmic contain C-terminal PDZ domain ","2-alkenal reductase","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Lipinska B., Sharma S., Georgopoulos C. Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mechanism of heat-inducible transcription. Nucleic Acids Res. 1988. 16(21):10053-10067. PMID: 3057437Lipinska B., Zylicz M., Georgopoulos C. The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 1990. 172(4):1791-1797. PMID: 2180903Clausen T., Southan C., Ehrmann M. The HtrA family of proteases: implications for protein composition and cell fate. Mol. Cell 2002. 10(3):443-455. PMID: 12408815Waller P.R., Sauer R.T. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol. 1996. 178(4):1146-1153. PMID: 8576051","","","

InterPro
IPR001254
Domain

Peptidase S1 and S6, chymotrypsin/Hap
PF00089	$\"[296-473]T$	Trypsin

InterPro
IPR001478
Domain

PDZ/DHR/GLGF
PF00595	$\"[476-561]T$	PDZ
SM00228	$\"[486-564]T$	PDZ
PS50106	$\"[474-564]T$	PDZ

InterPro
IPR001940
Family

Peptidase S1C, HrtA/DegP2/Q/S
PR00834	$\"[303-315]T$ $\"[324-344]T$ $\"[366-390]T$ $\"[410-427]T$ $\"[432-449]T$ $\"[522-534]T$	PROTEASES2C

noIPR
unintegrated

unintegrated
G3DSA:2.30.42.10	$\"[500-572]T$	no description
G3DSA:2.40.10.10	$\"[264-356]T$ $\"[357-490]T$	no description
PTHR22939	$\"[270-576]T$	SERINE PROTEASE FAMILY S1C HTRA-RELATED
PTHR22939:SF10	$\"[270-576]T$	SERINE PROTEASE DO/HTRA-RELATED
tmhmm	$\"[207-227]?$	transmembrane_regions

","BeTs to 20 clades of COG0265COG name: Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domainFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0265 is -om---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001940 (HtrA/DegQ protease family signature) with a combined E-value of 1.1e-51. IPB001940A 303-315 IPB001940B 324-344 IPB001940C 366-390 IPB001940D 410-427 IPB001940E 432-449 IPB001940F 522-534","","","-58% similar to PDB:1KY9 Crystal Structure of DegP (HtrA) (E_value = 3.2E_45);-54% similar to PDB:1Y8T Crystal Structure of RV0983 from Mycobacterium tuberculosis- Proteolytically active form (E_value = 1.2E_44);-56% similar to PDB:1L1J Crystal structure of the protease domain of an ATP-independent heat shock protease HtrA (E_value = 3.8E_38);-48% similar to PDB:1SOT Crystal Structure of the DegS stress sensor (E_value = 7.9E_36);-48% similar to PDB:1SOZ Crystal Structure of DegS protease in complex with an activating peptide (E_value = 7.9E_36);","Residues 280 to 473 (E_value = 2.1e-16) place ANA_1628 in the Trypsin family which is described as Trypsin.Residues 476 to 561 (E_value = 4e-05) place ANA_1628 in the PDZ family which is described as PDZ domain (Also known as DHR or GLGF).","","DO serine protease","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1629","1762507","1760756","1752","5.40","-16.48","59729","GTGGCGGCCCTCCTGGCCGAGGGCGTGCGCGAAGTCGTCCTGTGCCCGGGATCGCGCAGCGCCCCGCTGGCGGATGCCCTGGCCGATGCCGCCGACGCCGGGCGCCTACGGCTGCGCGTCGTCCTGGATGAGCGCAGCGCCGGTTTCATCGCCCTGGGGGCCGCCCGGGCCCACGCCCTGAACGGGCACAGCCACTGTGCCGCTGTCGTGACCACCTCGGGCACGGCCGTCTCCAACCTCCATCCGGCCGTCAGTGAGGCCGACGCCGCCGGCATCCCCCTGCTCGTCATCAGTGCCGACCGGCCCCACGAGCTGGTCGGCACCGGCGCCAGCCAGACCACCGAGCAGACCGGGCTCTTCGTCCCGGCCTTGCGCCTGGGTGTGGACCTGCCCGCTGACCTGGCCGCCGACCTCGGCGGCTGCGCGGCCGACGCCGCCATCGCCGGGCAGGTGCGCCGCGCCGTCGCCGCCGCCACCGGGACCCTCAGTCGGGATCCCGGGCCGGTCCAGATCAACGCCCGCTTCCGTCCGCCCCTGACAGTGGAGGACTCAACGGAGAGCTCAGTGGGGGACTCCGTGGAGGATGCGGTGCCGGCCGCTCCGGTGCCACCCTCCCCGCCCATGGTCCCGGCTGCCCGGGCAGCTGTGCTGGCCGGAGCCCCGGAGACCAGTGCTGGCCAGCCGGCCGGCACTGGCTCCTCCACGCAGGGGAGGGGGATCGTCGTCGCCGGAGACACCGCCCACCTGGCCGTCGGCTCCCTGGCCAGGTCTCTGGCCGAGCACCTCGACTGGCCACTCCTGGCCGAACCCACCTCCCAGGCCCGCAGCGGCCCCCAGGCCCTGAGCCGTTACGCCGAGCTACTGGGCACCCCGGTGGGCCGCGTGCTCGCGGAGCAGGCCGAGCACCTCCTCGTCCTGGGCCACCCCAGCCTCAGTCGATCCATCACCGCGCTCCTGGGGTGCGACGACCTCGACATCACCGTCCTGACCGAACGCGCCCAGTGGACCGACGTCTCCGGACGGGCCCGACGGGTCGTCCCCATTGACGGTCCCGATCATGAGCCTGCCGACGACGCCGCCCTCCATGCAGCCCGGCTCGCCGCCCGGCTCGGCCTGGAGAGGGCCGACGCGGCCTGGACCGACTCCTGGCGCCGGGCCGTGGCGGATCTTCCCGAACCGGACTGTTCCAGCAGCCCCGACGCCCTGGCCCGGGCCGTGTGGGAGGCCGGCCAGGCCCCCGGCGCCCCCACCCTCCTGCTGGGCTCATCCATGACGGTGCGGCGCCTGGACCGACTCGCCCAGCCCGGCGCCGCCGCCCCGAAGGCGGTCGCGAACCGCGGCCTAGCGGGCATCGACGGCACCATCGCCACCGGGATCGGACTGTGGATGGCCTCAGGGGAACCGGTTCGCGCCGTCATGGGTGACCTCACCTTCCTCCACGACGCCATGTCCTTGAACCGGGGCGTGCGTGAGGAGGAGGCCGACCTGCAGGTGATCGTCGTCGACGACGGCGGGGGTGCGATCTTCTCCCAGCTCGAGTACGCCCGCACCACGCCATCTGCCCGGTTCGAACGGCTCTTCACCGCCCCTCAGCGGGCGGATATCGCTGCGCTGGCGGCAGCCCTGGGGGCCCGCGTCCATGTCCTCAACGATATCGCCGCCCTCCGCAGGCTCCTGGCTGAGCCGGTCGACGGTGTGAGCGTTGTCGTCTGGGAGACCACAAGGCACGGTCCTCACACCGTGACAACATGA","VAALLAEGVREVVLCPGSRSAPLADALADAADAGRLRLRVVLDERSAGFIALGAARAHALNGHSHCAAVVTTSGTAVSNLHPAVSEADAAGIPLLVISADRPHELVGTGASQTTEQTGLFVPALRLGVDLPADLAADLGGCAADAAIAGQVRRAVAAATGTLSRDPGPVQINARFRPPLTVEDSTESSVGDSVEDAVPAAPVPPSPPMVPAARAAVLAGAPETSAGQPAGTGSSTQGRGIVVAGDTAHLAVGSLARSLAEHLDWPLLAEPTSQARSGPQALSRYAELLGTPVGRVLAEQAEHLLVLGHPSLSRSITALLGCDDLDITVLTERAQWTDVSGRARRVVPIDGPDHEPADDAALHAARLAARLGLERADAAWTDSWRRAVADLPEPDCSSSPDALARAVWEAGQAPGAPTLLLGSSMTVRRLDRLAQPGAAAPKAVANRGLAGIDGTIATGIGLWMASGEPVRAVMGDLTFLHDAMSLNRGVREEEADLQVIVVDDGGGAIFSQLEYARTTPSARFERLFTAPQRADIAALAAALGARVHVLNDIAALRRLLAEPVDGVSVVVWETTRHGPHTVTT$","Menaquinone biosynthesis protein","Cytoplasm, Membrane","2-oxoglutarate decarboxylase","2-oxoglutarate decarboxylase / 2-succinyl-6-hydroxy-2;4-cyclohexadiene-1-carboxylate synthase ","2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PS00211	$\"[463-477]?$	ABC_TRANSPORTER_1

InterPro
IPR004433
Family

Menaquinone biosynthesis protein
PIRSF004983	$\"[1-581]T$	2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenD

InterPro
IPR012001
Domain

Thiamine pyrophosphate enzyme, N-terminal TPP binding region
PF02776	$\"[1-147]T$	TPP_enzyme_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.970	$\"[1-172]T$ $\"[386-564]T$	no description
PTHR18968	$\"[417-543]T$	THIAMINE PYROPHOSPHATE ENZYMES
PTHR18968:SF3	$\"[417-543]T$	MENAQUINONE BIOSYNTHESIS PROTEIN

","BeTs to 7 clades of COG1165COG name: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1165 is -o--------rlbce-gh--------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 147 (E_value = 0.00048) place ANA_1629 in the TPP_enzyme_N family which is described as Thiamine pyrophosphate enzyme, N-terminal TPP binding domain.","","decarboxylase (KDC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1630","1763675","1762653","1023","8.32","3.58","36182","CTGCTGGCTCGCATTGATCGCGCGGTCGTCTGGGACATTCCTCTGACGACGCCGTTTCGCGGCATCACCCGCCGCGACGGCGTCCTGCTCCATGGCCCCGGGGGCTGGGGCGAGGTCGCGCCCTTCTGGGACTACGGGCTGGAGGCCAGCGCTCCCTGGCTCGCCTCCGGACTGTGCCAGGCCCTGGGAAACTCCCTCCTTCCCCGCTACCGCGAGACCATCCCCGTCAACGTGACCGTCCCTGAGGTCGGTGCTCAGGACGCCTCCGATCTGGTGCGGGCCTCCGGCGCCAGGACCGCCAAGGTCAAGGTCAGCGGCAGCAGTGACAAGCGCTCGGCGGACCTGGAGCGCCTCGAGGCGGTCCGCTCGGCACTGGGGCGTTCCGGCAAGGTGCGTATCGACGTCAACGGCGCCTGGGACCTGGACACCGCCCGCGAGAACCTGCCCCTCATGGACCGGGCCGCCGGAGGGCTGGAGTACGCCGAACAGCCCTGCGCCACCGTCTACGACCTGGCCGACCTGCGCCGCGCCGTCGACGTGCCCATCGCCGCCGACGAGTCGATCCGGCTGTCCGCCAACCCCCTGGAGATCGTCCACCGGCGCGCCGCCGACGTCGCCATCCTCAAGGTGGCCCCGCTGGGCGGGGTGCACCGGGCCCTGGACATGGCCGAACGCCTCGGACTGCCCGCGGTCGTCTCCTCCGCCCTGGACACCTCCGTGGGCATCATGGCCGGCGCGACCCTCGCCTTCAGCCTGCCCTCCCTCAGTCACGCCTGCGGTCTTGGGACCACGCGCCTGCTGGCCCAGGACGTCGCCGAGCCCAGCGTCCGTCCCAGTAATGGGACCCTGCGTCTGGACGCCGCCGCCCCCGTCTCCGAACGCCTCCTGAGCGAGGTCAAGGCGGGGCCCTACCTCACCAGGCACTGGCAGACGCGCCTGCTGCACCTGGCCGGCGCCCTCCACGCCCGCCGCCAGCGCGAGGCCCGCGACCCCAGCCGGGCCGTGGCCGGGTTGCCGCTGTAG","LLARIDRAVVWDIPLTTPFRGITRRDGVLLHGPGGWGEVAPFWDYGLEASAPWLASGLCQALGNSLLPRYRETIPVNVTVPEVGAQDASDLVRASGARTAKVKVSGSSDKRSADLERLEAVRSALGRSGKVRIDVNGAWDLDTARENLPLMDRAAGGLEYAEQPCATVYDLADLRRAVDVPIAADESIRLSANPLEIVHRRAADVAILKVAPLGGVHRALDMAERLGLPAVVSSALDTSVGIMAGATLAFSLPSLSHACGLGTTRLLAQDVAEPSVRPSNGTLRLDAAAPVSERLLSEVKAGPYLTRHWQTRLLHLAGALHARRQREARDPSRAVAGLPL$","O-succinylbenzoate-CoA synthase","Cytoplasm","Probable O-succinylbenzoate synthase (OSBsynthase)(OSBS) (4-(2'-carboxyphenyl)-4-oxybutyric acid","O-succinylbenzoate-CoA synthase ","Mandelate racemase/muconate lactonizing enzyme, C-terminal domain protein","","Neidhart D.J., Kenyon G.L., Gerlt J.A., Petsko G.A. Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature 1990. 347(6294):692-694. PMID: 2215699Petsko G.A., Kenyon G.L., Gerlt J.A., Ringe D., Kozarich J.W. On the origin of enzymatic species. Trends Biochem. Sci. 1993. 18(10):372-376. PMID: 8256284Huisman G.W., Kolter R. Sensing starvation: a homoserine lactone--dependent signaling pathway in Escherichia coli. Science 1994. 265(5171):537-539. PMID: 7545940Schneider D., Aigle B., Leblond P., Simonet J.M., Decaris B. Analysis of genome instability in Streptomyces ambofaciens. J. Gen. Microbiol. 1993. 139(11):2559-2567. PMID: 8277241","","","

InterPro
IPR001354
Family

Mandelate racemase/muconate lactonizing enzyme
PTHR13794	$\"[72-299]T$	ENOLASE SUPERFAMILY, MANDELATE RACEMASE

InterPro
IPR013342
Domain

Mandelate racemase/muconate lactonizing enzyme, C-terminal
PF01188	$\"[81-181]T$	MR_MLE

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.120	$\"[58-290]T$	no description
PTHR13794:SF12	$\"[72-299]T$	MANDELATE RACEMASE

","BeTs to 12 clades of COG1441COG name: O-succinylbenzoate synthase and related enzymesFunctional Class: HThe phylogenetic pattern of COG1441 is a-----vcEBrh---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-67% similar to PDB:2OPJ Crystal structure of O-succinylbenzoate synthase (E_value = 2.2E_74);-50% similar to PDB:1JPM L-Ala-D/L-Glu Epimerase (E_value = 1.2E_19);-50% similar to PDB:1TKK The Structure of a Substrate-Liganded Complex of the L-Ala-D/L-Glu Epimerase from Bacillus subtilis (E_value = 1.2E_19);-48% similar to PDB:1NU5 Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme (E_value = 3.0E_15);-47% similar to PDB:1CHR CRYSTAL STRUCTURE OF CHLOROMUCONATE CYCLOISOMERASE FROM ALCALIGENES EUTROPHUS JMP134 (PJP4) AT 3 ANGSTROMS RESOLUTION (E_value = 8.7E_15);","Residues 149 to 249 (E_value = 1.4e-18) place ANA_1630 in the MR_MLE family which is described as Mandelate racemase / muconate lactonizing enzyme, C-terminal domain.","","O-succinylbenzoate synthase (OSB synthase)(OSBS) (4-(2-carboxyphenyl)-4-oxybutyric acid synthase) (O-succinylbenzoic acid synthase)","","1","","","Tue Aug 7 10:10:59 2007","","Tue Aug 7 10:10:59 2007","","","Tue Aug 7 10:10:59 2007","Tue Aug 7 10:10:59 2007","Tue Aug 7 10:10:59 2007","","","Tue Aug 7 10:10:59 2007","","","Tue Aug 7 10:10:59 2007","Tue Aug 7 10:10:59 2007","","","Tue Aug 7 10:10:59 2007","Tue Aug 7 10:10:59 2007","","","","","yes","","" "ANA_1631","1763969","1764541","573","10.42","8.55","20475","ATGAACGAGGGCAGCACAGGGTCAGGGGACGCAGGGCGCCATCACTGGAAGCCCGTCACACCCGTCTCCGCAATGGTTGTGGGCCGCCTGGTTCTCGGGCTGCCCAGCGCCGTCGGCCTGACGGTCATCGTGCTGATCTGGTCGGCGCTGACCCGCGCCGGGCTGGGATTCGGCAGGGCGTGCCTGTTCTCCCTGGTGGCAGTGGCGATTCGCGAGCTCATCGACGCCTCGGCCCACCGGCTCATCATGCGGGCCTGGCGCTCACGGGATCCTCATGGCCTGCTGCTGACGATCATCGCCGCGACCTGCCCCGCGGTCGCAGGATTCCTGGCCGCTCGCCTCCTCGCCCCGGCATCGACGACGGCACTGACGGTCCTCGCGTGGCTGCCGTTCATGGCTTTCGTCGCCCTCATTGAGAGGCCGTGGGACACCTCGCTCGGATACGACGCCCTCCAGAAGCGCATCCATCAGCCCCAGCCGATCCCACCGGAATACGTCACCGCAGACTTCCGCGACGCCCGCAAGCACCTGCCCGAGCTCCGGCGCATCGCACTGGCCCACGCGGCGCTGTAG","MNEGSTGSGDAGRHHWKPVTPVSAMVVGRLVLGLPSAVGLTVIVLIWSALTRAGLGFGRACLFSLVAVAIRELIDASAHRLIMRAWRSRDPHGLLLTIIAATCPAVAGFLAARLLAPASTTALTVLAWLPFMAFVALIERPWDTSLGYDALQKRIHQPQPIPPEYVTADFRDARKHLPELRRIALAHAAL$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[30-50]?$ $\"[93-113]?$ $\"[119-137]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[23-45]?$ $\"[95-117]?$ $\"[123-143]?$	transmembrane_regions

InterPro
IPR007210
Domain

Substrate-binding region of ABC-type glycine betaine transport system
PF04069	$\"[53-303]T$	OpuAC

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[61-306]T$	no description
tmhmm	$\"[29-51]?$	transmembrane_regions

","BeTs to 4 clades of COG2113COG name: ABC-type proline/glycine betaine transport systems, periplasmic componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2113 is -----------lb-ef-----j--t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-58% similar to PDB:2B4L Crystal structure of the binding protein OpuAC in complex with glycine betaine (E_value = 5.0E_17);-58% similar to PDB:2B4M Crystal structure of the binding protein OpuAC in complex with proline betaine (E_value = 5.0E_17);-38% similar to PDB:1IA6 CRYSTAL STRUCTURE OF THE CELLULASE CEL9M OF C. CELLULOLYTICUM (E_value = 5.0E_17);-38% similar to PDB:1IA7 CRYSTAL STRUCTURE OF THE CELLULASE CEL9M OF C. CELLULOLYTICIUM IN COMPLEX WITH CELLOBIOSE (E_value = 5.0E_17);-46% similar to PDB:1CEL THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI (E_value = 5.0E_17);","Residues 53 to 303 (E_value = 1.3e-54) place ANA_1633 in the OpuAC family which is described as Substrate binding domain of ABC-type glycine betaine transport system.","","betaine transport system permease protein (proX)","","1","","","","","","","","","","","Tue Aug 14 15:26:17 2007","","Tue Aug 14 15:26:17 2007","","","Tue Aug 14 15:26:17 2007","","","","Tue Aug 14 15:26:17 2007","Tue Aug 14 15:26:17 2007","","","","","yes","","" "ANA_1634","1767336","1766458","879","9.44","4.42","31257","ATGATTCCCGTACAGACTCCTCTTCCCAAGATTCCCCTGGGCACAGCGGTCGAGGTCCTCATCGAGTGGATCCAGGTCCACCTCCATGGCTTCCTCAGCGCGATCTCCCGGGCCGGCACCCTGGTCAACGACAACCTCGTGGACCTGCTCCTGGCCGTGCCTCCGCTGCTCATGGTGGTGGTCTTCGTCCTGGTCGCCTGGATGGCGAAGTCGTGGAGACTGGCAGTGGGGACCGCCGTCACCTTCCTCATCATCATCTCCCTGGGCCAGTGGGTCAACGCGATGGAGACGCTGGTCCTGGTCACCCTGGCGACCCTGACCGCCCTCGTCTTCGCCATCCCCCTGGGGATCTGGGCCGCCCGCAACAAGTACGTCAGCATCCTCATCCGCCCGGTCCTCGACCTCATGCAGACGATGCCGGCCTTCGTCTACCTCATCCCCTCGGTCCTGTTTTTCTCCATCGGGGTGGTGCCCGGGATGTTCGCCACGCTCATCTTCGCGATGCCCCCCGGGGTGCGCATGACCGAGCTGGGCATCAAGCAGGTGGACAAGGAGACCGTGGAGGCGGGGCGTTCTTTCGGAGCGACCGACTGGCAGATCCTGCGGGGCATTCAGCTGCCCCTGGCCGTCCCCACCATCATGGCGGGCGTCAACCAGGTCATCATGCTGGCCCTGTCGATGGCCGTCATCGCGGGCATGGTCGGTGCCGACGGCCTGGGGAAGGAGGTCGTCAAGGCGCTCGCGACGATCGACATCGCCAAGGGCACCGAGGCGGGCCTGTCCATCGTGTTCCTGGCGATCTACCTGGACCGGGTGACCGCGGCCCTCGGGGCGCCGCGGGAGAAGGGCTCGCTGCTCTCACTGATCAAGAAGCGGTGA","MIPVQTPLPKIPLGTAVEVLIEWIQVHLHGFLSAISRAGTLVNDNLVDLLLAVPPLLMVVVFVLVAWMAKSWRLAVGTAVTFLIIISLGQWVNAMETLVLVTLATLTALVFAIPLGIWAARNKYVSILIRPVLDLMQTMPAFVYLIPSVLFFSIGVVPGMFATLIFAMPPGVRMTELGIKQVDKETVEAGRSFGATDWQILRGIQLPLAVPTIMAGVNQVIMLALSMAVIAGMVGADGLGKEVVKALATIDIAKGTEAGLSIVFLAIYLDRVTAALGAPREKGSLLSLIKKR$","ABC-type proline/glycine betaine transport system, permease component","Membrane, Cytoplasm","glycine betaine transport system permeaseprotein","binding-protein-dependent transport systems inner membrane component","binding-protein-dependent transport systems inner membrane component","","Saenz H.L., Augsburger V., Vuong C., Jack R.W., Gotz F, Otto M. Inducible expression and cellular location of AgrB, a protein involved in the maturation of the staphylococcal quorum-sensing pheromone. Arch. Microbiol. 2000. 174(6):452-455. PMID: 11195102Zhang L., Gray L., Novick R.P., Ji G. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 2002. 277(38):34736-34742. PMID: 12122003","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[94-282]T$	BPD_transp_1
PS50928	$\"[94-273]T$	ABC_TM1

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[19-165]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-94]?$	signal-peptide
tmhmm	$\"[49-69]?$ $\"[74-94]?$ $\"[100-120]?$ $\"[141-161]?$ $\"[215-235]?$	transmembrane_regions

","BeTs to 8 clades of COG1174COG name: ABC-type proline/glycine betaine transport systems, permease componentFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1174 is a--------drlb-ef----uj--t-Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 94 to 282 (E_value = 1.9e-26) place ANA_1634 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","betaine transport system permease protein (permease)","","1","","","","","","","","","","","Tue Aug 14 15:25:56 2007","","Tue Aug 14 15:25:56 2007","","","Tue Aug 14 15:25:56 2007","","","","Tue Aug 14 15:25:56 2007","Tue Aug 14 15:25:56 2007","","","","","yes","","" "ANA_1635","1768643","1767336","1308","5.88","-7.56","47123","GTGAGGAGTGCAGTGAAAGTCATTGAGGCCAACCATGTCTACAAGGTCTTCGGGCGGCGACCGTCCGATGGCGTCAAGAAGCTCAAGGCCGGCAGGACGCGGGACCAGCTGAGGAAGTCAGGGCAGACCGCCGCCGTCATCGACACCTCCTTCGACGTCGACAAGGGCGAGATCTTCGTGGTCATGGGCCTGTCGGGCTCCGGGAAGTCCACCCTCATCCGCATGGTCAACGGCCTGCTGCCCATCACGGCCGGAAGCATGACCCTCTATGGGGAGGACCTGGCGCACGTCTCGAAGTCGAAGCTGCGCGAGCTGCGCCGCGAGCGCGTCTCCATGGTCTTCCAGAACTTCGCTCTCCTGCCGCACCGGACGGTGGGGGAGAACGCCGCCTACGGCCTGGAGATCCAGGGTGTGAATCGCTCCGAGCGCGAGCGTCGGGCAGAAGATGCCCTGTCCCTGGTGGGCCTGGAGGGGTGGGGCGGCTACAAGCCCGGTGAGCTCTCGGGTGGCATGCAGCAGCGGGTCGGCCTGGCCCGGGCCCTGGCCGCCGAGACCGACATCCTGCTCATGGACGAGGCCTTCTCCGCGCTCGACCCGCTCATCCGCCGGGAGATGCAGGACCAGCTCATCGACCTGCAGGGCAAGCTCGGCAAGACGATCCTGTTCATCACCCACGACCTCAACGAGGCCATGCGCCTGGGAGACCGTATCGCCATGATGCGCGACGGTCGCGTCGAGCAGGTCGGCACCGCCGAGGAGATCCTGCGCGACCCGGCCTCCGACTACGTCTCCCGGTTCGTGGCCGACGTCGACCGTAGCCGGGTCCTGACGGCCGGCTCCATCGCGGAGCCCCCGTACGCGGTCCTGGGCTCGGACCGCAGCCCCCACGCCGCCCACAAGCTCCTGCGGGAGAACCAGCCGCCGTGGCTGCTCGTCCAGAACCGCGACCGCACACCCTTCGGCTACGTCTGGGAGGACGACGTCGCCCGGGCAGTCAAGGAGGGCTCCAACGCCCTGCCGCTGTCCACGATCCACGAGATGCCGGTCGTGTCGCACTCGACCCCCGTCAACGAGCTGTTCGCCCACGCCGCGCAGCACGCCGCCCCCATCGTCGTCGTCGACGACGACGGACGGATCTCCGGCGTCATCCCGCGCGTCACCCTGCTGGCCGCCATCAGTGAGCAGAACCAGGAGACCGGGGCATCCAGCGCCGCCAGTGCCTCCAGCGCCGATCCGGCCGCGGAGCAGACCGACGAGCAGGCCGGCAAGGCCAGTGAGACCACCGAGGCCGAAGGAGCCGACGCCTGA","VRSAVKVIEANHVYKVFGRRPSDGVKKLKAGRTRDQLRKSGQTAAVIDTSFDVDKGEIFVVMGLSGSGKSTLIRMVNGLLPITAGSMTLYGEDLAHVSKSKLRELRRERVSMVFQNFALLPHRTVGENAAYGLEIQGVNRSERERRAEDALSLVGLEGWGGYKPGELSGGMQQRVGLARALAAETDILLMDEAFSALDPLIRREMQDQLIDLQGKLGKTILFITHDLNEAMRLGDRIAMMRDGRVEQVGTAEEILRDPASDYVSRFVADVDRSRVLTAGSIAEPPYAVLGSDRSPHAAHKLLRENQPPWLLVQNRDRTPFGYVWEDDVARAVKEGSNALPLSTIHEMPVVSHSTPVNELFAHAAQHAAPIVVVDDDGRISGVIPRVTLLAAISEQNQETGASSAASASSADPAAEQTDEQAGKASETTEAEGADA$","ABC-type proline/glycine betaine transport system, ATPase component","Cytoplasm, Membrane","glycine betaine ABC transporter ATP-bindingprotein","glycine betaine ABC transporter ATP-binding protein ","glycine betaine/L-proline ABC transporter, ATPase subunit","","Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 2004. 113(2):274-284. PMID: 14722619Carr G., Simmons N., Sayer J. A role for CBS domain 2 in trafficking of chloride channel CLC-5. Biochem. Biophys. Res. Commun. 2003. 310(2):600-605. PMID: 14521953Hebeisen S., Biela A., Giese B., Muller-Newen G., Hidalgo P., Fahlke C. The role of the carboxyl terminus in ClC chloride channel function. J. Biol. Chem. 2004. 279(13):13140-13147. PMID: 14718533","","","

InterPro
IPR000644
Domain

Cystathionine-beta-synthase
PF00571	$\"[280-393]T$	CBS
SM00116	$\"[346-393]T$	CBS

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[166-209]T$	Q6A7P1_PROAC_Q6A7P1;
PF00005	$\"[56-243]T$	ABC_tran
PS50893	$\"[31-267]T$	ABC_TRANSPORTER_2
PS00211	$\"[167-181]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[55-252]T$	AAA

InterPro
IPR005892
Family

Glycine betaine/L-proline transport ATP-binding subunit
TIGR01186	$\"[38-399]T$	proV: glycine betaine/L-proline transport A

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[41-270]T$	no description
PTHR19222	$\"[8-17]T$ $\"[41-288]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF48	$\"[8-17]T$ $\"[41-288]T$	GLYCINE BETAINE/L-PROLINE ABC TRANSPORTER

","BeTs to 7 clades of COG1125COG name: ABC-type proline/glycine betaine transport systems, ATPase componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1125 is a--------drlb-ef----uj--t-Number of proteins in this genome belonging to this COG is 2","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 9.6e-44. IPB013563A 45-79 IPB013563B 110-123 IPB013563C 164-191 IPB013563D 219-271***** IPB005116 (TOBE domain) with a combined E-value of 1.5e-33. IPB005116A 63-79 IPB005116B 108-125 IPB005116C 167-180 IPB005116D 187-206 IPB005116E 221-234***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 3.5e-28. IPB005074C 45-92 IPB005074D 155-198 IPB005074E 219-239***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.9e-17. IPB010509B 56-81 IPB010509D 162-206","","","-60% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 3.1E_42);-58% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 1.2E_41);-60% similar to PDB:1G29 MALK (E_value = 3.4E_41);-58% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 7.9E_38);-58% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 7.9E_38);","Residues 56 to 243 (E_value = 1.1e-64) place ANA_1635 in the ABC_tran family which is described as ABC transporter.Residues 280 to 393 (E_value = 8e-11) place ANA_1635 in the CBS family which is described as CBS domain pair.","","betaine ABC transporter ATP-binding protein","","1","","","","","","","","","","","Tue Aug 14 15:25:19 2007","","Tue Aug 14 15:25:19 2007","","","Tue Aug 14 15:25:19 2007","Tue Aug 14 15:25:19 2007","","","Tue Aug 14 15:25:19 2007","Tue Aug 14 15:25:19 2007","","","","","yes","","" "ANA_1636","1769183","1770487","1305","5.61","-8.96","46169","GTGCCGGCTGCAGGATGGATCCCGGCAGGCGGTCCAGACCTCTGGGGAACCCTCGGGGGCCCGGGCACACACAGCCCCAAGGCCCACGCCGACGTGCGCATCTCGAACATGTCGCTCATCCTGCGTCACCTTCAGACGAGCCCCGCCCTGTCGCGCACACGCCTGGCCCGTGAGACGGGGCTGTCCAAGGCGACGGTCTCGACCCTCGTGGCCGAGCTGTGCTCCCGGGGGCTGCTCACCGAGGAGGAGCCGGATCTGTCCGGCAACGTCGGCAGGCCGAGCACGGGCCTGCGTCCGGCCCCCCGCACAGCAGCCGGCATCGGACTGGAGATCAGCGGGGCATCGCTGCTCCTGTCCGTCACAGACCTGACCGGAGAGGTCATCGCGCGCCGCTGCGAACTCGTCGCCGACACCGGCCACAACCCTGACACGATGATCGAGCATGTGGCGGCCATGTTGTCCCAGGCCCTGGAGCAGCTGACGCAGCAGGGGACGACAGTGCCGGGCATCGTCCTGGCCCAGCCCGGGATCATCGACTACGCCGACAACACCGTGCGCTACTCCTCCACCCTGGAGTGGCACGACGTCGCCGTGGCGGACCAGGTCCGCGACGCGGTCACCCGCCGCATCGGCCGCGGCCGGAGCGTCCCCGCCATCACACTGGAGAACGACGCCAAGCTCGCCGCACTGGCCACCTATGAGCGCTACGCGCAGGACGGGGTGCGCAACCTGCTCTACCTGTCGGGAGGTGAGGGGATCGGCGCCGGCATCATCTCCGACGGCCACCTCCTGCGCGGCTGGCTGGGCCTGACCGGCGAGGTCGGCCACATGCCCGTGGAGCCCGAGGGCCTGGAGTGCCGGTGCGGGCGGCGCGGCTGCTGGGAGACCCGCTCCGGGCTGCAGGCCCTGACCTCGGCCTACCCGCCGGGCGACGCGGCGCGTGACGAGACCACCTCCCTGGATGAGCGCATCGAGCTCCTGCGCCGGCGCTTCGACGCCGGGGACGCCGAGCTCACCCGGAGACTGGAGCTCTCCCAGCGGGCGCTCGCGCGCGCCCTGGCGATCCTCACGGACGTCCTCAACCCTGAGGTGATCGTGCTGTCGGGGTACCTGGCCGCCTTCGCCGACGTGTTCGTCTCCCCCACCGCCTCCGCCCTGAGGGATCGGCTGCTGGACCAGCGCGCCGCCGTGAGGCTGGAGACCTCCCACCTGGGCCAGTGGGCCTCGTCCTACGGGGCGGCCCTGGTGGCGCTGGAGTCCGTGCTCGACAACCCCACCCTGGTCGATCTCAGGCCCTCCCCCTAG","VPAAGWIPAGGPDLWGTLGGPGTHSPKAHADVRISNMSLILRHLQTSPALSRTRLARETGLSKATVSTLVAELCSRGLLTEEEPDLSGNVGRPSTGLRPAPRTAAGIGLEISGASLLLSVTDLTGEVIARRCELVADTGHNPDTMIEHVAAMLSQALEQLTQQGTTVPGIVLAQPGIIDYADNTVRYSSTLEWHDVAVADQVRDAVTRRIGRGRSVPAITLENDAKLAALATYERYAQDGVRNLLYLSGGEGIGAGIISDGHLLRGWLGLTGEVGHMPVEPEGLECRCGRRGCWETRSGLQALTSAYPPGDAARDETTSLDERIELLRRRFDAGDAELTRRLELSQRALARALAILTDVLNPEVIVLSGYLAAFADVFVSPTASALRDRLLDQRAAVRLETSHLGQWASSYGAALVALESVLDNPTLVDLRPSP$","Xylose repressor","Cytoplasm","putative xylose repressor","putative xylose repressor","ROK family protein","","Titgemeyer F., Reizer J., Reizer A., Saier Jr M.H. Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 1994. 140:2349-2354. PMID: 7952186","","","

InterPro
IPR000600
Family

ROK
PF00480	$\"[221-296]T$	ROK

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.160	$\"[224-425]T$	no description
PTHR18964	$\"[173-423]T$	ROK FAMILY
PTHR18964:SF37	$\"[173-423]T$	GLUCOSE KINASE

","BeTs to 13 clades of COG1940COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1940 is ao-p-z-qvdrlbce-gh---j--t-Number of proteins in this genome belonging to this COG is 5","***** IPB000600 (ROK family) with a combined E-value of 1.5e-13. IPB000600B 218-232 IPB000600C 247-258 IPB000600D 271-277 IPB000600E 286-295","","","-41% similar to PDB:1Z6R Crystal structure of Mlc from Escherichia coli (E_value = 2.8E_19);-42% similar to PDB:1Z05 Crystal structure of the ROK family transcriptional regulator, homolog of E.coli MLC protein. (E_value = 6.4E_16);-40% similar to PDB:2HOE Crystal structure of N-acetylglucosamine kinase (TM1224) from Thermotoga maritima at 2.46 A resolution (E_value = 1.3E_13);-43% similar to PDB:2AA4 Crystal structure of Escherichia coli putative N-ACETYLMANNOSAMINE KINASE, New York Structural Genomics Consortium (E_value = 7.4E_12);-44% similar to PDB:2BCK Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide (E_value = 7.4E_12);","Residues 108 to 303 (E_value = 2e-21) place ANA_1636 in the ROK family which is described as ROK family.","","xylose repressor","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1637","1770585","1772795","2211","5.24","-28.51","81172","ATGTCTCTCCAGACCCAGCCCGCGGCGCCGCTCCCCTCTCAGGCGGGGGGACGCCTCACCCTGCCGATCCAGACCGGCATGGACGAGGAGGTCCGCCGCCTCATCGCCCGCCTGGGCGCCGACGCCGTGCGGAACTCCGACGGCACCGAGCTGCCCGGCATCGTCTCGGAGCTGGCCACCAGGGTCTACTCCACCTACTTCGTGGGACGCGGCGACAACGCCTGGGCCGACGCCCACCCCGATGAGGCCACCCGGATCTTCCTCATGTCCGACCGGGTCGCCGCCACTGCCGACGGCCCTGTCAGCATCGACCTGCTGGCCTCCTGGTTCGCCGACCAGGTCCGCCCCGACACCGGCTGCGACGTGACGCGCTGGTGGCAGGCCCACGACCGCACCACCGGCCAGGAGCTGCCCGTCTCCGCCTGGAGCATCGAAGCCGACGGCCGCACGGTCACCGTGCACGAGGCCCTCGCCGGGCACGTCTACACCGTCAGCTTCCTGGCGATCCAGACCTGGGACCCCACCCAGATGTACAACTACCTCACCAACGGCTGGGACGAGGACCCCACGCGCGTCAAGGACAAGCCCTTCGACGTGCGTCACGAGGCCACGTGGTCCCACGTGCGCACCCACCTGAGCGCCTGGCTCACGGAGCACCCCGAGGTGGACGTGGTCCGCTTCACCACCTTCTTCTACCACTTCACCCTCGTCTACGGCGCCGACGCCACCGAGCGCTTCGTCGACTGGTTCGGCTACTCCGCCTCGGTGAGCGTCCCCGCCCTGGAGGCCTTCGAGGAGGAGTACGGCTACCGCCTGACCGCCGAGGACTTCGTCGACGCCGGCTACTACAACTCCCCCTTCCGGGTGCCCACCCGCGCCTTCCGCGACTGGATCGACTTCCAGCAGCGCTTCGTGTGCTCCCGGGTGCGCGAGCTGACCGACGCCGTCCACGCCCAGGGCAAGGAGGCGATGATGTTCCTGGGCGACAACTGGATCGGCACCGAGCCCTACGGCGAGCACTTCGCCACCACCGGCCTGGACGCCGTCGTCGGCTCGGTCGGATCGGGGGCGACCTGCCGGATGATCGCCGACATCCCGCACGTGCGCTACACCGAGGGCCGGTTCCTGCCGTACTTCTTCCCCGATGTCTTCCACCCGGGGGGCGATCCCGTCTCCGAGGCCAACCGCAGCTGGCTGGAGGCCCGGCGCGCCATCGTGCGCTCCCCCCTGGATCGGATCGGCTACGGCGGTTACCTGTCCCTGGCCGTGGAGCACCCCGATTTCATCGACCGCGTCGAGCAGATCGTCGCGGAGTTCCGCTCCATCCACGAGCGCTCCGCGGGGCTGCGTCCGCTGACCCCGGGCTTCAAGGTCGCGGTCATCAACTCCTGGGGCCGTCTGCGCTCCTGGATGACACATATGGTCGCGCACGCCCTGTGGTACCGCCAGACCTACACCTACCTGGGGGTCCTCGAGGCGCTGTCGGGGCTGCCGGTGGACGTGGAGTTCCTGTCCTTCGACGACGTGCGCGCCGGCCTGGCCCCGGACGTCAAGGTCCTCATCTGCGCCGGCGCCGAGGGGACCGCCTTCTCCGGGGGCGAGCAGTGGGCGGATGCGGAGCTGGTGGCCGCAGTCAGCTCCTTCGTGGCCGGCGGCGGCGGCCTCATCGGGGTCGGGGCTCCCAGCGCCCACCCCGCCCACGGGGTCACCTTCCAGCTCGCCGATGTCCTGGGAGTGGACCGGGAGATCGGCTGGGGCCTGAGCACGCGCCGTCGTGCGCCCGAGGTGGAGGAGCACTTCATCACCCGGGACCTGACCGGCGGCCTCGACGACGGCGAGGGCACCCCCGACATCGTCGTCACCAGTCCCGCCACCCGAGTGCTCGACGCCGCGGACGGCCAGGTCCGCCTCGCGGTCCACGAGCTGGGGAGGGGCCGGGCGGTCTACGCCACGGGACTGCCCTACAGCGCCCAGAACTCCCGGCTGCTGCACCGGGCCATCTTCTGGGCCGCAGGGTGCCAGGAGGAGTTCTCCGCCTGGGCGGCCCTCGACCCCAGGGTGGAGGTGGCCGCCTACCCCGATCGCCGGACCACCCTCGTCATCAACAACTCCCTGGAGCCCGTCACCACGACGGTGCCGACGCCCCAGGGCCCCCGGACGGTCCGTCTGGAGGAAGGAGGGCACCAGTGGCTCACCGCTGCCTCGCAGTGA","MSLQTQPAAPLPSQAGGRLTLPIQTGMDEEVRRLIARLGADAVRNSDGTELPGIVSELATRVYSTYFVGRGDNAWADAHPDEATRIFLMSDRVAATADGPVSIDLLASWFADQVRPDTGCDVTRWWQAHDRTTGQELPVSAWSIEADGRTVTVHEALAGHVYTVSFLAIQTWDPTQMYNYLTNGWDEDPTRVKDKPFDVRHEATWSHVRTHLSAWLTEHPEVDVVRFTTFFYHFTLVYGADATERFVDWFGYSASVSVPALEAFEEEYGYRLTAEDFVDAGYYNSPFRVPTRAFRDWIDFQQRFVCSRVRELTDAVHAQGKEAMMFLGDNWIGTEPYGEHFATTGLDAVVGSVGSGATCRMIADIPHVRYTEGRFLPYFFPDVFHPGGDPVSEANRSWLEARRAIVRSPLDRIGYGGYLSLAVEHPDFIDRVEQIVAEFRSIHERSAGLRPLTPGFKVAVINSWGRLRSWMTHMVAHALWYRQTYTYLGVLEALSGLPVDVEFLSFDDVRAGLAPDVKVLICAGAEGTAFSGGEQWADAELVAAVSSFVAGGGGLIGVGAPSAHPAHGVTFQLADVLGVDREIGWGLSTRRRAPEVEEHFITRDLTGGLDDGEGTPDIVVTSPATRVLDAADGQVRLAVHELGRGRAVYATGLPYSAQNSRLLHRAIFWAAGCQEEFSAWAALDPRVEVAAYPDRRTTLVINNSLEPVTTTVPTPQGPRTVRLEEGGHQWLTAASQ$","Lacto-N-biose phosphorylase","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR012711
Family

Conserved hypothetical protein CHP02336
TIGR02336	$\"[14-732]T$	TIGR02336: conserved hypothetical protein T

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:1HI9 ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE. (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1638","1773082","1774233","1152","5.05","-9.60","40329","ATGACGAAGGTCAACGACATCGTGGCCCGCTGGAACGCCGCGCACCCCGACATGAAGGTCGAGGCCACCAAGTTCGACGGCAAGGCCGCGGACATGAACGTCAAGCTGGAGAACGACGTCAAGGCCGGAACCGGCCCCTGCCTGGCCCAGGTCGGCTACGCCGAGATCCCCAAGCTCTACACCTCCGGCCTGCTCACTGACGTCTCCGCCCAGGCTGAGAAGTACAAGGAGCACTTCTCCGAGGGGTCGATGTCGCTGATGACCGTGGGCAAGACCGTTGTCGGCCTGCCGCAGGACTCCGGCCCGCTGGTCTACTTCTACAACAAGGCAGCCTTCGACCAGCTCGGGCTGAAGGTGCCCACGACGAGCGCCGAGCTGGCCGAGGTCGCCAAGAAGGCGGCCGAGCAGGGCAAGTACGCCCTGGCCTTCGAGCCCGACGAGGCCCCCAACACCCTGGCGGGCCAGGCGGCCGCGGCCAATGCCCAGTGGTTCAGCGCCGAGAACGACAAGTGGAAGGTCAACGTCTCCAGCCCCGAGACCGCCAAGGTCTCCTCCTTCTGGCAGGGGGTCCTGGACTCCAAGACGGCCCTCGTGGCCAACCGCTGGGACGACTCCTTCGGCAAGGCGCTGGTCGACCAGCAGCTCATCGGCACCATCGGAGCCGCCTGGGAGGGCGCGCTCCTGGCCGACACCATGAAGGACTCCCCCAATGCCGGGTCCTGGGCGGTCGCCCAGCTGCCCGCCTTCGGTGACAAGGCCATGTCCGGTCCCGACGGCGGCTCGGGCGTGGCCGTCCTCAAGGGCTGCTCCAACCCCGAGGGGGCCATGGCCTTCAACGACTGGTTCAACACCCAGGTCGACGACCTGGCCACCCAGGGGCTGGTCCTGACCGCGAAGGCCCCGGTGAAGACCCCGCAGACCATCTCCACCTTCTTCGGAGGCCAGGACGTCTACGCCGAGTTCACCAAGGCCAACGCGGCCGTGAACTCCAAGTTCGGCTTCATGCCGACCTGGCCCTCCCTGGCCGACCCCATGACCAAGGCCGCCGAGGCGGCCGGGAAGGGGACCGGCAAGGTCGATGAGATCTTCCAGGCGGCCCAGAAGACCTCGGTCAGCTCCCTGAAGGACGCCAACCTGCCCGTCGCCGAGTAG","MTKVNDIVARWNAAHPDMKVEATKFDGKAADMNVKLENDVKAGTGPCLAQVGYAEIPKLYTSGLLTDVSAQAEKYKEHFSEGSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLGLKVPTTSAELAEVAKKAAEQGKYALAFEPDEAPNTLAGQAAAANAQWFSAENDKWKVNVSSPETAKVSSFWQGVLDSKTALVANRWDDSFGKALVDQQLIGTIGAAWEGALLADTMKDSPNAGSWAVAQLPAFGDKAMSGPDGGSGVAVLKGCSNPEGAMAFNDWFNTQVDDLATQGLVLTAKAPVKTPQTISTFFGGQDVYAEFTKANAAVNSKFGFMPTWPSLADPMTKAAEAAGKGTGKVDEIFQAAQKTSVSSLKDANLPVAE$","ABC-type multiple sugar transport system, substrate-binding component","Periplasm, Membrane, Extracellular","solute binding protein of ABC transporter forsugars","K02027 multiple sugar transport system substrate-binding protein","extracellular solute-binding protein, family 1","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[4-289]T$	SBP_bac_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[103-284]T$	no description

","BeTs to 6 clades of COG1653COG name: Sugar-binding periplasmic proteins/domainsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1653 is -o-pkz--vdrlbcefghs--j--t-Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 289 (E_value = 0.015) place ANA_1638 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","binding protein of ABC transporter for sugars","","1","","","","","","","","","","","Tue Aug 14 16:18:11 2007","","Tue Aug 14 16:18:11 2007","","","Tue Aug 14 16:18:11 2007","","","","Tue Aug 14 16:18:11 2007","Tue Aug 14 16:18:11 2007","","","","","yes","","" "ANA_1639","1774300","1775253","954","9.94","9.93","34365","ATGAGCACGACGACAACGACCACGGGCGCATCCGCCATCCGCACCACCTCGCTGCGAAAGCGCAGGGAGGCCCGGGCGGGCATCGGGTTCGTGGCCCCGTTCCTGGCCATGTTCGCCGTCGTCTTCCTCATTCCGATCGTGGTGTCGGTCTACAGGTCCTTCTTCCGCGACGTCGCCTCCGGCTCGGACCTCTACGGCGGCGGGGAGAAGGTGAGCACCTTCGTGGGCCTGGACAACTACGTCCAGGCGGCGGGACAGCCCGCCTTCTGGAAGGGACTGGGGCGGGTCCTGCTGTTCGGCGTGGTCCAGGTCCCGGTCATGATCCTGGCGGCCCTCGCCCTGGCCCTGGTGCTCGACTCCCTCCTGGTCAAGCGGGTGACGGTCTTCCGCCTGGGCTTCTTCCTGCCCTACGCGATCCCCGGGATCGTGGCCGCCATCATGTGGCTCTACATGTACAACCCCAGCTTCTCCCCCATCAATGAGCTGCTGGGACTGGTGGGCCTCAAGGTGGACTTCTTCGGTCGCAGCATCATCCTGTGGTCGATGGCCAACATCACGACGTGGACCTTCACCGGGTACAACATGCTCATCTTCCTGGCGGCGCTGCAGTCCGTGCCCCGCGAGCTCTACGAGGCCGCCCGCATCGACGGGGCCACCGGGTGGCAGATCGTCCGGCGCATCAAGATCCCCATGGTCCGTTCGGCCTCACTGCTGGCGGTCCTGCTCTCCATCATCGGGACGGTGCAGCTGTTCAACGAGCCCACTGTTCTGTACAGCCAGAACCAGTGGATGGGGCTGGACTACACGCCAATGATGATGGCCTACAACTCGATGACCGGTGCGCTCTCGCCGTCCGGCTCGGGGCCGGCCTCGGCGATCTCCGTCCTCATCGCCCTGGTGGCCGGAGCCCTGGCCGCCCTCTACGCCCTCGTACAGAACAGGATCGACAAGTGA","MSTTTTTTGASAIRTTSLRKRREARAGIGFVAPFLAMFAVVFLIPIVVSVYRSFFRDVASGSDLYGGGEKVSTFVGLDNYVQAAGQPAFWKGLGRVLLFGVVQVPVMILAALALALVLDSLLVKRVTVFRLGFFLPYAIPGIVAAIMWLYMYNPSFSPINELLGLVGLKVDFFGRSIILWSMANITTWTFTGYNMLIFLAALQSVPRELYEAARIDGATGWQIVRRIKIPMVRSASLLAVLLSIIGTVQLFNEPTVLYSQNQWMGLDYTPMMMAYNSMTGALSPSGSGPASAISVLIALVAGALAALYALVQNRIDK$","ABC-type multiple sugar transport system, permease component","Membrane, Cytoplasm","permease of ABC transporter for sugars","K02025 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[89-317]T$	BPD_transp_1
PS50928	$\"[93-308]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-49]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[96-118]?$ $\"[133-153]?$ $\"[177-197]?$ $\"[238-258]?$ $\"[291-311]?$	transmembrane_regions

","BeTs to 13 clades of COG1175COG name: ABC-type sugar transport systems, permease componentsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1175 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 89 to 317 (E_value = 2.8e-12) place ANA_1639 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","of ABC transporter for sugars (permease)","","1","","","","","","","","","","","Tue Aug 14 16:19:00 2007","","Tue Aug 14 16:19:00 2007","","","Tue Aug 14 16:19:00 2007","","","","Tue Aug 14 16:19:00 2007","Tue Aug 14 16:19:00 2007","","","","","yes","","" "ANA_1640","1775250","1776113","864","9.57","6.13","31179","GTGAAGCCCACCGACACTCCTCGCTCGCTGCGCCCGTCGGTGCCCGCACGGGCCGTGACCATCGCGGTTCTGATCATCGTCCTGGCCTACATGCTCGGCCCGGTCTACTGGCTCATCGTCTCCTCCACCAAGTCCAACTCCGACCTGCTGACCACCTCCGGGTGGTGGTTCTCCGGACGCAACAGCTTCTCCACCAACTACAGCGCGCTCATGAGCTGGACCCAGGGGCTCTTCTGGCGCTGGATCCTCAACTCCCTGCTCTACTCGAGCGTCGCCGGGGTGCTGGGCACGCTGCTGTCGGTGGCCGCCGGCTACGGCCTGGCGAAGTTCGAGTTCGCGGGCCGGGGCGCCGTCCAGGTCGTCATCCTCTCCGGCCTGCTCATGCCCATCGCGCTGCTGACCATTCCGCTGTACCTGGTCCTCGACGCCGTGCACCTGACCAACACCGTCTGGTCGATCATCCTGCCGTGCTCGGTCAGCCCCTTCGGGGTCTTCCTGGGCCGCGTCTACGCCGACTCCTCGGTGCCCAACGAGATCATCGACTCCGCCCGCATCGACGGGGCCAGCGAGATCCGTATCTTCTTCACCATCGTGCTGCGGCTGCTCGCACCGGCGATGGTGACCATCTTCCTGTTCATCTTCGTGGCCACCTGGAACAACTTCTTCCTGCCGCTGATGACGATCAACTCCGCCGAGCTCAAGCCCGTCACCCTGGGGCTCTACGGCATGTCGACCTACTTCAACCCCCAGTACGGGGCGCTCCTCCAGGGCGCTCTCCTGGGCGTCATCCCCCTGATCGTGCTGTTCCTTGGCCTGCAGCGCTTCTGGCAGTCCGGCCTGGCCGCCGGCGCCGTCAAGGGCTGA","VKPTDTPRSLRPSVPARAVTIAVLIIVLAYMLGPVYWLIVSSTKSNSDLLTTSGWWFSGRNSFSTNYSALMSWTQGLFWRWILNSLLYSSVAGVLGTLLSVAAGYGLAKFEFAGRGAVQVVILSGLLMPIALLTIPLYLVLDAVHLTNTVWSIILPCSVSPFGVFLGRVYADSSVPNEIIDSARIDGASEIRIFFTIVLRLLAPAMVTIFLFIFVATWNNFFLPLMTINSAELKPVTLGLYGMSTYFNPQYGALLQGALLGVIPLIVLFLGLQRFWQSGLAAGAVKG$","ABC-type multiple sugar transport system, permease component","Membrane, Cytoplasm","permease of ABC transporter for sugars","K02026 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[78-282]T$	BPD_transp_1
PS50928	$\"[82-272]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[19-41]?$ $\"[62-80]?$ $\"[86-108]?$ $\"[120-140]?$ $\"[150-170]?$ $\"[201-221]?$ $\"[252-272]?$	transmembrane_regions

","BeTs to 15 clades of COG0395COG name: Sugar permeasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0395 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 78 to 282 (E_value = 1.2e-16) place ANA_1640 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","of ABC transporter for sugars (permease)","","1","","","","","","","","","","","Tue Aug 14 16:19:23 2007","","Tue Aug 14 16:19:23 2007","","","Tue Aug 14 16:19:23 2007","","","","Tue Aug 14 16:19:23 2007","Tue Aug 14 16:19:23 2007","","","","","yes","","" "ANA_1641","1776198","1777616","1419","5.58","-13.49","51215","ATGATCCACTTCGGCACCGGCGGCTGGAGAGCCGTGATCGGCGATGAGTTCACCCGCGCCAATGTCAGGCTCCTGACCCAGGGGCTGGCCAACCGCATCCTGAAGGAGGGCACGGCCGAGCAGGGCGTCGTCATCGGCTACGACCGGCGCTTCCTGTCCGACACCGCCGCCTGGTGGGCCATTGAGGTGCTCGTCGGCAACGGCATCCGGGTCACCCTCATCGACCGCCCCTCCCCGACCCCCACCACCATGTGGACGGTGCGCCGCCTGGGGGCCGCCTACGGGATGGCCGTAACCGCCTCCCACAACCCGGCCCTGTACAACGGCATCAAGATCTTCCTGCCCGGCGGCCGCGACGCCGACCAGGCCGTCACCGACGAACTCACCGCCTCCCTGCACGGCCTGACCGACGCGGACGTGCGCAGCGTCGAGGCCCATGAGGCCCGCTCCAGCGAGCTCGTCACCATCCAGCGCTCCATCAACTGGTACCTGGACGCCATCATCGACAAGCTCGACACCGAGACCATCCGCCACGCCCACATGCACATCGTGCTGGACCCGATGTTCGGGGTCTCCGAGACGAGCCTGCAGACGATCCTGCTGACCGCCCGCTGCCAGGTGGACGTCATCCACGACCGCCACGACCCTCTCTTCGGGGGCCGCATGCCCTCGCCCACTGAGGGGACCGTCACCACCCTGCGCAACGCCGTCGTCGAGTCCGGCGCGGACCTGGGCATCGCCACCGACGGGGACGCGGACCGCCTGGGCATCATCGACGACACCGGCGCCTACCTCACCCCCAACCAGGTCCTGGTCCTGCTCTACGACTACCTGCTGACCCGCAAGGGGTGGAGCGGTCCGGCTGTGCGCAACATGTCCACCACTCACCTGCTGGACCGGGTCGCGGCCGCCCACGGGCAGGTCTGCTACGAGGTGCCCGTCGGCTTCAAGTGGATCAGCGCCAAGATGGCCGAGACCGGGGCCGTCATCGGGGGCGAGTCCTCCGGGGGCCTGACCGTGCGCGGTCACATCCCCGGCAAGGACGGGGTCTACGCCGGCTCGCTACTGGTGGAGGCGGTGGCGGCCTCGGGCAAGCGGCTCTCCGAGCTCTACGCCGACATCGTGGCCCGGTACGGTGAGCTCGTCATGGTGGAGAACGCCTACGGCTTCACCTCCGAGCGGCGTACTGAGCTTCAGGAGCGCATCTTCGGGGCTCACGACCTGCCCGACTTCACCCACGATGTCGAGCGCGTCTCGTGGGAGGACGGCTGCAAGGTCTACTTCACCTGCGGCGGCTGGGTGACGATCCGCTTCTCGGGTACCGAGCCGCTCCTGCGGGTCTTCGCCGAGATGCCCACCGGTGACGAGGCCCGGGCGACCGCGGCCGCCGTCGCGAGCCACTACGGCCTGGATGCCTGA","MIHFGTGGWRAVIGDEFTRANVRLLTQGLANRILKEGTAEQGVVIGYDRRFLSDTAAWWAIEVLVGNGIRVTLIDRPSPTPTTMWTVRRLGAAYGMAVTASHNPALYNGIKIFLPGGRDADQAVTDELTASLHGLTDADVRSVEAHEARSSELVTIQRSINWYLDAIIDKLDTETIRHAHMHIVLDPMFGVSETSLQTILLTARCQVDVIHDRHDPLFGGRMPSPTEGTVTTLRNAVVESGADLGIATDGDADRLGIIDDTGAYLTPNQVLVLLYDYLLTRKGWSGPAVRNMSTTHLLDRVAAAHGQVCYEVPVGFKWISAKMAETGAVIGGESSGGLTVRGHIPGKDGVYAGSLLVEAVAASGKRLSELYADIVARYGELVMVENAYGFTSERRTELQERIFGAHDLPDFTHDVERVSWEDGCKVYFTCGGWVTIRFSGTEPLLRVFAEMPTGDEARATAAAVASHYGLDA$","Phosphomannomutase","Cytoplasm","Phosphomannomutase","phosphoglucomutase/phosphomannomutase ","Phosphomannomutase","","Dai J.B., Liu Y., Ray Jr W.J., Konno M. The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution. J. Biol. Chem. 1992. 267(9):6322-6337. PMID: 1532581Zielinski N.A., Chakrabarty A.M., Berry A. Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase. J. Biol. Chem. 1991. 266(15):9754-9763. PMID: 1903398","","","

InterPro
IPR005841
Family

Phosphoglucomutase/phosphomannomutase
PR00509	$\"[94-108]T$ $\"[180-199]T$ $\"[214-227]T$ $\"[242-257]T$	PGMPMM
PS00710	$\"[95-104]T$	PGM_PMM

InterPro
IPR005844
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I
PF02878	$\"[1-139]T$	PGM_PMM_I

InterPro
IPR005845
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II
PF02879	$\"[161-264]T$	PGM_PMM_II

InterPro
IPR005846
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III
PF02880	$\"[266-378]T$	PGM_PMM_III

noIPR
unintegrated

unintegrated
G3DSA:3.40.120.10	$\"[4-172]T$ $\"[182-258]T$ $\"[264-383]T$	no description
PTHR22573	$\"[60-466]T$	PHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF2	$\"[60-466]T$	PHOSPHOGLUCOMUTASE

InterPro
IPR005835
Domain

Nucleotidyl transferase
PF00483	$\"[18-276]T$	NTP_transferase

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[15-273]T$	no description
PTHR22572	$\"[53-239]T$	SUGAR-1-PHOSPHATE GUANYL TRANSFERASE

","BeTs to 8 clades of COG1209COG name: dTDP-glucose pyrophosphorylaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1209 is aompkz--vdrlbcef--sn-j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","-44% similar to PDB:1FXO THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TMP COMPLEX. (E_value = 2.7E_11);-44% similar to PDB:1FZW THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). APO ENZYME. (E_value = 2.7E_11);-44% similar to PDB:1G0R THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). THYMIDINE/GLUCOSE-1-PHOSPHATE COMPLEX. (E_value = 2.7E_11);-44% similar to PDB:1G1L THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-GLUCOSE COMPLEX. (E_value = 2.7E_11);-44% similar to PDB:1G23 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). GLUCOSE-1-PHOSPHATE COMPLEX. (E_value = 2.7E_11);","Residues 18 to 276 (E_value = 9e-11) place ANA_1642 in the NTP_transferase family which is described as Nucleotidyl transferase.","","thymidylyltransferase (grad)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1644","1778535","1779743","1209","6.19","-2.92","41885","GTGCCCGGGCGCGTCGAGGTGCTGGGCAAGCACACCGACTACGCCGGCGGCTCGGTCCTGGTCGGCGCCGTCGACCGGGCGATCACGGCGCGGACGCGTCGCGTGGCAGGGCCGCTGGGGTCACTGACCGCCACCACGGACTACGGCGATCCGGTGACCCTGCGCGCCGGGGTGGACCCGGGCCTGGAGCCGGGCCACTGGGGCCGCTACCTTCAGACCGTGCTGGACCGCCTCACCCTCAACTTCGGGGCGGGCGCCGCGGCCCACCTGTCCCTCTCCTCGGACCTGCCGCCGGCCTCTGGGATGAGCTCGTCCTCCGCGCTGGTGTGCGCCACGGCCCTGGCCCTGGCCTCCCTCAACGGCTGGGACAAGGATCCCCGGTGGGTCGAGTCGATGCCCGACCGGCTGTCCCTGGCCGGCTACCTCGCCGCCGTGGAGGGCGGACGGGCGTGGCGGGACCTGCCGGGGACCAGCGGAGTCGGTACCCGCGGCGGGAGCGAGGACCACACCGGCATGCTGTGCGGTGCCCAGGACCGGCTGCTCCTGGCCGGATTCGACCCGATGCGCATCGATCAGACCATCTCCTTCCCCACCCAGTGGGCGCTCGTCGTCGGCGTGAGCGGGGTGCTGGCCCAGAAGACCGGCGCGGCCCTGGAGGACTACAACCGCGGGCCGAACACCGTCCAGGCGGTGCTGGCCAGGTGGAATGAGACCACCGGACGCACTGACGCCTCCCTGGCCGGCGCGGTCAGGCACCTGATCGGGGAGGCCACCGGCGAGCAGGCGGCCGGCGACCCGGCTCTGAAGAAACTGCTGGGGCTGTGCGAGCCCGGCTACGAGAGGCAGCGCATCGAGCAGTTCCTCATCGAGTCCCTCGTCCTGGTTCCCGCCGGTGCCCGGATGATCGCCGCGGCCGACCCGGACGTAGGTGAGGTCCTCCGGCGCTCCCAGGAGCTGGCCGACCGCGGCCTGGGCAACCAGGTGCCGCAGACTCGGCTCATGGTGTCGTTGGCCCGCAAGGCGGGCGCCATTGGCGCCTCCTCCTTCGGCGCCGGGTGGGGCGGGTCGGTGTACGCCCTGGTGCGGGCCGACGACGCCGAGACCTTCGCCGCGCAGTGGCTCGGGGCCTACCGGGACCGCGAGCCGGGCGCGGAGCAGGCCGCGGTGATCGTCACCAGGCCGGGGCCGGGGGCCTGCCGGCTGCTCTGA","VPGRVEVLGKHTDYAGGSVLVGAVDRAITARTRRVAGPLGSLTATTDYGDPVTLRAGVDPGLEPGHWGRYLQTVLDRLTLNFGAGAAAHLSLSSDLPPASGMSSSSALVCATALALASLNGWDKDPRWVESMPDRLSLAGYLAAVEGGRAWRDLPGTSGVGTRGGSEDHTGMLCGAQDRLLLAGFDPMRIDQTISFPTQWALVVGVSGVLAQKTGAALEDYNRGPNTVQAVLARWNETTGRTDASLAGAVRHLIGEATGEQAAGDPALKKLLGLCEPGYERQRIEQFLIESLVLVPAGARMIAAADPDVGEVLRRSQELADRGLGNQVPQTRLMVSLARKAGAIGASSFGAGWGGSVYALVRADDAETFAAQWLGAYRDREPGAEQAAVIVTRPGPGACRLL$","Galactokinase","Cytoplasm, Extracellular","N-acetylgalactosamine kinase (GalNAckinase)(Galactokinase 2), putative","galactokinase ","GHMP kinase, C terminal domain protein","","Tsay Y.H., Robinson G.W. Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase. Mol. Cell. Biol. 1991. 11(2):620-631. PMID: 1846667Lee M., Leustek T. Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene. Arch. Biochem. Biophys. 1999. 372(1):135-142. PMID: 10562426","","","

InterPro
IPR000705
Family

Galactokinase
PR00473	$\"[3-21]T$ $\"[67-78]T$ $\"[87-105]T$	GALCTOKINASE

InterPro
IPR006203
Domain

GHMP kinase, ATP-binding region
PS00627	$\"[96-107]?$	GHMP_KINASES_ATP

InterPro
IPR006204
Domain

GHMP kinase
PF00288	$\"[89-162]T$	GHMP_kinases_N

InterPro
IPR006206
Family

Mevalonate and galactokinase
PR00959	$\"[1-25]T$ $\"[94-116]T$ $\"[166-185]T$ $\"[345-362]T$	MEVGALKINASE

InterPro
IPR013750
Domain

GHMP kinase, C-terminal
PF08544	$\"[301-379]T$	GHMP_kinases_C

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[1-207]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.890	$\"[309-398]T$	no description
PTHR10457	$\"[58-121]T$	MEVALONATE KINASE/GALACTOKINASE
PTHR10457:SF7	$\"[58-121]T$	GALACTOKINASE 2

","BeTs to 7 clades of COG0153COG name: GalactokinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0153 is ----k-y-v-rlb-e-gh------t-Number of proteins in this genome belonging to this COG is 2","***** IPB000705 (Galactokinase) with a combined E-value of 2.6e-19. IPB000705A 1-24 IPB000705C 87-108 IPB000705D 155-188 IPB000705H 345-358***** IPB006203 (GHMP kinase, ATP-binding region) with a combined E-value of 1e-08. IPB006203A 1-16 IPB006203B 96-110","","","No significant hits to the PDB database (E-value < E-10).","Residues 89 to 162 (E_value = 9e-07) place ANA_1644 in the GHMP_kinases_N family which is described as GHMP kinases N terminal domain.Residues 301 to 379 (E_value = 2.2e-07) place ANA_1644 in the GHMP_kinases_C family which is described as GHMP kinases C terminal.","","kinase (GalNAc kinase)(Galactokinase 2), putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1645","1781064","1779763","1302","5.04","-19.43","46638","GTGGCCGAGGGCGGGGGGCGAATCGACTCCGAGACCGGCGCCCTGCGCGAGGTGATCGTCCACCGTCCCGGTGGGGAGATCGCCCGCCTGACCCCCATCAACGCCGACTCCCTGCTCTTCGACGACGCCCTCAACATCCCCCGGGCCCAGGCCGAGCACGACGCCTTCACCGCGATCCTGCGCTCCGAGGGGGTCATCGTCCACGACTTCCGCGAGCTGTTCACCGAGGTCCTGGCCGTCCCCGAGGCCCGCCGGCTGGTCCTGGACGAGGCCGTCGGTCCCGACGTCGTCGGCGTCTCCGCCTCCGAGCTGCTCATTGACTACTTCCAGTCCCTGCCCGACGCCGACCTCGCCGAGGTGCTCCTGGGCGGCATCACCCGCACCGAGCTGCGCGATCGCCTCAGCTCCTCCGAGGGGCGCGACCTGTTCTCCTCCACCTACCTGTCCACCCTCGAGGGGCCGTTCGTCGTCACCCCCCTGCCCAACCTGCTCTTCACCCGCGACGCGTCGGCCTGGCTCTACGGCGGGGTCTCGGTCAACTCCATGGCCCTGGAGCCGCGCCGTCGTGAGGCCATTGGCTATGAGGCCGTCTACCGCCACCACCCGGCCTTCGGCCCGCGCCTGGCCGAGCTCGCCGGCTGCGATGACCCGGAGGCCCGCCTGTGGCGAGAGGTGGGGCGGGTCTCGGCCGCCTCGACCATCGAGGGCGGCGACTTCCAGATCCTGGGCAACCGGACCCTCGTCATGGGCCTGACCCACCGCTCCACCGCTGCCGGCGTGGAGCGCCTGGCCTCCCAGCTCTTCGCCTCCGGCGTGGCCGACCGGGTCATCGGTGTCCACATGCCCGACGCCGCCTTCTACACCCAGCTCGAGGCCGTCATGCACCTGGACACCCTCATGACAATGGTCAGCCCCGACACCTACCTGCGCTTCCCCGGATTCACCGAGGTCACCACCGTGGAGATCGAGCCCGCAGCGGCCGGACGCTCCCTCCAGGTGACGGTCCACGACGGCTCTCAGATGGATGCGGTCCTCGCTCGCGCCGCCGGCATCGACTCCTTCCGCGTCATCAGCCCCGGCGCCTCCGACGAGGCCGAGGCCCTGCGCGAGCTCGCCCGGGACTCCTGCAACGTCGTGGCCCTTGCCCCCTGGCGCGTCATCGGCTACGCCCACAACCAGCGCGCCAACGACGCCCTGCGCAAGGCCGGCATCGAGGTCGTCGAGACCCCCGGCGTCGAGCTCGTGCGCGGCCGCGGCGGCTCGCACTGCATGACCTGCCCCGTCACCCGCGACGCGGTGTGA","VAEGGGRIDSETGALREVIVHRPGGEIARLTPINADSLLFDDALNIPRAQAEHDAFTAILRSEGVIVHDFRELFTEVLAVPEARRLVLDEAVGPDVVGVSASELLIDYFQSLPDADLAEVLLGGITRTELRDRLSSSEGRDLFSSTYLSTLEGPFVVTPLPNLLFTRDASAWLYGGVSVNSMALEPRRREAIGYEAVYRHHPAFGPRLAELAGCDDPEARLWREVGRVSAASTIEGGDFQILGNRTLVMGLTHRSTAAGVERLASQLFASGVADRVIGVHMPDAAFYTQLEAVMHLDTLMTMVSPDTYLRFPGFTEVTTVEIEPAAAGRSLQVTVHDGSQMDAVLARAAGIDSFRVISPGASDEAEALRELARDSCNVVALAPWRVIGYAHNQRANDALRKAGIEVVETPGVELVRGRGGSHCMTCPVTRDAV$","Arginine deiminase","Cytoplasm","arginine deiminase","arginine deiminase ","Arginine deiminase","","Kanaoka M., Fukita Y., Taya K., Kawanaka C., Negoro T., Agui H. Antitumor activity of streptococcal acid glycoprotein produced by Streptococcus pyogenes Su. Jpn. J. Cancer Res. 1987. 78(12):1409-1414. PMID: 3123442","","","

InterPro
IPR003198
Domain

Amidinotransferase
PF02274	$\"[10-430]T$	Amidinotransf

InterPro
IPR003876
Family

Arginine deiminase
PR01466	$\"[4-24]T$ $\"[159-177]T$ $\"[187-202]T$ $\"[369-386]T$ $\"[389-403]T$ $\"[412-430]T$	ARGDEIMINASE

noIPR
unintegrated

unintegrated
G3DSA:3.75.10.10	$\"[159-428]T$	no description

","BeTs to 8 clades of COG2235COG name: Arginine deiminaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2235 is -o-p------rl---fg----j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB003876 (Bacterial arginine deiminase signature) with a combined E-value of 2.8e-44. IPB003876A 4-24 IPB003876B 159-177 IPB003876C 187-202 IPB003876D 369-386 IPB003876E 389-403 IPB003876F 412-430***** IPB003198 (Amidinotransferase) with a combined E-value of 2.7e-43. IPB003198A 10-41 IPB003198B 166-190 IPB003198C 294-314 IPB003198D 399-430","","","-51% similar to PDB:1RXX Structure of arginine deiminase (E_value = 1.4E_66);-51% similar to PDB:2ABR Structure of D280A arginine deiminase with L-arginine forming a S-alkylthiouronium reaction intermediate (E_value = 1.2E_65);-51% similar to PDB:2ACI Structure of D166A arginine deiminase (E_value = 1.2E_65);-51% similar to PDB:2A9G Structure of C406A arginine deiminase in complex with L-arginine (E_value = 1.5E_65);-51% similar to PDB:2AAF Structure of H278A arginine deiminase with L-arginine forming a S-alkylthiouronium reaction intermediate (E_value = 2.0E_65);","Residues 10 to 430 (E_value = 6.6e-97) place ANA_1645 in the Amidinotransf family which is described as Amidinotransferase.","","deiminase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1646","1781304","1781498","195","9.19","3.10","7017","ATGAAATCTGTTGTCCGCATCTCCCTGGTCGCACTCCTCATGGCGGGCTTCGCCGCGCCGGCCAGCGCCGCGCCGGCCACCGCCCCCGCCCGCCACGACGACTCAGCGAGCGCCTTCCTGAGGCCCCGTCCCGACTGGTGCATCTTCCCCCCCAGTGCTTGGTGCGACTGGAAGACGAACCGCTGGTACTCCTGA","MKSVVRISLVALLMAGFAAPASAAPATAPARHDDSASAFLRPRPDWCIFPPSAWCDWKTNRWYS$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide

noIPR
unintegrated

unintegrated
signalp	$\"[1-96]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[47-67]?$ $\"[72-90]?$ $\"[96-114]?$ $\"[124-144]?$	transmembrane_regions

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[166-218]T$	Q8XWL9_RALSO_Q8XWL9;
PR00038	$\"[166-180]T$ $\"[180-196]T$ $\"[196-208]T$	HTHLUXR
PF00196	$\"[163-220]T$	GerE
SM00421	$\"[163-220]T$	HTH_LUXR
PS50043	$\"[159-223]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[9-124]T$	Q6NKE1_CORDI_Q6NKE1;
PF00072	$\"[9-125]T$	Response_reg
SM00448	$\"[9-124]T$	REC
PS50110	$\"[10-128]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[157-220]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[4-132]T$	no description
PTHR23283	$\"[5-113]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF43	$\"[5-113]T$	TWO-COMPONENT SENSOR PROTEIN HISTIDINE PROTEIN KINASE (SENSOR PROTEIN TORS)

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 5.5e-14. IPB000792 166-212***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 1e-10. IPB001867A 58-71 IPB001867B 86-130***** IPB001789 (Response regulator receiver) with a combined E-value of 2.6e-08. IPB001789A 58-71 IPB001789B 106-116***** IPB000673 (CheB methylesterase) with a combined E-value of 3e-08. IPB000673A 12-21 IPB000673B 30-83***** IPB005143 (Autoinducer binding domain) with a combined E-value of 9.3e-07. IPB005143B 166-209","","","-59% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 7.9E_29);-59% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 7.9E_29);","Residues 9 to 125 (E_value = 3.1e-31) place ANA_1648 in the Response_reg family which is described as Response regulator receiver domain.Residues 156 to 208 (E_value = 3.7e-10) place ANA_1648 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 163 to 220 (E_value = 3.2e-12) place ANA_1648 in the GerE family which is described as Bacterial regulatory proteins, luxR family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1649","1783541","1784620","1080","6.31","-3.88","39494","ATGAACGCCACCACCGCCCACCCGCTGCCGCGCCGAGTCTCAGAGATCTTCTCCCCCGACCGCTGGCGGGAGGTGTCCGGTTTCCCCCACGCCGAGGCCGGCACGGAGCCCTCACAGCAGCAGGCACAGGCCCTCACGGACATCACCTACCACAGGGGCTGCGTCCGAGACGAGGACGGCACCTGGCTCCGGGACCTGCCGGTGGTCCGGGTGGCCTTCAACCGGCCCGAGGTCCGTAACGCCTTCCGCCCCCGCACCGTCGATGAGCTCTACCGGGTCCTGGACCACGCGCGCATGAGCGGCGACGTCGGCGCCGTCATCCTCACCGGCAACGGCCCCTCGCCGCGCGACGGCGGCTGGGCCTTCTCCTCCGGCGGCGACCAGCGCATCCGCGGCCGGGACGGCTACCGCTACGAGCGGGAGGCCTCGCCGCAGTCCCCAACGGCCGCCGGCGAGCCCGAGGATCGCGCCTACAGCCACGAGGCCGACGTTGCCGCCGCCCAGGCCCGCCTCGACACCGCACGGGCCGGCCGGCTCCACATCCTGGAGGTTCAGCGCCTCATCCGCACCATGCCCAAGGCCGTCATCGCCGCTGTCCCGGGCTGGGCCGCCGGCGGCGGTCACAGCCTCAACGTCGTGTGCGACCTGTCGCTGGCCTCGATCGAGCACGCGCGCTTCAAGCAGACTGACGCCGATGTCGGCAGCTTCGACGCCGGCTACGGCTCCGCGCTCCTGGCCCGGCAGGTCGGGGACAAGCGGGCCCGTGAGATCTTCTTCCTGGCCCGCACCTACGACGCCGTCACCGCCGAGCGCTGGGGCGTCGTCAATGAGGCGGTCCCCCACGCTGAGCTCGAGGAACGGGCCCTGGAGTACGCGGCCACCGTGGCGGGCAAGTCCCCGCAGGCCATCCGCATGCTCAAGCTCGCCTTCAACCTGGCCGACGACGGCCTGGCCGGCCAGCAGGTCTTCGCCGGCGAGGCCACACGCCTGGCCTATATGACCGACGAGGCCGTAGAGGGGCGCGATGCATTCCTCCAGCGCCGTACTCCCGACTGGTCGCCCTTCCCGTACTACTTCTGA","MNATTAHPLPRRVSEIFSPDRWREVSGFPHAEAGTEPSQQQAQALTDITYHRGCVRDEDGTWLRDLPVVRVAFNRPEVRNAFRPRTVDELYRVLDHARMSGDVGAVILTGNGPSPRDGGWAFSSGGDQRIRGRDGYRYEREASPQSPTAAGEPEDRAYSHEADVAAAQARLDTARAGRLHILEVQRLIRTMPKAVIAAVPGWAAGGGHSLNVVCDLSLASIEHARFKQTDADVGSFDAGYGSALLARQVGDKRAREIFFLARTYDAVTAERWGVVNEAVPHAELEERALEYAATVAGKSPQAIRMLKLAFNLADDGLAGQQVFAGEATRLAYMTDEAVEGRDAFLQRRTPDWSPFPYYF$","Naphthoate synthase","Cytoplasm","naphthoate synthase","naphthoate synthase ","naphthoate synthase","","Minami-Ishii N., Taketani S., Osumi T., Hashimoto T. Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system. Eur. J. Biochem. 1989. 185(1):73-78. PMID: 2806264Muller-Newen G., Stoffel W. Mitochondrial 3-2trans-Enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid beta-oxidation. Biol. Chem. Hoppe-Seyler 1991. 372(8):613-624. PMID: 1958319Palosaari P.M., Hiltunen J.K. Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. J. Biol. Chem. 1990. 265(5):2446-2449. PMID: 2303409Nakahigashi K., Inokuchi H. Nucleotide sequence of the fadA and fadB genes from Escherichia coli. Nucleic Acids Res. 1990. 18(16):4937-4937. PMID: 2204034Driscoll J.R., Taber H.W. Sequence organization and regulation of the Bacillus subtilis menBE operon. J. Bacteriol. 1992. 174(15):5063-5071. PMID: 1629163Babbitt P.C., Kenyon G.L., Martin B.M., Charest H., Slyvestre M., Scholten J.D., Chang K.H., Liang P.H., Dunaway-Mariano D. Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases. Biochemistry 1992. 31(24):5594-5604. PMID: 1351742Beckman D.L., Kranz R.G. A bacterial homolog to the mitochondrial enoyl-CoA hydratase. Gene 1991. 107(1):171-172. PMID: 1743516Eichler K., Bourgis F., Buchet A., Kleber H.P., Mandrand-Berthelot M.A. Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol. Microbiol. 1994. 13(5):775-786. PMID: 7815937","","","

InterPro
IPR001753
Domain

Enoyl-CoA hydratase/isomerase
PF00378	$\"[69-280]T$	ECH

InterPro
IPR010198
Family

Naphthoate synthase
TIGR01929	$\"[45-355]T$	menB: naphthoate synthase

noIPR
unintegrated

unintegrated
G3DSA:3.90.226.10	$\"[50-353]T$	no description
PTHR11941	$\"[64-153]T$ $\"[189-352]T$	ENOYL-COA HYDRATASE-RELATED

","BeTs to 8 clades of COG0447COG name: Dihydroxynaphthoic acid synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0447 is ao--------rlbce-gh--------Number of proteins in this genome belonging to this COG is 1","***** IPB001753 (Enoyl-CoA hydratase/isomerase) with a combined E-value of 2.5e-24. IPB001753A 67-78 IPB001753B 111-133 IPB001753C 193-219 IPB001753D 224-250","","","-66% similar to PDB:1Q51 Crystal Structure of Mycobacterium tuberculosis MenB in Complex with Acetoacetyl-Coenzyme A, a Key Enzyme in Vitamin K2 Biosynthesis (E_value = 7.4E_108);-66% similar to PDB:1Q52 Crystal Structure of Mycobacterium tuberculosis MenB, a Key Enzyme in Vitamin K2 Biosynthesis (E_value = 7.4E_108);-66% similar to PDB:1RJM Crystal Structure of MenB (Rv0548c) from Mycobacterium tuberculosis (E_value = 7.4E_108);-66% similar to PDB:1RJN The Crystal Structure of MenB (Rv0548c) from Mycobacterium tuberculosis in Complex with the CoA Portion of Naphthoyl CoA (E_value = 7.4E_108);-39% similar to PDB:1UIY Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8 (E_value = 2.7E_17);","Residues 69 to 280 (E_value = 5.9e-26) place ANA_1649 in the ECH family which is described as Enoyl-CoA hydratase/isomerase family.","","synthase (menB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1650","1785952","1785005","948","4.51","-26.76","32876","ATGAGCGACCGCGACGACACTCACGAGGACGCCATCAACGGCGAGGCCGATCTGCAGGGCACCGAGGGTCTCGACGGCACGCAGAGTGGAGACGACGTCGAGTACTTCGACGACGAGCTCGACTCGGAGACGGCCGCCCTGCTGGGGGCCGCACTGCGGCCCGTGGACCCGCCGACAGCGATCCGCGCCTCCCTTCTGGAGACCATTGCGCGCGAGCCCCAGACGGAACGCGCAGACCAGGCCGACGACACCGCGGAGGAGGAAGCCGGCGACCGCGACGCTCTCGGTGGCAGTAACAGAGGCAGCAACAGCGACAGTGATGGTGACAGTGATGGCGACTCGGTGGGCTCTGAGGTCCTCAGTCTCGATGCGCACCGCCGTCGCCGCTCGACCTGGCGCACCGGCCTGCTGCGGGCGGCCGCGGCCGTGGTCCTGCTCAGTGTCGGCATCGGTGTGGGGCGCTGGAGCGTGCGGGGCGCGGTCGATGAGGCCAAGGACTCCATGGCCAGCTCCATGGCATCGACCCAGCACTACGCCCACCTCAACCAGGCCCAGGACGTCCAGCGGGTCACCGACACGATGCCCGACGGGCACGTCGCGACCCTCACCTGGTCCCGGGACATGAGCATGACCGCGCTGACCCTCCCGGCCGCCATGAAGGAGTCCGCCAGTGGGCGCAGCCTCCAGGTCTGGCTCAAAGAGGGGGAGACGACCACCTCACTGGGCGTCTACGACCCCCGGGACGGGGCCGGCTTCTCCTTCCTGGACGTCATGCCCAAGCCCGGCCAGCAGATCGTCATCACCATGGAGCCGGCCGGAGGATCGGCCCAGCCGACGACGCCGCCCCTGGTCACCCTGCGAGTGAGTGAGGATGCCGGCCGGTCCGGCGCCGCCACCGGCTCGCCGAGCCCCACGTCCTCGGCCGCTCCCACCGGAGACTCCGCCTAG","MSDRDDTHEDAINGEADLQGTEGLDGTQSGDDVEYFDDELDSETAALLGAALRPVDPPTAIRASLLETIAREPQTERADQADDTAEEEAGDRDALGGSNRGSNSDSDGDSDGDSVGSEVLSLDAHRRRRSTWRTGLLRAAAAVVLLSVGIGVGRWSVRGAVDEAKDSMASSMASTQHYAHLNQAQDVQRVTDTMPDGHVATLTWSRDMSMTALTLPAAMKESASGRSLQVWLKEGETTTSLGVYDPRDGAGFSFLDVMPKPGQQIVITMEPAGGSAQPTTPPLVTLRVSEDAGRSGAATGSPSPTSSAAPTGDSA$","Conserved hypothetical protein","Periplasm, Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Novoseler M., Hershkovits G., Katcoff D.J. Functional domains of the yeast chromatin protein Sin1p/Spt2p can bind four-way junction and crossing DNA structures. J. Biol. Chem. 2005. 280(7):5169-5177. PMID: 15563464","","","

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[63-139]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[135-155]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-50% similar to PDB:2B9W Crystal Structure of CLA-producing fatty acid isomerase from P. acnes (E_value = );-50% similar to PDB:2B9X Crystal Structure of CLA-producing fatty acid isomerase from P. acnes (E_value = );-50% similar to PDB:2B9Y Crystal structure of CLA-producing fatty acid isomerase from P. acnes (E_value = );-50% similar to PDB:2BA9 Crystal structure of CLA-producing fatty acid isomerase from P. acnes (E_value = );-50% similar to PDB:2BAB Crystal structure of CLA-producing fatty acid isomerase from P. acnes (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1651","1786581","1785949","633","9.60","4.66","23669","ATGAGCCTGGCCACGCTGGAGGCGCGGAACGGGACGCGCACCGCCTCCGCCCGTGCACTCGCCTACCATTCCCCTGTGACACGCAGCAACTGCGCCGGCTCAGAGGGAGAGTGGATCGCGCAGGTGGCCGACGGTGACGCCGACGCCTTCGCCCGCCTCTACGACGCCTGGTCCTCTCGGCTGTTCGCGCTGATCGTCCAGATCGTCGTCGATCGCGCCCAGAGCGAGGAGGTCCTCCAGGAGGTCTTCCTCGAGGTGTGGCGCACGGCAGGCTCCTACTCCCCGGCGCGGGGCAGCGTCCGGGCCTGGCTGGTGACCATGGCCAGGCGCCGGGCCATCGACCGGGTCCGCTCCTCCCAGTCCTCCCGGGAGCGGGAGAGCCGCTGGCGTGACTACATGCCCGACGTCGACCAGACGGTTCAGCAGGTCGAGGACAGACTCGTGGGCGAACAGGTGCACCGGGCGCTCGAGGCGGTGGGGGAGCCCTACCGCTCCACCATTGAGCTCGCCTACTTCACAGGTCTGACCCACCGCGAGATCGCCCGCCGCACGGGCACGCCGCTGGGAACGGTCAAAACCCGCATCAGGGACGGAATGGCACGGTTACGACGAGAGCTGGGGGTGCAGTCATGA","MSLATLEARNGTRTASARALAYHSPVTRSNCAGSEGEWIAQVADGDADAFARLYDAWSSRLFALIVQIVVDRAQSEEVLQEVFLEVWRTAGSYSPARGSVRAWLVTMARRRAIDRVRSSQSSRERESRWRDYMPDVDQTVQQVEDRLVGEQVHRALEAVGEPYRSTIELAYFTGLTHREIARRTGTPLGTVKTRIRDGMARLRRELGVQS$","RNA polymerase sigma factor","Cytoplasm","RNA polymerase sigma factor","K03088 RNA polymerase sigma-70 factor; ECF subfamily","sigma-70 region 2 domain protein","","Helmann J.D., Chamberlin M.J. Structure and function of bacterial sigma factors. Annu. Rev. Biochem. 1988. 57:839-872. PMID: 3052291Gribskov M., Burgess R.R. Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins. Nucleic Acids Res. 1986. 14(16):6745-6763. PMID: 3092189Lonetto M., Gribskov M., Gross C.A. The sigma 70 family: sequence conservation and evolutionary relationships. J. Bacteriol. 1992. 174(12):3843-3849. PMID: 1597408Campbell E.A., Muzzin O., Chlenov M., Sun J.L., Olson C.A., Weinman O., Trester-zedlitz M.L., Darst S.A. Structure of the bacterial RNA polymerase promoter specificity sigma subunit. Mol. Cell 2002. 9(3):527-539. PMID: 11931761Malhotra A., Severinova E., Darst S.A. Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase. Cell 1996. 87(1):127-136. PMID: 8858155","","","

InterPro
IPR007627
Domain

RNA polymerase sigma-70 region 2
PF04542	$\"[53-122]T$	Sigma70_r2

InterPro
IPR013249
Domain

RNA polymerase sigma factor 70, region 4 type 2
PF08281	$\"[149-202]T$	Sigma70_r4_2

InterPro
IPR014284
Domain

RNA polymerase sigma-70
TIGR02937	$\"[48-206]T$	sigma70-ECF: RNA polymerase sigma factor, s

noIPR
unintegrated

unintegrated
G3DSA:1.10.1740.10	$\"[37-124]T$	no description

","BeTs to 11 clades of COG1595COG name: DNA-directed RNA polymerase specialized sigma subunits, sigma24 homologsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1595 is --------vdrlbcefghsn-j--t-Number of proteins in this genome belonging to this COG is 3","***** IPB000838 (Sigma factor, ECF subfamily) with a combined E-value of 1e-19. IPB000838A 77-113 IPB000838B 156-202 IPB000838A 78-114***** IPB007630 (Sigma-70 region 4) with a combined E-value of 1.5e-10. IPB007630A 71-104 IPB007630B 176-203 IPB007630A 77-110","","","No significant hits to the PDB database (E-value < E-10).","Residues 53 to 122 (E_value = 7.7e-18) place ANA_1651 in the Sigma70_r2 family which is described as Sigma-70 region 2.Residues 149 to 202 (E_value = 1e-11) place ANA_1651 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 155 to 204 (E_value = 6.5e-11) place ANA_1651 in the Sigma70_r4 family which is described as Sigma-70, region 4.","","polymerase sigma factor (AL133424)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1652","1788249","1786621","1629","6.47","-3.51","57155","GTGCTCCCCGTCATCCTCCTCTCCGCAGGAGCACAGGGCGCACGCGGCGATGGCGGCGATGACAAGGGGGCCGACGGCGGCTTCGCCTCCCGCTTCCACCCGTACCTCGTGGTAACCGGCCTTGTGGTCAGTTTCACGGTCTTCACGCTCCTCGGATCGACCGTGCTGAGCCTGCTCCACCTGCCGCAGGACCTCATCCGCTGGGTCGGCATCGTCATGCTCGCCCTGATCGGCCTGGGCATGATGGTCCCGAAGGTCATGGAGATCCTCGAGCGCCCCTTCGCGCGCTTCCAGCGCTTCGGCGGCTCGAAGAACCCCTCCAACGGCTTCCTTCTGGGCCTGGTCCTGGGCGCTGCGTACGTGCCCTGCGCGGGCCCGGTCCTGGCGGCCGTTGCCGTCGCGGGAGCCACCGGGAGGATTGGCGCCGACACCGTCGCCCTGGCCGTGTCCTTCGCCGTCGGCACAGCGATCCCGCTGCTGGCCTTCGCCCTGGCCGGACGCGGTATCACGGAGAGGATTCAGGCCTTCCGCACCCGCCAGCGCGCCATCCGCGTCACCGCCGGCGTCGTCATGCTCGGGCTGGCCGTGGCCCTGGTCCTGGACGCCCCGGCCGCTCTCCAGCGCCGCCTGCCCGACTACACCGCCTCCCTTCAGGCCCGCACCGACGACCTTCTCCACGGTGACTCCTCTTCCGGCCCCTGCCGCCCCGGAGCCGCCACTCTCGGTGACTGCGGCCCCCTCCCTGCCATCGACGGCGCAGTGGCCTGGATCAACACGCCCGGCGACCAGCCCCTGACCCAGCAGAGCCGCGCAGGCAAGGTCACCCTGGTCGACTTCTTCGCCTACTCGTGCATCAACTGCCAGCGCTCGGTCCCCGGCATCGAGAAGCTCTACGAGACCTATGCGGCCTCCGGCCTGCAGGTGATCGGCGTCCACTCCCCGGAGTACGCCTTCGAGAAGGAAGTGGACAACGTACGTGGCGGCGTCAAGCACCTCGGCATCACCTACCCCGTGGCCGTCGACTCCAACCTGACCACCTGGACCAACTTCGACAACCATTACTGGCCCGCCCACTACCTGGCCGATGCCCAGGGCAACGTCCGCCAGACCCATGTCGGAGAAGGTGGGGAGGCGGCCACGGAGAAGCTCGTCCGCGAGCTGCTCATGCAGGCCAACCCGAAGGTGACCCTCCCCGCCCCCGTCTTCTCTGAGGCGAAGGACGACGCCGGCATGAACAGCCCCCGCACCCCCGAGACCTACCTGGGCTCGGACCGGGCCTCCGGCTTCGCCCAAGGAACCCTCCAGAAGGGACAGCACGCCTTCTCCTTCCCCTCCAGCCTCCAGGCCGACACCTTCGCCCTGGACGGCACGTGGACAGTGGAGCCGCAGTCCATCGCCCCGGTCGAGGGCAAGGGCCGCCTGCGCCTGTCCTACCGCGGCAAGCAGGTCAACCTTGTTGTCTCCGGCGAGGGGGACCTGACCTGGACGGTCAACGGGAAGACGCGCACCACCCACGTCTCCGGTGTTCCCAATGGCATGGAGCTGGTCCACACCGAGGAGGTGGGCTCGGGTGAGCTCGAGCTGGAGGCCTCGCCCGGGCTGCAGCTCTACTCCTTCACTTTCGGGTGA","VLPVILLSAGAQGARGDGGDDKGADGGFASRFHPYLVVTGLVVSFTVFTLLGSTVLSLLHLPQDLIRWVGIVMLALIGLGMMVPKVMEILERPFARFQRFGGSKNPSNGFLLGLVLGAAYVPCAGPVLAAVAVAGATGRIGADTVALAVSFAVGTAIPLLAFALAGRGITERIQAFRTRQRAIRVTAGVVMLGLAVALVLDAPAALQRRLPDYTASLQARTDDLLHGDSSSGPCRPGAATLGDCGPLPAIDGAVAWINTPGDQPLTQQSRAGKVTLVDFFAYSCINCQRSVPGIEKLYETYAASGLQVIGVHSPEYAFEKEVDNVRGGVKHLGITYPVAVDSNLTTWTNFDNHYWPAHYLADAQGNVRQTHVGEGGEAATEKLVRELLMQANPKVTLPAPVFSEAKDDAGMNSPRTPETYLGSDRASGFAQGTLQKGQHAFSFPSSLQADTFALDGTWTVEPQSIAPVEGKGRLRLSYRGKQVNLVVSGEGDLTWTVNGKTRTTHVSGVPNGMELVHTEEVGSGELELEASPGLQLYSFTFG$","Thiol-disulfide isomerase","Membrane, Cytoplasm, Extracellular","DipZ protein","hypothetical protein","Redoxin domain protein","","Missiakas D., Schwager F., Raina S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 1995. 14(14):3415-3424. PMID: 7628442Crooke H., Cole J. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Mol. Microbiol. 1995. 15(6):1139-1150. PMID: 7623667","","","

InterPro
IPR003834
Domain

Cytochrome c biogenesis protein, transmembrane region
PF02683	$\"[1-200]T$	DsbD

InterPro
IPR011594
Domain

Thioredoxin-like
PD003679	$\"[294-387]T$	Q6NKD1_CORDI_Q6NKD1;

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[259-381]T$	no description

InterPro
IPR013740
Domain

Redoxin
PF08534	$\"[240-388]T$	Redoxin

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide
tmhmm	$\"[35-55]?$ $\"[65-87]?$ $\"[108-130]?$ $\"[144-164]?$ $\"[185-205]?$	transmembrane_regions

","BeTs to 12 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones] Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB003834 (Cytochrome c biogenesis protein, transmembrane region) with a combined E-value of 9.7e-09. IPB003834D 108-149 IPB003834F 275-288","","","-48% similar to PDB:2B5X Solution Structure of a Thioredoxin-like Protein in the Reduced Form (E_value = 2.3E_13);-48% similar to PDB:2B5Y Solution Structure of a Thioredoxin-like Protein in the Oxidized Form (E_value = 2.3E_13);","Residues 1 to 200 (E_value = 2.6e-05) place ANA_1652 in the DsbD family which is described as Cytochrome C biogenesis protein transmembrane region.Residues 240 to 388 (E_value = 9.7e-10) place ANA_1652 in the Redoxin family which is described as Redoxin.Residues 241 to 370 (E_value = 3.6e-05) place ANA_1652 in the AhpC-TSA family which is described as AhpC/TSA family.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1654","1789374","1789487","114","7.43","0.40","4424","TTGGGGCACGTCATCTGGTTGTGGTCGATTGAGCTCGTGCGTCGGGACGTGCGCAACCGCATCACCCACCAGCCCGACCCGTGGGTTCCGCTCGACGCCGAACCGGCCCGCTGA","LGHVIWLWSIELVRRDVRNRITHQPDPWVPLDAEPAR$","Hypothetical protein","Cytoplasm, Extracellular","YagU","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1655","1789598","1790359","762","9.44","6.11","27618","ATGGTCACTCTCATCACCGGTGCGTCGTCGGGGATCGGCGAGGAGTTCGCCCGCCGCTACGCCGCCAAGAAGCATGACTTGGTGCTGGTGGCACGCCGGCAGGACAAGCTCGACGCCTTGGCCGAAGAGCTCCGAAAGGAGCACGGCGTGGAGGTCACCACCATCTCCCTGGACCTGTCCGAGCCGGACGCCGCCCAACGGCTGTGGAACGAGACCAACCGCAGAGGTCTGCACGTTGACGTCCTGGTCAACAACGCCGGCTTCGGCACTGGGAAGGACGTCGCCGACGACGCCCCCGAACGCCTGGAGCAGGAGGTGCGCCTCAACTGTCTTGCGGTGGTGGGCCTGACGGCCAGATACCTGCCGGCCATGCGCAAGCGCGGGAGCGGCACGATCATCAACATCTCTTCCGCCGCAGCCTTCCAGCCAATGCCCCACATGGCCGTCTACGGGGCCACCAAGGCCTTCGTGCTCTCCTTCACCGAGGCGCTCTGGCGAGAGACAAGGAGGGACGGCATCCGTGTCCTGGCCGTGTGCCCCGGCTCCACAGACACCCCGTTCTTCCAGGTCGCCGACGAGGGCACGGTCGTCGGCAGGCTCCGTTCCACGCGCCAGGTCCTCGATACGACGATGCGAGCCCTGAGAGGGAGCGGGCCCAGCGTTGTCGACGGGCTGGGGAACGCCGTCGTCGCACGATTCCTCACCCGTGTCCTTCCTCAGCGGGCGCTCCTGGCAGCAGTGGACCGGGTGTTCCGTCACTAG","MVTLITGASSGIGEEFARRYAAKKHDLVLVARRQDKLDALAEELRKEHGVEVTTISLDLSEPDAAQRLWNETNRRGLHVDVLVNNAGFGTGKDVADDAPERLEQEVRLNCLAVVGLTARYLPAMRKRGSGTIINISSAAAFQPMPHMAVYGATKAFVLSFTEALWRETRRDGIRVLAVCPGSTDTPFFQVADEGTVVGRLRSTRQVLDTTMRALRGSGPSVVDGLGNAVVARFLTRVLPQRALLAAVDRVFRH$","Short-chain dehydrogenase/reductase SDR","Cytoplasm","short-chain dehydrogenase Atu4220","short-chain dehydrogenase/reductase SDR","short-chain dehydrogenase/reductase SDR","","Jornvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 1995. 34(18):6003-6013. PMID: 7742302Villarroya A., Juan E., Egestad B., Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 1989. 180(1):191-197. PMID: 2707261Persson B., Krook M., Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 1991. 200(2):537-543. PMID: 1889416Neidle E., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 1992. 204(1):113-120. PMID: 1740120Benyajati C., Place A.R., Powers D.A., Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 1981. 78(5):2717-2721. PMID: 6789320","","","

InterPro
IPR002198
Family

Short-chain dehydrogenase/reductase SDR
PR00080	$\"[77-88]T$ $\"[130-138]T$ $\"[150-169]T$	SDRFAMILY
PTHR19410	$\"[1-217]T$	SHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106	$\"[1-169]T$	adh_short

InterPro
IPR002347
Family

Glucose/ribitol dehydrogenase
PR00081	$\"[2-19]T$ $\"[77-88]T$ $\"[124-140]T$ $\"[150-169]T$ $\"[171-188]T$	GDHRDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[2-237]T$	no description
PTHR19410:SF38	$\"[1-217]T$	17-BETA HYDROXYSTEROID DEHYDROGENASE

noIPR
unintegrated

unintegrated
tmhmm	$\"[45-65]?$ $\"[75-95]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-39% similar to PDB:2FUG Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1657","1792187","1791207","981","7.47","1.27","33214","GTGAGCGGCGAGAACGGCGAACACGCGCAGGACAGCGGCCCCCGCGCCACCAGCTGGGGGGAGGTGGTGCGACTGCGCACCCTGCCGGCCGCCGTCGCCCCCGTCATCCTGGGCGCCGGGGCAGCCGCCGCGATGGGGGAGCTCTCAGTGCTGCGGAGCCTGCTGGCCGCGGGCGTGGCCCTGGCGCTGCAGATCGGCTGCAACCTGGCCAATGACTACTCCGACGGCGTGCGCGGCACCGACGACGATCGCACCGGGCCGCCGCGCCTGACCGCCTCCGGGCAGGTCGCCCCCCGCACCGTCAAGCTCGCCGCCTTCGGCTGCTTCGGGATCGGAGCCCTCCTGGGCCTGGCACTCGTGGTCCTCAGCGGCCAGTGGTGGCTGCTCGCCGTCGGCGCCGCAGCGATCGCGGCCGCCTGGTTCTACACCGGAGGCTCCCACCCCTACGGCTACGCCGGCCTGGGGGAGGTCTTCGTCTTCGTCTTCTTCGGCCTGGTGGCCACGGTGGGCACCACCTACGTCCAGGCCGGCACGGTCCCGGGGTGGCTGTGGCCCTCGGCCTGCGGGATCGGACTGCTCGCCTGCTCCCTGCTCATGGTCAACAACCTGCGCGACATCGATACCGATCCCGCCCACGGCAAGATGACCCTGGCAGTTCGCCTGGGGGAGGGGGGAGCCCGGCACGCCTTCTCCCTCATGCTTCACGTGCCTCTGCTGCTGGGGGCCGTCGCCCTGGTGTGGGCGCGCGAGACCGGTTCGGCCAGCCCCGTCGACGGCGGCGGGCACATCAGCCCGCTGCTGACCCTGGTCATCGCGCTGGCGGCGCCGCTCCTGCTCCTGCCGCTGGTGCGGCGGGCCACCGCGCCGGTGCGCTCCGGCGCCCGGGGGCGCGATCTCATCGCCTCCCTGCGTGACGCCGGCCTGCTGGAGCTGGCCTACGGCGTCGTCTTCGCCGCCGCCACCGTCATCATCACTCTGTGA","VSGENGEHAQDSGPRATSWGEVVRLRTLPAAVAPVILGAGAAAAMGELSVLRSLLAAGVALALQIGCNLANDYSDGVRGTDDDRTGPPRLTASGQVAPRTVKLAAFGCFGIGALLGLALVVLSGQWWLLAVGAAAIAAAWFYTGGSHPYGYAGLGEVFVFVFFGLVATVGTTYVQAGTVPGWLWPSACGIGLLACSLLMVNNLRDIDTDPAHGKMTLAVRLGEGGARHAFSLMLHVPLLLGAVALVWARETGSASPVDGGGHISPLLTLVIALAAPLLLLPLVRRATAPVRSGARGRDLIASLRDAGLLELAYGVVFAAATVIITL$","1,4-dihydroxy-2-naphthoate octaprenyltransferase","Membrane, Cytoplasm","1,4-dihydroxy-2-naphthoateoctaprenyltransferase","1;4-dihydroxy-2-naphthoate octaprenyltransferase ","1,4-dihydroxy-2-naphthoate octaprenyltransferase","","Suvarna K., Stevenson D., Meganathan R., Hudspeth M.E. Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli. J. Bacteriol. 1998. 180(10):2782-2787. PMID: 9573170","","","

InterPro
IPR000537
Family

UbiA prenyltransferase
PF01040	$\"[28-321]T$	UbiA

InterPro
IPR004657
Family

1,4-dihydroxy-2-naphthoate octaprenyltransferase
TIGR00751	$\"[24-320]T$	menA: 1,4-dihydroxy-2-naphthoate octaprenyl

noIPR
unintegrated

unintegrated
PTHR13929	$\"[15-326]T$	1,4-DIHYDROXY-2-NAPHTHOATE OCTAPRENYLTRANSFERASE
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[25-43]?$ $\"[49-69]?$ $\"[100-118]?$ $\"[124-142]?$ $\"[157-177]?$ $\"[183-203]?$ $\"[229-249]?$ $\"[263-283]?$	transmembrane_regions

","BeTs to 6 clades of COG1575COG name: 1,4-dihydroxy-2-naphthoate octaprenyltransferaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1575 is -o------v-rlbce-gh--------Number of proteins in this genome belonging to this COG is 1","***** IPB000537 (UbiA prenyltransferase) with a combined E-value of 3.5e-12. IPB000537A 59-99 IPB000537B 149-196 IPB000537B 117-164","","","No significant hits to the PDB database (E-value < E-10).","Residues 28 to 321 (E_value = 3.2e-15) place ANA_1657 in the UbiA family which is described as UbiA prenyltransferase family.","","octaprenyltransferase (menA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1658","1792367","1792254","114","8.66","2.10","3831","ATGGGTGAAGGAGTGCGAGGGCGGGGATCGGGCTGTCTCACGGAGGTCCTTCTGGCGATCGCGGTGCCGGTTGCCTCACCGGCCGAGGTGTGTCTCAGGCGCTCGCACCGGTGA","MGEGVRGRGSGCLTEVLLAIAVPVASPAEVCLRRSHR$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide

InterPro
IPR005502
Family

ADP-ribosylation/Crystallin J1
PF03747	$\"[11-328]T$	ADP_ribosyl_GH

InterPro
IPR012242
Family

ADP-ribosylglycohydrolase
PIRSF006017	$\"[8-336]T$	ADP-ribosylglycohydrolase

noIPR
unintegrated

unintegrated
PTHR16222	$\"[1-347]T$	ADP-RIBOSYLGLYCOHYDROLASE

","BeTs to 3 clades of COG1397COG name: ADP-ribosylglycohydrolaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1397 is a-m----q-d----e------j----Number of proteins in this genome belonging to this COG is 1","***** IPB005502 (ADP-ribosylglycohydrolase) with a combined E-value of 1.2e-24. IPB005502A 9-24 IPB005502B 137-150 IPB005502C 284-303","","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 328 (E_value = 1.1e-51) place ANA_1659 in the ADP_ribosyl_GH family which is described as ADP-ribosylglycohydrolase.","","superfamily ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1660","1795701","1794337","1365","6.56","-2.14","46809","GTGCCCGCCCCGCCCGCCCTCCGCCTCCTGACCGGCGGAACTGCCCCCGACGACGTCGCCGTCCTGCGCGCAGCCCTCGCCGAGCGCCTGGCCCTGCGCGGCCTGCTCACCACCCGCGATGGACTCCCGGCCCCCGCCGCCGAGGACGGGGAGGACCGGGCGGTCTCGCTGCTGCCACTGCTCGTCCCCATTGCCCCCGGGGAGGACGAGGAGCAGGTCCGGTCCGACCTGGCCCGCCGTATCACCCGCGTCCCGGCACGCACAGACCTCATCCTGCGCACGTCGGGCTCCACCACCGGTACCGGCCGACTCATCGCCATGAGCGCCGCCGCCCTCGTGGCCTCCGCCCGCGCCACCCACGCGCGCCTTGGTGGCCCGGGAACCTGGCTCCTGCCCCTGCCGGCCCACCACGTCGCCGGCCTGCAGATCCTCATCCGTTCCCTGGAGGCCGGAACCGAGCCCGTCGTGGTCGACACGAGCTCAGGATTCAGCCCGGCGGCGCTCGCGGAGGCCCTGAGGTCGGCGCGCCGGTCCACCGGGGCGACCGCCTCCCGGCTCTACGTCTCCCTGGTCCCCACCCAACTGGTGCGCGTCCTGCAGGACCCGCAGGCCCGCCGGGCCCTGGCAGGAGCCGACGCCGTCCTCCTGGGCGGCGCCGCCGCCGACCCCGCGCTCCTGGACCGGGCCCGCGGGGCGGGCGTCACCGTGGTCACCACCTACGGCATGAGCGAGACCGGCGGGGGCTGCGTCTACAACGGCCGCCTCCTGGAGGGGGTCGAGATCACCATCCAGGCCCCCGACGCCGCCGGCGCCGGCCGCATCCTCATCTCCGGTCCCGTCCTGGCCGAGGACTACCTCGACACCCCCGGCCACAGCCCCGCAGGCAGTCCCAACGCCGGCGAGGGCTTCCACCGCAGCGGCAGCACGCGCGTCCTGGCCACCTCCGACCGCGGCCGGCTGCACCCCGACGGGCGCCTGGAGGTCCTGGGCCGCCTGGACGACGTCATTATCACCGGGGGCGTCAAGGTCGAGCCCCGCCACGTGGAGGAGGCCCTCACCTGTATCGACGGCGTGGCCGAGGCCTGCGTCGTCGGCCTGCCCGACGAGCAGTGGGGAAGCACCGTCGTTGCCGCTGTCGTGCTTGAGACGGGGAGGGAGCCGGGCAGCCCGAAGCGGCGGGACGGCGCCGCCCTGCGCGAGGCGGCCCGCGCCCGGCTGGACGGCGCCCACGCCCCCAAACGGGTCGTCGTCCTGGAGGCCCTGCCGTTGCGCCCCAGCGGGAAGGTCGATCGGCGTGAGGTCGCCCGGCTCCTCGCTGCGACCACGACAGATGTGACCCCGGAGCCTTCTACACCAGAGCCCTGA","VPAPPALRLLTGGTAPDDVAVLRAALAERLALRGLLTTRDGLPAPAAEDGEDRAVSLLPLLVPIAPGEDEEQVRSDLARRITRVPARTDLILRTSGSTTGTGRLIAMSAAALVASARATHARLGGPGTWLLPLPAHHVAGLQILIRSLEAGTEPVVVDTSSGFSPAALAEALRSARRSTGATASRLYVSLVPTQLVRVLQDPQARRALAGADAVLLGGAAADPALLDRARGAGVTVVTTYGMSETGGGCVYNGRLLEGVEITIQAPDAAGAGRILISGPVLAEDYLDTPGHSPAGSPNAGEGFHRSGSTRVLATSDRGRLHPDGRLEVLGRLDDVIITGGVKVEPRHVEEALTCIDGVAEACVVGLPDEQWGSTVVAAVVLETGREPGSPKRRDGAALREAARARLDGAHAPKRVVVLEALPLRPSGKVDRREVARLLAATTTDVTPEPSTPEP$","AMP-dependent synthetase and ligase","Cytoplasm, Membrane","o-succinylbenzoic acid-CoA ligase","AMP-dependent synthetase and ligase","AMP-dependent synthetase and ligase","","Smith D.J., Earl A.J., Turner G. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 1990. 9(9):2743-2750. PMID: 2118102Schroder J. Protein sequence homology between plant 4-coumarate:CoA ligase and firefly luciferase. Nucleic Acids Res. 1989. 17(1):460-460. PMID: 2911486Mallonee D.H., White W.B., Hylemon P.B. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 1990. 172(12):7011-7019. PMID: 2254270","","","

InterPro
IPR000873
Domain

AMP-dependent synthetase and ligase
PF00501	$\"[105-363]T$	AMP-binding

noIPR
unintegrated

unintegrated
G3DSA:3.30.300.30	$\"[333-448]T$	no description
G3DSA:3.40.50.980	$\"[85-245]T$	no description
PTHR11968	$\"[85-440]T$	ATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF14	$\"[85-440]T$	O-SUCCINYLBENZOIC ACID--COA LIGASE

","BeTs to 13 clades of COG0318COG name: Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases IIFunctional Class: I [Metabolism--Lipid metabolism] Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0318 is aomp-zy--drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-45% similar to PDB:1T5D 4-Chlorobenzoyl-CoA Ligase/Synthetase bound to 4-chlorobenzoate (E_value = 1.9E_13);-45% similar to PDB:1T5H 4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine (E_value = 1.9E_13);","Residues 6 to 363 (E_value = 1.7e-08) place ANA_1660 in the AMP-binding family which is described as AMP-binding enzyme.","","acid-CoA ligase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1661","1793424","1794353","930","4.92","-15.99","31907","ATGGGACGGGTCATTCACACCGGTCAGGTCGTCATTGACCTGACCTTGCGCATCGAGGCGATTCCCGAGCCCGGCGGTGACGTGTTCGCCGACGAGTCCTCCATGGCGGTCGGTGGTGGCTTCAACGTGCTGGCCGCCGCCCGCCGGATGGGGGTCGAGACCCTGTACGCGGGGCCGCTGGGCGAGGGACCCTTCGCCGAGGCGGCCCGGCGGGCCCTGGAGGAGATCGGGGTGGATCATGTCGGCCCGGTTACAGCCGGCGACCAGGGCTACTGCGTGGCCATGACCGATGCGAGGGCCGAGCGCACCTTCATCTCCACCTGCGGGGCCGAGACTCGTGGCCCGGTGGATGCCTTCGACCATCTGGAGGTGAGTGGCGACGACGTCGTCTACCTCTCCGGCTACTCCCTGGCCGATGAGGCCTCCAGGGTGGCGCTGGAGCGGTTGGCCAGGAGACTGACCGAGGCCCGGACGGGGTGCACGGCGCTGTTCGACGTCTCCCCCATGGTTGGTTCGGTCCCCATGAGCTCGCTGGAGCACCTCGGTGCGCTGGGGCCCGTCTGGTCTCTCAATGAGCGTGAGGCCGGGCTGCTCGCCGACCGCCTGGGGCTGCGGGTGGAGGCCGGTGACCACGCCGGCGTCTGCGAGGCGCTATCGGGTCGGCTCGGCACGGTGCTGGTGCGGGTTGGGGAGCAGGGCTCCTGGTTCTCCGACGGCGGCGCGGCGCACCATACCCCAAGTATCCCGGTGACGCCGGTGGACACCAACGGAGCCGGTGACGCGCACTCCGGTGTCCTGGCCGCGGCCCTGGCCCGGGGCATCGACCTGACGACGGCGCTGCGCTGGGCGAATGTGGCCGGAGCCTTGACCGTGACGCACTTCGGCCCGGCCACCTGCCCGAGTGAGGCAGAGATCAGGGCTCTGGTGTAG","MGRVIHTGQVVIDLTLRIEAIPEPGGDVFADESSMAVGGGFNVLAAARRMGVETLYAGPLGEGPFAEAARRALEEIGVDHVGPVTAGDQGYCVAMTDARAERTFISTCGAETRGPVDAFDHLEVSGDDVVYLSGYSLADEASRVALERLARRLTEARTGCTALFDVSPMVGSVPMSSLEHLGALGPVWSLNEREAGLLADRLGLRVEAGDHAGVCEALSGRLGTVLVRVGEQGSWFSDGGAAHHTPSIPVTPVDTNGAGDAHSGVLAAALARGIDLTTALRWANVAGALTVTHFGPATCPSEAEIRALV$","Ribokinase","Cytoplasm","ribokinase","putative sugar kinase","PfkB domain protein","","Sigrell J.A., Cameron A.D., Jones T.A., Mowbray S.L. Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures. Structure 1998. 6(2):183-193. PMID: 9519409","","","

InterPro
IPR011611
Domain

PfkB
PF00294	$\"[1-303]T$	PfkB

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[3-309]T$	no description
PTHR10584	$\"[7-309]T$	SUGAR KINASE RELATED

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[35-55]?$	transmembrane_regions

InterPro
IPR013078
Domain

Phosphoglycerate mutase
PF00300	$\"[5-159]T$	PGAM

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1240	$\"[3-193]T$	no description
PIRSF001490	$\"[4-215]T$	Cofactor-dependent phosphoglycerate mutase
PTHR23029	$\"[4-173]T$	PHOSPHOGLYCERATE MUTASE

","BeTs to 6 clades of COG0406COG name: Fructose-2,6-bisphosphataseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0406 is ---p--yqvdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 3","***** IPB001345 (Phosphoglycerate/bisphosphoglycerate mutase) with a combined E-value of 1.8e-14. IPB001345A 6-34 IPB001345B 52-64 IPB001345D 119-137 IPB001345E 144-187","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 159 (E_value = 2.7e-31) place ANA_1664 in the PGAM family which is described as Phosphoglycerate mutase family.","","mutase family protein (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1665","1797876","1798859","984","8.64","4.80","34418","ATGACGACTCGCAGCGCATGGGGTCTCGGCCTGGCGACCGTGACCGACGACGGCAACACCCTCGACGTGTGGTACCCCCGACCGGTTCTCGGCGACGAGCCCGAGAACGGGCACGCCGACCTCCTGGCCTCCCTGAGCGCCATGGAGCGCCGCGATGAGGCTCGCGGCGTCCACACCACCGTGGTGCGCACCTGGGCCGACCTCGACGACGCCCCCCAGACCGTGGCCGGCGCTTACCTGCGCCTGCACACACTGTCCCACCGCCTGGTCAAGCCCAACACCGTCAATCTGGACGGGATCTTCTCCCGCCTGCCCAACGTGGTGTGGACCTCCGCCGGCCCCTGCCGTGCCGAGGACTTCGAGAACACCCGCATGCGCCTGCGCGCCGCCGTAGGGCGCCCCGTCCAGGTGCACTCGGTGGACAAGTTCCCCCGCATGACCGACTACGTGCTGCCCTCGGGGGTGCGCATCGGCAACGGCGCGAACGTGCGCCTGGGCGCCTACCTGTCAGAGGGCACCACGGTCATGCACTCCGGCTTCGTCAACTACAACGCCGGGACGCTGGGGCGCTCCATGGTCGAGGGCCGCATCTCCCAGGGGGTCGTCATCGGCGACGGCTCCGACATCGGCGGCGGCGCCTCCACGATGGGCATGCTCTCGGGCGGTGGGCGCCAGCGCGTGGCCCTGGGCAAGCGCTGCCTGCTGGGGGCGAACTCGGGGCTCGGGATCCCGCTGGGTGACGACTGCGTCGTCGAGGCAGGCCTGTACCTGACGGCCGGCACGAAGGTCTCCCTCATGCCGCAGGGCGGCGTGGTGCCCGGCAACCACGGCCTGTTCAAAGAGCCGCGCGTGGTCCCGGCCCGCGAGCTGGCCGGCGCCTCCAACGTCCTGTTCCGCCGCAACTCCCAGTCCGGCGCCGTCGAGGCCCTGGCCCGCGGCGGCAAGAGCATCGAGCTGGGCTCGCCCCAGCACGCCGGCCAGTAG","MTTRSAWGLGLATVTDDGNTLDVWYPRPVLGDEPENGHADLLASLSAMERRDEARGVHTTVVRTWADLDDAPQTVAGAYLRLHTLSHRLVKPNTVNLDGIFSRLPNVVWTSAGPCRAEDFENTRMRLRAAVGRPVQVHSVDKFPRMTDYVLPSGVRIGNGANVRLGAYLSEGTTVMHSGFVNYNAGTLGRSMVEGRISQGVVIGDGSDIGGGASTMGMLSGGGRQRVALGKRCLLGANSGLGIPLGDDCVVEAGLYLTAGTKVSLMPQGGVVPGNHGLFKEPRVVPARELAGASNVLFRRNSQSGAVEALARGGKSIELGSPQHAGQ$","Tetrahydrodipicolinate N-succinyltransferase","Cytoplasm, Extracellular","tetrahydropicolinate succinylase","2;3;4;5-tetrahydropyridine-2-carboxylate N-succinyltransferase ","Tetrahydrodipicolinate N-succinyltransferase-like","","","","","

noIPR
unintegrated

unintegrated
G3DSA:2.160.10.10	$\"[139-301]T$	no description

","BeTs to 9 clades of COG2171COG name: Tetrahydrodipicolinate N-succinyltransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2171 is --------v-rlb-efghsnujx---Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","succinylase (dapD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1666","1799038","1799817","780","11.79","21.51","27491","ATGGCTGCGATATCCACGGCCGCCCGTGTCCCCGAGTCTGCTCAGCCTGTTGGCGACGCGCTTCCTCCCCGGCGCAGGCGCCGCACCCCCGTGTGGGCCTCACAGCGCGTCCTCAAGGCGACGATGGCGATCACCGGCACGATCATGGCCCTGTTCGTCGTGGTCCACATGGTCGGCAACCTCAAGGTTCTCGCGGGCCCGCACGCCTTCAACGGCTACGCCGCCTGGCTGCGGCAGGTCGCCTACCCGCTCCTGCCGCACGAGGGGCTCCTGTGGGCGATGCGCTTGGCCCTGGGGGCCTGCGTCGTGGCGCACATGGCTGCGGGAATCGCGCTGTGGCGCCGGGCGAGGAGCGCTCGCGGGGCCTTCCGGCGCCGGGCCCTGCCCGCCCGCACCATTGGCGCCCGTTCCATGCTGGCGACCGGCGTCCTCATCGGGGTCTTCGTCCTCATCCACGTCCTCGACCTGACCATCGGCCGCCTCATCGCCCCTGAGAGCTTTCAGGCGCCGACGACGTCGAACGGCGAGCTGCGGGTCAGCGCCTACCACAACCTCGTGGCGAGCCTGTCGCGCCCCGGCATGGCGCTCTTCTACAGCCTGGTCATGCTGGCACTCTCCCTCCATCTGGCGCAGGGCCTGTGGAACGTGGTCATCGATCTGGGCGGCACCGGCCCCAGGCTGCGCAAGGCCTGCCGCGCCCTCGCCCTGGGCGTGGCCCTGGCCGTCGCCGTCGTCAACGGCCTGCTGCCCGTCCTCATCTGCACGGGGGTGATCGGATGA","MAAISTAARVPESAQPVGDALPPRRRRRTPVWASQRVLKATMAITGTIMALFVVVHMVGNLKVLAGPHAFNGYAAWLRQVAYPLLPHEGLLWAMRLALGACVVAHMAAGIALWRRARSARGAFRRRALPARTIGARSMLATGVLIGVFVLIHVLDLTIGRLIAPESFQAPTTSNGELRVSAYHNLVASLSRPGMALFYSLVMLALSLHLAQGLWNVVIDLGGTGPRLRKACRALALGVALAVAVVNGLLPVLICTGVIG$","Succinate dehydrogenase subunit C","Membrane, Cytoplasm","putative succinate dehydrogenase subunit C","putative succinate dehydrogenase subunit C ","succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family","","Magnusson K., Philips M.K., Guest J.R., Rutberg L. Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex. J. Bacteriol. 1986. 166(3):1067-1071. PMID: 3086287","","","

InterPro
IPR011138
Family

Succinate dehydrogenase, cytochrome b558 subunit
TIGR02046	$\"[34-258]T$	sdhC_b558_fam: succinate dehydrogenase (or

noIPR
unintegrated

unintegrated
tmhmm	$\"[37-57]?$ $\"[91-113]?$ $\"[134-154]?$ $\"[196-218]?$ $\"[233-253]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB011997 (Succinate dehydrogenase/Fumarate reductase respiratory complex) with a combined E-value of 1.2e-12. IPB011997A 42-78 IPB011997B 138-154 IPB011997C 197-221 IPB011997B 42-58","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","succinate dehydrogenase subunit C","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1667","1799814","1801775","1962","6.38","-6.78","71330","ATGAGTGCGAGTGTGCCGGGTGCCGTCGGTGGCCTGTACGACGTCGGCGAGGACCTGGATGCGCACCTGCCGGACTGTCCGCCTGAGCAGGCCTGGGCGCGCCGGCGCGACGAGTACCGCCTGGTCAATCCTGCCAACCGCCGCAAGCTGACCGTCATCGTGGTGGGTGCCGGACTGGCCGGTGCCGGGGCGGCCGCGACCCTAGGGCGCCTGGGCTACCGGGTGGAGTGCTTCAGCCTGCACGACGCCCCGCGGCGCGCCCACTCGGTGGCCGCACAGGGCGGGATCAACGCCGCCCGGGCCCGCAAGGTCGACGGCGACTCCCTGACGCGCTTCGTCAAGGACACCGTCAAGGGCGGGGACTATCGGGGGCGGGAGGCCGACGTCGTGCGCCTGGGGCTGGAGTCCGGCCGGGTCATCGACCACATGGAGGCGATCGGGGCGCCCTTCGCCCGCGAGTACGGCGGCCAGCTCGCCACCCGCTCCTTCGGCGGGGTGCAGGTCTCGCGCACCTACTACACGCGCGGGCAGACCGGTCAGCAGTTGGAGATCGCCTGCGCCCAGGCCCTCCAGGAGCAGGTCGCCGCCGGGAGCGTCCGCATGCACACCCGCACCGAGATGCTCGACCTCATCGTGGCCGACTCCCGCGCGCAGGGCATCGTCACCCGGGACCTGCTCTCCGGCGAGGTACAGGCCCACACCGCGCACGCCGTCGTGCTGGCCACCGGCGGCTACGGCAGCGTCTACCACTACTCGACCCTGGCCATGGCCTCCAATGCCACCGCCACCTGGCGCGCCCACCGGCGTGGGGCGGCCTTCGCCTCGGCCTGCATGGTGCAGTTCCACCCCACGGCGCTGCCGGTGAGCTCCCACTGGCAGTCCAAGACGACGCTCATGAGCGAGTCGCTGCGCAACGATGGGCGCATCTGGGTGCCCGTGCGCCCCGGGGATGAGCGGACCCCGAACGAGATCCCCGAGGACGAGCGCGACTACTACCTGGAGCGCAAGTACCCGGCCTTCGGCAACCTCACCCCGCGCGACGTGGCCTCGCGCAACGCCCGCGAGCAGATCGAGTCCGGCCGCGGCGTCGGGCCGCTGCGCAACTCGGTCTACCTCGACTTCCGCGACGCGCTGGAGCGGCTGGGCAAGGAGACCATCGCCTCGCGCTACGGCAACCTGTTCGAGATGTACCTCGACGCCACCGGGGAGGACCCCTACGAGGTGCCCATGCGCATCGCCCCGGGAGCCCACTTCACGATGGGAGGGCTGTGGGTGGACTTCGACCAGATGTCCACCATCCCGGGACTGTTCGTGGGCGGGGAGGCATCGAACAACTACCACGGCGCCAACCGTCTGGGGGCGAACTCGCTGCTGAGCGCCAGCGTGGACGGCTGGTTCGTGCTTCCGCTGGCCGTGCCGAACTACCTGGCCGGGCTGGTGGGCAGTAGGCTCCTGAGCCCCGACGCGCCGGAGGCGCTTCAGGCCGTGGCGGATACCCGCGAGCGCATTGAGGCGCTCATGGCGGTGGGCGGGACCCACCGTCCGGTGTGGTTCCATCGCCGGCTAGGTGAGATCCTCTACGCCGGCTGCGGGGTCAGCCGCTCCGAGGCGGGGCTGCTGCATGCCCTGGAGGAGGTGCGCGCCCTGCGCGAGGAGTTCTGGGCCGATGTCACCGTGGTCGGTGGTCAGGCGCGGCTCAACCAGGAGCTGGAGAAGGCGCTGAGGGTCGCCGACTTCCTGGAGCTGGCCGAGGTCATGATCCTTGACGCCCTGGACCGGCGCGAGTCCGCAGGCGCCCACTTCCGCGAGGAGTACGCGACCCAGGGCGGCGAGGCCCAGCGCAATGACGAGACCTGGTGCTCGGTATCGGCCTGGCAGACCGGGGACGACGGCGGGCACACGCGCCGCACGGAGCCGCTGAGCTTCTCGCTGGTGCCCATGCAGGTGAGGGACTACCGATGA","MSASVPGAVGGLYDVGEDLDAHLPDCPPEQAWARRRDEYRLVNPANRRKLTVIVVGAGLAGAGAAATLGRLGYRVECFSLHDAPRRAHSVAAQGGINAARARKVDGDSLTRFVKDTVKGGDYRGREADVVRLGLESGRVIDHMEAIGAPFAREYGGQLATRSFGGVQVSRTYYTRGQTGQQLEIACAQALQEQVAAGSVRMHTRTEMLDLIVADSRAQGIVTRDLLSGEVQAHTAHAVVLATGGYGSVYHYSTLAMASNATATWRAHRRGAAFASACMVQFHPTALPVSSHWQSKTTLMSESLRNDGRIWVPVRPGDERTPNEIPEDERDYYLERKYPAFGNLTPRDVASRNAREQIESGRGVGPLRNSVYLDFRDALERLGKETIASRYGNLFEMYLDATGEDPYEVPMRIAPGAHFTMGGLWVDFDQMSTIPGLFVGGEASNNYHGANRLGANSLLSASVDGWFVLPLAVPNYLAGLVGSRLLSPDAPEALQAVADTRERIEALMAVGGTHRPVWFHRRLGEILYAGCGVSRSEAGLLHALEEVRALREEFWADVTVVGGQARLNQELEKALRVADFLELAEVMILDALDRRESAGAHFREEYATQGGEAQRNDETWCSVSAWQTGDDGGHTRRTEPLSFSLVPMQVRDYR$","Succinate dehydrogenase/fumarate reductase, flavoprotein subunit","Cytoplasm","Succinate dehydrogenase/fumarate reductase,flavoprotein subunits","succinate dehydrogenase ","succinate dehydrogenase or fumarate reductase, flavoprotein subunit","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Kunert K.J., Cresswell C.F., Schmidt A., Mullineaux P.M., Foyer C.H. Variations in the activity of glutathione reductase and the cellular glutathione content in relation to sensitivity to methylviologen in Escherichia coli. Arch. Biochem. Biophys. 1990. 282(2):233-238. PMID: 2241146Shames S.L., Fairlamb A.H., Cerami A., Walsh C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 1986. 25(12):3519-3526. PMID: 3718941Carothers D.J., Pons G., Patel M.S. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 1989. 268(2):409-425. PMID: 2643922Misra T.K. Bacterial resistances to inorganic mercury salts and organomercurials. Plasmid 1992. 27(1):4-16. PMID: 1311113","","","

InterPro
IPR001100
Family

Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411	$\"[51-73]T$ $\"[479-494]T$	PNDRDTASEI

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[414-423]?$	AA_TRNA_LIGASE_I

InterPro
IPR003953
Domain

Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00890	$\"[51-457]T$	FAD_binding_2

InterPro
IPR004112
Domain

Fumarate reductase/succinate dehydrogenase flavoprotein, C-terminal
PF02910	$\"[519-652]T$	Succ_DH_flav_C

InterPro
IPR011280
Family

Succinate dehydrogenase or fumarate reductase, flavoprotein subunit, low-GC Gram-positive bacteria
PTHR11632:SF4	$\"[32-652]T$	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
TIGR01811	$\"[52-652]T$	sdhA_Bsu: succinate dehydrogenase or fumara

noIPR
unintegrated

unintegrated
G3DSA:1.20.58.100	$\"[489-609]T$	no description
G3DSA:3.50.50.60	$\"[45-471]T$	no description
PTHR11632	$\"[32-652]T$	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT

InterPro
IPR001450
Domain

4Fe-4S ferredoxin, iron-sulfur binding
PR00353	$\"[152-163]T$ $\"[164-175]T$	4FE4SFRDOXIN
PF00037	$\"[152-175]T$	Fer4
PS00198	$\"[159-170]T$	4FE4S_FERREDOXIN

InterPro
IPR004489
Family

Succinate dehydrogenase/fumarate reductase iron-sulfur protein
PIRSF000176	$\"[3-247]T$	Fumarate reductase/succinate dehydrogenase (ubiquinone), iron-sulphur protein
TIGR00384	$\"[5-236]T$	dhsB: succinate dehydrogenase and fumarate

InterPro
IPR006058
Binding_site

2Fe-2S ferredoxin, iron-sulfur binding site
PS00197	$\"[58-66]T$	2FE2S_FER_1

InterPro
IPR012285
Domain

Fumarate reductase, C-terminal
G3DSA:1.10.1060.10	$\"[126-243]T$	no description

InterPro
IPR012675
Domain

Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30	$\"[1-116]T$	no description

noIPR
unintegrated

unintegrated
PTHR11921	$\"[15-245]T$	SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN

InterPro
IPR013216
Domain

Methyltransferase type 11
PF08241	$\"[63-158]T$	Methyltransf_11

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[59-207]T$	no description
PTHR10108	$\"[61-228]T$	METHYLTRANSFERASE
PTHR10108:SF36	$\"[61-228]T$	MCCD PROTEIN

","BeTs to 7 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 63 to 158 (E_value = 1.1e-12) place ANA_1669 in the Methyltransf_11 family which is described as Methyltransferase domain.Residues 63 to 156 (E_value = 0.0004) place ANA_1669 in the Methyltransf_12 family which is described as Methyltransferase domain.","","methyltransferases ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1670","1803556","1804122","567","6.04","-3.60","20770","ATGCTCGTGGGTGCTGCCAACCCCACCATCGATGGCGGGCTCGTTATCGCAGTAGAGCATGAGTGGACGTACGGACCGAGTTGGGCGCCACCCTACGAGACCAGAGGGCTGAAAGCGCTCCGAGACGACCCAATGGGGGCGGAGACCATTCTCGAAATCTCCGCCGTCTTCACCGATTCATGGGAGCTGCCCACGTGGTTTCAGTGGAAGTACGGGGACGTCTCGCTACGTCGGCGGCTCTATGACGCAAGGAGGACTCCCGCGGAGCTCACGAGCCTCTTCGCCGACTACGCCAAGAGCCACGACTGGACGAAGAATCCCAGACCGTCCACACCCGAGTCATGGATCGGCCACCACGGCGGGACGGAGCCGACTGACGGCATGCCCCTCACTGTCGCCCCAATATCGGGCAGCGCGAGACTGACCCGCTCAACGGCTCGATTGTTGTCGGACTTGGATACGCCTGAGACAACGCCATCCCCTCCCCGTCAAGCGAGAGCCTCTCATCGTAGCGGCACACATGGCGACGAACCTCCACGGCAAAACCCCCTCAGTAACACTGACTAA","MLVGAANPTIDGGLVIAVEHEWTYGPSWAPPYETRGLKALRDDPMGAETILEISAVFTDSWELPTWFQWKYGDVSLRRRLYDARRTPAELTSLFADYAKSHDWTKNPRPSTPESWIGHHGGTEPTDGMPLTVAPISGSARLTRSTARLLSDLDTPETTPSPPRQARASHRSGTHGDEPPRQNPLSNTD$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1671","1805745","1808009","2265","5.11","-28.54","80915","GTGAATCGCCCTTCACAACATGACAAGCCAAACGTTGCACACTACATGAAACAGTTAACTTTCATCATTCTAGTCACATTACTACTATTCAACCAGGAACTTCCCTTACCTACCACTCTTCCAACCGCCTCTGCCGCGATCACAACCAACGTTCCCCTCAGAGTAGCCCTACTCGGAGACTCTTATTCTGCCGGGAATGGCGCAGGACACTACTACGGCGATGACAAGACAGCCTACAGAAGTTCTCGCAATTGGGCGCACAACTACGTGAACTGGCTTAACGATCAGGGAGCTCACGCAATATTAAATAATATTGCACATAGCGGCAACGTTTCGGACGACGTCCTAGGTGCCCAAATGAAAAAATTGGACTCTAACACAAATTTAGTGATGTTCACTATCGGTGGCAACGATGTCAATTTTTCCGATATTGTTTCGCAGTGTTTCATGATTGGAATGAGAGACCCTGCCACTTGCCGTCAGAAAATCGATGGCGCTAACTCTAAGCTACCACGGGTGAAGAAGCAAACTCTTGACATTCTTCAGGCAATTGATGATCGCTTAGACGACAACGCCCAGGTGGTCATCGTAGGCTACCCTCGACTATCATCCAAGGATAATTTTACCCTCAGGGACAGCCACGCATTATGGACAGATTCATACAATGCCGGCGCGGCAGTCAGAAAACTCGGTGACGACGCAAAGGTCATTCAATCAGACCTTGTTTCTGAATGGAATAGCTCACACCCAAGCCTGAAGGTAACCTACGTAGATGGCGTCATCAACTCATTCAATGGACATGAACCAGACCCATCATTCCCTGTCGTCAATCATCACCGCTGGATTAATGAGTTCTTTGAGACAGAGGGGCAGGAAGACCAAAATGGAAACACGCACGCCAAGACAAGCGGGGACCCGAATGAATTCTACCACCCCAATCTCATCGGACACGAAGAGATAGCAAAACTCATAGAGACCAAAATCGGGGTCCCATCCATCAAGAGCCCCAAAAGCAATGGAGAGGATATCGATATCGCGTTCGTTGTAGACTCTACGGGCTCGATGGACAGTAATGTCGAGGCAGTTCGATCGAAGATTCATTCGATAGCGGAAGAAACAAGCAAGAAGGCGCTGTCTTATCGATTCGCACTCGTAGACTACAAAGACCACCCTCAGTACAACCCAAAGAACTACCTAGCCCGGACCGACGTCGATTTCACGTCCGACATACCTACATTGGATGCAGGGCTGAGTTCTCTAACCTACGAGGGAGGGAATCTCGGCAATACTAACGCCAGCGTTTACAGCGGCGTCATGCAGGCCGTCAACATGAAGTGGCGCAATGGGGTCAAGAAGATCGTCGTTGTCATCGGTGACGCGCCTCCACGCGACCCCGAGCCGGGCACTGGTTACACCGCCGCCTCCGTCGCCAAGGCCGCCTACGAAGTAGACCCGGTCAGTGTCTACGGTATTGATACCGGAGACCTCAACTCCACCAGCTTCCAGACGCTGGTCACCTCCAGCACGGGCACGACCGCCAACGCCTCCTCGCCCGATCAGGTCAGCGACCTCGTCAACAAGGCCATCAGCAGCGAGCTCAACAAGCCCTTCGCCTGGATCCAGGGCCCCTATGTCGCCAAGGTCGGAGATCCTGTCGACATCGATGCCGCAGCCTCCCACGCAGTCTCTGGCTCCCTGACCTCCTATGAGTGGGACTTCAACGGTGACGGCGTCTACGACGAGACCGGAACCTCCCCGCGCATCACCCATACCTTCAGCCAGGAGTTCAGCGGCGTCATCGGCCTACGCGTCACTCAATCCGACGGGCAGACCGCCGTCGCCACCACCCAGGTCGATATCACCGATGACGGCGACAACACGCCACGCGACCAAGACAACTGCCCCGACGTCAGTAACTGGGGTCAGACCGACTACGACAACGACGGGGTCGGAGACGAGTGCGACCCCGACCCCGGCTTCCCCACCCAGGACAAGCCCGGTGTCTGCGTCGTCGGCGAGAACTGCCCACCCGACAGCGGAACGCCCAGCACCCAGCCAACACCCGCACCGAGTGGAGGCTCAACGCCCACTCCGGCCGTCGCACCAGCACCCACCCAGACGCCCACGGCCTCTCCGACAACTACTGCTTCAAAGCGCCCCCTCCCCAACACGGGAATCAACGCGAGCAGGTTGACGGCCCTGGCGATCCTCGGGCTGCTCACCGGCGCAGCAGTTCTCCACTACCGCCGCAAGGTCACCTCATAG","VNRPSQHDKPNVAHYMKQLTFIILVTLLLFNQELPLPTTLPTASAAITTNVPLRVALLGDSYSAGNGAGHYYGDDKTAYRSSRNWAHNYVNWLNDQGAHAILNNIAHSGNVSDDVLGAQMKKLDSNTNLVMFTIGGNDVNFSDIVSQCFMIGMRDPATCRQKIDGANSKLPRVKKQTLDILQAIDDRLDDNAQVVIVGYPRLSSKDNFTLRDSHALWTDSYNAGAAVRKLGDDAKVIQSDLVSEWNSSHPSLKVTYVDGVINSFNGHEPDPSFPVVNHHRWINEFFETEGQEDQNGNTHAKTSGDPNEFYHPNLIGHEEIAKLIETKIGVPSIKSPKSNGEDIDIAFVVDSTGSMDSNVEAVRSKIHSIAEETSKKALSYRFALVDYKDHPQYNPKNYLARTDVDFTSDIPTLDAGLSSLTYEGGNLGNTNASVYSGVMQAVNMKWRNGVKKIVVVIGDAPPRDPEPGTGYTAASVAKAAYEVDPVSVYGIDTGDLNSTSFQTLVTSSTGTTANASSPDQVSDLVNKAISSELNKPFAWIQGPYVAKVGDPVDIDAAASHAVSGSLTSYEWDFNGDGVYDETGTSPRITHTFSQEFSGVIGLRVTQSDGQTAVATTQVDITDDGDNTPRDQDNCPDVSNWGQTDYDNDGVGDECDPDPGFPTQDKPGVCVVGENCPPDSGTPSTQPTPAPSGGSTPTPAVAPAPTQTPTASPTTTASKRPLPNTGINASRLTALAILGLLTGAAVLHYRRKVTS$","Adhesion protein","Extracellular, Periplasm, Cellwall","Thrombospondin type 3 repeat family","hypothetical adhesion protein","LPXTG-motif cell wall anchor domain","","Upton C., Buckley J.T. A new family of lipolytic enzymes?. Trends Biochem. Sci. 1995. 20(5):178-179. PMID: 7610479","","","

InterPro
IPR000601
Domain

PKD
PF00801	$\"[540-620]T$	PKD
SM00089	$\"[540-623]T$	PKD
PS50093	$\"[563-621]T$	PKD

InterPro
IPR001087
Family

Lipolytic enzyme, G-D-S-L
PF00657	$\"[55-223]T$	Lipase_GDSL

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
PF00746	$\"[713-751]T$	Gram_pos_anchor
TIGR01167	$\"[720-753]T$	LPXTG_anchor: LPXTG-motif cell wall anchor

InterPro
IPR002035
Domain

von Willebrand factor, type A
PR00453	$\"[343-360]T$ $\"[381-395]T$ $\"[453-461]T$	VWFADOMAIN
PF00092	$\"[344-528]T$	VWA
SM00327	$\"[342-526]T$	VWA
PS50234	$\"[344-533]T$	VWFA

InterPro
IPR003367
Repeat

Thrombospondin type 3 repeat
PF02412	$\"[643-655]T$	TSP_3

InterPro
IPR013831
Domain

Esterase, SGNH hydrolase-type, subgroup
G3DSA:3.40.50.1110	$\"[48-334]T$	no description

InterPro
IPR015455
Domain

Thrombospondin II
PTHR10199:SF10	$\"[619-657]T$	THROMBOSPONDIN 2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.410	$\"[336-549]T$	no description
PTHR10199	$\"[619-657]T$	THROMBOSPONDIN
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[728-748]?$	transmembrane_regions

","BeTs to 3 clades of COG3291COG name: PKD repeat proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG3291 is a-m-kz-----lb---g---------Number of proteins in this genome belonging to this COG is 1","***** IPB008859 (Thrombospondin, C-terminal) with a combined E-value of 7.8e-09. IPB008859F 627-664 IPB008859D 628-670 IPB008859D 592-634 IPB008859E 619-662 IPB008859E 642-685 IPB008859G 604-644 IPB008859H 621-671 IPB008859H 608-658","","","No significant hits to the PDB database (E-value < E-10).","Residues 55 to 223 (E_value = 4.1e-05) place ANA_1671 in the Lipase_GDSL family which is described as GDSL-like Lipase/Acylhydrolase.Residues 344 to 528 (E_value = 0.00011) place ANA_1671 in the VWA family which is described as von Willebrand factor type A domain.Residues 540 to 620 (E_value = 0.0017) place ANA_1671 in the PKD family which is described as PKD domain.Residues 643 to 655 (E_value = 0.00049) place ANA_1671 in the TSP_3 family which is described as Thrombospondin type 3 repeat.Residues 713 to 751 (E_value = 7.3e-05) place ANA_1671 in the Gram_pos_anchor family which is described as Gram positive anchor.","","type 3 repeat family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1672","1808106","1808954","849","4.73","-18.47","31347","ATGGACCAGCACATCACTCCCGCCATCCGGTGCAACGGCACCGCCGATGAGGCGGCCCGGTTCTACGCCGACGCCTTCCGTGAGGGCTCCGTCGTCGAGCAGGTGCCCGGGTACGCGTCCACGGTCAGCATCCATGGCTTCCGCCTCTCGCTCATCAACGGCGGTGACCAGGACGCCCCGAACCCGTCGATCAGCTGCATCCTGAACTTCGACCCGCTCCTGTTCGGTGGCGAGGAGCAGGCCCGGGCCTACCTCGATGAGCTCTACGAGCGTCTGTCCACCGGCGGCGTGCTCATGGAGCTGGGCGAGTACCCCTTCTCACCGCGCTACGCCTGGGTCCGCGACCGCTTCGGCATGACCTGGCAGCTCATGCTCACTGACCCGGCCGGCGAGCCGCGCCCCTTCATCCTGCCCTCCTTCATGTTCGGCGGTACCAATCACGCCAACGCCGAGGAGGCCACCGAGACCTGGATCGCCCTGTTCGACGACGCCCGCCGCGGGGCCCTGTACCGCTATGAGGAGGGCGGGCCGATGGAGGCGGGGACCGTCATGTTCACCGACTTCACGCTGCGCGGCACCTGGATGGCGGCCAGGGACTCGGGCCCATCCCACGACCTCACCTTCACACCCGGGGTCTCCATGATCGTCTCCTGCCGGGACCAGGAGGAGATCGACCACTACTGGGCGGGTCTGTCGGCCGTGCCCGAGGCCGAGCGCTGCGGCTGGTGCGTCGACCGCTGGGGCGTGTCCTGGCAAGTCGTCCCCCACAACATCGCCGAGCTCATGGCCGACGCCACCACACGCGAGAAGCTCCTGCACATGGGCAAGATCGACCTGGCCGGCCTGTAG","MDQHITPAIRCNGTADEAARFYADAFREGSVVEQVPGYASTVSIHGFRLSLINGGDQDAPNPSISCILNFDPLLFGGEEQARAYLDELYERLSTGGVLMELGEYPFSPRYAWVRDRFGMTWQLMLTDPAGEPRPFILPSFMFGGTNHANAEEATETWIALFDDARRGALYRYEEGGPMEAGTVMFTDFTLRGTWMAARDSGPSHDLTFTPGVSMIVSCRDQEEIDHYWAGLSAVPEAERCGWCVDRWGVSWQVVPHNIAELMADATTREKLLHMGKIDLAGL$","3-demethylubiquinone-9 3-methyltransferase","Cytoplasm","uncharacterized conserved protein, phnB familyCAC3467","hypothetical protein","3-demethylubiquinone-9 3-methyltransferase","","","","","

InterPro
IPR009725
Family

3-demethylubiquinone-9 3-O-methyltransferase
PF06983	$\"[3-124]T$ $\"[134-254]T$	3-dmu-9_3-mt

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.30	$\"[3-124]T$ $\"[131-267]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-48% similar to PDB:1U69 hypothetical protein PA2721 from Pseudomonas aeruginosa PAO1 (E_value = 1.4E_10);-49% similar to PDB:1U7I X-ray crystal structure of hypothetical protein PA1358 from Pseudomonas aeruginosa (E_value = 4.0E_10);","Residues 3 to 124 (E_value = 2.6e-13) place ANA_1672 in the 3-dmu-9_3-mt family which is described as 3-demethylubiquinone-9 3-methyltransferase.Residues 134 to 254 (E_value = 1.2e-44) place ANA_1672 in the 3-dmu-9_3-mt family which is described as 3-demethylubiquinone-9 3-methyltransferase.","","conserved protein, phnB family CAC3467","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1673","1809020","1809268","249","5.04","-3.05","9026","ATGGAATCCATTAATGGCGTGCCAGTCACCGACGAGATGATCCAGGAGTGGGCTGACGAAGCGGAACGTGGATACGACGTCGAAGTGCTGAAGAAGCGAGGACGCCGCCCCATCGGGGATGGTGCGGCGCGGGTCGTCCCAGTCCGTATGGACGACAGTCTGGTAGCCGCGGTCGACCAGCGCGCTGAGAAGGACGGCACCAGCCGCTCCGAGATCATTCGCTCGGCCGTACGAGCCTTCGTCGCGTGA","MESINGVPVTDEMIQEWADEAERGYDVEVLKKRGRRPIGDGAARVVPVRMDDSLVAAVDQRAEKDGTSRSEIIRSAVRAFVA$","CopG domain protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","CopG domain protein DNA-binding domain protein","","Acebo P., Garcia de Lacoba M., Rivas G., Andreu J.M., Espinosa M., del Solar G. Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and beta-sheet DNA binding proteins. Proteins 1998. 32(2):248-261. PMID: 9714164Gomis-Ruth F.X., Sola M., Acebo P., Parraga A., Guasch A., Eritja R., Gonzalez A., Espinosa M., del Solar G., Coll M. The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator. EMBO J. 1998. 17(24):7404-7415. PMID: 9857196","","","

InterPro
IPR002145
Domain

CopG-like DNA-binding
PF01402	$\"[45-82]T$	RHH_1

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 45 to 82 (E_value = 5e-05) place ANA_1673 in the RHH_1 family which is described as Ribbon-helix-helix protein, copG family.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1674","1811084","1809663","1422","6.15","-6.91","52182","ATGACGAGCACCCCCACCACCGCCGCGGCCGAGCAGCCCGATCAGAGCCGGCCCAGCGCCGTCGGCGGTCCTGGCCTGCTGGCCGTTGACGGCCATGAGCTTGAGCTGCCGCGCACCCCGGCGACCGACGGTGCCGACGGCCTGGGCGTGTCCAAGCTGCTGGGCTCCACCGGCGTGGTGACGCTCGACCCGGGCTTCACCAACACGGCGTCGTGCACCTCGCAGATCACCTACATCGACGGCGCGGCCGGGATTCTGCGCTACCGCGGCTACCCGATCGAGGAGCTGGCCAAGTCCTCGACCTTCCTGGAGGTCGCCTACCTCCTCATCAACGGTGAGCTGCCCGACCGTGAGTCCTTCGCGCGCATGGAGCGGCGCATCTCGCGCCACCGGCTCCTGCATGAGGACTTCCGTGGCTTCTTCACCTCCTTCCCCTCCTCGGGCCACCCGATGGCGATCCTCCAGGCCGGGATCGCGGGCCTGGCCACCTACTACGAGGACACCCTCGACCCGCACGACCCCTACGAGCGCGAGCTCGCCACCGTGCTGCTGCTGGCCAAGATGCCCACGATGATCAGCTACATCGCCCGGCGCGCCATCGGCCTGCCGCTGCTCTACCCCGACCCGCAGCGCTCCTACGTCGAGGACTTCATCCGCCTGACCTTCGGCATGCCCTTCCAGTCCTACGACATCGACCCGGCTGTCGTGCGGGCCCTGGACATGCTGCTCATCCTGCATGCCGACCACGAGCAGAACTGCTCGACCTCCACCGTGCGCCTCGTGGGATCGGCCGACGCCAACATGTACGCCTCCGTGGCTGCGGGCGTGGGCGCCCTGTCCGGGCCGCTGCACGGCGGCGCCAACGAGGCCGTCCTGCGGATGCTGGACACCATCCAGAGCTCGGGGATGAGCACGGCCGAGTTCGTCCGCAAGGTCAAGGACAAGGAGGACGGAGTGCGGCTCATGGGCTTCGGCCACCGGGTCTACAAGAACTACGACCCGCGCGCCGCCATCGTCAAGGAGACCGCCCACGACGTCCTGACCCGCCTGGGCTCCGACGACGGCGACCGCAAGCTCGAGATCGCCATGGAGCTGGAGGAGACGGCGCTTCGCGACGAGTACTTCGTCTCGCGCAGCCTCTACCCGAATGTCGACTTCTACACCGGCCTCATCTACCAGGCGATGGGCTTCCCCACGAAGATGTTCACACCCCTGTTCGCCCTGGGGCGCCTGCCGGGCTGGATCGCCCAGTACCGCGAGATGATCGCCGATCCTGCCAAGCGCATCGGGCGGCCCCGACAGGTTTACGACGGCTCCACCGAGCGCCACTACGTGGCCATGCACCGCCGCAAGCACGACGACGGCCAGTACCCGGACACCCGCGCCGGAGTCCCCAGCCTCGACCGCGTCACCAGGGTCTGA","MTSTPTTAAAEQPDQSRPSAVGGPGLLAVDGHELELPRTPATDGADGLGVSKLLGSTGVVTLDPGFTNTASCTSQITYIDGAAGILRYRGYPIEELAKSSTFLEVAYLLINGELPDRESFARMERRISRHRLLHEDFRGFFTSFPSSGHPMAILQAGIAGLATYYEDTLDPHDPYERELATVLLLAKMPTMISYIARRAIGLPLLYPDPQRSYVEDFIRLTFGMPFQSYDIDPAVVRALDMLLILHADHEQNCSTSTVRLVGSADANMYASVAAGVGALSGPLHGGANEAVLRMLDTIQSSGMSTAEFVRKVKDKEDGVRLMGFGHRVYKNYDPRAAIVKETAHDVLTRLGSDDGDRKLEIAMELEETALRDEYFVSRSLYPNVDFYTGLIYQAMGFPTKMFTPLFALGRLPGWIAQYREMIADPAKRIGRPRQVYDGSTERHYVAMHRRKHDDGQYPDTRAGVPSLDRVTRV$","Citrate synthase I","Cytoplasm","citrate synthase I","citrate synthase ","citrate synthase I","","Karpusas M., Branchaud B., Remington S.J. Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A. Biochemistry 1990. 29(9):2213-2219. PMID: 2337600Hull E.P., Spencer M.E., Wood D., Guest J.R. Nucleotide sequence of the promoter region of the citrate synthase gene (gltA) of Escherichia coli. FEBS Lett. 1983. 156(2):366-370. PMID: 6343122Remington S., Wiegand G., Huber R. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. J. Mol. Biol. 1982. 158(1):111-152. PMID: 7120407","","","

InterPro
IPR002020
Family

Citrate synthase
PR00143	$\"[184-197]T$ $\"[238-253]T$ $\"[260-288]T$ $\"[316-336]T$ $\"[381-397]T$ $\"[401-415]T$	CITRTSNTHASE
PTHR11739	$\"[58-473]T$	CITRATE SYNTHASE
PF00285	$\"[65-432]T$	Citrate_synt
PS00480	$\"[323-335]T$	CITRATE_SYNTHASE

InterPro
IPR010953
Family

Citrate synthase I
TIGR01798	$\"[31-444]T$	cit_synth_I: citrate synthase I

noIPR
unintegrated

unintegrated
G3DSA:1.10.580.10	$\"[70-335]T$	no description
PIRSF001369	$\"[62-450]T$	Citrate synthase

","BeTs to 20 clades of COG0372COG name: Citrate synthaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0372 is aomp-zyqvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB002020 (Citrate synthase) with a combined E-value of 8.3e-69. IPB002020A 86-96 IPB002020B 149-161 IPB002020C 184-197 IPB002020D 210-221 IPB002020E 259-298 IPB002020F 323-335 IPB002020G 401-417","","","-66% similar to PDB:2H12 Structure of Acetobacter aceti citrate synthase complexed with oxaloacetate and carboxymethyldethia coenzyme A (CMX) (E_value = 2.6E_114);-66% similar to PDB:1K3P Three Dimensional Structure Analysis of the Type II Citrate Synthase from E.coli (E_value = 2.0E_111);-65% similar to PDB:1OWB Three Dimensional Structure Analysis Of The Variant R109L NADH Complex of Type II Citrate Synthase From E. Coli (E_value = 1.3E_110);-65% similar to PDB:1OWC Three Dimensional Structure Analysis Of The R109L Variant of the Type II Citrate Synthase From E. Coli (E_value = 1.3E_110);-65% similar to PDB:1NXE A Novel NADH Allosteric Regulator Site is Found on the Surface of the Hexameric Type II Phe383Ala Variant of Citrate Synthase (E_value = 1.7E_110);","Residues 65 to 432 (E_value = 4.9e-173) place ANA_1674 in the Citrate_synt family which is described as Citrate synthase.","","synthase I (gltA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1675","1811281","1812561","1281","6.37","-4.90","46483","TTGATAAACTTATCAAGCCAGTCGCTCGTTGATAAACTTATCATCATGAGGACTCCTCTTGACTCGCCGTTCAGCCCAGGATCAGACACGGTGCCCCTGGTGTGGGCGGGGCGCATCGAGCACCTCAGCGACTGGCGCGACGCTCTTCGCCCGCGCCGCGCCGCAGGCATCCACGAGCGCGGCCGCACCATCCTGGGGGAAGCCGGCTCCGGAAAATCCGCGTTGGTGCGTCGGATCTCGAGTGAGGCCTTGGATGCGGGCGACTGGGTCACGCCACAGCTGCGTATCCCGTCAGGGAGCGACCCCATCAAGCGAGTCGCCTCGGCTCTACTGACCCTCGCCGACACGGCGGGTCTGCCAGCAGCCAGGGAGCAGCGCATCGGCGACCTGCTGCGCCGCGTTGAGTCCGTGGCCGCTTCCGGCATCTCCCTGTCCGTGCGAGCCCAGGACGGTCCCGAGCCGTATTCCGCCCTGACCGATCTGCTCATTGAGATCGGCCGTGCGGCCACCAAGCGCCATGCCGTGGTGATGATCCACATCGACGAGGTCCAGAACATCACTGATGAGCACGCGCGCTCCCAGCTGCTCATCGCCCTGGGTGACGCACTCACTCACGAGGAGCCCACGCCCCTTCCCGGCGGCCTGAGCGTTGGCTCGGCGCTTCCTATCGCCGTCTACCTGACCGGGCTGCCCGAGTTCGCGGACATGGCCGGAGCCCGATCCGGTGCCACCTTCGCGCGTCGTTTCCAGACCACCACGCTGGAGACCATCGACGACGACGACCTTCTGACCGCACTCCACCCCTTCATCAGCCAGGGGTGGCCTATCACCACCGCCGACGGCGGCACAGACCGGATCTTCATGGAGCCCGACGCCCAACGCGCCATCATCGAGCTCTCCTGCGGCGAGCCGTTCCTCTTCCAGCTCGCCGGGCAGTGCGCCTGGCACGCCAGCACCGACAGCATCATCACCGCCGAGCACGTCCGCACCGGATGGAGCAGGCAGGCGGTCCACGAGGCGGAGGCGCATGTGCAGCGCATTCTCGACCGGCTCCCACCGCGCGAGAGGGAGTTCGTCGAGGCAATGGCCGAGCTCGCACCCGAGGAGCGTTCTCTGACGAACATCGCCAACCGGCTCGGGCACAAGAGGGCCACGGACGCAGGCCCCACCGCGCAGCGGCTCGACCTGACCCGCAGGATCATCCGGCGCGGTAGGCCCTACCGATTCCAGCACCGGGCCGTCGGGGCCTATCTCACTTCCGAGTGGCCCGAGGTGGGCTGA","LINLSSQSLVDKLIIMRTPLDSPFSPGSDTVPLVWAGRIEHLSDWRDALRPRRAAGIHERGRTILGEAGSGKSALVRRISSEALDAGDWVTPQLRIPSGSDPIKRVASALLTLADTAGLPAAREQRIGDLLRRVESVAASGISLSVRAQDGPEPYSALTDLLIEIGRAATKRHAVVMIHIDEVQNITDEHARSQLLIALGDALTHEEPTPLPGGLSVGSALPIAVYLTGLPEFADMAGARSGATFARRFQTTTLETIDDDDLLTALHPFISQGWPITTADGGTDRIFMEPDAQRAIIELSCGEPFLFQLAGQCAWHASTDSIITAEHVRTGWSRQAVHEAEAHVQRILDRLPPREREFVEAMAELAPEERSLTNIANRLGHKRATDAGPTAQRLDLTRRIIRRGRPYRFQHRAVGAYLTSEWPEVG$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-53% similar to PDB:1X3S Crystal structure of human Rab18 in complex with Gppnhp (E_value = );-42% similar to PDB:1UDX Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1676","1813825","1812578","1248","4.96","-16.32","43643","GTGGAGACGCCCCTGGCCCGTGAGGAAGAATCAGGGCCCGTGACCACCAGCGCGACACCTGAGACCGCCTCCAGCCTCCACCTGCCCCGCCGACTCGCCCTGCCCGACTTCCCCTGGGACTCGCTGACCCCCTATCGGGAGCGGGCCGCCCAGCACCCGGACGGCGTCGTTGACCTCGCGGTGGGCACGCCCGTCGACCCCACCCCCGAGATCGCCCGCAACGCCCTGTTCTCGGCGGCCAACGCCCCCGGCTACCCGACGGCGGTCGGTGCCCCCGTGGTGCGTGCCGCCATCGCCGAGTGGATGGAGAGACGTCGGGGCGTGGCCGGCCTGGGCGATGACGAGGTCATCCCCACCATCGGCTCCAAGGAGTCCGTGGCCCTCCTGCCGCTGCACCTGGGGGTGCGTCCCGGCGACCTCGTCCTGCACCCGCGTGCCGCCTACCCCACCTACGACGTCGGCGCCCGCCTCGTGGGGGCCACCCCGGTCCCGGTGGACACCGACGCCGACCCCGCCACCTGGGGCATCACCGAGGACGCGCCCGTGGCCGTCGTCTGGCTCAACAGCCCCGGCAACCCCGACGGGCACGTCCTGAGCGTCGAGCAGATGGCCCGGATCGTCGCCTGGGCCCGGGCGCGGGGCGCCGTCGTCATCTCCGATGAGTGCTACGCCGAGCTCGGCTGGGAGGCGCCGTGGGACACCCAACCGATCCCGAGCCTCCTGGACCCCCGGGTCGGAGGGGAGGCGGGCCGAAGCGGCCTGCTCGCCCTGTACTCCCTGTCCAAGCAGTCCAACCTGGCCGGCTACCGGGCGGCCTTCCTCGCCGGTGACGCGCGGCTCGTGGGTGCCGTCACCGAGGTGCGCAAGCACACCGGCATGCTCATGCCGACTCCGGTGCAGGCGGCCCTCGTGGCCGCCCTCGGCGACGAGGCGCACATGGAGGTGCAGAAGGAGGTCTACCGGGAGCGCCGCGAGGTCCTCGTTGAGGCGACCGCCGCCGCCGGGCTCGTCAACGACCCGGCCTCCGTGGCCGGCCTGTACCTGTGGCTCCGGGGGCCCGAGTCGATGAGCGCCTACGAGCTCGTGGGGGCCTTCGCCGAGCTGGGGATCGTTGTGGCCCCCGGCGACTTCTACGGTCAGGCTGGGGCCGGGCGGGTGCGGATGAGCCTGACCGACACCGACGAGCGCGTGGCCGCCGCCGCCGCGCGCCTGCGCTCGCCCGAGGCCGCCGCCCTCTTCGCCGGCTGA","VETPLAREEESGPVTTSATPETASSLHLPRRLALPDFPWDSLTPYRERAAQHPDGVVDLAVGTPVDPTPEIARNALFSAANAPGYPTAVGAPVVRAAIAEWMERRRGVAGLGDDEVIPTIGSKESVALLPLHLGVRPGDLVLHPRAAYPTYDVGARLVGATPVPVDTDADPATWGITEDAPVAVVWLNSPGNPDGHVLSVEQMARIVAWARARGAVVISDECYAELGWEAPWDTQPIPSLLDPRVGGEAGRSGLLALYSLSKQSNLAGYRAAFLAGDARLVGAVTEVRKHTGMLMPTPVQAALVAALGDEAHMEVQKEVYRERREVLVEATAAAGLVNDPASVAGLYLWLRGPESMSAYELVGAFAELGIVVAPGDFYGQAGAGRVRMSLTDTDERVAAAAARLRSPEAAALFAG$","Aminotransferase, class I and II","Cytoplasm","N-succinyl-aminoketopimelate aminotranferase","putative aminotransferase ","aminotransferase, class I and II","","Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K., Okamoto A., Higuchi T., Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 1991. 266(4):2567-2572. PMID: 1990006","","","

InterPro
IPR004838
Binding_site

Aminotransferases class-I pyridoxal-phosphate-binding site
PS00105	$\"[259-272]?$	AA_TRANSFER_CLASS_1

InterPro
IPR004839
Domain

Aminotransferase, class I and II
PF00155	$\"[54-404]T$	Aminotran_1_2

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[84-309]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[71-405]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF19	$\"[71-405]T$	AMINOTRANSFERASE RELATED

","BeTs to 22 clades of COG0436COG name: PLP-dependent aminotransferasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0436 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB001176 (1-aminocyclopropane-1-carboxylate synthase signature) with a combined E-value of 2.8e-15. IPB001176D 138-159 IPB001176E 179-203 IPB001176F 215-238 IPB001176G 253-277 IPB001176H 286-309","","","-43% similar to PDB:2O1B Structure of aminotransferase from Staphylococcus aureus (E_value = 2.8E_24);-42% similar to PDB:2DOU probable N-succinyldiaminopimelate aminotransferase (TTHA0342) from Thermus thermophilus HB8 (E_value = 2.3E_23);-43% similar to PDB:2O0R The three-dimensional structure of N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis (E_value = 5.0E_18);-41% similar to PDB:1DJU CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3 (E_value = 6.8E_15);-41% similar to PDB:1GD9 CRYSTALL STRUCTURE OF PYROCOCCUS PROTEIN-A1 (E_value = 6.8E_15);","Residues 54 to 404 (E_value = 2.3e-36) place ANA_1676 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.Residues 67 to 301 (E_value = 0.0027) place ANA_1676 in the Beta_elim_lyase family which is described as Beta-eliminating lyase.","","aminotranferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1677","1814191","1813841","351","3.95","-20.28","12928","ATGACGTACGTCATTGCCCAGCCCTGCGTCGACGTCAAGGACCGCGCCTGCGTCGACGAGTGTCCCGTCGACTGCATCTACGAGGGTGAACGCAGCCTCTACATCAACGCCGACGAGTGCGTCGACTGCGGTGCCTGCGAGCCCGTCTGCCCCACCGAGGCGATCTTCTACGAGGACGATGTTCCCGAGGAGTGGGAGGACTACACCCGCGCCAACATCGACTTCTTCGAGCTCAAGGGACTCGGCTCGCCCGGCGGCGCCCAGAGGACCGGCGCGCTGGACTACGACGACCCCATGATCGCCGCCCTGCCCCCGCAGAACGAGGAGTGGAAAGAGGCCAACGGCTACTGA","MTYVIAQPCVDVKDRACVDECPVDCIYEGERSLYINADECVDCGACEPVCPTEAIFYEDDVPEEWEDYTRANIDFFELKGLGSPGGAQRTGALDYDDPMIAALPPQNEEWKEANGY$","Ferredoxin","Cytoplasm, Extracellular","ferredoxin","ferredoxin","4Fe-4S ferredoxin, iron-sulfur binding domain protein","","George D.G., Hunt L.T., Yeh L.S., Barker W.C. New perspectives on bacterial ferredoxin evolution. J. Mol. Evol. 1985. 22(1):20-31. PMID: 3932661Trower M.K., Marshall J.E., Doleman M.S., Emptage M.H., Sariaslani F.S. Primary structure of a 7Fe ferredoxin from Streptomyces griseus. Biochim. Biophys. Acta 1990. 1037(3):290-296. PMID: 2106913Stout C.D. Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 A resolution. J. Mol. Biol. 1989. 205(3):545-555. PMID: 2926817","","","

InterPro
IPR000813
Family

7Fe ferredoxin
PR00354	$\"[9-19]T$ $\"[19-29]T$ $\"[35-52]T$	7FE8SFRDOXIN

InterPro
IPR001450
Domain

4Fe-4S ferredoxin, iron-sulfur binding
PR00353	$\"[33-44]T$ $\"[45-56]T$	4FE4SFRDOXIN
PF00037	$\"[33-56]T$	Fer4
PS00198	$\"[40-51]T$	4FE4S_FERREDOXIN

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.20	$\"[2-78]T$	no description

","BeTs to 9 clades of COG1146COG name: Ferredoxin 3Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1146 is aompk---vdr--cefg-s-ujx---Number of proteins in this genome belonging to this COG is 1","***** IPB000813 (7Fe ferredoxin signature) with a combined E-value of 2.6e-25. IPB000813A 9-19 IPB000813B 19-29 IPB000813C 35-52 IPB000813B 48-58","","","-76% similar to PDB:1BC6 7-FE FERREDOXIN FROM BACILLUS SCHLEGELII, NMR, 20 STRUCTURES (E_value = 4.6E_26);-76% similar to PDB:1BD6 7-FE FERREDOXIN FROM BACILLUS SCHLEGELII, NMR, MINIMIZED AVERAGE STRUCTURE (E_value = 4.6E_26);-75% similar to PDB:1BQX ARTIFICIAL FE8S8 FERREDOXIN: THE D13C VARIANT OF BACILLUS SCHLEGELII FE7S8 FERREDOXIN (E_value = 5.1E_25);-75% similar to PDB:1BWE ARTIFICIAL FE8S8 FERREDOXIN: THE D13C VARIANT OF BACILLUS SCHLEGELII FE7S8 FERREDOXIN (E_value = 5.1E_25);-76% similar to PDB:1H98 NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS (E_value = 6.2E_23);","Residues 33 to 56 (E_value = 4.7e-08) place ANA_1677 in the Fer4 family which is described as 4Fe-4S binding domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1678","1814794","1814474","321","11.89","11.13","11774","ATGACCTCATGGCACCTGCGCGGAATCCGGAAGGGGGTGGGGAAGGGACTGCTGGTGCCGGGGTGGGAGCGCCCGACACCGCCACCAAGGCTCCGTGAAGGCGATCAGGCCCGAGACTTGGTGACCACCGTGCTGACATTATCGGGACCACCGTTGACGCGTCCGACCAGGATCCTTGGAATGCTGCGGTTCTTCTTCGGGGTGCGGCGTCGATGCAGGGTTGATGTCAGCGCGGTGGACACTCGTGTCCTGGCGGGTTTCGTCATTCGGTCCACCGTTGCCTCCAGCATCACCGGCCTACCTCGGTTCCTGCCAGAGTGA","MTSWHLRGIRKGVGKGLLVPGWERPTPPPRLREGDQARDLVTTVLTLSGPPLTRPTRILGMLRFFFGVRRRCRVDVSAVDTRVLAGFVIRSTVASSITGLPRFLPE$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1679","1816212","1814983","1230","7.55","1.12","43916","ATGAGTGTGTCCGCTTCGAGTAGGTCGTCTGGCCTGGATGTTGCGGTTGTAGCGCTTCTGGTGTCTGCGCTCGTTGGAGCGATAGGTCATCGGATGGTATTCCTGTACCAGGATATGTTCTGGAGCGAGAGTTTGCTGTGGGAATTCGTTCTTGATTCTCTACTCAATAATCTTTTGTGGACTCTTGTTGTTGCCGTTGCAATCTCTGTGAAGGGGCGCGGTCAGGTGGGGGTGCTGGCCTCGTTGGTCGCCGCCGTTCCATGGGTGGTGGGATATCCGGGTACATTTCAATCGACAGTGTGGGGGGTTGTATGTATTTTGTTGCCGATCATCATTGCCTTGGCGCTCTCCTTTGGGAGTGCTCACATTAAGCGGAGGCGGTTGCCTCTGGGGGTTGTCTTTGCTGAGGGGTTGGCAATTGTCGCTGTTGTAGACGGATTTGCGAGGTTGCTTTACTTCTTTTATGGGGTTGCTGGTTATCCAGGGCATCCTTTTTCTGATACGCTCATCAGTTATGGGGTGGGTTTGACGGATGGTGGAATTTTCGATGTTGTGAGGCTTCTTCTGGGTGTGCTGGTGCTCGTCTTGGTGAGCAGGAGGCGTTGGTATGTCGTCTTCGCTGTTCTCGTAGTGGCTCAGGTAATCATCTATGTGTTCGAGTATGTGTCTTGGTATAGGGATGAGATCAGCCCTCTGGTGGTTGTCGCTGCCGCGGTTGTGGTGTGGATGCGCTCAGTTCGGCAGTGGTTCTCCGGTACCTGGAATCCCAGTGACGTTCCGGTGGATCACTCCCCCGTTGTCGTTCCGGTGGGGATGGCTGTGACCGTTCCAGGCGTCCACCCTCAGGGGCAGCGGGTGCTCGGTTCGGACGGGAACCTGTCTATGGCGGTCCCCGCTGCTTCCTCACTGTTCGAGTCGATGGGTACTCAGGGTGCCGGAGGTGATCCGGCACCGTCAGTGGATGTGCCGCCGGCCGATGTGGACATTTACGCTCGCGTGGCGGCGATGTTGCCTTCGACGCGAACAACCTTCTGGATCAGCTTCTTCTTCGGTTTGTTCGGATTGATACCCATGATGATGGGGAACAGTATGGCGCGGAACCTCGGCGTGGTGACGAACTCCTACAACCGAGAGTTTCTTAAAGGGTGGCTCATTGGCGTGGCGGTGTGGGGAGGGCTGAGCCTCCTCTCGCTTCTCCTCCTCTACGGCAGTGTGTCGTCGAGCTACTGA","MSVSASSRSSGLDVAVVALLVSALVGAIGHRMVFLYQDMFWSESLLWEFVLDSLLNNLLWTLVVAVAISVKGRGQVGVLASLVAAVPWVVGYPGTFQSTVWGVVCILLPIIIALALSFGSAHIKRRRLPLGVVFAEGLAIVAVVDGFARLLYFFYGVAGYPGHPFSDTLISYGVGLTDGGIFDVVRLLLGVLVLVLVSRRRWYVVFAVLVVAQVIIYVFEYVSWYRDEISPLVVVAAAVVVWMRSVRQWFSGTWNPSDVPVDHSPVVVPVGMAVTVPGVHPQGQRVLGSDGNLSMAVPAASSLFESMGTQGAGGDPAPSVDVPPADVDIYARVAAMLPSTRTTFWISFFFGLFGLIPMMMGNSMARNLGVVTNSYNREFLKGWLIGVAVWGGLSLLSLLLLYGSVSSSY$","Membrane protein","Membrane, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[49-69]?$ $\"[74-92]?$ $\"[98-118]?$ $\"[128-148]?$ $\"[179-197]?$ $\"[202-224]?$ $\"[228-246]?$ $\"[344-364]?$ $\"[383-403]?$	transmembrane_regions

InterPro
IPR007391
Family

VanW
PF04294	$\"[394-531]T$	VanW

InterPro
IPR013222
Domain

Glycosyl hydrolase family 98, putative carbohydrate-binding module
SM00776	$\"[67-202]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[35-57]?$	transmembrane_regions

","BeTs to 3 clades of COG2720COG name: Uncharacterized BCR, vancomycin resistance proteinFunctional Class: SThe phylogenetic pattern of COG2720 is a-----vcEBrh---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-54% similar to PDB:1WIB Solution structure of the N-terminal domain from mouse hypothetical protein BAB22488 (E_value = );-37% similar to PDB:1F8N LIPOXYGENASE-1 (SOYBEAN) AT 100K, NEW REFINEMENT (E_value = );-37% similar to PDB:1FGM LIPOXYGENASE-1 (SOYBEAN) AT 100K, N694H MUTANT (E_value = );-37% similar to PDB:1FGO LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495A MUTANT (E_value = );-37% similar to PDB:1FGQ LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495E MUTANT (E_value = );","Residues 777 to 914 (E_value = 1.4e-39) place ANA_1681 in the VanW family which is described as VanW like protein.","","like protein family","","1","","","Tue Aug 7 11:34:40 2007","","Tue Aug 7 11:34:40 2007","","","Tue Aug 7 11:34:40 2007","Tue Aug 7 11:34:40 2007","Tue Aug 7 11:34:40 2007","","","Tue Aug 7 11:34:40 2007","","","Tue Aug 7 11:34:40 2007","","","","Tue Aug 7 11:34:40 2007","Tue Aug 7 11:34:40 2007","","","","","yes","","" "ANA_1682","1821232","1819310","1923","5.08","-25.28","69570","ATGAGCGTGCGCCAGGATCTGCGCAACGTCGCCATTGTCGCCCACGTCGACCACGGCAAGACCACTCTTGTCGACGCCATGCTTTGGGAGGCGGGGGCCTTCGGGGCCCGGGCCACCGAGGAGACCACAGGTGAGCGCGTCATGGACTCCGGCGAGCTGGAGCGCGAGAAGGGCATCACGATCCTCGCGAAGAACACGGCGGTCCACTACTCGGGCCCCTCCGCTGCGGACGCCGGCTGCCCCGAGGGCATCGTCATCAACGTCATCGACACCCCCGGTCACGCCGACTTCGGCGGCGAGGTCGAGCGCGGGCTGTCCATGGTCGACGGCGTCGTCCTCCTCGTCGACGCCTCCGAGGGGCCCCTGCCCCAGACCCGCTTCGTGCTGCGCAAGGCCCTGGCCGCGAACCTGCCGGTCATCCTCGTGGTCAACAAGGTGGACCGCCCCGACTCCCGGCTCGACGAGGTCGTCTCCGAGTCCACTGATCTGCTGCTGTCCCTGGCCAGCGACCTGGCCGACGAGCACCCCGACATCGACCTCGACGCCGTCCTGGACGTGCCCGTCATCTACGCCTCCGCCAAGGCTCGCCGCGCCGACACCGAGGCCCCGGCCGACGGCGAGCTGCCGGCCAACGAGAACCTCGAGCCGCTCTTCCGCACCATCATCGAGCGGATCCCCGGCCCCTCCTACGAGGAGGGCGCCCCCCTGCAGGCCCACGTCACCAACCTGGACGCCTCACCCTTCCTGGGCCGCCTGGCGCTGCTGCGCATCCACAACGGCACCCTGCGCAAGGGGCAGACGGTGGCCTGGGCCCGCCACGACGGCTCCCTGTCCTCCGCCCGCGTCTCCGAGCTCCTCGTCACCGAGGGGCTGGATCGCAAGCCCGCCGAAGAGGCGCACGCCGGCGACATCGTCGCCGTCGCCGGGATCGAGGACATCACCATCGGCGAGTCCCTCGTGGACCCCGAGGACCCGCGGCCCCTGCCGCTCATCACCGTGGACGACCCGGCCATCGCCATGACCATCGGCATCAACACCTCCCCGATGGCCGGGCGCACCAAGGGCGCCAAGGTCACCGCCCGTCAGGTCAAGGACCGCCTGGACCGCGAGCTCATCGGCAACGTATCCCTGCGGGTCCTGCCCACCTCCCGACCCGACGCCTGGGAGGTGCAGGGACGCGGCGAGCTGGCGCTGGCGATCCTCGTGGAGCAGATGCGCCGCGAGGGATTCGAGCTGACCGTCGGCAAGCCCCAGGTGGTCACCCGCACCATCGACGGCAAGCGCCACGAGCCCATCGAGCGCATGACCATCGATGTCCCCGAGGAGTACCTGGGCGCCGTCACCCAGCTCATGGCCGCCCGCAAGGGCCAGATGGAGACCATGACCAACCACGGCACCGGCTGGATCCGCATGGAGTTCCTCGTGCCGGCCCGCGGCCTCATCGGCTTCCGCACCCAGTTCCTCACCGAGACCCGCGGTACCGGCATCGCCTCCTCCATCGCTGAGGGCTACGCCCCCTGGGCCGGCAAGATCGTCTCGCGCACCACAGGCTCCCTCGTCTCCGACCGCGCCGGGGCCGTGACCGCTTACGCGCTCATCCGCCTGCAGGACCGCGGCAGCTTCTTCGTTGAGCCCACCCAGGAGACCTACGAGGGGCAGGTCGTGGGGGAGAACCCCCGCGGCGAGGACATGGACGTCAACGTGGTCCGTGAGAAGCAGCAGACCAACATGCGCTCCTCGACGGCGGACACCTTCGAGGCCCTCGTGCCGCCGCGCCGCCTCACCCTGGAGGAGGCCCTCGAGTTCGCCGCCGACGACGAGTGCGTCGAGGTCACCCCGGAGGCCGTGCGCATCCGCAAGGTCATCCTCAACTCCCAGGAGCGTTTCCGCGAGAACGCCCGCCGTCGTCGTGCCGAGGCCTGA","MSVRQDLRNVAIVAHVDHGKTTLVDAMLWEAGAFGARATEETTGERVMDSGELEREKGITILAKNTAVHYSGPSAADAGCPEGIVINVIDTPGHADFGGEVERGLSMVDGVVLLVDASEGPLPQTRFVLRKALAANLPVILVVNKVDRPDSRLDEVVSESTDLLLSLASDLADEHPDIDLDAVLDVPVIYASAKARRADTEAPADGELPANENLEPLFRTIIERIPGPSYEEGAPLQAHVTNLDASPFLGRLALLRIHNGTLRKGQTVAWARHDGSLSSARVSELLVTEGLDRKPAEEAHAGDIVAVAGIEDITIGESLVDPEDPRPLPLITVDDPAIAMTIGINTSPMAGRTKGAKVTARQVKDRLDRELIGNVSLRVLPTSRPDAWEVQGRGELALAILVEQMRREGFELTVGKPQVVTRTIDGKRHEPIERMTIDVPEEYLGAVTQLMAARKGQMETMTNHGTGWIRMEFLVPARGLIGFRTQFLTETRGTGIASSIAEGYAPWAGKIVSRTTGSLVSDRAGAVTAYALIRLQDRGSFFVEPTQETYEGQVVGENPRGEDMDVNVVREKQQTNMRSSTADTFEALVPPRRLTLEEALEFAADDECVEVTPEAVRIRKVILNSQERFRENARRRRAEA$","GTP-binding protein TypA","Cytoplasm","widely conserved protein similar to thoseannotated as GTP-binding elongation factor TypA/BipA","K06207 GTP-binding protein","GTP-binding protein TypA","","Paduch M., JeleD F., Otlewski J. Structure of small G proteins and their regulators. Acta Biochim. Pol. 2001. 48(4):829-850. PMID: 11995995","","","

InterPro
IPR000640
Domain

Translation elongation factor EFG/EF2, C-terminal
G3DSA:3.30.70.240	$\"[430-519]T$	no description
PF00679	$\"[427-515]T$	EFG_C

InterPro
IPR000795
Domain

Protein synthesis factor, GTP-binding
PR00315	$\"[9-22]T$ $\"[56-64]T$ $\"[87-97]T$ $\"[103-114]T$ $\"[139-148]T$	ELONGATNFCT
PF00009	$\"[5-171]T$	GTP_EFTU
PS00301	$\"[49-64]?$	EFACTOR_GTP

InterPro
IPR004161
Domain

Translation elongation factor EFTu/EF1A, domain 2
PF03144	$\"[250-320]T$	GTP_EFTU_D2

InterPro
IPR005225
Domain

Small GTP-binding protein domain
TIGR00231	$\"[5-195]T$	small_GTP: small GTP-binding protein domain

InterPro
IPR006298
Family

GTP-binding protein TypA
TIGR01394	$\"[7-630]T$	TypA_BipA: GTP-binding protein TypA

noIPR
unintegrated

unintegrated
G3DSA:2.40.30.10	$\"[230-330]T$	no description
G3DSA:3.40.50.300	$\"[3-168]T$	no description
PTHR23115	$\"[4-197]T$ $\"[213-352]T$	TRANSLATION FACTOR
PTHR23115:SF14	$\"[4-197]T$ $\"[213-352]T$	GTP-BINDING PROTEIN TYPA/BIPA

","BeTs to 13 clades of COG1217COG name: Predicted membrane GTPase involved in stress responseFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1217 is ---------drlbcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB000640 (Elongation factor G, C-terminal) with a combined E-value of 2.9e-58. IPB000640A 8-28 IPB000640B 48-70 IPB000640C 86-125 IPB000640D 137-147 IPB000640E 481-495***** IPB005517 (Elongation factor G, domain IV) with a combined E-value of 9.4e-47. IPB005517A 8-32 IPB005517B 48-70 IPB005517C 86-125 IPB005517E 424-458***** IPB013842 (GTP-binding protein LepA, C-terminal) with a combined E-value of 3.4e-45. IPB013842A 7-41 IPB013842B 80-120 IPB013842C 211-265 IPB013842F 419-463***** IPB000178 (Initiation factor 2) with a combined E-value of 5.4e-18. IPB000178B 6-44 IPB000178C 86-121 IPB000178D 122-148***** IPB004160 (Elongation factor Tu, C-terminal) with a combined E-value of 4.9e-13. IPB004160A 7-27 IPB004160B 78-128","","","-60% similar to PDB:1N0U Crystal structure of yeast elongation factor 2 in complex with sordarin (E_value = 1.1E_22);-60% similar to PDB:1N0V Crystal structure of elongation factor 2 (E_value = 1.1E_22);-60% similar to PDB:1S1H Structure of the ribosomal 80S-eEF2-sordarin complex from yeast obtained by docking atomic models for RNA and protein components into a 11.7 A cryo-EM map. This file, 1S1H, Contains 40S subunit. The 60S Ribosomal Subunit Is In File 1S1I. (E_value = 1.1E_22);-60% similar to PDB:1U2R Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae (E_value = 1.1E_22);-60% similar to PDB:1ZM2 Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA (E_value = 1.1E_22);","Residues 5 to 229 (E_value = 1.3e-61) place ANA_1682 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain.Residues 82 to 147 (E_value = 1.7e-08) place ANA_1682 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 250 to 320 (E_value = 7.5e-12) place ANA_1682 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2.Residues 427 to 515 (E_value = 7e-24) place ANA_1682 in the EFG_C family which is described as Elongation factor G C-terminus.","","conserved protein similar to those annotated as GTP-binding elongation factor TypA-BipA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1683","1822644","1821442","1203","7.64","1.46","41530","ATGAAGCTGTTGGTGGAGGACCACGTCGTTGAGTTTCTCGTGTCGCGAGGCCTGTATGTCCTGGCGAATTCGGCAGTTCCCGTATTGCTGGCGATAGCTGTCGCATCGGAGGGTTACAGTGCCTCCGGTGTCGGGCTGGTTCTCGGCGTGGGTGCGCTGCCGGGCATCTTGGGTGCGTTGTTGGCTCCGCAGATGCTGGTCCACGTCAGCCCCAAGACCATGTTCGGCGGTGCGGCAGCCGCATGGATCGTGATCTGTGGTGGGATCGCGATACTGAGTCGTGCCGGCTCGGTTGGCCTCGGCGTGTACGTCACTGTGTCGTTCGCCTTGGAGTTTGTCGCATCGATCATGTATCCAACGATGGGGTCCTATGTCGCAGACCTCGTGCGGTCGGATCTGCTGGATCGGATGAATTCTGCCAGGGCTGTCGTCGCTGGCCTGTGCGCGGTCGCCGGCCCTGGAGTTATTGCGCTGGTGCAGTCATGGCGAGGTGTTTCAGATGCTTGGTGGCTGGTATCCCTGCTGATGCTCGTGTGCCTGCTGTCGCAGAGCCGCCTGCCGAAGGGGCGTAGAACGGGTGGTGCGGATCGTGTGACTGCGCTGAAGCGGGGCCTGCGGGCCGCTGCACGTTCCCGAGGTGTTCTCGTTGTGCTGGTCGGCTCCGGGGTGTGGCACTTTACTGTGTGGGGAAGTTACATGACGCTATGCCCCGTCGTGCTGCGCGATGAGTATCAGGCGTTATGGTTCATCGGTGTCAGCGAGTCCCTGTTTGCGGTCGGTGGGATCGTGGGGTCCTTGGTTCGTCTGCCATCCCGCTTGTCGCGCCCAGTGCTGTGCCTGGTTGCGCTTCTCAGCTTCGTTCCGGTTCCGGTCAGCGTGGTGCTCGGTGCGCCTCTGTGGCTGGTCGCTGTGACCCTCTTCGTGTCAAGTGCTGTGATTGCGTCGACGAGTGTGGCTTGGGAGACGTTTCTTCAGTCTCGAGTCGAGCGTGACGCACTGCCCTCTGTGTTCGCCTTGGACTACCTCGCCGGGGATGGTGTCGCTCCGCTTGGCTATGTGGCTGTTCCTGCTCTTGCGGTGTGGCTGGGGCAGGGGGCGGGTGTGCTGGTGGCCGCTGGGGTATGTGTCGTGGTGCTGCTCGGTTGCCTGTGGGCGTATGCCGTTTCTCCGGAGGTGGAGGACGTCGAATCGGCTGCGGAGTGA","MKLLVEDHVVEFLVSRGLYVLANSAVPVLLAIAVASEGYSASGVGLVLGVGALPGILGALLAPQMLVHVSPKTMFGGAAAAWIVICGGIAILSRAGSVGLGVYVTVSFALEFVASIMYPTMGSYVADLVRSDLLDRMNSARAVVAGLCAVAGPGVIALVQSWRGVSDAWWLVSLLMLVCLLSQSRLPKGRRTGGADRVTALKRGLRAAARSRGVLVVLVGSGVWHFTVWGSYMTLCPVVLRDEYQALWFIGVSESLFAVGGIVGSLVRLPSRLSRPVLCLVALLSFVPVPVSVVLGAPLWLVAVTLFVSSAVIASTSVAWETFLQSRVERDALPSVFALDYLAGDGVAPLGYVAVPALAVWLGQGAGVLVAAGVCVVVLLGCLWAYAVSPEVEDVESAAE$","Permease of the major facilitator superfamily","Membrane, Cytoplasm, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[12-360]T$	MFS_1

noIPR
unintegrated

unintegrated
tmhmm	$\"[15-35]?$ $\"[41-61]?$ $\"[76-94]?$ $\"[100-122]?$ $\"[143-163]?$ $\"[169-189]?$ $\"[213-233]?$ $\"[247-267]?$ $\"[276-294]?$ $\"[300-320]?$ $\"[341-361]?$ $\"[367-387]?$	transmembrane_regions

","BeTs to 3 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 360 (E_value = 1.8e-08) place ANA_1683 in the MFS_1 family which is described as Major Facilitator Superfamily.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1684","1823087","1822641","447","11.31","15.86","15526","GTGACGACGTCGAGGTGCGGGCCTCGGCCGCTCCCCGTCGCGGCGGCATGGCCGAGTCCTTCCGGCGCCGCCAGGAGCTGCGTGAGCAGCAGGAGCGGCGCGACGGCCTGCGAGATGCCGAGCCGGCCCCGGCGGTGCGCCCGGAGTACCTGGCGGGGGAGGGAACTCACCGCACCAACCTCGACACCGGTGATGCCGGATCCCTCATCGAGGCCTACGCCGAGCAGGTGCGCAGCCTTCCCGCTCGGGCCGCGGACGATGCGGCGCCCGGCGCGGCCACCGGCGCCACCAGCAGCCTCAACCGCACGGTCGTCGCCGCCGCCGGACTGCTCGCCGTCGCGCTCGCGGCCGCGACCGTGCTGCTGTGAGATGACCTACCACTGCTCCGATGGACGGCGAGACGGACGAGCACGCACGGGGAGTGCGGCGGGAGGGGTAGTCGAATGA","VTTSRCGPRPLPVAAAWPSPSGAARSCVSSRSGATACEMPSRPRRCARSTWRGRELTAPTSTPVMPDPSSRPTPSRCAAFPLGPRTMRRPARPPAPPAASTARSSPPPDCSPSRSRPRPCCCEMTYHCSDGRRDGRARTGSAAGGVVE$","Hypothetical protein","Extracellular, Cytoplasm","Immediate-early protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein (E0889)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1685","1825156","1823489","1668","5.40","-8.32","60551","ATGAAGCTCAACCGTCGCATGTTCCTCGCCACGACGGCCTCCGCGGCCGTCCTGACCGCCCTGGCGGCCTGCGCCAAGAACGGCTCCGGCTCCTCGGGCTCCACCGCCGGCGTGCCCACGGCCGCCCCCGACGAGCTCCAGGACGGGGGCACGCTGCGCTTCGGCATCGGCTCGGCGCCGGCGAACTGGAACGTCGCGACCGTCGACGGCAACGTCGTCGACACACGCCTGGTCATGAAGTTCGTCGCCCCCTACGTCGTCGACTGGGCCGAGGACGGCAAGGCGACGCCGAACCCCGACTTCCTCACCAAGCTCGAGGCCGCGGAGGTCAGTGACAAGACCGTGGTCACCGTGGCCGTTAACGAGAAGGCCACCTGGGGCAATGGGCGAAAGTGGGACTCCGAGGACATCAAGGCGTTCTTCGACCACGTCAAGGACTCCAGCTACTCCTGGGCCTCCGTCGAGGGGCTCGACAAGGTCGAGAAGGTCGAGATCGTGGACAAGCAGACCGCCAAGGTCACCTTCAACTCGGTCTACCCCGACTGGTCCTATGCCCTGTCCGGCATCACCCCCAGGGAGCTCATGGCCGACGCCAAGACCTTCAACGAGTCGATGGCCGGCGCCACCAAGTTCAACAACGACTACTTCGCCGGTCCCTTCAAGATCAAGAGCTACGACGAGTCCAAGCAGGTCATCACCCTGGAGCGCAACGACAAGTGGTGGGGCGCCACCCCCAAGCTCGAGACCGTCACCCTGCACGTCCTGGACGACTCGGCCATGGGACAGGCCTTCGCCAACAAGGAGATCGACGTCCTGGACTACATCTTCTCCGCCGACGTCTACCAGCAGGCCAGCGGCCGCGACGACGCCGAGGTCCGTCAGAACACCGGCCTGGAGTGGCGTCACATCATGTTCAACGCCTCCTCCGGCCCCCTGGCGGACAAGGCCGTGCGTCAGGCCATCACCCGGGCCTGCAACCGTGAGGCCATCGCCGCCTCCGACCTGGCGGGTCTGCCCGTGGACGCCAAGAAGACCCTCTTGGGCAACCGCTTCTTCCTGCCCGTGCAGGAGGGCTACCAGGACAACTCCACCAGCTGGGGCTACGACGTCGAGGCCGCCAAGAAGCTGCTCGACGGCGCCGGCTGGGTGGCCGGCTCCGACGGGGTCCGCGCCAAGGACGGTAAGAAGCTCGAGCTGGTGATGACCATCCCCAGCAACGCTCCTGTGGCCACCAACGAGGCCAACCTCCTCCAGAAGCAGCTGAACGAGGTCGGCATCAAGCTCAGTGTCTCCACGGTCGAGATCGACAAGTACTTCCCGGAGTACATCAACAAGAAGAACTACGCACTGACGGCCTTCACCTCCGAGAAGACCCAGTACCCCCTGTCCAACGCGGGCCAGTACTACGCCTCGACCAGCCAGTCGAACTACACCGGACTGTCCGTCCCCGAGGTCGACCAGTACGTCGCCAAGATCGGCTCGACCCCCGATGGTGCCGAGCGCAACAAGCTCGCCAACGAGCTCGACAAGGTCCTGTGGGAGAACGTCTTCAGCATCCCGATCTACCAGCGCATGCAGTTGACCGCCGTGCCCAAGACGCTGCGCAACTTCGGCGCCCAGGGACTGGCCTCCTTCCGGCCCGAGAGCATCGGCTACGTCAAGAGCTGA","MKLNRRMFLATTASAAVLTALAACAKNGSGSSGSTAGVPTAAPDELQDGGTLRFGIGSAPANWNVATVDGNVVDTRLVMKFVAPYVVDWAEDGKATPNPDFLTKLEAAEVSDKTVVTVAVNEKATWGNGRKWDSEDIKAFFDHVKDSSYSWASVEGLDKVEKVEIVDKQTAKVTFNSVYPDWSYALSGITPRELMADAKTFNESMAGATKFNNDYFAGPFKIKSYDESKQVITLERNDKWWGATPKLETVTLHVLDDSAMGQAFANKEIDVLDYIFSADVYQQASGRDDAEVRQNTGLEWRHIMFNASSGPLADKAVRQAITRACNREAIAASDLAGLPVDAKKTLLGNRFFLPVQEGYQDNSTSWGYDVEAAKKLLDGAGWVAGSDGVRAKDGKKLELVMTIPSNAPVATNEANLLQKQLNEVGIKLSVSTVEIDKYFPEYINKKNYALTAFTSEKTQYPLSNAGQYYASTSQSNYTGLSVPEVDQYVAKIGSTPDGAERNKLANELDKVLWENVFSIPIYQRMQLTAVPKTLRNFGAQGLASFRPESIGYVKS$","Peptide/nickel transport system periplasmic protein","Extracellular, Periplasm, Membrane","putative extracellular solute-binding dependenttransport lipoprotein","bacterial extracellular solute-binding protein; family protein 5","extracellular solute-binding protein, family 5","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670","","","

InterPro
IPR000914
Family

Bacterial extracellular solute-binding protein, family 5
PF00496	$\"[96-475]T$	SBP_bac_5

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[3-36]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.10.105.10	$\"[296-521]T$	no description
G3DSA:3.90.76.10	$\"[50-197]T$	no description
PS51257	$\"[1-24]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 18 clades of COG0747COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0747 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-42% similar to PDB:2NOO Crystal Structure of Mutant NikA (E_value = 3.4E_20);-41% similar to PDB:1XOC The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide. (E_value = 2.9E_19);-41% similar to PDB:1ZLQ Crystallographic and spectroscopic evidence for high affinity binding of Fe EDTA (H2O)- to the periplasmic nickel transporter NikA (E_value = 3.2E_18);-41% similar to PDB:1UIU Crystal structures of the liganded and unliganded nickel binding protein NikA from Escherichia coli (Nickel unliganded form) (E_value = 9.2E_18);-41% similar to PDB:1UIV Crystal structures of the liganded and unliganded nickel binding protein NikA from Escherichia coli (Nickel liganded form) (E_value = 9.2E_18);","Residues 96 to 475 (E_value = 9.4e-48) place ANA_1685 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 Middle.","","extracellular solute-binding dependent transport lipoprotein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1686","1827472","1825265","2208","5.45","-17.79","79375","ATGAGCCCCACGAGCAGCACCCGCACGTCCGCCGAGTCCACGAAGAGTGCCGCGGCCGTGCGCGCCGTCGATGCCCGCAGAGGCGACGACGCGCTGCCGGACCCCACCAGCACCGCCCCGCTGCTGGAGGTCTCCGACCTGAAGGTCTCCTTCCCCTCCGAGGACGGGCGCGTCAACGCCGTGCGCGGAGTCAACCTGTCCGTCGCCCGCGGTGAGGTGCTGGCCCTGGTCGGTGAGTCCGGCTCGGGCAAGTCCGTCACCTCGACGGCGGTCATGGGACTGCTCGACGAGTCCGCCGAAGTCACCGGCTCGGTGCGCCTCCACGGCACCGAGCTGCTGGGGCGGCCCGACGGCTACATGTCCCGCATCCGCGGCTCCCAGGTCGCCATGGTCTTCCAGGACCCGCTCAGCGCCCTGACCCCCGTGTACACGGTGGGCGCCCAGATCGTCGAGGCCCTGCGGATCCACCAGCCCGGCATGAGCGAGGCGGACGCCCACAAGCGCGCCGTCGAGCTGCTCGACCTGGTGGGCATCCCCAACCCGCAGGTGCGTGCCAAGGCCTACCCCCACGAGTTCTCCGGCGGCATGCGCCAGCGGGCCGTCATCGCCATCGCGATCGCCAACGACCCCGATCTCATCATCGCCGACGAGCCCACCACGGCCCTCGACGTCACCATCCAGGCCCAGATCCTTGACGTGCTGCGCACCGCCCAGAAGGAGACCGGTGCCGGCGTCATCATGATTACCCACGACCTGGGGGTCGTGGCCGGCATGGCCGACCGGGTGGCCGTCATGTACGCCGGGCGCATCGTGGAGACCGGCGACGTCGATGACATCTTCTACCGCTCGCGCATGCCCTACACGATCGGCCTGCTCGGCTCCCTGCCCCGTCTGGACGCGCGCAAGGACTCGGCCCTGGCCACCCTGGAGGGCAACCCGCCCTCCCTGCTCGAGCTGCCCCGAGGGTGCCCCTTCATCCCCCGCTGCCCCATGGCCCAGGCCGAGTGCGCCCAGGGGGAGCCGGAGCTCACCCTCGTGGAGCGCGAGGGGACCGACGGCCAGGAGGCCGGCTCCGGCGCCCAGTACTCGGCCTGCCACCGCCGCGACGAGATCGAGCGGGACCAGCTCGACTACTCCCACATCTACCCCGTGCCGGCACTCAAGACTCCCGAGACCATGAGCCTGCCGCACGCCGAGCGTCCCGAGGTCCTGCGCGTCACCGACCTCGTCAAGGAGTTCCCCCTCATGAAGGGCGCCGTCTTCAAAAGACGCGTGGGCACCGTCCACGCCGTCGACGGCGTCTCCTTCGACGTCCGCCGGGGCGAGACCCTGGCCCTGGTCGGCGAGTCCGGATGCGGCAAGACCACCACCCTCATGGAGGTCCTCTCCCTCCAGGCGCCCCAGGAGGGCACGATCGTGGTCCTGGGCAAGGACACGGCCGACCTGGGGCGGGCCCAGCGTCGCCAGGTGCGCCGCGACCTGCAGATCGTCTTCCAGGACCCCATGGCCTCCCTGGACCCGCGCCTGCCGATCTTCGACATCATCGCCGAGCCGCTGCGGGCCAACGGTTGGAAGAAGACGGACATCGGGCCGCGCATCGAGGAGCTCATGGAGCTCGTCGGGCTCGAGCCCAGCCACGCCAACCGCTACCCGCGCAACTTCTCCGGCGGGCAGCGCCAGCGCATCGGCATCGCCCGCGCCCTGGCCCTCGAACCCAGCCTCCTGGTCCTCGACGAGCCGGTCTCCGCCCTGGACGTGTCCATCCAGGCCGGCGTCATCAACCTGCTTGACGAGCTGCGCGCCACCATGGGCCTCAGCTACCTCTTCGTGGCCCACGACTTGTCAGTGGTGCGTCACATCGCCGACCGCGTCGCCGTCATGTACCTGGGGCGGATCGTGGAGATCGGCGACGTCGACACCATCTTCGAGGCCCCGGCCCATCCCTACACCCAGGCTCTGCTCTCGGCGATCCCCATCCCGGACCCGGCCAAGGAGCGCGGTCGCAGCCGCATCGTCCTGGAGGGCGACATGCCCAGCCCCGCCAACCCGCCCTCGGGTTGCCGCTTCCGCACGCGCTGCCCGAAGTTCGCCTCAGGACTCACTGACGACGAGCGCTCGGCCTGCCTGGGGGCCATGCCGGAGTTCCGCTCCCAGGGCGAGGACCACGACGTCGCCTGCTACTACCCCGAGCGCACCGCGGTCTTCTGA","MSPTSSTRTSAESTKSAAAVRAVDARRGDDALPDPTSTAPLLEVSDLKVSFPSEDGRVNAVRGVNLSVARGEVLALVGESGSGKSVTSTAVMGLLDESAEVTGSVRLHGTELLGRPDGYMSRIRGSQVAMVFQDPLSALTPVYTVGAQIVEALRIHQPGMSEADAHKRAVELLDLVGIPNPQVRAKAYPHEFSGGMRQRAVIAIAIANDPDLIIADEPTTALDVTIQAQILDVLRTAQKETGAGVIMITHDLGVVAGMADRVAVMYAGRIVETGDVDDIFYRSRMPYTIGLLGSLPRLDARKDSALATLEGNPPSLLELPRGCPFIPRCPMAQAECAQGEPELTLVEREGTDGQEAGSGAQYSACHRRDEIERDQLDYSHIYPVPALKTPETMSLPHAERPEVLRVTDLVKEFPLMKGAVFKRRVGTVHAVDGVSFDVRRGETLALVGESGCGKTTTLMEVLSLQAPQEGTIVVLGKDTADLGRAQRRQVRRDLQIVFQDPMASLDPRLPIFDIIAEPLRANGWKKTDIGPRIEELMELVGLEPSHANRYPRNFSGGQRQRIGIARALALEPSLLVLDEPVSALDVSIQAGVINLLDELRATMGLSYLFVAHDLSVVRHIADRVAVMYLGRIVEIGDVDTIFEAPAHPYTQALLSAIPIPDPAKERGRSRIVLEGDMPSPANPPSGCRFRTRCPKFASGLTDDERSACLGAMPEFRSQGEDHDVACYYPERTAVF$","Peptide/nickel transport system ATP-binding protein","Cytoplasm, Membrane, Extracellular","dipeptide ABC transporter ATP-binding","K02031 peptide/nickel transport system ATP-binding protein","oligopeptide/dipeptide ABC transporter, ATPase subunit","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[191-234]T$ $\"[554-596]T$	Q82IT8_STRAW_Q82IT8;
PF00005	$\"[71-268]T$ $\"[441-630]T$	ABC_tran
PS50893	$\"[42-292]T$ $\"[404-654]T$	ABC_TRANSPORTER_2
PS00211	$\"[192-206]?$ $\"[554-568]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[70-269]T$ $\"[440-639]T$	AAA

InterPro
IPR010066
Domain

Oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal
TIGR01727	$\"[269-367]T$ $\"[631-728]T$	oligo_HPY: oligopeptide/dipeptide ABC trans

InterPro
IPR013563
Domain

Oligopeptide/dipeptide ABC transporter, C-terminal
PF08352	$\"[271-336]T$ $\"[633-708]T$	oligo_HPY

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[36-301]T$ $\"[398-663]T$	no description
PTHR19222	$\"[404-732]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28	$\"[404-732]T$	OLIGOPEPTIDE ABC TRANSPORTER

","BeTs to 5 clades of COG1123COG name: ATPase components of various ABC-type transport systems, contain duplicated ATPaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1123 is -omp------r--cefg---uj----Number of proteins in this genome belonging to this COG is 3","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.1e-90. IPB013563A 60-94 IPB013563B 128-141 IPB013563C 189-216 IPB013563D 606-658***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.9e-24. IPB005074C 430-477 IPB005074D 542-585 IPB005074C 60-107 IPB005074D 180-223***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.7e-13. IPB010509B 441-466 IPB010509D 549-593 IPB010509B 71-96***** IPB005116 (TOBE domain) with a combined E-value of 2.2e-13. IPB005116A 448-464 IPB005116C 554-567 IPB005116D 574-593 IPB005116A 78-94 IPB005116C 192-205 IPB005116D 212-231 IPB005116E 246-259***** IPB010929 (CDR ABC transporter) with a combined E-value of 4.9e-07. IPB010929K 428-472 IPB010929M 551-597 IPB010929C 536-569","","","-57% similar to PDB:1G29 MALK (E_value = 1.1E_34);-56% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 1.1E_34);-56% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 1.9E_34);-56% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 2.4E_32);-56% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 2.4E_32);","Residues 71 to 268 (E_value = 3e-56) place ANA_1686 in the ABC_tran family which is described as ABC transporter.Residues 271 to 336 (E_value = 1.6e-26) place ANA_1686 in the oligo_HPY family which is described as Oligopeptide/dipeptide transporter, C-terminal region.Residues 441 to 630 (E_value = 2.9e-58) place ANA_1686 in the ABC_tran family which is described as ABC transporter.Residues 633 to 708 (E_value = 3.9e-33) place ANA_1686 in the oligo_HPY family which is described as Oligopeptide/dipeptide transporter, C-terminal region.","","ABC transporter ATP-binding (D90720)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1687","1828482","1827469","1014","9.38","5.64","36100","ATGGCGCGCAATGCTGAACCCAACGGTATGGCCTCCATCGGCAAGCAGATGACGGTGGGTGGCTACGCCCCCGTCGAGCAGGGCGGGGAGGCCCCACTGAGCCCCGAGGACCTGGGCGACATCACCAAGGAGACCCCCAGGGACTCCCGGCGTCTGACCCGCAGGCAGATCATCACCCGGCGCTTCTGGCGCAACAAGGGGGCCGTCGTCGGAGCGATCGGCTTCCTGCTCATGGTGCTCTTCGCTCTCTTCGGGGGCCTCCTGACCCACTGGACCTTCACCGACGTCGACTCCTCCGCCTTCCTGCAGGCCCCCAGCGCTGATCACTGGTTCGGCACCACCCAGGGCGGCCGCGACGTCTACGCGATGGTCGTGGAGGGCACCCGCAAGTCCATGATGATCGGCGTCTTCGTCGCCCTGCTCCAGACGGGCATCGCCGCCGTCATCGGATCCTCGGCCGCCTACTTCGGCGGCTGGTGGGAGAAGATCGCCCTGTGGGCCACCGACCTGCTCCTGGTGGTGCCCTCCTTCCTCATCATCGCGATCCTCTCCCAGCGGGCCGGAGCCGCCAAGGGCTCCATCGTGCTGTTCATCATCCTCCTGGCCGGATTCGGGTGGATGCTCACGGCCCGCGTGGTGCGCTCCCTGACCCTGAGCGTGAAGAACCTGGAGTACGTCAATGCCGCCCGCTTCATGAACGTGCCCAGTCCCGTCATCATCGCCCGGCACATCCTGCCCAATATCGCCTCCCTGCTCATCGTGGACGCCACCATCAACGTGGCCTACGCCGTCATCAGCGAGACGACGCTGTCCTACTTCGGTTTCGGGGTCCAGTCGCCCAACACCTCCCTGGGCACCCTCATTGCCGAGGGGCAGCGCTCCGCGACCACCTACCCCTGGATCTTCCTGGCCCCGGCCGCCGTGCTCGTCCTCATGCTCCTGTGCGTCAACGTCATGGGTGACGGTCTGCGCGATGCCATCGATCCCTCGTCCAAGTCAGGAGGCAAGGCATGA","MARNAEPNGMASIGKQMTVGGYAPVEQGGEAPLSPEDLGDITKETPRDSRRLTRRQIITRRFWRNKGAVVGAIGFLLMVLFALFGGLLTHWTFTDVDSSAFLQAPSADHWFGTTQGGRDVYAMVVEGTRKSMMIGVFVALLQTGIAAVIGSSAAYFGGWWEKIALWATDLLLVVPSFLIIAILSQRAGAAKGSIVLFIILLAGFGWMLTARVVRSLTLSVKNLEYVNAARFMNVPSPVIIARHILPNIASLLIVDATINVAYAVISETTLSYFGFGVQSPNTSLGTLIAEGQRSATTYPWIFLAPAAVLVLMLLCVNVMGDGLRDAIDPSSKSGGKA$","Peptide/nickel transport system permease protein","Membrane, Cytoplasm","EppC","K02034 peptide/nickel transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[128-333]T$	BPD_transp_1
PS50928	$\"[132-320]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-89]?$	signal-peptide
tmhmm	$\"[68-88]?$ $\"[133-153]?$ $\"[163-183]?$ $\"[189-209]?$ $\"[300-320]?$	transmembrane_regions

","BeTs to 20 clades of COG1173COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1173 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-54% similar to PDB:2GKS Crystal Structure of the Bi-functional ATP Sulfurylase-APS Kinase from Aquifex aeolicus, a Chemolithotrophic Thermophile (E_value = );","Residues 128 to 333 (E_value = 3.8e-35) place ANA_1687 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","(AA1) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1688","1829445","1828486","960","9.93","11.35","34942","ATGCTCCCGTACCTGGCGCGCCGGATCGCGAACTACGCGGTCCTGCTGTTCATCGCCACGTCGTTGGCCTATCTGCTGGCCTCGGCCTCCCTGGATCCCTCGGCCCTGTGGAACCGTCAGGATCCCTCCCTCAACTGGGACGCCATTCACGCCAACCTCGTGAAGTACAACATCAGTCATGACCTGCCCGTGTGGGACCGCTACGTCACCTGGCTGCGCAACGTGCTCTTCCACTGGGACTGGGGGCGCACCCCCAAGGGCGAGCTCATCAACACCCTCATCGGCACCAAGATCTTCGTCTCGGTGCGGCTGGTCTTCCTGGGTGCAGCCATCGGCATGGTCGGGGGAGTGGCCCTGGGGGCCTGGACCGCCACGCGCCAGTACCGCTTCTCCGACCGCGCGATCTCCCTGATCTCCATGATTATCATCTCCACCCCCGCCATGGTCATCGCGATCCTCCTGCAGGTCCTGGCCGTCCAGATCAACCGCAGCTCCGGCTTCCAGATCTTCGAGTTCACCGGTGAGGGGGAGGGCGCCCTCGGTCGCCTCCAGCACCTGCTGCTTCCCACCCTGTCGATGTCGCTGGGCGGTATCGCCTCCTACTCCCGCTTCCAGCGCAACCTCATGCTCGACACCCTGGGCGCCGACTACGTGCGCACCGCCCGCGCCAAGGGCCTCATCAAGCGCAAGGCGCTGACCCGCCACGCGCTGCGCACCGCGCTCATCCCCATGGCCACCTACTTCGCCTTCGCCCTGGCCACCCTGTTCACCGGTGCCGCCATCACCGAGCGGGTCTACGGCTGGCACGGCATGGGCGAGTACTCCATCAGTGCGATCGCCGGTATGGACATCAACGGGGTGACGGCCGTGGTCGCCTTCTCCGGGCTGTGCACCCTCACCGGTGCGCTCCTGTCCGATGTCTTCGTGGCGATCGTCGACCCGAGAGTGAGGGTGAGCTGA","MLPYLARRIANYAVLLFIATSLAYLLASASLDPSALWNRQDPSLNWDAIHANLVKYNISHDLPVWDRYVTWLRNVLFHWDWGRTPKGELINTLIGTKIFVSVRLVFLGAAIGMVGGVALGAWTATRQYRFSDRAISLISMIIISTPAMVIAILLQVLAVQINRSSGFQIFEFTGEGEGALGRLQHLLLPTLSMSLGGIASYSRFQRNLMLDTLGADYVRTARAKGLIKRKALTRHALRTALIPMATYFAFALATLFTGAAITERVYGWHGMGEYSISAIAGMDINGVTAVVAFSGLCTLTGALLSDVFVAIVDPRVRVS$","Peptide/nickel transport system permease protein","Membrane, Cytoplasm, Extracellular","ABC transport protein inner membrane component","K02033 peptide/nickel transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[98-318]T$	BPD_transp_1
PS50928	$\"[98-309]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[9-29]?$ $\"[99-119]?$ $\"[134-154]?$ $\"[186-204]?$ $\"[240-262]?$ $\"[290-312]?$	transmembrane_regions

","BeTs to 20 clades of COG0601COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0601 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-53% similar to PDB:1RZT Crystal structure of DNA polymerase lambda complexed with a two nucleotide gap DNA molecule (E_value = );-53% similar to PDB:1XSL Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap (E_value = );-53% similar to PDB:1XSN Crystal Structure of human DNA polymerase lambda in complex with a one nucleotide DNA gap and ddTTP (E_value = );-53% similar to PDB:1XSP Crystal Structure of human DNA polymerase lambda in complex with nicked DNA and pyrophosphate (E_value = );-53% similar to PDB:2BCQ DNA polymerase lambda in complex with a DNA duplex containing an unpaired Dtmp (E_value = );","Residues 98 to 318 (E_value = 8.4e-40) place ANA_1688 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transport protein inner membrane component (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1689","1831582","1829681","1902","6.66","-3.88","67734","GTGACACCCTCCAACGCATCCACCGCCACCGCATCAGGTGCCTCCGACAAGATCTTCGCCCCCGCGGCCTCCTGGAAGGCCGAGAGCGACCCCCTCCTGGAGATCAGCGACCTGGAGGTCGCCTTCCGCTCCTCGACCGGGCTCGTCCCAGCCGTGCGCAAGGCGAACCTGACCCTCTACCCCGGCCAGTCGGTCGCCATCGTGGGGGAGTCGGGCTCGGGCAAGTCCACCCTGGCCCACGCCGTCATCGGGCTGCTGCCCGGAACCGGCCGGGTCACCGGCGGCACGATCCGCTTCCAGGGCCGCGACATCACCCACCTGGGCACCCAGGAGCTCACCGCCCTGCGCGGCTCCTCCATCGGCCTGGTGCCCCAGGACCCCATGTCCAACCTCAACCCCGTGTGGTCCATCGGCTTCCAGGTCAAGGAGGCGCTGCGGGCCAACGGCCTGGCCGGCGTCGCCGACGACCGCCTCGCCCACCTCATGGCCGAACATGCCGGGCACGCCGGACACACCGGGCACGCGGGGCGCACTGGGCACGCCGACCGCGCCCAGAAGGCGGCCCCCTCGGCCGGCGGGCGCATCGACGTCGACGAGCAGGTGGCCCTCCTGCTGGAGCAGGCCGGCCTGCCCGAGGCCTCCCGGCGGGCCAAGCAGTACCCCCACGAGTTCTCCGGCGGCATGCGCCAGCGCGCCCTCATCGCCATCGGCCTGGCTGCCCGCCCCGACCTGCTCATCGCCGATGAGCCCACCAGCGCCCTGGACGTCACCGTCCAGCGACGTATCCTCGACCACCTCCAGACCCTCGTGCGCGAGCTGGGCACCGCGATGCTCTTCATCACCCACGACCTGGGGCTGGCCGCTGAGAGGGCCGAGCACATCGTCGTCATGCACCGCGGCCGGGTCGTCGAGTCCGGCCCCAGCCTCGAGGTGCTCCAGGACCCCCGCCACCCATACACCCAGCGCCTGGTCAAGGCCGCCCCCTCCCTGGCCTCCCGGCGCATCGAGTCCGCCCACGCCCGCGGCATCCAGGTCACCGACGACGAGCTCCTGGGCGCCAGCCTGGGATCGAGCGCCACAGAGGAGATCCTGCGCGTGGAGCACCTCACCAAGGTCTTCGAGGTGCGCGGCGCCAAGGGCAAGGACAAGACCCTCACCGCCGTCGACGACGTCAGCTTCGGTATCCGCAAGGGCACGACGACGGCGCTCGTCGGCGAGTCCGGCTCCGGCAAGTCCACGGTCGCCAACATCATCCTGAACCTCATCGACCCCACCTCCGGCAAGGTGTTCCACGACGGGGCGGACCTGTCCACCCTGGGGCCCAAGGAGCTCTTCGCCCTGCGGCGCATCATGCAGCCGGTCTTCCAGAACCCCTACGGCTCCCTGGACCCGATGTACTCGATCTTCCGCGTCGTCGAGGAGCCGCTGCGGGTCCACGGGATCGGCACGGCCAAGGAGCGCGAGGCGCGCGTCGCCGAGCTGCTCGACATGGTCTCCCTGCCGCGCTCGGTCATGCGCCGCTACCCCCACGAGCTCTCCGGCGGTCAGCGCCAGCGCGTCGCCATCGCCCGCGCCCTGGCCCTCAAGCCGCAGATCGTCGTCCTCGACGAGGCGGTCTCCGCCCTGGACGTGCTGGTCCAGGCCCAGATCCTGCGTCTGCTGTCCGACCTGCAGGCCGAGCTGGAGCTGACCTATCTGTTCATCACCCATGATCTGGCCGTCGTGCGCCAGATCGCCGACGACGTCGTCGTCATGGAGCACGGGCGCATCGTGGAGTCCGGGGCGGCCGACGAGCTCTTCGCCAACCCGCGCCAGGACTACACCCGCGAGCTCATCCGGGCCGTCCCCGGAGCCGGCATCGACCTCTACGGCGATGAGGCTCCCTCGAGGTCCGAGAGCTGA","VTPSNASTATASGASDKIFAPAASWKAESDPLLEISDLEVAFRSSTGLVPAVRKANLTLYPGQSVAIVGESGSGKSTLAHAVIGLLPGTGRVTGGTIRFQGRDITHLGTQELTALRGSSIGLVPQDPMSNLNPVWSIGFQVKEALRANGLAGVADDRLAHLMAEHAGHAGHTGHAGRTGHADRAQKAAPSAGGRIDVDEQVALLLEQAGLPEASRRAKQYPHEFSGGMRQRALIAIGLAARPDLLIADEPTSALDVTVQRRILDHLQTLVRELGTAMLFITHDLGLAAERAEHIVVMHRGRVVESGPSLEVLQDPRHPYTQRLVKAAPSLASRRIESAHARGIQVTDDELLGASLGSSATEEILRVEHLTKVFEVRGAKGKDKTLTAVDDVSFGIRKGTTTALVGESGSGKSTVANIILNLIDPTSGKVFHDGADLSTLGPKELFALRRIMQPVFQNPYGSLDPMYSIFRVVEEPLRVHGIGTAKEREARVAELLDMVSLPRSVMRRYPHELSGGQRQRVAIARALALKPQIVVLDEAVSALDVLVQAQILRLLSDLQAELELTYLFITHDLAVVRQIADDVVVMEHGRIVESGAADELFANPRQDYTRELIRAVPGAGIDLYGDEAPSRSES$","Peptide/nickel transport system ATP-binding protein","Cytoplasm, Membrane","ABC-type transporter, duplicated ATPasecomponent","K02031 peptide/nickel transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[223-266]T$ $\"[511-554]T$	Q8G4J2_BIFLO_Q8G4J2;
PF00005	$\"[62-300]T$ $\"[398-588]T$	ABC_tran
PS50893	$\"[33-324]T$ $\"[364-612]T$	ABC_TRANSPORTER_2
PS00211	$\"[224-238]?$ $\"[512-526]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[61-301]T$ $\"[397-589]T$	AAA

InterPro
IPR013563
Domain

Oligopeptide/dipeptide ABC transporter, C-terminal
PF08352	$\"[303-348]T$ $\"[591-616]T$	oligo_HPY

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[27-333]T$ $\"[358-621]T$	no description
PTHR19222	$\"[364-621]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28	$\"[364-621]T$	OLIGOPEPTIDE ABC TRANSPORTER

","BeTs to 9 clades of COG1123COG name: ATPase components of various ABC-type transport systems, contain duplicated ATPaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1123 is -omp------r--cefg---uj----Number of proteins in this genome belonging to this COG is 3","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 7.7e-75. IPB013563A 387-421 IPB013563B 451-464 IPB013563C 509-536 IPB013563D 564-616 IPB013563B 120-133***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 5.8e-31. IPB005074C 387-434 IPB005074D 500-543 IPB005074C 51-98 IPB005074D 212-255***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 4.6e-23. IPB010509B 62-87 IPB010509D 507-551 IPB010509B 398-423***** IPB005116 (TOBE domain) with a combined E-value of 2.7e-18. IPB005116A 405-421 IPB005116C 512-525 IPB005116D 532-551***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.2e-09. IPB010929K 385-429 IPB010929M 509-555 IPB010929M 221-267","","","-55% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 2.2E_31);-55% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 7.9E_29);-55% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 7.9E_29);-54% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 5.1E_28);-56% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 1.9E_27);","Residues 62 to 300 (E_value = 1.7e-54) place ANA_1689 in the ABC_tran family which is described as ABC transporter.Residues 303 to 348 (E_value = 2.1e-05) place ANA_1689 in the oligo_HPY family which is described as Oligopeptide/dipeptide transporter, C-terminal region.Residues 398 to 588 (E_value = 5.2e-62) place ANA_1689 in the ABC_tran family which is described as ABC transporter.Residues 591 to 616 (E_value = 5.4e-07) place ANA_1689 in the oligo_HPY family which is described as Oligopeptide/dipeptide transporter, C-terminal region.","","transporter, duplicated ATPase component (D90720)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1690","1832538","1831579","960","6.94","-0.14","33772","ATGCCTGAGAACACCACGTCCCCCACTACCCGTCCGGGCCAGGAACGCTTCGTCATCGCCGACGACGAGATCGGCCTGGGTGCCGTCGACGCCGTCGCCGACGAGTCCGCCCCGGCCTCCGTCTGGGTCGACGCCTGGAGGCAGCTGCGCCGTCGGCCCATCTTCTGGGCGGCCTCGGTGCTCATCGCCGTGGCCGTGGCCTTCTCCCTGGTTCCCGGGCTCATCGCCCCGCGCGACCCCGGCTACTGCACGCTGGTCAACTCCTACCAGGGGCCCTCCTGGGGCCATCCCTTCGGATTCGACATCCAGGGCTGCGACATCTTCGCCCGCACCGTCCACGGCGCCCGGGCCTCGGTGAGCGTGGGCATCTTCACCACCCTCGTCGTGGTCCTCGTGGGCTCGGCCGTCGGGGCCCTGGCCGGATTCTTCGGCGGGTTCTTCGACGCGCTACTCTCGCGCGTCACCGACATCTTCTTCGCCGTGCCCTTCGTCCTGGCGGCCATCGTCGTCATGCAGATGTTCCGCAACGACCGCTCGATCCTCACCGTCATCCTGGTCCTGGCCCTGTTCGGCTGGCCCCAGATCGCCCGCATCACGCGAGGCTCGGTCATGAGCGTCAAAAACGAGGACTACGTGACCGCCTCACGGGCGCTGGGCTCGGGACGCATGGCCATGCTGCTGCGCCACGTCATGCCCAACGCGGCCGCCCCCATCATCGTGACCGCCACCGTCGAGCTCGGCGTCTTCATCGTCTCGGAAGCTACCTTGAGCTTCCTGGGCATCGGGCTGCCTTCCTCGGTCGTCTCCTGGGGTGCGGACATCGCGGCCGCCAAGGACGCCCTCAACAGCCACCCCAGCGTCCTGCTCTTCCCCTCCGGCGCACTGGCCCTGACCGTGCTCGGCTTCATCATGCTCGGCGACGTCGTCCGCGACGCCCTGGACCCGAAGGCCCGCAAGTGA","MPENTTSPTTRPGQERFVIADDEIGLGAVDAVADESAPASVWVDAWRQLRRRPIFWAASVLIAVAVAFSLVPGLIAPRDPGYCTLVNSYQGPSWGHPFGFDIQGCDIFARTVHGARASVSVGIFTTLVVVLVGSAVGALAGFFGGFFDALLSRVTDIFFAVPFVLAAIVVMQMFRNDRSILTVILVLALFGWPQIARITRGSVMSVKNEDYVTASRALGSGRMAMLLRHVMPNAAAPIIVTATVELGVFIVSEATLSFLGIGLPSSVVSWGADIAAAKDALNSHPSVLLFPSGALALTVLGFIMLGDVVRDALDPKARK$","Peptide/nickel transport system permease protein","Membrane, Cytoplasm, Extracellular","ABC-type transporter, permease components","K02034 peptide/nickel transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[115-319]T$	BPD_transp_1
PS50928	$\"[115-306]T$	ABC_TM1

noIPR
unintegrated

unintegrated
tmhmm	$\"[54-76]?$ $\"[127-147]?$ $\"[149-171]?$ $\"[177-195]?$ $\"[232-252]?$ $\"[258-276]?$ $\"[286-306]?$	transmembrane_regions

","BeTs to 20 clades of COG1173COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1173 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 115 to 319 (E_value = 1.6e-41) place ANA_1690 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter, permease components (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1691","1833460","1832531","930","9.49","5.66","33135","ATGCTTCGCTACGTCGCACGCAGGCTGCTGCAGATGGTCCCGGTGTTCTTCGGTGCCACGCTGCTCATCTACGCCATGGTCTTCGCCCTGCCGGGCGACCCGATCGCCGCGCTCGGGGGCCAGCGCTCGCTCAGCCCCGAGGTGATCGACCAGATCAAGGCCAGCTACCACCTCGACAAGCCCTTCATCGTCCAGTACCTGCTCTACCTCAAGGGACTGTTCACCCTGGACCTGGGCCAGTCGCTGCGGGGGACCGAGTCCGTCCTCGACGTGCTGGTGCGGGCCTACCCGATCACCATCAAGCTCTCCCTCATGGCCCTGGCCTTCGAGGCCATCGCGGGCATCGGCTTCGGCCTCATCGCCGGGCTGAGGAAGGGCGGCTGGTTCGACGCCACCGTCCTGGTGCTCTCCCTGGTGGTCATCGCCGTGCCCACCTTCGTCATCGGCTTCGTCCTGCAGTTCATCGTCGGGGTGCGGCTGGGCTGGCTGCCCGTGACCGCCGGTGAGAGCCCCGGTTTCACCGAGCTCCTCATGCCCGCGGTCGTGCTGGGCGCCGTCTCCTTCGCCTACGTGCTGCGCCTGACCCGCACCGAGGTGGCCGAGAACCTCACCGCCGACCACGTGCGCACCGCCCGAGCCAAGGGCCTGAGCGGGGTCCGCGTCATGATCGTCCACGTCCTGCGCAACTCCCTGGTCCCGGTCGTCACCTTCCTGGGCGCGGACCTGGGGGCCCTCATGGGAGGCGCCATCGTCACCGAGGGCATCTTCAACATCAAGGGAGTGGGAGGCACCCTCTACTCCGCCATCATCCGCGGTGACGGCCCCATGGTCGTGTCCTTCACGACCGTGCTCGTGCTCGTCTTCATCGTCTCCAACCTCCTGGTGGACCTGCTCTACGCCGCCCTGGACCCGAGGATCCGCTATGCCTGA","MLRYVARRLLQMVPVFFGATLLIYAMVFALPGDPIAALGGQRSLSPEVIDQIKASYHLDKPFIVQYLLYLKGLFTLDLGQSLRGTESVLDVLVRAYPITIKLSLMALAFEAIAGIGFGLIAGLRKGGWFDATVLVLSLVVIAVPTFVIGFVLQFIVGVRLGWLPVTAGESPGFTELLMPAVVLGAVSFAYVLRLTRTEVAENLTADHVRTARAKGLSGVRVMIVHVLRNSLVPVVTFLGADLGALMGGAIVTEGIFNIKGVGGTLYSAIIRGDGPMVVSFTTVLVLVFIVSNLLVDLLYAALDPRIRYA$","Peptide/nickel transport system permease protein","Membrane, Cytoplasm","ABC-type transporter, permease components","K02033 peptide/nickel transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[96-308]T$	BPD_transp_1
PS50928	$\"[96-299]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[103-123]?$ $\"[133-153]?$ $\"[172-192]?$ $\"[231-251]?$ $\"[282-302]?$	transmembrane_regions

InterPro
IPR000914
Family

Bacterial extracellular solute-binding protein, family 5
PF00496	$\"[247-535]T$	SBP_bac_5

noIPR
unintegrated

unintegrated
G3DSA:3.10.105.10	$\"[44-171]T$ $\"[476-535]T$	no description
G3DSA:3.90.76.10	$\"[205-360]T$	no description
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[12-32]?$	transmembrane_regions

","BeTs to 18 clades of COG0747COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0747 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-48% similar to PDB:1B05 Structure of oligo-peptide binding protein complexed with LYS-CYS-LYS (E_value = 5.5E_15);-48% similar to PDB:1B0H OLIGO-PEPTIDE BINDING PROTEIN COMPLEXED WITH LYSYL-NAPTHYLALANYL-LYSINE (E_value = 5.5E_15);-48% similar to PDB:1B1H OLIGO-PEPTIDE BINDING PROTEIN/TRIPEPTIDE (LYS HPE LYS) COMPLEX (E_value = 5.5E_15);-48% similar to PDB:1B2H Oligo-Peptide Binding Protein Complexed with Lysyl-Ornithyl-Lysine (E_value = 5.5E_15);-48% similar to PDB:1B32 OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KMK (E_value = 5.5E_15);","Residues 247 to 540 (E_value = 2.9e-22) place ANA_1692 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 Middle.","","transporter, periplasmic component","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1693","1836383","1835268","1116","5.44","-8.34","39176","ATGAGTCAGCCCGAAAGGCGGGCCGTACCCGTCCTGTCCGTCATGGACATGGTCCCCGTCAGCGCCGGATGCAGCCGCACCGACGCCCTCACCGACATGATCGCCCTGGCTCGAGCCGCCGACGCCGCCGGCTATGAGCGCTACTGGTTGGCCGAGCACCACGGCTCCACCACCTACCTGTCCTCGGCGACCATCGTCCTCATGGGGCAGGTCCTGGCCGCCACCGAGCGCCTGGGTGTCGCCTCCGGCGGGATCATGCTGCCCAACCACGCCCCGCTCGTTGTCGCCGAGCAGATCGGAACCCTGGCCACCCTCTACCCCGGCCGGGTTGATCTGGGACTGGGGCGGGCCCCGGGCACCGACCGGCGCACGGCCGCTGCACTGCGCCGGCGGGCCTCCGAACCGGGTCGTTTCGCCGAGGAGATCCTGGAGATCCTCGCCTACCTCGGTGACGAGCCCGTGCCAGAACGGGTCCCCGGCTCCCTCCTCCTGGGCGCCCCCGGCAATCCCGACGACGACCTCCACGCCCCTGAGCCCGGCGGCCCCCGCGTGCGGGCCATCCCCGGGGAGGGCACCCACCCGACCGTGTGGGTGCTCGGCTCCTCGGTCAACGGCGCCCGCGTGGCCGGCCGGCTCGGACTTCCCTTCGCCGTGGCCTCGCACTTCGCCCCGGTCCAGGCCGAGGCGGCGATCGCCACCTACCGCTCCGTCCTGGAGTCCCGTACCGAAGACGCTCCCGGCCCTCAGTACGCGCCGGATGTCCCCCGGGTCGCAGCCGCCGTCAACGTCATGGTGGCCCCCAGCCAGGAGGAGGCCCGCCTGCTGTTCAGCACCGCCATGGCCGCCGCTGCCCGCATCGTCGGCAACCGGCCCGGGCCGCTGGACCCGCCCAGCCAGGACCCCGAGGCCTGGCGCGCCTACGCGCCCGGCCGGGAGGGGGCCGTCGAGGCGGCCATGTCCCTGTCCTTCGTGGGCACGGCCGACGACGTCGCCGCCCGCCTGCGTGAGCAGGCCGCCCGTTGGGACCTCGACGAGATCCTCGTGGTCACCTACGCCCACGACCCGGCCCTGCGGCGCCGCTCCTACGAGCTGCTCGCCCAGGCCTGGAACGCCTGA","MSQPERRAVPVLSVMDMVPVSAGCSRTDALTDMIALARAADAAGYERYWLAEHHGSTTYLSSATIVLMGQVLAATERLGVASGGIMLPNHAPLVVAEQIGTLATLYPGRVDLGLGRAPGTDRRTAAALRRRASEPGRFAEEILEILAYLGDEPVPERVPGSLLLGAPGNPDDDLHAPEPGGPRVRAIPGEGTHPTVWVLGSSVNGARVAGRLGLPFAVASHFAPVQAEAAIATYRSVLESRTEDAPGPQYAPDVPRVAAAVNVMVAPSQEEARLLFSTAMAAAARIVGNRPGPLDPPSQDPEAWRAYAPGREGAVEAAMSLSFVGTADDVAARLREQAARWDLDEILVVTYAHDPALRRRSYELLAQAWNA$","Peptide/nickel transport system permease protein","Cytoplasm","flavin dependant oxidoreductase","putative monooxygenase ","luciferase family protein","","Fisher A.J., Thompson T.B., Thoden J.B., Baldwin T.O., Rayment I. The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 1996. 271(36):21956-21968. PMID: 8703001Moore S.A., James M.N. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 1995. 249(1):195-214. PMID: 7776372Eichhorn E., Davey C.A., Sargent D.F., Leisinger T., Richmond T.J. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J. Mol. Biol. 2002. 324(3):457-468. PMID: 12445781Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J. Mol. Biol. 2000. 300(4):935-950. PMID: 10891279","","","

InterPro
IPR011251
Family

Bacterial luciferase-like
G3DSA:3.20.20.30	$\"[12-367]T$	no description
PF00296	$\"[13-369]T$	Bac_luciferase

InterPro
IPR003784
Family

BioY protein
PF02632	$\"[44-195]T$	BioY

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[26-44]?$ $\"[48-68]?$ $\"[73-91]?$ $\"[97-115]?$ $\"[135-153]?$ $\"[159-179]?$	transmembrane_regions

","BeTs to 9 clades of COG1268COG name: Uncharacterized ACRFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1268 is aom-k---vd-lbc-------jxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003784 (BioY protein) with a combined E-value of 7.3e-14. IPB003784 64-114 IPB003784 65-115 IPB003784 131-181","","","No significant hits to the PDB database (E-value < E-10).","Residues 44 to 195 (E_value = 7.6e-11) place ANA_1694 in the BioY family which is described as BioY family.","","involved in biotin metabolism homolog lin0607 (BioY)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1695","1838242","1837217","1026","7.36","1.75","36238","ATGCAGACCAGCCTTACTCGGCTCACGGCCGACGACGGAACGCGTCTGGTCGTGCACATCTGGCTCCCCGAGTGGCTCATCGACGGCTCCCTCCTGGTGGCCGACGTCCCCGAGGCCGACTCCCCAGCGCCCACCTCGGCTGCGACGCGCCCACAGGTACCCGGCGCCGCCCGCCCCCGGGGCATCATCGTCATCGCCCACGGCATGGCCGAGCACGCCTCGCGCTACGCCCGCTTCGCCGCCTCCGCTGTGGAGGAGGGCTATGCGGTCCTGGCCGGCGACCACCGCGGCCACGGGGCCACCGCCGCCCCGGGCGGCTTCGGCTTCGTCGCCGAGAAGGGCGGCTGGGAGAGGGTCGCGGCCGACATGGGCACCGTGCTGGACGCGGCCCGGCGGGCCTGGCCCGATGTTCCGGTCTTCCTCATGGGCCACTCCTGGGGCTCCTTCCTGGCCCGCGACCTGGCCGCGCGCCGCGGCGGTGAGCTGGCCGGCCTCATCCTGCTGGGGACCGGCTCAGGAACTGGTGCGCTGACCCGTCCCGCCGCCGCGGTCTGTGCCGGGGAGTCCCGGCTGCGCGGCCCGCGCCACCCCTCTCGGCTGCTCAACGCGCTCGCCTTCGGCCCCTACCAGCGCCACTTCGCCCCCAACCGCACCGAGGCCGACTGGATCAGCCGGGACGTTCATGAGGTCGACCGCTACGTCGCCGACCCCTGGTGCGGATTCGTGTGCACCGCGAGCTTCTTCCGCGACCTCGTTGCCGGAGGAAGGGCCGTCAATACGGCCGCCCACGCCGCGGCCGTGCCCGCGCAGCTGCCTATGCTCCTGGCGTCCGGTGACCGGGACCCGGTCGGCGCCATGGGGCGGGGCGTCCAGCGCTCCGCCACCCTCTACCGCCGCGCCGGCGTGCGGGAGGTCTGCGTCATCCTCTATCCGGGCGGGCGCCACGAGCTGCTCAACGAGACCAATCGGGATCAAGTCACCGGCGACATCCTCACCTGGATCGACGGACACCTGCCTGAACTGTGA","MQTSLTRLTADDGTRLVVHIWLPEWLIDGSLLVADVPEADSPAPTSAATRPQVPGAARPRGIIVIAHGMAEHASRYARFAASAVEEGYAVLAGDHRGHGATAAPGGFGFVAEKGGWERVAADMGTVLDAARRAWPDVPVFLMGHSWGSFLARDLAARRGGELAGLILLGTGSGTGALTRPAAAVCAGESRLRGPRHPSRLLNALAFGPYQRHFAPNRTEADWISRDVHEVDRYVADPWCGFVCTASFFRDLVAGGRAVNTAAHAAAVPAQLPMLLASGDRDPVGAMGRGVQRSATLYRRAGVREVCVILYPGGRHELLNETNRDQVTGDILTWIDGHLPEL$","Hydrolase, alpha/beta fold family","Cytoplasm, Extracellular","Lysophospholipase L2","hydrolase; alpha/beta fold family","alpha/beta hydrolase fold","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[88-170]T$	Abhydrolase_1

InterPro
IPR008262
Active_site

Lipase, active site
PS00120	$\"[139-148]?$	LIPASE_SER

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[63-334]T$	no description
PTHR11614	$\"[59-337]T$	PHOSPHOLIPASE-RELATED
PTHR11614:SF8	$\"[59-337]T$	LYSOPHOSPHOLIPASE-RELATED

","BeTs to 11 clades of COG2267COG name: LysophospholipaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG2267 is a---k-y-vdrlb-efgh---j----Number of proteins in this genome belonging to this COG is 3","***** IPB008262 (Lipase, active site) with a combined E-value of 3.5e-08. IPB008262A 88-103 IPB008262B 138-149***** IPB003089 (Alpha/beta hydrolase fold signature) with a combined E-value of 4.7e-07. IPB003089A 87-102 IPB003089B 141-154***** IPB000639 (Epoxide hydrolase signature) with a combined E-value of 6.8e-07. IPB000639B 87-102 IPB000639C 141-154***** IPB002410 (Prolyl aminopeptidase (S33) family signature) with a combined E-value of 8.8e-06. IPB002410B 90-101 IPB002410C 141-155","","","No significant hits to the PDB database (E-value < E-10).","Residues 88 to 332 (E_value = 0.00076) place ANA_1695 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","L2 ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1696","1838629","1839195","567","4.87","-12.38","20263","ATGGCCGCCCACTCCTTCACCCTCGTTCCCGCCGCCTACGTCTACCTCCTGCGTCCCGATCCGGGTGCCGTGGAACGGGACGCCGGGGCGGCGAGCACGGCGACCCAGGTGCTCCTCCAGCTGCGGCAGAACACTGGCTACATGGACGGGCACTGGGCCTGCGGCGCCTCGGGGCACGTCGAGGCCGCCGAGAGCGTCCTGGAGGCGGCTCTGCGCGAGACCGACGAGGAGCTGGGAATCGACGTCGAGGTGAAGGACCTCGACGCGCTGACGGCGATGCACCGCACCAACGATCTGGGCGGGGCAGCTCTGGAGCAGCGCATCGACCTGTTCTTCACGCTGCGGACCTGGACGGGCACGCCGGCCGTGCGCGAGCCGGCCAAGAACGCGGGGCTGCGCTGGTTCTCCCTGACCGACCTGCCCGAGGCGGTCCCGCCGCACGAGCGCCACGTCCTGGAACTGCTGGCCGCCTCCCTCGATGGCGGTAGGCCGGTGCCCCCGATCATCACCTTCGGCTTCGATGAGGGCGAGGACATCGCCCGCTACGGCGTCGCCCTGCCGCACTGA","MAAHSFTLVPAAYVYLLRPDPGAVERDAGAASTATQVLLQLRQNTGYMDGHWACGASGHVEAAESVLEAALRETDEELGIDVEVKDLDALTAMHRTNDLGGAALEQRIDLFFTLRTWTGTPAVREPAKNAGLRWFSLTDLPEAVPPHERHVLELLAASLDGGRPVPPIITFGFDEGEDIARYGVALPH$","NUDIX hydrolase","Cytoplasm","putative MutT-family protein","NUDIX hydrolase","NUDIX hydrolase","","Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 1992. 174(20):6321-6325. PMID: 1328155Koonin E.V. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 1993. 21(20):4847-4847. PMID: 8233837Mejean V., Salles C., Bullions L.C., Bessman M.J., Claverys J.P. Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydrolases. Mol. Microbiol. 1994. 11(2):323-330. PMID: 8170394Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 1993. 268(31):23524-23530. PMID: 8226881McLennan A.G. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int. J. Mol. Med. 1999. 4(1):79-89. PMID: 10373642Bessman M.J., Frick D.N., O. Handley S.F. The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes. J. Biol. Chem. 1996. 271(41):25059-25062. PMID: 8810257","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
G3DSA:3.90.79.10	$\"[36-146]T$	no description
PF00293	$\"[8-157]T$	NUDIX
PS00893	$\"[58-79]T$	NUDIX

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide

","No hits to the COGs database.","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 7.5e-08. IPB000086 53-80","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 157 (E_value = 5.9e-12) place ANA_1696 in the NUDIX family which is described as NUDIX domain.","","MutT-family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1697","1840163","1839198","966","5.57","-5.90","35467","GTGATCTCGCGTCCCGTCCCCGTCACCGACCCTGTTCAACGGCCCGTCCCCGTCTCCGACCCCAACCACCGGCCCGCTCCCGTCACCCATGGCCCCGACGACGTCGCCCTCGTCTTCGAGAGCGGCGGCATGCGCGGGGCCTACACGGCCGGTCTCGTGCGCGTCATGCTGGAGGCCGGACTCTCCTTCCCCTGGGTCGGGGGCATCTCGGCCGGCTGTACCAACACCTGCAACTTCGTCTCCCGGGACACCTGGCGCACCCGCGAGGCCTACCTGGGACTGACCACCGACCCCCAGGCCGGCGGCTGGGGCAGCTTCGTGACCGGCAAGGGCTACTTCAACTCCGAGCACATCTACCTGCACACCTCCGCCCCCGACGAGTCCATCCCCTTCGACTGGGAGACCTTCGCCGCCTCACCGGTCACGGTGCGCCTGGGCGCCTTCCGCTGCGACACCGGCGAGGAGGTCTACTGGGGCCTGGAGGACATGCCCACCATGGCGGACCTGCAGGTGCGGGCCCGGGCGTCGTCGTCGATGCCGGTGCTCATGCCCATGGTCGAGGTCGACGGCGCCCCCTACGTGGACGGTGCCGTCGGGCCCACCGGCGGCTTCGCCATCGACGCCGCCCGCGCTGACGGCTACGACAAGCAGCTCGTGGTCATGACCCGCCCCGAGGGCTACCGCAAGCCGCCCATGCGTCGCCACGAGATCGAGATCCTCCAACGGCTCTACCCCCGCTACCCGGCCCTGGTTCAGGCCGTCACCGACCGCCCCGAGAACTACAACCGCACCGTCGAGGAGCTGGAACGCCTGCGCAGCCAGGGGCGCGTCTACCTCTTCCGGCCCGAGCGCATGCCCATCGCCAACGGCGAGCTGCGCTACGACCGCATCGTCACCGCCTTCGAGGCCGGACTGGCCCAGGCCCGCCGTGAGCTGCCCGCCATCGAGGCCTTCCTGGCGAGCTGA","VISRPVPVTDPVQRPVPVSDPNHRPAPVTHGPDDVALVFESGGMRGAYTAGLVRVMLEAGLSFPWVGGISAGCTNTCNFVSRDTWRTREAYLGLTTDPQAGGWGSFVTGKGYFNSEHIYLHTSAPDESIPFDWETFAASPVTVRLGAFRCDTGEEVYWGLEDMPTMADLQVRARASSSMPVLMPMVEVDGAPYVDGAVGPTGGFAIDAARADGYDKQLVVMTRPEGYRKPPMRRHEIEILQRLYPRYPALVQAVTDRPENYNRTVEELERLRSQGRVYLFRPERMPIANGELRYDRIVTAFEAGLAQARRELPAIEAFLAS$","Patatin-like phospholipase","Cytoplasm","Predicted esterase of the alpha-beta hydrolasesuperfamily","patatin","Patatin","","Mignery G.A., Pikaard C.S., Park W.D. Molecular characterization of the patatin multigene family of potato. Gene 1988. 62(1):27-44. PMID: 3371664","","","

InterPro
IPR002641
Family

Patatin
PF01734	$\"[37-205]T$	Patatin

","BeTs to 6 clades of COG1752COG name: Predicted esterase of the alpha-beta hydrolase superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1752 is ------yqv-rlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 37 to 205 (E_value = 5.5e-08) place ANA_1697 in the Patatin family which is described as Patatin-like phospholipase.","","esterase of the alpha-beta hydrolase superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1698","1840253","1841359","1107","5.42","-9.87","39207","ATGAGCACCTCCAGCGCGCTGCGCATTCTTGAGCCCATGACCATGCGCGGGCTGACCGCCCGCAACCGCCTATGGCTGCCGCCGATGTGCATGTACTCGGTCGAGGCGCAGGACGGCATCGTCACCGACTGGCACGTGGTCCACTACGCCAGCCGCGCGGTGGGCGGTTTCGGCACGGTCATCGTGGAGGCCACGGCAGTCACCCCCGAGGGGCGCCTGTCCCCCAACGACCTGGGGCTGTGGTCGGACGAGCAGGTCGCCGGCCAGCGCCGCCTGGTGGAGGCGATCCACGCCGGCGGGGCCCTGGCCGGCATCCAGATCGGGCACGGCGGACGCAAGTCGGGGACCCCTCCGTGGCGCCCCAAGGTGGAGGGCGCGCGCACCGGCACCCTGGAGGGCTGGGAGCTGCTGGCCCCCAGCGCGATCCCCTTCCCCCAGCACGCGGTTCCCACCGAGCTGGACGAGGCCGGGATCAGTCGGATCGTGGAGGCCTTCGCGGCGGCCGCGCGGCGCGCCGTCGAGGCCGGCTACGACGTCGTCGAGATCCACGGCGCCCACGGCTACCTCATCCACGAGTTCCGCTCCGCCCTGTCCAATCAGCGCACCGACTCCTACGGCGGAAGCGTGGAGAACCGGCAGCGCTTCCCGCTTGAGGTGGTGCGGGCCGTGCGCGAGGCCATCGGGTCGCAGACGGTGCTCGACATCCGCCTGTCGGCCTCGGACTGGGCCGAGGGCGGCGTCACCGGTGAGGAGACCGCCGCCTTCAGCCGCGAGCTGGTGGAGGCCGGCGTCGACGTCCTGCACATCTCCAGCGGCGGGAACGTCCCGGCCGCGGTCCCGGTGGGGCCCGGCTACCAGCTGCCGCTGGCCCAGCAGGTCAAGCAGGCCGTCGCCGGCAGCGACGTCCCGGTGGTGGGTGTGGGTCTCATCGAGGAGGCGGCCCAGGCCGAGCAGGCGCTCATCTCCGGCCAGGCCGATGCGATCGCCGTGGGCCGAGCGGCTCTGCGCGACCCCTACCTGCCGCTGCGCTGGGCGGCCGACCTGGGGGTGCGCTCCTGGGACGAGGCCCCCTGGCCCATCCAGTACTGGCGCGGCGCCTGGAGCTGA","MSTSSALRILEPMTMRGLTARNRLWLPPMCMYSVEAQDGIVTDWHVVHYASRAVGGFGTVIVEATAVTPEGRLSPNDLGLWSDEQVAGQRRLVEAIHAGGALAGIQIGHGGRKSGTPPWRPKVEGARTGTLEGWELLAPSAIPFPQHAVPTELDEAGISRIVEAFAAAARRAVEAGYDVVEIHGAHGYLIHEFRSALSNQRTDSYGGSVENRQRFPLEVVRAVREAIGSQTVLDIRLSASDWAEGGVTGEETAAFSRELVEAGVDVLHISSGGNVPAAVPVGPGYQLPLAQQVKQAVAGSDVPVVGVGLIEEAAQAEQALISGQADAIAVGRAALRDPYLPLRWAADLGVRSWDEAPWPIQYWRGAWS$","NADH-dependent flavin oxidoreductase","Cytoplasm, Extracellular","NADH-dependent flavin oxidoreductase","putative NADH-dependent flavin oxidoreductase","NADH:flavin oxidoreductase/NADH oxidase","","","","","

InterPro
IPR001155
Domain

NADH:flavin oxidoreductase/NADH oxidase, N-terminal
PF00724	$\"[8-351]T$	Oxidored_FMN

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[8-347]T$	no description

noIPR
unintegrated

unintegrated
PTHR22893	$\"[11-351]T$	NADH OXIDOREDUCTASE-RELATED
PTHR22893:SF7	$\"[11-351]T$	2,4-DIENOYL-COA REDUCTASE [NADPH]

","BeTs to 12 clades of COG1902COG name: NADH:flavin oxidoreductases, Old Yellow Enzyme familyFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1902 is ao-p--y-vdrlb-efg-s--j----Number of proteins in this genome belonging to this COG is 1","***** IPB001155 (NADH:flavin oxidoreductase/NADH oxidase) with a combined E-value of 4.6e-43. IPB001155A 9-24 IPB001155B 175-221 IPB001155C 327-347","","","-57% similar to PDB:1Z41 Crystal structure of oxidized YqjM from Bacillus subtilis (E_value = 3.0E_67);-57% similar to PDB:1Z42 Crystal structure of oxidized YqjM from Bacillus subtilis complexed with p-hydroxybenzaldehyde (E_value = 3.0E_67);-57% similar to PDB:1Z44 Crystal structure of oxidized YqjM from Bacillus subtilis complexed with p-nitrophenol (E_value = 3.0E_67);-57% similar to PDB:1Z48 Crystal structure of reduced YqjM from Bacillus subtilis (E_value = 3.0E_67);-54% similar to PDB:2H8X Xenobiotic Reductase A-oxidized (E_value = 9.2E_61);","Residues 8 to 351 (E_value = 2e-93) place ANA_1698 in the Oxidored_FMN family which is described as NADH:flavin oxidoreductase / NADH oxidase family.Residues 292 to 340 (E_value = 0.00029) place ANA_1698 in the Dus family which is described as Dihydrouridine synthase (Dus).","","flavin oxidoreductase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1699","1841468","1841833","366","8.57","3.32","13557","GTGCGCAGCACGCAGAGGCACCGCGGGGACGTGTACTCCTCGCAGTGCCCGTGCCGCGACCTTCTGGACGTCGTGGCCAACAAGTGGTCCGCGCTGGCCATCGGCGCACTGGCCGAGGGACCGTTGCGCTTCGGGGAGCTGCAACGGCGCCTTCAAGGAATCTCGCCGAAGGTGCTGACCGCTACGCTGCGCCGGTTGGAGGACCACGGACTCGTGCACCGAGAGGTGATCCCGGAGGTTCCTCTTCACGTGGAGTACTCCCTGACGGAGGTCGGCCGGAGCGCCGTCGAACCGGTATTCGCGCTTCGGGAATGGGCCGAGTCCCGATACGCGCATGCGCTGACTCACGCGAGGTCGACCCCCTAG","VRSTQRHRGDVYSSQCPCRDLLDVVANKWSALAIGALAEGPLRFGELQRRLQGISPKVLTATLRRLEDHGLVHREVIPEVPLHVEYSLTEVGRSAVEPVFALREWAESRYAHALTHARSTP$","Transcriptional regulator","Cytoplasm","transcriptional regulatory protein PadR-","putative transcriptional regulator","helix-turn-helix, HxlR type","","Yasueda H., Kawahara Y., Sugimoto S. Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression. J. Bacteriol. 1999. 181(23):7154-7160. PMID: 10572115Huffman J.L., Brennan R.G. Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr. Opin. Struct. Biol. 2002. 12(1):98-106. PMID: 11839496","","","

InterPro
IPR002577
Domain

Helix-turn-helix, HxlR type
PD004032	$\"[42-80]T$	Q8PWJ9_METMA_Q8PWJ9;
PF01638	$\"[24-107]T$	DUF24
PS51118	$\"[16-114]T$	HTH_HXLR

","BeTs to 14 clades of COG1733COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1733 is aomp-z---drlbcefghs-uj----Number of proteins in this genome belonging to this COG is 4","***** IPB002577 (Protein of unknown function DUF24) with a combined E-value of 4.3e-30. IPB002577 43-90","","","-63% similar to PDB:1YYV Putative transcriptional regulator ytfH from Salmonella typhimurium (E_value = 1.1E_19);-56% similar to PDB:1Z7U Crystal Structure of the Putitive Transcriptional Regulator of MarR Family from Enterococcus faecalis V583 (E_value = 5.8E_13);-58% similar to PDB:2FSW Crystal Structure of the Putative Transcriptional Regualator, MarR family from Porphyromonas gingivalis W83 (E_value = 2.9E_12);-55% similar to PDB:2F2E Crystal Structure of PA1607, a Putative Transcription Factor (E_value = 6.4E_12);-60% similar to PDB:2HZT Crystal Structure of a putative HTH-type transcriptional regulator ytcD (E_value = 2.1E_10);","Residues 24 to 115 (E_value = 2.1e-31) place ANA_1699 in the DUF24 family which is described as HxlR-like helix-turn-helix.","","regulatory protein PadR-","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1700","1842143","1843183","1041","5.43","-9.84","36926","ATGCCCTCAAGCAGCCCTGACACCCAACGCACCATGACCGCTGTCGTCACTCGATCCGGAGGCTCGGTGGACATCCCGGACGCCCTGGTCGATGCCACCGTCCCCGCCCCGGCGGCTCCCACTGGCCACGACATCCTCGTGGAGGTCAAGGCACTGTCCGTCAACCCCGTTGACGTCAAAGTGCGCACCGCCCTCAACCACGCCGGCGGCGAGGAACGCATCCTGGGATGGGATGCAGCGGGAACGGTCATCGCGGTCGGCGAGCAGACCACCCTCTTCCAGCCCGGCGATGACGTCTACTACGCCGGAGCACTGGAGCGTCCCGGCTCCTACGGACAGCTACAGCTCGTGGACGAACGCATCGTTGGACCGAAGCCGAGATCGTTGGACTACGCGAGTGCGGCGGCTCTGCCCCTGACCTCCCTCACCGCGTGGGAGGCTCTTTTCGACAAGCTCCACCTGAGCAGGGACTCCGCAGGCACGATCCTCGTGCTGGGAGCCGCAGGAGGGGTGGGCTCCATGGTGATCCAGCTGACCAAGGCCCTCACCGATGTCTCCGTCATCGCCACTGCCTCACGTGAGGAGTCCCGCGACTGGGTCCGGTCACTGGGTGCCGACGCAGTGGTGGACCACTTCGCCGAGGACCTCGCACAGCAGGTTCTCGCCATCGCACCGGACGGCGTCGAATACGTCTTCACCCCGCAGAGCCGAGGGCGCGTGCCGCTGCTGACCACGGTGGTTCGTCCTTTCGGGGAGATCGTCGCCATCGACGACGAGCGAGACCTGGACCTGTACGCGCTCAAGGACAAGGCCATCTCATGGCACTGGGAGTTCATGTTCGCCCGCCCCAGGCACGGCTACGACCTCATCACCCAGCACCACATCCTCTCCACCGTCGCCGAGCTCATCGACAGTGGAAGGATCCGTGGCACTGCGTCCCAGACGCTCACGCCTCGCAATGCTGCGCAGATACGGGCAGCTCACCGCCTCATCGAGAGCGGGCGCACGGTGGGAAAGATCGTCGTGACCGACGCCGGCTGA","MPSSSPDTQRTMTAVVTRSGGSVDIPDALVDATVPAPAAPTGHDILVEVKALSVNPVDVKVRTALNHAGGEERILGWDAAGTVIAVGEQTTLFQPGDDVYYAGALERPGSYGQLQLVDERIVGPKPRSLDYASAAALPLTSLTAWEALFDKLHLSRDSAGTILVLGAAGGVGSMVIQLTKALTDVSVIATASREESRDWVRSLGADAVVDHFAEDLAQQVLAIAPDGVEYVFTPQSRGRVPLLTTVVRPFGEIVAIDDERDLDLYALKDKAISWHWEFMFARPRHGYDLITQHHILSTVAELIDSGRIRGTASQTLTPRNAAQIRAAHRLIESGRTVGKIVVTDAG$","Alcohol dehydrogenase, zinc-binding domain protein","Cytoplasm","alcohol dehydrogenase, zinc-containing","alcohol dehydrogenase; zinc-binding domain protein","Alcohol dehydrogenase, zinc-binding domain protein","","Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Taneja B., Mande S.C. Conserved structural features and sequence patterns in the GroES fold family. Protein Eng. 1999. 12(10):815-818. PMID: 10556240","","","

InterPro
IPR002085
Family

Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695	$\"[34-343]T$	ALCOHOL DEHYDROGENASE RELATED

InterPro
IPR013149
Domain

Alcohol dehydrogenase, zinc-binding
PF00107	$\"[158-292]T$	ADH_zinc_N

InterPro
IPR013154
Domain

Alcohol dehydrogenase GroES-like
PF08240	$\"[42-125]T$	ADH_N

InterPro
IPR014182
Family

Alcohol dehydrogenase. zinc-binding type 1
TIGR02817	$\"[13-341]T$	adh_fam_1: zinc-binding alcohol dehydrogena

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[119-316]T$	no description
PTHR11695:SF34	$\"[34-343]T$	ALCOHOL DEHYDROGENASE, ZINC-CONTAINING

","BeTs to 9 clades of COG0604COG name: NADPH:quinone reductase and related Zn-dependent oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0604 is -o-p-zyq-drlb-efghs--j----Number of proteins in this genome belonging to this COG is 4","***** IPB002364 (Quinone oxidoreductase/zeta-crystallin) with a combined E-value of 2e-28. IPB002364A 53-66 IPB002364B 71-91 IPB002364C 109-136 IPB002364D 157-180***** IPB011597 (GroES-related) with a combined E-value of 1.3e-19. IPB011597A 41-68 IPB011597B 72-99 IPB011597C 108-145 IPB011597D 160-204***** IPB002328 (Zinc-containing alcohol dehydrogenase) with a combined E-value of 3.8e-06. IPB002328A 29-60 IPB002328B 72-99","","","-48% similar to PDB:1YB5 Crystal structure of human Zeta-Crystallin with bound NADP (E_value = 1.9E_12);","Residues 42 to 125 (E_value = 8.5e-08) place ANA_1700 in the ADH_N family which is described as Alcohol dehydrogenase GroES-like domain.Residues 158 to 292 (E_value = 4.9e-12) place ANA_1700 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase.","","dehydrogenase, zinc-containing (PA3567)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1701","1843688","1843233","456","7.37","0.97","16368","ATGGCGGGGAAGCAGGCGGGCCGCAGGGGCCGGCCGGACTCGCCGGTCCGCGCCGCCGGCGTGCACGGCGCCGACCCCTGCCCCTGCGGCAGCGGGCGCACCTACGCCCAGTGCTGCGAGCCGCTCCACGACGGCGCCCCGGCGCCCACCGCCCAGGCCCTCATGCGCTCGCGCTACACGGCCTTCGTCGTCGGCGACGAGGACTACCTCTTCCGCACCTGGCACCCGCGCACCCGCCCCGAGGGGCCCTACTGCCACCCCGGGACCCGGTGGACGGGACTGACCATCCACGAGACCGTCGACGGCGGGGCGGACGACGAGACCGGCATCGTGGAGTTCACCGCCACCTACTGCAGCGGCGACGGGCGCGGGGGAGTGGTGGATGACGCCCTGCGCGAGCGCTCCCGCTTCACCCGCCGCGCCGGCCGCTGGCTCTACCTCGACGCCGTCGGATAG","MAGKQAGRRGRPDSPVRAAGVHGADPCPCGSGRTYAQCCEPLHDGAPAPTAQALMRSRYTAFVVGDEDYLFRTWHPRTRPEGPYCHPGTRWTGLTIHETVDGGADDETGIVEFTATYCSGDGRGGVVDDALRERSRFTRRAGRWLYLDAVG$","SEC-C motif domain protein","Cytoplasm, Extracellular","GTG start codon","hypothetical protein","SEC-C motif domain protein","","","","","

InterPro
IPR004027
Domain

SEC-C motif
PF02810	$\"[23-43]T$	SEC-C

","BeTs to 5 clades of COG3012COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3012 is ---------d----efgh-n------Number of proteins in this genome belonging to this COG is 1","***** IPB004027 (SEC-C motif) with a combined E-value of 3.3e-08. IPB004027 23-40","","","No significant hits to the PDB database (E-value < E-10).","Residues 23 to 43 (E_value = 7.3e-06) place ANA_1701 in the SEC-C family which is described as SEC-C motif.","","start codon","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1702","1845037","1843691","1347","5.35","-17.04","46825","ATGACTGATGCTGCCAGCACGCTCACCAGCGCCCCCACCTGTGACGCCGCCGCGATCCTGCGCGACGACGACGCCTACACCGACTCGCTCATCGACTTCGTCACCGCCTCACCCAGCTCCTACCACGCCGCCGCCGAAGTCGCCCGCCGCCTGGAGGCAGCCGGCTTCACCGGCGCCGATGAGACCGTCACCTGGCAGGAGGACCTGCCGCGGCGCGGCTACGTCATCCGCGACGGTGCCATCGCCGCCTGGGCGCTGCCCGAGACGCTCAGCCCGGGGGCGGGCCTGCGCATCGTCGGCGCCCACACCGACTCCCCGGCCCTCAAGCTCAAGCCCGCCGCCGCCCTCGTCCGCTCCGGCTGGCAGCTCATCAACGCCGAGGTCTACGGAGGCCCCCTGCTCGCCTCCTTCCTCGACCGCGAGCTGGGCCTGGCCGGGCGCCTGACCACCCGCGACGGCGCCGTCCACCTCGTGCGCACCGGACCCATCGCCCGCGTGGCCCAGATCGCCCCGCACCTGGACCGCAGCGTCAACGACACCCTCCACCTGGACCGCCAGACCCACCTGCTGCCCCTGTGGTCACTGGCCGAACCCGACGCCGCCCCCGACGCGGTCGAGACCCACCTGTGCGAGATCGCCGGCATCGACCCGGCCGAGCTCGCCGGCCACGACGTCCTGACCTACCCCACCCAGGCGCCCGCCCGCTTCGGCCGTGACGGAGAGTTCCTGGCCTCCTCCCGCCTGGACAACCTCTCCTCCGTCCACGCCGGACTGGTCGCCCTCGAGGCGCTCGCGGTCGCCGGGACCGAACTCGCCGAGCCCGTCATCCTGGTTGCCTTCGACCACGAGGAGGTCGGCTCGGACACCCGCTCCGGGGCGGGTGGCCCCTTCCTCGAGACGCTCCTGCGGCGCCTGGCCCGGGTCCTGGGCGTCAGCGGTGACGGCCTCGAGGCCCTCATGGCCCGCTCGACCTGCGTGAGCGCCGACGCCGGGCACTCCGTCCACCCCGCCTACTCCCACCTGCACGACCCGGCCGTCCAGCCGCTCATCAACCACGGGCCCCTGCTCAAGATCAACGCCCAGCAGCGCTACGCCACCGACGCCGCGGGCGCCGCGATCTGGGCGCGGGCCTGCACGGCGGCGGGCGTGCCCAGCCAGGACTTCGTCTCCAACAACGCCGTGCCCTGCGGCTCCACCATCGGCCCCATCACCGCCACCCGCCTCGGCATCACCACGGTCGATGTCGGCGTGCCCCTGCTGAGCATGCACTCGGCCCGCGAGATGGGCGGAGTCCAGGACGGCCCCTGGCTCGCCCAGGCCCTGCACGCCTACTGGCAGGGGGCCTGA","MTDAASTLTSAPTCDAAAILRDDDAYTDSLIDFVTASPSSYHAAAEVARRLEAAGFTGADETVTWQEDLPRRGYVIRDGAIAAWALPETLSPGAGLRIVGAHTDSPALKLKPAAALVRSGWQLINAEVYGGPLLASFLDRELGLAGRLTTRDGAVHLVRTGPIARVAQIAPHLDRSVNDTLHLDRQTHLLPLWSLAEPDAAPDAVETHLCEIAGIDPAELAGHDVLTYPTQAPARFGRDGEFLASSRLDNLSSVHAGLVALEALAVAGTELAEPVILVAFDHEEVGSDTRSGAGGPFLETLLRRLARVLGVSGDGLEALMARSTCVSADAGHSVHPAYSHLHDPAVQPLINHGPLLKINAQQRYATDAAGAAIWARACTAAGVPSQDFVSNNAVPCGSTIGPITATRLGITTVDVGVPLLSMHSAREMGGVQDGPWLAQALHAYWQGA$","Aspartyl aminopeptidase","Cytoplasm, Extracellular","Aspartyl aminopeptidase","aspartyl aminopeptidase ","Aspartyl aminopeptidase","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Chang Y.H., Smith J.A. Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae. J. Biol. Chem. 1989. 264(12):6979-6983. PMID: 2651436","","","

InterPro
IPR001948
Family

Peptidase M18, aminopeptidase I
PR00932	$\"[96-112]T$ $\"[129-149]T$ $\"[280-298]T$ $\"[323-339]T$ $\"[412-427]T$	AMINO1PTASE
PF02127	$\"[33-445]T$	Peptidase_M18

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.10	$\"[25-447]T$	no description

","BeTs to 6 clades of COG1362COG name: Aspartyl aminopeptidaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1362 is ------y-v-r----f--------t-Number of proteins in this genome belonging to this COG is 1","***** IPB001948 (Aminopeptidase I zinc metalloprotease (M18) signature) with a combined E-value of 1.9e-57. IPB001948A 96-112 IPB001948B 129-149 IPB001948C 160-177 IPB001948D 280-298 IPB001948E 323-339 IPB001948F 412-427","","","-51% similar to PDB:2IJZ Crystal structure of aminopeptidase (E_value = 3.8E_67);-39% similar to PDB:2GLF Crystal structure of Aminipeptidase (M18 family) from Thermotoga Maritima (E_value = 1.3E_14);","Residues 33 to 445 (E_value = 4e-113) place ANA_1702 in the Peptidase_M18 family which is described as Aminopeptidase I zinc metalloprotease (M18).","","aminopeptidase (M18)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1703","1845166","1845774","609","4.76","-12.12","21786","GTGCGCGCCGTCCTGCTCGATGCTGACGGCGTTCTGCAGCTCATCGGCACCCCGTGGGGCGAGGCGCTGACCCGCGGCGGCGGCCCCGCCTTCGCCCAGGCCATGATCGATGGTGAGACCGATGCCTTGGCGGGTCGGGAGACCCTGACCGAGCTGCTGGAGCGGGTGGTGACGAGCCTGGGGCTGGAGCTACGCGCATCGGATCTGTTGGAGATGTGGCACCGGGCCACACCCGACCCTGTGGCCTGGCAGCTGGTGAGGGACCTGCGCGAGGCGGGATACACCACGGTCCTGGCCACCAATCAGCAGTGGGAGCGTCGGGCCTGGATGCGTGAGCAGCTGGGCTATGACGGCCTGTGCGACATCGACGGCTACTCCTGCACGCTGGGGGTGGCCAAACCGGATGCCGCCTACTTCCACCGGCTGCTGGAGCTGGCGGGGGTGGAGGCGGACCAGGCCCTGTTCGTCGATGACAGCGCCACCAACATCGCCGCGGCCCGCGAGGTGGGCTTGCGCACTATCCACCACCCGGCCGACGCCGGCGGCGAGCTGTTGCGCCGCGAGGTGGCCCAGGCCCTGACGCCGGCCGCCTCTGCGCCGCAAGGATGA","VRAVLLDADGVLQLIGTPWGEALTRGGGPAFAQAMIDGETDALAGRETLTELLERVVTSLGLELRASDLLEMWHRATPDPVAWQLVRDLREAGYTTVLATNQQWERRAWMREQLGYDGLCDIDGYSCTLGVAKPDAAYFHRLLELAGVEADQALFVDDSATNIAAAREVGLRTIHHPADAGGELLRREVAQALTPAASAPQG$","HAD-superfamily hydrolase, subfamily IA, variant 3","Cytoplasm, Extracellular","haloacid dehalogenase-like hydrolase, putative","K07025 putative hydrolase of the HAD superfamily","HAD-superfamily hydrolase, subfamily IA, variant 3","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317Selengut J.D. MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases. Biochemistry 2001. 40(42):12704-12711. PMID: 11601995Morais M.C., Zhang W., Baker A.S., Zhang G., Dunaway-Mariano D., Allen K.N. The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry 2000. 39(34):10385-10396. PMID: 10956028","","","

InterPro
IPR005833
Family

Haloacid dehydrogenase/epoxide hydrolase
PR00413	$\"[1-12]T$ $\"[89-102]T$ $\"[138-158]T$	HADHALOGNASE

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[1-179]T$	Hydrolase

InterPro
IPR006402
Domain

HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509	$\"[3-176]T$	HAD-SF-IA-v3: HAD-superfamily hydrolase, su

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[66-178]T$	no description
PTHR12725	$\"[78-182]T$	HALOACID DEHALOGENASE-LIKE HYDROLASE
PTHR12725:SF3	$\"[78-182]T$	HALOACID DEHALOGENASE-LIKE HYDROLASE-RELATED

","BeTs to 10 clades of COG1011COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1011 is -ompk-yqvdrlb-efghsn-j--t-Number of proteins in this genome belonging to this COG is 2","***** IPB005833 (Haloacid dehalogenase/epoxide hydrolase family signature) with a combined E-value of 4.9e-12. IPB005833A 1-12 IPB005833D 89-102 IPB005833F 138-158 IPB005833G 165-178","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 179 (E_value = 1.6e-14) place ANA_1703 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","dehalogenase-like hydrolase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1704","1845871","1846434","564","7.96","2.52","20669","ATGGCAGGAACCGCGACGGACGACCGGGCCCCCGGGACCACCACCGCTGAAGGAGCTGCGTCCACCGTCGAGTCCTCCGCCTCCACGACCCGCCGCGCCCCGGAGGTCTTCCTGCGCCTCATCACGGCGATCCACTCCGTCCTGCCGGGCTTCGTGCGCCGTCGGCTGCCGGTGACCTTCATCGGCTACGCGATCATCAACGGCTCCGCCTTCCTCCTGGACATCACCTGCCTGTGGGTGTTCTACAACCACCTCCACTGGTTCTACCCCGTGGCGGTCACGGTCGGCTACGCCATCGCGGCCGTCTACTCCTTCCTGCTCAACCGGTGGCTGAACTTCCAGGCCCACGGGCACGTCGTCCAGCAGGGGGCGGGCTACATGGCCGGGGTCGTCAGCCAGTACGTCATCTTCATCCTGGGGCTGTCCTCACTGCTGCACTGGTTCGGGGTCAACGCCGAGCTGGCGCGCGTCATCTCGGCCTGCTGCGAGGGCATCTACCTCTACGTGTTCATCCGGCTGTGGGTGTTCCGCGGGGTGCCGGAGCCCGAGCACGCTGATCGCTGA","MAGTATDDRAPGTTTAEGAASTVESSASTTRRAPEVFLRLITAIHSVLPGFVRRRLPVTFIGYAIINGSAFLLDITCLWVFYNHLHWFYPVAVTVGYAIAAVYSFLLNRWLNFQAHGHVVQQGAGYMAGVVSQYVIFILGLSSLLHWFGVNAELARVISACCEGIYLYVFIRLWVFRGVPEPEHADR$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[62-82]?$ $\"[88-107]?$ $\"[128-148]?$ $\"[154-176]?$	transmembrane_regions

","BeTs to 5 clades of COG2246COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2246 is ao-pkz----r-bce------j----Number of proteins in this genome belonging to this COG is 3","***** IPB007267 (GtrA-like protein) with a combined E-value of 8.4e-14. IPB007267A 63-89 IPB007267B 90-121 IPB007267C 164-177 IPB007267B 153-184 IPB007267C 101-114","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1705","1847257","1846445","813","6.80","-0.65","28644","GTGCCGCACTCCGCATCTCCGTCCTCACCGTTCTTGCCCTCGCAGCCTCTGCCCTCCCTGTCCGGGAACCCGGACCACGCCGTGCCCTGGGGCATGCAGATCGCCGTGCGCTACGACAAGGTCCACCCGCCCCGGAGGATCGACGTCGCCGAGGCGGCCGCCCGCGCCGTCGTCTGCCTCCTGGCCTCACCCGCCGCCGCCCCCGGCGGGCCGTGGAACCCGGCCGTCGACTACTGGCGCGACGGGCGCATCCGCAAGCTCGTGCGCCGGGCCCGCGGCAAGCGCTGGGAGGAGGTCCAGGCCATCGACGGCGTCACCGTCACCCAGGACGGTCCGGCCGGCTGGGGGCAGGCCGCTGCCCGCGCCTTCGTCCCCGGGCCGGTGCGCCCCCTGCCCGGGGCCCTGGCCAAGACTCAGGTGGAGGGCACCCACTTCCCACCCGGTGACGAGCTGCCCCCGCCGCCCGCCGAGATCACCGCGCGCGTCGCCCAGGACCCGGCTGCGGCCGAGCAGATCGTGCTCACGGCGGCGTCGGCCTCCACCGGTGCCCTCGTGACGATCGAGGTGACCCCCCTGCACGAGATGACCTCGGGCAAGCTGGCCGCCCAGTGCGGCCACGCCGCCCAGCTGGCCTGGGAGAGCAGCGCCATGCCGCCCACCCTGAGACAGGCATGGGCCGACGACGGCTACCGGGTGCGCGTCGTCGTGCCCAGCCGGGAGCAGTGGGAGACCACCACCCGGCCCGTCAGCGTCACCGACGCCGGCTTCACCGAGCTCGACGGCCCCACCGAGACGACCCGCGCCTCCTGGTGA","VPHSASPSSPFLPSQPLPSLSGNPDHAVPWGMQIAVRYDKVHPPRRIDVAEAAARAVVCLLASPAAAPGGPWNPAVDYWRDGRIRKLVRRARGKRWEEVQAIDGVTVTQDGPAGWGQAAARAFVPGPVRPLPGALAKTQVEGTHFPPGDELPPPPAEITARVAQDPAAAEQIVLTAASASTGALVTIEVTPLHEMTSGKLAAQCGHAAQLAWESSAMPPTLRQAWADDGYRVRVVVPSREQWETTTRPVSVTDAGFTELDGPTETTRASW$","Peptidyl-tRNA hydrolase PTH2","Periplasm, Membrane, Cytoplasm","Uncharacterized ACR","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR002833
Domain

Peptidyl-tRNA hydrolase, PTH2
PF01981	$\"[194-264]T$	PTH2

","BeTs to 3 clades of COG1990COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1990 is aompkzy-------------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 194 to 264 (E_value = 2.9e-06) place ANA_1705 in the PTH2 family which is described as Peptidyl-tRNA hydrolase PTH2.","","ACR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1706","1847456","1848820","1365","9.79","10.85","48438","ATGCCACCACATGTTCCATCCACCGCCCTCGGCTCTTCTGACCCGACGCCGCCGGCCGTACCGACCTCCCGTCCACGGATGTTCAATGGCGCGACCATTCACGGCTTCAAGGGCATCCGTCAGCTGCGTCACCCTGCCGAGATCCCGCTCCTGGTCGTGACCAGCCTGGCGACTGCACTGGCCTACCTGGCGTGGATCGCCCTGGTGATCTGGCTGGTGGCCGTGCCTGAACCGACCGGCCTGGGGGCTCAGGTTCGCGACTTCTTCCTCAGCGAGGCGGGCGGCGGCGCGCGGTTCCTCCTGCTGGTGCCCGTCATCCCGATCATCCTGTGGGTGGCGCGCGCGATGCTGTACGCCAAGCTTCGTGCGACCGCGGTCCAGATGAGTCCCACCCAGTTCCCGGAGGGCTATCGGATGGTTGTCGAGGCTGCCCGGCAGTTCGGTCTGCGCCGGGTTCCCGATGCCTACGTGACCATGGGCAACGGTCAGATCAACGCCTTCGCAGCCGGCCACGGCTACCGGCGCTTCGTGGTCGTCAACTCCGATCTGTTCGAGATCGGCGGCCGGGCCCGCGACCCTGAGGCGCTGCGCTTCGTGATCGGGCACGAGGTCGGGCACCTCGCCGCGGGTCACATCTCCATGCTGCGTCTGCTGTTCGTCACCCTCGGCCTCAACGTCCCGCTGGTGGGCAAAGCGCTGGTTCGGGCCCAGGAGTACACGGCGGACAACCACGGCTACTCCTACGCGCCCGAGGGGGTACCCGGGGTCGTGGGGGTGCTCTCCGGGGGCAAGTACCTGGGGGCCGAGGTCAACACCCACGCCGTGGCGGATCGCGCCACGCGGGAGAAGGGGCTGTGGCTCCACATGACCGTCTGGCGGTCCACGCACCCGGTGATCACCTGGCGCGCCCACGCCCTGCGCGACCGCAGCCGCCCGGGGCGGATCATGATCCGCCCGCCGGAGTCCACGGCGTGGTTCCCGCCGTCGGCTCCCAGCGGCGGCGGGCGGTCCGGTTCGTGGCCGACGCCGGAGCAGATGCTGGCGGTGCTGAACTCCACCTCCTCGGCCGTGCCCAGCGAGGAGCAGTTCGGTCGCTACCCCGGTGTGGTCTACGAGGTCCCTCGCGATGAGCTGCGCTGGGCCTCCCCCGTTCCCGTGCCCGTTCCGGTGGGAACCGCGCCTGTCGGACAGGCGGCCTTTGGAGCGCCCCCGAACATGACCGGTCCCGTCGGGCCGCAGCAGCCCACCCCCTACGGGTACGGCTCACCGACGGGATCTGTGAGCGGGTCCACGGGATTCTCTGACACAGCTGTCCCCGATACCTCGGCTCGCCTGTGGCCAGGCGACGGGCCCGGCCAGAACTGA","MPPHVPSTALGSSDPTPPAVPTSRPRMFNGATIHGFKGIRQLRHPAEIPLLVVTSLATALAYLAWIALVIWLVAVPEPTGLGAQVRDFFLSEAGGGARFLLLVPVIPIILWVARAMLYAKLRATAVQMSPTQFPEGYRMVVEAARQFGLRRVPDAYVTMGNGQINAFAAGHGYRRFVVVNSDLFEIGGRARDPEALRFVIGHEVGHLAAGHISMLRLLFVTLGLNVPLVGKALVRAQEYTADNHGYSYAPEGVPGVVGVLSGGKYLGAEVNTHAVADRATREKGLWLHMTVWRSTHPVITWRAHALRDRSRPGRIMIRPPESTAWFPPSAPSGGGRSGSWPTPEQMLAVLNSTSSAVPSEEQFGRYPGVVYEVPRDELRWASPVPVPVPVGTAPVGQAAFGAPPNMTGPVGPQQPTPYGYGSPTGSVSGSTGFSDTAVPDTSARLWPGDGPGQN$","Peptidase M48, Ste24p","Membrane, Extracellular","putative peptidase A","hypothetical protein","peptidase M48, Ste24p","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Fujimura-kamada K., Nouvet F.J., Michaelis S. A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor. J. Cell Biol. 1997. 136(2):271-285. PMID: 9015299","","","

InterPro
IPR001915
Family

Peptidase M48, Ste24p
PF01435	$\"[140-311]T$	Peptidase_M48

noIPR
unintegrated

unintegrated
tmhmm	$\"[55-75]?$ $\"[96-118]?$	transmembrane_regions

","BeTs to 16 clades of COG0501COG name: Zn-dependent protease with chaperone functionFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0501 is aompkzyq-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 140 to 311 (E_value = 4.9e-20) place ANA_1706 in the Peptidase_M48 family which is described as Peptidase family M48.","","peptidase A","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1707","1850285","1848927","1359","5.03","-17.88","48268","ATGCCGCAGGTCACCGGAGCCGTTCATGAGGTGGGTGTCGACCAGCTCTTCTTCTCCACCACAGACGCGCGTGGTGTCATCCGCCACTCGAACAACGTCTTCATCGAGCTCTCGCGCTATCGGCGTGACGAGCTCTCCGGCGCCCCGCACAACATCATCCGCCACCCGGAGATGCCCGGTGGCGCCTTCAAGGCCATGTGGGACACCCTCAAAGCCGGCAGCCCCTTCGCCGCCTACGTGCGTAACCTCGCCGCCGACGGCAGTGAGTACGACGTCTTCGCCACCGTCACCCCACTGTCCGACGGAGGCTACCTCTCGGTGCGCACCCGTCCGGTGTGCTCCGACCTGTTCGACACCGCCTGCGCCATCTACAGCGACGCTCGCGCCGTCGAGGATGAGGCCATCCACGCCGGGGCCAACCGCCGGGCGGCGGCCGAGGAGGGGTTGAACCGCATCGCCGAGAAGCTGGCCGGAGCGGGCCTGTCCTCCTACGAGGAGTTCCAGAACACGGCCCTGCCGGCGGAGGTGGCGCGTCGGGAGGAGCTCTCCGAGGGCATCCCGGTGCGCCCGGACGCCACCGGGGACCTGCGCGTCATGCTCGACTCGGTCACCAGGATCGCCGCCGGGCTCGACTCGTGGATGTCCGGTCAGCAGCAGCTCGCCGAGCTCTCCGCCTCCCTCAAGGCCGCGGGGAAGGGACTGACCCGAACCCTGGAGGACCCTCGCCTGAACTCCGCGCATATCTCCGCCCTGGACCGCTCCGACCCCCGGGTCAAACCCCTGGCCGACCTGCTGGACCTGTGGACCCAGATGCAGGGCCTGGTCAGTCCCCTCGTGGCGAGGCTCGTCGACACCCTGGCCCAGCTCGACACCAACGGCGCCCGCACCCGCTTCCGCATCGCCCTGGCCCGTCTGCACACCACCATCAGCTCGCTGTTCACCGTCGAGCTCATCGACGGCGTCGGAGACCCGCAGTACTCGGCGCAGGCCATCCCCGACCTCATCGAGTCGCTCCGTGAGGGCATCGCCGAGATGGAGCGTCAGGCCCAGGCCCACAGTGCGCTCGCGGCCCAGGCGGTCGCCTACATCGGCGAGGCCAGCCGTATGATGACGATCCCGAACCAGCTCCTCATGCTGTGGACCGGATCGGCCGCGTCGAGCGACCCGGAGCTGCCCGCCACCGCCGCAGAGCTCTCCAGTGCCGCCTCCGGCGTGGTGGAGTCCGTGGGCCGTCGCCTGGCCGAGCTCGATGACCTTGCCGCCCGCTGCCAGGCCGCTCATGTCGCCGACAACTTCGCGGAGCTGAGGGAGGCCCTGGACTCCTTCACGACGGCGGCCGGTGCCGTCGCCCCGAGCTGA","MPQVTGAVHEVGVDQLFFSTTDARGVIRHSNNVFIELSRYRRDELSGAPHNIIRHPEMPGGAFKAMWDTLKAGSPFAAYVRNLAADGSEYDVFATVTPLSDGGYLSVRTRPVCSDLFDTACAIYSDARAVEDEAIHAGANRRAAAEEGLNRIAEKLAGAGLSSYEEFQNTALPAEVARREELSEGIPVRPDATGDLRVMLDSVTRIAAGLDSWMSGQQQLAELSASLKAAGKGLTRTLEDPRLNSAHISALDRSDPRVKPLADLLDLWTQMQGLVSPLVARLVDTLAQLDTNGARTRFRIALARLHTTISSLFTVELIDGVGDPQYSAQAIPDLIESLREGIAEMERQAQAHSALAAQAVAYIGEASRMMTIPNQLLMLWTGSAASSDPELPATAAELSSAASGVVESVGRRLAELDDLAARCQAAHVADNFAELREALDSFTTAAGAVAPS$","Methyl-accepting chemotaxis protein","Cytoplasm, Extracellular","methyl-accepting chemotaxis protein VCA0658","hypothetical protein","PAS fold-3 domain protein","","Hefti M.H., Francoijs K.J., De vries S.C., Dixon R., Vervoort J. The PAS fold. Eur. J. Biochem. 2004. 271(6):1198-1208. PMID: 15009198","","","

InterPro
IPR013655
Domain

PAS fold-3
PF08447	$\"[27-101]T$	PAS_3

noIPR
unintegrated

unintegrated
G3DSA:3.30.450.20	$\"[10-116]T$	no description

InterPro
IPR002657
Family

Bile acid:sodium symporter
PF01758	$\"[39-225]T$	SBF

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[38-56]?$ $\"[71-91]?$ $\"[95-115]?$ $\"[130-152]?$ $\"[158-180]?$ $\"[195-217]?$ $\"[227-247]?$ $\"[262-282]?$ $\"[292-312]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 39 to 225 (E_value = 2.6e-05) place ANA_1708 in the SBF family which is described as Sodium Bile acid symporter family.","","bile acid-Na+ symporter family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1709","1852715","1851891","825","5.27","-9.32","29957","ATGCGCTATGAGAACCCGCTCTACCTGGCCGAGGAGGTCGCCGCCCTCGACCTGCTCACCGACCAGCGCATCGCCATCGGCATCTCCCGGGGCTCACCGGAGCAGGCCCGCCGCGGCTGGGAGACCTTCGGCTATACCGGCGGCGCCGACCCGCGCGGAGCCGACGTCGCCCGTGCCCACACCGCCCAGTTCCTCGACGCCGTCCGGGGCGTCCCGCAGGCGGACCTCGACACCAGCGGTGGCATGGCACCCGGCGCGAGCTCCCGTCTGCGTATCGAGCCGCACGCCTCCGGCGTGGACCGCCGCCTGTGGTGGGGTGCCGGCTCGCGGGAGACCGCTGAGTGGACCGCCCGCCAGGGTCTGAACCTCATGAGCTCGACCCTCCTGACCGAGGCCACTGGGGAGGGCTTCTCCCACCTTCAGGCCGAGCAGATCCGCCGCTACCGCGAGGCGTGGAAGGAGGCCGGCCACGACTGGACCCCGCGCGTGAGCGTCTCGCGCTCCATCTTCCCGATCGTCTCCGAGGTGGACCGGAAGTTCTTCGCGCTGCGCGGCGAGGACTCCCGCGACCAGATCGGCGTCATCGACGGCCTGCAGTCGACCTTCGGGCGCACCTATGCCGCCGAGCCCGACGTCCTCGTCGAGCAGCTCGCCCGGGACGAGGCGCTCCATGCCGCCGACACCCTCATGCTCACCATTCCCAGCCAGCTCGGCGTCGACTTCAACCTCCACATCTTGCAGGCCTTCGCAGAGCATGTCGCCCCGGCACTGGGGTGGCAGGCCAACACCGCCGGACCGGTGACGGGCTATTCCCTGGAGGTGTAG","MRYENPLYLAEEVAALDLLTDQRIAIGISRGSPEQARRGWETFGYTGGADPRGADVARAHTAQFLDAVRGVPQADLDTSGGMAPGASSRLRIEPHASGVDRRLWWGAGSRETAEWTARQGLNLMSSTLLTEATGEGFSHLQAEQIRRYREAWKEAGHDWTPRVSVSRSIFPIVSEVDRKFFALRGEDSRDQIGVIDGLQSTFGRTYAAEPDVLVEQLARDEALHAADTLMLTIPSQLGVDFNLHILQAFAEHVAPALGWQANTAGPVTGYSLEV$","Alkanal monooxygenase","Cytoplasm","alkanal monooxygenase (bacterial liciferasealpha chain) like protein","alkanal monooxygenase alpha chain ","Coenzyme F420-dependent N5 N10-methylene tetrahydromethanopterin reductase and related flavin-dependent oxidoreductase-like","","Fisher A.J., Thompson T.B., Thoden J.B., Baldwin T.O., Rayment I. The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 1996. 271(36):21956-21968. PMID: 8703001Moore S.A., James M.N. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 1995. 249(1):195-214. PMID: 7776372Eichhorn E., Davey C.A., Sargent D.F., Leisinger T., Richmond T.J. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J. Mol. Biol. 2002. 324(3):457-468. PMID: 12445781Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J. Mol. Biol. 2000. 300(4):935-950. PMID: 10891279","","","

InterPro
IPR011251
Family

Bacterial luciferase-like
G3DSA:3.20.20.30	$\"[1-257]T$	no description

","BeTs to 3 clades of COG2141COG name: Coenzyme F420-dependent N5,N10-methylene tetrahydromethanopterin reductase and related flavin-dependent oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2141 is aom------drlb-ef--s--j----Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","monooxygenase (bacterial liciferase alpha chain) like protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1710","1854648","1852744","1905","5.26","-15.65","64728","GTGAGCGCCGCCTGCGGCTGCGACGAGCCGACGACCAGCCCCGCGGACGAGGCAGAGGAGGCAGAGCGCCCGTGGTGGCGTGATCCCGGCCTGGTCGTGCCGATCCTCTCCGGCGTCGCGTTCGGCACCGGCCTGGCGCTGGAGTGGTCGGGGCTGCACATCGCGGCGCTGGTCGCGTTCTGGGCGGGCCTGCTGCTGGGCGCGTACACGTTCGTGCCCGGTGCGATCCGGAATCTCGTTGTGAAGCGCAAGCTCGGGATCGCGCTGCTGATGACGATCAGCGCCGTGGGCGCGGTGATCCTCGGCTACGTCGAGGAGGCGGCCGCGCTGGCGTTCCTCTACTCGATCGCCGAGGCCCTGGAGGACAAGGCGATGGACCGCGCCCGCGGCGGGCTGCGCGCGCTGCTGAAGCTCGTGCCGGAGACCGCGACCGTGCTGCGCGACGGGACCTCCGCCTCGGTCCCGGCCAGGGAGATCGCCGTCGGCGACGTGCTGCTGGTCCGCCCTGGCGAGCGGGTCGCGACCGATGGGCTGGTCCGCTCGGGCCGGTCGAGCCTGGACACTTCGGCGATCACCGGTGAATCGATCCCGGTCGAGGTCGCGCCCGGAGAAGCGGTGTCGGCGGGCGCGATCAACAGCGCCGGCGTGCTGGAGGTCGAGGCGACCGCCGCGGGCACCGACAACTCGCTGACCACGATCGTGGAGCTGGTAGAGCAGGCCCAGGCCGAGAAGGGCGACCGAGCCCGGATCGCTGACCGGATCGCCCGCCCGCTGGTGCCCGGCGTGATGGTCCTCGCCGTCCTCGTCGGCGTGCTCGGGTCCCTGCTCGGCGACCCGGAGACCTGGATCACCCGCGCCCTGGTCGTCCTCGTCGCGGCCAGCCCCTGCGCGCTGGCGATCGCGGTGCCCGTCACCGTGGTCTCCGCGATCGGCGCGGCGACCAAGTTCGGCGTCGTCATCAAGAGCGGGGCCGCCTTCGAGCGCCTCGGCGGCATCCGGCACCTGGCCGTGGACAAGACCGGCACTCTGACCCGCAACCGGCCCGAGGTAACCGCCATCGTCGCCGCCCATGGGTTCGACGATGCGCAGGTGCTTGCTTGGGCTGCCGCCGTGGAGCAGCACTCGACGCACCCACTCGCCGCCGCCATCGCCGCCGCGGGCCGGGGAACCCCCGCCGCGCAGGACGTGGCCGAGGAGGCCGGGCACGGCATCGGTGGCCTGGTCGACGGCCGCAGGGTGGCGGTGGGCAGTCCGCGCTGGATCGACGCCGGTCCGCTCAAGGCCCGGGTCGAGGACCTGGAGGCCGAGGGACAGACCTGCGTGCTCGTCACCGTCGACGGCTTCCTGGCCGGGGCGATCGGCGTCCGCGACGAGCTGCGCCCCGAGGTCCCCGAGGTCGTGCGGAGCCTGCGCGACCAGGGCGTCGAGGTGAGCATGCTCACCGGCGACAACTCCCGCACCGCTGCTGCGCTGGCGAAGCTGGCCGGGATTGGCGACGTGCACGCCGAGCTGCGTCCCGAGGACAAGGCTCGCATCGTCGCCGGGTTCTCGGAGACGTCGCCGACCGCGATGATCGGCGACGGCATCAACGACGCGCCCGCCCTGGCCGGGGCGACCGTGGGCATCGCGATGGGCGCGACCGGCTCCGACGCCGCGATCGAGTCCGCCGACGTCGCCTTCACCGGCCACGACCTCGGCCTCATCCCGCAGGCTCTGCGCCACGCCCGCCGCGGCGGCAGGATCATCAACCAGAACATCGTGCTGTCCTTGGCGATCATCACTGTGCTGCTGCCGCTGGCGATCACCGGCGTGCTCGGCCTGGCAGCGGTCGTCCTCGTGCACGAGGTCGCCGAAGTCGTCGTCATCGCCAACGGACTGCGGGCTGCGCGTGCCCGCAAGCAATAG","VSAACGCDEPTTSPADEAEEAERPWWRDPGLVVPILSGVAFGTGLALEWSGLHIAALVAFWAGLLLGAYTFVPGAIRNLVVKRKLGIALLMTISAVGAVILGYVEEAAALAFLYSIAEALEDKAMDRARGGLRALLKLVPETATVLRDGTSASVPAREIAVGDVLLVRPGERVATDGLVRSGRSSLDTSAITGESIPVEVAPGEAVSAGAINSAGVLEVEATAAGTDNSLTTIVELVEQAQAEKGDRARIADRIARPLVPGVMVLAVLVGVLGSLLGDPETWITRALVVLVAASPCALAIAVPVTVVSAIGAATKFGVVIKSGAAFERLGGIRHLAVDKTGTLTRNRPEVTAIVAAHGFDDAQVLAWAAAVEQHSTHPLAAAIAAAGRGTPAAQDVAEEAGHGIGGLVDGRRVAVGSPRWIDAGPLKARVEDLEAEGQTCVLVTVDGFLAGAIGVRDELRPEVPEVVRSLRDQGVEVSMLTGDNSRTAAALAKLAGIGDVHAELRPEDKARIVAGFSETSPTAMIGDGINDAPALAGATVGIAMGATGSDAAIESADVAFTGHDLGLIPQALRHARRGGRIINQNIVLSLAIITVLLPLAITGVLGLAAVVLVHEVAEVVVIANGLRAARARKQ$","Heavy metal translocating P-type ATPase","Membrane, Cytoplasm","cadmium-translocating P-type ATPase","heavy metal translocating P-type ATPase","heavy metal translocating P-type ATPase","","Smith D.L., Tao T., Maguire M.E. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 1993. 268(30):22469-22479. PMID: 8226755Fagan M.J., Saier Jr M.H. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 1994. 38(1):57-99. PMID: 8151716","","","

InterPro
IPR001366
Family

Cadmium-transporting ATPase
PR00941	$\"[67-79]T$ $\"[122-142]T$ $\"[203-219]T$ $\"[222-236]T$	CDATPASE

InterPro
IPR001757
Family

ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
PR00119	$\"[187-201]T$ $\"[336-350]T$ $\"[451-462]T$ $\"[473-483]T$ $\"[525-544]T$ $\"[549-561]T$	CATATPASE
PTHR11939	$\"[47-633]T$	CATION-TRANSPORTING ATPASE
TIGR01494	$\"[109-354]T$ $\"[425-612]T$	ATPase_P-type: ATPase, P-type (transporting
PS00154	$\"[338-344]?$	ATPASE_E1_E2

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[332-548]T$	Hydrolase

InterPro
IPR006404
Family

Heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase
TIGR01512	$\"[87-630]T$	ATPase-IB2_Cd: cadmium-translocating P-type

InterPro
IPR006416
Family

Heavy metal translocating P-type ATPase
TIGR01525	$\"[87-628]T$	ATPase-IB_hvy: heavy metal translocating P-

InterPro
IPR008250
Domain

E1-E2 ATPase-associated region
PF00122	$\"[109-328]T$	E1-E2_ATPase

noIPR
unintegrated

unintegrated
G3DSA:2.70.150.10	$\"[41-205]T$	no description
G3DSA:3.40.50.1000	$\"[446-570]T$	no description
PTHR11939:SF31	$\"[47-633]T$	HEAVY METAL CATION TRANSPORT ATPASE (CADMIUM/ZINC TRANSPORTING ATPASE)
tmhmm	$\"[30-50]?$ $\"[56-76]?$ $\"[86-104]?$ $\"[257-277]?$ $\"[287-307]?$ $\"[589-623]?$	transmembrane_regions

","BeTs to 23 clades of COG2217COG name: Cation transport ATPasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2217 is aompkzyqvdrlbcefgh-nuj-itwNumber of proteins in this genome belonging to this COG is 4","***** IPB008250 (E1-E2 ATPase-associated region) with a combined E-value of 4.2e-38. IPB008250A 336-346 IPB008250B 457-497 IPB008250C 522-545***** IPB006068 (Cation transporting ATPase, C-terminal) with a combined E-value of 1.8e-30. IPB006068B 154-194 IPB006068E 315-341 IPB006068H 457-498 IPB006068J 543-594***** IPB000695 (H+-transporting ATPase (proton pump) signature) with a combined E-value of 4.8e-18. IPB000695B 498-514 IPB000695C 525-541 IPB000695D 557-582***** IPB001757 (ATPase, E1-E2 type) with a combined E-value of 4e-17. IPB001757A 336-346 IPB001757B 522-544***** IPB001366 (Cadmium-transporting ATPase signature) with a combined E-value of 2.7e-14. IPB001366F 122-142 IPB001366G 142-158 IPB001366H 203-219","","","-54% similar to PDB:2B8E CopA ATP Binding Domain (E_value = 1.5E_32);-66% similar to PDB:2HC8 Structure of the A. fulgidus CopA A-domain (E_value = 1.0E_20);-42% similar to PDB:1MHS Model of Neurospora crassa proton ATPase (E_value = 7.2E_14);-45% similar to PDB:1IWO Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+ (E_value = 5.7E_11);-45% similar to PDB:1KJU Ca2+-ATPase in the E2 State (E_value = 5.7E_11);","Residues 109 to 328 (E_value = 3.6e-69) place ANA_1710 in the E1-E2_ATPase family which is described as E1-E2 ATPase.Residues 332 to 548 (E_value = 1.3e-28) place ANA_1710 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","P-type ATPase (cadA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1711","1855013","1854645","369","5.42","-3.52","12772","ATGCTGACCATTGCTTCGCGTCTTGACGTCATGAACCGGCTCGGCCGGGCCATGGCCGACCCGACACGCTCCCGCATCCTGATGTCCCTGCTCGACAGCCCGAGCCACCCCGCGGTGCTCTCGCGCGAGCTGGGGCTGACCCGCTCGAACGTGTCCAACCACCTGACCTGCCTGCGCGACTGCGGGATCGTGGTCGCCGAGCCCGAGGGCCGCCAGACTCGCTACGAGATCGCCGACCCGCACCTGGCCGCGGCGCTGACGGCACTGGTCGATGTGACCCTCGCCGTGGACGAGAGCGCGCCGTGCATCGACCCGGCCTGCTCGGTGCCGGGCTGCTGCGCCGCGAGCAGTTCGGGGGACGCCTCGTGA","MLTIASRLDVMNRLGRAMADPTRSRILMSLLDSPSHPAVLSRELGLTRSNVSNHLTCLRDCGIVVAEPEGRQTRYEIADPHLAAALTALVDVTLAVDESAPCIDPACSVPGCCAASSSGDAS$","Transcriptional regulator, ArsR family","Cytoplasm, Periplasm","Predicted transcriptional regulators","probable transcriptional regulatory protein","regulatory protein, ArsR","","Morby A.P., Turner J.S., Huckle J.W., Robinson N.J. SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 1993. 21(4):921-925. PMID: 8451191Bairoch A. A possible mechanism for metal-ion induced DNA-protein dissociation in a family of prokaryotic transcriptional regulators. Nucleic Acids Res. 1993. 21(10):2515-2515. PMID: 8506147Eicken C., Pennella M.A., Chen X., Koshlap K.M., VanZile M.L., Sacchettini J.C., Giedroc D.P. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins. J. Mol. Biol. 2003. 333(4):683-695. PMID: 14568530Cook W.J., Kar S.R., Taylor K.B., Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J. Mol. Biol. 1998. 275(2):337-346. PMID: 9466913Busenlehner L.S., Pennella M.A., Giedroc D.P. The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 2003. 27(2):131-143. PMID: 12829264Liu T., Nakashima S., Hirose K., Shibasaka M., Katsuhara M., Ezaki B., Giedroc D.P., Kasamo K. A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPx-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II). J. Biol. Chem. 2004. 279(17):17810-17818. PMID: 14960585","","","

InterPro
IPR001845
Domain

Bacterial regulatory protein, ArsR
PR00778	$\"[15-30]T$ $\"[47-62]T$ $\"[62-77]T$	HTHARSR
PF01022	$\"[20-66]T$	HTH_5
SM00418	$\"[13-91]T$	HTH_ARSR
PS50987	$\"[4-97]T$	HTH_ARSR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[1-97]T$	no description

","BeTs to 15 clades of COG0640COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0640 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB001845 (Bacterial regulatory protein, ArsR family) with a combined E-value of 4.7e-12. IPB001845 33-77","","","No significant hits to the PDB database (E-value < E-10).","Residues 20 to 66 (E_value = 8e-13) place ANA_1711 in the HTH_5 family which is described as Bacterial regulatory protein, arsR family.","","transcriptional regulators (merR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1712","1855557","1855102","456","10.10","5.90","16051","GTGAGCCAGGTCGGCGGCGCGGTCCAGCGGATCGAGAAGCGCACCGAGGAACGGGTCGAGAAGGCTGTCGAGCAGGTCGCCGGGGAGGCTTCGGCCACGATGACCGCGAGCCTCGACGCCTCGAACGCGCGGGCGGAGCGGATCATCGCCGCAACGGCGAAGCTGGAGGCGCGACAGCTCTGGTCCGCCGCCGCCGCGATGTGCCTCGTTCTCCTGCCGGTGGCCGTGGTCGTCGCCGGTCTCTGGATGGGCATCGCCGGGCTCATCACGGGTGTTCAGTGGGCGCTGGACGTGGACGGGAGCGTGTGGCTCGGCATCGGCCGGTGGCTCGTGGTCGGCGCTGGCCTCGCCGGGGCCGGCTACGGGCTCTTCGCGTCCGTCCGCTGGGTTGCGGGTCTCGTGGAGACCTGGAAGGGCCGCGGGATGCCGAAGTGGCCCCGCTGGCGCAAGAGGTGA","VSQVGGAVQRIEKRTEERVEKAVEQVAGEASATMTASLDASNARAERIIAATAKLEARQLWSAAAAMCLVLLPVAVVVAGLWMGIAGLITGVQWALDVDGSVWLGIGRWLVVGAGLAGAGYGLFASVRWVAGLVETWKGRGMPKWPRWRKR$","Methyl-accepting chemotaxis protein","Membrane, Cytoplasm","extracellular protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-79]?$	signal-peptide
tmhmm	$\"[68-90]?$ $\"[109-131]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","Wed Aug 15 14:38:27 2007","","Wed Aug 15 14:38:27 2007","","","Wed Aug 15 14:38:27 2007","Wed Aug 15 14:38:27 2007","Wed Aug 15 14:38:27 2007","","","","","","Wed Aug 15 14:38:27 2007","","","","Wed Aug 15 14:38:27 2007","Wed Aug 15 14:38:27 2007","","","","","yes","","" "ANA_1713","1856881","1855595","1287","7.18","1.35","48217","ATGAGCACCACGCACTACAGCCCGAGCGCCAGCGCCGCCGACACGGAGCGCTATATCCGTGGCAAGGAGGACGAGCGGGGCATCGCGATCACGTGCGATGTGCCGGGAGGCCCCGGCGCGTTCTCGGCGCGCGCTCGGTCGCTCACGCAGAACACGACGCGCGAGGTCGAGGCGGTGCATTACCGCCAGTCGTTCAGCGACGAGGAGTTCGACCCGAAGAGTCCGGAGGACGTGCAGCGGGTGAACGATCTCGGCTATCAGCTCGCGAAGAAGATGCACCCGGATTCCGACTGCCTCGTAGTCAGTCATGTGGATGGGCGGGGCAAGAAGCCGCACAACCACATCTTGGTCATCAACCACAACAACCGGACGGGGAAGGCGCTCTCGGACTATCGCACGTTCCACGACCGCAAGGCCGGGAATCAGCGGGGCGTCCAGTCGGCGAACGACCAGCTGATGCGAGAACACGGGCTCTCGGTCGTGAAGCGGCTGGAGCACGCACCGAAGGACTGGGAGCTGCGCCGCGAGGACTTCGCCGAGGGATCGCTCGACCGCGAGATGGGCGACCGGATGAGCGCGGCGCTGGCCGATCCCCGGGCGGTGGACAAGGCCGGTCTGGTCTCGGTGATCGAGGAGCAGAACCAGCGGCTCGGCGATGACGGGGAGCGGGTGCCGCGGATGCGGTTGCACAGCCCCGTCAGCAAGAAGGGCAAGCGCGCCGGGCAAGAGACCTGGACGCTCTACATCGAGGATCGCCGCGGCGAGTCCGGCCGCGCTGAGCGCCGCAAGCGCGCGAGCGCCCTCTCGGCGGACTTCACCCCGGAGGGCGCGCAGGCGTTCTTCGACTACCACCAGCAGCAGAAGGAGAAGGAACATGAGCGCAGCGCTCGACAGGCTGAAGCAGTAGAACGAGCCCGAGCAGTCGCAGCAGCAGCTCGGCAGTCCGGAGACGATGGAGCTGTTGACCTCGATCCTCGCCGCCGTCGAGGCGCAGAACACGAGGATCGCCACGCTGACCGAACAGCAGAAGAAGCTCGCGGGGTTCGTGAAGGTCATGGACGAGGAGACGACGAGGCGGCTGGAGCGGATCACGGCCCCGGCGTCGACCTCCTCGCCCTCCAGCGACGTGTCCGCGAGGATCGCGAGTATCGAGAGCAGGCAGAACGAGATCGCGAGCACGCTCGGCGAGTTCGCGCAGAGTCTCAACGGCGAGAGCTTGAACGCCGCTTCGCGGAGCTTGGTCGCGGAGGCGCAGAAGAATCGCGCGGCTACGGCCTCGGCGATTGA","MSTTHYSPSASAADTERYIRGKEDERGIAITCDVPGGPGAFSARARSLTQNTTREVEAVHYRQSFSDEEFDPKSPEDVQRVNDLGYQLAKKMHPDSDCLVVSHVDGRGKKPHNHILVINHNNRTGKALSDYRTFHDRKAGNQRGVQSANDQLMREHGLSVVKRLEHAPKDWELRREDFAEGSLDREMGDRMSAALADPRAVDKAGLVSVIEEQNQRLGDDGERVPRMRLHSPVSKKGKRAGQETWTLYIEDRRGESGRAERRKRASALSADFTPEGAQAFFDYHQQQKEKEHERSARQAEAVERARAVAAAARQSGDDGAVDLDPRRRRGAEHEDRHADRTAEEARGVREGHGRGDDEAAGADHGPGVDLLALQRRVREDREYREQAERDREHARRVRAESQRRELERRFAELGRGGAEESRGYGLGD$","Relaxase/mobilization nuclease family protein","Cytoplasm, Extracellular","Octapeptide-repeat protein","hypothetical protein","Relaxase/mobilization nuclease family protein","","Byrd D.R., Matson S.W. Nicking by transesterification: the reaction catalysed by a relaxase. Mol. Microbiol. 1997. 25(6):1011-1022. PMID: 9350859","","","

InterPro
IPR005094
Family

Relaxase/mobilization nuclease
PF03432	$\"[8-256]T$	Relaxase

","BeTs to 3 clades of COG1157COG name: Flagellar biosynthesis/type III secretory pathway ATPaseFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG1157 is -------qv---b-efg---uj-it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 256 (E_value = 1.4e-06) place ANA_1713 in the Relaxase family which is described as Relaxase/Mobilisation nuclease domain.","","protein (C0699)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1714","1857393","1856878","516","6.95","-0.10","18226","ATGAGCGCCAGCGAAATGTCCGACACGGCTACTGCTTGCCACTCTGGCGTACAGGTGGAGCAGCAGACCGACTCCCAGGTGAACACCGGTCGGGCTGATGCGGAGGCTGTGCGTCAGAGTCACGGCGGCGCGAAGCGTCGTCGTGGGGGCCGCGCGAAGCTCGATACCGACTTCGGAGAGGAGACGCTCGCGGCGCTTCGCACTCGTGCGAAGCGGCTCGGGCTGGCTCCGAGCACGTGGGTGCGGACCGTCGTCCGGGATGCCCTCCACGCCTCTCGGAGCGAGGAGTTGGACGCCGCCGTGGCCGCGCACCTGCTCGGGGTCGAGGCGCGGGTGCAGGCGTCGGCGGATGCTCGCGAGCTGGCCGCGCAGATTCGCCCGCTGGCGATCAACGTCAACGACCTCGACCGCCGGGCGCGGGCTGGTGAGTCAGTGGCGCTGTCGGCGGAGGTGCCCGAGCTGATCGAGTTGCTGCGCGAGGTCCGCGCCCTGCTCGGGGATCGGGCGGCCTCATGA","MSASEMSDTATACHSGVQVEQQTDSQVNTGRADAEAVRQSHGGAKRRRGGRAKLDTDFGEETLAALRTRAKRLGLAPSTWVRTVVRDALHASRSEELDAAVAAHLLGVEARVQASADARELAAQIRPLAINVNDLDRRARAGESVALSAEVPELIELLREVRALLGDRAAS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1715","1858877","1857465","1413","5.91","-10.42","52577","GTGGCTAAGCAGGAGAACAACCCGACGAGCATCGGGCTCACGCAGTACCTCGATCCGTCGTACTGGACCTGGGCTGCCGAGGACCCGAACGGGGCCGCGCTGCTCCAGCAGGGAGCCGAAGCGATCCTCGCCTACGTGGTGCAGCGGCTCGAGGCCACCGGCTGCGAGGTCGTCGAGGCCTACGGCATCGTGCATGACAAGGACGAGCGCGAGGTCTGGAGCGACACGGAGAAGGCTCTGGTGATCGAGCCGAAGCCCGATCACCTGCACGCGGTCATCAAGTTCGCCAGCCGTGCGAAGAGCGCACCGCTGGATCGGCTCGCGTTCGGCATCGGCGTCGAGCCCCAGTACGTCGAGAAGCCGGGCCGCGGGCGGTACGCCTACGACAACATGCTGTCGTATCTGACGCACGTGAAGTACGCGGACAAGCACCAATACGCGCCTTCGGAGGTCGCTACGGTGCGTGGGCCTGACTACCTCGGGATCGACGCCCAGCGTCGGGAGACCTGGCTCAAGGGGCGCGCGCACGTGAAGAAGAAGGTCGTCGCCGAGAACTTCGAGGACATGCGCGAGCGCGTGCTCCAGGGCGAGTTCACGCGGGATCAGATCATGCTCACGGACGAGCTGTTCGACATCTACTCGCGGCATCAGCGGGAGATCGACGACGCGCTGTCGGCCTACGGCCAGCGCCGCGCATACCGGGCGGCGGCGAAGCTCCGCGCCGGTGAGTTCTCGACGCACGTGGTGTTCGTCCATGGGGATGCCGGGATCGGCAAGACCCGGTTCGCCACGGACTTCATCACCGAGGCGATCAACGCGGCGAACGCGCACGGCGAGCGGTGGCAGGTCTACCGGGCCGCGACGGGGAACCCGCTTGATGACTGGCGAGGCGAGGAGGTGCTGCTGCTGGACGATCTGCGGGCCTCGGCGATGGATGCGAACGACTGGCTGCTGCTGCTTGATCCGTACAACGCCTCGCCTGCGAAGGCTCGGTACAAGAACAAGGGCGAGGTGGCCCCGCGCCTTATCGTCATCACGGCGACGATCGAGCCTGTCGAGTTCTTCTACTACGCCCGCCAGAAGGGCAACGTGGACGAGGCGTTGGACCAGTTCATCCGCCGCTTGGCCTCGGTCGTGAAGGTCTATCGTGCCGACGACATCAATCGTTACCTCGTGCAGCACATTGGGAAGATCGAGCCCTACGAGTGGCACCAGTGCAGCATCCCGACCGCCGCACACACGCCCGGCATGTACGGCAACGCGTATCACCAGAACGTCGGGTCGCGGGAGCTGACCTACGGTCCGGAGACCTCGGCGGAACATGACGCTGAGGGCGCGGTTGCTGAGCTGCTGGGCGGGCTCGCGGTGCGGAGCCCTGACGTGCCGCTGGCGCTGATCGGAGGTGCCGCATGA","VAKQENNPTSIGLTQYLDPSYWTWAAEDPNGAALLQQGAEAILAYVVQRLEATGCEVVEAYGIVHDKDEREVWSDTEKALVIEPKPDHLHAVIKFASRAKSAPLDRLAFGIGVEPQYVEKPGRGRYAYDNMLSYLTHVKYADKHQYAPSEVATVRGPDYLGIDAQRRETWLKGRAHVKKKVVAENFEDMRERVLQGEFTRDQIMLTDELFDIYSRHQREIDDALSAYGQRRAYRAAAKLRAGEFSTHVVFVHGDAGIGKTRFATDFITEAINAANAHGERWQVYRAATGNPLDDWRGEEVLLLDDLRASAMDANDWLLLLDPYNASPAKARYKNKGEVAPRLIVITATIEPVEFFYYARQKGNVDEALDQFIRRLASVVKVYRADDINRYLVQHIGKIEPYEWHQCSIPTAAHTPGMYGNAYHQNVGSRELTYGPETSAEHDAEGAVAELLGGLAVRSPDVPLALIGGAA$","Hypothetical protein","Cytoplasm","hypothetical protein","replication protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","Wed Aug 15 14:53:20 2007","","Wed Aug 15 14:53:20 2007","","","Wed Aug 15 14:53:20 2007","Wed Aug 15 14:53:20 2007","Wed Aug 15 14:53:20 2007","","","","","","Wed Aug 15 14:53:20 2007","","","","Wed Aug 15 14:53:20 2007","Wed Aug 15 14:53:20 2007","","","","","yes","","" "ANA_1715.1","1859370","1859158","213","11.15","2.16","7022","ATGTCTGTCGTTATCGACGTTCCCCGCGCATCCGCGCTCGACCGCCCTGGCCTCGATCAGGGCTCCACTCCTTCTCCGCAGGCAGACGGCCTCGATCCCGTCATCGCCGCCGCTCGCGCTGCTGGTCGTCTGGCCGGTGAACGCCTGGCTCGCACGCCCCTGACCCCGCGACAGCGCGCCGCGGTCGCCGCCGTGATGGGCGGTGGTCACTGA","MSVVIDVPRASALDRPGLDQGSTPSPQADGLDPVIAAARAAGRLAGERLARTPLTPRQRAAVAAVMGGGH$","Hypothetical protein","Cytoplasm, Extracellular","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 15:00:12 2007","Wed Aug 15 15:00:12 2007","Wed Aug 15 15:00:12 2007","Wed Aug 15 14:59:17 2007","","","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","Wed Aug 15 14:59:17 2007","","Wed Aug 15 14:59:17 2007","","Wed Aug 15 14:59:17 2007","yes","","" "ANA_1716","1860001","1859552","450","4.65","-15.29","16794","ATGGAGGACGCAGGCGATCAGGCCCCGGTGGTCGTGCACGACCTCGTGATGCCACAGGAGGACGATGGGCCGGATCGCGAGGAGCTGCTGACGGAGCGGAACGCCCTGGTCGATCGGGTGAAGGAGCTGAGCCCGCTGCTGCGCGACATCCATCAGCCGGTCCTGGAGATAACGGCAGCGATCAACGACGTGAAGGCCCGCATCGACGAGATCGACGCGGAGCTGCTCGACCGTTCGGTGTCGGCGGCGGCGAAGCTGCTCGCGGACGTCGAGGAGCCGGTCGGCACCGCGGAGCGCCGCGAGGTGGTCGAGGCGAAGTGGAAGGTGTTGGACGTGGACCGCCGCCGGATGCTCGTGGACGAGCTGGTGACGGTGACCATCGAGCCCATCACGCCCGGTCACGTGAAATTCGACCCCGACCTGATTCGGATAGAGCCGCGTCGCGACTGA","MEDAGDQAPVVVHDLVMPQEDDGPDREELLTERNALVDRVKELSPLLRDIHQPVLEITAAINDVKARIDEIDAELLDRSVSAAAKLLADVEEPVGTAERREVVEAKWKVLDVDRRRMLVDELVTVTIEPITPGHVKFDPDLIRIEPRRD$","Site-specific recombinases, DNA invertase Pin homolog","Cytoplasm","homologous to Saccharopolyspora erythraeabeta-ketoacyl synthase","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","to Saccharopolyspora erythraea beta-ketoacyl synthase","","1","","","Sun Jul 15 22:53:48 2007","Sun Jul 15 22:53:48 2007","Sun Jul 15 22:53:48 2007","","","Sun Jul 15 22:53:48 2007","Sun Jul 15 22:53:48 2007","Sun Jul 15 22:53:48 2007","Sun Jul 15 22:55:13 2007","","","","","Sun Jul 15 22:53:48 2007","","","","Sun Jul 15 22:53:48 2007","Sun Jul 15 22:53:48 2007","","","","","yes","","" "ANA_1717","1861117","1860050","1068","5.78","-8.35","38551","ATGAAAGCATTCGGGTTCCTCAGCTTCGGACACTACGGACACGGTCGCGGCCCTGGCGACCCCGACGCCCGCCAGGCGCTCAAGGAGGCCGTCGAGATCGCCGTCGGCGCTGACGAGATCGGTGTCAACGGCGCCTACTGGCGCGTCCACCACTACACCCGCCAGGCCGCCGCGCCCATCCCGCTGCTCTCCGCGGCCGGCGCCCGTACCCGGCGCATCGAGGTCGGCACCGGCGTCATCGACATGCGCTATGAGAACCCGCTCTACCTGGCTGAGGAGGTCGCTGCCCTCGACCTGCTCACCGACCAGCGCATTGCCATCGGCATCTCCCGGGGCTCGCCGGAGCAGGCCCTCCGTGGCTGGGAGACCTTCGGCTATACCGGCGGCGTCGACCCGCGCGGAGTCGACGTCGCCCGTGCCCACACCGCCCAGTTCCTCGACGCCGTCCGGGGCGTCCCGCAGGCGGACCTCGACACCAGCGGTGGCATGGCACCCGGCGCGAGCTCCCGTCTGCGTATCGAGCCGCACGCCTCCGGCGTGGACCGCCGCCTGTGGTGGGGTGCCGGCTCGCGGGAGACCGCTGAGTGGACCGCCCGCCAGGGTCTGAACCTCATGAGCTCGACCCTCCTGACCGAGGCCACTGGGGAGGGCTTCTCCCACCTTCAGGCCGAGCAGATCCGCCGCTACCGCGAGGCGTGGAAGGAGGCCGGCCACGACTGGACCCCGCGCGTGAGCGTCTCGCGCTCCATCTTCCCGATCGTCTCCGAGGTGGACCGGAAGTTCTTCGCGCTGCGCGGCGAGGACTCCCGCGACCAGATCGGCGTCATCGACGGCCTGCAGTCGACCTTCGGGCGCACCTATGCCGCCGAGCCCGACGTCCTCGTCGAGCAGCTCGCCCGGGACGAGGCGCTCCATGCCGCCGACACCCTCATGCTCACCATTCCCAGCCAGCTCGGCGTCGACTTCAACCTCCACATCTTGCAGGCCTTCGCCGAGCACGTCGCCCCGGCACTGGGGTGGCAGCCCAACACCGCCGGACCGGTGACGGGCTACTCCCTGGAGGCGTAG","MKAFGFLSFGHYGHGRGPGDPDARQALKEAVEIAVGADEIGVNGAYWRVHHYTRQAAAPIPLLSAAGARTRRIEVGTGVIDMRYENPLYLAEEVAALDLLTDQRIAIGISRGSPEQALRGWETFGYTGGVDPRGVDVARAHTAQFLDAVRGVPQADLDTSGGMAPGASSRLRIEPHASGVDRRLWWGAGSRETAEWTARQGLNLMSSTLLTEATGEGFSHLQAEQIRRYREAWKEAGHDWTPRVSVSRSIFPIVSEVDRKFFALRGEDSRDQIGVIDGLQSTFGRTYAAEPDVLVEQLARDEALHAADTLMLTIPSQLGVDFNLHILQAFAEHVAPALGWQPNTAGPVTGYSLEA$","Alkanal monooxygenase","Cytoplasm","alkanal monooxygenase (bacterial liciferasealpha chain) like protein","alkanal monooxygenase alpha chain ","luciferase family protein","","Fisher A.J., Thompson T.B., Thoden J.B., Baldwin T.O., Rayment I. The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 1996. 271(36):21956-21968. PMID: 8703001Moore S.A., James M.N. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 1995. 249(1):195-214. PMID: 7776372Eichhorn E., Davey C.A., Sargent D.F., Leisinger T., Richmond T.J. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J. Mol. Biol. 2002. 324(3):457-468. PMID: 12445781Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J. Mol. Biol. 2000. 300(4):935-950. PMID: 10891279","","","

InterPro
IPR011251
Family

Bacterial luciferase-like
G3DSA:3.20.20.30	$\"[7-338]T$	no description
PF00296	$\"[7-338]T$	Bac_luciferase

noIPR
unintegrated

unintegrated
PTHR12714	$\"[61-156]T$	PROTEIN-S ISOPRENYLCYSTEINE O-METHYLTRANSFERASE
signalp	$\"[1-22]?$	signal-peptide

","BeTs to 7 clades of COG2020COG name: Putative protein-S-isoprenylcysteine methyltransferaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG2020 is a---kzy---r--c--gh---j----Number of proteins in this genome belonging to this COG is 1","***** IPB007269 (Isoprenylcysteine carboxyl methyltransferase) with a combined E-value of 4.2e-21. IPB007269B 61-107 IPB007269C 109-152","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","to protein-S-isoprenylcysteine O-methyltransferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1719","1863409","1861718","1692","5.88","-3.89","59187","TTGCCCTCAACCGACAAGGCCACACCTATGACTCAACGCACTTCGACGCCGGCCTCCGCCGGCACCGCCCTCCATGAACCGGGGGCGGAGTTCCACCCCGACCGCCGCTTCTGGGCCGTCTACGCCTCGCTCCTGATCGTCATGTTCCTGTCCGCCATGGACCAGACGATCGTCGGCACGGCCCTGCCCACCATCGTGGGCGATCTCGGCGGCGCCGCCCACATGGCCTGGATCCTGACCGCCTACACCCTGGCCATCACTGTGGCCATGCCGGTCTACGGCAAGCTCGGCGACCTCGTGGGACGCAAGAACCTCTTCCTGGTGGCCATCGCCCTGTTCCTGATCGGCTCAGCCCTGTGCGGCACCGCCGACTCCATGACCCAGCTCATCATCTACCGCTTCATTCAGGGGCTGGGTGGCGGCGGCCTCATGATCTCCTCCCAGGCGATCACCGGCGACCTCATCCCGCCGCGCGTGCGCGGCACCTACATGGCCCCCATGGGAGCCATGTTCGGCATCGCCTCCATCCTGGGACCCATCATCGGTGGCTGGCTCACCGACTCGGTCTCCTGGCGCTGGACCTTCTGGATCAACCTGCCGCTGGGCGTCCTGGCCTTCATCGCCATCTTCCTGGTGCTGCGCCTGCCCAGCAGTCGCCTGACCAGCCCCATTGACTGGTGGGGGCTCGGGCTCATGAACGCCGGCGCCATCGCCATCGTCCTCATGGCCACCTGGGGCGGCAACCAGTACGAGTGGACCAGCCCGGTCATCATCGGCCTGGGCGTGGTCGGTCTGGTCTGCTGGGGGCTGTTCGGCTTCGTCGAGACGCGCGCCATCGACCCCATCCTGCCCTGGTCGATCCTCACCAGCCGCACCTTCATCGTCTCCACGCTCGTCGGCATGCTCGCGATGGGCGGCATGATCGGCGTGCTGAGCTACCTGCCCACCTACCTCCAGATGGTCTACGGCTACTCGGCCACCACCTCCGGCCTGCTCCTGGTGCCCATCACCATCGGGATGCTCATCTCCTCGATCCTCTCCGGTGTGCTCGTCTCGCGCACCGACCGCTACAAGATCTACCCGGTCGCGGGACCCCTGGTTGCCGCTGGCGCCGCCTTCTGGCTCTCCCGCCTGTCGACGACGTCGCCCGTCTGGCAGATCTCCGCGGCCACCTTCCTCATGGGGGCGGGTATCGGGCTGTTCTTCCAGCTCCTGGTCACCGTGGTGCAGAACGCTCTGCCGGCCAAGCACCTGGGCACGGCCACCAGCGGCAACAACTTCTTCCGCGAGGTCGGCGTCTCCCTGGGCGCCTCGCTCATCGGTGCGGCCTTCTCCTCCGGCCTGACCTCCAACCTCGCGGATCGGATCGGGGCGCTGGCCCGCAGCGCGGACCCGTCCGTCCTGGGGGCGCTGGCCCAGTTCAAGGACGCCGACACCTCCTCGCTCACGCCCGCCCTGGTCAACCAGCTGCCCACCGCCCTGCACGACGCCGTGGCCGGCTCCTACGCTGACGCCCTCCTGCCGATCTTCGGCTGGATGATCCCGCTGTTCGTGGCGACCTCCGTCGTCGCCCTCTTCCTGCCCGAGGTGCCCCTGTCCCAGAAGACCGCCATGGAGCAGGTCGCCGAGGCCGAGGGTGCTGCCGAGGCTGAGGGCAGCGAGCCGACGGCGTTGCGGGATGAGGCGCAGTAG","LPSTDKATPMTQRTSTPASAGTALHEPGAEFHPDRRFWAVYASLLIVMFLSAMDQTIVGTALPTIVGDLGGAAHMAWILTAYTLAITVAMPVYGKLGDLVGRKNLFLVAIALFLIGSALCGTADSMTQLIIYRFIQGLGGGGLMISSQAITGDLIPPRVRGTYMAPMGAMFGIASILGPIIGGWLTDSVSWRWTFWINLPLGVLAFIAIFLVLRLPSSRLTSPIDWWGLGLMNAGAIAIVLMATWGGNQYEWTSPVIIGLGVVGLVCWGLFGFVETRAIDPILPWSILTSRTFIVSTLVGMLAMGGMIGVLSYLPTYLQMVYGYSATTSGLLLVPITIGMLISSILSGVLVSRTDRYKIYPVAGPLVAAGAAFWLSRLSTTSPVWQISAATFLMGAGIGLFFQLLVTVVQNALPAKHLGTATSGNNFFREVGVSLGASLIGAAFSSGLTSNLADRIGALARSADPSVLGALAQFKDADTSSLTPALVNQLPTALHDAVAGSYADALLPIFGWMIPLFVATSVVALFLPEVPLSQKTAMEQVAEAEGAAEAEGSEPTALRDEAQ$","Permease of the major facilitator superfamily","Membrane, Cytoplasm","Permeases of the major facilitator superfamily","permease of the major facilitator superfamily","drug resistance transporter, EmrB/QacA subfamily","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR001411
Family

Tetracycline resistance protein TetB
PR01036	$\"[43-67]T$ $\"[133-153]T$ $\"[293-318]T$ $\"[328-352]T$ $\"[427-446]T$	TCRTETB

InterPro
IPR004638
Family

Drug resistance transporter EmrB/QacA subfamily
TIGR00711	$\"[38-527]T$	efflux_EmrB: drug resistance MFS transporte

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[40-481]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[44-445]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[3-228]T$ $\"[277-447]T$ $\"[505-563]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57	$\"[3-228]T$ $\"[277-447]T$ $\"[505-563]T$	DRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
tmhmm	$\"[37-57]?$ $\"[76-94]?$ $\"[104-122]?$ $\"[132-150]?$ $\"[165-185]?$ $\"[191-213]?$ $\"[228-248]?$ $\"[254-272]?$ $\"[293-313]?$ $\"[332-352]?$ $\"[357-377]?$ $\"[383-405]?$ $\"[482-502]?$ $\"[508-528]?$	transmembrane_regions

","BeTs to 22 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","***** IPB001958 (Tetracycline resistance protein signature) with a combined E-value of 1.6e-09. IPB001958B 75-94 IPB001958C 106-130 IPB001958E 164-186","","","-48% similar to PDB:2GFP Structure of the Multidrug Transporter EmrD from Escherichia coli (E_value = 5.5E_10);","Residues 44 to 445 (E_value = 5.8e-63) place ANA_1719 in the MFS_1 family which is described as Major Facilitator Superfamily.Residues 94 to 142 (E_value = 3.1e-08) place ANA_1719 in the Sugar_tr family which is described as Sugar (and other) transporter.","","of the major facilitator superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1720","1864146","1863442","705","5.16","-8.87","25158","GTGACCGGAACCGACCTGCGCGCCACCCAAGCGCAACGCACCCGCGCTGCCATCCGGGCCGCCGCTCTCACCCTGACCCGGGAGCGCGGCTATGCCGCGATGACGGTGGATGACGTCGCCGCCCTCGCCGGAGTCTCCCGGCGCACTGTCTTCAACCACTTCGCCTCCAAGGCCGACCTCCTCGTCGTGGGCCTGGAGCCCCCGGCGCCCGAGGTTGTCGAGGCCTTCGTCGACGGCTCCGGAAGCCTCCTGGAGGACCTCGGTACCCTGCTCGCCTCCGGTGCGGAGACTGTCGAGTCCGAGCGCGGCTGGCTCCTGTCCTTCCCGGAGATCGTGCGGGACAACCCCGAGGTGGAGCGCGCCGTCCACGAGCGGCTGCGCATCGTCGCCCAGTCCCTGGCGGAGGCCGCCGGCCGCCGTCTGGGAGCCGAGCCCGACGACCCGCGCACCCGCGCCGTCGTCGCCCTGGCCATGGCCATCCAACGCAGCTCCCTGGATCTGTGGTGTGGGCGCTCCCACCCCTGGGAGGAACGCCGCGAGGTGGCGGCGCGCACCGAGCTCACCGAGCTCACCGAGCCCGCCGGGGCCTCCGAGAGCCCCGAGGTCTCAGGCCAGTGCCCCCAGTCCCACTTGGTCGACGCCGTTCGCACCATGGTCGAGGCGATCTCCGAGGTCGTCTCCCCACCCCATCCTTCTCGCAACTGA","VTGTDLRATQAQRTRAAIRAAALTLTRERGYAAMTVDDVAALAGVSRRTVFNHFASKADLLVVGLEPPAPEVVEAFVDGSGSLLEDLGTLLASGAETVESERGWLLSFPEIVRDNPEVERAVHERLRIVAQSLAEAAGRRLGAEPDDPRTRAVVALAMAIQRSSLDLWCGRSHPWEERREVAARTELTELTEPAGASESPEVSGQCPQSHLVDAVRTMVEAISEVVSPPHPSRN$","Transcriptional regulator, TetR family","Cytoplasm","CalR1","transcriptional regulator; TetR family protein","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[18-31]T$ $\"[39-62]T$	HTHTETR
PF00440	$\"[18-61]T$	TetR_N
PS50977	$\"[12-72]T$	HTH_TETR_2
PS01081	$\"[30-61]T$	HTH_TETR_1

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[5-62]T$	no description

InterPro
IPR003500
Family

Ribose/galactose isomerase
PIRSF005384	$\"[1-148]T$	Sugar-phosphate isomerase, RpiB/LacA/LacB types
PF02502	$\"[2-141]T$	LacAB_rpiB
TIGR00689	$\"[3-146]T$	rpiB_lacA_lacB: sugar-phosphate isomerases,

noIPR
unintegrated

unintegrated
G3DSA:3.40.1400.10	$\"[1-145]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide

","BeTs to 4 clades of COG3315COG name: O-Methyltransferase involved in polyketide biosynthesisFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG3315 is ----------r-b--fgh---j----Number of proteins in this genome belonging to this COG is 2","***** IPB003455 (Protein of unknown function DUF142) with a combined E-value of 9.8e-11. IPB003455A 4-38 IPB003455B 83-116 IPB003455C 146-159 IPB003455D 168-201","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1723","1866474","1866025","450","5.26","-4.39","15661","ATGCGAATCGCCATCGGTGCCCCGGGCAATGGAGCCCTCCTGAAGGACGCTCTTGCGGAACGACTGGCCGAGGACGGGCGCGTGAGCGACGTCCTCGACCTGTCCACGCCGGAGATCACCTACCCGGAGGTCTCCTTCCAGGTCGCCCGGGCAGTCGCCGAGGGGCGGGTCGACCGGGGGCTTCTCATCTGCGGCACCGGCGTGGGAACGGCCATCGCGGCCAACAAGGTGCCGGGGGTGCGTGCGGCGACCGCGCACGACCTGCTCACCGTGCGCGGCTCGGTGGAGAACTACGACGCCCAGGTCCTGTGCATGGGACAGAACGTCATCGCGGCCCCCGCCGCCTGGGCGCTCATCGACATCTGGCTCGACCTGCGCCACGACCCCACCAGCAGCTACGGCCCCAAGGTCGGCGAGATCACCGCCTACGAGGCGCGCCTCCACTCCTGA","MRIAIGAPGNGALLKDALAERLAEDGRVSDVLDLSTPEITYPEVSFQVARAVAEGRVDRGLLICGTGVGTAIAANKVPGVRAATAHDLLTVRGSVENYDAQVLCMGQNVIAAPAAWALIDIWLDLRHDPTSSYGPKVGEITAYEARLHS$","Ribose 5-phosphate isomerase","Cytoplasm","ribose 5-phosphate epimerase (pentosephosphate)","ribose 5-phosphate isomerase ","sugar-phosphate isomerase, RpiB/LacA/LacB family","","Rosey E.L., Stewart G.C. Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans. J. Bacteriol. 1992. 174(19):6159-6170. PMID: 1400164","","","

InterPro
IPR003500
Family

Ribose/galactose isomerase
PIRSF005384	$\"[1-148]T$	Sugar-phosphate isomerase, RpiB/LacA/LacB types
PF02502	$\"[2-141]T$	LacAB_rpiB
TIGR00689	$\"[3-146]T$	rpiB_lacA_lacB: sugar-phosphate isomerases,

noIPR
unintegrated

unintegrated
G3DSA:3.40.1400.10	$\"[1-145]T$	no description

","BeTs to 10 clades of COG0698COG name: Ribose 5-phosphate isomerase RpiBFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0698 is -------qv-rlbce--h--ujx--wNumber of proteins in this genome belonging to this COG is 3","***** IPB003500 (Ribose/galactose isomerase) with a combined E-value of 1.7e-23. IPB003500A 1-31 IPB003500B 56-97","","","-53% similar to PDB:1NN4 Structural Genomics, RpiB/AlsB (E_value = 4.7E_19);-51% similar to PDB:1O1X Crystal structure of ribose-5-phosphate isomerase RpiB (TM1080) from Thermotoga maritima at 1.90 A resolution (E_value = 6.7E_10);","Residues 2 to 141 (E_value = 6.9e-42) place ANA_1723 in the LacAB_rpiB family which is described as Ribose/Galactose Isomerase.","","5-phosphate epimerase (pentose phosphate)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1724","1868103","1866583","1521","5.33","-13.76","53210","ATGCCATCACTCCTCTGCGAGTGGCCTGAGGTTCGACATGCCGCGCAGGTCGGCCGGCCGGCCAAGATGCGTGGCAGCATCGGTGGCATGAGCAAGGAAACAGTGCCTGAGCAGACCAGCACCTACGATGTCGTCGTGATCGGTGGCGGGCCGGCGGGGGAGAACGTTGCCCAGTACGCCATCGAGGGCACCGACCTGACCGCGGTCCTCGTTGAGGGCGAGCTCCTGGGTGGCGAGTGCTCCTACTACGCCTGCATGCCCAGCAAGGCGTTCCTCGTGCCTATCGAGGTCGCGGCGGCGTCCGCCAACCTCGGCGGCTTGCGCCCTGCCGAGCTGTCCGCGCTCGATCTGCTCAAGCGTCGTGACGAGTGGGTTTCCCGCTATGACGACGTTGGTCAGGTGCGTTGGGCCGAGGGTGCCGGTCTCGACATCGTTCGCGGATGGGCACGCCTCGACGGCGAACGGCGCGTCGCCGTGAGAACCGCTGAGGGGGAGCGGGTCCTTCGCGCCCGCCGCGCTGTCGTTCTCGCCACTGGCGCGCAGCCCGTCGTGCCCGCTGCGTTCCAAGGCCTCGAGGCCTGGGACTCGCGTGACGCCACCGGCGTGCAGGAGATCCCGCAGCATCTCATCGTTGTCGGTGGCGGGGTCGTCGCCTGCGAGGCCGCCACGTGGATGTCCGCCCTGGGCTGCGATGTCACCATGCTGGTGCGTGGTCCCCGCCTCCTGTCGGCTTCGGAGTCCTTCGCCTCCCGACTCATCGAGGAGGCTCTCACTGCCCGCGGTGTCACCGTCATGACGGATGCCCGGGTGACTGCCGCCGAGCGGTCCCAGGCCAGTGACACCGGGCTCGGTCGTATCCATGGCGGCCCTGTCACGGTCACCTGTGCCGGTCGAACCATCGAGGCCGATGAGATTCTGGTCGCCACCGGCCGTCGCCCGCTCCTGACCGGCATAGGGCTGGAGACCGTCGGCCTGGAGCCCGACGACGTCCTGGACGGTCGCCTACCCGACTGGCTCTACGCCGTCGGCGACGCCAGTGGCGAGGCCCAGTTGACCCACATAGGCAAGTACCGGGCGCGCGTCATAGGGGAGAGGATCGCCGCCCTTGCGGCTGGCTGCGAGCCCGAACCAGTGCCCGAGAGCATCCCGGTCCCGCAAGTCGTCTTCACCGATCCTCAGCTCGCCTCCAGCGGCCTGACCGAGCAGAAGGCCCGGGCCCTCGACCACGACGTCGTCACCGCCCAGGTCGGTTACACCTCGGCTGCTGGAGCTGCCCTCCTGCGCGACGATGCCCACGGTGAGGCCAAGCTCGTCGTCGACCGGCAGACGGGGGCCGTGCTGGGAGCCACCTTCGTCGGCCCCGGTGCGGGTGAGCTCATCCACGCCGCCACCATCGCTATCACTGCGGGCGTCCCCGTCCATCGGCTGCGTCACGCCGTGCCCGCCTACCCCACCGCCAGTGAGATATGGCTGCGCCTCATCGAATCCCTCCCGAGCGAGTTGCTCCACCCGAAGAGGTGA","MPSLLCEWPEVRHAAQVGRPAKMRGSIGGMSKETVPEQTSTYDVVVIGGGPAGENVAQYAIEGTDLTAVLVEGELLGGECSYYACMPSKAFLVPIEVAAASANLGGLRPAELSALDLLKRRDEWVSRYDDVGQVRWAEGAGLDIVRGWARLDGERRVAVRTAEGERVLRARRAVVLATGAQPVVPAAFQGLEAWDSRDATGVQEIPQHLIVVGGGVVACEAATWMSALGCDVTMLVRGPRLLSASESFASRLIEEALTARGVTVMTDARVTAAERSQASDTGLGRIHGGPVTVTCAGRTIEADEILVATGRRPLLTGIGLETVGLEPDDVLDGRLPDWLYAVGDASGEAQLTHIGKYRARVIGERIAALAAGCEPEPVPESIPVPQVVFTDPQLASSGLTEQKARALDHDVVTAQVGYTSAAGAALLRDDAHGEAKLVVDRQTGAVLGATFVGPGAGELIHAATIAITAGVPVHRLRHAVPAYPTASEIWLRLIESLPSELLHPKR$","Dihydrolipoamide dehydrogenase/glutathione oxidoreductase","Cytoplasm","mercuric reductase/transcriptional regulator,fusion","putative oxidoreductase ","pyridine nucleotide-disulphide oxidoreductase dimerisation region","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Kunert K.J., Cresswell C.F., Schmidt A., Mullineaux P.M., Foyer C.H. Variations in the activity of glutathione reductase and the cellular glutathione content in relation to sensitivity to methylviologen in Escherichia coli. Arch. Biochem. Biophys. 1990. 282(2):233-238. PMID: 2241146Shames S.L., Fairlamb A.H., Cerami A., Walsh C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 1986. 25(12):3519-3526. PMID: 3718941Carothers D.J., Pons G., Patel M.S. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 1989. 268(2):409-425. PMID: 2643922Misra T.K. Bacterial resistances to inorganic mercury salts and organomercurials. Plasmid 1992. 27(1):4-16. PMID: 1311113","","","

InterPro
IPR001100
Family

Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411	$\"[43-65]T$ $\"[76-91]T$ $\"[174-183]T$ $\"[208-233]T$ $\"[303-317]T$ $\"[380-401]T$ $\"[446-461]T$ $\"[468-488]T$	PNDRDTASEI

InterPro
IPR001327
Domain

Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139	$\"[178-237]T$	Q825V0_STRAW_Q825V0;
PF00070	$\"[208-310]T$	Pyr_redox

InterPro
IPR004099
Domain

Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30	$\"[384-504]T$	no description
PF02852	$\"[384-494]T$	Pyr_redox_dim

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368	$\"[43-65]T$ $\"[174-183]T$ $\"[208-233]T$ $\"[303-317]T$ $\"[339-346]T$	FADPNR
PF07992	$\"[43-326]T$	Pyr_redox_2

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[41-368]T$	no description
PTHR22912	$\"[45-497]T$	DISULFIDE OXIDOREDUCTASE
PTHR22912:SF29	$\"[45-497]T$	MERCURIC REDUCTASE

","BeTs to 21 clades of COG1249COG name: Dihydrolipoamide dehydrogenase/glutathione oxidoreductase and related enzymesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1249 is aomp-zyqvdrlbcefghsn-jxi-wNumber of proteins in this genome belonging to this COG is 4","***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 2.3e-60. IPB001100A 42-67 IPB001100B 77-89 IPB001100C 194-234 IPB001100D 303-325 IPB001100F 380-404 IPB001100G 445-490 IPB001100A 207-232***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 6.5e-23. IPB013027A 43-65 IPB013027B 174-183 IPB013027C 208-233 IPB013027D 303-317 IPB013027A 208-230***** IPB000759 (Adrenodoxin reductase family signature) with a combined E-value of 1.2e-07. IPB000759A 43-65 IPB000759D 209-223 IPB000759D 44-58***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase, class-II) with a combined E-value of 1.5e-07. IPB000103A 44-62 IPB000103D 300-315 IPB000103A 209-227","","","-44% similar to PDB:1EBD DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE (E_value = 1.7E_34);-43% similar to PDB:3LAD REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE (E_value = 1.3E_31);-41% similar to PDB:2A8X Crystal Structure of Lipoamide Dehydrogenase from Mycobacterium tuberculosis (E_value = 4.7E_29);-41% similar to PDB:1LVL THE REFINED STRUCTURE OF PSEUDOMONAS PUTIDA LIPOAMIDE DEHYDROGENASE COMPLEXED WITH NAD+ AT 2.45 ANGSTROMS RESOLUTION (E_value = 1.8E_28);-42% similar to PDB:1DXL DIHYDROLIPOAMIDE DEHYDROGENASE OF GLYCINE DECARBOXYLASE FROM PISUM SATIVUM (E_value = 1.2E_27);","Residues 43 to 463 (E_value = 0.00083) place ANA_1724 in the DAO family which is described as FAD dependent oxidoreductase.Residues 43 to 349 (E_value = 7.6e-12) place ANA_1724 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 208 to 310 (E_value = 5.2e-25) place ANA_1724 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 384 to 494 (E_value = 2.1e-34) place ANA_1724 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain.","","reductase-transcriptional regulator, fusion","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1725","1868386","1868075","312","7.51","0.65","11370","TTGACTACCACTGAAACGAACAGCAAGCACGCCCCTGTTCATCCGGGGGAGGTCCTCATGGAGGACTTCATCAAGGGATTCGGTATCACCCAGAACAAACTGGCTGTTGCTATCGGTGTGCCGCCGAGGCGTATCAATGAGATCGTGCACGGTAAGCGTGCGGTGACTGCGGATACGGCGCTGCGGCTCGGCAAGTACTTCGGGGTATCAGCGCAGTTCTGGTTGAACCTGCAGACCCAGTATGACCTTGACGTGGCGGAGGACCGTCTTTCGATGCAGATCGATGCCATCACTCCTCTGCGAGTGGCCTGA","LTTTETNSKHAPVHPGEVLMEDFIKGFGITQNKLAVAIGVPPRRINEIVHGKRAVTADTALRLGKYFGVSAQFWLNLQTQYDLDVAEDRLSMQIDAITPLRVA$","Addiction module antidote protein, HigA family","Cytoplasm","addiction module antidote protein, HigA family","plasmid maintenance system antidote protein; XRE family","addiction module antidote protein, HigA family","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[20-74]T$	HTH_3
SM00530	$\"[19-74]T$	HTH_XRE
PS50943	$\"[20-74]T$	HTH_CROC1

InterPro
IPR013430
Family

Addiction module antidote protein, HigA
TIGR02607	$\"[9-89]T$	antidote_HigA: addiction module antidote pr

","BeTs to 5 clades of COG3093COG name: Plasmid maintenance system antidote proteinFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG3093 is --------------efghs--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 20 to 74 (E_value = 4.8e-09) place ANA_1725 in the HTH_3 family which is described as Helix-turn-helix.","","module antidote protein, HigA family (higA)","","1","","","Wed Aug 15 16:21:28 2007","","Wed Aug 15 16:21:28 2007","","","Wed Aug 15 16:21:28 2007","Wed Aug 15 16:21:28 2007","Wed Aug 15 16:21:28 2007","","","","","","Wed Aug 15 15:11:28 2007","","","","Wed Aug 15 15:11:28 2007","Wed Aug 15 15:11:28 2007","","","","","yes","","" "ANA_1726","1868654","1868373","282","8.25","1.63","10813","GTGATCAGGTCGTTCGGTAGTAAGGACACTGAGCGGTTGTGGCACCGAGAACGAGTCCCATCGATTGACCCTCGCATACAACGGGTTGCCTTGCGTGAGTTACGTCAGATCGCTTCTGTGCAGTCTGTCGATGAGCTGAGAGTGCCGCCGGGGAACCGACTCGAGGTGCTCAAAGGTGATCGGACCGGCCAGCACAGCATCAGAGTGAATGACCAGTGGCGGATCTGCTTCGTATGGACTGGCGCTGGAGCGGAGGAGGTTGAGATCGTTGACTACCACTGA","VIRSFGSKDTERLWHRERVPSIDPRIQRVALRELRQIASVQSVDELRVPPGNRLEVLKGDRTGQHSIRVNDQWRICFVWTGAGAEEVEIVDYH$","Plasmid maintenance system killer","Cytoplasm","","","","","Tian QB, Ohnishi M, Tabuchi A, Terawaki Y.A new plasmid-encoded proteic killer gene system: cloning, sequencing, and analyzing hig locus of plasmid Rts1.Biochem Biophys Res Commun. 1996 Mar;220(2):280-4.PMID: 8645296","","","

InterPro
IPR007711
Family

Plasmid maintenance system killer
PF05015	$\"[1-93]T$	Plasmid_killer

","BeTs to 4 clades of COG3549COG name: Plasmid maintenance system killer proteinFunctional Class: NThe phylogenetic pattern of COG3549 is --------ebrh---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 26-93 are similar to a (KILLER PROTEIC SUPPRESSION PLASMID PROTEIN SIMILAR RTS1 BSL3012 BIOSYNTHESIS SSR5020) protein domain (PD029323) which is seen in Q82X09_NITEU.","","","Residues 1 to 93 (E_value = 1e-18) place ANA_1726 in the Plasmid_killer family which is described as Plasmid maintenance system killer protein.","","","","1","","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 16:22:25 2007","Wed Aug 15 16:22:25 2007","Wed Aug 15 16:22:25 2007","Wed Aug 15 15:33:54 2007","","Wed Aug 15 16:30:30 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","Wed Aug 15 15:33:54 2007","","Wed Aug 15 15:33:54 2007","","Wed Aug 15 15:33:54 2007","yes","","" "ANA_1727","1869051","1870010","960","7.72","3.24","33829","ATGAGACGCGCACGGCTCGCCGCGGGACTCCTCGGCGCCGGGATCGTCATCTACGGCGCGGCTCAGGCCCTCGCTCTCAGCCGAGCCCGCGCCGCAGCCCGCGCGCGACTGCTCGCCCATCCGGTGCGAAGGATGGCCCTCAGTCACGGCGAGGTCGCCTACGTCGACTGTGGACCGCAGCCCTCGGGAGGAGGCTCCGGCTTCGACCCCGGCTCCGGCTGCGAGACGATTCTGTCGGTCCACGGGCTGTACGGCGGATACGACCAGGCGCTTGACAGCGTCGGGAGCCTGGTCGAGCACTGCCGGGTCATCGCGCCGTCGCGCTTCGGCTACCCCGGCAGCGCTGTGCGAGGCGACGGCTCGCCGGCCGCCCAGGCCGCCGTCTTCGCCGAGATGCTCGACCGTCTGGGGATCGAACGAGTCTTCGTCCTGGGAGCCTCAGCCGGCGGCACCCCCGCCATCCGCTTCGCCCTGGACCACCCCGAGCGCGTCTCGGGGCTCATTCTCCTGAGCTCGGCCGCGCCCTGGCCGTCCCGGCCCACGACACCGCCCGGGCGCATGGGGCCGCCGGCGATCATGAACCACGACTGGATCATGTGGCTGCTCTCGCCATTCTTCAGTCCCGTCCTGGGCATGGATCCCCGGACCATCCACGGCATGCTCCCTCTGTCCGAACGCAGGACAGGGGCAGACATCGACGCCTCGATCACCAACCGGGACATGGCGGTGCACTTCGAGGACTATCCGATCGAGGAGCTCAAGCCGCCCGTCCTGCTCCTGCACGCCCGGGACGACCGAATAGCGCCTTTCGCTCCCCCGGCGGGGCACGTGCAGTCCTCCATGCACCGCTACCCGGACCTGACGACGTCGCTCTTCCCCACCGGCGGTCACCTCATCGCCGGCCACGGCCGCCAGCTCGAGGAGGCGATCCTCCGCTTCATCGGCCAGCACGCCGGCTGA","MRRARLAAGLLGAGIVIYGAAQALALSRARAAARARLLAHPVRRMALSHGEVAYVDCGPQPSGGGSGFDPGSGCETILSVHGLYGGYDQALDSVGSLVEHCRVIAPSRFGYPGSAVRGDGSPAAQAAVFAEMLDRLGIERVFVLGASAGGTPAIRFALDHPERVSGLILLSSAAPWPSRPTTPPGRMGPPAIMNHDWIMWLLSPFFSPVLGMDPRTIHGMLPLSERRTGADIDASITNRDMAVHFEDYPIEELKPPVLLLHARDDRIAPFAPPAGHVQSSMHRYPDLTTSLFPTGGHLIAGHGRQLEEAILRFIGQHAG$","Hydrolase, alpha/beta fold family","Cytoplasm, Extracellular","lactone-specific esterase","hypothetical protein","alpha/beta hydrolase fold","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[101-207]T$	Abhydrolase_1

InterPro
IPR003089
Family

Alpha/beta hydrolase
PR00111	$\"[100-115]T$ $\"[143-156]T$ $\"[157-170]T$ $\"[257-271]T$	ABHYDROLASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[71-314]T$	no description
PTHR10992	$\"[71-271]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF20	$\"[71-271]T$	ALPHA/BETA HYDROLASE
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[7-27]?$	transmembrane_regions

","BeTs to 12 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","***** IPB003089 (Alpha/beta hydrolase fold signature) with a combined E-value of 7.2e-15. IPB003089A 100-115 IPB003089B 143-156 IPB003089C 157-170 IPB003089D 257-271***** IPB000639 (Epoxide hydrolase signature) with a combined E-value of 5.6e-13. IPB000639B 100-115 IPB000639D 157-170 IPB000639E 255-271","","","No significant hits to the PDB database (E-value < E-10).","Residues 101 to 318 (E_value = 8.8e-06) place ANA_1727 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","esterase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1729","1870214","1871257","1044","5.18","-11.37","38180","GTGGACGCCTGGGGGCCGGACTTCCTGGGCCCGGGCTTCGAGGCCCGCACCCTGGAGCTGCTGCCCGACGACGAGGACGACGGCGCCGTCGCCACCCTGGTGCGCCACCTGCCGGCCCTCGACCCCGGCGCCCTGCCGGGCACCCCCACCACCCCCACCTTCATCTACCTCTACCTGCACGGCTGGAACGACTACTTCTTCCAGACCCACCTGGCCCGCGAGATCTCCCGCCTGGGTGGCGCCTTCTACGCCCTGGACCTGCGCCGCTACGGCCGTTCCTGGCGCGAGGGCCAGATGCTGGGCTGGTGCACCTCGCTGGCCGAGTACGACGAGGACCTGGGCCTGGCCCTGTCGGCCATCCGCGCCGAGCAAGGCTGGGAGGCCGAGCTCGTCCTGTCGGGTCACTCCACGGGCGGGCTCGTCGCCTCCCTGTGGGCCGACCGCCACCCGGGGGCCCTGCGCGCCCTGGTTCTGAACTCCGCCTGGCTCTCGCTCCAGGGCTCCGAGATCGTGCGCACCGTCGGCGACTCGGTCCTGCGTACCCTGGCGCTGCGCGACCCGCGCATGTCGATCCTCGACGGCTGGGTCGACCCGGCGCGCGTCTTCTCCATCACCGACGGCTGGCTCCCCGAGCGTGACGGCGAGCTGCCCGATCCCGCCTGGGCCGACGATCCCTACGTGACCGGCTGGGACATCAACCCAGCCTGGTCGATCAAGCCCTCCGCGCCCGTGCGCGTGGGCTGGCTCCAGGCTGTCATGGAGGGCCACAACCGCGTCGCCCAGGGCCTGGACATCCGCTGTCCGGTGCTGTCCATGGGCGCGGCCTCCACCCGGCTCGGGGTGACGTGGATGCCGGAGTCGCGCAGCGCGGACACGATCATCGACGCCGACGCCACCGCCCGCCGCGCCGTCATGCTCGGCAAGCTGGTGACCATCGCCCGCTTCCCCGGCGGCGTCCATGACCTCACCCTGTCCGAGCCGCCCGTGCGAGAGCAGGTCTTCTCGGCCCTGCGCCGCTGGATGGCTGCCTACGTGTTGCGCTGA","VDAWGPDFLGPGFEARTLELLPDDEDDGAVATLVRHLPALDPGALPGTPTTPTFIYLYLHGWNDYFFQTHLAREISRLGGAFYALDLRRYGRSWREGQMLGWCTSLAEYDEDLGLALSAIRAEQGWEAELVLSGHSTGGLVASLWADRHPGALRALVLNSAWLSLQGSEIVRTVGDSVLRTLALRDPRMSILDGWVDPARVFSITDGWLPERDGELPDPAWADDPYVTGWDINPAWSIKPSAPVRVGWLQAVMEGHNRVAQGLDIRCPVLSMGAASTRLGVTWMPESRSADTIIDADATARRAVMLGKLVTIARFPGGVHDLTLSEPPVREQVFSALRRWMAAYVLR$","Lysophospholipase","Cytoplasm","conserved hypothetical protein","hypothetical protein","Lysophospholipase-like","","Chapus C., Rovery M., Sarda L., Verger R. Minireview on pancreatic lipase and colipase. Biochimie 1988. 70(9):1223-1234. PMID: 3147715Persson B., Bengtsson-Olivecrona G., Enerback S., Olivecrona T., Jornvall H. Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase. Eur. J. Biochem. 1989. 179(1):39-45. PMID: 2917565Blow D. Enzymology. More of the catalytic triad. Nature 1990. 343(6260):694-695. PMID: 2304545McLean J., Fielding C., Drayna D., Dieplinger H., Baer B., Kohr W., Henzel W., Lawn R. Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. Proc. Natl. Acad. Sci. U.S.A. 1986. 83(8):2335-2339. PMID: 3458198","","","

InterPro
IPR008262
Active_site

Lipase, active site
PS00120	$\"[130-139]?$	LIPASE_SER

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[57-341]T$	no description
PTHR11614	$\"[59-191]T$	PHOSPHOLIPASE-RELATED

","BeTs to 3 clades of COG2267COG name: LysophospholipaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG2267 is a---k-y-vdrlb-efgh---j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1730","1873365","1871299","2067","4.51","-57.99","69339","ATGGCCATGTACGAGCTCGACGGCAACCACCTCCTGCCCGTGCGCCTGGGTCGCTCCGCTGACGCCATCACCCTGTCTCACAGTCTGGTCGCCATCCAGCGTCAGATCGTCGATGTCCTGCGCCGTCCACTCTTCCCCCTGTCATGGGAGGAGCTCGAGACCGGGGCGAGCCTGACCGCCCTGGACGCCACCGGTCAGGTCGTCGTCGTCGAGGTCCTGGAGAGAGTCGACTCCACGGGGCTGCTGGCCGCCATGTCGCGCCTGACCCAGGCCGCCACCGCGGGCCGCCGTGAGATCGCCAGCAGGTACGCCGGCGGGCTGGGGGCCTTCAGCCAGGACTGGAACGAGTTCCGTGAGGCGATGCCCGCCCAGGTCGAGGCCGGACCGCGGCTGACGATCCTGAGCGCCTCCCTGGAGCCCGACGTCGTTGGAGGGTTGGGAGTACTGGCCTCCTCCGGGCTGGAGATCCACGAGGTCGACGTGCGTATCGTGGACGAGTCGCGCATCGTCGTCGTGGTGGAGAAGATCTCCGGAATGGACGTGGCCGCCGGTGGGCCGCTGCTCGTGGCCCGCGCCCCCCGGCCGGCCCTGGCCGGTTCCGCCTCCGCCGGCTCGAACGGCTCACGGGCCATTGACGCCACGGAGCAGGCCGAGCACATGAGTCCGGTCACCGGCCCCATCGAGATCGTCATGCCCGCCGAGCCGGCGCACACCCCTGAGACCGAGGGCACCGAAGATGCCAGCGCCACCATCCCGGCGGGGGCCTTCGCTGCGACGGGTGCCGCCGATGCGCTCTCCGAGCTGTTCGAGCCGGTGGCCGTCACCGCCGAGCAGCCCCAGGTGCATGCCCTCTCCGACCAGGGCGGGGAGGAGTCCTCACCCGAGGAGCCCGATGAGGCCGGCGCCGCCCCGCCCGCCGGGCAGGCCGCGTCCGAACCGGCTGAGGGGGCTGCCGAAGCCCCGGCCGATGACGCCCACGCACAGGGCCCGGCCCAGGACGCCGCTGATGGCGCCGCTGCAGCCACCAATGAGGGCGCAGCCGATGCTGTCCGCGGCCCCGAGACCGAGCAGGAGGCTGATCCCGAGGCCCCTCAGAGCCGGCCCGAGCCGGACCCGGAGCGCCCCGACAGCGCCCCTCAGGCGCCCGCCGCCTCCAAGCCCGAGAACGACTCTGGTGACTCCGACCACCCCGACCACGCTGCCGGTGACCACGGTGCAGGTGGACACGACGCCGCCGGCAGTGTCGGCAGTGTCGGCAGTGTCGGTCAGGACCTGGCCGACATCCTCAGCGGGGACACTGTGGCCGTTCCCGCCTCCGTCGATCTGGGGGAGGAGCCCTCCGCCGACAATGCCGGCCACCGGGGGCGCCCCGACTCCGCCGATGACTCCAGTGCCGGGCAGCGGGCCGTCGCCGCCCTGGCCGGAGGCGTGGACATCCTTGGTGGGAGCAGCCTGTCCGGAGGCAGCGGTTCAGCGGCGTCGGCCGGCTCGGCACCTTCCGACGCTCCGCTCGGTCCGGACCGAGCCCCGCAGGCCGGCGAAGCCCCGAGCGAGCCCGGTTCGCGCACCCGCATGGGACGGCGCTCGCGGGCGGCGCACTCTCAGTCCGAGGCATCCTCGGCCGCGCCCGCCGCGCAGGCCTGGTCCACGGTGGCTCCCAACGAGTCCCGCCCGGAGGCGCCCACCGGTGCTGTGCCGCTCGTGTCCTGGGAGCCGCTGCGCGGGTCGGCCGACGGGCTCGACCCGGTGGCCGAGGCACTGGGCGGCGACCCCTCGAAGTCCCTCCTGGTCCAGGAGACCGCGGAGCTGGCGGCCGTGGCGGCCTCGCTGGGCAAACCGACCCAGATCGTCTGGCAGCGGCTGCGCCGAGGTATCTACCACGAGGCGATCCTGTCGGTGGAGGGGGTCATCACCCTGTCTGACGGGCGATCCTTCACCGACCCGACATCGGCCGCCAACGCCGCCCAGGCCGTCACCGACGCCGACGGCTGGCGCGTGTGGCGCGTGGGGGTGCACGGTCCCCACCTGGGGGACCTGCGCGACGACCTGGCCGACCGCGGCCTCTGA","MAMYELDGNHLLPVRLGRSADAITLSHSLVAIQRQIVDVLRRPLFPLSWEELETGASLTALDATGQVVVVEVLERVDSTGLLAAMSRLTQAATAGRREIASRYAGGLGAFSQDWNEFREAMPAQVEAGPRLTILSASLEPDVVGGLGVLASSGLEIHEVDVRIVDESRIVVVVEKISGMDVAAGGPLLVARAPRPALAGSASAGSNGSRAIDATEQAEHMSPVTGPIEIVMPAEPAHTPETEGTEDASATIPAGAFAATGAADALSELFEPVAVTAEQPQVHALSDQGGEESSPEEPDEAGAAPPAGQAASEPAEGAAEAPADDAHAQGPAQDAADGAAAATNEGAADAVRGPETEQEADPEAPQSRPEPDPERPDSAPQAPAASKPENDSGDSDHPDHAAGDHGAGGHDAAGSVGSVGSVGQDLADILSGDTVAVPASVDLGEEPSADNAGHRGRPDSADDSSAGQRAVAALAGGVDILGGSSLSGGSGSAASAGSAPSDAPLGPDRAPQAGEAPSEPGSRTRMGRRSRAAHSQSEASSAAPAAQAWSTVAPNESRPEAPTGAVPLVSWEPLRGSADGLDPVAEALGGDPSKSLLVQETAELAAVAASLGKPTQIVWQRLRRGIYHEAILSVEGVITLSDGRSFTDPTSAANAAQAVTDADGWRVWRVGVHGPHLGDLRDDLADRGL$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1731","1873777","1876335","2559","8.93","11.68","91029","ATGCCGTCGGTCTCATCCACCACGACTCCCCCGGACGCACCTGAGCTCGCGCCCTCCCCGGCGCCCTCCTCCACCTCATCGCCCGCACCATCACCGTCATCGGCGTCGGCCGCTCCTGCGTCTGAGCCCTCGCACCTGAGCGTCTACGCGCGTCAAGCCCGGCGGGCCGCGCGCGCCTGGCTGGCCCCGGCGCCGGCTGCGACCAGCTGTGCCGCGCTGACCCTGGTCATCGGGATCGTCCTGCTGCCCTGGGGGTCCCGGGGGCAGATCGCCCTGTCCGCCTACATCCACCAGCCCCAGCGGGTGTGGACCCTGCTGACCGCCTGGGCGGTCCCCGGTCACCTGCTGCCGGTGACCGGCTGCCTCATGCTGCTGTCCGTCGGCGTGCTGCTGGAGCGGCTCCTGGGCACTCGACGGTGGCTGGCCACCGCCGTCGTCTCCTGCGCAGGAGGCATCGTCCTGGCCCAGGCGCTCTACCCCCTCATCCGCCACGTGTGGGACGCCTGGTCCCCCTACCTCGTCCTCGCCCCGATCCAGGGCATCAGCCTGCCCACCGCCGGCCTGGTGGCGGCCTCCACCAGTGTCATGCGTCCGTCCTGGCGACGGCGTACGCGCTTGGCGACCTTCGCCGTCCTCGTCGTCTCGGCCGCTGTGACCGGAACCGTGGGCGCCCTGGCCCGCCTGGGAGCAGGGGTCATCGGCCTCATCATGGGAGTCGTCCTGGAGCGTGGGCAGCAGACGGCCCCCTCCCAGGAGCTGCCCCGGCGCTCGGAGCGCGAGCTCGTGGCCTTCCTGGTGGCCTGCTGGGCCGTGAGCTGCGCCCTGGCGGTGGTGAGTAACGCCGCCGGCCCCCTGGCCGACGCCCGCTACGGGCTGACCCCCGCCATCCTGCCCAAGGACGCCGTCATCTATCCGGTCGAGCAGCTTCTGATGTGCATGCCGGCGTTCCTGCAGCTGGTCCTGGCCGACGGCCTGCGCCGGGGGCGCCGTTCAGCGGCCTACGGCACCATCGCCCTGCAGATCTTCCTGGGGGTGTGCGCGGCCCTGTTCGCCCTGGTGGAGAAGATCGGCGAGCAGATGCCCGCGTCAGGTCCCACCACGACCCAGCTCCTGCACAGCTGGCTGCGCTCGGGGCACCTGCTGGTGCCGCTGTTGCTCAACATCGTGGTCATCAGCCTGGTGGTGTGGACCAGGAGGCGCTTCACCCTGGGCTCGCGCCCCGGCGTCATTCGTCGCGCCGTCGTCGCCTGGATCCTGACCCTCCTGGGCGGGGCGGTCCTGACCGTCGCCGGGGGCCTGCTCATGTCTCACGACTTCTCCCCCTACGCGACCTGGCCCGCCCTGCTGGAGACCTACGTGTCCTACCTGCTGCCCATCAGCACCGGCGGCATCATGAGCCTGATCGTCGAGCCCCTGACCCCGCTGGCCCACCTGCTCACCGGGTGGGTGCCGGTCCTGGTGTGGCTCCTGACGATCCTGTGGGTGTGGCTGGCCCAGTCCGCTCCCGCCCGCACCCGGATCTCCGACCGCGAGGAGCTCATCGACCTGGTGCGCAGCCGCGGCGCCGGGACCCTGGGGTGGATGCTCACTTGGCAAGGCAACGAGGCCTGGGTCAACGAGGCGGGCACGGCCGGCTTCTCCTACCGGCCCAGCCGCGACGTCGCCCTGACGGTCGGGGACCCCGCCGCCGACGACGCCGACGTGGCCCAGGCGGTGCGCGACTTCGCCGACTTCGCCACCGACGCCGGACTCATCCCGGCCCTGTACTCGGTGCACGCCCCGGCGATGGAGGCCGCCCGCGCCATGGGCTGGACGATCATGCAGGTGGCCGAGGAGGCCGTCCTGGACCTACCGGACCTGGCCTTCCGCGGCAAGGCCTACCAGGACGTGCGCACCGCCCTCAACCACGCCAAGAAGGAGGGCGTCGAGGCGGTGTGGACCAGCTTCCGCGACTGCCCCGCCGGCCGGCGCGACCAGATCCGGGCCATCTCCCAGGCCTGGGCCAGCGACAAGCCGCTGCCAGAGATGGGCTTCACCCTGGGCGGCCTGGCCGAGCTCGACGACGCCGAGACGCGCCTGCTGCTGGCCGTGGACGCCGAGGGCACCGTCCAGGGCGTCACCTCCTGGCTGCCGGTGTACCGCGATGGGCGCGTCATCGGCCTGACCCTGGACTTCATGCGGCGCCGCGAGGGCGGTTTCCGGCCCGTCATGGAGTACCTCATCGGGCGCGCCGCCCAGGACGCCCAGGCCGAGGGCCTAGAGATCCTGTCCCTGTCCGGGGCGCCGCTGTCGCGCTCCGCACCGGCCGACGGCGGCTCCTCCTCACGCTTCGACCCGCTCCTGAACCTCTTGGCCTCCGTGCTGGAGCCGGCCTACGGATTCGGCTCCCTGCACGCCTACAAGCGCAAGTTCAAGCCGCGCTCCGTGCCCATGTACCTGGCGGTTCCCGACCTGGTGGACCTGCCCACGGTGGGGATCGCCATCGCCCGGGCCTACCTTCCCGGTCTCAAGCCCTCCCAGACGGCGCGCTTCGCCCATGTGCTGATGAACCGTGACTGA","MPSVSSTTTPPDAPELAPSPAPSSTSSPAPSPSSASAAPASEPSHLSVYARQARRAARAWLAPAPAATSCAALTLVIGIVLLPWGSRGQIALSAYIHQPQRVWTLLTAWAVPGHLLPVTGCLMLLSVGVLLERLLGTRRWLATAVVSCAGGIVLAQALYPLIRHVWDAWSPYLVLAPIQGISLPTAGLVAASTSVMRPSWRRRTRLATFAVLVVSAAVTGTVGALARLGAGVIGLIMGVVLERGQQTAPSQELPRRSERELVAFLVACWAVSCALAVVSNAAGPLADARYGLTPAILPKDAVIYPVEQLLMCMPAFLQLVLADGLRRGRRSAAYGTIALQIFLGVCAALFALVEKIGEQMPASGPTTTQLLHSWLRSGHLLVPLLLNIVVISLVVWTRRRFTLGSRPGVIRRAVVAWILTLLGGAVLTVAGGLLMSHDFSPYATWPALLETYVSYLLPISTGGIMSLIVEPLTPLAHLLTGWVPVLVWLLTILWVWLAQSAPARTRISDREELIDLVRSRGAGTLGWMLTWQGNEAWVNEAGTAGFSYRPSRDVALTVGDPAADDADVAQAVRDFADFATDAGLIPALYSVHAPAMEAARAMGWTIMQVAEEAVLDLPDLAFRGKAYQDVRTALNHAKKEGVEAVWTSFRDCPAGRRDQIRAISQAWASDKPLPEMGFTLGGLAELDDAETRLLLAVDAEGTVQGVTSWLPVYRDGRVIGLTLDFMRRREGGFRPVMEYLIGRAAQDAQAEGLEILSLSGAPLSRSAPADGGSSSRFDPLLNLLASVLEPAYGFGSLHAYKRKFKPRSVPMYLAVPDLVDLPTVGIAIARAYLPGLKPSQTARFAHVLMNRD$","Lysyl-tRNA synthetase","Membrane, Cytoplasm","Family of unknown function (DUF472) family","hypothetical protein","protein of unknown function DUF471","","Peschel A., Jack R.W., Otto M., Collins L.V., Staubitz P., Nicholson G., Kalbacher H., Nieuwenhuizen W.F., Jung G., Tarkowski A., Van kessel K.P., Van strijp J.A. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine. J. Exp. Med. 2001. 193(9):1067-1076. PMID: 11342591","","","

InterPro
IPR007425
Domain

Protein of unknown function DUF471
PF04330	$\"[659-732]T$	DUF471

InterPro
IPR007426
Domain

Protein of unknown function DUF472
PF04331	$\"[737-835]T$	DUF472

noIPR
unintegrated

unintegrated
tmhmm	$\"[60-82]?$ $\"[113-131]?$ $\"[140-162]?$ $\"[172-192]?$ $\"[202-217]?$ $\"[223-241]?$ $\"[262-282]?$ $\"[301-321]?$ $\"[331-353]?$ $\"[380-398]?$ $\"[413-435]?$ $\"[451-469]?$ $\"[478-498]?$	transmembrane_regions

","BeTs to 5 clades of COG2898COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2898 is ----------rlb--f--s--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 659 to 732 (E_value = 8.4e-11) place ANA_1731 in the DUF471 family which is described as Family of unknown function (DUF471).Residues 737 to 835 (E_value = 1.3e-10) place ANA_1731 in the DUF472 family which is described as Family of unknown function (DUF472).","","of unknown function (DUF472) family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1732","1876427","1877767","1341","8.57","4.80","47123","ATGGGGGCGGTCTGCGTGGTCGTGGCCGCGGTGGTCATTGCCTGGCTGTGGTGGCGGCGCACCCGCTACCTGCCCTGGCATCGCCAGCTCGTCGTGCCCGCTGCCGCAGCAGTGAGCGCGGTGACCTCCTGGCTGGCCGTGGACGTCATCTGGCATCCCGTCGCCGACGGCGTCGGCTGGTTCGTGTGGACCTGGGTGGGCGTCATCGGCCTCGTCATCGCCCAGCTGGTCACCGGCAACCGCACCGAGGGACGTCACCGGGCGGTGCGTTCACGTAACCGCCGCCTGGTGCGTGCCACGGAGTCCGCCTCCAGCCTCGTGGCCGTGGTGGCCTCCTCCTTACTGGCGATCAACACCTTCTTCGCCTCCTACCCCACCCTGGCATCGGTCCTGGGCTACGGGGTGGCGACCACGCCACTCAGCCGTCTGCAGGGCGCCGCGGCCCGGTCTCCGGCACCCGTGCGCGGCCGCGGAATGCTGGAGGAGACCTGGAGGCCGCCGTCGGACATGCCCGCCCGCGGCCAGGCGGTCACCGCCGACATCCCGGCCGGCGACCAGTCCGGAACGAAGGGCTTCACGCCACGAGGGGCCTTCATCTATCTGCCGCCGGCCTACCTGGGCTCTCAGCGCCCGGCCCTGCCGGTCCTGGTCCTGCTCACCGGGCAGCCGGGAAGCCCGTCAGACTGGTTCGAGCTGGGGAACCTGAAGGACACGATGGACGCCTACGCGGCCGACCACCACGGCCTGGCCCCGGTAGTCGTCGTCGCCGACCTCCTGGGCAGCCCGTACGCCAATCCCCTGTGCTCCGACACGAAGGCGGGCGGCAAGGTGGCCACCTACCTGGACAAGGACGTCCCGGCCTGGATCCGGGCGAACCTGCAGGTCGACGACGACCCCGCCCACTGGGCGGTAGCCGGCCTGTCCAACGGGGGCACCTGCGCGATGCAGGTCGTCACGCGCTCTCCGGGCGTCTACCGCACCTTCCTGGCGATCAGCGCCGAGGAGCACCCCACGCTGGGCAGCGTGGAGCGCACCATCTCCCAGGGCTTCGGAGGGGACCGTGCCGCCTACGAGGCCAACGACCCGCTCTCCCTGATGTCCTCCGCCCCACCCGGCCGCTACGACGGCATCGCCGGCATCGTGTCGGTGGGCCGTCAGGACACCAGCTACCGCGGGGCCGTGCCCGTCCTGGCCGAGGCCGCCACGAGGGCCGGGATGACGGTGAGCACCCGCCAGTACGACGGCGCCCACACCTGGGCCGTGTGGGGGCCGGCGCTGGCCGACCAGCTCGACTGGCTGGGCGGGCGCCTGGGTATCGCCTCGCCGTCGCCGGCCTCCTGA","MGAVCVVVAAVVIAWLWWRRTRYLPWHRQLVVPAAAAVSAVTSWLAVDVIWHPVADGVGWFVWTWVGVIGLVIAQLVTGNRTEGRHRAVRSRNRRLVRATESASSLVAVVASSLLAINTFFASYPTLASVLGYGVATTPLSRLQGAAARSPAPVRGRGMLEETWRPPSDMPARGQAVTADIPAGDQSGTKGFTPRGAFIYLPPAYLGSQRPALPVLVLLTGQPGSPSDWFELGNLKDTMDAYAADHHGLAPVVVVADLLGSPYANPLCSDTKAGGKVATYLDKDVPAWIRANLQVDDDPAHWAVAGLSNGGTCAMQVVTRSPGVYRTFLAISAEEHPTLGSVERTISQGFGGDRAAYEANDPLSLMSSAPPGRYDGIAGIVSVGRQDTSYRGAVPVLAEAATRAGMTVSTRQYDGAHTWAVWGPALADQLDWLGGRLGIASPSPAS$","Putative esterase","Membrane, Cytoplasm, Extracellular","Putative esterase family","possible esterase","putative esterase","","","","","

InterPro
IPR000801
Family

Putative esterase
PF00756	$\"[173-433]T$	Esterase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[193-433]T$	no description
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[4-18]?$ $\"[33-55]?$ $\"[61-81]?$ $\"[102-122]?$	transmembrane_regions

","BeTs to 3 clades of COG0627COG name: Predicted esteraseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0627 is ------y---rl-cef-h-n-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 173 to 433 (E_value = 6.1e-07) place ANA_1732 in the Esterase family which is described as Putative esterase.","","esterase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1733","1880751","1877842","2910","5.06","-41.77","105495","GTGAGTCCCTGTCCACCCGCATCACCCTGCCGGGACACACCGGCCTGCTGGCGCTGCGCCCTTAAGCCCTGGGGCCGGCCGGCGCAGCCCTGTTCGCGGCTGGATGAGTCACCTGCAACATGGGACCGAAGTCACATAGAGTGCTTCGTGTGCGCCTGCGCGTGCACGGAGTCCCTAGTTCCACAAGAACCGAAAGAGGCAAGGATGCCCAAGTACGTGTACCGCTTCAGCGAGGGTGACAAGGACCAGAAGGACCTCCTGGGAGGCAAGGGAGCGAACCTGGCGGAGATGACCCGGCTGGATCTCCCCGTTCCCCCCGGCTTCACCATCACCACCGACGCCTGTCGCGCCTACCTGGCCAGCGGCGAGGTCCCCGAGGAGCTCTCGGTCCAGGTCACCACCGCTCTGCGTGGAGTCGAGGAGGAGCTGGGGCGCGAGCTCGGCGCCGCCGAGGATCCCCTGCTCGTCTCGGTGCGAAGCGGCGCCAAGTTCTCCATGCCCGGCATGATGGAGACCGTCCTCAACATCGGCCTCAACGACGTCTCCGTCAAGGGCCTGGCCGCCGCCAGCTCCGACGAGCGCTTCGCCTGGGACTCCTACCGCCGCCTCATCCAGATGTTCGGCAAGACCGTCCTGGACATCGACGGCGACCACTTCTCCGACGCCCTGGACGCCAAGAAGGACGCGCGGGGCGTCTCCATGGACTATGAGCTCCCCGTGGACGCCCTCCAGGAGCTGGTCGAGGAGTACAAGGCCATCGTCAAGGAGCACGCCGGCATCGACTTCCCGCAGGATCCCCGCTCCCAGCTGGACATGGCCACCGAGGCCGTCTTCCGCTCCTGGAACACCGAGCGCGCCCACATCTACCGCCGCCGCGAGAAGATCCCGCACGACCTGGGCACCGCGGTCAACGTGTGCACCATGGTGTTCGGCAACATGGGGGAGACCTCGGGCACCGGCGTGTGCTTCACCCGCGACCCCTCCACCGGGCGCACCGGCGTCTACGGCGACTACCTGGTCAACGCCCAGGGCGAGGACGTCGTCGCCGGTATCCGCAACACCCTGTCCCTGGCCGACCTCGAGCGCCTGGACAAGGCCTCCTACGACGAGCTGCGCTCCATCATGCGCCGCCTGGAGACCCACTACCGCGACCTGTGCGACATCGAGTTCACCATCGAGCGCGGCAAGCTGTGGATGCTTCAGACCCGCGTGGGCAAGCGCACCGCCGCGGCCGCATTCCGCGTGGCCACCCAGCTCGTGGACGAAAAGCTCATCACCATGGACGAGGCCCTCACGCGCGTCTCCGGCGAGCAGCTCACCCAGCTGATGTTCCCCCAGTTCGACGACGACTCCAGCCGCGACCTGCTCACCCGCGCCATGGCCGCCTCCCCGGGCGCCGCCGTGGGCTACATCGCCTTCGACAACGACGAGGCCGTCTCCCGTGCCGAGAAGGGCGACTCCGTCATCCTCGTGCGCCGCGAGACCAACCCCGACGACCTGCCCGGCATGGTCGCGGCCGCCGGCGTACTCACGGCCCGCGGCGGCAAGACCAGCCACGCCGCCGTCGTCGCCCGCGGCATGGGCAAGACCTGCGTGTGCGGCGCCGAGGCCCTCGAGGTCGACTCCGCCGCCAAGACCCTGCGCATCGCGGGGCGCGATGAGGTCCTCACCAGTGAGGACATCATCGCCATCGACGGCACCACCGGCGAGGTCTTCCTCGGCGAGGTCGGCGTCGTCGACTCCCCGGTCATGACCTACCTGCGCCGAGGCCTGGACGAGGCGCTCAAGGCGGCCGGCGACGACGACACCCGCGAGCTCGTCACTGCCGTGGACCGCCTCATGGGCCACGCCGATGCGGTCCGCCGCCTGGAGGTGCGCGCCAATGCCGACACCCCCGACGACGCCCGCCACGCCATCCACCGCGGCGCCCAGGGCGTGGGGCTGTGCCGCACCGAGCACATGTTCCTGGGCGAGCGCAAGCAGTTCGTCCAGAACCTCATCCTGGCCTCCTCCGACGCCGAGCGCGAGGCCGCCCTGGCCGCCCTCCTGCCGCTGCAGAAGGGCGACTTCATCCAGATGTTCGAGACGATGAACGGCAAGCCCATGACGGTGCGCCTCATCGACCCGCCGCTGCACGAGTTCCTGCCGGACCTGACCGAGCTGAGCGTCAAGGTGGCCGTGGACCGCGAGCGTGGCGAGCTGGACCCGGCCGACGAGGAGCTCCTGGCCGTGGTGCGCAAGAGCCACGAGGCCAACCCGATGCTCGGCCTGCGCGGGGTCCGCCTGCTGCTGACCATGCCGGGCCTCATCGAGCTCCAGGTGCGCGCCATCGCCGAGGCCGCCGTCGAGCGCCTCAAGGCCGGCGGCGACCCGCACCCCGAGATCATGATCCCGCTCATCGGATCGGTGCGTGAGCTCCAGCTGGCGCGCGAGCGCGTGGAGCACGTGCTGCAGGAGGTCTCCCAGGCCTCCGGCTATGCCCTCGACTTCCCGGTGGGTTGCATGATCGAGCTGCCGCGCGCTGCCGTCACCTCCGCCCACGTCGCCGAGGAGGCCGACTTCTTCTCCTTCGGCACCAACGACCTGACCCAGACCACCTGGGGCTTCTCACGCGACGACGTCGAGGGCTCCTTCGTGGGCCACTACACCGACGACGGCATCTTCGGGGTCTCCCCCTTCGAGACCATCGACACCGATGGCGTGGGCGGCATGGTGCGCCTGGGGGTCGAGGGCGGCCGCTCCACCAAGCCGACGATGAAGATGGGCGTGTGCGGCGAGCACGGCGGGGACCCCGAGTCCATCGGCTTCTTCCACCGGGTGGGCCTGAACTACGTCTCCTGCTCGCCCTTCCGGGTGCCGGTGGCCCGCCTGGAGGCCGGGCGCGCGGCCGTCGCGGACAAGGCTGAGTAG","VSPCPPASPCRDTPACWRCALKPWGRPAQPCSRLDESPATWDRSHIECFVCACACTESLVPQEPKEARMPKYVYRFSEGDKDQKDLLGGKGANLAEMTRLDLPVPPGFTITTDACRAYLASGEVPEELSVQVTTALRGVEEELGRELGAAEDPLLVSVRSGAKFSMPGMMETVLNIGLNDVSVKGLAAASSDERFAWDSYRRLIQMFGKTVLDIDGDHFSDALDAKKDARGVSMDYELPVDALQELVEEYKAIVKEHAGIDFPQDPRSQLDMATEAVFRSWNTERAHIYRRREKIPHDLGTAVNVCTMVFGNMGETSGTGVCFTRDPSTGRTGVYGDYLVNAQGEDVVAGIRNTLSLADLERLDKASYDELRSIMRRLETHYRDLCDIEFTIERGKLWMLQTRVGKRTAAAAFRVATQLVDEKLITMDEALTRVSGEQLTQLMFPQFDDDSSRDLLTRAMAASPGAAVGYIAFDNDEAVSRAEKGDSVILVRRETNPDDLPGMVAAAGVLTARGGKTSHAAVVARGMGKTCVCGAEALEVDSAAKTLRIAGRDEVLTSEDIIAIDGTTGEVFLGEVGVVDSPVMTYLRRGLDEALKAAGDDDTRELVTAVDRLMGHADAVRRLEVRANADTPDDARHAIHRGAQGVGLCRTEHMFLGERKQFVQNLILASSDAEREAALAALLPLQKGDFIQMFETMNGKPMTVRLIDPPLHEFLPDLTELSVKVAVDRERGELDPADEELLAVVRKSHEANPMLGLRGVRLLLTMPGLIELQVRAIAEAAVERLKAGGDPHPEIMIPLIGSVRELQLARERVEHVLQEVSQASGYALDFPVGCMIELPRAAVTSAHVAEEADFFSFGTNDLTQTTWGFSRDDVEGSFVGHYTDDGIFGVSPFETIDTDGVGGMVRLGVEGGRSTKPTMKMGVCGEHGGDPESIGFFHRVGLNYVSCSPFRVPVARLEAGRAAVADKAE$","Pyruvate, phosphate dikinase","Cytoplasm","pyruvate,phosphate dikinase","pyruvate phosphate dikinase ","pyruvate, phosphate dikinase","","Wei M., Ye D., Dunaway-Mariano D. Investigation of the role of the domain linkers in separate site catalysis by Clostridium symbiosum pyruvate phosphate dikinase. Biochemistry 2001. 40(45):13466-13473. PMID: 11695893Nakanishi T., Ohki Y., Oda J., Matsuoka M., Sakata K., Kato H. Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize. Acta Crystallogr. D 2004. 60:193-194. PMID: 14684927Chastain C.J., Fries J.P., Vogel J.A., Randklev C.L., Vossen A.P., Dittmer S.K., Watkins E.E., Fiedler L.J., Wacker S.A., Meinhover K.C., Sarath G., Chollet R. Pyruvate,orthophosphate dikinase in leaves and chloroplasts of C(3) plants undergoes light-/dark-induced reversible phosphorylation. Plant Physiol. 2002. 128(4):1368-1378. PMID: 11950985","","","

InterPro
IPR000121
Domain

PEP-utilizing enzyme
PD000940	$\"[612-955]T$	Q9WXH8_BBBBB_Q9WXH8;
PF02896	$\"[604-964]T$	PEP-utilizers_C

InterPro
IPR002192
Domain

Pyruvate phosphate dikinase, PEP/pyruvate-binding
PF01326	$\"[72-428]T$	PPDK_N

InterPro
IPR008279
Domain

PEP-utilising enzyme, mobile region
PF00391	$\"[477-569]T$	PEP-utilizers
PS00370	$\"[514-525]T$	PEP_ENZYMES_PHOS_SITE

InterPro
IPR010121
Family

Pyruvate, phosphate dikinase
PIRSF000853	$\"[70-968]T$	Pyruvate, phosphate dikinase
TIGR01828	$\"[70-964]T$	pyru_phos_dikin: pyruvate, phosphate dikina

InterPro
IPR013815
Domain

ATP-grasp fold, subdomain 1
G3DSA:3.30.1490.20	$\"[70-309]T$	no description

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[310-407]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.60	$\"[621-967]T$	no description
G3DSA:3.50.30.10	$\"[447-572]T$	no description
PTHR22931	$\"[302-581]T$ $\"[605-969]T$	PHOSPHOENOLPYRUVATE DIKINASE-RELATED
PTHR22931:SF9	$\"[302-581]T$ $\"[605-969]T$	PYRUVATE, PHOSPHATE DIKINASE, CHLOROPLAST

","BeTs to 15 clades of COG0574COG name: Phosphoenolpyruvate synthase/pyruvate phosphate dikinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0574 is aompkz-qvdr-bcefg-snujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB002192 (Pyruvate phosphate dikinase, PEP/pyruvate-binding) with a combined E-value of 1.2e-104. IPB002192A 88-97 IPB002192B 165-176 IPB002192C 277-289 IPB002192D 490-506 IPB002192E 509-534 IPB002192F 565-574 IPB002192G 624-655 IPB002192H 701-713 IPB002192I 750-759 IPB002192J 795-805 IPB002192K 855-873 IPB002192L 920-929***** IPB008731 (PEP-utilising enzyme, N-terminal) with a combined E-value of 1.4e-23. IPB008731B 494-534 IPB008731D 732-762 IPB008731E 780-805 IPB008731F 848-891 IPB008731G 918-948 IPB008731C 642-671","","","-40% similar to PDB:2HRO Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus (E_value = 8.1E_28);","Residues 72 to 428 (E_value = 2.7e-165) place ANA_1733 in the PPDK_N family which is described as Pyruvate phosphate dikinase, PEP/pyruvate binding domain.Residues 477 to 569 (E_value = 4.3e-35) place ANA_1733 in the PEP-utilizers family which is described as PEP-utilising enzyme, mobile domain.Residues 604 to 964 (E_value = 2.2e-118) place ANA_1733 in the PEP-utilizers_C family which is described as PEP-utilising enzyme, TIM barrel domain.","","dikinase (ppdK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1734","1881670","1881215","456","4.80","-6.90","15756","ATGTCATCCGTGACCTATACCACCATTGTCGCCGGAGTCGGCGATGTCGAGGCGAACACCCACGTCATCGATCGCGCCTGCGAGATGGCTCGCCTGTGCGACGCCGCTCTTCTCCTCGTCGCCGGCTTCGACCCCGTCTCGGCGCGGGACAAGGCTCGCATCAACGAGTTTGCCCCCGTCGCCGATGTGCGGGTCGGGCTCACCGAGGACCAGGCCTACGCCGTCGTCGAGAAGGCGCGTGATATCGCCGTTGAGCGCGGCGTCGCCCTCGCCCAGGGCGTCGTCGTCGAGGGCACGGCGGTCGATGCCGTCACCCTCGTCACCTTGGAGACCGAGGCGGACCTCGTCATCGTCGGATCCAAAGGCGTCGATTCGCTGTTCGGCCGCGTCTTCGGAGCCGTCTCCGTCCAGGTGCTCCGCAAGTCGAAGTGCGACGTCCTCGTCGTCGTTCCCTAG","MSSVTYTTIVAGVGDVEANTHVIDRACEMARLCDAALLLVAGFDPVSARDKARINEFAPVADVRVGLTEDQAYAVVEKARDIAVERGVALAQGVVVEGTAVDAVTLVTLETEADLVIVGSKGVDSLFGRVFGAVSVQVLRKSKCDVLVVVP$","Universal stress protein UspA","Cytoplasm","universal stress protein family, putative","hypothetical protein","UspA domain protein","","Nystrom T., Neidhardt F.C. Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. Mol. Microbiol. 1994. 11(3):537-544. PMID: 8152377Sousa M.C., McKay D.B. Structure of the universal stress protein of Haemophilus influenzae. Structure 2001. 9(12):1135-1141. PMID: 11738040Zarembinski T.I., Hung L.W., Mueller-dieckmann H.J., Kim K.K., Yokota H., Kim R., Kim S.H. Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(26):15189-15193. PMID: 9860944","","","

InterPro
IPR006015
Family

Universal stress protein (Usp)
PR01438	$\"[110-122]T$ $\"[128-150]T$	UNVRSLSTRESS

InterPro
IPR006016
Domain

UspA
PF00582	$\"[5-151]T$	Usp

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[6-149]T$	no description

","BeTs to 15 clades of COG0589COG name: Universal stress protein UspA and related nucleotide-binding proteinsFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0589 is aompkzyq-drlbcefgh-n-jx---Number of proteins in this genome belonging to this COG is 2","***** IPB006015 (Universal stress protein signature) with a combined E-value of 2.4e-10. IPB006015B 110-122 IPB006015C 128-150","","","-52% similar to PDB:1TQ8 Crystal Structure of hypothetical protein Rv1636 from Mycobacterium tuberculosis H37Rv (E_value = 2.0E_12);","Residues 5 to 151 (E_value = 1.4e-12) place ANA_1734 in the Usp family which is described as Universal stress protein family.","","stress protein family, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1735","1883102","1881690","1413","8.55","6.20","50885","ATGGCACAGACTTCTCAGAATAGCGCGGCGGACATCGCGCACAAGCCCATGATGAGCACTGCTCAGATCCTGCTGATGAACGTCGGATTCTTCGGCATCCAGTACTCCTTCGGCATGCAGCAGAACGCCATGTCGCCCATCTACCAGTTCCTCGGGGCTTCCGCTGACGAGATCCCCATCCTCAATCTGGCCGGACCCGTCACCGGCCTGCTCATCCAACCGCTCATCGGGGCGCTCTCGGACCGGACCTGGAGCGAGAAGTGGGGACGCCGTAAGCCCTTCTTCCTGATCGGGGCCGTCGGCTGCTCCGTGTTCCTGTTCCTCATGCCCTTCGTCACCGCCTTGTGGATGGCGGTGCTGTGCCTGTGGCTGCTGGACGCCTCGAACAACACGGCCATGGAGCCCTACCGGGCCTTCATCGGCGACCGCCTGCCCTCCAAGCAGCTCGCCAAGGGCTTCCTCGCCCAGTCCCTGTTCATCGGCGCCGGCTCGGCCCTGGCCGCCGGGACCCTCGTCGTTCTGGAGAAGACCCTGGCGGGCGCCACCGCCGCCGGCATCCCCTACTGGGTCTTCGGCGCCTTCATGGTGGGCTCGGTGTGCTCCATCGGCTCGGTGCTCATCTCGGTGCTCTCCACCAAGGAGCTGCCGCCCACGCCGGAGGGCTTGGTCGAGCTCGAGCGCAAGAAGCGGGAGGAGGGCCCCTTCGGCTTCCTCAAGGACATCGGCGTCGCCATCGTCGAGATGCCCCGCGGCCTGAAGAAGATGGCCCTGGTCTACCTCTTCCAGTGGTACGCCATGAACGTCTTCTGGCAGTACCTGGGCCTCATGTGCGCCGTCACCTACTTCGGCGTGAACCTGTCCGACCCGGGGTACGCCAAGACCGAGGCCTTCAACGACGCCTCCGGCTTCGCCACCGGGCTCATGGTCGCCTACTACGTCTCCTGCACGGTCGTCGCCCTCTTCCTGGCGCGACTGTCCAACCGCATCGGCCCCAAGCACGTCCACACCGCGGCGCTGTTCCTCGCCGCCGTCTGCCTGGTCCTGCTCACCCGCATCGGCAGCCCCGGCCACACCGCGGTCCTCTACCTGCCCATGATCGGCATTGGTGTGGCCTGGGCTTCTATTACGGGCGTGCCCTACATCATGGCCATTGAGATGATCCGCAAGGAGCGCCGAGGCGTCTACATGGGCGTTATCAATATGATGATCGTCATCCCCCAGTTCATCCAGACCCTCACCTTCGGTCCCATTTACAAGCACCTGCTCGGCGATCACCCGGTCAACGCCATGCTCTTCGTCGCAGTCTTCCTCGTCATCGCCGGTCTGCTCATCGAGTGGATCGACACCGTCAAGGACGCGGACCCGCGGGTGCGCGCCGCCGCCGTGTCCGCCACTGAGACTGCCGTGGCCTGA","MAQTSQNSAADIAHKPMMSTAQILLMNVGFFGIQYSFGMQQNAMSPIYQFLGASADEIPILNLAGPVTGLLIQPLIGALSDRTWSEKWGRRKPFFLIGAVGCSVFLFLMPFVTALWMAVLCLWLLDASNNTAMEPYRAFIGDRLPSKQLAKGFLAQSLFIGAGSALAAGTLVVLEKTLAGATAAGIPYWVFGAFMVGSVCSIGSVLISVLSTKELPPTPEGLVELERKKREEGPFGFLKDIGVAIVEMPRGLKKMALVYLFQWYAMNVFWQYLGLMCAVTYFGVNLSDPGYAKTEAFNDASGFATGLMVAYYVSCTVVALFLARLSNRIGPKHVHTAALFLAAVCLVLLTRIGSPGHTAVLYLPMIGIGVAWASITGVPYIMAIEMIRKERRGVYMGVINMMIVIPQFIQTLTFGPIYKHLLGDHPVNAMLFVAVFLVIAGLLIEWIDTVKDADPRVRAAAVSATETAVA$","Sugar transporter","Membrane, Cytoplasm","sugar transporter","sugar transporter","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[22-452]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[26-419]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR19432	$\"[1-450]T$	SUGAR TRANSPORTER
PTHR19432:SF2	$\"[1-450]T$	SUCROSE TRANSPORT
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[21-39]?$ $\"[58-78]?$ $\"[93-108]?$ $\"[114-132]?$ $\"[153-173]?$ $\"[187-207]?$ $\"[263-283]?$ $\"[302-322]?$ $\"[337-357]?$ $\"[363-383]?$ $\"[398-418]?$ $\"[424-444]?$	transmembrane_regions

","BeTs to 15 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 419 (E_value = 5.8e-32) place ANA_1735 in the MFS_1 family which is described as Major Facilitator Superfamily.Residues 67 to 117 (E_value = 1.6e-06) place ANA_1735 in the Sugar_tr family which is described as Sugar (and other) transporter.","","transporter (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1736","1884258","1883305","954","5.05","-13.43","34122","ATGACGGTCCTGGCCTACCGGTGCCTGTCCTCCACGCGAGACTTCGAGCCGGACTCCATGCGCGCCTCGGGGCTGTCCTACCGCGAGGCCCGACGCCGCGGCTGGCTCGCCAGGCGTGACAACGGCGACCTGGTCGAGTGGAACACCTACCCCGGCCACTTCCAGGCCCGCGTGTGGGACCCCGACTACCGCGCCCGCTGGGTGGAGGAGGTCTGCCAGGCCACCGCTGAGACCGCCTTCGACGGCGTCATGGCGGACAACGACGTCTTCGACGACTACTACGGCCTGGACCTCCCCCTGGACGGAATCGCCGACACCGCCGCCCTGCGCGCCGAGTTGAACATCTTCGTGGACCAGGCCGGTGCCGGCCTCAACGGCGTCGGCAAGATCCTCATCCCCAACGTGGCCGAGGCCCGCCGGGAACCCGGCCGCTGGGAGCGCCACTCGGCCTGGGGTGGTGGCTTCGACGAGTGCTGGCTGGGCTGGGGGGACCATCACCTCTTCGATGAGGCCACGGCCCTGGCCCAGATTCACGAGCTGCGAGGGCCGGGCCTGTCCATCGTGCGCACGCCCGACGGCGGGGGCGGCGGCTCCATGTCCGGTGCCCGCACGTCCCCCGGCCTCTACGGGCTGGCGGCCTTCTGGGTCTTCGGGGGAGGGGAGGGCGCCTACACGGCCACCGGTCACGACGACTACTCGCGCACTCCCTGGTTCCCCGCCCTCGACGCCGACCTGGGGCGCCCGCTGGGACGGCCCCGGAGGACCTCGGGCGCCTGGGTGCGCGAGTTCGAGGGCGGAGTGGCCGCCGTCGCGCTCGGCGAGGAGGGAGGCGGCACCGTGCGTCTCCCGGCGGGCCTCAGGTCACCGGGGCCCACCGGGGACCCGGACGGTGAGGCGCTGGCTCTGGAGGTGCCCCTCAGTGCGCATTGTGGGATGATTGCCCTGCGTGCATGA","MTVLAYRCLSSTRDFEPDSMRASGLSYREARRRGWLARRDNGDLVEWNTYPGHFQARVWDPDYRARWVEEVCQATAETAFDGVMADNDVFDDYYGLDLPLDGIADTAALRAELNIFVDQAGAGLNGVGKILIPNVAEARREPGRWERHSAWGGGFDECWLGWGDHHLFDEATALAQIHELRGPGLSIVRTPDGGGGGSMSGARTSPGLYGLAAFWVFGGGEGAYTATGHDDYSRTPWFPALDADLGRPLGRPRRTSGAWVREFEGGVAAVALGEEGGGTVRLPAGLRSPGPTGDPDGEALALEVPLSAHCGMIALRA$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1737","1885991","1884411","1581","4.71","-47.64","59219","GTGTACGTGGACGTCGATGTCGCCATCGTCATGGAGTCCACCTACCCCTACCTCAAGGGCGGGGTCTCCGCGGTGGTCCACGACATCATCACCGGCAACCCGGACCTCACCTTCGGGATCATCCACATCACCTGGGACTCCCACTCGCCACTCAAGGACCTCTACGGCATGCCGGACAACGTCGCCTGGGTGAAGGTCCTCTACCTGTCCATGGAGGAGCACCAGGAGGACTTCCTGCGCGCCCGCCCGCGCGACCTGCGCATGAACCGCCGCCAGCGCCGCGAGCTGTCCCGGCGCATCCTGGGCGCGATGCTCTCCCTGGCTCAGGACGGCCAGACCGAGCCCCTGTGGGACCTCATCAGCGAGGGCCTGAGCGCCTCGCGCCGCTACCCGGTCTGGGCGATCCTGGGCACGCGCGAGTTCATGGAGGCCTACCACGACATGATGCCGGACCTGGGGATGTCGATGACCGACATCTTCTGGTGCCTGCGTGACTTCTTCTCCCTGGCCTACGCGGTCCTGGCCGAGCCGGTCCCGCGCGCCCAGGTCTACCACGCCCACACCACCGGCTACGCCATGCTCCTGGGCGTCAACGCCGCCCGCGAGCACGGCACCAAGGTGCTGCTGACCGAGCACAACCTCTATGTGCGCGACACCGTCAACACCCTCCTGGAACGCCGGCTGGACCTCAACGTCAGGCTCACCGACTACCGCACCTTCGACGTCAGCGGGCGCGAGCGCATGTGGATGGCCTGGTGGCTGGAGATGGGGCGCCTGTGCTACCCCTACGCCTACGCCTCCACCTACCTCTACCCGCGGGCCATCACCGAGGCCAATGAGCTCGGCGGCGACTCCGGGCGCGCCATCGTCATCCCCAACGGGATCGTCACCTCGGAGTTCGACGCCTCCTACGCTGCGCGCCTGGCGGCCATCGAGGAGATCAAGAAGGAGGGTGCGGACAAGCACCTGTGGAAGCTGGTGTACATCGCCCGCGTCGTGCCCATCAAGGGGCTGCTGGACATGATCGACTCGGTGCGCCTCATGGTGGACCGGGGCCTGAACATCCACCTGGACGTGTGCGGGCCCACCGAGCACATGCCCTCCTACTTCGAGCAGTGCCTGACCCGCATCGTCGAACTGGGCCTGGAGAGCGTCATCACCATCCGCGGCACCGTCAAGGTCCGCGAGCTCCTGCCCGAGTTCGACCTGTTCGTCCTGCCCAGCTACAACGAGGGCCTGCCGGTCGTGTCCCTGGAGACCATGGGGGCCGGCATCCCCACGGTGAGCACCGACGTCGGCGCCGTGCGCTCGGTCGTCGAGGACATGATCGTCACCGATGACGGACAGACCTGGGATCCCTGCGGCATCATCATCGAGCCCGGCGACCCCACCGTCATGGCGGACAAGGTCCAGGAGGTCATCTCCGACGTCGATCTCTACGAGCGTCTGAGCCTCAACGCCCGCGGCCGAGTGGAGGCGGCCTACGACCTGGTCAAGGTCAACGCCTCCTACAACACGATCTACCGTCAGGGGGGCGCCGGCGAGCAGACCGTTACCCGCACCGACCAAGGAGGAGCATGA","VYVDVDVAIVMESTYPYLKGGVSAVVHDIITGNPDLTFGIIHITWDSHSPLKDLYGMPDNVAWVKVLYLSMEEHQEDFLRARPRDLRMNRRQRRELSRRILGAMLSLAQDGQTEPLWDLISEGLSASRRYPVWAILGTREFMEAYHDMMPDLGMSMTDIFWCLRDFFSLAYAVLAEPVPRAQVYHAHTTGYAMLLGVNAAREHGTKVLLTEHNLYVRDTVNTLLERRLDLNVRLTDYRTFDVSGRERMWMAWWLEMGRLCYPYAYASTYLYPRAITEANELGGDSGRAIVIPNGIVTSEFDASYAARLAAIEEIKKEGADKHLWKLVYIARVVPIKGLLDMIDSVRLMVDRGLNIHLDVCGPTEHMPSYFEQCLTRIVELGLESVITIRGTVKVRELLPEFDLFVLPSYNEGLPVVSLETMGAGIPTVSTDVGAVRSVVEDMIVTDDGQTWDPCGIIIEPGDPTVMADKVQEVISDVDLYERLSLNARGRVEAAYDLVKVNASYNTIYRQGGAGEQTVTRTDQGGA$","Glycosyl transferase, group 1","Cytoplasm","glycosyl transferase, group 1 family proteindomain protein","glycosyl transferase; group 1","glycosyl transferase, group 1","","Munoz M.J., Bejarano E.R., Daga R.R., Jimenez J. The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts. Genetics 1999. 153(4):1561-1572. PMID: 10581266","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[638-818]T$	Glycos_transf_1

InterPro
IPR012642
Domain

Mitotic Wos2
SM00772	$\"[223-317]T$	no description

noIPR
unintegrated

unintegrated
PTHR12526	$\"[336-392]T$ $\"[481-559]T$ $\"[575-838]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF37	$\"[336-392]T$ $\"[481-559]T$ $\"[575-838]T$	GLYCOSYLTRANSFERASE
signalp	$\"[1-22]?$	signal-peptide

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[291-307]?$	SUGAR_TRANSPORT_1

noIPR
unintegrated

unintegrated
tmhmm	$\"[103-123]?$ $\"[129-149]?$ $\"[164-184]?$ $\"[203-223]?$ $\"[244-266]?$ $\"[272-294]?$ $\"[304-324]?$ $\"[386-406]?$ $\"[443-465]?$ $\"[471-491]?$ $\"[501-519]?$ $\"[525-545]?$	transmembrane_regions

InterPro
IPR001270
Family

Chaperonin clpA/B
PR00300	$\"[545-563]T$ $\"[590-608]T$ $\"[619-637]T$ $\"[652-666]T$	CLPPROTEASEA
PS00870	$\"[300-312]?$	CLPAB_1

InterPro
IPR001943
Domain

UvrB/UvrC protein
PF02151	$\"[421-456]T$	UVR
PS50151	$\"[421-456]T$	UVR

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[205-347]T$ $\"[541-720]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[208-292]T$	AAA

InterPro
IPR004176
Domain

Clp, N-terminal
PF02861	$\"[16-68]T$ $\"[91-143]T$	Clp_N

InterPro
IPR013093
Domain

ATPase AAA-2
PF07724	$\"[540-713]T$	AAA_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.60	$\"[719-824]T$	no description
G3DSA:3.40.50.300	$\"[164-356]T$ $\"[493-718]T$	no description
PTHR11638	$\"[1-642]T$	ATP-DEPENDENT CLP PROTEASE
PTHR11638:SF19	$\"[1-642]T$	ATP-DEPENDENT CLP PROTEASE

","BeTs to 20 clades of COG0542COG name: ATPases with chaperone activity, ATP-binding subunitFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0542 is --m---yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001270 (Chaperonin clpA/B) with a combined E-value of 1.5e-272. IPB001270A 184-236 IPB001270B 279-293 IPB001270C 302-356 IPB001270D 366-407 IPB001270E 506-556 IPB001270F 560-609 IPB001270G 610-663 IPB001270H 702-716 IPB001270I 742-787***** IPB013093 (ATPase AAA-2) with a combined E-value of 9e-218. IPB013093A 168-204 IPB013093B 206-227 IPB013093C 247-267 IPB013093D 280-293 IPB013093E 300-340 IPB013093F 362-402 IPB013093G 541-563 IPB013093H 575-625 IPB013093I 628-665 IPB013093B 542-563 IPB013093E 299-339 IPB013093G 205-227 IPB013093H 576-626***** IPB001943 (UvrB/UvrC protein) with a combined E-value of 6e-45. IPB001943A 211-220 IPB001943B 350-377 IPB001943C 542-553 IPB001943D 580-596 IPB001943E 626-667","","","-62% similar to PDB:1KSF Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains (E_value = 2.7E_139);-62% similar to PDB:1R6B High resolution crystal structure of ClpA (E_value = 2.7E_139);-79% similar to PDB:1JBK Crystal Structure of the First Nucelotide Binding Domain of ClpB (E_value = 1.4E_58);-78% similar to PDB:2P65 Crystal Structure of the first nucleotide binding domain of chaperone ClpB1, putative, (Pv089580) from Plasmodium Vivax (E_value = 6.7E_58);","Residues 16 to 68 (E_value = 4e-20) place ANA_1739 in the Clp_N family which is described as Clp amino terminal domain.Residues 91 to 143 (E_value = 4.3e-21) place ANA_1739 in the Clp_N family which is described as Clp amino terminal domain.Residues 208 to 400 (E_value = 9.5e-07) place ANA_1739 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).Residues 421 to 456 (E_value = 9.8e-08) place ANA_1739 in the UVR family which is described as UvrB/uvrC motif.Residues 540 to 713 (E_value = 5.7e-104) place ANA_1739 in the AAA_2 family which is described as ATPase family associated with various cellular activities (AAA).Residues 544 to 714 (E_value = 1.7e-05) place ANA_1739 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).","","Clp protease, ATP-binding subunit ClpC (CD4A)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1740","1892007","1894121","2115","7.12","1.06","75255","ATGCCTCCCGCGACTTCTCCCGCCGACGCCGACCACGACGACACGGCGCCGACCAACCCCGCCGGCAAGTCCACCGGTCAGGCCCCTGACACCGAGGCGCGGGACGCCGAGCGAGGGGCCACGGATATCGCGCAACGCCTTCTGCCCGCCCTGCCGACATTGAGAACCGGGGCGTTGCTCAGCGTCATCGGAGCCGTCGTGCTCTTCTTCGCCTGGGGAAGCGGCGTCCACGTCTTCGCCTTCGACTCCCGCAACGCCTGGTGGACACCCATATCCGGGATTCCGGCCTTCTGGGCGCTGTCCCTCCTTTTCCGCTCGCTACCCCACCGGTCCCAGGATCCTGACCACGGCAAATCCATCGCCACCGCACATAGGGTGGTCGCCACTCTGGCGATCAGCGGAATCGTGGTGTGCGCGGTCCGGCTCATATGGAAGGCTCTTTCAATATGGTCGTCCGTGCTATCCCGCACGGGAATCAACACCGTGGAACTCGCCGTCATCGCGGCAGGAACGGCGGGACTGGCCCTTCTGGCTGTCACCGACATTCTCATCCACACACTCTGGGCCACCGAACTATCACCGAATCCCCCACGGAGGAAAGGTTTGGCCCGCCTCCGGCGGTCCAGAAAGCCGGTTCGACACCCCGAAGGCCCGCGACGTCGGACACTCGCACGTGCCGCCCTGGTGCTGGCACCCTCCCTCATCCTTGCCGGGGCGGCGGCCGTCCCACTGAGCCGGCGCAATAAGGCCATTCAAAAGCTGGCTGCACCATCGGTCGCCAAGAACCTTCCCGCCTACCCCAACTCCATAGCCGGCAAGCCGGCCTGGGTCAAGGACATCGACAACGTCCTGGACATTGTGGCGGGAGCCGCCGGCCCCGTCATACACACGGCCGACGGCGTCATGGGCCTCAACCCCGCGGACGGCAGCGTCCTGTGGAGCTACGAACGCCCGAGTTCAACGTACCTAGAGACTTTCGGCAGTCTCCCTAACTTCACAGGCATAGGAACCCGTCGGACACTGGCGGTCAGCCCCGACCACCGCCACATCGCCTTTCGTATCGCCGGCCCCAGCAAATTGGCGGACCTTCCATATGCCGACCAGACAGCAGTGACGATCGTTTTGGACACCACCACCGGTCAGGTAACCAATGAACATCTCTCCGATGACGGCATCCTTCAGATCACCGATTCTGCGATCATGGACAGCAACAAGATCTACACCATCGGCAGCAACGTCGAGAGGTGGGATTTTGATAAGCACGGTACCATCCCCTTTGGGAGAGGGACGAACTACTCAGGGACAGCGGGACACTCAACCTTCATCGTCAATATCGACATTGACGTCGAAGACAGCCACGGCAACAGTAGCCCACAATACGGCCGCCTATCCCTTGTTTCACAGGACAATCCAGATCAGATCCACACCTCTCCACCATCTGCGCTGACAACAGAATCCCCAAATGCAATCAGCATTAACGGCTGGACGGCCATCTATCGGGACGGAGTCCCCACAAGCACCAACGGCTCCTTCCACAGGGGCTGGGAGATGCAAGCCGCCACTCTGGACTCCCTAGTCTCCGAAGAAGAATCTCAGCAGCAAAGACATGACCTGGGGCGAGGTGCGGGCATCAACGACAACGCATCAATCACCACAGGAAAGATCGTCACGCTTCCAGCAACAGCTTCGTCGTCAGCACAAGAGACCTTGACGGAGCACTCTTTCCTCTTCTGGAAGGAACCCACGACGATCTCAGCAGTCTTCGATCCCTCAACACAGAAGCTCCTACCCATGGACCAGCCCTCAGGCCTCATTCGAGCAATCGGTATATCACCAGAGAGCTCACCCGACAGCCTCGAAGCGAGGGTGCGACTCACCCCCATGAGTCACGGAGAGGAGGCCTCCTTCACTATTTCCACAGGAAGCATTTTCCACACACCAGGATCATATGAATACAATCCCGAAATGAAGGATGTCGCCATCCGAAGTTCTTCGAAGCTATCCGCACTCCACACCCCAGGCGCCAACATCATCATCCTCAACCCCACCGCGCGCCCCAATTTTGAGAGCCGATCCTATCGCCTCTACGGGATCACGGAGGCCACGAAGCAATGA","MPPATSPADADHDDTAPTNPAGKSTGQAPDTEARDAERGATDIAQRLLPALPTLRTGALLSVIGAVVLFFAWGSGVHVFAFDSRNAWWTPISGIPAFWALSLLFRSLPHRSQDPDHGKSIATAHRVVATLAISGIVVCAVRLIWKALSIWSSVLSRTGINTVELAVIAAGTAGLALLAVTDILIHTLWATELSPNPPRRKGLARLRRSRKPVRHPEGPRRRTLARAALVLAPSLILAGAAAVPLSRRNKAIQKLAAPSVAKNLPAYPNSIAGKPAWVKDIDNVLDIVAGAAGPVIHTADGVMGLNPADGSVLWSYERPSSTYLETFGSLPNFTGIGTRRTLAVSPDHRHIAFRIAGPSKLADLPYADQTAVTIVLDTTTGQVTNEHLSDDGILQITDSAIMDSNKIYTIGSNVERWDFDKHGTIPFGRGTNYSGTAGHSTFIVNIDIDVEDSHGNSSPQYGRLSLVSQDNPDQIHTSPPSALTTESPNAISINGWTAIYRDGVPTSTNGSFHRGWEMQAATLDSLVSEEESQQQRHDLGRGAGINDNASITTGKIVTLPATASSSAQETLTEHSFLFWKEPTTISAVFDPSTQKLLPMDQPSGLIRAIGISPESSPDSLEARVRLTPMSHGEEASFTISTGSIFHTPGSYEYNPEMKDVAIRSSSKLSALHTPGANIIILNPTARPNFESRSYRLYGITEATKQ$","Hypothetical protein","Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[59-81]?$ $\"[86-104]?$ $\"[123-143]?$ $\"[164-184]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-91]?$	signal-peptide
tmhmm	$\"[38-58]?$ $\"[72-90]?$ $\"[111-131]?$ $\"[150-170]?$ $\"[217-237]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[41-63]?$ $\"[77-97]?$ $\"[118-140]?$ $\"[150-170]?$ $\"[223-243]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-52]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[95-117]?$ $\"[127-149]?$ $\"[174-194]?$ $\"[204-224]?$ $\"[273-293]?$	transmembrane_regions

InterPro
IPR001957
Family

Bacterial chromosomal replication initiator protein, DnaA
PR00051	$\"[143-163]T$ $\"[173-187]T$ $\"[205-219]T$	DNAA

InterPro
IPR002611
Domain

IstB-like ATP-binding protein
PF01695	$\"[97-274]T$	IstB

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[142-275]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[106-251]T$	no description

","BeTs to 3 clades of COG1484COG name: DNA replication proteinFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1484 is -------q--rlb-e------j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB002611 (IstB-like ATP-binding protein) with a combined E-value of 4.8e-37. IPB002611A 82-108 IPB002611B 139-176 IPB002611C 236-269***** IPB001957 (Bacterial chromosomal replication initiator protein, DnaA) with a combined E-value of 7.4e-08. IPB001957A 143-162 IPB001957B 198-240***** IPB010921 (Trp repressor/replication initiator) with a combined E-value of 1.4e-06. IPB010921A 143-164***** IPB013317 (Chromosomal replication initiator, DnaA) with a combined E-value of 2.8e-06. IPB013317B 143-164","","","No significant hits to the PDB database (E-value < E-10).","Residues 97 to 274 (E_value = 1.4e-73) place ANA_1753 in the IstB family which is described as IstB-like ATP binding protein.","","sequence (AJ238712)","","1","","","Tue Aug 7 13:57:57 2007","","Tue Aug 7 13:57:57 2007","","","Tue Aug 7 13:57:57 2007","Tue Aug 7 13:57:57 2007","Tue Aug 7 13:57:57 2007","","","Tue Aug 7 13:57:57 2007","","","Tue Aug 7 13:57:57 2007","Tue Aug 7 13:57:57 2007","","","Tue Aug 7 13:57:57 2007","Tue Aug 7 13:57:57 2007","","","","","yes","","" "ANA_1754","1909374","1906789","2586","6.98","-0.29","89804","ATGTCGGCCACCCACGCCTGCCCTGATGGCGCGGCTGCCCCCTTGCGGCAGCCTCACCATCGCCGTCTGCAGAGCTTGACCAGACCTTCACCAAACCTCGCGAGCTCATTGACCTCGCCCCGTCACCGTGGAAGTGGAAGGAAAACCCCTTCCCCGAGCAGACAAGGACACGCCATGTACACGAGCCCCGACCAGGCCCCCCGCTCCTTCGGCGAGGCCCCCACCAGCACCACCCACCAGCACGGCAACTCCCACCAGCACGGACACGGCCGCCAGAACGGACATGCCCAGCAGCACGACACCCACGACAAGGGCACGTGGCTCTGCCCGATGCACCCCGAGGTGACCAGCGACCACCCGGGACGCTGCCCCAAGTGCGGGATGTTCCTGCAACCCGCCGACGGTGGGGACGCGCCGGCCGCACAGCACCACGACCACCAGCACCCCACCGGCGAGCCGGCGGTGGTGGCCGGTGCGGTCGCTGCAGGGGACTGGACCTGCCCAATGCACCCCGAGGTCCGCAGCGACGGCCCCGGTGACTGCCCGATCTGTGGCATGGCGCTGGAGCGGGTCTCGGCCGGGCTCGACGACGGCCCGAACCAGGAGCTCGTCGACATGCGTCGCCGGTTCCGGGTGGCGGCGGTGCTGAGCGTGCCGCTGGTGGCGATGGTGATGGTTCCCATGGTGCTGGGGCGTGCGCTGCCCGGCAGCGTCGCGCCGTGGCTCGAGCTGGCCCTGTCGACGCCGGTGGTGTGGTGGGCTGGGTGGCCGTTCTTCGTGCGCGGCGCGAAGTCGGTGGTCAGCCGTCACCTGAACATGTTCACCCTGGTGTCGTTGGGTGTCGGTGCCGCGTGGCTGTACAGCGTGGTCGCGGTGCTGGCGCCGGGGTTGTTCCCGTCCGGGATGCGGGCGATGGACGGCCGGGTCGGCACTTACTTCGAGGCCGCGGCAGTCATCATCACCCTGGTGCTGCTCGGCCAGGTCCTCGAGCTGCGGGCCCGCGACCAGACCTCCGGTGCGATCCGCACCCTGCTCGACCTGTCACCGGCCACCGCGCACCGCATCGGGGCCGACGGCACCGAGACCGACGTGCCGGCCGCCGAACTGCAGCTGGGCGATCGGTGCCGGGTGCGGCCGGGCGAGAAGGTGCCGGCCGACGGCACCGTGGTCGATGGTCACGCGTATGTGGACGAGTCGATGATCACCGGCGAGCCGGTTCCGGTCGACAAGAGCCCCGGTGACCGGGTCATCGGCGGCACGATCATCCAGGGCGGCAGCCTGGTGGTGGAGGCCACTGGCCTGGGCGCCGACTCGACCCTGGCCCGGATCGTCGACCTGGTCTCCCAGGCGCAGCGGTCCCGTGCTCCGATCCAGGGACTGGTCGACAAGATCTCGGCGGTGTTCGTGCCGGTCGTGATCGCCGTCGCCCTGGCCACCTTCGGGTTGTGGCTGGCGATTGGGCCGCAGCCGCGGCTGCCGTTCGCGATCGTGGCCGCCGTCAGCGTGCTGATCATCGCCTGCCCGTGTGCGCTGGGTCTGGCCACGCCAATGTCGATCATGGTCGGGGTCGGGCGCGGCGCCAGCGAGGGCGTGCTGGTCAAGAACGCCGAGGCCCTCGAACGACTGCAGAAGGTCGACACCGTCGTCGTCGACAAGACCGGTACCCTCACCCAGGGCCGCCCCAGCCTGGTCGACCAGCAGGGCGTCGACGGCCACGAGGACGCCCGGACACTGCTGCTCGCCGCGGCTGTGGAGGCCGGCTCCGAACACCCCCTCGCCAGGGCGGTGGTCGATGCTGCCCGCCAGACGGGACGCACGGTGCCGGCGGCCAGCGATTTCGCCGCCCACCCGGGTGGCGGTGTCAGCGCCACCGTCGACGGTCAGCACGTGCTCGTCGGCAGCCCCGCCTTCCTGGGCAGCCAGCACGTCGACACCCATGCCCTGGACGCCGTGGTGGAGGCCTACCGTCGCCGTGGCGCGACCGCGATCGTCGTGGCCGTCGATGGCAGGCCCGCCAGTGTGCTGGCCATCGCCGACCCGCTCAAGGCGACCACCGCCGGCGCGATCGAGGACCTGCGTCGGCGCGGGATGAAGGTCGTCATGCTCACCGGCGACAATGCCACCACCGCCCGGGCCATCGCCGACGAGCTGCGCATCGACCAGGTCGTCGCCGACGTCCTGCCCGACCAGAAGCACGGCCACGTGCAGGCCCTGCAGGCCCAGGGCCACACGGTCGTTATGGCCGGCGACGGCGTCAACGACGCCCCCGCCCTCGCCGTGGCCGACGTGGGTGTGGCCATGGGCACCGGCACCGACGTGGCCATCGAGAGCGCCGACGTGACCCTGCTCGGCGGTGACCTGGCCGCCCTGGTCAAGGCCCGCGACCTGTCGGTCGACACGATGCGCAACATCCGCCAGAACCTGGTCTTCGCGTTCGTGTACAACGTGTTCGGTATCCCGCTGGCCGCCGGCGCCCTCTACCCGACCTTTGGCTGGCTGCTGTCGCCCGTCATCGCGGCCGCCGCCATGGCCCTCAGCTCGGTCAGCGTGATCACCAACTCGCTGCGGTTGCGCCGTCACCGCTGA","MSATHACPDGAAAPLRQPHHRRLQSLTRPSPNLASSLTSPRHRGSGRKTPSPSRQGHAMYTSPDQAPRSFGEAPTSTTHQHGNSHQHGHGRQNGHAQQHDTHDKGTWLCPMHPEVTSDHPGRCPKCGMFLQPADGGDAPAAQHHDHQHPTGEPAVVAGAVAAGDWTCPMHPEVRSDGPGDCPICGMALERVSAGLDDGPNQELVDMRRRFRVAAVLSVPLVAMVMVPMVLGRALPGSVAPWLELALSTPVVWWAGWPFFVRGAKSVVSRHLNMFTLVSLGVGAAWLYSVVAVLAPGLFPSGMRAMDGRVGTYFEAAAVIITLVLLGQVLELRARDQTSGAIRTLLDLSPATAHRIGADGTETDVPAAELQLGDRCRVRPGEKVPADGTVVDGHAYVDESMITGEPVPVDKSPGDRVIGGTIIQGGSLVVEATGLGADSTLARIVDLVSQAQRSRAPIQGLVDKISAVFVPVVIAVALATFGLWLAIGPQPRLPFAIVAAVSVLIIACPCALGLATPMSIMVGVGRGASEGVLVKNAEALERLQKVDTVVVDKTGTLTQGRPSLVDQQGVDGHEDARTLLLAAAVEAGSEHPLARAVVDAARQTGRTVPAASDFAAHPGGGVSATVDGQHVLVGSPAFLGSQHVDTHALDAVVEAYRRRGATAIVVAVDGRPASVLAIADPLKATTAGAIEDLRRRGMKVVMLTGDNATTARAIADELRIDQVVADVLPDQKHGHVQALQAQGHTVVMAGDGVNDAPALAVADVGVAMGTGTDVAIESADVTLLGGDLAALVKARDLSVDTMRNIRQNLVFAFVYNVFGIPLAAGALYPTFGWLLSPVIAAAAMALSSVSVITNSLRLRRHR$","Heavy metal translocating P-type ATPase","Membrane, Cytoplasm","cation transporting P-type ATPase","heavy metal translocating P-type ATPase","heavy metal translocating P-type ATPase","","Smith D.L., Tao T., Maguire M.E. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 1993. 268(30):22469-22479. PMID: 8226755Fagan M.J., Saier Jr M.H. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 1994. 38(1):57-99. PMID: 8151716","","","

InterPro
IPR000579
Family

ATPase, P type cation-transporter
PR00940	$\"[245-267]T$ $\"[276-294]T$ $\"[350-369]T$ $\"[425-445]T$	CATPATPASEA

InterPro
IPR001757
Family

ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
PR00119	$\"[397-411]T$ $\"[549-563]T$ $\"[673-684]T$ $\"[695-705]T$ $\"[748-767]T$ $\"[771-783]T$	CATATPASE
PTHR11939	$\"[107-857]T$	CATION-TRANSPORTING ATPASE
TIGR01494	$\"[318-564]T$ $\"[646-843]T$	ATPase_P-type: ATPase, P-type (transporting
PS00154	$\"[551-557]?$	ATPASE_E1_E2

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[545-771]T$	Hydrolase

InterPro
IPR006403
Family

ATPase, P type cation/copper-transporter
TIGR01511	$\"[254-858]T$	ATPase-IB1_Cu: copper-translocating P-type

InterPro
IPR006416
Family

Heavy metal translocating P-type ATPase
TIGR01525	$\"[273-857]T$	ATPase-IB_hvy: heavy metal translocating P-

InterPro
IPR008250
Domain

E1-E2 ATPase-associated region
PF00122	$\"[318-541]T$	E1-E2_ATPase

noIPR
unintegrated

unintegrated
G3DSA:2.70.150.10	$\"[296-428]T$	no description
G3DSA:3.40.50.1000	$\"[668-792]T$	no description
PTHR11939:SF35	$\"[107-857]T$	COPPER-TRANSPORTING ATPASE P-TYPE ATPASE
tmhmm	$\"[212-232]?$ $\"[238-260]?$ $\"[270-290]?$ $\"[309-329]?$ $\"[464-484]?$ $\"[494-514]?$ $\"[808-828]?$ $\"[832-852]?$	transmembrane_regions

","BeTs to 23 clades of COG2217COG name: Cation transport ATPasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2217 is aompkzyqvdrlbcefgh-nuj-itwNumber of proteins in this genome belonging to this COG is 4","***** IPB006068 (Cation transporting ATPase, C-terminal) with a combined E-value of 6.8e-49. IPB006068B 364-404 IPB006068C 411-443 IPB006068E 528-554 IPB006068H 679-720 IPB006068I 723-755 IPB006068J 765-816***** IPB001756 (Copper-transporting ATPase signature) with a combined E-value of 9.6e-48. IPB001756C 237-255 IPB001756D 258-277 IPB001756E 316-335 IPB001756F 336-354 IPB001756G 470-484 IPB001756H 532-547 IPB001756I 725-742 IPB001756J 782-796 IPB001756K 821-835***** IPB008250 (E1-E2 ATPase-associated region) with a combined E-value of 8.2e-39. IPB008250A 549-559 IPB008250B 679-719 IPB008250C 745-768***** IPB000695 (H+-transporting ATPase (proton pump) signature) with a combined E-value of 8.3e-18. IPB000695B 720-736 IPB000695C 748-764 IPB000695D 779-804***** IPB001757 (ATPase, E1-E2 type) with a combined E-value of 6.2e-15. IPB001757A 549-559 IPB001757B 745-767***** IPB001366 (Cadmium-transporting ATPase signature) with a combined E-value of 1.9e-08. IPB001366F 331-351 IPB001366H 413-429 IPB001366I 432-446 IPB001366G 653-669***** IPB000579 (Cation-transporting P-type ATPase A signature) with a combined E-value of 3.8e-07. IPB000579D 245-267 IPB000579H 425-445","","","-60% similar to PDB:2B8E CopA ATP Binding Domain (E_value = 2.9E_45);-43% similar to PDB:1MHS Model of Neurospora crassa proton ATPase (E_value = 5.7E_33);-66% similar to PDB:2HC8 Structure of the A. fulgidus CopA A-domain (E_value = 3.1E_23);-48% similar to PDB:1IWO Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+ (E_value = 2.7E_14);-48% similar to PDB:1KJU Ca2+-ATPase in the E2 State (E_value = 2.7E_14);","Residues 318 to 541 (E_value = 5.1e-95) place ANA_1754 in the E1-E2_ATPase family which is described as E1-E2 ATPase.Residues 545 to 771 (E_value = 8.9e-33) place ANA_1754 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","transporting P-type ATPase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1755","1910872","1909388","1485","7.56","3.50","52975","ATGAACACACTTTCCCGCCGCCACGTGCTGTTCACCGGTCTCGGCCTGGCCTCGGCAGGGGCCTTGAGCGCCTGCGGCGCCAAGAACACCCCGGCCGCAGCACCCGCCGCGCCGAACTCCCCATTGACGATCCCCAGCCAGACCCCGCTGGTCGCAGCCCCCGGCACGAAGACCGTCAACCACGTCCTCACGCCCCGGCCGGTCACCCTCGATCTGGGCGGCGTCACGGCCAGGACTTGGGCCTACGACGAGACCCTCGACGCCCCCGTCCTGCGGGCCCGCGCCGGAGACCTGCTGCAGGTCCGCGTCGAGAACAAGCTTCCCACCAGCACCTCCGTCCACTGGCACGGCATCGCGCTGCGCCAGCCAAGCGACGGCGTGCCCGGCGTCACCCAGCAACCCATCGAGGCCGGCAGCAGCTTCACCTACCAGTTCGTCGCCCCCGACCCCGGCACCTACTTCTTCCACCCCCACACCGGGGTGCAGATCGACCGCGGCCTGTACCGGCCGCTGGTCATCGACGACCCCGCTGAACCCGGCCGCTACGACCACGAGTGGATCATCACCCTCGACGACTGGGCCGATGGCGTGGGCACCTCACCCGATGACATCCTCGCCGCGTTCAAGGCCCAGAACGGCACCGTGTCCAGCGGCATGAACCACGACATGGGCGGCATGGACCACGGCATGTCACCCTTGGGTGACGCCGGGGACGTCACCTACCCCCACTACCTCGTCAACGGCCGCGTCCCCGCCGCGCCCCGCACCCTGACCGCCAAGCCCGGGCAGAAGGTACGACTGCGCGTCGTCAACGCCTCCTCCGACACCATCTTCAAGCTCGCCCTGCAGGGCCATCGACTCACCGTCACCCACACCGACGGGTTCCCTGTGACCCCCACCCAGGCCAGCGCCGTCTACCTCGCGATGGGAGAACGACTGGATGCGACCATCACCCTCGGCGACGGCGTGTTCGTGCTGCAGGCCGCGCCCGAGGGCAAGAAGGGCACCCCGGCCCGCGCCATCGTGCGCACCGGCTCCGGCAACGTCCCGGCCCCGGACACCCGCATCGCAGAACTCGACGGCAAGGCCCTGCTGACCACCCAGCTCAAGCCCGCCGACAGCGCCCGACTGCCCGACCGCAAGCCCGACACCACCCTCGACGTGGCACTCAACGGCCAGATGAAGCCCTACGCGTGGGGCCTCAACGGCAAACGCTTCGGCGAGGACACCCCACTGGCGCTCAGCCGCGGCCAGCGCGTGCGGCTGCGGATGACGAACATGACGATGATGGCCCACCCCATGCACATCCACGGCCACACTTGGGCCCTGCCCGGCAGCGACGGGCTGCGCAAGGACACCGTCCTGATCCGCCCCATGGAGACCGTCGAGGCCGACCTGCAGGCCGACAACCCCGGCACCTGGATGCTGCACTGCCACAACATCTACCACGCCGAACTCGGCATGATGACGACCCTGCGCTACTGA","MNTLSRRHVLFTGLGLASAGALSACGAKNTPAAAPAAPNSPLTIPSQTPLVAAPGTKTVNHVLTPRPVTLDLGGVTARTWAYDETLDAPVLRARAGDLLQVRVENKLPTSTSVHWHGIALRQPSDGVPGVTQQPIEAGSSFTYQFVAPDPGTYFFHPHTGVQIDRGLYRPLVIDDPAEPGRYDHEWIITLDDWADGVGTSPDDILAAFKAQNGTVSSGMNHDMGGMDHGMSPLGDAGDVTYPHYLVNGRVPAAPRTLTAKPGQKVRLRVVNASSDTIFKLALQGHRLTVTHTDGFPVTPTQASAVYLAMGERLDATITLGDGVFVLQAAPEGKKGTPARAIVRTGSGNVPAPDTRIAELDGKALLTTQLKPADSARLPDRKPDTTLDVALNGQMKPYAWGLNGKRFGEDTPLALSRGQRVRLRMTNMTMMAHPMHIHGHTWALPGSDGLRKDTVLIRPMETVEADLQADNPGTWMLHCHNIYHAELGMMTTLRY$","Multicopper oxidase, type 3","Extracellular, Periplasm","potential multicopper oxidase","putative multicopper oxidase","multicopper oxidase, type 3","","Messerschmidt A., Huber R. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur. J. Biochem. 1990. 187(2):341-352. PMID: 2404764Ouzounis C., Sander C. A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins. FEBS Lett. 1991. 279(1):73-78. PMID: 1995346Roberts S.A., Weichsel A., Grass G., Thakali K., Hazzard J.T., Tollin G., Rensing C., Montfort W.R. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 2002. 99(5):2766-2771. PMID: 11867755","","","

InterPro
IPR001117
Domain

Multicopper oxidase, type 1
PF00394	$\"[184-347]T$	Cu-oxidase

InterPro
IPR002355
Binding_site

Multicopper oxidase, copper-binding site
PS00080	$\"[477-488]?$	MULTICOPPER_OXIDASE2

InterPro
IPR011706
Domain

Multicopper oxidase, type 2
PF07731	$\"[379-494]T$	Cu-oxidase_2

InterPro
IPR011707
Domain

Multicopper oxidase, type 3
PF07732	$\"[62-178]T$	Cu-oxidase_3

noIPR
unintegrated

unintegrated
G3DSA:2.60.40.420	$\"[22-176]T$ $\"[181-356]T$ $\"[370-492]T$	no description
PTHR11709	$\"[109-223]T$ $\"[254-494]T$	MULTI-COPPER OXIDASE
PTHR11709:SF4	$\"[109-223]T$ $\"[254-494]T$	MULTICOPPER OXIDASE
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-19]?$	signal-peptide

","BeTs to 11 clades of COG2132COG name: Putative multicopper oxidasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG2132 is -o----yq--r-b-ef-hsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB001117 (Multicopper oxidase, type 1) with a combined E-value of 4.1e-31. IPB001117A 93-105 IPB001117B 109-120 IPB001117C 151-169 IPB001117D 431-441 IPB001117E 469-488 IPB001117A 259-271 IPB001117C 472-490***** IPB011706 (Multicopper oxidase, type 2) with a combined E-value of 2.3e-12. IPB011706B 431-441 IPB011706C 471-483","","","-38% similar to PDB:1GYC CRYSTAL STRUCTURE DETERMINATION AT ROOM TEMPERATURE OF A LACCASE FROM TRAMETES VERSICOLOR IN ITS OXIDISED FORM CONTAINING A FULL COMPLEMENT OF COPPER IONS (E_value = 2.9E_28);-39% similar to PDB:1V10 STRUCTURE OF RIGIDOPORUS LIGNOSUS LACCASE FROM HEMIHEDRALLY TWINNED CRYSTALS (E_value = 9.5E_27);-38% similar to PDB:1KYA ACTIVE LACCASE FROM TRAMETES VERSICOLOR COMPLEXED WITH 2,5-XYLIDINE (E_value = 3.6E_26);-39% similar to PDB:1GW0 CRYSTAL STRUCTURE OF LACCASE FROM MELANOCARPUS ALBOMYCES IN FOUR COPPER FORM (E_value = 4.7E_26);-39% similar to PDB:2IH8 A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase (E_value = 4.7E_26);","Residues 61 to 177 (E_value = 2.2e-05) place ANA_1755 in the Cu-oxidase_2 family which is described as Multicopper oxidase.Residues 62 to 178 (E_value = 7.5e-38) place ANA_1755 in the Cu-oxidase_3 family which is described as Multicopper oxidase.Residues 184 to 347 (E_value = 5e-20) place ANA_1755 in the Cu-oxidase family which is described as Multicopper oxidase.Residues 379 to 494 (E_value = 1.7e-28) place ANA_1755 in the Cu-oxidase_2 family which is described as Multicopper oxidase.","","multicopper oxidase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1756","1912036","1910930","1107","6.48","-5.43","39129","ATGCCGCGCAACCCGCGCGGCAGTTGGGGACGCCGACTGCTGTGGACCCAGATGGCCGTGGTGGCGGCGATGGCCGCCACCACGGTGCTGACGGCACTGCTGGTCGGCCCGGCATGGTTCCGGATGCACATGCTCGAAGCCGGCCACGCCCAGCCCGATGTTGTCGAGCACGCTCAGCAGGCCTTCCACGACGCGGGCCTGGTGTCACTGGCCGTGGGTCTGGGCACCGCGATGCTCGCCGCCCTCGGGGTCGCCACCGTCCTCAACCGGAACCTGTCGCGCGGGGTCGAAGCCCTCGTGGACGGTGCCCAACATGTCGCCGCCGGACACTACGACCAACCCGTCATGATGACCTCGGCCAGCCCCGAGCTGACCCAGGTCGCTGACGCCTTTAACCACATGGCCAGCCAGATCGCCTCCACGGAGCAGACCCGACGACGCATGCTCACCGACCTGGGCCATGAGCTGCGCACCCCGCTGGCCGCCACCCAGGTCACCCTCGAAGGACTGCAGGACGGTGTGGTCGACTTCACCCCTGCAAACGTCGAGATCCTGCTAAGGCAGAACCAGCGGCTGGCCGCCCTGGCCGCCGACATCTCCGAGGTCTCCCGCGCCGAGGAAGGCCGCATCCCACTGTCGCTGAGCCACCAGGACCTCGACCAGATCGTGACGGCCAGCGTCGCCGCAGCCCGGCACGCCTACGACGCCGCCGGGGTGACGCTGCACGCCCAGACCGTTCCCGGCCTGCGCGTCGACGTGGATGCCGCTCGCATCGGGCAAGTCCTGGACAACCTGCTGCGCAACGCCCTGCAACACACGGTGGGCGGCAACCGGGTCGAGGTCGCGATGAGACACGAGCACGACCGGGCCGTGGTCCGCGTCACCGACAACGGCGTCGGCATCCCCACCGAGGCCCTCACCCACGTCTTCGAACGCTTCTACCGCGTCGAGGACACCCGCACTCGCGACGTCGACGGTGGAACCGGTGTCGGCCTGGCGATCTCCAGGGCCATTGCCCACGCCCACGGCGGTGACCTGACGGCCCACAGCGACGGCCCCGGCCACGGCGCAACCTTCGCGCTGACCCTGCCCACCGTGACTTCTTGA","MPRNPRGSWGRRLLWTQMAVVAAMAATTVLTALLVGPAWFRMHMLEAGHAQPDVVEHAQQAFHDAGLVSLAVGLGTAMLAALGVATVLNRNLSRGVEALVDGAQHVAAGHYDQPVMMTSASPELTQVADAFNHMASQIASTEQTRRRMLTDLGHELRTPLAATQVTLEGLQDGVVDFTPANVEILLRQNQRLAALAADISEVSRAEEGRIPLSLSHQDLDQIVTASVAAARHAYDAAGVTLHAQTVPGLRVDVDAARIGQVLDNLLRNALQHTVGGNRVEVAMRHEHDRAVVRVTDNGVGIPTEALTHVFERFYRVEDTRTRDVDGGTGVGLAISRAIAHAHGGDLTAHSDGPGHGATFALTLPTVTS$","Two-component system sensor kinase","Membrane, Cytoplasm","Two-component system, sensory transductionhistidine kinases","periplasmic sensor signal transduction histidine kinase","ATP-binding region, ATPase domain protein domain protein","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[214-364]T$	no description
PF02518	$\"[253-366]T$	HATPase_c
SM00387	$\"[253-367]T$	HATPase_c

InterPro
IPR003660
Domain

Histidine kinase, HAMP region
PF00672	$\"[70-140]T$	HAMP
SM00304	$\"[90-143]T$	HAMP
PS50885	$\"[90-143]T$	HAMP

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[144-208]T$	HisKA
SM00388	$\"[144-208]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[290-304]T$ $\"[308-318]T$ $\"[326-344]T$ $\"[351-364]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[151-367]T$	HIS_KIN

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.240	$\"[134-204]T$	no description
PTHR23283	$\"[67-365]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23	$\"[67-365]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[20-40]?$ $\"[65-85]?$	transmembrane_regions

","BeTs to 16 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB004358 (Bacterial sensor protein C-terminal signature) with a combined E-value of 5.3e-23. IPB004358A 290-304 IPB004358B 308-318 IPB004358C 326-344 IPB004358D 351-364***** IPB003661 (Histidine kinase A, N-terminal) with a combined E-value of 1e-12. IPB003661A 148-160 IPB003661B 294-313***** IPB003660 (Histidine kinase, HAMP region) with a combined E-value of 1e-08. IPB003660B 123-134 IPB003660C 329-347","","","-50% similar to PDB:2C2A STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN (E_value = 6.0E_20);","Residues 70 to 140 (E_value = 7e-10) place ANA_1756 in the HAMP family which is described as HAMP domain.Residues 144 to 208 (E_value = 8.5e-12) place ANA_1756 in the HisKA family which is described as His Kinase A (phosphoacceptor) domain.Residues 253 to 366 (E_value = 1.1e-36) place ANA_1756 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","system, sensory transduction histidine kinases","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1757","1912752","1912036","717","5.48","-5.91","25793","ATGAACAGCGCTTCTGTTGCGGTTGTACCGAGTGTCCTGGTCGTCGACGACGAGCCGGTGCTGTCGGGCACAGTGAAGAACTACCTCGAGCGGGCCGGCATGTCGGCCCAGACCTGCGGGGACGGGCTGGCCGCGCTTGACCTTGTCCGGGCCACGGCCCCCGACGTGGTGGTGCTGGATCTGGGCCTGCCGGGCATGGACGGGGTGGAGGTGTGCCGCCAGCTGCGCACCTTCAGCGACTGCTACGTGTTGATGCTCACGGCCCGCGCCGACGAGGTCGACAAGCTGATCGGGTTGTCGGTTGGCGCGGACGACTACATGACCAAACCGTTCAGCCCGCGTGAGCTGGTGGCTCGCATCCAGGTGCTGCTGAGACGCCCCCGCGCCGGAAGTACGGGCGCCACGGCCGCGGTGGTGCACCGCATCGGCGCCCTCACCCTGGACCCGTCGTCGCGTCGGGTGGAGCTCGACGCGTCACCGGTGGAGCTGACCCGTACCGAGTTCGACCTGTTGCAGGCCCTGGCGGAACACCCCGGTTGGGTGCTGAACCGCCGCCAGCTCACCGACGCCGTGTGGGGCGAGGACTGGGTCGGCGACGACCACCTGGTCGACGTGCACATCGCGCACCTGCGCAAGAAGCTCGGTGATGACCCCTCCCAGCCCCGGTTCGTGCAGACGGTGCGCGGCGTCGGCTACCGGATGGGCCAAGGGCAGTGA","MNSASVAVVPSVLVVDDEPVLSGTVKNYLERAGMSAQTCGDGLAALDLVRATAPDVVVLDLGLPGMDGVEVCRQLRTFSDCYVLMLTARADEVDKLIGLSVGADDYMTKPFSPRELVARIQVLLRRPRAGSTGATAAVVHRIGALTLDPSSRRVELDASPVELTRTEFDLLQALAEHPGWVLNRRQLTDAVWGEDWVGDDHLVDVHIAHLRKKLGDDPSQPRFVQTVRGVGYRMGQGQ$","Two-component system response regulator","Cytoplasm","Two-component system, response regulatorsconsisting of a CheY-like receiver domain and a HTH","two-component system; response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[25-125]T$	Q8NLH7_CORGL_Q8NLH7;
PF00072	$\"[10-121]T$	Response_reg
SM00448	$\"[10-120]T$	REC
PS50110	$\"[11-124]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[145-233]T$	Q8YS31_ANASP_Q8YS31;
PF00486	$\"[158-234]T$	Trans_reg_C

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[132-234]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[11-126]T$	no description
PTHR23283	$\"[10-126]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[10-126]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

noIPR
unintegrated

unintegrated
signalp	$\"[1-72]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[64-84]?$ $\"[105-125]?$ $\"[139-157]?$ $\"[172-192]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-71% similar to PDB:1IOK CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS DENITRIFICANS (E_value = );-54% similar to PDB:1ZT4 The crystal structure of human CD1d with and without alpha-Galactosylceramide (E_value = );-47% similar to PDB:2G23 The crystal structure of hexameric phenoxazinone synthase (E_value = );-41% similar to PDB:2HB6 Structure of Caenorhabditis elegans leucine aminopeptidase (LAP1) (E_value = );-41% similar to PDB:2HC9 Structure of Caenorhabditis elegans leucine aminopeptidase-zinc complex (LAP1) (E_value = );","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1760","1913682","1914938","1257","5.20","-14.91","43453","ATGAGCCAACAAGCCGTTTGGCACCCCCACCGCACGTCCACGGCACCTGCGCACCGTCAACATCGATCCTCCCGGCTGCTGCTCCTTGCCGCAGTACTACTGGCCCTCCCGTTGAGCGCCTGCGCCGGTCAGCTGACCTCGGCCCCGATCCAGGCCACACAGGAGGTCACCGTCAAGGCCACTGCGCTCACCGCCGAACAGGTCACGAGCCTCGAGGCCGATGCCAACACGGGCCCGGACATGGAGTTCCCAACGCTTCCCACTGAGAACAGCACCATCACGGTGCTCATCAACTGGCAGAAGAACCATCGCACGCCCGTGGGAACCACCCTCGTCAGCCGGAACCGATCAGACGGCGCCCTGAAGTGGGCGGTGACGATCACGCCGCCGGGCGCATCAAGCAACGCTCTGGAGAATGCAGACGCCCCGCAGCACAACGTCTCAGACCTGATGACGTCCCAAACCAGCGGAGAGATCGTCGTCAGCCCCGACGGGCGCCGCGTCTCCCTCATCCTCACCCCGCATCACGGACAGCTCGAGGAGAGGCTCGCCGAGCAGGAGTCCTACGTCGTCGTGCTGGACGCCACCAGCGGCGCCGTGGTGCGCACGGAGGAGCTCAACGGGGTGATCCTGGGGCAGGGTCTGACGAACGGCTCTCTGGCCGTGGAGACCGCCAACGACTACTTCCCCGGAGGTACGGGGGAGGGCCAAGTCCATGTCTTCGGGCTGGACGACCCATCCGCCCCGCCCTCGTCATTCGCCACCGATCAGTGGCTAGCGGGGGCCGGGACCGACTCGCTGCTGCTGTCACCGCAGCCGCCTTCCCCGTACGGGCCGGAAAGCAACTCCGGCGCATCAACGGTCACCCAGGTGGATACCTCCGGGAAGGTCCGCGCAACCATCAAGGGTGTTGAGGCCGTGCACCCCGGTGGCTGGGTGACACAGGTCAGTGACCCGGCAGCCGTCAATGCTTCGGCCAACCACGCGGCGACAGGCAAGAAGGAGAAACCGGCCTCTCTCAACGCTGCCCTGCAGGGCCTGACGCGGCAGGTCGTCAATGTCTCCACGGGAAGCAGCGTGGATGTCACCGGAACGATCGTCGAAGACCTGGGAGTCCCGACCGGACCCGGGCTGGTGGTCGGCCGGACGAGCACTGACGCGAGCGGTGAGACAACCTACACCCCGCTCTTCTGGCTCAGCTCTGCCGATGACGGACACCCCCACACCGAGAACCTTGAGCAGTTCACCAGCAAGTAG","MSQQAVWHPHRTSTAPAHRQHRSSRLLLLAAVLLALPLSACAGQLTSAPIQATQEVTVKATALTAEQVTSLEADANTGPDMEFPTLPTENSTITVLINWQKNHRTPVGTTLVSRNRSDGALKWAVTITPPGASSNALENADAPQHNVSDLMTSQTSGEIVVSPDGRRVSLILTPHHGQLEERLAEQESYVVVLDATSGAVVRTEELNGVILGQGLTNGSLAVETANDYFPGGTGEGQVHVFGLDDPSAPPSSFATDQWLAGAGTDSLLLSPQPPSPYGPESNSGASTVTQVDTSGKVRATIKGVEAVHPGGWVTQVSDPAAVNASANHAATGKKEKPASLNAALQGLTRQVVNVSTGSSVDVTGTIVEDLGVPTGPGLVVGRTSTDASGETTYTPLFWLSSADDGHPHTENLEQFTSK$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[26-46]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[80-100]?$ $\"[106-126]?$ $\"[152-174]?$ $\"[188-208]?$ $\"[239-259]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PS51257	$\"[1-31]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[13-33]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[109-129]?$ $\"[143-161]?$ $\"[170-190]?$ $\"[204-224]?$ $\"[279-299]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PS51257	$\"[1-34]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-41]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[47-67]?$ $\"[88-106]?$ $\"[125-145]?$ $\"[160-182]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PS51257	$\"[1-34]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-33]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[112-132]?$ $\"[151-169]?$ $\"[179-197]?$ $\"[216-236]?$ $\"[290-310]?$	transmembrane_regions

InterPro
IPR002139
Family

Ribokinase
PR00990	$\"[32-53]T$ $\"[59-78]T$ $\"[130-143]T$ $\"[199-214]T$ $\"[255-266]T$	RIBOKINASE

InterPro
IPR011611
Domain

PfkB
PF00294	$\"[27-334]T$	PfkB

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[29-340]T$	no description
PTHR10584	$\"[31-337]T$	SUGAR KINASE RELATED
PTHR10584:SF29	$\"[31-337]T$	RIBOKINASE

","BeTs to 18 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is 6","***** IPB002139 (Ribokinase signature) with a combined E-value of 9.7e-34. IPB002139A 32-53 IPB002139B 59-78 IPB002139C 130-143 IPB002139D 199-214 IPB002139E 255-266***** IPB002173 (Carbohydrate kinase, PfkB) with a combined E-value of 1.8e-10. IPB002173A 63-78 IPB002173B 283-296","","","-46% similar to PDB:2FV7 Crystal structure of human ribokinase (E_value = 8.7E_34);-49% similar to PDB:1GQT ACTIVATION OF RIBOKINASE BY MONOVALENT CATIONS (E_value = 5.3E_31);-49% similar to PDB:1RK2 E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP, SOLVED IN SPACE GROUP P212121 (E_value = 5.3E_31);-49% similar to PDB:1RKA THE APO FORM OF E. COLI RIBOKINASE (E_value = 5.3E_31);-49% similar to PDB:1RKD E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP (E_value = 5.3E_31);","Residues 27 to 334 (E_value = 1.4e-56) place ANA_1770 in the PfkB family which is described as pfkB family carbohydrate kinase.","","kinase in PfkB family (rbsK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1771","1930500","1929583","918","6.26","-2.16","32404","GTGATCGATGTGCAGCAGCTGCGGGCCCTCGTGGAGCTCTCCCGTCTCGGCACCGTCTCGGCCGCCGCCGAGTCCCTGGGCTTCAGCCAGTCCACCGTCTCCCACCAGCTCGCCGCCCTGTCGCGCGCAACCGGCGCGGTCCTGCTGACGCGGGCCGGACGCGGCGTACGGCTCACCGAGGAGGGCCGGGCGCTGGCGGCCCGCGGCCAGGAGGTTCTCGACCTGCTGGACCGCACCGAGCGCGAGGTCGTCTCCATGGCACGCGCCGAGGCGGGGCGCGTGCGCCTGGCCGCCTTCCCCTCCGCCGTGGCCTCCCTGGTGCCGGGGGTGCTCGACGTCGTCGGCCGGCAGTACCCGGGCCTGGAGGTCGAGCTCGTCGACGCCGAGCCGCCCGAGGCCCTCGACGCGCTGCGGCGCGGGCGGGTGGACGCGGCCCTGTCCTTCTCCTACGTCGACGACGACGCCGGCGAGGGCCTTCAGGCCGAGCACCTGCTCGACGACGTCCTCTACCTCGTCACCCATCCCGGCGGCATCACGCGCATCGCCGACGGCGCCCAGTGCCGGTGGGTGACCGGCTGCGCGCGCTGCCGCGAGGAGCTCCTCGCTGTGGGGCGGGCCAATGGGTTCACGCCCGAGACCGCCTACGCCTCCGACGACTATGTGGCCGTGCAGGCGCTCGTCGCCGCCGGGGTGGGGGCGGCCCTGCTGCCCGGGATGGCGCTGAGCGCCTACCGGCACGAGGGGGTCCAGGTGCGGCCCCTGGCCCGCGAGCAGCGGCGCGTCGAGGTGGTCACTCGCGCCGAGCAGCCCCGCCCGCTGGCCATCGACGTCCTGGTGGAGGCCTGCCAGGCGGCGGCCCTCCGCACGAGCCTGCGCCGACCGATGGTCAGGACCGGCAGGAGTGCTGCCTCACGGTGA","VIDVQQLRALVELSRLGTVSAAAESLGFSQSTVSHQLAALSRATGAVLLTRAGRGVRLTEEGRALAARGQEVLDLLDRTEREVVSMARAEAGRVRLAAFPSAVASLVPGVLDVVGRQYPGLEVELVDAEPPEALDALRRGRVDAALSFSYVDDDAGEGLQAEHLLDDVLYLVTHPGGITRIADGAQCRWVTGCARCREELLAVGRANGFTPETAYASDDYVAVQALVAAGVGAALLPGMALSAYRHEGVQVRPLAREQRRVEVVTRAEQPRPLAIDVLVEACQAAALRTSLRRPMVRTGRSAASR$","Transcriptional regulator, LysR family","Cytoplasm","putative LysR-family transcriptional regulator","LysR-family transcriptional regulator","LysR, substrate-binding","","Viale A.M., Kobayashi H., Akazawa T., Henikoff S. rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum. J. Bacteriol. 1991. 173(16):5224-5229. PMID: 1907267Sung Y.C., Fuchs J.A. The Escherichia coli K-12 cyn operon is positively regulated by a member of the lysR family. J. Bacteriol. 1992. 174(11):3645-3650. PMID: 1592818Kondorosi E., Pierre M., Cren M., Haumann U., Buire M., Hoffmann B., Schell J., Kondorosi A. Identification of NolR, a negative transacting factor controlling the nod regulon in Rhizobium meliloti. J. Mol. Biol. 1991. 222(4):885-896. PMID: 1840615Henikoff S., Haughn G.W., Calvo J.M., Wallace J.C. A large family of bacterial activator proteins. Proc. Natl. Acad. Sci. U.S.A. 1988. 85(18):6602-6606. PMID: 3413113Thony B., Hwang D.S., Fradkin L., Kornberg A. iciA, an Escherichia coli gene encoding a specific inhibitor of chromosomal initiation of replication in vitro. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(10):4066-4070. PMID: 2034653","","","

InterPro
IPR000847
Domain

Bacterial regulatory protein, LysR
PF00126	$\"[4-63]T$	HTH_1
PS50931	$\"[2-59]T$	HTH_LYSR

InterPro
IPR001199
Domain

Cytochrome b5
PS00191	$\"[170-177]?$	CYTOCHROME_B5_1

InterPro
IPR005119
Domain

LysR, substrate-binding
PF03466	$\"[87-287]T$	LysR_substrate

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[2-88]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[91-176]T$ $\"[196-257]T$	no description
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 13 clades of COG0583COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000847 (Bacterial regulatory protein LysR, HTH motif) with a combined E-value of 1.2e-13. IPB000847 7-51***** IPB005119 (LysR substrate binding domain) with a combined E-value of 1.8e-10. IPB005119A 19-41 IPB005119B 48-59","","","-47% similar to PDB:1IXC Crystal structure of CbnR, a LysR family transcriptional regulator (E_value = 1.3E_12);-47% similar to PDB:1IZ1 CRYSTAL STRUCTURE OF CBNR, A LYSR FAMILY TRANSCRIPTIONAL REGULATOR (E_value = 1.3E_12);","Residues 4 to 63 (E_value = 5.5e-16) place ANA_1771 in the HTH_1 family which is described as Bacterial regulatory helix-turn-helix protein, lysR family.Residues 87 to 287 (E_value = 4.2e-33) place ANA_1771 in the LysR_substrate family which is described as LysR substrate binding domain.","","LysR-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1772","1930583","1931608","1026","6.37","-3.80","34885","ATGACCGTCACCGACACCCTGCCCCAGGCTCCTGCCGACACTCAGTCCAGCCTCGACTTCGACGCCGTCCTGCGCACCTACGAGGTCGTCTCGCGGGTCCTGCCCGAGACTCCCGCCTGGTCCTACCCGCTGCTCAACGCCGAGGCCGGGGTGGAGGTCACGGTCAAGCACGAGAACGTCCAGCCCACCGGCGCCTTCAAGGTCCGCGGCGGGGTGGCGCTCATGGCGGCGCTCCGCCCCGAGGAGCGGCGCCGCGGCGTCGTGACCGCCTCCACCGGCAACCACGCCCAGTCCCTGGCCTGGGCGGGCGCCCGCAGCAAGGTCCCCGTGACCGTCGTCGTCCCGGTGGGCGCGCCGGCCCGCAAGGTGGCCGCGGTGCGCGCGCTGGGGGCTCGGGTCGTCGTGGAGGGAGAGACGATGTGCGAGTCGCTGGCGCACGCCGAGGCCCTCTCCCTGCGTGAGGGGATGCGCATGGTCTCCCCCGGGGACGAGCCGGCCATCGTGCTCGGGCACGCCACCGTCTACCTCGAGCTCTTCCGCCGTCACCCGGGCCTGGAAGCCGTCTACGCGCCGGTCGGCTCGGGCTCCGGGGCGGCAGGCGCCTGCCTCGTGCGCGACGTCCTGGCCCCCGGGTGCCGGGTCATCGGCGTCCAGTCCAGCGCCGCGCCGGCCGCGCACCGCGCCTGGACCTCCGGGGAGCCGGCCACCATCCACAGCCGCACGCGCGTGGCGGGGCTGGCCGTCGGGGCGAGCTTCGCCCTCACCCAGTCGGTGCTGGGTCGCAGCCTCAACGACTTCATCCTGGTCGACGACGAGGCGATCCAGGGCGCCGTCGGCCTCATGGCCACCCACGCCCACACCCTGGCTGAGGGCGCCGGGGCTGCGAGCCTGGCCGGGCTCATGGCCGATCCCACCCGCCAGGGCCCCTGCGCGATCGTCTGCACCGGCGGCAACGCCGACGACCACGAGCTCGCCGGCATCTCCGCCGGTTCCGTCGTCAGCACCGACGCGACCCTCAACTGCTGA","MTVTDTLPQAPADTQSSLDFDAVLRTYEVVSRVLPETPAWSYPLLNAEAGVEVTVKHENVQPTGAFKVRGGVALMAALRPEERRRGVVTASTGNHAQSLAWAGARSKVPVTVVVPVGAPARKVAAVRALGARVVVEGETMCESLAHAEALSLREGMRMVSPGDEPAIVLGHATVYLELFRRHPGLEAVYAPVGSGSGAAGACLVRDVLAPGCRVIGVQSSAAPAAHRAWTSGEPATIHSRTRVAGLAVGASFALTQSVLGRSLNDFILVDDEAIQGAVGLMATHAHTLAEGAGAASLAGLMADPTRQGPCAIVCTGGNADDHELAGISAGSVVSTDATLNC$","Threonine dehydratase","Cytoplasm, Membrane","threonine dehydratase biosynthetic","threonine dehydratase ","Pyridoxal-5'-phosphate-dependent enzyme, beta subunit","","","","","

InterPro
IPR001926
Domain

Pyridoxal phosphate-dependent enzyme, beta subunit
PF00291	$\"[30-317]T$	PALP

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1100	$\"[126-328]T$	no description
PTHR10314	$\"[45-243]T$ $\"[263-321]T$	SER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF17	$\"[45-243]T$ $\"[263-321]T$	THREONINE DEHYDRATASE-RELATED

","BeTs to 17 clades of COG1171COG name: Threonine dehydrataseFunctional Class: EThe phylogenetic pattern of COG1171 is ----Y-vcEbrh--------xNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-44% similar to PDB:1TDJ THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI (E_value = 3.4E_21);-46% similar to PDB:2GN0 Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 1.7 A resolution (Triclinic form with one complete subunit built in alternate conformation) (E_value = 3.2E_19);-46% similar to PDB:2GN1 Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 2.2A resolution (Triclinic form with one dimer of TdcB in the asymmetric unit) (E_value = 3.2E_19);-46% similar to PDB:2GN2 Crystal structure of tetrameric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium in complex with CMP at 2.5A resolution (Hexagonal form) (E_value = 3.2E_19);-41% similar to PDB:1V71 Crystal Structure of S.pombe Serine Racemase (E_value = 1.6E_18);","Residues 75 to 362 (E_value = 1.1e-34) place ANA_1772 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme.","","dehydratase biosynthetic (tdcB)","","1","","","Tue Aug 7 14:06:28 2007","","Tue Aug 7 14:06:28 2007","","","Tue Aug 7 14:06:28 2007","Tue Aug 7 14:06:28 2007","Tue Aug 7 14:06:28 2007","","","","","","Tue Aug 7 14:06:28 2007","Tue Aug 7 14:06:28 2007","","","Tue Aug 7 14:06:28 2007","Tue Aug 7 14:06:28 2007","","","","","yes","","" "ANA_1773","1931662","1932855","1194","10.93","28.06","44239","ATGCGGAGAATCGGGCGACACTCGGTTGAGGGCCGGGGAGCGCAGTCGGGGGCGCATACCCGGCCCTCTCCTCTGCCCCGGCGGCCCGCGCCGCCACAAGCGCTCTTGCGTCACCCCGCCACGGCCCCTCCCGCGGCCACGAGTGTCCACAGAAATGACATTAGCTCGCACAAGCCACCCGCCCACCACCTAGAACCACGGAATCACACGGTTTTCAAGCCAGCACCAACCTTGTCGGGCATCCAATGTCATTTCTGTGGACGTCAAGCAGGAGACGCGGCTCGTCAACGCCGGAAGTTATCCACAGGAACCAGCCACTTCCTAGCGCCTCAGCTCCGGCAGTCCAAGAATTGTCTCATGGACGACAATGTGCTGACCCGCATCGGCGATGCGCTTGGCGCCGTTGCACAGGCTGATCTACACCTGAACCGTACCGGGCGCCGCCGCCTCCAGGCCCTGGTAGACGCGGGCGAGCTCAAACGGTACCCGCACGGAATCGTAGCGCTGCCCGGCACCGACCGACGCATCCTCATCGCCCGCCTCCACCGAGGTCTTATCACCTGCGAGCATGCAGCCGCCTACTACGGCCTTCCGCTCCCTTCTCCACCGCGCAGTGTCCATGTTCTGACTCCACAAGGACGTCGATTACCTCCGTTATGGGGTGAGCACAGACACGAGACTCGTGGGCGTTCCGTCCTTCGGCTGGAAGACTTCCCGGTTGTCTCCCTCGCCCGCTGCATCGCCGATCTCCTGTGCTGCGCAGAAGAGTGGACGGCTCTGGTCGCCGCCGACGCAGCCCTGCATCGGGGCAGAACGACTCGCCAGCAGGTATCCGCATATCTGCGCGGTCCTCGCCGTGTTCTTGGCCGGAATCGCCTGAAGCGCACCAGCGATCGCGCTCGCAGCCCACTGGAGACCCTGGCCAGAGTTCAGCTGCAGGACGCTGGAATAGATGTTTCCGACGGCATGGTCATCTCAGACGTTGGAGAAGTGGACCTGGTGGTGGCCGGGTGGCTTGTCATCGAGCTGGACGGCTACGATTTCCATTCCGACCGTTGGTCCTTCCACCACGACCGGGAACGCGATCGCGAACTGGTCCGGCAGGGTTATACGCCCATCCGCTTCACGTCCAACAATGTGCGTTCAGGGAGGATCGTCACCGATGTCCAACGGATTCTCTCCACCCACCCATAG","MRRIGRHSVEGRGAQSGAHTRPSPLPRRPAPPQALLRHPATAPPAATSVHRNDISSHKPPAHHLEPRNHTVFKPAPTLSGIQCHFCGRQAGDAARQRRKLSTGTSHFLAPQLRQSKNCLMDDNVLTRIGDALGAVAQADLHLNRTGRRRLQALVDAGELKRYPHGIVALPGTDRRILIARLHRGLITCEHAAAYYGLPLPSPPRSVHVLTPQGRRLPPLWGEHRHETRGRSVLRLEDFPVVSLARCIADLLCCAEEWTALVAADAALHRGRTTRQQVSAYLRGPRRVLGRNRLKRTSDRARSPLETLARVQLQDAGIDVSDGMVISDVGEVDLVVAGWLVIELDGYDFHSDRWSFHHDRERDRELVRQGYTPIRFTSNNVRSGRIVTDVQRILSTHP$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1774","1933537","1933031","507","11.31","8.37","18497","ATGACAGGGCGCTCACGGGCGGTGGTGGTCGCCATGATGCTGTGGTGGGCCGTCTTCGGCTGTATCAGCGTCTCCTGGGCGCTGGGCTCCCCGTGGCTCGTCGACACGGTCCTTCAGGGTGAGGGGCTGAGGCTCGCCCAGGAGCGGCCCACCTGGTTCGTCGTGGTCGTCCTCGTCTCCGGGCTGGTGAAGTTGGGGTTCGTCGTCTTCGGCTTCGCGCTCCTGCGCCCGGATGTCATCAGGGTGCCGCGCTGGATGCGCCTGGCCTTCGGCTGGGTCTCAGGAGCCCTGCTCATCGCCTACGGGGTGGTCGGCTCGGTGCCGGCGATCCCGACAATCTTGTCGGGGGAACCGCTCTCCCGCTATGGCTGGTGGCGGCTGGTTCTGTGGATGCCTCACTTCTGGGCGGGTGGGATCCTGGTGCTGGCCGCGACGGTCGTATATTTTCGCTGGAGCCGGCCCGTGGCGATCGATCCCGCCGTGCATGCAGGACCCGCTGGGCGCTGA","MTGRSRAVVVAMMLWWAVFGCISVSWALGSPWLVDTVLQGEGLRLAQERPTWFVVVVLVSGLVKLGFVVFGFALLRPDVIRVPRWMRLAFGWVSGALLIAYGVVGSVPAIPTILSGEPLSRYGWWRLVLWMPHFWAGGILVLAATVVYFRWSRPVAIDPAVHAGPAGR$","Hypothetical protein","Membrane, Extracellular","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-21]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[12-34]?$ $\"[53-75]?$ $\"[90-110]?$ $\"[129-149]?$	transmembrane_regions

InterPro
IPR003732
Family

D-tyrosyl-tRNA(Tyr) deacylase
PD005653	$\"[11-139]T$	Q73ZI0_MYCPA_Q73ZI0;
G3DSA:3.50.80.10	$\"[1-141]T$	no description
PTHR10472	$\"[1-142]T$	D-TYROSYL-TRNA(TYR) DEACYLASE
PF02580	$\"[2-141]T$	Tyr_Deacylase
TIGR00256	$\"[1-142]T$	TIGR00256: D-tyrosyl-tRNA(Tyr) deacylase

noIPR
unintegrated

unintegrated
PTHR10472:SF4	$\"[1-142]T$	D-TYROSYL-TRNA(TYR) DEACYLASE

","BeTs to 11 clades of COG1490COG name: D-Tyr-tRNAtyr deacylaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1490 is ------yqvdrlb-efgh-n------Number of proteins in this genome belonging to this COG is 1","***** IPB003732 (D-tyrosyl-tRNA(Tyr) deacylase) with a combined E-value of 1.4e-54. IPB003732A 1-36 IPB003732B 57-105 IPB003732C 116-140","","","-57% similar to PDB:2DBO Crystal structure of D-Tyr-tRNA(Tyr) deacylase from Aquifex aeolicus (E_value = 5.3E_22);-57% similar to PDB:1JKE D-Tyr tRNATyr deacylase from Escherichia coli (E_value = 7.7E_21);-57% similar to PDB:1J7G Structure of YihZ from Haemophilus influenzae (HI0670), a D-Tyr-tRNA(Tyr) deacylase (E_value = 4.7E_18);-53% similar to PDB:2OKV c-Myc DNA Unwinding Element Binding Protein (E_value = 2.4E_14);","Residues 2 to 141 (E_value = 3.2e-70) place ANA_1775 in the Tyr_Deacylase family which is described as D-Tyr-tRNA(Tyr) deacylase.","","deacylase (dtd)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1776","1934385","1933996","390","11.66","10.16","13895","GTGAGCGTCCTTTATGCTGTGTCATTCTTTCTCTCCGAGGCGGTCAGGTGGAGCTGGTTGGCCGCCCAGTTCATCTCCCTCGTTATGGGGGTCTGGGCGCTGATCGACTCCCTGATGCGGCCCGCGGAGCACTACGCGGCGGCCGGTAAGAACACCAAGCGATTCTGGAACCTGGTCAACGCGGTGGGCACGGTGGTGGTCGGCCTGCTCGGGGCTGCCTCGATGTTCGGCCTGCTGGGCGTCGTGGCCAGTGCCGTCTACCTGGTGGACGTGCGCCCCGCCCTGCAGGCGCTGGCGCCGGTGCGGGTGCGCTCATCGATCCGCATCCCGGGGCGGGCCTCCCAGCGTCGGCCGGGGCGCGATGGGCGCGGCTGGAGCGCTGGTCGCTGA","VSVLYAVSFFLSEAVRWSWLAAQFISLVMGVWALIDSLMRPAEHYAAAGKNTKRFWNLVNAVGTVVVGLLGAASMFGLLGVVASAVYLVDVRPALQALAPVRVRSSIRIPGRASQRRPGRDGRGWSAGR$","Hypothetical protein","Extracellular, Membrane","putative membrane protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PD057095	$\"[19-93]T$	Q9FCG9_STRCO_Q9FCG9;
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[55-89]?$	transmembrane_regions

InterPro
IPR006222
Family

Glycine cleavage T protein (aminomethyl transferase)
PF01571	$\"[49-271]T$	GCV_T

InterPro
IPR013977
Domain

Glycine cleavage T-protein, C-terminal barrel
PF08669	$\"[280-332]T$	GCV_T_C

noIPR
unintegrated

unintegrated
PTHR13847	$\"[234-308]T$	FAD NAD BINDING OXIDOREDUCTASES
PTHR13847:SF1	$\"[234-308]T$	YIPPEE PROTEIN

","BeTs to 11 clades of COG0354COG name: Predicted aminomethyltransferase related to GcvTFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0354 is ------yq-dr--cefghsn-jx---Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 49 to 271 (E_value = 0.0024) place ANA_1777 in the GCV_T family which is described as Aminomethyltransferase folate-binding domain.Residues 280 to 374 (E_value = 0.00042) place ANA_1777 in the GCV_T_C family which is described as Glycine cleavage T-protein C-terminal barrel domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1779","1936567","1935818","750","4.15","-26.52","26565","ATGGCATTCACGCTTCCTGACGACCTGGCACCCGAGCTCTACCCGCTGGCCTGGCTGGCCGGCACCTGGCGCGGCTACGGCATCCTCACCTACGGCGAGACCGTGCCCGAGCAGGCCGTCTACCAGGAGATGACCTTCGACCACGACGGCGGCCCCTACCTGCGCCAGACCACCACCATCTGGACGGTCGACGCCACCCGCTCCAAGAACCTCGACTTCGAGATGCCCGGCCTCCAGGGCGCCTCCCTCCTGGCCCCCGCCCAGATCTGGTCCACCGAGACCACCTACTGGCGGCCTGTCGGCCAGGAGCAACCCGATGGCGCCGAGACCACTGAGCCCGCCGAGGACGACGCCGACACCAAGGGCTCCGGCGGTCCGCTCGTCCCCGTCACTCAGCTCGAGCTCGTCTCGGCCGACCCTGCCGGCCACGTCGCCGTCTGGGAGGGCTGGATCCAGGGGCCGCGCGCCCAGGTCGGCACCCAGGCCGTGGGCCGGGCCCGCACCGCTGTCCCCGTGGAGGAGATGACCCGCATGTTCGGGCTCGTGGGCGGCGACCTCATGTGGACCCAGGACATGGCCGCCTTCGGCCAGAGCGAGGTGACTACTTACGCCTCCGGCCGCCTCGGCCGCGTCGACGACTTAGATGACCCCGCCGCCCAGCCCGGCTCCGCCCTCGACCCGGCTGAGCCGGAGGGCGAGTCCTCCACCTCCTCCTCTCCCGCCTCCGACGACGCCGAGCCGACCGCCTGA","MAFTLPDDLAPELYPLAWLAGTWRGYGILTYGETVPEQAVYQEMTFDHDGGPYLRQTTTIWTVDATRSKNLDFEMPGLQGASLLAPAQIWSTETTYWRPVGQEQPDGAETTEPAEDDADTKGSGGPLVPVTQLELVSADPAGHVAVWEGWIQGPRAQVGTQAVGRARTAVPVEEMTRMFGLVGGDLMWTQDMAAFGQSEVTTYASGRLGRVDDLDDPAAQPGSALDPAEPEGESSTSSSPASDDAEPTA$","Hypothetical protein","Periplasm, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR014878
Domain

Domain of unknown function DUF1794
PF08768	$\"[8-211]T$	DUF1794

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 211 (E_value = 1.5e-17) place ANA_1779 in the DUF1794 family which is described as Domain of unknown function (DUF1794).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1782","1938007","1936871","1137","7.92","3.01","38080","ATGCGTTCTGTGACTACCCACCACCGACGAGCCCAACCGGCCGCGCGCACCCGCAGAGCCTCCCGCGGCTCGCGCCATGACTCCCATGCCGCAGCCGTTCCGACGGCCGCCGGTGGCGCGTCGGACTGGGCCAGCGTCATCGGCGCGGGCGACTCTCACGCCTCGGCCGGGCCCGACGGGTCGGAACCCACCGCGGCCTCAGCCGTCTCGGATGCCGTTGGTGAGCCGACCGGCTCCTCCGACGCTCCAGAGGCGGCCCGCTCGGCGGACTCAGGTGACACTGCCGACCTCGCCGAGGACCTGGGATACGCCACCCGTCGCGCCTCCAACCGCCCCAAGGAGCCGGGCCTGGTGGACCCGGCCTGGACCCGGCTCGCCTTCGCGGGCGTGGTGCCGCTGCTGCTGGCGGTCGGCTCAGTGCTGCCCGGCTGGGTGAGGCTGGCCCTCGTGGCCGTCCTGGTGCCGGCCGCCGCACAGGGCTGGCCCGCGCTCGTGCGCGCCCGGCACGACCTGGGCGGCACGATCGTCATGACGATCAGCGGGCTGTCGGCCGCAGTCAGCGTCTACCTCCTCGACGACATGGGGGTGGCCGGCCTGATCATGGCCTTCTCGATCCTGCTGGCCTTCGTCGGCCAGATGCTGCGCCGCGACGGCCGGCACAACCTGGTCGAGGACCTGTCCTCAACGGTGGCCGGCTGCCTCGTGGCGGTCTCCGGCTCGGCCTGGTGCGCCCTGGAACCGGGACTGGCCGACCCTGCCATCGTTGTGCCCACCTGCCTGGCGCTGTTCGTCGGCGCCGTCCTGACCGTCCTCAACGTGCGCGCCCGGATGTTGGAGGCCCTCACCGTCACGGTGCCGGCCCTGTTCGCCGGCGGCGCCGGCTACGTGCTGGCCTCGGCCGGCTTCTTCGGCCTGTCCCACATCAGTGCGACCGCGGCCCTGCAGAGTGCCGTGGCCTGCGTGGCCGTCGGCTTCGTGGCAGGGGTTCTCATGGCCTCGGGCAACCGCGTCCTGTGGACCCACCGCTGGGTGCCCGGTGGGCGGGCGGCGGTGGCCTCCGCGCTCGTGCCGATCCTGTCGGTCGGCGTACCGGTCTACGCCATCGCCCGCCTCCTGGGCGGCTTCATCGCCGGCTGA","MRSVTTHHRRAQPAARTRRASRGSRHDSHAAAVPTAAGGASDWASVIGAGDSHASAGPDGSEPTAASAVSDAVGEPTGSSDAPEAARSADSGDTADLAEDLGYATRRASNRPKEPGLVDPAWTRLAFAGVVPLLLAVGSVLPGWVRLALVAVLVPAAAQGWPALVRARHDLGGTIVMTISGLSAAVSVYLLDDMGVAGLIMAFSILLAFVGQMLRRDGRHNLVEDLSSTVAGCLVAVSGSAWCALEPGLADPAIVVPTCLALFVGAVLTVLNVRARMLEALTVTVPALFAGGAGYVLASAGFFGLSHISATAALQSAVACVAVGFVAGVLMASGNRVLWTHRWVPGGRAAVASALVPILSVGVPVYAIARLLGGFIAG$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[121-139]?$ $\"[145-165]?$ $\"[170-189]?$ $\"[195-213]?$ $\"[223-243]?$ $\"[253-273]?$ $\"[283-303]?$ $\"[309-329]?$ $\"[350-370]?$	transmembrane_regions

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[127-220]T$	Q8GD11_AMYMD_Q8GD11;
PF00486	$\"[142-217]T$	Trans_reg_C

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[117-217]T$	no description

noIPR
unintegrated

unintegrated
PD015901	$\"[3-126]T$	Q743D6_MYCPA_Q743D6;

","BeTs to 16 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 4.4e-07. IPB001867B 69-113 IPB001867C 207-217","","","-61% similar to PDB:2D1V Crystal structure of DNA-binding domain of Bacillus subtilis YycF (E_value = 8.7E_20);-63% similar to PDB:2HWV Crystal structure of an essential response regulator DNA binding domain, VicRc in Enterococcus faecalis, a member of the YycF subfamily. (E_value = 1.3E_18);-51% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 8.2E_18);-51% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 3.6E_13);-51% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 3.6E_13);","Residues 142 to 217 (E_value = 2.3e-25) place ANA_1784 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","REGULATORY PROTEIN","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1786","1940114","1939335","780","5.73","-3.40","28173","GTGTCCAAGCGCATCGACGTCATCGGCGAGAACATCTACTACGGCGACTTCCTGGCCGTGAAGGACGTCAACGTCGTCATCGAGCCCAAGTCCGTCACCGCCCTCATCGGCCCCTCCGGCTGCGGGAAGTCCACCTTCCTGCGCACCCTCAACCGCATGCATGAGACCATCCCCGGCGCCCGCGTCGAGGGGCAGGTCATCGTCGATGGCGTCAACCTCTACGGTCCCGGCGTCGATGCCGTCCAGGTGCGCCGCGCCATCGGCATGGTCTTCCAGCGGCCCAACCCCTTCCCCACCATGTCCATCGCCGAGAACGTCCTGGCCGGCGTGCGCCTCAACAACCGGCGCATCAAGAAGTCCGACGCGGACGACCTGGTGGAGGCCTCCCTACGCGGGGCCAACCTGTGGGACGAGGTCAAGGACCGTCTGGACCGGCCGGGCCTGGGACTGTCCGGCGGCCAGCAGCAGCGCCTGTGCATCGCCCGCGCCATCGCGGTCAAGCCCGCCGTCCTGCTCATGGACGAGCCCTGCTCCGCCCTGGACCCCATCTCTACGCTCGCCATCGAGGACCTCATCTCCGAGCTCAAGACGGACTACACGATCGTCATCGTCACCCACAACATGCAGCAGGCCTCGCGCGTGAGCGACATGACCGGATTCTTCAACCTGGAGGCCACCGGCAAGCCGGGGCACCTGGTCGAGTACGACTCCACCGACAAGATCTTCTCCGCCCCCAGCCAGCAAGCCACCGAGGACTACATCTCGGGCCGCTTCGGCTGA","VSKRIDVIGENIYYGDFLAVKDVNVVIEPKSVTALIGPSGCGKSTFLRTLNRMHETIPGARVEGQVIVDGVNLYGPGVDAVQVRRAIGMVFQRPNPFPTMSIAENVLAGVRLNNRRIKKSDADDLVEASLRGANLWDEVKDRLDRPGLGLSGGQQQRLCIARAIAVKPAVLLMDEPCSALDPISTLAIEDLISELKTDYTIVIVTHNMQQASRVSDMTGFFNLEATGKPGHLVEYDSTDKIFSAPSQQATEDYISGRFG$","ABC-type phosphate transport system, ATPase component","Membrane, Cytoplasm","PstB","phosphate transport system permease protein 1 ","phosphate ABC transporter, ATPase subunit","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[159-192]T$	PSTB_COREF_Q8FMN9;
PF00005	$\"[30-216]T$	ABC_tran
PS50893	$\"[2-248]T$	ABC_TRANSPORTER_2
PS00211	$\"[150-164]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[29-224]T$	AAA

InterPro
IPR005670
Family

Phosphate transport system permease protein 1
PTHR19222:SF24	$\"[5-257]T$	PHOSPHATE ABC TRANSPORTER
TIGR00972	$\"[4-259]T$	3a0107s01c2: phosphate ABC transporter, ATP

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[5-254]T$	no description
PTHR19222	$\"[5-257]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 20 clades of COG1117COG name: ABC-type phosphate transport system, ATPase componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1117 is aom-kz-qvdrlbcefghs-uj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.9e-26. IPB005074C 19-66 IPB005074D 138-181***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.1e-26. IPB013563A 19-53 IPB013563B 87-100 IPB013563C 147-174***** IPB005116 (TOBE domain) with a combined E-value of 4e-26. IPB005116A 37-53 IPB005116B 85-102 IPB005116C 150-163 IPB005116D 170-189 IPB005116E 202-215***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3.4e-15. IPB010509B 30-55 IPB010509D 145-189***** IPB010929 (CDR ABC transporter) with a combined E-value of 4.2e-09. IPB010929K 17-61 IPB010929M 147-193","","","-47% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 2.4E_19);-47% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 2.4E_19);-46% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 1.1E_16);-46% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 1.9E_16);-45% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 5.6E_16);","Residues 30 to 224 (E_value = 1.2e-54) place ANA_1786 in the ABC_tran family which is described as ABC transporter.","","(AF196490) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1787","1941418","1940195","1224","9.30","4.43","42322","ATGACGCCCACGAACACCCCCGAGCCCACCGCCGGCGCCGCTCCCGACGGCGCGGTCTCCCGCCCCGCCCCGGCCGCCGCTGCCGGTGCGGCCGGCGAGACCGTCACCCCCGCGCCCAAGTCCCTCAAGGCCGCGCTCGCGGCCGCCGAGGCCCCGGCCGCCCCCGTCGACCCCCTGGCCGACCCGCCCTCCATCGAGGGCGTGCCCCTGACCTCCTACCGCCTGCCCGACTGGTTCATCTGGGCTGCGCTGGGAGCCGCCTTCGTCGTCGTCGGCGGGATCGGCCTGCTGGCAGGGTGGAGCATCGCCGCCGTCGTGGCCCTGACCGCCCTGGTGTGGGTGGTGGGCGCCACCGCCGTCTCCTGGGTGCGCGAGGGCGAGCGCTGGGGCCGCAACACCCTGGTGACGCTCCTCATCTACCTGTCCTTCGCCGTCGTCATGGTGCCGCTGGTCTCCCTGGTGTGGATGGTCCTGTCGGGCGGCTCGGCCCGCTTTGGCTACGACTTCCTGACCACGAACATGCGCGGCGCCGACGCCTCCAACGGCGGCTTCTACCACGGCATCGTCGGCACCCTCCAGATCACCGGGATCGCTACCCTCATCTCGGTGCCCCTGGGGCTGTTCACCGCCGTCTTCCTCGTGGAGTACAACGGCGGCTGGATCGCCCGGGCCATCACCTTCCTCGTCGACGTCATGACCGGCATCCCCTCGATCGTGGCCGGGCTGTTCGCCTACTCGATCTTCCTCATCGCGGCCGGCCCCCGCTACCAGGCCGGCATCATCGGGGCCGTCGCCTTAAGCGTCCTCATGACGCCGGTGGTCATCCGCGGCGTGGAGGAGATGCTCAAGCTCGTTCCCTCCCACCTGCGCGAGGCCTCCTACGCGCTGGGCGTGCCCAAGTGGCTCACCATCGTCAAGGTTGTACTGCGCACCGCGGTGGCCGGCATCACCACCTCCGTCATGATCGCCATCGCCCGCGTCATCGGCGAGACCGCCCCGCTGCTCATCACTGTGGGCCTGACGATCCGCACCAACACCAACCCGCTGGACGGCTCCATGTCCACCCTGCCGGTGCTCGTCTACGACCAGTACTCCCGCGGGGAGGCCGCCGCCATGGAGCGGGCCTGGGCCGGGGCACTGACCCTCATCATCCTGGTCATGCTGCTCAACCTCGCGGCCCGCCTCATCTCCAAGTACTTCAGCCCCAAGGGCGGCCGGCGCTAG","MTPTNTPEPTAGAAPDGAVSRPAPAAAAGAAGETVTPAPKSLKAALAAAEAPAAPVDPLADPPSIEGVPLTSYRLPDWFIWAALGAAFVVVGGIGLLAGWSIAAVVALTALVWVVGATAVSWVREGERWGRNTLVTLLIYLSFAVVMVPLVSLVWMVLSGGSARFGYDFLTTNMRGADASNGGFYHGIVGTLQITGIATLISVPLGLFTAVFLVEYNGGWIARAITFLVDVMTGIPSIVAGLFAYSIFLIAAGPRYQAGIIGAVALSVLMTPVVIRGVEEMLKLVPSHLREASYALGVPKWLTIVKVVLRTAVAGITTSVMIAIARVIGETAPLLITVGLTIRTNTNPLDGSMSTLPVLVYDQYSRGEAAAMERAWAGALTLIILVMLLNLAARLISKYFSPKGGRR$","ABC-type phosphate transport system, permease component","Membrane, Cytoplasm","phosphate ABC transport system permease protein","K02038 phosphate transport system permease protein","phosphate ABC transporter, inner membrane subunit PstA","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[188-406]T$	BPD_transp_1
PS50928	$\"[188-393]T$	ABC_TM1

InterPro
IPR005672
Family

Phosphate transport system permease protein 2
TIGR00974	$\"[132-402]T$	3a0107s02c: phosphate ABC transporter, perm

noIPR
unintegrated

unintegrated
tmhmm	$\"[78-96]?$ $\"[102-122]?$ $\"[137-159]?$ $\"[194-214]?$ $\"[234-254]?$ $\"[260-278]?$ $\"[376-396]?$	transmembrane_regions

","BeTs to 20 clades of COG0581COG name: ABC-type phosphate transport system, permease componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0581 is aom-kz-qvdrlbcefghs-uj--twNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-51% similar to PDB:1E2X FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI (E_value = );-51% similar to PDB:1H9G FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, IN COMPLEX WITH MYRISTOYL-COA (E_value = );-51% similar to PDB:1H9T FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI IN COMPLEX WITH FADB OPERATOR (E_value = );-51% similar to PDB:1HW1 THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI (E_value = );-51% similar to PDB:1HW2 FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ECHERICHIA COLI (E_value = );","Residues 188 to 406 (E_value = 3.8e-25) place ANA_1787 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","ABC transport system permease protein (pstA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1789","1942436","1941420","1017","8.56","1.67","35583","GTGGCCAGCACCACCGCACCGCCGTCGTCGCCGCCCCCAACGGGAGCCGCGACCGCCTCCAGCAGCGCCGACGACGCCATCATCCAGCCCGGCAAGGCCCCCGGGCAGACCGGCAACCGGATCTTCACCGGCCTGTCCTTCGGCGCCGGCACCTTCATCATGGTGGTGCTCGCCCTCGTGGCCGCCTTCCTCATCCGGGAGGCGCTGCCCGCCCTGACGGCCTCGAGCGAGACCCTGGAGTCGGTCTCCTTCATGCGCGACCGCAGCCTGTGGGGCTATGTGGCCCCGCTCGTCTTCGGCACGCTGTTGTCCTCGACCATCGCTCTGGGCGTCGCGGTGCCGCTGAGCATCGGGGTGGCCCTGTTCATCTCCCACTTCGCCCCGCGCCGCCTGGCCCAGGCCCTGGGCTACATGGTGGACCTGCTGGCCGCGATCCCCTCCGTGGTCTTCGGCCTGTGGGGATTCCTGTGGCTGGTGCCGCTGCTCGACCCCCTCAACACCTGGCTGAGCGAGCACCTCGGATTCATCCCGCTGTTCGCCGACTACACGGCACCGGCCAAGAACATCACCACCGCCTCCCTGGTCCTGGCCGTCATGATCCTGCCGATCATCACCGCCACCATCCGCGAGATCTTCCTCCAGACGCCCACCCTCCAGGAGGAGGCCTCCCTGGCCCTGGGCGCCACCCGCTACGAGATGATCCGCCAGGCCGTCCTGCCCTTCGGCCGCTCCGGCATCATCTCCGCCTCCATGCTGGGGCTCGGGCGCGCCCTGGGGGAGACCATGGCCGTCCTCATGATCCTCTCGCCCGGCATGGGGCTGAACCTGCGTATCCTCCAGGCCGGCCAGCACCAGACCATCGCCGCCAACATCGCCTCGCAGTTCCGCGAGGCCTACGGATTGAGCGTCAACGTGCTCATCGCCACCGGCCTGGTCCTGTTCATCATCACCTTCGCGGTCAACTCCCTGGCGCGGTGGATCATCGCGCGCCGCTCCGAGTTCTCAGGAGCCAGCTGA","VASTTAPPSSPPPTGAATASSSADDAIIQPGKAPGQTGNRIFTGLSFGAGTFIMVVLALVAAFLIREALPALTASSETLESVSFMRDRSLWGYVAPLVFGTLLSSTIALGVAVPLSIGVALFISHFAPRRLAQALGYMVDLLAAIPSVVFGLWGFLWLVPLLDPLNTWLSEHLGFIPLFADYTAPAKNITTASLVLAVMILPIITATIREIFLQTPTLQEEASLALGATRYEMIRQAVLPFGRSGIISASMLGLGRALGETMAVLMILSPGMGLNLRILQAGQHQTIAANIASQFREAYGLSVNVLIATGLVLFIITFAVNSLARWIIARRSEFSGAS$","ABC-type phosphate transport system, permease component","Membrane, Cytoplasm","phosphate ABC transport system permease protein","phosphate ABC transporter; inner membrane subunit PstC","phosphate ABC transporter, inner membrane subunit PstC","","Saenz H.L., Augsburger V., Vuong C., Jack R.W., Gotz F, Otto M. Inducible expression and cellular location of AgrB, a protein involved in the maturation of the staphylococcal quorum-sensing pheromone. Arch. Microbiol. 2000. 174(6):452-455. PMID: 11195102Zhang L., Gray L., Novick R.P., Ji G. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 2002. 277(38):34736-34742. PMID: 12122003","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[98-333]T$	BPD_transp_1
PS50928	$\"[98-324]T$	ABC_TM1

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[63-232]T$	no description

InterPro
IPR011864
Family

Phosphate ABC transporter, permease protein PstC
TIGR02138	$\"[39-332]T$	phosphate_pstC: phosphate ABC transporter,

noIPR
unintegrated

unintegrated
signalp	$\"[1-62]?$	signal-peptide
tmhmm	$\"[45-65]?$ $\"[90-124]?$ $\"[139-159]?$ $\"[188-208]?$ $\"[252-272]?$ $\"[304-324]?$	transmembrane_regions

","BeTs to 20 clades of COG0573COG name: ABC-type phosphate transport system, permease componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0573 is aom-kz-qvdrlbcefghs-uj--twNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 98 to 333 (E_value = 2.7e-08) place ANA_1789 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","ABC transport system permease protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1790","1943601","1942528","1074","5.39","-5.36","36386","GTGCTCCTGACCCGTCGCGGCGCCCTGGGCGCCCTGAGCGTGGCCACCCTGACTGCGCTGACCGCCTGCGGGCGCGACGCCGGCGCCGCCGACCCCAACGCCTCCAGCGACCTGGTGGGGGAGATCCGCGGTGCGGGCGCCACCTCCCAGTCCGACGCGCAGGACGCCTGGATGAACACCTTCATGGGCGCCAACCTGCGCGCCACTGTCGACTACGCCGGCGGCGGCTCCGGGGCCGGGCGCACCAAGCTCGTCGAGGGTGCCGTCGACTTCGCCGGCACCGACACCCCCATGACCGCCGACGAGATCAGCCGGATCGGCGGCGCCGTCGAGCTGCCCCTCTACATCTCGCCCATCGCCGTGGCCTACAACCTGCCCGGCTTCACCGGCGAGTCCCACGTCAACATGACCGGCGAGGTCCTCGCCAAGGTCCTCTCCGGGGCCATCACCCGCTGGAACGACCCCGCCCTGGCCGCCCTCAACCCCGGCTTCGCCCTGCCCGACCTGCGAATCATCGTCGTGGGCCGCTCCGACGACTCCGGCACCACCAAGGCTCTGACCACCTACCTGGCCACCGTCGCCCCCAAGGCCTGGCCCCACGAGCCCGAGGAGACCTGGCCACTGCGCGGCGGCCAGTCCGGCGACGGCACCGCCGGCATGATCCAGACCGTTTCCGCGGCCACCGGCACCATCGGCTACGCCGACGCCTCCAAGGTCCCCGCCACCCTGGGAACCGTCGCCGTCGGCTCCAACGGGGCCTACGTGCCCGTCTCCGCCAAGGCCGCGGCCGCCGCCCTCGATGCCGCCACCCTGGGCTCCGAGGCCGACGAGACCCGCCTGCTCTACCAGCCCAGCCACGATGCCGAGGGCGCCTACCCCATCGTCCTGGTCTCCTACCTCGCCGCCCGCCTGCGCTACGACGACGCCCGGATCGCCGCCGTCGTCAAGGCCTACCTGCGCTTCGCCGCCTCCACCCGGGGGCAGGACGCCTCCACCAAGGCCACCGGCTGCGCCCCCATCACCCGCCAGATGCGCGAGAAGATCAACGCCGCCATCGACAAGATCGCCGCCTGA","VLLTRRGALGALSVATLTALTACGRDAGAADPNASSDLVGEIRGAGATSQSDAQDAWMNTFMGANLRATVDYAGGGSGAGRTKLVEGAVDFAGTDTPMTADEISRIGGAVELPLYISPIAVAYNLPGFTGESHVNMTGEVLAKVLSGAITRWNDPALAALNPGFALPDLRIIVVGRSDDSGTTKALTTYLATVAPKAWPHEPEETWPLRGGQSGDGTAGMIQTVSAATGTIGYADASKVPATLGTVAVGSNGAYVPVSAKAAAAALDAATLGSEADETRLLYQPSHDAEGAYPIVLVSYLAARLRYDDARIAAVVKAYLRFAASTRGQDASTKATGCAPITRQMREKINAAIDKIAA$","ABC-type phosphate transport system, periplasmic component","Extracellular, Membrane","phosphate-binding transport protein of ABCtransporter system","K02040 phosphate transport system substrate-binding protein","phosphate ABC transporter, periplasmic phosphate-binding protein","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR005673
Family

Periplasmic phosphate binding protein
TIGR00975	$\"[42-356]T$	3a0107s03: phosphate ABC transporter, phos

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[7-329]T$	SBP_bac_1

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[3-29]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[118-281]T$	no description
signalp	$\"[1-29]?$	signal-peptide

","BeTs to 15 clades of COG0226COG name: ABC-type phosphate transport system, periplasmic componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0226 is aom-kz-qvdrlbcefghs-uj--twNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-42% similar to PDB:1PC3 Crystal structure of the extracellular phosphate ABC transport receptor (PstS-1) and immunodominant antigen of M. tuberculosis. (E_value = 1.0E_24);-51% similar to PDB:1IXH PHOSPHATE-BINDING PROTEIN (PBP) COMPLEXED WITH PHOSPHATE (E_value = 1.3E_24);-51% similar to PDB:2ABH PHOSPHATE-BINDING PROTEIN (RE-REFINED) (E_value = 1.3E_24);-51% similar to PDB:1A54 PHOSPHATE-BINDING PROTEIN MUTANT A197C LABELLED WITH A COUMARIN FLUOROPHORE AND BOUND TO DIHYDROGENPHOSPHATE ION (E_value = 3.9E_24);-51% similar to PDB:1A55 PHOSPHATE-BINDING PROTEIN MUTANT A197C (E_value = 3.9E_24);","Residues 7 to 329 (E_value = 4.7e-11) place ANA_1790 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","transport protein of ABC transporter system (PHOS1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1792","1944832","1943804","1029","9.77","19.00","38203","ATGAGCCCGTCCAGCAAGAAGAACCGGTCGCGCGAGACCGTGAAGGCCGCCGGCGCCCTCGTGTGGCGTGAGAACGGCAAGCACCTCGAGGTGCTCCTGGTCCACCGTCCCCGCTACGACGACTGGTCCATCCCCAAGGGCAAGGTCGAGCCCTGCGAGTCGGTGCGCACCTGCGCCGTGCGCGAGGTCGCTGAGGAGACCGGCGTCCAGGTCATCCTGGGCCAGCCACTCAGCCGCGTGCACTACAAGATCGCCGACGGCTCGCGCAAGGAGGTCCACTACTGGGCCGCCCGCGTCGCCCCCGAGGCCTCGGCCGCCGTCGCCGCCCGCTGCGCCGTCAAGCCCGCCTCGACCAAGGAGATCGACGCCGTCGAGTGGCTGCGCGTGGGACAGGCCCGCAAGCGCCTGACCTACTCCTACGACCGCGACCTGCTCGGCGAGCTCGTCGACCTGTGGGAGGACGGCAAGCTCGACACCTGGACCCTGGTCCTCGTGCGCCACGGCCGCGCCGTCAAGCGCTCCGTATGGAACCGCCCCAAGGAGCGGGACAAGGAGACCGACGAGGCCACCCGCCCCCTGACCCACGACCAGGGCGAGACCCGGGCCCGCGCCCTCGTCCCGATCCTGGCCGCCTACGGGGTGGGGCGCGTCCTTACCAGCCCCTGGAAGCGCTGCGTGGACACGGTCGCCCCCTACGCCGCGGCCGCGGGCCTGGACCTGGAGACGGCCGGGGCGCTGACCGAGATGGCCCATGCGGAGAGCCCCAAGGGAGTGCGCTCCGTGGTCAAGAAGGTCCTTCGTGTGCGCGAGGAGCCGACGGCGCTGTGCACCCACCGGCCGGTCCTGCCCACCATCATGGAGGTCGTCTCCCAGTACGCCCCCGGCCGGCTCCTGCGCTCCGTGCCCGACCGGGACCCCTGGCTCAAGACCGGCGAGATCCTCGTGGTCCACATGGCCCGCCGCCCCCGCGGCAAGATCCGCGCCGTCGCCATCGAGAAGCAGCGCCCCGTCCTGTCCGAAGGCCGCTGA","MSPSSKKNRSRETVKAAGALVWRENGKHLEVLLVHRPRYDDWSIPKGKVEPCESVRTCAVREVAEETGVQVILGQPLSRVHYKIADGSRKEVHYWAARVAPEASAAVAARCAVKPASTKEIDAVEWLRVGQARKRLTYSYDRDLLGELVDLWEDGKLDTWTLVLVRHGRAVKRSVWNRPKERDKETDEATRPLTHDQGETRARALVPILAAYGVGRVLTSPWKRCVDTVAPYAAAAGLDLETAGALTEMAHAESPKGVRSVVKKVLRVREEPTALCTHRPVLPTIMEVVSQYAPGRLLRSVPDRDPWLKTGEILVVHMARRPRGKIRAVAIEKQRPVLSEGR$","NUDIX hydrolase","Cytoplasm","NTP pyrophosphohydrolases including oxidativedamage repair enzymes","hydrolase; NUDIX family protein","NUDIX hydrolase","","Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 1992. 174(20):6321-6325. PMID: 1328155Koonin E.V. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 1993. 21(20):4847-4847. PMID: 8233837Mejean V., Salles C., Bullions L.C., Bessman M.J., Claverys J.P. Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydrolases. Mol. Microbiol. 1994. 11(2):323-330. PMID: 8170394Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 1993. 268(31):23524-23530. PMID: 8226881McLennan A.G. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int. J. Mol. Med. 1999. 4(1):79-89. PMID: 10373642Bessman M.J., Frick D.N., O. Handley S.F. The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes. J. Biol. Chem. 1996. 271(41):25059-25062. PMID: 8810257","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[42-56]T$ $\"[56-71]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[12-155]T$	no description
PF00293	$\"[13-151]T$	NUDIX
PS00893	$\"[47-68]T$	NUDIX

InterPro
IPR013078
Domain

Phosphoglycerate mutase
PF00300	$\"[161-285]T$	PGAM

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1240	$\"[159-249]T$	no description
PTHR22769	$\"[19-103]T$	MUTT/NUDIX HYDROLASE

","BeTs to 17 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 8.4e-12. IPB000086 42-69","","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 151 (E_value = 1.4e-24) place ANA_1792 in the NUDIX family which is described as NUDIX domain.Residues 161 to 285 (E_value = 3.7e-09) place ANA_1792 in the PGAM family which is described as Phosphoglycerate mutase family.","","pyrophosphohydrolases including oxidative damage repair enzymes","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1793","1947730","1944845","2886","4.91","-57.26","104021","ATGCGTCACCCCAGCCCCCAGGAGCCCGAGCAGGTGCCCGACGCCGCCGAGGCGACCGAGGTTGTCGAAACCGCTGAAGCCACAGAGGCCGCCGAGTCGGCGGTCTCGCCCGAGGCCGCGAGCACCGACGGACCGGCTGTCTCCGCCGAGGTCCCCGGCCCCGACACCCAGGGCGAGCCCGACGCCGCTCCGACCGCCCCCGGCGACTCCTCCACCGGTGGCGCGGCCCCCGTGGGGCAGGAGACCCCTGAGCGCGCCGAGGCCCCGGAAGAATCAGGCGACCCCACCAACCCCACCAACCCCACCAACCCCACCAACCCCGACGACCCCGAGGGCGCCGAGGAGACAGTCGAGGAGGAGCACATCATCGAGGTCGCTGACCCGCGCGACTTCGCCGACGATTCCGGCCCCCAGTACGAGGACGAGGACTTCGACGACATCGTTGACGGCGAGGCGGCCCCCGCCCCCGGCCCCATCGGCACTGCGACCCCCGCCATCGCCCCCTCCTCCATCACCTCCGCCAGCTCGCACTCGGCCCCGTCGGCCGCCGAGGCTCAGACGGCGCCGGCCGCCACGGCATCGGGGGACCCGGGTCTGCCCGCTCCCGGCAGCGCCCCCAGCGCGGGCCCCGCCGCCGGCTCCGCCAGCGCCCCCTCCGCGCCCTCCTCACTGAGCGCGGCCGGCGCGGCCGACACGGCCGGTGCCGACGCCGCCGACGACGCCGCGGCCTCAGCCGCTTCCGCCGACACCGCCCAGGTGGATCCCGAGGATCTCCTGCCGCCCCTGAAGTCCTTCAAGAACCGCTTCATCGACCGCGAGCTGACCTGGCTGGACTTCAACGAGCGCGTCCTGGAGCAGGCCGAGGACCACACCCTGCCCCTGCTGGAGCGCGCCTGGTTCCTGTCGATCTTCTCCTCCAACCTGGACGAGTTCTACATGGTGCGCGTCGCCGGGCTCATGCGCCGCATCAAGGCCGGCATCACCCCGGTGCGCGCCTCCGGCCTGGACGCCCACCAGGTCCTGGCCCAGGTCACCAGCCGCACCAAGGAGCTCACCGCCCGCCAGGCCGCCCTCTTCCAAGAGGACATCCGCCCGGCCCTGGCCGAGCACAACGTGAAGATCCTTGGCTGGGACGAGCTCAACTCCGACCAGCAGGAGCGCCTGACCCGCTACTTCCGCCACCAGATCTACCCGGTCCTCACCCCGCTGGCGGTCGACCCTTCCCACCCCTTCCCCTACATCTCGGGCCTGTCCCTCAACCTCGCCGTCATCCTGCGCAACCCGCGCAGCGGCAAGGAGCACTTCGCCCGCATCAAGGTGCCCGACTCCCTGCCGCGCCTCATCCAGGTCCCCGGCCGCGAGCTCGACGCCGCGGACAAGGCCGCCGGCTGCGCCGTCATCCCCATCGAGATCGTCATCGGCCAGCACCTCGACCACCTCTTCCCGGGCATGGACATCCTGGAGCACCACCTCTTCCGGGTCACCCGCAACGAGGACCTCGAGGTCGAGGAGGACGACGCCGAGAACCTCCTCAAGGCCATGGAGAAGGAGCTCGAGCGGCGCCGCTTCGGCGACTGCGTGCGCCTGGAGGTGGAGGACACCATCTCCTCCTTCACCCGCCGCTACCTGGTGCGCGCCCTGGGCCTCAAGGGCGACGACGTCTTCGAGCTCCCCGCACCCCTGGACCTGACCTGCCTCAACCAGCTCCACGACCTGGACATCCCCGACCTGAAGTACCCGCGCTTCGTGCCGGTGACGGCCGCGGGCCTGGCCGCCTACGAGTCCTCCTCCGCGCCGGACGTCTTCGCCGCCATGCGTGAGCACGACGTCCTGCTGCACCACCCCTACGACTCCTTCTCCACCTCCGTCCAGGAGTTCGTGGCCCAGGCCGCCGCCGACCCCAAGGTCCTGGCCATCAAGCAGACCCTCTACCGCACCTCCGGCGACTCCCCGATCGTGGACGCCCTCATCGAGGCCGCCGAGGCCGGCAAGCAGGTCGTGGCCATCGTGGAGATCAAGGCCCGTTTCGATGAGGAGGCCAACATCTCCTGGGCCCGCAAGCTCGAGCGCGCCGGCGTCCACGTCGTCTACGGCATGGTCGGCCTCAAGACGCACTGCAAGCTGCTGCTGGTCGTGCGCCAGGAGTCCGACGGCCTGCGCCGCTACTGCCACGTCGGCACCGGCAACTACCACCCCAAGACCGCCCGCGGCTACGAGGACCTGGGGCTGCTGACCTGCGACCGCGACGTCGCCCAGGACCTGACCACCCTGTTCAACCAGCTCTCCGGCTACGCCCCGCGCGCCCGCTTCCGCCGCCTGCTCGTGGCCCCCCGCGGCCTGCGCGACGGGCTCGTGGAGCACATCGAGCAGGAGATCGCCAACCACAAGGCCGGCCTGCCCGCCTGGATCCGCATCAAGGTCAACTCCATCGTTGACGAGACCGTCATCGACGCCCTCTACCGCGCCTCGCGCGCCGGGGTGCCGGTCGACATCGTCGTGCGCGGCATCTGCGGCCTGCGCGCCGGCGTCGAGGGCCTCAGCGAGAACATCCGCGTCCGCTCGATCCTGGGGCGCTTCCTGGAGCACTCGCGCATCTACGCCTTCGCCGCCGGAGGCCAGACCGAGCTGTTCATCGGCTCGGCCGACCTCATGCACCGCAACCTCGACCGCCGCGTCGAGGCCCTGGTGCGCATCACCGACCCCGCCATGGTTGAGGACCTCGAGTGGCTGGTCACCCACTGCGCCTCCGACGACGTCGCCTCCTGGCACCTCCAGCCCGACGGCTCCTGGGAGCGTCGCCTCCTCGACGCCGAGGGCAACCGCCTCGAGGACATCCAGGACAGCCTCATGGCCCGGGCGCGCTCGCGCGTCAAGGGCCGGCACTGA","MRHPSPQEPEQVPDAAEATEVVETAEATEAAESAVSPEAASTDGPAVSAEVPGPDTQGEPDAAPTAPGDSSTGGAAPVGQETPERAEAPEESGDPTNPTNPTNPTNPDDPEGAEETVEEEHIIEVADPRDFADDSGPQYEDEDFDDIVDGEAAPAPGPIGTATPAIAPSSITSASSHSAPSAAEAQTAPAATASGDPGLPAPGSAPSAGPAAGSASAPSAPSSLSAAGAADTAGADAADDAAASAASADTAQVDPEDLLPPLKSFKNRFIDRELTWLDFNERVLEQAEDHTLPLLERAWFLSIFSSNLDEFYMVRVAGLMRRIKAGITPVRASGLDAHQVLAQVTSRTKELTARQAALFQEDIRPALAEHNVKILGWDELNSDQQERLTRYFRHQIYPVLTPLAVDPSHPFPYISGLSLNLAVILRNPRSGKEHFARIKVPDSLPRLIQVPGRELDAADKAAGCAVIPIEIVIGQHLDHLFPGMDILEHHLFRVTRNEDLEVEEDDAENLLKAMEKELERRRFGDCVRLEVEDTISSFTRRYLVRALGLKGDDVFELPAPLDLTCLNQLHDLDIPDLKYPRFVPVTAAGLAAYESSSAPDVFAAMREHDVLLHHPYDSFSTSVQEFVAQAAADPKVLAIKQTLYRTSGDSPIVDALIEAAEAGKQVVAIVEIKARFDEEANISWARKLERAGVHVVYGMVGLKTHCKLLLVVRQESDGLRRYCHVGTGNYHPKTARGYEDLGLLTCDRDVAQDLTTLFNQLSGYAPRARFRRLLVAPRGLRDGLVEHIEQEIANHKAGLPAWIRIKVNSIVDETVIDALYRASRAGVPVDIVVRGICGLRAGVEGLSENIRVRSILGRFLEHSRIYAFAAGGQTELFIGSADLMHRNLDRRVEALVRITDPAMVEDLEWLVTHCASDDVASWHLQPDGSWERRLLDAEGNRLEDIQDSLMARARSRVKGRH$","Polyphosphate kinase","Cytoplasm, Extracellular","polyphosphate kinase","polyphosphate kinase ","Polyphosphate kinase","","","","","

InterPro
IPR003414
Family

Polyphosphate kinase
PF02503	$\"[266-951]T$	PP_kinase

InterPro
IPR013989
Domain

Development and cell death
SM00767	$\"[303-394]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.870.10	$\"[641-772]T$	no description

","BeTs to 11 clades of COG0855COG name: Polyphosphate kinaseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0855 is ---------dr-bcefg-snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003414 (Polyphosphate kinase) with a combined E-value of 1.1e-178. IPB003414A 269-300 IPB003414B 301-315 IPB003414C 614-623 IPB003414D 649-698 IPB003414E 699-747 IPB003414F 806-856 IPB003414G 860-907***** IPB007758 (Nsp1-like, C-terminal) with a combined E-value of 1.7e-06. IPB007758C 204-248 IPB007758B 177-214 IPB007758C 207-251 IPB007758C 154-198 IPB007758C 200-244 IPB007758C 206-250 IPB007758C 195-239 IPB007758C 185-229 IPB007758C 211-255 IPB007758C 186-230 IPB007758C 203-247 IPB007758C 175-219","","","-57% similar to PDB:1XDO Crystal Structure of Escherichia coli Polyphosphate Kinase (E_value = 3.1E_104);-57% similar to PDB:1XDP Crystal Structure of the E.coli Polyphosphate Kinase in complex with AMPPNP (E_value = 3.1E_104);-55% similar to PDB:2O8R Crystal Structure of Polyphosphate Kinase from Porphyromonas Gingivalis (E_value = 2.7E_100);-49% similar to PDB:2FK5 Crystal structure of l-fuculose-1-phosphate aldolase from Thermus thermophilus HB8 (E_value = 2.7E_100);-49% similar to PDB:2FLF Crystal structure of l-fuculose-1-phosphate aldolase from Thermus Thermophilus HB8 (E_value = 2.7E_100);","Residues 266 to 951 (E_value = 0) place ANA_1793 in the PP_kinase family which is described as Polyphosphate kinase.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1794","1948712","1948050","663","4.56","-18.27","23445","ATGGCCCGCCAGTTCCACCGCCCCGCCCGGCTCGACCCCGAGGCCGCCGAACAGATCGAGGGCAGCACCGACACCGCCGTCGCCTCCGAGCTCGCCCACCGCGCCGCCCAGGCCCTCATCGGCGGCTTCCCCGGCACCGAGACCGAGGACGACCCCATCACCCGCTCCGGCGTCGTCGCCGCGGTCGCCACCAACGGCATCGACGACATCGCCGAGCTGTGGGCCGACTCCCCGGCCACCACCCTACCCGGCACCCTGTGGCGCCTCTTCCTCGTGCGCGAGTGGATCCGCCGCGACCCCGAGCTCGTCGCCCGCCGCTACGCCACTGTCATCGACCTCACCGAGGCCGACGACACCACGAACGCCCGCCTCGAGTCCGCCCTCGGCGAGGCGCGCCCCGTGCCTTCCCCGACCGACCTGCGCGAGCACCTCGACGCCGTCCTGGCCGGCAGCGTCGAGGGCTCGGTCACCGAGATCGCCCCGCTGCTGAGCGCCACCGCCGGATTCCTGCGCGCCCTGGCGGCCGGCTCCAACCCCGTGTGGATCGAGGACGACACCGACGAGCTCGCCGACCGCGTCACCCGCCGTGACTCCGCCCTCCTGGCCACCGCCGACGAGCTCACTGACGCCGCCCGCCGCGCCTCCGCCGGCCTCCTCGACTGA","MARQFHRPARLDPEAAEQIEGSTDTAVASELAHRAAQALIGGFPGTETEDDPITRSGVVAAVATNGIDDIAELWADSPATTLPGTLWRLFLVREWIRRDPELVARRYATVIDLTEADDTTNARLESALGEARPVPSPTDLREHLDAVLAGSVEGSVTEIAPLLSATAGFLRALAAGSNPVWIEDDTDELADRVTRRDSALLATADELTDAARRASAGLLD$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-44% similar to PDB:1A6D THERMOSOME FROM T. ACIDOPHILUM (E_value = );-44% similar to PDB:1A6E THERMOSOME-MG-ADP-ALF3 COMPLEX (E_value = );-44% similar to PDB:1ASS APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM (E_value = );-44% similar to PDB:1ASX APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM (E_value = );-54% similar to PDB:1Y97 The human TREX2 3' exonuclease structure suggests a mechanism for efficient non-processive DNA catalysis (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1797","1950192","1949338","855","4.62","-19.66","30045","ATGGTGGGCCTCATCCTGGCCGGCTGCGCTTCGCAGGGACCGCAGCGAGCGGCAACGCACTCGACTCCGCCGCCGTACCTGCGCTCGCGCGGGGCCGGCGCTGCGCCAAGCCTGCGGCCGACGTCGGGCGACCTGTCGGTTCCCGCCGCGTTCTCCTACACCGATGATGAGGACGAGACCTCCGACTGCATCTTCTACGCGACCACGGGAGCGCCGGTCGGACTGGTCGTCTACCTCGACGGCGACGGGCAGTCCTTCCACAGTGAAGGGAACCAGGACCAGGACGAGAGATCCCGCGGTGGCCTGGCCGGCGCCGGGGGAGTCGTCGAGGCGGCGAGCGCTCGCGGGTACGACGTGGTCTCGGTGCGCGCTCCCGGAGACGACGGGACCTGGTGGCTGGAGGATCAGGACGGCAAGGTCCACTACCTGGAGCAGGCGCTCGACTACGTGGTTGCCGAGTGCGGCGCCACCACGGATCGGGTCTGGCTCGTGGGCTACTCCGGCGGCTCGGAGTTCATCAGCCAGTGGTTCTTCCCGGCCTACGCCGAGCGCATGGCGGGTGGGGGCTTCCTGCTCTTCGGGGGCGGCGACGCGCCCGAGGAACAGGCGGCCTTCTCTTCAGGCGCCAAAGAGCGGCTCTGGCTGAACTGGGTGACCGGGACACGCGACGTGCCCGCCAACAGCCTCGACGGATTCGACGGCAGCGGGCATGCCCGCAACAGCCTGGCCTACTACCGCTCGGCGGGCTTCGGCCACACCTGGAGCGAATGGCCCGACGACGACCATGGCAGCATCACCGAGAAGTTCGGCAGCTACGTCGGTCGCGTGCTCGACGCCGCTGAAAACGGAAAATGA","MVGLILAGCASQGPQRAATHSTPPPYLRSRGAGAAPSLRPTSGDLSVPAAFSYTDDEDETSDCIFYATTGAPVGLVVYLDGDGQSFHSEGNQDQDERSRGGLAGAGGVVEAASARGYDVVSVRAPGDDGTWWLEDQDGKVHYLEQALDYVVAECGATTDRVWLVGYSGGSEFISQWFFPAYAERMAGGGFLLFGGGDAPEEQAAFSSGAKERLWLNWVTGTRDVPANSLDGFDGSGHARNSLAYYRSAGFGHTWSEWPDDDHGSITEKFGSYVGRVLDAAENGK$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-69% similar to PDB:1K6W The Structure of Escherichia coli Cytosine Deaminase (E_value = );-69% similar to PDB:1K70 The Structure of Escherichia coli Cytosine Deaminase bound to 4-Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-one (E_value = );-69% similar to PDB:1R9X Bacterial cytosine deaminase D314G mutant. (E_value = );-69% similar to PDB:1R9Y Bacterial cytosine deaminase D314A mutant. (E_value = );-69% similar to PDB:1R9Z Bacterial cytosine deaminase D314S mutant. (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1799","1950784","1950359","426","5.26","-4.36","14953","GTGGACTACAACGCCACGCTCACGATTCACACGAACAAGCCCGCCACTGAGAATGACGACATCGACGACGTCATGGAGGCCTTCGCCTCCTACCACCCCGCCGTCGGGGACGCACCCGCATGCCCCGGGGCTCTCAATGCAGTCATCACCCTGCCCGCCCACACGCTGACCCAGGCCGTGGCCACAGCCACCGCCCTGGCCGCCCAGGTCGGCGACCTGGTGGGGATCGAGGTCATCCCCACCAGAATGTGGGACCGCCGCGAGAGCCTGAAGATCGACGACGTCGAGTTCGTGGGCGTGTCCGAGGCTGCCGTCCGGCTCGGGATCACTCCGCAGGCGGTGCGCGACCGCATCACCTCCGGGCGCCTGCCCGGCAAGAAGGTCGGACGCAACTGGGTCGTGTCCGACGCCGCGCTCCCGCGCTGA","VDYNATLTIHTNKPATENDDIDDVMEAFASYHPAVGDAPACPGALNAVITLPAHTLTQAVATATALAAQVGDLVGIEVIPTRMWDRRESLKIDDVEFVGVSEAAVRLGITPQAVRDRITSGRLPGKKVGRNWVVSDAALPR$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:2BX6 CRYSTAL STRUCTURE OF THE HUMAN RETINITIS PIGMENTOSA PROTEIN 2 (RP2) (E_value = );-51% similar to PDB:1W25 RESPONSE REGULATOR PLED IN COMPLEX WITH C-DIGMP (E_value = );-52% similar to PDB:1JOI STRUCTURE OF PSEUDOMONAS FLUORESCENS HOLO AZURIN (E_value = );-56% similar to PDB:1SOR Aquaporin-0 membrane junctions reveal the structure of a closed water pore (E_value = );-56% similar to PDB:1YMG The Channel Architecture of Aquaporin O at 2.2 Angstrom Resolution (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1800","1952609","1950849","1761","10.81","26.84","60800","TTGCGGGATCTCAGGCAGGATGGCTCCCTGGTCCGGGCGCCGCCCGGCCTGGCTGGTGCCCCGGCCCCGGCGCGCGTCGCCCCACAGACGCTCCGCGCCGTTGAGCCGCGTACGCCGGCACCTCACGCACCGACGCGCACGCTGCCAGCGACACGCGCCGGCGTGCCCGCGGTCCCAAACGACAGGATCCTCGTGGCCGCACACCGCACCTCCGCCTCACACCGCTTCGCCTCCGGGAAGACCCCGGCCGCGGGTGAGACCACCTTCGCCGACCTCGGCGTGGACTCAGACCTCGCCGCCGACCTCGACGCCCGCGGCTTCACCGCGCCCTTCCCCATTCAGGCCGCCACCCTGCCTGACACCCTCGCCGGGCGTGACGTGCTCGGCCGCGGCCGCACCGGCTCGGGCAAGACCCTGGCCTTCAGCCTGCCGCTGGTCCAGCGTCTGGCGCAGCAGGACAAGGCCCGCCCCGGCCACCCCATCGGCCTGGTCCTGGCCCCCACCCGTGAGCTCGCCCTCCAGATCGCCGAGGTTATCGAGCCCCTGGCCCGCGTCGTCGACATGGACGTCACCACCATCTTCGGCGGGGTCTCCGCCAAGCCCCAGGAGAAGGCCCTCAAGGCTGGGGTCGACGTCGTCGTCGCCTGCCCCGGCCGGCTCCTGGACCTCATGGGGCAGGGGCTCGTCAGTCTCGACGAGGTCGAGATCACCGTCCTGGACGAGGCCGACCACATGGCCGACCTCGGCTTCCTGCCCAATGTCCGCCGCATCCTGCGCGCCACCCCGCAGCGCGGCCAGCGCCTGCTGTTCTCCGCGACCCTGGACAACGGCGTGGACACCCTGGTCAAGGAGTTCCTCCACGACCCGCTGCAGCACTCCGTGGACCCCTCGACCTCGCCCGTGGACGCCATGACTCACCGCGTGTGGATGGTCGCGGACAAGACCGCCAAGGACGGCATCGTGCGGCGCCTGGCCTCGGGGGAGGGGCAGCGCATCCTGTTCACCCGCACCAAGCACCTCGCCCGGCGCCTGGCCCGCAAGCTCGTCCAAGCCGGGATTCCGGCCGTCGAGCTCCAGGGCAACATGAGCCAGAACGCGCGCGAGCGCGCCATGAGGGCCTTCTCGACCGGACAGGTGCACGTCATGGTCGCCACCGACATCGCCGCCCGGGGCATCGACGTCTCCGGCGTCGAGCTCGTCGTCCACGTCGACCCGCCCGCCGAGCACAAGGCCTACCTGCACCGCTCGGGCCGCACCGCGCGCGCCGGGGCCGCCGGCAGCGTCATCACCCTGGTCCTGCCTGAGCAGAAGCACGATGTGCAGGTCCTGCTCAAGAAGGCGCGGATCCGCGCGGACATCGAGCGTATCCGTCCCGACGACGACGCCGTGTCCGCCCTCGTGGGGCAGGTCGCCGAGGCCGTGGCGTTGGAGGACATGCCCGAGGGTGTTGCCATCAAGGGCGGCAGCCCCAGCGGTCGGGCCTCCACCGGGCGTCCGGGGCACGGCCACGGAGAAGCGGCGCGCGGCCGGTCCGGTCGCGGGGCCAAGGGTGGTCAGGGCGGCCGGGGTGGCCGCAGCGGGGGAGCGCGCGGCGGGCGCGGCGGGAATGCTGGGCAAGGCGGGCGCAGTGCGAAGCGACGTGGCGGAAGTGGCGAGCAGGGCGCCGGGCAGCCCTCCGGCCGGGGCGGCCTCAGCGGCGGCTCCCGTGGGCGTGGCTCCCGCGGTCGCGGGGCCAAGGGAGGTCAGGGCAGTCCTGCCTGA","LRDLRQDGSLVRAPPGLAGAPAPARVAPQTLRAVEPRTPAPHAPTRTLPATRAGVPAVPNDRILVAAHRTSASHRFASGKTPAAGETTFADLGVDSDLAADLDARGFTAPFPIQAATLPDTLAGRDVLGRGRTGSGKTLAFSLPLVQRLAQQDKARPGHPIGLVLAPTRELALQIAEVIEPLARVVDMDVTTIFGGVSAKPQEKALKAGVDVVVACPGRLLDLMGQGLVSLDEVEITVLDEADHMADLGFLPNVRRILRATPQRGQRLLFSATLDNGVDTLVKEFLHDPLQHSVDPSTSPVDAMTHRVWMVADKTAKDGIVRRLASGEGQRILFTRTKHLARRLARKLVQAGIPAVELQGNMSQNARERAMRAFSTGQVHVMVATDIAARGIDVSGVELVVHVDPPAEHKAYLHRSGRTARAGAAGSVITLVLPEQKHDVQVLLKKARIRADIERIRPDDDAVSALVGQVAEAVALEDMPEGVAIKGGSPSGRASTGRPGHGHGEAARGRSGRGAKGGQGGRGGRSGGARGGRGGNAGQGGRSAKRRGGSGEQGAGQPSGRGGLSGGSRGRGSRGRGAKGGQGSPA$","ATP-dependent RNA helicase","Cytoplasm, Membrane, Extracellular","possible ATP-dependent RNA helicase","ATP-dependent RNA helicase","DEAD/DEAH box helicase domain protein","","Gorbalenya A.E., Koonin E.V., Donchenko A.P., Blinov V.M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989. 17(12):4713-4730. PMID: 2546125","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[347-423]T$	Helicase_C
SM00490	$\"[342-423]T$	HELICc
PS51194	$\"[319-464]T$	HELICASE_CTER

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[111-281]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[106-307]T$	DEXDc

InterPro
IPR014014
Domain

DEAD-box RNA helicase Q motif
PS51195	$\"[87-115]T$	Q_MOTIF

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[118-292]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[74-302]T$	no description
PTHR10967	$\"[82-462]T$ $\"[498-554]T$	DEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF51	$\"[82-462]T$ $\"[498-554]T$	ATP-DEPENDENT RNA HELICASE

InterPro
IPR001441
Family

Di-trans-poly-cis-decaprenylcistransferase
PD003461	$\"[33-269]T$	UPS1_CORGL_P38118;
G3DSA:3.40.1180.10	$\"[8-274]T$	no description
PTHR10291	$\"[6-137]T$ $\"[160-275]T$	DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE
PF01255	$\"[31-275]T$	Prenyltransf
TIGR00055	$\"[165-274]T$	uppS: undecaprenyl diphosphate synthase
PS01066	$\"[220-237]T$	UPP_SYNTHETASE

InterPro
IPR004254
Family

Hly-III related proteins
PTHR20855	$\"[27-236]T$	ADIPOR/PROGESTIN RECEPTOR-RELATED
PF03006	$\"[24-227]T$	HlyIII

InterPro
IPR005744
Family

HylII
PTHR20855:SF3	$\"[27-236]T$	HEMOLYSIN III

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[37-57]?$ $\"[63-81]?$ $\"[102-120]?$ $\"[126-146]?$ $\"[151-169]?$ $\"[179-199]?$ $\"[214-234]?$	transmembrane_regions

","BeTs to 10 clades of COG1272COG name: Predicted membrane proteins, hemolysin III homologsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1272 is ------y--drlb-efg-sn-j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB004254 (Hly-III related proteins) with a combined E-value of 1.4e-10. IPB004254A 183-197 IPB004254B 212-227","","","-38% similar to PDB:1OCC STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE (E_value = );-38% similar to PDB:1OCO BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE (E_value = );-38% similar to PDB:1OCR BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE (E_value = );-38% similar to PDB:1OCZ BOVINE HEART CYTOCHROME C OXIDASE IN AZIDE-BOUND STATE (E_value = );-38% similar to PDB:1V54 Bovine heart cytochrome c oxidase at the fully oxidized state (E_value = );","Residues 24 to 227 (E_value = 4.2e-60) place ANA_1803 in the HlyIII family which is described as Haemolysin-III related.","","membrane proteins, hemolysin III homologs","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1804","1955048","1955533","486","4.77","-11.30","17426","ATGTCCGAGCAGTCACAGGGCACCTGGCTCACCCAGGAGGCCTACGACCGGCTGGCCGCCGAGCTCGAGCACCGCAAGACGACCGAGCGCAAGGAGATCGCCCAGCGCGTGGAGGCGGCCCGCCAGGAGGGTGACCTGCGGGAGAACGCCGGCTACCACGCCGCCCGCGAGGAGGCGGGGCTCAACGAGGCGCGCATCATCCAGCTCGAGGAGACCCTGGAAAACGCCCAGATCGGCGAGGCGGCCGACGACGGCTCGGTCTCGGCCGGCACCATCGTCACCGCGAAGGTGGCCGGCAAGGAGCAGGTCTTCGCCCTGGGTGGCCAGGAGATCACCGAGGACGTGCCCGACGGCGTCAAGGTCTTCTCCCCCGACGCCCCGCTGGGGCAGGCCCTCATGGGGCACCGCGCGGGCGACACCGTCTCCTACGAGGCCCCCAACGGCCGGAAGATCCAGGCCGAGATCGTCAAGGTCGAGCGGGTCTGA","MSEQSQGTWLTQEAYDRLAAELEHRKTTERKEIAQRVEAARQEGDLRENAGYHAAREEAGLNEARIIQLEETLENAQIGEAADDGSVSAGTIVTAKVAGKEQVFALGGQEITEDVPDGVKVFSPDAPLGQALMGHRAGDTVSYEAPNGRKIQAEIVKVERV$","Transcription elongation factor greA","Cytoplasm","Transcription elongation factor greA (Transcriptcleavage factorgreA)","putative transcription elongation factor","transcription elongation factor GreA/GreB domain protein","","Opalka N., Chlenov M., Chacon P., Rice W.J., Wriggers W., Darst S.A. Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase. Cell 2003. 114(3):335-345. PMID: 12914698Von hippel P.H. An integrated model of the transcription complex in elongation, termination, and editing. Science 1998. 281(5377):660-665. PMID: 9685251","","","

InterPro
IPR001437
Domain

Transcription elongation factor, GreA/GreB region, prokaryotic
PD004918	$\"[111-148]T$	Y1I8_MYCTU_P72054;
G3DSA:1.10.287.180	$\"[5-79]T$	no description
PF01272	$\"[81-160]T$	GreA_GreB
PF03449	$\"[4-78]T$	GreA_GreB_N
PS00829	$\"[21-52]T$	GREAB_1

InterPro
IPR012243
Family

Prokaryotic transcription elongation factor GreA, GreB
PIRSF006092	$\"[5-161]T$	Transcription elongation factor GreA/GreB

","BeTs to 16 clades of COG0782COG name: Transcription elongation factorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0782 is --------vdrlb-efghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001437 (Prokaryotic transcription elongation factor GreA/GreB) with a combined E-value of 7.5e-27. IPB001437A 14-66 IPB001437B 102-148","","","-54% similar to PDB:1GRJ GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI (E_value = 1.9E_16);-52% similar to PDB:2EUL Structure of the transcription factor Gfh1. (E_value = 1.1E_11);-51% similar to PDB:2ETN Crystal structure of Thermus aquaticus Gfh1 (E_value = 1.9E_11);-52% similar to PDB:2F23 Crystal structure of GreA factor homolog 1 (Gfh1) protein of Thermus thermophilus (E_value = 2.5E_11);","Residues 4 to 78 (E_value = 8e-27) place ANA_1804 in the GreA_GreB_N family which is described as Prokaryotic transcription elongation factor, GreA/GreB, N-terminal domain.Residues 81 to 160 (E_value = 0.00083) place ANA_1804 in the GreA_GreB family which is described as Prokaryotic transcription elongation factor, GreA/GreB, C-terminal domain.","","elongation factor greA (Transcript cleavage factorgreA) (greA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1805","1955702","1956418","717","5.22","-10.06","25415","ATGTTCAACGCCCTCCGTCACTCGCTCAGCGGATCGGCACCGGCCGGTCGTGAGACACCGGTCCTGCCCGTTCCCGGAGACCACCCGGCACTGGGAACGCCCCTGGACGGGCCGTGGCCCGAGGGCAGCCGGGTCATCTACCTCGCGGCTGGCTGCTTCTGGGGTGTGGAGCGGATCCTGTGGCGCCAGGACGGCGTCGTCTCGACGTCGGTGGGCTACATGGGCGGCCAGACGCCCAACCCCACGTACCAGGAGGTGTGCACCGGGACGACCGGTCACGCCGAGACGGTGCGCGTCGTCTACGACCCGGCCGTCTGCGGCGAGGGCGGGGAGACCCTGCTCAAGACTTTCTGGGAGAACCACGACTCCACTCACCTGAACCGCCATGGCAACGACGTCGGCACCCAGTACCGCTCGGCGGTGTGGACGACGACACCCGCCCAGCGCGAGGCGGCCGCACGGATCCGTGAGGCCTTCCAGGGCGAACTGACCCGCCTGGGCCTGGGAACCTGCGTCACCACCATCGAGGAGGCCGCGGACGCGCCGGCTCAGTTCGGCGGCCCCTACTACCTGGCCGAGGACTACCACCAGGCCTACCTGCACAAGAACCCCGGCGGCTACTGCAACCACGGCCCCAACGGGGTGACCTGCCCGGTCGGCCTCACGGACCTTCCCGCACAGACCGACATCCTGGCCCCCGACGACGCGCCGGCCTGA","MFNALRHSLSGSAPAGRETPVLPVPGDHPALGTPLDGPWPEGSRVIYLAAGCFWGVERILWRQDGVVSTSVGYMGGQTPNPTYQEVCTGTTGHAETVRVVYDPAVCGEGGETLLKTFWENHDSTHLNRHGNDVGTQYRSAVWTTTPAQREAAARIREAFQGELTRLGLGTCVTTIEEAADAPAQFGGPYYLAEDYHQAYLHKNPGGYCNHGPNGVTCPVGLTDLPAQTDILAPDDAPA$","Peptide methionine sulfoxide reductase","Periplasm, Cytoplasm, Extracellular","Peptide methionine sulfoxide reductase msrA 1(Protein-methionine-S-oxide reductase 1) (Peptide Met(O)","peptide methionine sulfoxide reductase ","peptide methionine sulfoxide reductase","","Lowther W.T., Brot N., Weissbach H., Honek J.F., Matthews B.W. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proc. Natl. Acad. Sci. U.S.A. 2000. 97(12):6463-6468. PMID: 10841552Koonin E.V., Mushegian A.R. Complete genome sequences of cellular life forms: glimpses of theoretical evolutionary genomics. Curr. Opin. Genet. Dev. 1996. 6(6):757-762. PMID: 8994848Mushegian A.R., Koonin E.V. A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(19):10268-10273. PMID: 8816789Taylor A.B., Benglis D.M., Dhandayuthapani S., Hart P.J. Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine. J. Bacteriol. 2003. 185(14):4119-4126. PMID: 12837786","","","

InterPro
IPR002569
Domain

Methionine sulfoxide reductase A
PD003489	$\"[10-208]T$	Q6AAA5_PROAC_Q6AAA5;
G3DSA:3.30.1060.10	$\"[1-209]T$	no description
PF01625	$\"[44-213]T$	PMSR
TIGR00401	$\"[44-208]T$	msrA: methionine-S-sulfoxide reductase

noIPR
unintegrated

unintegrated
PTHR10173	$\"[22-208]T$	METHIONINE SULFOXIDE REDUCTASE

","BeTs to 17 clades of COG0225COG name: Peptide methionine sulfoxide reductaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0225 is -om---y--drlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002569 (Peptide methionine sulfoxide reductase) with a combined E-value of 5.6e-48. IPB002569A 48-87 IPB002569B 108-142 IPB002569C 179-204","","","-57% similar to PDB:1FF3 STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI (E_value = 1.6E_46);-57% similar to PDB:1FVA CRYSTAL STRUCTURE OF BOVINE METHIONINE SULFOXIDE REDUCTASE (E_value = 1.6E_46);-57% similar to PDB:2GT3 Solution structure and dynamics of the reduced form of Methionine Sulfoxide Reductase A from Escherichia coli, a 23 kDa protein (E_value = 1.6E_46);-57% similar to PDB:2IEM Solution structure of an oxidized form (Cys51-Cys198) of E. coli Methionine Sulfoxide Reductase A (MsrA) (E_value = 1.3E_45);-56% similar to PDB:1FVG CRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASE (E_value = 3.6E_43);","Residues 44 to 213 (E_value = 7.6e-73) place ANA_1805 in the PMSR family which is described as Peptide methionine sulfoxide reductase.","","methionine sulfoxide reductase msrA 1 (Protein-methionine-S-oxide reductase 1) (Peptide Met(O) reductase 1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1806","1957317","1956562","756","5.78","-6.18","25598","GTGGCGAAGCGGCTCGCGTTAAGCGGCAGAGCCGGCCCGGTACTCGGCGCGGTACTCGCTAGTGCGGGTGTGGATGAGGCGGGGGATGGAGATGGTCTTGTCGAAGCTGCCGTCGCGGTAGCCGGCCTGGAGGTTGAACAGCACCATGAGCCGCAGCGCCATGGGGTTGCTCGTGCGAGCCACGCGCCGCAGCGTCGAGACGGGCATCTTGCGCAGGATGCCCGCGATCTTGCCGGCGTCACGCCAGTTGGCACGCACCGCTGGAACGTTGAGACGGTTGAGGGCCTCGACCTCGCGCAGGAAGAAGTCGGCGCCCTCCCTCTCTGCCGCGCGCCACCAGCCGGCGCGGTAGGTGGCCTCGAGCTGCTTAACGGCGTCACACAGGGCGTCGTAGTCGACGCCGACGACCTCGGTGCGCAGCTCCTCGGCCCGGATCCGCTCCAGGGCGGCGTGGGCCAGCGGCAGGATGGCGCGGGCGACGGCGTCGACGGCGTTGTTGCGGGTGAGGCGGTCCGTTTCCGGCAGGGGCTTGCCGTCGCGGGGCAGGTGCGCGTCGACCTCCTCCAGGTGCGCGATAGAGGTGCGCAGGTCGCCGGTGAGGCGGGCGGTGGAGCGTGGGACCCCCATGGCGATGAGCAGCTCGGTCGCGGCGCGCCACTGGAAGTCTGTGTCCTCAGACCAGTGGGGCTGCGATGCCTCCCCCGCTGGAGACCGGTCCAACGGGGTGCTCGTCTGCTGGCTGCTCATCGGGGTTGA","VAKRLALSGRAGPVLGAVLASAGVDEAGDGDGLVEAAVAVAGLEVEQHHEPQRHGVARASHAPQRRDGHLAQDARDLAGVTPVGTHRWNVETVEGLDLAQEEVGALPLCRAPPAGAVGGLELLNGVTQGVVVDADDLGAQLLGPDPLQGGVGQRQDGAGDGVDGVVAGEAVRFRQGLAVAGQVRVDLLQVRDRGAQVAGEAGGGAWDPHGDEQLGRGAPLEVCVLRPVGLRCLPRWRPVQRGARLLAAHRG$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-54% similar to PDB:1A49 BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE (E_value = );-54% similar to PDB:1A5U PYRUVATE KINASE COMPLEX WITH BIS MG-ATP-NA-OXALATE (E_value = );-54% similar to PDB:1AQF PYRUVATE KINASE FROM RABBIT MUSCLE WITH MG, K, AND L-PHOSPHOLACTATE (E_value = );-54% similar to PDB:1F3W RECOMBINANT RABBIT MUSCLE PYRUVATE KINASE (E_value = );-54% similar to PDB:1F3X S402P MUTANT OF RABBIT MUSCLE PYRUVATE KINASE (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1807","1958176","1957403","774","9.20","5.36","28235","ATGGAGCGCTACGAGCTGCTGCTCGAGGCGGCGCACCTGAAGTACGGCGAGGACCTGGTGCTGGCGGGCGCCTCCGCCGTCGCCGCCTACGGGCTGCCACTGGTGGGGACGGTCCTGCGCCGGGTGGAGGTCGTGGACGGGCGCCCTGGCCGGGTACGGACCTCCTTGCTGAGGCGCCACGTGCGGCGCCGTGGCACTGAGGTCGTCAGAGTGGGCGGGCATCTCGCCGTCGCGCTGCCGGACGCGCTCATTGACCTGGCTCGGTGGAACGGCCTCATGGCGGGAGTCGCCGCCATGGACGCGGCCCTGCACAACGGGTTGTGCTCTGCGGAGGGACTGCAAGAGGCGCTGGAGCGTCTGCCCGAGACGGCAGGTGGCGGCCCTCGTGCGCGGCAGGCTGTGTGCCTGGCCGACGGCCGCTCCGAGTCGCCGGGCGAGTCGATGTCCCGCGTGCGCATGTGGGAGCACCGGCTTCCCAAGCCGGAGCTGCAGGTGAGCGTGCGGGTCGGGTCGGAGCTCTACATCCTGGACTTCTACTGGCCGGATCATGGGGTGGCCGGGGAGTTCGACGGTCGGGTCAAGTACCGGTCGGCCTCCTTCGGGCAGGACCCGGAGGATGTCGTATGGCGTGAGAAGCTCCGAGAGGACGCGCTGCGGGCCTCGGGCCTGACGGTGGCCCGCTGGACATGGGCGCAGGCATGGGGCGACGCCGGGGCGCAGATGCTGCGACGACTGGCCGCTGCCGGGGTCAGGCCCACTGGCCGACGTTGGTAA","MERYELLLEAAHLKYGEDLVLAGASAVAAYGLPLVGTVLRRVEVVDGRPGRVRTSLLRRHVRRRGTEVVRVGGHLAVALPDALIDLARWNGLMAGVAAMDAALHNGLCSAEGLQEALERLPETAGGGPRARQAVCLADGRSESPGESMSRVRMWEHRLPKPELQVSVRVGSELYILDFYWPDHGVAGEFDGRVKYRSASFGQDPEDVVWREKLREDALRASGLTVARWTWAQAWGDAGAQMLRRLAAAGVRPTGRRW$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1808","1960471","1958384","2088","5.99","-13.07","74802","ATGACTGAGCGCAGCGAGCGAGGCGGTTCCCGCCGGGACGACAGGGGCGGACACGGCGACCGCGGTGACCGCGGTTATCGGGGCGGCTCTGGTGGCGGAGGGGGCCGAGGCGGCGACCGCGGCTACCGGGGCGGCTCGGGCTACCGGGGAGGCTCGGGAGGCGGCCGCGGTGGTGACCGTGGCTACCGGGATGGCGAGCGCGGCCGCTCGCGCCGCGTCTATGACGACGAGCCCCGCGACGGCCTCCTGGCAGATCTCGTCGGCCACCTCCACGCCCTCGACGGACGCTCCTACGCCGCCTATAAGGCGATCGTCGGACGCTACCGGGCGCCCGCCGGCTGGTTCCTGCACATTGACCGCGTCCAGTCCGACCCCTACGCCCCGCCCACGCGCATCCACGTGGACGTGCCCACCGACCTGCACGGCCTGGAGCTGCTCGACGAGGCCGACCTGCTGGCCGATGCAGACCGCCGCCTGGCCGTGGGCGACTTCCTCACCCGCGAGCTGCACGCGGGCTTCCGCGGCACGGCGCTGTCCATCGCCTCCCCGGGCCAGGAGATCCTGCAGCGCTCCAGCATCATCCTGCGCCCCGAGGAGAAGAAGGAGGGGACCGGCTGGGTGCTGGAGGTCCGAGCCCGCCTGGCCCTGCCCGCCCAGGGTCGCTCCATCCAGGGCCACGAGGCCTCCCGGATCGTGGGGCGCGACCTCGTGCGTGAGCTGGAGGAGGCCATGGACCTCACCGGCGAGCGGGGCGACCGGCTCGTGCACCACGTCGCCACCCTTGAGGATCACCGGGCCCTGACCGCGACGGTGGCCCGCAATGGCTGGGTGGCCTTCCTCGCCGACGGCTCCGTCCTGCCGCGCCGTTCCGGGGTGAGCGACGATCCCCTGGACGGCGGTGTTCCCCTCCAGGCCCCCGAGTCCATGGCCGCCACGGTAGAGCTCCCGCACGCCGGAATGGTGCGCGGCACCGTCGTCGAGGCGGGCGTCAACGTCATCGTCGGAGGCGGCTACCACGGCAAGTCCACGCTGCTGAGCGCCATCGAGCGCGGCGTCTACCCACACGTGCCCGGGGACGGGCGCGAGCTCGTCGCCACGGTCCCGGACACGGTCAAGGTGCGGGCCGCCGACGGGCGCGCCGTGACCGGCGTCGACCTGACCCCCTTCATCTCCCACCTGCCGGCCGGGCGCGACACCGCCTCCTTCACCACCCGCAACGCCTCGGGATCCACCTCCCAGGCCGCCTCCATCATCGAGGCCGTCGAGGCCGGCGCCACGACGCTGCTGCTGGACGAGGACACCTCCGCCACGAACCTGCTCATCCGCGACTCGCGCATGCGCGAGCTGGTGGCCGCTGAGCGCGAGCCCATCACGCCCCTGGTGGATCGCATCACCGCGCTGTTCCGCCGGAGGGGCGTCTCCACGGTCATGGTCATGGGTGGCTCCGGGGACTACCTGGACGTGGCCGACCGGGTCCTGCTCATGGACGCCTACCACCTGCGCGACGTCACCGAGCAGGCCCGCCGTGTCGTGGCTGACCAGCCCCGGCCCCTGACCGGGCTGGAGGACTTCGCCGAGCCGCGCCAGCGCGTCCCCGAGCCCGCCCCGCCGCGCACCCGCCGGGGGCCGGTGCGCACTCGCACCCACGGTACCTCCACCCTCGTCCTGGACCGGGAGGACATCGACATCTCCGACGTCGGCGGCGTCACCGACCCGGGGCAGGCCGAGGCCATCGCCTACGCGCTGCGCGCCCTGCTGGAGCAGCGCTTCGACGGGGTCTCCCCGCTGCGCGAGTGCCTGGACGACCTCGAAGCCCTGCTCGATGAGGAGGGCCTGGACGCTCTGACCGACGAGCGCGAACGGCCCGCCTTCCTCGTGCGCCCCCGCATGGTCGACGTCGCCGCGGCCGTCAGCCGCTACCGCAAGCTCGAGCTGGTCTCCCTCCCACCACACACTTCGACCAAAACTTCAGAATCGACCCGGAGCCGCGTCGATTCTGAAGATTCGGTCGAAGTGATCGGCGATCCCGGTCTCCACAACGGCGCCGTCGGCCACCTGTTTCCACAGGACGGTGGGCGCGCCGAGTGA","MTERSERGGSRRDDRGGHGDRGDRGYRGGSGGGGGRGGDRGYRGGSGYRGGSGGGRGGDRGYRDGERGRSRRVYDDEPRDGLLADLVGHLHALDGRSYAAYKAIVGRYRAPAGWFLHIDRVQSDPYAPPTRIHVDVPTDLHGLELLDEADLLADADRRLAVGDFLTRELHAGFRGTALSIASPGQEILQRSSIILRPEEKKEGTGWVLEVRARLALPAQGRSIQGHEASRIVGRDLVRELEEAMDLTGERGDRLVHHVATLEDHRALTATVARNGWVAFLADGSVLPRRSGVSDDPLDGGVPLQAPESMAATVELPHAGMVRGTVVEAGVNVIVGGGYHGKSTLLSAIERGVYPHVPGDGRELVATVPDTVKVRAADGRAVTGVDLTPFISHLPAGRDTASFTTRNASGSTSQAASIIEAVEAGATTLLLDEDTSATNLLIRDSRMRELVAAEREPITPLVDRITALFRRRGVSTVMVMGGSGDYLDVADRVLLMDAYHLRDVTEQARRVVADQPRPLTGLEDFAEPRQRVPEPAPPRTRRGPVRTRTHGTSTLVLDREDIDISDVGGVTDPGQAEAIAYALRALLEQRFDGVSPLRECLDDLEALLDEEGLDALTDERERPAFLVRPRMVDVAAAVSRYRKLELVSLPPHTSTKTSESTRSRVDSEDSVEVIGDPGLHNGAVGHLFPQDGGRAE$","ATPase of the ABC class","Cytoplasm","Predicted ATPase of the ABC class","hypothetical protein","ATPase of the ABC class-like","","","","","No hits reported.","BeTs to 3 clades of COG3044COG name: Predicted ATPase of the ABC classFunctional Class: R [General function prediction only]The phylogenetic pattern of COG3044 is --m--z----------g---------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","ATPase of the ABC class","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1809","1961168","1960614","555","4.84","-7.33","19299","ATGACCCGTCTTGCCGTCGTCGTCGGTTCCGTTCGCCCCAACCGCGTGGGTGGCTCCATCGCTCAGTGGGTGGTCGACCAGGCCAACAAGATCGAGGGCGTTGAGGCTGAGATCGTCGACATCGCCTCCTTCAACCTGCCCCTGTTCGCCGAGGAGATCCCCCCGCGCATGGCCGTCCCCAGCGACCCGGCCGGCGCCGCCTTCGATGAGGCCCTGAAGTCCTTCGACTCGCTGATCTTCGTCACCCCCGAGTACAACTTCTCCATCCCCGGCGCGCTGAAGAACGCCATCGACTTCCTCCAGCCCGGCGCAGTGGCCAACAAGGGCGTGGGCGTGGTCGGCTACTCCTACAGCGTCGGCATCCGCGCCGTCAGCCACCTCCAGCAGATCCTCCAGGGCATGGGCGCCACCGTCGTGGCCTCCAACGTGTTCCTGTCGCTCAACACCGACTTCGCCGACGGCGCCTTCTCGCCGGCCGCCTTCCACGACGCCGAGGTGCCGGCCATGGTGCGCGACGTCGTCGCCCACTCCGACGCCCTGGCCTCCCTGCGCTGA","MTRLAVVVGSVRPNRVGGSIAQWVVDQANKIEGVEAEIVDIASFNLPLFAEEIPPRMAVPSDPAGAAFDEALKSFDSLIFVTPEYNFSIPGALKNAIDFLQPGAVANKGVGVVGYSYSVGIRAVSHLQQILQGMGATVVASNVFLSLNTDFADGAFSPAAFHDAEVPAMVRDVVAHSDALASLR$","NADPH-dependent FMN reductase","Cytoplasm","Predicted flavoprotein","putative reductase","NADPH-dependent FMN reductase","","Eichhorn E., Van Der Ploeg J.R., Leisinger T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 1999. 274(38):26639-26646. PMID: 10480865","","","

InterPro
IPR005025
Domain

NADPH-dependent FMN reductase
PF03358	$\"[2-175]T$	FMN_red

InterPro
IPR014479
Family

NAD(P)H-dependent FMN reductase
PIRSF016214	$\"[2-184]T$	NAD(P)H-dependent FMN reductase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[3-154]T$	no description

","BeTs to 10 clades of COG0431COG name: Predicted flavoproteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0431 is -o----y--drlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is 2","***** IPB005025 (NADPH-dependent FMN reductase) with a combined E-value of 9.3e-12. IPB005025A 75-98","","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 175 (E_value = 3e-33) place ANA_1809 in the FMN_red family which is described as NADPH-dependent FMN reductase.","","flavoprotein (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1810","1962946","1961381","1566","5.43","-16.42","56539","GTGAATGAGCTCGACAGCGTCAGCAGCAACGGAACTCCAGCCTGGGACAGCGCCCGCTACCTGCGGGAGATCCTCAAGGCCCCCGTCTACGAGGCGGCCGAGCACACGCCCCTGCAGGAGATGCCTGCCCTGTCGGCCCGCCTGGGCAACACCGTCGAGGTCAAGCGCGAGGACCTCCAGACCGTCCACTCCTTCAAGATCCGCGGCGCCTACAACGCCATGCGCTCCCTGAGCCCGGCCGAGCGCGAGCGCGGCGTCGTCACCGCCTCGGCCGGCAACCACGCCCAGGGCGTGGCCCGCTCCGCCGCCCTGCTGGGGATGAGCGCCATCATCGTCATGCCCACCGTCACCCCCCAGATCAAGGTCGACGCCGTTCGCGCCCTGGGCGGCGAGGTCCGCCTCCACGGGGACAACTTCGACGCGGCCAAGGCTGAGGCCACCCGCCTGGCCGAGGCCGAGGGCCTGTCCTACATCGCCCCCTTCGACGACCCCCGTGTCATTGCCGGTCAGGGCACCATCGGTCTGGAGCTCATCCAGCAGGACGCCCATCTCGACCGCGTCTTCGTGCCCGTGGGCGGCGGCGGGCTGGCGGCCGGTGTCGCCGTCCTCATCAAGCAGCTCATGCCCGGGATCAAGGTCATCGGCGTCGAGCACGAGGAGTCGGCCTGCCTCAAGGCCGCCCTGCTGGGCGGGGAGCCCATCACCCTGCACCACGTGGGCCTGTTCGCTGAAGGGGTGGCCGTGCGCCGCATCGGCGAGGAGACCTTCCGCATGTGCCGGGCCCTGCTTGACGACGTCGTTACCGTCTCCTCCGACGAGACCTCCGCCGCCGTGCGTGACATCTTCGACGACGTGCGCGCCATCTCCGAGCCCTCCGGCGCCCTGGCCCTGGCGGGGCTCAAGCGCTACGTCGCCGAGCACCACCTGTCCGGCGAGCGCCTCGCCTTCATCCTGTCCGGCGCCAACCTCAACTTCCACCAGCTGCGCTACATCTCCGAGCGCAGCGAGATCGGTGAGCAGCGCGAGGCCATCCTCGGGGTCACCATCCCCGAGGAGCAGGGCTCCTTCCTGCGCTTCGCCTCGGTCCTGGGGGCCCGCTCGGTCACCGAGTTCAACTACCGCCTCTCCGCGGCCCGCACCGAGACCGACCCCGCCCGCATCTTCGTGGGCGTGCGTATCGCCCGGCGCCAGGAGCGCGCCGAGATCGTGGCGGACCTGGAGGAGGCCGGCTACGACGTCATCGACCTCACTGACGACGAGCTCGCCAAGGTCCACGTGCGCTCCATGATCGGCGGGCGCGCCACCCCGGGCGTGCCCGAGCGCCTCTTCTCCTTCCTCTTCCCCGAGTCGCCCGGGGCGCTGGCCCACTTCCTTGAGGTCCTGGGGACCCGCTGGAACATCACCCTGTTCCACTACCGCACCGACGGCGCCGACTACGGCCGCATCCTGTGCGCCTTCGCGGCCGGGCCCGACGACGTCGAGCTGACCGAGCACATGGACCGCCTCGGCTACTCCTACAACGAGGAGACCGCCGACCCCGCCTTCCGTTTCTTCTTGGCCCGATAA","VNELDSVSSNGTPAWDSARYLREILKAPVYEAAEHTPLQEMPALSARLGNTVEVKREDLQTVHSFKIRGAYNAMRSLSPAERERGVVTASAGNHAQGVARSAALLGMSAIIVMPTVTPQIKVDAVRALGGEVRLHGDNFDAAKAEATRLAEAEGLSYIAPFDDPRVIAGQGTIGLELIQQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPGIKVIGVEHEESACLKAALLGGEPITLHHVGLFAEGVAVRRIGEETFRMCRALLDDVVTVSSDETSAAVRDIFDDVRAISEPSGALALAGLKRYVAEHHLSGERLAFILSGANLNFHQLRYISERSEIGEQREAILGVTIPEEQGSFLRFASVLGARSVTEFNYRLSAARTETDPARIFVGVRIARRQERAEIVADLEEAGYDVIDLTDDELAKVHVRSMIGGRATPGVPERLFSFLFPESPGALAHFLEVLGTRWNITLFHYRTDGADYGRILCAFAAGPDDVELTEHMDRLGYSYNEETADPAFRFFLAR$","Threonine dehydratase","Cytoplasm","threonine ammonia-lyase, biosynthetic","threonine deaminase ","threonine dehydratase, biosynthetic","","Ogawa H., Gomi T., Konishi K., Date T., Nakashima H., Nose K., Matsuda Y., Peraino C., Pitot H.C., Fujioka M. Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. J. Biol. Chem. 1989. 264(27):15818-15823. PMID: 2674117Datta P., Goss T.J., Omnaas J.R., Patil R.V. Covalent structure of biodegradative threonine dehydratase of Escherichia coli: homology with other dehydratases. Proc. Natl. Acad. Sci. U.S.A. 1987. 84(2):393-397. PMID: 3540965Parsot C. Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase. EMBO J. 1986. 5(11):3013-3019. PMID: 3098560","","","

InterPro
IPR000634
Binding_site

Serine/threonine dehydratase, pyridoxal-phosphate-binding site
PS00165	$\"[57-70]T$	DEHYDRATASE_SER_THR

InterPro
IPR001721
Domain

Threonine dehydratase, C-terminal
PF00585	$\"[333-426]T$ $\"[432-519]T$	Thr_dehydrat_C

InterPro
IPR001926
Domain

Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291	$\"[29-321]T$	PALP

InterPro
IPR005787
Family

Threonine dehydratase I
TIGR01124	$\"[19-519]T$	ilvA_2Cterm: threonine ammonia-lyase, biosy

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1100	$\"[125-351]T$	no description
PTHR10314	$\"[44-388]T$	SER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF17	$\"[44-388]T$	THREONINE DEHYDRATASE-RELATED

","BeTs to 17 clades of COG1171COG name: Threonine dehydrataseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1171 is -o-p-zy-vdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 2","***** IPB001721 (Threonine dehydratase, C-terminal) with a combined E-value of 2.9e-117. IPB001721A 56-99 IPB001721B 187-224 IPB001721C 227-280 IPB001721D 311-359***** IPB000634 (Serine/threonine dehydratase, pyridoxal-phosphate attachment site) with a combined E-value of 1.8e-14. IPB000634A 57-80 IPB000634B 164-176***** IPB001926 (Pyridoxal-5'-phosphate-dependent enzyme, beta family) with a combined E-value of 8.5e-14. IPB001926A 64-73 IPB001926B 88-113","","","-74% similar to PDB:1TDJ THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI (E_value = 4.2E_174);-55% similar to PDB:2GN0 Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 1.7 A resolution (Triclinic form with one complete subunit built in alternate conformation) (E_value = 6.5E_50);-55% similar to PDB:2GN1 Crystal structure of dimeric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium at 2.2A resolution (Triclinic form with one dimer of TdcB in the asymmetric unit) (E_value = 6.5E_50);-55% similar to PDB:2GN2 Crystal structure of tetrameric biodegradative threonine deaminase (TdcB) from Salmonella typhimurium in complex with CMP at 2.5A resolution (Hexagonal form) (E_value = 6.5E_50);-49% similar to PDB:1V71 Crystal Structure of S.pombe Serine Racemase (E_value = 1.1E_36);","Residues 29 to 321 (E_value = 1.2e-93) place ANA_1810 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme.Residues 333 to 426 (E_value = 2.8e-33) place ANA_1810 in the Thr_dehydrat_C family which is described as C-terminal regulatory domain of Threonine dehydratase.Residues 432 to 519 (E_value = 4.1e-29) place ANA_1810 in the Thr_dehydrat_C family which is described as C-terminal regulatory domain of Threonine dehydratase.","","ammonia-lyase, biosynthetic (ilvA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1811","1963451","1963774","324","6.53","-0.59","11163","ATGAGCACCGCCGCGAACAGCTCCACCGTCACCACCTCGTGGGAGCAGCTCAGGCAGGAGTCGCTGGCCGCCATGACCGAGGCCGAGCGAGCCGAGTACAACCGGGCTGCCATCGAGACCGAGGCCCGCCTCCAACTTGCCGAGCTGGTTTACAACGCGCGTGCGGCCGCAGGAATCTCCCAGACAGAACTGGCCCGACGCGCAGGAACACGTCAGTCCGTCATCTCAGCGATTGAAAACGGCGCTCAAGCACCCGGTGGCGTCATGCTCGCACGTATCGCTCACGCCCTCGGCGGAACTCTCGGGATTCACGTCGCCGCCTAA","MSTAANSSTVTTSWEQLRQESLAAMTEAERAEYNRAAIETEARLQLAELVYNARAAAGISQTELARRAGTRQSVISAIENGAQAPGGVMLARIAHALGGTLGIHVAA$","Transcriptional regulator","Cytoplasm, Extracellular","Helix-turn-helix domain protein","hypothetical protein predicted by Glimmer/Critica","helix-turn-helix domain protein","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[50-104]T$	HTH_3
SM00530	$\"[49-104]T$	HTH_XRE
PS50943	$\"[50-104]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[46-98]T$	no description

","BeTs to 8 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 50 to 104 (E_value = 4.8e-12) place ANA_1811 in the HTH_3 family which is described as Helix-turn-helix.","","domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1812","1963929","1964462","534","4.50","-16.60","19367","ATGTCGCTCCAGCTCTTCGAGCTCGTCCCCACCACCCCGTCACGCGAGGCCGCCGAGGCCCTCATCGCGCAGGTCTCCCAGGCCGTTGAGGCCGCCGGCGCCTCCGTCCTGGAGTCGCAGGTCACCGCCAGTCACGAACGCATCTTCACCATCGTCGAGCTCGACTCCGACGACGTCACCGGCCTGACCGAGGCCGTCCGGTCCGCTGCGGCCGACGCCGAGGTCACCGGCCCCGACGAGGTCCGCCTCGTGGGCGCCGAGCTGGAGGACGTGCGAGCCCTGGCCCGCAAGGCCGACTACCTCGTGGAGTGGGACATCCCCGAGGAGATCTCCATGGAGACCTACCTGGCGCGCAAGAAGGCCAACTCCCCCAAGTACGCCCAGGTGCCGGAGGTGAGCTTCCTGCGCACCTACGTGCGTGAGGACACGGTCAAGTGCCTGTGCTTCTACGACGCCCCCGATGAGGAGGCCGTGGTGCGCGCCCGCGAGGCCGTCTCCACCCCGATCGACCGCCTCCACGCCCTGGAGGGCTGA","MSLQLFELVPTTPSREAAEALIAQVSQAVEAAGASVLESQVTASHERIFTIVELDSDDVTGLTEAVRSAAADAEVTGPDEVRLVGAELEDVRALARKADYLVEWDIPEEISMETYLARKKANSPKYAQVPEVSFLRTYVREDTVKCLCFYDAPDEEAVVRAREAVSTPIDRLHALEG$","Hypothetical protein","Cytoplasm","SrpF","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1813","1966370","1964625","1746","11.02","18.36","58364","GTGAGCGGCGTGCTCTCCCGGCTCGCCGGGCGCTTGCGCACGGGTGACATTGTCACCGGCATCTCGCGCCTGCTCGCCCTGGCCTGTCTCGTGGGCCTGGTGGGCATGCTGCCGTGGCTCTCGGGCAAGGACCCGGCCCTGACGATCCTGCGCGCCACCTCCTCCGACCGGGAGCCCACACCGGAGGTCCTGGCATCCATCCGCAAGAGCATCGGGATCGACGGCGGCCCCCTCCACGTCATCGGGCACTGGCTGGCCGGAGTGGCCCGCGGCGACCTGGGCCGCTCCTGGGTCTCGGGAGCTGACGTCGGCCCGGACGCCGTGGACGCCTTCGGAGTCTCCCTGAGCCTCATGGCTGCCGCGCTCGGCGTCGGGGTCGTCGTGGCCGCCGCCCTGGTCCTGCCCGCCCTGCGCGACGGGCTGCGAGGGCGCCCCCGGCCTCGCGGCGGCGCCGCCTCCGCGGTCCTCATCTCCCTGCCCGAGTACCTCCTGGCCCCGATCCTCATGCTCGTCCTGGCCGTCTACCTCAGGATCCTGCCGCCCTTCGGGTGGGGCAGCCCCGAGAAGGTCATCATGCCGGCCCTCAGCCTGGGCCTGCCCACCGGCGGCTACCTCGGTGGACTCGTCTCCGACGCCGTCACCGCCACCTTCTCCGAACGCTGGGTGGCCACCTGGTCCACCGCCGGCATCCGCGGCCGGACCCTGGCCGGAGCCGTCCTGCGGCGGGCCCTGGCGCCACTGACCGGGCAGGTGGCGCTCGTCGTCGTCGCCCTGACCGGCGGCGCGGTCGCCGTGGAGAAGATCTTCGCCATCCCCGGGCTGGGGCGCGAGCTCCTGGACGCCGCCTCCGCCCAGGACGTGCCGGCCCTCCAGGCCCAGATCCTGCTGCTGCTCGCCCTGGCGCTGACCACCGGCGTCATCGCCGGAGCGGTCCGGCGCCTCCTCATGGGGCGGGCCGCCGGGGCGGGAGGACTGACAGCCCCGCCCCCGGTGGAGCACCCGGGGCGGGCCGCCCGCGTCATCGCCGTCAGTGGCGCCGCCCTGCTGGCCCTCATGGTGGCCGTCGGGATTCGGCGCGACCCCTACGCCGTCGTCGCGGACAAGCTCGCGCAGCCCAGCGCCGCCCTCCCGCTGGGTGCCGACTCGCTCGGGCGCGACGTCCTAGCGCGGGTGGCCCACGGGGCCGTGTCCACCGTGAGCGGCGCCGTCATCGTCACCGTGGTGTGCTTCGTCATCGCCATGCTGGTGGGGCTGGCGCCGCGGGCGGCCACGGGCTTCATCGAGGTCGCCAACGCCGCCCCGCCGATCCTGGCCGGGCTCATCGTCGCCGGCGTCTCCGGGCCCAGCGCCACGGGCGCCGCCATCGCCGTGGCCGGCGTCGGGTGGGCACCCCTGGCCTCCCACGCCGCCGGGCTCGTCGCCGAGAACCGGCAGCGCCCCGACGTCCTCCTCGCCCCGGTCCTGGGGGAGGGGCGGTTGCGGATCACCCTGACCCGGGTCCTGCCCGCCGTCGTCGGCCCCCTGGCGCGCCACGCGGCCCTGAGGCTGCCCGGCAAGGCCCTGGCCCTGGCCGCCCTGGGATTCCTCGGCCTGGGCGCCCAGAGCCCCGCACCGGAGTGGGGGCTGGTCCTGTCCGACGCGCTGCCCTACATCGAACGGGCCCCCTGGGCCGTGGCCACGCCCGCCGCCGCCCTCGTGGTCCTGTCGATCACATCGGTCGCCGCCTCCCGTAGCATGCGGCGCTGA","VSGVLSRLAGRLRTGDIVTGISRLLALACLVGLVGMLPWLSGKDPALTILRATSSDREPTPEVLASIRKSIGIDGGPLHVIGHWLAGVARGDLGRSWVSGADVGPDAVDAFGVSLSLMAAALGVGVVVAAALVLPALRDGLRGRPRPRGGAASAVLISLPEYLLAPILMLVLAVYLRILPPFGWGSPEKVIMPALSLGLPTGGYLGGLVSDAVTATFSERWVATWSTAGIRGRTLAGAVLRRALAPLTGQVALVVVALTGGAVAVEKIFAIPGLGRELLDAASAQDVPALQAQILLLLALALTTGVIAGAVRRLLMGRAAGAGGLTAPPPVEHPGRAARVIAVSGAALLALMVAVGIRRDPYAVVADKLAQPSAALPLGADSLGRDVLARVAHGAVSTVSGAVIVTVVCFVIAMLVGLAPRAATGFIEVANAAPPILAGLIVAGVSGPSATGAAIAVAGVGWAPLASHAAGLVAENRQRPDVLLAPVLGEGRLRITLTRVLPAVVGPLARHAALRLPGKALALAALGFLGLGAQSPAPEWGLVLSDALPYIERAPWAVATPAAALVVLSITSVAASRSMRR$","Peptide/nickel transport system permease protein","Membrane, Cytoplasm","probable transport system permease protein","K02033 peptide/nickel transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[107-321]T$ $\"[391-581]T$	BPD_transp_1

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[113-133]?$ $\"[154-176]?$ $\"[190-210]?$ $\"[251-271]?$ $\"[290-310]?$ $\"[399-419]?$ $\"[438-458]?$ $\"[520-538]?$ $\"[557-575]?$	transmembrane_regions

","BeTs to 16 clades of COG1173COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1173 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 107 to 321 (E_value = 8.1e-08) place ANA_1813 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.Residues 391 to 581 (E_value = 4.1e-10) place ANA_1813 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transport system permease protein (AE005264)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1814","1967920","1966367","1554","6.32","-3.89","53233","ATGTCCCTGCCCGCCCCCGCCGTCACCCGCCGCCAGGTCCTCGCCGCCCTCGGCGTCGGAGCAGGCGCCGCCGCCATCGCCTCCTGCTCGCGCAGCTCCTCGGGCGACGGTCGCATCCGCCTGGCCATGTTCCACGCCCCCGAGGGCAAGCTCAACCCACTCACCGACGGCCTCAAGCTCACCCGGTGGTCCTGCGCCGAGAGCCTCACCACGCTCAACGCCGACGGCGATGCCCAGGAGCTGCTCGCCACCGCCTGGAAGCGCGAGAGCGAGACCACTTGGCGACTCACCCTGCGCGAGGGCGTCACCTTCCACGACGGCACCGCCCTGAGCGCCGAGAACGTGGCCGCCGCCCTCACCTTCGCCGCCACCGCGGCCAAGCCGCCGCGCGTCCTGGACGGAGTCAAGCTCACCGCGAAGGCCGACGGCAAGGACCTCCTCCTGACGACCGCGGCCCCCGACCCCCTCATACCGCAGCGCCTCTCCAGTCCCCAGCTCGTCATCCTGTCCCCGGCCGCCTACCCCAGTTCCGCCGACGGCGCCATCGACCCCGTCGGCCACGGCACCGGCGCCTTCATCCTCAAGCAGGCCAACGGCTCCTCCGGTGCCACCCTGGAACGCAACGACAAGTACTGGGGCACGAAGGCCACCGCCCCCGGCATCGACGTCACCTACGTTCCCGACGGCGCCGCCCGCGCCAACGCCCTGCGCACCGACACCGCTGACATCGTCGAGGCCGTCCCCGTCGCCCAGGTCGGCAATATCGACAAGAACCTTCTCCACGAGGTGGCCACCCCGCGCACCTCCACCCTCTACCTCAACACCCGCTCCGGCCCCTTCGCCGACCCCGCCCTGCGCGCCGCCGCCCGCAATGCCGTCGACCCCGCCGCCCTCATCAAGACCGTCTTCGAGGGCCACGCCGACTCCCCCGTCGGGCTCCTGGGGCCAGCCGTGCCGTGGGCCGCCGAGCTGCGCGCCTGGAAGAAGGAGACCTACCCCGGAGCCTCGGGTGCGGCCGCCACCGGCAAGGTCCCCGGCGCCACCGCCGCCGGGACCGTCCCCGCCGGCACCGCCATCACCCTGGCCTCCTACACCGACCGCCCCGAGCTCGGAGAGATGGTCCCCCTCCTGGCCCAGCAGCTCGAGGCTGCCGGCTTCAAGGTCACCCAGGACGTGCGCGAGTACAACCAGATCGAGTCCGAGGCCCTGGCCGGCAAGTTCCACGCCGTCCTCGTGTCGCGCTCCACCGTCCTGGACTCCGGCGACGCCGTCGCCTACATGACCGCCGACTTCTCCTCCTCCGGCTCCTACTCCATGAGCGGCCTGCACGACGAGAAGGTCGACGCCGCCATCTCCAAGGCCGCCGCCACGCAGCCCGGCGACGAGCGCCACAAGGCCATCATGGCCGCCGAGCAGGCCATCCTCGCCTCCGGCGCCGCCATCCCGCTGGCCCACGAGCGCGTCATCCAGGGCGAGGCCGCCGGAGTCACCGGCGCCCAGCGCGACCCGGGCGAGCGCGCCCTCATCACCTCGGCCACGACCGTGAAGAAGTGA","MSLPAPAVTRRQVLAALGVGAGAAAIASCSRSSSGDGRIRLAMFHAPEGKLNPLTDGLKLTRWSCAESLTTLNADGDAQELLATAWKRESETTWRLTLREGVTFHDGTALSAENVAAALTFAATAAKPPRVLDGVKLTAKADGKDLLLTTAAPDPLIPQRLSSPQLVILSPAAYPSSADGAIDPVGHGTGAFILKQANGSSGATLERNDKYWGTKATAPGIDVTYVPDGAARANALRTDTADIVEAVPVAQVGNIDKNLLHEVATPRTSTLYLNTRSGPFADPALRAAARNAVDPAALIKTVFEGHADSPVGLLGPAVPWAAELRAWKKETYPGASGAAATGKVPGATAAGTVPAGTAITLASYTDRPELGEMVPLLAQQLEAAGFKVTQDVREYNQIESEALAGKFHAVLVSRSTVLDSGDAVAYMTADFSSSGSYSMSGLHDEKVDAAISKAAATQPGDERHKAIMAAEQAILASGAAIPLAHERVIQGEAAGVTGAQRDPGERALITSATTVKK$","Peptide/nickel transport system substrate-binding protein","Periplasm, Membrane, Cytoplasm, Extracellular","probable solute-binding lipoprotein","K02035 peptide/nickel transport system substrate-binding protein","extracellular solute-binding protein, family 5","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670","","","

InterPro
IPR000914
Family

Bacterial extracellular solute-binding protein, family 5
PF00496	$\"[77-438]T$	SBP_bac_5

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[8-35]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.10.105.10	$\"[264-486]T$	no description
G3DSA:3.90.76.10	$\"[67-170]T$	no description
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 11 clades of COG0747COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic componentsFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0747 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-35% similar to PDB:1UQW CRYSTAL STRUCTURE OF YLIB PROTEIN FROM ESCHERICHIA COI (E_value = 5.0E_10);","Residues 77 to 438 (E_value = 1.1e-45) place ANA_1814 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 Middle.","","solute-binding lipoprotein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1815","1968936","1967968","969","7.52","1.14","33590","ATGAGCGGACTTGAGACCCGTGGCCTCAGGCGCTCCCACCCGGGGGCGGGCGGCGAGCGGCGAGAGGTGCTGCGCGGCGTGGACCTGCGCCTGGAGCCGGGGGAGAACGTGGCCCTCATCGGACGCTCAGGATGCGGCAAGACGACGCTGCTGCGCGCCCTGCTGCTGCTCGACTCCCCGGGGTCGGAAGACGCCGGCGAGATCCTGCTCGACGGCGAACCCGTGCGCCGAGGCGGAGCCCGAGCGCTGCGGGCCTTCCGGCGGGCGGTGCAGTACGTGCCCCAGGACGCCGCCGCCACCCTCCACCCGCGCCGCTCAGTGCTGGCGCAGGTGGCCACCCCGCTGCGCACCCTGGGGGTGGTGCGCGACCGTGAGGAGGCCACCAGTCGGGCCCGGCGGGTGCTGGAGAGCCTCGAGATTCGCCGCGAGATATGGGAGAGCCGGCCCCACGAGATCTCCGGCGGCCAGGCGCAACGGGTCTCCATCGCCCGGGCCCTGGCCCTGTCCCCGCGCTACCTCCTGCTCGACGAACCGGTCTCCGGGCTCGACCCCGCCCTGCGCCGCCAGACCCTCGACCTGCTTGCGGCCATCGAGGCCGACCCCGACGCCGCCACCAGCGATGAGCAGGAGCCCCCCGCCAAGTCCGGCGTGAGTGGCGAGCCGGAGCCTGCCCCGGCTGGTTCCGGCGCCGTGCCCGCCCCGGCTGGTTCCGGCGCCGTGCCCGCCCCGGCTGGTTCCGGCGCCGTGCCCGCCCCAGCTGGTTCCGGCGCCGTGCCCGCCCCAGCCCTGCTGGTGGTGTCGCACGACCTGGCCGCCGTCGCCCGCGTCTGCCAGCGGGCCCTGGTCATGGACGAGGGCTCCATCGTCGAGGACGCCCCCATGCGCCGCCTCCTCACTAAGCCCACGCACACGGCCACCCGCGCCCTGCGCGACGCCGTCCCCACCCTGCCGACCGCCGCCACCGACTGA","MSGLETRGLRRSHPGAGGERREVLRGVDLRLEPGENVALIGRSGCGKTTLLRALLLLDSPGSEDAGEILLDGEPVRRGGARALRAFRRAVQYVPQDAAATLHPRRSVLAQVATPLRTLGVVRDREEATSRARRVLESLEIRREIWESRPHEISGGQAQRVSIARALALSPRYLLLDEPVSGLDPALRRQTLDLLAAIEADPDAATSDEQEPPAKSGVSGEPEPAPAGSGAVPAPAGSGAVPAPAGSGAVPAPAGSGAVPAPALLVVSHDLAAVARVCQRALVMDEGSIVEDAPMRRLLTKPTHTATRALRDAVPTLPTAATD$","Peptide/nickel transport system ATP-binding protein","Cytoplasm, Membrane","ABC transporter, ATP-binding protein","K02031 peptide/nickel transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[151-194]T$	Q9FCU6_LACRE_Q9FCU6;
PF00005	$\"[34-197]T$	ABC_tran
PS50893	$\"[4-310]T$	ABC_TRANSPORTER_2
PS00211	$\"[152-166]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[33-287]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-197]T$ $\"[262-319]T$	no description
PTHR19222	$\"[4-197]T$ $\"[253-317]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 3 clades of COG1123COG name: ATPase components of various ABC-type transport systems, contain duplicated ATPaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1123 is -omp------r--cefg---uj----Number of proteins in this genome belonging to this COG is 3","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.6e-53. IPB013563A 23-57 IPB013563B 90-103 IPB013563C 149-176 IPB013563D 262-314***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 8.2e-25. IPB005074C 23-70 IPB005074D 140-183***** IPB005116 (TOBE domain) with a combined E-value of 1.7e-20. IPB005116A 41-57 IPB005116C 152-165 IPB005116D 172-191***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.4e-16. IPB010509B 34-59 IPB010509D 147-191***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.7e-10. IPB010929K 21-65 IPB010929M 149-195 IPB010929A 33-52","","","-47% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 9.9E_16);-47% similar to PDB:1OXT Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 9.9E_16);-47% similar to PDB:1OXU Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 9.9E_16);-47% similar to PDB:1OXV Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 9.9E_16);-48% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 1.7E_15);","Residues 34 to 209 (E_value = 6.5e-38) place ANA_1815 in the ABC_tran family which is described as ABC transporter.","","transporter, ATP-binding protein (AP001519)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1816","1969736","1968933","804","5.08","-8.91","26864","TTGGTCAACGGCGTCGCCCTCCGCCTGGCCCCCGCAAGCCGGACTGCCCTGGTCGGCGCCTCTGGGGCGGGCAAGTCCCTCACCTGCGCCGCGCTCGCGGGTACCCTCCCGGCCTCCCTGGAGGTCGCCGGCTCCCTGACCGTTGAGCCCGACGCCGCCGACGCAGGCAGCGACCCGCGCGCGAGCTCCGACCAGGCGGACAGGGCAAGTGGCGTCAACCTCCTGGGTCTGCCCGCCGCCCGGCGCCCCCGGGGCAGCCGCATCGCGCTGGTCCCGCAGGACCACTCCACCGCCCTGCACCCGCTCATCGCGGTCGGCCGCCAGATCGCCCTGGCCTCCCAGGCCGCCGGACGCACCCGGGACGAGGCAGATGAGCGAGCCATCGACTACCTCTACGCCGTCGGGCTCGACGAGTCCTTCGCCGACCGCGTCCCCGGGCGCCTCTCCGGAGGCCAGCGCCAACGCGTCAGCCTGGCCCTTGCCCTGGCCGCCGAACCCGCCCTCATCATCGCCGACGAGCCCACCACCGCCCTCGACGTCGTCGCCCGCGCCGAGATCCTCGGGCTCCTGAGCTCCCTGACCAGCCTGCCCCAGGCCCCCGCCCTGCTCCTCATCACCCACGACCTGCCCGCCGCCGCCATCTGCGAGAACATCGCCGTCCTCCACGACGGCGCCATCATCGAGTCGGGGCAGACCCGCTCCGTCCTGACCCGCCCCGAGCACCCGGTCACGGCCGCCATGTGCGAGGCCGGCGCCGAGGAAACCATCGACGGGGCCCTGGCCGCAGCGGGAGCCGCCGCATGA","LVNGVALRLAPASRTALVGASGAGKSLTCAALAGTLPASLEVAGSLTVEPDAADAGSDPRASSDQADRASGVNLLGLPAARRPRGSRIALVPQDHSTALHPLIAVGRQIALASQAAGRTRDEADERAIDYLYAVGLDESFADRVPGRLSGGQRQRVSLALALAAEPALIIADEPTTALDVVARAEILGLLSSLTSLPQAPALLLITHDLPAAAICENIAVLHDGAIIESGQTRSVLTRPEHPVTAAMCEAGAEETIDGALAAAGAAA$","Peptide/nickel transport system ATP-binding protein","Membrane, Cytoplasm","ATP-binding protein","K02031 peptide/nickel transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[12-224]T$	ABC_tran
PS50893	$\"[7-248]T$	ABC_TRANSPORTER_2
PS00211	$\"[148-162]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[11-240]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-257]T$	no description
PTHR19222	$\"[2-54]T$ $\"[76-250]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28	$\"[2-54]T$ $\"[76-250]T$	OLIGOPEPTIDE ABC TRANSPORTER

","BeTs to 14 clades of COG0444COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0444 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is 2","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 9e-35. IPB013563A 1-35 IPB013563B 88-101 IPB013563C 145-172 IPB013563D 200-252***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 3.4e-19. IPB005074C 1-48 IPB005074D 136-179 IPB005074E 201-221***** IPB005116 (TOBE domain) with a combined E-value of 6.3e-15. IPB005116A 19-35 IPB005116C 148-161 IPB005116D 168-187***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.8e-11. IPB010509B 12-37 IPB010509D 143-187***** IPB010929 (CDR ABC transporter) with a combined E-value of 3.1e-09. IPB010929M 145-191 IPB010929C 130-163","","","-44% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 2.1E_13);-45% similar to PDB:2ONK ABC transporter ModBC in complex with its binding protein ModA (E_value = 1.4E_12);","Residues 12 to 224 (E_value = 3e-40) place ANA_1816 in the ABC_tran family which is described as ABC transporter.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1817","1971751","1969865","1887","5.26","-21.38","66250","ATGCCGCAGTACCGCAGCGCCACCTCCACCCACGGCCGCAACATGGCGGGCGCCCGTGCACTGTGGCGTGCCACCGGCGTCAAGGACTCCGACTTCGGCAAACCGATCATCGCCATCGCGAACTCCTTCACCCAGTTCGTCCCCGGGCACGTGGGCCTGCGCGACGTCGGACGCCTCGTGGCCACCGAGATCGAGGCCGCCGGGGGCCTGGCCAAGGAGTTCAACACCATCGCCGTCGACGACGGCATCGCCATGGGCCACGACGGCATGCTCTACTCCCTGCCCAGTCGCGATCTCATCGCGGACTCCGTGGAGTACATGGTCAGCGCCCACTGCGCCGACGCCCTCGTGTGCATCTCCAACTGCGACAAGATCACCCCGGGCATGCTCATGGCCGCCATGCGCCTCAACATCCCGGCCATCTTCATCTCCGGCGGCCCCATGGAGTCGGGCAAGATGACCGCCGCCGACGGCACCACCCGCAAGCTCGACCTCATCGACGCCATGATGGACGCCGCCGACCCCACCGTGGCCGACGAGACCATCAGCGCCATCGAGCGCCTGGCCTGCCCCACCTGCGGCTCCTGCTCGGGCATGTTCACCGCCAACTCCATGAACTGCCTCACCGAGGCCCTCGGCCTGGCCCTGCCCATGAACGGCACCCTGCTGGCCACCCACGCCGACCGCGGCGAGCTCTTCAAGCGCGTCGGCCACCAGATCGTCGAGATCACCCGGGCCTACTACGAGCACGACGACGCCTCCGTCCTGCCGCGCTCCATCGCCACCAAGGCGGCCTTCGAGAACGCCATGAGCCTGGACATCGCTATGGGCGGCTCCACCAACACCGTCCTGCACCTGCTGGCCGCCGCCCAGGAGGCCGAGGTCGACTTCACCATGGCCGACATCGACCGCCTCTCGCGCAAGGTCCCCCACCTGGCCAAGGTCGCGCCCTCGACGAACCTTTACCACATCGAGGACGTCCACCGCGCCGGCGGCATCATCGGCATCCTCGGCGAGCTCGACCGCGGCGGCCTGCTGGAGACCACCACCTCCAACGTCCTGGGCACCACCCTGGGTGAGGAGCTCGCCGCCTACGACATCGCCCGCCCCGGCCCCGACGGCGTTCCCGGCTCCCAGGTCAGCGAGGAGATCCGCACCGGCTACCTCGCCGCCCCCGCCGGCGTGCGCACCACCGAGATGTTCTCCCAGGCCTCCCGCTGGGAGTCCCTCGACACCGACCGCGCCGCCGGCTGCATCCGCGACATCGAGCACGCCTACTCCGCCGACGGCGGCCTGGCCGTCCTCTTCGGCAACATTGCCGAGAAGGGCTGCATCGTCAAGACCGCCGGCGTGGACGAGTCGATCCTGACCTTCTCCGGGCCCGCCGTCGTCTTCGAGTCCCAGGAGGATGCCGTCGCCGGGATCCTCGGCAAGCAGGTGAAGTCCGGCGACGTCGTCATCATCAGCCACGAGGGACCGCGCGGCGGCCCCGGCATGCAGGAGATGCTCTACCCGACCACCTACATCAAGTCCATGCACCTGGGCAAGGAGTGCGCCCTGCTCACCGACGGGCGCTTCTCCGGGGGCACCTCCGGGCTCAGCATCGGCCACGTCTCCCCGGAGGCCGCGGCCGGGGGGCTCATCGGCCTGGTGCGCAGCGGCGACGTCATCGACATCGACATCCCGGGCCGCTCCATCTCCGTGCGCCTGAGCGATGAGGAGATCGAGCGCCGCCGCGCCGAGGAGGAGGCCCGCGGCGAGGACGCCTGGACCCCGCACGTGGACCGCCCCCGCAAGGTCTCCGCAGCGCTGCGCGCCTACGCCATGCTCGCCACCAGCGCCGACCTGGGCGCCGTGCGCGACCTCAAGCGCCTCGGGATCAAGTAG","MPQYRSATSTHGRNMAGARALWRATGVKDSDFGKPIIAIANSFTQFVPGHVGLRDVGRLVATEIEAAGGLAKEFNTIAVDDGIAMGHDGMLYSLPSRDLIADSVEYMVSAHCADALVCISNCDKITPGMLMAAMRLNIPAIFISGGPMESGKMTAADGTTRKLDLIDAMMDAADPTVADETISAIERLACPTCGSCSGMFTANSMNCLTEALGLALPMNGTLLATHADRGELFKRVGHQIVEITRAYYEHDDASVLPRSIATKAAFENAMSLDIAMGGSTNTVLHLLAAAQEAEVDFTMADIDRLSRKVPHLAKVAPSTNLYHIEDVHRAGGIIGILGELDRGGLLETTTSNVLGTTLGEELAAYDIARPGPDGVPGSQVSEEIRTGYLAAPAGVRTTEMFSQASRWESLDTDRAAGCIRDIEHAYSADGGLAVLFGNIAEKGCIVKTAGVDESILTFSGPAVVFESQEDAVAGILGKQVKSGDVVIISHEGPRGGPGMQEMLYPTTYIKSMHLGKECALLTDGRFSGGTSGLSIGHVSPEAAAGGLIGLVRSGDVIDIDIPGRSISVRLSDEEIERRRAEEEARGEDAWTPHVDRPRKVSAALRAYAMLATSADLGAVRDLKRLGIK$","Dihydroxy-acid dehydratase","Cytoplasm","dihydroxy-acid dehydratase","dihydroxy-acid dehydratase ","dihydroxy-acid dehydratase","","Egan S.E., Fliege R., Tong S., Shibata A., Wolf Jr R.E., Conway T. Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon. J. Bacteriol. 1992. 174(14):4638-4646. PMID: 1624451Velasco J.A., Cansado J., Pena M.C., Kawakami T., Laborda J., Notario V. Cloning of the dihydroxyacid dehydratase-encoding gene (ILV3) from Saccharomyces cerevisiae. Gene 1993. 137(2):179-185. PMID: 8299945","","","

InterPro
IPR000581
Family

Dihydroxy-acid and 6-phosphogluconate dehydratase
PD002691	$\"[443-620]T$	Q6LLH7_PHOPR_Q6LLH7;
PTHR21000	$\"[1-366]T$ $\"[411-626]T$	DIHYDROXY-ACID DEHYDRATASE (DAD)
PF00920	$\"[34-621]T$	ILVD_EDD
PS00886	$\"[122-132]T$	ILVD_EDD_1
PS00887	$\"[519-530]T$	ILVD_EDD_2

InterPro
IPR004404
Family

Dihydroxy-acid dehydratase
TIGR00110	$\"[17-622]T$	ilvD: dihydroxy-acid dehydratase

","BeTs to 20 clades of COG0129COG name: Dihydroxyacid dehydratase/phosphogluconate dehydrataseFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0129 is a-m-kzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000581 (Dihydroxy-acid and 6-phosphogluconate dehydratase) with a combined E-value of 4.2e-160. IPB000581A 31-53 IPB000581B 100-151 IPB000581C 186-220 IPB000581D 257-295 IPB000581E 430-452 IPB000581F 519-560 IPB000581G 604-619","","","-43% similar to PDB:2GP4 Structure of [FeS]cluster-free Apo Form of 6-Phosphogluconate Dehydratase from Shewanella oneidensis (E_value = 2.6E_40);","Residues 34 to 621 (E_value = 0) place ANA_1817 in the ILVD_EDD family which is described as Dehydratase family.","","dehydratase (ilvD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1819","1972512","1972120","393","4.41","-8.06","13574","ATGCCCTCCGTCGAGGGCGCCAAGGGCACGAAGCCCACGCTCACCTTCCCCGGGACCGAGGCCCCCGAGGGGCTCCAGGTCCAGGTGCTCGACGCCGGCGACGGCCAGGTGGTCGAGGCCGGCGACACGATCGTGGCCAACTACCTGGGCCAGATCTGGGGCGGCGACGTCTTCGACAACTCCTACGACCGCGGCCAGCCGCTGAACTTCCAGGTCGGCGTCGGCATGGTCATCCGCGGCTGGGACGACGGCCTCGTGGGCCAGCGCGTCGGCTCGCGCCTGCTGCTGTCCATCCCCTCCGAGCTCGGCTACGGCGACCGCGGCGTCCCGCAGGCCGGCATCCGCGGCGGCGACACCCTCGTCTTCGTCACGGAGATCCTCGGCGTCATGTGA","MPSVEGAKGTKPTLTFPGTEAPEGLQVQVLDAGDGQVVEAGDTIVANYLGQIWGGDVFDNSYDRGQPLNFQVGVGMVIRGWDDGLVGQRVGSRLLLSIPSELGYGDRGVPQAGIRGGDTLVFVTEILGVM$","Peptidylprolyl isomerase, FKBP-type","Cytoplasm, Periplasm","Fk506-binding protein","peptidylprolyl isomerase; FKBP-type","peptidylprolyl isomerase, FKBP-type","","","","","

InterPro
IPR001179
Domain

Peptidyl-prolyl cis-trans isomerase, FKBP-type
PTHR10516	$\"[28-129]T$	FK506 BINDING PROTEIN
PF00254	$\"[33-127]T$	FKBP_C
PS50059	$\"[41-130]T$	FKBP_PPIASE

noIPR
unintegrated

unintegrated
G3DSA:3.10.50.40	$\"[12-130]T$	no description
PTHR10516:SF29	$\"[28-129]T$	FK506-BINDING PROTEIN 1

","BeTs to 11 clades of COG0545COG name: FKBP-type peptidyl-prolyl cis-trans isomerases 1Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0545 is ------y--d---cefghsn-j-it-Number of proteins in this genome belonging to this COG is 2","***** IPB000774 (Domain amino terminal to FKBP-type peptidyl-prolyl isomerase) with a combined E-value of 4.2e-09. IPB000774D 78-105 IPB000774E 114-129","","","-61% similar to PDB:1Q6H Crystal structure of a truncated form of FkpA from Escherichia coli (E_value = 3.4E_19);-61% similar to PDB:1Q6I Crystal structure of a truncated form of FkpA from Escherichia coli, in complex with immunosuppressant FK506 (E_value = 3.4E_19);-61% similar to PDB:1Q6U Crystal structure of FkpA from Escherichia coli (E_value = 3.4E_19);-58% similar to PDB:1U79 Crystal structure of AtFKBP13 (E_value = 9.9E_19);-58% similar to PDB:1Y0O crystal structure of reduced AtFKBP13 (E_value = 9.9E_19);","Residues 33 to 127 (E_value = 1.1e-35) place ANA_1819 in the FKBP_C family which is described as FKBP-type peptidyl-prolyl cis-trans isomerase.","","protein (PPIase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1820","1973815","1972751","1065","8.94","4.12","38089","ATGCGCAGTTTCCGGTGCCGGTCCGTGGCGGCCGGACTGGACTGCGAGCGGCGGCCTCTCCGGGCCGACGGTCCCAGCCCCCTCAGAGAGGATGAGAGGAACATGTCCAATCCCTTCTTCAGCCGAAGCACCGCCTTCAAGGAAGGCGGCCATGCGCCCGGGACCGCCCCGGCCCAGACGCCCAACGGCTACCCCACCATGCCCGGCTACCAGGCCGGCCAGTACGGCCAGCAGGCAACCGGCTACGGCCAGCAGTACGGCCAGTACGGCAACCAGTACGGTCAGCAGGTGGCCGGCTACGGCCAGGTGACTCCCGAGCAGATGGCCGGCCTGGAGACCCAGTACCAGGCGCCGTCGGCCACCAACGCGGACATGCGCCGCATGACCTACGACGACGTCATCATCCGCACCGCCGGCATGTTCGCCGTCATCCTGGCCATGGGCGCCCTGACCTGGAGCCTGGTGACCAATGAGGCGACTTTCGGTATGGGCGCCGCGGCAGTGCTCGCCGGCATCGTCGGCAGCGGCGTCCTCGGTCTGGTCAACAGCTTCAAGCGGGAGCCCTCCCCGGCCCTCATCCTGGCCTACGCGGCCTTCGAGGGACTGATGCTGGGTGGCGTCTCCGGCGTCATGGAGGCCCGCTACGAGGGGATCGTCGTCCAGGCCGTGCTCGCGACGCTGGCCACCTTCGGCGCCATGCTCGCGGCCTACTCCTACGGCGGCTTCCGGGTCCAGGGCAGGTTCCGTCGAGTGGTGGTCGTGGCCACCTTCGGCTACATGATCTTCAGCCTCATCAACTTCGTCCTCATGATGACCGGCGCCACCACCGGCGCCTGGGGCCTGCGCTCCCTGACCATCATGGGGATTCCGCTGGGAGTCCCGCTGGGAATTCTTGCGGTCATCCTGGCCTCCTTCTTCCTGGCGATCGACTTCGAGTCCATTGAGAACGGGGTCCGCAACGGGCTGCCCCGGCGCTACGCCTGGGCGGGGGCCTTCGGCCTGGTCGTCACCCTCGTGTGGCTCTACGTGGAGTTCCTCCGCCTGCTGAGCTACTTCCGCGACTGA","MRSFRCRSVAAGLDCERRPLRADGPSPLREDERNMSNPFFSRSTAFKEGGHAPGTAPAQTPNGYPTMPGYQAGQYGQQATGYGQQYGQYGNQYGQQVAGYGQVTPEQMAGLETQYQAPSATNADMRRMTYDDVIIRTAGMFAVILAMGALTWSLVTNEATFGMGAAAVLAGIVGSGVLGLVNSFKREPSPALILAYAAFEGLMLGGVSGVMEARYEGIVVQAVLATLATFGAMLAAYSYGGFRVQGRFRRVVVVATFGYMIFSLINFVLMMTGATTGAWGLRSLTIMGIPLGVPLGILAVILASFFLAIDFESIENGVRNGLPRRYAWAGAFGLVVTLVWLYVEFLRLLSYFRD$","Integral membrane protein","Membrane, Extracellular","B1306.07 protein","hypothetical protein","protein of unknown function DUF1112","","","","","

InterPro
IPR010539
Family

Protein of unknown function DUF1112
PF06539	$\"[125-354]T$	DUF1112

noIPR
unintegrated

unintegrated
tmhmm	$\"[133-153]?$ $\"[159-181]?$ $\"[191-211]?$ $\"[217-237]?$ $\"[252-272]?$ $\"[291-311]?$ $\"[326-346]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB001285 (Synaptophysin/synaptoporin) with a combined E-value of 7.5e-06. IPB001285F 68-112 IPB001285F 50-94 IPB001285F 69-113 IPB001285F 57-101 IPB001285F 62-106 IPB001285F 64-108 IPB001285F 58-102 IPB001285F 51-95 IPB001285F 75-119","","","-39% similar to PDB:1CQI CRYSTAL STRUCTURE OF THE COMPLEX OF ADP AND MG2+ WITH DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE (E_value = );-39% similar to PDB:1CQJ CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE (E_value = );-39% similar to PDB:1JKJ E. coli SCS (E_value = );-39% similar to PDB:1JLL Crystal Structure Analysis of the E197betaA Mutant of E. coli SCS (E_value = );-39% similar to PDB:1SCU THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION (E_value = );","Residues 125 to 354 (E_value = 9.1e-64) place ANA_1820 in the DUF1112 family which is described as Protein of unknown function (DUF1112).","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1821","1973872","1974048","177","7.46","0.62","6290","GTGGGGAGAGATCCCCACTCGCGCACCAAGTGCCGCCGTCTCCTCGACGCCCTACGGCGTCACATCGACCGATCGGTTCTCATCCTCCAGGAGGACCCTCCTCCCCCTGACGGACCCGCCCCGGCCGAACCCGGGTTCGTCACCTCGGCCGATTCGCCGACGACGGCGCATTCCTAG","VGRDPHSRTKCRRLLDALRRHIDRSVLILQEDPPPPDGPAPAEPGFVTSADSPTTAHS$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-66% similar to PDB:1HRU THE STRUCTURE OF THE YRDC GENE PRODUCT FROM E.COLI (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1822","1974064","1975119","1056","9.54","8.36","37270","TTGCTCCGTGGGAGCAGCCCCCTGGAGGAACCACGGAGATCCATCCACCCCCTGGCCAGAGGCCCACGTGGAAGAGAGAACATCATGATCGAGGCAGTCAATCTCACCAAGCGCTACGGCAAGAAGACCGCGGTGGACAACATCTCCTTCACCGTCGAGCCCGGCACCGTCACCGGCTTCCTGGGTCCCAACGGGGCGGGCAAGTCCACCACGATGCGCATGATCATGGGCCTGGACAAGCCCACCAGCGGCAAGGTCACCATCAACGGGCGCCCCTACCGGCAGCTGTCGGCCCCCCTGTGCGAGGTCGGCGCCCTGCTGGACGCCAAGGGCCTACACGGCTCGCGCAGCGCCCGCAGCCACCTTCGCCAGCTGGCCGCCTCCAACGGTATCCCCGCCAAGCGGGTCGATGAGGTCCTCGACATCACTGGCCTGACCTCGGTGGCCAAGAAGCGCGTCAAGGGCTTCTCCCTGGGCATGGGCCAGCGCCTGGGCATCGCGGCGGCACTGCTGGGCGACCCCGGTGTGCTCCTGTTCGACGAGCCCGTCAACGGCCTGGACCCCGAGGGCGTCAAGTGGGTGCGTGAGACCTGCCGCCGTCTGGCCGGCGAGGGCCGCACCGTGTTCATCTCCTCCCACCTCATGAGCGAGATGGCTCAGACCGCCGACCACCTCCTGGTCATCGGTCGTGGCCGGATCCTGACCTCCGGCCCGGTCGACGACGTCATCGCCTCGGCCACCACCGACCGGGTGCGCGTGGCCTCCCCTCAGGCCACCCAGCTCGCCGAGCTCATGGCCTCCCGCAACCTGGCCGCCCAGCCCGTGGCCCCCAACGTCCTGGAAACCACCGCGACCACCGCCGCCACCATCGGTGAGCTGGCCGCCCAGGGCGGCATCGTCCTGCACGAGCTCACCACCATCCGCGCCAGCCTCGAAGAGGCCTACATGACTCTGACCAGCGACTCCGTGGAGTACCGCACCGACCCCGCCTCCCAGGACCAGATGCAGCAGGCCCCGGTGCGCCAGGTCGTGCCGCAGGGCTCCACCCGGGGCTGA","LLRGSSPLEEPRRSIHPLARGPRGRENIMIEAVNLTKRYGKKTAVDNISFTVEPGTVTGFLGPNGAGKSTTMRMIMGLDKPTSGKVTINGRPYRQLSAPLCEVGALLDAKGLHGSRSARSHLRQLAASNGIPAKRVDEVLDITGLTSVAKKRVKGFSLGMGQRLGIAAALLGDPGVLLFDEPVNGLDPEGVKWVRETCRRLAGEGRTVFISSHLMSEMAQTADHLLVIGRGRILTSGPVDDVIASATTDRVRVASPQATQLAELMASRNLAAQPVAPNVLETTATTAATIGELAAQGGIVLHELTTIRASLEEAYMTLTSDSVEYRTDPASQDQMQQAPVRQVVPQGSTRG$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Periplasm, Membrane","ABC transport protein","putative ABC transporter ATP-binding subunit","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[156-196]T$	Q9S6T6_STRCO_Q9S6T6;
PF00005	$\"[55-231]T$	ABC_tran
PS50893	$\"[30-255]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[54-232]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[23-259]T$	no description
PTHR19222	$\"[30-251]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[30-251]T$	ABC TRANSPORTER

noIPR
unintegrated

unintegrated
tmhmm	$\"[63-83]?$ $\"[97-117]?$ $\"[145-165]?$ $\"[184-206]?$ $\"[211-231]?$ $\"[276-296]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-52% similar to PDB:1JGJ CRYSTAL STRUCTURE OF SENSORY RHODOPSIN II AT 2.4 ANGSTROMS: INSIGHTS INTO COLOR TUNING AND TRANSDUCER INTERACTION (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","Tue Aug 14 16:27:18 2007","","","","","Tue Aug 14 16:27:18 2007","","","","Tue Aug 14 16:27:18 2007","Tue Aug 14 16:27:18 2007","","","","","yes","","" "ANA_1826","1976131","1978005","1875","8.86","5.15","66473","ATGTCAGCCCCCGCGCCCCTGACCGACCCCGCACTTCTACGGACCCTCATCCGTTCCCTGCCCGCGACGCCCTCCCCCGGCCCGACGATCCCCGCCTCCGACCAGGGAGGGAAGAGCCCTCATCGTCGCAAGCGGGTCCCTCAACCGCACACGTCAGCGTCGATCACGACCCCTTGGAATGACACACTGACTCCTATGTCCAGCCAGCTGCCACCCCCTCAGCCCGGCCGCAGCACCACCATGCCCGATGAGGACGACCTGGAGCTCGCGCCCGAGCCACGGGGACTGCTGCGCGCGATCCGCTCGTGGTACCACCGCCACCCGATGATCGTCGACATCTCCATCGCCGCCGGCGTCATCGTCTACACCCTCGTCACGGGTATCGCTTTTCTCCTGCGGCCGAGTAGCCCGGTGAAGACCTACCCCATCCTGCCCCTGGCCTTGATCGCGATCGCGCTGTTGGGAATTGCGCTGGCACTTCGTCGGCGCTACCCCGTGTGGAGCTGGGCCGCCATCCTCCTGATCCCGGAGGTCTATCAGTTCGCAGTCCTGCGGTTCTTCCACTTCACGACGGAGCAGCAGCTGTACGCGACCCTCGGCGTCAGTGGTATGGGGCTGATGTCACTCCCCTTCGCCCTGGGCACCATCGCCTCGCACCGCAGGCCGGCCGCTGCATGGACCGCGGGGGCCATCTCCCTGGCGGTTCTCACGGCGGACCTCAGCCTGACGACTCCCAGCATGACGGTTGGGGAGCTCCTGCGCACCACCGTCATCCTCGTTCTCTTCATCCTGGTCGGCATCCTGGTCGGCTTCAACGCCCGCTCCGCCCGCCTGCGGCTCAAGGCCATGGAGCTGCGCTCGACCCGAATGGCTCTGGCCAGTGAGCAGGCGGCGCTGCTGGCGGCCGCTGAGGAGCGCAGTCGCATCGCCCGGGAGATGCACGACGTCGTCGCCCATTCCCTGGCCGTCATGATCACCATGGCCGACGGCGCCGCCGCCACCGTGGAGCGCAACCCGGCCACGGCCAAGCAGGCCATGGAGACCCTGGCCGAGGCCGGACGCAGTGCCCTGGCCGACACCCGCCGCCTGGTGGGGGTCCTGCGAGAGGACCCCTCAGTCGCCGCGGGGCAGACCACCGCCTCGGAGGCCTCATCGGGACCTGCCTCCTCAACCGGCGTTGACAGCGCGGCGCCGCTCTCCGACCAGCCCGACCCCTCCGGCCGCCCCCGCTGGAACCTGACGGGCAGGAGTGCGCAGTCCCCGGAGCCCTCAGCCCCCTCAGAGGGCTCCTCGTCGTCGGCCCATCAGCACGAGGTCCGCGACCTGCCGGTGCCCGAGTTCGCCCCCCTGGGGACGGTGACGCCGGTCGAGCCCAGCGCCCCCATCGCCAACCTGCGCCAGCAGGCCACCAACGGTGCGGGCGACCGCTCCCGCGGTGACCTGCCCCTGGCCCCCTCCCCCGAGCAGGCCGACATCACCGAGCTCGTCAAACGCTTCGAGGCAGCAGGAGTGCCGGTCACCTACCGGTGGGTGGGCGCGGCGCTCCCGGAGGACAAGGCCCTCCAGCTCACCGTGTTCCGCATCGCCCAGGAGGCCCTGACCAACGTGCTGCGCTACGCGCCCACGACGCCGGCCGTCAGCGTCGACGTCGAGCGGCACATCGGCACCGTGGTCCTCACCGTGGACAACGAGGCCGCCCCCGGCACGCGCCCGATGCACGGATCCGGCAAGGGGCTGATCGGCATGCGCGAACGCGCATCGGTCTATGGTGGGACCGTACAGGCCGGCCCGACTCCCACGGGTTGGCGAGTCCGCGCGGTCCTGCGCTGGGACGAGCATGACGAAGGGACTTTCTCATGGCAGACGCCCCTGTGA","MSAPAPLTDPALLRTLIRSLPATPSPGPTIPASDQGGKSPHRRKRVPQPHTSASITTPWNDTLTPMSSQLPPPQPGRSTTMPDEDDLELAPEPRGLLRAIRSWYHRHPMIVDISIAAGVIVYTLVTGIAFLLRPSSPVKTYPILPLALIAIALLGIALALRRRYPVWSWAAILLIPEVYQFAVLRFFHFTTEQQLYATLGVSGMGLMSLPFALGTIASHRRPAAAWTAGAISLAVLTADLSLTTPSMTVGELLRTTVILVLFILVGILVGFNARSARLRLKAMELRSTRMALASEQAALLAAAEERSRIAREMHDVVAHSLAVMITMADGAAATVERNPATAKQAMETLAEAGRSALADTRRLVGVLREDPSVAAGQTTASEASSGPASSTGVDSAAPLSDQPDPSGRPRWNLTGRSAQSPEPSAPSEGSSSSAHQHEVRDLPVPEFAPLGTVTPVEPSAPIANLRQQATNGAGDRSRGDLPLAPSPEQADITELVKRFEAAGVPVTYRWVGAALPEDKALQLTVFRIAQEALTNVLRYAPTTPAVSVDVERHIGTVVLTVDNEAAPGTRPMHGSGKGLIGMRERASVYGGTVQAGPTPTGWRVRAVLRWDEHDEGTFSWQTPL$","Two-component system sensor kinase","Membrane, Periplasm","chitinase two-component sensor kinase","two-component system sensor kinase","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[520-611]T$	HATPase_c
SM00387	$\"[520-614]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[305-372]T$	HisKA_3

noIPR
unintegrated

unintegrated
tmhmm	$\"[110-130]?$ $\"[140-160]?$ $\"[165-183]?$ $\"[193-213]?$ $\"[223-245]?$ $\"[251-271]?$	transmembrane_regions

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[178-220]T$	Q9X850_STRCO_Q9X850;
PR00038	$\"[178-192]T$ $\"[192-208]T$ $\"[208-220]T$	HTHLUXR
PF00196	$\"[175-232]T$	GerE
SM00421	$\"[175-232]T$	HTH_LUXR
PS50043	$\"[174-236]T$	HTH_LUXR_2
PS00622	$\"[192-219]T$	HTH_LUXR_1

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[23-138]T$	Q6AFS8_BBBBB_Q6AFS8;
PF00072	$\"[21-135]T$	Response_reg
SM00448	$\"[21-134]T$	REC
PS50110	$\"[22-138]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[151-238]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[16-142]T$	no description
PTHR23283	$\"[52-143]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF49	$\"[52-143]T$	TWO-COMPONENT SENSOR PROTEIN HISTIDINE PROTEIN KINASE (DHKK, DHKJ)

InterPro
IPR001328
Family

Peptidyl-tRNA hydrolase
PD005324	$\"[78-167]T$	PTH_STRCO_Q9K3T8;
G3DSA:3.40.50.1470	$\"[5-197]T$	no description
PTHR17224	$\"[4-198]T$	PEPTIDYL-TRNA HYDROLASE
PF01195	$\"[6-197]T$	Pept_tRNA_hydro
TIGR00447	$\"[4-198]T$	pth: peptidyl-tRNA hydrolase
PS01195	$\"[17-30]?$	PEPT_TRNA_HYDROL_1
PS01196	$\"[119-129]T$	PEPT_TRNA_HYDROL_2

","BeTs to 19 clades of COG0193COG name: Peptidyl-tRNA hydrolaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0193 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001328 (Peptidyl-tRNA hydrolase) with a combined E-value of 6.8e-36. IPB001328A 6-21 IPB001328B 98-129 IPB001328C 138-148","","","-52% similar to PDB:1RYM Structure of the Group II Intron Splicing Factor CRS2 (E_value = 9.9E_25);-51% similar to PDB:1RYN Structure of the Chloroplast Group II Intron Splicing Factor CRS2 (E_value = 1.3E_24);-51% similar to PDB:1RYB Crystal Structure of the Chloroplast Group II Intron Splicing Factor CRS2 (E_value = 2.9E_24);-47% similar to PDB:2PTH PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI (E_value = 1.0E_21);-47% similar to PDB:2HLP CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM (E_value = 1.0E_21);","Residues 6 to 197 (E_value = 1.7e-69) place ANA_1828 in the Pept_tRNA_hydro family which is described as Peptidyl-tRNA hydrolase.","","hydrolase (pth)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1829","1980384","1979434","951","7.35","1.73","33453","ATGAGACAACACAGTGCCTTCAACCCTCGACCGCGCGACCTAAGGATCGACCGCGCGAGCCGGGCCGGCCTTGCGGGGCTCATTGCCTGCGCCTGCCGGCCTGCCGGCCTGCCAGCCCGCCGGCCCTGCCAGGTGGGGCGCCTCACCGGCTGTGCGGCTGTTCGCCCGCCCCGCCCATGCCGTAGTCTTGCCCACGTTGCCCCGGCGAGGGACGCGCCAACACGGCGCGCATCCGTGATCGACGTGGTGGTACCTGGCGGTACTGCGCGTCGTCGCGCCCAGCCGGACCACCATCAGCCGCGGGGCACCGGGCCCCGCCTCATCCGCAAGGAGAGCCACATGGCCAACAACGCCATCACCCTCAAGGCCCAGGACCGCACCGAGTTCGGCAAGGGCTCGGCCCGCCAGGCCCGCCGCGCCGGCCAGGTCCCCGCCGTCGTCTACGGCCACGGCACCGAGCCCCGCCACCTCCTGCTCGAGGAGCACGCCACCCGCCTGGCCCTGCGCAGCAACGACAACGCCCTGGTCGAGCTGGACCTCGCCAGCGGCGAGACCCTCCTGGCCCTGGCCAAGGACGTGCAGCGTCACCCCATCCGCCCCGGCGTGCAGCACGTCGACTTCCTCCTGGTGGACCGCAACGAGCGTGTCGACGTCGAGGTCCCGGTCACCGTCATCGGTGAGGCCGCCCCCGGCACCATCCACATGATCGAGGCCGCCACCGTCATGGTCTCCGCCCCGGCCGTCTCCGTGCCCGAGGCCATCGAGGTCGATGTCACCGGCGTCGCCGCCGGCACCGTCCTGACCCTTGCCGACATCACCCTGCCCAAGGGCGTCGAGGCCGTCGCCGACGCCGAGACCGCCGTGGTCAACGTGGCCAACGAGCACGCCGTCGCCTCCGAGGTCCCCGAGGAGGCCCCCGCTGAGGGCGACGCCGAGGCCGAGGCCGAGTGA","MRQHSAFNPRPRDLRIDRASRAGLAGLIACACRPAGLPARRPCQVGRLTGCAAVRPPRPCRSLAHVAPARDAPTRRASVIDVVVPGGTARRRAQPDHHQPRGTGPRLIRKESHMANNAITLKAQDRTEFGKGSARQARRAGQVPAVVYGHGTEPRHLLLEEHATRLALRSNDNALVELDLASGETLLALAKDVQRHPIRPGVQHVDFLLVDRNERVDVEVPVTVIGEAAPGTIHMIEAATVMVSAPAVSVPEAIEVDVTGVAAGTVLTLADITLPKGVEAVADAETAVVNVANEHAVASEVPEEAPAEGDAEAEAE$","Ribosomal protein L25","Cytoplasm","ribosomal L25p family protein","50S ribosomal protein L25","ribosomal 5S rRNA E-loop binding protein Ctc/L25/TL5","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Stoldt M., Wohnert J., Gorlach M., Brown L.R. The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases. EMBO J. 1998. 17(21):6377-6384. PMID: 9799245","","","

InterPro
IPR001021
Family

Ribosomal protein L25
PD012503	$\"[121-210]T$	Q6AAC8_PROAC_Q6AAC8;
PF01386	$\"[121-207]T$	Ribosomal_L25p
TIGR00731	$\"[121-293]T$	ctc_TL5: ribosomal protein L25, Ctc-form

noIPR
unintegrated

unintegrated
G3DSA:2.170.120.20	$\"[212-302]T$	no description
G3DSA:2.40.240.10	$\"[118-208]T$	no description
PS51257	$\"[1-32]T$	PROKAR_LIPOPROTEIN

","BeTs to 17 clades of COG1825COG name: Ribosomal protein L25 (general stress protein Ctc)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1825 is -------qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001021 (Ribosomal protein L25) with a combined E-value of 5.9e-23. IPB001021A 126-149 IPB001021B 184-207","","","No significant hits to the PDB database (E-value < E-10).","Residues 121 to 207 (E_value = 9.2e-31) place ANA_1829 in the Ribosomal_L25p family which is described as Ribosomal L25p family.","","L25p family protein (rplY)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1830","1980448","1981746","1299","10.52","21.28","47845","ATGGGTAACTCGATTTCGCCGTCTCGGCGTGAGCAGGTCATAGGTTTTGACTCCAGGACCAGTGGGATGAGCGTGGAGGAGTTCTGCGCTCAGGTGGGTATCTCGCGGGCCTCGTTCTACCGGATACGCCGACGCGCTGAGCACGAGGGCCTGGCTGCCGCGCTGACACCGCGTTCACGGGCCCCGCGCCACCCGGCGCGGGTGTGGGACCAGGGCACTGATGAGCGCATCGCTCAGGTTCGTGCCGACCTGCTCGCCGCCGGCCGGGAGGCGGGTCCGGCCTCGGTGTGGTGGGTGATGAGCCAGGGCGCCAGCGTTCCGGCTCCTTCGCGCGCGACGATCGCCCGCAGCCTACGCAGAGCCGGCCTGGTGGTCCCCGCCCCGCGCAAGCGGCCCAGGACGTCGTACAAGCGCTTCACCCGCAGCGCGGCCAACGAGCTGTGGCAGATCGACGGCTTCCAATGGCACCTGGAGGACCATCTGGTGACCGTCTACCAGGTCGTTGACGACTGCTCGCGGGTCATCACCGCCCTGAGGGCCTGCTGGGGCGGTGAGAGCGTGGCAGGCACCCGCATGGTCCTTGAGGAGGCCTTCGCCACCTGGGGGCGCCCGGCGGCGATCCTGTCGGACAACGCACTGGCGTTCAACACCAGCCGTATCACTGGCCCGGGAGCCACCGAGAAGTGGCTGGCATCCCTGGGGGTGCGTCCCATCAGCGGGCGGGTGGGCCACCCTCAGACCCAGGGCAAGGTCGAGCGCTCCCACCAGCCGGCAGCCGCCTGGCTGCGCGCCCACCCGGCCAGCACCCTTGAGGAGCTCAACGCCGAGCTGGACCGCTTCACCAGCTACTACAACACCGAACGCCAGCACCAGGGCCACGGCGTCGCACTGACCCCGCTGAGGGTATGGGCTCAGACCCCCAGGGCGCTGGCCAGCCCAGCCCCCATCGACCTGGAGCGCCTACCAGCCGGCGGCGGCCCCATCAGCCTGCCCGACCCCGCCGATCCCGACCAGGCCGTGGACCGCGCCCGACGCACCGTGATGTCCAACGGGTGCGTGTCCTACAAGGACCGTGCACTGTCACTGGGCCAGACCATGCGCGGCGTCGAGGTCACCCTGATCGAGTACACCACGCGCCTGGACCTCTACGACCCCGACGGACGCCGCTTCGTGTCCCTGCCCTGGCCCCAACCCACCCAGAGGCAGCAAGGCAACCGCTCCACCATCGACACCAAGAAACCGCCCTACAGACTCATCCCGCTCCCACCCCGACGCCCCCGAACGTCTCACAGGTCATAA","MGNSISPSRREQVIGFDSRTSGMSVEEFCAQVGISRASFYRIRRRAEHEGLAAALTPRSRAPRHPARVWDQGTDERIAQVRADLLAAGREAGPASVWWVMSQGASVPAPSRATIARSLRRAGLVVPAPRKRPRTSYKRFTRSAANELWQIDGFQWHLEDHLVTVYQVVDDCSRVITALRACWGGESVAGTRMVLEEAFATWGRPAAILSDNALAFNTSRITGPGATEKWLASLGVRPISGRVGHPQTQGKVERSHQPAAAWLRAHPASTLEELNAELDRFTSYYNTERQHQGHGVALTPLRVWAQTPRALASPAPIDLERLPAGGGPISLPDPADPDQAVDRARRTVMSNGCVSYKDRALSLGQTMRGVEVTLIEYTTRLDLYDPDGRRFVSLPWPQPTQRQQGNRSTIDTKKPPYRLIPLPPRRPRTSHRS$","Integrase","Extracellular, Membrane","Predicted transposase","integrase; catalytic region","Integrase, catalytic region","","Asante-Appiah E., Skalka A.M. HIV-1 integrase: structural organization, conformational changes, and catalysis. Adv. Virus Res. 1999. 52:351-369. PMID: 10384242Thomas M., Brady L. HIV integrase: a target for AIDS therapeutics. Trends Biotechnol. 1997. 15(5):167-172. PMID: 9161051Katzman M., Katz R.A. Substrate recognition by retroviral integrases. Adv. Virus Res. 1999. 52:371-395. PMID: 10384243","","","

InterPro
IPR001584
Domain

Integrase, catalytic core
PF00665	$\"[140-304]T$	rve
PS50994	$\"[128-307]T$	INTEGRASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[143-310]T$	no description

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[4-30]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
tmhmm	$\"[10-30]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","(twin-arginine translocation) pathway signal sequence domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1833","1982620","1983243","624","5.39","-7.41","22785","ATGCCCCGGCCATGTGGGCACTCCACGGGTGAGGAACTGGGATCATCCCCAGGACAACGGCCCCGAGCCCGCCAGCGCCTCGCAACGCCGGCAGCACTCCCGCACCCGACTACCAGAGAGCAGACCATGAGGTACTTCGCCGAGTACATCGTCGGCAGGAACGGTCCCATCGACGTCTTCCTGCAGCCCCAGACCCCTCAGCTCGTCGCCGATGAGGTCGCCCGCAAGCTCACTTCGCCCGCCTACCTGGACGGCGCAAGGCACTTCGCCCTTGCGGTGTGGGCGCTGCCCGACGGAATGACGCATATGGACGAGGTCCCCGAGTCCTCCCCGGCGCGGGCCACCTACATCCAGTGCGGCGGCTCGGCAGCCGCCATGAGCGTTGAGATACGCGTGACTCACGAGGACGACTCCTACGAGCACTACGCGGTGGCCCGCGAGCCCGTCGCCGACCCCGCAGCGTGGACCACGATCACCTGGGACAACGGGGGTCCCGAGCCCTTCTCGCTGCGTCTGCACCCCGAGGAGGTCTTCACCGGCGAGCAGGCAACCCCTGTCTTTCGTGCCTACATCGAGAACGGGGCGCTTCCACCCACGGAGCTCCTGCGCAGGCTCGACATCTAG","MPRPCGHSTGEELGSSPGQRPRARQRLATPAALPHPTTREQTMRYFAEYIVGRNGPIDVFLQPQTPQLVADEVARKLTSPAYLDGARHFALAVWALPDGMTHMDEVPESSPARATYIQCGGSAAAMSVEIRVTHEDDSYEHYAVAREPVADPAAWTTITWDNGGPEPFSLRLHPEEVFTGEQATPVFRAYIENGALPPTELLRRLDI$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1834","1984145","1983273","873","4.76","-12.71","29444","GTGAGCGCGACGTCGCTGACCTGGGACGGGCGCAGCATCCCCGGCCCCGGCGGCCTGCCCGCGGTGGCCGTCTCCCTGACCGGGCCGAGCCTCGCCCAGGCGCGGACCCAGGCCCGCAGCGCCATCGACGCCGGTGCCGACGTCCTCGAGCTGCGCGTCGACCTGCTCGAAGAGGCCGGTGCCCTGGCCGCCCCCGCCCCGCTGGACGCGGCCACGGCCGCCGCCCAGGTCCTGGAGTGCCTGCGGGGACTGAGGGAGGCCATCGACACCACCACCGACGGCGCTGCTGCCGGTTCCCCGGTGCTGCTCACCTGCCGCACCGCCGCCGAGGGGGGCCGGGCCCAGCTGGACGACGCCGCCTACGGCTCCCTTCTGCGCTCCGTCCTCGACGGGCTCGCCGACTGGGCGCCCGAGCGCCGCCCGGCCGCCATCGACGTCGAGGTTCAGCGCGGCTGCCTGCCTCAGGTCTGCGCACAGGCCCATGCACTGAGCATCGACGTCGTCGCCTCCTTCCACGACTTCGAGGCCACCCCCGCCGATGAGGCCCTCGAGGAGGTCCTGGCCCGCATGGCCCGTGAGGGTGCGGACCTGGCCAAAATCGCCGTGTGGCCCACGAGTGCCGACGACGTCGCCCGCCTCCTGGGCGTGTGCGCGCGGGCCACGGCAGGCGCGGGGGAGCGCAGCGGCCTGGGTGTGCCCGTGGCGGCCATGTCCATGGGGGCGCTCGGGGTGGTCAGCCGTGTGGCGCCGGCCTTCGGGTCGGCGCTGACCTTCGCCGTCGTCCCCGACGAGCAGGGACAGGCCAGGGCCTCCGCCCCCGGCCAGATGCCGATCCAGGACGTGCGCCGCTGCCTGGAGCTCCTGCGCGCCTGA","VSATSLTWDGRSIPGPGGLPAVAVSLTGPSLAQARTQARSAIDAGADVLELRVDLLEEAGALAAPAPLDAATAAAQVLECLRGLREAIDTTTDGAAAGSPVLLTCRTAAEGGRAQLDDAAYGSLLRSVLDGLADWAPERRPAAIDVEVQRGCLPQVCAQAHALSIDVVASFHDFEATPADEALEEVLARMAREGADLAKIAVWPTSADDVARLLGVCARATAGAGERSGLGVPVAAMSMGALGVVSRVAPAFGSALTFAVVPDEQGQARASAPGQMPIQDVRRCLELLRA$","3-dehydroquinate dehydratase","Cytoplasm","3-dehydroquinate dehydratase (3-dehydroquinase)(Type IDHQase)","3-dehydroquinate dehydratase ","3-dehydroquinate dehydratase","","Deka R.K., Kleanthous C., Coggins J.R. Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase. J. Biol. Chem. 1992. 267(31):22237-22242. PMID: 1429576","","","

InterPro
IPR001381
Domain

Dehydroquinase class I
PD005337	$\"[170-289]T$	Q8ELI5_OCEIH_Q8ELI5;
PF01487	$\"[22-284]T$	DHquinase_I

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[5-288]T$	no description

noIPR
unintegrated

unintegrated
PTHR21088	$\"[162-289]T$	3-DEHYDROQUINATE DEHYDRATASE

","BeTs to 9 clades of COG0710COG name: 3-dehydroquinate dehydrataseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0710 is aompkzyq---lb-e----n---i--Number of proteins in this genome belonging to this COG is 1","***** IPB001381 (Dehydroquinase class I active site) with a combined E-value of 2.3e-24. IPB001381A 47-57 IPB001381B 102-112 IPB001381C 168-178 IPB001381D 237-247 IPB001381E 269-282","","","-50% similar to PDB:1GQN NATIVE 3-DEHYDROQUINASE FROM SALMONELLA TYPHI (E_value = 4.4E_20);-50% similar to PDB:1L9W CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT (E_value = 4.4E_20);-50% similar to PDB:1QFE THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE DEHYDRATASE FROM SALMONELLA TYPHI (E_value = 4.4E_20);-48% similar to PDB:2GPT Crystal structure of Arabidopsis Dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (E_value = 1.4E_13);-50% similar to PDB:1SFJ 2.4A Crystal structure of Staphylococcus aureus type I 3-dehydroquinase, with 3-dehydroquinate bound (E_value = 3.4E_12);","Residues 22 to 284 (E_value = 7.4e-36) place ANA_1834 in the DHquinase_I family which is described as Type I 3-dehydroquinase.","","dehydratase (3-dehydroquinase) (Type IDHQase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1835","1985167","1984142","1026","4.79","-17.34","35822","ATGACCCGCGTCGCCGCAATCGACTGCGGCACCAACACCATCCGCCTCCTCATCGCCGAGGCCGACCGCGACGACTTCGGGCGCCCCCGCTTGGAGGTGCTGCGCCGCCGCAACGAGATTGTGCGCCTGGGCCAGGGGGTGGACCGCACCGGCCTGCTGGACCCCGAGGCCCTGGAGCGCACCCTGGCCGCCGTGGCCTCCTACGTCGCCGACTGCACCGAGCTGGGCGTCGCCCCCGGGGGCGACGTGCGGCGCTTCGTGGCCACCTCCGCCACCCGCGATGCCCGCAACCGTGAGGACTTCGTGGCCGGGGTCAGGCGCCTGCTGGGCATTGATCCTGAGGTCGTCAGCGGCCAGGAGGAGGCCCGGCTGTCCTTCACCGGCTCGCTGCTGGGCGCCGGTGAAGACGAGGGCACGCCGGAGTCGGGGGAGCACGCGCCCGCGCCGCGGCTCGTCGTCGACCTCGGGGGCGGCTCCACCGAGCTGGTCCTGGGCGTGGATGAGCCCAGCGCCGCCATCAGCCTGGACACCGGCAGCGTGCGTATCACCGAGCGCTTCCTCGCAGGCGGCGTCACCCCCGAGGTCGAGGCCGCCGCTCGGGCCGAGGTGCGTGGCCTGCTCGATGAGGCCGAGCGGGTCGTCGACCTGTCCGCCCCGGGGCGGCTGGTCGGCCTGGCCGGCACCATCACCACCGTCACCGCCCACGCCCTGGATCTTCAGTCCTTCGACCCGCAGGCCCTGAACGGTGCCGAGCTGAGCCCGCAGGCGGTCCTGGCCTCCTGCGAGGCGATCATCCACTCCACGCCCGAGCAGCGCGCCTCCTGGGGCTACCTGGCCCCCGGCCGCCGCGACGTCATCGCCGCGGGCGCCCTCGTGTGGAGCGAGGTCGTCACCCGCGTCGTGGAACGGACGGCCGCCGCCGGGCGCCCGCTGAAGCGGGTCACCACCAGCCTCTACGACATCCTCGACGGCATCGCCCTGTCGCTCGTGCCCGAGCCGGAGCCGACCGAAGGGACCCCGGCGTGA","MTRVAAIDCGTNTIRLLIAEADRDDFGRPRLEVLRRRNEIVRLGQGVDRTGLLDPEALERTLAAVASYVADCTELGVAPGGDVRRFVATSATRDARNREDFVAGVRRLLGIDPEVVSGQEEARLSFTGSLLGAGEDEGTPESGEHAPAPRLVVDLGGGSTELVLGVDEPSAAISLDTGSVRITERFLAGGVTPEVEAAARAEVRGLLDEAERVVDLSAPGRLVGLAGTITTVTAHALDLQSFDPQALNGAELSPQAVLASCEAIIHSTPEQRASWGYLAPGRRDVIAAGALVWSEVVTRVVERTAAAGRPLKRVTTSLYDILDGIALSLVPEPEPTEGTPA$","Ppx/GppA phosphatase","Cytoplasm","possible exopolyphosphatase-like protein","Ppx/GppA phosphatase","Ppx/GppA phosphatase","","Reizer J., Reizer A., Saier M.H., Bork P., Sander C. Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily. Trends Biochem. Sci. 1993. 18(7):247-248. PMID: 8212131","","","

InterPro
IPR003695
Family

Ppx/GppA phosphatase
PF02541	$\"[17-329]T$	Ppx-GppA

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.150	$\"[145-336]T$	no description
G3DSA:3.30.420.40	$\"[3-133]T$	no description

","BeTs to 15 clades of COG0248COG name: ExopolyphosphataseFunctional Class: F [Metabolism--Nucleotide transport and metabolism] Functional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0248 is ------yqvdr-bcefghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003695 (Ppx/GppA phosphatase) with a combined E-value of 9.8e-36. IPB003695A 5-18 IPB003695B 68-121 IPB003695C 148-188 IPB003695E 282-292 IPB003695C 147-187","","","-47% similar to PDB:1T6D MIRAS phasing of the Aquifex aeolicus Ppx/GppA phosphatase: crystal structure of the type II variant (E_value = 5.5E_20);-47% similar to PDB:1T6C Structural characterization of the Ppx/GppA protein family: crystal structure of the Aquifex aeolicus family member (E_value = 2.1E_19);-47% similar to PDB:1U6Z Structure of an E. coli Exopolyphosphatase: Insight into the processive hydrolysis of polyphosphate and its regulation (E_value = 1.5E_14);-47% similar to PDB:2FLO Crystal structure of exopolyphosphatase (PPX) from E. coli O157:H7 (E_value = 1.5E_14);","Residues 17 to 329 (E_value = 3.5e-40) place ANA_1835 in the Ppx-GppA family which is described as Ppx/GppA phosphatase family.","","exopolyphosphatase-like protein (AL442120)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1836","1985738","1985223","516","5.33","-6.02","18056","GTGAGCCCCACGCCCCAGACGCAGGAGCCGGTGTCGTCAGCCGACCTCGAGGCCCTGGCCGAGCAGCTGGGGAGAGTGCCGCGCGGAGTCGTCGCCATCGCGGCCCGCTGCGTGTGCGGTCGCCCCACCGTGGTGCGCACCGCCCCGCGTCTCGACGACGGAACCCCCTTCCCAACCAGCTACTACCTCACCCACCCGGCCGCCGTGAAGGGCTGCTCCACCCTGGAGGCCGAGCACCTCATGGAGACCTTCAACGCGGACCTGGCTGCCGACGCCGAGCTGGCCGCCGCCTACGCCTCCGCCCACGCCGACTACCTGGCCCGCCGCGCCGAGCTCGGGCAGGTCCCCGAGATCGAGGGGGTCTCTGCCGGCGGCATGCCCACGCGCGTCAAGTGCCTCCACGCCCTGCTCGGGCACACCCTGGCCGCCGGAGCCGGCGTCAACCCCATCGGCGACCGCACGCTGGAGGTCCTGCGCGAGCGCGAACTGTGGGATCCTGAGCGCTGCTCCTGCTGA","VSPTPQTQEPVSSADLEALAEQLGRVPRGVVAIAARCVCGRPTVVRTAPRLDDGTPFPTSYYLTHPAAVKGCSTLEAEHLMETFNADLAADAELAAAYASAHADYLARRAELGQVPEIEGVSAGGMPTRVKCLHALLGHTLAAGAGVNPIGDRTLEVLRERELWDPERCSC$","Uncharacterized conserved protein","Cytoplasm","Uncharacterized ACR","K09009 hypothetical protein","protein of unknown function DUF501","","","","","

InterPro
IPR007511
Family

Protein of unknown function DUF501
PF04417	$\"[31-158]T$	DUF501

","BeTs to 3 clades of COG1507COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1507 is -------qv-r---------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 31 to 158 (E_value = 9.7e-49) place ANA_1836 in the DUF501 family which is described as Protein of unknown function (DUF501).","","ACR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1837","1986427","1985735","693","9.20","3.93","24181","ATGACTCCACGCCGCCCCTCCTCCAGCCAGTCCGGGACGCGCCGCGTCGCCGGCGGCGCCCGGCCCCGCCAGGTACCGGCCGAGCGGGCGGCATCAGCGGGCGGATCCGGGGCCGGATCGTCCCGCTCCCGGTCCCGGGGCCTGCCGACGGCGGTGCCCGAGCGGACCCTGCCGCCCCGGGTCGTCATCCTGGCGGTCGTGTGCCTGCTGGCCTTCGTCGTCATCTTCACCTCCCTGCGCGCCTACCTGTCCCAGCAGGCCCAGTACGACGCCGTCGTCGACAGGATCAAGGAGGCCTCCGACACCTCCACCACCCTGGAGAACGAGTTGGCCCAGTGGAAGGACGACACCTACGTGCGCTCCCAGGTCCGTGAGCGCCTCGGCTACGTCATGCCCGGCGACACCAGCTACGTCGTCGTCGGTGCCGACTCCATGAAGGAGACCGAAGCCAGTGGTGGGGCCACCCCGGGCTCCCAGGACGCCCCCTGGTACAAGGAGCTCCGGGACTCCTCGCGGGCCGCCGGCCAGGCCGAGAGCACCGCCCCGGCAGGAGCGAAGGACGGGGCGGACGGCAAGACCCTCAACCCCGCCCAGAAGGATCTGCCGACCGGGGAGCCTAGCCAGGCACCCACCGATCCGCCCAAGACCACGCCGAAACCGGCCGCCACCCCGCAGACGAAGGAGACCCCGTGA","MTPRRPSSSQSGTRRVAGGARPRQVPAERAASAGGSGAGSSRSRSRGLPTAVPERTLPPRVVILAVVCLLAFVVIFTSLRAYLSQQAQYDAVVDRIKEASDTSTTLENELAQWKDDTYVRSQVRERLGYVMPGDTSYVVVGADSMKETEASGGATPGSQDAPWYKELRDSSRAAGQAESTAPAGAKDGADGKTLNPAQKDLPTGEPSQAPTDPPKTTPKPAATPQTKETP$","Septum formation initiator","Extracellular, Membrane","conserved hypothetical protein","hypothetical protein","Septum formation initiator","","Levin P.A., Losick R. Characterization of a cell division gene from Bacillus subtilis that is required for vegetative and sporulation septum formation. J. Bacteriol. 1994. 176(5):1451-1459. PMID: 8113187","","","

InterPro
IPR007060
Family

Septum formation initiator
PF04977	$\"[64-142]T$	DivIC

noIPR
unintegrated

unintegrated
tmhmm	$\"[61-83]?$	transmembrane_regions

","BeTs to 3 clades of COG2919COG name: Septum formation initiatorFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG2919 is ----------r-b-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 64 to 142 (E_value = 1.9e-14) place ANA_1837 in the DivIC family which is described as Septum formation initiator.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1839","1987948","1986662","1287","4.67","-28.51","45584","GTGGCCCTCATCGAGAACGTTCACGCCCGCGAGATCCTCGACTCCCGTGGCAACCCGACCCTCGAGGTCGAGATCCTTCTGGAGGACGGTGCTTCCGCTCGCGCCGCCGTCCCCTCGGGCGCCTCCACCGGTGCCTTCGAGGCCGTTGAGCTGCGCGACGGCGACAAGGGCCGCTACGGCGGCAAGGGCGTGGAGAAGGCCGTCGACAACGTCAACGACATCATCGCCCCCGAGATCATCGGCTTCGACGCCGCCGACCAGCGCGGCCTCGACCAGCTCATGATCGAGCTCGACGGCACCCCCAACAAGGGCAAGCTCGGCGCCAACGCCATCCTCGGCGTCTCCCTGGCCGCCGCCCAGGCCTCCGCCGAGTCCGCCGGTCTGGACCTGTTCCAGTACGTCGGCGGCCCCAACGCCCACGTCCTGCCCGTGCCCATGATGAACATCCTCAACGGTGGCTCCCACGCCGACTCCAACGTGGACATCCAGGAGTTCATGATCGCCCCCATCGGCGCCCCCACCTTCCGTGAGGCCCTGCGCATGGGCGCCGAGGTCTACCACGCCCTCAAGGCGGTCGTGAAGGACCGCGGCCTGTCCACCGGCCTGGGCGACGAGGGTGGCTTCGCCCCCAACCTCGACTCCAACCGTGAGGCCCTTGAGCTCATCGTCGAGGCCATCGAGAAGGCCGGCTACAAGCCCGGCAAGGACGTGGCCCTGGCCATGGACGTCGCCTCCTCGGAGTTCTTCGACGAGAAGACCAAGACCTACCAGTTCGAGGGCGAGGCCCGCGACAACGCCTTCATGGTCGACTACTACGAGAAGCTCATCACCGACTTCCCGATCGTCTCCATCGAGGACCCGCTCTCCGAGGACGAGTGGGACGACTGGAAGGCCCTGACCGACAAGATCGGCGACCGGGTCCAGCTCGTCGGTGACGACTTCTTCGTCACCAACCCCGAGCGCCTCGCCAAGGGCATCCAGCTCGGCGCCGCCAACGCCCTGCTGGTCAAGGTCAACCAGATCGGCTCCCTGACCGAGACCCTCGAGGCCGTGGAGATGGCCCACCGCGCCGGCTACAAGTCCATGACCTCCCACCGCTCCGGTGAGACCGAGGACGTCACCATCGCCGACCTGGCCGTGGCCACCAACTCCGGCCAGATCAAGACCGGCGCCCCCGCCCGCGGCGAGCGCGTCAACAAGTACAACCAGCTCCTGCGCATCGAGGAGGCCCTCGGCGACGCCGCGGTCTACGCCGGCGCCGGCGCCTTCCCCCGCTTCCAGGCCTGA","VALIENVHAREILDSRGNPTLEVEILLEDGASARAAVPSGASTGAFEAVELRDGDKGRYGGKGVEKAVDNVNDIIAPEIIGFDAADQRGLDQLMIELDGTPNKGKLGANAILGVSLAAAQASAESAGLDLFQYVGGPNAHVLPVPMMNILNGGSHADSNVDIQEFMIAPIGAPTFREALRMGAEVYHALKAVVKDRGLSTGLGDEGGFAPNLDSNREALELIVEAIEKAGYKPGKDVALAMDVASSEFFDEKTKTYQFEGEARDNAFMVDYYEKLITDFPIVSIEDPLSEDEWDDWKALTDKIGDRVQLVGDDFFVTNPERLAKGIQLGAANALLVKVNQIGSLTETLEAVEMAHRAGYKSMTSHRSGETEDVTIADLAVATNSGQIKTGAPARGERVNKYNQLLRIEEALGDAAVYAGAGAFPRFQA$","Phosphopyruvate hydratase","Cytoplasm","enolase","phosphopyruvate hydratase ","Phosphopyruvate hydratase","","Lal S.K., Johnson S., Conway T., Kelley P.M. Characterization of a maize cDNA that complements an enolase-deficient mutant of Escherichia coli. Plant Mol. Biol. 1991. 16(5):787-795. PMID: 1859865Peshavaria M., Day I.N. Molecular structure of the human muscle-specific enolase gene (ENO3). Biochem. J. 1991. 275:427-433. PMID: 1840492Segil N., Shrutkowski A., Dworkin M.B., Dworkin-Rastl E. Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence. Biochem. J. 1988. 251(1):31-39. PMID: 3390159Wistow G., Piatigorsky J. Recruitment of enzymes as lens structural proteins. Science 1987. 236(4808):1554-1556. PMID: 3589669","","","

InterPro
IPR000941
Family

Enolase
PD000902	$\"[145-419]T$	Q82HH5_STRAW_Q82HH5;
PR00148	$\"[37-51]T$ $\"[107-123]T$ $\"[161-174]T$ $\"[311-322]T$ $\"[334-348]T$ $\"[363-380]T$	ENOLASE
PTHR11902	$\"[1-210]T$	ENOLASE
PF00113	$\"[139-426]T$	Enolase_C
PF03952	$\"[3-134]T$	Enolase_N
TIGR01060	$\"[4-426]T$	eno: phosphopyruvate hydratase
PS00164	$\"[334-347]T$	ENOLASE

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.120	$\"[128-428]T$	no description
G3DSA:3.30.390.10	$\"[3-127]T$	no description
PIRSF001400	$\"[2-428]T$	Enolase

","BeTs to 25 clades of COG0148COG name: EnolaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0148 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB000941 (Enolase) with a combined E-value of 7.3e-181. IPB000941A 34-56 IPB000941B 90-135 IPB000941C 142-194 IPB000941D 200-231 IPB000941E 279-296 IPB000941F 307-337 IPB000941G 372-412 IPB000941G 353-393","","","-76% similar to PDB:1IYX Crystal structure of enolase from Enterococcus hirae (E_value = 2.0E_147);-75% similar to PDB:1W6T CRYSTAL STRUCTURE OF OCTAMERIC ENOLASE FROM STREPTOCOCCUS PNEUMONIAE (E_value = 8.1E_144);-70% similar to PDB:1E9I ENOLASE FROM E.COLI (E_value = 5.1E_122);-70% similar to PDB:2FYM Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E. (E_value = 5.1E_122);-66% similar to PDB:1TE6 Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom (E_value = 3.4E_110);","Residues 3 to 134 (E_value = 2.6e-66) place ANA_1839 in the Enolase_N family which is described as Enolase, N-terminal domain.Residues 139 to 426 (E_value = 1.5e-173) place ANA_1839 in the Enolase_C family which is described as Enolase, C-terminal TIM barrel domain.","","(eno) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1840","1986518","1988071","1554","4.27","-64.67","50415","ATGCTGCGGCACTGCTCCGTAGACGACGCTTCGGGGCAGGCGGGAGAACCCGTCTGCCCCGAAGCGGTGGGGTGCGTCGTCGTCGAGGCGCGGCTGAGGCGTCGCGTCAGTCAGCGGCTCGACGTCGGCAGGTCGCCGTCAGGCTCAGGCCTGGAAGCGGGGGAAGGCGCCGGCGCCGGCGTAGACCGCGGCGTCGCCGAGGGCCTCCTCGATGCGCAGGAGCTGGTTGTACTTGTTGACGCGCTCGCCGCGGGCGGGGGCGCCGGTCTTGATCTGGCCGGAGTTGGTGGCCACGGCCAGGTCGGCGATGGTGACGTCCTCGGTCTCACCGGAGCGGTGGGAGGTCATGGACTTGTAGCCGGCGCGGTGGGCCATCTCCACGGCCTCGAGGGTCTCGGTCAGGGAGCCGATCTGGTTGACCTTGACCAGCAGGGCGTTGGCGGCGCCGAGCTGGATGCCCTTGGCGAGGCGCTCGGGGTTGGTGACGAAGAAGTCGTCACCGACGAGCTGGACCCGGTCGCCGATCTTGTCGGTCAGGGCCTTCCAGTCGTCCCACTCGTCCTCGGAGAGCGGGTCCTCGATGGAGACGATCGGGAAGTCGGTGATGAGCTTCTCGTAGTAGTCGACCATGAAGGCGTTGTCGCGGGCCTCGCCCTCGAACTGGTAGGTCTTGGTCTTCTCGTCGAAGAACTCCGAGGAGGCGACGTCCATGGCCAGGGCCACGTCCTTGCCGGGCTTGTAGCCGGCCTTCTCGATGGCCTCGACGATGAGCTCAAGGGCCTCACGGTTGGAGTCGAGGTTGGGGGCGAAGCCACCCTCGTCGCCCAGGCCGGTGGACAGGCCGCGGTCCTTCACGACCGCCTTGAGGGCGTGGTAGACCTCGGCGCCCATGCGCAGGGCCTCACGGAAGGTGGGGGCGCCGATGGGGGCGATCATGAACTCCTGGATGTCCACGTTGGAGTCGGCGTGGGAGCCACCGTTGAGGATGTTCATCATGGGCACGGGCAGGACGTGGGCGTTGGGGCCGCCGACGTACTGGAACAGGTCCAGACCGGCGGACTCGGCGGAGGCCTGGGCGGCGGCCAGGGAGACGCCGAGGATGGCGTTGGCGCCGAGCTTGCCCTTGTTGGGGGTGCCGTCGAGCTCGATCATGAGCTGGTCGAGGCCGCGCTGGTCGGCGGCGTCGAAGCCGATGATCTCGGGGGCGATGATGTCGTTGACGTTGTCGACGGCCTTCTCCACGCCCTTGCCGCCGTAGCGGCCCTTGTCGCCGTCGCGCAGCTCAACGGCCTCGAAGGCACCGGTGGAGGCGCCCGAGGGGACGGCGGCGCGAGCGGAAGCACCGTCCTCCAGAAGGATCTCGACCTCGAGGGTCGGGTTGCCACGGGAGTCGAGGATCTCGCGGGCGTGAACGTTCTCGATGAGGGCCACTTGGTGCTCCTTGCTGAGGGGATCGTGATGCGGTCGTCGGCGTCGGGCACGCTCGCGCGCGACTGCCGAATGCAGGATCAGCCTAGCGGGCCGACTCCCCCACCACGAGGGCCATGGTCCTGA","MLRHCSVDDASGQAGEPVCPEAVGCVVVEARLRRRVSQRLDVGRSPSGSGLEAGEGAGAGVDRGVAEGLLDAQELVVLVDALAAGGGAGLDLAGVGGHGQVGDGDVLGLTGAVGGHGLVAGAVGHLHGLEGLGQGADLVDLDQQGVGGAELDALGEALGVGDEEVVTDELDPVADLVGQGLPVVPLVLGERVLDGDDREVGDELLVVVDHEGVVAGLALELVGLGLLVEELRGGDVHGQGHVLAGLVAGLLDGLDDELKGLTVGVEVGGEATLVAQAGGQAAVLHDRLEGVVDLGAHAQGLTEGGGADGGDHELLDVHVGVGVGATVEDVHHGHGQDVGVGAADVLEQVQTGGLGGGLGGGQGDAEDGVGAELALVGGAVELDHELVEAALVGGVEADDLGGDDVVDVVDGLLHALAAVAALVAVAQLNGLEGTGGGARGDGGASGSTVLQKDLDLEGRVATGVEDLAGVNVLDEGHLVLLAEGIVMRSSASGTLARDCRMQDQPSGPTPPPRGPWS$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1842","1988075","1989049","975","6.09","-7.04","33283","TTGCACAGTGTTCACGCCCGGCGAGAAACACTGGACGACGACGGTCCCTGGGTTCCGCCGTCGTCCTGGGGGCCCTGTACGGCCCTACTGGCCGCTGGTCTCGGGCTGCTCGGCGCCCTGGCCAACCTCGCCCGCAGCACCGTCGGCCTGACCGGTCTGGCCCTGCCCGTCGGTCTGGCCGGAGTCGGCGGGCTGCTGGCCGCCCTGCTGAGGAGCCTGTTGCTGAGGCTGCTGCTGTTGCTGCGGGGCCTGCTGCTGGCCTCCACCCTGCTGTTGCTGGGGCGCCTGCTGCTGGCCACCATCCTGCTGAGGGGCTTGCTGCAGGCCACCACCGAAGGGGTTGTTGCCCGCTTCCAGACGGGGATCCGTCTGGGTCAACCAGGTCTGAGCCTTGTTGGAGTAGCGCGGGGAGACGTCGCCGTCGAGCGTGCCGTAGAGCTTCTGCAGCTCGCTGATCACGGCCTGCCCCTGCTGCCCCTGCTGAGCGAGCTCCTGGTACTTACCCGACAGGACAATCGCCCGCAGATAGGTGATCGTTGCCGCCTGGCGGGGCTCGAAGCCCAGGCGCTCCTTGGACCACTGCACGGTCTGCGCGTCAGTGACGGTCACTCCGTGGGCCTGGCCGACCTCCACCATGGCGGGGGCCTGAACGAGGAGTCCCGCGATCTGAGGCCGGTTCACGCCCTGACGCTCCAGGGTTTCCCGGCCGAGTGCGGAGTCCAGTTCCTTGACGACGACGTCGACGTCCTTCTCACTGACGACCACGGAGTGGCGGGCCCCGTCCAGGCCGGTGTAGTGCATGTCGGCCACCTGACCGGGGTGGTCGGAGCAGCCGGCGAGCGCCCCGACGGCAAGGAGGAGTGCAGCGCTGGCGGCGAGGACGCGCGTGCGTGCGGCAAGGCTTCGGGTCACGGTCTGCTCCTGGAAGGGGACGACGCCGGAGGGCGACATGGTGTCACAACATTTCTGCCCTGA","LHSVHARRETLDDDGPWVPPSSWGPCTALLAAGLGLLGALANLARSTVGLTGLALPVGLAGVGGLLAALLRSLLLRLLLLLRGLLLASTLLLLGRLLLATILLRGLLQATTEGVVARFQTGIRLGQPGLSLVGVARGDVAVERAVELLQLADHGLPLLPLLSELLVLTRQDNRPQIGDRCRLAGLEAQALLGPLHGLRVSDGHSVGLADLHHGGGLNEESRDLRPVHALTLQGFPAECGVQFLDDDVDVLLTDDHGVAGPVQAGVVHVGHLTGVVGAAGERPDGKEECSAGGEDARACGKASGHGLLLEGDDAGGRHGVTTFLP$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Eriani G., Delarue M., Poch O., Gangloff J., Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 1990. 347(6289):203-206. PMID: 2203971Sugiura I., Nureki O., Ugaji-Yoshikawa Y., Kuwabara S., Shimada A., Tateno M., Lorber B., Giege R., Moras D., Yokoyama S., Konno M. The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. Structure 2000. 8(2):197-208. PMID: 10673435Perona J.J., Rould M.A., Steitz T.A. Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry 1993. 32(34):8758-8771. PMID: 8364025","","","

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[260-271]?$	AA_TRNA_LIGASE_I

noIPR
unintegrated

unintegrated
signalp	$\"[1-99]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[47-69]?$ $\"[78-98]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-54% similar to PDB:2BUF ARGININE FEED-BACK INHIBITABLE ACETYLGLUTAMATE KINASE (E_value = );-56% similar to PDB:1VR5 Crystal structure of Oligopeptide ABC transporter, periplasmic oligopeptide-binding (TM1223) from THERMOTOGA MARITIMA at 1.73 A resolution (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1843","1990525","1990196","330","8.89","7.16","11999","ATGCGGCGCCCACAGCGCCCGCGATCTCGGTGTGGATCATGCTCGGACACCTCTGAGCTCGAGATGCAACCAGATGGCAAAGGTGATCCGGCGTGCCATCCACAGCACGGCTCCGCCCACCACCGCCCCCACGGCCAGAACCTCCAGCTCCGGCAGTGCGGGAGGAGCCTGAGCCACCAACGCCGTCGCAGCGCCTGCTCCCAACGCTCCGACTGCGGTCCCCGCGATGACCCGAAGCAGCTCCCGGCCACAGCGCTCGCGGACCAGTGCCGCCTCGGTGGCGCCGATCAGGCGACGCAGCCGGATCTCTCCGCGTTGCTCAGGCAGTGA","MRRPQRPRSRCGSCSDTSELEMQPDGKGDPACHPQHGSAHHRPHGQNLQLRQCGRSLSHQRRRSACSQRSDCGPRDDPKQLPATALADQCRLGGADQATQPDLSALLRQ$","Hypothetical protein","Extracellular","CG15720-PA","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-32% similar to PDB:2E31 Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase (E_value = );-32% similar to PDB:2E32 Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase (E_value = );","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1844","1990561","1991577","1017","6.07","-3.64","35863","ATGTTCACGCTGGTCAGCGTCATCCTCACCATGACACTGGCCGAGGTGATGACCCAGTCGTCAGTGGTCATGGCGGCCCAGCGTCTGCGCGAGCTCGACGCCACCACCTTCACGCCCTACTACCTCGGGGATCTGGACAACGATCCGAGTACTGGTTTGATGGAGGACCTGGGTGATCGCATCGCCTCAGGCTCCGCTTACACGATGATCCTCGGCAACGTGGAGGTCGACGACCCCTCCTTCGCCGGAGGCAATCCAGTGGTGATCGTCGTCGGGCAGGCCGCTCAAAACGCCATGACCGGAGCCAGGCTCTGCTCGCCAGCGCCCTGCGCCATGGTTGGGGGTCAGGTCCCCCATCCTGTGGACGGACCGCTGCACGTCGGAGGTCGCAGCGTGCCGGTGGCAGGCCGAACGCCGTCGTCGGCCTCGCTCTTCGACCCCGCTGCGGTGGGAATCGACCTGGACAGGTCGGTGCTGATCGCGCTGCCGCCCTCGAGCCTGGATCACCTGGATAGCACCGAGCAGGAGGAGGCCGTGTGGCGCACGGTTCTGCTCTCCGCCACCGACGACGACACCGAGCAGTTCCTCACGGCTGCCAGGCAGGATCGGCTCGCCCTGGTTCCGCACCGGTTGGCCGCCGATCAGCCCGAGCGCTTCCGCAAGCTGGTGGTGTGGGCTGCCATGCACGGCGTCGGCTTGCTGGGACTGACTGCCCTGGTCTCCATCGCCTACAGCGCCTCCATTCGGTCGGTGCTGCGACGCGAACGAGCCGACCTGCTGCTGCGTCATCTCTATGGCGCGACGTCGGCTCAGCTCACCATACGCCTGGCGGCCTTCCTGGCCGTCACCATGCTGGTGCTTCCGGCTCTGACGCTTCTGGCCTTGGCGGCCAGCACTCTGTTGAGGGGCGCCGCAGCGGCAGCCGGGAGCGCCCTCATCATCATCTACCTGGTCTTTCTCATGACGACAGTCCGCCGTGTGCGATTCGAGTTCGCGCGATCCGGGACAGTCCGATGA","MFTLVSVILTMTLAEVMTQSSVVMAAQRLRELDATTFTPYYLGDLDNDPSTGLMEDLGDRIASGSAYTMILGNVEVDDPSFAGGNPVVIVVGQAAQNAMTGARLCSPAPCAMVGGQVPHPVDGPLHVGGRSVPVAGRTPSSASLFDPAAVGIDLDRSVLIALPPSSLDHLDSTEQEEAVWRTVLLSATDDDTEQFLTAARQDRLALVPHRLAADQPERFRKLVVWAAMHGVGLLGLTALVSIAYSASIRSVLRRERADLLLRHLYGATSAQLTIRLAAFLAVTMLVLPALTLLALAASTLLRGAAAAAGSALIIIYLVFLMTTVRRVRFEFARSGTVR$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PS00211	$\"[81-95]?$	ABC_TRANSPORTER_1

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[224-244]?$ $\"[272-294]?$ $\"[300-320]?$	transmembrane_regions

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[145-188]T$	Q8YZL0_ANASP_Q8YZL0;
PF00005	$\"[34-221]T$	ABC_tran
PS50893	$\"[5-224]T$	ABC_TRANSPORTER_2
PS00211	$\"[146-160]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[33-224]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[2-224]T$	no description
PTHR19222	$\"[5-224]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32	$\"[5-224]T$	ABC TRANSPORTER

","BeTs to 22 clades of COG1136COG name: ABC-type transport systems, involved in lipoprotein release, ATPase componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1136 is aom--z-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 10","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.7e-33. IPB005074C 23-70 IPB005074D 134-177 IPB005074E 198-218***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 6.7e-22. IPB013563A 23-57 IPB013563C 143-170***** IPB005116 (TOBE domain) with a combined E-value of 1.5e-21. IPB005116A 41-57 IPB005116B 85-102 IPB005116C 146-159 IPB005116D 166-185***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 3.7e-16. IPB010509B 34-59 IPB010509D 141-185***** IPB010929 (CDR ABC transporter) with a combined E-value of 4e-09. IPB010929K 21-65 IPB010929M 143-189 IPB010929A 33-52 IPB010929D 162-190","","","-53% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 1.4E_28);-53% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 3.0E_28);-49% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 2.8E_21);-49% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 2.6E_19);-49% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 2.6E_19);","Residues 34 to 221 (E_value = 6e-46) place ANA_1845 in the ABC_tran family which is described as ABC transporter.","","releasing system ATP-binding protein","","1","","","","","","","","","","","Tue Aug 14 16:28:25 2007","","Tue Aug 14 16:28:25 2007","","","Tue Aug 14 16:28:25 2007","Tue Aug 14 16:28:25 2007","","","Tue Aug 14 16:28:25 2007","Tue Aug 14 16:28:25 2007","","","","","yes","","" "ANA_1846","1996035","1992286","3750","5.39","-29.99","133643","GTGCTCCTGACTGCGCTCCTGCCTCCGCTGCTCGCCGACGCCGACATCGCCCGCACCGTCCGCGCCGCCTCCTCCCGCTCGCGCACCGACCGCAGCCTCGTCGTCGCCCCGGGCGCCCGGCCCGCCGTCCTGGCCGCCATGGCCCTGGGGGAGGAGGGCGTCCAGAGGGTCGCCGGCGGCGACGCGCCGGCGACCGGCTCCGCCGAGGTCTCCGGCACGCCCCTGCTCGTCGTCACCGCCACCGGCCGCGAGGCCGAGGAAACCGCCCTTGCCCTGCGCAGCTACCTGCCGGCCGACGACGTCGCCGTCATGCCCGCCTGGGAGACCCTGCCCCACGAGCGCCTCTCGCCGCGCGCCGACACCGTCGCCCAGCGCCTGTCCGTCCTGCGCCGCCTGGCCCACCCCGAGGAGGGTGGGGCGATCCGCGTCCTCATCGTTCCCGTGCGTGCCCTGCTGGCCCCCGTCATTGCCGGACTCGGCGAGCTTGAGCCCGTCCAGCTGGCCCCCGGTCTGACCGTCGGCCTGGAGGAGACCGCCCGCCGCCTGGAGGCCGCCGCCTACACGCGCGTCGACATGGTCGAGTCCCGCGGCGAGTACGCCGTGCGCGGCGGCATCCTCGACGTCTTCCCGCCCTCCGAGCCCCGGCCGGTGCGCGTGGACTTCTTCGGCGACGAGATCGACGAGGTCTCCTCCTTCGCCGTCGCCGACCAGCGCACCATCGAGACGCTGGGCGCCGTCACCGCCACCGCCTGCCGAGAGCTGGTCCTCACCGACGCGGTGCGCGAGCGCGCCGCCGCCCTGGTCGACGCCGTCCCCGGCGCCGCCGACATGCTGGAGAAGATCAGTCAGGGCATCGCCGTGGAGGGCATGGAGTCCCTCGCCCCGGTGCTGGTCGAGGCGATGGTCCCGCTGCTGGACCTCGTCGGCGACCGGCTCACGGTGCTGCTGGAGCCCGAGCGGGTGCGCAAGCGCGCCGAGGACCTGACCGCCACCACTACCGAGTTCCTCGCCGCCGCCTGGACCTCGGCGGCCTCCGGCGGCACGGTTCCCGTCGACCTGTCCGCCGCCGCCTTCGCCCACCTGGCCGAGGCCCGGGCCCTGGCCCTGTCCTCCAACCGCGGCTGGTGGTCCTTCACCGCCCTGGCCGCCGGCCCCGAGACCACCCGCCTGGACCTCAGCGACCCCCACACCTACCGCGGCGAGCTCGAGCGGGCCGTGGCCGACCTGGGCCGGCTGGCCCGCCAGGGCTGGACCGTCGTCGTGGCTACCGACGGTCCCGGACCCGGCCGGCGCATGGCCCAGCTCCTGGGCGACGGCGACGTCCCCGCCCGCATCGTCGACCAGCTCTCGGAGGTCGGTGAGCTCGGCCGCGACGGCGACTGGGTCCCCGACCCGGCCGCTGTTTCTGATGACGCCGACGGCTCGGCCGGTGCCCCGACGGCGGGCCCCGGCGACGGCGTCGTGCGCGTCACCCAGGCCAGCGCCGGCCATGGCTTCCTCGCCGAGGGCCTGCGCCTGGCACTCATCGCCGAGTCCGACCTCACCGGGCGGGCCTCGGCAGGCCCCCGCGAGCGCCGCAGCCTGCCGGCCCGCCGCGCCCGCCGCTCCGTGGACCCCCTGTCCCTGCACGCCGGGGACCTTGTGGTTCATGCCCAGCACGGGGTGGGGCGCTTCATCGAGCTGAGCCGGCGCACTGTGGGTGGGGCCCGCTCCTCGGCCACCCGCGAGTACCTCGTCATCGAGTACGCCCCCTCCAAGCGCGGCCAACCCGGCGACCGCCTCCTGGTGCCGACCGACGCCCTGGACCAGGTCACCAAGTACGTCGGCGGCGACAGCCCCGCCCTGAGCAAGATGGGCGGCGCCGACTGGGCCAAGACCAAGTCCAAGGCCCGCAAGGCCGTGCGCGAGATCGCCGGCGAGCTCGTGCGCCTCTACGCCGCCCGCGCCGCCACCACCGGTCACGCCTTCAGCCCCGACACCCCCTGGCAGACTGAGCTGGAGGAGGCCTTCCCCTACACCGAGACCCCCGACCAGCTCTCCACCATCGACGAGGTCAAGGCCGACATGGAGAAGGCCCAGCCGATGGACCGCCTCGTGTGCGGCGACGTCGGCTACGGCAAGACCGAGATCGCCGTGCGCGCCGCCTTCAAGGCCGTCCAGGACGGCAAGCAGGTCGCGGTCCTGGTGCCCACCACGCTCCTGGTGAGCCAGCACGCCGAGACCTTCACCGAGCGTTACGCAGGCTTCCCGGTGACCGTGGGGGCCCTGTCCCGCTTCCAGGACGCCGCCGAGTCCGCCAAGGTGCTCGAGGGCCTGGAGAAGGGGAGTGTCGACGTCGTCGTCGGCACCCACCGCCTCATCACCGGCCAGGTGAAGTTCAAGGACCTGGGCCTGGTCATCATCGATGAGGAGCAGCGCTTCGGGGTGGAGCACAAGGAGACCCTCAAGGCGCTGCGCACCAACGTGGATGTCCTGTCCATGTCCGCCACCCCGATCCCACGGACCCTGGAGATGGCGGTCACCGGCCTGCGCGAGATGTCCACCCTGGCGACCCCGCCCGAGGACCGCCACCCGATCCTGACCTACGTGGGCGCTTACGAGACCAAGCAGGTCTCCGCCGCGATCCGCCGTGAGCTGCTGCGCGAAGGGCAGGTGTTCTTCGTCCACAACCGGGTCGAGGACATTGACGCCACCGCCGCGCACTTGGCCGAGCTGGTGCCCGAGGCGCGCGTGGCCACCGCCCACGGGCAGATGAACGAGCACCAACTCGAGGCCGTCATCGACTCCTTCTGGCGCAAGGAGACCGACGTGCTCGTGTGCACCACGATCGTGGAGACCGGGCTGGACGTGTCCAATGCCAACACCCTCATCGTGGACCGTGCCGACCGCATGGGCCTGTCCCAGCTCCACCAGCTGCGCGGGCGCGTGGGGCGCGGCCGGGAGCGGGCCTACGCCTACTTCCTCTACCCCTCGGACAAGCCGCTGACCGAGACGGCCCTGGAGCGCCTGCGCACCATCGCCACCAACACGGATCTCGGGGCCGGGATGCAGGTGGCCATGAAGGACCTGGAGATCCGCGGCTCGGGCAACCTGCTCGGCGGCGAGCAGTCCGGGCACATCGCCGGGGTCGGCTTCGATTTGTACGTGCGCATGGTCTCCGAGGCCGTGGCCGCTTACAAGAAGGCCCTGGCCCGCTCCGGGAAGGCCGGGGCCGACGTGATCGGCTTTGAGGAGGGCGACGAGGAGGACGTCGAGCTGCGCATCGAGCTGCCCGTGGACGCCACCGTCCCCGAGGACTACATCCCCCACGAGCGCCTGCGCCTGGAGGCGTACACCAAGTTCGCGGCGGCGCGCTCGGGGGAGCAGGTCGACGACGTCCTGGAGGAGCTGGCCGACCGCTACGGGCCCGTGCCCGAGGCGACCGCCCGCCTGGCGGCGCTGGCGCGGCTGCGGGCCCTGGCCGCCGAGCTGGGGGTGCGCGAGATCGTCGCCCAGGGCAAGTCGGTGCGCTTCGCCCCGGTGGACCTGCCCGAGTCGGCGCGCATGAAGGTTACCCGCCTCTACCCGGGGACCGTGCTGAAGCCCGCCACGCGCACCATCGTGGTGCCCGCGCCGGGCACCAACCGCATGGGCGGGGCGGCCCTGTCCGGCGAGGAGGTCGTGCGGTGGGCCGAGGTGCTCCTGCGCGCCGTCGTCCAGGGCGACACCTCCTACGAGACCGAGGCCACCACCTACCGCAAGCGCCGCTGA","VLLTALLPPLLADADIARTVRAASSRSRTDRSLVVAPGARPAVLAAMALGEEGVQRVAGGDAPATGSAEVSGTPLLVVTATGREAEETALALRSYLPADDVAVMPAWETLPHERLSPRADTVAQRLSVLRRLAHPEEGGAIRVLIVPVRALLAPVIAGLGELEPVQLAPGLTVGLEETARRLEAAAYTRVDMVESRGEYAVRGGILDVFPPSEPRPVRVDFFGDEIDEVSSFAVADQRTIETLGAVTATACRELVLTDAVRERAAALVDAVPGAADMLEKISQGIAVEGMESLAPVLVEAMVPLLDLVGDRLTVLLEPERVRKRAEDLTATTTEFLAAAWTSAASGGTVPVDLSAAAFAHLAEARALALSSNRGWWSFTALAAGPETTRLDLSDPHTYRGELERAVADLGRLARQGWTVVVATDGPGPGRRMAQLLGDGDVPARIVDQLSEVGELGRDGDWVPDPAAVSDDADGSAGAPTAGPGDGVVRVTQASAGHGFLAEGLRLALIAESDLTGRASAGPRERRSLPARRARRSVDPLSLHAGDLVVHAQHGVGRFIELSRRTVGGARSSATREYLVIEYAPSKRGQPGDRLLVPTDALDQVTKYVGGDSPALSKMGGADWAKTKSKARKAVREIAGELVRLYAARAATTGHAFSPDTPWQTELEEAFPYTETPDQLSTIDEVKADMEKAQPMDRLVCGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLVSQHAETFTERYAGFPVTVGALSRFQDAAESAKVLEGLEKGSVDVVVGTHRLITGQVKFKDLGLVIIDEEQRFGVEHKETLKALRTNVDVLSMSATPIPRTLEMAVTGLREMSTLATPPEDRHPILTYVGAYETKQVSAAIRRELLREGQVFFVHNRVEDIDATAAHLAELVPEARVATAHGQMNEHQLEAVIDSFWRKETDVLVCTTIVETGLDVSNANTLIVDRADRMGLSQLHQLRGRVGRGRERAYAYFLYPSDKPLTETALERLRTIATNTDLGAGMQVAMKDLEIRGSGNLLGGEQSGHIAGVGFDLYVRMVSEAVAAYKKALARSGKAGADVIGFEEGDEEDVELRIELPVDATVPEDYIPHERLRLEAYTKFAAARSGEQVDDVLEELADRYGPVPEATARLAALARLRALAAELGVREIVAQGKSVRFAPVDLPESARMKVTRLYPGTVLKPATRTIVVPAPGTNRMGGAALSGEEVVRWAEVLLRAVVQGDTSYETEATTYRKRR$","Transcription-repair coupling factor","Cytoplasm","transcription-repair coupling factor","K03723 transcription-repair coupling factor (superfamily II helicase)","transcription-repair coupling factor","","Nicolas F.J., Cayuela M.L., Martinez-argudo I.M., Ruiz-vazquez R.M., Murillo F.J. High mobility group I(Y)-like DNA-binding domains on a bacterial transcription factor. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(14):6881-6885. PMID: 8692912","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[903-980]T$	Helicase_C
SM00490	$\"[896-980]T$	HELICc
PS51194	$\"[874-1024]T$	HELICASE_CTER

InterPro
IPR003711
Domain

Transcription factor CarD
PF02559	$\"[541-646]T$	CarD_TRCF

InterPro
IPR004576
Family

Transcription-repair coupling factor
TIGR00580	$\"[182-1163]T$	mfd: transcription-repair coupling factor

InterPro
IPR005118
Domain

TRCF
PF03461	$\"[1089-1195]T$	TRCF

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[675-839]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[670-862]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[688-849]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[163-251]T$ $\"[646-853]T$ $\"[853-1009]T$	no description
PTHR10967	$\"[3-13]T$ $\"[715-989]T$	DEAD BOX ATP-DEPENDENT RNA HELICASE
signalp	$\"[1-22]?$	signal-peptide

","BeTs to 16 clades of COG1197COG name: Transcription-repair coupling factor - superfamily II helicaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1197 is --------vdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB003711 (Transcription factor CarD) with a combined E-value of 5.2e-208. IPB003711A 548-558 IPB003711B 670-694 IPB003711C 695-732 IPB003711D 793-834 IPB003711E 835-863 IPB003711F 905-948 IPB003711G 949-988 IPB003711H 1012-1056","","","-63% similar to PDB:2EYQ Crystal structure of Escherichia coli transcription-repair coupling factor (E_value = 1.5E_159);-55% similar to PDB:1GM5 STRUCTURE OF RECG BOUND TO THREE-WAY DNA JUNCTION (E_value = 2.6E_66);-43% similar to PDB:2B2N Structure of transcription-repair coupling factor (E_value = 1.3E_17);","Residues 541 to 646 (E_value = 3.9e-43) place ANA_1846 in the CarD_TRCF family which is described as CarD-like/TRCF domain.Residues 675 to 839 (E_value = 3.8e-39) place ANA_1846 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 903 to 980 (E_value = 4.6e-17) place ANA_1846 in the Helicase_C family which is described as Helicase conserved C-terminal domain.Residues 1089 to 1195 (E_value = 1.2e-26) place ANA_1846 in the TRCF family which is described as TRCF domain.","","coupling factor (TRCF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1847","1997419","1996046","1374","9.87","12.27","48639","ATGTCCTTCGTCAGGACCCTGTTCATCGTCCTCCCCATGGTGGCCGCCGGTCTGGCGGTCCTCATCTTCGTGGCCGACCGCATCCACCGCCGCCCCATTGTCGGGGCCGGCCTGGTCATGGGCGCCATCGGCTTCGTGCCGGTGTGGGTGATGATCCCCTTCGAGCCCAATGTGCCTCCGGCCACCCTGGCCTGCTTCCTGGTGATCGTTGCCCTCCTGCCCGGTTTCTCGTGGCGGCTGACCAGCGGTGACTTCATGGTCGCCACCGCTTGGTGCCTGGTGGGCCTGTCCGTCGCCGCGGGCTCGCCGCTCAACTACGTCCTGTCCGACGTCGTCTTCGGCGCCCTGCCCGCCTACCTCGCCGGACGGCTGCTCGTGGAGCGGCTTGGGCTGCGGCGCATGGCCGAGGTCCTGGCGGTCGTGTGGATCGTGGTGGCGGTGCTGGCGCTGTTCGAGGCCGTCACCACCATCAACCCCTTCAGCTACATCACCATCGACAACAACCTCTACGAGGAGTGGGCCCCGCCCCTGGCTCGGGGCAGTTTCACCCGCGTCGAGGGGGCCTTCGGCCACCCCATCGCCCTAGGCGTGTGCCTGGCGGCCGGGATTCCCCTCATCCTGGCCACGCGGTGGAGGCCCGGCTACCGGATCGCGGCCGGCGCCCTCGTGCTGGGGGCGACCATCCCGACCTTCTCCCGCTCGGCGATCGCCTGCGCCGTCATCGCCGTCATCCTCAGCCTTATGCAGGTGCACACCAACATCCCCGCCCTGTGGCGGATGAGCTTCCTCATGGTGCTGGTCGGCGTGGGCAGCGTGCTGCTGCCCTACGTCCTGGGCGTCTTCGACTCAGCCGGCCGTGAGCAGGAGGACTCGGCCGGCTACCGCGGCGACATCCTCGTCCTGGTGCGTCAGCTCAAGCCGCTGGGACTGTCCCCGGTCTACCAGAAGTCAGGGGACTCGGTGTCCTGGGGCGGCTACAGCTCCATCGACAACCACCTGCTGCTGACCGCGTTGCGCTTCGGCTGGCTCCCCGTGGTGCTCATCATGGTGGGGCTGCTGGTCTACGGCTTCAGGGCCGTCGTTCAGCGTTCCAACCCCGCGCAGATCGCCCTGCTCAGCCTCATTCCGGCCTACGGCACGGTCGCCTTCATCACCCAGATCGGCACCGTTGTGTGGCTCATCGCCGGCATGGCCGCCTCAGCGCAGGTCTCCGTCCTGCTGGAGAGTCGCAACAAGACCACGGGTGGGGGCGTGGGCGTCGTCGCCGGGCACGCCAACCCCTGGAACCGGATCCGCAGCGGGGACTGGTCCCGCCGGGCCTTCGCCGGCCGATCGGTCCGGCCCGTCAGTGGTGCTGAGGCGGGGAGTCACTAG","MSFVRTLFIVLPMVAAGLAVLIFVADRIHRRPIVGAGLVMGAIGFVPVWVMIPFEPNVPPATLACFLVIVALLPGFSWRLTSGDFMVATAWCLVGLSVAAGSPLNYVLSDVVFGALPAYLAGRLLVERLGLRRMAEVLAVVWIVVAVLALFEAVTTINPFSYITIDNNLYEEWAPPLARGSFTRVEGAFGHPIALGVCLAAGIPLILATRWRPGYRIAAGALVLGATIPTFSRSAIACAVIAVILSLMQVHTNIPALWRMSFLMVLVGVGSVLLPYVLGVFDSAGREQEDSAGYRGDILVLVRQLKPLGLSPVYQKSGDSVSWGGYSSIDNHLLLTALRFGWLPVVLIMVGLLVYGFRAVVQRSNPAQIALLSLIPAYGTVAFITQIGTVVWLIAGMAASAQVSVLLESRNKTTGGGVGVVAGHANPWNRIRSGDWSRRAFAGRSVRPVSGAEAGSH$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[33-53]?$ $\"[59-78]?$ $\"[80-100]?$ $\"[106-126]?$ $\"[138-160]?$ $\"[188-208]?$ $\"[218-247]?$ $\"[261-281]?$ $\"[340-360]?$ $\"[374-394]?$	transmembrane_regions

InterPro
IPR003856
Domain

Lipopolysaccharide biosynthesis
PF02706	$\"[4-129]T$	Wzz

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 129 (E_value = 3.3e-05) place ANA_1849 in the Wzz family which is described as Chain length determinant protein.","","length determinant protein family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1850","2002283","2000301","1983","4.85","-29.68","70119","ATGTCAATGGTGTGCCGTGATCCGCCTGCGCGTTGCTCGCCATATGTACCGGAGGTTTCCGTGCGTCGTCTCTCCACCATCCCTCGTCTCGCCATCATCCTGTCCCTCCTGCCGCTGCTGCTCGCCTCGATGGTTGTCCTGACCCCCGCCGCGCCGGTGGCCATGGCTCAGGAGGCCGATGCCGATGGGAAGGACCAGGGCGACGGCTCGGACAACGTCGGTGACGACGAGGGCCCCGCCGCTGCAGGCGCCGACCCCTCCGGCCAGTCCTCTCGTGAGCCCGTGTACACGGCGGCACCCCTGCCCACGGTGCAGATCGACGGCGTCGCCTGGGGGCAGCTCGTCGTCGGCGACGTGGTCTACGTCGTCGGCAGCTTCGATAACGCCCGCCCGGCCGGCGCTCCCAAGAAGCAGCAGCAGGTCGCGCGCTCCAACATCCTGGCCTATGACCTCAACACCGGGAAACTCATCGAGGACTTCGCCCCCACCCTCAACGGGCCAGGACGCAGCCTGGCCCTCTCCCAGGATGGCAAGACCCTCTATGTGGCCGGGGAGTTCGACCAGGTCAACGGCGAGTGGCACAGCCGCCTGGCGGCCTTCGACCTCACCCAGGGGCATGGAACCCTCATCTCCTCCTTCAAGCCCATGTTCAACACGACCGTCAAGGACATCGCGGTCGCCGGCGACACCCTCTACGCCGGGGGCTACTTCACCAAGGTGAACGGTCAGCCGCGCGTCAGGGTGGCCGCCCTCAAGGCCTCCACCGGCCAGCTGCTGAACTGGACCGCCTCCGCGGAAGGGCCCAACGCCCAGGTGTACGCGATTGAGGTCTCCCCGGACCACTCCAAGGTCGTCATCGGCGGCTCCTTCTCCACGGTCAACGGCTCGAGCAAACCCGGCTACGGGATGGCGCTCCTGAGCGCCTCCACCGGCGAGCTGCTGCCCATGCCCGTCAATGACATCGTGCGCACAGCCGGTGAGAAGGCCGCCATCTTCGACATCGCCGTCGACGACGACGGTTTCTACGGCACCGCCTACTCCGCCGTCGGACGCCTTGACGAGGCCAACCTTGAGGGGAGCTTCAGGGCGGACTGGGACGGCAACCTCGTCTGGCTCGAGCCCTGCCACGGTGACACTTACGGGATCGCCCCCACCAAGGACACCGTCTACACGGTGGGGCACGCCCACTCCTGCGAGACCATCTACGGGTTCCCCAATATGCCCGAGGTTCGCAAGGACGGTCCGCACCCCCTGTATGTGCGGGCAATGGCCTTCACCAACAGCCCCGATATCACCATCCGCCACCAGGGGGTGGTCGACGGGTACCAGGACTGGTCGACGTCGGGCTACAAGAGCCCCACGATCATCGGCTGGTACCCGGACCTGGAGGCGGGCAAGTACACGGGTATGTCCCAGGCCGCCTACAAGGTGGACGTCACCGACTCCTACGTCCTCATGGTGGGTGAGTTCGTCGAGGCCAACGGCACGACCCAGCAGGGGATCGTGCGCTACCCCAAACGTGCGGGCCAGCCCACGCTGCCCCCCGAGGGCAAGGCCGAGACCCTGGCCGCCAAGGCGGAGGTGACGGCCTCGGGCTCGGTGAAGGTGGGGTTCAAAGCCACCTGGGACCGCGACGACCCGACCCTGACCTACAGCCTCTACCGGGATGACGAGACCACGCCGGTGGCCACCGAGAAGATCGGCGACACCCGCTGGGCTCTCACGAACCACAGCCTGGAGGACACCAGCTGCTCGCCCGGCGATCACACCTACCGCCTGGTGGTCTCCGACCCCAGCGGCAACACCATCACCGCCCAGATCCCCAGTGTCACGGTCCCCCAGACGGCGCAGAACAACAAGGAGAAGGGCAAGAAGGCGCAGCCCGCCGCTGAGGCGAAGGACGCCGCCAAGGACGCGGACCAGGGCGGCAACCAGCAGGACGCCGATGAGGACCAGGCCGCCGATGAGGAGGACGACAACTAG","MSMVCRDPPARCSPYVPEVSVRRLSTIPRLAIILSLLPLLLASMVVLTPAAPVAMAQEADADGKDQGDGSDNVGDDEGPAAAGADPSGQSSREPVYTAAPLPTVQIDGVAWGQLVVGDVVYVVGSFDNARPAGAPKKQQQVARSNILAYDLNTGKLIEDFAPTLNGPGRSLALSQDGKTLYVAGEFDQVNGEWHSRLAAFDLTQGHGTLISSFKPMFNTTVKDIAVAGDTLYAGGYFTKVNGQPRVRVAALKASTGQLLNWTASAEGPNAQVYAIEVSPDHSKVVIGGSFSTVNGSSKPGYGMALLSASTGELLPMPVNDIVRTAGEKAAIFDIAVDDDGFYGTAYSAVGRLDEANLEGSFRADWDGNLVWLEPCHGDTYGIAPTKDTVYTVGHAHSCETIYGFPNMPEVRKDGPHPLYVRAMAFTNSPDITIRHQGVVDGYQDWSTSGYKSPTIIGWYPDLEAGKYTGMSQAAYKVDVTDSYVLMVGEFVEANGTTQQGIVRYPKRAGQPTLPPEGKAETLAAKAEVTASGSVKVGFKATWDRDDPTLTYSLYRDDETTPVATEKIGDTRWALTNHSLEDTSCSPGDHTYRLVVSDPSGNTITAQIPSVTVPQTAQNNKEKGKKAQPAAEAKDAAKDADQGGNQQDADEDQAADEEDDN$","Hypothetical protein","Periplasm, Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[30-50]?$	transmembrane_regions

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[147-279]T$	Pribosyltran

InterPro
IPR002375
Family

Purine/pyrimidine phosphoribosyl transferase
PS00103	$\"[226-238]?$	PUR_PYR_PR_TRANSFER

InterPro
IPR005946
Family

Ribose-phosphate pyrophosphokinase
TIGR01251	$\"[12-323]T$	ribP_PPkin: ribose-phosphate pyrophosphokin

InterPro
IPR006034
Family

Asparaginase/glutaminase
PS00144	$\"[232-240]?$	ASN_GLN_ASE_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2020	$\"[3-178]T$	no description
PTHR10210	$\"[9-327]T$	RIBOSE-PHOSPHATE PYROPHOSPHOKINASE
PTHR10210:SF14	$\"[9-327]T$	RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1,2,3,4

","BeTs to 24 clades of COG0462COG name: Phosphoribosylpyrophosphate synthetaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0462 is aompkzyqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB000842 (Phosphoribosyl pyrophosphate synthetase) with a combined E-value of 1.2e-92. IPB000842A 72-104 IPB000842B 112-154 IPB000842C 170-203 IPB000842D 233-286***** IPB002375 (Purine/pyrimidine phosphoribosyl transferase) with a combined E-value of 1e-06. IPB002375 223-238","","","-67% similar to PDB:1DKR CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION. (E_value = 4.5E_72);-67% similar to PDB:1DKU CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION. (E_value = 4.5E_72);-67% similar to PDB:1IBS PHOSPHORIBOSYLDIPHOSPHATE SYNTHETASE IN COMPLEX WITH CADMIUM IONS (E_value = 4.5E_72);-61% similar to PDB:2H06 Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 (E_value = 7.7E_64);-61% similar to PDB:2HCR crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with AMP(ATP), cadmium and sulfate ion (E_value = 7.7E_64);","Residues 147 to 279 (E_value = 5.6e-29) place ANA_1851 in the Pribosyltran family which is described as Phosphoribosyl transferase domain.","","pyrophosphokinase (fragment)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1853","2004945","2003770","1176","6.20","-6.71","41117","ATGAGCGGCGTTGGGGTTCCCTCGCTCTCACGCCCGACGACGGTCACCCGGCCGCCGGCGGTATACGCGCCAACCGTCCATCCGTACCTGATTTCAGAAACCGTTGGAGTCCGTCCCCGGCCTCCGCCCGGTCACGGCCGGAGACGTCGGGAGCCCGGGCGCGAACCTGTGAGAAGAGGACACGTGACGCCAACCGCACCCGCCGCCGTCATCGTCATGGCCGCAGGCAAGGGAACTCGTATGCGATCGGTCACCCCCAAGGTCCTGCACCGGATCGGCGGTCGCAGCCTGGTGGACCACGCCGTCACCGCGGCCAGGGGGCTGGAGCCCCAGCACCTCGTCGTCGTCGTACGCCACGAGCGCGACGCCGTCATCGCCCATCTCGCCGAGGTCGCCCCCGACGCCGTCCCGGCCGACCAGGACGAGGTCCCCGGCACCGGGCGGGCCGTCGCCTGCGGGCTGGCCGCCCTGCCCGAGGACCTGGACGGGCCCGTCGTCGTCACCAGCGGGGACGTCCCGCTGCTGGACACCGCCACCCTGAAGGATCTCCTGGCTCAGCACCATGAGCGCGGGGATGCCGTCACCCTGCTGACCACCGAGCTCGAGGACCCCACCGGCTACGGGCGCGTCGTGCGCGAGGCCGACGGCACCGTCTCGGCCGTCGTCGAGCAGCGCGACGCCAGCGAGGCCCAGCGCGCCATCCGCGAGATCAACGCCGGCGTCTACGTCTTCGACGCCGCCCACCTGCGTACCGCTCTGGCGACCCTGGGCACGGACAACGAGCAGGGCGAGGTCTACCTCACCGACGTCGTCGCCCACGCCCACCGGGCCGGGCGGTCCACCAGCGCGCTGGTCGCCACCGACCACTGGCTCGTCGAGGGCTGCAACGACCGTGCCCAGCTCGCCGAGCTCGGCGCCGAGCTCAACCGCCGCGTCCTGGCCAACTGGATGGCCCAGGGCGTCGGCGTCGTCGACCCCTCCTCCACCTGGGTGGACGTCACCGCCGAGCTCGCCCAGGACGTCACCCTCGAGCAGGGCGTCCTCGTGCGCGGAAGCACCCGGATCGGCCAGGGCGCCCGCGTGGGCGCCTACGCGATCCTCACCGACGCCGTCATCCCGGCCGGCTGCGTCGTGGCCCCCTTCAGCCAGCTCGACGCCGACGCCGCCCAGGCCTGA","MSGVGVPSLSRPTTVTRPPAVYAPTVHPYLISETVGVRPRPPPGHGRRRREPGREPVRRGHVTPTAPAAVIVMAAGKGTRMRSVTPKVLHRIGGRSLVDHAVTAARGLEPQHLVVVVRHERDAVIAHLAEVAPDAVPADQDEVPGTGRAVACGLAALPEDLDGPVVVTSGDVPLLDTATLKDLLAQHHERGDAVTLLTTELEDPTGYGRVVREADGTVSAVVEQRDASEAQRAIREINAGVYVFDAAHLRTALATLGTDNEQGEVYLTDVVAHAHRAGRSTSALVATDHWLVEGCNDRAQLAELGAELNRRVLANWMAQGVGVVDPSSTWVDVTAELAQDVTLEQGVLVRGSTRIGQGARVGAYAILTDAVIPAGCVVAPFSQLDADAAQA$","UDP-N-acetylglucosamine pyrophosphorylase","Cytoplasm, Extracellular","UDP-N-acetylglucosamine pyrophosphorylase","glucosamine-1-phosphate N-acetyltransferase / UDP-N-acetylglucosamine pyrophosphorylase ","Nucleotidyl transferase","","","","","

InterPro
IPR001228
Domain

4-diphosphocytidyl-2C-methyl-D-erythritol synthase
PF01128	$\"[68-105]T$	IspD

noIPR
unintegrated

unintegrated
G3DSA:2.160.10.10	$\"[321-388]T$	no description
G3DSA:3.90.550.10	$\"[57-320]T$	no description
PTHR22572	$\"[76-384]T$	SUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF17	$\"[76-384]T$	UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE-RELATED

","BeTs to 15 clades of COG1207COG name: N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch acetyltransferase domains)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1207 is -------qvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-53% similar to PDB:1HM0 CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU (E_value = 2.7E_50);-53% similar to PDB:1HM8 CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A (E_value = 2.7E_50);-53% similar to PDB:1HM9 CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A AND UDP-N-ACETYLGLUCOSAMINE (E_value = 2.7E_50);-53% similar to PDB:1G95 CRYSTAL STRUCTURE OF S.PNEUMONIAE GLMU, APO FORM (E_value = 4.6E_50);-53% similar to PDB:1G97 S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+ (E_value = 4.6E_50);","Residues 68 to 105 (E_value = 1.4e-05) place ANA_1853 in the IspD family which is described as Uncharacterized protein family UPF0007.Residues 69 to 301 (E_value = 3.4e-11) place ANA_1853 in the NTP_transferase family which is described as Nucleotidyl transferase.","","pyrophosphorylase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1854","2005311","2006480","1170","11.30","21.48","42990","GTGCGACTCATCGAGCTCGACGGGCTGCGCGGGCTGGCCGCCGTCGTCGTGCTCATCCACCACGCCCTGGAGACCGTCCCCGCGCTGGCGGAGGTCGGGGCGCGGCCCGGCACCGTGCCCACCGGCACCTTCAACCGGATCCTCACCCAGAGCCCACTCCACCTGCTGTGGGCGGGCCACGAGGCCGTCCTCATCTTCTTCGTCCTGTCCGGTGTGGCCCTGACCTACCCGGTGGCCCGCCGCCACGCCCAGGGGCGGCGCTTCGACTGGGTCGACTACGCCCCGAGGCGCTTCGTGCGCCTGTGGCTGCCGGCGGCGGCCTCCACCACCTTCGCGGTCATCGCGATGCTGCTCGTGCCGCGCTCGGAGAATCCGGCGCTGGGGCACTGGATGACCGTCACCCACCCCGTGGGGCTCGGGGCGCGCCAGATGCTCATGGAGTACCTGCTCATCCCCAAGCACGCCTACCGCAACACCGTCCTGTGGTCCTTGCACGCCGAGGCGATCTTCTCCTTCGTGCTGCCCCTGATGATCCTCGGGGTGGCCCTGTGCGCCCGCTGGCGGATCTCCTGGCTGCCGGTGGTGGCAGCCCTGGCGGTGCCCGTCATCACCGCCAGCCCCGGCTCGGGCAGCTACCTGCCGGTCTTCACCATCGGTGCGGTCATGGGCTGGGCCTGGGGGCACAACCCCGCCCCGGTGCCGCAGCGCCCCCAGCCCTGGGCGACGGCGCAGGCCCTGGTGTGCCTGCTGCTCATCACCCTGGCCTGGTGGCCGGGGATGGAGAGCCACACGGCCCAGCGCCTGGCCAACGCGGTCACCCTGGCGGCGGCGGCCTACCTGGTCCACCTCGTGGTGCGGGCCGGGGCGCTGCGCGGCCTGCTGCGCTCGCGCACGGTTCAGTACCTGGGGCTCATGTCCTTCTCCCTGTACCTGGTGCACGAGCCGGTCGTGGTCTCGCTGCGGCTGCTGACGCAGCCGATGTCGCCGTGGTGGGTGCTCATCCTAGCGCCGGTGGTCTCGGCGCCGCTGACCTGGATGTTCCAGCGCTACATCGAGGCCCCCAGCCACCGGCTGGCCCGCCGCACCGGGGCTCTGGCCTCGGCGCGCTTCGCCCAGTGGTCCGAGCGCCGTCGCCCCACCCGGTCGGCGGACCACAGCGAGAGGGGCTAG","VRLIELDGLRGLAAVVVLIHHALETVPALAEVGARPGTVPTGTFNRILTQSPLHLLWAGHEAVLIFFVLSGVALTYPVARRHAQGRRFDWVDYAPRRFVRLWLPAAASTTFAVIAMLLVPRSENPALGHWMTVTHPVGLGARQMLMEYLLIPKHAYRNTVLWSLHAEAIFSFVLPLMILGVALCARWRISWLPVVAALAVPVITASPGSGSYLPVFTIGAVMGWAWGHNPAPVPQRPQPWATAQALVCLLLITLAWWPGMESHTAQRLANAVTLAAAAYLVHLVVRAGALRGLLRSRTVQYLGLMSFSLYLVHEPVVVSLRLLTQPMSPWWVLILAPVVSAPLTWMFQRYIEAPSHRLARRTGALASARFAQWSERRRPTRSADHSERG$","Acyltransferase","Membrane, Cytoplasm, Extracellular","","","","","","","","

InterPro
IPR002656
Domain

Acyltransferase 3
PF01757	$\"[3-358]T$	Acyl_transf_3

noIPR
unintegrated

unintegrated
PTHR23028	$\"[53-350]T$	ACETYLTRANSFERASE
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[62-80]?$ $\"[101-121]?$ $\"[159-179]?$ $\"[189-207]?$ $\"[213-228]?$ $\"[238-258]?$ $\"[264-284]?$ $\"[299-321]?$ $\"[327-347]?$	transmembrane_regions

","BeTs to 6 clades of COG1835COG name: Predicted acyltransferasesFunctional Class: IThe phylogenetic pattern of COG1835 is ---------bRh---------Number of proteins in this genome belonging to this COG is","***** IPB012429 (Protein of unknown function DUF1624) with a combined E-value of 1.3e-09. IPB012429A 2-26 IPB012429B 66-76 IPB012429E 303-317","Residues 2-112 are 52% similar to a (ACYLTRANSFERASE TRANSFERASE MEMBRANE O-ANTIGEN ACETYLASE PROBABLE ACETYLTRANSFERASE LIPOPOLYSACCHARIDE 2.3.1.- TRANSMEMBRANE) protein domain (PD274832) which is seen in Q6HHW5_BACHK.","","","Residues 3 to 358 (E_value = 2.2e-16) place ANA_1854 in the Acyl_transf_3 family which is described as Acyltransferase family.","","","","1","","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:04:25 2007","Wed Aug 15 17:04:25 2007","Wed Aug 15 17:04:25 2007","Wed Aug 15 17:01:37 2007","","","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","Wed Aug 15 17:01:37 2007","","Wed Aug 15 17:01:37 2007","","Wed Aug 15 17:01:37 2007","yes","","" "ANA_1856","2006485","2007246","762","5.12","-9.58","26260","ATGGCGGCCAAGCGCACCCGCATGAGCGCCAGCGAGCGGCGCGAGCAGCTCATCGCCGTGGCCCGCGGACTGTTCGCCGAGCGCGGCTTCGACGCCACGAGCGTGGAGGAGGTGGCGGCCCGCGCCCAGGTGTCCAAGCCTGTGGTCTACGAGCACTTCGGCGGCAAGGAGGGCCTGTACGCCGTCGTTGTCGACCGGGAGATCACCACGATCTCGGCCGCGATCTCCTCTGCGATCGCGGACCCGGCCGCGGACGCCACGGCGGCGCCGGAGGCCGACCGACACGCACAGGAAGGATCCGACGCCTCCGGCTCGGCCTCTCGGATCGCCGAGCGGGCCGCGCTGGCCCTGCTGACCTACATCGAGGACTCCCCCGACGGTTTCCGCATCCTCTCGGCGGGCTCGGACCGCGCGGCCGGCACCTACTCGACGCTGCTGGCCGACGTCGCCATCGAGGTCTCCGGGATCCTCGCCTCGCAGTTCGCGGCCCACGACCTCGACCCGCGCACGGCCCCGTTGTACGCCCAGATGCTGGTGGGTATCGTGGCGATGCCGGCTCAGTGGTGGTTGGAGAACCGCTCGATGAGTAAGGAGGAGGTGGCCGCCCACATGGTCAACCTCGCCTGGAACGGCCTGCGCGGCTTGAAGGCCGAGCCCACGCTCCACTCCGGGCCCGTAGGCGACTCCAGGGGCTCCAGCAGCCCCGAGGGCGCTTCGGGGCCGGGGGCCGACTCGCACACCGGGGGCTCCGACGGACCCTGA","MAAKRTRMSASERREQLIAVARGLFAERGFDATSVEEVAARAQVSKPVVYEHFGGKEGLYAVVVDREITTISAAISSAIADPAADATAAPEADRHAQEGSDASGSASRIAERAALALLTYIEDSPDGFRILSAGSDRAAGTYSTLLADVAIEVSGILASQFAAHDLDPRTAPLYAQMLVGIVAMPAQWWLENRSMSKEEVAAHMVNLAWNGLRGLKAEPTLHSGPVGDSRGSSSPEGASGPGADSHTGGSDGP$","Transcriptional regulator, TetR family","Cytoplasm","transcriptional regulator, TetR family domainprotein","transcriptional regulator; TetR family protein","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[17-30]T$ $\"[38-61]T$	HTHTETR
PF00440	$\"[17-63]T$	TetR_N
PS50977	$\"[11-71]T$	HTH_TETR_2
PS01081	$\"[29-59]T$	HTH_TETR_1

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[4-63]T$	no description

","BeTs to 16 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 2.7e-18. IPB001647 17-59***** IPB013573 (Tetracycline transcriptional regulator YcdC-like, C-terminal) with a combined E-value of 1.1e-10. IPB013573B 38-79***** IPB013571 (Tetracycline transcriptional regulator QacR-related, C-terminal) with a combined E-value of 1.4e-07. IPB013571A 11-61***** IPB013572 (Tetracycline transcriptional repressor MAATS-type, C-terminal) with a combined E-value of 4.1e-06. IPB013572A 2-22 IPB013572B 38-60","","","-70% similar to PDB:2HYT Crystal structure of TetR-family transcriptional regulator (YP_049917.1) from Erwinia Cartovora Atroseptica SCRI1043 at 1.64 A resolution (E_value = 7.5E_10);","Residues 17 to 63 (E_value = 2.1e-18) place ANA_1856 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator, TetR family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1857","2007488","2008147","660","5.37","-3.60","23126","ATGGACCCGGAAACCCTCATCATCGCGTTGCGCAAGAACGCAGTCCTGGTGGTCATGCACGTTGTGCTGGGCACCATCATCGGCACTGTCTTCGGCCTGTTGACGCCGGCGCAGTACACCTCCACTGCCAACGCGAACCTGTACGTGGAGAACGGTGAGGCCAACCTCCCCAGCACCTTCAACTATCTGACCTCCGTCATGCCGACGCTGGTGGAGATCGGAACCTCGGAGAGCACCTTCGCGGAGGTCTCCAAGAACACAGGAATCAGCCAGGACGAGCTGCGCAGGTCCGTGTCGGTGACCAGCAAGACCGGCACCACGCTGGTGGAAATCCGGTGCACCAGCACGGATCCCGAACGCGCCCACAGGATCGCCGAGGCCGAGCTGAGCGCCCTGGACTCGGTGGCCCGTGACCTGTCCAGCTCCGGGCAAGCGGGGAACACCACCGCATCCCTCAAGGTGGTCGACTCCCCCACGACCCCCTCCTCCCGCTCGAGCCTGTCGGCCGTGTCCACCGCACTGATCGGGACCGCCATCGGACTGGCCGCCGGCGCCATCATGGCGATCCTGCTGTACTTCCTGAGTCAGAAGAACCCGCAGGACAAGGTCGAGGACCCGCTGCTCATCATTGGGCGTCGTCGCTCTCGGGAAGACGCCTGA","MDPETLIIALRKNAVLVVMHVVLGTIIGTVFGLLTPAQYTSTANANLYVENGEANLPSTFNYLTSVMPTLVEIGTSESTFAEVSKNTGISQDELRRSVSVTSKTGTTLVEIRCTSTDPERAHRIAEAELSALDSVARDLSSSGQAGNTTASLKVVDSPTTPSSRSSLSAVSTALIGTAIGLAAGAIMAILLYFLSQKNPQDKVEDPLLIIGRRRSREDA$","Lipopolysaccharide biosynthesis protein","Membrane, Cytoplasm, Extracellular","possible Etk-like tyrosine kinase involved inEps biosynthesis, putative","hypothetical protein predicted by Glimmer/Critica","lipopolysaccharide biosynthesis protein","","Franco A.V., Liu D., Reeves P.R. The wzz (cld) protein in Escherichia coli: amino acid sequence variation determines O-antigen chain length specificity. J. Bacteriol. 1998. 180(10):2670-2675. PMID: 9573151Morona R., Van Den Bosch L., Daniels C. Evaluation of Wzz/MPA1/MPA2 proteins based on the presence of coiled-coil regions. Microbiology 2000. 146:1-4. PMID: 10658645","","","

InterPro
IPR003856
Domain

Lipopolysaccharide biosynthesis
PF02706	$\"[3-131]T$	Wzz

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[173-193]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 131 (E_value = 0.00032) place ANA_1857 in the Wzz family which is described as Chain length determinant protein.","","Etk-like tyrosine kinase involved in Eps biosynthesis, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1858","2008154","2009524","1371","9.42","6.36","48402","GTGGCCCAGACATGGTCGCAGGCCACCTCCTACCAGGGCTCGCAAGCGCCGGCGGACACTGATCCCGGAACGGGCCGGGAACCGGGGACGACGTGGCGGCGGCTGGAGATGGCGATCGCCGTCGTCCTGCTGGTCTGCGTGGGTGTGCGCCGTGAGCTGACGGCCGCCCTGAGCGTCGGGGACTGCGTCGCGCTCGTCTCGGTCCCCATCACCTGGACGGCCGTGCGCAAGGCGCGCCGCTTCTCGCTGCTGCTCGTGCTGTCCATCCTGGCGGCGGGCACGGCCTACATCATGTCCCTGCTGGCCGAGAGCAGCTTCGTCGTGGAGGCCTGGGCCCGCCGTGTCACCACCTTGAGCCTGCTGGCCGTCCCCTGCGCGGTGGCCGTCTTCGTGTGGGGGGCGCGCCGGCTGGGAACAAGACGCGCGGCCCTGGCAGTCGGCTTCGGCATGTTCCTGGACTCGCTACCCCTGTTGCAGACCAACACCAACCCGTGGAAGTTCGGGGTCGGTGCGGCGGTGACGATCATGGTCCTCAGCCTCGTCGCCGACCGGCGCCGACTGGTGCAGATCGCGGCCCTGCTGGTGCTCAGCGGCGTCTTCCTCGTCTCCGACTCACGCTCCACCCTGGCCTTCCTGGCCATCATCCTGGGCACGGTCATCTGGCAGGCCCTGGCGTCCTGGGCCCGGTGGCACGTGCCCACTCCCCGGCGTCTGGCGGTCTCCCAGATCCTCGTCCTGGCGGTCGTGGGGATCGTGGCGATGGCCGGGGTCGTCATGGCCTCGGAGTCCGGGACCCTGGGCGAGGACGCCCAGAACCGGACCATCGCCCAGTCCTCGAGCTCGGCGGGGCTGCTGCTGTCCGCCCGCCCCGAGCTGGGAGCCTCCTGGGCCCTGTTCCAGAACCGGCCCTGGGGGTACGGCGCCGGCGTCAAGCCCCGTTTCGAGGACCTGTGGGTGGCCAAGCAAGGCATGGCGGCCCTGGGCTACGACCCGGAGAACGGGTACGTCGAGAACTTCATGTTCGGCGGCCGCATCGAGCTGCACTCGGGTCTCATGGACATGTGGGCGGCGGCCTCGATCCCGGGAGGTCTCCTGCTACTGCTCATCGCCGGGATGGCGCTGGCGGCGATGATGCGCGACCTGGGGCGACTCAAGGCCACGCCCTGGCTATTCTTCGCGGCTCTGACCGTGGTGCAGAACGTGTTCGTGGGGCCCTGGACGGTGCTGCCCGCCTACCTGCCGATCGTGCTGGGGGCCGCCGTCCTGCAACCGCCCCTGCGTGAGGCCGCCCAGTTGGGCGCCGACGACGAGCCGGCCGCCCCACCACGGGACGCGTCCTCCGACTCCACGGCGCCCGCCCAGCAGGCGTGA","VAQTWSQATSYQGSQAPADTDPGTGREPGTTWRRLEMAIAVVLLVCVGVRRELTAALSVGDCVALVSVPITWTAVRKARRFSLLLVLSILAAGTAYIMSLLAESSFVVEAWARRVTTLSLLAVPCAVAVFVWGARRLGTRRAALAVGFGMFLDSLPLLQTNTNPWKFGVGAAVTIMVLSLVADRRRLVQIAALLVLSGVFLVSDSRSTLAFLAIILGTVIWQALASWARWHVPTPRRLAVSQILVLAVVGIVAMAGVVMASESGTLGEDAQNRTIAQSSSSAGLLLSARPELGASWALFQNRPWGYGAGVKPRFEDLWVAKQGMAALGYDPENGYVENFMFGGRIELHSGLMDMWAAASIPGGLLLLLIAGMALAAMMRDLGRLKATPWLFFAALTVVQNVFVGPWTVLPAYLPIVLGAAVLQPPLREAAQLGADDEPAAPPRDASSDSTAPAQQA$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[81-101]?$ $\"[115-133]?$ $\"[138-158]?$ $\"[164-182]?$ $\"[187-202]?$ $\"[208-228]?$ $\"[238-258]?$ $\"[357-377]?$ $\"[389-409]?$	transmembrane_regions

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[14-402]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[21-212]T$ $\"[239-429]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF7	$\"[21-212]T$ $\"[239-429]T$	PERMEASE-RELATED
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[77-111]?$ $\"[153-185]?$ $\"[260-280]?$ $\"[290-310]?$ $\"[315-335]?$ $\"[341-363]?$ $\"[378-398]?$ $\"[408-428]?$	transmembrane_regions

","BeTs to 6 clades of COG0477COG name: PermeasesFunctional Class: G,E,RThe phylogenetic pattern of COG0477 is AMTKYQVCEBRHUJGPo-INXNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","Residues 14 to 394 (E_value = 1.3e-23) place ANA_1858.1 in the MFS_1 family which is described as Major Facilitator Superfamily.","","","","1","","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:33:13 2007","Sun Jul 15 23:33:13 2007","Sun Jul 15 23:33:13 2007","Sun Jul 15 23:33:13 2007","","Mon Aug 20 18:21:31 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Mon Aug 20 18:21:31 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Sun Jul 15 23:31:39 2007","Mon Aug 20 18:21:31 2007","","Sun Jul 15 23:31:39 2007","","Sun Jul 15 23:31:39 2007","yes","","" "ANA_1859","2013246","2012203","1044","6.44","-1.88","36189","ATGAACCGGCTGACAATCGCCATCCCCACTTTCCGCCGCCCGCAGGACCTCAAACGGGCCGTCAGTGGGGTCCTGGAGCAGGCCGGTGCGCTGGTCGGCGGCGTGGGTGCCGAGGCCAGGGAACCCGAGAGTGATGCGGCGGACGGGGACGGGGGAGCCGATAGGGGCGTGAGCGATGTCGAGGTCCTCGTTATCGACAACGACGCCCAGGGCTCCGGCCGCGAGGCCGCCCTCGCCGCAGCGGCCGACGCCGGGGTGCCGGTGCGTTCCTCCGCGGAGGGCTCGGAGGAGCCCGGGGGCGTGGGCCTGCGCTACGTCATCGAGGAGAGGCCCGGTGTGGCGGCGGTGCGCAACCGCGCCCTGGACGAGACCGGTGGGCGCGACCTGCTCGTCTTCATCGACGACGACGAGGAGCCCGAGCCCGGCTGGCTCGCCGCCCTCGTGGGGCTGTGGGCCTCGACCGGCTGCCAAGCGGTGGCCGGACCCGTCATCCCCGCCTACGAGGTCGAGCCCGAGGCGTGGGTGCGTCAGGGCGAGTTCTTCGTGCGCAGGACCTGGCCCACTGGCACGGTCCGCCCAGTGGCGGCCTCCAACTGCCTGCTGCTGGACCTGGGTTTCGTGCGCCGGGCCGGGCTGCGCTTCGATGAGGCCTTCGGCGCCACTGGGGGAGAGGACACGCTCTTCACCCGCCGGCTGAGCGCCGCCGGCGGAGTCATCCGCTGGTGCGATGAGGCGCGCGTGCGCGACCACGTGCCGGCCTCGCGCCTCACCCGCCCCTGGATTCTGCGACGTCAGCGCTCCCACGCCGCCACCTCGGTACGTGTGGAGCTGGCGCTGGCCGGTGGCGGGGCACAGCCGGCCATCCGGGCCAAGGCCGCTGCCGGTGGCCTGGTGCGTATCGTCGTCGGCGGCCTGCGAACCGCCGGCGGAACCCTCATCGGCAGTCCTCAGCATGCTGCTAAGGGAGCTCGGCTGTTGGCGCGTGGCCGCGGCATCCTGGCGGCCAGCGTCGGAGGTGGCGTCCACCGCGAGTACGACCACTGA","MNRLTIAIPTFRRPQDLKRAVSGVLEQAGALVGGVGAEAREPESDAADGDGGADRGVSDVEVLVIDNDAQGSGREAALAAAADAGVPVRSSAEGSEEPGGVGLRYVIEERPGVAAVRNRALDETGGRDLLVFIDDDEEPEPGWLAALVGLWASTGCQAVAGPVIPAYEVEPEAWVRQGEFFVRRTWPTGTVRPVAASNCLLLDLGFVRRAGLRFDEAFGATGGEDTLFTRRLSAAGGVIRWCDEARVRDHVPASRLTRPWILRRQRSHAATSVRVELALAGGGAQPAIRAKAAAGGLVRIVVGGLRTAGGTLIGSPQHAAKGARLLARGRGILAASVGGGVHREYDH$","Glycosyl transferase, family 2","Cytoplasm, Extracellular","pssC","glycosyl transferase; family 2","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[5-211]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[103-258]T$	no description

","BeTs to 7 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 211 (E_value = 7.3e-14) place ANA_1859 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","(AF039306) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1860","2014277","2013243","1035","9.54","6.65","36116","ATGCTCACCTACCGCCGCAACAACTACCTCGCGCAGGTGATCCCCGAGCTGCTGGCGCAGGCCGACGACGTCTGTGACGCGCAGACGACGGCAAGCGTGCTCATTGTGGACAACGACCCGCAGGCCGGGGCGAGGGCCGTCGTCGAGGCCGCCCGGGCGGCCCTGGGCGGCGAGCAGCCGGAGGCGGCGGAAGCGTCCGGGGTAGCTGACTCGGACGCGGTGGCGATGTCGCGGCTGGTCTACGTTCACGAGCCCGAGCCGGGCATCGTGGCCGGCCGCAACCGGGCCCTGAGCCAGGCCCACGGCTCTGACGCCCTCGTCTTCATCGACGACGACGAGATCCCCTCACCGGGCTGGCTCAAGGCCCTCGTGAGCACCTGGCGCGCCCAGGGCTGCGCCGCCGTCACCGGCCCCACGCCGCCGACCTTCGAGGTCGACCCCTCGGCGTGGGTCACCGCCTCAGGCGCCTTCGACTCCTGGGAGGCCGCCGACGGCGCCCAGGTCCGCAGCGCCGACACCGGCAACCTGCTCCTGGACCTGGCCGTCGTCGAGGGCCTGGGGCTGCGCTTCGACCCACGCTACGGGCTCACCGGCGGCGAGGACTCCCTGTTCACCCGCCAGCTCACCCGCGCCGGCGGCGTCATCCGATTCGCGGCCGGGGCGGTGGTCACCAAGCGCGTGCCCGCGGCCCGCGCCCGGCGCACCTGGGTGCTGGAGCGCTCCTTGCGCTCGGGCTCGTCCTGGGCCCGGGTGCGCATCGACACAGCCGCGCCCGACGGCGGTGCCTCCGGCAGGCTCGCGCGTCTCAGGCTGCGCCTGGGCTATGGCGCCAAGGGACTGGCCAAGGCCGGAATCGACGGGGCTCGCGCCGGCGTGGCCCGCATCCGCGGTGACGTGCCCGCCCAGGCCCGCTACGAGGTCTCCTCGCGCGGGGGACTGGGCATGGTCGTGGGCGCGCTGGGCGTCCACGTGCGCGAGTACGGACGCCCCCGGCGCCGGAGGAACACAACACCGGCCGGCAGGAGCAAGGCATGA","MLTYRRNNYLAQVIPELLAQADDVCDAQTTASVLIVDNDPQAGARAVVEAARAALGGEQPEAAEASGVADSDAVAMSRLVYVHEPEPGIVAGRNRALSQAHGSDALVFIDDDEIPSPGWLKALVSTWRAQGCAAVTGPTPPTFEVDPSAWVTASGAFDSWEAADGAQVRSADTGNLLLDLAVVEGLGLRFDPRYGLTGGEDSLFTRQLTRAGGVIRFAAGAVVTKRVPAARARRTWVLERSLRSGSSWARVRIDTAAPDGGASGRLARLRLRLGYGAKGLAKAGIDGARAGVARIRGDVPAQARYEVSSRGGLGMVVGALGVHVREYGRPRRRRNTTPAGRSKA$","Glycosyl transferase, family 2","Cytoplasm, Extracellular","glycosyl transferase, putative","glycosyl transferase; family 2","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[1-187]T$	Glycos_transf_2

InterPro
IPR003778
Domain

Allophanate hydrolase subunit 2
SM00797	$\"[151-337]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[1-138]T$	no description

","BeTs to 6 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 187 (E_value = 3.1e-13) place ANA_1860 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.Residues 3 to 187 (E_value = 1.9e-05) place ANA_1860 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","transferase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1861","2014504","2015583","1080","5.82","-4.09","38206","ATGACCTCCACCGCTGACCCCGCCCAGGGCGCCGAGACCCCCGAGGCCGCCGATCCGATCGGCCCCGCCACCGGCGCCCCCGCCCAGGCCGTCGAGATCACCGAGGCCTCCGAGGCTCTCTCCGGCGGCGAGCTGCTCTCGCGCACGGCGGTCATCGTCGTCAGCTACGACTCGGCGAAGCTCCTGGAGCGCACACTGGCGCGCGTGGCCGAGGACTCCCCTGAGGCCCGCATCATCGTCGTCGACAACTACTCCACACCCGCCGCCCGCGACGAACTGGTGGCGCTGGCCTCCTCGCGGGGCTGGGAGGCGGTCCTGCCGGAGACGAACACCGGCTTCGGCGGCGGCATGAACCTGGGTGCGGCCCGGGCCCGCGAGCTCGGAGCTGACCTGCTGGTCCTGCTCAATCCCGACGCCGTCATCGCCCGGGCCGACCTCATCCGCCTGGCGGCCAGGGCGCACGCGGACCGGCTCGCTCTGGTGGCGCCGGTGCTCAAGGACTCCAGTGGCCGCATTGTCTCCGACGGGATCGTCGTGTGCCTGGCCGATGGCTCGATGCGCTCGCGCCGCTCACCGCGCCCGATTCCCCCCGGCGGCACCCAGCCGTGGCTCTCGGGTGCCTGTCTGGCGCTGTCGGCGGACCTGTTCGAGGCCGCCGGCGGCCTGGACGCGCGCTACTTCCTGTACTGGGAGGACGTGGACTTCTCGGCCCGGGTCCTGGCGGCCGGGGGCAGCCTGGCCCTGGTGCGCGACGCCGTGGCCGTCCACGATGAGGGCGGCACCCACTCCGAGGACGACCAGCCCGACCGCGCCAAGTCGGACATCTACTACTACTACAACGTGCGCAACCGGCTGCTGTACGCGGGGCTGCACCTGGATCGGGCCACACAGCGCCGGTGGGTGGCCACGGCGGGCCGGGCCGCCCGCGAGATCGTCCTGCGCGGCGGCCGGCGCCAGCTGCTGAGCACTCGCCGCCCGCTCATCACGGCGGCGCAGGCCACCCGCGACGGGATGAGGCTCCTGCGTGCCGCCCGCCGCGGCGAGCTGCCCGACGTCGATGTCCCCCTCATCCGCGACTGA","MTSTADPAQGAETPEAADPIGPATGAPAQAVEITEASEALSGGELLSRTAVIVVSYDSAKLLERTLARVAEDSPEARIIVVDNYSTPAARDELVALASSRGWEAVLPETNTGFGGGMNLGAARARELGADLLVLLNPDAVIARADLIRLAARAHADRLALVAPVLKDSSGRIVSDGIVVCLADGSMRSRRSPRPIPPGGTQPWLSGACLALSADLFEAAGGLDARYFLYWEDVDFSARVLAAGGSLALVRDAVAVHDEGGTHSEDDQPDRAKSDIYYYYNVRNRLLYAGLHLDRATQRRWVATAGRAAREIVLRGGRRQLLSTRRPLITAAQATRDGMRLLRAARRGELPDVDVPLIRD$","Glycosyl transferase, family 2","Cytoplasm","glycosyltransferase","glycosyl transferase; family 2","glycosyl transferase, family 2","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[50-220]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[50-298]T$	no description

","BeTs to 8 clades of COG1216COG name: Predicted glycosyltransferasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1216 is a-m-kz---dr--cef--s--j----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 50 to 220 (E_value = 1.1e-14) place ANA_1861 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1862","2016627","2015656","972","4.93","-17.68","34163","ATGATCAGGGTAGCGATCAACGGATACGGCAACCTCGGCCGCGGTGTCGAGCAGGCCATCACCAAGAACGCGGACATGGAGGTCGCCGTCGTCTTCACCCGGCGCGACCCGGCCACCGTCACCACCCAGGGGGCGCCCGTCGCCCACGTTGACGACATGGCCGCCTGGGCCGACAAGGTTGATGTCTGCCTGAACTGCGGAGGCTCGGCCACCGACCTGATCGAGCAGACCCCGGCCGCCGCGGCCCTGTTCAACACGGTCGACTCCTTCGACACCCACGCCCGCATCCCCGAGCACTTCGCCGCCGTCGACGCCGCCGCCAAGGCCTCGGGCCACGTCGCCCTGATCTCCGCCGGCTGGGACCCGGGCCTGTTCTCCATGCTGCGGGTCCTGGGCGAGGCCGTCCTGCCCGATGGCGCCACCACCACCTTCTGGGGGCCCGGCGTCTCCCAGGGGCACTCCGACGCCCTGCGCCGCATCGACGGCGTCGTCGACGCCAAGCAGTACACCCGCCCGGTGGAGGCCACCGTCGCCGCCGTTAAGGCCGGTGACGACGTCGAGCTGACCACCCGTTCCATGCACACGCGCGACTGCTACGTGGTGGCCGAGGAGGGCGCCGACCTGGCCCGCATCGAGCGGGAGATCGTGGAGATGCCCAACTACTTCGCCGACTACGACACCACCGTCACCTTCATCACCGCCGAGGAGCTGGCCGCCGAGCACGCCGGGATCCCGCACGGCGGCTCCGTCATCCGCCGTGGGCACACCTCCGAGGGTGTGGCTGAGACCGTGAGCTTCGAGCTCCAGCTCGGCTCCAACCCTGAGTTCACCGGCTCGATCCTGGTCGCCACGGCGCGCGCGGTGGCGAGGCTGGCCGCTCGCGGCGAGACCGGTGCGCGCACCGTTTTCGATGTCACGCTCGCCGACCTGTCCCCGACGAGCCCTGAGGAGCTGCGCGCCCACTACCTGTGA","MIRVAINGYGNLGRGVEQAITKNADMEVAVVFTRRDPATVTTQGAPVAHVDDMAAWADKVDVCLNCGGSATDLIEQTPAAAALFNTVDSFDTHARIPEHFAAVDAAAKASGHVALISAGWDPGLFSMLRVLGEAVLPDGATTTFWGPGVSQGHSDALRRIDGVVDAKQYTRPVEATVAAVKAGDDVELTTRSMHTRDCYVVAEEGADLARIEREIVEMPNYFADYDTTVTFITAEELAAEHAGIPHGGSVIRRGHTSEGVAETVSFELQLGSNPEFTGSILVATARAVARLAARGETGARTVFDVTLADLSPTSPEELRAHYL$","Diaminopimelate dehydrogenase","Cytoplasm","diaminopimelate dehydrogenase","diaminopimelate dehydrogenase ","diaminopimelate dehydrogenase","","Scapin G., Reddy S.G., Blanchard J.S. Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum. Biochemistry 1996. 35(42):13540-13551. PMID: 8885833","","","

InterPro
IPR000173
Family

Glyceraldehyde 3-phosphate dehydrogenase
PF00044	$\"[2-28]T$	Gp_dh_N

InterPro
IPR010190
Family

Diaminopimelate dehydrogenase
TIGR01921	$\"[1-323]T$	DAP-DH: diaminopimelate dehydrogenase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[1-323]T$	no description

","BeTs to 15 clades of COG0057COG name: Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0057 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-60% similar to PDB:1DAP C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH NADP+ (E_value = 1.4E_70);-60% similar to PDB:1F06 THREE DIMENSIONAL STRUCTURE OF THE TERNARY COMPLEX OF CORYNEBACTERIUM GLUTAMICUM DIAMINOPIMELATE DEHYDROGENASE NADPH-L-2-AMINO-6-METHYLENE-PIMELATE (E_value = 1.4E_70);-60% similar to PDB:2DAP C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH DAP (E_value = 1.4E_70);-60% similar to PDB:3DAP C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH NADP+ AND THE INHIBITOR 5S-ISOXAZOLINE (E_value = 1.4E_70);","Residues 2 to 120 (E_value = 0.00054) place ANA_1862 in the DapB_N family which is described as Dihydrodipicolinate reductase, N-terminus.Residues 2 to 28 (E_value = 1.6e-07) place ANA_1862 in the Gp_dh_N family which is described as Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain.","","dehydrogenase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1863","2017008","2016760","249","4.65","-4.86","8616","ATGGGCATGTCAGTGAACACCTCCGTCAGCCTCGATGACCACTTCGTCGGATTCATCGCGAGCCAAGTCGGGTCCGGACGGTACCGGTCCGCGAGCGAGGTCATCCGCGCCGGCCTGTGCCTTCTGGAGAACCAGGAGACAGAGATGTCGGCGCTGCGCGAGGCACTCGCATCCGGTGAGGCGAGCGGACAGGCGGAGCCCTTCGACTTCGACGCCTTCATCGCCGCCAAGGCGGCAAGGACGTCGTGA","MGMSVNTSVSLDDHFVGFIASQVGSGRYRSASEVIRAGLCLLENQETEMSALREALASGEASGQAEPFDFDAFIAAKAARTS$","Addiction module antidote protein, CC2985 family","Cytoplasm, Periplasm","putative addiction module antidote protein,CC2985 family","K07746 hypothetical protein","putative addiction module antidote protein, CC2985 family","","","","","

InterPro
IPR005360
Family

Putative addiction module antidote protein, CC2985
PF03693	$\"[3-80]T$	RHH_2
TIGR02606	$\"[6-75]T$	antidote_CC2985: putative addiction module

InterPro
IPR011570
Family

Protein of unknown function UPF0156
PD060431	$\"[3-66]T$	Q6ADK3_BBBBB_Q6ADK3;

","BeTs to 3 clades of COG3609COG name: Predicted transcriptional regulators containing the CopG/Arc/MetJ DNA-binding domainFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG3609 is aompkz----r-b-e---s--j----Number of proteins in this genome belonging to this COG is 1","***** IPB005360 (Protein of unknown function UPF0156) with a combined E-value of 1.3e-24. IPB005360A 3-22 IPB005360B 26-63","","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 80 (E_value = 5.6e-42) place ANA_1863 in the RHH_2 family which is described as Uncharacterised protein family (UPF0156).","","addiction module antidote protein, CC2985 family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1864","2020198","2017145","3054","6.24","-7.39","106276","GTGAAGCTCCCCCGCCGACTCCTGAGCGGCCTGCTGGCCGCGGCTCTCGTTCCCCTCGGTGCCGTCACGCTCGCTCCGGCCTCCCCTGCCACCGCGGACCCGGCCCCTGCCCCAGCCGGCGCCGCCGGTACTCCCAGCACCGTCTCCGCCGATGCCCTGCCCACCGCCCAGATCAACGGCATTGTCTGGGACCAGGTTGTGGTCGGGGACATCGTCTACGCTGTCGGGAAGTTCTCCGCGGTCAGGCCGGCAGGATCGCCTGCCGGCCAGAACGAGTCGCCGCGCAGCAACGCGATGGCCTACAACATCAACACCGGCGAGATTCTCGACTGGGCGCCCACCACCAACGGCACCATCAACACCATTGCCGCCTCCGCTGACGGGCAGACCCTCTATCTGGGCGGGGAGTTCACCGCGCTGAACAACCAGACCGCCTGGCGCGTCGGAGCGGTTAGGACCGCTGATGGTCAGCGCGCTCCGCTGGGCGCCTCGGCCAACGGCAGCGTCAAGGCGCTGAGCGTCTCCCCCGATGGTCAGACTCTCTACATCGGTGGGGCCTTCACTCAGATCAACTCCTCGGCCCGTCAGCGCGTCGCAGCGCTCAACCTGGGTAGCCAGCAGCTGACCAGCTTCGCGCCGAAGATCGACAACTACTACGTGCGCAGCATCGTCGAGGCCGTTGACGGCTCGGCCGTGGCCATCGGTGGTGCCTTCGAGTCCGTCGGGGGCAGCGACAAGCCCGGTCACGGGATCGCCATCTTCGAGAAGGACGGCAGCCTGCGCAAGAACAACGCCTCCAGCGTGGTGCGTGGAGCCGGCGCCGAGGCGTCCGTCATGAGCGTCAAGGCTGACGAGCACGGTCTGTACGCGTCGAGCTACTCCCGGCTGGGCACCTTCGAAGGCGTCATGCGCCTGAACTGGGTCACCGGGGACATCGACTACATGGCCGAATGCCACGGCGACTCCTACGACGTCCTGCCCGCCGGTGACGTCGTCTATGCCGCCAGCCACTCCCACGACTGCTCCAACATCGGTGGCTTCCCGGACGTCTCCTACCACTACCACAACGCGATGGCCTACACGAACGCCGCCACCGGAACGGTGGGGGAGAACAAGGTAGCGGGCTACAAGAACTACGCAGGCCAGAACGCCACCACGAACCTCAACTTCTATCCCGACTTCACGCCGGGCAAGATCTCCGGCGCCATCCAGGCGACCTGGACCGTTGAGGGCAACGACAAGTACGTCGTCTACGGCGGCGAGTTCCTGGCCGTCAATGGCACCGCCCAGCAGGGATTGGTGCGCTTCGCCCGCCGTGACATCGCCCCGAACAAGCAGGGACCCATGGACAAGGGCGGTGCCTTCAAGGTCTCCGGCACCTCGCCGCGCGCCGGGGTCGTCTCCCTGTCCTTCAAGGCCAACTGGGACCGGGACGACAAGACCCTGACCTACAACGTCTACCGGGACGACATGAACGCCCAGCCGGTCACCAGTCAGACGGCGACCGCCGGCTTCTGGGAGCGCCCCGACCTCAGCGCCACCGACGTCGTCGAGCCCGGAAGCACGCACCGCTACCGGGTCCAGGTGACCGACCAGTGGGGGGCCTCCACGGTCTCGGACTGGGTGACGGTCAAGGCCGCTGAGGGTCAGGGCCTGAGCAAGTACGGCGCCCGGGTGCTGGCCGACGGCGCCGCCCACTACTGGTCCTTCGACGAGACCAGCGGTGACAAGGCCGAGGACTTCGTGGCCCAGCGCAACCTGACGATTCGTGGCAAGGCCTACAAGCGCGGAAGCGGGTCCGTCCTGGGCTCGGGCGCCTCGCTCGGCCTGACCTCGGACGCCACGAACAAGTCGCACGCCGCCACGCGCGTCGCCTCCCAGGCCCCCACCACCTTCTCCATGGAGGCGTGGGTCCGCACGACCTCGACCTCGGGCGGGGAGATCATGGGCTACGGCTCCTCAGCGGCCAACCAGTCGTGGAACCGTGACCGCATGGTGTACATGCGCAATGACGGTACGCTCAGCTTCATGCTCTACCCGGGCAAGCTGACCACGATCACCACTCCCAAGAGCTACAACGACGGGCAGTGGCACCACATCGTGGCCTCCCTGAGCCCGACCGCCGGTGCCATGCTCTACGTGGACGGCAATCTCGCCGCCTTCGACGCCGCCATGACCGCGGGTGAGAGTTACTCCGGTTACTGGCGCATCGGTGGGGACGCCCTCGGCGGTGTCAACGGTCAGCCCTCCAACACCAACATCCAGGCCGACATCGACGAGGCCGCCGTCTACAGCACGCCGCTGTCGGCGCGGCAGATCGCCGAGCACTACACCGCCGCCACCGGCAAGCAGGTCGAGCCGGACAAGGGTGATGACAAGGGCAAGGACAACGCCGGAAAGGACAAGGGCAAGCAGCCCGAGGGCAAGGCCCTGCTGGACGACTCCTTCGAGCGCAGCGTGAACGGCGGCTGGGGCAAGGCCCAGGCCGGCGGTGCCTGGAAGACCACCTGGAACGCCGCGGCATTCTCCGTCGATGGTACCAGCGGCCGGATTGCCATGGCCGGTCCGCGCTCCTCGGCCTCCATCATCTCCGACCCGATCAAGTCCACCTCCACCGACGCCGTCGTGGACTTCTCCCTGGACGCGGTGCCCACTGGTAACGGTGCCTTCATCTCCTACGCCGCCCGCACGACCAAGGCCGGTCAGTACCAGGCCACGGTCCGCATCGGCAGCGCCGGCAACCCGGTGGTCACGGTCTCGCGCGTGGTCAAGGGCAAGGAGACCTCCCTGGGCTCCTACGTCATGAAGCAGCCCTACACGGCCGGTCAGCCGCTCCACCTGCGCATGGTGGTTGACGGCGCGGAGTCGACCAACATCCAGGCCAAGCTCTGGGCCGGAGACGCCGAGCCCGCCGAGTGGGGGATCGAGGCCGTTGACAACGACAAGACCCTCAACGAGGCCGGAACCGTGGGGCTGACCACCTACATGTCCGGCTCGGCCGGACCGGAGACCGTCACCCTGTCGGTCGACAAGGTCACCATCAAGCAGCACTGA","VKLPRRLLSGLLAAALVPLGAVTLAPASPATADPAPAPAGAAGTPSTVSADALPTAQINGIVWDQVVVGDIVYAVGKFSAVRPAGSPAGQNESPRSNAMAYNINTGEILDWAPTTNGTINTIAASADGQTLYLGGEFTALNNQTAWRVGAVRTADGQRAPLGASANGSVKALSVSPDGQTLYIGGAFTQINSSARQRVAALNLGSQQLTSFAPKIDNYYVRSIVEAVDGSAVAIGGAFESVGGSDKPGHGIAIFEKDGSLRKNNASSVVRGAGAEASVMSVKADEHGLYASSYSRLGTFEGVMRLNWVTGDIDYMAECHGDSYDVLPAGDVVYAASHSHDCSNIGGFPDVSYHYHNAMAYTNAATGTVGENKVAGYKNYAGQNATTNLNFYPDFTPGKISGAIQATWTVEGNDKYVVYGGEFLAVNGTAQQGLVRFARRDIAPNKQGPMDKGGAFKVSGTSPRAGVVSLSFKANWDRDDKTLTYNVYRDDMNAQPVTSQTATAGFWERPDLSATDVVEPGSTHRYRVQVTDQWGASTVSDWVTVKAAEGQGLSKYGARVLADGAAHYWSFDETSGDKAEDFVAQRNLTIRGKAYKRGSGSVLGSGASLGLTSDATNKSHAATRVASQAPTTFSMEAWVRTTSTSGGEIMGYGSSAANQSWNRDRMVYMRNDGTLSFMLYPGKLTTITTPKSYNDGQWHHIVASLSPTAGAMLYVDGNLAAFDAAMTAGESYSGYWRIGGDALGGVNGQPSNTNIQADIDEAAVYSTPLSARQIAEHYTAATGKQVEPDKGDDKGKDNAGKDKGKQPEGKALLDDSFERSVNGGWGKAQAGGAWKTTWNAAAFSVDGTSGRIAMAGPRSSASIISDPIKSTSTDAVVDFSLDAVPTGNGAFISYAARTTKAGQYQATVRIGSAGNPVVTVSRVVKGKETSLGSYVMKQPYTAGQPLHLRMVVDGAESTNIQAKLWAGDAEPAEWGIEAVDNDKTLNEAGTVGLTTYMSGSAGPETVTLSVDKVTIKQH$","Hypothetical protein","Extracellular","hypothetical protein","peptidase S26B; signal peptidase","Laminin G","","Sasaki T., Fassler R., Hohenester E. Laminin: the crux of basement membrane assembly. J. Cell Biol. 2004. 164(7):959-963. PMID: 15037599Tisi D., Talts J.F., Timpl R., Hohenester E. Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin. EMBO J. 2000. 19(7):1432-1440. PMID: 10747011Ichikawa N., Kasai S., Suzuki N., Nishi N., Oishi S., Fujii N., Kadoya Y., Hatori K., Mizuno Y., Nomizu M., Arikawa-hirasawa E. Identification of Neurite Outgrowth Active Sites on the Laminin alpha4 Chain G Domain. Biochemistry 2005. 44(15):5755-5762. PMID: 15823034Beckmann G., Hanke J., Bork P., Reich J.G. Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins. J. Mol. Biol. 1998. 275(5):725-730. PMID: 9480764","","","

InterPro
IPR001791
Domain

Laminin G
SM00282	$\"[630-766]T$	LamG

InterPro
IPR012680
Domain

Laminin G, subdomain 2
PF02210	$\"[638-716]T$	Laminin_G_2

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 638 to 716 (E_value = 1.3e-06) place ANA_1864 in the Laminin_G_2 family which is described as Laminin G domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1865","2021476","2020655","822","5.42","-2.83","26581","ATGAGGCCTGTCGGGTCAGCGGATCGCCGCGGGGTATCCCCTGAATCGTCCGGTTCTATCGTCAGCGGGGGTGTGCTTCCCAACTCAGTGGTCGCTGAGGGTGACGCAGTGATCGGCGGAGGTCGTACGCTTCGGCACGTGTCACGAACTCGAATGCTGATCCTCCCCACTGTCCTGGTGCTGGGCCTAGGGCTGGCCGCCTGCGGAGGCGGAAAGTCTCAGAGCGCTGCCAGTCCCTCCGCCTCCGCCGCAGCCTCTGCCAGCGGCTCGGCCTCCGCTCAGGCCGCCCCCTCGAATGTCGCCACACCGACGGTCCAGACCGCGAAGCCGACGGTGGCGCCTGCGTCCCCCTCGGGTGACGTCTCGACCCCGGACGCCTCCTCGATCGACCCCAAGGCCGTTGAGACCGGTGACCTGTCGAAGGATGAGTACCCCGAGGTGGGCCTGGACAAGTCTGTCCGCGTTGACGGGGACCTGGTGATCTCCCTGGGGCAGATGCAGGCGAAGGACTTCGCAAGCGCTCCCGGCGAAGTGGGAGGCGCTGGTGTCCTGATCCCGGTGACGGTGACCAACAGGTCCAGTCAGGAGCTGCCACTGGCCAGCGTGCTGTCCACCACCGTCAACTACGGCGAGGGTGCTGGCACTCCTGCCTCCGAGATCGTCTCGGCCTCGGATGCGGTGCCGGCCAAGCTCGCCGCCGGTGAGACGGTGACTGTGAATCGAGCCTTCGTCATCCCGGCGGATGGGCGAGGGAATGTCAAGGTCGTCGTGGACCTGGGGGCGGGCCGTGGGGCCGCCACCTTCCGGGGGTCTGCCGGCTGA","MRPVGSADRRGVSPESSGSIVSGGVLPNSVVAEGDAVIGGGRTLRHVSRTRMLILPTVLVLGLGLAACGGGKSQSAASPSASAAASASGSASAQAAPSNVATPTVQTAKPTVAPASPSGDVSTPDASSIDPKAVETGDLSKDEYPEVGLDKSVRVDGDLVISLGQMQAKDFASAPGEVGGAGVLIPVTVTNRSSQELPLASVLSTTVNYGEGAGTPASEIVSASDAVPAKLAAGETVTVNRAFVIPADGRGNVKVVVDLGAGRGAATFRGSAG$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[52-70]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[184-346]T$	Glycos_transf_1

InterPro
IPR015393
Domain

Protein of unknown function DUF1972
PF09314	$\"[5-180]T$	DUF1972

noIPR
unintegrated

unintegrated
PTHR12526	$\"[7-366]T$	GLYCOSYLTRANSFERASE
PTHR12526:SF3	$\"[7-366]T$	GLYCOSYLTRANSFERASE

","BeTs to 7 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 180 (E_value = 2.3e-14) place ANA_1869 in the DUF1972 family which is described as Domain of unknown function (DUF1972).Residues 184 to 346 (E_value = 0.0009) place ANA_1869 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1871","2024850","2026025","1176","6.64","-1.86","41192","GTGAGCCGGGGCGGGGCGGCCGGCGCCCGCACCGGTGCCGTCCGAGTCCTCGTGGCCCACCCCTCCCCCGACCTGTACGGCTCGGACTGGCAGCTGGTGGAGACCATTCACGGACTCATCGAGACCGGCCACGAGGTCCTCGTGGCCCTGCCGCAGGACGGCCCCCTGGTAGCGGTGCTGCGCGACGCCGGTGCCCGCGTGGCCGTCATGCCCTTCACGGTCCTGCGCAAGGCCCTGCTGAGCCCCACCGGCCTGGCGAAGCTGTCCGCTCAGGCCGCCCCCGAGGTCGCCCGCCTGCGGTCGGTCATCCGTGCCAGCCGCGCCGACGTGGTTCTCAGCAATACGGTGACGATCCCCTGGTGGCCGGTGGCCGCGAGCGCGGCCGGCGTGCCGGTACTGGCCCACGTGCATGAGGCCGAGGACACCCAGCGCCGGATCATCCGCACCGGGCTCAACGCCCCGCTGCTGGCGGCCTCCCGGATCGTGGCGAACTCCGGAGCGGCCCGCGACGCGCTCCTGGATGCTCAGCCGCGACTGGCCTCGCGCACGGAGGTGGTCCACAACGGGGTCGCCGGGCCGGACCGGCCCCTGGAGCCCCTGCGCCCCAGGCAAGCCGGGGACTCCTTCCGTATCGCCATGGTGGGGCGCCTGTCCCCGCGCAAGGGCGTGGACGTGGCTCTCGACGCCGTCGGGCTGCTGCGCCGCTCGGGGGTGGATGCCTCCTTAAGCGTGTGCGGCTCGGTCTTCCCGGGCTACGAGTGGTACGAGGCCGAGCTGCGTGAGCGCGCCGGTCAGGAGGACCTGGAGGGGCACGTCGAGCTGCTGGGTTACGTGCACCCCACCTGGCCGGTGCTGGAGGCCGCCGACGCCGTTGTCGTGCCCTCCCGGGCCGAGCCCTTCGGGAACACAGCCGTCGAGGCGATGCACGCGGCCCGGCCGCTGGTGGCCTCCCGGGTTCAGGGCCTGGCCGAGGTCGTCACCGACTCGGTGACTGGTCTGCTCGTGCCCGCTGACGACGCGCAGGCCCTGGCCGATGCCCTCGGCTCCCTGGCGGCCAACCCGGCCCTGGCGGCCCGGCTCGCCGAGCAGGGTGAGCGCGAGGCCGCCGAGCGCTTCTCCGTGGCCGGGTACCGCGCCACGATGACGCGGATCATCGACGAGTTCGTCAGGCGCTGA","VSRGGAAGARTGAVRVLVAHPSPDLYGSDWQLVETIHGLIETGHEVLVALPQDGPLVAVLRDAGARVAVMPFTVLRKALLSPTGLAKLSAQAAPEVARLRSVIRASRADVVLSNTVTIPWWPVAASAAGVPVLAHVHEAEDTQRRIIRTGLNAPLLAASRIVANSGAARDALLDAQPRLASRTEVVHNGVAGPDRPLEPLRPRQAGDSFRIAMVGRLSPRKGVDVALDAVGLLRRSGVDASLSVCGSVFPGYEWYEAELRERAGQEDLEGHVELLGYVHPTWPVLEAADAVVVPSRAEPFGNTAVEAMHAARPLVASRVQGLAEVVTDSVTGLLVPADDAQALADALGSLAANPALAARLAEQGEREAAERFSVAGYRATMTRIIDEFVRR$","Glycosyl transferase, group 1","Cytoplasm","glycosyltransferase, putative","glycosyl transferase; group 1 family protein","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[195-367]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[15-390]T$	GLYCOSYLTRANSFERASE

","BeTs to 21 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","***** IPB001296 (Glycosyl transferase, group 1) with a combined E-value of 8.3e-11. IPB001296B 294-326***** IPB013534 (Starch synthase catalytic region) with a combined E-value of 1.1e-10. IPB013534F 286-326","","","No significant hits to the PDB database (E-value < E-10).","Residues 195 to 367 (E_value = 1.5e-39) place ANA_1871 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1872","2026889","2026113","777","6.45","-2.94","28989","GTGTGGAGCACCGACGAGCACTTCGGCCCCCGCATGGATGAGCTGTGGCGCTTTGAAGGGGGGAGTTCTGTATCGCGCCTGACCTCCCGGGCGCTCCTGCCCGTGGCCCGCTACCGTCAGCCCAAGGGGGTTCGGATCACCGCCGACCTGCGCCGCCGCCACCTGTGGCAGATCCACTCCCACGGCCTGCCCATCACCTGGGAGGACCCCGCGTGGAGGGGGAGCGCCCAGGAGGGGGCGGGGTCCACCGGGCCGCGCCCCTGGACCGAGCGGCTGCGCGAGCTCACCCCCGTCGATGAGATCGCCGACGAGGTCCGCTCCCTCTACGACGCCCACCTGCGGGGACGCCCTTACGTCGGCATCCAGGTGCGCACCCACGCGGTCTCCCACGCCAAGACCATCGAGTCCTCCCCGGTGGAGTGGTTCGCCAACCGGATGCGCCAGATCCGCGCCGACCACCCCGACGTCCCCTTCTTCCTGTCCTGCGACACTCCCGAGGCCCAGGAGCAGCTGGCCGGTGAGTTCGACGGCTGCGTCTTCCTGACCGACAAGGGCGGGTACAACACCGTCAAAGGTGTGCGCTCGGGCCTGGTCGACCTCTATCTGCTGGCCAGCTCCCAGCACCTCATTGGGGCCTCCTTCTCCAGCTTCGTGGAGATGGCCGTCTTCCTGTGTAACGGCGTTGTCCCCTTCGAGCGACCCGACCAGCCCCTTGACGGCGAGTTCAGCCTCTCCCTGGGGCTGGCCGAGGACCCGCTGCGCCCCGCCCAGCGTTGA","VWSTDEHFGPRMDELWRFEGGSSVSRLTSRALLPVARYRQPKGVRITADLRRRHLWQIHSHGLPITWEDPAWRGSAQEGAGSTGPRPWTERLRELTPVDEIADEVRSLYDAHLRGRPYVGIQVRTHAVSHAKTIESSPVEWFANRMRQIRADHPDVPFFLSCDTPEAQEQLAGEFDGCVFLTDKGGYNTVKGVRSGLVDLYLLASSQHLIGASFSSFVEMAVFLCNGVVPFERPDQPLDGEFSLSLGLAEDPLRPAQR$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1873","2027878","2027144","735","9.71","10.06","26359","ATGAGCTCCCCCGCTGGTTCCCCCACCATCGCCGAGAACATCAGGGCCCTGTCCCGGGCTCAGAAGTCCAAGGCCGGTGCCCCCCTCTACTCCCGCATCATCAACCGCCCCGCGGGCCGGGTCCTGGCCGCGATCGCCCACCGGCTGGGCGCGACCCCGGACCAGGTGACGGTCCTGTCGGCACTGTGCACCTACAGCGGTATCGCCCTCATCGCCCTGTGGCGTCCCACAGTCGTGTCCGCCGTCGCCACCGCCCTGCTGCTCATGTTCGGATACGCCCTCGACGCCGCTGACGGGCAGCTGGCGAGATTACGCAACGGTGGTTCCAAAGCCGGTGAATGGCTTGATCACGTCGCCGACGTTATCAAGCTCTCGACAATTCACGGGGCCATTGCGATCTCACTGTTCCGTTTTGCAGAACTACCTCCCTCGGTTCTGCTTATTCCGCTGGCTTTCGGAGCGGTTCAGAATATTCACTTCTTCAGTTACATCCTGACGTATCAGCTGCGTTATCACGGTGGAACGCCTTTGGCTAAGGATGAGTCCCGCCCCGGCATTCTCAAGTCGGTCCTGTCGGCTCCCACGGACTACGGGCTCATGTGCTTCGTGCTCATGACCCGCTTCGCGCCCACGGTCTTCCTGTGGGTGTACGGCATCATGCTCCTGGGCTACGCGGGCTACGTGGCGCTGGCCCTGCCCAAGTGGTACCGAGACCTGCGTAACGACCTCCAGTAG","MSSPAGSPTIAENIRALSRAQKSKAGAPLYSRIINRPAGRVLAAIAHRLGATPDQVTVLSALCTYSGIALIALWRPTVVSAVATALLLMFGYALDAADGQLARLRNGGSKAGEWLDHVADVIKLSTIHGAIAISLFRFAELPPSVLLIPLAFGAVQNIHFFSYILTYQLRYHGGTPLAKDESRPGILKSVLSAPTDYGLMCFVLMTRFAPTVFLWVYGIMLLGYAGYVALALPKWYRDLRNDLQ$","CDP-alcohol phosphatidyltransferase","Cytoplasm, Membrane","putative transferase","hypothetical protein predicted by Glimmer/Critica","CDP-alcohol phosphatidyltransferase","","Nikawa J., Kodaki T., Yamashita S. Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae. J. Biol. Chem. 1987. 262(10):4876-4881. PMID: 3031032Hjelmstad R.H., Bell R.M. sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products. J. Biol. Chem. 1991. 266(8):5094-5134. PMID: 1848238","","","

InterPro
IPR000462
Family

CDP-alcohol phosphatidyltransferase
PF01066	$\"[86-235]T$	CDP-OH_P_transf
PS00379	$\"[98-120]?$	CDP_ALCOHOL_P_TRANSF

noIPR
unintegrated

unintegrated
tmhmm	$\"[72-94]?$ $\"[145-165]?$ $\"[185-207]?$ $\"[213-233]?$	transmembrane_regions

","BeTs to 10 clades of COG0558COG name: Phosphatidylglycerophosphate synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0558 is aompkzyqv-rlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 4","***** IPB000462 (CDP-alcohol phosphatidyltransferase) with a combined E-value of 1.2e-10. IPB000462 84-131","","","No significant hits to the PDB database (E-value < E-10).","Residues 86 to 235 (E_value = 0.00034) place ANA_1873 in the CDP-OH_P_transf family which is described as CDP-alcohol phosphatidyltransferase.","","transferase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1874","2029340","2028048","1293","10.61","18.77","45516","GTGGGAACCACAGCCGTGGCCAAGGTGGTGGTCATGGGGGTCTCGGGCGTCTTCGGCCTGGTCAACACCAGTCTCATCATTCGACACTTTGGGGCCGACGCCTTCGCTCAGTACGGTCTGCTGGCCACCTTCCCCACCCTCATGCCCTTCACCGACCTGGGCATCGGCGCGGTCATCCTCAACACGGTGGCGAGCTCGACCGACCCGGCCCACGACTCGACCGTGCGGCGCACGATCACCACCGCCGTCCGCGTGCTGCTCGGCTCCGCCCTGGTCATCAGCACCGTCGGCATCGTCATCCTGTTGCTGGGCGCCTGGCCCGGGCTGCTGGGGGGCAAGCTCATGGAGGGCGGCGGACTCACTGCCACCGTCTGCCTCATCATCTACGCCGCGGCTCTGCCGCTGTCCGTGGGACAGCGGGTCATCATCGGCCTGGGGCGCTCCACCACCCAGGTCATCAGCCAGGGGGTCGTCTCCCCGGCCATGTCCTGCTTCCTGCTGCTGGCCATCGTCACCGGCCTGGGGCGCGGCAACGCCGTGTCCATCTACTCCTACATCGCCAACGCCCTGGTCTCGGTCATCTGCATCGTCGTCGCCTGGCGTGCCACCCGCCCCCTGTTCAAGGGTGCCTTGAGGGACGTACCGCGGCTGCGCAGCGTGCGCGGCGTGCGCATCGTCAACACCGCGGGCCCCCAGCTGCTGCAGTCCCTGGCCATCCCGATCGCCTTCCAGACTGACCGCCTCCTCCTGTCCCACCTGGGGCAGTCCCAGGCCCTGGCCGAGTACAACCTGGCCAACAACCTGTTCAACATGCTCACCCAGACCGTCATGGCGGCCGGCGTGGCCATGTGGCCCATGTTCGCCAGGGCCCGGGCCGACAAGCGCATCGAGAGCCCCTTCAAGCCGGCCATCGCCTTCAGTGGGGGCGGCTTCCTCCTGGCTCTCACCCTCGTCGCCATCACGCCCTGGGCCGCTCGGGTCATGTCTCACGGCAAGATCGTCCTGCCGGCCGCGCTCGTGTGGGCCTTCGCCGCCTACGTCGCCGTCGAGGCCGGCAAGCAGCCGCTGGGCATGTACATGACCGATCCGCGCGGCCTGCAGTTCCAGGTCGTCCCGGTGCTCATCCTGGTGCCGATGAATCTCGCCATCTCCTGGGTCCTCATTGGGCCCTTCGACGCCGCCGGGCCTATCCTGGGCTCGGTGATCTCGGTGGTCCTGTGCCAGATCCTCCCGTATGCCTGGTGGGTGCGCCGGGACGTGGCCAGGCGCCGTCGAGAGCTGGCCCAGCAGTGA","VGTTAVAKVVVMGVSGVFGLVNTSLIIRHFGADAFAQYGLLATFPTLMPFTDLGIGAVILNTVASSTDPAHDSTVRRTITTAVRVLLGSALVISTVGIVILLLGAWPGLLGGKLMEGGGLTATVCLIIYAAALPLSVGQRVIIGLGRSTTQVISQGVVSPAMSCFLLLAIVTGLGRGNAVSIYSYIANALVSVICIVVAWRATRPLFKGALRDVPRLRSVRGVRIVNTAGPQLLQSLAIPIAFQTDRLLLSHLGQSQALAEYNLANNLFNMLTQTVMAAGVAMWPMFARARADKRIESPFKPAIAFSGGGFLLALTLVAITPWAARVMSHGKIVLPAALVWAFAAYVAVEAGKQPLGMYMTDPRGLQFQVVPVLILVPMNLAISWVLIGPFDAAGPILGSVISVVLCQILPYAWWVRRDVARRRRELAQQ$","Polysaccharide biosynthesis protein","Membrane, Cytoplasm","Polysaccharide biosynthesis protein domainprotein","hypothetical protein","polysaccharide biosynthesis protein","","Becker A., Kleickmann A., Kuster H., Keller M., Arnold W., Puhler A. Analysis of the Rhizobium meliloti genes exoU, exoV, exoW, exoT, and exoI involved in exopolysaccharide biosynthesis and nodule invasion: exoU and exoW probably encode glucosyltransferases. Mol. Plant Microbe Interact. 1993. 6(6):735-744. PMID: 8118055Yao Z., Valvano M.A. Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a. J. Bacteriol. 1994. 176(13):4133-4143. PMID: 7517390Popham D.L., Stragier P. Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis. J. Bacteriol. 1991. 173(24):7942-7949. PMID: 1744050","","","

InterPro
IPR002797
Family

Polysaccharide biosynthesis protein
PF01943	$\"[5-291]T$	Polysacc_synt

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[9-27]?$ $\"[46-64]?$ $\"[85-105]?$ $\"[119-137]?$ $\"[158-176]?$ $\"[182-202]?$ $\"[223-243]?$ $\"[268-288]?$ $\"[303-323]?$ $\"[329-349]?$ $\"[370-390]?$ $\"[396-416]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 88 to 374 (E_value = 1.3e-05) place ANA_1874 in the Polysacc_synt family which is described as Polysaccharide biosynthesis protein.","","biosynthesis protein domain protein","","1","","","Tue Aug 7 15:20:47 2007","","Tue Aug 7 15:20:47 2007","","","Tue Aug 7 15:20:47 2007","Tue Aug 7 15:20:47 2007","Tue Aug 7 15:20:47 2007","","","Tue Aug 7 15:20:47 2007","","","Tue Aug 7 15:20:47 2007","","","","Tue Aug 7 15:20:47 2007","Tue Aug 7 15:20:47 2007","","","","","yes","","" "ANA_1876","2030026","2031483","1458","11.01","22.15","52233","TTGTCTAGTTCGACCCTGACACTGCCCCAGCGCGAGCAGCACCGGCGTCCCTCGACAGCAGCAGCAGCCGACGCCACCTCCCCCACCGCTCCGCGCAGTCCTTGGGCACGCACGCGCCATGACCTCGTCATCTGGCTCGTCCTGTCCGACCTCTTCGCCGTCGCCGTCCCCTTCTGGCTCGCCCTCCTGGGCGGCCACCTGCCACTGGTCTGGTCCGCGACCACCGTGGGCATCACGATGGTGCTCATCGCCTGGTTCCTGGGAGCGCTCGGTATCGACGCCGTCGAGCAGGCCGGCCCCGGTACGGGCCGCTTCGTCGCCGCGGCCGCCGTGAGCCTCCCAGTGGCCCTGCTGCTGGCCGACCTGTCCGGAGTCGCCCGAACCACCCTGCTGGCCACTCTGGCGGCCCAGCTCCTCCTGGCCGTCACCGGACGCTCCATCGAGGCCGGGTGGCTGCGCCGCCGCCGCCTCGAGGGGCACGCCCTGCGTCGCACCCTCATCGTCATGGGCTCGGGTTCCCAGCCCATGCTCACCCAGCTGCGCCGCCATCCCATGGACGGCTTCCTCATCGTGGGCTACCTGTCCTCCGGGCAGGACCGCGCCTTCCACTCGGCCGAGCCCGTGCGCAGCCCCCAGCACATCGCCCAGACCCTGCACGCCGAGCGCATCGACGCCGTCATGACGGTCGGCTCGGTCATCCCCGAGGACCTGGTCACCCTCATGCGCGGTCTGGAGGGCACCCAGGTGCGCCTCGTCGTCGCCCCCGGGCTGCAGGACGTCGTGCCCGGGCGTATGCGGGCCCTGACCGTGACGAACGGCTGGACCGGTCTCATCGCCGTCAAGACCCGCCGCACACGTGCCGCGGGCAAGGCCCTGTTCGACCGCCTCGCCGGCGCCATCGGGCTGGCCCTCATCTCGCCGCTGCTGGCGGCCACCGCGCTCGCCATCCGCCTCGACTCCCCCGGTCCGGTCTTCTACACCCAGACCCGCGTCGGCCAGGACGGCAAGCCCTTCACCATGTGGAAGTTCCGCTCCATGTACATCGACTCCGACGCGCGCCGCGCCTCGGTGGTCAAGGCCGGCGGCGACGCCGGCAACGAGGTCATGTTCAAGGACCGTCAGGACCCGCGCATCACCCGCGTGGGCCGCTGGATCCGCCGCCTGTCGATCGACGAGCTCCCCCAGCTCATCAACGTCGTGCGCGGGGACATGAGCCTGGTGGGGCCCCGCCCCGCACTTCCCGTCGAGGTCGCCAAGTACGACGCCGAGGCGCTGCGTCGTCTCCTGGTCAAGCCCGGGCTGACCGGCCTGTGGCAGATCTCCGGACGCTCGGACCTGTCCTGGGCCTCGACCGTGGCCCTGGACCGTCACTACGTGGAGAACCGGGGCGGAGCCCTGGACGCCAAGATCTTCGCCGGAACGCTGCGCGCGGTCATCGGCGGAAAGGGAGCCTACTGA","LSSSTLTLPQREQHRRPSTAAAADATSPTAPRSPWARTRHDLVIWLVLSDLFAVAVPFWLALLGGHLPLVWSATTVGITMVLIAWFLGALGIDAVEQAGPGTGRFVAAAAVSLPVALLLADLSGVARTTLLATLAAQLLLAVTGRSIEAGWLRRRRLEGHALRRTLIVMGSGSQPMLTQLRRHPMDGFLIVGYLSSGQDRAFHSAEPVRSPQHIAQTLHAERIDAVMTVGSVIPEDLVTLMRGLEGTQVRLVVAPGLQDVVPGRMRALTVTNGWTGLIAVKTRRTRAAGKALFDRLAGAIGLALISPLLAATALAIRLDSPGPVFYTQTRVGQDGKPFTMWKFRSMYIDSDARRASVVKAGGDAGNEVMFKDRQDPRITRVGRWIRRLSIDELPQLINVVRGDMSLVGPRPALPVEVAKYDAEALRRLLVKPGLTGLWQISGRSDLSWASTVALDRHYVENRGGALDAKIFAGTLRAVIGGKGAY$","Undecaprenyl-phosphate galactose phosphotransferase","Membrane, Cytoplasm, Extracellular","galactosyl transferase CpsD","undecaprenyl-phosphate galactose phosphotransferase ","Undecaprenyl-phosphate galactose phosphotransferase","","","","","

InterPro
IPR003362
Family

Bacterial sugar transferase
PF02397	$\"[290-485]T$	Bac_transf

noIPR
unintegrated

unintegrated
tmhmm	$\"[42-62]?$ $\"[68-90]?$ $\"[105-125]?$	transmembrane_regions

InterPro
IPR004820
Domain

Cytidylyltransferase
PF01467	$\"[5-74]T$	CTP_transf_2

InterPro
IPR004821
Domain

Cytidyltransferase-related
TIGR00125	$\"[3-69]T$	cyt_tran_rel: cytidyltransferase-related do

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[1-133]T$	no description

noIPR
unintegrated

unintegrated
PTHR10739	$\"[5-72]T$	CHOLINE/ETHANOLAMINE PHOSPHATE CYTIDYLYLTRANSFERASE
PTHR10739:SF14	$\"[5-72]T$	ETHANOLAMINE-PHOSPHATE CYTIDYLYLTRANSFERASE

","BeTs to 10 clades of COG0615COG name: CytidylyltransferaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane] Functional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG0615 is aompkzyq---lb-------------Number of proteins in this genome belonging to this COG is 3","***** IPB001980 (Lipopolysaccharide core biosynthesis protein signature) with a combined E-value of 1.1e-07. IPB001980A 2-20 IPB001980B 20-41","","","-50% similar to PDB:2B7L Crystal Structure of CTP:Glycerol-3-Phosphate Cytidylyltransferase from Staphylococcus aureus (E_value = 8.4E_10);","Residues 5 to 132 (E_value = 3.5e-12) place ANA_1877 in the CTP_transf_2 family which is described as Cytidylyltransferase.","","cytidyltransferase (rfaE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1878","2031920","2038210","6291","4.86","-80.00","216143","GTGACCACTTCACGCAACGACTTCGAGACGCCCGACACCCCGTCGAGCAGTATCGACTCCGCCGCAGCCACCTCCGGTGCCGGTGACGGCGGAAGCAACCGATCCGACTCCCGCACCGCTCAGACCGAAGCGTCCGCCGCGGACCGTCCCGGTCTGCTCGCCCGCGCCGCCGGCGCCCTGCGCCCCCGGCGACGGAGCCGGGACTCCCGATCCGACGACGTTCAGGACGTCGGCTCGGGCCTGACCTCCGGCACCACCACCTCCCGACTGGCCGCGACCTTCCGCATCCCCCAGTCGCGCGCCCAGCGCGTGCGACTGCGCAAGCGCCTGTCGACGCTGGCCGCCGTCGTATGTGTCACCGCCCTGGGAACGGCCGCCTGGCTCCACGAGGGCGTGGCCCAGGCCGACCTGCACCTCAACGACGGCGGCGTATGGGTCACCTCCACCTCCAAGCACCTGGTGGCCCGCCTCAACTACCCCTCCCGCGAGGTCGACGGCGCGATCCGCACCTCCTCATCCTCCTTCGACGTCACCCAGAACGCCGAGGACATCCTGGTCCCCGACTCCGGCGACGCCTCCGTCTCCTCGGTCGATCCCTCCCAGGTCGCCTTCTCCGGGCGCACCCAGCTCACCAAGGGCGTGACCATCGCCCAGGGCGGGGACCGGGTCATGGCAGTCGACAAGGTTCAGGGCACCATCCGCGCCGCCAAGGCCAAGGAGGCCGGCTCGCTGGCCGCGGCCGCCCCCGTGGTGACCGGCATGCCCGACGTCGTGGCCGCCATCGGCAAGGACGGTGCCATCCACGCCGTCTCAGCCACCAGCAAGTCGCTGGTCTCCCTGGAGACCAGCGACAAGGGCTGGAAGGAGGCCACGAACACCTCCCTGAAGCTGACCGCCGGGACCGATCTGGCCATCACCGCCGTCGGCGACCAGCCCGTGGTCCTGGAGCGCGGCACCGGCATCCTCCACCTGCCCGAGGGCAAGTCCGTCAGCCTGGGGACCTCCGGCCTGGTGCTCCAGCAGCCCGGCCCCGAGGCGGACTCGGTCCTGGTTGCCTCCCGCAACGAGCTCATCTCCGTCCCCATGGACGGGGGCAAGGTCACCAGAACGCCGTCGGCCAAGGAGGGCTCCGCCCCAGAGGGCGTGCCCGCCCAGCCGGTGCGCCTGGGCAAGTGCGTCTACGCGGCCTGGTCCGGCTCGGGCCAGTTCGTGCGCAGCTGCTCGGGACTGTTCGGCGGCGGCACCGACACCGCCCACGACGACAAGCTCGCCTCCTCCTCCGCCCCGATCTTCCGGGTCAACCGCGACGCCATCGTGCTCAACGACCTGGACACGGGCTCGGTGTGGCTACCCAACGAGGACCTCGTCCTCATCGACGACTGGACGGACAAGACCGCCCAGACCGACGACAACGCCGATCAGAAGGACGACTCGGCCAACACCTCGGACTCCCAGACCCCGCCGGAGCGCACCGAGGAGAACCATCCCCCCAAGGCGGCCGACGACAGCTTCGGCGTGCGCCCGGGCCGCTCCGCGCTCCTGCCGGTGCTGGCCAACGACTCCGATCCCGACGGTGACGTCCTCACCGCCACTCCCCAGGACAACGGCGGGTCGCTCAAGGCCACCAAGGCCCAGGGCGGACTGGCTCTGCGGATGGACATCCCGGACAACGCCTCCGGCAGCTTCTCCGTGCCCTACACGGCCGACGACGGCCGCGGGATGAGCGACTCCGCCGTCGCCACCGTTGACGTCCACGGCTGGGACGTCAACGGCGCCCCGAAGCAGATCACCACCCCCACCCTCACCGTCGCCGAGAAGGCCTCCGGCTCCCTGGACGTGCTGGGCCACTGGCTGGACCCCGACGGGGACGACCTCTACCTGGTCTCCGCCCAGGGCGAGGGCCTGGACACCAAGGTCTCCAACGAGGGCACCGTCACGGTGCGCGAGCTGGGCGCCGGCACCGGCACCCGCGACCTGACCGTCACCGTCTCCGACGGCCGGGAGACCACCTCCGGCGTGGTCAAGGTCGACGTGCAGCCGGCCCAGTCGGCCAAGCCGATCGCCAACGCCGACCACGTGCGCGTCGTCGCCGGCTCCAAGACCGTCGTCTCGCCCCTGGACAACGACACCTCCCCCTCCGGGGGGACCCTGCGCCTGGCCGCGGTGCAGGAGGCCCCGGCCGGAACCTCGATCAGCATCGACCAGCAGGCCGGTGTCTTCACCTTCTCCACTGAGGCCAACGCCCAGGCCCAGACCTACTACCTCACCTACGACGTCATGGACGGGGCCAACACGGCCCAGGGCATCGTGCGCGTGGACGTCACGCCCAAGGCCGACGCCACCGTGCCTCCCGAGGTCGAGAACGACACCGCCCTGCTGCGCAACGGCGGCTCGACGACCATCGCCCCGCTCACCAACGACTTCGACCCCTCCGGGGGGATCCTGGTCCTGCAGTCGGTCAAGACCCCGCCGGACTCCGGGGTCACCGTCACGGTCGTGGACCACTCCCTGCTGCAGATCAGCGCGGCCAGCACCGTCCCAGCCAACCTGACGGTGGAGTACACAGTCACCAACGGCACCTCCAGCGCCACCGGGAAGGTGTCCATCGTCCCGGTGACCCAGTCCCAGCCCCAGCCACCGGTGGTCACCAATGACACCGCCGTCGTGCGAGCCGGCGACGTCGTCACCGTGCCGGTTCTGGACAACGACTCCTCCCCCGCCGGTCTCAACCTGTCGGTGGACTCCCAGGTGAGCCTGGTGGGCGACGAGCTGGGCACCGCCTGGGTCAGCGAGAACACCGTCCGCTTCCGCGCCGGCAACCAGCCCGGCCGCACCTCCTACGCCTACACGGCCAAGGACGACCAGGGCCAGACCGCCTCGGGCATTCTCACCGTGGAGGTGCGCGCCCAGGACGCCGAGCACAACTCCGCGCCCTCACCGCGCAACCTGGAGGCCCGCACCCTGGCCGGCTCGGCCACGAACATCACCGTGCCGCTGGACGGCATCGATCCCGACGGCGACTCGGTGAGCCTCGTGGGCCTCAACCAGGCCCCCTCCTTGGGCTCAGTGGAGATCAACTCCTCGTGGCTGACCTACACGCCCTCCGAGGGAGCCACCGGCACCGACACCTTCACCTACGTCGTCGAGGACCGCTTCGGGGCTCAGGCCACCGGCACGGTCCGGGTGGGCGTCGCCCAGGCCTCGCCCCTCAACGTGGCCCCGGTGGCCACCGACGACCTGGTCGTGGCCAAGCCCGGACGCACCGTGGCCGTGGACGTGCTGTCCAACGACCTGGACACTGACGGCGACAGCCTGTCCCTGGAGGGCGACCCGGTCTCCTCCGACCCCTCCCTGGGCGTGTCCACCCGCGCCGGCCGCCTGGTGCTCGACCTGCCGGAGAAGGAGGGCAACCACTCGGTCACGTACACCGTCTCCGACGGACGCGGCGGTACCGACACCGGCACCGTCACCGTCCAGGTCTCGAGCAACGCCCCCCTGGCCAACCCGGTGGGCGTGGACGACTACGTCACCGTCGACCAGGTCGATGCCAACGGCCGGGTCACCGTCCCGGTCCTGGACAACGACAAGGACACCGACGGCTCGCCGTGGGACCTCAAGCTGTCCTCCTCCGACCCCGACGTCGAGGTGGGCAAGGACTCCCTGAGCCTGACGGTGGGCGAGACCCAGCGGCTCGTGCTCTACACGATCACCGACGCCGACGGGCTGACCGGCCACGCCGTCGTCGTCGTGCCGGCCCGCTCGGCCCTGCGGCCCCGCATCAACCCCTCGGCCGTGCCCGCCCGGGTGCTGGCGGACAAGACCACCGACATCAGCCTGTCCTCCTACATCCTCACCCGAGAGGGCACCAAGCCCGTCATCTCGGACACCTCCTCCATCCACATGGCCAAGGGCACCAAGGACGCCAAGGTCGCCTCGGGCGGGTCCGCGCTGTCCTTCACCCCCGACTCGGGCTTCACCGGGCAGACCTCGGTGACCTTCACCGTGGCCGACGGCACCGGTTCGGACGCCCTGAGCTCGACGCTCACGCTGCCGATCATCGTGGAGTCCTCGACGAACCGGCCGCCGACCTTCACCCCCACCGAGGTGACGGTGGCCCCCGGCGAGGGGGCCGTGACGGCCAATCTGGCAGCCATGGCCACCGACCCCGACCCGAGTGACAAGCTCTCCTTCCAGGCCGGTCCCGCCCCCGCGGGATTCGAGATCTCCCTGAGCGGCTCGACGCTGTCCGTCAAGGCCTCCGACAAGACCGCCGAGGGCACCACGGGCTCCATCCCGATCACGGTCTCCGACGGCGTCAACCCGCCGGTGAGCGCCTCCCTGCCCGTGCGGGTCAGCGCCTCCAACAAGCCCCGCATGACCACCGCCCCGATCAACCTGGAGTCCCGCAACGGCGAGGCGGTCAGCACCGACGTGTCCAAGGCGGTGAGCAACCCCTTCCCGGACAAGCCGATCACCCTGTCCGGCACCCCGACAATCACCTCCGGCCAGGGCTCGATCAGCGCCTCGGGAACCACCGTGACGATCACCCCCAACAGCGGGTTCCACGGCACCATCACCGCGCAGTACAAGGTGCTGGACTCCACCGGCTCGGAGTCCCGGGCCGTCACCGGCACCATCACCGTGCAGGTCGGTGGGGTGGCCCCCGCCGCCCCCTCCGGGGTGAGCGTGGCCCCCGTGGGCGCCGACTCGGCACGCGTGTCCTGGGCCGACGGCTCCGCCAACGGCTCCCCCATCACCGGCTACAAGGTCAGTGTCAACGGCACCGAGCAGTCCTGCTCGACCTCGAACTGCCTCATCAGCGGCCTGACGCCCGGTCAGAGCTACAGCATCCAGGTCGTGGCCACCAACAAGTACGGCGACTCCGAGGCCGCGACGGTGTCCTACCAGCACAACGCCACCGCTAAGACCCCGGCTGCGCCCACACTGACAGCCGGCTCGGGCAAGGTCACCGCCACCTGGACCGAGGTGGACGACCCCTTCGGGGGCACGACGACCTATGACGTGCGCCTATCGGACGGCAGCGTGCAGACGGGCGTCTCCGGGAGCTCGGCCTCCTTCGACGTCGCCCCGGGACGCGCCTACACCGCTCAGGTGCGCGCCAGGTCCAGCCAGGGGACGGTCTCGGAGTGGTCCTCCCCGTCCAACTCGGTGACGCCCTACGGCGAGCCCGGCACCCCCGGGACTCCCGTCATCACCCCCAACGGGGACACAGTCACCATCAGCTGGCAAGCCGCTAACGGCAACGGCAGCCCCGTGAGCTACACGCTGCACTACTCCAACGGGCACACCAGCGACTCCAAGAACGTGGGAGGAGCCACCTCCACCACGGTCTCGGTCTCGCGCGGGACCTGGACCTTCTGGGTCGAGGCCGACAACGGTCACGGCACCAAGACCTCGGGCCAGGCCAGCTACGCCTACAAGCCGACCCCGCTGACGCCGTCGACCCCGGCCGTCAAGGCCACCGGCAACAGCGGCGAGCTGTCCGTGAGTGCCTCACCCCGCGCCGGCAACGGCTGGAGCGTGGGCGAGCTGACGGTGGAGTACTCCGTCGATCAGGTCACCTGGACCAGCTCCTCGACCATCCGGGGACTGACCGACGGGCATGCCTACACCGTCTACGCCCGCACCAACGGCGGCGGCCAGTACTCCGACGTCGTCGCCTCCTCACCGGTGGCGCCCTACGGCCCGCCGTCGGCTCCCTCGGTCAGCTGTGAGCTCACCGGCAAGAAGCAGAAGAAGGTCTCCTGCTCCTGGAACCCCGGGGCCAACAGCGGCGCCGGCGCCGAGTACGAGCAGACCGACGACGGCGGCAAGTCCGTGGAGAACGTCGAGATCGGCGACACCTATGACGGCAAGCTCAAGCGCGGTGAGTCGCTCACCTGGTGCGTGCGGGCCCGGACCAACGCCGGTACCTCCGAGTGGGGCTGCGACACCGTAACCCGGCCGTCCAAGCACGACAACGATGACGACGATGATGACGCTGACAAGAAGCAGGCCTACCCGGTCGGCACTGAGCAGCAGTTCTACGTGGACTACACGCAGAGGTGCCACCCCTTCGGCCCCTGGGGCACCTGCTACCAGATGGTCTTCGACATCTCCGGAAACCCCAACAGCACCGTGTCCTGCGGCTACTGGTACTGGGACACCTGGAACTGGCAGCCCGCCTGGAACGAGGAGGAGATCGCCCTCGACAAGAACGGCTACGCCCGACACACGTTCCCCCACAGGACGCCCAACTGGGACCAGACCATCACCTGCACCCAGCAATAA","VTTSRNDFETPDTPSSSIDSAAATSGAGDGGSNRSDSRTAQTEASAADRPGLLARAAGALRPRRRSRDSRSDDVQDVGSGLTSGTTTSRLAATFRIPQSRAQRVRLRKRLSTLAAVVCVTALGTAAWLHEGVAQADLHLNDGGVWVTSTSKHLVARLNYPSREVDGAIRTSSSSFDVTQNAEDILVPDSGDASVSSVDPSQVAFSGRTQLTKGVTIAQGGDRVMAVDKVQGTIRAAKAKEAGSLAAAAPVVTGMPDVVAAIGKDGAIHAVSATSKSLVSLETSDKGWKEATNTSLKLTAGTDLAITAVGDQPVVLERGTGILHLPEGKSVSLGTSGLVLQQPGPEADSVLVASRNELISVPMDGGKVTRTPSAKEGSAPEGVPAQPVRLGKCVYAAWSGSGQFVRSCSGLFGGGTDTAHDDKLASSSAPIFRVNRDAIVLNDLDTGSVWLPNEDLVLIDDWTDKTAQTDDNADQKDDSANTSDSQTPPERTEENHPPKAADDSFGVRPGRSALLPVLANDSDPDGDVLTATPQDNGGSLKATKAQGGLALRMDIPDNASGSFSVPYTADDGRGMSDSAVATVDVHGWDVNGAPKQITTPTLTVAEKASGSLDVLGHWLDPDGDDLYLVSAQGEGLDTKVSNEGTVTVRELGAGTGTRDLTVTVSDGRETTSGVVKVDVQPAQSAKPIANADHVRVVAGSKTVVSPLDNDTSPSGGTLRLAAVQEAPAGTSISIDQQAGVFTFSTEANAQAQTYYLTYDVMDGANTAQGIVRVDVTPKADATVPPEVENDTALLRNGGSTTIAPLTNDFDPSGGILVLQSVKTPPDSGVTVTVVDHSLLQISAASTVPANLTVEYTVTNGTSSATGKVSIVPVTQSQPQPPVVTNDTAVVRAGDVVTVPVLDNDSSPAGLNLSVDSQVSLVGDELGTAWVSENTVRFRAGNQPGRTSYAYTAKDDQGQTASGILTVEVRAQDAEHNSAPSPRNLEARTLAGSATNITVPLDGIDPDGDSVSLVGLNQAPSLGSVEINSSWLTYTPSEGATGTDTFTYVVEDRFGAQATGTVRVGVAQASPLNVAPVATDDLVVAKPGRTVAVDVLSNDLDTDGDSLSLEGDPVSSDPSLGVSTRAGRLVLDLPEKEGNHSVTYTVSDGRGGTDTGTVTVQVSSNAPLANPVGVDDYVTVDQVDANGRVTVPVLDNDKDTDGSPWDLKLSSSDPDVEVGKDSLSLTVGETQRLVLYTITDADGLTGHAVVVVPARSALRPRINPSAVPARVLADKTTDISLSSYILTREGTKPVISDTSSIHMAKGTKDAKVASGGSALSFTPDSGFTGQTSVTFTVADGTGSDALSSTLTLPIIVESSTNRPPTFTPTEVTVAPGEGAVTANLAAMATDPDPSDKLSFQAGPAPAGFEISLSGSTLSVKASDKTAEGTTGSIPITVSDGVNPPVSASLPVRVSASNKPRMTTAPINLESRNGEAVSTDVSKAVSNPFPDKPITLSGTPTITSGQGSISASGTTVTITPNSGFHGTITAQYKVLDSTGSESRAVTGTITVQVGGVAPAAPSGVSVAPVGADSARVSWADGSANGSPITGYKVSVNGTEQSCSTSNCLISGLTPGQSYSIQVVATNKYGDSEAATVSYQHNATAKTPAAPTLTAGSGKVTATWTEVDDPFGGTTTYDVRLSDGSVQTGVSGSSASFDVAPGRAYTAQVRARSSQGTVSEWSSPSNSVTPYGEPGTPGTPVITPNGDTVTISWQAANGNGSPVSYTLHYSNGHTSDSKNVGGATSTTVSVSRGTWTFWVEADNGHGTKTSGQASYAYKPTPLTPSTPAVKATGNSGELSVSASPRAGNGWSVGELTVEYSVDQVTWTSSSTIRGLTDGHAYTVYARTNGGGQYSDVVASSPVAPYGPPSAPSVSCELTGKKQKKVSCSWNPGANSGAGAEYEQTDDGGKSVENVEIGDTYDGKLKRGESLTWCVRARTNAGTSEWGCDTVTRPSKHDNDDDDDDADKKQAYPVGTEQQFYVDYTQRCHPFGPWGTCYQMVFDISGNPNSTVSCGYWYWDTWNWQPAWNEEEIALDKNGYARHTFPHRTPNWDQTITCTQQ$","Fibronectin, type III domain protein","Extracellular, Periplasm, Cellwall","large protein with C-terminal fibronectin typeIII domain, putative","VCBS","Fibronectin, type III domain protein","","Skorstengaard K., Jensen M.S., Sahl P., Petersen T.E., Magnusson S. Complete primary structure of bovine plasma fibronectin. Eur. J. Biochem. 1986. 161(2):441-453. PMID: 3780752Dean D.C., Bowlus C.L., Bourgeois S. Cloning and analysis of the promotor region of the human fibronectin gene. Proc. Natl. Acad. Sci. U.S.A. 1987. 84(7):1876-1880. PMID: 3031656Gulcher J.R., Nies D.E., Marton L.S., Stefansson K. An alternatively spliced region of the human hexabrachion contains a repeat of potential N-glycosylation sites. Proc. Natl. Acad. Sci. U.S.A. 1989. 86(5):1588-1592. PMID: 2466295Schwarzbauer J.E., Tamkun J.W., Lemischka I.R., Hynes R.O. Three different fibronectin mRNAs arise by alternative splicing within the coding region. Cell 1983. 35(2):421-431. PMID: 6317187","","","

InterPro
IPR003961
Domain

Fibronectin, type III
PF00041	$\"[1555-1631]T$ $\"[1644-1718]T$ $\"[1730-1810]T$	fn3
SM00060	$\"[1555-1628]T$ $\"[1641-1714]T$ $\"[1730-1890]T$ $\"[1904-1979]T$	FN3
PS50853	$\"[1555-1637]T$ $\"[1640-1725]T$ $\"[1726-1813]T$ $\"[1817-1899]T$ $\"[1900-1989]T$	FN3

InterPro
IPR008957
Domain

Fibronectin, type III-like fold
G3DSA:2.60.40.30	$\"[1554-1634]T$	no description

noIPR
unintegrated

unintegrated
PTHR19900	$\"[1555-1634]T$	MYOSIN-BINDING PROTEIN-RELATED
PTHR19900:SF7	$\"[1555-1634]T$	TITIN
tmhmm	$\"[110-128]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1555 to 1631 (E_value = 1.9e-12) place ANA_1878 in the fn3 family which is described as Fibronectin type III domain.Residues 1644 to 1718 (E_value = 0.031) place ANA_1878 in the fn3 family which is described as Fibronectin type III domain.Residues 1730 to 1810 (E_value = 0.018) place ANA_1878 in the fn3 family which is described as Fibronectin type III domain.","","protein with C-terminal fibronectin type III domain, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1879","2038297","2039256","960","5.12","-11.32","34160","ATGACTCCCGAGAACGCGACATGGTTCGCTGACGCCTTCTCCACCATTGTCAACAACGTCGGTCAGGCGCTGCTCGACAAGGAGGACGTAATCAAGCTGGCCCTGACCACCATGCTCTCCGAGGGCCACCTCCTGCTCGAGGACGCCCCCGGCACCGGCAAGACGGCCCTGGCCCGGGCCCTGGCGGCCTCGGTGCAGGGGACGCACTCGCGCATCCAGTTCACCCCCGACCTGCTTCCCAGTGACATCACGGGTGTGACGATCTACGACCAGAAGACCGGCAACTGGGACTTCCACGCCGGCCCGATCTTCTCCTCCATCGTCCTGGCCGATGAGATCAACCGGGCCAGCCCCAAGACCCAGTCCGCCCTCCTGGAGGTCATGGAGGAGTCCCAGGTGACCGTCGACGGCGTGCGTCATACGACCGAGCGCCCCTTCATGGTCATCGCCACCCAGAACCCCATCGAGCAGGCCGGCACCTACCGCCTGCCCGAGGCCCAGCTCGACCGCTTCCTCATGAAGACCTCCGTGGGCTACCCCAACCGGGAAGCGCTCACCCGGATCCTCTCCAGCTCGGCCCACCCGGACCGCTCCAAGAGCCTGTCCGCGGTCGTGGCCTCCTCCGTGGTGGCCTCCATGGCCGACCTGGCCGCGGAGAACCACATCGAGAACTCGGTACTGGACTACATCGGAGCGCTGGTGGAGGCCACGCGCGCAGCCGACGAGACCCGCATGGGCGTGTCCACCCGTGGCGCCATCGGCATGGCTCGGGCCGCCCGGGTGTGGGCGGCCTCCCAGGGACGCAGCTACGTCCTGCCCGACGACGTCAAGGACCTCGCCGAAGTCGTGTGGGCCCACCGCCTGGTCATGGACCCCGACGCCGAGTTCACCGGCGCCACCGCCTCCGGCGTCATCACCACCGCCCTGGCCCAGGTCCCCGCCCCCACGACCCGCGACTGA","MTPENATWFADAFSTIVNNVGQALLDKEDVIKLALTTMLSEGHLLLEDAPGTGKTALARALAASVQGTHSRIQFTPDLLPSDITGVTIYDQKTGNWDFHAGPIFSSIVLADEINRASPKTQSALLEVMEESQVTVDGVRHTTERPFMVIATQNPIEQAGTYRLPEAQLDRFLMKTSVGYPNREALTRILSSSAHPDRSKSLSAVVASSVVASMADLAAENHIENSVLDYIGALVEATRAADETRMGVSTRGAIGMARAARVWAASQGRSYVLPDDVKDLAEVVWAHRLVMDPDAEFTGATASGVITTALAQVPAPTTRD$","Methanol dehydrogenase regulatory protein","Cytoplasm","methanol dehydrogenase regulatory proteinhomolog","K03924 MoxR-like ATPase","ATPase associated with various cellular activities, AAA_3","","","","","

InterPro
IPR011703
Domain

ATPase associated with various cellular activities, AAA-3
PF07726	$\"[43-173]T$	AAA_3

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.80	$\"[232-292]T$	no description
G3DSA:3.40.50.300	$\"[23-178]T$	no description

InterPro
IPR002881
Domain

Protein of unknown function DUF58
PF01882	$\"[97-199]T$	DUF58

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","BeTs to 13 clades of COG1721COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1721 is ao-pkz-qvdr-bc-fg----j--t-Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 97 to 199 (E_value = 3.1e-23) place ANA_1880 in the DUF58 family which is described as Protein of unknown function DUF58.","","of unknown function family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1881","2040638","2043223","2586","9.62","17.56","91283","ATGACCCCCACGACGACTCTCACCACCGCCTCCCCCCGCACCGCGGGCTCCCCGATCTCGGGCGCCTCGCCGGCCGGGGCGTCCTCTCCGGCCGAGGCCCCCTCACAGGTCACCGCCGCGCCCTTGAGCGGCTCGGACGAGTCCGCCTCCTGGTCGACGGCGACGTCGTCGTCGCGCACGCGCAGCCTCTACAGCAACGAGACGACGCGTCGGGCCCGCTCAATCACCGGCGCCGGCCCCCTTCTGTCGCGCCCCTCCCGGCCGGCCCTCTCCGCCCGCCGCTTCCTGCCTCCCCGGCGCGGCACCAAGCCGCCCACGCTGGCGGCCGCGACCCTCGAGCTGGTCCTCATGGCCGGGATCCTCGCCATCGGTGCGGTCCCTTTCCTGCCGGTCTTCGCCTCCGTGGCAGGCTGCCTGGCCGTCGGCTACGGCGCACTCATCGGCGCCCTGACCTCGTTGGTCTGCTCGCGCCTGCGCCTGTCCGTGCTGCCGAGCATGGCGGCCCTGGCGCTGGTCCACGTCCTGGTGGCCCCGTGGCTGCTGACCGATGTCGGCTCCGGGACAACGGCGATCAAGACGGTGCTGGGCTCCACGATCACCGTATGGCGAGACGCCCTGACCGTGCCGATGCCGCTGAGCTCCTTCAGCGGCATGACGGTGCTGCCCTGGTTGACCGGGCTGGTGGTCTCAGCGCTGGCGACCCGCCTCATCCTGGCGGGCCGTGAGGTCCTGGCCGGCCTGATCCTGGCCTGCCTGCCCGCCGTCGGCATCGGCTGGGGTGGGCAGGAGGCCGTGCGCCCCACCGTGCTGGGCGTCCTGTTCGTCGTCGGGATCCTGGCGCTGTGGACCTGCGGTTCCCTGCGGCAGCGGCGCAGTCACGTCGTCGAGGCCCTGGACCTGAACTCCTTCTCGACGACCTCGGGCACCACGAGCGCCCGCTCCACCGGGGACCTGGGTCGGGCGGCCCTGCGCGGGACGGTCATCGCCGCCGTGCTGCTCCTGGTCACCTCCCTGGCCGCCATGGTCCTCACCCCCGCCGTCCCCACCTCCCGGACGGTGGTGCGCGACCTGTTCCAGCCGCCGCTGGACGTGACCGAGTACGCCAGCCCACTGTCCCTGGTGCGCACCCTGGAGACCGACAAGGCCCACACCCGGCTCATGAAGCCCATCAACCTGCCCTCAGGCGGGCGCATCCGCATCGCCGCCCTGGACTCCTACGATGGGCTGTCGGCCCACATCGGCCAGAACGAGAACGGGCAGTCGCGCTTCGAGCGCATCGGTGACAAGACCCAGCTGACGGCCAGCCGGCTCGACGGGCGCAAGCAGACCTCCTCGCTGACCATCGAGGACTACAGCTTCCCCTGGGTGCCCACCATGCCCGAGACGATCCGCATCGAGTCCTCCGGGCCGCGTCAGTCGGCTCTGCGCGAGGGCATGTACTACGACAAGTTCTCCTCCACCGGGATCGCCACCAGCGGCCTGGCCTCGGGCGACGTTCTCACCGAGCGGGTCGCCCCCTACACCGCGCCCTCCGAGGCCGCCCTCAACAAGGCCTCCCTGGCGCAGACCTCGCTGGGACCGGTCGAGCAGGTACCGTCATCGGTGGCCTCCCTGGCCAAGGAGATCGTCGGGGCCGAGTCCAACCCCATCGCGCAGGTCCGGGCGCTCCAGCAGCGCCTGCGCACGAGCTACTACTCCGACGGCACCAAGAGCCCCTCCCAGCCCGGGCACGGGGCCGCCCGCATCGCCTCCATGGTGGAGGCCGACTCCCTCATCGGCGACGACGAGCAGTACTCGGTGCTCATGATGCTCATGTGCCGCTCACTCAACATCCCGGCCCGCGTCGTCATGGGCTTCGACCCTGCTACTGACGGCGATGCCAAGACCGTCACCGGCGAGGATGTCAAGGCCTGGGTGGAGATCCCCTTCGAGGGGCTGGGCTGGGTGTCCTTCGACGTCACGCCGGACCGCGACCAGGTTCCCCAGCAGCAGACCACCCAGAAGGTCTCCAACCCCGAGCCCAACGTCCTCCAGCCCCCGCTGCCCAACGAAGACCCGGCCCAGCTGCCCCCCAACTACGAGGACCCGCAGCGCGACGACCCCCAGGACAAGGACAAGGGCGGTCTGCCGACGGCGGTCATCGCCGTCGGAGGTTCCATCCTGGCGATCACGATGATCGTAGGCTCGGTCCTGGGATGGAAGGCCTGGCGCCGCCGCCGCCGGCGCGCACGCACCGGTGTCGGTAAAGCCCTGGGGGCCTGGGAGGAGATCCTCGACCGAGCCCGCGACCTGGGACGCTACCCCGGGTGGGGAGCCACTCGGAGGGAGGCGGCCGCGCAGCTGGCTCCTCACTTCCCGCAGGTCGATCTGCCTCGATTCGCCGGAGCAGTTGACACCCAGGTCTTCAGCTCCGGGGAGCCGCCATCGTACGCTCTAGGGGAGTTGTGGGAATCCTCAGATGCGATCGTCCGCTGCATGGGGGCGGAACGCTCGCGCCTGGGGCGGGTATGGGCCCGTCTGTCCCCGCGCTCCCTCGTCCATCCCGCCGGCAGGCGGTCACGTCCCCCCAGGAGGTTGCGGTCATGA","MTPTTTLTTASPRTAGSPISGASPAGASSPAEAPSQVTAAPLSGSDESASWSTATSSSRTRSLYSNETTRRARSITGAGPLLSRPSRPALSARRFLPPRRGTKPPTLAAATLELVLMAGILAIGAVPFLPVFASVAGCLAVGYGALIGALTSLVCSRLRLSVLPSMAALALVHVLVAPWLLTDVGSGTTAIKTVLGSTITVWRDALTVPMPLSSFSGMTVLPWLTGLVVSALATRLILAGREVLAGLILACLPAVGIGWGGQEAVRPTVLGVLFVVGILALWTCGSLRQRRSHVVEALDLNSFSTTSGTTSARSTGDLGRAALRGTVIAAVLLLVTSLAAMVLTPAVPTSRTVVRDLFQPPLDVTEYASPLSLVRTLETDKAHTRLMKPINLPSGGRIRIAALDSYDGLSAHIGQNENGQSRFERIGDKTQLTASRLDGRKQTSSLTIEDYSFPWVPTMPETIRIESSGPRQSALREGMYYDKFSSTGIATSGLASGDVLTERVAPYTAPSEAALNKASLAQTSLGPVEQVPSSVASLAKEIVGAESNPIAQVRALQQRLRTSYYSDGTKSPSQPGHGAARIASMVEADSLIGDDEQYSVLMMLMCRSLNIPARVVMGFDPATDGDAKTVTGEDVKAWVEIPFEGLGWVSFDVTPDRDQVPQQQTTQKVSNPEPNVLQPPLPNEDPAQLPPNYEDPQRDDPQDKDKGGLPTAVIAVGGSILAITMIVGSVLGWKAWRRRRRRARTGVGKALGAWEEILDRARDLGRYPGWGATRREAAAQLAPHFPQVDLPRFAGAVDTQVFSSGEPPSYALGELWESSDAIVRCMGAERSRLGRVWARLSPRSLVHPAGRRSRPPRRLRS$","Transglutaminase domain protein","Membrane, Periplasm, Cytoplasm","Transglutaminase-like superfamily domainprotein","hypothetical protein","transglutaminase domain protein","","Griffin M., Casadio R., Bergamini C.M. Transglutaminases: nature's biological glues. Biochem. J. 2002. 368:377-396. PMID: 12366374Yee V.C., Pedersen L.C., Le Trong I., Bishop P.D., Stenkamp R.E., Teller D.C. Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(15):7296-7300. PMID: 7913750Pfister P., Wasserfallen A., Stettler R., Leisinger T. Molecular analysis of Methanobacterium phage psiM2. Mol. Microbiol. 1998. 30(2):233-244. PMID: 9791169Makarova K.S., Aravind L., Koonin E.V. A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases. Protein Sci. 1999. 8(8):1714-1719. PMID: 10452618","","","

InterPro
IPR002931
Domain

Transglutaminase-like
PF01841	$\"[590-654]T$	Transglut_core

noIPR
unintegrated

unintegrated
tmhmm	$\"[102-122]?$ $\"[128-150]?$ $\"[160-180]?$ $\"[212-232]?$ $\"[237-259]?$ $\"[265-283]?$ $\"[327-347]?$ $\"[713-733]?$	transmembrane_regions

","BeTs to 9 clades of COG1305COG name: Transglutaminase-like enzymes, putative cysteine proteasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1305 is a-m-k--qvdr-bc-f-hs--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 590 to 654 (E_value = 4e-05) place ANA_1881 in the Transglut_core family which is described as Transglutaminase-like superfamily.","","superfamily domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1883","2043220","2046618","3399","5.26","-36.27","115290","ATGACGATCACTGCTGACGCCCGTAGCAGCGCTTCGACCGCTGCGGGCCCACCGGCGTCCTCCCGCCCGTCCGACGACGCGACGCGCACCGACGTCGTCAGTCCGTACGGCACGGCGCCGAGTGCCCCCGGTACCCCGCACGGCGGAGCGCAGACGGCCGACTCCCGGGGCTCGGAGCCCGGTGCGGCCCGGACGTCCTCGCACACGACCTCCTCTGCGCACCGCCGCCTCCCCCCGGCCCCGGTGCGGGCACGCGTGGTCGCCGGGGTCATCGATCTCGTCATCGGCTCACTTCTGGTGGGGGGCCTGACCGCCGTCATCTGGCGGGTGGGCGGCCGCCCGGTGCTGACCAGTGGACTCATCGCCTTCGGGCTGGTCGTCGGGGCGCGCTGGCTCACCATCGCCGCCACCGGCTGGTCCCTGGGCGGGAGGCTGCTCAGGATCCGCATGCTGGGGGCCCGCCACCAGACCCCCTCACCTCTGGGTTCCTTCCTCCACGCCGATCTCATCCTGGCCGTCAGCATCACCACGCTCGGCCTGGGCACCATCGCGCTCATGCGTACGGCGGCCGCCGACCCCGAGGGGCGCGGCTGGCACGACAAGCTCTCCGGGATGGCGCTGCTCAGCGCCCGCAGAACGAAGCGTCCTGCGCGGCCCGTCTCCTCGGCGACCGAGCCGCAGGGGCGCCCCGCCACCGAGCCCGACTCCTCCAGCCCCCGGGCCGATGCCGGGGCCGAGGCACCGGAGGCATCCTCCGCCCAGGACATCGGTGAGGCGTGGGATGCTGCCAGGCGAGCCTCCCTGTCCTCTTCCGAGTCTTCTTCCGGCGGGCAGAGCACCACGAGCCAGGAGCCCGCCGCGGCCCCCTCCTCTCCGGCCACTGAGGCACCAGACGAGTCCGCCTCCCGCACTCAGCACTCCGAGCGGGCTGAGCGCAAGGCTGAGAAGAAGGCTGGGAAGGCGGCTCGGGGCAAGAAGGCCAGGAAACGCGGCCCTCGTCCGGGCTCGACACGCGCACGCTCAGGTCAGGAGGCGGCACAGGAGGCGCAGCAGGCCACCACGGCGGGTCCCCAGAGCAGCACCGAGGCCGGCGCCACCGAGTCCTCCGGCAGGAGCGCGCACCCGACGACGTCGGATCCGGTCTCCTCCTCGATCCGTCGGCCCCGCCCGGCCCGCCCGGGGCGACCCGCACGTCATGCTGGTCGTGCCTTGAGTACTGGCTCGTCCAGCGGCTACGCATCAACGGCCTCAGAAACCTCCGCCGAGGAACAGGCCCTGAGCACAGCTGCCGCGGCGACCACAGCCACGTCTCAGAGCGCGGCCAAGGCCACCAAGGCGGCGACCGTCTCATCGTCGGCCTCTGCGAAGTCGGCGGCCTCCGCCGGTCCGGCGATCGTGGAGACCGACGCCCAGGCCGTTGCCGTCGCCTCCGCCACCCCTATGGACCCTCAGGCATCCGCTGCGATGGCTGCAGCCCGGGCCGAGTCCCGGCCGGCGGTGGAGAAGTCCTTGAGACCCCCGACGGGGCCGGTCGACGAGGACGCGGTCGCAACCGCCCCCGAGGCCCTGGAGGATACCGAGGCGGCGACTTCCCCGGCTCAGGAGGACACGGAGCCGGCACCGGCCGCCCCCACCGAGGCCATGGAGCCGACAGCGGACGACACGGCACCAGAGGCATCATCAGAGCCGATCAGCCCGGCACCGGCTGAGGAAGCCGAGGAACCAGCTGAGGAAGCCCAGGAGGCGGCTGACGAGCACGCCGAGGAACCAGTCGAGGAACCGGTCGATGAACCGGCTGCCGACGTCGAGGAACCATCCAACGAGCCGTCCGAGGCGGACGTCGAGGAGCCGCAGGCAACCGCATCATCGAGCTCCGACGACGCCGCGTCGCAGCAGCCCTCGCCGATGGACACCGAAACCGCTACGCTCGACGTTGTGGAGGACGCACCGTCTCAGCCCACGGATGACACCGACAGCCGGGGTGACGAGGCCGAGAAACCCTCGACCCATGCGCCGCCCTCATCTGAGCACCCGGCCGATCAGCAGCAGTCCGAAGCGACGACGCCCTCAGCGGAATCCTCCAAAACTGCTGATGATTCCGAGGCATCCCAGTCCTCCACGTCGCACGATGCGACTTCCACACCACAAGTCCCGCGCTCACAAGCCACAGAACCCGTAACATCACAAACGATGGAACCACGACACGCCCACGCCCAGCGCTGGAGGATTCAGCCCGGTCACACCGGCAAGAAGGCCTCCGGCTCGTCTGCTGCACCTACCGAGGATCAGCGAGAGTCGGTGTCACAGCCCGGCGTTCCTCGTCGCGAGAGCCTCTTCACCACCGAGCGGCAGCGCTTCGCTGCCGGGGCCGGCCCCGTCCCGGAGGTCGCGCACACCTTCGACACCTCCAGCATCCTGCCCTCGGGGGACCGCAACACGCAGGCCCTCATCGACTCGGTGCCCTGGTCCTCGGTTCCCACCTCGGTTGATGCCGCCACGGTGGACTCCCTGCCGGAAGGGGTCGTCGTCTCCGACGACGGCCTGCCCCAGCAGCCGACGACGGTTTCGGCGCCTGCGCAGCACGCCTCCCCGATGGACCTGACCAACCCCGCCACCGTGCCCGGTGGTGTCCCGGCCGCCTCGGAGGGCACGGCACACCCGACCGTGCGCAGCCACCGCAGCCACGCTCGGACCTCTGCCGGCAGTGCGACGAGCGCGGCCGTCCCGGAGGAGACCCCCTCGCGCCGGCCTCACGCCTCACACCGTTTCGCGGGGCCGGGAATCCCCTCGCCCACGGATGGACGCGCCGTCCCCAGTGAGTCCCGCAGCGACGCACGCGCCGCGGATGCCGGCACCGTTCGTCACGAGCGCTCCGCCTCCGTTCAGGCGCCGGAGCAGCCCCGCACGGGTGTGTCCAGGCGCAGTGCAGGCAGCGTGCCGGAGGCGGCCGCGCCGGTCTCCTCCCCCGCTGCAGGTGCCTCCCGGTCCCCGCTCACCCCGGTTCCTGACGCGAGCGCCCAGACTGCCACGCCGTCACTTCCGTCGGCCTCCTCGGCCGCTCCGGCCCTGTCGGTACGTCTCGTCCCGCTGCTGGGCGGCAACCCGATCCTCATCCACGAGCCCACGGTGGTGGGCCGCGACCCCGACAACATCTCGGCCTACCCCGGGGCGGAGCGTGTCGCTCTTGACGATCCCACCCGCTCGGTGTCCAAGACGCACGCGGCGATCTTCCCGCTGCTGGACGGAGTGTGGGTCACCGACCTGCACTCCACCAACGGGACTCGGGTGGAGTACCGCGATGGGCGCACCGTCGAGGCCGTTCCGGACAAGGCCCTGTCCGCCCTGGAGGGCAGCACGATCTTCTTCGGCCGCATCGCCTTCAAGGTGGAGGTCGTCTGA","MTITADARSSASTAAGPPASSRPSDDATRTDVVSPYGTAPSAPGTPHGGAQTADSRGSEPGAARTSSHTTSSAHRRLPPAPVRARVVAGVIDLVIGSLLVGGLTAVIWRVGGRPVLTSGLIAFGLVVGARWLTIAATGWSLGGRLLRIRMLGARHQTPSPLGSFLHADLILAVSITTLGLGTIALMRTAAADPEGRGWHDKLSGMALLSARRTKRPARPVSSATEPQGRPATEPDSSSPRADAGAEAPEASSAQDIGEAWDAARRASLSSSESSSGGQSTTSQEPAAAPSSPATEAPDESASRTQHSERAERKAEKKAGKAARGKKARKRGPRPGSTRARSGQEAAQEAQQATTAGPQSSTEAGATESSGRSAHPTTSDPVSSSIRRPRPARPGRPARHAGRALSTGSSSGYASTASETSAEEQALSTAAAATTATSQSAAKATKAATVSSSASAKSAASAGPAIVETDAQAVAVASATPMDPQASAAMAAARAESRPAVEKSLRPPTGPVDEDAVATAPEALEDTEAATSPAQEDTEPAPAAPTEAMEPTADDTAPEASSEPISPAPAEEAEEPAEEAQEAADEHAEEPVEEPVDEPAADVEEPSNEPSEADVEEPQATASSSSDDAASQQPSPMDTETATLDVVEDAPSQPTDDTDSRGDEAEKPSTHAPPSSEHPADQQQSEATTPSAESSKTADDSEASQSSTSHDATSTPQVPRSQATEPVTSQTMEPRHAHAQRWRIQPGHTGKKASGSSAAPTEDQRESVSQPGVPRRESLFTTERQRFAAGAGPVPEVAHTFDTSSILPSGDRNTQALIDSVPWSSVPTSVDAATVDSLPEGVVVSDDGLPQQPTTVSAPAQHASPMDLTNPATVPGGVPAASEGTAHPTVRSHRSHARTSAGSATSAAVPEETPSRRPHASHRFAGPGIPSPTDGRAVPSESRSDARAADAGTVRHERSASVQAPEQPRTGVSRRSAGSVPEAAAPVSSPAAGASRSPLTPVPDASAQTATPSLPSASSAAPALSVRLVPLLGGNPILIHEPTVVGRDPDNISAYPGAERVALDDPTRSVSKTHAAIFPLLDGVWVTDLHSTNGTRVEYRDGRTVEAVPDKALSALEGSTIFFGRIAFKVEVV$","Hypothetical protein","Extracellular, Periplasm, Cellwall","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","RDD domain containing protein","","Hofmann K., Bucher P. The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors. Trends Biochem. Sci. 1995. 20(9):347-349. PMID: 7482699Durocher D., Jackson S.P. The FHA domain. FEBS Lett. 2002. 513(1):58-66. PMID: 11911881","","","

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[1042-1108]T$	FHA
SM00240	$\"[1041-1101]T$	FHA
PS50006	$\"[1042-1097]T$	FHA_DOMAIN

InterPro
IPR010432
Domain

RDD
PF06271	$\"[79-209]T$	RDD

noIPR
unintegrated

unintegrated
tmhmm	$\"[87-107]?$ $\"[121-143]?$ $\"[164-184]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 79 to 209 (E_value = 0.00024) place ANA_1883 in the RDD family which is described as RDD family.Residues 1042 to 1108 (E_value = 3.3e-06) place ANA_1883 in the FHA family which is described as FHA domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1885","2047003","2047224","222","8.84","1.17","7787","GTGTCCACAGCGCTGACATCGCCGAGCCTGCCGTCAAAGCGCTCCTCGAGGATCCTTGGAATTCCACAGTTCGTCTTCGGCGTGCGACGTCGGAGCGGGGGTGATGTCAGCACCGTGGACACCGACGACCCTCCAGACCTCCTCCATCGGCCCTTCGGCGTCTCTAGGGCGACCGACCCCATCGCCGAGCTCCTGCCCGAGCCAGCGCCTCAGAAGCCATAA","VSTALTSPSLPSKRSSRILGIPQFVFGVRRRSGGDVSTVDTDDPPDLLHRPFGVSRATDPIAELLPEPAPQKP$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1887","2047432","2048523","1092","7.12","0.57","39791","GTGCTCGCATGGCGGCTGCACAGGCAGTACGTGGAGCCGTTGACGGACACAGGCCCTGTTGAGATCGTCGGACGGCTCTGCGGCGTACAGGCGCAGGTGGCGTCCGCAGCTGAGACCGCTGTCGCCTTACGGCAACGCAACCCGCAACCTGAAGGGGTCAAGCGTGCCTACTCCGACCGCTCGCTTGTCAAGACGTGGGCAATGCGCGGAACGCTGCACGCGATGCGGTCCTCAGACGTAGCGGAGTACCTGTCGCTGCTGGCCGGCGCCCGTACGTGGACCAAGCCCTCCTGGTCACGGCACTTCGGTGCGACGCCAGAGGAGGTCGAGCAGCTGACGGAGTCTGTCGCCGACCTTCTCCACGGTCAGGTGCTGTCTCGCGATGAGCTCGTGAGCGAACTGGTTCAGGACAATCGGTTCAAGGGGATGGAAGAACAACTGCGCTCCGGGTGGGGTGCTCTGCTCAAGCCTCTCGCATGGCAGGGTGCCCTGTGCTACGGCCCGAGCCCGTCTTCGAAGGCGACATTCACTCACCCCGCCAGCCTTCTGAAGAACTGGAATGGGCTGCCGGATCCTGCGGAGGCAGCACCAGCGGTCATTAAGCGATACCTCTCCGCCTACGGCCCGGCGACCCCTGAGACCTTTGATGCGTGGCTTTCGCGTAACAGCAACAAGAAGTCAACGCTCAGGAGCTGGTTCGCCAGTCTTGGCGAACAGATCGTCGAGGTGAGGGTGGAGGGTGAGACACGGTATCTGCTCGCCGAGCATGAGGACGAGCTCGCGGCCACCCGGCCCAGCCGCGCAACCCACCTCCTCGGAGCATTCGACCAGTTCGTCCTTGGTCCCGGAACGAAGGACACTCACATGCTGGCGCATGAGCATCGCCGGCTGGTGAGCAAGGCTGCGGGCTGGATCGCTCCCGTCCTGACCCAGGGAGGGCGGATCACCGGCGTCTGGGAGATGGATGATGGGAATCTTGTCGTTACCCCGTTTCCAGGTGAGCAGGCGCCGCCGTCCCAGGTGCTGGAGGATGCGGCTGCGCGGCTTACAGCGGTGCATGGTTCGGTGAAGGTGACGCCGCGGGTGGACTGA","VLAWRLHRQYVEPLTDTGPVEIVGRLCGVQAQVASAAETAVALRQRNPQPEGVKRAYSDRSLVKTWAMRGTLHAMRSSDVAEYLSLLAGARTWTKPSWSRHFGATPEEVEQLTESVADLLHGQVLSRDELVSELVQDNRFKGMEEQLRSGWGALLKPLAWQGALCYGPSPSSKATFTHPASLLKNWNGLPDPAEAAPAVIKRYLSAYGPATPETFDAWLSRNSNKKSTLRSWFASLGEQIVEVRVEGETRYLLAEHEDELAATRPSRATHLLGAFDQFVLGPGTKDTHMLAHEHRRLVSKAAGWIAPVLTQGGRITGVWEMDDGNLVVTPFPGEQAPPSQVLEDAAARLTAVHGSVKVTPRVD$","Hypothetical protein","Cytoplasm, Periplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1888","2050078","2048612","1467","5.26","-13.89","52434","ATGCTGGATCACAAGGGACCGCCTCCGGTCATCTCCGGGTTCACGTACCTGGAGAGACTCGGAGCGGGAGGCTACTCCACGGTCTACCTCTTCGAGCAGCACATGCCCCGCCGCGAGGTCGCGGTCAAGGTCATGAACGCTGACGTGGAGGACAAGACCGCCTCCCGCTTCGAGTCGGAGGCGAACCTCATGGCGCGGGTCTCCTCCCACCCGGCCATCCTGTCCATCTACGGTGCGGGCGTCTCCGCCGATGGCCACCCCTTCCTGGTCATGGAGTACTGCCCGCCGCCGCAGCTGGGCGCCATCTTGCGCCAGGGTCCCCTCAATGTCGCTGAGACCCTGTCCACGGCGATCCAGATCGCCGGAGCGGTGGAGACCGCTCACCGGGCCGGCATCGTCCACCGGGACATCAAGCCCGCCAACATCCTGTTCACCACGTACCGTCGTCCGGTGCTCTCGGACTTCGGCATCTCCGCCATGAGCGGCCCGGAGGGGACCGAGGAGCTGCGGGGGATGAGTGTGCCCTGGGCCCCGCCCGAGCAGCTGGTCGGGATGCGCTCGGCCAATCCCGCCTCCGACATCTACTCCTTGGGGGCGACCACCTTCGCGATGCTCACGGGGCGCAGCCCCTTCGAGACCGACGGAATCCCGGATGTCTACGAGCTCTCCCGCCGTATCGTCAAGGACCCCCTGCCTCCGCTGGGGCGCCAGGACGCCCCGCCGTCGTTGCACCGCGTGCTGTCGGTGGCGATGGACAAGAACCCGGACTCGCGCTACCCGACGGCGCTGGCCTTCGCCCGCGCGCTTCAGCAGGTCCAGGCCGAGCTCGACCTGCCGATCACGACCGTTGACCTGTTCCAGGAGCCGGACAAGGCCGCGAAGTCGGCTCGGCGCCCCAGTCACGACGAGACCGACACCGCCACGAAGATGGGGGTGTTCAACCAGGTCGATGTCACCAGCGAGCACATCGCCATGCGGGTGGAGCCCGACGGCGAGGACAAGGGCTCGTCGTCGGACTCGGAGGCTGGTGAGACGGGCCGCCCGAACCGCATGCGGGGTGTGCTGACCGGTCTGCTGGTCGTGGCCATGGTGGCGGCCGTCGTCGCTGCGATCGTGGTCTCCCAGAACCAGGACAAGCAGAAGAAGCCCAACAATCCCATTGCCACGATCGCCCCGCAGCCCGACGCCAACCCCCTGCAGGCCTCAGTGCCCATGGTCGGCGATATCGTCGGCGAGGCGCAGGGCGACGGCACGGTGAAGTTCAGCTGGGGTGAGCCGGAGACGAACTGGTCCGGCAGCTACCTCTACCGGGTCAAGCTGCCCGATGAGGAGACCGAGCTGGACTCCGTGCGCACCAATGAGGTCGTCGTCGACGCCCAGCCGGCACGCACCTGCCTCGAGGTCACCGCGGTGCGCTCGGACGGTAAGGCGTCCCCGGCCAAGACCGCCTGCGTCGACACGCCCTGA","MLDHKGPPPVISGFTYLERLGAGGYSTVYLFEQHMPRREVAVKVMNADVEDKTASRFESEANLMARVSSHPAILSIYGAGVSADGHPFLVMEYCPPPQLGAILRQGPLNVAETLSTAIQIAGAVETAHRAGIVHRDIKPANILFTTYRRPVLSDFGISAMSGPEGTEELRGMSVPWAPPEQLVGMRSANPASDIYSLGATTFAMLTGRSPFETDGIPDVYELSRRIVKDPLPPLGRQDAPPSLHRVLSVAMDKNPDSRYPTALAFARALQQVQAELDLPITTVDLFQEPDKAAKSARRPSHDETDTATKMGVFNQVDVTSEHIAMRVEPDGEDKGSSSDSEAGETGRPNRMRGVLTGLLVVAMVAAVVAAIVVSQNQDKQKKPNNPIATIAPQPDANPLQASVPMVGDIVGEAQGDGTVKFSWGEPETNWSGSYLYRVKLPDEETELDSVRTNEVVVDAQPARTCLEVTAVRSDGKASPAKTACVDTP$","Serine/threonine protein kinase","Membrane, Periplasm, Cytoplasm","serine/threonine protein kinase","protein kinase/transcriptional regulator; LuxR family ","protein kinase","","Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995. 9(8):576-596. PMID: 7768349Hunter T. Protein kinase classification. Meth. Enzymol. 1991. 200:3-37. PMID: 1835513Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth. Enzymol. 1991. 200:38-62. PMID: 1956325Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988. 241(4861):42-51. PMID: 3291115Knighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991. 253(5018):407-414. PMID: 1862342","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[14-270]T$	Q6AEZ5_BBBBB_Q6AEZ5;
PF00069	$\"[14-232]T$	Pkinase
PS50011	$\"[14-276]T$	PROTEIN_KINASE_DOM
PS00107	$\"[20-43]T$	PROTEIN_KINASE_ATP

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[132-144]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[84-260]T$	no description
PTHR22986	$\"[14-258]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES
tmhmm	$\"[354-374]?$	transmembrane_regions

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[630-715]T$	FHA
PS50006	$\"[630-693]T$	FHA_DOMAIN

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[195-263]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.20	$\"[628-716]T$	no description

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[279-345]T$	FHA
SM00240	$\"[278-338]T$	FHA
PS50006	$\"[279-338]T$	FHA_DOMAIN

InterPro
IPR010432
Domain

RDD
PF06271	$\"[131-255]T$	RDD

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.20	$\"[277-365]T$	no description
tmhmm	$\"[160-180]?$ $\"[212-234]?$	transmembrane_regions

","BeTs to 4 clades of COG1716COG name: FHA-domain-containing proteinsFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1716 is ------y--dr-bc----s----i--Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 131 to 255 (E_value = 0.0004) place ANA_1890 in the RDD family which is described as RDD family.Residues 279 to 345 (E_value = 3.4e-07) place ANA_1890 in the FHA family which is described as FHA domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1892","2055659","2053749","1911","6.20","-6.79","68140","ATGGCGCACCTGCTCGGCGTGGAGAACCTGCGCCTGACGGTCGGCTCCCGCCTGCTCCTGGACGAGGTCACCCTGGGACTGGAGGACGGCACCCGCGTCGGCGTCCTGGGCCCCAACGGTGCCGGCAAATCCACTTTCCTGGCGGCCCTGGCCGGTCGGCGCGAGCCCGACGGCGGCCGCGTCACCCGCACCGGCGGCGTGAGCGTGGCGGTCCTGAGCCAGGCCGACGACCTGCCGCCGGGCGCCACCGTGCGCACCGCCATCCACGGCCAGGCCCCCGAGCACGAGTGGGCCTCCGACCCGGCTGTGCGTGACATCCACGCCGGGCTCATCGCCGACCTCGACCTGTCTGCCGACGTCGCCACCCTCTCCGGGGGCCAGCGCCGCCGCGTCGCCCTGGCCGCGGTCCTCACTCGCCGCGCCGACGTCGTCATCCTCGACGAGCCCACCAACCACCTCGACGTCGAGGGCGTGGACTGGCTCGCCCGCCACCTGCGGGCCCGCTTCAACGGCCCGGGCGGCCGGGCCTCCGGCGCCCTGGTCACCGTCACCCACGACCGCTGGTTCCTGGACGCCATCTGCACCAACGTGTGGGAGGTCGTCCCCGGCATCGACCCCGGCGGCGGGCGCCCCCAGGTGGCCGGCCGCATCGAGACCTACGACGGCGGCTACGCCGCCTACGTCCTGGCCCGGGCCGAGCGCGCCCGCCAGGCCGCCGTGGCCGCCGTCAAGCGGGAGAACCTCCTGCGCAAGGAGCTGGCCTGGCTGCGTCGCGGCGCCCCCGCCCGCACCTCCAAGCCCCGCTTCCGCATCGATGCCGCCGAGGCCCTCATCGCCGACGTGCCGCCCCCGCGCGACACCGTGGCCCTGACCGCCATGGCCACCGCCCGCCTGGGCAAGAAGGTCCTCGACCTGGAGGACGTCACCGTGCGCTACCCCGGGCCGCCCACTGACACCGGCGAGGCGACCCAGCGGGAGGTCCTGCGCCGCGTCACCTGGCGGCTCGCCCCCGGTGAGCGCGTCGGCGTCGTCGGCGTCAACGGCGCCGGCAAGACCACCCTGCTGCGCCTGCTCGAAGGCGTCCAGGAGCCCACTGAAGGCCGCGTCGCCCGCGGCAAGACCGTTCAGGTGGCCACCCTGTCCCAGTCCACTCACGAGCTCGACGCGCTCGCGGACCTGCGCGTCGTCGAGGCCGTGGCCATGGTGGGGGAGAGAGTCATGGTCGGGGACAAGGAGATGACGGCGGCCCAGCTCGTCGAGCGCCTGGGCTTCACCCGTCAGCGCGCATGGACCCGGGTCGGGGAGGTCAGCGGCGGGGAGCGCCGTCGCCTCCAGCTCCTGCGCCTGCTCATGACCGAGCCCAATGTGCTCCTGCTCGACGAGCCCACCAACGACCTGGACACCGACACCCTGGCTGCCGTCGAGGACATCCTCGACTCCTTCCCCGGCACCCTCGTGGTCGTCTCCCACGACCGCTACCTCCTGGAACGGGTGACCGACCACCAGGTGGCGCTGCTGGGCGATGGCAGCGTGCGTGATCTGCCCGGCGGGGTCGAGCAGTACCTCCAGATGCGCCGCGAGGCCATGGGCGGCGTCGGGGGCCCGAGAACCTCAGCAGGCGCTGCGGCATCCGCGGCGACGCGGACGGCAGGCGAGTCCACCTCTGAGCGCAGCGCCTCGAGCGGGGCCCGCCGGCACGAGGCCCGCAAAGCCCTGGGGCGCATCGAGCGCAAGATGGAGCGTGCGGCTCAGTCCCTCGCCGCCCTGCACGCGCGCATGGAGGAGGTCTCGGCAGACCCGAACCGGGTCGGGGAGCTGGCCGAGCTCGGCCGTGAGCTCGTGGCCGCTGAGGCGACCCACGCCGATCTGGAGGAGCAGTGGCTTGAGGCGGCGGAGGCGCTGGAGGACTGA","MAHLLGVENLRLTVGSRLLLDEVTLGLEDGTRVGVLGPNGAGKSTFLAALAGRREPDGGRVTRTGGVSVAVLSQADDLPPGATVRTAIHGQAPEHEWASDPAVRDIHAGLIADLDLSADVATLSGGQRRRVALAAVLTRRADVVILDEPTNHLDVEGVDWLARHLRARFNGPGGRASGALVTVTHDRWFLDAICTNVWEVVPGIDPGGGRPQVAGRIETYDGGYAAYVLARAERARQAAVAAVKRENLLRKELAWLRRGAPARTSKPRFRIDAAEALIADVPPPRDTVALTAMATARLGKKVLDLEDVTVRYPGPPTDTGEATQREVLRRVTWRLAPGERVGVVGVNGAGKTTLLRLLEGVQEPTEGRVARGKTVQVATLSQSTHELDALADLRVVEAVAMVGERVMVGDKEMTAAQLVERLGFTRQRAWTRVGEVSGGERRRLQLLRLLMTEPNVLLLDEPTNDLDTDTLAAVEDILDSFPGTLVVVSHDRYLLERVTDHQVALLGDGSVRDLPGGVEQYLQMRREAMGGVGGPRTSAGAAASAATRTAGESTSERSASSGARRHEARKALGRIERKMERAAQSLAALHARMEEVSADPNRVGELAELGRELVAAEATHADLEEQWLEAAEALED$","Macrolide-transport ATP-binding protein ABC transporter","Cytoplasm, Membrane","ABC transporter, ATP-binding protein","macrolide-transport ATP-binding protein ABC transporter","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[123-165]T$ $\"[451-478]T$	Q740H7_MYCPA_Q740H7;
PF00005	$\"[30-203]T$ $\"[338-509]T$	ABC_tran
PS50893	$\"[5-227]T$ $\"[303-532]T$	ABC_TRANSPORTER_2
PS00211	$\"[123-137]T$ $\"[436-450]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[29-203]T$ $\"[337-508]T$	AAA

InterPro
IPR003833
Domain

Allophanate hydrolase subunit 1
SM00796	$\"[267-457]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[7-203]T$ $\"[323-511]T$	no description
PTHR19211	$\"[94-599]T$	ATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19211:SF7	$\"[94-599]T$	ABC TRANSPORTER ABCF3, UUP
signalp	$\"[1-15]?$	signal-peptide

InterPro
IPR004424
Family

4-diphosphocytidyl-2C-methyl-D-erythritol kinase
PIRSF010376	$\"[32-326]T$	4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate synthase
PTHR20861:SF2	$\"[76-293]T$	4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE
TIGR00154	$\"[26-326]T$	ispE: 4-diphosphocytidyl-2C-methyl-D-erythr

InterPro
IPR006204
Domain

GHMP kinase
PF00288	$\"[117-175]T$	GHMP_kinases_N

InterPro
IPR013750
Domain

GHMP kinase, C-terminal
PF08544	$\"[233-312]T$	GHMP_kinases_C

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[29-191]T$	no description

noIPR
unintegrated

unintegrated
PTHR20861	$\"[76-293]T$	HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE

","BeTs to 15 clades of COG1947COG name: 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1947 is -------qvdr-bcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB000870 (Homoserine kinase signature) with a combined E-value of 1.7e-07. IPB000870B 133-148 IPB000870E 276-291 IPB000870B 131-146","","","-47% similar to PDB:1OJ4 TERNARY COMPLEX OF 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE (E_value = 1.0E_15);-37% similar to PDB:1UEK Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase (E_value = 6.6E_15);-56% similar to PDB:1QIU A TRIPLE BETA-SPIRAL IN THE ADENOVIRUS FIBRE SHAFT REVEALS A NEW STRUCTURAL MOTIF FOR BIOLOGICAL FIBRES (E_value = 6.6E_15);-65% similar to PDB:1X4E Solution structure of RRM domain in RNA binding motif, single-stranded interacting protein 2 (E_value = 6.6E_15);","Residues 117 to 175 (E_value = 2.6e-13) place ANA_1893 in the GHMP_kinases_N family which is described as GHMP kinases N terminal domain.Residues 233 to 312 (E_value = 2.1e-11) place ANA_1893 in the GHMP_kinases_C family which is described as GHMP kinases C terminal.","","kinase (ispE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1894","2057736","2056642","1095","6.44","-1.83","37436","ATGACGTTGCCGGCCCCCGATTCACAGGTGCCCCCGGCAGGAGCCGCCCCCATCGACGGGCCCGACCCTGCAGGAGCCTGTGAGGCCACCTCCGAGACCCCCGCAGATGCCGCCCGAGCGGAGCACACCCACCAGGCCCCCCGGGATCCTGAGGATCACGGCGCCTCCGCGGGCTCCCGGGCCGCCGGCCTCCTGGGCCCCGCTGAGGTCCGCGGCCTGTCCCAGGCGCTGGGCATCCGCCCCACCAAGACGCTGGGGCAGAACTTCGTCCACGACGCCGGCACCGTGCGCCGCATCGTCAGGAGTGCGGGCGTGCGCCCCCAGGACACGGTCCTGGAGATCGGGCCGGGCCTGGGCTCCCTGACCCTGGCCCTCCTGGAGGCCGGGGCGCGAGTGGTCGCCGTCGAGATTGACCCCGCCCTGGCCCGGGCGCTGCCTGTCACCGTCGCCGACCGCATGCCGCCGGCCGCCGGCCGCCTGACCCTCATCCAGGCCGACGCGTTGAGCATCACCGGCCCGGACTCGCTGGGCGATGCCGGGGCCCCTCCCACCCGCCTCGTGGCGAACCTGCCCTACAACGTGGCCGTCCCCGTTCTGCTCACCGCGCTGGAGGCCCTGCCCAGCCTGGAGAGCGTCACCGTCATGGTCCAGGCCGAGGTCGCCGACCGCCTCGCCGCCGAACCCGGCTCGCGGACCTACGGGGTCCCCAGCGTCAAGGCCGCCTGGTACGCGGCCGCCCGCCGCACCCTGACCATCTCCCGCCACGTCTTCTGGCCCGTGCCCAACGTCGACTCCGCCCTCGTCGAGCTCGTGCGCCGTCGTCCCCCCACCACGCGCGCCAGCCGCGAGCAGGTCTTCGCCGTGGTTGATGCCGCCTTCGCCCAGCGCCGCAAGACCCTGCGCAAGGCCCTGGCCAGGCTCGCCGGAGGGGCCGACGCCGCCGAGTCCGCCCTGCGCGCCGCCGGCATCGACCCGACGCGGCGCGGCGAGACCCTCGACATCACCGCCTTCGCCGCCCTGGCCGAGGTGCTGCAGCCCGTCGCCGCCGATGGGACCGCCGCGCCAACGCCTCCCACCTCACAGGAGCAGTCATGA","MTLPAPDSQVPPAGAAPIDGPDPAGACEATSETPADAARAEHTHQAPRDPEDHGASAGSRAAGLLGPAEVRGLSQALGIRPTKTLGQNFVHDAGTVRRIVRSAGVRPQDTVLEIGPGLGSLTLALLEAGARVVAVEIDPALARALPVTVADRMPPAAGRLTLIQADALSITGPDSLGDAGAPPTRLVANLPYNVAVPVLLTALEALPSLESVTVMVQAEVADRLAAEPGSRTYGVPSVKAAWYAAARRTLTISRHVFWPVPNVDSALVELVRRRPPTTRASREQVFAVVDAAFAQRRKTLRKALARLAGGADAAESALRAAGIDPTRRGETLDITAFAALAEVLQPVAADGTAAPTPPTSQEQS$","Dimethyladenosine transferase","Cytoplasm","Dimethyladenosine transferase(S-adenosylmethionine-6-N',N'-adenosyl(rRNA)","putative dimethyladenosine transferase ","dimethyladenosine transferase","","O'farrell H.C., Scarsdale J.N., Rife J.P. Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli. J. Mol. Biol. 2004. 339(2):337-353. PMID: 15136037Schubot F.D., Chen C.J., Rose J.P., Dailey T.A., Dailey H.A., Wang B.C. Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription. Protein Sci. 2001. 10(10):1980-1988. PMID: 11567089Mcculloch V., Shadel G.S. Human mitochondrial transcription factor B1 interacts with the C-terminal activation region of h-mtTFA and stimulates transcription independently of its RNA methyltransferase activity. Mol. Cell. Biol. 2003. 23(16):5816-5824. PMID: 12897151","","","

InterPro
IPR001737
Family

Ribosomal RNA adenine methylase transferase
PTHR11727	$\"[73-345]T$	DIMETHYLADENOSINE TRANSFERASE
PF00398	$\"[78-340]T$	RrnaAD
SM00650	$\"[95-274]T$	rADc
PS01131	$\"[111-138]T$	RRNA_A_DIMETH

InterPro
IPR011530
Family

RRNA 16S rRNA dimethylase
TIGR00755	$\"[79-344]T$	ksgA: dimethyladenosine transferase

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.100	$\"[276-348]T$	no description
G3DSA:3.40.50.150	$\"[87-276]T$	no description

","BeTs to 26 clades of COG0030COG name: Dimethyladenosine transferase (rRNA methylation)Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0030 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB011530 (RRNA 16S rRNA dimethylase) with a combined E-value of 3.7e-43. IPB011530A 85-125 IPB011530B 186-199 IPB011530C 214-242***** IPB001737 (Ribosomal RNA adenine dimethylase) with a combined E-value of 3.8e-39. IPB001737A 82-90 IPB001737B 99-134 IPB001737C 186-198 IPB001737D 214-223 IPB001737E 252-270","","","-49% similar to PDB:1ZQ9 Crystal structure of human Dimethyladenosine transferase (E_value = 1.1E_21);-51% similar to PDB:1QYR 2.1 Angstrom Crystal structure of KsgA: A Universally Conserved Adenosine Dimethyltransferase (E_value = 1.6E_20);-47% similar to PDB:2H1R Crystal structure of a dimethyladenosine transferase from Plasmodium falciparum (E_value = 6.8E_16);","Residues 78 to 340 (E_value = 1.8e-38) place ANA_1894 in the RrnaAD family which is described as Ribosomal RNA adenine dimethylase.Residues 112 to 167 (E_value = 1.8e-05) place ANA_1894 in the Methyltransf_12 family which is described as Methyltransferase domain.","","transferase (S-adenosylmethionine-6-N,N-adenosyl(rRNA) dimethyltransferase) (16S rRNA dimethylase) (Highlevel kasugamycin resistance protein ksgA) (Kasugamycindimethyltransferase) (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1895","2058708","2057866","843","5.04","-6.62","27954","ATGCGCACCATCGCGCTGCGCGCCGGCCTGGCGGCTCTGGCCCTGTCGGTCGCGGTCTCCGGGGCCGCGTACGCCGCTGTCCGCGCGGGGGAGCCCTCGCGCACCTCCGGTGTCGAGGCGGACGCGAAGGGCACCGATGGTCTGGGGGCTGAAGGCGGTCGCAGCCGAGTCTCGGTCACGCCGAGTACCCAGAAGGTCACCACCGAGACGGTCGAAGCCGCCGACCCCCACGGGTCGGTCCAGCAGGAGAGCAGCGATCTGTCTGAAGGCGAGACCAAGGTGGCCACGGCGGGTGTCGACGGCGTCGTGCGCACCACCTACGAGGTCACCACCGTGGGCGGCAAGGAGGTCTCCCGCACTCCCGTCGCCCAGGTCGTCGTCACCCAGAAGGTCGATGAGGTCGTTCTGGTGGGCACCGGGGCGGCCAAGAAGCAGGAGAGCAAGCCGGAACAGTCTCAGGGGCAGGGCCAGTCTCAGTCTCAGGGGCAGGGCCAGTCTCAGTCTCAGGGGCAGGGTCAGACTCAGGCACCCTCGGAGTCCTCCGGAGGTTCTGGCGGTTCGGCGTCCGGCGGCAGTGCCGGCACGACCGGCGGCGGTGCCGGAGACGACGGTGTCTGGGCCCAGCTCGCCCAGTGCGAGTCCGGTGGCAACCCGGCAACCAACACCGGCAACGGTTTCTACGGCATGTACCAGTTCACCCTGGAGACCTGGCAGTCCCTGGGCGGAACCGGCTACCCCCACGAGGCCGATGCCGCCACCCAGACCGCCATGGCCAAGAAGCTTCAGGCCCAGGCCGGCTGGGGCCAGTGGCCCGGCTGCGCCGACAAGCTCGGCCTGCGCTGA","MRTIALRAGLAALALSVAVSGAAYAAVRAGEPSRTSGVEADAKGTDGLGAEGGRSRVSVTPSTQKVTTETVEAADPHGSVQQESSDLSEGETKVATAGVDGVVRTTYEVTTVGGKEVSRTPVAQVVVTQKVDEVVLVGTGAAKKQESKPEQSQGQGQSQSQGQGQSQSQGQGQTQAPSESSGGSGGSASGGSAGTTGGGAGDDGVWAQLAQCESGGNPATNTGNGFYGMYQFTLETWQSLGGTGYPHEADAATQTAMAKKLQAQAGWGQWPGCADKLGLR$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein","Transglycosylase domain protein","","Bateman A., Holden M.T., Yeats C. The G5 domain: a potential N-acetylglucosamine recognition domain involved in biofilm formation. Bioinformatics 2005. 21(8):1301-1303. PMID: 15598841","","","

InterPro
IPR010618
Domain

Transglycosylase-like
PF06737	$\"[200-274]T$	Transglycosylas

InterPro
IPR011098
Domain

G5
PF07501	$\"[65-141]T$	G5
PS51109	$\"[59-141]T$	G5

noIPR
unintegrated

unintegrated
G3DSA:1.10.530.10	$\"[195-280]T$	no description
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[9-27]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-62% similar to PDB:1XSF Solution structure of a resuscitation promoting factor domain from Mycobacterium tuberculosis (E_value = 8.1E_16);-43% similar to PDB:1RP5 PBP2x from Streptococcus pneumoniae strain 5259 with reduced susceptibility to beta-lactam antibiotics (E_value = 8.1E_16);-42% similar to PDB:1K25 PBP2x from a Highly Penicillin-resistant Streptococcus pneumoniae Clinical Isolate (E_value = 8.1E_16);-50% similar to PDB:2I0Z Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases (E_value = 8.1E_16);","Residues 65 to 141 (E_value = 1.1e-11) place ANA_1895 in the G5 family which is described as G5 domain.Residues 200 to 274 (E_value = 5e-30) place ANA_1895 in the Transglycosylas family which is described as Transglycosylase-like domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1896","2060049","2058982","1068","5.51","-5.89","35957","TTGGCACGCCCCTGGGTCATCGGTTACGGTGACACGCAGTCGTCAAACGAAGGAAGTTCTATCGTGGGTCGTCACTCCCAGACCAGCTCCCTGAGTACTACACTCTCCGGCCTTGGCTCCTTGGCCACCAAGAAGCGGACCGCCTCCGGTGGTCACGGCCGTCGTCGCGCCGAGGGGCCCGCCAAGACCTCCCTGACCCCCATGCTCTTCAAGGCAGGGGGTGCAGCTGCGGCCTTCTCCCTGGCGGTCTCCGGTGCCGCCTACGCGGCCATCTCCGCAGGGGATGACGAGGGTAGCTCCTCCGCGGGCGGTTCCTTCGGGCTGATCGGTGGTGAGTCGGACGGACAGGCCAAGGCCGCCGCCACACCGAAGGCCGGCGCCGGCAAGATCGCCAGCGCCCAGACCTCTACCACCACCGTCGACGAGCCGCAGGTTCACAGTACGGTGAAGAAGGAGACCGGCTCCCTGCCCAAGGGTGAGACCAAGGTTGAGACCGCCGGCGTTGATGGTCTCGTGCGCACCACCTACGAGGTCACCACTCAGGACGGCAAGGAGGTCTCCCGCACCCCGGTCGCCCAGGTCGTCGTCACCAAGAAGGTGGACGAGGTCGTCCTGGTGGGCACCGGCGAGCAGCAGGCCCAGCAGGAGGCCGCCCAGCAGGCTCAGTCGGCCGGTGACGGTCAGGCCGCCCAGGCCAACGGGGGCAGTGAGGGCTCGAACAGCAGCACTCCGGCGCCCGCGGCCAACCCCGGTGCGGGGACCGACCCCGACAGTGCCAAGGCCATCGCCCGCTCCATGATGGCCGGCCACGGTTGGGGGGACTCCGAGTTCTCCTGCCTGGAGAGCCTGTGGACCCGTGAGTCCAGCTGGAACTACCAGGCCGAGAACGCCTCCTCGGGCGCCTACGGCATCCCCCAGGCGCTGCCCGGCACCAAGATGAGCGAGGTCGCCGACGACTGGGCCACCAACCCCACCACCCAGATCACCTGGGGCCTGAACTACATCTCCGGCCGCTACGGCACCCCCTGCTCGGCCTGGGCTCACTCCGAGTCCGTCGGCTGGTACTGA","LARPWVIGYGDTQSSNEGSSIVGRHSQTSSLSTTLSGLGSLATKKRTASGGHGRRRAEGPAKTSLTPMLFKAGGAAAAFSLAVSGAAYAAISAGDDEGSSSAGGSFGLIGGESDGQAKAAATPKAGAGKIASAQTSTTTVDEPQVHSTVKKETGSLPKGETKVETAGVDGLVRTTYEVTTQDGKEVSRTPVAQVVVTKKVDEVVLVGTGEQQAQQEAAQQAQSAGDGQAAQANGGSEGSNSSTPAPAANPGAGTDPDSAKAIARSMMAGHGWGDSEFSCLESLWTRESSWNYQAENASSGAYGIPQALPGTKMSEVADDWATNPTTQITWGLNYISGRYGTPCSAWAHSESVGWY$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein","G5 domain protein","","Bateman A., Holden M.T., Yeats C. The G5 domain: a potential N-acetylglucosamine recognition domain involved in biofilm formation. Bioinformatics 2005. 21(8):1301-1303. PMID: 15598841","","","

InterPro
IPR011098
Domain

G5
PF07501	$\"[132-210]T$	G5
PS51109	$\"[130-210]T$	G5

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-53% similar to PDB:2AF5 2.5A X-ray Structure of Engineered OspA protein (E_value = );-53% similar to PDB:2FKG The Crystal Structure of Engineered OspA (E_value = );-53% similar to PDB:2FKJ The crystal structure of engineered OspA (E_value = );","Residues 132 to 210 (E_value = 2.1e-15) place ANA_1896 in the G5 family which is described as G5 domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1897","2061178","2060306","873","5.08","-16.26","30961","TTGGCGGCTCCGGTCACCGACAACCACACGCACCTACCGGTCGCGGCGGACGCCGGCGGCCCCGGCTCCGAGGCGCCACTGAGCGCCGCGGAGCTGGTCGAGCGCGCCGCCGCCGTGGGCGTGACCCGCGTGGTGACCTCCGCCTGCGAGGTCACCACCTGGCGGGAGAGCCTGGCCCTGGCCCGTGAGCTGCCGGGAGTGCGCGTGGCCCTGGCCGTGCACCCCAACGAGGCCGTCCTGCACGCCGGGGTGCGCGAGACCGGCCCCGACGGGCTCGAGCCGCGGGCTCAGGAGCACCATGCCGAGCCGCTCGAGGAGGTCATGGTGCGCCTGGAGGAGACGCTCAGGGCGAACGCCGACGTCGTCGTCGCCGTCGGGGAGAGCGGCCTGGATTTCTTCCGCACCGGTGAAAAGGGGGTCGTCGCCCAGCGTGAGGCCTTCCGGGCGCACATTGCCCTGGCCAAGGACCTCGACCTGCCCCTGCAGATCCACGACCGTGACGCGCACGCCGCCTGCGTGGAGGTCCTCGAGGCCGACGGTGTCCCCGAGCACACCGTCTTCCACTGCTTCTCAGGTGGGCCGCAGCTGGCCGCCGCCTGTGCTGAGCACGGCTGGTACGCCTCCATCGCGGGCCCGCTCACCTACCCGGCCAACGACTCTCTGCGGGAGGCGGTCGCCGCCCTGCCCGAGGCGCTGCTCCTGGTGGAGACCGACGCCCCCTACCTCCCGCCCAAGCGCTGGCGCGGCCGCCCCAATGCCTCCTACCTGCTGGGTGACACGGTCCGCTTCCTGGCTGAGCAGCGGGGCCTGAGTGAGGAAGACCTCTGCCGGCGTCTGCAGGCCACCACCGAAGCGGTCTACGGGGCCTGGTGA","LAAPVTDNHTHLPVAADAGGPGSEAPLSAAELVERAAAVGVTRVVTSACEVTTWRESLALARELPGVRVALAVHPNEAVLHAGVRETGPDGLEPRAQEHHAEPLEEVMVRLEETLRANADVVVAVGESGLDFFRTGEKGVVAQREAFRAHIALAKDLDLPLQIHDRDAHAACVEVLEADGVPEHTVFHCFSGGPQLAAACAEHGWYASIAGPLTYPANDSLREAVAALPEALLLVETDAPYLPPKRWRGRPNASYLLGDTVRFLAEQRGLSEEDLCRRLQATTEAVYGAW$","TatD-related deoxyribonuclease","Cytoplasm, Extracellular","deoxyribonuclease","putative deoxyribonuclease ","TatD-related deoxyribonuclease","","Wexler M., Sargent F., Jack R.L., Stanley N.R., Bogsch E.G., Robinson C., Berks B.C., Palmer T. TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export. J. Biol. Chem. 2000. 275(22):16717-16722. PMID: 10747959Weiner J.H., Bilous P.T., Shaw G.M., Lubitz S.P., Frost L., Thomas G.H., Cole J.A., Turner R.J. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 1998. 93(1):93-101. PMID: 9546395","","","

InterPro
IPR001130
Family

TatD-related deoxyribonuclease
PTHR10060	$\"[35-92]T$ $\"[113-289]T$	TATD DNASE-RELATED
PF01026	$\"[4-288]T$	TatD_DNase
PS01091	$\"[224-240]T$	TATD_3

InterPro
IPR012278
Family

Mg-dependent DNase, TatD
PIRSF005902	$\"[5-289]T$	Mg-dependent DNase, TatD type

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.140	$\"[5-287]T$	no description

","BeTs to 23 clades of COG0084COG name: Mg-dependent DNaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0084 is --m-kzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001130 (TatD-related deoxyribonuclease) with a combined E-value of 2.6e-43. IPB001130A 5-13 IPB001130C 122-132 IPB001130D 143-178 IPB001130E 186-215 IPB001130F 228-250","","","-48% similar to PDB:1J6O Crystal structure of TatD-related deoxyribonuclease (TM0667) from Thermotoga maritima at 1.8 A resolution (E_value = 3.6E_22);-54% similar to PDB:1YIX Crystal structure of YCFH, TATD homolog from Escherichia coli K12, at 1.9 A resolution (E_value = 8.3E_19);-50% similar to PDB:2GZX Crystal Structure of the TatD deoxyribonuclease MW0446 from Staphylococcus aureus. Northeast Structural Genomics Consortium Target ZR237. (E_value = 8.3E_19);-41% similar to PDB:1ZZM Crystal structure of YJJV, TATD Homolog from Escherichia coli k12, at 1.8 A resolution (E_value = 2.1E_14);-43% similar to PDB:1XWY Crystal structure of tatD deoxyribonuclease from Escherichia coli K12 at 2.0 A resolution (E_value = 4.7E_14);","Residues 4 to 288 (E_value = 2.3e-69) place ANA_1897 in the TatD_DNase family which is described as TatD related DNase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1898","2063085","2061238","1848","5.02","-28.22","67610","ATGACCCACATCCTGTCCGCAGTCGCCTGGCCGTACGCCAACGGCCCGCGTCACATCGGCCACGTCGCCGGCTTCGGTGTTCCCTCTGACGTCTTCTCGCGCTACATGCGCATGGCCGGTCATGACGTCCTCATGGTCTCGGGCACCGATGAGCACGGCACCCCGATCCTCGTCGCCGCCGACGAGGAGGGCCTCAGTGCCCGTGAGCTCGCCGACCGCAACAACCGGCTCATCGTCGAGGACCTCGTGGCCCTGGGCCTGTCCTACGACCTGTTCACCCGCACCACCGCCGGAAACCACTACCACGTGGTCCAGGACATGTTCACCACCGTGCGGGACAACGGCTACATGGTCCAGCAGGTGACCCGCTCGGCGATCTCCCCCTCCACCGGGCGCACCCTCCCCGACCGCTACATCGAGGGCACCTGCCCGATCTGCGGCGCCGACGGCGCCCGCGGGGACCAGTGCGACACCTGCGGCAACCAGCTCGACCCCACCGACCTCATCAGCCCACGCTCGCGGATCAACGGTGAGACCCCCGAGTTCGTGGAGACCACTCACTGGTTCCTCGACCTGCCCGCCCTGGCTCAGGCCCTGGGTGCCTGGCTCGACGAGCGCGAGGCCTCCGGCACCTGGCGGCCCAACGTCATCAAGTTCTCCCAGAACCTTCTGGGGGACATCCGCCCGCGCGCCATGACCCGGGACATCGACTGGGGCATCCCGGTGCCCGGCTGGGAGGACCAGCCCACCAAGCGCCTCTACGTCTGGTTCGACGCCGTTATCGGATACCTGTCCGCCTCCGTGGAGTGGGCGCGCCGCAGTGGCGACCCCGAGGCGTGGCGTGCCTGGTGGAACGACCCCCAGGCCCTGTCTTACTACTTCATGGGCAAGGACAACATCGTCTTCCACTCCCAGATCTGGCCCGCCGAGCTCCTGGGCTACAACGGCCAGGGCGCTGCCGGCGGCGAGCCCGGGCGCCTGGGCGTGCTCAACCTGCCCACCGAGGTCGTCTCCAGCGAGTTCCTCACCATGGAGGGCAAGAAGTTCTCCTCCTCCCACGGCATCGTCATCTATGTGCGTGACTTCCTCGAGCGCTACCAGGCCGACGCCCTGCGCTACTTCATCTGCGCGGCCGGTCCGGAGACCGCGGACGCGGACTTCACCTGGGCGGAGTTCGTACGGCGCACCAACGGCGAGCTCGTGGCCGGCTGGGGCAACCTGGTCAACCGCACCGCCTCCATGATCCACAAGCGCTTCGGGCAGATCCCCGAGCCCGCCGAGCTGGAGGACATCGACCGGGCCCTGCTCGACGCCGTCGAGGCCGGTTTCGCCTCCGTGGGCGACCTCATCGCCCAGCACCGCCAGAAGGCGGCCCTGGGGGAGGCGATGCGCCTGGTCGGCGAGGCCAACAAGTACGTGGCCGACACCCAGCCCTTCAAGCTCAAGGGCGAGGACCCCGCCACCCAGGCCCGCCTGGCCACGGTCCTGCACACGCTGGCCCAGGCGGTCACCGACCTCAACCTCATGCTCTCGCCCTTCCTGCCGCACGCCGCCAACGACGTCGACCGGGTCCTGGGCGGAAGCGGCCGGATCGCACCGATGCCTCGCATCGAGGAGGTCGACGAGCTCGACCCCGACCACCTGCCCGAGGCCTTCGACGGTCGCTCCGGCTACCCGATCATCACCGGCGACTACCAGGACGCCCCCACCTGGGGGCGCCACCCGGTGACCGTCGGCACTCCCGTGGCCAAGCCGGCCCCGGTGTTCACCAAGCTGGACGAGTCGATCGTCGAGGCCGAGCTGGCCCGTTACGCCGACTCCGTGCCCGACGACGTCACCGGCTCCTGA","MTHILSAVAWPYANGPRHIGHVAGFGVPSDVFSRYMRMAGHDVLMVSGTDEHGTPILVAADEEGLSARELADRNNRLIVEDLVALGLSYDLFTRTTAGNHYHVVQDMFTTVRDNGYMVQQVTRSAISPSTGRTLPDRYIEGTCPICGADGARGDQCDTCGNQLDPTDLISPRSRINGETPEFVETTHWFLDLPALAQALGAWLDEREASGTWRPNVIKFSQNLLGDIRPRAMTRDIDWGIPVPGWEDQPTKRLYVWFDAVIGYLSASVEWARRSGDPEAWRAWWNDPQALSYYFMGKDNIVFHSQIWPAELLGYNGQGAAGGEPGRLGVLNLPTEVVSSEFLTMEGKKFSSSHGIVIYVRDFLERYQADALRYFICAAGPETADADFTWAEFVRRTNGELVAGWGNLVNRTASMIHKRFGQIPEPAELEDIDRALLDAVEAGFASVGDLIAQHRQKAALGEAMRLVGEANKYVADTQPFKLKGEDPATQARLATVLHTLAQAVTDLNLMLSPFLPHAANDVDRVLGGSGRIAPMPRIEEVDELDPDHLPEAFDGRSGYPIITGDYQDAPTWGRHPVTVGTPVAKPAPVFTKLDESIVEAELARYADSVPDDVTGS$","Methionyl-tRNA synthetase","Cytoplasm","methionyl-tRNA synthetase","methionyl-tRNA synthetase ","methionyl-tRNA synthetase","","Fong D.H., Yim V. H., D'Elia M.A., Brown E.D., Berghuis A.M. Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism. Biochim. Biophys. Acta 2006. 1764(1):63-69. PMID: 16344011","","","

InterPro
IPR002304
Domain

Methionyl-tRNA synthetase, class Ia
TIGR00398	$\"[4-538]T$	metG: methionyl-tRNA synthetase

InterPro
IPR013991
Domain

PhnA protein N-terminal, proteobacterial
SM00782	$\"[133-164]T$	no description

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[3-403]T$	no description

InterPro
IPR014758
Domain

Methionyl-tRNA synthetase, class Ia, N-terminal
PR01041	$\"[6-19]T$ $\"[39-53]T$ $\"[87-98]T$ $\"[253-264]T$ $\"[293-308]T$ $\"[399-410]T$	TRNASYNTHMET

InterPro
IPR015413
Domain

tRNA synthetase class I (M)
PF09334	$\"[4-412]T$	tRNA-synt_1g

noIPR
unintegrated

unintegrated
G3DSA:1.10.730.10	$\"[404-545]T$	no description
PTHR11946	$\"[9-529]T$ $\"[569-607]T$	ISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES
PTHR11946:SF1	$\"[9-529]T$ $\"[569-607]T$	METHIONYL-TRNA SYNTHETASE

","BeTs to 26 clades of COG0143COG name: Methionyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0143 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002304 (Methionyl-tRNA synthetase signature) with a combined E-value of 6.8e-37. IPB002304A 6-19 IPB002304B 39-53 IPB002304C 87-98 IPB002304D 253-264 IPB002304E 293-308 IPB002304F 399-410***** IPB013155 (tRNA synthetase, valyl/leucyl, anticodon-binding) with a combined E-value of 2.2e-13. IPB013155B 11-53 IPB013155G 229-243 IPB013155H 346-372***** IPB002547 (t-RNA-binding region) with a combined E-value of 7.6e-12. IPB002547A 12-21 IPB002547B 27-38 IPB002547C 254-263","","","-59% similar to PDB:1RQG Methionyl-tRNA synthetase from Pyrococcus abyssi (E_value = 6.2E_111);-49% similar to PDB:1F4L CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE (E_value = 4.6E_66);-49% similar to PDB:1P7P Methionyl-tRNA synthetase from Escherichia coli complexed with methionine phosphonate (E_value = 4.6E_66);-49% similar to PDB:1PFU METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH METHIONINE PHOSPHINATE (E_value = 4.6E_66);-49% similar to PDB:1PFV METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH DIFLUOROMETHIONINE (E_value = 4.6E_66);","Residues 4 to 412 (E_value = 4.2e-190) place ANA_1898 in the tRNA-synt_1g family which is described as tRNA synthetases class I (M).","","synthetase (metG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1900","2063185","2064417","1233","6.75","-0.52","41936","GTGCGGCTCCCGCCCGGTGATTGTTCCGACATATCGACACCTCCTGTGAGGTCTCGGGTGCGCTGCGAGCTTCCAGCATCGCGTTGCTGCCGTGCACGCCGTCATGATGTGTTCCCACGCGCCTCTCACGGACACGATGGACCAGAAAGGCCAGTTATGTCCCAGTACCCCGGCTCCCAGTACCCAGCGAGCTCAGCAGGCTGGTCGGCCAACGGCTACGACCCGGCTCTCGCCGGCGGTCAGCCTCAGCCCTCGCAGTACCCGCCGGCCGCCCCGTTCCAGTCGCCTCAGGGCGGTTACTCAGGTGCCGCGAGCCAGCCGACGACGTCCAGGAGCCTGGCCGCCCCGACAGCCTTGGCGGCGGCCGGCCTGGCCATCCTCCTCATCGCCATCATCGGCGGAATCGGCTCGGCGGTCACCCGCGGCCAGTACAACGCCACCATCACCGACCTGCCAGGCGACCAGGCCGCCACGGTGAAGCTGGACAAGGGCAGCACCTACGGGCTGTTCTACAGCGACGGCGACGACGCTCCGGAGTGCTCGGTGACCTCTCCTGATGGCGACGACGTCAACACGAAGTCCAGCTCGTCATCCACGAAGGTCAAGGGCGGCAAGCTCTTCTCGACCTTCTCCTCCCAGAAGTCTGGCGCCTACACCGTTGACTGCAACAGCACGGCGGGAGTCTCCATGGGTGAGATCATCGCCCCCTCGTCGGCAACGGCCACTCTGATGTCCCTGTTCGGGGTTGTCGGCGCGATCATTATGGCGGTGGTGGGCCTGGCGATGGGCGCCGGCGGCATGGCCTGGCGCTCCAAGCTGGCAGCCGCCGGTACGGCTCCGACCACGGCGGGCGAGGCCTTCAGCACGACGAGCGGCGCGGCGCCCGGGACCCCGACGGTCTACACCCAGGGGGCCTGGCAGTCCGACCAGCAGCCCCAGGCGGCGCAGTACGCTCAGCAGCCCCAGTACCAGCAGCCCGAGCCGGCCCCCCAGCAGGCCCCTTACGCAGCTTCGGCCGCGGGAGCGGGAGCCCAGCCCCAGTACTCGCAGGTGGCCCCGACCGCCCAGTTCGGGTGGACAGGGCAGCAGCAGGCTCAGCAGCAGCCTCAGGCCGCGCAGCCCTCGGTCTTCACTCAGCCCATGCAGCAGGGCCAGCAGGGCCAGTACAACCCGCAGGCGCAGCCCGGGCAGCCCGGCCAGTACCAGCAGCCCGGCGGCTGGCCGGCCCAGTAG","VRLPPGDCSDISTPPVRSRVRCELPASRCCRARRHDVFPRASHGHDGPERPVMSQYPGSQYPASSAGWSANGYDPALAGGQPQPSQYPPAAPFQSPQGGYSGAASQPTTSRSLAAPTALAAAGLAILLIAIIGGIGSAVTRGQYNATITDLPGDQAATVKLDKGSTYGLFYSDGDDAPECSVTSPDGDDVNTKSSSSSTKVKGGKLFSTFSSQKSGAYTVDCNSTAGVSMGEIIAPSSATATLMSLFGVVGAIIMAVVGLAMGAGGMAWRSKLAAAGTAPTTAGEAFSTTSGAAPGTPTVYTQGAWQSDQQPQAAQYAQQPQYQQPEPAPQQAPYAASAAGAGAQPQYSQVAPTAQFGWTGQQQAQQQPQAAQPSVFTQPMQQGQQGQYNPQAQPGQPGQYQQPGGWPAQ$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[119-139]?$ $\"[215-235]?$ $\"[241-261]?$	transmembrane_regions

InterPro
IPR000868
Family

Isochorismatase hydrolase
G3DSA:3.40.50.850	$\"[12-199]T$	no description
PF00857	$\"[12-195]T$	Isochorismatase

noIPR
unintegrated

unintegrated
PTHR11080	$\"[82-196]T$	PYRAZINAMIDASE/NICOTINAMIDASE
PTHR11080:SF2	$\"[82-196]T$	PYRAZINAMIDASE/NICOTINAMIDASE

","BeTs to 16 clades of COG1335COG name: Amidases related to nicotinamidaseFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1335 is ao-pkzyqv-rlb-efg-snuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB000868 (Isochorismatase hydrolase family) with a combined E-value of 2.3e-16. IPB000868A 16-26 IPB000868B 122-173","","","-52% similar to PDB:1ILW Crystal Structure of Pyrazinamidase/Nicotinamidase of Pyrococcus horikoshii (E_value = 4.3E_20);-52% similar to PDB:1IM5 Crystal Structure of Pyrazinamidase of Pyrococcus horikoshii in Complex with Zinc (E_value = 4.3E_20);-42% similar to PDB:2H0R Structure of the Yeast Nicotinamidase Pnc1p (E_value = 2.4E_10);","Residues 12 to 195 (E_value = 1.7e-05) place ANA_1901 in the Isochorismatase family which is described as Isochorismatase family.","","(PZase) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1902","2066185","2065211","975","5.60","-6.60","33855","ATGACTGAGAGCAGCCCGCCCGCACCAGCCGCCACCGTCGAGGGCGGCCACGACGACACCCCCGGCCCGGGCGACCTGCCCGAATCCGCTGCTGCGGGTGACGCCTCAGCTCCTGCCGCTCACAGCCCGGATCTGCGCGGCGGGACGATTACCCTGGCCGCCACTCCGATCGGCAACGTCTCCGACGCCTCCCTGCGTCTGCGCCGTGCCCTGGAGCAGGCCGACCTCATCGCCGCCGAGGACACCCGCCGGCTGCGGTCCCTGGCTCAGCGCCTCGACGTCGAGCCCCGTGGGCGCGTCATCGCCTTCCACGAGCACAATGAGCGCGAGCGTGCCGCCGAGCTGCTCGAGGCTGCCCGCGCCGGCCTGCGCGTCCTGGTGGTCTCGGACGCCGGGATGCCCTCGGTCTCCGACCCCGGGTACCGGCTCGTCCAGGCGGCGGTGCGAGAGCAGGTGCCCGTCACGGTCGCACCGGGCCCCTCAGCGGTGCTGACCGCCCTGGCCCTGTCCGGACTGGCCTCCGACCGGTTCTGCTTCGAGGGTTTCCTGCCGCGCAAACCGGGGGAGCGGCGTCGTGCCCTGGAGTCCCTAGCCACCCAGGAGCGCACCATGATCTTCCTGGAGTCCCCCCGCCGCGTCCACGACTCCCTGGCCGCCATGGCCGAGGTCCTCGGCACTGATCGCCCCGCGGCACTGTGCCGGGAGCTGACCAAGACCCATGAGCAGGTGCTGCGGGCCCCCTTGTCCGAGCTGGCCCGGGCCACGGCCGACGGCGTCCTGGGGGAGGTGGTCCTCGTGGTCGCCGGAGCCGAGCCCGTCGTCGCCAGTCCTGAGGCCGCCGCGCGCAAGGCCCTGGCGCTGGCCGAGGCCGGCATGCGCCTCAAGGCGGCCGCGGCCCTGGCGGCCGGTGAGGCCGGTCTGCGCCCCAACGAGGTCTACCGTGCGGCCTTGGAGCTGCGTGACACCGCAGACTGA","MTESSPPAPAATVEGGHDDTPGPGDLPESAAAGDASAPAAHSPDLRGGTITLAATPIGNVSDASLRLRRALEQADLIAAEDTRRLRSLAQRLDVEPRGRVIAFHEHNERERAAELLEAARAGLRVLVVSDAGMPSVSDPGYRLVQAAVREQVPVTVAPGPSAVLTALALSGLASDRFCFEGFLPRKPGERRRALESLATQERTMIFLESPRRVHDSLAAMAEVLGTDRPAALCRELTKTHEQVLRAPLSELARATADGVLGEVVLVVAGAEPVVASPEAAARKALALAEAGMRLKAAAALAAGEAGLRPNEVYRAALELRDTAD$","Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase","Cytoplasm","conserved hypothetical protein TIGR00096","protein of unknown function UPF0011","Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase","","Raux E., Schubert H.L., Warren M.J. Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum. Cell. Mol. Life Sci. 2000. 57(13):1880-1893. PMID: 11215515","","","

InterPro
IPR000878
Domain

Tetrapyrrole methylase
PF00590	$\"[49-252]T$	TP_methylase

InterPro
IPR008189
Family

Protein of unknown function UPF0011
PIRSF005917	$\"[47-320]T$	Predicted methyltransferase, YraL type
TIGR00096	$\"[49-320]T$	TIGR00096: conserved hypothetical protein T
PS01296	$\"[129-140]T$	UPF0011

InterPro
IPR014777
Domain

Tetrapyrrole methylase, subdomain 1
G3DSA:3.40.1010.10	$\"[28-160]T$	no description

noIPR
unintegrated

unintegrated
PTHR21091	$\"[95-278]T$	METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
PTHR21091:SF18	$\"[95-278]T$	S-ADENOSYLMETHIONINE-DEPENDENT METHYTRANSFERASE

","BeTs to 18 clades of COG0313COG name: Predicted methyltransferasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0313 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB008189 (Protein of unknown function UPF0011) with a combined E-value of 3e-67. IPB008189A 50-91 IPB008189B 122-172 IPB008189C 203-213 IPB008189D 228-241 IPB008189E 260-271***** IPB003043 (Uroporphiryn-III C-methyltransferase) with a combined E-value of 6e-09. IPB003043A 50-80 IPB003043B 123-162 IPB003043C 227-248","","","-47% similar to PDB:1WYZ X-Ray structure of the putative methyltransferase from Bacteroides thetaiotaomicron VPI-5482 at the resolution 2.5 A. Norteast Structural Genomics Consortium target Btr28 (E_value = 6.1E_13);","Residues 49 to 252 (E_value = 4.4e-49) place ANA_1902 in the TP_methylase family which is described as Tetrapyrrole (Corrin/Porphyrin) Methylases.","","hypothetical protein TIGR00096","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1904","2066239","2068431","2193","6.61","-2.57","79697","GTGACGACTCCGAGCGCGCTGTCTCCCGAACAGTCCCCCGAGCAGTCCCGCGACGGTTCCCCCGGCCCGGACGCGGAGCAGGAACGAGCACAGGAACCCGTCTCAGGGCGGGATGAGGCCGCGGACCCCGCATTGGCCGAGTCCGCCCAGGAACCGGCCGAGCCCACGGGCCCTGCACCAGCAGAGCCCATCGTCGCCGAGCGCACTGAGAACGAGCTGCGCACCCTGCTCGGGCTGGGCCCAGTGAGGGCCGTGCTGCCCCTCGGCGTGAGGGCGCGCGGGTGGATCGTCACCGGCGTCGTCGGCCTCATCGCCGCGCTGCTGCGCCTCATCGGGTTGAACCACCCCAGAACGCTCATGTTCGATGAGATCTACTACGTCAAGGACGCCTACTCCCTGTGGCACCTGGGCTACGAAGGGAGCTGGGCGGCCAACTCTGATGCGGCCTTCGCCAGCGGAAACTTCTCGGGGCTATCCACGGAGGCCGCCTACGTCGTCCACCCGCAGCTGGGCAAATGGCTCATCGGCGCCGGCATGGAGATCTTCGGTCCGGAGTCACCCTTCGGTTGGCGGTTCATGCCGGCCGTCGCCGGAATCCTCACGGTGATGCTGCTGACGCGCCTGACGATGCGCCTGACGCGCTCACCGCTGCTGGCGGGCCTGGCCGGACTGCTCCTGGCCATCGACGGCGTGGCCCTGACCGAGTCCCGCATCGGGCTGCTGGACGTCTTCATCGGTTTCTTCGCCACCCTGACCCTGTACTGCCTGGTCCGCGATCGGGAGTGGTCGCGAGCAAGGCTGGCTCGCAAGATGGCAGGGACCGTGCCCGGGGCACGCGCCCCGCGAGCCACGATCCGTCCCTGGCTGCTGGCCGCCGCCATCGCGCTGGGTCTGACCTGCTCCATCAAGTGGTCGGGGCTCTACCTCGTCGCGGTGTGCGGCATCGCCGTCGTCATCTGGGACACGATGGCGCTACGGCGAGTGGGGGCACGGGCCTGGTTCCTGGAGGGGACGGTCGCCCAGGGCGTGAGCGACTTCCTGCAGGCGATTCCGTTGGTCATCGCGGTCTACGTCGGCTGCTGGTGGTCCTGGTTCACCCACCTGGGTGCCTTCAAGCACGGGTGGACGGCCGAGCAGATCAAGCAGGGGCTGCCGGTTCCTGCCCCCTGGCTATCCGGGTACGTGGACGACTCGACGTTCCAGAACATCAACGACTTCATCGCCTACCACCAGCAGATGTACGACTTCCACGTGGGCCTGGACTCTCCGCACACGTACCAGTCGAAGCCCTCCGGCTGGCTGCTGCAGACCCGACCGACATCCTTCTTCTGGGAGGACAAGGCTCAGGTGCCGCAGACCTGCACGGGCGGCGATTGCATTCAAGCCATCACCTCGATCGGGAACATCGTCATCTGGTGGTCGGCCGTGGTGGCGCTCGTGGCCGTGATCATCATCGGAGTGAAGAACCGCGACTGGCGGGCCTGGGTGCCCCTCATCGGCTACCTGGGCCTGTATGTGCCCTGGTTCCAGTACCGGGATCGCACCATCTTCACCTTCTACACGGTGGCCTTCGTGCCCTGCGTCGTGCTCGTCCTCATGCTGGCGCTGGGCATGGCCTCCGGGCTGCTACCACCGCTGCCCGGCTCGGCGAGCGCCGACACCCAGATGGTGGCCCTCCACAGACGGCAGATCGGCCCAGGTATCCGGCCGTGGCGCGGCATGGGCGCCAGATTCCTCGGTTTCGGCCCGCAGTTCGCACGTACGGCCGTGTGGACGCCGCCGATGGAGGAGACCGACCCCGGCATCTACCGCATCAATCCGGCCCTGACCGGCATCGACGACGACCTCGAGCCCGACATCCCCCTCGGCAGCCCGCCGGCCGATGCCGCCCAGGAACGGGCCTATGACGAGCTGACCGGACATCCCGGCCCCTCGACGTCGTCGGGCGCCTCAATGCCGGAATGGTCCAACGGCGGGATGCCACGGCTGGCTGGCCGCCGCAGCCCGTGGGCCTCCTTGGCGAAGTGGACGATGGTCCCCACGTGGCAGATCCGCACCGAGGGCATCGGACTCATCATCGTGGTCACGCTTCTGGCCTGCGCAGCGGCCGCCTTCTGGTGGCCGATCTGGACCGGGCAGACGGTCTCACGTTCCTTCTGGGTCTCCCACATGTTCCTGTCGTCCTGGATCTGA","VTTPSALSPEQSPEQSRDGSPGPDAEQERAQEPVSGRDEAADPALAESAQEPAEPTGPAPAEPIVAERTENELRTLLGLGPVRAVLPLGVRARGWIVTGVVGLIAALLRLIGLNHPRTLMFDEIYYVKDAYSLWHLGYEGSWAANSDAAFASGNFSGLSTEAAYVVHPQLGKWLIGAGMEIFGPESPFGWRFMPAVAGILTVMLLTRLTMRLTRSPLLAGLAGLLLAIDGVALTESRIGLLDVFIGFFATLTLYCLVRDREWSRARLARKMAGTVPGARAPRATIRPWLLAAAIALGLTCSIKWSGLYLVAVCGIAVVIWDTMALRRVGARAWFLEGTVAQGVSDFLQAIPLVIAVYVGCWWSWFTHLGAFKHGWTAEQIKQGLPVPAPWLSGYVDDSTFQNINDFIAYHQQMYDFHVGLDSPHTYQSKPSGWLLQTRPTSFFWEDKAQVPQTCTGGDCIQAITSIGNIVIWWSAVVALVAVIIIGVKNRDWRAWVPLIGYLGLYVPWFQYRDRTIFTFYTVAFVPCVVLVLMLALGMASGLLPPLPGSASADTQMVALHRRQIGPGIRPWRGMGARFLGFGPQFARTAVWTPPMEETDPGIYRINPALTGIDDDLEPDIPLGSPPADAAQERAYDELTGHPGPSTSSGASMPEWSNGGMPRLAGRRSPWASLAKWTMVPTWQIRTEGIGLIIVVTLLACAAAAFWWPIWTGQTVSRSFWVSHMFLSSWI$","Glycosyl transferase, family 39","Membrane, Cytoplasm, Extracellular","CONSERVED MEMBRANE PROTEIN","integral membrane protein","glycosyl transferase, family 39","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR003342
Family

Glycosyl transferase, family 39
PF02366	$\"[99-369]T$	PMT

noIPR
unintegrated

unintegrated
PTHR10050	$\"[255-537]T$	DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE
PTHR10050:SF1	$\"[255-537]T$	gb def: Putative integral membrane protein
tmhmm	$\"[92-112]?$ $\"[148-168]?$ $\"[187-205]?$ $\"[215-233]?$ $\"[237-257]?$ $\"[304-324]?$ $\"[343-365]?$ $\"[469-487]?$ $\"[516-536]?$ $\"[688-710]?$	transmembrane_regions

","BeTs to 4 clades of COG1928COG name: Dolichyl-phosphate-mannose--protein O-mannosyl transferase PMT1Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1928 is ------y---r--c------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 99 to 369 (E_value = 2.6e-07) place ANA_1904 in the PMT family which is described as Dolichyl-phosphate-mannose-protein mannosyltransferase.","","MEMBRANE PROTEIN","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1905","2069092","2068517","576","11.53","13.98","19795","GTGAAAGGACCCCGCATGAGAATCACCGTCCTTGGTGCCACCGGCATGGCCGGGACCGCAGTCGTCAACGAGGCGCTCAGCCGCAGTCACGAGGTGACCGCCGTATCCCGACGGCGTTGCCATCGGGGTGGCGCCCGCCTCACCTCGCGCCTGCTGGACGTCACCGACGTCGAGGGCGTGGCCGGTCTCCTGACAGACAGTGACGTGGCCGTCGTCGCACTGCGCCCGCCTGCCGGACACGAGAGCGACCTGGCCCGACTCACGACGGCCGTCCTGGACGCCGCTTCCAGGGGCCGAACGCCCCTGCTCATCATCGGGGGCGCGGCTCCGCTGAACTCGCCCGGCAATCCCCGCACCCTCGCCATTGGACGACCCCACCATTGTGCCGCCGGCCTGGAGAGACGTGGCCCAGGCGAGCCTCGATCAGTTCCGGGCGTGCCAGGCGCACAGTTACAAGGGCTGGGTCTATCTCAGCCCTCCGGCGATCTTTGCTCCAGGAGGTGCCACCGGCTCCTATCGCCGCGGAACCACCATGCTTCTGCGGGACGCCCGCGGGCAGTCCCGCATCAGCCCTGA","VKGPRMRITVLGATGMAGTAVVNEALSRSHEVTAVSRRRCHRGGARLTSRLLDVTDVEGVAGLLTDSDVAVVALRPPAGHESDLARLTTAVLDAASRGRTPLLIIGGAAPLNSPGNPRTLAIGRPHHCAAGLERRGPGEPRSVPGVPGAQLQGLGLSQPSGDLCSRRCHRLLSPRNHHASAGRPRAVPHQP$","NADH-flavin reductase","Membrane, Extracellular","B. subtilis YwnB protein homolog lmo0794","putative NADH-flavin reductase","Putative NADH-flavin reductase-like","","Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 1997. 36(21):6294-6304. PMID: 9174344","","","

InterPro
IPR001509
Family

NAD-dependent epimerase/dehydratase
PF01370	$\"[8-69]T$	Epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[7-97]T$	no description
PTHR15020	$\"[6-108]T$	FLAVIN REDUCTASE-RELATED
PTHR15020:SF10	$\"[6-108]T$	CHARACTERIZED

","BeTs to 4 clades of COG2910COG name: Putative NADH-flavin reductaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2910 is -----------lb-efg-s-uj----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 69 (E_value = 1.8e-06) place ANA_1905 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 8 to 37 (E_value = 0.00046) place ANA_1905 in the NmrA family which is described as NmrA-like family.","","subtilis YwnB protein homolog lmo0794","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1906","2070060","2069089","972","9.99","8.03","32774","ATGCGCGCACCTCAGGCTGGATGCATGACGACTCATGCCGCCCCTTCTCAAGTCACGTGCGACTCCAAGTCGGCCGCGCCCGGCGGCGCCCTGTCAGGCCTCCGGACGAGAATCGCCTGGATTGCTCTGACATCCCTGGCACCGGCCGTGTGGGGGACGACGTACATCGTCACCACCCACGTCCTTCCCCCGGGGCATCCGGTCTTCGCGGCACTGATGCGGACACTCCCAGCGGGTGTTCTCGCCCTCCTCGCCTCCCGTACGCTGCCGCACGGAACGTGGTGGTGGAAGAGTCTTGTCCTCGGAGCCCTCAACATGGCCTGCTTCTTCCCCCTCCTCTTCGTCGCCGCGCAGCGCCTGCCCGGAGGTGTGGCCGCGACACTCGGGGCCGCGCAACCGATCATCGTCGCAGGCTTCGCCGTTGCCGTCCTGGGTGAGCGCCTATCGGCATGGAGACTGATATGGGGCGTGGTCGGCGTCGTCGGTATCGCTCTCGTCGTCCTGGGACCACAGGCGCAGCTCGACGCCCTCGGGGTGGCGGCCGGCTTGGGCGGAGCCGCCTCGATGGGGCTGGGAGTCGTCCTCACCAAACGGTGGGGCAGGCCCGAGGGCGTCAGTGCCCTTGGGCTGGCCGGATGGCAGCTCACCGGTGCCGGCCTCCTGCTCATCGTGCCTGCCCTCATCATCGACGGCGTTCCAACCGGAATCGATACGGCGGCTGTGGCGGGATACGCCTGGCTCGGGCTCGTAGGAGGGCTGGCCGCCTACGTCCTGTGGTTCGAGGGTATCCGCAGGCTGCCGGTCATACCGACAGCACTGCTGGGCCTGCTCTCACCTCTGAACGCGGCGCTCCTCGGGCACGTCATCGCCGATGAGGCACTCACGTCCTTCCAGTTCCTGGGGTTCGCGCTCGCTCTCACTGCGATGAGCGCAGGTCAGCTCGCCCTTCCCTCCTCCCGCTCCTCCTCGTGA","MRAPQAGCMTTHAAPSQVTCDSKSAAPGGALSGLRTRIAWIALTSLAPAVWGTTYIVTTHVLPPGHPVFAALMRTLPAGVLALLASRTLPHGTWWWKSLVLGALNMACFFPLLFVAAQRLPGGVAATLGAAQPIIVAGFAVAVLGERLSAWRLIWGVVGVVGIALVVLGPQAQLDALGVAAGLGGAASMGLGVVLTKRWGRPEGVSALGLAGWQLTGAGLLLIVPALIIDGVPTGIDTAAVAGYAWLGLVGGLAAYVLWFEGIRRLPVIPTALLGLLSPLNAALLGHVIADEALTSFQFLGFALALTAMSAGQLALPSSRSSS$","Permease of the drug/metabolite transporter (DMT) superfamily","Membrane, Extracellular","regulatory protein PecM","hypothetical protein","protein of unknown function DUF6, transmembrane","","","","","

InterPro
IPR000620
Domain

Protein of unknown function DUF6, transmembrane
PF00892	$\"[49-168]T$ $\"[187-314]T$	DUF6

noIPR
unintegrated

unintegrated
signalp	$\"[1-52]?$	signal-peptide
tmhmm	$\"[38-58]?$ $\"[68-86]?$ $\"[95-117]?$ $\"[123-143]?$ $\"[148-170]?$ $\"[176-196]?$ $\"[206-226]?$ $\"[240-260]?$ $\"[270-290]?$ $\"[296-316]?$	transmembrane_regions

","BeTs to 9 clades of COG0697COG name: Permeases of the drug/metabolite transporter (DMT) superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],RThe phylogenetic pattern of COG0697 is aompkzyqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 4","***** IPB008217 (Protein of unknown function DUF125) with a combined E-value of 4.5e-06. IPB008217B 170-194 IPB008217D 220-257","","","No significant hits to the PDB database (E-value < E-10).","Residues 49 to 168 (E_value = 4.7e-18) place ANA_1906 in the DUF6 family which is described as Integral membrane protein DUF6.Residues 187 to 314 (E_value = 1.3e-14) place ANA_1906 in the DUF6 family which is described as Integral membrane protein DUF6.","","protein PecM (DMT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1907","2070130","2071023","894","8.20","2.58","31743","TTGAGGTACGCCGTGGCCATCGCTGAGGAACAGAGCTTCACGCGCGCGGCTCAGCGGTGCTTCGTGGTGCAGTCGGCTCTGAGCCGGCAGATCAAGTCCTTGGAGAGCGAGCTCGGGGTGAGGCTGTTCGCGCGCACGAGCCGCAAGGTGGAGGTGACGCCCGCTGGGGAGGCGTTCGTGAAGCAGGCTCGGTTGTGCCTCCAGGCGGCCGAGCGCGCGAAGGCCTCGGCAGCGGCCGCTCACGGACAGATCCGGGGGTCACTGACCATCGGGGTGATCCCGACTGTGACGGCAGTGGATATTGCGGCGGTTCTGGGCGCTTTCCGTCGCAGCTACCCCGAGGTCGGCGTTCACGTGCGCACTGGTGGCAGTGATGAGTTCCTGCGTCGTATTGCGGCTGGGGAGCTCGACGTGGGCTTCCTCGGCCTGGCGGAAGGCGTGACTCCGCGGGGCGTGCAGACGCAAGAGCTCTCACAGGAGCGCCTGGTGGCGGTGCTGTCAGAGGGGCACCGATTGGCGGGGCGACGCCGACTCCGCCTGAAGGACCTGGCAGACGAGCCGTTCGTGGACTTTCCGGAGGGGTCGTCAGGACGCGAGCAGTCCGATCTGGCCTTCGACAGGGCTGGGCTCCGCCGTGAGGTGAGCTTGGAGGTGAACACAGCCGACCTACTCACCGGATTGGTGCGTCAGGGACTGGGGGTCGCTCTTGTCGCTCCCAGCGTGGCCCGAGAGGCGCCCGGCTGCGTGTGCATCCCCGTCAGCGACGGTCCGGTACGGGTGGAGTACCTCGCGTGGGACTCCTTCAACCCCAGCCCGGTGGCACAGGTCTTCGTTGACTCCATCCTCATGCCCACAGGCCAACGCCCCTTGTCGCTCACGGCGACGACGGCGTAG","LRYAVAIAEEQSFTRAAQRCFVVQSALSRQIKSLESELGVRLFARTSRKVEVTPAGEAFVKQARLCLQAAERAKASAAAAHGQIRGSLTIGVIPTVTAVDIAAVLGAFRRSYPEVGVHVRTGGSDEFLRRIAAGELDVGFLGLAEGVTPRGVQTQELSQERLVAVLSEGHRLAGRRRLRLKDLADEPFVDFPEGSSGREQSDLAFDRAGLRREVSLEVNTADLLTGLVRQGLGVALVAPSVAREAPGCVCIPVSDGPVRVEYLAWDSFNPSPVAQVFVDSILMPTGQRPLSLTATTA$","Transcriptional regulator, lysR family","Cytoplasm","transcriptional regulator lysR family","LysR-family transcriptional regulator","LysR, substrate-binding","","Viale A.M., Kobayashi H., Akazawa T., Henikoff S. rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum. J. Bacteriol. 1991. 173(16):5224-5229. PMID: 1907267Sung Y.C., Fuchs J.A. The Escherichia coli K-12 cyn operon is positively regulated by a member of the lysR family. J. Bacteriol. 1992. 174(11):3645-3650. PMID: 1592818Kondorosi E., Pierre M., Cren M., Haumann U., Buire M., Hoffmann B., Schell J., Kondorosi A. Identification of NolR, a negative transacting factor controlling the nod regulon in Rhizobium meliloti. J. Mol. Biol. 1991. 222(4):885-896. PMID: 1840615Henikoff S., Haughn G.W., Calvo J.M., Wallace J.C. A large family of bacterial activator proteins. Proc. Natl. Acad. Sci. U.S.A. 1988. 85(18):6602-6606. PMID: 3413113Thony B., Hwang D.S., Fradkin L., Kornberg A. iciA, an Escherichia coli gene encoding a specific inhibitor of chromosomal initiation of replication in vitro. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(10):4066-4070. PMID: 2034653","","","

InterPro
IPR000847
Domain

Bacterial regulatory protein, LysR
PR00039	$\"[13-24]T$ $\"[24-34]T$ $\"[34-45]T$	HTHLYSR
PF00126	$\"[1-57]T$	HTH_1
PS50931	$\"[1-53]T$	HTH_LYSR

InterPro
IPR005119
Domain

LysR, substrate-binding
PF03466	$\"[81-286]T$	LysR_substrate

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[1-82]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[161-244]T$	no description

","BeTs to 12 clades of COG0583COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000847 (Bacterial regulatory protein LysR, HTH motif) with a combined E-value of 1.1e-23. IPB000847 1-45***** IPB005119 (LysR substrate binding domain) with a combined E-value of 5.6e-17. IPB005119A 13-35 IPB005119B 42-53 IPB005119C 227-235","","","-43% similar to PDB:1AL3 COFACTOR BINDING FRAGMENT OF CYSB FROM KLEBSIELLA AEROGENES (E_value = 5.0E_19);-42% similar to PDB:1IXC Crystal structure of CbnR, a LysR family transcriptional regulator (E_value = 7.5E_15);-42% similar to PDB:1IZ1 CRYSTAL STRUCTURE OF CBNR, A LYSR FAMILY TRANSCRIPTIONAL REGULATOR (E_value = 7.5E_15);","Residues 1 to 57 (E_value = 2.6e-18) place ANA_1907 in the HTH_1 family which is described as Bacterial regulatory helix-turn-helix protein, lysR family.Residues 81 to 286 (E_value = 8.4e-51) place ANA_1907 in the LysR_substrate family which is described as LysR substrate binding domain.","","regulator lysR family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1911","2078061","2077288","774","5.19","-7.89","26850","ATGACTTCGACAGCACCAGCAGTTTCCGTGGCATGCGGGATCGACATCGGCGGATCGGGCGTCAAGAGCGCCCTGGTCGACCTGGCCACGGGCACGTTCATTGGTGAGCGCGTCCGCATCGACACTCCCGAGGAGTCCACACCCGCGGCCGTCGCCGAGGTCTGCCGCGAGCTCCTCGAACAGCTCGAGGTGGGCGACGACGTCCCGGTCGGCGTGGCCCTGCCCGCTCCGATCGTCCACGGCACGGTCCCCTTCATCGCCAATCTCGACAAGTCCTGGACGGGCGTCAACCTCACCGAGCTCATGCGCGAGCACCTGGGCCGGCCGGTGACTGGGCTCAACGACGCCGACGCCGCGGGCCTGGCCGAGGTCGCCTTCGGTGCCGCCAAAGACGTGCCCGGGACCATCATTGTCACCACCCTGGGCACCGGGATCGGCTCGGCCGTCATTGTTGACGGAACCCTGGTCCCCAACACCGAGCTCGGGCACCTGGAGATTGACGGCTACGACGCCGAGAGCCGGGCCTCGGCCGGGCAGCGCACCGCCCAGGACCTGTCCTGGAAGAAGTGGGCCAAGCGCCTCCAGCGCTACTACTCCCACGTGGAGATGCTCTTCTCCCCGGACCTGTTCGTCGTGGGCGGGGGCGTCTCCCGCAAGCACGAGAAGTACCTGCCGCTGCTGGACCTCAAAACCCCGATCGTGCCGGCCCAGCTGCTCAACACGGCAGGCATCGTGGGGGCCGCCTACCAGGCCTCCCGCGCCCGCGCCTCCTGA","MTSTAPAVSVACGIDIGGSGVKSALVDLATGTFIGERVRIDTPEESTPAAVAEVCRELLEQLEVGDDVPVGVALPAPIVHGTVPFIANLDKSWTGVNLTELMREHLGRPVTGLNDADAAGLAEVAFGAAKDVPGTIIVTTLGTGIGSAVIVDGTLVPNTELGHLEIDGYDAESRASAGQRTAQDLSWKKWAKRLQRYYSHVEMLFSPDLFVVGGGVSRKHEKYLPLLDLKTPIVPAQLLNTAGIVGAAYQASRARAS$","Polyphosphate glucokinase/transcriptional regulator","Cytoplasm","similar to Mycobacterium tuberculosispolyphosphate glucokinase (polyphosphate-glucose","polyphosphate glucokinase ","ROK family protein","","Titgemeyer F., Reizer J., Reizer A., Saier Jr M.H. Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 1994. 140:2349-2354. PMID: 7952186","","","

InterPro
IPR000600
Family

ROK
PF00480	$\"[13-155]T$	ROK

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.160	$\"[115-249]T$	no description
G3DSA:3.30.420.40	$\"[11-114]T$	no description
PTHR18964	$\"[78-252]T$	ROK FAMILY
PTHR18964:SF7	$\"[78-252]T$	GLUCOSE KINASE

","BeTs to 6 clades of COG1940COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1940 is ao-p-z-qvdrlbce-gh---j--t-Number of proteins in this genome belonging to this COG is 5","***** IPB000600 (ROK family) with a combined E-value of 1.1e-09. IPB000600A 13-20 IPB000600B 109-123 IPB000600C 139-150","","","-60% similar to PDB:1WOQ Crystal Structure of Inorganic Polyphosphate/ATP-Glucomannokinase From Arthrobacter sp. strain KM At 1.8 A Resolution (E_value = 5.5E_56);","Residues 13 to 183 (E_value = 5e-09) place ANA_1911 in the ROK family which is described as ROK family.","","to Mycobacterium tuberculosis polyphosphate glucokinase (polyphosphate-glucose phosphotransferase) also similar to members of ROK family of transcriptional regulators","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1912","2080170","2078176","1995","7.61","1.63","68382","ATGTCCACAACAACCTCACGCGGCTCCACTGCGGCGAAGCCGTCCAGTGCCGGCTCCGGCCCGGTCAAGGAGCTGACTGCTCGCGGCATCGTCATCGGCGGCATCATCACGCTCATCTTCACCGCGGCGAACGTCTACCTCGGCCTCAAGGTGGGGCTCACCTTCGCCACCTCGATCCCGGCCGCCGTCATCTCCATGGCGATCCTGCGCCGCTTCTCCGATCACACGATCCAGGAGAACAACATCGTCCAGACGATCGCCTCGGCGGCCGGGACGCTGTCCGCCATCATCTTCGTGCTGCCCGGACTCATCATCGTGGGCTGGTGGACGGGATTCCCCTACCTCCAGACCGTCCTGGTCATCATCCTGGGCGGCATCCTCGGCGTCACCTACTCCATCCCGTTGCGGCGCGCGCTCGTGACCAACTCCGACCTGCCCTACCCCGAGGGCGTGGCCGGCGCCGAGGTCCTGCGCGTGGGCGACACCAGCGAAGGGGCCGAGGAGTCCAGCCGTGGACTGGGTGTCATCGTGCGGGGCTCCATCGCCTCGGCGGCCCTGTACTTCCTCAACGCCCTCAAGGCCATCAGCGTCGACATCGCCGGGGTCTTCCGGGTCGGTGCCGGTGCCACGATGATGGGCACCTCCCTGTCCCTGGCGCTGGCCGGCGTGGGCCACCTGGTCGGCGTCGGCGTCGGCATCGCCATGATCGTCGGCCTGCTCATCTCCTACGGGGTGCTGCTCCCGATGCGCACCTGGGGCACGGCAGTGGCCGACAAGGACCTCGCCGACTTCGTGGGCGCCACCTTCGCCAGTGAGGTTCGGATCGTCGGCGCCGGCGCCATCGCCATCGCTGCCATCTGGACCTTCCTGAAGATCCTCGGCCCCATCGTCACCGGTATCCGCGAGTCCCTGGCCTCCAGCGCCAAGCGCGACGCCGGTGAGGAGATCCCCCTGACCGAGCGCGACCTGTCGATGAAGACGGTCATCGGTGTCACCGTCGGCTCCATGCTGCCCATCGGTGTGCTCCTGTGGCTGTTCCTGCACGGGACCTCCATGGCTCACCACGCCACGGGCCTCATCATCGTCTCCATCCTCTTCATCCTGCTGACCGGACTGGTCGTCGCCTCGGTGTGCGGCTACATGGCCGGCCTCATCGGCTCCTCCAACTCGCCGATCTCCGGCGTCGGCATCCTCGTGGCGGTCACCGCGGCCGCGCTGGTTCGCACCATCGCCACCACCTCCTCGCCTGACGACGTCCGCACCCTGGTGGCCTACACCCTGTTCGTCACCGCGGTCGTCTTCGGCGTGGCCACCATCTCGAACGACAACCTCCAGGACCTCAAGACCGGCCAGCTCGTCGACTCCACCCCGTGGAAGCAGCAGGTGGCGCTCGTCATCGGTGTCGTCTTCGGCGCCATCGTCATCCCTCCGGTGCTCAGCCTCATGCAGGGCGCCTTCGGCTTCGCCGGCGCCCCCGATGCCGGTGACGACGCTCTGGCCGCGCCCCAGGCGAACCTCATCAAGCACCTGGTTCAGGGCGTCCTCGGCGGGGACCTCAACTGGAGCCTGCTGGGGCTGGGCGCCCTCATTGGCGCCGTCGTCATCGCCATCGATGAGATCCTGCGCCGCAACACCAAGTACTCCCTGCCGCCGCTCGCCGTCGGCATGGGCATGTACCTGCCCACTGCCGTCACCGTCATGATCCCGATCGGTGCCGCCCTCGGTCACCTCTACGACCGCTGGGCCGAGCGCACCGCCAACCCGGAGCGGGCCAAGCGCATGGGCACGCTCATGGCGACCGGCCTCATCGTCGGCGAGAGCCTCGCCGGGGTGGTCTACGCCGGGATCGTCGTGGCCTTCGGCGGCAAGGCGGACCCGCTGGCCATCATGCCCGAGAGCTTCGCAGGCATCGCCCCCTGGGTGGGCGTGGTGCTGTTCGTCGGCACTCTGTGGTACCTCTACCGGGGCGCCCGCCAGGAGAGCACTCGCGACTGA","MSTTTSRGSTAAKPSSAGSGPVKELTARGIVIGGIITLIFTAANVYLGLKVGLTFATSIPAAVISMAILRRFSDHTIQENNIVQTIASAAGTLSAIIFVLPGLIIVGWWTGFPYLQTVLVIILGGILGVTYSIPLRRALVTNSDLPYPEGVAGAEVLRVGDTSEGAEESSRGLGVIVRGSIASAALYFLNALKAISVDIAGVFRVGAGATMMGTSLSLALAGVGHLVGVGVGIAMIVGLLISYGVLLPMRTWGTAVADKDLADFVGATFASEVRIVGAGAIAIAAIWTFLKILGPIVTGIRESLASSAKRDAGEEIPLTERDLSMKTVIGVTVGSMLPIGVLLWLFLHGTSMAHHATGLIIVSILFILLTGLVVASVCGYMAGLIGSSNSPISGVGILVAVTAAALVRTIATTSSPDDVRTLVAYTLFVTAVVFGVATISNDNLQDLKTGQLVDSTPWKQQVALVIGVVFGAIVIPPVLSLMQGAFGFAGAPDAGDDALAAPQANLIKHLVQGVLGGDLNWSLLGLGALIGAVVIAIDEILRRNTKYSLPPLAVGMGMYLPTAVTVMIPIGAALGHLYDRWAERTANPERAKRMGTLMATGLIVGESLAGVVYAGIVVAFGGKADPLAIMPESFAGIAPWVGVVLFVGTLWYLYRGARQESTRD$","Oligopeptide transporter, OPT family","Membrane, Cytoplasm","oligopeptide transporter, OPT family","oligopeptide transporter; OPT family protein","oligopeptide transporter, OPT family","","Lubkowitz M.A., Hauser L., Breslav M., Naider F., Becker J.M. An oligopeptide transport gene from Candida albicans. Microbiology 1997. 143:387-396. PMID: 9043116","","","

InterPro
IPR004813
Family

Oligopeptide transporter OPT superfamily
PF03169	$\"[24-617]T$	OPT
TIGR00728	$\"[8-621]T$	OPT_sfam: oligopeptide transporters, OPT su

InterPro
IPR004814
Family

Oligopeptide transporter OPT
TIGR00733	$\"[24-618]T$	TIGR00733: oligopeptide transporter, OPT fa

noIPR
unintegrated

unintegrated
tmhmm	$\"[25-43]?$ $\"[49-69]?$ $\"[90-112]?$ $\"[118-136]?$ $\"[200-220]?$ $\"[226-246]?$ $\"[267-287]?$ $\"[327-347]?$ $\"[357-386]?$ $\"[392-412]?$ $\"[422-442]?$ $\"[461-481]?$ $\"[519-537]?$ $\"[556-576]?$ $\"[597-617]?$ $\"[636-654]?$	transmembrane_regions

","BeTs to 10 clades of COG1297COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG1297 is -o--k-y---r----f-hsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB004813 (Oligopeptide transporter OPT superfamily) with a combined E-value of 6.7e-18. IPB004813A 112-161 IPB004813C 446-457","","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 617 (E_value = 7.8e-133) place ANA_1912 in the OPT family which is described as OPT oligopeptide transporter protein.","","transporter, OPT family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1913","2081950","2080409","1542","9.78","14.96","57232","ATGACCTGGTCCTTCGGTCCGCTCGTGCTGCTGGTCTGCCTGGTCATCCTGCTGGCCTGCTTCGCGGTCAAGCTGCTGTTCAAGCGCGGGACACGGCTCCGGGCGGTCCGGGCGGTCCACAGAGAGGGATGCGGCGAGAAGCGGGGCGCAGGGCGCGGTGGGGTGGTCGCTGTGCGCAGCGCGGTGACGACGCCGGACGAGGCTCAGCGATCGGCCGACGCCACCGGGCTGCCCCGGGCACTCATGCGGGCCGGTGGGCCCCTGCCCGCCGTCGTCGTGACCCTCGGCGTGGCGGGGTGGCTCTGCTGGCGGGTGCTGGTCAGTCGGCACCACGTCCTGGACGCGTGGATCGTGTGGACCTTCGATGTCCTCTTCGTGATCGTGGCCGTGCAGCTCGTGGTGGCCGGTTTCGAGGGGCGCGTCATCGGCCGCGGCGAGGCGCATCGGGTCGCCGTGCTCGTGCCGCTCTACAACGAGGATCCCGACGTCGTGGTGCGGATGCTCTCCGCCCTGCTGCACCAGAGCTCGCCGCCGGCCGAGATCCACGTCGTCGACGACGGCTCCACCCAGGGCGCCTATGTGACGGAGCGGGACTGGTTCATCCGGCAGGCGGCGTTGGCCGGCATCTACGCCAGCTGGCAGCGCACCCCCAATGAGGGCAAGCGCCACGCGCAGGTGCACGGTTTCAGGAAGATCCGTGACGCCGACCTGTTCGTGACCGTCGACTCCGACTCCATGCTCGACGCCGAGGCCCTCCATGAGATCGTCCAGCCCTTCAGCGACCCCCGGGTCATGTCAGTGGCCGGTGTCATCCTGGCGATCAACAACCGGGAGAACCTGCTCGCCCGGGTCACCGACGTGATATTCGTCGGCCAGCAGCTCATCGACCGCTCCTTCATGTCGCAGCTCGGCTCGGTCATGGTCAACTCCGGCGGCCTGGCCGCCTACCGGTGCTCCATCCTGGCCGAGAACATCGACACCTACCTGAACGAGAGCTATCTGGGGCGGCACGTGGAGTTCTCCGACGACTCCTTGCTGACTCTCTTCGCCCTGCTGCACGGCAGGACCGTCCAGCAGCCCTCGGCCTTCGCCTTCGCCTGGATGCCTGACCGCTGGAGCCACCACTACCGCCAGCAGGAGCGCTGGTTCCGCGGCTCCTTCATCCGCGGGCTCTGGCGCATCCGCTTCCTGCCGGTCCTCTCGTGGGGCTGGTGGCGCCAGGCCACCGGGTGGATGCAGATCTGGCTGGTGATCTCGGTCTTCGTCTACCTGCTGCTGTGGCGTCCGCTCGTCCTGGGCGGCGGTGTGCCGCCGACGGTGGTGCTGGTGCCTTTGGCGATCGGGCTGGTGCAGGGCTCGCGGTACATCTCCGTGTGGCGCTCGGACACCACCGGCCCCCAGAGGTACGCCAGCCTCCTCCTGTCCCCGGTGGCGACGCTGTGGTCCGCACTGATCCTGCGTCCCCTGCGGGTCTGGGGGATGGCCACCAGCGCCAAGATGGGGTGGAACACCCGTCAGCAGGTCGAGGTGACCTCGCAGTGA","MTWSFGPLVLLVCLVILLACFAVKLLFKRGTRLRAVRAVHREGCGEKRGAGRGGVVAVRSAVTTPDEAQRSADATGLPRALMRAGGPLPAVVVTLGVAGWLCWRVLVSRHHVLDAWIVWTFDVLFVIVAVQLVVAGFEGRVIGRGEAHRVAVLVPLYNEDPDVVVRMLSALLHQSSPPAEIHVVDDGSTQGAYVTERDWFIRQAALAGIYASWQRTPNEGKRHAQVHGFRKIRDADLFVTVDSDSMLDAEALHEIVQPFSDPRVMSVAGVILAINNRENLLARVTDVIFVGQQLIDRSFMSQLGSVMVNSGGLAAYRCSILAENIDTYLNESYLGRHVEFSDDSLLTLFALLHGRTVQQPSAFAFAWMPDRWSHHYRQQERWFRGSFIRGLWRIRFLPVLSWGWWRQATGWMQIWLVISVFVYLLLWRPLVLGGGVPPTVVLVPLAIGLVQGSRYISVWRSDTTGPQRYASLLLSPVATLWSALILRPLRVWGMATSAKMGWNTRQQVEVTSQ$","Hyaluronan synthase","Membrane, Cytoplasm, Extracellular","hyaluronic acid synthase, putative","hyaluronan synthase ","Hyaluronan synthase","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[151-325]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[149-355]T$	no description
PTHR22913	$\"[150-389]T$	HYALURONAN SYNTHASE
PTHR22913:SF2	$\"[150-389]T$	HYALURONAN SYNTHASE
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[4-26]?$ $\"[87-107]?$ $\"[117-137]?$ $\"[391-406]?$ $\"[412-432]?$ $\"[441-459]?$ $\"[469-489]?$	transmembrane_regions

","BeTs to 6 clades of COG1215COG name: Glycosyltransferases, probably involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1215 is a-mpk-yq---lbcef-----j----Number of proteins in this genome belonging to this COG is 2","***** IPB004835 (Fungal chitin synthase) with a combined E-value of 2e-10. IPB004835B 279-320 IPB004835D 358-389","","","No significant hits to the PDB database (E-value < E-10).","Residues 151 to 325 (E_value = 3.1e-15) place ANA_1913 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","acid synthase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1914","2083271","2082006","1266","6.17","-6.30","46372","ATGAGGCGCCGCAGTTTTCTCATGGGCGGTCTCGCCCTGGCCGCCTCGAGCACTCTTCTACCTGAGCTGCAGACGGCGGCTCACGCCTCCCCGGTCCCGGCCGCCGGCCCTGCCGCGGCGCCCTCGCAGGTGCTGTCGGATATGCAGGACCCGCGCGCCTGGACCCTCTCATCCCCACACGGCTCCATCCGCCCCGACGCCTCCACCCACTCCCACGGGACCCAGTCGCTGGAGATCACCACCACCGGTGACTCCCGCCGTCCCACCAGCGCGGACCTGTCCCTGTCGGGCGTTGACATGACTGACTGCCAGTGGGACCTGTGGCTGCGCGCCGAGGACTACCGGCAGATCGAGAACATCCAGCTCGAGCTCGGCGGAGAGGGTGAGGACTGCCTGCGCCTCGACGTGGCTCCCGACATGCGCACGCTGCGCACCGGTACCTGGTGCCGGGTGACCGTCAACCGGGCCGCCGAGCGCGCCGTCGTCGGCCATCCTCGGCTGGACCGGGTGACGCGAGTGCGCCTGAAGATCGTCCCTGCCTCCGACTCGTCCTCGAGCCGCCTGTGGCTCGGCTACCTGGCCACCCTGCCGTCGGCCGCCAGCGGCATCGTCTCCATCTCCTTCGACGACGGCTACGACAGCGACTACAAGACGGCCCGGGCGATCCTGCAGGACTGCGGCATCGGCGCGGCGACCTCCTACGTCATCGCCGACAAGGTCGGGCTGCCCGGCCGCATGAGCACCGCCCAGCTCACCGAGATGCGCGAGCGTCACGGCTGGGACATCGCTGCCCACGCCTCCACCGATCTCACCACCCTCGACGAGGCGGGGGTGCGCCAGGAGTTCGAGACGATCAGATCCTTCCTCCTCGAGCACGGCTACCCCGAGGGCGCCGCCCACTTCGCCCTGCCCATGGGGCGGTACAACGACCTCGTGCTGCGCACCTCCCAGGACTACTTCACCTCGATGCGCACCATTGAGAACGCCCCGGAGACCCTCGCGCCAGGGGACCCGTTTCGGCTGCGCGTCTTCTACTGCGGCTCCTACACCACCGAGTCCCAGGTTGAGAAGGCGCTGGCCCGCTGCCGGGAGCACCGCTGCTGGACCCACATGGTCTTCCACCGCATCGACGAGCAGACCGACGGAGCCCCCGAGTCGATCAGAGCGGACAGCTTCGAGCGCTTCATGAGGCGAGTGGCTGACTCCGGCCTGCCCGTCAAGACGGTTCCCGAGGTCATGCGCAGCCAGTCGCCTGCCCTGCCTTGA","MRRRSFLMGGLALAASSTLLPELQTAAHASPVPAAGPAAAPSQVLSDMQDPRAWTLSSPHGSIRPDASTHSHGTQSLEITTTGDSRRPTSADLSLSGVDMTDCQWDLWLRAEDYRQIENIQLELGGEGEDCLRLDVAPDMRTLRTGTWCRVTVNRAAERAVVGHPRLDRVTRVRLKIVPASDSSSSRLWLGYLATLPSAASGIVSISFDDGYDSDYKTARAILQDCGIGAATSYVIADKVGLPGRMSTAQLTEMRERHGWDIAAHASTDLTTLDEAGVRQEFETIRSFLLEHGYPEGAAHFALPMGRYNDLVLRTSQDYFTSMRTIENAPETLAPGDPFRLRVFYCGSYTTESQVEKALARCREHRCWTHMVFHRIDEQTDGAPESIRADSFERFMRRVADSGLPVKTVPEVMRSQSPALP$","Polysaccharide deacetylase","Periplasm, Cytoplasm, Extracellular","Polysaccharide deacetylase family","hypothetical protein predicted by Glimmer/Critica","polysaccharide deacetylase","","Freiberg C., Fellay R., Bairoch A., Broughton W.J., Rosenthal A., Perret X. Molecular basis of symbiosis between Rhizobium and legumes. Nature 1997. 387(6631):394-401. PMID: 9163424Mishra C., Semino C.E., McCreath K.J., de la Vega H., Jones B.J., Specht C.A., Robbins P.W. Cloning and expression of two chitin deacetylase genes of Saccharomyces cerevisiae. Yeast 1997. 13(4):327-336. PMID: 9133736Millward-Sadler S.J., Poole D.M., Henrissat B., Hazlewood G.P., Clarke J.H., Gilbert H.J. Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases. Mol. Microbiol. 1994. 11(2):375-382. PMID: 8170399","","","

InterPro
IPR002509
Domain

Polysaccharide deacetylase
PF01522	$\"[197-319]T$	Polysacc_deac_1

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 197 to 323 (E_value = 1.3e-06) place ANA_1914 in the Polysacc_deac_1 family which is described as Polysaccharide deacetylase.","","deacetylase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1916","2085281","2083746","1536","7.57","1.44","53318","ATGGCTCGCCGCTCCAATGTCCAGGACCGCTACTCGGCTGAGCTGCGGGTCCTGGCCACGGGTGCGGCCGCCGTCGAACGCGACGACACCTGCGCGAACAGTGGGCATGCGGAGCTCTTTCGACGTCGACCGGAGGTGAGGGTGATGAACAGGCCCGCCGTGAGGAATGTGCGCGCCCTGCGCACCGAGCGTGAGCTCGACCGTGCCCGCCAGGTTCACGCCCAGGGGCGTGAGCGCCGCCGGGTCGCCGCCTCGCACCGTGGGATCGTCGCCAGCGTCCTGCTCGGAGTCACGCTCGGCGCCTGGGTGCTGGGCCTGGTCACCGCGCTGCCCTGGTGGCCCGCCCTGTTGCCCTCCGCCCTGCTGGGGGCCTCGATGGTGGCCGGGCGTCGCGCCGCTCTGGCCTCGGCCGCGGCGGACCGCCGTGAGTGCCGCCGCATCGCCGAGCTCGAGCAGACTCTGGTGACCCTGACCGGCCGGCGCTCCTCGGCCTCGGTCGTGGCCGCGCCCCGCTCCGTCGTCGACGGCCCTCGCAGCGCCTCCAGCGGTGCGGTCAGTGCTGTCAGCGCCAGTGCGGCCTCGCCGGCCGTGTCCGCGGTGTCGGCTGAGTCGGTCGAGGCTGCCGGCGACTCCGGCGCGCAGGACTCCTTCATCGAGCGCCTCACCCGCGAGGGCGTCCAGCGCCCGGCCGCGCGCTCGGTGTCTGCCGAGTCGGCTGGGTCCACTGAGTCCGCTGTGTCCGCCGAGCCCGTCGCCGGCAGCCCCTCCGAGGCGACCGGCACCACTGCTGCCCGTCCCTCCCGAGCCGTCGACTCTGAGGAGGAGCGCCTGGCCAGGCTCGACGCCGACCTCGATGACGAGACCGCCGCCGCCGTCGCCGCTGAGCGTGAGGCGACCCGTCGCGCCTCGGTCTACGTGCCCTCCCGCCACGCCGGCAGGGTCACTCGGGACATGGGCGTGCGCGAGGCGGTCTCCCGCGACGGCGACGAGGAGAGCTCGCCGCGCACCAAGGACTTCGTCGCCTCCCTGCCTGCCTCGACCTCCCGCAGTCTGTCCGGCTGGGGCAAGCTCTTCGCCGAGGCGAGTGCCATTGAGCAGGAGGCTCAGGAGCGCGCCGCTGCGGCCCCCTCCCCGCAGGCCGCCGCTGAGCCGGCCCGGCGCGCTGCCGACTCCGCTCCCCAAGCTGCCTCCCGCACTGCTTCAGAGCCTGCCCCCACGGCCGCCCGCCCGCAGGCCCCCGCTGCCGCTGCCCCGGCGGCGACGGAGGGAGTCGTCAAGGAGGAGGCGACGACGTCGACCCCGCCCCAGGGTTGGCGACCGGTCCACGTCCCCGCTCCGACCTACACGCTGGCGGCCCGCGCGCCCCGGCGCTCCTACGCCGACCCGGTGGTTGACCCGGGCACCTCCGCACCGGTGCCCGCCCGCCCGCAGTCGGCCCGCGGCTACATTCCCGCTCCCGTGGAGGATGAGGAGGAGCTCTTCCACCCCATCGACCTCGACGCGATCCTCGAGGGGCGGCGCGCAGCCGGCGAATAG","MARRSNVQDRYSAELRVLATGAAAVERDDTCANSGHAELFRRRPEVRVMNRPAVRNVRALRTERELDRARQVHAQGRERRRVAASHRGIVASVLLGVTLGAWVLGLVTALPWWPALLPSALLGASMVAGRRAALASAAADRRECRRIAELEQTLVTLTGRRSSASVVAAPRSVVDGPRSASSGAVSAVSASAASPAVSAVSAESVEAAGDSGAQDSFIERLTREGVQRPAARSVSAESAGSTESAVSAEPVAGSPSEATGTTAARPSRAVDSEEERLARLDADLDDETAAAVAAEREATRRASVYVPSRHAGRVTRDMGVREAVSRDGDEESSPRTKDFVASLPASTSRSLSGWGKLFAEASAIEQEAQERAAAAPSPQAAAEPARRAADSAPQAASRTASEPAPTAARPQAPAAAAPAATEGVVKEEATTSTPPQGWRPVHVPAPTYTLAARAPRRSYADPVVDPGTSAPVPARPQSARGYIPAPVEDEEELFHPIDLDAILEGRRAAGE$","Hypothetical protein","Cytoplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[93-113]?$	transmembrane_regions

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[94-176]T$	Acetyltransf_1
PS51186	$\"[33-202]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[29-203]T$	no description

","BeTs to 9 clades of COG1670COG name: Acetyltransferases, including N-acetylases of ribosomal proteinsFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1670 is -o-pk-y-vdrlb-efgh-nujx--wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 94 to 176 (E_value = 3.5e-10) place ANA_1917 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","acetytransferase (U33883)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1918","2087575","2086364","1212","5.55","-11.28","41664","ATGAGAACAGTGGCCGAGCACCTGGCCGCCTGCCTGGAGATCGCCCAGGCGGCAGCACCCCTCGACGTGGTCCTCCCCGACGCCGTCGGATGCGTCCTGGCCCAGGACGTCGCCGCCGGAATCGACCTGCCCGCCGTGGACCTGGCTGGACAGGACGGCTACGCGGTCATCGCCCAGGACGTCGCCGAGGCTGATCGCCACAACCCGCTCGTGCTCGACGTCGTCGACGCGGTGCGCGCCGGCGACATGCGCCCCTGCCACCTCGTCTCCGGTGCCGCCGTCCTCATTGACTCCGGCGCCCCCATGCCGCTGGGCGCCGACGCCGTCATCCCCTGGGCCGACACCGACCGCGGCGAGTCCCGGGTGACCATCCACCGCGCCGTCGCGGCCGGCGACAATGTCCGCCGCCGTGCCGAGGATGTGAAGTCGGGCACGACTGTCCTCAAGCGAGGCTCGCGCATCAGCGCCCGCCATGTGGCCCTGCTGGCGGGCCTCGGGATGCACCGGGTGCGCGTGCGCCCCGCCCCGCGCGTCGTCGTGGTCTCCATCGGGGACGAGCTGGTCGAGCCCGGCCAGTCCCGCGAGGCCGGGGACGTCTTCGACGCCAACGGCCACGCCCTGGCCTGCGCGGTCACCGACGCCGGCGGCCAGGCCTTCCGTGTGGCCGCCGTCCCCGACGAGCTGCGCGCCCTGGCCGACACCATCGAGGACCAGCTGGTGCGCGCCGACGTCCTCATCACCACCGGGGGCTTGAGCGTCGGGCAGGGCGACACCGTCAAAGACGTTCTGGCCCCCCTGGGCTCGGTGCGCTTCGACGCCGTCGCCATGTCCCCGGGCCGCCAGCTCGGCGTCGGGACGGTCGAGGGGACCCCGATCTTCTGCCTGCCCGGCGACCCGGTCAGCGCCCAGATCGCCTTCGAGACCTTCGTGCGCCCGGTCCTGCGCCAGATCGCCGGACGCACCTCCCTGCACCGCTCCAGCCTGGCGGCCACCATCTCCGAGGGCTGGCACTCCCCGAGCGGCAAGCGCGAATTCGTCCCCGTGCACGTCAGCGGCTCGCCATCCCGCGGATACCGCGCCGAGCCGACGGCGCCGCCGGGCACGGTCCGACTGCACGGCCTGTCCGAGGCCAACGCCATCGCCGTCGTGCCCGAGGACACGAGCACCGTGGTGGCCGGTGACACCCTCCACTGCCTTCTGCTGGACGCCTGA","MRTVAEHLAACLEIAQAAAPLDVVLPDAVGCVLAQDVAAGIDLPAVDLAGQDGYAVIAQDVAEADRHNPLVLDVVDAVRAGDMRPCHLVSGAAVLIDSGAPMPLGADAVIPWADTDRGESRVTIHRAVAAGDNVRRRAEDVKSGTTVLKRGSRISARHVALLAGLGMHRVRVRPAPRVVVVSIGDELVEPGQSREAGDVFDANGHALACAVTDAGGQAFRVAAVPDELRALADTIEDQLVRADVLITTGGLSVGQGDTVKDVLAPLGSVRFDAVAMSPGRQLGVGTVEGTPIFCLPGDPVSAQIAFETFVRPVLRQIAGRTSLHRSSLAATISEGWHSPSGKREFVPVHVSGSPSRGYRAEPTAPPGTVRLHGLSEANAIAVVPEDTSTVVAGDTLHCLLLDA$","Molybdopterin biosynthesis protein MoeA","Cytoplasm","molybdopterin biosynthesis protein.","molybdopterin biosynthesis protein MoeA","molybdenum cofactor synthesis domain","","Kamdar K.P., Shelton M.E., Finnerty V. The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin. Genetics 1994. 137(3):791-801. PMID: 8088525","","","

InterPro
IPR001453
Domain

Molybdopterin binding domain
PD002460	$\"[184-319]T$	Q9RKA7_STRCO_Q9RKA7;
PF00994	$\"[179-316]T$	MoCF_biosynth
TIGR00177	$\"[175-312]T$	molyb_syn: molybdenum cofactor synthesis do

InterPro
IPR005110
Domain

MoeA, N-terminal, domain I and II
PF03453	$\"[1-166]T$	MoeA_N

InterPro
IPR005111
Domain

MoeA, C-terminal, domain IV
PF03454	$\"[329-402]T$	MoeA_C

InterPro
IPR012088
Family

Molybdenum cofactor molybdenum incorporation protein MoeA
PIRSF004870	$\"[1-403]T$	Molybdenum cofactor molybdenum incorporation protein MoeA

noIPR
unintegrated

unintegrated
G3DSA:2.170.190.11	$\"[44-140]T$	no description
G3DSA:3.40.980.10	$\"[148-335]T$	no description
PTHR10192	$\"[1-401]T$	MOLYBDOPTERIN BIOSYNTHESIS PROTEIN

","BeTs to 18 clades of COG0303COG name: Molybdopterin biosynthesis enzymeFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0303 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is 2","***** IPB001453 (Molybdenum cofactor biosynthesis protein) with a combined E-value of 2.3e-68. IPB001453A 33-74 IPB001453B 96-118 IPB001453C 157-208 IPB001453D 243-264 IPB001453E 269-285 IPB001453F 293-317 IPB001453G 338-356 IPB001453H 360-384***** IPB008284 (Molybdenum cofactor biosynthesis protein, N-terminal) with a combined E-value of 7.2e-18. IPB008284B 244-274 IPB008284C 277-309","","","-49% similar to PDB:1UZ5 THE CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN FROM PYROCOCCUS HORIKOSII (E_value = 7.7E_48);-47% similar to PDB:2NRP MoeA R350A (E_value = 2.6E_40);-47% similar to PDB:1FC5 CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN (E_value = 3.4E_40);-47% similar to PDB:1G8L CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA (E_value = 3.4E_40);-47% similar to PDB:1G8R MOEA (E_value = 3.4E_40);","Residues 1 to 166 (E_value = 3.7e-48) place ANA_1918 in the MoeA_N family which is described as MoeA N-terminal region (domain I and II).Residues 179 to 316 (E_value = 2.2e-42) place ANA_1918 in the MoCF_biosynth family which is described as Probable molybdopterin binding domain.Residues 329 to 402 (E_value = 6.6e-09) place ANA_1918 in the MoeA_C family which is described as MoeA C-terminal region (domain IV).","","biosynthesis protein. (moeA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1920","2087605","2088333","729","5.99","-7.25","26118","ATGCGCCGTGCCCCGCCGGGACGAACGGTTCAGACACGACGCGTCATCACCTGCGAGGATGGGACCATGACGACCGGCGCGCTGGACCTTCCCGACACGGGCCGACTCGAGCTCGACGACGCCAAGGACGAGCTGCGCAAGGTGCTGCGGGCGCACCGACGCGCCCATCACCACCACCCGCCCCAGGGGCACACAGCGGACTGCGAGGCGCTGACTGAGCACGCTCTGGAGGCGGTGGCCGGCGCACAGAGGGTGGCGGCCTTCGTGTCCGTGGGGGCAGAGCCCTGTACCCGACTACTGCTGGAGCGGCTTCACGAGGGCGGCGTCCAGGTCCTGCTGCCGGTGCTCGGCCCTCGCCTGGCGCGCTGCTGGGGACTGTTCCAGGGAAGTGAGGACCTGGCGGAGCGGGCACCGAGGCGTCCTCCGGAGCCCAGTGGACCGACGCTGCCGGCCGAGGCGGTCGGCCAGGTGGACGCCCTCATCATTCCGGCACTGGCCGTGGACAGTGCCGGGCGCCGTCTGGGACAGGGCGGCGGCTGGTACGACCGGATGCTGCCGCTGCGCTCCCCGGAGGCCCACACCTTCGCCATCCTTCACCCCGAGGAGCTGGTGCCCGGACCGTTGCCGATGGAGGAGCATGACGAGCCCGTGGACGCCGTCATCACGGCCCAGGAGTGGTTCCTGCTGGCTGCCGGCTCACCGGCGCACTCCCTGTCGTCGGAGTCCTGA","MRRAPPGRTVQTRRVITCEDGTMTTGALDLPDTGRLELDDAKDELRKVLRAHRRAHHHHPPQGHTADCEALTEHALEAVAGAQRVAAFVSVGAEPCTRLLLERLHEGGVQVLLPVLGPRLARCWGLFQGSEDLAERAPRRPPEPSGPTLPAEAVGQVDALIIPALAVDSAGRRLGQGGGWYDRMLPLRSPEAHTFAILHPEELVPGPLPMEEHDEPVDAVITAQEWFLLAAGSPAHSLSSES$","5-formyltetrahydrofolate cyclo-ligase","Cytoplasm","5-formyltetrahydrofolate cyclo-ligase","hypothetical protein","5-formyltetrahydrofolate cyclo-ligase","","Dayan A., Bertrand R., Beauchemin M., Chahla D., Mamo A., Filion M., Skup D., Massie B., Jolivet J. Cloning and characterization of the human 5,10-methenyltetrahydrofolate synthetase-encoding cDNA. Gene 1995. 165(2):307-311. PMID: 8522195Maras B., Stover P., Valiante S., Barra D., Schirch V. Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase. J. Biol. Chem. 1994. 269(28):18429-18433. PMID: 8034591","","","

InterPro
IPR002698
Family

5-formyltetrahydrofolate cyclo-ligase
PTHR23407:SF1	$\"[41-240]T$	5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE
PF01812	$\"[42-223]T$	5-FTHF_cyc-lig
TIGR02727	$\"[42-223]T$	MTHFS_bact: 5,10-methenyltetrahydrofolate s

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.10420	$\"[42-231]T$	no description
PTHR23407	$\"[41-240]T$	ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE

","BeTs to 21 clades of COG0212COG name: 5-formyltetrahydrofolate cyclo-ligaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0212 is -om--zyq-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002698 (5-formyltetrahydrofolate cyclo-ligase) with a combined E-value of 2.3e-26. IPB002698A 88-114 IPB002698B 158-186 IPB002698C 196-221","","","No significant hits to the PDB database (E-value < E-10).","Residues 42 to 223 (E_value = 4.8e-27) place ANA_1920 in the 5-FTHF_cyc-lig family which is described as 5-formyltetrahydrofolate cyclo-ligase family.","","cyclo-ligase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1921","2088446","2089417","972","7.12","0.35","32878","ATGAGACCTCGCCACGGACTGCCCCGCCACCCCTCTCTCAGCGCCTCTCGGGATCCTCAGGATCACGGCGGGTCGCCGCGCTCCATCGCCTCCGACTCCCGTCCGGCCCGCCCCAGTGGCCGGGCCGGATGGACCGGATGGGCCGGGGGCCGTCCATCGCTTCTGCTGTGGCGCCATCGCCACCTGGTGGTGGCACTCTGCCTGGGAACCGCGGTCCTGGTGGCCCTCAGCGTGCTGCGTCCCGGCCCCGAACGCGGGCAGCAGGTTCTTGTCGCCTCGCGCTCGATCAGCGCCGGAGCGGTCCTCACCGAGCAGGACGTCTCGATCAGCAACCTTCCGGCCGGCGCCCTCCCCCAGTCCCCGTTGACCTCCGTGGGGCAGGTGGTCGGGAGTCGGGCCGCCATCTCCCTGGAGAAGGGCACGGTGCTGACGGCCTCAATGACCAGCGGCTCCTTGGCCCAGCAGCTGGGAGACGACGAGCGACTGGTCCAGGTGCCTATCGACGTCGGAGCCGAGCTGGCGCGCCCCGGCGCGCGGGTGGACATCATCGGGCAGGCCTCTGAGGACTGGGCGCCGCCGGGGCAGAACGACGCCTCTCAGGGCGGGACGGCACAGAATCCCGGAGAGCAGTCCGAGTCCCCCACCGCACCGAAAGACCCGGGGAACACCTCGACACCGAGTCCCACCGGAAGCCCCGACGCGCCTTTTTCGCCAACCGACCAGGAATCACCAGGATTTCAAGAGTCTTCTCTAAGCATTTCCCAAGGAATACCGGCAGCGCCTTTTGGAACACACAGCACAGTTCTCTGCTCCGGAGCGCGAGTAGTGATGATTCAACAGGTCGGAGAGGGTGGACAATGGACAGGAAACAAGAAAGTAACACTTATCACACTGGCTATTCCTGCAAGTAGCGCTACTCTGGTAGTTGGCGCGGCAACGAATAGCACGCTCGGCATTGCGCTGAGCCCGTAA","MRPRHGLPRHPSLSASRDPQDHGGSPRSIASDSRPARPSGRAGWTGWAGGRPSLLLWRHRHLVVALCLGTAVLVALSVLRPGPERGQQVLVASRSISAGAVLTEQDVSISNLPAGALPQSPLTSVGQVVGSRAAISLEKGTVLTASMTSGSLAQQLGDDERLVQVPIDVGAELARPGARVDIIGQASEDWAPPGQNDASQGGTAQNPGEQSESPTAPKDPGNTSTPSPTGSPDAPFSPTDQESPGFQESSLSISQGIPAAPFGTHSTVLCSGARVVMIQQVGEGGQWTGNKKVTLITLAIPASSATLVVGAATNSTLGIALSP$","SAF domain containing protein","Membrane, Periplasm","C. elegans COL-93 protein (correspondingsequence W05B2.5)","hypothetical protein predicted by Glimmer/Critica","SAF domain","","","","","

InterPro
IPR013974
Domain

SAF domain
PF08666	$\"[87-149]T$	SAF

noIPR
unintegrated

unintegrated
tmhmm	$\"[61-79]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 87 to 149 (E_value = 2.1e-12) place ANA_1921 in the SAF family which is described as SAF domain.","","elegans COL-93 protein (corresponding sequence W05B2.5)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1923","2089520","2089912","393","6.74","-0.07","14011","ATGATTAAGGGATTCAAGGAGTTCATTGCCCAGGGCAACGCCCTCGAGCTCGCCGTCGCCGTCATCATTGGTGGCGCGTTCAAGCCGATCGTTGACTCGATCACCACCGTCATCATGACCATCCTCGGTCAGCTCATCGGCCAGCCGAACTTCGATTCCGTCGGTCAGTTCAAGATCTTCGCGAGTGCCGATAAGTTCGTTCAGCCCGGCACGATCATTACCGCCGTGGTGAACTTCCTGCTCGTGGCCGCCGCGGTCTACTTCGCCATTGTCATGCCGATGAACAAGGTCAGGGAGCGCATGGCCAAGCAGAAGGCCGCCGAGGAGGCCGCCGAGGTCTCCGACGTCGAGCTGCTCACCGAGATCCGCGACCTGCTCGCCGCCAAGCGCTGA","MIKGFKEFIAQGNALELAVAVIIGGAFKPIVDSITTVIMTILGQLIGQPNFDSVGQFKIFASADKFVQPGTIITAVVNFLLVAAAVYFAIVMPMNKVRERMAKQKAAEEAAEVSDVELLTEIRDLLAAKR$","Large conductance mechanosensitive channel protein","Membrane, Cytoplasm","large conductance mechanosensitive channelprotein","large-conductance mechanosensitive channel","large conductance mechanosensitive channel protein","","Chang G., Spencer R.H., Lee A.T., Barclay M.T., Rees D.C. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 1998. 282(5397):2220-2226. PMID: 9856938Moe P.C., Blount P., Kung C. Functional and structural conservation in the mechanosensitive channel MscL implicates elements crucial for mechanosensation. Mol. Microbiol. 1998. 28(3):583-592. PMID: 9632260","","","

InterPro
IPR001185
Family

Large-conductance mechanosensitive channel
PD007253	$\"[5-45]T$	Q9A2H6_CAUCR_Q9A2H6;
PR01264	$\"[4-18]T$ $\"[78-86]T$ $\"[88-97]T$	MECHCHANNEL
PF01741	$\"[1-129]T$	MscL
TIGR00220	$\"[1-129]T$	mscL: large conductance mechanosensitive ch

noIPR
unintegrated

unintegrated
tmhmm	$\"[15-35]?$ $\"[71-91]?$	transmembrane_regions

","BeTs to 9 clades of COG1970COG name: Large-conductance mechanosensitive channelFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1970 is ---------drlbcefghs--j----Number of proteins in this genome belonging to this COG is 1","***** IPB001185 (Large-conductance mechanosensitive channel) with a combined E-value of 3.3e-37. IPB001185A 3-51 IPB001185B 67-96 IPB001185C 105-127","","","-50% similar to PDB:2OAR Mechanosensitive Channel of Large Conductance (MscL) (E_value = 1.2E_11);-50% similar to PDB:1VGP Crystal Structure of an Isozyme of Citrate Synthase from Sulfolbus tokodaii strain7 (E_value = 1.2E_11);","Residues 1 to 129 (E_value = 1.1e-30) place ANA_1923 in the MscL family which is described as Large-conductance mechanosensitive channel, MscL.","","conductance mechanosensitive channel protein (mscL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1925","2094755","2090397","4359","5.51","-35.30","156250","GTGCGTCTCCACGCCCAAGGGTCGATCGGCCTATATCTTGAGCGTATGACGCCTTCGTTCTTCTCCTTCGGCCGCAAACGGCGCGATGCTGCCCTGCGGGAGGAAGAACGCAAGGGAACCCGATCCTCGGCCGGCTCAGATCAAACCGCGAGCCGACGGCGTTTCGCCGCGGATCTGGGGGCTGTGGCCGCGGCGCCGCGTCAGCCTGAGTCCGCCCCTGCGCCGGCACCCCCCGCCCCCGCGCGCCCCGCGCCGGCACCCCCGCTGAGTGCGGCGGACGTCGAGCGGCGCGAGCGCATTGACACGGCCCTGTCCACCTGGCGCAGCCAGCTCGTGGACCTGGGGGGCGTCGCCAGCCTGGACGACATCACCCTGCTCGACGGCGTCGTCGACCTCACCGCAGCACACCCCTCCGGCCTGGCTCAGCTCTACGCAGGCCGCCCCACCAACCTGTCCAGCATCGTGCGCGAGCGCAACGCCCTTGGCGAGGCCCGCCAGTCCCTGCGCGAGGTCTCGGCGCGCACTGACGTCCTGGCCCGCCAGTTCGGCGTTGCCCCGGTCTACTTGGCCATTGGGGTGGCCACCTGGAACGAGACGGTCCCCGAGGACGGTGAGGACGACGGCAGCATCCACCTGGCTGACGGCGCCTCACCGGAGGCGGACCTGACCGCCCAGATCCCGCATGTCGAGCGCATCGCTGCCGAGCACGCCGCCCGCAACGCCCTGGCCGCCGCCGGCCTGACTGTCCCCGAGGCTCCCTCGGCCCCGCGCGTGCGCACGGTTAACGCCCCGGTCCTGCTGCGCCCCGTGCGCCTGACCACCGCCACCGCGGACGCCACCCTCACCCTGGACCCCACCATCGAGGTCAACCCGGTCCTCACCCGCGCCCTGCGCCGCTACCAGTGCACTACCGACATCGGGGACATCGCCCGCGCCGCCCTGTCCTCGGCGGGCTTCACACCGCGCGCGGCCCTGGCCCGCATCGGCGCCTTGGGCCGGCAGTTCCTGCCCGGCTTCGAGATCCACGAACGGCTCGTCGTCGGCGCCTTCGTCCACCCCGGTCAGGCCCTGGTGGAGGACTTCGACGCCGTCCTGGAGCGCTCACGCACCTCCGCCCTGGTCGCCGCCATCGCCGGGGACGAGGGCGCCCGCGAGGCCCTCAGCGTCGAGCTGCCCCCCGCTGTCCCCACTGATCGCGTCCCCGGCGCCGAGCGCGGCGTGGGTGATCTGGAGCCCGCCCAGCTCGACGTCATCGAGGCGGTGGGCACCGGGGCGAGCTTCCTCATCGACGCACCCCCCGGCTCCGACGTCGCCGGCACCCTGGCCGCCGTCTTCGCCGACGCCGCCGCCTCCGGACGCACCGTGCTGCACGTGCCCGCCACCAGCGCCGACGGGCACGCCGTCGCGGCCGCCCTGCGCGAGGAGGGTCTGGGATCCATGGTCCTGGACCTCACCGAGGACGCCGCCTGGCGCCAGCACGCCTCCGAGGGCATCCGCGAGAGTTTGGGCGTCCAGCCGCCCCAGCTCGACGTCGCCGGGATCATCTCCATGCGGGACCGTCTCACCTCGGTCCGCTCCCGCCTGGACCGCTACGTGCGCGCCCTGCACCGGCCCCGTGAGCCCTGGTCGGTCTCCGCCTACGAGGCGCTGCAGAAGCTCGCCGAGCTCACCAGCCGCCGCGACCGGGCCACCACCCGGGCCCGCATCGACGCCGAGCACCTGGGTCGCCTCGACGAGGACGGCCGAGAGCAGACCCTGACCCTCCTGCGCCGCGGGCACGCCCTGGGGCTGTTCACCCCGGAGGTCTCCTCCAGCGCCTGGAACGGGATCCCGGTGGAGGATATGGACGAGGCCACCGACGCGCTCGTCCACCTGCGTGCCCTGGCCAACGACCTGCTGCCCACCATCCAGGAGCACACGGCCGTGGTCGCCCGCACCACCGGCCTGAGCCGGGCCCGCAACCTGGGCCAGTGGATCGAGCAGCTTGACATGTTCGACGGCGTGCGCGAGTCCCTGGACGTCTTCCTGCCCGAGGTCTTCGAGCGCTCCGCCGCCGACATGGTCATCGCCACCGCCTCCAAGCGCTGGCGCGACGAGCGGGGCATCCACATGGACGGCTCGCGGCGCCGGCGCTTCACGCGCCAGGCCAATGACCTGGTGCGGCCGGGCCGCGTCGTCGATGACCTGCACGCCGAGCTGGTCAAGGTCCAGCGCCGCCGCGAGGTGTGGCGCCGTCACGACCCCGACGGCGGCTGGCCCCGCCTGCCCCAGGGCCTGGACGAGATGCGGCGCACCGCCGGCCGAGCGCGCGGCGCCGTGGTCGAGGTACAGCCGCTGCTGGGGCGCGCCCAGGACTCCCCGGTGCTCATGGAGATGCCCCTGGAGGATCTCCTGGAGCTGGCCCGCTCCCTGGCCGCCGACGACCTCACCGCCCAGAAGCTCCCCGAGGTCAACCGCATCCGCACCGAGCTCGAGGCTCTGGGGCTGAACGACTTCGTGGCGGACATGGCCGCCCGCGGCGTCGAGGCCGACCAGCTCGAGCCCGAGCTCACCTACTGCTGGTGGTCCTCCCTGCTGGCGCAGACCCTCGCGGCCGACCCCGACCTCGGTGGTCTCGACGCGCGCGCCCTGTCCCACATGGCCGTCTCGCTGCGCGAGCTCGACGCCGCCCACACGCGGTCCCTGTCGGGCCCCGTGGCCCAGGCCTGCGCCCGGCGGGTGCGGGCCGCCGTCGAGCAGGACAAGGCCGACGCGCGCGCCCTGTATATCGCCCTGGCCCGTGAGGACGGCGTCCCGCTGCGGGAGATCATCGACGCCCACCCCATGGCCCTGCTGGCCCGGCCGATCTGGATCGTCCCGCCCACACTCGTGCCCCAGATCTTCTCGCCCACCGCGGTGGTGGACCTGGCTGTGTTGGACGCCTCCACGCCCATGCCCGTCCCGCAGGTGCTGCCCGCCTTCGTGCGCGCCGACCAGGTGCTCGTCGTCGGCGACTCCCGGCGTGCCACGACCGGCCTGGCCGCAGAGCTCGGCCCGCTCCTGCCCTCGCGCACCCTGCCGACGGCCCGCAACAGCCTCGACGCCGGCATCGCCTCCTTCCTGGCGGCCAACGGCTACGAGGGGGTCGTCGAGGCCGTGCCCTCCCCGCCGGGGGACACCTCCCTGACCCTGGAGCTCGTGGACGGGCGGGGCATGCCGGCCCCCGGGCAGACGGCGGTCGAGACAGTGGAGGCCGAGGTCTCCCGCGTCGTCGACATGGTCATTGACCGGGCCCTGACCCGTCCCGAGGAGTCCCTGGCCGTCATCGCCCTCAACCGGCTGCACGCCGATGCCCTGCGCTCGGCCATCACCCGGGCGGCCGCCGGCGCCCCCGCACTGGAGGAGTTCTTCGCCCCCGGGGCGGCCGAACCCTTCACCGTCGTCGAGCTGGCCGAGGCCCGCGCCCTCCAGCGCGACCACATCATCATCTCGGTGGGTTACGCCAAGACCCCGCACGGGCGCACCATCCACAACTTCGGGCCCGTCTCGGACCACAGCGGCATGGTGGGGCTCGTCGAGGCCCTGTGCGCCTCGCGGGGCAGCACCCAGGTGGTCTCCTGCCTGGCGGCCGGCGACATCGACCGCGACCGGCTGCGCGCCCCTGGGGCCCGCCTGCTGCGTGAGGTCCTGGCCCGGGCCGAGGACTCCTCCCAGTCCGGCAACTCCGCCGGCAAGGTGCCCGACCGGCTCCTGGTGGACCTGGCCGAGCACCTGTGGCGCAAGGGCCTGTCGGTCGTCCCGCGCTACGGGACCGACGGCGGCGTGCGCATCCCGCTGGCCATCGGCCACCCCGACTACCCCGACGAGCTGCTCGTGGCGGTCCTGACCGACGACGTCGACTACATCAGCGAGCCCAGCCTGCGCCGGCGTGACCGGCACCGCGTCGAGCGCCTTGAGCGGCGCGGGTGGCGCGTCCACATGGCCTTCTCCGCCGGGGTGTTCGTGGACCCGGAGGCCGAGGCGAAGGCCGTTGAGGAGCTCGTCTTGGCCGTCCTGGTCGAGCGCCAGGGGGAGGCCGTCCCGGCCATGGAGGCCGTGCCGGACCGTGTCGACGACGCGGTGCGCGCCGTCCCCGAGGCGCCCGAGCCCGAGGCCACCGAGGCCCACGAGCGCACCGAGCGCCCCCGCATCGCCCAGGGGCTGCCGCTGCAGGCCTATTCCGACGACCAGCTCGATGACCTCATGGCCTGGATTCGCTCCGACGGCGTGGGCCGCTCCGAGGCCGGGGAAGTCGAGGAGCTGCGGTCCGCTCTGGCGCTGCGTCGCCGCGGATCGGGGATCGACGCGGTCCTGGCCAACGCCGTGCGGCGCACCCGCTGA","VRLHAQGSIGLYLERMTPSFFSFGRKRRDAALREEERKGTRSSAGSDQTASRRRFAADLGAVAAAPRQPESAPAPAPPAPARPAPAPPLSAADVERRERIDTALSTWRSQLVDLGGVASLDDITLLDGVVDLTAAHPSGLAQLYAGRPTNLSSIVRERNALGEARQSLREVSARTDVLARQFGVAPVYLAIGVATWNETVPEDGEDDGSIHLADGASPEADLTAQIPHVERIAAEHAARNALAAAGLTVPEAPSAPRVRTVNAPVLLRPVRLTTATADATLTLDPTIEVNPVLTRALRRYQCTTDIGDIARAALSSAGFTPRAALARIGALGRQFLPGFEIHERLVVGAFVHPGQALVEDFDAVLERSRTSALVAAIAGDEGAREALSVELPPAVPTDRVPGAERGVGDLEPAQLDVIEAVGTGASFLIDAPPGSDVAGTLAAVFADAAASGRTVLHVPATSADGHAVAAALREEGLGSMVLDLTEDAAWRQHASEGIRESLGVQPPQLDVAGIISMRDRLTSVRSRLDRYVRALHRPREPWSVSAYEALQKLAELTSRRDRATTRARIDAEHLGRLDEDGREQTLTLLRRGHALGLFTPEVSSSAWNGIPVEDMDEATDALVHLRALANDLLPTIQEHTAVVARTTGLSRARNLGQWIEQLDMFDGVRESLDVFLPEVFERSAADMVIATASKRWRDERGIHMDGSRRRRFTRQANDLVRPGRVVDDLHAELVKVQRRREVWRRHDPDGGWPRLPQGLDEMRRTAGRARGAVVEVQPLLGRAQDSPVLMEMPLEDLLELARSLAADDLTAQKLPEVNRIRTELEALGLNDFVADMAARGVEADQLEPELTYCWWSSLLAQTLAADPDLGGLDARALSHMAVSLRELDAAHTRSLSGPVAQACARRVRAAVEQDKADARALYIALAREDGVPLREIIDAHPMALLARPIWIVPPTLVPQIFSPTAVVDLAVLDASTPMPVPQVLPAFVRADQVLVVGDSRRATTGLAAELGPLLPSRTLPTARNSLDAGIASFLAANGYEGVVEAVPSPPGDTSLTLELVDGRGMPAPGQTAVETVEAEVSRVVDMVIDRALTRPEESLAVIALNRLHADALRSAITRAAAGAPALEEFFAPGAAEPFTVVELAEARALQRDHIIISVGYAKTPHGRTIHNFGPVSDHSGMVGLVEALCASRGSTQVVSCLAAGDIDRDRLRAPGARLLREVLARAEDSSQSGNSAGKVPDRLLVDLAEHLWRKGLSVVPRYGTDGGVRIPLAIGHPDYPDELLVAVLTDDVDYISEPSLRRRDRHRVERLERRGWRVHMAFSAGVFVDPEAEAKAVEELVLAVLVERQGEAVPAMEAVPDRVDDAVRAVPEAPEPEATEAHERTERPRIAQGLPLQAYSDDQLDDLMAWIRSDGVGRSEAGEVEELRSALALRRRGSGIDAVLANAVRRTR$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 4 clades of COG1112COG name: Superfamily I DNA and RNA helicases and helicase subunitsFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1112 is aompk-yqv-r--cef--s-u----wNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1927","2096022","2095084","939","5.78","-6.94","32087","ATGACTGATGACAACGTCGTCCTCGTCGGAGTCGATGGTTCGCCGGAGTCCCTGGCGGCAGTGGACTGGGCTGTGGCACGCGCTGAGCGCCAGGGCTGGCGTGTTCACATCCTGTGCGCCTACTCCCTGCCCTCCTTCACCACTGCCTCCCTTGACGGCGGCTACGCAGCGCTCGACGACTCAGCCATCAGGTCCGGCGCCCAGGCCGTCATTGACGAGGCCGTTGAGCGCGTCAAGAAGGCCGGAGTCACCGTCACCTCCTCCCTGGAGACCGGGGACCCCGCCGGGGTTCTCGTCGACCTCTCCGAGGAGGCGGCTCTGGCCGTCGTCGGCACCCGAGGCGGCGGTGGCTTTGCCGACCGGCTCCTGGGAACCGTCTCCTCCGCCCTGCCTGCGCACAGCCACTGCCCGGCCGTCGTCGTTCCTCGGCACAACGAGGGCGCCGACTACACGCCGGTGCGGCGCATCGTCGTCGGGGTCGATGGCTCCTCCTCGGCTCGCCGGGCCCTCAAGTGGGCTGTGACCGAGGCGGAGGCGTGGGGTGCCGAGCTCACCGCCATCGCCGCGGTGCCGATGGCCTCCGGTGCCGGGGCGCTGGCCTGGCTGCCTGCCGCGGTCGATCGTGAGCAGGTCCTGGCCGATGTCCGCTCCGGACTCGACCGCGCCATCAATGAGGCCCTCGAGGGCCATGAAGGCGTCACGGTGCGTCGCCACGCCCTGGACGGAAATCCGGCCGAGCTCCTGGCCGAGTTCTCCACCGCTGTAGACCTCATCGTCGTCGGCTCGCGTGGACGCGGTGGCTTCTCCGGGCTCCTGCTGGGCTCCACCAGCCAGGCCGTCCTGTCCCACGCCTCCTGCCCCGTGCTGGTCGCCCCCACGCACCACGCCAAGGGGGAGCGGCGCACCTCGCGCACCTCCACCCCGTGGGGCCGGGCCTGA","MTDDNVVLVGVDGSPESLAAVDWAVARAERQGWRVHILCAYSLPSFTTASLDGGYAALDDSAIRSGAQAVIDEAVERVKKAGVTVTSSLETGDPAGVLVDLSEEAALAVVGTRGGGGFADRLLGTVSSALPAHSHCPAVVVPRHNEGADYTPVRRIVVGVDGSSSARRALKWAVTEAEAWGAELTAIAAVPMASGAGALAWLPAAVDREQVLADVRSGLDRAINEALEGHEGVTVRRHALDGNPAELLAEFSTAVDLIVVGSRGRGGFSGLLLGSTSQAVLSHASCPVLVAPTHHAKGERRTSRTSTPWGRA$","Universal stress protein UspA","Membrane, Cytoplasm, Extracellular","widely conserved protein in universal stressprotein family","hypothetical protein","UspA domain protein","","Nystrom T., Neidhardt F.C. Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. Mol. Microbiol. 1994. 11(3):537-544. PMID: 8152377Sousa M.C., McKay D.B. Structure of the universal stress protein of Haemophilus influenzae. Structure 2001. 9(12):1135-1141. PMID: 11738040Zarembinski T.I., Hung L.W., Mueller-dieckmann H.J., Kim K.K., Yokota H., Kim R., Kim S.H. Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(26):15189-15193. PMID: 9860944","","","

InterPro
IPR006015
Family

Universal stress protein (Usp)
PR01438	$\"[153-171]T$ $\"[252-264]T$ $\"[270-292]T$	UNVRSLSTRESS

InterPro
IPR006016
Domain

UspA
PF00582	$\"[4-142]T$ $\"[152-292]T$	Usp

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[7-148]T$ $\"[153-298]T$	no description

","BeTs to 14 clades of COG0589COG name: Universal stress protein UspA and related nucleotide-binding proteinsFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0589 is aompkzyq-drlbcefgh-n-jx---Number of proteins in this genome belonging to this COG is 2","***** IPB006015 (Universal stress protein signature) with a combined E-value of 1.7e-23. IPB006015A 153-171 IPB006015B 252-264 IPB006015C 270-292 IPB006015B 102-114","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 142 (E_value = 2.6e-14) place ANA_1927 in the Usp family which is described as Universal stress protein family.Residues 152 to 292 (E_value = 7.3e-26) place ANA_1927 in the Usp family which is described as Universal stress protein family.","","conserved protein in universal stress protein family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1928","2097110","2096217","894","5.37","-4.35","29623","GTGAAGCCCGCATCTGCGGGCCGGACGTCTCCAGTCCGAACCCGACAGCTCACCTCGTCGGCTCAACAGGAGAAAGCATTCATGTCCTCACGCACCACCGCACGTCACCGCAAAGCCACCCGCGCCCTTACCCCACTGGATGACTTTGCTCCCACCGCGCGCCGCGGTCTGGCAGTCGCCGCTTCGTCCGGCCTCGCCCTGACCATGATCGCTTCGGGAGCCAACGCCGCCGGCCACACTGAGGTCACCTCCTCCGGCACCATCGAGGCTTCCGGCGTGACCCCCGGGGTCGGCATCTTCGCCGCCAACGCCCGCGAGGCCCTGGCTGCCCGCCAGCAGGTCACCATCTCCCAGGCGAGCTGGGTCACCGAGGCCGCCCCCGAGGTGGAGGCTGTCGCCCCCGCTCCTGCGGCTCCTCAGACGCCCGCCGCCCCCGAGGCCCCCGCTGCTCAGGCTGAGCAGAACTCCTCTGAGGCCGCCGCCCCGGCTGCTGCGAACCAGGGCACTGACGCCGCTGCCGCTGACACTCAGGCCACCCCGGCGGCCGCCGCGCCGACCGGCACCGCCAACTCCTCTGTCGTGGCCATCGCCATGCAGTACGTGGGTGCCCCCTACGTGTGGGGTGCCTCCGGCCCGAGCGCCTTCGACTGCTCCGGCTTCACCTCCTACGTGTACGCCCAGGTCGGCATCAGCCTGCCCCGCACCTCCGGCGAGCAGGCCGTGGCCGGTACCCAGGTGTCCGCCTCTGAGGCCCAGCCCGGCGACCTCGTCACCTGGCCCGGTCACGTCGGCATCTACGCTGGTGACGGCAAGGTCATCGACGCCGGTGACGAGTCCACCGGTGTGGTCTACCGCGAGATCTGGGGCTCCCCGAGCTTCGTCCGCGTCGGCTGA","VKPASAGRTSPVRTRQLTSSAQQEKAFMSSRTTARHRKATRALTPLDDFAPTARRGLAVAASSGLALTMIASGANAAGHTEVTSSGTIEASGVTPGVGIFAANAREALAARQQVTISQASWVTEAAPEVEAVAPAPAAPQTPAAPEAPAAQAEQNSSEAAAPAAANQGTDAAAADTQATPAAAAPTGTANSSVVAIAMQYVGAPYVWGASGPSAFDCSGFTSYVYAQVGISLPRTSGEQAVAGTQVSASEAQPGDLVTWPGHVGIYAGDGKVIDAGDESTGVVYREIWGSPSFVRVG$","Cell wall-associated hydrolase","Extracellular, Periplasm","Protein p60 precursor (Invasion-associatedprotein)","P60 extracellular protein; invasion associated protein Iap","NLP/P60 protein","","","","","

InterPro
IPR000064
Domain

NLP/P60
PF00877	$\"[202-297]T$	NLPC_P60

noIPR
unintegrated

unintegrated
PTHR21666	$\"[189-282]T$	PEPTIDASE-RELATED
PTHR21666:SF1	$\"[189-282]T$	NLP/P60 FAMILY SECRETED PROTEIN

","BeTs to 13 clades of COG0791COG name: Cell wall-associated hydrolases (invasion-associated proteins)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0791 is ---------drlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 2","***** IPB000064 (NLP/P60) with a combined E-value of 1.3e-11. IPB000064A 208-221 IPB000064C 262-279","","","No significant hits to the PDB database (E-value < E-10).","Residues 202 to 297 (E_value = 1.4e-31) place ANA_1928 in the NLPC_P60 family which is described as NlpC/P60 family.","","p60 precursor (Invasion-associated protein)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1929","2098316","2097645","672","4.94","-14.57","24827","ATGACCGAGCTGATCGACACCACCGAGATGTACCTCAAGACCGTCTATGAGCTTGAGGAGGACGGTGTTCCCCCGCTGCGTGCCCGCATCGTCGAGCGTCTCGACCACTCGGGCCCCACGGTCTCCCAGACGGTGGCGCGCATGGAGCGTGACGGTCTCATCAAGGTCGCCGAGGATCGCTCCCTGGAGCTCACCGATGAGGGGCGCAGGCGCGCTACCGACGTGATCCGCAAGCACCGGCTCGCAGAAAGACTGCTCCTGGACGTCATCGGCATCGAGCGCCGATTCGTCCATGAGGAGGCCTGCCGCTGGGAGCACGTCATGAGCGAGCAGGTCGAGGAGCGCCTCGCTGATATCCTCGACGACGTCTCCACCGACCCCTTCGGCAACCCCGTCCCGCCGCGGACCGCGGAGCACCCGAGGCCCTCCGCCGACGAGGTCAGTGTGGACCGCTTCGCCGGACGCGAGACCACCACGGCCGTCGTCAGCCGCATCGGGGAGCCGATTCAGGCCGACGCGGAGATCATCGCCGGCCTCGAGGACGCCCAGATCGTCGCCGGGGCTGAGGTCGAGCTGCGTGTCAGTGCCGGTGGGGTGAGGCTCGTCGGGCCCTCCGGTGACCCCGTGGTGCTGGCCGACGACGTCGCCCGCCACCTCTTCGTGCGGCGCTGA","MTELIDTTEMYLKTVYELEEDGVPPLRARIVERLDHSGPTVSQTVARMERDGLIKVAEDRSLELTDEGRRRATDVIRKHRLAERLLLDVIGIERRFVHEEACRWEHVMSEQVEERLADILDDVSTDPFGNPVPPRTAEHPRPSADEVSVDRFAGRETTTAVVSRIGEPIQADAEIIAGLEDAQIVAGAEVELRVSAGGVRLVGPSGDPVVLADDVARHLFVRR$","Iron-dependent repressor IdeR","Cytoplasm","diphtheria toxin repressor homolog","iron-dependent repressor IdeR","iron dependent repressor","","Schiering N., Tao X., Zeng H., Murphy J.R., Petsko G.A., Ringe D. Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(21):9843-9850. PMID: 7568230Qiu X., Verlinde C.L., Zhang S., Schmitt M.P., Holmes R.K., Hol W.G. Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors. Structure 1995. 3(1):87-100. PMID: 7743135","","","

InterPro
IPR001367
Family

Iron dependent repressor
PF01325	$\"[3-63]T$	Fe_dep_repress
PF02742	$\"[65-135]T$	Fe_dep_repr_C
SM00529	$\"[26-125]T$	HTH_DTXR
PS50944	$\"[1-65]T$	HTH_DTXR

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[1-73]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:1.10.60.10	$\"[74-143]T$	no description

","BeTs to 15 clades of COG1321COG name: Mn-dependent transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1321 is aompkz--vdrlb-e---s--j-it-Number of proteins in this genome belonging to this COG is 2","***** IPB001367 (Iron dependent repressor) with a combined E-value of 1.4e-36. IPB001367A 8-48 IPB001367B 64-86 IPB001367C 97-112","","","-68% similar to PDB:1FX7 CRYSTAL STRUCTURE OF THE IRON-DEPENDENT REGULATOR (IDER) FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.5E_59);-68% similar to PDB:1U8R Crystal Structure of an IdeR-DNA Complex Reveals a Conformational Change in Activated IdeR for Base-specific Interactions (E_value = 1.5E_59);-64% similar to PDB:1BI0 STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR (E_value = 2.9E_55);-64% similar to PDB:1BI1 STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR (E_value = 2.9E_55);-64% similar to PDB:1BI2 STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR (E_value = 2.9E_55);","Residues 3 to 63 (E_value = 2e-21) place ANA_1929 in the Fe_dep_repress family which is described as Iron dependent repressor, N-terminal DNA binding domain.Residues 65 to 135 (E_value = 3.6e-28) place ANA_1929 in the Fe_dep_repr_C family which is described as Iron dependent repressor, metal binding and dimerisation domain.","","toxin repressor homolog (dtxR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1930","2099914","2098580","1335","10.79","16.83","47593","ATGACCTCACCGCGCCGCCCCGGCGGTGGCATCTTCGCCTCCTTGAGATTCCACAACTACCGGCTCTGGTTCCTGTCCGCCCTCGTGGCCAACACCGGGACCTGGATGCAGCGCGTGGCTCAGGACTGGCTCGTGCTGCGTGTCCTCACCGACGACTCCGCCTCCGCCACCGGCCTGACCACGGCCCTGCAGTTCCTCCCCATGCTGCTGCTGTCCGCCCACGCCGGCCTCGTCGCCGACCGGGTCGATCAGCGCAAGTTCCTCATCCTCACCCAGAGCGCCATGGGCCTGGTCTCCGCCGTCCTCGCCCTTGACGTCCTGGCCGGCACCGCCCGCCTGTGGCACGTCTACTTGGCCGCCTTTCTCACCGGTGTCGCCGCCGCCTACGACGCCCCCGCCCGCCAGACCTTCGTGGCGCGGATGGTTCCCGCCGAGCACCTGTCCAACGCCGTAGGCCTCAACTCGGCCTCCTTCAACGCCGCGCGCCTCCTGGGGCCGGCCCTCGCCGGCGTCGTCATCACCTGGGTCGGCGCCGGCTGGGTCTTCGCCGTCAACGCCGCCACTTTCGTCTTCCCGGCCGTGGCGCTGGTCGCCATGCGCGTGAGTGAGCTGGTGGACATGCCGCGCGCCCGCCGCGCCGCCGGCCAGCTCCGCGAGGGTCTGACCTACCTGCGCGGCCGCACCGACCTCGTCGTCATCATCGCCGTGGTCGCCGTCGTCTCCATGCTCACCCTCAACTTCCAGGTCACCATGGCCGCGATGGTGCGCACCGTCTTCCACCTGGAGTCCGACGCCTACGGCACCGTCTCCTCAGTCTTCGCCGTCGGCTCCCTCTCCGGGGCCCTGTGGGCGGCCCGACGGCGCAACCCCCGCCCCCGCACCGTCGTGCTGGCAACCCTCGCCCTGGGGGTGTTCACCCTCCTGCTGGCCGCCATGCCCACCTACCCGACCTTCACGGTCATGACGGTCCCGGTGGGCCTGTGCGTGCTGACCCTCCTGACCAGCGCCAACCAGACCGTGCAGATGACCACCGAGCCGTCCATGCGGGGGCGGGTCCTGAGTATCTACATGATGTTCTTCCTGGGGTCGACGCCGCTCGGCTCCCCGCTCATCGGCTGGGTGGCCGACGCCTGGGGGCCGCGCATCGCGATCGCGGTTGGCGGCATGAGCGCTGTCCTCACTGCGCTGGTGGCCGCCGCTTGGAGCTACAGGCACTGGAACCTGTCCCTGCACTACTCCTCCACCCGCCCCTACCTCCGGGCCGCGCCTAAGTCGCCGACACCGCCGAAGCCGCCGCAGTCCCCGCAGCAGACCCATGCCGACGACGCCGACTAG","MTSPRRPGGGIFASLRFHNYRLWFLSALVANTGTWMQRVAQDWLVLRVLTDDSASATGLTTALQFLPMLLLSAHAGLVADRVDQRKFLILTQSAMGLVSAVLALDVLAGTARLWHVYLAAFLTGVAAAYDAPARQTFVARMVPAEHLSNAVGLNSASFNAARLLGPALAGVVITWVGAGWVFAVNAATFVFPAVALVAMRVSELVDMPRARRAAGQLREGLTYLRGRTDLVVIIAVVAVVSMLTLNFQVTMAAMVRTVFHLESDAYGTVSSVFAVGSLSGALWAARRRNPRPRTVVLATLALGVFTLLLAAMPTYPTFTVMTVPVGLCVLTLLTSANQTVQMTTEPSMRGRVLSIYMMFFLGSTPLGSPLIGWVADAWGPRIAIAVGGMSAVLTALVAAAWSYRHWNLSLHYSSTRPYLRAAPKSPTPPKPPQSPQQTHADDAD$","Permease of the major facilitator superfamily MFS_1","Membrane, Cytoplasm","PimH protein","major facilitator superfamily MFS_1","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[11-444]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[23-376]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[15-437]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF7	$\"[15-437]T$	PERMEASE-RELATED
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[21-39]?$ $\"[58-78]?$ $\"[87-109]?$ $\"[113-133]?$ $\"[163-183]?$ $\"[189-209]?$ $\"[230-250]?$ $\"[264-284]?$ $\"[294-312]?$ $\"[318-338]?$ $\"[353-375]?$ $\"[381-401]?$	transmembrane_regions

","BeTs to 21 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","","","-37% similar to PDB:1HTT HISTIDYL-TRNA SYNTHETASE (E_value = );-37% similar to PDB:1KMM HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE (E_value = );-37% similar to PDB:1KMN HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDINOL AND ATP (E_value = );-38% similar to PDB:1M57 Structure of cytochrome c oxidase from Rhodobacter sphaeroides (EQ(I-286) mutant)) (E_value = );","Residues 9 to 438 (E_value = 2.1e-08) place ANA_1930 in the DUF894 family which is described as Bacterial protein of unknown function (DUF894).Residues 23 to 376 (E_value = 6.2e-34) place ANA_1930 in the MFS_1 family which is described as Major Facilitator Superfamily.","","protein ","","1","","","","","","","","","","","Tue Aug 14 16:39:49 2007","","Tue Aug 14 16:39:49 2007","","","Tue Aug 14 16:39:49 2007","","","","Tue Aug 14 16:39:49 2007","Tue Aug 14 16:39:49 2007","","","","","yes","","" "ANA_1931","2102636","2101599","1038","4.94","-21.36","34400","TTGGCTGAGATGCTAGTTGGGTGGCGTGTAGAAGAGCTCGATCTCGGCAGGGAACTCGCCCCAATCCTGCTTCTCTCTGAGGACGTCGAAGGTTTCTTTCTCTGCGATGTGCCATTGGATGGGGGTGTCGGTGCCGGTGGCTCGCACGGCCTTGACCTGGTCTTTTCCGATCTGGAGCAGTCCTTTTTTGACGCGTTTCACCTCGCCTGTCACTGGGTCGGTCTTGTAGGTGCTCTTTGGTTCGTTCGACCAGTGTCCTTTGATGGGGTTGGCGTAGCCGGGGCCTTTGGCGTCGATGAGGGCGAAGCCGTCGTAGCCGTCGAACTCGACGCCGTTGACGATATAGGACTGCTCGATGGGGACTCTGGTGATCTGCTCCTCGTAGAGTTGGGAGCGGGCGGAGCCGTAGTTCTTTCCCTTGCCCCACAGGCCGGGGCCGCCGTCGGATCGTCCGGGTCTGGGGGTGCGCAGTCCGGGGTAGTGGAAGCCGTTGCGAGGGCTCCACATGGAGGTGCTGGCTGCGCCGGTCTCGTCGTGGAGGAGTCTGCGGCGTGCGTTTCGGGCGTAGTGGCGCCATGCGGTTCGGTCGGTGCGCCACAGGTAGGAGGCGTACCTGGCCTCGCGGGTGGCGGCGTAGGCGCCGCGGGCCATTTGCCCGCCCATGGCGCTGGCGGCTCCACCGCCGACCGTGGTCAGGGCGGCTGTCGCCATGTCCAGGGCGATCTCGGCTGGGGTGTGGGTGGACAGGTAGCGGGCCACCGTGCCCCGTGGGTCGCGCATGAGGGCCGCTGCCCCGCGAGCGCCCCCGAACACGGTGGCCACGCCCATGCCGATATCGAAGGCCAGGCCGAGCGTGCCCCCGGACAGGAGGATGAGGGCCCCAGCCAGAAGCATCAGCCCCAGCTTCTGCTCCCAGCTCAGCGACTCCCACACCGTCCCCAGCGCATCAAGAAGCCCCGCCAATCAGTAGGGCTGCCCTTCGCCCAGGCTGTCGGCCATGCTCCGCGTGAGACCGGGAACCATGGCAATGACGAGTAA","LAEMLVGWRVEELDLGRELAPILLLSEDVEGFFLCDVPLDGGVGAGGSHGLDLVFSDLEQSFFDAFHLACHWVGLVGALWFVRPVSFDGVGVAGAFGVDEGEAVVAVELDAVDDIGLLDGDSGDLLLVELGAGGAVVLSLAPQAGAAVGSSGSGGAQSGVVEAVARAPHGGAGCAGLVVEESAACVSGVVAPCGSVGAPQVGGVPGLAGGGVGAAGHLPAHGAGGSTADRGQGGCRHVQGDLGWGVGGQVAGHRAPWVAHEGRCPASAPEHGGHAHADIEGQAERAPGQEDEGPSQKHQPQLLLPAQRLPHRPQRIKKPRQSVGLPFAQAVGHAPRETGNHGNDE$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Dasso M. RCC1 in the cell cycle: the regulator of chromosome condensation takes on new roles. Trends Biochem. Sci. 1993. 18(3):96-101. PMID: 8480369Roepman R., van Duijnhoven G., Rosenberg T., Pinckers A.J., Bleeker-Wagemakers L.M., Bergen A.A., Post J., Beck A., Reinhardt R., Ropers H.H., Cremers F.P., Berger W. Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1. Hum. Mol. Genet. 1996. 5(7):1035-1041. PMID: 8817343","","","

InterPro
IPR000408
Repeat

Regulator of chromosome condensation, RCC1
PS00626	$\"[43-53]?$	RCC1_2

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-50% similar to PDB:2GF2 Crystal structure of human hydroxyisobutyrate dehydrogenase (E_value = );-50% similar to PDB:2I9P Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+ (E_value = );-52% similar to PDB:1CJY HUMAN CYTOSOLIC PHOSPHOLIPASE A2 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1932","2100150","2101673","1524","9.73","12.98","55416","ATGAGAGAGGGGTGGGCGTTGAACGATCACGGCCATAGGAACATTCCGAGCCCAGGAGCCGAGCAGCCTCCTCGGATCTGGCCGGCCTCACGGCGCCCACCCGAGCGAGAGGGCCAGGAGGAAACAACGCCGTCGGAACGACCGCCGAGACAGGAGTGGTGGGAACGATTGCGTGACCGCACGTCGAGGTCCCGGATCTTCCTGGCGCTGCGCCGAGTGCGGGCCGTTGCCTCCTGGTTCGCGCTGCTGGTGGTTCTCGTGGCCGTGGTGGTCTCGCCGACGGTCCGCACCGCACTGGGGGCCTGGATCGGGTGCATGTGGCTGGTGGTGTGCTGGTTCACTCTGGCCCGAGCCAAGACCGTCTCCTGGGCACTGACCTCGGGAGTGTTCGCCACCGGGATGCCCTTGGCGCTGCTGATCGCCATGGCGAGCCTGTGGGTCTGCAGCGCCGCCGGCGTCAGTCCGTCCAGCACAGCCGCATCCATAGTGGTCGCCTCCCTGGTGGAGGAAGTTCTCAAGCTGACGCCGTTGGCGGTTCTCACTTTGGTGGCTCCAGGGCGGGTGCGCCGTTTCCTGGTGAGCGACTGGATCGTTCTGGGGGTGGCGACGGGCGCCGCTTTCGAAGTGGTCGAGGAGGTCACCCGCCGCATCACGCTGCTGAACGGTGGCGGCAGCCTCCTGGATAGTCTTCTCTGCCCCAAGGGCGGGGTGCGCCAGGTGGAGTGCAGCGGCGCAACGACTTACTCCCTGAGCCCGTTCTCCGGGGTTGCCGGGAACATCTTCCCCTACGCCGGGCACGCAATTATCACCGGACTGGTGACCGGGGCGATCGGGCTGGGGATCGCCCTGTGGCGCCGTGCTCGGGTGCATCGCGGTGGATACAGGGCCGCGTTGCAGATTCTCTCCCCGGTGGTGCCGCTGTGGACGTGGTGGGTGGCGGTGGTCGACCACATGGGGCGCAACGCCTCCGACTACGTGATGTGGTTGCAGACGGGCGGCGAGGCGCCGTCGTGGCCCATTGAAGTGACGGCATCGCTGACCGGCTACGGGCAGGGACGTGGCGTCATTCTTCTCCTGATGCTGGCTCTGGCCTGGGTCATTGATAGCCGCACACTGTGGAGCGGTGGGTATGTGAGCACCCTCGAGAGCGACAACTACGGGAACCGATGGGGCCCGTGGCGGTGGCGCGTCTGGGCTGGAGTGCCACGCAATGCCTTCGGGCGCTTCTTGGCCGACGGCGCCTGCCTGGTCTCCGTCGTCGGGGTCGAGTGGCGGTGGGCGTGGATGACGCTCATGGAGGCGGCCACGTTCCGCGAGCCGAGACTGCTGCTGGAGACTCCCGCGAAGCTGCGGATCGCACGGGAGGAGGCGGCGCGCGCCGAGCTCGATCCGGCGCCGGAGCAGTGGTGGAGGGCACGGCTCGCAGGGCTGTGCGCGGTGGTGGCCGGCTTACTCGTCATTGCCATGGTTCCCGGTCTCACGCGGAGCATGGCCGACAGCCTGGGCGAAGGGCAGCCCTACTGA","MREGWALNDHGHRNIPSPGAEQPPRIWPASRRPPEREGQEETTPSERPPRQEWWERLRDRTSRSRIFLALRRVRAVASWFALLVVLVAVVVSPTVRTALGAWIGCMWLVVCWFTLARAKTVSWALTSGVFATGMPLALLIAMASLWVCSAAGVSPSSTAASIVVASLVEEVLKLTPLAVLTLVAPGRVRRFLVSDWIVLGVATGAAFEVVEEVTRRITLLNGGGSLLDSLLCPKGGVRQVECSGATTYSLSPFSGVAGNIFPYAGHAIITGLVTGAIGLGIALWRRARVHRGGYRAALQILSPVVPLWTWWVAVVDHMGRNASDYVMWLQTGGEAPSWPIEVTASLTGYGQGRGVILLLMLALAWVIDSRTLWSGGYVSTLESDNYGNRWGPWRWRVWAGVPRNAFGRFLADGACLVSVVGVEWRWAWMTLMEAATFREPRLLLETPAKLRIAREEAARAELDPAPEQWWRARLAGLCAVVAGLLVIAMVPGLTRSMADSLGEGQPY$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-97]?$	signal-peptide
tmhmm	$\"[75-93]?$ $\"[99-117]?$ $\"[127-147]?$ $\"[260-282]?$ $\"[297-315]?$ $\"[347-367]?$ $\"[474-494]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-39% similar to PDB:1EYS CRYSTAL STRUCTURE OF PHOTOSYNTHETIC REACTION CENTER FROM A THERMOPHILIC BACTERIUM, THERMOCHROMATIUM TEPIDUM (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1933","2102665","2103306","642","5.74","-5.36","23698","ATGGAATGGCGCCTACACATGAGGCGGCGGGCTCTTGGTGACCCGGTCTCGGAGGGGCGTCGGGTGTGGGAGTGGATTCAGCGGGTCAGGCCCCTGCACCCCTCCTTGGACCTGTGGCGCCCCACCGCCGAAAGCCGTGAGGAGGCTGAGCAGGCCCCGCCCATCACCCAGGACTACCTCCTCCACTTAATCCACGGCGTACAAGCCATCTCCGACGACCCCGACTTCGGCCTGGCCCCAGGCTTCTCCGGACAGATCAACCAAGGCAACAAGCTCGAGCTGAGTTTCAACATGCCCAACCCCGGAGACGCCAGCATCGGACTCATGATCGGAGAAGCCCTCGGCGCCGCCCTGGACGCCAGCGAGGACCTGGCCGACGCTCTCATGCACACCACCGCCAGCACCTTCGCCCCTAACACCATCGGAGGACTGTCGCGAAGCGACCACCCAACCAGAAACCTCAACCGGGACGGCCCCTACCCCTTCTACTACGTTCCGGGCTGGAAGATGTTCTTCGCCTCCGACTCACCCCACTACCAGCGCGCCACCCAACTGGCCACCCGAACCGCTCCCGTGGCCAACGGCGCCATCTTCACCTTCGGCACCCCCGACACCTACCCCACCATCCTCAACCAATGGTGA","MEWRLHMRRRALGDPVSEGRRVWEWIQRVRPLHPSLDLWRPTAESREEAEQAPPITQDYLLHLIHGVQAISDDPDFGLAPGFSGQINQGNKLELSFNMPNPGDASIGLMIGEALGAALDASEDLADALMHTTASTFAPNTIGGLSRSDHPTRNLNRDGPYPFYYVPGWKMFFASDSPHYQRATQLATRTAPVANGAIFTFGTPDTYPTILNQW$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-56% similar to PDB:2CIG DIHYDROFOLATE REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS INHIBITED BY THE ACYCLIC 4R ISOMER OF INH-NADP A DERIVATIVE OF THE PRODRUG ISONIAZID. (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1934","2103350","2103769","420","4.66","-11.61","15792","ATGGGCGTCAACTACCTCTACCCAGCCATCAATCCAGGACACATTATTGTCGATGTCGACACTTTTCTTTACGAAGGGTCAAGAAAATGGTCAGACAGCAGAGCATTGCGCTGGAGCGAGGAAGACATAACAGATGCCGACATCGTTCTTAATCCAGAAGGGCCATCAACAATCATCAGCCATTTCAAAGACAATCGACTGATCTCTGCCAGCGGACTAGATTTTGAGGAGGCGGCCAATATCGCCGCCTGGGTCCGTTCACTGAACCCCGACCCAAATCTGGTGCTGTGGTTCACCACCAGCGTCATCGACGGACACACTGTCCTTACACCTGGCATCACACCACAACAGGTCATCGACCAGTGGGTCAACCACACAGAGCACGACCCCTACATCGAGTACCCCCAGTACTTCCACTAA","MGVNYLYPAINPGHIIVDVDTFLYEGSRKWSDSRALRWSEEDITDADIVLNPEGPSTIISHFKDNRLISASGLDFEEAANIAAWVRSLNPDPNLVLWFTTSVIDGHTVLTPGITPQQVIDQWVNHTEHDPYIEYPQYFH$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-41% similar to PDB:1TYG Structure of the thiazole synthase/ThiS complex (E_value = );-41% similar to PDB:1XM3 Crystal structure of Northeast Structural Genomics Target SR156 (E_value = );-41% similar to PDB:2AJ2 X-Ray structure of hypothetical protein VC0467 from Vibrio cholerae: new fold. Northeast Structural Genomics Consortium target VcR8. (E_value = );-41% similar to PDB:2HAF Crystal structure of a putative translation repressor from Vibrio cholerae (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1935","2103781","2104410","630","5.19","-6.08","23259","ATGAGATGGGACCTCAGCTTCAGGCGACAAGCACTCGGCGACCCAGTCTCGGAGGGGCGTCGGGTGTGGGAGTGGATTCAGCGAGTCAGGCCGCTGCACCCCTCCCTGGACCTGTGGCGCCCCACCGCCGACAGCCCTCAGGAAGCCGAACAGTCACCACCCATCACCCAGGACCACTTCCTCCAACGCATCCAGCAGGCCCAAGTCGACTGGGAAAGTGAGAGCTTCGGCGTCGCCCCGGCCTTCTCCGGACAGATCAACCAGGGCAACAAGCTCACACTAAGTTTCAACATGCCCAACCCTGGAGACGCCAGCGTGGACCTGATGGTCGGCGAGGCGCTCGGGGCCGCCCTGGATGCCAGCGAGGACCTGGCCGACGCTCTCATGCACACCACCGCCAGCATCTTCGCCCCCGGCGTGATCGGAGCCCTGACTCGCGAAGACCGTCCGGTCACCCCAACTCCACCGCCTTACAGATACCTGCCGGGTTGGAAGATGTTCTTCGCTTCCGACTCACCCCACTACCAACGCGCCACCCAGCTAGCCACCCGATCCATTCCCGTGGCCAACGGCGCCATCTTCACCTTCGGCACCCCCGACACCTACCCCACCATCCTCAACCAATGGTGA","MRWDLSFRRQALGDPVSEGRRVWEWIQRVRPLHPSLDLWRPTADSPQEAEQSPPITQDHFLQRIQQAQVDWESESFGVAPAFSGQINQGNKLTLSFNMPNPGDASVDLMVGEALGAALDASEDLADALMHTTASIFAPGVIGALTREDRPVTPTPPPYRYLPGWKMFFASDSPHYQRATQLATRSIPVANGAIFTFGTPDTYPTILNQW$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-47% similar to PDB:1DDR MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE AND UREA (E_value = );-47% similar to PDB:1DDS MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE (E_value = );-47% similar to PDB:1DHI LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUTANT DIHYDROFOLATE REDUCTASE (E_value = );-47% similar to PDB:1DHJ LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUTANT DIHYDROFOLATE REDUCTASE (E_value = );-47% similar to PDB:1DRA CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1936","2106238","2104748","1491","6.44","-2.41","52094","ATGATCTGGAAGAATGCCGCCGTGAGCACACGTACCCCGACGAAGGCCTCATCTTCGTCCTCGCCCAGTCAGGTCTCTCGACTGGATCAGTTCTTCCACATCACTGAACGCGGTTCGAGCATCTCCCGAGAGATCCGTGGCGGCATCGTCACCTTCTTCTCGATGAGCTACATCCTCGTCCTCAACCCCGCGATCCTGTCCAAGGCGAGCCCCCCGGGAACCGAGGCCCAGCTCGCCGCAGGCACCGCCTTCGTCGCCGCAGTCATGACGATCCTCATGGGCGTCGTCGCCAACTACCCGATGGCCCTGGCCGCGGGCCTGGGGATCAACGCGATGGTCGCCTACACCCTCGTGGGCACCCAGGGCATGACCTACGCCGACGCCATGGGCCTCATCGTCATCGAGGGCATCATCATCCTCGTCCTGGTACTCACCGGCTTCCGGGAGGCCGTCTTCAAGGCCGTCCCCGACCAGCTCAAGACCGCGATCTCCGTGGGCATCGGCCTGTTCATCGCGCTCATCGGCCTGGTGGACGCCAAGATGGTGCGCCGCGGCGGCACCCCCCTGGAGCTGGGGCTGGGCGGCTCCCTCCAGGGCTGGCCGGTCCTCGTCTTCCTCTTCGGGCTCTTCCTCATGGTGGTGCTCCACGTGCGCAAGGTCCGCGGCGCCATCCTCATCGGCATCGCCTCGGCCACGGTCCTGGCCATCATCATCGACGCCGTCACCCACCTGGGCCCCTACAACGACGAGACGATGCCCGGTCCCGACAACCTCACCGGCTGGTCCCTGTCCGAGCCGCGTCTGGACGGTTTCCCGGTGGACCTGCCGAGCCTGTCGACGCTGGGCCACTTCAGCCTGCTGGGCAGTGTGCACAAGGTCGGGATCGTCTCGGTGATCCTCCTGGTCTTCTCCCTGCTGCTGGCCGACTTCTTCGACACGATGGGCACCATGGTCGCTATCGGCGCCGAGGGCGACCTGCTCGACGAGCACGGCAACCCGCCCAAGACGCGCGAGATCCTCGTCGTCGACTCCCTGGCCGCCATCGCTGGTGGTGTCGGGGGCGTGTCCTCCAACACCTCCTACGTGGAGTCCGCCGCGGGCGTGGGGGAGGGGGCCCGCACGGGCCTGGCCTCAGTGGTCACCGGCTGCATGTTCGCCCTGTCCATGTTCTTCGCGCCGCTGGTCAAGATGGTCCCCTACGAGGCGGCCACCCCGGCGCTGGTGGTGGTCGGTTTCCTCATGATGATGCAGGTGACCGACATCGACTGGAAGTCCCCGGAGATCGCTCTGCCGGCCTTCCTGACCATCATCATGATGCCCTTCTCCTACTCGATCACCAACGGGATCGGGGCCGGCTTCGTGTCCTACCTGGTCATCGAGGTGGCGCAGGGCCGGGCGCGGAGGATCCACCCGCTCATGTGGGTGGCCTGCGCGATGTTCGTCGTCTACTTCACCCTCGCCCCCATCAAGGCGATCCTCGGCGTCTCCTGA","MIWKNAAVSTRTPTKASSSSSPSQVSRLDQFFHITERGSSISREIRGGIVTFFSMSYILVLNPAILSKASPPGTEAQLAAGTAFVAAVMTILMGVVANYPMALAAGLGINAMVAYTLVGTQGMTYADAMGLIVIEGIIILVLVLTGFREAVFKAVPDQLKTAISVGIGLFIALIGLVDAKMVRRGGTPLELGLGGSLQGWPVLVFLFGLFLMVVLHVRKVRGAILIGIASATVLAIIIDAVTHLGPYNDETMPGPDNLTGWSLSEPRLDGFPVDLPSLSTLGHFSLLGSVHKVGIVSVILLVFSLLLADFFDTMGTMVAIGAEGDLLDEHGNPPKTREILVVDSLAAIAGGVGGVSSNTSYVESAAGVGEGARTGLASVVTGCMFALSMFFAPLVKMVPYEAATPALVVVGFLMMMQVTDIDWKSPEIALPAFLTIIMMPFSYSITNGIGAGFVSYLVIEVAQGRARRIHPLMWVACAMFVVYFTLAPIKAILGVS$","Xanthine/uracil/vitamin C permease","Membrane, Cytoplasm","Permeases","K06901 putative MFS transporter; AGZA family; xanthine/uracil permease","Xanthine/uracil/vitamin C permease","","","","","

InterPro
IPR006043
Family

Xanthine/uracil/vitamin C permease
PTHR11119	$\"[26-483]T$	XANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER
PF00860	$\"[42-451]T$	Xan_ur_permease

noIPR
unintegrated

unintegrated
PTHR11119:SF9	$\"[26-483]T$	XANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER
tmhmm	$\"[47-67]?$ $\"[77-97]?$ $\"[102-122]?$ $\"[128-146]?$ $\"[161-179]?$ $\"[198-217]?$ $\"[222-242]?$ $\"[287-307]?$ $\"[375-395]?$ $\"[441-459]?$ $\"[469-487]?$	transmembrane_regions

","BeTs to 14 clades of COG2252COG name: PermeasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2252 is -om-k---vd-lb-efgh-nuj--t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 42 to 451 (E_value = 1e-08) place ANA_1936 in the Xan_ur_permease family which is described as Permease family.Residues 151 to 460 (E_value = 0.0057) place ANA_1936 in the Sulfate_transp family which is described as Sulfate transporter family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1937","2106366","2111363","4998","6.13","-15.56","176264","ATGGCCGTGACCGAGGCAGCAGAGGACCCGGCCGCCGCGGCAGGTCCGCGCGAGCCGGGCTGGGAGGGATTCTCCTCGGCCACCCGCACCTGGTTCCTCGACGCCTTCCCCACCGGCCCCACCTCGGTGCAGGAGCGGGCATGGGCCACGATCGGCCGGGGTGAGAACGCCCTGGTCATCGCCCCTACCGGCTCGGGCAAGACGCTCGCGTCCTTCCTGTCCGCCATCGACCGCCTGGGGCGGGAGCCGGCCGCGGAGGAACAGGGGGCCGAGGCGGCAGGAGGGGGTGCCCGGGCTGAGGCCGACGGCGTGCGGGTCCTCTACATCTCCCCGCTCAAGGCGCTGGGAGCGGACGTGGAGCGCAACCTGCGCCGGCCGCTGGCGGGAATCCGCGCCGTCGGCCCCACCCGCCCGATCTCGGTGGGGGTGCGCTCGGGGGACACGCCCGCGCGGGAGCGTCGTCGGCTGCGCAGCCACCCGCCCAGCATCCTCATCACAACGCCGGAGTCGCTCTACCTCATGCTCACCAGCGCCGTGCGAGAGACGCTGCGGACAGTGGAGACGGTCATCGTCGACGAGATCCACTCCTTCGCCGGTTCCAAGCGCGGCACGCACCTGGCCGTGTCCCTGGAGCGCCTCGATGACCTCCTGGGGCGGCCGGCGCAGCGCATCGGCCTGTCCGCCACCGTCTCACCGCCGGAGGAGGTCGCCCGCTTCCTCGGCGGGCCGCACCCGGTGACGATCATCTCCGACGACGGCCGGGCGACACCGGAGGTCACAGTGTCCGTGCCGGTGGAGAACATGGCCCGCATCCCGGCGATCTCGGACCGGCGCACCCGGATGGAACGGGCCCTGGCAGCCCCCACGAGCGCGGGCGGCGGCCGCGGCTCCCGGCCCTCCGGGCTCGGACGGGCGGGGTCCTCGCAGGCCTGGCGCTCCGATAAGGCGCTGGGTCGAGCCATGGCGGCGGGGCGGGCTGACGAGCCCGGTGCGGGGGTGCCCGCCCGGGTGTCGGCCTCGATCTGGCCGCACCTTGAGAACGCGATCCTCGACCAGGTCCTGGCCCACCGCACGACGCTGGTCTTCGTCAACTCCCGGGGCGCCTGCGAGCGGCTCACCGCGCACCTCAACGAGGCCTACGCCGCGCGTCTCGGGGCGGTGGCACCAGCGCCGCAGGCGCCGGTTCACCGGGAGTCCTGGGAGATGGGAACCGGTTCGCACACCGAGCCCCTGGCGGCGGGCGCCCCGGTGATCGCCAAGGCACACCACGGGTCAGTCTCCAAGGAACAGCGTCTGGGCGTGGAGCGGGAGCTGGCCGCGGGCGAGCTGAGGTGCGTGGTGGCCACGGCCTCCCTCGAGCTCGGCATCGACATCGGCTCGGTCGACCTCGTGCTCCAGGTGGCGCCGCCCCCGTCGGTCGCTGCGGGCCTGCAGCGGGTGGGGCGCGCCGACCACCGGGTGGGCGGGCGGCCGCGCGGCGTCATCTACCCCGTGGAGCGCACTCACCTGGTGGACGCCGTCGTCGCCGCAGAGGGGATGCGCGCCGGGGAGATCGAGCGCACCGAGCTGGTGTCCAACGCTCTGGACGTGCTGGCCCAGCAGACGGTCGCCGCGGTGAGTGTGGCGGAGGGGCTGACGGCCGAGGCCTGGTTCACCGCCGTCAGGCGGGCGGCCCCCTACTCCTCGCTGCCGCGCCCGGCCTTCGACTCGGTCCTGGAGCTGCTGGCCGGCGGTTTCGCCTCGGCGGATCTGACGGACTTCTCGCCGCGGATCGTGTGGGACCGCGCCACCGGTGAGCTCAGTGCCCGGCCCAGCACGCAGCGGCTGGCGGTGGCCTCCTCGGGAACGATCCCGGACCGGGGCATGTTCCCCGTCGTCCTGCCCGAGGGGGCGCAGGATGCCGGGCGGCGGCGGGTCGGGGAGCTCGACGAGGAGATGGTGCACGAGTCCAGCCCGGGCGACATCATCACGCTGGGGACGTCGAGCTGGCGGATCCGCCAGATCACGGGGGACCGCGTCGTCGTCGACCCGGCCGAGGGGCGCAGCGCCCGCCTGCCGTTCTGGAAGGGCGAGGGGCTGGGCAGGCCGGCGGCCACCGGGCTCGCCAAGGGCGTCTTCCTGCGTGAGGCTCAGGCCTCCTTGCCGGCGGAGGCGGGAGCCGGGGAGTCGGAGGGCGAGCGGGCACTGCGGCAGCGGCTCACGGAGGCGGGGCTGGATGACCATGCCCGCAGCAACCTGCTGGCGCTGCTGCGCGAGCAGTACCGAGCCACCAGCGCCCTGCCGACCGATGAGACCCTGGTCCTGGAGCGCTATGAGGACGAGTCCGGCAGCTGGCGGATCATCGTCCACAGCACGCTGGGTCGGTGCGTCCACGAGCCCTGGGCGATGGCGATCCGGGAGCGGGTGCACCAGGTGCTGGGGGTGCGCCCGCAGATCATCGTGGCCGACGACGGCATCGTCCTGCAGATCCCGCCGGTTGAGGGCGACCTCCCGGGGGCCGGGCTCATCACCTTCGACGCCGCGGAGATCTCCTCCCTGGTGCGCAGCCGGATCGAGACGACGGCGCTGTTCGCGGCCCGGTTCCGCGAGTGCGCAGCCCGCGCCCTGCTCATGCCCGCCGCCCGCCCGGGGCGCCGCACGCCGTTGTGGCTGCAGCGGGTCAAAGCCGGACAGCTGCTCGAGGCCTCCCGCCAGTTCCGGGACTTCCCCGTCAGCGTGGAGGCGGCGCGCGAGTGCCTCCAGCAGTACTACGACCTGCCCGCGCTCACCGCCCTCATGGAGCGTCTCGCCTCCGGCCGGGTGCGCGTCGTCGAGGCCATCACCACTGAGCCGTCGCCCTTCGCCCACCCGCTGCTGTTCGGGTACGCGAGCACCCTGATCTACCAGGAGGACCTGCCCCACGCCGAGCGCCGGGCCCAGCTGCTCTCCCTGGACCCCAAGGCGCTCGACGCCCTGCTGGGCGACGCCGGCATCGCGGACCTGCTCGACGACGAGGTCCTGGCCCAGGTGGAGGCCGAGCTCCAGCACCTGGCCCCCGGCAGGCGGGTACGCGCCGACGCCGAGGGGATCGCTGATCTTCTGCGTGAGCTGGGCCCGTTGAGCGTGGCCGAGCTGGCTGAGCGGTGCACCGACGTCGACCGGCGGGATCCGGGGGAGGACGGGCAAGGAGACGGCGCGGTCGGGGCCGGCGACGGCTTCGAGGGCGCGGACAAGCACGCAGTCGAGCGGGAGGTCGGTCGGGCACTCGCCGAGCTGGCCGGGGCTCGCCGAGCCGCCGCGGTGCGGGTCGGCGGGCGGGAGCTGTGGGCCCGGGTCGAGGACGCCCCGGATCTGCAGCGGGCCCTGGGAGTGAAGGCCCCCGAGTGGGCGCTGGAGCGGGCCGGTGACGCGGTCGAGCGGAGGGCGGCGGCCCGCTCGCCGCTGAACGACCTGCTTCTGCGCTACGCGCGCACCCACACGACCGTGACACCGCAGCGCGTGGCGCGGGCCTTTGGGCTGGGGCCGGCGGTGGCGGAGGGAGCCCTGGCCGAGCTGGCCGGGGCTGGTTCCCTGGTGGACCTGGGCGCGGCGGGATGGATGGAGCCGACGGTCCTCACCCGGGTGCGCCACCGCTCCCTGGACCGGGCGCGGGCCGCCGTCGCACCGGTGCCACCCGCGGCGCTCCAGCGTCTCGTGCTGGAGCGGGCGGGGCTGGATGAGCCGGGCGGCGGCGTCGACGCCCTGGCGGAGGCCCTGGCGGCGTTGGAGGGTGTGTGGCTGCCGGCCGGTCTGTGGGAGTCGGTGGTGCTGCCCGCGCGCGTAGTCGACTACCGGCCGGCCATGCTTGATGAGCTCATCGCCGCCGGGGAGGTCGTCTGGCAGGCGCGGCCCGTCGGCGATGCCGCGTCCCGGTCCGGTCCCACCCGGGTGAAGACCGAGGCCGATGACATCCCCGCTCCAGGCGAGATCGCCTTCTTCCCCACGGACTCCGCCCTGGCGCCGGTCGCCGGGGAGGCGACCGCCCCGGGTGAGCCGGAGGCAGCGGAGAGCCGGGAGACGGGAGTCACTGAGGAGGAGCTCTGGAGGCTGGTTCGTGAGGGGGCCGCCACGGGCCGCTCCTTCGAACCGGTGCGCCGGGCACTGGTGCCCGCGGCCGGGACACGTACCGCCCCGCCCTCACGGCGAGTGCGCAGCCGCCGGGGCCGTCGCCTCATGATGGGGATACCGAGCGCTGGGGAGGTGACGGCGGCCGGGCGGTTGTCCTCCGTTCTGGGCTCCACCTCCTGGGTGAGGCTGTCTTCCGCCTCGGCGGGCGATGAGGAGCGGGCGATCGCGGAGGTGGAGTCTCTGCTGGACCGCTACGGGGTCGTCTCCCGCGATCTCGCCCTGACCTTCGGCGGGGCGGGAGGGCTCGGGCCGCTCATGCCGGTGCTGCGGCGCATGGAGGAGACCGGGGTGGTTCTGCGCGGCGGTTTCATTGAGGGCCTGGGGCCGGTGCAGTTCGCCGAGCGGGAGAGCGTTGACCGGCTGCGATCCCTCAGCCACGACCCCGGCGGCGCGGCGGCGACACCGGCCGTGCTCGATCTCAAGGACCCGGCCTGTCTCATCGGGCGCGGGGTGCCGTGGCCTGAGCCGGTACTGCCCGCAGGCCTCGGCGAGCCGTCCGGGGTCCACGGTGAGGAGACGAGTGGTCCGCCGGTCCGGCGCCAGGGGGCGAGCGTCGTCGTGCTGGGTGGTGCCCCGGTGCTCTACGCCTCGGAGAACCTCAAGGTCCTCATCTCCTACACGTCCGCGCGCGAGGAGCTGGCACGCGCCCTGACCGCGCTGGCGGCCGACAGGCAGGCGATGTTCGCGCGCCAGGGGACCGCCGCAATCAGGCGCCGCACAGTGGTGGAGTCCCTCAACGGGGTCACCGCGCTGGAGCCCACCGTGAGCGACCTCCTGCGTCAGGCCGGTTTCGTGCGCGACCCCAGGGGGATGCGGCTCGCCGTCGGCCCTTACGGGGCCGCCTGGCGATGA","MAVTEAAEDPAAAAGPREPGWEGFSSATRTWFLDAFPTGPTSVQERAWATIGRGENALVIAPTGSGKTLASFLSAIDRLGREPAAEEQGAEAAGGGARAEADGVRVLYISPLKALGADVERNLRRPLAGIRAVGPTRPISVGVRSGDTPARERRRLRSHPPSILITTPESLYLMLTSAVRETLRTVETVIVDEIHSFAGSKRGTHLAVSLERLDDLLGRPAQRIGLSATVSPPEEVARFLGGPHPVTIISDDGRATPEVTVSVPVENMARIPAISDRRTRMERALAAPTSAGGGRGSRPSGLGRAGSSQAWRSDKALGRAMAAGRADEPGAGVPARVSASIWPHLENAILDQVLAHRTTLVFVNSRGACERLTAHLNEAYAARLGAVAPAPQAPVHRESWEMGTGSHTEPLAAGAPVIAKAHHGSVSKEQRLGVERELAAGELRCVVATASLELGIDIGSVDLVLQVAPPPSVAAGLQRVGRADHRVGGRPRGVIYPVERTHLVDAVVAAEGMRAGEIERTELVSNALDVLAQQTVAAVSVAEGLTAEAWFTAVRRAAPYSSLPRPAFDSVLELLAGGFASADLTDFSPRIVWDRATGELSARPSTQRLAVASSGTIPDRGMFPVVLPEGAQDAGRRRVGELDEEMVHESSPGDIITLGTSSWRIRQITGDRVVVDPAEGRSARLPFWKGEGLGRPAATGLAKGVFLREAQASLPAEAGAGESEGERALRQRLTEAGLDDHARSNLLALLREQYRATSALPTDETLVLERYEDESGSWRIIVHSTLGRCVHEPWAMAIRERVHQVLGVRPQIIVADDGIVLQIPPVEGDLPGAGLITFDAAEISSLVRSRIETTALFAARFRECAARALLMPAARPGRRTPLWLQRVKAGQLLEASRQFRDFPVSVEAARECLQQYYDLPALTALMERLASGRVRVVEAITTEPSPFAHPLLFGYASTLIYQEDLPHAERRAQLLSLDPKALDALLGDAGIADLLDDEVLAQVEAELQHLAPGRRVRADAEGIADLLRELGPLSVAELAERCTDVDRRDPGEDGQGDGAVGAGDGFEGADKHAVEREVGRALAELAGARRAAAVRVGGRELWARVEDAPDLQRALGVKAPEWALERAGDAVERRAAARSPLNDLLLRYARTHTTVTPQRVARAFGLGPAVAEGALAELAGAGSLVDLGAAGWMEPTVLTRVRHRSLDRARAAVAPVPPAALQRLVLERAGLDEPGGGVDALAEALAALEGVWLPAGLWESVVLPARVVDYRPAMLDELIAAGEVVWQARPVGDAASRSGPTRVKTEADDIPAPGEIAFFPTDSALAPVAGEATAPGEPEAAESRETGVTEEELWRLVREGAATGRSFEPVRRALVPAAGTRTAPPSRRVRSRRGRRLMMGIPSAGEVTAAGRLSSVLGSTSWVRLSSASAGDEERAIAEVESLLDRYGVVSRDLALTFGGAGGLGPLMPVLRRMEETGVVLRGGFIEGLGPVQFAERESVDRLRSLSHDPGGAAATPAVLDLKDPACLIGRGVPWPEPVLPAGLGEPSGVHGEETSGPPVRRQGASVVVLGGAPVLYASENLKVLISYTSAREELARALTALAADRQAMFARQGTAAIRRRTVVESLNGVTALEPTVSDLLRQAGFVRDPRGMRLAVGPYGAAWR$","ATP-dependent DNA helicase","Cytoplasm","ATP-dependent helicase homolog","putative ATP-dependent DNA helicase ","DEAD/H associated domain protein","","Gorbalenya A.E., Koonin E.V., Donchenko A.P., Blinov V.M. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 1989. 17(12):4713-4730. PMID: 2546125","","","

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[652-661]?$	AA_TRNA_LIGASE_I

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[412-488]T$	Helicase_C
SM00490	$\"[370-488]T$	HELICc
PS51194	$\"[349-529]T$	HELICASE_CTER

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[41-236]T$	DEAD

InterPro
IPR013701
Domain

DEAD/H associated
PF08494	$\"[760-948]T$	DEAD_assoc

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[36-262]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[48-248]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[23-258]T$ $\"[357-484]T$	no description
PTHR11752	$\"[37-82]T$ $\"[102-297]T$ $\"[1429-1450]T$	HELICASE SKI2W

","BeTs to 10 clades of COG1201COG name: Lhr-like helicasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1201 is aompkz----r---ef-----j----Number of proteins in this genome belonging to this COG is 1","***** IPB013701 (DEAD/H associated) with a combined E-value of 1.2e-215. IPB013701A 31-74 IPB013701B 107-127 IPB013701C 138-171 IPB013701D 176-203 IPB013701E 223-240 IPB013701F 241-267 IPB013701G 356-376 IPB013701H 437-470 IPB013701I 471-504 IPB013701J 505-551 IPB013701K 615-626 IPB013701L 636-675 IPB013701M 683-707 IPB013701N 780-819 IPB013701O 847-892 IPB013701P 902-919 IPB013701Q 944-964***** IPB012562 (GUCT) with a combined E-value of 1.1e-10. IPB012562A 40-79 IPB012562G 431-485***** IPB000629 (ATP-dependent helicase, DEAD-box) with a combined E-value of 2.2e-08. IPB000629A 36-76***** IPB012961 (DSH, C-terminal) with a combined E-value of 6.9e-06. IPB012961A 77-123 IPB012961E 417-458","","","No significant hits to the PDB database (E-value < E-10).","Residues 41 to 236 (E_value = 1e-42) place ANA_1937 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 412 to 488 (E_value = 1.7e-12) place ANA_1937 in the Helicase_C family which is described as Helicase conserved C-terminal domain.Residues 760 to 948 (E_value = 7.6e-64) place ANA_1937 in the DEAD_assoc family which is described as DEAD/H associated.","","helicase homolog (lhr)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1938","2111383","2112267","885","7.82","2.27","31118","GTGACAGAAGCCGGCCCATGGTGCGCTCCACGCGTCCACAATGAGGACATGGCTGACCCGCACCCCGTCACCGGAGCGTTCTTCGATTCCCCGGTCCCTCCCGGGACCGGGTGGCCCGAGGATCCCGCTACTGCTGCCACACCCGTGGCCCGATCGGCCGCCGATGTGGCGCGCCTGGCCGACTCGTCGTCGGATCTGCCCGAACTCGACGCCCGGATCACGGTGTGCCGTGCCTGCGACCGGCTCGTGGCCTGGCGTGAGGAGGTGGCCCGGACCGGCCGTCGCGCCTCCTTCGCCCATGAGCCGTACTGGGGGCGACCGGTGGCGAGTGTCGGGTCGGCGGATGCCCGCATCTACGTCGTCGGGCTGGCACCCGCGGCCAATGGGGCGAACCGCACCGGCCGCATGTTCACGGGGGACCGCTCCGGGGACTGGCTGTGGGCGGCATTCCACCGGGCGGGCCTGGCGACGTCCCCCACCTCGACGGCGGCAGGTGACGGGCAGCGGCTCACCGGGGCGCGCATGGGCGCCGCTGTGCGTTGCGCCCCGCCGGCCAACAAGCCGACGGCCGTCGAGCGCGCCACCTGCGCCCCGTGGCTCGCCCGCGAGATCGCCCTCATGCCTGAGATCAGGGTGCTGCTGGCGCTGGGCGGGATCGGATGGGGCGCGGTGCTGCGAGTCACCCGGGAGGCCGGATGGACCCTCCCCCGCCCCCAGCCGCGCTTCGGCCACGGGGCGACGGCGGAGCTGACGACGCCCGATGGCAGGGCGGTGACACTGCTCGGCAGTTACCACCCCAGCCAACAGAACACGTTCACCGGTCGGCTCACCGAGACGATGCTCGATGAGGTGCTGGCGACCGCCAAGCGCCTCGCTGAGGCATGA","VTEAGPWCAPRVHNEDMADPHPVTGAFFDSPVPPGTGWPEDPATAATPVARSAADVARLADSSSDLPELDARITVCRACDRLVAWREEVARTGRRASFAHEPYWGRPVASVGSADARIYVVGLAPAANGANRTGRMFTGDRSGDWLWAAFHRAGLATSPTSTAAGDGQRLTGARMGAAVRCAPPANKPTAVERATCAPWLAREIALMPEIRVLLALGGIGWGAVLRVTREAGWTLPRPQPRFGHGATAELTTPDGRAVTLLGSYHPSQQNTFTGRLTETMLDEVLATAKRLAEA$","Uracil-DNA glycosylase","Extracellular","uracil-DNA glycosylase","hypothetical protein","Uracil-DNA glycosylase superfamily","","Olsen L.C., Aasland R., Wittwer C.U., Krokan H.E., Helland D.E. Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J. 1989. 8(10):3121-3125. PMID: 2555154","","","

InterPro
IPR005122
Family

Uracil-DNA glycosylase superfamily
PF03167	$\"[109-289]T$	UDG

noIPR
unintegrated

unintegrated
G3DSA:3.40.470.10	$\"[64-267]T$	no description

","BeTs to 7 clades of COG1573COG name: Uracil-DNA glycosylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1573 is ao-pkz-qvdrl-c--gh-nujx-t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-62% similar to PDB:2D3Y Crystal structure of uracil-DNA glycosylase from Thermus Thermophilus HB8 (E_value = 7.6E_52);-62% similar to PDB:2DDG Crystal structure of uracil-DNA glycosylase in complex with AP:G containing DNA (E_value = 7.6E_52);-62% similar to PDB:2DEM Crystal structure of Uracil-DNA glycosylase in complex with AP:A containing DNA (E_value = 7.6E_52);-62% similar to PDB:2DP6 Crystal structure of uracil-DNA glycosylase in complex with AP:C containing DNA (E_value = 7.6E_52);-37% similar to PDB:1GRQ CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH P-AMINO-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE (E_value = 7.6E_52);","Residues 109 to 289 (E_value = 3.3e-17) place ANA_1938 in the UDG family which is described as Uracil DNA glycosylase superfamily.","","glycosylase (Pa-UDGb)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1939","2112227","2112832","606","11.27","11.06","20359","ATGAGGTGCTGGCGACCGCCAAGCGCCTCGCTGAGGCATGACGTCGGGCTGCGGCCGACGCGGTATCAGGTGCGGTTGGGCAGGATGGCCTCGAGCTCGGCGAGGGTCCGCGGCGTCTGCTCCGCGGGAGCGTCGACCTCGGCGCTCTCGGTGTCGTCGGAGGTTGCGTCGCCCTGGGGTACGTCGATCCCCAGGGCCAGGGACAGGCCGGCGACGGCGGCGCGGGCCGAGGCGGCCCGCTCGCTGGGTGTGTCGCTGGACTCGCCGCTGGCGGGGGCCGGTGAGGGCAGCTCCGCGGTTGCCTGGAGAGGCTCGGCGGTTCTCGCGGCATCGGGGGCTGAGGAGGCCGACGCCGCGGCGGTCGCCCGCTCGAGCTCTCCCAAGTCGAGCCCCACCAGGCGGCTGCTGCGCTCCTCGGAGGCTTCCTCGGGCGAGTCGGCCGTGCGACGGCGGCGCGTCGAGGAGGCCGCGCGGCGGGAGCGCTTCGCGGCGGGCTTCTGCTCGGACGCGGCGGACTTCTTGGTGGTCTTCGTCCCGGGATCCTCCGCCTGCTCCTCGGCCGCGGGCGCGGTGGCATCCGTGCCGGCGGCGCCGTCCTCGGCTTGA","MRCWRPPSASLRHDVGLRPTRYQVRLGRMASSSARVRGVCSAGASTSALSVSSEVASPWGTSIPRARDRPATAARAEAARSLGVSLDSPLAGAGEGSSAVAWRGSAVLAASGAEEADAAAVARSSSPKSSPTRRLLRSSEASSGESAVRRRRVEEAARRERFAAGFCSDAADFLVVFVPGSSACSSAAGAVASVPAAPSSA$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1940","2114104","2112998","1107","12.52","96.95","41714","GTGTCGATTATGAAGATTCGGTCGAAGTGTGGGAGGGCGGGGTGGTGTGCCCAGGCCAACCCGCGCGGGCCGGGGCAGTTTCAGGAGCCTCCCCTACACTGGCCGAGTGACCGACACGATCGACTCTCACACCGACGCCTCAGGCAAGCCCGCAACCGGGACCGACTCGGGTTCACCGGCGGGCGCCGCCACCGGGGCGCGCACCTCCACGGCGACCCTGGAGCGCCCGGCTCTGGCACCGAGTGCGGCCTCGCCCTCTCCGACGCAGGCCCCCGTGCCCCGCGCCGGTGCCCTGCCGACCCCGGCCGAGCAGGCCCTGGCCGCCAAGGACAAGACCCTCACCTCCCCGGCGGCCATCGAACTGGCCCGCCACGCGCTGGAGGAGGTCACCGACCCCATCACCGTCGGCGAGTACGTGGCCGTCGCGCCCGACGCCGAGCGCCTCGTCACCCACCTGTTCGACTGCACCCTGAGCGGCTACCGCGGCTGGCGCTGGGCGGTCACCCTCAGTCGCGTCCCGCGCGGCCGCACCGCCACCGTCTGCGAGGTGGAGCTCCTCCCCGGCGAGGAGGCCCTCCTCGCGCCCGCCTGGGTCCCGTGGGCCGAGCGCCTCGAGCCCGGCGACATCACCCGCTCCGACCGCCTGCCCCGCAAGGAGACCGACGAGCGCCTCGAGCCCGGGTGGGAGGCCACCGGCGAGGATGCCGACGCCGTCGCCCTGGACGAGCTCGACCTGGGCCGCCCCCGGGTGCTGAGCGCCCAAGGCGTCGCCAGCGCCGCCGAGCGCTGGTACGGCGGCGACCACGGCCCCGAGGCCGAGGGTGTCCGCAAGGCCCACGCCACCTGCTCCACCTGCGGCTTCTTCGTGCCGATGGCCGGCGCCCTGCGCGCCATCTTCGGTGTGTGCGCCAACGAGTGGGCCGCCGACGACGGCAGCGTCGTCTCTCTGGACCACGGCTGCGGTGCCCACTCCGAGACCGACCTGCCCGATCAAGGCCCGGAGTGGCCCATCAACCCCTCCCGGGTCGACGACCACCTCATGGTGCCGCTGAGCACCAACGGGCTCGATTTGCGCGAGGGCCGCAGCATCGCCGAGCTCGCCGCTGA","VSIMKIRSKCGRAGWCAQANPRGPGQFQEPPLHWPSDRHDRLSHRRLRQARNRDRLGFTGGRRHRGAHLHGDPGAPGSGTECGLALSDAGPRAPRRCPADPGRAGPGRQGQDPHLPGGHRTGPPRAGGGHRPHHRRRVRGRRARRRAPRHPPVRLHPERLPRLALGGHPQSRPARPHRHRLRGGAPPRRGGPPRARLGPVGRAPRARRHHPLRPPAPQGDRRAPRARVGGHRRGCRRRRPGRARPGPPPGAERPRRRQRRRALVRRRPRPRGRGCPQGPRHLLHLRLLRADGRRPARHLRCVRQRVGRRRRQRRLSGPRLRCPLRDRPARSRPGVAHQPLPGRRPPHGAAEHQRARFARGPQHRRARR$","Hypothetical protein","Extracellular, Membrane, Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-49% similar to PDB:1Y0F The structure of collagen type I. Single type I collagen molecule (E_value = );-49% similar to PDB:1YGV The structure of collagen type I. Single type I collagen molecule: rigid refinment (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1941","2116742","2114151","2592","5.15","-28.74","88564","ATGAGCCCTTCCGCCTCCACCCAGGACCTCGCCGTGCACCTGACGGCGCTGCCGGACCGCGAGGTCGCCGCCCTGCTGGTGGCGCGCCCGGACCTGGCCGCGCCGCCGTCCTCCTCCTTCCTGGCGCTGGCGACCCGTGCGGGGGCCCCGGGCAGCATCGAGCACGCCCTGGCCGGGCTGGATGCGCCGACGCTGGCCGTGGCCGAGGCGGTGGTGGCACTCAGCCGGCCCGATGAGTCGCGCCGGGCGGGCGGGGCCGGGCCGAGCAAAGTCACCGAGGGCATCGAGGCAGCCGGGGATGGACTCGCCGAGGTGGCCGAGAACGGGCAGGATGGCGGGGTCGGTGGAGAACCTGCCGGTGGTGAGCCGGCCGATGACGAGACTGTCGGCCATCCCGCCGGCAATCCGGCCAACCCGGACCACACTGACCTGGCCGGGTTGGTCGCCGCCCACCTGCCGCTGCCCGCCGAGCAGGTCACCAATGCGCTGGAGCACCTGGGCCGGCTGGCGCTCGTCATCGAGGGCAGGCCCGTGGCCGCGCTCGAGGCGGCCTTTGGACCACACCCCTTCGGCCTGGGGCCCTGGGCCGCTGAGCCCCTGAGCACCGAGCAGCTGCCACCCACCCTGGAGGAGCTGAGCGAGCACTCGGCCAGTGGAGCCGGCGGCGAGCCGGTCATCCCGGCGGCCTCCGTGGAGATGCTCCAGGCCCTCACCTGGGGGCCGCCCGCCGGCACCCTGCGCGCCGGCGGCACCGCACCGGGCGCGGCCCCACTCATCGAACGCGGCTGGCTGGAGCGCAGCAGCGATACCCACGGGCGCACCCGCTTCATCCTGCCGCGCCAGGTCGCCCTCGCCCTGCGCGGCGGCCACCTGACCCGCGAACCCCTGACCGCCCCCGAGGCCAGCGACCTCGAGACGGTGGGCGCCGACGTCGTCGCCTCCGAGGCCTCCTTCCACGCCGAGGAGGCCGTCCGGCTCGTGGCCGCCCTCCTGGAGGAGTGGGGCCGCGAGGGCGGGACGATTCGCCGCACCGGCGGAGTGAGCGCGCGCGCTCTAGCCCGCACCGCCGACGCCCTCGACCTGGAGGCCGACGCCGCCGCCCGCATCATCGAGATCGCCGCGGGCGCCGGGCTCCTGGGACTCGACGAGGACGGCGCCGCCTGGGTGCCCTCCTCCTTGGCCGCCGGCTGGCTCACCGACAGCCTCCCGCAGCGCTGGGCGCCGCTCGCCCTGACCTGGTCGGGCAGCGCCCGCACCCCCTGGCTGACGGGCACCCGCGATGACGACGGCACCCTGCGCGCCGTCCTCAGCCCGGACCTGGAGGCCGGGTGGGCGGCGCGACTGCGCGCTCGGGTGCTCGCCCTCCTGGGCGACCTCCCGCCAGGCGCCAGCGCGACCCCCGCCTTCGTGCGGGCGGCCCTGACCTGGCAGAGCCCCCGGCGCCCCATCCCCGGCGGGGCCATCTCCGCGGTCCTGGCCGAGGCCGAGACCCTCGGGATCACCGGCGGCGGGGCGCTCACCGAGGCCGGCAGGATCCTCGCCCGACGAGCGGCAGCGAGCCTCGACGAACAGGACCCCGGACTCAGCGGCAGGCCCGGCGGTCGCACCGACCCCGGAGACGCAGGCCGCGTTGAGGAGGCGGGTGGTGAGGCACACGCCGTGCCGTTGTCGGACGGCGAGGCCCTCCCCGCCCTGGAGGCGGCCCTGGCCGCAGACCTGCCGGCCGCCGTCGAGATGATTCTCGTCCAGTCCGATCTCACCGCCATCGTGCCGGGCCGCCCCGCCCCCGAGCTGGCCGCACTGCTGGAGCGCACGAGCGTCGTCGAGTCGCGTGGTGGGGCGCTCACCGTGCGCTTCACCCCCGAGTCGGTGCGCGGCGCGCTCGACGTCGGCTACCGGGCCGAGGAGATCACCCAGGAGATCGTCCGCTACAGTCCCACGCCCCTGCCGGACTCGCTGAGCGTGCTCATCCAGGACGCGGCCCGCCACCACGGGGCGGTGCGGGTGCGGGCCGTGTCCGCGCTGCTGCGGATCGGCGACGAGGCCACGGCCGCCGGGCTCCTGGCCGAACCGCGATTGAAGGACCTCGGCCTGGACCAGGTGGCTCCCGGGATCCTCGTGGCCACGGCCAGCGCCGGGCAGGTACTGCGCGAGCTGCGCGCCACCGGGCTGGCGCCGGTGACCGAGGACGCCAGCGGCCACCTGGTGGTTGGGCCGGCCACCGCGCAGCAGGCCCGCCGGGCCCCCGAGCCGACGCGCCCCGGCAGCGAGTACTCGGTGCGACGACGTCGGCCCGGGAGGCGCGAGCTGACAACCCTCGTGGGGCGGCTGCGTGTGGGGCAGGAGGCGCTGCAGGCCGCCGGAGAGACGGCTGTGGCCACCGACCCGGTGCACGCCCTGGCGGTGCTGCGCCAGGCCCAGTCCTCGCGCTCGCGGCTGCGGCTGAGCCTGGCCGGCCCCGACGGCGCCGTGCAGGAGCGGCAGGTGCGGGTCATGGCCGTGGAGCCTGGGCGGGTGCGCCTGCGCGACGTCGTGCGCGAGACCGAGCTGACCGTGGCCGTCCACCGCATCGTCTCGGTCGAGGCGAGCTGA","MSPSASTQDLAVHLTALPDREVAALLVARPDLAAPPSSSFLALATRAGAPGSIEHALAGLDAPTLAVAEAVVALSRPDESRRAGGAGPSKVTEGIEAAGDGLAEVAENGQDGGVGGEPAGGEPADDETVGHPAGNPANPDHTDLAGLVAAHLPLPAEQVTNALEHLGRLALVIEGRPVAALEAAFGPHPFGLGPWAAEPLSTEQLPPTLEELSEHSASGAGGEPVIPAASVEMLQALTWGPPAGTLRAGGTAPGAAPLIERGWLERSSDTHGRTRFILPRQVALALRGGHLTREPLTAPEASDLETVGADVVASEASFHAEEAVRLVAALLEEWGREGGTIRRTGGVSARALARTADALDLEADAAARIIEIAAGAGLLGLDEDGAAWVPSSLAAGWLTDSLPQRWAPLALTWSGSARTPWLTGTRDDDGTLRAVLSPDLEAGWAARLRARVLALLGDLPPGASATPAFVRAALTWQSPRRPIPGGAISAVLAEAETLGITGGGALTEAGRILARRAAASLDEQDPGLSGRPGGRTDPGDAGRVEEAGGEAHAVPLSDGEALPALEAALAADLPAAVEMILVQSDLTAIVPGRPAPELAALLERTSVVESRGGALTVRFTPESVRGALDVGYRAEEITQEIVRYSPTPLPDSLSVLIQDAARHHGAVRVRAVSALLRIGDEATAAGLLAEPRLKDLGLDQVAPGILVATASAGQVLRELRATGLAPVTEDASGHLVVGPATAQQARRAPEPTRPGSEYSVRRRRPGRRELTTLVGRLRVGQEALQAAGETAVATDPVHALAVLRQAQSSRSRLRLSLAGPDGAVQERQVRVMAVEPGRVRLRDVVRETELTVAVHRIVSVEAS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1945","2117544","2117155","390","5.52","-5.69","14536","ATGCGGATCGGGGAGCTCGCTGAAGCGGCCGGCACGACCACGAAGACTCTGCGGTTCTATGAAGACCAGGGGCTCTTGCCCCCGGCCGAGCGCACGCCCGGCGGCTACCGCGACTACACGACCGAGAGCCTCACCCGGATCGACTTCATCCACCGCGGCCAAGCCGTCGGACTCTCCCTCGCCCAGATCCGGCAGGTCCTCGACATCCACGACCACGGCCAAGCTCCCTGCGATCACGTACGCGACCTGCTCGACGCACGCCTGACCGACATTGACCTGAAACTCAGACAGCTCCACGACCTGCGCGACACCCTCGCCGGGCTACGCGACCAGGCCGAGCACGTTGAGCCCGACACGTGCAGCTCCGACCAGGTCTGCCGGTACCTGTAG","MRIGELAEAAGTTTKTLRFYEDQGLLPPAERTPGGYRDYTTESLTRIDFIHRGQAVGLSLAQIRQVLDIHDHGQAPCDHVRDLLDARLTDIDLKLRQLHDLRDTLAGLRDQAEHVEPDTCSSDQVCRYL$","Transcriptional regulator, MerR family","Cytoplasm","transcription regulator alr7637","transcriptional regulator; MerR family","regulatory protein, MerR","","Holmes D.J., Caso J.L., Thompson C.J. Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 1993. 12(8):3183-3191. PMID: 7688297Helmann J.D., Wang Y., Mahler I., Walsh C.T. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons. J. Bacteriol. 1989. 171(1):222-229. PMID: 2492496Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 1995. 177(14):3904-3910. PMID: 7608059Nakano Y., Kimura K. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 1991. 109(2):223-228. PMID: 1677938Sadowsky M.J., Cregan P.B., Gottfert M., Sharma A., Gerhold D., Rodriguez-Quinones F., Keyser H.H., Hennecke H., Stacey G. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(2):637-641. PMID: 1988958Helmann J.D., Ballard B.T., Walsh C.T. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. Science 1990. 247(4945):946-948. PMID: 2305262","","","

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PR00040	$\"[2-13]T$ $\"[13-26]T$ $\"[37-57]T$	HTHMERR
PF00376	$\"[2-39]T$	MerR
SM00422	$\"[1-70]T$	HTH_MERR
PS50937	$\"[1-69]T$	HTH_MERR_2

InterPro
IPR015358
Domain

Transcription regulator MerR, DNA binding
PF09278	$\"[44-108]T$	MerR-DNA-bind

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[1-114]T$	no description

","BeTs to 13 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 8","***** IPB000551 (Bacterial regulatory protein, MerR family) with a combined E-value of 1.9e-21. IPB000551 1-41***** IPB012925 (TipAS antibiotic-recognition) with a combined E-value of 2.4e-09. IPB012925A 11-64","","","-56% similar to PDB:1Q05 Crystal structure of the Cu(I) form of E. coli CueR, a copper efflux regulator (E_value = 3.0E_12);-56% similar to PDB:1Q06 Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator (E_value = 3.0E_12);-56% similar to PDB:1Q07 Crystal structure of the Au(I) form of E. coli CueR, a copper efflux regulator (E_value = 3.0E_12);","Residues 2 to 39 (E_value = 4.4e-16) place ANA_1945 in the MerR family which is described as MerR family regulatory protein.Residues 44 to 108 (E_value = 2.5e-21) place ANA_1945 in the MerR-DNA-bind family which is described as MerR, DNA binding.","","regulator alr7637 (merR2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1948","2117652","2119076","1425","5.29","-9.96","49549","ATGCAGTCGAAGATTGATCTGGCCGTGATCGGGTCGGGTGGCGCGGCGTTCGCCGCAGCGATCCGCGCCACCACGCTGGGCAAGTCGGTGGTGATGGTCGAGCGCGGTACGTTCGGCGGCACCTGCGTGAACACCGGGTGCGTGCCGTCCAAGGCGCTGATAGCGGCCGCCGAGGCCCGCCACGTGGCCGCGGACGCGGGCTCCCGGTTCCCGGGGATCGCCGCCACCGCGGGCGCGGTCGACATGCCCGGGCTGGTGGGTGGCAAGCAGGACCTGGTCGAGGCGATGCGGGGTGAGAAGTACTTCGACGTGGCCGAAGCCTACGGCTGGCCGGTCCGCCAGGGCCAGGCGGCCTTCGCCGGCACCCCGGATGCGCCTGTGCTGGAGGTCACCGCCGCTGAAGGCACCGTGGAAACCATCGAGTCCGCCCATTACCTGATCGCTACCGGCACCCGTCCCTGGGTCCCGCTCATCCAGGGGCTGGACGGCGTCGAGTACCTGACCTCGACGTCGGCGATGGAACTGTCCGAGCGCCCCGACTCGCTGCTGGTGCTCGGCGGTGGCTACGTGGCGCTGGAGCTGGCCCAGATGTTCGCCCGGCTCGGCTCGAAGGTGACCCTGCTGGTGCGTTCTCGGCTGGCGTCGAAGGAGGAGCCGGAGGTTTCCAGATCATTGCAGGAAGTCTTCGCCGACGAGGGCATCCGGGTGGTCCGCCGCGCTGTTCCCTCCCGCGTTGCCCGCGATACCGTCACCGGGCAGGTCGTCGTCATGGCCGAGGTCTCGGGCGGCGAGCAGGAGTTCCGTGCCGACGAGATCCTCGTCGCGCTCGGACGCCGCCCGGTCACCGAGGGGCTCAACCTCGAGGCCGTGGGGGTGAAGACCGGCGAGGCCGGACAGATCGTGGTCACCGACCAGTTGCAGACCGCCAACCCCCGCGTCTGGGCGGGCGGGGATGTCACCGGGCACCCCGAGTTCGTCTATGTCGCGGCCCGGCACGGCACGATCGTCGCCGAGAACGCCTTCACCGACGCCAACACTTCGGTCGACTACACACGGATGCCTCGGGTGACGTTCACCGGTCCCGCCATCGGCGCGGTCGGGATGACCGAGAAGGAGGTCATCGCGGCCGGGATCCGCTGCGACTGCCGCGTCCTGCCACTGGAGTACGTGCCCCGTGCGCTGGTGAACCGGGACATGCGTGGGTTCATCAAGATGGTCGCCAACGCCGACACCGGCGAGATCCTCGGTCTCACCGCTGTCGCCAAGGACGCCGGCGAGCTCGCCGCCGCCGGCGTCCACATCCTCGGCAAGACCATCGCAGAAGTCGCCGACGCGTGGGCCCCATACCTGACCATGGCCGAAGGCATCCGCATCGTCGCCAAGGCCTTCACCACCGACGTCTCGAAGCTGTCCTGCTGCGCCTGA","MQSKIDLAVIGSGGAAFAAAIRATTLGKSVVMVERGTFGGTCVNTGCVPSKALIAAAEARHVAADAGSRFPGIAATAGAVDMPGLVGGKQDLVEAMRGEKYFDVAEAYGWPVRQGQAAFAGTPDAPVLEVTAAEGTVETIESAHYLIATGTRPWVPLIQGLDGVEYLTSTSAMELSERPDSLLVLGGGYVALELAQMFARLGSKVTLLVRSRLASKEEPEVSRSLQEVFADEGIRVVRRAVPSRVARDTVTGQVVVMAEVSGGEQEFRADEILVALGRRPVTEGLNLEAVGVKTGEAGQIVVTDQLQTANPRVWAGGDVTGHPEFVYVAARHGTIVAENAFTDANTSVDYTRMPRVTFTGPAIGAVGMTEKEVIAAGIRCDCRVLPLEYVPRALVNRDMRGFIKMVANADTGEILGLTAVAKDAGELAAAGVHILGKTIAEVADAWAPYLTMAEGIRIVAKAFTTDVSKLSCCA$","Mercuric reductase","Cytoplasm","mercuric reductase","mercuric reductase","mercuric reductase","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Rice D.W., Schulz G.E., Guest J.R. Structural relationship between glutathione reductase and lipoamide dehydrogenase. J. Mol. Biol. 1984. 174(3):483-496. PMID: 6546954Carothers D.J., Pons G., Patel M.S. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 1989. 268(2):409-425. PMID: 2643922Walsh C., Bradley M., Nadeau K. Molecular studies on trypanothione reductase, a target for antiparasitic drugs. Trends Biochem. Sci. 1991. 16(8):305-309. PMID: 1957352Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G. Cloning and sequencing of a human thioredoxin reductase. FEBS Lett. 1995. 373(1):5-9. PMID: 7589432Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P. Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). Plant J. 1992. 2(1):129-131. PMID: 1303792","","","

InterPro
IPR000815
Family

Mercuric reductase
PR00945	$\"[16-34]T$ $\"[51-70]T$ $\"[146-163]T$ $\"[181-198]T$ $\"[201-216]T$ $\"[385-405]T$ $\"[448-467]T$	HGRDTASE

InterPro
IPR001100
Family

Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411	$\"[6-28]T$ $\"[38-53]T$ $\"[145-154]T$ $\"[181-206]T$ $\"[270-284]T$ $\"[313-320]T$ $\"[349-370]T$ $\"[414-429]T$	PNDRDTASEI

InterPro
IPR001327
Domain

Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139	$\"[149-211]T$	Q6SKF3_ARTAU_Q6SKF3;
PF00070	$\"[181-277]T$	Pyr_redox

InterPro
IPR004099
Domain

Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30	$\"[353-458]T$	no description
PF02852	$\"[353-460]T$	Pyr_redox_dim

InterPro
IPR011796
Domain

Mercuric reductase MerA
TIGR02053	$\"[5-474]T$	MerA: mercuric reductase

InterPro
IPR012999
Active_site

Pyridine nucleotide-disulphide oxidoreductase, class I, active site
PS00076	$\"[39-49]T$	PYRIDINE_REDOX_1

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368	$\"[6-28]T$ $\"[145-154]T$ $\"[181-206]T$ $\"[270-284]T$ $\"[313-320]T$	FADPNR
PF07992	$\"[6-323]T$	Pyr_redox_2

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[4-351]T$	no description
PTHR22912	$\"[8-473]T$	DISULFIDE OXIDOREDUCTASE
PTHR22912:SF29	$\"[8-473]T$	MERCURIC REDUCTASE

","BeTs to 21 clades of COG1249COG name: Dihydrolipoamide dehydrogenase/glutathione oxidoreductase and related enzymesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1249 is aomp-zyqvdrlbcefghsn-jxi-wNumber of proteins in this genome belonging to this COG is 4","***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 1.9e-70. IPB001100A 5-30 IPB001100B 39-51 IPB001100C 167-207 IPB001100D 270-292 IPB001100E 298-319 IPB001100F 349-373 IPB001100A 180-205***** IPB000815 (Mercuric reductase class II signature) with a combined E-value of 5.8e-45. IPB000815B 16-34 IPB000815D 146-163 IPB000815E 181-198 IPB000815F 201-216 IPB000815G 385-405 IPB000815H 448-467***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 2.8e-29. IPB013027A 6-28 IPB013027B 145-154 IPB013027C 181-206 IPB013027D 270-284 IPB013027E 313-320***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase, class-II) with a combined E-value of 2.4e-17. IPB000103A 7-25 IPB000103B 39-52 IPB000103D 267-282 IPB000103E 308-345 IPB000103A 182-200***** IPB001327 (Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region) with a combined E-value of 8.8e-08. IPB001327A 42-51 IPB001327B 307-320***** IPB000759 (Adrenodoxin reductase family signature) with a combined E-value of 3.1e-07. IPB000759A 6-28 IPB000759D 182-196","","","-53% similar to PDB:1ZK7 Crystal Structure of Tn501 MerA (E_value = 1.1E_77);-53% similar to PDB:1ZX9 Crystal Structure of Tn501 MerA (E_value = 1.1E_77);-48% similar to PDB:3LAD REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE (E_value = 2.0E_42);-48% similar to PDB:1DXL DIHYDROLIPOAMIDE DEHYDROGENASE OF GLYCINE DECARBOXYLASE FROM PISUM SATIVUM (E_value = 1.3E_41);-47% similar to PDB:1EBD DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE (E_value = 2.9E_41);","Residues 6 to 323 (E_value = 7.2e-50) place ANA_1948 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 6 to 41 (E_value = 3.8e-08) place ANA_1948 in the FAD_binding_2 family which is described as FAD binding domain.Residues 181 to 277 (E_value = 4.2e-21) place ANA_1948 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 353 to 460 (E_value = 4.3e-31) place ANA_1948 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain.","","reductase (merA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1949","2119413","2120009","597","9.60","7.37","21630","ATGTCCGCTTTGAAGGTCGGGTACGCCCGGGTCTCCACCGATGAACAGGACCTCACCGCCCAGCGCGATGGCCTCAGCGCTCTCGGTGTCGACGCGATGCGCATATACGTCGATCACGGACTGACCGGCCGCAATGCGGATCGCGCCGGGCTGCGGCAGGCGCTGGCGGCATGCCGGGCCGGTGACACGTTCGTGGTCACCAAGCTCGACCGGTTGGCACGTTCGGTGCGCGATGCTCACGAGATTGCCGATGACCTCGCGGCCCGCGAGGTGAAACTCAGCATCGCCGGATCGGTGTATGACCCGACGGACCCGATGGGCAAACTGCTGTTTAACGTGCTGGCGATGGTCGCCGAGTTCGAAGCCGACCTCATTCGCGCCCGCACCCGCGAAGGGATGAAGGTCGCCAAGGCCAAGGGCCGGCTGCGCGGGAAGTCTCCGAAGCTCACCCCACGACAGGAGGCTCACCTCGTCCACCTGCATGCCGCCAAGGAGCACACCGTGGGCGAGCTGGCCGAGCTGTTCAGCGTCGGCCGCTCCACGGTCTACCGTGCCCTTGAGCGCGCGCAGCGTGGCCGCGAGAGCCTCGTGCAGTAG","MSALKVGYARVSTDEQDLTAQRDGLSALGVDAMRIYVDHGLTGRNADRAGLRQALAACRAGDTFVVTKLDRLARSVRDAHEIADDLAAREVKLSIAGSVYDPTDPMGKLLFNVLAMVAEFEADLIRARTREGMKVAKAKGRLRGKSPKLTPRQEAHLVHLHAAKEHTVGELAELFSVGRSTVYRALERAQRGRESLVQ$","Resolvase","Cytoplasm","DNA recombinase homolog Pin","resolvase-like","Resolvase, N-terminal domain","","Skarstad K., Boye E. The initiator protein DnaA: evolution, properties and function. Biochim. Biophys. Acta 1994. 1217(2):111-130. PMID: 8110826Yoshikawa H., Ogasawara N. Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial replication origins. Mol. Microbiol. 1991. 5(11):2589-2597. PMID: 1779750Georgopoulos C. The E. coli dnaA initiation protein: a protein for all seasons. Trends Genet. 1989. 5(10):319-321. PMID: 2558436Skovgaard O. Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli. Gene 1990. 93(1):27-34. PMID: 2172087","","","

InterPro
IPR006118
Family

Site-specific recombinase
PS00397	$\"[8-16]T$	RECOMBINASES_1
PS00398	$\"[61-73]T$	RECOMBINASES_2

InterPro
IPR006119
Domain

Resolvase, N-terminal
PF00239	$\"[5-142]T$	Resolvase

InterPro
IPR006120
Domain

Resolvase, helix-turn-helix region
PF02796	$\"[144-189]T$	HTH_7

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[121-189]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1390	$\"[3-125]T$	no description

","BeTs to 8 clades of COG1961COG name: Site-specific recombinases, DNA invertase Pin homologsFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1961 is ---pk----drlb-efg-s--j----Number of proteins in this genome belonging to this COG is 1","***** IPB006118 (Site-specific recombinase) with a combined E-value of 3.5e-54. IPB006118A 6-20 IPB006118B 36-86 IPB006118C 107-146 IPB006118D 165-184","","","-50% similar to PDB:2GM4 An activated, tetrameric gamma-delta resolvase: Hin chimaera bound to cleaved DNA (E_value = 9.4E_20);-48% similar to PDB:1GDT CRYSTAL STRUCTURE OF A SITE-SPECIFIC RECOMBINASE, GAMMA-DELTA RESOLVASE COMPLEXED WITH A 34 BP CLEAVAGE SITE (E_value = 1.0E_18);-49% similar to PDB:1ZR2 Structure of a Synaptic gamma-delta Resolvase Tetramer Covalently Linked to two Cleaved DNAs (E_value = 2.3E_18);-49% similar to PDB:1ZR4 Structure of a Synaptic gamma-delta Resolvase Tetramer Covalently linked to two Cleaved DNAs (E_value = 2.3E_18);-50% similar to PDB:1GDR MODEL FOR A DNA MEDIATED SYNAPTIC COMPLEX SUGGESTED BY CRYSTAL PACKING OF GAMMA DELTA RESOLVASE SUBUNITS (E_value = 4.8E_16);","Residues 5 to 142 (E_value = 1e-56) place ANA_1949 in the Resolvase family which is described as Resolvase, N terminal domain.Residues 144 to 189 (E_value = 5.2e-06) place ANA_1949 in the HTH_7 family which is described as Helix-turn-helix domain of resolvase.","","recombinase homolog Pin (pin)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1950","2120017","2121231","1215","8.54","7.00","45162","ATGGACGCTGCGGCGCGGTGGCGCATTCTCCGGCTCCATGTGGAGGACGAGGTTCCGCTCGCGCGTCTGGCCCGCGAGTCCGGCGTCGGGCTGCGGACCCTGGAGCGCTGGCACGCCCGCTACCGGACCGACGGCTACGCGGGCCTGGAGACGGCCCCGCGAATGGACGCCGGCACCCACCGCTTGCCGACCGATCTCGTCCACGTGATCGAGGGTCTGGCGCTGAGCAAGCCGCGGCCGGCTATCGCCACGATCCATCGCAAGGTCACCGGCATCTGCGGCATCCACGGGTGGCCGGTCCCGTCCTATTCGGTGGTGTGGGAGATCGTGCGCGCCCTGGACCCGGGCATGGTCACCCTCGCCCTGGAAGGCGCGGCGTCCTACCGCGACAAGCACGAGCTGGTGCTGCGGCAGGCGATCTGGCACAAGGCCGACCCGGCCTGGCCGATGTGCGGCCTACCGGACGTGCTCTACGTCGATCACGGCAGCGACTTCATCAGCCACCAGCTCGCCGGCACCGCCGTCGACCTCCACATCCGGCTGATCCATTCCACCGTCGCCCGCCCCCAGGGCCGGGGCAAGATCGAGCGGTTCTTCGGCACCGTCAACACCGAGCTGCTGGCCGACCTGCCCGGATACATCGGCGAAGGCCAGCCCTGGCCAACACCGACACTGTCCCTGGCCGAGCTCGACACCGCCGTCGAAAGGTTCGTGGCCACCTACAACGACCGCACGCACAGCGAGATCGGCACCTCCCCGCGCAGCGCGTGGATCGCCGAGGGCTGGCTGCCCCGCATGCCCGAGAGCCTGGAAGCTCTCGACGGACTGTTGCTGACCGTGGCCAAGACCCGCGTCGTGCGCCGCGATGGCATCCGATTCCAGGGCCTGCGCTACGTCTCCCCGACCCTGGCCGGCTACGTCGGACAGTCGGTCGTGATCCGTTACGACCCTCGCGACATCACCGAGATCCGCGTCTTCGACCACGACGAGTTCCTCTGCAAGGCCGTCAACCAGGAGCACCACGACCAGAAGGTCAGCCTCAAAGAGATCCAGGCCGCTCGCAACGCGAGACGCCGGGCACTACGGGCCGGCATCAACGAACGCATCGCTGTCGTGGCCGCACACACCACCGAGACACCACCTCCCGCGGAGGAACCAGCGGCGGCGCAGACGCCGAAACGGAAGTTGAAGGTCTACAAGGAGGACCTGAGGTGA","MDAAARWRILRLHVEDEVPLARLARESGVGLRTLERWHARYRTDGYAGLETAPRMDAGTHRLPTDLVHVIEGLALSKPRPAIATIHRKVTGICGIHGWPVPSYSVVWEIVRALDPGMVTLALEGAASYRDKHELVLRQAIWHKADPAWPMCGLPDVLYVDHGSDFISHQLAGTAVDLHIRLIHSTVARPQGRGKIERFFGTVNTELLADLPGYIGEGQPWPTPTLSLAELDTAVERFVATYNDRTHSEIGTSPRSAWIAEGWLPRMPESLEALDGLLLTVAKTRVVRRDGIRFQGLRYVSPTLAGYVGQSVVIRYDPRDITEIRVFDHDEFLCKAVNQEHHDQKVSLKEIQAARNARRRALRAGINERIAVVAAHTTETPPPAEEPAAAQTPKRKLKVYKEDLR$","Transposase","Cytoplasm, Extracellular","Tn552 transposase","K07497 putative transposase","Integrase, catalytic region","","Rice P., Mizuuchi K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell 1995. 82(2):209-220. PMID: 7628012","","","

InterPro
IPR001584
Domain

Integrase, catalytic core
PF00665	$\"[148-258]T$	rve
PS50994	$\"[76-261]T$	INTEGRASE

InterPro
IPR015378
Domain

Transposase-like, Mu, C-terminal
PF09299	$\"[273-335]T$	Mu-transpos_C

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[147-267]T$	no description

","BeTs to 6 clades of COG1425COG name: Predicted transposaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1425 is a--p-----dr---efgh-n-j----Number of proteins in this genome belonging to this COG is 7","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 85 to 258 (E_value = 1.3e-11) place ANA_1950 in the rve family which is described as Integrase core domain.Residues 273 to 335 (E_value = 8.8e-31) place ANA_1950 in the Mu-transpos_C family which is described as Mu transposase, C-terminal.","","transposase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1951","2121228","2122046","819","8.75","4.84","31224","GTGAGCCAGCGCTTCATCGTCACCAAAGAACACCGCCGCTTCACCGAGTTCGCCGACGCCGTGCGCCGCGGCCACACCATCGGCCTGTGCTTCGGGTCGGCCGGAGTGGGCAAGACGCTCTCGGCGCGCCGCTACGCGCACTGGGACAAGGCCCTCGATCTGCTGACCTACTGGGGGCCGCGCTCCGACGACGACGCCAAGATCTACGCCGCCCTGAACCGGAGCCGCACCGTGCTCTACACCCCCAGCGTGCTGACCACCCCGCGGACCCTGAAGGATGAGCTCAATCAGGCCATCACCCGCACCAACATCTGCATCGAACAGCACCTCGCGCCGCACGGCGACGTCACGCCCGAGACCTGGGGATGGCGCCGCAGCAGGAACTACGTGGAGCTGATCATCGTCGACGAGTCCGAACGGCTCCGCCCCGCCGCCCTGGAACTGCTGCGCGACCGCTACGACCGAGACGACATCGCACTGATCCTGATCGGCATGCCCGGACTGGAGAAGCAGTTCAGCCACTACCCCCAGTTCTACAGCCGGGTCGGGTTCGCCCATCAATACCGACCCCTGGGTCAGGACGAACTGTTGTTCGTCTTGCAACGACACTGGCGCTCCCTCGGCAAGACCCTCGACCCCGAAGACTTCACCGACGCCCAAGCCATCGCCGCCATCGCGCGGGTCACCCGCGGCAACTTCCGGCTGCTCGAACGCCTCATCCCCCAGATCCAGCGCGTGCTGAAGATAAACGAACTCGACACCATCACCAACGATGTCATCGAAGCCGCCCAAAGCACCCTGGTCATCGGCGTCACCTGA","VSQRFIVTKEHRRFTEFADAVRRGHTIGLCFGSAGVGKTLSARRYAHWDKALDLLTYWGPRSDDDAKIYAALNRSRTVLYTPSVLTTPRTLKDELNQAITRTNICIEQHLAPHGDVTPETWGWRRSRNYVELIIVDESERLRPAALELLRDRYDRDDIALILIGMPGLEKQFSHYPQFYSRVGFAHQYRPLGQDELLFVLQRHWRSLGKTLDPEDFTDAQAIAAIARVTRGNFRLLERLIPQIQRVLKINELDTITNDVIEAAQSTLVIGVT$","Uncharacterized ATPase, putative transposase","Cytoplasm","ATP-binding protein p271","ATP-binding protein","Uncharacterized ATPase putative transposase-like","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein p271","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1953","2122185","2124182","1998","6.47","-6.81","72918","TTGTCACCGATTTGGACACAACCCCGCAGATGTCACCGTTTCTGGCCCCTTGTAGCGCTTGCCGCCCCGCCTCCGGGGCTCGTGTTCACGTCCCACGGCTCGCGCTCCGCCGAGGCAGCCCAAGATCCGGGCCGTCAGCTGCGCTTGCGCGGTCATGACGCGAATGGATGTGACGTCACTGTCGGTAGCACTGTCAGCCACGCGCGCCCAGGCATGACGCCGGCCGGCTCGCCCCTCCCGCTGGAAGAGGAACGTCTCCTCCGTCACGGCGGCGCGCTGCCCCGGCTTGGGATACTCCCGCCCATGTCCGCCACGCCCAGCGATCCTACGTCCCCGGCGCCGTCCGCCCCCGACGGCCCGCTCATCGTCCAGTCCGACAAGTCCGTCCTCCTGGAGGTCGCCCACCCCCAGGCCGGGCAGGCCCGCCGCGCCATCGCCGCCTTCGCCGAGCTGGAGCGCGCCCCCGAGCACATCCACACCTATCGAATCACGCCGCTGGCCCTGTGGAACGCACGCGCCGCGGGCCTGGACGCGGAGACGGTCGTCCACACGCTCATCACCTACTCGCGCTTCCCGGTGCCGCACGCCCTGCTCACCGAGATCGCCGAGACGATGAGCCGCTACGGCCGCCTCCAGCTGCTCACCGACCCCGCCCACGGCCTGGTCCTGCACGCCACCGACGTGCCGGTCCTGGAGGAGGTCATGCGCTCCAAGCGCACCAAGGGCCTGCTGGGGACGCGACTCGGGGAGGCCGACATCGTCGTCCACCCCTCCGAGCGCGGCCACCTCAAGCAGGTGCTCATCAAGCTGGGCTGGCCGGCCGAGGACCTGGCCGGCTACGTCGACGGCGAGGCCCACCCCATCACCCTGACCGACTCCCCCGACACCTTCCAGCTGCGCCCCTACCAGAGCGAGGCGGTGGAGAGCTTCTGGTCGGGGGGCTCAGGCGTGGTCGTCCTGCCCTGTGGGGCCGGCAAGACCCTCGTGGGCGCCGCCTCCATGGCCAAGAGCTCGACGACGACGCTCATCCTGGTCACCAACGCGGTCTCGGCGCGTCAGTGGAAGGAGGAGCTCATCCGCTTCACCTCCCTGACCGAGGAGGAGATCGGCGAGTACTCCGGCTCGCGCAAGGAGGTCCGCCCCGTCACGATCGCCACCTACCAGGTGCTCACCACCCGCCGCAAGGGCGTTTACCCGCACCTGGACCTGCTGGACTCCCACGACTGGGGGCTCATCGTCTATGACGAGGTCCATCTCCTGCCAGCCCCGATCTTCCGTATGACCGCGGACCTGCAGGCGCGCCGCCGCCTGGGCCTGACCGCGACCCTGGTGCGCGAGGACGGCCGCGAGGACGAGGTCTTCAGCCTCATCGGCCCCAAGCGCTACGACGCCCCCTGGAAGGACCTGGAGAACCAGGGCTGGATCGCCCCGGCGATCTGCACCGAGGTGCGCCTGACCCTCGACGCCGGTGAGCGCATGGCCTACGCGACCGCCGAGCCCGACGAGCGCTACCGCCTGGCCGCCTGCTCACCGCGCAAGCTGCCGATCATCGAGGCCCTCCTGGCCCGCCACGAGGGCGAGTCGGCCCTGGTCATCGGCCAGTACGTGGACCAGCTCACCGAGATCGCCGAGCACCTGGACGCCCCCGTCATCACCGGGGCGACGACGGTGCGCGAGCGCCAGCGCCTCTACGACGCCTTCCGCTGCGGGGAGATCCGCACGCTCGTGGTCTCCAAGGTCGCGAACTTCTCCATCGACCTGCCCGGGGCGAGCGTCGCGATCCAGGTCTCGGGCTCCTTCGGCTCGCGCCAGGAGGAGGCCCAGCGGCTCGGGCGGATCGTGCGCCCCAAGGAGGACGGCCGCCAGGCCCACTTCTACACGGTCGTCGCCCGCGACACCGCCGACCAGGAGTACGCCGCCCACCGGCAGCGCTTCCTGGCCGAGCAGGGCTACGCCTACGCCATCATCGACGCCGAGGACCTCACCGAGAACAACTGA","LSPIWTQPRRCHRFWPLVALAAPPPGLVFTSHGSRSAEAAQDPGRQLRLRGHDANGCDVTVGSTVSHARPGMTPAGSPLPLEEERLLRHGGALPRLGILPPMSATPSDPTSPAPSAPDGPLIVQSDKSVLLEVAHPQAGQARRAIAAFAELERAPEHIHTYRITPLALWNARAAGLDAETVVHTLITYSRFPVPHALLTEIAETMSRYGRLQLLTDPAHGLVLHATDVPVLEEVMRSKRTKGLLGTRLGEADIVVHPSERGHLKQVLIKLGWPAEDLAGYVDGEAHPITLTDSPDTFQLRPYQSEAVESFWSGGSGVVVLPCGAGKTLVGAASMAKSSTTTLILVTNAVSARQWKEELIRFTSLTEEEIGEYSGSRKEVRPVTIATYQVLTTRRKGVYPHLDLLDSHDWGLIVYDEVHLLPAPIFRMTADLQARRRLGLTATLVREDGREDEVFSLIGPKRYDAPWKDLENQGWIAPAICTEVRLTLDAGERMAYATAEPDERYRLAACSPRKLPIIEALLARHEGESALVIGQYVDQLTEIAEHLDAPVITGATTVRERQRLYDAFRCGEIRTLVVSKVANFSIDLPGASVAIQVSGSFGSRQEEAQRLGRIVRPKEDGRQAHFYTVVARDTADQEYAAHRQRFLAEQGYAYAIIDAEDLTENN$","ATP-dependent DNA helicase","Cytoplasm","DNA or RNA helicases of superfamily II","DNA or RNA helicase of superfamily protein II","helicase domain protein","","Tanaka K., Wood R.D. Xeroderma pigmentosum and nucleotide excision repair of DNA. Trends Biochem. Sci. 1994. 19(2):83-86. PMID: 8160271Vermeulen W., Scott R.J., Rodgers S., Muller H.J., Cole J., Arlett C.F., Kleijer W.J., Bootsma D., Hoeijmakers J.H., Weeda G. Clinical heterogeneity within xeroderma pigmentosum associated with mutations in the DNA repair and transcription gene ERCC3. Am. J. Hum. Genet. 1994. 54(2):191-200. PMID: 8304337","","","

InterPro
IPR001161
Family

Xeroderma pigmentosum group B protein (XP-B)
PR00851	$\"[111-131]T$ $\"[510-525]T$ $\"[573-591]T$ $\"[592-617]T$	XRODRMPGMNTB

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[545-617]T$	Helicase_C
SM00490	$\"[540-617]T$	HELICc
PS51194	$\"[516-665]T$	HELICASE_CTER

InterPro
IPR006935
Family

Type III restriction enzyme, res subunit
PF04851	$\"[296-445]T$	ResIII

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[295-472]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[307-461]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[493-650]T$	no description
PTHR11274	$\"[120-665]T$	RAD25/XP-B DNA REPAIR HELICASE
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 10 clades of COG1061COG name: DNA or RNA helicases of superfamily IIFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1061 is ao-pkzy--drl--e-g-------t-Number of proteins in this genome belonging to this COG is 2","***** IPB001161 (Xeroderma pigmentosum group B protein signature) with a combined E-value of 9.9e-43. IPB001161D 308-330 IPB001161E 408-428 IPB001161F 473-495 IPB001161G 510-525 IPB001161I 573-591 IPB001161J 592-617 IPB001161K 619-642","","","-49% similar to PDB:2FWR Structure of Archaeoglobus Fulgidis XPB (E_value = 4.6E_43);-56% similar to PDB:2FZ4 Crystal Structure of the N-terminal half of Archaeoglobus Fulgidus XPB (E_value = 8.1E_24);-57% similar to PDB:2FZL Structure of C-terminal domain of Archaeoglobus fulgidus XPB (E_value = 1.4E_15);","Residues 296 to 445 (E_value = 7.3e-12) place ANA_1953 in the ResIII family which is described as Type III restriction enzyme, res subunit.Residues 300 to 451 (E_value = 5.9e-09) place ANA_1953 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 545 to 617 (E_value = 6e-12) place ANA_1953 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","or RNA helicases of superfamily II (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1954","2125075","2124266","810","5.60","-7.88","27691","ATGGTGCGCCCCTGGCGGGGCGAGCCCATCCCCTCCCTGGACGAGATCGGCGACGGCCTCGTTGTGCTGGGCGGCTCCATGAGCGCCCACGACGAGGGCGAGCACCCCTGGCTGGCGGACCTGCGTGAGCTGCTGCGCGGCGTCGTCGCCGACGACGTCCCCGCCATCGCCATCTGCCTGGGCGCCCAGGTGGCCGCCGAGGCCCTCGGGGGCTCCACGGCCGTGCCGGCGCTGGGCAACGACGAGGTCGGCGTCGTCGAGCTGACCATCACGGCCGCAGGCGAGAGTGACCCGGTCTTCGGGGCCGTGGCCGCCGAGGCCATCCGCGCCGCTCACCGCGCCGGAATCTCCACCTCCGACGGCACCCGCCTGCCCGTCATCGTCTCCCACCACGACGCCGTCACCCAGCTGCCCGAGGCCGCCACCCTGCTGGCCTCCTCCGACCGCTCCCCGGTTCACACCTGGCGGGCCGGGCGACTCCTGGCCTTCCAGCACCACCCCGAGTCCGACCCGGCGCGCGTGGCCTACTGGCGCACCCGCGACGCCCTCAACGACCTGGCCGGGACCATGGACGCGGCCTCCCTCCAGGCTGCCCGCGATGCCCTGGAGGTGGCCGCCGGCCGGAGCGCCGCGCCGGGCGCCGCCGGAACCCACGGGGCCACGGCCGCCGACCTGCCCGAGGTGGCCGCCAGCGCCGGGGCCGCTGCCCGCGAGCAGGCCGAGAGGGTCGACCCCGCCATCCAGGCCTTCGGCCGCGGCCTGGCCCGCGTCCTCGTGCGCAACGTGCGCGCCCGCCGTCTGGCGCGCTGA","MVRPWRGEPIPSLDEIGDGLVVLGGSMSAHDEGEHPWLADLRELLRGVVADDVPAIAICLGAQVAAEALGGSTAVPALGNDEVGVVELTITAAGESDPVFGAVAAEAIRAAHRAGISTSDGTRLPVIVSHHDAVTQLPEAATLLASSDRSPVHTWRAGRLLAFQHHPESDPARVAYWRTRDALNDLAGTMDAASLQAARDALEVAAGRSAAPGAAGTHGATAADLPEVAASAGAAAREQAERVDPAIQAFGRGLARVLVRNVRARRLAR$","Glutamine amidotransferase class I","Cytoplasm","hypothetical protein","glutamine amidotransferase class-I","GMP synthase - Glutamine amidotransferase domain-like","","Konig V., Vertesy L., Schneider T.R. Structure of the alpha-amylase inhibitor tendamistat at 0.93 A. Acta Crystallogr. D 2006. Protein of the Month alpha-Amylase.:2003-McDowall J.. PMID: 14501112","","","

InterPro
IPR000833
Family

Alpha-amylase inhibitor
SM00783	$\"[166-232]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[1-201]T$	no description

","BeTs to 21 clades of COG0518COG name: GMP synthase - Glutamine amidotransferase domainFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0518 is aompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 3","***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 3.7e-07. IPB000991A 54-71 IPB000991B 159-169","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1955","2125287","2127482","2196","5.24","-18.33","75082","ATGAAGAACCAGCAGCCCCCACTCCCCCGTCCTTGGCACCAGATGGCCCTTTCCGGCGTCGCGACGGCGGCCGCCCTGGGGCTGCTGGGGCTCTCGGCAAGCGCCACGGCGGCGCCGACAACGCCCGGCTCCGCACCCCTGGCCCTGGCCTCCTCCGCACAGACCTCGGCCGCCTCGGTGGGCGTGCCCCGGGCCCTCCCGGCGGCGTCGACCACCCTGACCGAGCACGTCACCGATGAGCTCGGGATCCTGGATGCCTCCAAGGCCCAGCAGGCCGTGGACACCATGTCCTCCAAGTACGGCGTGGGCCTGTGGGTGCTGACCGTCTCCGACTCCAGCCAGAAGGCCTCCGCCATCGCCGAGCAGGCCTTCAAGGACACGAAGCTGGGACGCGACGACATGCTCCTGGTCATCAACATCCCCTCCGACGGCTCGACCTCGAAGAGCTACAAGCTGCAGGCGCACGACAACTCCTCGAAGTTCTCCGAGTCCGACTACAAGCGCATTGACTCGGCCATCAAGAAGCAGCTGCGCGCAGGCAACTACGACGACGCCGTGGCCGCCATCCCGGACAACATGTCCGGCTCATCAGGCTCGGGCAGCTCGGGCGACTCGGGGGACTCAGGCTCCTCGGCGCTTCCGCTCCTGCTGGGCGGGGGCGCGGTCGCGGCAGGCGGGGCCGCCGCCTGGACGGTGTACAAGCGCAGGAAGAACAAGGAGAACGACGACATGCTGTTCGGCAAGCGCAGGAATCAGGGCGGCACCCCCGGGAACCAGCCCGCGGGCCCCGCGGCGATGACGGTGGAGCAGCTGCGCACCCAGGCCGGCAGCGCCCTAGTCCAGGCCGATGACACGGTGCGCGCCGCCGCCGAGGAGTTGTCCTACGCGCAGGCGCAGTTCGGCCTGTCCGCCACGGATGCCTTCACCGCCGCCCTGGACAGCGCCCGCAAGCACCTGTCGCGGTGCTTCGAGCTGCGCAAAATCCTCGACGACGACATCCCCGAGACCGAGCCGCAGCAGCGCCAGATGTACACCGAGATCCTCCAGCACTGCTCGGAGGCGGTCGGTGAGATCCGCGCTCAGGAAGAGGCATTCAACAAGCGGCGCGGCATCGAGGCAAACCTGCCGACGTCGATCGCCGAGACCGCCCAGCGGGCCGACGAGACCGAGCAGGCCATCGTCATGGCCGAGACGATCTTGGTGACGCTCAGCGCCGCCTACCCCGCCTCCTCTCTGACCAGTGTGGCCCAGGCCCCCGAGCAGGCCCGCCGCCTGCTGGCCGCCGGGCGCACCGCCCTGGACCAGGCCCGCGCCAGCGTCGAGGCCTCCCAGGAGGCGACGGCGGTCGAACAGGTCCGCATCGCCCAGGGTTCCATCGCCCAGGCCGGACAGCTGGCCGCCCAAGTCACCGGGGCCCGCGAGCGCCTCCAGAGCGCGGCCAAGGACCTGGAGGCGGCCATCGCCTCGATCTCCTCGGACCTGGTGGACGCCAAGCGCCTGGAGGGCGCGGTGCCGGCGGCGACCCTGGCCCCGCTGGTGGCCGACGCCGAGGCCGCCGTCGCCGAGGGCCGTCAGGCCAGTGGCGCCAACCCGAGCGGCGACCCCCTGGCCGCCCTGGACCATCTGGCCCGGGCCGAGGCCGCCATCGACGCCGCCCTGGCCCCGGCCCGCGAGCGCGAGGAGAACGACTCGCGCGCCCGGGCCTCCCTGGGCTCGCGCCTGGCCCGCCTCAACTCCCAGGTGGAGTCCGTGACCTCCTACATCACCACCTATCGCGGGGCGGTGGGCCCCTCGGCGCGCACCGCACTCAGTGAGGCCGCCCGTCACGCCACGGCCGCCACCACCGTCCAGACCACTGACCCGGTGGCCGCCCTGGCGGAGGTCGCGGCGGCCGAGCCGCTCGTGGCCCAGGCCCAGGCCCTGGCCGAGGCCGACGTGCGCGGATCGTCGAGCTCGTGGAGCCCGAATTCCGGTGAGCGCTACTCCTACTCCCGCGATTACGGCCGCTCAGGCGGCGGGCTCGACCTGGGCTCTCTCCTGCTGGGCGGGCTGCTGCTGGGCGGCGGCCACAACTACGGCGGCTGGAGCTCCCACCACCACGACAGCGACTGGGGCGGAGGCGGCGGCTTCTTCTCCGGCGGCGGGGACTTCTCGGGTGGAGGCGGCGGCTTCTTCGACGGCGGCGGCGACTTCTGA","MKNQQPPLPRPWHQMALSGVATAAALGLLGLSASATAAPTTPGSAPLALASSAQTSAASVGVPRALPAASTTLTEHVTDELGILDASKAQQAVDTMSSKYGVGLWVLTVSDSSQKASAIAEQAFKDTKLGRDDMLLVINIPSDGSTSKSYKLQAHDNSSKFSESDYKRIDSAIKKQLRAGNYDDAVAAIPDNMSGSSGSGSSGDSGDSGSSALPLLLGGGAVAAGGAAAWTVYKRRKNKENDDMLFGKRRNQGGTPGNQPAGPAAMTVEQLRTQAGSALVQADDTVRAAAEELSYAQAQFGLSATDAFTAALDSARKHLSRCFELRKILDDDIPETEPQQRQMYTEILQHCSEAVGEIRAQEEAFNKRRGIEANLPTSIAETAQRADETEQAIVMAETILVTLSAAYPASSLTSVAQAPEQARRLLAAGRTALDQARASVEASQEATAVEQVRIAQGSIAQAGQLAAQVTGARERLQSAAKDLEAAIASISSDLVDAKRLEGAVPAATLAPLVADAEAAVAEGRQASGANPSGDPLAALDHLARAEAAIDAALAPAREREENDSRARASLGSRLARLNSQVESVTSYITTYRGAVGPSARTALSEAARHATAATTVQTTDPVAALAEVAAAEPLVAQAQALAEADVRGSSSSWSPNSGERYSYSRDYGRSGGGLDLGSLLLGGLLLGGGHNYGGWSSHHHDSDWGGGGGFFSGGGDFSGGGGGFFDGGGDF$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

","BeTs to 3 clades of COG0840COG name: Methyl-accepting chemotaxis proteinFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0840 is ao--k---vd--bcefg-s-uj--t-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1957","2127703","2128548","846","5.10","-7.77","30072","ATGGCTGAGAAGCAGTCGATCCTGGGGCGCATCGCCCAGCTCACCCGTGCCAACATCAACGCGCTCCTGGACCGCGCCGAGGACCCGGAGAAGATGCTCAACCAGCTGGTGCGGGACTACACGGCGTCCATCGCCGAGGCCCGTGACGCCGTCGCCCAGACGATCGGCAACCTGCGCCTGGCGGAGAAGGACCACGACGCCGACGTCGCCGAGGCCAAGGACTGGGGCAACAAGGCCCTGGCCGCCTCCCGCAAGGCCGACCAGCTGCGCTCCGGCGGTGACACGGCCGGCGCGGACAAGTGGGACTCACTGGCCAAGATCGCGCTGACCAAGCAGATCACGGCGGAGAACGAGGCCAAGGCCGCCGAGCCGATGATCGCCTCCCAGCGCCAGGTCGTCGAGCAGCTCAAGACCGGCCTGCAGCAGATGGAGGTCAAGCTCGGCGAGCTGCGCTCCAAGCGCGACCAGCTCATCGCCCGCCAGAAGACCGCCGAGGCCCAGGTCAAGGTGCAGGGCGCCATCCGCTCCATCAACGTCCTGGACCCCACCAGCGAGCTGTCTCGCTACGAGGACCAGGTGCGTCGGGTCGAGGCCCAGGCCGCCGGGCAGATGGAGCTGGCCGGCTCCTCCCTGGAGTCCCAGTTCGCCGAGCTCGAGGCCTCCGGGGCCAGCCTGGAGGCCGAGGCCCGGCTGGCGGCCCTGAAGTCCGGGCAGAACCCGGCCCTTCCGGGCGCCCAGCAGCAGGCCCCCGCCCAGATCACCGACGGCGACGACGCGATCAACGCCGCCTTCGCGGCCCTGAAGAACCAGGGTCAGCCGGCCGGCGAGGAGACCTCCTCCTACTGA","MAEKQSILGRIAQLTRANINALLDRAEDPEKMLNQLVRDYTASIAEARDAVAQTIGNLRLAEKDHDADVAEAKDWGNKALAASRKADQLRSGGDTAGADKWDSLAKIALTKQITAENEAKAAEPMIASQRQVVEQLKTGLQQMEVKLGELRSKRDQLIARQKTAEAQVKVQGAIRSINVLDPTSELSRYEDQVRRVEAQAAGQMELAGSSLESQFAELEASGASLEAEARLAALKSGQNPALPGAQQQAPAQITDGDDAINAAFAALKNQGQPAGEETSSY$","Phage shock protein A","Cytoplasm, Periplasm","similar to chloroplast membrane-associated 30 kDprotein","K03969 phage shock protein A","PspA/IM30 family protein","","Elderkin S., Jones S., Schumacher J., Studholme D., Buck M. Mechanism of action of the Escherichia coli phage shock protein PspA in repression of the AAA family transcription factor PspF. J. Mol. Biol. 2002. 320(1):23-37. PMID: 12079332","","","

InterPro
IPR007157
Family

PspA/IM30
PF04012	$\"[6-240]T$	PspA_IM30

","BeTs to 8 clades of COG1842COG name: Phage shock protein A (IM30), suppresses sigma54-dependent transcriptionFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1842 is -------q-dr-bcefg----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 240 (E_value = 5.8e-39) place ANA_1957 in the PspA_IM30 family which is described as PspA/IM30 family.","","to chloroplast membrane-associated 30 kD protein (IM30)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1958","2128627","2129574","948","7.20","0.76","33978","ATGAGTACCGGGCGGCTTCGTGCGCCTCGACGTCGGCCGACGCCCGCCGACACAGGCCGACCCGGGCCGCCCCGGGCCGACACGGGCCCCGGCCGGGGACATTCCGCGCGCCCGGGGACAGTCCGTCCCGGCGAGGGACATCCCACGCCTGCGGGGACAGGATTTCCGCACCCGACGGCGTCGATCGTCCCCATCGGGAAGGTTTTGTCCCCGCCGGGAAGATTTTGTCCCCGACCGCGCAGACCGCACCCGACGGCGTCGTCGGCACGGGGAGACCGGTATCGGTGCGGTGTCATCGAGCGTCGCCGGAGGCTAGTGGACGCCGTGACCGGTAGCATGAGCCTCATGAGCGTACCGACTTATCTTCTCGTCGATGGCGAGAACATTGACGCCACTCTCGGCATGAGTGTGCTGGGGCGGCGTCCCGAACCTGAGGAGCGGCCCCGCTGGGACCGAGTCCTCGCATACTGCGATGAACTGTCCTCCGCCGGCACCGCCGAGGGCGAGGGGAACGAGGCCCGTGCCCTGTTCTTCCTCAACGCCACCAGCGGCCATATGCCCATGAGCTTCATCCAGGCCCTCCTGGCCATGGACTATCGCCCCGTGCCGCTGGCCGGGTCCGGCAGCAACGACGAGAAGGTCGTCGACATCGGTATTCAGCGCACCCTGGAGGCGCTGGCCGAACGGGCCGAGTCCGGGCAGGAGGCCCACGTCCTGCTGGGCAGCCACGACGGCGACTACATCCCCCACATCGAGCGGCTCCTGCAGGCCGGCGCCAAGGTGGGGATCCTGTGCTTCCGAGAGTTCCTCAACGCCCAGCTGGCCGCCCTGGAGGGCGAGGGCCTGACGGTCTACGACCTGGAGAGTGACGTCAAGGCCTTCACCATCCCGCTGCCACGCGTGTGCATCATCCCGCTGGAGGACTTCGACCCTCTCGCCTTCCTCTGA","MSTGRLRAPRRRPTPADTGRPGPPRADTGPGRGHSARPGTVRPGEGHPTPAGTGFPHPTASIVPIGKVLSPPGRFCPRPRRPHPTASSARGDRYRCGVIERRRRLVDAVTGSMSLMSVPTYLLVDGENIDATLGMSVLGRRPEPEERPRWDRVLAYCDELSSAGTAEGEGNEARALFFLNATSGHMPMSFIQALLAMDYRPVPLAGSGSNDEKVVDIGIQRTLEALAERAESGQEAHVLLGSHDGDYIPHIERLLQAGAKVGILCFREFLNAQLAALEGEGLTVYDLESDVKAFTIPLPRVCIIPLEDFDPLAFL$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1959","2129701","2130564","864","5.38","-7.79","32072","GTGGGAACTGCAAGACTCCCTGGGTCTACAATTGGAACGAGGTCACACCAACCACTTGACCTATCAACAGCGACCATTCGGACGTCGTTCAGGAAACGACCAGAAACTGAAGGAATGGTGAGACTCATGGAGCGTTCCCAGCAGTCCCGCACCGAAGCTCACCTCCTTGTCGTCGACGATGAACCCAACATCCGCGATCTGCTGGCCTCGTCCCTGCGCTTCGCAGGCTTCGAGGTCTCGATCGCGGGCGACGGCAACGGCGCACTGAAGACAGTGGAGAAGACGTCTCCCGACCTGGTGGTCCTCGACGTCATGCTGCCCGACATGGACGGCTTCACCGTGGCACGACGCCTGCGCGAGCGCGACGTGACCACCCCGATCCTCTTCCTGACCGCCCGCGACGACATGGCCGACAAGGTTCAGGGCCTGACCGTCGGCGGCGATGACTACGTCACCAAGCCCTTCGGGCTGGAGGAGGTCATCGCCCGTATCCGCGCCATCCTGCGCCGCACCCACGCCATTGAGAACCAGGACGACGGCGTCGTGCGCGTGGCCGACCTGGTCCTGGACGAGGACGCCCACGAGGTGTACCGCGCCGAGGTCGAGGTGGATCTGTCGCCCACCGAGTTCAAGCTCCTGCGCTACCTCATGCTCAACGCCGGGCGCGTCGTGTCCAAGGCCCAGATCCTCGACCACGTCTGGGAGTACGACTGGAACGGTGACGCCGCGATCGTGGAGTCCTACATCTCCTACCTGCGCCGCAAGGTGGACCAGATCCAGGGCGCTGACGGCCAGCCCGTCACCCCGCTCATCCAGACTCGTCGCGGAGTCGGCTACATGCTCCGCGAACCCAAGGCCGAGTGA","VGTARLPGSTIGTRSHQPLDLSTATIRTSFRKRPETEGMVRLMERSQQSRTEAHLLVVDDEPNIRDLLASSLRFAGFEVSIAGDGNGALKTVEKTSPDLVVLDVMLPDMDGFTVARRLRERDVTTPILFLTARDDMADKVQGLTVGGDDYVTKPFGLEEVIARIRAILRRTHAIENQDDGVVRVADLVLDEDAHEVYRAEVEVDLSPTEFKLLRYLMLNAGRVVSKAQILDHVWEYDWNGDAAIVESYISYLRRKVDQIQGADGQPVTPLIQTRRGVGYMLREPKAE$","Two-component system response regulator","Cytoplasm","response regulator of two-component system","K02483 two-component system; OmpR family; response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[55-169]T$	Q8G876_BIFLO_Q8G876;
PF00072	$\"[53-165]T$	Response_reg
SM00448	$\"[53-164]T$	REC
PS50110	$\"[54-168]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[192-284]T$	Q9K850_BACHD_Q9K850;
PF00486	$\"[200-281]T$	Trans_reg_C

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00217	$\"[140-165]?$	SUGAR_TRANSPORT_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[50-204]T$	no description
PTHR23283	$\"[43-170]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[43-170]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 2.1e-45. IPB001867A 98-111 IPB001867B 126-170 IPB001867C 271-281***** IPB000673 (CheB methylesterase) with a combined E-value of 7.3e-14. IPB000673A 56-65 IPB000673B 70-123 IPB000673C 124-154***** IPB001789 (Response regulator receiver) with a combined E-value of 1.3e-12. IPB001789A 98-111 IPB001789B 146-156","","","-59% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 1.5E_41);-59% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 1.5E_41);-62% similar to PDB:1KGS Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima (E_value = 7.6E_41);-58% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 4.6E_38);-71% similar to PDB:1MVO Crystal structure of the PhoP receiver domain from Bacillus subtilis (E_value = 1.1E_28);","Residues 53 to 165 (E_value = 1.6e-41) place ANA_1959 in the Response_reg family which is described as Response regulator receiver domain.Residues 200 to 281 (E_value = 3.7e-24) place ANA_1959 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","regulator of two-component system","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1960","2130564","2132162","1599","8.87","6.35","57630","ATGGCGGCGGCGCGTGGGGGGAGCACGCGCCCGGCCAAGTCGTCCGGTAAGCAGCACCGCCCGATCAAACGGGGCCGATGGCACCCGATCACCGCGATTCAGCGGCCGTGGCAGGCGATGCCACTGCGCACGCGCCTGACCCTCATGACCACCGGCCTGCTGGCCATCGGGCTCATCGTCGTCTCCTTCGTGGTGACCTCACTGCTCTACAGCCACATGATGGGCCAGATCGACAGCCAGCTGCGCACCACCTCGGTGGCGATCGGAAGCCAAGGACTGGCCCAGATCCGCGAGGGAGGGACCAGCAGCACCACCTTCCCCTCGAACTACTACGTCAAGGCCGAGTACCTCGACCCCAGCCGCAACGGGGAGTGGATCTCCCCGGACACCGCCGCCACCTACGGCCGCCCCCAGATCAAGGGCCTGGACTACCGGCGCGCCCTGGCCCACGCGGACAAGAACGACTTCCCGATCACGACGGTCAACTCCGATCAGCCCGGCCACCAGTGGCGGATGATCACCCTGCTCATCAGGGACCAGAACACCGGCGAGTACACCGGCGCCGTGGCCCTGGCCCTCCCGCTGAGCGACGTCATGGAGACCGTCGAGCGCACCCGCCTCGTGGTGGCCCTGGCTGACGTCTCGATCATCTCGGTGGGCGCCGTCTTCGCCACCTACCTGGTTCACCGCTCGTTCCGCTCCCTGCGCCAGATCGAGAGCGTGGCCGCCCGGATCGCCCACGGCGACCTGTCCGCCCGCATTCTGGTCACCGAGCCGCGCACCACGGAGGTCGGCTCCCTGCAGCGGGCGATCAACACGATGCTCACCCAGAACGAGAGCTCCTTCGCCGCCCAGGTCGTGGCTCAGGAGCGGATGACGCGCTTCGTCTCCGACGCCTCCCACGAGCTGCGCACACCCCTGGCCGCGATCCGCGGCTACGGCGAGCTCTACCGGATGGGCGGGGTGCCGGCGAACAAGACCGGTGAGGTCATGGGACGCATCGAGACCGAGTCCAACCGGATGGGGCGCCTCGTCGATGACCTCCTCCAGCTGGCCCGGATCGACGAGGGCCGGGAAATGTCCATGGAGCCGGTCAACCTCACCGACCTGGCCGCCGGGGCCCTGAGCGACATGATGGTGCTGGCCCCCGAGCGCGACTGCGGACTCATCCCCCTCGACCCCCACGACGAGGCCGCCGGCAAGGAGGCCCCCTCGCTCCAGGTCATCGGTGACCGCGACCGCCTCTCCCAGATCCTCACCAACCTGCTGGGCAACGTGGTGCGCCACACCCCCTCCGGGACGCCGGTGGAGATCGCCATCGGCATGGCGCCCCCGCGCGCCAACCCGACGGCGCAGCCAGTCGTCGTCGTCGAGGTCCGCGACCACGGCCACGGCGTGCCACCGGAGGCGGCCGAGAAGGTCTTCCAGCGCTTCTACCGCTCGGACACCTCCCGCAACCGGGAGACCGGGGGCTCCGGCCTGGGACTGGCGATCGTGCTGGGGATCGTGGCCGCTCACAAGGGCACGGTCCAGATGCTCCAGACCCCCGGCGGCGGCGCCACCGTCCACATCGAGCTGCCGCCCGCACCGGCCTGGTAG","MAAARGGSTRPAKSSGKQHRPIKRGRWHPITAIQRPWQAMPLRTRLTLMTTGLLAIGLIVVSFVVTSLLYSHMMGQIDSQLRTTSVAIGSQGLAQIREGGTSSTTFPSNYYVKAEYLDPSRNGEWISPDTAATYGRPQIKGLDYRRALAHADKNDFPITTVNSDQPGHQWRMITLLIRDQNTGEYTGAVALALPLSDVMETVERTRLVVALADVSIISVGAVFATYLVHRSFRSLRQIESVAARIAHGDLSARILVTEPRTTEVGSLQRAINTMLTQNESSFAAQVVAQERMTRFVSDASHELRTPLAAIRGYGELYRMGGVPANKTGEVMGRIETESNRMGRLVDDLLQLARIDEGREMSMEPVNLTDLAAGALSDMMVLAPERDCGLIPLDPHDEAAGKEAPSLQVIGDRDRLSQILTNLLGNVVRHTPSGTPVEIAIGMAPPRANPTAQPVVVVEVRDHGHGVPPEAAEKVFQRFYRSDTSRNRETGGSGLGLAIVLGIVAAHKGTVQMLQTPGGGATVHIELPPAPAW$","Two-component system sensor kinase","Membrane, Cytoplasm","histidine kinase sensor of two-component system","periplasmic sensor signal transduction histidine kinase","ATP-binding region, ATPase domain protein domain protein","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[402-527]T$	no description
PF02518	$\"[410-529]T$	HATPase_c
SM00387	$\"[410-530]T$	HATPase_c

InterPro
IPR003660
Domain

Histidine kinase, HAMP region
PF00672	$\"[210-280]T$	HAMP
SM00304	$\"[229-283]T$	HAMP
PS50885	$\"[229-283]T$	HAMP

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[291-357]T$	HisKA
SM00388	$\"[291-357]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[455-469]T$ $\"[473-483]T$ $\"[490-508]T$ $\"[514-527]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[298-530]T$	HIS_KIN

noIPR
unintegrated

unintegrated
PTHR23283	$\"[35-527]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23	$\"[35-527]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
tmhmm	$\"[52-72]?$	transmembrane_regions

","BeTs to 16 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB004358 (Bacterial sensor protein C-terminal signature) with a combined E-value of 3e-19. IPB004358A 455-469 IPB004358B 473-483 IPB004358C 490-508 IPB004358D 514-527***** IPB003661 (Histidine kinase A, N-terminal) with a combined E-value of 3.5e-13. IPB003661A 295-307 IPB003661B 459-478***** IPB003660 (Histidine kinase, HAMP region) with a combined E-value of 1e-08. IPB003660B 263-274 IPB003660C 493-511","","","-52% similar to PDB:2C2A STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN (E_value = 2.7E_22);-46% similar to PDB:1YS3 Crystal Structure of the ATP binding domain of PrrB from Mycobacterium Tuberculosis (E_value = 3.2E_12);-46% similar to PDB:1YSR Crystal Structure of ATP binding domain of PrrB from Mycobacterium Tuberculosis (E_value = 3.2E_12);","Residues 210 to 280 (E_value = 1.7e-11) place ANA_1960 in the HAMP family which is described as HAMP domain.Residues 291 to 357 (E_value = 1.7e-22) place ANA_1960 in the HisKA family which is described as His Kinase A (phosphoacceptor) domain.Residues 410 to 529 (E_value = 1.2e-38) place ANA_1960 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","kinase sensor of two-component system","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1961","2132300","2133718","1419","5.04","-24.93","51125","ATGGGTGTTATCGAAGCACCGCAATGGCTTCTGCCCGCCTTCACCCGCTCGGTGAAGGCGATTGGCGCCACGCAGCCCCCAGAGGCGATCGGCTCCGCCGGCGAGCTCCTCATTGAGCGCTGGTCCACACCGGACCGTCGCTTCCACAACCTTCGCCACCTCATCGACATGCTCGCGCGGGTCGATGAGCTGGCCGAGGAGTCGCACAACCCGGACATCATGCGGGTCGCCTGCTGGTACCACGGCTGCGTCTTCTCCTCCGACGTCGAGGAGGTCATCCGCGGCAACGGCGGCGAGGACGAGACCGCCTCGGCAGCCTTCGCCGAGGCCGACCTGCGTCACCTGGGTGTCCCGATGGAGACGGTCAAGCGGGTGTGCAGCCTCATCGTCAACCTCAAGCGGCACATGCTCGCCGATGACGACATCGACGCCCAGGCCCTCATCGACGCCGACCTGGGAACCCTGGCCGTGGACCCCCAGACCTACACCGAGTACGTGCGGCTTCTGCGTGAGGAGTACTCCCACATCCCCGTGGAGGAGTACCTGCGCGGCCGCCTGACGATCGTCTCCCGGCTCCTGGACCGTGAGCACCTCTTCCACTCCCCACTGGGCGAGCGCTGGGAGCACCCGGCTCGGGAGAACCTGTCAGCCGAGCAGCGGCGTCTCCACGAGAAGCTCACCAAGCTCGCCGAGGAGCGGGGAGCGCAGGCCGATCCGGCGGCCCTGGAGGCCGCGGCCGCGCAGGAACCGACGCGCCCCGCCCCGGTGGCCTTATCGGCCAGCCCCACCGCTGTCGAAGACCTCGCTCCCGGGGCTGCCGAGCAGCCGGACGAGACCGCCGAACGCGCTCCCCGCACCCCTCCGCTGGGCCTCCAAGCGCTGCCCGTCAAGGACCCCACGACCGGCCCCGCCCGGGACGGCGACACCCTGCGCCTGGACTCAACCGCGCTCAGGGCCCTGCGATCCACGGTGACGGCATCGACCGCGACGCCGCCCGCCTCCCCGGCCTCCGTGGCGTCCTCAGGATCGCCGGAGGCTCCGTCCTCATCCGCCTCCCCATCGAGCGTCTCCTCGCCGCGTACCCCCGCCCGCGGGATCCCGGCCGTGGCCTCAGCGCGCCACCCCGTCGATGCACCCGCTGAGCGGGGCGAGGGTCGCGAGGACAAGGACGGGGAGGAGGCGATGGCGCACACCGCCTCCATGGAGTCGTGCATCGCGGACCTGGACCTGCTCATGTGCTCGCGCAACCGCTCCGACGATGCCGAGGACCGCCGCGCCCGGGTCCAGGCCGAGCGGGACAAGCTCACCGAGAAGCTACGAGCCAAGACCCAGGAGGCCAAGGAGCTGCGCGAGGCCCGTACCGGCGAGATCGCTCCCATCACCGAGGAGATCATCGACGACGGCGCCGGGGACCTCTGA","MGVIEAPQWLLPAFTRSVKAIGATQPPEAIGSAGELLIERWSTPDRRFHNLRHLIDMLARVDELAEESHNPDIMRVACWYHGCVFSSDVEEVIRGNGGEDETASAAFAEADLRHLGVPMETVKRVCSLIVNLKRHMLADDDIDAQALIDADLGTLAVDPQTYTEYVRLLREEYSHIPVEEYLRGRLTIVSRLLDREHLFHSPLGERWEHPARENLSAEQRRLHEKLTKLAEERGAQADPAALEAAAAQEPTRPAPVALSASPTAVEDLAPGAAEQPDETAERAPRTPPLGLQALPVKDPTTGPARDGDTLRLDSTALRALRSTVTASTATPPASPASVASSGSPEAPSSSASPSSVSSPRTPARGIPAVASARHPVDAPAERGEGREDKDGEEAMAHTASMESCIADLDLLMCSRNRSDDAEDRRARVQAERDKLTEKLRAKTQEAKELREARTGEIAPITEEIIDDGAGDL$","Uncharacterized conserved protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","Uncharacterized protein-like","","Novoseler M., Hershkovits G., Katcoff D.J. Functional domains of the yeast chromatin protein Sin1p/Spt2p can bind four-way junction and crossing DNA structures. J. Biol. Chem. 2005. 280(7):5169-5177. PMID: 15563464","","","

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[375-453]T$	no description

InterPro
IPR010310
Family

Protein of unknown function DUF909
PF06013	$\"[29-117]T$	WXG100

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 29 to 117 (E_value = 1.1e-05) place ANA_1962 in the WXG100 family which is described as Proteins of 100 residues with WXG.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1963","2136126","2134504","1623","4.79","-27.43","56707","ATGTCCAAGATCATCGCCTTTGACGAGGAGGCCCGCCGCGGCATGGAGCGCGGCCTCAACACCCTCGCCGACACCGTCAAGGTCACCCTGGGCCCCAAGGGCCGTAACGTCGTGCTCGACAAGAAGTGGGGCGCCCCCACGATCACCAACGACGGCGTGACCATCGCCAAGGAGATCGAGCTCGAGGAGCCCTACGAGAAGATCGGCGCCGAGCTCGTCAAGGAGGTCGCCAAGAAGACCGACGACGTCGCGGGTGACGGCACCACCACCGCCACCGTCCTGGCCCAGGCCCTGGTGCGTGAGGGCCTGCGCAACGTCGCCGCCGGCGCCAACCCGATCGCCGTTCGCCGCGGTATCGAGAAGGCCGTCGCGGCCGTCGTCGAGCGCCTGCTGGCCGACGCCAAGGAGGTCGAGACCCAGGAGGAGATCGCGGCCACCGCCTCCATCTCCGCCGCCGACGAGCAGATCGGTGCCTTCATCGCCGAGGCCCTGGAGAAGGTCGGCCATGAGGGTGTCGTCACCGTCGAGGAGTCCAACACCTTCGGCCTCGAGCTCGAGGTCACCGAGGGTATGCGCTTCGACAAGGGCTTCATCTCCCCCTACTTCGTCACCGACCCCGACCGCCAGGAGGCCGTCCTGGAGGACGCCTACGTCCTGCTGGTCGAGTCCAAGATCTCCAACGTCAAGGACCTGCTCCCGCTGCTGGAGAAGGTCATGCAGACCGGCAAGCCGCTGGCCATCATCGCCGAGGACGTCGAGGCCGAGGCCCTGGCCACCCTCGTCGTCAACCGCATCCGCGGCACCTTCAAGTCCGTGGCCGTCAAGGCCCCCGGCTTCGGTGACCGCCGCAAGGCGATGCTGCAGGACATGGCCATCCTCACCGGCGGTACGGTCATCTCCGAGACCGTCGGCCTCAAGCTCGAGAACGCCACCCTGGAGGACCTGGGTCAGGCCCGCAAGGTCGTCGTCACCAAGGACGACACCACCCTGGTCGAGGGCGCCGGCGACAAGGAGGCCATCGAGGCCCGCACCGCCCAGATCCGCATGGAGATCGAGAACTCCGACTCCGACTACGACCGCGAGAAGCTCTCCGAGCGTCTGGCCAAGCTGGCCGGCGGCGTGGCCGTCCTCAAGTCCGGTGCCGCCACCGAGGTGGAGCTCAAGGAGCGCAAGCACCGCATTGAGGACGCCGTGCGCAACGCCAAGGCCGCCGTCGAGGAGGGCATCGTCGCCGGTGGTGGCGTCGCCCTGCTCCAGGCCGCCGAGGTCCTCGACACCCTCAAGCTCGAGGGCGACGAGGCCACCGGTGCCGCGATCGTCAAGGTCGCCGTGGAGGCCCCGCTCAAGCAGATCGCTGCCAACGCCGGCCTCGAGGGCGGCGTGGTCGTGGACCGCGTGCGCAACCTGCCCACCGGTGAGGGCCTCAACGCCGCCACCGGCGAGTACGTCAACCTGCTGGCCGCCGGCATCGCCGACCCGGTCAAGGTGACCCGCTCCGCCCTGCAGAACGCCGGGTCCATCGCCGGTCTGTTCCTGACCACCGAGGCCGTCGTGGCCGACAAGCCCGAGCCCCCGGCCGCCCCGGCCGATGGTGGCGCCGGTGACATGGGTGGCATGTACTGA","MSKIIAFDEEARRGMERGLNTLADTVKVTLGPKGRNVVLDKKWGAPTITNDGVTIAKEIELEEPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPIAVRRGIEKAVAAVVERLLADAKEVETQEEIAATASISAADEQIGAFIAEALEKVGHEGVVTVEESNTFGLELEVTEGMRFDKGFISPYFVTDPDRQEAVLEDAYVLLVESKISNVKDLLPLLEKVMQTGKPLAIIAEDVEAEALATLVVNRIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGTVISETVGLKLENATLEDLGQARKVVVTKDDTTLVEGAGDKEAIEARTAQIRMEIENSDSDYDREKLSERLAKLAGGVAVLKSGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALLQAAEVLDTLKLEGDEATGAAIVKVAVEAPLKQIAANAGLEGGVVVDRVRNLPTGEGLNAATGEYVNLLAAGIADPVKVTRSALQNAGSIAGLFLTTEAVVADKPEPPAAPADGGAGDMGGMY$","Chaperonin GroEL","Cytoplasm","65K antigen mbaA","60 kDa chaperonin","chaperonin GroEL","","Wang J., Boisvert D.C. Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution. J. Mol. Biol. 2003. 327(4):843-855. PMID: 12654267","","","

InterPro
IPR001844
Family

Chaperonin Cpn60
PR00298	$\"[26-52]T$ $\"[82-109]T$ $\"[266-289]T$ $\"[348-373]T$ $\"[396-417]T$	CHAPERONIN60
PS00296	$\"[403-414]T$	CHAPERONINS_CPN60

InterPro
IPR002423
Family

Chaperonin Cpn60/TCP-1
PR00304	$\"[24-40]T$ $\"[46-64]T$ $\"[80-99]T$ $\"[376-398]T$ $\"[409-421]T$	TCOMPLEXTCP1
PTHR11353	$\"[2-539]T$	CHAPERONIN
PF00118	$\"[22-522]T$	Cpn60_TCP1

InterPro
IPR012723
Family

chaperonin GroEL
TIGR02348	$\"[2-524]T$	GroEL: chaperonin GroL

noIPR
unintegrated

unintegrated
G3DSA:1.10.560.10	$\"[390-522]T$	no description
G3DSA:3.50.7.10	$\"[172-374]T$	no description
PTHR11353:SF10	$\"[2-539]T$	CHAPERONIN-60KDA, CH60

","BeTs to 26 clades of COG0459COG name: Chaperonin GroEL (HSP60 family)Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0459 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001844 (Chaperonin Cpn60) with a combined E-value of 7.2e-156. IPB001844A 23-77 IPB001844B 172-226 IPB001844C 249-302 IPB001844D 343-394 IPB001844E 474-511 IPB001844A 101-155 IPB001844E 407-444***** IPB002194 (Chaperonin TCP-1) with a combined E-value of 1.3e-28. IPB002194A 15-61 IPB002194B 73-122 IPB002194D 373-416 IPB002194E 433-470 IPB002194F 484-518","","","-78% similar to PDB:1SJP Mycobacterium tuberculosis Chaperonin60.2 (E_value = 7.8E_179);-70% similar to PDB:1WE3 Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus (E_value = 1.4E_156);-70% similar to PDB:1WF4 Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus (E_value = 1.4E_156);-66% similar to PDB:1AON CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7 (E_value = 3.3E_137);-66% similar to PDB:1GRU SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM (E_value = 3.3E_137);","Residues 22 to 522 (E_value = 3.4e-196) place ANA_1963 in the Cpn60_TCP1 family which is described as TCP-1/cpn60 chaperonin family.","","antigen mbaA (GROEL2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1967","2137843","2136443","1401","8.23","2.17","47892","ATGGGCACCGGTCGCCGCGCCCCGACTCTGCTCAGCGGCGGCCTCATTGTGGGCGGGGGCGGGGCCCTGTACCCCCTGGCCCCGGGTCACACGGTTGCCTACGTCTCGGGGACCCGCCTGCCCCAGGCTCCCGAACCGTGGGGCTTGACCACCTCGCAGCAGAGCGCCCTGGCCCGTCAGGCGCTCGCCCGCCGCAAGACGGCCCGTCTCCCTCAAGGCCGGTGGGCGGACCTGGCCGACGGCGCCCTGACCGATCTGCTGGCCCTGACCGGACCCGCGTTCATGCCCGACCCGACCCGCCCCGCCGGTCCTGCTGTCCCGTCGGCCCGGCTGACGGCGTCTCCGGCTCCCGTCCCCACTGCCGGCGCTGCCTCCGCCGCCTCTGGGAGCGCCGGCCTGGAGGGCCGCGACTCGCGCGAACCCCTCCCGCAAGGGGCGGAGGTCTTCCCGCAGGGCGCGGTCGTGGCGGCGCCCGTGAGCATCTGGCGCTACGTCTGGCCCCGGGACGCCGCCTTCGCCGCGGCCGCCCTCAGCGCGGTGAACCTGGCCGGCGAAGCGCTGGGCGTCCTGGGCAACCTGGCGTCCTGGCAGCGGGCCGACGGCGGCTTCGAGGCCCGCTACACCAGTAGCGGCCGAGTGCCGGACCACCGCCCGGCTCAGGCCGACGGCGCCGGGTGGTTCCTGTGGGCTGCGGGCCGGCTCCTGGCCGACGGCGTTTCAGCCGCCAACCTGCGTGACCGCCTGGGGGCACCTCTGGCGCGCGCCGCCTCCCGGCTCCTGGAGATCACGGACACGCCCTCCCACCTGCCCGCGGCCTCGCCCGACTACTGGGAGGTCGCCGAGACGGTGCTCACCCTGGGCACGGCCGCCCCGGTGCTTCTGGGGCTGGAAGCGGCGACAGCGCTGACCCGGGCCGGGATCGACCTCGGCGGCCCCGCTCAGGCCCTGGCCGAGCGGGTGACAGCGGTGCGCAGCGCCATGGAGCGCAACTTCGCCCCCGCCTGGGGCCGCCACCTGCGGCGCGACGACGTCGATGCCACCATCGCCCTGGTCCTGCCGCCCTTCACCCAGCCGCTGACCGGGGCACGAGCGGTGCGGCAGACGGCGACCGAGCGCATGCGCCGCCCCGCCGGGGGGCTCGCTCCGGGAGCGGGCTGGCGTGATGACGGCGTGTCCTGGACGCCGGAGACCGCCCTCATGGCCTGGTCGGCACTGTCCCTGGGGATGGAGGAGGAGGGAACCCGGCTGCTGGCGTGGCTGGAGGCGCACCGCACCGCTGCCGGAGCCCTGCCGGAGAAGGTCTTGGCCGACGGCGCCCCGGCGGGGCCCGCGCCCCTGGCCTGGACCTGTGCACTCATCCTGCTGGCCACCGCCTCACGGCCCGCAGACCCGCCCTCCTGA","MGTGRRAPTLLSGGLIVGGGGALYPLAPGHTVAYVSGTRLPQAPEPWGLTTSQQSALARQALARRKTARLPQGRWADLADGALTDLLALTGPAFMPDPTRPAGPAVPSARLTASPAPVPTAGAASAASGSAGLEGRDSREPLPQGAEVFPQGAVVAAPVSIWRYVWPRDAAFAAAALSAVNLAGEALGVLGNLASWQRADGGFEARYTSSGRVPDHRPAQADGAGWFLWAAGRLLADGVSAANLRDRLGAPLARAASRLLEITDTPSHLPAASPDYWEVAETVLTLGTAAPVLLGLEAATALTRAGIDLGGPAQALAERVTAVRSAMERNFAPAWGRHLRRDDVDATIALVLPPFTQPLTGARAVRQTATERMRRPAGGLAPGAGWRDDGVSWTPETALMAWSALSLGMEEEGTRLLAWLEAHRTAAGALPEKVLADGAPAGPAPLAWTCALILLATASRPADPPS$","Glycoside hydrolase","Periplasm, Membrane, Extracellular","hypothetical protein","glycoside hydrolase 15-related","Glucoamylase and related glycosyl hydrolase-like","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR012341
Domain

Six-hairpin glycosidase
G3DSA:1.50.10.10	$\"[150-460]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[10-28]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-41% similar to PDB:1HZO STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1 (E_value = );-49% similar to PDB:1W3O CRYSTAL STRUCTURE OF NIMA FROM D. RADIODURANS (E_value = );-49% similar to PDB:1W3P NIMA FROM D. RADIODURANS WITH A HIS71-PYRUVATE RESIDUE (E_value = );-49% similar to PDB:1W3Q NIMA FROM D. RADIODURANS WITH COVALENLY BOUND LACTATE (E_value = );-49% similar to PDB:1W3R NIMA FROM D. RADIODURANS WITH METRONIDAZOLE AND PYRUVATE (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1969","2137847","2138713","867","11.26","18.46","30283","ATGAGCCCCGCCCCAGAGGGCCGCGGCGGCGGTGAGCGGGACCGCCGCGGCGAGAGTCAGGAACCGACGACGCCCAAGAAGCGCCAGTGGCCTCATGCCCCTCTACTGCGGCTTGTAGTCATCACGCAGGATGACCGCGATCGGGGCATCCTGGGTGTTCTCCGCGGTGCCCTCCACCACGTTGCTGATCCCCAGGCGCTTGCCGATCTCCTGGGCGGCGGTCCGGGCCTCCGGGGAGCTGAAGTAGACCGTCGACTTGGCCGGCTCCGCGTTCTCGTAGATCCCGGGGATGACCTCCACCGCAGTGAAGCCGCCGTTGGTGAGCTTCTCGCTGGCCCCCTTGGCCAGGCCGTCGGTATTCGTCCCGTTGGCCACCGTCACCCTGGTGGTGAAGTCCACGTTGCCGGAGGGGCTGGCCGAGGCGCTGGGCTTGGCCGAGGCGGCGCCGGCCTTGTTGTTCGCACTGTCCGCGTTCTTGTCCGCGTTCTTGTTGCCACCGGCCTGGCCGCCCTGGGCGGGTTGAGAGGAGGAGACCGCGTCCGACGAGCCGGAGCCTCCCGAGCCGTTGAGGAACAGCGTCACCGCGCCCCAGGCGAGCGCCGGGACAATGACGATGATCGCCAGCAGCGGCACCCAGCTGCGCCACCTGGGCACCTGGGCCCGGTGCACGCCCACGGGAACCGGGCCGTCATCATCGCCGACGTCGAACTCGTCCTCGGGGTAGTCATAGTTGCTCACGCTCACAAGATACCGGTCCGAGCGTCATTCGTCGGGTATTGCTCACCACGTCCGGCTCACACGGCCGCGGTGTCCGGCCCGACAAGATCCTGCAGGTGCTGCCGATGGGCCATTAGGCTCATGGCGTGA","MSPAPEGRGGGERDRRGESQEPTTPKKRQWPHAPLLRLVVITQDDRDRGILGVLRGALHHVADPQALADLLGGGPGLRGAEVDRRLGRLRVLVDPGDDLHRSEAAVGELLAGPLGQAVGIRPVGHRHPGGEVHVAGGAGRGAGLGRGGAGLVVRTVRVLVRVLVATGLAALGGLRGGDRVRRAGASRAVEEQRHRAPGERRDNDDDRQQRHPAAPPGHLGPVHAHGNRAVIIADVELVLGVVIVAHAHKIPVRASFVGYCSPRPAHTAAVSGPTRSCRCCRWAIRLMA$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1971","2138710","2139387","678","8.22","1.88","24146","GTGACTTCCGCCAAGCCCCTGTCTGAGATCATCGATCCCTCCTGGGCGAGCGCCCTGGCCCCCGTGGAGCCCACGGTCCATGAGATCGGGGAGCGGCTGCGCCAGGAGGTGGCCTCCGGCGTCGGGTATCTCCCGGCGGGCACCGACGTGCTGCGCGCCTTCACCTACCCGATGGATGACGTGCGCGTCCTCATCGTCGGCCAGGACCCCTACCCCACCCCGGGTCACCCCATGGGGCTGAGCTTCTCGGTGGCGCCCGGCGTCAAGCCCCCGCGCAGCCTGGAGAACATCTTCCGCGAGCTGGTCAGCGACCTGGGCGTGCCCAGGCCGACATCGGGGGACCTGACGCCGTGGTGCCAGCAGGGCGTCATGCTGCTCAACCGGGTGCTCACCGTTCGCCCGGGGGCGCCGGCCTCACACAAGGGCTGGGGCTGGGAGAAGGTGACGCAGCGGGCGATCGAGGCCCTGGTGGAGCGTGGCGGCCCGCTCGTGGCGATCCTGTGGGGGCGGCCGGCGCAGTCGCTCACCCCGATGCTGGGGCAGACCCCCATCATCGCCTCGCCGCACCCGTCGCCGCTGTCGGCCTCGCGCGGGTTTTTCGGCTCGCGCCCCTTCAGCCGCGCCAACACGATCCTCACCGAGATGGGGGCCGCGCCCGTGGACTGGCGCCTGCCCTGA","VTSAKPLSEIIDPSWASALAPVEPTVHEIGERLRQEVASGVGYLPAGTDVLRAFTYPMDDVRVLIVGQDPYPTPGHPMGLSFSVAPGVKPPRSLENIFRELVSDLGVPRPTSGDLTPWCQQGVMLLNRVLTVRPGAPASHKGWGWEKVTQRAIEALVERGGPLVAILWGRPAQSLTPMLGQTPIIASPHPSPLSASRGFFGSRPFSRANTILTEMGAAPVDWRLP$","Uracil-DNA glycosylase","Periplasm, Membrane, Cytoplasm","Uracil-DNA glycosylase (UDG)","uracil-DNA glycosylase ","uracil-DNA glycosylase","","Sancar A., Sancar G.B. DNA repair enzymes. Annu. Rev. Biochem. 1988. 57:29-67. PMID: 3052275Olsen L.C., Aasland R., Wittwer C.U., Krokan H.E., Helland D.E. Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J. 1989. 8(10):3121-3125. PMID: 2555154Upton C., Stuart D.T., McFadden G. Identification of a poxvirus gene encoding a uracil DNA glycosylase. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(10):4518-4522. PMID: 8389453Slupphaug G., Markussen F.H., Olsen L.C., Aasland R., Aarsaether N., Bakke O., Krokan H.E., Helland D.E. Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene. Nucleic Acids Res. 1993. 21(11):2579-2584. PMID: 8332455Savva R., McAuley-Hecht K., Brown T., Pearl L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 1995. 373(6514):487-493. PMID: 7845459Mol C.D., Arvai A.S., Slupphaug G., Kavli B., Alseth I., Krokan H.E., Tainer J.A. Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 1995. 80(6):869-878. PMID: 7697717","","","

InterPro
IPR002043
Family

Uracil-DNA glycosylase
PTHR11264	$\"[26-225]T$	URACIL-DNA GLYCOSYLASE
TIGR00628	$\"[12-217]T$	ung: uracil-DNA glycosylase
PS00130	$\"[62-71]T$	U_DNA_GLYCOSYLASE

InterPro
IPR003249
Family

Uracil-DNA glycosylase, not poxvirus
PD001589	$\"[11-222]T$	UNG_CORGL_Q8NQU9;

InterPro
IPR005122
Family

Uracil-DNA glycosylase superfamily
PF03167	$\"[54-213]T$	UDG

noIPR
unintegrated

unintegrated
G3DSA:3.40.470.10	$\"[9-222]T$	no description

","BeTs to 15 clades of COG0692COG name: Uracil DNA glycosylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0692 is ------y--drlb-efghsnu--itwNumber of proteins in this genome belonging to this COG is 1","***** IPB003250 (Poxvirus uracil-DNA glycosylase) with a combined E-value of 2.9e-86. IPB003250A 57-79 IPB003250B 91-100 IPB003250C 113-146 IPB003250D 152-170 IPB003250E 189-222***** IPB003249 (Uracil-DNA glycosylase, not poxvirus) with a combined E-value of 4.7e-67. IPB003249B 61-100 IPB003249C 112-153 IPB003249D 164-209***** IPB005122 (Uracil-DNA glycosylase superfamily) with a combined E-value of 2.3e-27. IPB005122A 62-72 IPB005122B 118-146 IPB005122C 163-175 IPB005122D 189-199","","","-59% similar to PDB:2BOO THE CRYSTAL STRUCTURE OF URACIL-DNA N-GLYCOSYLASE (UNG) FROM DEINOCOCCUS RADIODURANS. (E_value = 9.8E_43);-56% similar to PDB:1FLZ URACIL DNA GLYCOSYLASE WITH UAAP (E_value = 5.0E_39);-56% similar to PDB:2EUG CRYSTAL STRUCTURE OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE AND ITS COMPLEXES WITH URACIL AND GLYCEROL: STRUCTURE AND GLYCOSYLASE MECHANISM REVISITED (E_value = 5.0E_39);-56% similar to PDB:3EUG CRYSTAL STRUCTURE OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE AND ITS COMPLEXES WITH URACIL AND GLYCEROL: STRUCTURE AND GLYCOSYLASE MECHANISM REVISITED (E_value = 5.0E_39);-58% similar to PDB:1EUI ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN (E_value = 1.9E_38);","Residues 54 to 213 (E_value = 2.2e-58) place ANA_1971 in the UDG family which is described as Uracil DNA glycosylase superfamily.","","glycosylase (UDG) (UDG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1972","2140134","2139469","666","10.09","7.11","23652","ATGACTGGTCTGGCTGGCGTGCGGACATGGGGCCGTGTCTACCAGATGGGACCTGGCCGCGTTCTGAGCGGGGCGGCCCGGTCGTTGGCGGCCCGGTCTGGTGGAGGGGCGCGGCAGGATGAGGAGACGACATGCGGGTGGAGAGTTGTCCCCGTAGCCCTCCAAGCCGGGCGCCGTTACGTTGCCGTCATGATTATCTGGCGTGGCTGGGGCATTCTCAGCGTCTTCATCACTTTACTGGTGGCGGGCATTGTGGGGTCGACCTTCCAAGCGTTTCTTGGCAGCGGCAACACGTCGGTCTTTTTCGGGTATGGACTCGGGCTCATCCTGGCTGGGGTGGCCAACTACTTCTTCGGGCGTCAGGTGAATGAGCTTGCTCCCGCCAGGAAGATCGAGGCGTTCAAGGACCAGATGCGCCACGAGATGTGGGACCGCGTGGCTCACGGGTCCTTTCAGGTGGGGCCGGGAGCGCCTCCGCCGGCAAACCGCGACGAGGCGCATCAGCAGGTCGAGCACGTTGTCGAGCAGGCGAGTGCGAACGCTGCGAAGGGTCTCCGTAACATCCACTCCGTTTTCTTCATCCCGGTCCAGTGGATCGGAGCGGTCGAGGGCGTGCTGGGAGTGGTCCTGATCGTGCTGTCGGTCGTGATGTCCTTCTCCGGCTGA","MTGLAGVRTWGRVYQMGPGRVLSGAARSLAARSGGGARQDEETTCGWRVVPVALQAGRRYVAVMIIWRGWGILSVFITLLVAGIVGSTFQAFLGSGNTSVFFGYGLGLILAGVANYFFGRQVNELAPARKIEAFKDQMRHEMWDRVAHGSFQVGPGAPPPANRDEAHQQVEHVVEQASANAAKGLRNIHSVFFIPVQWIGAVEGVLGVVLIVLSVVMSFSG$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-86]?$	signal-peptide
tmhmm	$\"[66-95]?$ $\"[101-119]?$ $\"[196-216]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:1CT9 CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI (E_value = );-50% similar to PDB:1AVF ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH (E_value = );-50% similar to PDB:1HTR CRYSTAL AND MOLECULAR STRUCTURES OF HUMAN PROGASTRICSIN AT 1.62 ANGSTROMS RESOLUTION (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1973","2140260","2140784","525","5.75","-3.94","17892","CTGGACCAGATCGCCCAGTTCCTGCCGCGCACCGGCATCGGCACCGACGTGCACGCCTTCGCCGCCCCCGACTCGGGCACCCCCATGCACCTGGCCTGCCTGGAGTGGCCCGGCGAGGTGGGCCTTGCCGGTCACTCCGACGGCGACGTCGTCGCCCACGCCTGCTGCGACGCCCTGTTCTCGGCCGCCGGACTGGGCGACCTGGGCTCGAACTTCGGCACCGCCGAGCCCCAGTGGAAGGGGGCCTCCGGGACTGCGCTCCTGAGCGAGGCCGCCCGCCGGGTGCGCCAGGCCGGCTTCGAGATCGGCAACATCGCCGTCCAGCTCGTGGGTGAGCGCCCGCGCGTGGCCGCCCGCTCCGCCGAGGCCTCCCGGGCGCTGTCCGAGGCCGCCTCCGCCCGGGTCTCCTTCTCCGCCACCACCACTGACCACCTGGGTTTCCTGGGCCGCACTGAGGGCCTGCTCGCCGTCGCCACCGCCCTGGTCTACCCGGTCCCCGACGCCGTCCGCAGGTTCGTACCTTAG","LDQIAQFLPRTGIGTDVHAFAAPDSGTPMHLACLEWPGEVGLAGHSDGDVVAHACCDALFSAAGLGDLGSNFGTAEPQWKGASGTALLSEAARRVRQAGFEIGNIAVQLVGERPRVAARSAEASRALSEAASARVSFSATTTDHLGFLGRTEGLLAVATALVYPVPDAVRRFVP$","2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","Cytoplasm","2-C-methyl-D-erythritol 2,4-cyclodiphosphatesynthase(MECPS) (MECDP-synthase)","2C-methyl-D-erythritol 2;4-cyclodiphosphate synthase ","2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","","","","","

InterPro
IPR003526
Domain

2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, core
G3DSA:3.30.1330.50	$\"[9-160]T$	no description
PF02542	$\"[9-165]T$	YgbB
TIGR00151	$\"[10-164]T$	ispF: 2C-methyl-D-erythritol 2,4-cyclodipho
PS01350	$\"[46-61]?$	ISPF

InterPro
IPR010925
Family

2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
PIRSF005911	$\"[9-166]T$	2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

","BeTs to 17 clades of COG0245COG name: Putative enzyme of deoxyxylulose pathway (terpenoid biosynthesis), YgbB familyFunctional Class: RThe phylogenetic pattern of COG0245 is -----qvcebrhujgp-lin-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-48% similar to PDB:1GX1 STRUCTURE OF 2C-METHYL-D-ERYTHRITOL-2,4-CYCLODIPHOSPHATE SYNTHASE (E_value = 2.3E_20);-48% similar to PDB:1H47 STRUCTURES OF MECP SYNTHASE IN COMPLEX WITH (I) CMP AND (II) CMP AND PRODUCT (E_value = 2.3E_20);-48% similar to PDB:1H48 THE STRUCTURE OF 2C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE IN COMPLEX WITH CMP AND PRODUCT (E_value = 2.3E_20);-48% similar to PDB:1JY8 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (IspF) (E_value = 2.3E_20);-48% similar to PDB:1KNJ Co-Crystal Structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate Synthase (ispF) from E. coli Involved in Mevalonate-Independent Isoprenoid Biosynthesis, Complexed with CMP/MECDP/Mn2+ (E_value = 2.3E_20);","Residues 60 to 216 (E_value = 3e-49) place ANA_1973 in the YgbB family which is described as YgbB family.","","2,4-cyclodiphosphate synthase(MECPS) (MECDP-synthase)","","1","","","Tue Aug 7 17:41:54 2007","","Tue Aug 7 17:41:54 2007","","","Tue Aug 7 17:41:54 2007","Tue Aug 7 17:41:54 2007","Tue Aug 7 17:41:54 2007","","","","","","Tue Aug 7 17:41:54 2007","Tue Aug 7 17:41:54 2007","","","Tue Aug 7 17:41:54 2007","Tue Aug 7 17:41:54 2007","","","","","yes","","" "ANA_1974","2140905","2142494","1590","5.33","-19.17","57159","GTGCCTGTGAGCATCACCCCCACTGAGTCCCCTGAGTCCGCGGGCCCCGCCGACTCCGCCGCCCGAGCGGGCGAGCCAGCCCTGCGCCTGTACGACTCCGCCGCCCGCGCGATCGTGCCGCTGGCCCCCACGGCCACCCCCGGCCTGGTGACGATCTACCTGTGTGGTGCCACCGTCCAGGGCTCGCCCCATATCGGCCACATGCGCAGTGGCATCGCCTTCGACGTCCTGCGCCGCTGGCTCGAGCGCGGCGGCCAGGAGGTCCGCCTCATCCGCAACGTCACCGACATTGACGACAAGATCCTCAGTAAGTCGGCCGCCGCCGAGCCGCCGGTGCCGTGGTGGGCCTGGGCCCAGCGCTTCGAGCGGGAGTTCGACGCCGCCTACCGCGCCCTGGGCGTGAACGCCCCCACCTACGAGCCGCGCGCCACCGGCCACATCCCCGAGATGATCGATCTGGTCCAGCGCCTGCTGGACGCCGGCCACGCCTACGTCGGAGAGTCCGGCAACGTCTACTACGACGTGCGCTCCCTGCCCGGCTACGGCTCCCTCACCAACCAGCGACTGGAGGACCTGGCCACCACCGAGGACGAGTCCCAGCTCGATGACGACGTCGAGGCCGACAAGCGCGACCCACGCGACTTCGCCCTGTGGAAGGCCGCCAAGCCCACCGAGCCGGCCGACGCCGCCTGGGACGCCCCCTGGGGCCGGGGCCGGCCCGGCTGGCACCTGGAGTGCTCGGCCATGTCGCGCCGCTACCTGGGCGAGACCTTCGACATCCACGGCGGCGGCATCGACCTGCGTTTCCCGCACCACGAGAACGAGCAGGCCCAGTCCCACGGCGCCGGCTGGGGCTTCGCGCGCCACTGGGTCCACAACGCCTGGGTGACCATCAAGGGCGAGAAGATGAGCAAGTCGCTGGGCAACTCCCTGGTGGTGGCCGAGCTGCTCAAACGCTACGACGCCGCCGTGCTGCGCCTGGCCCTGGGCACCGTCCACCACCGCTCCACCGTGGAGTTCTCCGAGGAGACCCTGGCCGACGCCGCCGCCCTGTGGGAGCGCCTGTCGGGCGCGATCCTGCGGGCCTACGAGTTCTGCGACGGCGAGGGCGCCAACCCCGTCGACGCCCCCGCCGAGCAGGTGCGCGCCCGGGCCCTGCCGGCCGAGTTCACCGCCGCCATGGATGAGGACCTCAACCTGGCCGGCGCCATGGCGGTCGTCCACGCCACCCTCAAGGCCCTCAACGTGGCCCTCACCCAGGCCGCCCCGAGCGGCGGCCAGGGGGCCGACGACGACCTGCGCGCCTCGGTGACCGGCCTCGCCCTGGACCTGCGCTCCCAGCTCGACGTCCTGGGCTTGGACCCGCTGGCCGAGCCCTGGCGCGCCCGGGTGCTCGACGGCGCCGGCTCCTCCCAGGGCGGCGCCGCCATGGAGGCCCTCGACCGTCTCATCCGCCACGACCTCGACGAGCGGGCCCAGGCCCGTGCCGCCAAGGACTGGGCGCGCGCCGACGCCCTGCGCGACAAGCTGACCGGGGCCGGCGTCGTCGTCGAGGACTCCCCCTCGGGCGCCCGCTGGCACCTGGCCTGA","VPVSITPTESPESAGPADSAARAGEPALRLYDSAARAIVPLAPTATPGLVTIYLCGATVQGSPHIGHMRSGIAFDVLRRWLERGGQEVRLIRNVTDIDDKILSKSAAAEPPVPWWAWAQRFEREFDAAYRALGVNAPTYEPRATGHIPEMIDLVQRLLDAGHAYVGESGNVYYDVRSLPGYGSLTNQRLEDLATTEDESQLDDDVEADKRDPRDFALWKAAKPTEPADAAWDAPWGRGRPGWHLECSAMSRRYLGETFDIHGGGIDLRFPHHENEQAQSHGAGWGFARHWVHNAWVTIKGEKMSKSLGNSLVVAELLKRYDAAVLRLALGTVHHRSTVEFSEETLADAAALWERLSGAILRAYEFCDGEGANPVDAPAEQVRARALPAEFTAAMDEDLNLAGAMAVVHATLKALNVALTQAAPSGGQGADDDLRASVTGLALDLRSQLDVLGLDPLAEPWRARVLDGAGSSQGGAAMEALDRLIRHDLDERAQARAAKDWARADALRDKLTGAGVVVEDSPSGARWHLA$","Cysteinyl-tRNA synthetase","Cytoplasm","cysteinyl-tRNA synthetase","cysteinyl-tRNA synthetase ","cysteinyl-tRNA synthetase","","Wolf Y.I., Aravind L., Grishin N.V., Koonin E.V. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999. 9(8):689-710. PMID: 10447505","","","

InterPro
IPR002308
Family

Cysteinyl-tRNA synthetase, class Ia
TIGR00435	$\"[28-529]T$	cysS: cysteinyl-tRNA synthetase

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[46-345]T$	no description

InterPro
IPR015273
Domain

Cysteinyl-tRNA synthetase, class Ia, DALR
PF09190	$\"[389-461]T$	DALR_2

InterPro
IPR015803
Domain

Cysteinyl-tRNA synthetase, class Ia, N-terminal
PR00983	$\"[52-63]T$ $\"[88-97]T$ $\"[228-246]T$ $\"[259-280]T$	TRNASYNTHCYS
PF01406	$\"[41-350]T$	tRNA-synt_1e

InterPro
IPR015804
Domain

Cysteinyl-tRNA synthetase, class Ia, C-terminal
PTHR10890	$\"[227-420]T$	CYSTEINYL-TRNA SYNTHETASE

","BeTs to 24 clades of COG0215COG name: Cysteinyl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0215 is ao-pkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002308 (Cysteinyl-tRNA synthetase signature) with a combined E-value of 1.2e-32. IPB002308A 52-63 IPB002308B 88-97 IPB002308C 228-246 IPB002308D 259-280***** IPB013155 (tRNA synthetase, valyl/leucyl, anticodon-binding) with a combined E-value of 1.1e-10. IPB013155B 56-98 IPB013155H 300-326","","","-52% similar to PDB:1LI5 Crystal Structure of Cysteinyl-tRNA Synthetase (E_value = 8.9E_79);-52% similar to PDB:1LI7 Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound (E_value = 8.9E_79);-52% similar to PDB:1U0B Crystal structure of cysteinyl-tRNA synthetase binary complex with tRNACys (E_value = 8.9E_79);","Residues 41 to 350 (E_value = 9.1e-160) place ANA_1974 in the tRNA-synt_1e family which is described as tRNA synthetases class I (C) catalytic domain.Residues 59 to 363 (E_value = 1.6e-05) place ANA_1974 in the tRNA-synt_1g family which is described as tRNA synthetases class I (M).Residues 389 to 461 (E_value = 2.1e-05) place ANA_1974 in the DALR_2 family which is described as DALR domain.","","synthetase (cysS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1976","2142570","2143568","999","9.98","14.85","34944","ATGCCCGGCAACGAGCAGTACCCCGGCGCCAAGCGCCGCCCCGGCTCGAAGAAGGGCCCCACGAAGGGCTCGGGCGGCCAGCGCCGCAAGGGCCTGGAGGGCAAGGGCCCCACCCCGCGCGCGGAGAACCGCGTCGGCCACCCCAAGGCCCGGGCGAAGGCCCGCGCCGAGTCCCGGGCCGCCCAGCCCACTCGCGCCAAGCAGTTGGAGAAGATCAAGCGCCGCTTCGACGTGCCCGAGGGCCACGAGATCCTGTGCGGGCGCAACGCCGTGGCCGAGGCCGCCTACGCCTCGGTGCCCATCACCCGGGTCTTCATGGCGGTCTCCGCCCAGTCCGACGAACGCCTGGGCGCCGTGGTGCGCCGCGCCGCCCTGCTGGGCGCCCCGGTGCTGGAGACCACCAAGCTGGACCTGGACGCCCTGACCGACTCCGCCACCCACCAGGGCGTCGCCATCGAGGTACCCGCCTACGAGTACACCACCGCCCGCGACCTGCTGGAGCGCGCCCGCGCCCTGGGCCGCACGCCGCTGCTCGTGGCCCTGGACCAGGTGACCGACCCCCACAACCTGGGCGCGGTCCTGCGCAGCGCCGGGGCCTTCGGGGCCGACGGCGTCATCATCCCCGAGCGCCGCTCGGTGGGCGTCAACGCCACCGTGTGGAAGGTGTCGGCCGGTGCCGCCGCCCGAGTGCGCGTGGCCCGCGAGACGAACCTCGTGCGCTCCCTGGAGCAGCTGAAGAAGGAGGGCTGCTTCGTCGTCGGCCTGGACGGCTCGGGCAGCACCGCCGTCGAGGACCTCACCCTGGCCGACTCACCCCTGGTGCTGGTCACCGGCGCGGAGGGCGCGGGCCTGTCCCGCCTGGTGCGCGAGACCTGCGACGTGCTGGCCTCGGTGCCGATCAGCCGCAGCGTGGAGTCCCTCAACGCGGCCGTGGCCACGGGGATCAGCCTCTACGAGGTCGACCGCCTGCGGCGTCGGGCCGCCGGCGCCGGCAGCTGA","MPGNEQYPGAKRRPGSKKGPTKGSGGQRRKGLEGKGPTPRAENRVGHPKARAKARAESRAAQPTRAKQLEKIKRRFDVPEGHEILCGRNAVAEAAYASVPITRVFMAVSAQSDERLGAVVRRAALLGAPVLETTKLDLDALTDSATHQGVAIEVPAYEYTTARDLLERARALGRTPLLVALDQVTDPHNLGAVLRSAGAFGADGVIIPERRSVGVNATVWKVSAGAAARVRVARETNLVRSLEQLKKEGCFVVGLDGSGSTAVEDLTLADSPLVLVTGAEGAGLSRLVRETCDVLASVPISRSVESLNAAVATGISLYEVDRLRRRAAGAGS$","tRNA/rRNA methyltransferase","Cytoplasm","rRNA methylases","putative tRNA/rRNA methyltransferase ","RNA methyltransferase, TrmH family, group 3","","Sirum-Connolly K., Mason T.L. Functional requirement of a site-specific ribose methylation in ribosomal RNA. Science 1993. 262(5141):1886-1889. PMID: 8266080Yu L., Petros A.M., Schnuchel A., Zhong P., Severin J.M., Walter K., Holzman T.F., Fesik S.W. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nat. Struct. Biol. 1997. 4(6):483-489. PMID: 9187657","","","

InterPro
IPR001537
Domain

tRNA/rRNA methyltransferase, SpoU
PD001243	$\"[176-324]T$	Q9L0Q5_STRCO_Q9L0Q5;
PF00588	$\"[176-318]T$	SpoU_methylase

InterPro
IPR004441
Family

RNA methyltransferase TrmH, group 3
TIGR00186	$\"[81-324]T$	rRNA_methyl_3: RNA methyltransferase, TrmH

InterPro
IPR013123
Domain

RNA 2-O ribose methyltransferase, substrate binding
PF08032	$\"[84-160]T$	SpoU_sub_bind

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.30	$\"[71-158]T$	no description
G3DSA:3.40.1280.10	$\"[159-325]T$	no description
PTHR12029	$\"[129-327]T$	RNA METHYLTRANSFERASE
PTHR12029:SF7	$\"[129-327]T$	RRNA METHYLASE

noIPR
unintegrated

unintegrated
signalp	$\"[1-10]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[123-145]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[131-151]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","Wed Aug 15 17:12:36 2007","","Wed Aug 15 17:12:36 2007","","","Wed Aug 15 17:12:36 2007","Wed Aug 15 17:12:36 2007","Wed Aug 15 17:12:36 2007","Wed Aug 15 17:16:20 2007","","Wed Aug 15 17:19:17 2007","","","Wed Aug 15 17:12:36 2007","","","","Wed Aug 15 17:12:36 2007","Wed Aug 15 17:12:36 2007","","","","","yes","","" "ANA_1981","2148570","2147326","1245","6.82","-0.86","44800","ATGAGCCCGTCCGCGGTCGAACGGCTGACCGCGGCACGTGTCAATGCGGACACGCATCGGCACCTTTCACGACGGATCGTCCGGCACGTACCTGCCGGTGAAGGGATAGCACTACTCATGGCAACTGTGACTTTCGAGAACGCCACACGTATTTACCCGGGCAATGACCGCCCCAGTGTTGACGCTCTCAACCTCGAGATCGCCGATGGCGAGTTCCTCGTGCTCGTTGGCCCCTCCGGCTGCGGTAAGTCCACCTCCCTGCGCATGCTTGCGGGCCTGGAGGACGTCAACGCCGGTCGCATCCTCATCGGTGACCGCGACGTCACCGACGTTCAGCCCAAGGACCGTGACATCGCCATGGTCTTCCAGAACTACGCGCTCTACCCGCACATGACCGTGCACGACAACATGGGCTTCGCCCTCAAGATCGCCGGCACCCCCAAGGCCGAGATCGACAAGCGCGTGCGCGAGGCCGCCAAGATCCTCGGCCTGACCGAGTACCTGGACCGCAAGCCCAAGGCCCTCTCCGGTGGTCAGCGTCAGCGTGTGGCCATGGGCCGCGCCATCGTACGTAAGCCCAAGGTCTTCCTCATGGACGAGCCGCTGTCCAACCTGGACGCCAAGCTCCGTGTGCAGACCCGCACCCAGATCGCCTCGCTCCAGCGCTCGCTGGGCGTCACCACGGTCTACGTCACCCACGACCAGACCGAGGCCCTCACCATGGGTGACCGCATCGCGGTCCTCAAGGACGGCGTGCTCCAGCAGGTCGGCACCCCGCGCGAGATGTACGACCACCCCGCCAACGAGTTCGTCGCCGGCTTCATCGGCTCGCCGGCCATGAACCTGGGGCAGTTCACGGTCAAGGGGGACGTCGCCACCGTCGGCGCCGCCAAGATCCAGCTGTCCAAGGCGACCCTGGACGCCATCACTCCCGAGGACGGCGGCAAGGTGACCATCGGGTTCCGCCCCGAGTCGCTCGACGTCGTCTCCGCCCAGGACGAGCACTCCATCCCGGTGCGCCTGTCCTTCGTGGAGGAGCTGGGCTCCGACGCCTACATCTACGGTGAGCTCGTCGGCGCCGAGGAGTCCGAGGCCAAGCTCGGCTCCGGTGAGGACTCCAGCCAGATCATCGTGCGCGTGCCTCCGCGCACCGCCCCCGAGCCGGGTGAGACCGTCTACGTGCGGATCCGCCCCGGTCAGGAGCACATCTTCTCCGCCTCCACCGGCAAGCGTCTGCCCGCCTGA","MSPSAVERLTAARVNADTHRHLSRRIVRHVPAGEGIALLMATVTFENATRIYPGNDRPSVDALNLEIADGEFLVLVGPSGCGKSTSLRMLAGLEDVNAGRILIGDRDVTDVQPKDRDIAMVFQNYALYPHMTVHDNMGFALKIAGTPKAEIDKRVREAAKILGLTEYLDRKPKALSGGQRQRVAMGRAIVRKPKVFLMDEPLSNLDAKLRVQTRTQIASLQRSLGVTTVYVTHDQTEALTMGDRIAVLKDGVLQQVGTPREMYDHPANEFVAGFIGSPAMNLGQFTVKGDVATVGAAKIQLSKATLDAITPEDGGKVTIGFRPESLDVVSAQDEHSIPVRLSFVEELGSDAYIYGELVGAEESEAKLGSGEDSSQIIVRVPPRTAPEPGETVYVRIRPGQEHIFSASTGKRLPA$","ABC-type multiple sugar transport system, ATPase component","Cytoplasm, Membrane","ABC-type transporter, ATPase component","K02023 multiple sugar transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[175-217]T$	Q97E78_CLOAB_Q97E78;
PF00005	$\"[70-251]T$	ABC_tran
PS50893	$\"[43-275]T$	ABC_TRANSPORTER_2
PS00211	$\"[175-189]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[69-252]T$	AAA

InterPro
IPR013611
Domain

Transport-associated OB
PF08402	$\"[319-404]T$	TOBE_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[40-278]T$	no description
PTHR19222	$\"[43-282]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF42	$\"[43-282]T$	SUGAR ABC TRANSPORTER

","BeTs to 15 clades of COG3839COG name: ABC-type sugar transport systems, ATPase componentsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG3839 is -o-pkz-qvdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB005116 (TOBE domain) with a combined E-value of 4.9e-63. IPB005116A 77-93 IPB005116B 116-133 IPB005116C 175-188 IPB005116D 195-214 IPB005116E 229-242***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.8e-33. IPB013563A 59-93 IPB013563B 118-131 IPB013563C 172-199 IPB013563D 227-279***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1.8e-32. IPB005074C 59-106 IPB005074D 163-206***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.7e-18. IPB010509B 70-95 IPB010509D 170-214","","","-65% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 2.4E_92);-67% similar to PDB:1G29 MALK (E_value = 3.1E_92);-63% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 2.1E_85);-63% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 2.1E_85);-62% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 2.5E_78);","Residues 70 to 251 (E_value = 2.6e-61) place ANA_1981 in the ABC_tran family which is described as ABC transporter.Residues 319 to 404 (E_value = 1.1e-05) place ANA_1981 in the TOBE_2 family which is described as TOBE domain.Residues 331 to 403 (E_value = 0.00013) place ANA_1981 in the TOBE family which is described as TOBE domain.","","transporter, ATPase component","","1","","","","","","","","","","","Tue Aug 14 16:44:24 2007","","Tue Aug 14 16:44:24 2007","","","Tue Aug 14 16:44:24 2007","Tue Aug 14 16:44:24 2007","","","Tue Aug 14 16:44:24 2007","Tue Aug 14 16:44:24 2007","","","","","yes","","" "ANA_1982","2148637","2150859","2223","7.05","0.35","78132","ATGGCTGCCGGTGGAGACCTCCCCATCCCCGTCGTCGGACACCGCCCGGCCCGATACCCACAATGCGGCTCTATCACTGGCTTTACTCCCGCGACATGGCCCACAGTCGGGCGAAGAGCCCCACAGCGTCGGGGCGCCCACGAGCGAATCCGGCCCGGTACTGTGGGGGCCATGACGCAGAACTTCGACGCGCACCCGGGCGAGCCGGTCACCCTGAGCAAGCTGCGCGCCGGCACCTCAGTGGGGGGATACCGACTTCTGCGTCGCCTGGGCGCCGGAGGCATGGGCGTGGTGTGGGAGGCCACCGATGAGGGTGGGCGCCACGTGGCCATGAAGATCCTCCACCCGCAGATCGCCGCGGACCCCACCGCTCGGCGCCGTCTGGACCGGGAGGCCAGCGTCCTGGCCCGGGTGAGGGACACGCGCGTGGCGCGCATCCTGGACATCGAGACCGGGGACGGCTCCCAGGGCATCACCTTCGTCATCACCGAGCTCATCGAGGGCCCCACCCTGCAGCACGAGGTGGAGCACGAGGGCGTCTACGACCTGACCACTGATGCCCGCGACCTGGCCGACCTGGCCCACGGGCTGGTCGATTCCCTGCGCGCGGTGCACGCCGCCGGCGTCATCCACCGCGACCTCAAGCCCTCCAACGTCATGCTCGGCGCACAGGGGCCGGTTCTCATCGACTTCGGTATCGCCCAGGTGGCCGACGACGTCCGGCTCACGCAGACCGGCCAGGTCACGGGTACACCGGGGTTCATCCCCCCGGAGATGCTCGACGGCGGGGAGCCGAATGCCGACGTCGACTGGTACGCCTGCGCGGGCGTGCTCCTGTTCACCGTCACCGGACTGGCGCCCTTCGGTTCGGGCGCCTGGCAGGTGGTCTTCCGGCGCGTCTACGCGGGCACCCCGGAACTGGGCAACCTGGAGGAGGAGAACCCGGCGCTGGCTCGGGCGTTCACGGCGGCTCTCGCCCCTGAGGCGGAGAACCGTCTGAGCCCGGACGGCCTGCTGGAGGTGCTCGATGAGATCGCCGAGGGCGGGACCGGGCAGGAGGCGGTCAACCGGCTCCTGGGGCCCGAGGACGAGGAGCCGGAGTCCAGTGAGCTGGAGCGGACCACCAGCACTTTCGTTCCTGGCTACGGCTCGACCCCGGGCTCGCCTCGCGATGCTCGCAGTGCGACCTCGGCGTCCCCGGCCTCATACGGCAGTCCCGTCTCCGCGGCCTCCGGTGCGGAGGGCGGATACGGTTACTCGGCGCCGTCGGCTCCCTCCGGCGCTTCCACCCAGCCCCCACCGGCCATCCCGCCGCGCCAGTGGTACCAGAACAGTTCGGCCATGCCCTCACGGGGAGCGCAGTCGATGCAGTACGGCGTGGGCGCTCCTGCGCCTGCAGCCTCCTCAGGGGCGTACCCGCGGCCGGCGCTGTCGGGGCAGGTGCCGATGTTCCCCTACTCCGGCCAGCATCCGACGGCGTATCAGCCCGGCTACTCCCAGGCCGTCGCTGCTCCGACGGCTGCGCCGTCGGCGGGAGCGATGACAGGGCCGATGGCAGCCGGCGCCCCCGGGGCACAGGTACGCCGGTTCGGCTCCCCCAGACGTCCAGGGGAGCTGCCCCAGTGGGCGAAGGAGCCGACGCGTCACCCGATGGCAATGCTGGCCCTGTTGTTCATGCTGTCCTCGATCGGGATGTTTAGACCGGCATGGATGGCGATCATTGGGGCGATTCTGTCAGCAGTGGCCGGCACTGTGGGCCGGGCCCAGGACGCTCGGCGGTGGAACCGCCTCCAGCGGGGCGGCACCTCGCCGTCGGACAACTCCCGCATGTGGGCGATGACCCCGTGGTATCTGGTGCGTTCGGCGATATCTGCCGGCTTCGCTTTTCTTCTGGCTGCGGGAACGTCGTTCCTCTTCCTGAGGACCATTTTCTGGTCAGATTTCGGGGAGAAAGACTCCGTGGCTTTTGGATCGATCCCGCTACCTGTCCGCATCTACACCATCTTTTTCTTGGAGGTCGCCCTACACCTTCTCGTCCTGTGGCTGGTGCCGTGGGGTACGGCGACTCGACGCGGTGGCGCACATATCCTCAATTCCTTCATCTCCAGTGACAACGGTAGAAGGAACCTGGTCGTGGCCATGTTGGGCATTGGAGCCGTGATATTGATTCTGTCCTTTGCCGGGCTGATGCCGATTCCGAATTTGACCCCGTACGGGAACTGA","MAAGGDLPIPVVGHRPARYPQCGSITGFTPATWPTVGRRAPQRRGAHERIRPGTVGAMTQNFDAHPGEPVTLSKLRAGTSVGGYRLLRRLGAGGMGVVWEATDEGGRHVAMKILHPQIAADPTARRRLDREASVLARVRDTRVARILDIETGDGSQGITFVITELIEGPTLQHEVEHEGVYDLTTDARDLADLAHGLVDSLRAVHAAGVIHRDLKPSNVMLGAQGPVLIDFGIAQVADDVRLTQTGQVTGTPGFIPPEMLDGGEPNADVDWYACAGVLLFTVTGLAPFGSGAWQVVFRRVYAGTPELGNLEEENPALARAFTAALAPEAENRLSPDGLLEVLDEIAEGGTGQEAVNRLLGPEDEEPESSELERTTSTFVPGYGSTPGSPRDARSATSASPASYGSPVSAASGAEGGYGYSAPSAPSGASTQPPPAIPPRQWYQNSSAMPSRGAQSMQYGVGAPAPAASSGAYPRPALSGQVPMFPYSGQHPTAYQPGYSQAVAAPTAAPSAGAMTGPMAAGAPGAQVRRFGSPRRPGELPQWAKEPTRHPMAMLALLFMLSSIGMFRPAWMAIIGAILSAVAGTVGRAQDARRWNRLQRGGTSPSDNSRMWAMTPWYLVRSAISAGFAFLLAAGTSFLFLRTIFWSDFGEKDSVAFGSIPLPVRIYTIFFLEVALHLLVLWLVPWGTATRRGGAHILNSFISSDNGRRNLVVAMLGIGAVILILSFAGLMPIPNLTPYGN$","Serine/threonine protein kinase","Membrane, Extracellular","serine/threonine protein kinase homolog","tyrosine protein kinase:serine/threonine protein kinase","protein kinase","","Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995. 9(8):576-596. PMID: 7768349Hunter T. Protein kinase classification. Meth. Enzymol. 1991. 200:3-37. PMID: 1835513Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth. Enzymol. 1991. 200:38-62. PMID: 1956325Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988. 241(4861):42-51. PMID: 3291115Knighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991. 253(5018):407-414. PMID: 1862342","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[99-273]T$	Q8G6I0_BIFLO_Q8G6I0;
PF00069	$\"[84-345]T$	Pkinase
PS50011	$\"[84-346]T$	PROTEIN_KINASE_DOM
PS00107	$\"[90-112]?$	PROTEIN_KINASE_ATP

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[209-221]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[167-339]T$	no description
G3DSA:3.30.200.20	$\"[76-165]T$	no description
PTHR22986	$\"[84-340]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES
tmhmm	$\"[566-586]?$ $\"[617-639]?$ $\"[665-685]?$ $\"[710-730]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[87-107]?$ $\"[122-144]?$ $\"[163-183]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1985","2152147","2151569","579","5.99","-5.12","22214","ATGTCAATTACGCAAGGTAACCAGGGTAATTCGGTTATTCTGAAATTTGAGGGGTTGTTGCGTGACTGGTTAGTAGATGAAGGCGGAGTCCGGGTCGATATCGATTATCATGCGATCCACCGGACGGGCCGTGTGAAGGTGTGGCTGATGCGCGGAGAAGAGCGAAAGTCTGTTCATCTCCCTCGTGAGGTGAGTTTCGCAATGCATGATATTCGTGGTTCTCAGGCGGATCCGCATCGGGGTGCGTGGTTGTACTCGCATTTTTGGATGGAGGCCACCGATGGGGTGCTGCATCAGGAGTGCGACTGGATGCGTGAGCCAGTGATTGATGATGATGAGCCAGTGATGGATGGAGATGCTGCTCTTGAGCTGGACTACTATCCGCGGGATCCGCAGTGGATTCCGGAATGGATGGCAACCAAGGCTGCGGCTCATCAGAAGGTGAGGGAAGCTCGGGAACGCCGTCGCCAGCGAGACCGTGAGCGGCGGGCTAAGAAGAAGGCCGAGGCTGCCCAGGCTGAAGGCAATGGCGATGATGAGCCGAGTTCGGGTAGAGTCGGCCGCTCTGATATTGAGTGA","MSITQGNQGNSVILKFEGLLRDWLVDEGGVRVDIDYHAIHRTGRVKVWLMRGEERKSVHLPREVSFAMHDIRGSQADPHRGAWLYSHFWMEATDGVLHQECDWMREPVIDDDEPVMDGDAALELDYYPRDPQWIPEWMATKAAAHQKVREARERRRQRDRERRAKKKAEAAQAEGNGDDEPSSGRVGRSDIE$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1986","2155194","2152147","3048","5.18","-51.27","109763","ATGAATCCGGTTGAGACGAATACCGACGACTTGGCTGACGATCTGGAAAAGATTGCGGGTTATGTTTCGACCTTTGCCGGCACAGCAAGGGGGATTAAGTCCGACGCACAGACCTTGAAGAAAGACGGCCAAGCATTCAAGGCAAAAATTGCAAAAAAGCCGGATTGGCAATACGATCAGGAGCTCGTTAACGAAAACACGCGTCTCGTGAATCGGGCAAGCGCGCTTCAAATTCGTTTATGGAACGCTGAAAGAGAGTGCGTTAACAATATTCGGGCACTGGACTCCCTACCTCCTTATCATGCTGACCAAAAAAGCGATAATGACAAGTTATTTTATGGGTTGAGTTCCATTCCGCAGGACGCCAACAAGCCTTGGGGAAAGTCTGTTCCCCGGCAGGACAAGTGCCCCAAGAAAGCCGTAGTCTCAGTTAAGCGGTTTGTGTGGGACGGATTTTTATATGATGGGCTGGGGGGAGACATAAGTGGGATTGCCGATATTTTTAGCATCGACGCCTGGAAGGGGCTGGGTGGCCTTATCGGCATGAGTGACGATGAGAATGGTCACTATTCACTCCATGATAATTGGAAAGATGTTGCTTGGAACACTTGGAAAGGGACGTTTAAAGAGTTGTCTCACTGGGACATGTGGGGCACTGATCCGGCGCGAGCTCTCGGGGCAACTGCCTACGACGTAGCCTCTCTTGCTACCTTCTTTATTCCATATGTCGGTCCTGCTGTTGGAGCGGTAGTAGCGGGGAGTAAAATCGCGAAGGCTGCGAAAACCGCTAAAGTGGCTCGTGCTGCGTCGAAGGCGGCGAAGGTCGCGAAGGTTGCCGGCAAAGTGGCGGACGCAGTGGATGTTCCTGGGCATATCGCTGGTGCAGCCGCTAAAGCTACGGGCAAAGTGACTGTTGCGGCTGCCAAAAAAATTTGGCCTGACTTGGACCTCGATGAGGTTTTTAAGGCATGGCGTGGTCACGGAAATAGTGATGGGGCAGACCTGGACATGGATGCGCCAGAGCTGCCGGAGCTGACAGCTGACAAGGGAGGTAAGGCGCCATCTATTCGTATGGACGACTCTGAGGTTCCTGACCTTTCGTCGAGGCCGCACTCAAGTGACGGTGATGCTAATTCAACAAGGGCTCATGACGGTGCTCGTGTGGATGTGGATGGTGACACTGGGCGTGCTGATGCCGATGGGCGTCGTGAGTCGGCCAAGGACGGTGCTGAGCCCGCTGACGGTGCGGATCGTGACCGCGCTGGCCGTGGCGCCGATGCTGATGCTGGTCGGGACCGGGCTGACCGTGACGCGTCTGCGGGGCACGAGCGCGGTGGTGACGCTGACGGACGTCGTGCGGATGCTGATGGTCACCACGATCAGGCCAAGAATGATGCTGATGCGGATAACAATGTCGACCATGATCGGACAGACCGCAATAGCGACTCGGACGGCGAGCGCGATCGCGGTATGACCGACAGCGACGCTCATGAGGGTCGCGACAGGGCGCGGCATGCCGATGGTGACACTGGGCGTGCTGATGCCGATGGGCGTCGTGAGTCGGCCAAGGACGGTGCTGAGCCCGCTGACGGTGCGGATCGTGACCGCGCTGGCCGTGGCGCCGATGCTGATGCTGGTCGGGACCGGGCTGACCGTGACGCGTCTGCGGGGCACGAGCGCGGTGGTGACGCTGACGGACGTCGTGCGGATGCTGATGGTCACCACGATCAGGCCAAGAATGATGCTGATGCGGATAACAATGTCGACCATGATCGGACAGACCGCAATAGCGACTCGGACGGCGAGCGCGATCGCGGTATGACCGACAGCGACGCTCATGAGGGTCGCGACAGGGCGCGGCATGCCGATGGTGACACTGGGCGTGCTGATGCCGATGGGCGTCGTGAGTCGGCCAAGGACGGTGCTGAGCCCGCTGACGGTGCGGATCGTGACCGCGCTGGCCGTGGCGCCGATGCTGATGCTGGTCGGGACCGGGCTGACCGTGACGGGTCTGCGGGGCACGAGCGCGGTGGTGACGCTGACGGACGTCGTGCGGATGCTGATGGTCACCACGATCAGGCCAAGAATGATGCTGATGCGGATAACAATGTCGACCATGATCGGACAGACCGCAATAGCGACTCGGACGGCGAGTCTGGTCGAGACAAGGGCAATGGTGATGGTTCTGGCGAGTTCCCCGATGGCACCAGAGAAGAGCCTCTGACGGCTGAGGAACGTCAGCGGTGGATTGATCAGGTGGACCAGGGTCGTGATCAGGATGCATTCAATGAGAAGCATCGTACGGCCGGTTCGGAGGTGAAGCCAGAGCATCAGCGGACGCTGGGGATTAATGAGCAGTTTGGTGTGGGAGAAAAGCTTGACGCTAATGCTCATTATGAGGTGACTCGTACAACGGGTGATGGCGTGAGCTATAAGTCACACTACTACACAGATGCTTCTGGCGAGGTGCGGCATGTGGAGACGAGTTCTCGGGCGATGACGGGTGCGTATAATCCTGATTTGCGTAACCCGTTGCCGAATGCGACGTATACGGTGGATGGGCGGTTCCATTACACGACTGATGGTTGGGCGCGGACGGTGCGCTTGGAGGTCGACAGGCTTGACAAGGTCGGTGAGGCGTTCCGGTCAAGGTCTAACTACATCCAGTCCAGGGTGAACAAGTACGGTAGTGAACTCGCCGCTGACATTGATCAGCGGTATGAGGGTGGGCATATTGTGGGTGACCAGTTCGGTGGGCCGCCGGAGGAGATCAATACGGTGGCGATGCTTGAGGAGGTGAACCAGACGCGTATTGGGAAGGAGTCGAACTCGTACCTGCTTCTCGAACGAAAGGTCGCAGCTAAACCAGAGAACTACAACAATCTTGTGCTAGAGTTCGAGTACCCAGAACCGGCTGATCCCACAAAGTTGACCAATACTGAACGGGTCCCAAAAAAGTTCGAGGTAAAATGGACGAATGCCGCTGGAGAGGCAGACTCGAAGCCATTTGAGAATCTTCCGCCACAGAAACGGGTAGGGGTAAACTGA","MNPVETNTDDLADDLEKIAGYVSTFAGTARGIKSDAQTLKKDGQAFKAKIAKKPDWQYDQELVNENTRLVNRASALQIRLWNAERECVNNIRALDSLPPYHADQKSDNDKLFYGLSSIPQDANKPWGKSVPRQDKCPKKAVVSVKRFVWDGFLYDGLGGDISGIADIFSIDAWKGLGGLIGMSDDENGHYSLHDNWKDVAWNTWKGTFKELSHWDMWGTDPARALGATAYDVASLATFFIPYVGPAVGAVVAGSKIAKAAKTAKVARAASKAAKVAKVAGKVADAVDVPGHIAGAAAKATGKVTVAAAKKIWPDLDLDEVFKAWRGHGNSDGADLDMDAPELPELTADKGGKAPSIRMDDSEVPDLSSRPHSSDGDANSTRAHDGARVDVDGDTGRADADGRRESAKDGAEPADGADRDRAGRGADADAGRDRADRDASAGHERGGDADGRRADADGHHDQAKNDADADNNVDHDRTDRNSDSDGERDRGMTDSDAHEGRDRARHADGDTGRADADGRRESAKDGAEPADGADRDRAGRGADADAGRDRADRDASAGHERGGDADGRRADADGHHDQAKNDADADNNVDHDRTDRNSDSDGERDRGMTDSDAHEGRDRARHADGDTGRADADGRRESAKDGAEPADGADRDRAGRGADADAGRDRADRDGSAGHERGGDADGRRADADGHHDQAKNDADADNNVDHDRTDRNSDSDGESGRDKGNGDGSGEFPDGTREEPLTAEERQRWIDQVDQGRDQDAFNEKHRTAGSEVKPEHQRTLGINEQFGVGEKLDANAHYEVTRTTGDGVSYKSHYYTDASGEVRHVETSSRAMTGAYNPDLRNPLPNATYTVDGRFHYTTDGWARTVRLEVDRLDKVGEAFRSRSNYIQSRVNKYGSELAADIDQRYEGGHIVGDQFGGPPEEINTVAMLEEVNQTRIGKESNSYLLLERKVAAKPENYNNLVLEFEYPEPADPTKLTNTERVPKKFEVKWTNAAGEADSKPFENLPPQKRVGVN$","Hypothetical protein","Extracellular, Cellwall","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1987","2156085","2155774","312","4.62","-6.06","11387","TTGGCAAATCAGACTGAAATGCGTTCCTATGACGTCAATGCGTCCCAGGAGTCGCAGAGCAATTTTGATCGCGTGGCTTCCCGCCTGGAGACGCTGATTACCCAGCGTGACAGTGACGTCAAGGCGGCGATGGCTCAGTATCAAGCGGATGGTGTCTCCGAAGAGTATCAGGTCAAGGAGACGCGGTGGAACAATGCTGCGGGAGAGGTTCGAGGAATCATTTCTACGCTGCGCGGGTCTATGCAGACGACGGACGAGGGCGCGCAGACTGCACTCCAGCAGGCCCGCCAGTCTGTTGATGACATAGCCTGA","LANQTEMRSYDVNASQESQSNFDRVASRLETLITQRDSDVKAAMAQYQADGVSEEYQVKETRWNNAAGEVRGIISTLRGSMQTTDEGAQTALQQARQSVDDIA$","Hypothetical protein","Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1988","2156475","2156137","339","4.75","-5.06","11569","ATGAAATTCGACATGGGCGCATCGACGCTGTCCACTCTGACGAAGCAAACCTCAGGCTCGAGCGATGATCTGGGAGGGCTTGTTAAGGAGCTGGTTGTTGCTGCCGAGCCGCTTGAGGGGAAGTTCAACGGGTTTGCTCGCGCTGCATTTGATGCCTTCAAGGAGCGAACTGATGATATTGCTGCCGAGTTGAACGGGGCGCTTTCCGCTATTCTTGGCGGAGTCATTGGTATGGATACTGCTTTTGTCCGGGGCGAGCAGGACATGGCTGAATCCACCAAGAGTGCGCAGTCTTCTGTCAACTTCGATGCGGCGCGTTTCGGTGCTGGGCGAGCCTGA","MKFDMGASTLSTLTKQTSGSSDDLGGLVKELVVAAEPLEGKFNGFARAAFDAFKERTDDIAAELNGALSAILGGVIGMDTAFVRGEQDMAESTKSAQSSVNFDAARFGAGRA$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1989","2157016","2158821","1806","9.97","21.31","66303","ATGTTCTTCGAGGCAGGAGCCTGGGTGGGGCACTTCTTGGGCTCCGCGCAGTCGACATCGAAGCCGGGCTTCCACCGGCATCCCTCCATTCCATCCTTGCAGCGGTTCGCCTTGGTTCGGCGGAGGATGTGGTCATCGTCTGCACACGGCGCGGTCCTGACCCCGCCCAGGGCACTCTTGCCGACCTTGAGCGCATTCCAGCTCTTGCATCCCCTTCCATACCCAACGGGCCGGTGCCTGCCAGAGGCCCCGAGACCGTATACAGTCCGTCTCCTTCCCGTCCTGACGGTCAGTACTCCGCCTCACCCACCCGCCGGCCCGACGCGGCACCGGTTCCAGCAGTGGAACGCTCAGTCAGTGGCCCAGTCCCATCCCCCGCGCCGACGCCCACCTCAACCAGACCGCCATCGTTGCCGCCGAGCATTCCGGTGCAACGGTCCCGTCCTCCTGCTCCTGCTCCCAGCCTGTCGCGAGCCCAGCAGCACACATATCCCCAGCAACGTTCAGACACAGTGGAGATCCAACCGATCCGTGCCGACTCTCCGCGTCCGGCGGATCTCGGCGACCTCCCGCCTTCACCACCGCCCCCTCCAGCACCGCCATTACAGCGGGCGCTCTGAGTACCCGCATCAATCGCCCTTAAGCAGCCACGGCTTTCGCAACAGGACACAAGGTCGCCTTACGCAGGCCTCACGTCGGAAACGAGTTCCCATGTCAGACGAACACATTCCAGAGACCAACCACCACATGTTCGATGCACAGGTAGGCACCACTGTTGCCGTGACTTACCTGCATGATCCCTGTATCGGCTGGACGGAGTACCTCCTCGACTTCATCGGTTCCGCTCTCAGCAACGAGAACGAGATCACCCCTGCGCTCGTCATCCCAGAGACCTCCCACGTCACCCCCGCCTTCGATCGCCTCACCGAGGCCACTGGCACCCCCGTCTTCGTTGAGGACAGCGGCGGGCATCGCGACTTTCGCAGCGGCATGTGGGCACCGAATCTCGCACACTTCTTCGAAGACGGGCCACACTCACGGTTCAAGGTGTCCCAGCAGTTCCTCCACCCGAACCCCGAACCCGCCCTCGTCCCAACCCTCATGCTCTCGGCTTCGATCTACCACCCCGCACGGCGCACCACGAAGCTCGGGCGGGTCACTGAGATCATCACAGAGACACTCCTGCCAGGCCCGTCCACAACGCTCTCCTGGGGACGCTACGAACCAGTGGGGGCCCCGTGGGATCGGGGACAGCTCACGGACCTCGCCCGCAAACTCATGCCCGAGGCCCACTTCAACCTCGCCGCGCACTCAGACCTGGGCACGCTCAGTGGGACGATGACAGTGGCCAGGACCAGTAGCGGCCTTGAGGAGTATGTCGAGGTTTCCATCGCCATCCCCGATCTGGCTCCCAGCCAGCAGGCCGATGCGGTCAACACGCTCCTTGACACGCTCGCTGAGCAGACCAAACCCCAGTTCGTACTCGCCGTACGCATCCAGGCCTTTGCGGACACGTCTTTGCCGACGTCCATCCGTCGGCCCCCAGTTCCACTCGCCATCCTCATCGGCGCCGCCGGTATCCGCCAGCTCGGCGTCGACGTCCATGACATCGCCAGGCAGCACGCCGGGCGCACCTACGGCAGCGGCAGACGACAGGGGCTCATAGTCCCGTTTGAGACCATGCAGGCCGACTGGAGCGCGCTGTCCTCCCTCGTGGCCACGCTCGACGGCGACGCCGGTAACATCGCCCGGGTCCTGGAGGATCCCACTGACGGCACAGGGGCGGGCAGCACTCATGCCTCGTGA","MFFEAGAWVGHFLGSAQSTSKPGFHRHPSIPSLQRFALVRRRMWSSSAHGAVLTPPRALLPTLSAFQLLHPLPYPTGRCLPEAPRPYTVRLLPVLTVSTPPHPPAGPTRHRFQQWNAQSVAQSHPPRRRPPQPDRHRCRRAFRCNGPVLLLLLPACREPSSTHIPSNVQTQWRSNRSVPTLRVRRISATSRLHHRPLQHRHYSGRSEYPHQSPLSSHGFRNRTQGRLTQASRRKRVPMSDEHIPETNHHMFDAQVGTTVAVTYLHDPCIGWTEYLLDFIGSALSNENEITPALVIPETSHVTPAFDRLTEATGTPVFVEDSGGHRDFRSGMWAPNLAHFFEDGPHSRFKVSQQFLHPNPEPALVPTLMLSASIYHPARRTTKLGRVTEIITETLLPGPSTTLSWGRYEPVGAPWDRGQLTDLARKLMPEAHFNLAAHSDLGTLSGTMTVARTSSGLEEYVEVSIAIPDLAPSQQADAVNTLLDTLAEQTKPQFVLAVRIQAFADTSLPTSIRRPPVPLAILIGAAGIRQLGVDVHDIARQHAGRTYGSGRRQGLIVPFETMQADWSALSSLVATLDGDAGNIARVLEDPTDGTGAGSTHAS$","Hypothetical protein","Periplasm, Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1990","2159453","2160553","1101","9.32","5.55","38256","GTGCTTGACGGGGAGATCGTCCGGATCATGACCGACGATGAGGTTCCCCCACCGGCCGAGGTCTCTGACATCTCCGGCCTACTCACGGACATGACGGACACGCACCCGGGCCGATGGAACGATCGCAGTCGGCTGCTCGGCGCGGGAATTCTACTGACGATAAGTACTGTGGCCGCCGCCTGGGCAACTCCTCGGGAACTCATCACCGCCGTACCCTCATGGACTCTTCTCCTGCCGGGGCTGGTGACCATGCTCCTGGCCGCCTTCATCTCCCAGGGACGATCCATCAGCGCACGACGGATCGGCGCCCTGGCAACCTTCCTCGCCTTCGGACTGTTGGTTCCCGCGATCTATACCATGGCCACGGGTCCCGTGAGTGACCGTCTGCTGTCCGTCGCGGCCTCGCTCACCGCTGTCGCGCTGGCCGTCCTGGGCAGGGGCAATGTGGGGTGGGCATTCGGAATTCTGGTGGGAATGGCCCTCTACGGCGTGTGGATCACCTTCAACATGGTTTCCATCGCACCTCTGGGCGACGGGCTCACAGCTGTCACGGCATTAGTGTGTCTCGGTATCCTGCCGTGGCTGGCACTCCTCATTTCCGGAACATCGAGGCTCGACGACGCCGCTCTCGCCGGGGCCCTACCCTCACGACGCCGCGTCCTTCAGGATCTGACGACTGCTCACGAGACCCTCGCCGGTAGCTGCCTCACTGCAGCAGCCATGCTCTCCTGGAGCTCCACCATTCTTGCCTCCAGCACAAACATGTGGGCTCGTGCACTGAGCACCGTCATCATCATCGCCGCGCTCCTGAGGTCACGGGCCTTTCCCCTGCGAAGTGAAGTCCTCTCGCTGTGGCTGGCCGCCGTTCCCCCAGCCCTAGTCCTCAGCGGAGCAATCACTCAGCCCGCGGCACGCGCCGCTCTACTCTTCGTCGCCGGTCTCGTGCTGGCCTCGCTGTCCCTCTACCGGCCCGCACCCCAAACCAGGGTCCGTCTCCGGCGTCTAGGGGATCGCCTCGAATCCCTGTGCTTGGCCGCAACACTGCCTCTCCTGTGCGGTATCGGCGGTCTGTTCACCCATCTTCTGGGGGTGTTCGCATGA","VLDGEIVRIMTDDEVPPPAEVSDISGLLTDMTDTHPGRWNDRSRLLGAGILLTISTVAAAWATPRELITAVPSWTLLLPGLVTMLLAAFISQGRSISARRIGALATFLAFGLLVPAIYTMATGPVSDRLLSVAASLTAVALAVLGRGNVGWAFGILVGMALYGVWITFNMVSIAPLGDGLTAVTALVCLGILPWLALLISGTSRLDDAALAGALPSRRRVLQDLTTAHETLAGSCLTAAAMLSWSSTILASSTNMWARALSTVIIIAALLRSRAFPLRSEVLSLWLAAVPPALVLSGAITQPAARAALLFVAGLVLASLSLYRPAPQTRVRLRRLGDRLESLCLAATLPLLCGIGGLFTHLLGVFA$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[44-64]?$ $\"[70-90]?$ $\"[100-118]?$ $\"[124-144]?$ $\"[149-169]?$ $\"[179-199]?$ $\"[220-242]?$ $\"[248-270]?$ $\"[282-300]?$ $\"[306-326]?$ $\"[341-361]?$	transmembrane_regions

InterPro
IPR002543
Domain

Cell divisionFtsK/SpoIIIE
PF01580	$\"[594-796]T$ $\"[950-1199]T$ $\"[1235-1452]T$	FtsK_SpoIIIE
PS50901	$\"[621-821]T$ $\"[975-1166]T$ $\"[1261-1435]T$	FTSK

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[637-816]T$ $\"[985-1181]T$ $\"[1271-1474]T$	AAA

noIPR
unintegrated

unintegrated
PTHR22683	$\"[227-913]T$	SPORULATION PROTEIN RELATED
PTHR22683:SF1	$\"[227-913]T$	DNA TRANSLOCASE FTSK
tmhmm	$\"[211-233]?$ $\"[301-321]?$	transmembrane_regions

InterPro
IPR001853
Family

DSBA oxidoreductase
PF01323	$\"[117-271]T$	DSBA

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[108-280]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[41-61]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 117 to 271 (E_value = 7.9e-06) place ANA_1994 in the DSBA family which is described as DSBA-like thioredoxin domain.","","thioredoxin domain family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1996","2168055","2169281","1227","6.54","-2.79","43748","ATGTCGGTGACCGCAGCACCCGCGGCGTCCTGTGCCCTCCACGACGCCGGCACCTGCCGCTCCTGCCCTCACCTGTCCCTGCCGATGCCCGACCAGCTGGCCGCCAAGCAGTCCCGTGTCGCCGCCCTCCTGGCCGAGCACATCCCGGCCGACCTGTGGCAGGCGTCAGCGGCGAGCGCCCCCACCGGCTTCCGCAACAAGGCGAAGATGGCGGTGGCCGGGACCGCCGCACACCCCACCCTGGGGATCCTCGATGGCGCCGGGTGCGGCATCGATCTGCGCACCTGCCCACTGCACGTGCCCGCCATCGAGGCGGCCCTGCCGGTGCTGGCCGACCTCATCACCGAGCTGGGCCTGCGCCCCTACGACGTGCCCTCGCGCCGCGGCGAACTCAAGTACGTCCTGGTGACCGCCTCGCCCGACGATGACCTCATGGTGCGCTTCGTCCTGCGCTCTCGCCGCTACCTGGAGCGGCTGCGCGCCGCCGTGCCGGACCTGCACCGGCGCCTGCCCCAACTAGCGGTGGCCGCCATCAACATCCAGAGCGTCCACCAGGCCATCATCGAGGGGCCCGAGGAGATCGTCCTGACCGAGGAGGACCGCCTCCTCATGCGCCTCAGCCTGCCGTCACCGGAGCTGGGCGGCCAGACAGGCCGGCGAGCCGAGAGCGTCGAGCTACCCCTCTACCTGCCCACCCGTTCCTTCTTCCAGACCAATACGGCCGTGGCCGAGGCGCTCTACGCCACCGCCCGCAACTGGGCCGAGGAGGCCGAGCCGGCCCGGGTGTGGGACCTGTTCTGCGGCGTCGGCGGTTTCGCCCTGGCCCTGGCCGCGCCCAACCGCCGGGTGCTGGGGGTGGAGGTCTCGGCGTCGGCCATTGACGGGGCGCGTGCGGCGGCCGACCTCATGGGACTGGACCCAGCCCTGGTGCGCTTCGAGGCCGGCGACGCCCGTGTCCTGGACCCGGCCGCCGGGGATCGCGCCGCCGGGGCGCGGCGCCCGGACCTGCTCGTGGTCAACCCGCCCCGGCGCGGAATCGGGGAGCAGCTGGCCACTCGGATCGAGGCCTCCGGCGTGGAGCGGGTGCTCTACTCCTCCTGCAACCCGCGCACGCTGGCGGCGGACCTGGCGCACCTGCCCTCGATGCGGGTGGTGCGCTCGCGCCTGTTCGATATGTTCCCGCACACCGAGCACGCCGAGGTGCTCGTAGAGCTGGTACGGGACTGA","MSVTAAPAASCALHDAGTCRSCPHLSLPMPDQLAAKQSRVAALLAEHIPADLWQASAASAPTGFRNKAKMAVAGTAAHPTLGILDGAGCGIDLRTCPLHVPAIEAALPVLADLITELGLRPYDVPSRRGELKYVLVTASPDDDLMVRFVLRSRRYLERLRAAVPDLHRRLPQLAVAAINIQSVHQAIIEGPEEIVLTEEDRLLMRLSLPSPELGGQTGRRAESVELPLYLPTRSFFQTNTAVAEALYATARNWAEEAEPARVWDLFCGVGGFALALAAPNRRVLGVEVSASAIDGARAAADLMGLDPALVRFEAGDARVLDPAAGDRAAGARRPDLLVVNPPRRGIGEQLATRIEASGVERVLYSSCNPRTLAADLAHLPSMRVVRSRLFDMFPHTEHAEVLVELVRD$","SAM-dependent methyltransferase related to tRNA (uracil-5-)-methyltransferase","Cytoplasm","RNA methyltransferase, TrmA family","putative enzyme ","(Uracil-5)-methyltransferase","","Johansson M.J., Bystrom A.S. Dual function of the tRNA(m(5)U54)methyltransferase in tRNA maturation. RNA 2002. 8(3):324-335. PMID: 12003492Agarwalla S., Kealey J.T., Santi D.V., Stroud R.M. Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli. J. Biol. Chem. 2002. 277(11):8835-8840. PMID: 11779873","","","

InterPro
IPR010280
Family

(Uracil-5)-methyltransferase
PF05958	$\"[102-408]T$	tRNA_U5-meth_tr
PS01230	$\"[340-371]T$	TRMA_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[244-342]T$	no description
PTHR11061	$\"[19-407]T$	RNA M5U METHYLTRANSFERASE FAMILY

InterPro
IPR000014
Domain

PAS
SM00091	$\"[6-72]T$	PAS

noIPR
unintegrated

unintegrated
G3DSA:3.30.450.20	$\"[11-99]T$	no description

InterPro
IPR000215
Family

Proteinase inhibitor I4, serpin
PTHR11461	$\"[161-444]T$	SERINE PROTEASE INHIBITOR, SERPIN
PF00079	$\"[61-444]T$	Serpin
SM00093	$\"[77-444]T$	SERPIN

noIPR
unintegrated

unintegrated
G3DSA:3.30.497.10	$\"[61-292]T$	no description
PTHR11461:SF23	$\"[161-444]T$	SERINE PROTEASE INHIBITOR, SERPIN
signalp	$\"[1-35]?$	signal-peptide

","No hits to the COGs database.","***** IPB000215 (Serpin) with a combined E-value of 9.3e-06. IPB000215A 91-118 IPB000215C 232-246","","","-42% similar to PDB:1SNG Structure of a Thermophilic Serpin in the Native State (E_value = 5.8E_15);-43% similar to PDB:1MTP The X-ray crystal structure of a serpin from a thermophilic prokaryote (E_value = 8.3E_14);-38% similar to PDB:1HP7 A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS (E_value = 1.0E_11);-38% similar to PDB:1IZ2 Interactions causing the kinetic trap in serpin protein folding (E_value = 1.3E_11);-38% similar to PDB:1OO8 CRYSTAL STRUCTURE OF A1PI-PITTSBURGH IN THE NATIVE CONFORMATION (E_value = 2.3E_11);","Residues 61 to 444 (E_value = 5.5e-13) place ANA_1998 in the Serpin family which is described as Serpin (serine protease inhibitor).","","homolog, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_1999","2172533","2172979","447","4.97","-4.84","16028","ATGACCATCGAGCTCGTCACCACCTCCAGCCCGGAGATCGTCGAGGCCATGGAGCGCCTCATCCCGCAGCTCTCCCGCAGCGCCCCGGCACTGACCGCCGAGCAGTGCGAGGCCCTCATCGCTCAGGAGGGGGTCTTCCTCTTCATCTTCCGGCCTGAGGTCGAGGCCGGCCAGAGCGCACCGATCCTGGGCATGCTCACCCTGGCGACCTTCACGATCCCTACGGGCCTGCGCGCATGGGTGGAGGACGTCGTCGTCGACGGTGAGGCCCGTGGCCAGGGCGCCGGGCAGGCCCTCGTGGAGGCCGCCGTCGAGCACGCCGGGAAGCTGGGCGCACGCACTGTAGACCTCACCTCCCGCCCCACGCGCGAGGCCGCCAACCGCCTCTACCGCCGCGCCGGCTTCGAGCTGCGGGAGACCAACGTCTACCGCTACGCCCAGGCCTGA","MTIELVTTSSPEIVEAMERLIPQLSRSAPALTAEQCEALIAQEGVFLFIFRPEVEAGQSAPILGMLTLATFTIPTGLRAWVEDVVVDGEARGQGAGQALVEAAVEHAGKLGARTVDLTSRPTREAANRLYRRAGFELRETNVYRYAQA$","GCN5-related N-acetyltransferase","Cytoplasm","acetyltransferase, GNAT family family","hypothetical protein predicted by Glimmer/Critica","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[54-136]T$	Acetyltransf_1
PS51186	$\"[1-148]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[54-146]T$	no description
PTHR23091	$\"[78-147]T$	N-TERMINAL ACETYLTRANSFERASE

","BeTs to 15 clades of COG0454COG name: Histone acetyltransferase HPA2 and related acetyltransferasesFunctional Class: K [Information storage and processing--Transcription] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0454 is aompkzyqvdrlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 54 to 136 (E_value = 8.2e-15) place ANA_1999 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","GNAT family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2000","2173947","2173132","816","4.79","-13.93","28139","ATGCTCGCCGACATGCGTCTGCTCGCCACGGATCTTGACGGCACCCTCGTCTTCCACCACGTCGTCGGGCAGGCCGACGCCGAGGCCCTCGTGCGCTGGCGGGCGGCCGGCAACCTCCTGGTGCTGGCCACGGGGCGCTCGGTGCGGCTGGTGCAGCACGCCGTCGAGGTGGCCCGGGCCTCGACGTCCATCGGCCTGGACTACGACTACGCCGTGTGCGCCACGGGCACGACCGTCATCGACGCCGCCGGTCAGGTGCACTGCACCCGGATGCTTGAGGCCGACCAGGTGCGGGCGGTCGTGCGGGCGATCGGCGACGTCGTCCAGGCCCCTGTCTCCGTGTTCGCCTCGACCCTTGAGCGCGACTACGTGCTGGACGACCCGATCGGCCTGTCCACCGACCAGCGCACGCCGCCGGACCGCTTCACCGCGGCGCCTCTGTCGCAGGTCGCGGGCCGGGGGGTGACCTCGATGCCGCTGCACATCCCCGACGTTCGGGCTGCTGCGGCGCTGGCCCGAGGCCTGGAGGAGACGGTGGATGGCATCAGCTGCACCCGCTCGACCGGCTTCGTGGACGTCACGGCCGCAGGCGAGTCCAAGGGAACGGGCCTGGGCCGGCTCGCCGAGCTCCTGGCCAGCCAGGGCGTGGAGGTCAGTGAGATGGCCGCCGTGGGCGACTCCTGGAATGACATCTCGATGTTCGAGCGGGCCGACGTCCCCTGTGCGATCGGTGGCGCCCCGGACGAGGTCGTCGAGGCCGCCGGCGGGCGCACCACCCCGAGCGTGGCCGCCTTCATCGAGGCTCTGCTGGCCTGA","MLADMRLLATDLDGTLVFHHVVGQADAEALVRWRAAGNLLVLATGRSVRLVQHAVEVARASTSIGLDYDYAVCATGTTVIDAAGQVHCTRMLEADQVRAVVRAIGDVVQAPVSVFASTLERDYVLDDPIGLSTDQRTPPDRFTAAPLSQVAGRGVTSMPLHIPDVRAAAALARGLEETVDGISCTRSTGFVDVTAAGESKGTGLGRLAELLASQGVEVSEMAAVGDSWNDISMFERADVPCAIGGAPDEVVEAAGGRTTPSVAAFIEALLA$","HAD-superfamily hydrolase, subfamily IIB","Cytoplasm","hydrolase, haloacid dehalogenase-like hydrolase","putative phosphatase","HAD-superfamily hydrolase, subfamily IIB","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317","","","

InterPro
IPR006379
Family

HAD-superfamily hydrolase, subfamily IIB
TIGR01484	$\"[7-243]T$	HAD-SF-IIB: HAD-superfamily hydrolase, subf

InterPro
IPR013200
Domain

HAD superfamily hydrolase-like, type 3
PF08282	$\"[8-266]T$	Hydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[3-270]T$	no description

","BeTs to 16 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0561 is aompkzy-vdrlbce-gh-n-j-itwNumber of proteins in this genome belonging to this COG is 6","***** IPB000150 (Cof protein) with a combined E-value of 4.3e-21. IPB000150A 8-17 IPB000150B 37-46 IPB000150D 186-204 IPB000150E 215-246","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 270 (E_value = 8.2e-06) place ANA_2000 in the S6PP family which is described as Sucrose-6F-phosphate phosphohydrolase.Residues 8 to 266 (E_value = 2.3e-13) place ANA_2000 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.Residues 207 to 247 (E_value = 5.6e-08) place ANA_2000 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","haloacid dehalogenase-like hydrolase","","1","","","","","","","","","","","","","Tue Jul 31 23:05:15 2007","","","Tue Jul 31 23:02:35 2007","Tue Jul 31 23:02:35 2007","","","Tue Jul 31 23:02:35 2007","Tue Jul 31 23:02:35 2007","","","","","yes","","" "ANA_2001","2175028","2174102","927","4.61","-19.09","32191","ATGCCACGCAGGCTCATCTCCACCGACCTGGACGGCACCATCGTCTTCAACGGGACGATCTCGCTGCGTGACCGCGAGGCCATGGCCCGGTGGCGGGCGGCCGGCAACCTCCTGGTCATCAACACTGGCAGGTCGGTCTCGGCGCTGGAGCACGTCGTGGTGCCCATGGGCCTAGAGTTCGACAACGCCATCCTCTACACGGGCGCCGCCATCGTGGACGCGGACATCCGGGTGCAGTGCTCCACGGCGCTGCCGGCCGGCGTCGTCGAGGACATTCTTGACTTCGTCGAAGGGGCGCCGGGCGTCACCGTCTTCACCACCGGGCTGGACGAGGACCTGCTCGTCTACGACACGATCGGCTCTGGCTCCGAGCTGCTGACGCTGTTCCGGCCGGCCACCCGGCGAGAGCTCGACGGGCGCGAGGTCATCGGGGTGCCGATGCGCTTCATCGACCCGGAGATGGCCGCGCGCACCGAGACCTACCTGCACCGGCGCTGGGAGGGGCAGGCGGTGGGCTTCCGCAACCAGGACTTCATCGACGTCGTGCCCGCCTCGGCCTCCAAGGGGGCGGGCCTCAGGCGGCTGGTGGTGAGCCTGTCTGAGCCGCCCGCCGCGGAGGCGGCCGGGGCTGCCGGAGAGGGTGCGTCCAGGGCGGGCGCGGCCAGCGGGGCCGGGGAGGCTTCGACCGGTGAGGCGAGCGAGGCGCCGGTCGGCGGCTCGGCGGGGCTCGGCGTCGGCCCGGGGACGGCGGAGCTGGTGGAGACCTGGTCCATCGGGGACTCCTGGAACGACATCTCCATGCACCAGGCTGCCGACCACTCCTACGCCCTGCCCTGGTCACCGCCGGAGGTGGTGGCCCAGTGTGACGGCACGGTCTCCAGCCTCGCCGACCTCATCGACTCCCTCATGGGGCGACCGACGCTTTAG","MPRRLISTDLDGTIVFNGTISLRDREAMARWRAAGNLLVINTGRSVSALEHVVVPMGLEFDNAILYTGAAIVDADIRVQCSTALPAGVVEDILDFVEGAPGVTVFTTGLDEDLLVYDTIGSGSELLTLFRPATRRELDGREVIGVPMRFIDPEMAARTETYLHRRWEGQAVGFRNQDFIDVVPASASKGAGLRRLVVSLSEPPAAEAAGAAGEGASRAGAASGAGEASTGEASEAPVGGSAGLGVGPGTAELVETWSIGDSWNDISMHQAADHSYALPWSPPEVVAQCDGTVSSLADLIDSLMGRPTL$","HAD superfamily hydrolase","Cytoplasm","putative hydrolase","putative Cof-like hydrolase","Haloacid dehalogenase domain protein hydrolase, type 3","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317","","","

InterPro
IPR013200
Domain

HAD superfamily hydrolase-like, type 3
PF08282	$\"[6-195]T$	Hydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[1-297]T$	no description

","BeTs to 9 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0561 is aompkzy-vdrlbce-gh-n-j-itwNumber of proteins in this genome belonging to this COG is 6","***** IPB000150 (Cof protein) with a combined E-value of 5.4e-13. IPB000150A 6-15 IPB000150B 35-44 IPB000150D 174-192 IPB000150E 249-280","","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 48 (E_value = 0.00014) place ANA_2001 in the S6PP family which is described as Sucrose-6F-phosphate phosphohydrolase.Residues 6 to 299 (E_value = 2.2e-06) place ANA_2001 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.","","hydrolase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2003","2176495","2175713","783","4.48","-24.64","28286","GTGACCCGACTCCTCGTCACCGACCTGGACGCCACCATCGTCTTCGACCGCTCCGTCTCCCCGGCCGACCGCGAGGCCATGGCCCGCTGGCGGGCCGCCGGCAACCTCCTGGCCGTGGACACCGGCAAGTCCTCCTTCGCCACCCGCGACGTCCTGGCGCCTCTGGGCGTCGACTTCGACTACGGCGTCGTCTTCACCGGGGCGGTCCTCATCGACGGCAGCTACCAGGTCCTCTCGGCCTGCTACCTGCCCGACGGCGTCGCCCGCGACGTGGCGACCCGCACCGTCGACTTGCCAGGGGTGACCACCTACGCCACCACCATCGAGACCGACTACATCCTGGCCGACAACAACGAGGAGATTTCCTCCATCCTCGCGGTCTTCGAGCATCTGAGCCTGGAGGAAATGGACGCCCACCGCTTCATCGGCGTGCCCCTGCGCGTCACCGACGACGCCCTGCGCGAGCGCCTCCAGGATGACCTCACCTGGCGCTGGGAGGGCGTCCTGGACTGCCACCGCAACCAGGAGTTCCTTGACCTCGTGCCCGCCGGTGCCACCAAGGGCGCGGGACTACGCGCCCTCCTGGACGGGCCCCTGGCGGGACAGGACATCGAGGTCTGGACCATCGGCGACTCCTGGAACGACCTGGACATGCACGCCGTCGCCGACCACTCCGTCGCCCTGCCCTGGTCCCCGCCGGAGGTGACGGCTGCGTGCGAGACGACCACGGGCTCCATGGCCGAGCTCATCACCACGATCCTGGAAGGAGACCGGCATGAGTGA","VTRLLVTDLDATIVFDRSVSPADREAMARWRAAGNLLAVDTGKSSFATRDVLAPLGVDFDYGVVFTGAVLIDGSYQVLSACYLPDGVARDVATRTVDLPGVTTYATTIETDYILADNNEEISSILAVFEHLSLEEMDAHRFIGVPLRVTDDALRERLQDDLTWRWEGVLDCHRNQEFLDLVPAGATKGAGLRALLDGPLAGQDIEVWTIGDSWNDLDMHAVADHSVALPWSPPEVTAACETTTGSMAELITTILEGDRHE$","HAD-superfamily hydrolase, subfamily IIB","Cytoplasm","hydrolase, haloacid dehalogenase-like family,putative","putative Cof-like hydrolase","HAD-superfamily hydrolase, subfamily IIB","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317","","","

InterPro
IPR006379
Family

HAD-superfamily hydrolase, subfamily IIB
TIGR01484	$\"[4-228]T$	HAD-SF-IIB: HAD-superfamily hydrolase, subf

InterPro
IPR013200
Domain

HAD superfamily hydrolase-like, type 3
PF08282	$\"[5-250]T$	Hydrolase_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[2-245]T$	no description

","BeTs to 12 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0561 is aompkzy-vdrlbce-gh-n-j-itwNumber of proteins in this genome belonging to this COG is 6","***** IPB000150 (Cof protein) with a combined E-value of 3.1e-09. IPB000150A 5-14 IPB000150D 173-191 IPB000150E 200-231","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 249 (E_value = 0.00047) place ANA_2003 in the S6PP family which is described as Sucrose-6F-phosphate phosphohydrolase.Residues 5 to 250 (E_value = 1.4e-07) place ANA_2003 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.","","haloacid dehalogenase-like family, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2004","2175022","2175747","726","5.09","-11.69","24470","GTGGCATGGGAGTCCTTTCCGTTCAGGTTCTGCCGGTCTCCAGCTGCTCAGAGCGGCTCGCGGGCTGCCTACGAGCCGCCCGGGAGCCGCCCAGAATCGCTAAGAGCCGTCAGCAGCCTTATTCTCCTCATTCTTCGCCGCAGCGTCAGCGGACTCGTCAGCGTCTTGGACCGTACTCTCCCGCCGGGCCTTCTTCTCCGCCTTACGGGCCTTCTTGGACTGCTTCTTGTCCTCGCGCTCCAGGCGCTCGTGGGCCCACTGGGCGTAGCCCTGCAGGAGGCTGCGCGAGTCGGGGGTGAGGATCTTGTTGTCCTCGAGCAGCCCCTCGGCGCGCAGGGTCATGAACCGCAGGTACTCGGGGTTGCGGGTGAGCCCCCACTGGCGCTTGGCCTCCTCCAGATCGGAGACGTCACGGCGCACCTGCCGCTCGATCATGGCACGCCCACCCATGAGGAAGATGGCCACGAGCAGAGCCACGATCGAGCCGATCCCCCGGGTGAAGGGGTAGAGGACGCAGGCGATGACCATGAGCCAGGTGACGTACTTGCCCATGGAGTGGGTGTATCCGCGCCAGCGGCCGTCATCCCCGGTGGCCCAGGCGCGCAGCTTGGCGCGCCCGTCGGGATCCCCGCCGTTGAACCAGTCGCGCACCCGGGCGCCCAGCGTCCGTGCGCCATCGGTCTTGCTGTTCTCACTCATGCCGGTCTCCTTCCAGGATCGTGGTGA","VAWESFPFRFCRSPAAQSGSRAAYEPPGSRPESLRAVSSLILLILRRSVSGLVSVLDRTLPPGLLLRLTGLLGLLLVLALQALVGPLGVALQEAARVGGEDLVVLEQPLGAQGHEPQVLGVAGEPPLALGLLQIGDVTAHLPLDHGTPTHEEDGHEQSHDRADPPGEGVEDAGDDHEPGDVLAHGVGVSAPAAVIPGGPGAQLGAPVGIPAVEPVAHPGAQRPCAIGLAVLTHAGLLPGSW$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-51]?$	signal-peptide
tmhmm	$\"[64-84]?$	transmembrane_regions

InterPro
IPR004704
Family

Phosphotransferase system, mannose/fructose/sorbose family IID component
PF03613	$\"[12-282]T$	EIID-AGA
TIGR00828	$\"[12-282]T$	EIID-AGA: PTS system, mannose/fructose/sorb
PS51108	$\"[12-282]T$	PTS_EIID

noIPR
unintegrated

unintegrated
tmhmm	$\"[111-129]?$ $\"[135-155]?$ $\"[239-257]?$ $\"[263-281]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB004704 (PTS system mannose/fructose/sorbose family IID component) with a combined E-value of 2.3e-113. IPB004704A 13-48 IPB004704B 65-101 IPB004704C 107-148 IPB004704D 187-214 IPB004704E 229-272","","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 282 (E_value = 3.4e-154) place ANA_2005 in the EIID-AGA family which is described as PTS system mannose/fructose/sorbose family IID component.","","system, mannose-specific IID component (PTS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2007","2178487","2177558","930","5.51","-6.42","31653","GTGCATGACATCAATCTGATCCAGATCATTCTGGTCACGCTCGTGGCGTTCGTCGCGGGTATGGCCAGCGTCCTGGACGAGCGGCAGTTCCACCGCCCGCTCGTCGCCTGCACCCTGACCGGGATCGCCCTGGGCAACCCCACCATTGGCATCATGGTCGGCGGCTCCCTGGAGCTGCTCGCCCTGGGCTGGATGAACGTCGGTGCCGCCATGGCTCCCGACTCCGCCCTGGCGTCCACCGTCTCCACCATCATCGCCGTGGCCTCGGTCGGTGACGCCTCCTCCACCAAGAGCGCCATCGCGGCCGCCATCGGTGTGGCCGTCCCGCTGGCCGTCGCCGGCCAGGCCCTGACGATCTTCGTACGAACGATCGCCATCTTCTTCGCCCACCAGGCGGACCGCTTCGCGGAGCAGGCCAACTACCGGGGCATCGCCATCATGCACTTCACGACCCTGGGCCTGCAGGGACTGCGCGTCGCCATCCCGACCGCAGTGGTTGCCGGACTGGCCTCAGGCGACACGGTCAAGCACGCCCTCGACGCCATTCCGAAGGTCATCACCGAGGGCCTGGGCATTGCCGGAGGCTTCATCGTCGTCGTCGGTTACGCCATGGTCATCAACATGATGAAGGCGCGCAAGCTCATGCCCTTCTTCTTCCTGGGCTTCATCTTCGCCACCTTCGCCACCACCGTGGGCGGCTCGGCCTCGGTCGGTGACCACAGCAAGGGCATCGACAAGTGGGTCATCAACCTCGCTCCCAACGGCGCCACCCTCGTGGCGCTGGGCATCCTGGGGGCCTGCCTGGCCGTCATCTACGTCCAGCTCAACCCCGAGTTCCATGACTCCGTGCGCCTGCCCGCCGCCTCCCCCGCAGCCAGCGGCGGCTCCAGCAGCGACCTGGATGACGACCTCGACGACGAGCTCGACTGA","VHDINLIQIILVTLVAFVAGMASVLDERQFHRPLVACTLTGIALGNPTIGIMVGGSLELLALGWMNVGAAMAPDSALASTVSTIIAVASVGDASSTKSAIAAAIGVAVPLAVAGQALTIFVRTIAIFFAHQADRFAEQANYRGIAIMHFTTLGLQGLRVAIPTAVVAGLASGDTVKHALDAIPKVITEGLGIAGGFIVVVGYAMVINMMKARKLMPFFFLGFIFATFATTVGGSASVGDHSKGIDKWVINLAPNGATLVALGILGACLAVIYVQLNPEFHDSVRLPAASPAASGGSSSDLDDDLDDELD$","PTS system, mannose-specific IIC component","Membrane, Cytoplasm","mannose-specific phosphotransferase systemcomponent IIC homolog lmo0782","PTS enzyme IIC; mannose-specific","phosphotransferase system PTS, sorbose-specific IIC subunit","","","","","

InterPro
IPR004700
Family

Phosphotransferase system, sorbose-specific IIC subunit
PF03609	$\"[4-272]T$	EII-Sor
PS51106	$\"[4-245]T$	PTS_EIIC_TYPE_4

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[45-65]?$ $\"[71-91]?$ $\"[101-121]?$ $\"[186-206]?$ $\"[216-236]?$ $\"[255-275]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB004700 (Phosphotransferase system PTS, sorbose-specific IIC subunit) with a combined E-value of 2.8e-55. IPB004700A 3-29 IPB004700B 32-67 IPB004700C 182-222","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 272 (E_value = 7.5e-114) place ANA_2007 in the EII-Sor family which is described as PTS system sorbose-specific iic component.","","phosphotransferase system component IIC homolog lmo0782 (PTS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2009","2179087","2178596","492","8.31","1.42","17389","ATGGACGTCAAGCTCCTGCGTATTGATTCCCGCCTGGTTCACGGACAGGTCGCCAACAACTGGGCCGGATCCCTGGGCGCCGAGGCCATCCTCGCCGTTTCCGACGGCGCCGCCAACGACGAGCTGCGCAAGACCCTCATGCTGCAGACCGGTGGCGGCAAGGTGAAGGTCCACGTGCTGGGCGTGGAGAAGGCCGCCCGCGTCTACAAGAACCCCAAGTACGAGACCCTCAAGGCCGTCATCGTCGTCGAGACCCCGGCCGACATCGTGCGCCTGCTCGACCTGGGCGTGGAGGCCAAGGAGGTCAACGTCGGCGGCATGACCTTCAAGCAGGGCACCAGCCAGGTCTCCCAGGCCGTCTACGCCAGCCCTGCCGACGTCGAGGCCTTCAAGGAGATCGACTCCCGCGGCATCAAGCAGTACATCCAGCAGGTGCCCTCCACCGCGAGCTCCGACCTCATGGGGGCCCTCAAGGAGAAGGGCCTGCTCTAA","MDVKLLRIDSRLVHGQVANNWAGSLGAEAILAVSDGAANDELRKTLMLQTGGGKVKVHVLGVEKAARVYKNPKYETLKAVIVVETPADIVRLLDLGVEAKEVNVGGMTFKQGTSQVSQAVYASPADVEAFKEIDSRGIKQYIQQVPSTASSDLMGALKEKGLL$","PTS system, mannose-specific IIAB component","Cytoplasm","protein-Npi-phosphohistidine-sugarphosphotransferase IIAB component","PTS system; mannose-specific IIAB component ","Protein-N(pi)-phosphohistidine--sugar phosphotransferase","","Orriss G.L., Erni B., Schirmer T. Crystal structure of the IIB(Sor) domain of the sorbose permease from Klebsiella pneumoniae solved to 1.75A resolution. J. Mol. Biol. 2003. 327(5):1111-1119. PMID: 12662934","","","

InterPro
IPR004720
Domain

Phosphotransferase system, sorbose subfamily IIB component
PD008332	$\"[9-147]T$	Q8ZFF4_YERPE_Q8ZFF4;
G3DSA:3.40.35.10	$\"[1-159]T$	no description
PF03830	$\"[2-152]T$	PTSIIB_sorb
PS51101	$\"[1-163]T$	PTS_EIIB_TYPE_4

","No hits to the COGs database.","***** IPB004720 (PTS system sorbose subfamily IIB component) with a combined E-value of 5.5e-12. IPB004720A 30-42 IPB004720B 86-107","","","-59% similar to PDB:1BLE PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM (E_value = 2.3E_28);-55% similar to PDB:1NRZ Crystal structure of the IIBSor domain of the sorbose permease from Klebsiella pneumoniae solved to 1.75A resolution (E_value = 3.4E_24);-53% similar to PDB:1EA6 N-TERMINAL 40KDA FRAGMENT OF NHPMS2 COMPLEXED WITH ADP (E_value = 3.4E_24);-53% similar to PDB:1H7S N-TERMINAL 40KDA FRAGMENT OF HUMAN PMS2 (E_value = 3.4E_24);-53% similar to PDB:1H7U HPMS2-ATPGS (E_value = 3.4E_24);","Residues 2 to 152 (E_value = 3.4e-52) place ANA_2009 in the PTSIIB_sorb family which is described as PTS system sorbose subfamily IIB component.","","phosphotransferase IIAB component (ptsL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2010","2179530","2179087","444","4.21","-15.59","15018","ATGGTGGTCTGCCTGGTCGTAGCCGCGCACGGACACTTGGCTGAAGGTCTTGTCGCCTCCTCAGCGATGATCGTCGGTCCCAGTGACGACGTCGTCGCCGTCACCTTCGAGCCCTCCGAGGGCCCCGATGACCTGCTGGCGAAGTACGCCGCCGCGGTCGAGGCCTCCTCCAGCCAGGAGTACCTCATCCTCGTCGACCTCTTCGGCGGCAGCCCCTACAACGCCGCTGCCCGGTTCGCGGCGGGACGCGACGACGCCGACGTCGTCACCGGCGTCAACCTGCCCATGGTCATCGAGGTCCTGTCCCGACGTCTCACCGGCGCCGGCCTCGCCGAGCTCGTGGAGGCCGCCCGCACCTCCGCCGTTGACGGCGTCAAGGTCCTCTCCGAAGTCTTCACCCCTGCCCCCACCACCACTTCCGACGATGAAGGAGACGAGCTCTGA","MVVCLVVAAHGHLAEGLVASSAMIVGPSDDVVAVTFEPSEGPDDLLAKYAAAVEASSSQEYLILVDLFGGSPYNAAARFAAGRDDADVVTGVNLPMVIEVLSRRLTGAGLAELVEAARTSAVDGVKVLSEVFTPAPTTTSDDEGDEL$","PTS system, mannose-specific IIA component","Cytoplasm","PTS system mannose-specific, factor IIAB homologlmo0096","similar to mannose-specific phosphotransferase system (PTS) component IIA ","PTS system, mannose/fructose/sorbose family, IIA subunit","","Postma P.W., Lengeler J.W., Jacobson G.R. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 1993. 57(3):543-594. PMID: 8246840Meadow N.D., Fox D.K., Roseman S. The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Annu. Rev. Biochem. 1990. 59:497-542. PMID: 2197982Saier Jr M.H., Reizer J. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 1992. 174(5):1433-1438. PMID: 1537788Saier Jr M.H., Reizer J. The bacterial phosphotransferase system: new frontiers 30 years later. Mol. Microbiol. 1994. 13(5):755-764. PMID: 7815935Tchieu J.H., Norris V., Edwards J.S., Saier Jr M.H. The complete phosphotranferase system in Escherichia coli. J. Mol. Microbiol. Biotechnol. 2001. 3(3):329-346. PMID: 11361063","","","

InterPro
IPR004701
Domain

Phosphotransferase system, fructose subfamily IIA component
G3DSA:3.40.50.510	$\"[2-135]T$	no description
PF03610	$\"[3-118]T$	EIIA-man
PS51096	$\"[2-125]T$	PTS_EIIA_TYPE_4

InterPro
IPR013789
Domain

Phosphotransferase system, fructose subfamily IIA component, subgroup
TIGR00824	$\"[2-117]T$	EIIA-man: PTS system, mannose/fructose/sorb

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide

","BeTs to 4 clades of COG2893COG name: Phosphotransferase system, mannose/fructose-specific component IIAFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2893 is -----------lb-e--hsn-j----Number of proteins in this genome belonging to this COG is 1","***** IPB004701 (PTS system fructose subfamily IIA component) with a combined E-value of 4.8e-17. IPB004701 62-105 IPB004701 61-104","","","-53% similar to PDB:1VRC Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure (E_value = 1.8E_15);-54% similar to PDB:1PDO PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM (E_value = 6.7E_15);-52% similar to PDB:2IAC Mannose/sorbose specific IIA subunit of phosphotransferase system from Enterococcus faecalis. (E_value = 6.5E_10);-46% similar to PDB:2JG5 CRYSTAL STRUCTURE OF A PUTATIVE PHOSPHOFRUCTOKINASE FROM STAPHYLOCOCCUS AUREUS (E_value = 6.5E_10);","Residues 3 to 118 (E_value = 1.5e-35) place ANA_2010 in the EIIA-man family which is described as PTS system fructose IIA component.","","system mannose-specific, factor IIAB homolog lmo0096 (ptsL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2011","2182064","2179833","2232","5.19","-20.46","79304","GTGACCGACACCGTGAATGACGCCGCAACCAACGCCGTGACTGCTTCAGCGACCGACATCGAGTTCCTCTCCGCCTACGACCAGGGCTTCGCCCGCGTCGCCGCCGTCACCCTGCCGGTGGTGCCCGTCGACCCGGCCGCCAACGCCGCCGCCATCATCGAGCAGGCCCGCACTCTGGCCGAGGACGGCGTCTGCCTGGCCGCCTTCCCCGAGCTGTGCCTGACCGGCTACGCCATCGACGACCTCCTGCTGTCCGACGTCCTGCTGTCCGACGTGCTCGCCGCCATCGAGACCCTGCGCGCTGCCAGCGCCGGCCTCCTGACCGCCCTCGTCGTCGGCGCCCCCCTGCGCCTGGGTGACCGCCTCTACAACTGCGCCCTGGTCATCCAGGGCGGGCGGGTGCGCGGTGTCGCCCCCAAGTCCTACCTGCCCACCTACCGGGAGTTCTACGAGAAGCGGCACTTCGCCCCCGGCGACGCCCTGCCCGCCGGGGTGGAGAGCATTGAGCTGCCCGGCGTGCGCAGCGGTTCCGGCAGCACCGACGGTGTCGAGCCTTCAGCGCGAGTCCCCTTCGGGGCGAACCTCCTGTTCGAGGTCGCCGACGTCCCCGGCCTGACCTTCCACGTCGAGGTCTGCGAGGACATGTGGGTGCCCGTCCCGCCGTCGTCGCTGGCGGCGCTGGCCGGGGCGACGGTCCTGGTCAACCTCTCCGGCTCGCCCATCACGGTGGGGCGGGCCGAGGACCGCGAGCTGCTGGCCCGCTCCTCCTCGGCCCGGGGGCTGGCCGCCTACGTCTACGCCGCCGCCGGGCAGGGCGAGTCCTCCACGGACCTGGCCTGGGACGGCCAGACCCTCGTCTATGAGAACGGCGACCTGCTCGGCACCACCGAACGCTTCCCCGACGGGCCGCGCGCCACCGTCGTCGACGTCGACATCGAGGGCCTGCGCGCCGAGCGCCTGCGCCAGGGGACCTTCGCCGACAACGCCCGCACCCTGAGCTCCCCGGTCGCCGGCGCCCCGACCCCGGCCACCACCTTCACCGACCCGGCGGCCTTCCGCCGCATCCAGATCAGCGCCGCCGACCTGGCCGCCCCGCGCACGGACATCGGCCTGCGCCGCCGCGTGGACCGCTTCCCCTTCGTGCCCGACGACCCGGCCCGACTCGCCCAGGACTGCTACGAGGCCTACAACATCCAGGTGGCCGCCCTCGTCCAGCGCCTGGGGGCCATCGGCAACCCCAAGATCGTCATCGGCGTCAGCGGCGGCCTGGACTCCACCCACGCCCTCATCGTGGCCGCCCGCGCCATGGACCGCCTGGGTCGGCCCCGCTCGGACATCCACGCCATCACCATGCCCGGCTTCGCCACGAGCGCCGGCACGCGCCGCAACGCCGAGGACCTCGCCGTCGGCCTGGGCTGCACCTTCGAGGAGCTCGACATCCGGGCCACCGCCACCCAGATGCTCACCGAGATGGGCCATCCCTACGGCGAGTACGCCCGCACCGGGGCCCTGCCCGAGGGGGTGAGCGAGCGGGACCTCTACGACGTCACCTTCGAGAACGTCCAGGCGGGCCTGCGCACCGACTTCCTCTTCCGCATCGCCAACCACCGCGGCGGCATCGTCCTGGGCACCGGGGACCTCTCCGAGCTCGCCCTGGGCTGGTGCACCTTCGGGGTGGGCGACCAGATGGCCCACTACGGCGTCAACGCCGGCATCCCCAAGACCCTCATTCAGCACCTCATCCGCTGGGTGGTTGCCGAGGGGTTGTTCGACGAGGCCGTCGGCCGCACGCTGCTGTCCATCCTGGACACCGAGATCAGCCCCGAGCTGGTCCCGGCCGAGGCCGGCGGCGCCATCCAGTCAACCCAGGCCAAGATCGGTCCCTATGCCCTGCAGGACTTCACCCTGTGGCACGTGCTGCGTCGAGGCTCGCGCCCCAGCCGCATCGCCTTCCTGGCGCACCGGGCGTGGGCGGACGCGCAGAGCGGGGACTGGCCCGAGGGGCTGCCGCAGGCCGAGAGGGTCGCCTACGACCTTCCCGAGATCCGGCGCTGGCTCGAGCTGTTCCACCGGCGCTTCTTCACCAACCAGTTCAAGCGCTCCACCCTGCCCAACGGGCCCAAGGTGGTGGCCGGCGGTTCGCTGTCCCCCCGTGGGGACTGGCGCATGCCCTCCGACGCCGCAGCGACCGCCTGGCTGGCCGAGCTCGAGCGCAACGTGCCGCGGGCGTGA","VTDTVNDAATNAVTASATDIEFLSAYDQGFARVAAVTLPVVPVDPAANAAAIIEQARTLAEDGVCLAAFPELCLTGYAIDDLLLSDVLLSDVLAAIETLRAASAGLLTALVVGAPLRLGDRLYNCALVIQGGRVRGVAPKSYLPTYREFYEKRHFAPGDALPAGVESIELPGVRSGSGSTDGVEPSARVPFGANLLFEVADVPGLTFHVEVCEDMWVPVPPSSLAALAGATVLVNLSGSPITVGRAEDRELLARSSSARGLAAYVYAAAGQGESSTDLAWDGQTLVYENGDLLGTTERFPDGPRATVVDVDIEGLRAERLRQGTFADNARTLSSPVAGAPTPATTFTDPAAFRRIQISAADLAAPRTDIGLRRRVDRFPFVPDDPARLAQDCYEAYNIQVAALVQRLGAIGNPKIVIGVSGGLDSTHALIVAARAMDRLGRPRSDIHAITMPGFATSAGTRRNAEDLAVGLGCTFEELDIRATATQMLTEMGHPYGEYARTGALPEGVSERDLYDVTFENVQAGLRTDFLFRIANHRGGIVLGTGDLSELALGWCTFGVGDQMAHYGVNAGIPKTLIQHLIRWVVAEGLFDEAVGRTLLSILDTEISPELVPAEAGGAIQSTQAKIGPYALQDFTLWHVLRRGSRPSRIAFLAHRAWADAQSGDWPEGLPQAERVAYDLPEIRRWLELFHRRFFTNQFKRSTLPNGPKVVAGGSLSPRGDWRMPSDAAATAWLAELERNVPRA$","NAD(+) synthetase","Cytoplasm","Glutamine-dependent NAD(+) synthetase (NAD(+)synthase[glutamine-hydrolyzing])","NAD(+) synthetase ","NAD(+) synthase (glutamine-hydrolyzing)","","Rizzi M., Nessi C., Mattevi A., Coda A., Bolognesi M., Galizzi A. Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. EMBO J. 1996. 15(19):5125-5134. PMID: 8895556","","","

InterPro
IPR003010
Domain

Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase
G3DSA:3.60.110.10	$\"[26-330]T$	no description
PF00795	$\"[32-238]T$	CN_hydrolase
PS50263	$\"[31-334]T$	CN_HYDROLASE

InterPro
IPR003694
Domain

NAD+ synthase
PF02540	$\"[399-629]T$	NAD_synthase

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[391-652]T$	no description

noIPR
unintegrated

unintegrated
PTHR23090	$\"[35-345]T$ $\"[371-660]T$ $\"[677-739]T$	NH(3)/GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE
PTHR23090:SF1	$\"[35-345]T$ $\"[371-660]T$ $\"[677-739]T$	GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE

","BeTs to 19 clades of COG0171COG name: NAD synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0171 is aompkzyqvdrlbcefg-snuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB003694 (NAD+ synthase) with a combined E-value of 3.8e-22. IPB003694A 416-431 IPB003694B 519-531 IPB003694C 540-573 IPB003694D 621-636***** IPB000132 (Nitrilase/cyanide hydratase) with a combined E-value of 1.3e-06. IPB000132A 32-74","","","No significant hits to the PDB database (E-value < E-10).","Residues 32 to 238 (E_value = 4.2e-06) place ANA_2011 in the CN_hydrolase family which is described as Carbon-nitrogen hydrolase.Residues 399 to 629 (E_value = 1.9e-07) place ANA_2011 in the NAD_synthase family which is described as NAD synthase.","","NAD(+) synthetase (NAD(+) synthase[glutamine-hydrolyzing]) (nadE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2012","2182772","2182230","543","11.26","14.56","19446","GTGTTGTCCTCCGGGAAGCGGGCTCGGCGTGAACGAGGGCGGGCGCTGTTGCGGGTCGGGGCGGTGCTCAGGGGCTGTCGCCCCGTTTCCTACGCCGATCCGATAACGCGCGTTAGCGCCAGTATTAAACTACGCGGGCCCTCGACGTCGGGCAAGCACCCGGGGGTCATTCCCGATCAACATCGGGGACTTCTCAGGGTGCTCCCCGATAGCGGATGGCAGGCCCCAGCACCCAGACTGGTTGCCATGACGCAGCAGCAGTACCCCGGTCAGTTCAGCCAGTCCGCCCGCTCCGAGGGCGGGGGCGCCGCCTCCGGTCGGACGGGCGAGTTCTTCCGTTTCCGCGACTCCCTGCCCCGACGTTCCCGTGAGCACCGCATCCTCGGCGGCGTCTGCGGAGGCCTGGCCGAGGCCTGGAACATGCCCGTGACCGCGGTGCGCGTCGGGGTGATCCTGGCCAGCTTCCTGCCCGGCCCCATGTTCCTGGTCTACGTCGCGGCATGGTGCCTCATGCTCGACGAGCCCGCTCCCGCCCAGTACTGA","VLSSGKRARRERGRALLRVGAVLRGCRPVSYADPITRVSASIKLRGPSTSGKHPGVIPDQHRGLLRVLPDSGWQAPAPRLVAMTQQQYPGQFSQSARSEGGGAASGRTGEFFRFRDSLPRRSREHRILGGVCGGLAEAWNMPVTAVRVGVILASFLPGPMFLVYVAAWCLMLDEPAPAQY$","Phage shock protein C, PspC","Membrane, Extracellular","PspC domain family","hypothetical protein predicted by Glimmer/Critica","PspC domain protein","","","","","

InterPro
IPR007168
Domain

PspC
PF04024	$\"[116-176]T$	PspC

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[148-168]?$	transmembrane_regions

","BeTs to 5 clades of COG1983COG name: Putative stress-responsive transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription] Functional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1983 is ----k---v--lb-e-g---------Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 116 to 176 (E_value = 1.4e-14) place ANA_2012 in the PspC family which is described as PspC domain.","","domain family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2013","2182773","2185604","2832","5.46","-20.41","99353","ATGAGTCGGACCGCCCGAGCACTCAGCGCCCTGACCGCCTTCTGCCTGCTGGCAGCCGCCTCTACGCTGACCTCCGTGCCCGCAGCCGCCTCCGGCCAGGCCCGACCGGCCTCCACCGCGCCGAACGCACCAGCCGCACCGACGGCCCCGAAGGCCGACCAGTCCGGCGAGCGGTGGCGCCCGCAGAGCCACTACACTCCCCAGAAGAACTGGATGAACGACCCCAACGGGCTCGTCTACTACGACGGCGAGTACCACATGTTCTACCAGTACAACCCCGAGGGCTCGGACTGGGGCAACATGTCCTGGGGCCACGCCGTCTCCAAGGACCTGGTCCACTGGCAGGAGCTGGGGGTGGCGATCCCGCACACCTCGCAGTACGGGGTGTTCTCCGGATCGGCGGTCATCGACACCAAGAACACCTCCGGCCTGGGCAGCCCGGACAACCCGGCGATGGTCGCGGTGTGGACGCGGGCCGACGTCGGCGGCAACCAGTCCCAGTCCCTGGCCTACTCCACGGACAAGGGCCGCACCTGGAACCTGTACAACAACGGTGACCCGGTCCTCGACATCGGCTCCAAGGAGTTCCGCGACCCGAAGGTCTTCTGGGACCAGACCTCCGGGCGCTGGACGATGGTGGTCTCCCACGCCACCGAGCACCGCGTCTCCTTCTACTCCTCCCCCGACCTCATCCACTGGACCGAGCAGTCCAGCTTCGGCGGGGAGGGCATCACCTCGGCGGTGTGGGAGTGCCCGGACTTCTTCCCGCTGCCGGTCGACGGCAGCTCCCAGGAGGTCAAGTGGGTCCTGGTAGTCACGGTGGCCGACTCGGCCCAGTACTTCGTGGGCAGCTGGGACGGCACCACCTTCACCCCCGACGCAATCCCCCACTACAGCGGTGAGGAGGGCACGACCCTGGCCGACTTCGAGAACGGCTACGCCGGCTGGAAGGCCGACGGCGCCGCCTTCGGCTCGGGCCCGGCCACCGGGGACCTGCCCGGACACCAGGGCAAGGCCTACGTGGACTCCTTCGGCAGCGGCGACGCCGACACCGGCACGCTGACCTCGGATGAGTTCACGGTCTCCTCGTCCTACATCAACCTGCGCACCGCCGGAGGCAAGCACCCCTACAACCCGCAGGCCACCGGCGACAACGGCGGCGGCAGGCTCCTGGCCGGCTTCGACGGCTCCTGGGAGGGCTGGACCGTGGAGGGCAGTGCCTTCGCGGCCACGCCCCCTCAGGGCGCCACCCCCGGCCAGCAGCCGCTGGTCAACCACTCCAGCGCCGGGCTGCTCAACACCTATCTCGACGCCGCCACCGGGCAGGGCTCTGACGCCCCCACCGGCACCGCCACCTCGCCGACCTTCACCATCGACTCCGCCTACCTCAACCTCCTCATGGGCGGCGGCAACAACCCCCGCCCCGAGGGCGGCGCCGACGGGGGCTCCAGGGTGAGCGTCGTCGAGCTGATCGTTGACGGCAAGGTGGTGCGCTCGGCCACCGGCCGCAACCTGGAGGAGCTCAACTGGCAGAGCTGGGACGTCAGCGACCTCAAGGGCAAGTCCGCCCAGATCGTCGTCACCGACACGGCCACCGGAGGCTGGGGACACATCCTCCTGGACGAGGTGCGCGCCTCGGACAAGAAGGCCTCCCCCATCGCAGACAACACCTCCGTCAACCTCGTCGTGGACGGAAAGGTCGTCGCCTCCGCCACCGGCAACAACTCCGGGACCCTGGAGTGGACGAGCATGAACGTGGCGGCCTACAAGGGCCGCAAGGCCCGCCTCGTCATCGAGGACCGCAACGGCAACGCCGAGGACTGGGGCCACCTCATGGTCGACCAGATCCTCCAGTCGGACACCAAGGCCTTCTCCGGGGCCGACGTCGTCCCGCGCCTGGACTACGGCAAGGACTACTACGCGGCCGTCACGTGGGACAACGTCCCCAACGGCAAGCGCTACCAGGTGGGCTGGATGAGCAACTGGGCCTACGTGCGCGACCTGCCCACCACCACCTGGCGCACCGCCATGTCCACGGTGCGCGAGATGGGACTGACCCGGGTGAACGGCACGCTGCGCCTGACCGCCCAGCCCGTCACCGCCCTGGAGTCCCTGCGCACCGGCCAGGAACTCACCCGGAAGGACACCGACATCCCGGTGGGCGAGACCTCTCTGGGCAAGGCCGCTCAGGGCACCTCCCTGGACATCAGCGTGGACCTGAGCCCCAGCGCCTCCTCCTTCGCCGGTCTCAAGGTCCTCGATAACGGCGAGCAGTACACGCTCATCGGCTACGACTCCCAGGCCAAGCAGCTCGTCGTGGACCGCACCCACTCCGGGGTCACCGACTTCTCCCCGAAGTTCCCGGCCCGGTCCACCGCACCCCTGTCACCGGACAGCAAGGGACAGGTCCACCTGCGCATCATTGTTGACGCCCACTCCGTGGAGGTCTTCGCGGCCGACGGCACTCCTGTCATCACCCAGACCGTCTACCCCGAACAGGACGCCACGGGGGTCTCACTCTACGCCGAGGGCGGCACGGCGCATCTGGGTTCCCTGAGCCTGTGGCACCTGGGTTCCGTCCAGGACGCCGGCGCCCCGGCCGAGGGCCCCGACTCCCCCGGGGCCGGCAAGCCCGCCGTCCAGGGGCCGGCCCGTGGCCAGGCGAAGGCGGCATCGGCGTCGGCGAGCCCCACCGCCGCTGCGGCCGGTAAGAGCGTCTCCGCCCGCTTCCCGCTGGCCCGCACCGGCACCTCCCTGACCCTGGGCGCCCTGGGGGCGGCCGCCGCCGCGACCGGCGCCTACGCACTGCGCCTACGCCGTCGGCGCTCCTGA","MSRTARALSALTAFCLLAAASTLTSVPAAASGQARPASTAPNAPAAPTAPKADQSGERWRPQSHYTPQKNWMNDPNGLVYYDGEYHMFYQYNPEGSDWGNMSWGHAVSKDLVHWQELGVAIPHTSQYGVFSGSAVIDTKNTSGLGSPDNPAMVAVWTRADVGGNQSQSLAYSTDKGRTWNLYNNGDPVLDIGSKEFRDPKVFWDQTSGRWTMVVSHATEHRVSFYSSPDLIHWTEQSSFGGEGITSAVWECPDFFPLPVDGSSQEVKWVLVVTVADSAQYFVGSWDGTTFTPDAIPHYSGEEGTTLADFENGYAGWKADGAAFGSGPATGDLPGHQGKAYVDSFGSGDADTGTLTSDEFTVSSSYINLRTAGGKHPYNPQATGDNGGGRLLAGFDGSWEGWTVEGSAFAATPPQGATPGQQPLVNHSSAGLLNTYLDAATGQGSDAPTGTATSPTFTIDSAYLNLLMGGGNNPRPEGGADGGSRVSVVELIVDGKVVRSATGRNLEELNWQSWDVSDLKGKSAQIVVTDTATGGWGHILLDEVRASDKKASPIADNTSVNLVVDGKVVASATGNNSGTLEWTSMNVAAYKGRKARLVIEDRNGNAEDWGHLMVDQILQSDTKAFSGADVVPRLDYGKDYYAAVTWDNVPNGKRYQVGWMSNWAYVRDLPTTTWRTAMSTVREMGLTRVNGTLRLTAQPVTALESLRTGQELTRKDTDIPVGETSLGKAAQGTSLDISVDLSPSASSFAGLKVLDNGEQYTLIGYDSQAKQLVVDRTHSGVTDFSPKFPARSTAPLSPDSKGQVHLRIIVDAHSVEVFAADGTPVITQTVYPEQDATGVSLYAEGGTAHLGSLSLWHLGSVQDAGAPAEGPDSPGAGKPAVQGPARGQAKAASASASPTAAAAGKSVSARFPLARTGTSLTLGALGAAAAATGAYALRLRRRRS$","Levanase","Extracellular, Cellwall","sucrase/fructanase precursor","levanase ","Levanase","Norman JM, Bunny KL, Giffard PM.Characterization of levJ, a sucrase/fructanase-encoding gene from Actinomyces naeslundii T14V, and comparison of its product with other sucrose-cleaving enzymes.Gene. 1995 Jan;152(1):93-8.PMID: 7828936","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR001362
Family

Glycoside hydrolase, family 32
SM00640	$\"[64-821]T$	Glyco_32
PS00609	$\"[64-77]T$	GLYCOSYL_HYDROL_F32

InterPro
IPR013148
Domain

Glycosyl hydrolases family 32, N-terminal
PF00251	$\"[64-327]T$ $\"[620-698]T$	Glyco_hydro_32N

InterPro
IPR013189
Domain

Glycosyl hydrolase family 32, C-terminal
PF08244	$\"[736-821]T$	Glyco_hydro_32C

noIPR
unintegrated

unintegrated
G3DSA:2.60.120.560	$\"[703-862]T$	no description
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[916-936]?$	transmembrane_regions

","BeTs to 5 clades of COG1621COG name: Beta-fructosidases (levanase/invertase)Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1621 is ------y-v--lb-e-gh--------Number of proteins in this genome belonging to this COG is 5","***** IPB001362 (Glycoside hydrolase, family 32) with a combined E-value of 1.7e-20. IPB001362 63-91***** IPB013148 (Glycosyl hydrolases family 32, N terminal) with a combined E-value of 1.9e-10. IPB013148A 636-651 IPB013148B 805-831","","","-55% similar to PDB:1Y4W Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21 (E_value = 1.2E_60);-55% similar to PDB:1Y9G Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose (E_value = 1.2E_60);-55% similar to PDB:1Y9M Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 (E_value = 1.2E_60);-57% similar to PDB:1UYP THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA (E_value = 1.6E_33);-57% similar to PDB:1W2T BETA-FRUCTOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH RAFFINOSE (E_value = 3.7E_33);","Residues 64 to 327 (E_value = 7.8e-81) place ANA_2013 in the Glyco_hydro_32N family which is described as Glycosyl hydrolases family 32 N terminal.Residues 620 to 698 (E_value = 3.7e-18) place ANA_2013 in the Glyco_hydro_32N family which is described as Glycosyl hydrolases family 32 N terminal.Residues 736 to 821 (E_value = 6.3e-21) place ANA_2013 in the Glyco_hydro_32C family which is described as Glycosyl hydrolases family 32 C terminal.","","precursor ","","1","","","","","","","","","","","","Thu Jul 26 15:11:13 2007","","","","Thu Jul 26 15:11:13 2007","Thu Jul 26 15:11:13 2007","","","Thu Jul 26 15:11:13 2007","Thu Jul 26 15:11:13 2007","","","","","yes","","" "ANA_2014","2186821","2185811","1011","5.80","-7.02","36033","GTGGGCGACACCTACAGGACCACGATGGCGGACGTGGCCAAGGCGGCCGGCGTCTCGCGCACCACGGTGTCCTTCGTGCTCAACAACCGCGACGGCGCTCGGATCCCACCGCAGACCCGTGAGCGCGTCCAGCAGGTGGCTGCCGAGCTCGGCTACCGCCCGCACGGTGGGGCACGGGCCCTGGCTTCGCGCCGGTCCTCGCTCATCGGCCTGGTCTCCGAGATCGTCACCAGTCCCTTTGCCGCCGCCACGATCCGCGGGATCCAGGACACTGTCCGGGCCGCCGGCTACACGCTGTTCATCGTGCCGACCTCGACGGAGGCCACTGTGGAGGCCGAGGCCTTCGAGACGCTGCTGAAGTCCCGGGTCGAGGGGATCATCTACGCCACCGGGTGGAACTGCCGGGTTCGCATGCCGGCGCAGGCCCGCGAGATCCCCACCGTCCTGGTCCACTGCATCGACCCGGTCTCCGGCCTTCCCTGCGTGCGCCCCGACGAGGAGCAGATGGGGCGCCTGACCGCGCAGGCGCTCTTGGAGGGCCATCACCGCGACATCGGTGTCATCGAGCTCGACCCCAACGACGGTGAGGCCGCCCCGGGGCGGCGTATCGGCTGCCGGACCTACCTGGAGCAGGCCGGCATCCCCTGGAGCACCGTGCACGTGGCCGTCGGTCACGGCACCACCCGGGACGGGTACGCGGCCGCCTCCCGCCTGCTGACGGACCATCCCTGGCTGACCGGGCTGGTGTGCGGCAACGACTGCATGGCGATGGGCGCCTATGCCGCGATCCGTGAGCAGGGGCTGCGAGTGCGCGAGGACGTGGCCGTCATCGGGATCGACGACCAGGAGCTCATCGCGGATCAGGTCCATCCGGCCCTGACGACGGTCGCGCTGCCCTTCGAGGAGATGGGCCAGGTGGCCGTCTCCCACCTGCTGGCCCTCATGGAGGGCGAGGAGGTGCCCGCTGAGACGCTCCTGCCGGGCACGATCATCCGTCGCTCCTCGGCCTGA","VGDTYRTTMADVAKAAGVSRTTVSFVLNNRDGARIPPQTRERVQQVAAELGYRPHGGARALASRRSSLIGLVSEIVTSPFAAATIRGIQDTVRAAGYTLFIVPTSTEATVEAEAFETLLKSRVEGIIYATGWNCRVRMPAQAREIPTVLVHCIDPVSGLPCVRPDEEQMGRLTAQALLEGHHRDIGVIELDPNDGEAAPGRRIGCRTYLEQAGIPWSTVHVAVGHGTTRDGYAAASRLLTDHPWLTGLVCGNDCMAMGAYAAIREQGLRVREDVAVIGIDDQELIADQVHPALTTVALPFEEMGQVAVSHLLALMEGEEVPAETLLPGTIIRRSSA$","Transcriptional regulator, LacI family","Cytoplasm","transcriptional regulator, LacI (ribose operonrepressor) family","transcriptional regulator; LacI family","periplasmic binding protein/LacI transcriptional regulator","","Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 1992. 267(22):15869-15874. PMID: 1639817Vartak N.B., Reizer J., Reizer A., Gripp J.T., Groisman E.A., Wu L.F., Tomich J.M., Saier Jr M.H. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 1991. 142(9):951-963. PMID: 1805309","","","

InterPro
IPR000843
Domain

Bacterial regulatory protein, LacI
PF00356	$\"[7-32]T$	LacI
SM00354	$\"[6-78]T$	HTH_LACI
PS50932	$\"[7-63]T$	HTH_LACI_2
PS00356	$\"[9-27]T$	HTH_LACI_1

InterPro
IPR001761
Domain

Periplasmic binding protein/LacI transcriptional regulator
PF00532	$\"[66-334]T$	Peripla_BP_1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[7-70]T$	no description
G3DSA:3.40.50.2300	$\"[165-305]T$	no description

InterPro
IPR005833
Family

Haloacid dehydrogenase/epoxide hydrolase
PR00413	$\"[11-22]T$ $\"[139-155]T$ $\"[157-177]T$ $\"[184-197]T$	HADHALOGNASE

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[11-198]T$	Hydrolase

InterPro
IPR006402
Domain

HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509	$\"[13-195]T$	HAD-SF-IA-v3: HAD-superfamily hydrolase, su

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[6-220]T$	no description
PTHR18901	$\"[8-195]T$	2-DEOXYGLUCOSE-6-PHOSPHATE PHOSPHATASE 2

","BeTs to 10 clades of COG0637COG name: Predicted phosphatase/phosphohexomutaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0637 is ----k-y-vdrlbcefghsn-j-i--Number of proteins in this genome belonging to this COG is 1","***** IPB005833 (Haloacid dehalogenase/epoxide hydrolase family signature) with a combined E-value of 2.8e-16. IPB005833A 11-22 IPB005833E 139-155 IPB005833F 157-177","","","-47% similar to PDB:1TE2 Putative Phosphatase Ynic from Escherichia coli K12 (E_value = 3.8E_18);-48% similar to PDB:2HDO Crystal structure of putative phosphoglycolate phosphatase (np_784602.1) from Lactobacillus plantarum at 1.50 A resolution (E_value = 8.4E_10);","Residues 11 to 198 (E_value = 7.7e-26) place ANA_2015 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","hydrolase (YniC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2016","2188659","2187856","804","5.19","-10.42","28784","ATGAACACTGTCAGTACCCCGACTTCGCCCCAAGCTGCCCCGGCTAGGCGGCGCGGACCCGGGCGCCCCCGAGCGGGCAGCGAGGACAAGCGAGCACGCATCCTCAATGAAGCCGTGGTTCTCTTCGGAGAGCACGGGTATGCCGGCACCTCCCTGGCCGACATCGCCAACGCGGCAGACATTTCCAAGGCCGGGCTCCTGCACCACTTCTCCTCCAAGGACGAGCTCTTCTGCAAGGTGCTGGAGCGCCGTGACCGCGAGGACGCCCTGAGCATTCTCGTTGAGTCCCCGGCCGTTGAGGGCGACGCCGCCGCGGCCCCCGTTGACACCGTCGGCAACCTGGACACCCTCGACGTCGCGGGTGTCTCCGACCTGGACGGCAACCCTTGGGCCCTGCTGGAGCGCTACATCGAGCTGCTCGAGCGCAACGTCGCCCACCGGGACCTCACGGCGATCTACACCGCGACGGCAGTCTCGGTCCTCGACGCCGAGCACCCTGCGCACCGGTGGATGGCCAACCACCTCAACAGCGCCGTCGAGCGCTTCGAGTCCAGCTTCGAGGCCGGTAAGACCGCCGGGATCGTGGACCCGCAGATGCCTTCGCGCCTCGTGGCTCGCAGCCTGGTCGCCCTCATCGACGGTCTGCAGCTGCAGTGGCTGTGCTCGACGACGCCCGGGACGGCCGCCTCGGAGGCCCTGTCCACCGACCTGGTGGCGGAGATCCGCCTCTACGCCGACTGCCTGCGCAGCCAGTGGGAGGTCCAGGAGACCCCGGAGACCCCTCAGCGGCCCAAGGCGGCCTGA","MNTVSTPTSPQAAPARRRGPGRPRAGSEDKRARILNEAVVLFGEHGYAGTSLADIANAADISKAGLLHHFSSKDELFCKVLERRDREDALSILVESPAVEGDAAAAPVDTVGNLDTLDVAGVSDLDGNPWALLERYIELLERNVAHRDLTAIYTATAVSVLDAEHPAHRWMANHLNSAVERFESSFEAGKTAGIVDPQMPSRLVARSLVALIDGLQLQWLCSTTPGTAASEALSTDLVAEIRLYADCLRSQWEVQETPETPQRPKAA$","Transcriptional regulator, TetR family","Cytoplasm","transcriptional regulator, TetR family","transcriptional regulator; TetR family","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[34-47]T$ $\"[55-78]T$	HTHTETR
PF00440	$\"[34-77]T$	TetR_N
PS50977	$\"[28-88]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[12-80]T$	no description

InterPro
IPR013188
Domain

Influenza matrix M1, C-terminal
SM00759	$\"[164-256]T$	no description

","BeTs to 17 clades of COG1309COG name: Transcriptional regulators, AcrR familyFunctional Class: KThe phylogenetic pattern of COG1309 is a-T--QVCEBRH---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 52 to 98 (E_value = 1.1e-15) place ANA_2016 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator, TetR family","","1","","","Tue Aug 7 18:07:16 2007","","Tue Aug 7 18:07:16 2007","","","Tue Aug 7 18:07:16 2007","Tue Aug 7 18:07:16 2007","Tue Aug 7 18:07:16 2007","","","Tue Aug 7 18:07:16 2007","","","Tue Aug 7 18:07:16 2007","Tue Aug 7 18:07:16 2007","","","Tue Aug 7 18:07:16 2007","Tue Aug 7 18:07:16 2007","","","","","yes","","" "ANA_2017","2189044","2189673","630","7.24","0.82","22553","ATGCATGCACATGCACGCTCGGTGCATTACACTTGTTCCATGACTGTTCTTGCCGGCCTGCTCGACCACCTCGACCTCAGCGACGAGGAGCTCGCGGACGCGATGCGCGAGGCCACTGCCCGCACGTCGCAGGGCGGCGTCGGCCCGGTGTCCGCCGGCATGACCGACTTCCTGGCTCGAACCACCCCTCGCAGCCACAGCAAGTCCACAGCCCGCACAGTGGAGCGCGTCCTGTCCGATCGCACGTACGCCGAGCAGCTCACCGCCCAGCATGAGGCCGTCCAGGCGGCCTGCACGCTGGCGCGCTCTCTGAGTACCCGCCAGGTCGCCACCCTGCTCAGCCGGACAACGACGACGATCACCCGCGCGGCCGGGCGCACCCTCTACGCCTACCGCGAGGGGCGGTCGCTGAGATTCCCCACGTGGCAGTTCCATGAGGGCCGCCCGATCCCGGGCCTGGCAACGGTGGTGCCCGCCCTGCGCGAGGGGCTGACGCCGGCCACCATCGAGGCGCGGATGACGACGTCGGATCCCGAGCTGCTCGACGGGGCGTCACCCGCACAGTGGCTGATCGCCGGCGGGGACCCGGCGGCGGTCGTCCAGCAGTTCTCGGATGCGGACCACCGGTGA","MHAHARSVHYTCSMTVLAGLLDHLDLSDEELADAMREATARTSQGGVGPVSAGMTDFLARTTPRSHSKSTARTVERVLSDRTYAEQLTAQHEAVQAACTLARSLSTRQVATLLSRTTTTITRAAGRTLYAYREGRSLRFPTWQFHEGRPIPGLATVVPALREGLTPATIEARMTTSDPELLDGASPAQWLIAGGDPAAVVQQFSDADHR$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Skarstad K., Boye E. The initiator protein DnaA: evolution, properties and function. Biochim. Biophys. Acta 1994. 1217(2):111-130. PMID: 8110826Yoshikawa H., Ogasawara N. Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial replication origins. Mol. Microbiol. 1991. 5(11):2589-2597. PMID: 1779750Georgopoulos C. The E. coli dnaA initiation protein: a protein for all seasons. Trends Genet. 1989. 5(10):319-321. PMID: 2558436Skovgaard O. Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli. Gene 1990. 93(1):27-34. PMID: 2172087","","","

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[70-127]T$	no description

InterPro
IPR014914
Family

RES
PF08808	$\"[46-182]T$	RES

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 46 to 182 (E_value = 1.6e-08) place ANA_2018 in the RES family which is described as RES domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2019","2190385","2191416","1032","10.53","15.00","36118","ATGCGTCCCTCGACCCCGCAGCCGCCGCGGCGCCCCTCCCGCCCCGGCCGCGCCTCGTCGTCGGCGTCCGGACGCCGTCGAACGTCCGCCGGTCATCGACGCAGCCCTGGGGGCCGGCCCTCCCCGCAGCGTCCTTCGTCGGACGCCCCCGATCCCGCCAGCCGGCGAGCCCTCACCATCGCCCGCCGGGAGCAGCGTCGGCGTCGCACCCGCAACCGGCTCCTGTACAGCACGACCTTCGTCGTGGCGCTGGCCCTGATCGTCATCGGACTGCGAGCCTGGGGGCTCCACCCCGGTTTCGCCCTGCCGCTGAGCTCCTCCGCAAGCCGGTCCTCAACCCCGGCCAAGGCCGCCGCCCAGTCCTCCGCCCGGGCGTCCGCCAGCCGCGCGGCCTCGCCGTCAGCCTCGGCCGCCCCCTCCGCCTCATCGACGCCGTCGGCCTCGGCGCTGCCGTCCCCACAGCTGGACTCCGAGGGCTTCGCGCACTCCGGCGCCGTCGGCAACGGCAGCTGGACTATCGCACCGGCCGTGCCCGTCTCCCGGCCCGCGGCCGCCACCGTCTACCGCTACGTGCTGCGGGTCGAGGGCGGCACGCATGTCGACGCCGCAGCCGCGGCCCCCATCGTGGAGCGCATCCTCAATGACGAGCGCGGCTGGCCCACCGCGCAGAACACGTCCTTCCAGCCCGTGGCCGACCCCGCGAGCGCGGACTTCACCTTCAACATCGCCACGCCACCCAGCGCCGACGCCCTGTGCTCACCGCTGGACACCGGCGGCATGTGGAGCTGCCGCAACGGGGACAACGTGGTCATCAACTCCGACCGGTGGAACTGGGGCGCCGTGACCTACCCCGACGTCGACTCCTACCGCACCTACGTCACCAACCACGAGGTGGGCCACTTCCTCGGCCACGAGCACGAGTTCTGCGCCGGGGCCGGCCTCAAGGCCCCACTCATGGCTCAGCAGAGCCACGACCTGGCCGGCGGCTGCGTCTACAACGCCTGGCCCACCCAGGACAACCAGCCCGGCTGA","MRPSTPQPPRRPSRPGRASSSASGRRRTSAGHRRSPGGRPSPQRPSSDAPDPASRRALTIARREQRRRRTRNRLLYSTTFVVALALIVIGLRAWGLHPGFALPLSSSASRSSTPAKAAAQSSARASASRAASPSASAAPSASSTPSASALPSPQLDSEGFAHSGAVGNGSWTIAPAVPVSRPAAATVYRYVLRVEGGTHVDAAAAAPIVERILNDERGWPTAQNTSFQPVADPASADFTFNIATPPSADALCSPLDTGGMWSCRNGDNVVINSDRWNWGAVTYPDVDSYRTYVTNHEVGHFLGHEHEFCAGAGLKAPLMAQQSHDLAGGCVYNAWPTQDNQPG$","Hypothetical protein","Extracellular","putative membrane protein.","hypothetical protein","hypothetical protein","","Novoseler M., Hershkovits G., Katcoff D.J. Functional domains of the yeast chromatin protein Sin1p/Spt2p can bind four-way junction and crossing DNA structures. J. Biol. Chem. 2005. 280(7):5169-5177. PMID: 15563464","","","

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[8-77]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[74-94]?$	transmembrane_regions

InterPro
IPR001270
Family

Chaperonin clpA/B
PR00300	$\"[621-639]T$ $\"[666-684]T$ $\"[695-713]T$ $\"[728-742]T$	CLPPROTEASEA
PS00870	$\"[303-315]T$	CLPAB_1
PS00871	$\"[651-669]T$	CLPAB_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[206-352]T$ $\"[617-785]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[209-404]T$	AAA

InterPro
IPR004176
Domain

Clp, N-terminal
PF02861	$\"[16-67]T$ $\"[97-153]T$	Clp_N

InterPro
IPR013093
Domain

ATPase AAA-2
PF07724	$\"[616-778]T$	AAA_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.60	$\"[784-889]T$	no description
G3DSA:3.40.50.300	$\"[165-360]T$ $\"[569-783]T$	no description
PTHR11638	$\"[1-411]T$ $\"[474-718]T$	ATP-DEPENDENT CLP PROTEASE
PTHR11638:SF18	$\"[1-411]T$ $\"[474-718]T$	CHAPERONE CLPB

","BeTs to 20 clades of COG0542COG name: ATPases with chaperone activity, ATP-binding subunitFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0542 is --m---yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001270 (Chaperonin clpA/B) with a combined E-value of 0. IPB001270A 185-237 IPB001270B 281-295 IPB001270C 305-359 IPB001270D 370-411 IPB001270E 582-632 IPB001270F 636-685 IPB001270G 686-739 IPB001270H 767-781 IPB001270I 807-852 IPB001270C 306-360***** IPB013093 (ATPase AAA-2) with a combined E-value of 6.3e-241. IPB013093A 169-205 IPB013093B 207-228 IPB013093C 248-268 IPB013093D 282-295 IPB013093E 303-343 IPB013093F 366-406 IPB013093G 617-639 IPB013093H 651-701 IPB013093I 704-741 IPB013093B 618-639 IPB013093G 206-228 IPB013093H 652-702***** IPB001943 (UvrB/UvrC protein) with a combined E-value of 7.8e-45. IPB001943A 212-221 IPB001943B 354-381 IPB001943C 618-629 IPB001943D 656-672 IPB001943E 702-743","","","-86% similar to PDB:1JBK Crystal Structure of the First Nucelotide Binding Domain of ClpB (E_value = 2.3E_77);-89% similar to PDB:2P65 Crystal Structure of the first nucleotide binding domain of chaperone ClpB1, putative, (Pv089580) from Plasmodium Vivax (E_value = 4.3E_76);-67% similar to PDB:1KSF Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains (E_value = 5.9E_73);-67% similar to PDB:1R6B High resolution crystal structure of ClpA (E_value = 5.9E_73);","Residues 16 to 67 (E_value = 1.2e-06) place ANA_2020 in the Clp_N family which is described as Clp amino terminal domain.Residues 97 to 153 (E_value = 3.5e-11) place ANA_2020 in the Clp_N family which is described as Clp amino terminal domain.Residues 209 to 404 (E_value = 1.5e-15) place ANA_2020 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).Residues 616 to 778 (E_value = 1.2e-105) place ANA_2020 in the AAA_2 family which is described as ATPase family associated with various cellular activities (AAA).Residues 620 to 783 (E_value = 8.8e-07) place ANA_2020 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).","","of ClpA-ClpB type (ClpB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2021","2192167","2194341","2175","4.65","-64.31","70474","GTGGGCCTTCTCGACCTCGTCGAGCAGGACCACGGAGTAGGGCCGACGCCGCACGGCCTCAGTGAGCTGGCCGCCCTCCTCGTAGCCGACGTACCCGGGAGGGGCACCCACAAGGCGCGCCACAGAGTGCTTCTCGGAGTACTCGGACATGTCGATACGCACGATGGCACGCTCGTCGTCGAAGAGGAACTCGGCCAGGGCCTTGGCCAGCTCGGTCTTGCCCACGCCCGTGGGGCCCAGGAAGAGGAAGGAGCCGGTGGGGCGGTCGGGGTCGGAGATGCCGGCCCGCGAGCGGCGCACCGCGTCGGCCACGGCGGCCACGGCGGCCTTCTGACCGATGAGGCGCTCGCCGATGACGTCCTCCATGGTCAGGAGCTTCTCGGTCTCCCCCTGGAGGAGCTTGCCCACGGGGATGCCGGTCCAGGCCCCCACGACCTCGGCGATCTCGGGGGCGCCGACCTGCTCGGCGATCATCGGCTCGCCTGCCGCCTGCTCGGCAGCGTCGTCGGCGGCCTCGGCCTCGCGGATCTGGCGCTCCAGGGCGGGCATGTCGCCGTAGCGCAGGCGACCGGCCTCCTCGAAGTTGCCCTCGCGCTCGGCCAGGTCGGCGCGGGTGCGCATCTCGTCCAGGGCGGCGCGCAGCTCACCGACCTTGTTGTGGCCAGCCTTCTCGGCCTCCCAGCGGGCGTTGAGCGAGGCCAGCTCCTCGGAGGCGTCGGCCAGCTCGGCGCGCAGGCGCTCGAGGCGCTCGACGTCAGCCGGGTCGGCCTTGGAGACGTCCTCGATGGACTCATCCAGGTAGGCCTCCTCCATGCGCATGCGGTCCACGCGGCGGCGCAGCTCGTCGATCTCGACGGGGCTGGAGTCGAGCTCCATGCGCAGCCGGGAGGCGGCCTCATCGACCAGGTCGATGGCCTTATCGGGCAGCTGGCGACCGGTGATGTAGCGGTCGGAGAGGGTCGCGGCCGCCACGAGGGCACCGTCGGAGATGGTCACCTGGTGGTGGGCCTCGTACTTGGGGGCGATGCCGCGCAGGATGGCCACGGTGTCCTCGACACTGGGCTCACCGACGAAGACCTGCTGGAAGCGGCGCTCCAGGGCGGGGTCCTTCTCGATGTTCTCGCGGTACTCGTCCAGGGTGGTGGCGCCCACCATGCGCAGCTCGCCGCGAGCCAGCATGGGCTTGAGCATGTTGCCGGCGTCCATGGCGCCCTCGGAGCCGCCGCCGGCGCCGACGACGGTGTGCAGCTCGTCGATGAAGGTGATGACCTCGCCGTCGGAGTCCTTGATCTCCTTGAGGACGGCCTTGAGGCGCTCCTCGAACTCACCGCGGTACTTGGCGCCGGCCACCATCCCGGACAGGTCCAGGGAGATGAGGCGCTTGCCGCGCAGGGACTCCGGGACGTCGCCGGCGACGATGCGCTGGGCCAGGCCCTCGACGACGGCGGTCTTGCCCACGCCCGGCTCCCCGATGAGGACGGGGTTGTTCTTGGTGCGCCGGGACAGGACCTGCACGACGCGGCGGATCTCGGCGTCGCGGCCGATGACCGGGTCGAGCCGGCCCTCCCGGGCGGCCTCGGTGAGGTCGGTGCCGTACTTCTCGAGGGTCTTGTAGGTGCCCTCGGGGTTGGCGGAGGTGACGCGGGAGGAGCCTCGGACCTGGGGCAGGGCCTCGATGAGGGCCTCCGGGGTGGCACCGGCGTCGGCCAGGATGCGGGCCACGGTGGGGGCGGAGCCGGAGGTGTCGCCCTTGGCCAGGCCGATGAGCAGGTGCTCGGTGGAGATGTACTCGTCGGACAGCTCCTTGGCGACCGTCGAGGCGGCCTCGAGGGCGGCCAGCAGGGAGCGCGAGGGCTGAGGCTGGGTCATGGAGGAGCCCGAGGAGGCGGGCAGCTGGGTGAGGATGCGGCGCGCGGAGGCGCCGACGGCCTGGCGGGCCGCCGCATCGGGGCAGACTGCGGCCAGGAGTCCGGCGGCGACGCCGTCGGGCTGGGAGAGGAGCTCAACGAGCAGGTGCGCGGGCTCGATCTGGGGGTTGCCGGCCGCGGCGGCGGCCTGCATCGCCCCGGAGATCGCCTCCTGCGACTTGGTGGTGTAGTTGGTGTCCATGCGGATCTCCTTCGAGAGATGGTCACGTGTTGCGTCTTCTGGTCACCACAACCTTCGCAGAGTTGA","VGLLDLVEQDHGVGPTPHGLSELAALLVADVPGRGTHKARHRVLLGVLGHVDTHDGTLVVEEELGQGLGQLGLAHARGAQEEEGAGGAVGVGDAGPRAAHRVGHGGHGGLLTDEALADDVLHGQELLGLPLEELAHGDAGPGPHDLGDLGGADLLGDHRLACRLLGSVVGGLGLADLALQGGHVAVAQATGLLEVALALGQVGAGAHLVQGGAQLTDLVVASLLGLPAGVERGQLLGGVGQLGAQALEALDVSRVGLGDVLDGLIQVGLLHAHAVHAAAQLVDLDGAGVELHAQPGGGLIDQVDGLIGQLATGDVAVGEGRGRHEGTVGDGHLVVGLVLGGDAAQDGHGVLDTGLTDEDLLEAALQGGVLLDVLAVLVQGGGAHHAQLAASQHGLEHVAGVHGALGAAAGADDGVQLVDEGDDLAVGVLDLLEDGLEALLELTAVLGAGHHPGQVQGDEALAAQGLRDVAGDDALGQALDDGGLAHARLPDEDGVVLGAPGQDLHDAADLGVAADDRVEPALPGGLGEVGAVLLEGLVGALGVGGGDAGGASDLGQGLDEGLRGGTGVGQDAGHGGGGAGGVALGQADEQVLGGDVLVGQLLGDRRGGLEGGQQGARGLRLGHGGARGGGQLGEDAARGGADGLAGRRIGADCGQESGGDAVGLGEELNEQVRGLDLGVAGRGGGLHRPGDRLLRLGGVVGVHADLLREMVTCCVFWSPQPSQS$","Hypothetical protein","Cytoplasm, Extracellular","63 kDa protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","kDa protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2022","2194302","2195207","906","6.09","-2.94","30485","GTGTTGCGTCTTCTGGTCACCACAACCTTCGCAGAGTTGAGTCTATTCCACTCAACTTCTGGGACCAGCAGTGACGTGGGCTACTCCTTGAGATGCTGCCGCTGGAATTCCGCCGGTCGTCGCGCCGACCTGCAACATGCCAACCAACCGCTTGAAACACCGCTGTTCGACGACACCGCTATGGTCACGTCACGATCACGCCCTCACCCCGGAGACACCATGAGAACCACGCGCGCCACCCTGGCTCTGGCCACCATCCTCATCCTGGCGGGCTGCTCGCAGACCAGCCCCTCGTCGGCGGGCTCGGCCGCTGCGACAGCGACCGGCTCGACCCCCGCAGCCGCGGCGACTTCGTCGAGCGGGGGCGGCGCGAGCGCCTCCGGCAGCGCCGCCCCCTCCATCCCGGCGGGCCACCAGGCGGTCACCGCACCGACATCCGGCCTCACCTTCGCGATCCCCGAGGACTGGGAGGACCTCAATGCTCTTCCCGAGGCCCAGAAGGCGCTGCTCGCCCGGGCCCAGGGGGTGGATCCGTCCACCCTCACCCAGCGCCTGAGCAGCACCGACGCCTTCTACGGCCGGTTCTCGCAGAGCGGCGGCTTGTCCTTCAACAGCGTCGCGGTCGCCAAGGAGGCCGAGACCTCCTCCACGCCCCCGTCCCAGGCGAGCCTGGACGAGACCATCACCCGGCAGGGAGGCACGCCGACGGGCTACTCCACCAAGCCATCCACCTACGGGCAGGCCGCCGTCGACACCTCGACCGCACAGGTTCAGGGCGTCCAGACGGCCGGCGCGGTCATCGCCGTTCCGACGTCGTCGGGCACCTACGTGCGCATCGCCGTGACGGCCGGCAGCGACCAGGAGGTCAACACCATCGTGTCCACCATCCTCACGACCGCCCACTGA","VLRLLVTTTFAELSLFHSTSGTSSDVGYSLRCCRWNSAGRRADLQHANQPLETPLFDDTAMVTSRSRPHPGDTMRTTRATLALATILILAGCSQTSPSSAGSAAATATGSTPAAAATSSSGGGASASGSAAPSIPAGHQAVTAPTSGLTFAIPEDWEDLNALPEAQKALLARAQGVDPSTLTQRLSSTDAFYGRFSQSGGLSFNSVAVAKEAETSSTPPSQASLDETITRQGGTPTGYSTKPSTYGQAAVDTSTAQVQGVQTAGAVIAVPTSSGTYVRIAVTAGSDQEVNTIVSTILTTAH$","Hypothetical protein","Extracellular, Periplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide

noIPR
unintegrated

unintegrated
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-23]?$	signal-peptide

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[8-63]T$	HTH_3
SM00530	$\"[7-63]T$	HTH_XRE
PS50943	$\"[8-63]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[7-65]T$	no description
signalp	$\"[1-22]?$	signal-peptide

","BeTs to 3 clades of COG3655COG name: Predicted transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG3655 is ------------b--f-----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 63 (E_value = 4.9e-06) place ANA_2026 in the HTH_3 family which is described as Helix-turn-helix.","","regulator homolog yozG (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2027","2197502","2198131","630","9.85","6.61","22715","GTGCGGCCGGGGACTTTCTCGTGCGGCCGGGGGCATTCGACGCCGTCGGGGACAGCAATCCCGTCCCCGCACGCGCAGGATGTCCCCGGCCGGAAATTTCCGCACCCGGCCGCGCGGAATGTCCCCCGCCGCAGCGAGACCGTAGGCTCGACGTCGATGACCACACCGCTCCGCCGCAGCCCTCGCCCCGACGGGTCCTCCACGCGCGTCGGCAAGGCCACCGTGGCTGCCCGGCGCGACGAGCTCCTGGCCACGGCGGCCACGCTGCCTGGCGCCTGGGCGGGGAACAAGCCCGAGTGGGACATCCCCGTGGCCTCAGTGGGCCCCCGCCTCTTCCTGCTGCTCATCCCCCACACCGACGGCCGCCTCCTGGCCAACGTCAAGCTCGACCCCGAGGACGTCGTCGCCGTGCGGGCCACCTTCGAGTGGGTGGAGCCGGGCTTTCACCAGTCCAAGCGGCACTGGGTGAGCATCGACCTCACCAGCCCCGACTACCGCGCGGACGAGGCCACCGCCATGGTCGAGGACTCCTACCGGCTCGTCCTGTCCCTCCTGACCCACCGCGTGCGCGAGGCCGTCCTGCTGGCCGACGCCGCAGGCTCCCCCGCCCGCCCCACCTGGCAATGGTGA","VRPGTFSCGRGHSTPSGTAIPSPHAQDVPGRKFPHPAARNVPRRSETVGSTSMTTPLRRSPRPDGSSTRVGKATVAARRDELLATAATLPGAWAGNKPEWDIPVASVGPRLFLLLIPHTDGRLLANVKLDPEDVVAVRATFEWVEPGFHQSKRHWVSIDLTSPDYRADEATAMVEDSYRLVLSLLTHRVREAVLLADAAGSPARPTWQW$","Uncharacterized conserved protein","Periplasm, Cytoplasm","Protein of unknown function (DUF419) family","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF419","","","","","

InterPro
IPR007351
Family

Protein of unknown function DUF419
PF04237	$\"[79-182]T$	DUF419

","BeTs to 3 clades of COG2315COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2315 is ---------d-lb-ef-----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 79 to 182 (E_value = 3.8e-10) place ANA_2027 in the DUF419 family which is described as Protein of unknown function (DUF419).","","of unknown function (DUF419) family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2028","2198296","2198634","339","9.00","2.18","11573","GTGCCCCTCCGGAGAGGGAGCCTCCCCTCCCGCGGAGTTCCCTCCCCCAGATCTGCGGCCAATCCAGCCTCAGATGACGCGGGTGCGCAAACCTGGCACTATTCAGCCGAGGCCGTCGTCATCCGACGTCTGGCCACCCGACGGAAGGAGACACAGATGGGACTTGATGACCTGGCGAAGAAGGCCGGTGACGCTCTCAGCTCCGACAAGGCCGAGGCGATCAGCGACAAGGCGCTGGACGCCGCAGCCGGTGCTGCCAAGAAGGCGACCGGCGGCAAGTACGACGACAAGATCGACGCCGCCCGCGACGCCGTCGACGGCAAGCTCGGCACGGAGTGA","VPLRRGSLPSRGVPSPRSAANPASDDAGAQTWHYSAEAVVIRRLATRRKETQMGLDDLAKKAGDALSSDKAEAISDKALDAAAGAAKKATGGKYDDKIDAARDAVDGKLGTE$","Hypothetical protein","Periplasm, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2029","2200109","2198856","1254","10.77","19.40","42786","ATGACGACGTCTACGCACCGGCGTGACCGGTCCGCGGCCGAGCGGGGCGGCCGCGCCCCGGCCCGGCGGATCCAGCGCTCGCGGCTGCGTCTGGCCGACGTGCTGCGTCTGGGAGGCACCGGCATCAGGGCCCGCCCCACCCGCGCCTTCCTGTCCGCACTGGGGATCGCCATCGGCATCGCCGCCATGATCTCGGTGGTGGGCATCTCGGCCTCCAGCCGCGCCCAGCTCTCCGCCCAGCTCGACTCCCTGGGGACGAACCTGCTGACGGCCACCGCCGGCCAGGACCTGTTCGGCAACTCCTCCTCCCTGCCGCAGGACAGCGTCGGCAAGGTCCGCCTCATCGACAACGTCCAGAGCGCCTCGAGCACAGGGCTGGTCAAGAACTCGCTGGTTTACCGCACTCCGCTCATCGACAAGAACGCCTCTGGCGGCATCACCACCCTGGCCGCGGACAAGTCACTGCTCGACGTCGTGGCCGGACAGGTGGACAAGGGCACCTGGCTCAACGAGGCCACCAGCAAGTACCCGGCAACGGTCCTGGGGCAGACGGCGGCCCAGCGCCTCGGCGTCGTCTCACCGGGAACCAAGGTGTGGCTCGGCGGGAACTGGTTCACGGTGGTCGGCATCCTCAAGCCGGTGGTGCTGGCGCCCGAGCTCAACAACGCCGCCCTCATCGGTCAGGGAGTGGCCAGCGACCTGCTGGGGTACGACGCCAAGCCGACGACGGTCTACACGCGCAGCCAGGACGCCGCCGTTCCCACGGTGCGCAAGCTGCTGGCGCCGTCGATCTCGCCGCAGGCCCCCAACGAGGTCAAGGTCTCGCGCCCCTCGGACGCGCTAGAGGCCAAGAACGCGGCCGACAAGGCCTTTACCGGTCTGCTGCTGGGCGTGGGCTCGATTGCCCTGCTCGTCGGCGGTATCGGGGTGGCCAATACGATGATCATCTCGGTGCTCGAGCGCCGTCGGGAGATCGGACTGAGGCGGTCCCTGGGGGCGATGCGCGGACACATCCTCGTGCAGTTCATGACCGAGGCGCTGCTGCTGGCCTCCCTGGGCGGTGCCCTGGGGTGCATCATCGGGATCGGGGTGACCGCCGGGATGTCGGCTGCCAACGGCTGGCCCTTCTCCCTGCCAGTGATCGCGGTCGTCGGTGGGCTGGGTGTCACCATCGCCATCGGCGCCCTGGCCGGCGTGTACCCGGCCGTTCGGGCCTCCCGCACTCCTCCGACCGCCGCGCTCAACGCGCAGTAG","MTTSTHRRDRSAAERGGRAPARRIQRSRLRLADVLRLGGTGIRARPTRAFLSALGIAIGIAAMISVVGISASSRAQLSAQLDSLGTNLLTATAGQDLFGNSSSLPQDSVGKVRLIDNVQSASSTGLVKNSLVYRTPLIDKNASGGITTLAADKSLLDVVAGQVDKGTWLNEATSKYPATVLGQTAAQRLGVVSPGTKVWLGGNWFTVVGILKPVVLAPELNNAALIGQGVASDLLGYDAKPTTVYTRSQDAAVPTVRKLLAPSISPQAPNEVKVSRPSDALEAKNAADKAFTGLLLGVGSIALLVGGIGVANTMIISVLERRREIGLRRSLGAMRGHILVQFMTEALLLASLGGALGCIIGIGVTAGMSAANGWPFSLPVIAVVGGLGVTIAIGALAGVYPAVRASRTPPTAALNAQ$","ABC-type transport system involved in lipoprotein release, permease component","Membrane, Extracellular","ABC transporter, ATP-binding protein","K02004","protein of unknown function DUF214","","Pugh E.L., Wakil S.J. Studies on the mechanism of fatty acid synthesis. XIV. The prosthetic group of acyl carrier protein and the mode of its attachment to the protein. J. Biol. Chem. 1965. 240(12):4727-4733. PMID: 5321311Wong H.C., Liu G., Zhang Y.M., Rock C.O., Zheng J. The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 2002. 277(18):15874-15880. PMID: 11825906","","","

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[241-410]T$	FtsX

InterPro
IPR006162
PTM

Phosphopantetheine attachment site
PS00012	$\"[78-93]?$	PHOSPHOPANTETHEINE

noIPR
unintegrated

unintegrated
tmhmm	$\"[49-69]?$ $\"[299-319]?$ $\"[348-370]?$ $\"[376-398]?$	transmembrane_regions

","BeTs to 17 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 241 to 410 (E_value = 4.2e-43) place ANA_2029 in the FtsX family which is described as Predicted permease.","","transporter, ATP-binding protein","","1","","","","","","","","","","","Tue Aug 14 16:49:41 2007","","Tue Aug 14 16:49:41 2007","","","Tue Aug 14 16:49:41 2007","","","","Tue Aug 14 16:49:41 2007","Tue Aug 14 16:49:41 2007","","","","","yes","","" "ANA_2030","2200797","2200084","714","6.35","-3.13","25232","ATGAGCCGCATCCTGTCCCTGCGCGACGTCAAGCGCACCTACGGGGAGCCGCCCGTGGCCGCCTGCGCCGGCGTGAGCCTGGAGATCGATTACGGCGAGTTCGTCGCCATCGTCGGCCCCTCCGGCTCGGGCAAGTCCACGCTCCTCAACCTCATCGGCACCCTGGACCGGCCCAGCTCCGGCACCGTCGAGATCGACGGCGTCGACGTCGGCTCCCTGTCCGACGCCAAGCTCTCGGCCCTGCGGGCCAGCCGCATCGGCTTCGTCTTCCAGCAGTTCCACCTGGCAGACGGCGTCAACGCGGTGGACAACGTCGCCGACGGCCTGCTCTACAGCGGGGTCCCCCGCTCCGAGCGGCGTCGGCGCGCCCGGGCCGCCCTGGAGCGCGTCGGCCTGGCCCACCGGCTCGACCACCGCCCCCACCAGATGAGCGGCGGCGAGCGCCAGCGCGTGGCCATCGCCCGGGCCGTCGTCGGCGAGCCCCCGCTGCTGCTGGCCGACGAGCCCACCGGGAACCTCGACTCCACCTCCGGGGCCTCGATCGTTGAGCTCCTCCACGAGCTCCACGCCCAAGGCACCACGATCATCGTCATCACCCACGACAACGAGCTGGCCGCCCAGCTCCCGAGGCAGATCGCCATCCGCGACGGCCGCATCGTGGGGGACTCAAGCCTGAAGGAGATCGTCCATGACGACGTCTACGCACCGGCGTGA","MSRILSLRDVKRTYGEPPVAACAGVSLEIDYGEFVAIVGPSGSGKSTLLNLIGTLDRPSSGTVEIDGVDVGSLSDAKLSALRASRIGFVFQQFHLADGVNAVDNVADGLLYSGVPRSERRRRARAALERVGLAHRLDHRPHQMSGGERQRVAIARAVVGEPPLLLADEPTGNLDSTSGASIVELLHELHAQGTTIIVITHDNELAAQLPRQIAIRDGRIVGDSSLKEIVHDDVYAPA$","ABC-type transport system involved in lipoprotein release, ATPase component","Cytoplasm, Membrane","ABC transporter, ATP-binding protein VC1568","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[142-185]T$	Q6ACK5_BBBBB_Q6ACK5;
PF00005	$\"[32-217]T$	ABC_tran
PS50893	$\"[5-235]T$	ABC_TRANSPORTER_2
PS00211	$\"[143-157]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[31-225]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-231]T$	no description
PTHR19222	$\"[5-231]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32	$\"[5-231]T$	ABC TRANSPORTER

InterPro
IPR002477
Domain

Peptidoglycan-binding domain 1
PF01471	$\"[172-218]T$	PG_binding_1

noIPR
unintegrated

unintegrated
tmhmm	$\"[54-74]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","Residues 172 to 230 (E_value = 0.0014) place ANA_2031 in the PG_binding_1 family which is described as Putative peptidoglycan binding domain.","","","","1","","Wed Aug 8 09:50:11 2007","Wed Aug 15 17:27:42 2007","Wed Aug 8 09:50:11 2007","Wed Aug 15 17:27:42 2007","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","Wed Aug 15 17:27:42 2007","Wed Aug 15 17:27:42 2007","Wed Aug 15 17:27:42 2007","Wed Aug 15 17:34:15 2007","","","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","Wed Aug 8 09:50:11 2007","","Wed Aug 8 09:50:11 2007","","Wed Aug 8 09:50:11 2007","yes","","" "ANA_2032","2202518","2202051","468","4.83","-6.26","16179","ATGAAGCAGCCCCTCAACACCCGGATCCTCACCCGCGCCGCCACCGTGCTGACCTGCGCCGTGTGCGCCGTCGGACTCATGACCGGATGCTCCCAGGGCTCGAAGGCGGACTCGGCCGCCTCCGCCTCCGCCTCCAGCGGGGACGACTACCTGCTCAAGATGGCCAAGTGCATGCGTGACAAGGGCATCGACGTCTCCGACCCCGACGCCAACGGCAACGTGCAGTTCCCCGACAACGAGGCCGCCACCAAGGCCGCCCAGGAGTGCGAGCAGATCGTCGGCCCCGCCCCCGGCACCGAGGACCTCGCCAAGCCCGAGACGCAGCAGGACCTGGTCAAGGCCGCCGAGTGCCTGCGCAAGGAGGGCTACGACGTGCCCGACCCCGAGGCCGGCAAGGGCATCCAGATCAACGGTGACATCCCCCAGGACGTCATGAACAAGTGCTTCTCCCAGGTCGGGAGCAAGTGA","MKQPLNTRILTRAATVLTCAVCAVGLMTGCSQGSKADSAASASASSGDDYLLKMAKCMRDKGIDVSDPDANGNVQFPDNEAATKAAQECEQIVGPAPGTEDLAKPETQQDLVKAAECLRKEGYDVPDPEAGKGIQINGDIPQDVMNKCFSQVGSK$","Hypothetical protein","Extracellular, Periplasm","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-30]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-25]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-52% similar to PDB:1QWJ The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase (E_value = );","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2033","2203481","2203338","144","12.30","3.15","4355","GTGCCGGGCGCGACGCAAGCGCTCCGGGCGGCCCGGCCGGGCATCGCGGGCGTCACGGGCGCCATGGGGCTCGGCGCCGGCGGCCCCGGCGTCGTCGGCCCGGCACCCTTCAGCCGCCTGCCCGCTCATGCGCTGAACCTGTAG","VPGATQALRAARPGIAGVTGAMGLGAGGPGVVGPAPFSRLPAHALNL$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2034","2202697","2203356","660","5.69","-4.85","24382","ATGCGCGTGCTCGTCGTGGAGGATGAGGAGTACCTGGCTGAGGCCATCGCCACCGGGCTGCGGCGCGAGGCGATGGCCGTGGACGTCGTCGGCGACGGGGCCAGCGCCCTGGAGCAGGTGGCGGTCAACGACTACGACATCATCGTCCTGGACCGGGACCTGCCCGTGGTCCACGGTGACGAGGTCTGCCGGCGGGTGGTGCGCGACTACCCCAGCACGCGGATCCTCATGCTCACTGCATCCCGGACGTTGGACGCGCGCGTGGGCGGTTTCGAGCTCGGGGCCGACGACTACCTCACCAAGCCCTTCGAGTTCCCCGAGCTGGTGGCCCGGCTGCGGGCCCTGGGGCGGCGCAGCCAGCCGGCGCGCACCCCGGTCCTCGAGGCCCACGGGGTGCGCCTGGATCCCTTCCGCCGGGAGGTCTACCGCGACGGGCACTTCATTCACCTCAGCCCCAAGGAGTTCGCGGTCCTTCAGGTCCTCATGGAGGCCGAGGGCGGGGTCCTCAGCGCAGAGACGCTCCTGGAGAAGGCATGGGACGCCAACGCCGACCCCTTCACCAACTCCACGCGGGTGACGATCTCCCACCTGCGTCGCAAGCTCGGTGAGCCGCGCGTGATCCAGACGGTCCCCGGCGCGGGCTACAGGTTCAGCGCATGA","MRVLVVEDEEYLAEAIATGLRREAMAVDVVGDGASALEQVAVNDYDIIVLDRDLPVVHGDEVCRRVVRDYPSTRILMLTASRTLDARVGGFELGADDYLTKPFEFPELVARLRALGRRSQPARTPVLEAHGVRLDPFRREVYRDGHFIHLSPKEFAVLQVLMEAEGGVLSAETLLEKAWDANADPFTNSTRVTISHLRRKLGEPRVIQTVPGAGYRFSA$","Two-component system response regulator","Cytoplasm","Transcriptional regulatory protein cutR(Defective melC1 suppressorprotein)","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[1-115]T$	Q6ACK7_BBBBB_Q6ACK7;
PF00072	$\"[1-113]T$	Response_reg
SM00448	$\"[1-112]T$	REC
PS50110	$\"[2-116]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[126-216]T$	Q8CJW1_STRCO_Q8CJW1;
PF00486	$\"[145-217]T$	Trans_reg_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[1-152]T$	no description
PTHR23283	$\"[2-115]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[2-115]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 2.1e-33. IPB001867A 46-59 IPB001867B 74-118 IPB001867C 207-217***** IPB001789 (Response regulator receiver) with a combined E-value of 9e-10. IPB001789A 46-59 IPB001789B 94-104***** IPB000673 (CheB methylesterase) with a combined E-value of 5.8e-09. IPB000673B 18-71 IPB000673C 72-102","","","-57% similar to PDB:1KGS Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima (E_value = 6.0E_34);-53% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 2.6E_29);-52% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 4.5E_29);-52% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 4.5E_29);-50% similar to PDB:1P2F Crystal Structure Analysis of Response Regulator DrrB, a Thermotoga maritima OmpR/PhoB Homolog (E_value = 1.7E_20);","Residues 1 to 113 (E_value = 4.3e-36) place ANA_2034 in the Response_reg family which is described as Response regulator receiver domain.Residues 145 to 217 (E_value = 2.3e-17) place ANA_2034 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","regulatory protein cutR (Defective melC1 suppressorprotein)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2035","2203524","2204630","1107","5.35","-10.82","38928","GTGACGGCCGCCGGAGTGGTCCTCATCGCCCTGGTCTACTTCTACACGCGCTACGTCACGCTGAGCATCCAGATCGGCGACCCGGTCGGGGAGACCGCCGCCGTGCCGGTCTCACAGGTCGGCGAGGTCGCCAAGGTGGACACGAACCTGTTCGATCTGCTCAGCAGCATCATGCGCTCTGCCGTCGGCGCGCTGGCGCTGCTGGTGGTGCTCTCCGGGACCGTCGGATGGATCCTGGCGGGGCGGATGCTGCAGCCGCTGTCCTCGATGAATGCGGCGGCTAAGCGCGCCGCCTCGGGCGACCTCAGTCAGCGGCTGGACCTGTCCGGCCCGCGCGACGAGATCCACGACCTGGCGGACACCTTCGACAACATGCTGGCCTCCTTGGAGCGGTCCTTCTCCGTCCACCGCCGGTTCGCGGCCAACGCCTCCCACGAGCTGCGCACGCCCCTGGCCACCACGCAGACGATGATCGACGTCGCCCTGTCCGACCCGCAGGCCTCGGCCGAGGACCTGCGCCGGGTGCTGACCCGGGTCCTGGAGACCAACCGCGCCAACCGGGAGACGATTGACGCCCTGCTGGACCTGGCCGACGCCCAGTCCGGCAAGCTGGCCGTCGAGGACGTGGACATGGAGGCCACGGTCCGTGACGCCCTGGGCCTCATCGCTCCGGAGGTCGCTGAGCGCCACCTTCACGTCTCCACCCATCTGCTGCCCGCCCGGGTCCCCGGGGATCCGGTGCTGCTGCGCCAGAGCGTGTCCAACCTGCTGCGCAATGCGGCCCGCTACAACGTCGAGGGCGGTCGTATCACGGTGGGCATGGCGCGTCTGGACGACGGCGTGCGCCTGACGATCCGCAACGAGGGCCCCGTGGTGGCGGCCGAGAGCGTGGAGTCCCTGCGCGAGCCCTTCGTGCGTGGCGAGGGGCGGGGGCGGACCCGGGGCTCCGGGCACGGACTGGGCCTGGCCATCGTCACGGCCGTGGCCACCGCGCACGGTGGCGAGCTGCACCTGAGCGCCAACCCCGACGGCGGACTGACGGCTGTCCTCGAGCTGCCGGTGGGGCAGGTCGAGGACGACACGATCACGGCCGGCCCCAACGACTGA","VTAAGVVLIALVYFYTRYVTLSIQIGDPVGETAAVPVSQVGEVAKVDTNLFDLLSSIMRSAVGALALLVVLSGTVGWILAGRMLQPLSSMNAAAKRAASGDLSQRLDLSGPRDEIHDLADTFDNMLASLERSFSVHRRFAANASHELRTPLATTQTMIDVALSDPQASAEDLRRVLTRVLETNRANRETIDALLDLADAQSGKLAVEDVDMEATVRDALGLIAPEVAERHLHVSTHLLPARVPGDPVLLRQSVSNLLRNAARYNVEGGRITVGMARLDDGVRLTIRNEGPVVAAESVESLREPFVRGEGRGRTRGSGHGLGLAIVTAVATAHGGELHLSANPDGGLTAVLELPVGQVEDDTITAGPND$","Two-component system sensor kinase","Membrane, Cytoplasm","sensory protein kinase","periplasmic sensor signal transduction histidine kinase","ATP-binding region, ATPase domain protein domain protein","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[206-362]T$	no description
PF02518	$\"[244-355]T$	HATPase_c
SM00387	$\"[244-356]T$	HATPase_c

InterPro
IPR003660
Domain

Histidine kinase, HAMP region
PF00672	$\"[61-131]T$	HAMP
SM00304	$\"[81-134]T$	HAMP
PS50885	$\"[81-134]T$	HAMP

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[135-202]T$	HisKA
SM00388	$\"[135-202]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[281-295]T$ $\"[316-334]T$ $\"[340-353]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[142-356]T$	HIS_KIN

noIPR
unintegrated

unintegrated
PTHR23283	$\"[52-354]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23	$\"[52-354]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[61-81]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[81-99]?$ $\"[128-148]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB008883 (Tumour susceptibility gene 101) with a combined E-value of 1.6e-06. IPB008883C 10-50 IPB008883C 2-42 IPB008883C 19-59 IPB008883C 4-44 IPB008883C 5-45 IPB008883C 15-55 IPB008883C 22-62 IPB008883C 20-60 IPB008883C 3-43 IPB008883C 13-53 IPB008883C 16-56 IPB008883C 7-47 IPB008883C 17-57 IPB008883C 21-61 IPB008883C 6-46 IPB008883C 0-40 IPB008883C 27-67***** IPB001359 (Synapsin) with a combined E-value of 9.8e-06. IPB001359H 12-62 IPB001359H 4-54 IPB001359H 9-59 IPB001359H 3-53 IPB001359H 15-65 IPB001359H 27-77 IPB001359H 7-57 IPB001359H 10-60 IPB001359H 21-71 IPB001359H 6-56 IPB001359H 24-74 IPB001359H 14-64 IPB001359H 30-80","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2037","2206913","2205435","1479","10.99","21.25","51829","GTGACCGACGCCATCGCGAGAGGGAAGAGCCCTGGTCCTTGGGGAGGAGGACCAGGGCTCAGCCCATCCTCCCGGGAGGAGAGGAGCGACCCGTCACGATGGCCCCGGCGGCGGAGGTGTCCCCGGCTGCCACCCTCTAGCGTGGAGGGCATGAGACTTGCGACGTCATTCACCGGTGCTCGAGGGGTGCGCTATCCCGCCCCGGACGTGGCCCGTGGCTTCATGCTCCTGTTCATCGCCCTGGCCAACGTCCCCTTCTGGACCGCTGTGACGCACGTTTCCGCCCCATCTGATGCCGTCGACACGGCATGGCTGTGGGTGCGCTCCCTCCTGATCGACTCGCGGGCCTACCCGCTGTTCGCGATGCTCTTCGGCTTCGGACTGGTCACCATGGTCAACCGGCGCATCGCCTCAGGTGCCTCCTCCTATCTCAGCTCCCTGCCCGGCGTGGAGGCCGGCCGTGAGCCGACGTCGCAGGAGGCGGCCTGGGCCCGTGAGCAGGCCACCGTCGACGCACGTCGCCTGGTGCGGCGTCGGGGCCTGTGGATGATCCTCTTCGGCGCCGTACACGCCCTGCTCTTCTCCGGTGACATCATCGGCTCCTACGGCCTGGTCGCCGTCATCTTCGCCGGCTGGATCGCCCGCAAGCACTGGAAGCGGGCCGTGGCCTTCTGCGCCGTCGTCGTTGTTGCCGGCGCCGTCACGTTCCTCAACATGGGCAGCTTCCTGGCCTCCCAGGGGGCCGCCTCGGCGACGGACGCGCACCAGGGGGCCGGCGCCTCGACCGATACGGTCCTGTCCTACGTCTCCGACGGACTCCTGGCCTGGGGTGGAAGCCTGGTCTCGGCGCTGTTCTTCTCCATGATCGTTCCGGCGATGTTCCTCGGCGCCCGGCTGGCCGACACCGACCTCATCACCCACCCCGAGCGCCACCGCCGGCTCCTGGTCGCCGTCGGCCTGGGCGGTCTGGGGCTCGGTGCCGCGGGCGGTATCGGGTTCGCCGTGTGGGCCGCCGGTGGACACCTGGCTGTCTGGACCATGCCCCTTCACTCGCTCACGGGCGTGGCCGGGGCCTGCGGCTGGCTGGCACTGCTGTCCCTGTACGCCGGTGGGCCGCGGCCGGATGGTCGGCTGACGGGGCTACGTCGGCTCGCCTCCACCGTGGGGCGCCGCTCCATGACGGCCTACCTCAGCCAGACCCTCCTCTTCGCCATCATCTTCATGGCCCTTCCCGCCCTGACCGGGATCGAGCTCCATCTGGGCGAGGCCCGGGCCGCCGGGATCGCGCTGGCGGTCTGGCTAACGACGGTCGGGCTGTGCGCCGTTCTGGAGCGGGGCGGACATACCGGTCCCTTCGAGGCCCTGCTGCGCACCGCCGTCGCCCGCAGCGAGCGCCGGCGCCGGCCGGCGGCCCCTCCTGCCCCTGCGACCCCGGCCTCACCGGTGGGTGACTCCAGCACGTACGACCTGGCGCGCTGA","VTDAIARGKSPGPWGGGPGLSPSSREERSDPSRWPRRRRCPRLPPSSVEGMRLATSFTGARGVRYPAPDVARGFMLLFIALANVPFWTAVTHVSAPSDAVDTAWLWVRSLLIDSRAYPLFAMLFGFGLVTMVNRRIASGASSYLSSLPGVEAGREPTSQEAAWAREQATVDARRLVRRRGLWMILFGAVHALLFSGDIIGSYGLVAVIFAGWIARKHWKRAVAFCAVVVVAGAVTFLNMGSFLASQGAASATDAHQGAGASTDTVLSYVSDGLLAWGGSLVSALFFSMIVPAMFLGARLADTDLITHPERHRRLLVAVGLGGLGLGAAGGIGFAVWAAGGHLAVWTMPLHSLTGVAGACGWLALLSLYAGGPRPDGRLTGLRRLASTVGRRSMTAYLSQTLLFAIIFMALPALTGIELHLGEARAAGIALAVWLTTVGLCAVLERGGHTGPFEALLRTAVARSERRRRPAAPPAPATPASPVGDSSTYDLAR$","Uncharacterized membrane protein","Membrane, Extracellular","hypothetical conserved protein, putative","hypothetical protein","protein of unknown function DUF418","","","","","

InterPro
IPR007349
Domain

Protein of unknown function DUF418
PF04235	$\"[299-463]T$	DUF418

noIPR
unintegrated

unintegrated
tmhmm	$\"[116-136]?$ $\"[191-213]?$ $\"[222-242]?$ $\"[273-295]?$ $\"[316-338]?$ $\"[352-372]?$ $\"[393-413]?$ $\"[423-443]?$	transmembrane_regions

","BeTs to 4 clades of COG2311COG name: Uncharacterized membrane proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2311 is -o-------d--b-e---s--j----Number of proteins in this genome belonging to this COG is 1","***** IPB007349 (Protein of unknown function DUF418) with a combined E-value of 2e-19. IPB007349A 63-80 IPB007349B 107-135 IPB007349E 388-402 IPB007349F 439-461","","","No significant hits to the PDB database (E-value < E-10).","Residues 299 to 463 (E_value = 6.1e-08) place ANA_2037 in the DUF418 family which is described as Protein of unknown function (DUF418).","","conserved protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2038","2208337","2206925","1413","10.38","13.75","49011","ATGAACACGACGACTTCCTCCGCGACCTCATTCACTGGTTCCCGCGGCCTGCGCTACCCCGCCCCCGACGTCGCCCGCGGCTTTATGCTGCTGCTCATCGCCCTGGCCAATGTGGGGTCGTGGGTGGCAGGCCCCGAGGGCCATGCGCCATCGACCGCCGACAGGACCTGGGCCTTCATGAGTGCCCTGTTCATCGACCAGCGCGCCTACCCGCTGTTCGCACTGCTCTTCGGCTTCGGGCTGGCCACCATGGTCAACCGGCGCATGGCATCGGGCATCGACGCCTACTGCCAGCAGCTGACCGGCGGGCTCCGGGCGCCGTCGGCGGCTGAGCTCGACCAGGCCCGGGAGCAGGCGGCCGTCGATGCCCGCCGCCTCGTGCGGCGCCGCGGCCTGTGGATGGTCCTGTTCGGGCTCATCCACGGAGCCTTCTTCCCCTCGGAGATCATCGGCACCTACGGCATCGTCGCCGTCGTCTTCGCCGGGTGGTTCGCCCACAAGCACCACAAGCGCCAGCTGGCGGTGTGCGCCCTGGTTCTTCTGTCCCAGTTCGTGCCGGTGGTCCTGGCCATGCTCTTTGGTCCCGGCGGTGAAGCGGCCGCCTCCGGCGCAGCGGTCCCCGCCCCGGCGGCTGCGGCACCCACCGGAGCAGGTGAGTCCATGGCCTCAGCGCTTCCCTGGTTCGTGACCAACGTGTTCGGGTGGTTCTTCACCGCTCTGAGTGCGGCCTTCACCACGATGATTCTTCCCGCCGCCTTCCTCGGCGCCCGCCTGGCCGACACCGACCTCATCGCCCACCCCGAGCGCCACCGCGGCCTGCTGACGGTGGCCGGGATCGGTGGTCTGGCCCTGGGGGCGCTCGGTGCGCTTCACCAGCTCCTGGTCCCGCTCACCAGCGCTCAGCCCTGGGCGGCCGACTCCGCCCTGATCATGGTCCTGGGCCTGGCCGGGGGCTGCGGCTGGCTCGCCGTCCTGGCCCTCTACGCCGGCGGGCCGACGGCGGACAACCGGCTGACCGGCCTCAAGCGGCTGCTGTCCAATGTGGGGCGCCGCTCCATGACCGCCTACCTGTCCCAGACGGCCATGTTCGCCGGCATCTTCGTCATCGCGCCGCGACTGACCGGGAGGTCCGTGTCGCCGGGGTTGGTGGCATCCGCCGCGGTGGCGGTGATGGTCTGGCTGACGACCGTGGTCCTGTGCGCGGTGCTGGAGAGGCTCGGCATGCCCGGTCCCTTCGAGGTCCTGCTGCGCGCCGCCGTCGCCCGCAGCGAGCGCAGCCGCACGAACCCGTTCCCCCAGCAGGTCCCCGACCAGCGCACGGCCCAGCTCCCCGGCCAGCCGACGAGCGCCCCGGTGCCGCCCGCCCCGTGGGGTGCTCAGGTCCCCGTCGCCCCGGTTCCCGCCGGAGCCTGA","MNTTTSSATSFTGSRGLRYPAPDVARGFMLLLIALANVGSWVAGPEGHAPSTADRTWAFMSALFIDQRAYPLFALLFGFGLATMVNRRMASGIDAYCQQLTGGLRAPSAAELDQAREQAAVDARRLVRRRGLWMVLFGLIHGAFFPSEIIGTYGIVAVVFAGWFAHKHHKRQLAVCALVLLSQFVPVVLAMLFGPGGEAAASGAAVPAPAAAAPTGAGESMASALPWFVTNVFGWFFTALSAAFTTMILPAAFLGARLADTDLIAHPERHRGLLTVAGIGGLALGALGALHQLLVPLTSAQPWAADSALIMVLGLAGGCGWLAVLALYAGGPTADNRLTGLKRLLSNVGRRSMTAYLSQTAMFAGIFVIAPRLTGRSVSPGLVASAAVAVMVWLTTVVLCAVLERLGMPGPFEVLLRAAVARSERSRTNPFPQQVPDQRTAQLPGQPTSAPVPPAPWGAQVPVAPVPAGA$","Membrane protein","Membrane, Cytoplasm","hypothetical conserved protein, putative","hypothetical protein","membrane protein-like","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290","","","

InterPro
IPR000223
Family

Peptidase S26A, signal peptidase I
PS00501	$\"[218-225]?$	SPASE_I_1

noIPR
unintegrated

unintegrated
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[70-90]?$ $\"[143-163]?$ $\"[173-193]?$ $\"[232-252]?$ $\"[273-295]?$ $\"[309-331]?$ $\"[352-372]?$ $\"[378-400]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB007349 (Protein of unknown function DUF418) with a combined E-value of 4.4e-20. IPB007349A 17-34 IPB007349B 60-88 IPB007349E 348-362 IPB007349F 399-421","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","conserved protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2039","2208657","2208379","279","11.90","11.35","9503","GTGGATGGGGCAGGCCGCGGCCGCCCTCGTCGCCCTGGGTGTCTGGCTGGCGTGCGTGGTCCTGTGTCTCCTGCTGGAGCGCGGCGGTCATGCAGGCCCCTTCGAGACCCTGCTGCGCACCGCCGTCGCGCGCAGCGAGCGCAGGAGGACGCCGCCGCCGCCCACCGTCTGGCCCGGAATGCAGTCGGCCCCCTGAGCCGGCCCGACCAGGGGCCGTCCGCCGGAAGAATGGTCGGGCGTCAGGCTCCTCCTTTCGGTGGAGACGATCTCGGCGCTTAA","VDGAGRGRPRRPGCLAGVRGPVSPAGARRSCRPLRDPAAHRRRAQRAQEDAAAAHRLARNAVGPLSRPDQGPSAGRMVGRQAPPFGGDDLGA$","Hypothetical protein","Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2040","2209464","2208967","498","11.45","11.15","17936","ATGAGCCGGCACCGGGCCGGGCAGGGCCTGGGCGTCCTGGCCGACGACGCCGCTGAGCGCGCGGTCTACGTGGTCTCGGTGGCGGCCGAGCTCGCCGGGATGCACCCCCAGACCCTGCGCCAGTACGACCGGCTCGGGCTGGTCAGCCCCGCCCGGACCCGCGGGCGGGGTCGGCGCTACTCCCACCGCGACGTCGAGCGCCTGCGTCGCATCCAGTCCCTGTCCCAGGAGGGCATCAACCTCGAGGGCATCCGCCGCATCCTTGCCCTGGAGGCCCGCGTGGAGGAGCTGGAGGCCGACAACGCCCGCATGCGCAGCCGCGAGGCCGTCGTCCAGCGGATCTTCGCGGCGGCCGCCGACGGCGAGGTCCAGGTCGTCGCCCCCGGCCGCCAGGGCCGCGGGCCCGCCGGGCGCCACCCCGAGGCGGGGCGCGGACGTCCCGCAGGTACAGCGGGAGGCGCGAGCACTGCTTTGGTGCCCGTGCGTCGGTGGCACTGA","MSRHRAGQGLGVLADDAAERAVYVVSVAAELAGMHPQTLRQYDRLGLVSPARTRGRGRRYSHRDVERLRRIQSLSQEGINLEGIRRILALEARVEELEADNARMRSREAVVQRIFAAAADGEVQVVAPGRQGRGPAGRHPEAGRGRPAGTAGGASTALVPVRRWH$","Transcriptional regulator, MerR family","Cytoplasm, Extracellular","HspR","transcriptional regulator; MerR family","regulatory protein, MerR","","Holmes D.J., Caso J.L., Thompson C.J. Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 1993. 12(8):3183-3191. PMID: 7688297Helmann J.D., Wang Y., Mahler I., Walsh C.T. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons. J. Bacteriol. 1989. 171(1):222-229. PMID: 2492496Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 1995. 177(14):3904-3910. PMID: 7608059Nakano Y., Kimura K. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 1991. 109(2):223-228. PMID: 1677938Sadowsky M.J., Cregan P.B., Gottfert M., Sharma A., Gerhold D., Rodriguez-Quinones F., Keyser H.H., Hennecke H., Stacey G. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(2):637-641. PMID: 1988958Helmann J.D., Ballard B.T., Walsh C.T. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. Science 1990. 247(4945):946-948. PMID: 2305262","","","

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PR00040	$\"[24-35]T$ $\"[35-48]T$ $\"[58-78]T$	HTHMERR
PF00376	$\"[24-60]T$	MerR
SM00422	$\"[23-91]T$	HTH_MERR
PS50937	$\"[22-90]T$	HTH_MERR_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[23-116]T$	no description

InterPro
IPR001063
Family

Ribosomal protein L22/L17
PS00464	$\"[196-220]?$	RIBOSOMAL_L22

InterPro
IPR001623
Domain

Heat shock protein DnaJ, N-terminal
PF00226	$\"[4-66]T$	DnaJ
SM00271	$\"[3-61]T$	DnaJ
PS50076	$\"[4-69]T$	DNAJ_2
PS00636	$\"[46-65]T$	DNAJ_1

InterPro
IPR002939
Domain

Chaperone DnaJ, C-terminal
PF01556	$\"[196-319]T$	DnaJ_C

InterPro
IPR003095
Family

Heat shock protein DnaJ
PR00625	$\"[15-34]T$ $\"[46-66]T$ $\"[186-202]T$ $\"[235-252]T$	DNAJPROTEIN

InterPro
IPR015609
Family

Molecular chaperone, heat shock protein, Hsp40, DnaJ
PTHR11821	$\"[2-115]T$ $\"[155-305]T$	DNAJ/HSP40

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.110	$\"[3-75]T$	no description
G3DSA:2.60.260.20	$\"[145-224]T$ $\"[225-316]T$	no description
PTHR11821:SF76	$\"[2-115]T$ $\"[155-305]T$	DNAJ-RELATED

","BeTs to 7 clades of COG2214COG name: Molecular chaperones, DnaJ classFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG2214 is -o----y-vd---cefg-snuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB001305 (DnaJ central domain (CXXCXGXG)) with a combined E-value of 3e-41. IPB001305A 4-31 IPB001305B 45-70 IPB001305E 217-252 IPB001305F 278-315 IPB001305C 234-277 IPB001305F 199-236***** IPB003095 (DnaJ protein family signature) with a combined E-value of 4.4e-39. IPB003095A 15-34 IPB003095B 46-66 IPB003095G 186-202 IPB003095H 235-252 IPB003095G 267-283***** IPB012895 (HSCB oligomerisation, C-terminal) with a combined E-value of 8.2e-06. IPB012895A 13-36","","","-61% similar to PDB:2DN9 Solution structure of J-domain from the DnaJ homolog, human Tid1 protein (E_value = 1.3E_13);-46% similar to PDB:1XBL NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ, 20 STRUCTURES (E_value = 7.1E_12);-47% similar to PDB:1BQ0 J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES (E_value = 1.2E_11);-59% similar to PDB:1BQZ J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-78) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES (E_value = 3.5E_11);-59% similar to PDB:2CTW Solution structure of J-domain from mouse DnaJ subfamily C menber 5 (E_value = 6.0E_11);","Residues 4 to 66 (E_value = 7e-36) place ANA_2041 in the DnaJ family which is described as DnaJ domain.Residues 155 to 223 (E_value = 1.7e-10) place ANA_2041 in the DnaJ_C family which is described as DnaJ C terminal region.Residues 196 to 319 (E_value = 4.7e-40) place ANA_2041 in the DnaJ_C family which is described as DnaJ C terminal region.","","protein similar to DnaJ (dnaJ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2042","2211234","2210686","549","4.54","-15.30","19098","GTGCCCGACGACGTCCGTGAAGGACTCGCCCAGGGCTCGTCCGAGGGCACGGCCGGCCAGGCCGACGCCGCCTCCGATGAGGCGGCGGGGGAGGACCCCCTGGCCCAGGCTCAGGCCCAGGCCGCTCAGGCGGCCGACGACCTGGCCCGGGCCCGGGCGGACCTCTACAACCTCCAGCAGGAGTACCAGGGGTTCGTGCGCCGCTCCCGTGAGGGCGCGGCCTCCCACCGGGACGCCGGTGCGGCCGGCGTCGTCGAGGCTCTCATCCCGGTCCTCGACGAGATCGAGCTGGCCCGCCAGCACGGCGACCTGACCGGCACCTTCGAGACCACGGCCGGCAAGCTCGAGTCGATCCTGGCCGAGAAGTACTCCCTGGAGCGCTTCGGCGCCGTTGGGGAGGTCTTCGACCCCACGCTGCACGAGGCCCTCATGGCCACCGAGTCCAGCGAGGTCACCGAGCCCACCATCGCCGCGGTCCTCCAGCCCGGATACCGCCTGGGTGAGCGCGTCGTGCGCGCCGCCCGCGTCCAGGTCGCCAACCCGGCCTGA","VPDDVREGLAQGSSEGTAGQADAASDEAAGEDPLAQAQAQAAQAADDLARARADLYNLQQEYQGFVRRSREGAASHRDAGAAGVVEALIPVLDEIELARQHGDLTGTFETTAGKLESILAEKYSLERFGAVGEVFDPTLHEALMATESSEVTEPTIAAVLQPGYRLGERVVRAARVQVANPA$","Molecular chaperone GrpE","Cytoplasm","co-chaperone GrpE","GrpE protein","GrpE protein","","Harrison C.J., Hayer-Hartl M., Di Liberto M., Hartl F., Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 1997. 276(5311):431-435. PMID: 9103205","","","

InterPro
IPR000740
Family

GrpE nucleotide exchange factor
PR00773	$\"[49-65]T$ $\"[132-147]T$ $\"[159-178]T$	GRPEPROTEIN
PTHR21237	$\"[20-181]T$	GRPE PROTEIN
PF01025	$\"[18-180]T$	GrpE
PS01071	$\"[135-178]T$	GRPE

InterPro
IPR009012
Domain

GrpE nucleotide exchange factor, head
G3DSA:2.30.22.10	$\"[124-179]T$	no description

InterPro
IPR013805
Domain

GrpE nucleotide exchange factor, coiled-coil
G3DSA:3.90.20.20	$\"[20-121]T$	no description

noIPR
unintegrated

unintegrated
PTHR21237:SF1	$\"[20-181]T$	GRPE PROTEIN (HSP-70 COFACTOR)

","BeTs to 19 clades of COG0576COG name: Molecular chaperone GrpE (heat shock protein)Functional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0576 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000740 (GrpE protein) with a combined E-value of 6.1e-19. IPB000740A 53-89 IPB000740B 124-143 IPB000740C 154-178","","","No significant hits to the PDB database (E-value < E-10).","Residues 18 to 180 (E_value = 4.3e-28) place ANA_2042 in the GrpE family which is described as GrpE.","","GrpE (grpE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2043","2213171","2211312","1860","4.80","-36.19","66181","ATGGCACGCGCTGTCGGTATCGACCTGGGTACCACCAACTCTGCTATCGCCGTCCTCGAGGGTGGCGAGCCCACCATCATCCCGAACGCCGAGGGCGGCCGCACGACCCCCTCCGTCGTCGCCTTCTCCAAGTCCGGCGAGATCCTCGTCGGCGAGATCGCCAAGCGTCAGGCGGTCACCAACGTCGATCGCACCATCTCTTCGGTCAAGCGCCACATGGGCACTGACTGGTCCGTCGAGATCGACGACAAGAAGTACACCGCCCAGGAGATCAGCGCCCGCATCCTGGCCAAGCTCAAGGCCGACGCCGAGGCCTACCTGGGTGAGCCCGTCACCAACGCGGTCATCACCGTCCCGGCCTACTTCAACGACGCCGAGCGCCAGGCCACCAAGGAGGCCGGCACCATCGCGGGCCTGACCGTGGACCGCATCGTCAACGAGCCCACCGCCGCGGCCCTGGCCTACGGCCTGGACAAGGGCAAGGAGGACGAGCTCATCCTCGTCTTCGACCTCGGTGGCGGTACCTTCGACGTCTCCCTGCTCGAGGTCGGCAAGGACGACGACGGCTTCTCCACCATCCAGGTGCGCGCCACCAACGGTGACAACCGTCTGGGCGGTGACGACTGGGACGCCCGCATCGTCGACTGGCTGGTCAAGCAGGTCAAGAGCAAGGACGGCGTGGACCTGTCCAAGGACAAGATCGCCATGCAGCGTCTCAAGGACGCCGCCGAGCAGGCCAAGAAGGAGCTGTCCTCGGCGACCTCCACGAACATCAACCTGCAGTACCTCTCCATGAGCGAGTCCGGCCCCATCCACCTCGATGAGAAGCTCACCCGCTCCAACTTCCAGGAGATGACCGCGGACCTGCTCGAGCGCACCAAGATTCCCTTCCACAACGTCATCAAGGACGCCGGGGTTAAGGTCTCCGACATCGACCACGTGGTCCTCGTGGGTGGCTCCACCCGCATGCCCGCTGTCGCCGACGTGGTGCGCGAGCTGACCGGCAAGGACCCCAACAAGGGCGTCAACCCCGATGAGGTCGTCGCCGTCGGCGCGGCCCTCCAGGCCGGCGTCATCCAGGGCGACCGCAGCGACGTCCTGCTCATCGACGTCACGCCGCTGTCCCTGGGCATCGAGACCAAGGGCGGGGTCATGACCAAGCTCATCGAGCGCAACACGGCCATCCCGACCAAGCGCTCCGAGGTCTTCTCCACCGCCGAGGACAACCAGCCCTCCGTGCTCATCCAGGTCTACCAGGGCGAGCGCGAGTTCGCTCGGGACAACAAGCCGCTGGGCACCTTCGAGCTGACCGGCATCGCCCCGGCCCCCCGCGGCGTGCCCCAGATCGAGGTCTCCTTCGACATCGACGCCAACGGCATCGTCCACGTCTCGGCCAAGGACCGCGGCACCGGCAAGGAGCAGTCCATGACCATCTCCGGCGGCTCCGCCCTGCCCAAGGAGGACATCGACCGCATGGTCAAGGAGGCCGAGGCCCACGCCGAGGAGGACAAGAAGCGCCGCGAGGACGCCGAGACCCGCAACTCCGCCGAGCAGCAGGCCTACTCCATCGAGAAGCTCCTCAAGGACAACAAGGACAAGCTGCCCGAGGACGTCCACTCCGAGGTCTCCGAGGCCGTCGCCGACCTCAAGAAGGCCCTCGAGGGTGACGACATCGAGCCGGTCAAGACCGCTCAGGAGAAGCTGAGCTCGGTGGCCCAGAAGGTCGGTGAGGCCCTCTACCAGGCCGACGCCGCCGCCCAGGCCGCGGGTGACGCCTCCGCTTCCTCGGCCGGCTCCACGTCCTCCGACGACGAGGACATCGTGGACGCCGAGATCGTCGACGACGAGGACTCCAAGTGA","MARAVGIDLGTTNSAIAVLEGGEPTIIPNAEGGRTTPSVVAFSKSGEILVGEIAKRQAVTNVDRTISSVKRHMGTDWSVEIDDKKYTAQEISARILAKLKADAEAYLGEPVTNAVITVPAYFNDAERQATKEAGTIAGLTVDRIVNEPTAAALAYGLDKGKEDELILVFDLGGGTFDVSLLEVGKDDDGFSTIQVRATNGDNRLGGDDWDARIVDWLVKQVKSKDGVDLSKDKIAMQRLKDAAEQAKKELSSATSTNINLQYLSMSESGPIHLDEKLTRSNFQEMTADLLERTKIPFHNVIKDAGVKVSDIDHVVLVGGSTRMPAVADVVRELTGKDPNKGVNPDEVVAVGAALQAGVIQGDRSDVLLIDVTPLSLGIETKGGVMTKLIERNTAIPTKRSEVFSTAEDNQPSVLIQVYQGEREFARDNKPLGTFELTGIAPAPRGVPQIEVSFDIDANGIVHVSAKDRGTGKEQSMTISGGSALPKEDIDRMVKEAEAHAEEDKKRREDAETRNSAEQQAYSIEKLLKDNKDKLPEDVHSEVSEAVADLKKALEGDDIEPVKTAQEKLSSVAQKVGEALYQADAAAQAAGDASASSAGSTSSDDEDIVDAEIVDDEDSK$","Chaperone protein DnaK","Cytoplasm","Chaperone protein dnaK (Heat shock protein 70)(Heat shock 70 kDaprotein) (HSP70)","chaperone protein DnaK","chaperone protein DnaK","","Georgopoulos C., Welch W.J. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 1993. 9:601-635. PMID: 8280473","","","

InterPro
IPR001023
Family

Heat shock protein Hsp70
PR00301	$\"[3-16]T$ $\"[31-43]T$ $\"[54-62]T$ $\"[114-134]T$ $\"[174-184]T$ $\"[311-327]T$ $\"[342-362]T$ $\"[365-384]T$ $\"[446-462]T$	HEATSHOCK70
PTHR19375	$\"[1-501]T$	HEAT SHOCK PROTEIN 70KDA

InterPro
IPR012725
Family

Chaperone DnaK
TIGR02350	$\"[3-581]T$	prok_dnaK: chaperone protein DnaK

InterPro
IPR013126
Family

Heat shock protein 70
PD000089	$\"[79-138]T$	DNAK_MYCPA_Q00488;
PF00012	$\"[4-581]T$	HSP70
PS00297	$\"[7-14]T$	HSP70_1
PS00329	$\"[168-181]T$	HSP70_2
PS01036	$\"[314-328]T$	HSP70_3

noIPR
unintegrated

unintegrated
G3DSA:2.60.34.10	$\"[348-538]T$	no description
G3DSA:3.30.420.40	$\"[4-186]T$	no description
G3DSA:3.90.640.10	$\"[205-292]T$	no description
PTHR19375:SF1	$\"[1-501]T$	HEAT SHOCK PROTEIN 70 (HSP70)

","BeTs to 22 clades of COG0443COG name: Molecular chaperoneFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0443 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB001023 (Heat shock protein Hsp70) with a combined E-value of 6.9e-202. IPB001023A 5-38 IPB001023B 45-91 IPB001023C 100-154 IPB001023D 174-228 IPB001023E 335-362 IPB001023F 367-421 IPB001023G 431-483","","","-63% similar to PDB:1YUW crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant (E_value = 6.1E_127);-69% similar to PDB:1DKG CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK (E_value = 1.2E_103);-63% similar to PDB:1S3X The crystal structure of the human Hsp70 ATPase domain (E_value = 1.1E_78);-63% similar to PDB:1HJO HEAT-SHOCK 70KD PROTEIN 42KD ATPASE N-TERMINAL DOMAIN (E_value = 1.4E_78);-62% similar to PDB:1HPM HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE (E_value = 3.8E_76);","Residues 4 to 581 (E_value = 0) place ANA_2043 in the HSP70 family which is described as Hsp70 protein.","","protein dnaK (Heat shock protein 70) (Heat shock 70 kDaprotein) (HSP70) (HSP70)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2044","2211555","2213189","1635","4.21","-75.57","53642","GTGGACGTCCTCGGGCAGCTTGTCCTTGTTGTCCTTGAGGAGCTTCTCGATGGAGTAGGCCTGCTGCTCGGCGGAGTTGCGGGTCTCGGCGTCCTCGCGGCGCTTCTTGTCCTCCTCGGCGTGGGCCTCGGCCTCCTTGACCATGCGGTCGATGTCCTCCTTGGGCAGGGCGGAGCCGCCGGAGATGGTCATGGACTGCTCCTTGCCGGTGCCGCGGTCCTTGGCCGAGACGTGGACGATGCCGTTGGCGTCGATGTCGAAGGAGACCTCGATCTGGGGCACGCCGCGGGGGGCCGGGGCGATGCCGGTCAGCTCGAAGGTGCCCAGCGGCTTGTTGTCCCGAGCGAACTCGCGCTCGCCCTGGTAGACCTGGATGAGCACGGAGGGCTGGTTGTCCTCGGCGGTGGAGAAGACCTCGGAGCGCTTGGTCGGGATGGCCGTGTTGCGCTCGATGAGCTTGGTCATGACCCCGCCCTTGGTCTCGATGCCCAGGGACAGCGGCGTGACGTCGATGAGCAGGACGTCGCTGCGGTCGCCCTGGATGACGCCGGCCTGGAGGGCCGCGCCGACGGCGACGACCTCATCGGGGTTGACGCCCTTGTTGGGGTCCTTGCCGGTCAGCTCGCGCACCACGTCGGCGACAGCGGGCATGCGGGTGGAGCCACCCACGAGGACCACGTGGTCGATGTCGGAGACCTTAACCCCGGCGTCCTTGATGACGTTGTGGAAGGGAATCTTGGTGCGCTCGAGCAGGTCCGCGGTCATCTCCTGGAAGTTGGAGCGGGTGAGCTTCTCATCGAGGTGGATGGGGCCGGACTCGCTCATGGAGAGGTACTGCAGGTTGATGTTCGTGGAGGTCGCCGAGGACAGCTCCTTCTTGGCCTGCTCGGCGGCGTCCTTGAGACGCTGCATGGCGATCTTGTCCTTGGACAGGTCCACGCCGTCCTTGCTCTTGACCTGCTTGACCAGCCAGTCGACGATGCGGGCGTCCCAGTCGTCACCGCCCAGACGGTTGTCACCGTTGGTGGCGCGCACCTGGATGGTGGAGAAGCCGTCGTCGTCCTTGCCGACCTCGAGCAGGGAGACGTCGAAGGTACCGCCACCGAGGTCGAAGACGAGGATGAGCTCGTCCTCCTTGCCCTTGTCCAGGCCGTAGGCCAGGGCCGCGGCGGTGGGCTCGTTGACGATGCGGTCCACGGTCAGGCCCGCGATGGTGCCGGCCTCCTTGGTGGCCTGGCGCTCGGCGTCGTTGAAGTAGGCCGGGACGGTGATGACCGCGTTGGTGACGGGCTCACCCAGGTAGGCCTCGGCGTCGGCCTTGAGCTTGGCCAGGATGCGGGCGCTGATCTCCTGGGCGGTGTACTTCTTGTCGTCGATCTCGACGGACCAGTCAGTGCCCATGTGGCGCTTGACCGAAGAGATGGTGCGATCGACGTTGGTGACCGCCTGACGCTTGGCGATCTCGCCGACGAGGATCTCGCCGGACTTGGAGAAGGCGACGACGGAGGGGGTCGTGCGGCCGCCCTCGGCGTTCGGGATGATGGTGGGCTCGCCACCCTCGAGGACGGCGATAGCAGAGTTGGTGGTACCCAGGTCGATACCGACAGCGCGTGCCATGTGGTGTGCTCCTTGTGA","VDVLGQLVLVVLEELLDGVGLLLGGVAGLGVLAALLVLLGVGLGLLDHAVDVLLGQGGAAGDGHGLLLAGAAVLGRDVDDAVGVDVEGDLDLGHAAGGRGDAGQLEGAQRLVVPSELALALVDLDEHGGLVVLGGGEDLGALGRDGRVALDELGHDPALGLDAQGQRRDVDEQDVAAVALDDAGLEGRADGDDLIGVDALVGVLAGQLAHHVGDSGHAGGATHEDHVVDVGDLNPGVLDDVVEGNLGALEQVRGHLLEVGAGELLIEVDGAGLAHGEVLQVDVRGGRRGQLLLGLLGGVLETLHGDLVLGQVHAVLALDLLDQPVDDAGVPVVTAQTVVTVGGAHLDGGEAVVVLADLEQGDVEGTATEVEDEDELVLLALVQAVGQGRGGGLVDDAVHGQARDGAGLLGGLALGVVEVGRDGDDRVGDGLTQVGLGVGLELGQDAGADLLGGVLLVVDLDGPVSAHVALDRRDGAIDVGDRLTLGDLADEDLAGLGEGDDGGGRAAALGVRDDGGLATLEDGDSRVGGTQVDTDSACHVVCSL$","Glutamate dehydrogenase","Cytoplasm, Extracellular","LAC ORF","putative NAD-specific glutamate dehydrogenase encoded in antisense gene pair with dnaKJ","Glutamate dehydrogenase","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-44]?$	signal-peptide
tmhmm	$\"[21-43]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[14-32]?$	transmembrane_regions

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[188-325]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[191-375]T$	AAA

InterPro
IPR003960
Domain

AAA ATPase, subdomain
PS00674	$\"[293-311]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.60	$\"[324-397]T$	no description
G3DSA:3.40.50.300	$\"[140-321]T$	no description
PTHR23073	$\"[152-412]T$	26S PROTEASE REGULATORY SUBUNIT
PTHR23073:SF2	$\"[152-412]T$	gb def: Cell division cycle protein 48-related protein

InterPro
IPR011990
Domain

Tetratricopeptide-like helical
G3DSA:1.25.40.10	$\"[10-198]T$	no description

InterPro
IPR013026
Domain

Tetratricopeptide region
SM00028	$\"[41-74]T$ $\"[75-108]T$	TPR
PS50293	$\"[1-175]T$	TPR_REGION

InterPro
IPR013105
Repeat

Tetratricopeptide TPR_2
PF07719	$\"[75-108]T$	TPR_2

noIPR
unintegrated

unintegrated
PTHR23083	$\"[1-191]T$	TETRATRICOPEPTIDE REPEAT PROTEIN, TPR
tmhmm	$\"[229-247]?$ $\"[253-271]?$ $\"[298-318]?$ $\"[324-344]?$	transmembrane_regions

","BeTs to 8 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 75 to 108 (E_value = 0.00013) place ANA_2048 in the TPR_2 family which is described as Tetratricopeptide repeat.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2049","2217827","2217069","759","6.88","-0.44","26969","ATGAGCCTCATCCTGAACGACCTCACCTTCTCCTACGGCAGGCGCGCCGTCCTCAAGGGCGTCGACGCCACCTGGGAGACCGGCCAGACGGTCGGGCTGCTCGGCCCCAACGGCGCCGGCAAGTCCACTCTGGTCACCTGCGTGGCCCAGCTGCGTCGTCACCTGGGGGAGGTGAGCTTCGCCGGGCGGCGGGGCCACGACCTGCGCGGAATGATCGGCTACATGCCGCAGGGCCTGCCCGGCGACGCCGCCCTGACCGCCCTGGAGTCGGTGCTCACCGCCTCGCGGCGCGGCATGACCTGGCACACGAGTCGGGCCGACATCGACCTGGCCTGGAGCGCCTTGGACGAGCTCGGGGTGGCCGAGCTGGCCGACCGCCCACTGGGCCAGCTCTCCGGCGGGCAGCGCCAGCTCGTCGCCCTGGCCCAGACACTCGTGCGCGAGCCCGGACTCATCCTGCTCGACGAGCCCACCTCCGCCCTCGACCTGCGCCGCCAGGTCTCGGTCCTCTCCCACGTGCGCCGGATCTGCCACCGGGACACCGGGCGCCTCGCCGTCGTCGCCCTGCACGACCTCAACCTGGCGGCCCGCTTCTGCGACCGCCTCGCCATCCTCGCCGGCGGGACGATCCGCGCCGAGGGGCCGCCCGCCGAGGTGCTCCAGCCCGACATCCTCGCCGAGGTCTACGGGCTGCGGGTACGGATCGTGCCCGACGGCGACCACGTCATGGTCGCCCCCGAGGCCGAGCAGGGGGCTTGA","MSLILNDLTFSYGRRAVLKGVDATWETGQTVGLLGPNGAGKSTLVTCVAQLRRHLGEVSFAGRRGHDLRGMIGYMPQGLPGDAALTALESVLTASRRGMTWHTSRADIDLAWSALDELGVAELADRPLGQLSGGQRQLVALAQTLVREPGLILLDEPTSALDLRRQVSVLSHVRRICHRDTGRLAVVALHDLNLAARFCDRLAILAGGTIRAEGPPAEVLQPDILAEVYGLRVRIVPDGDHVMVAPEAEQGA$","ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component","Cytoplasm, Membrane","ATP-binding protein Irp6C","Fe(III) dicitrate ABC transporter; ATP-binding protein ","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[130-170]T$	Q8VVA6_CORDI_Q8VVA6;
PF00005	$\"[28-208]T$	ABC_tran
PS50893	$\"[3-232]T$	ABC_TRANSPORTER_2
PS00211	$\"[131-145]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[27-208]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[3-230]T$	no description
PTHR19222	$\"[3-235]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31	$\"[3-235]T$	METAL ABC TRANSPORTER

","BeTs to 15 clades of COG1120COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1120 is aompk---vdrlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 4","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.3e-22. IPB013563A 17-51 IPB013563C 128-155 IPB013563D 184-236***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 1e-20. IPB005074C 17-64 IPB005074D 119-162***** IPB005116 (TOBE domain) with a combined E-value of 1.4e-16. IPB005116A 35-51 IPB005116C 131-144 IPB005116D 151-170***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 6.3e-13. IPB010509B 28-53 IPB010509D 126-170***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.1e-07. IPB010929K 15-59 IPB010929M 128-174 IPB010929A 27-46","","","-51% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 1.4E_19);-51% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 3.1E_19);-49% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 2.6E_18);-49% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 2.6E_18);-49% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 2.6E_18);","Residues 28 to 208 (E_value = 4.4e-42) place ANA_2049 in the ABC_tran family which is described as ABC transporter.","","protein Irp6C (III)","","1","","","","","","","","","","","Tue Aug 14 16:54:46 2007","","Tue Aug 14 16:54:46 2007","","","Tue Aug 14 16:54:46 2007","Tue Aug 14 16:54:46 2007","","","Tue Aug 14 16:54:46 2007","Tue Aug 14 16:54:46 2007","","","","","yes","","" "ANA_2050","2218999","2217824","1176","10.62","10.10","39955","ATGGGGGACCCCCACGTCACGGCTCCTTCCGACGACGTCGCAGCGCACCAGTCCGATACCGGCCGGGTACCGGACGGTGCGGCGTCGACGACGAAGGCCGACGGGCCGGCCGATGCGCCCACGGACACGGCGGCGTCGGCCTACGCCTCCTACCGCCGTCGAACCGCGCGGCGAGTCGCGATGCTCCTGGGGCTGGCCACGCTGCTCCTGACCGTCTTCCTCGTGGCCCTCATGGTGGGGCCCCTGGGGTTCAGCCCGGCCCAGGTGCTCGGAGCCCTCTTCGACGCCGACTACGACCCGTGGGTCGCCAACATCGTCATCAACCTGCGCCTGCCGCCGGCACTGCTTGCGGTCCTGGTCGGCGGGGCACTGTCCCTGGCCGGCGTGCAGATGCAGACCATCCTCGACAACCCGCTGGCCGAGCCCTTCACCCTGGGCATCTCGGCGGCCTCGGCCCTGGGGGCGGCGCTGGCCATCGTCACGGGCCTCGTGCTGCCTGTGGCCACCGGCGCCACCCTGCCGATCGTGGCGATGACGGCGGGGCTGGCGGCCTCCCTCACCATTGCGATGGTCTCGAGGCTGCCCTCGGTGACCAAGGAGATGACGATCCTGCTGGGCATCGCCCTGGTCTTCAGCTGCCAGGCGCTCCTGGCGCTCGTGCAGTACCGGGCCTCCACCGAGAGCCTTCAGCAGATCGTGTTCTGGTCGATGGGCTCCCTCATGCGCGCCACCTGGCCGGCCGTGGGCACCGTCTCGGCGGCCCTGCTCGTGGCCACGCCCGTCTTCTGGGTCAACGGCTGGCGGCTGACCGCCGTCACCCTGGGGGAGGCGCGCGCCGCAGCCATGGGCATCAACGTGGCGCGCCTGCGGGCGTGGACCCTGGTCGGCGTCTCGTTGCTGGCCGCCCTGTCCGTGGCCTTCGTCGGGATCATCGGATTCGTGGGGCTCGTGGGGCCGCATATGGCCCGCGGCCTGGTGGGGGAGGACCAGCGCTTCCTCGTGCCCGCCTCCATCCTGTGCGGCGCCACCCTGCTGACCGCCGCCCACACCGCCAGCCAGCTCATCGTGCCGGGTGTCGCCGTGCCCGTCGGCATCCTGACCGCCCTGGTGGGTGTGCCGGTATTCCTCACCATCATCTTCGGACGCCAGCGCTCGGCGGTCAGGAGCGGTTCATGA","MGDPHVTAPSDDVAAHQSDTGRVPDGAASTTKADGPADAPTDTAASAYASYRRRTARRVAMLLGLATLLLTVFLVALMVGPLGFSPAQVLGALFDADYDPWVANIVINLRLPPALLAVLVGGALSLAGVQMQTILDNPLAEPFTLGISAASALGAALAIVTGLVLPVATGATLPIVAMTAGLAASLTIAMVSRLPSVTKEMTILLGIALVFSCQALLALVQYRASTESLQQIVFWSMGSLMRATWPAVGTVSAALLVATPVFWVNGWRLTAVTLGEARAAAMGINVARLRAWTLVGVSLLAALSVAFVGIIGFVGLVGPHMARGLVGEDQRFLVPASILCGATLLTAAHTASQLIVPGVAVPVGILTALVGVPVFLTIIFGRQRSAVRSGS$","ABC-type cobalamin/Fe3+-siderophores transport system, permease component","Membrane, Cytoplasm","membrane protein permease Irp6B","K02015 iron complex transport system permease protein","transport system permease protein","","","","","

InterPro
IPR000522
Family

Bacterial transport system permease protein
PF01032	$\"[105-413]T$	FecCD

noIPR
unintegrated

unintegrated
tmhmm	$\"[96-116]?$ $\"[146-166]?$ $\"[181-203]?$ $\"[209-229]?$ $\"[239-259]?$ $\"[281-301]?$ $\"[328-348]?$ $\"[396-416]?$	transmembrane_regions

","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 7","***** IPB000522 (FecCD transport family) with a combined E-value of 5.1e-46. IPB000522A 147-188 IPB000522B 272-282 IPB000522C 342-360 IPB000522D 395-418","","","-48% similar to PDB:2NQ2 An inward-facing conformation of a putative metal-chelate type ABC transporter. (E_value = 2.4E_18);-41% similar to PDB:1L7V Bacterial ABC Transporter Involved in B12 Uptake (E_value = 3.5E_14);-51% similar to PDB:1MG1 HTLV-1 GP21 ECTODOMAIN/MALTOSE-BINDING PROTEIN CHIMERA (E_value = 3.5E_14);","Residues 105 to 418 (E_value = 1.7e-74) place ANA_2050 in the FecCD family which is described as FecCD transport family.Residues 159 to 415 (E_value = 0.039) place ANA_2050 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component.","","protein permease Irp6B (III)","","1","","","Wed Aug 8 10:02:04 2007","","Wed Aug 8 10:02:04 2007","","","Wed Aug 8 10:02:04 2007","Wed Aug 8 10:02:04 2007","Wed Aug 8 10:02:04 2007","Tue Aug 14 16:54:24 2007","","","","","Wed Aug 8 10:02:04 2007","Wed Aug 8 10:02:04 2007","","","Wed Aug 8 10:02:04 2007","Wed Aug 8 10:02:04 2007","","","","","yes","","" "ANA_2051","2220171","2218999","1173","8.35","3.86","42634","ATGCGCCGTCGTACCCTGCTCATGGCCCTCCCACTGACCGCCGTCCTCGCCAGCTGCGGAGTCGCCTCCCGCGCCGGCAAGGGCTCCAGCGCCGGCGCCTCCGCGGGCGCCTCCAACGGCGGCTTCGAGGTCACCGACGTCGTCGGCCGCAAGGTCACCTTCAGCGCCCAGCCCCAGAGGATCGTCCTGAGCGAGTCTCGCCACGTCTACTCCCTGGCCTTCCTCAACAAGACCAACCCCATCGACAAGGTGGTCGCCTGGGGTGAGGACCTCCAGAAGGCCGCCCCCGACTTCTACGAGAAGATCCTCTCCGTGGCCCCCAAGGCCGCCGACCTGCCGAAGATCGGCAACATCGCCAAGGACGGCCTGCCCATCGAGACCCTGGTGAGCCACAAGCCCGACGTCTTCATCATGACTCTGGACGCCTACAACTCCGCTAAGGAGAAGGGCTACCTCGAGAAGCTGGACGGCCAGAAGATCACCTACGTCGTCACCGACTTCCGCCGCGACCCGGTGAAGAACACCGTCCCCTCGGTCACCCTCATGGGCGCCATCTTCGACAAGCGCAAGGAGGCCGAGACCTTCGTCAGCTTCTACAAGAAGCAGGTCGATCCCATCGTGGCCAAGGCGAAGTCCCTGAGCTCAAAGCCCACCACCTTCCTGTGGCGCAGCCCGGGCGTCAACGACCCCGGCGCCACCTACTCCACCGCGAACCTCGGTGCGATCGTCACCGCCACCGGCGGCACCAACATCGCCGACAGCCTCCTGTCCGGCGAGGAGGGCGTGCTCACCCCCGAGCAGGTCATCGCCTCCAACCCCCAGCACATCATCGCCACCGGCGGCGAGTGGCAGCAGCAGAAGATCAAGGACACCGCCCAGACCAGCTACGTCCACCTCGGCTACAAGGCCGACGAGGCCTCCGCCAAGGCCAGCCTGGAGCAGCTGAAGAACCAGCCCGGCTACGACCAGATCCAGGCCTTCACCGACCGGCACGTCTACGGCATCTACCACCAGTTCTACGACGCCCCCTACAACTTCATCGCCTACCTCACCTTCGCCAAGTGGCAGAACCCCGAGGCATTCTCCGACGTCGACCCCGCCAAGGTCTGGAAGGACTTCCACGAGCAGCACATGCCCTGGAAGGCCGAGGGCGTCTTCTTCGCCGCGATCTGA","MRRRTLLMALPLTAVLASCGVASRAGKGSSAGASAGASNGGFEVTDVVGRKVTFSAQPQRIVLSESRHVYSLAFLNKTNPIDKVVAWGEDLQKAAPDFYEKILSVAPKAADLPKIGNIAKDGLPIETLVSHKPDVFIMTLDAYNSAKEKGYLEKLDGQKITYVVTDFRRDPVKNTVPSVTLMGAIFDKRKEAETFVSFYKKQVDPIVAKAKSLSSKPTTFLWRSPGVNDPGATYSTANLGAIVTATGGTNIADSLLSGEEGVLTPEQVIASNPQHIIATGGEWQQQKIKDTAQTSYVHLGYKADEASAKASLEQLKNQPGYDQIQAFTDRHVYGIYHQFYDAPYNFIAYLTFAKWQNPEAFSDVDPAKVWKDFHEQHMPWKAEGVFFAAI$","ABC-type cobalamin/Fe3+-siderophores transport system, periplasmic component","Extracellular, Periplasm, Membrane","ferrisiderophore receptor Irp6A","K02016 iron complex transport system substrate-binding protein","periplasmic binding protein","","Mahe B., Masclaux C., Rauscher L., Enard C., Expert D. Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: characterization of a novel ferrisiderophore permease of the ABC transporter family. Mol. Microbiol. 1995. 18(1):33-43. PMID: 8596459Borths E.L., Locher K.P., Lee A.T., Rees D.C. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proc. Natl. Acad. Sci. U.S.A. 2002. 99(26):16642-16647. PMID: 12475936","","","

InterPro
IPR002491
Family

Periplasmic binding protein
PF01497	$\"[58-339]T$	Peripla_BP_2
PS50983	$\"[60-364]T$	FE_B12_PBP

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1980	$\"[57-200]T$	no description
PS51257	$\"[1-19]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-22]?$	signal-peptide

","BeTs to 9 clades of COG0614COG name: Ferrichrome-binding periplasmic proteinsFunctional Class: PThe phylogenetic pattern of COG0614 is aM-K--VCEBRhUJ-------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 339 (E_value = 9e-06) place ANA_2051 in the Peripla_BP_2 family which is described as Periplasmic binding protein.","","receptor Irp6A (III)","","1","","","","","","","","","","","Tue Aug 14 16:53:58 2007","","Tue Aug 14 16:53:58 2007","","","Tue Aug 14 16:53:58 2007","","","","Tue Aug 14 16:53:58 2007","Tue Aug 14 16:53:58 2007","","","","","yes","","" "ANA_2052","2220562","2220392","171","11.60","2.92","5868","GTGGTTGTGGTGCTCAACGTGATGGTGGCTGTCGTCTCCTTCCGGCGGGGAGACACCTCGGCCATGGTCATCGCCATTGCTGTTGCCGCGCTCTTCCTGATCCAGCTGGCCCGTTCATCCTCCGACGGTAGAGGCCGTGGTCGAGACGACCGGACGCCTCCGAGCTCATGA","VVVVLNVMVAVVSFRRGDTSAMVIAIAVAALFLIQLARSSSDGRGRGRDDRTPPSS$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[19-37]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PTHR11219	$\"[169-236]T$	TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE
PTHR11219:SF2	$\"[169-236]T$	N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[57-222]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
PTHR10859	$\"[62-303]T$	GLYCOSYLTRANSFERASE RELATED
tmhmm	$\"[279-297]?$ $\"[303-321]?$ $\"[336-356]?$ $\"[362-382]?$	transmembrane_regions

","BeTs to 12 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 57 to 222 (E_value = 1.2e-06) place ANA_2056 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","glycosyl transferase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2057","2223856","2223587","270","4.95","-5.34","9873","ATGAGCGCCAGAATTGGTTCCATCCAGCAGTTCCTTCTCATCTATGACCGTAAGCGAGATGAGCTCTTGTCTCACGAGTCGTTCGGAGATGATGTTGTGGCCGCAACTACTGCATACCGTGCCGCTGAGATCGAGTACCAGAATCACCCCGAGATGGACATCGTGCTTGTCGGAGCTGAATCATTGGAGACGATTAAAGTCACGCACAGCACCTACTTCACCGGATCAGCCGCGCGCCTCCTTGATGAGATTCGCGCCGGTGTGAGTTGA","MSARIGSIQQFLLIYDRKRDELLSHESFGDDVVAATTAYRAAEIEYQNHPEMDIVLVGAESLETIKVTHSTYFTGSAARLLDEIRAGVS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-3]?$	signal-peptide

InterPro
IPR007685
Domain

RelA/SpoT
PF04607	$\"[4-41]T$	RelA_SpoT

noIPR
unintegrated

unintegrated
PTHR21262	$\"[4-43]T$	GUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE

","BeTs to 14 clades of COG0317COG name: Guanosine polyphosphate pyrophosphohydrolases/synthetasesFunctional Class: T,KThe phylogenetic pattern of COG0317 is -----qvcEbrHujgpo----Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","Residues 4 to 41 (E_value = 2.3e-08) place ANA_2057.1 in the RelA_SpoT family which is described as Region found in RelA / SpoT proteins.","","","","1","","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:53:05 2007","Wed Aug 15 17:53:05 2007","Wed Aug 15 17:53:05 2007","Wed Aug 15 17:51:47 2007","","Mon Aug 20 18:22:46 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Mon Aug 20 18:22:46 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Wed Aug 15 17:51:47 2007","Mon Aug 20 18:22:46 2007","","Wed Aug 15 17:51:47 2007","","Wed Aug 15 17:51:47 2007","yes","","" "ANA_2058","2224977","2224246","732","5.22","-5.63","25815","ATGACGGACTCCAGCAACGCGCCGACCGACAAGACCGACAAGACCGACGAGGCTCCCGGCGCCCCCATCCGAGTCCTCATCGCCGAGGACCAGGCCCTCCTGCGCACCACCCTGGCCGCCCTGCTCGAGGCCGAGCCCGGCATGAGCGTCGTCGGCCTGGCCGAGGACGGTGCCCGTGCGGTCGCCCTGGCCGCCGAGCTGCGCCCCGACGTCGTCCTCATGGACATCCAGATGCCGGGCCTGACCGGCATCGAGGCCACCAGAAGGATCTGCGCCGACCCGGCGCTCGCGGCCACGCGCGTCCTCATCCTCACCATGTTCGAGATTGACGACTACGTCCTGGGCGCCCTGCGCGCCGGCGCCTGCGGCTTCCTCCTCAAGGATGCCGACCCCCAGTCCCTCGTTGACGCCGTGCGCACCGTCCATGAGGGGCAGTCACTGCTCAGCCCCCAGGTGCTGGCCCGCCTCGTGGCCCGCATGCCGCGCACGACGTCGACCGGCACCTCCCGTAGCACCTGGACCGGTGAGGTCGAGGCCCTCACGCCCCGCCAGCGCGAGGTGCTGCTGCTCATCGCCCGGGGCTTGTCCAACAGTGAGATCGAGGTCGAGCTCGGCATCACCCGGGCCACTTGCCGCAGTCACATCACCGCGCTCCTGGCCCGTCTGGGCGCCCGCGACCGCGCCCAGCTCGTCATCGCCGCCTACGAGGCCGGCCTCATCAGCCCCCGCTGA","MTDSSNAPTDKTDKTDEAPGAPIRVLIAEDQALLRTTLAALLEAEPGMSVVGLAEDGARAVALAAELRPDVVLMDIQMPGLTGIEATRRICADPALAATRVLILTMFEIDDYVLGALRAGACGFLLKDADPQSLVDAVRTVHEGQSLLSPQVLARLVARMPRTTSTGTSRSTWTGEVEALTPRQREVLLLIARGLSNSEIEVELGITRATCRSHITALLARLGARDRAQLVIAAYEAGLISPR$","Two-component system response regulator","Cytoplasm, Membrane","response regulator of two-component system","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[180-215]T$	Q9S285_STRCO_Q9S285;
PR00038	$\"[180-194]T$ $\"[194-210]T$ $\"[210-222]T$	HTHLUXR
PF00196	$\"[177-234]T$	GerE
SM00421	$\"[177-234]T$	HTH_LUXR
PS50043	$\"[173-238]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[23-141]T$	Q9X8S0_STRCO_Q9X8S0;
PF00072	$\"[23-139]T$	Response_reg
SM00448	$\"[23-138]T$	REC
PS50110	$\"[24-142]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[153-240]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[18-146]T$	no description
PTHR23283	$\"[24-142]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF47	$\"[24-142]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (DHKB)

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[197-290]T$	HATPase_c
SM00387	$\"[197-291]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[62-128]T$	HisKA_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[19-39]?$	transmembrane_regions

","BeTs to 7 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 1.2e-12. IPB011712A 61-78 IPB011712B 202-222","","","No significant hits to the PDB database (E-value < E-10).","Residues 62 to 128 (E_value = 2e-11) place ANA_2059 in the HisKA_3 family which is described as Histidine kinase.Residues 197 to 290 (E_value = 1.4e-11) place ANA_2059 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2061","2226160","2226963","804","10.31","7.15","27683","ATGATCGCTATTGAGAATCTCGTCAAGCGGCACGGGGTGCGGGAGGTGCTTCACGGCGTGAGCCTGGAGGCGCGTCCGGGCCGCGTCACCGGATTCGTGGGGCCGAATGGCGCCGGTAAGTCCTCGACCCTGCGGTGTCTGCTGGGTCTGGACCGGGCCGACGGCGGGCGGGCGCTTATCGGTGGGCGCACCTACCGCGAGCTGCGTGAGCCGCTGCGCACGGTGGGGGCGGTGCTCGACGGCTCGGGCGCGCATCCCTCGCGCACGGCCCGCGGTCACCTGGGTTGGGTGGCCTCGGGTGCGGGAATCAGTCGGCGTCGGGTGGCTGAGGTGCTCGACGTCGTCGGGCTGAGTGAGGCGGCCGGGCGGCGGGTGCGCACCTTCTCCCTGGGAATGGGGCAGCGCCTGGGGCTAGCGACGGCGCTGCTGGGTGACCCGGAGGTGCTCATCCTCGACGAGCCGGTCAACGGCCTGGACCCGGAGGGGATCCGGTGGATCCGCAGGCTGCTTCGGCAGCGGGCCGATGCCGGGGGCACGGTCCTGCTGTCCAGTCATGTTCTAGCTGAGCTGGCTGAGGTGGCTGACGACGTCGTCGTCATCGCCAGCGGGCGGGTGCGGGCGGCCGGGACGCTGGAAGAGGTCGCGGCGGGCTACGCGAACCTGGAGGAGGCGTTCTTCTCACTGACCGCCCCGACCGGGGGCGAGGTCGGCAGCGGGGTCGGCGGTGGGGCCGGTCAGGCTGGCCGGACTGGACGAGCCGACCGGGCGGGCCGGGCCGAGCGCAAGGAAGGAGTCCGTTCGTGA","MIAIENLVKRHGVREVLHGVSLEARPGRVTGFVGPNGAGKSSTLRCLLGLDRADGGRALIGGRTYRELREPLRTVGAVLDGSGAHPSRTARGHLGWVASGAGISRRRVAEVLDVVGLSEAAGRRVRTFSLGMGQRLGLATALLGDPEVLILDEPVNGLDPEGIRWIRRLLRQRADAGGTVLLSSHVLAELAEVADDVVVIASGRVRAAGTLEEVAAGYANLEEAFFSLTAPTGGEVGSGVGGGAGQAGRTGRADRAGRAERKEGVRS$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Membrane, Extracellular","ABC-type transporter, ATPase component","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[128-170]T$	Q6NF51_CORDI_Q6NF51;
PF00005	$\"[27-203]T$	ABC_tran
PS50893	$\"[2-227]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[26-204]T$	AAA

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[114-131]?$	SUGAR_TRANSPORT_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-218]T$	no description
PTHR19222	$\"[2-231]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[66-86]?$ $\"[123-143]?$ $\"[162-182]?$ $\"[187-207]?$ $\"[242-264]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[35-55]?$ $\"[76-105]?$ $\"[111-133]?$ $\"[138-158]?$ $\"[184-204]?$	transmembrane_regions

InterPro
IPR003615
Domain

HNH nuclease
SM00507	$\"[162-215]T$	HNHc

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-37% similar to PDB:2GTQ Crystal structure of aminopeptidase N from human pathogen N. meningitides (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2065","2229729","2230169","441","5.50","-6.36","15660","ATGATTCACCCACGAGACGTCACGACTGAAGCCGAGGCGGCGGTGCTTGAACACGCTGATCGCCTCGCCGCCGTCATCGGCAAGCACTGGCACCCCACGGACGACACCGCTACAGACGACGTCATGCTGCTCGTTGCCGATCTCCTGCGCGCTCACGCCGAGACCGGGATTGAGATGCAGACCTGGAGAGCGGCGCTCGACGTCGTTATGGATCATCTCGCCGCCGAGCCTGAAGGCGGCGATCTGCTCCACCGCCTCGGCCGGCCGGCCTGGTTCACCGTCATCGGCACGACCAAGGACGGCCAGAGAGAACCCGTCGCCGTCCTGCCGGGACGCCGCCGCCCGGAGGTAGCCATCGGCGCCTGGAGCACACAGGTTCAGGCACCCACCGCAGCAGACGCCGTCCGAGCCGCGTCAAGTGGGGACCGGCCTGCAGCCTGA","MIHPRDVTTEAEAAVLEHADRLAAVIGKHWHPTDDTATDDVMLLVADLLRAHAETGIEMQTWRAALDVVMDHLAAEPEGGDLLHRLGRPAWFTVIGTTKDGQREPVAVLPGRRRPEVAIGAWSTQVQAPTAADAVRAASSGDRPAA$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2066","2230444","2230941","498","4.53","-10.08","15533","GTGCTCTCCTGCTTCCGCTCCGGCGCAGGTGCGGGAGCCGCCCCACCACCGCCGGCCTGCGGTTCCGCCTCCTGTGTCGGCTCCGACTCTTGTGTCGGCTCGGACTCCTGCATGAGAGGCTGTAACGGAGGCTGCGTCGTCGGGGCTTGCGTCGTCGGAATCGGCGACGGCGTTGGACTCGGGGTCGGGGATGGGGTGGGACTCGGAGTAGGCGACGGGGAGGGAGTCGGAGTAGGTGACGGCGACGGCGAAGCAGTCACCGTCGGAGATGTTGCCGGTACAGGCGACCCCGCATCGTCAGCCACAGACGGAACCCCACACCCGGCGATTCCAACGCCAAGAACCAGGGCGAGGAGGACGGGCGCCGCCGCCCTCAGCATCCCCCGACGCTGCGGCGTTGACGAAGGCAGTGACTCCACAGAAGAGCGGGACAATATAGGAGAAATAGGGGACAACATGGGCGTGCTCACGAAAGCCTCAAGTAACGAGAAGGGATGA","VLSCFRSGAGAGAAPPPPACGSASCVGSDSCVGSDSCMRGCNGGCVVGACVVGIGDGVGLGVGDGVGLGVGDGEGVGVGDGDGEAVTVGDVAGTGDPASSATDGTPHPAIPTPRTRARRTGAAALSIPRRCGVDEGSDSTEERDNIGEIGDNMGVLTKASSNEKG$","Lipoprotein","Extracellular","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-13]?$	signal-peptide

InterPro
IPR000415
Family

Nitroreductase
PF00881	$\"[28-190]T$	Nitroreductase

noIPR
unintegrated

unintegrated
G3DSA:3.40.109.10	$\"[22-212]T$	no description
PIRSF000232	$\"[22-212]T$	NADH dehydrogenase/NAD(P)H nitroreductase
PTHR23026	$\"[53-211]T$	NADPH NITROREDUCTASE
PTHR23026:SF43	$\"[53-211]T$	NADPH NITROREDUCTASE

","BeTs to 11 clades of COG0778COG name: NitroreductaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0778 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000415 (Nitroreductase family) with a combined E-value of 1.4e-10. IPB000415A 57-80 IPB000415B 140-165","","","-42% similar to PDB:1NOX NADH OXIDASE FROM THERMUS THERMOPHILUS (E_value = 5.6E_13);","Residues 28 to 190 (E_value = 7e-10) place ANA_2067 in the Nitroreductase family which is described as Nitroreductase family.","","(AE005300) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2068","2233412","2232372","1041","4.64","-21.35","36489","ATGACCGCAGGCCTTGCCGTGGCGACGGCCACCGCCTGCTTCCCGGTCCAGCCCCAGGGTGCAAACCCAGCGGCTGCGGCGCCGTCGACCAGCCTCAGCGCCGAGCAGGCATTCTCCAGCGGCCCGGCCGGCACGGCGGCCTCGGCGACATCGGTCGGTGACGTCTCCACGCCGGCGGCGCCGTCGTCGAGCATGGGGGAGCCGACCGCTGCCGCCCCCTCCGGTGAGCCCTCAGTCTCGCCGAACGGGACCGCAGGCTCCCCGTCCGACGCTGCAACCGCCTCGCCCTCGCAGCTCTCTGAGGCTCCGGGTTGGGGACGCTCCGATGCTGAGATCAACGGCTGGAGCGTCGACTATTTCGAGGGCTTCGACGGCTCCTTCGAGGATACGAAGTGGGGGCACTACGGGTGGAAGGATCCAGAGGTTGGGCATGGGGCCATGGGCGTGATGTCACAGAAGAACTCCTTCGTTGAGAACGGTCATCTCGTCATCCGCACCCAGTACCAGGACGGTCAGTGGAGCGCCGGCGGCGCCTCGAGCGCTGATGCTTTTGCGGCTTCGCGCGGCCGGTGGGAGGTGCGGGCCAAGTTCCCCCGGGGTAAGGGAATCGGTTACGCCTTCCTGCTGTGGCCCCAGGATGAGCGCTGGCCCCCGGAGATCGACTTCGCCGAGGGGCGCGTCAATGGGCCGCAGGTGTCGGGCACCTACCACTGGGGTGACTCCACTGAGGAGGGGCACAAGCAGGACCAGCGGGTCTTCGACAACACGGACATGGGCGGCTGGCACACCTACGGCGTCATCGTGGAGGAGGACTACATCGTCTTCACCTTCGATGGCCAGGAGTGGGGTCGGATCACGCGGGACGACGTCGGCGAGGGCATCACTGACAAGCGGATGTGGTTCGGGGTTCAGACCGGGGCGATGGATCCCAATGGGAAGGCGAACCAGTACGAGACCGTCGACGGCGGTGTCCCCGGCCCGCTCACTCCGGCCGTCTCCGACATCCAGATCGACTACGTCGCCCACTACACCAGGGGGTAG","MTAGLAVATATACFPVQPQGANPAAAAPSTSLSAEQAFSSGPAGTAASATSVGDVSTPAAPSSSMGEPTAAAPSGEPSVSPNGTAGSPSDAATASPSQLSEAPGWGRSDAEINGWSVDYFEGFDGSFEDTKWGHYGWKDPEVGHGAMGVMSQKNSFVENGHLVIRTQYQDGQWSAGGASSADAFAASRGRWEVRAKFPRGKGIGYAFLLWPQDERWPPEIDFAEGRVNGPQVSGTYHWGDSTEEGHKQDQRVFDNTDMGGWHTYGVIVEEDYIVFTFDGQEWGRITRDDVGEGITDKRMWFGVQTGAMDPNGKANQYETVDGGVPGPLTPAVSDIQIDYVAHYTRG$","Glycoside hydrolase, family 16","Extracellular","Endo-1,3-1,4-beta-glycanase exsH(Succinoglycanbiosynthesis protein exsH)","hypothetical protein predicted by Glimmer/Critica","glycoside hydrolase, family 16","","Sanz-aparicio J., Hermoso J., Grangeiro T.B., Calvete J.J., Cavada B.S. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett. 1997. 405(1):114-118. PMID: 9094437Ackerman S.J., Liu L., Kwatia M.A., Savage M.P., Leonidas D.D., Swaminathan G.J., Acharya K.R. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. J. Biol. Chem. 2002. 277(17):14859-14868. PMID: 11834744Hahn M., Pons J., Planas A., Querol E., Heinemann U. Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett. 1995. 374(2):221-224. PMID: 7589539Michel G., Chantalat L., Duee E., Barbeyron T., Henrissat B., Kloareg B., Dideberg O. The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases. Structure 2001. 9(6):513-525. PMID: 11435116","","","

InterPro
IPR000757
Domain

Glycoside hydrolase, family 16
PF00722	$\"[142-321]T$	Glyco_hydro_16

InterPro
IPR013320
Domain

Concanavalin A-like lectin/glucanase, subgroup
G3DSA:2.60.120.200	$\"[102-343]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 142 to 321 (E_value = 7.8e-09) place ANA_2068 in the Glyco_hydro_16 family which is described as Glycosyl hydrolases family 16.","","exsH (Succinoglycanbiosynthesis protein exsH) (glcA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2070","2233955","2233566","390","4.25","-13.04","14581","ATGAGTTACGACCTCCTGATCTTCGAGCCGGACTCCACGACCGATGAGGACTTCCCCCAGTGGTGGAAGCAGGTGGTCGCCCAGTGGGACGGGCCGCGCGACTTCAGCACCATCGACGGCTCCACCCCGGCGATCAGGTCTATCTACCGCGACCTCATCCGCGCCTTTCCGCCGTTCAACGGCCCCGACGCGCTGAGTGAGGCGGAGTTGGAGGAGCGGGAGGTCGAAGGGCTGCCGGTCGCCGACTACACCATCGGCGCCGACTACATCTACATCAGCGTCGGCTGGTCGGACGCGAACGCGCTGGTCAAGATCGTCGGCCAGATGGCCTGGACGCAGCGACTCGCGGTCGCCTATGTCAGCGAGGACAACTCGATCTTCCGGCCCTAG","MSYDLLIFEPDSTTDEDFPQWWKQVVAQWDGPRDFSTIDGSTPAIRSIYRDLIRAFPPFNGPDALSEAELEEREVEGLPVADYTIGADYIYISVGWSDANALVKIVGQMAWTQRLAVAYVSEDNSIFRP$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2071","2235832","2234081","1752","5.43","-17.25","65090","ATGAACGACACCAACCTGCCCGAGACCCCTCAGGACGGTGCTCCCGCCGGCTGCCCCATGTCCCGCGCTGGCCTCGGCGAGCACCTGCCCAGCCGCAACAACGCCGCCGGCCAGGGCCGCATGACGATGGCCAACGGCTCGCCCGTCTACAACAACCAGGACTCCATGACCGCCGGGCCCCGCGGTCCCGTCGCCCTCCAGGACGCCTGGCTGCTGGAGAAGCACGCCCACTTCAACCGCGAGGTCATCCCCGAGCGCCGCATGCACGCCAAGGGCTCGGGCGCCTGGGGCACCTTCACCGTCACCCGCGCCATTCCCGAGCTCACCCGCGCCGCGATCTTCTCCGCCGAGGGCAACCAGTGCGAGCTCTTCATGCGCTTCTCCACCGTCGCCGGGGAGCGCGGGGCCGCCGACGCCGAGCGCGACATCCGCGGCTTCGCCATGCGTTTCTTCACCTCCGAGGGAAACTGGGACGTCGTCGGCAACAATACCCCCGTCTTCTTCTTCCGTGACGGCAAGAAGTTCATCGACCTCAACCACGCCGTCAAGCGCGACCCCCGCACCAACCTGCGCAGCCCCAACACCAACTGGGACTTCTGGACCAGCCTGCCTGAGTCGCTCCTCCAGGTGACCATCACCATGTCCGACCGCGGCATCCCGCTGTCCTACCGCTACATGCACGGCTTCTCCTCGCACGCCTACTCCTTCATCAACGCCGAGGGCGTGCGCACCTGGGTCAAGTTCCACTTCCGCTCCCAGCAGGGTCTCGCCAACCTCACGGACCAGGAGGCCGCCACCGTCATCGCCGAGGACCGCGAGTCCAACCAGCGTGATCTGTACGAGTCCATCGAGAAGGGCCAGTACCCCCGCTGGACCATGTACGTCCAAACCATGACCGTTGAGCAGGCCGAGGCCCTGACCGACTTCAACCCCTTCGACCTGACGAAGATGTGGCCCAAGGCGGACTTCCCCTTCCAGGAAGTCGGCGTCCTCGAGCTCAACAGGAACCCCGACAACTACTTCCAGGACGTCGAGCAGGCCGGCTTCACGCCCCAGAACATCGTGCCCGGCATCGGCTACTCGCCGGACAGGATGCTCCAGGCCCGCCTCTTCTCCTACGGTGACGCTCAGCGCTACCGCCTCGGCGTCAACCACCACCAGATTCCGGTCAACTCCCCGCGCGGCGTCGCCTGCCCCCACGGCTTCCACCGCGACGGCGCCATGCGGGTGGACGGCAACGCCGGGTCCCAGAACGCCTACGAGCCCAACTCCTACGGCAACTGGCAGGACTCGCGCGAGCTCTCCGAGCCCGTCCAGGCCGGAGGCGACGTCGCCATGTACGACTTCCGCGAGGACGACCACAACTACTACACCCAGCCCGGCATGCTCTGGCGCGCCATGACGCCCGAGCAGCAGCTCGTCCTGTGCGAGAACACCGCCCGCGCCATGGGGGACTCGACCCTGCAGATCAAGCACCGCCACATCTTCAACTGCTACCACGCGGACCCCGACTACGGCCGTGGCGTGGCCCAGGCGCTGGGCATCGACATCGACAGCGTGGACCTCGACGGCGCCACCGCCGACTCCTACGAGCTGTGGCTCGCGCGCAACCGCGCCAACGCCGAGCTCGACGTCCCGACGTCGCCCGCGGCCCCCGCCTCGGCCGCGAACCTCGGCCCGGCCGGCCGCGACACCAACGTGGCTGACCCGACCACCCTGACCGACCCGATGAACGACCCCTACGTGCTCTGA","MNDTNLPETPQDGAPAGCPMSRAGLGEHLPSRNNAAGQGRMTMANGSPVYNNQDSMTAGPRGPVALQDAWLLEKHAHFNREVIPERRMHAKGSGAWGTFTVTRAIPELTRAAIFSAEGNQCELFMRFSTVAGERGAADAERDIRGFAMRFFTSEGNWDVVGNNTPVFFFRDGKKFIDLNHAVKRDPRTNLRSPNTNWDFWTSLPESLLQVTITMSDRGIPLSYRYMHGFSSHAYSFINAEGVRTWVKFHFRSQQGLANLTDQEAATVIAEDRESNQRDLYESIEKGQYPRWTMYVQTMTVEQAEALTDFNPFDLTKMWPKADFPFQEVGVLELNRNPDNYFQDVEQAGFTPQNIVPGIGYSPDRMLQARLFSYGDAQRYRLGVNHHQIPVNSPRGVACPHGFHRDGAMRVDGNAGSQNAYEPNSYGNWQDSRELSEPVQAGGDVAMYDFREDDHNYYTQPGMLWRAMTPEQQLVLCENTARAMGDSTLQIKHRHIFNCYHADPDYGRGVAQALGIDIDSVDLDGATADSYELWLARNRANAELDVPTSPAAPASAANLGPAGRDTNVADPTTLTDPMNDPYVL$","Catalase","Cytoplasm, Periplasm","Catalase","catalase ","Catalase","","Chelikani P., Fita I., Loewen P.C. Diversity of structures and properties among catalases. Cell. Mol. Life Sci. 2004. 61(2):192-208. PMID: 14745498Safo M.K., Musayev F.N., Wu S.H., Abraham D.J., Ko T.P. Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallogr. D 2001. 57:1-7. PMID: 11134921Reiter R.J., Tan D.X., Osuna C., Gitto E. Actions of melatonin in the reduction of oxidative stress. A review. J. Biomed. Sci. 2000. 7(6):444-458. PMID: 11060493","","","

InterPro
IPR002226
Family

Catalase
PD000510	$\"[46-523]T$	Q8PU00_METMA_Q8PU00;
PR00067	$\"[55-78]T$ $\"[118-136]T$ $\"[139-156]T$ $\"[158-176]T$ $\"[324-351]T$ $\"[356-382]T$	CATALASE
PTHR11465	$\"[117-523]T$	CATALASE
PS00437	$\"[369-377]T$	CATALASE_1
PS00438	$\"[78-94]T$	CATALASE_2

InterPro
IPR011614
Domain

Catalase, N-terminal
G3DSA:2.40.180.10	$\"[29-532]T$	no description
PF00199	$\"[42-429]T$	Catalase

","BeTs to 10 clades of COG0753COG name: CatalaseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0753 is ------y--d--b-efgh-nuj----Number of proteins in this genome belonging to this COG is 1","***** IPB002226 (Catalase) with a combined E-value of 8.1e-139. IPB002226A 63-114 IPB002226B 127-177 IPB002226C 197-231 IPB002226D 262-315 IPB002226E 342-393","","","-75% similar to PDB:2ISA Crystal Structure of Vibrio salmonicida catalase (E_value = 2.3E_176);-74% similar to PDB:1M85 Structure of Proteus mirabilis catalase for the native form (E_value = 4.3E_167);-74% similar to PDB:1MQF Compound I from Proteus mirabilis catalase (E_value = 4.3E_167);-74% similar to PDB:1NM0 Proteus mirabilis catalase in complex with formiate (E_value = 4.3E_167);-74% similar to PDB:2CAG CATALASE COMPOUND II (E_value = 4.3E_167);","Residues 42 to 429 (E_value = 1.8e-249) place ANA_2071 in the Catalase family which is described as Catalase.","","(hktE) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2072","2237067","2236129","939","5.11","-10.94","33383","GTGACCTCACCGCAGACACGTCCGCCGACCAACTCACAGACTGCCCAGCCGGCCCGGGTCACTGAGGACGGTGCGGGCCGGGATACCTCCGTCGGCTCGAGGTCCGCGGGTGCCCACATCGGTGGGACCGGCGGAACCGGCGAGCCCGGCCTTCCCGAAACCGAGCTGGGAGCGACCGGGTTTCGGGAGGGTGTCGTTGCCGGCCCCGACCGCCGGCCCGCCGACGACCTGGTGATCGCCGGGCTCGTCCCCATGAGCACGGTCGACTGGCCCGACCGCCTGACCGCGACCGTCTTCATGCAGGGCTGCCCCTGGAACTGCTTCTACTGCCACAACCAGGACCTCATCCCCACCCGCACGCCCGGCCAGGTGGCGTGGGAGGAGGTGCGCGCCCTGCTGCGCCGCCGGCGCGGGCTGCTCGACGGCGTCGTCCTCACCGGCGGAGAGGCCCTGCGCCAGGACGCCCTGGCCGACGCCGCCCGCGAGGTCATCGACATGGGCTTCCAGGTGGGGCTGCACACGGCTGGGCCCTACCCGCGGCGGCTGCGGGACATGATCGAGGCCGGGCTCGTCGACTGGGTGGGGCTGGACATCAAGGCCCTGCCCGAGCACTACGGGCGGGTGGTCGGCCGGGAGGGCGCGGCTGCGAGGGCCTGGGAGAGTCTGGAGGTGCTCATCGAGGCGGCCGGCTGCGGCGGGCCCGACTTCGAGGTTCGCACCACCGTGGTGCCCGGGGATGTGACGGCCGACGACGCCGTCGAGGTGGCTCGGCGGGTGCACGCGGCGGGGGTGCGGGTCTACGCCCTCCAGCAGGCCCGCTCCGAGGGGACGAGCGGCGAATTCGACGTCGTGGCGCCCGGTTGGGACGGGACGTGCGAGCGCATGGCCGAGCGCATCGAGGCCCTGGGCTGGGACCGCTTCACCTACCGCCAGGCGTAG","VTSPQTRPPTNSQTAQPARVTEDGAGRDTSVGSRSAGAHIGGTGGTGEPGLPETELGATGFREGVVAGPDRRPADDLVIAGLVPMSTVDWPDRLTATVFMQGCPWNCFYCHNQDLIPTRTPGQVAWEEVRALLRRRRGLLDGVVLTGGEALRQDALADAAREVIDMGFQVGLHTAGPYPRRLRDMIEAGLVDWVGLDIKALPEHYGRVVGREGAAARAWESLEVLIEAAGCGGPDFEVRTTVVPGDVTADDAVEVARRVHAAGVRVYALQQARSEGTSGEFDVVAPGWDGTCERMAERIEALGWDRFTYRQA$","Anaerobic ribonucleoside-triphosphate reductase activating protein","Cytoplasm","NrdG protein","radical SAM domain protein","anaerobic ribonucleoside-triphosphate reductase activating protein","","Sofia H.J., Chen G., Hetzler B.G., Reyes-spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 2001. 29(5):1097-1106. PMID: 11222759","","","

InterPro
IPR006638
Domain

Elongator protein 3/MiaB/NifB
SM00729	$\"[93-297]T$	Elp3

InterPro
IPR007197
Domain

Radical SAM
PF04055	$\"[97-259]T$	Radical_SAM

InterPro
IPR012840
Family

Ribonucleoside-triphosphate reductase, anaerobic-like
TIGR02495	$\"[78-273]T$	NrdG2: anaerobic ribonucleoside-triphosphat

","BeTs to 8 clades of COG1180COG name: Pyruvate-formate lyase-activating enzymeFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1180 is a-mpkz-qv-rl--efgh--------Number of proteins in this genome belonging to this COG is 2","***** IPB001989 (Radical-activating enzyme) with a combined E-value of 6.6e-10. IPB001989A 89-117 IPB001989B 142-160","","","-54% similar to PDB:2I7G Crystal Structure of Monooxygenase from Agrobacterium tumefaciens (E_value = );","Residues 97 to 259 (E_value = 2.9e-21) place ANA_2072 in the Radical_SAM family which is described as Radical SAM superfamily.","","protein (act)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2073","2239368","2237215","2154","5.17","-25.23","78986","ATGTGTCTCAATGTGGCTCTTGCGGTGTATCTGGGCGTAGGGTCGGCACCGGTGCCGCCGACCGACCCGCTCCCCGCAGGCAGCGCGCAGCCGCTGACGGCACCCGGAAGGACTGGCCCCATCCACGCTCGACGGGGCCGCGAACAGGAACGAGAAGGACCATCGGAGAGACCCGTGCTCGAGAAGAACCTTGCCTCCACCGCTCCCGCAGCTGACGGCTCGGCGCAGCCGCCGGCCGCCACCCCCGCCACCGACCCACGCCTCGTGGCCCCCGGCTCGGCCGACTCCGCCGTCGCCCTCGGCGAGCGCCCCACCGTGGACGCCATCGCCACCATCACCGAGTACCTGGACCGCTCCGACTGGCGCGTCAACGCCAACGCCAACCAGGGATACTCGCTGGGCGGGATGATGCTCAACACCTCCGGCAAGGTCGTCGCCAACTACTGGCTCAGCCAGGTCTACTCGGCCGCCGCCGGCCAGGCCCACCGCAACGCGGACCTCCACATCCACGACCTGGACATGTTCGCCGGCTACTGCGCCGGCTGGTCCCTCAAAGATCTCCTCCAGCAGGGCTTCAACGGCGTCCCCGGCGCCATCGCCGCCGGCCCCGCCAAGCACTTCTCCTCGGCGGTCGGGCAGATCGTCAACTTCCTGGGCACGCTTCAGAACGAGTGGGCCGGCGCCCAGGCCTTCTCCTCCTTCGACACCTACATGGCGCCCTTCGTCCGCCTGGACGACATGACCTACGACCAGGTCAAGCAGTGCATGCAGGAACTCATCTTCAACCTCAACGTCCCCTCGCGCTGGGGCACCCAGACGCCCTTCACCAACCTCACCTTCGACTGGACCTGCCCCGCGGACCTCGCGGACGAGCACCCCCTCATCGGCGACGACGTCTGCGACTTCGCCTACGGCGACCTTCAGGCGGAGATGGACCTCATCAACCGCGCCTTCATGGAGGTCATGACCGAGGGTGACGCCGAGGGCCGCGTCTTCACCTTCCCCATCCCCACCTACAACATCACCCGCGACTTCGACTGGGACGCCCCCAACACCGAGCTGCTGTTCACCATGACCGCGAAGTACGGCCTGCCCTACTTCCAGAACTTCATCAACTCCGAGCTCGACCCCGGCATGATCCGCTCCATGTGCTGCCGCCTCCAGCTCGACCTGCGCGAGCTGCTCAAGCGCGGCAATGGCCTGTTCGGCTCGGCCGAGCAGACCGGCTCGGTCGGCGTCGTCACCATCAACATGGCCCGCCTCGGCTACCTCTACGCCGACGACGAGGCCGCCCTGACTGCCCGGCTCGACGAGCTGCTCGAGATCGGCCGCGACACCCTGGAGCTCAAGCGCACCGTCATCCAGCACCACATCGACGCCGGCCTGTTCCCCTTCACCAAGCGGTACCTGGGCACCCTGGACAACCACTTCTCCACCCTGGGCGTCAACGGCATGAACGAGATGGTTCGCAACTTCACCCGCGACGCCTACGACCTGACCGACCCGCGCGGCCACGCCATGTGCGTGCGCCTCCTGGACCACGTGCGCGACAAGATGGTCGAGTTCCAGGAGGCCACCGGCCACCTCTACAACCTCGAGGCCACGCCGGCCGAGGGCACCACCTACCGCTTCGCCAAGGAGGACCGCAAGCGTTACCCCGGCATCCTCCAGGCCGGTACGGAGACCAACCCCTACTACACGAACTCCTCTCAGATCCCCGTGGGCTACACCGACGACCCCTTCGAGGCCCAGGAGATGCAGGAGGAGCTCCAGACCAAGTACACCGGCGGCACCGTCCTGCACCTGTACATGAACGAGCGGATCTCCTCGGCCGCCGCCTGCAAGGAGCTGGTGCGCCGCTCCCTGACCGCCTTCCGCACGCCTTACATCACCATCACGCCGACCTTCTCCATCTGCCCCGTCCACGGCTACCTCGTGGGCGAGCACCTCACCTGCGACAAGTGCGCCGAGCTCCACCCCGAGGCCGAGCCGGTCGAGTGCGAGGTGTGGACCCGCGTCATGGGCTACTTCCGCCCGGTGCGCTCCTTCAACATCGGCAAGAAGGGCGAGTACGCCGAGCGGCAGATGTTCACCGAGGTCGCCGCCGGTGGTCACGGCCCGGCCATCTCGCGCCTGAGTACGGTCAGCGCCTGA","MCLNVALAVYLGVGSAPVPPTDPLPAGSAQPLTAPGRTGPIHARRGREQEREGPSERPVLEKNLASTAPAADGSAQPPAATPATDPRLVAPGSADSAVALGERPTVDAIATITEYLDRSDWRVNANANQGYSLGGMMLNTSGKVVANYWLSQVYSAAAGQAHRNADLHIHDLDMFAGYCAGWSLKDLLQQGFNGVPGAIAAGPAKHFSSAVGQIVNFLGTLQNEWAGAQAFSSFDTYMAPFVRLDDMTYDQVKQCMQELIFNLNVPSRWGTQTPFTNLTFDWTCPADLADEHPLIGDDVCDFAYGDLQAEMDLINRAFMEVMTEGDAEGRVFTFPIPTYNITRDFDWDAPNTELLFTMTAKYGLPYFQNFINSELDPGMIRSMCCRLQLDLRELLKRGNGLFGSAEQTGSVGVVTINMARLGYLYADDEAALTARLDELLEIGRDTLELKRTVIQHHIDAGLFPFTKRYLGTLDNHFSTLGVNGMNEMVRNFTRDAYDLTDPRGHAMCVRLLDHVRDKMVEFQEATGHLYNLEATPAEGTTYRFAKEDRKRYPGILQAGTETNPYYTNSSQIPVGYTDDPFEAQEMQEELQTKYTGGTVLHLYMNERISSAAACKELVRRSLTAFRTPYITITPTFSICPVHGYLVGEHLTCDKCAELHPEAEPVECEVWTRVMGYFRPVRSFNIGKKGEYAERQMFTEVAAGGHGPAISRLSTVSA$","Anaerobic ribonucleoside-triphosphate reductase","Cytoplasm","anaerobic class III ribonucleotide reductase","anaerobic ribonucleoside-triphosphate reductase","anaerobic ribonucleoside-triphosphate reductase","","Logan D.T., Andersson J., Sjoberg B.M., Nordlund P. A glycyl radical site in the crystal structure of a class III ribonucleotide reductase. Science 1999. 283(5407):1499-1504. PMID: 10066165Logan D.T., Mulliez E., Larsson K.M., Bodevin S., Atta M., Garnaud P.E., Sjoberg B.M., Fontecave M. A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase. Proc. Natl. Acad. Sci. U.S.A. 2003. 100(7):3826-3831. PMID: 12655046Andersson J., Bodevin S., Westman M., Sahlin M., Sjoberg B.M. Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4. J. Biol. Chem. 2001. 276(44):40457-40463. PMID: 11526118","","","

InterPro
IPR012833
Domain

Ribonucleoside-triphosphate reductase, anaerobic
TIGR02487	$\"[124-697]T$	NrdD: anaerobic ribonucleoside-triphosphate

noIPR
unintegrated

unintegrated
G3DSA:3.20.70.20	$\"[129-677]T$	no description
signalp	$\"[1-16]?$	signal-peptide

","BeTs to 8 clades of COG1328COG name: Oxygen-sensitive ribonucleoside-triphosphate reductaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG1328 is --m-k---v--l--efgh--------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-36% similar to PDB:1H78 STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DCTP. (E_value = 4.2E_10);-36% similar to PDB:1H79 STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DTTP (E_value = 4.2E_10);-36% similar to PDB:1H7A STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DATP (E_value = 4.2E_10);-36% similar to PDB:1H7B STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES, NATIVE NRDD (E_value = 4.2E_10);-36% similar to PDB:1HK8 STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DGTP (E_value = 4.2E_10);","No significant hits to the Pfam 21.0 database.","","class III ribonucleotide reductase (nrdD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2074","2240650","2239823","828","7.06","0.27","30182","ATGCGGGACCTGGAGCCGACTCGCACCCAGCGCCGTCACATCGCCTCGCTGGTGAGGACCGGTGAGCTCATCGCCTATGAGCATGGGGTTGTTGGTATCCCGGGTGCTGAGCGCGCCGTTGTTCTGGCGCGCATTCATGGAGGGCTCCTCACCTGCCAGGCCGCTATGCGCTACTACGGGCTGCCCGTAGCCCATGGGGCCGAGCAGGTTCACCTCGTGGTTTCGGATAGCGGACGATTCGCAGCCGTGGGACGTGAGGTTATCCATGTCGATCGGAGCCAGGGCTCAGCATCTCCGACTCGTTTCCCCGTACAGGCACTTCCTGAGGCTCTGGCGCGTTTTCTGCGCTGTCACCTCCAGGACGACTCCCCACTCATCGCTCTCGATGCGGCACTTCATGATGAGCGCGTCACTGCCGAGCAGATTCGCAATCTGCTTCGTGGCCCTGGCTCGGCTCGGGCGCTCGCACGACTCGATCGCGCCAGTGACCGGGCCCGTTCCCCGTTGGAGACGCTGGCGCGTTTGGACCTTGAGGCTGCGGGTTTGGGCTTCGAGGTCGGAGTGGAGATCGAGGGGGTTGGTGAGGTGGACCTGGTGGTCGAGGGGTGGGTGGTCGTAGAACTGGACGGCTACACCTACCACTGCGACGAGTACCAGTTCGGCCTCGACCGCTGGCGCGACCGCCGGCTCGTCGCCCGTGGCTTCCTGCCGCTGCGCTTCACGAGGAAGGATGTCTACGCGCATCAGGTCGTTCCGGACGTGCTGAAGGCCGTGGAGTGCTGGGGAGTGTCCAAATCTGCCACAAAGGCTGCTGTGAGTCTCGGATAG","MRDLEPTRTQRRHIASLVRTGELIAYEHGVVGIPGAERAVVLARIHGGLLTCQAAMRYYGLPVAHGAEQVHLVVSDSGRFAAVGREVIHVDRSQGSASPTRFPVQALPEALARFLRCHLQDDSPLIALDAALHDERVTAEQIRNLLRGPGSARALARLDRASDRARSPLETLARLDLEAAGLGFEVGVEIEGVGEVDLVVEGWVVVELDGYTYHCDEYQFGLDRWRDRRLVARGFLPLRFTRKDVYAHQVVPDVLKAVECWGVSKSATKAAVSLG$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Cleveland D.W. Autoregulated instability of tubulin mRNAs: a novel eukaryotic regulatory mechanism. Trends Biochem. Sci. 1988. 13(9):339-343. PMID: 3072712","","","

InterPro
IPR013838
Binding_site

Beta tubulin, autoregulation binding site
PS00228	$\"[1-4]?$	TUBULIN_B_AUTOREG

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-49% similar to PDB:1AAT OXOGLUTARATE-INDUCED CONFORMATIONAL CHANGES IN CYTOSOLIC ASPARTATE AMINOTRANSFERASE (E_value = );-49% similar to PDB:2CST CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION (E_value = );-50% similar to PDB:2IEL CRYSTAL STRUCTURE OF TT0030 from Thermus Thermophilus (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2075","2240700","2240831","132","9.79","0.91","4563","ATGGTGTTCACGGAACTCATTGCCGCCCGTCTGCGGAGTGGACGCAACCCGGCCACCGTCACTCTGTGGACAACTGGCGCATCCGCCAGCCTGTGGCCTCCAGGACCCATCGAAGTGTCACCGATGCCGTGA","MVFTELIAARLRSGRNPATVTLWTTGASASLWPPGPIEVSPMP$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2076","2241135","2241569","435","11.70","12.78","16128","GTGGACCGTCACGGTGTTGTCGGGCTGGCCCGACATCGACCGACCAGGTGGCTGGATCGTGTGGACGATCACGCTCCGACAGCCTGGTTCCATGAGCACGGATACCTCTCCCTTCCACCGTTCCCGACCTCCGTCGCAGCAGGTCAGACCCACATCTCCCACCCGGTCTCGGGGCCCTGGGCGCACGTGCCCACCTGGATCCTGGCGGCGGCATCGCTGCCCGGCCCGTACGGGATCGTCCGAGGCATCACGCTGTGGCCGGATCTGCCGGCCCTGCCGCGTCGCCGGGCCTGGCTCGACTGGACGCAGGTGGCGGACTGTCGGCTTCATCGCCGTCTGCCTGGTCGTCGCTTGGCCCAAGGCCTGAGCCGGCCACGCCTGGCGTCGCCTTCGCTCCCCACGCCGCATCCCGGGCCCCATCCTCACCGCCGGTGA","VDRHGVVGLARHRPTRWLDRVDDHAPTAWFHEHGYLSLPPFPTSVAAGQTHISHPVSGPWAHVPTWILAAASLPGPYGIVRGITLWPDLPALPRRRAWLDWTQVADCRLHRRLPGRRLAQGLSRPRLASPSLPTPHPGPHPHRR$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2077","2241579","2243423","1845","6.97","-0.19","65197","GTGAAGGCGACGCCGCCCCTCCTCCCCCGTTCACCACCGATTCACGTCCGGAAAGCTGACACCATGACTGATCGCCGTTTCTCCACGCCCGGTCTCACCCGGCGCCTACTGGCCCCGATCGCCGTCCTGCTGGGTCTGGTGGCGGGCCTGAGCGTCCTCATCCTGCCCTCCCCCACACCGACCACCGCCGACCCGACCACGTTCTCCGCCGAGCGCGCCATGGCCGCCATCAACCGCCTCGCCGACGAGCCCCACAGTGTCCTGCGCCGCGAGGCGCACGACCGGGCACGCGACGACGTCATCGGCATGTTCACCGACCTCGGCTACACCCCCACAGTGCACTCCGACCCGCTATTCGACCTCACTAACCCGGAGGACAAGGAGAACTTCCAGACGCTCCCCGCAGAACTGCAGACGGAGATCAAAGACGCGCCGGCTGAGACGATCGTCGTCGACGTACCGGGGAAGTCCGAACGCACCATGGCGCTCATGGCCCACTACGACTCGTCCACGGTCGAGGAGGACGAGGACGGCGTAGTACGCAAGGTTCCCGGGAACTCCTACGGGGCTTCCGACGACGGCTACGGCGTGGCCGCCATCGTCGAGACGCTCCGGGCTATCAAGGCAGAGGGGCGCCAACCGGAGAACTCGCTGAAGATCGTCATCACCGACGGCGAGGAAGTCGGCCTCGTCGGCGCCCGCAACGAGATGCGCCACCACCGCACCGACTACAAGAACGTCGACCTGGTCCTCAACCTCGAGGCGCGCGGCACGAGCGGCCCGGCGCTCATGTTCGAGACCTCCTCGAACAACAGCGCCGTCGCCGGCTACTTCCTCAGCCACGTGAAGCAGCCCGTGGCCGGCTCGCTCCTGCCCTCGCTGTACGCGCGCATGCCCAACACCACTGACATGGCGGCGTTCATCCCCGAGGGTTTCACGGTGCTCAACATCGCGGCGATTGGGGACGCCGAGCACTACCACCACCCCACCGACGCCCCGCGCTACGTCGACCACTCGACCCTCCAGCACTACGGCGACCAGGTCCTGGACCTCGCGCGGGCCTGGGCCTTCGACGGGCAGGCCCCCACGCTCACGGCCGACGGCGACCTTCACTTCTTCCAGCTGTGGCGGGGGCTGACGGTGCGCTACCCGGCGGCGGTCGGGATGGGGCTGGGGTGCCTGGCCGTCATCGCCGCGCTCGGCGTCGTTGCGGTACGGGCACGGTCGCTGCGCTGGAAGCGGGTCCTGGGGAGCGTCTGGGGCCTGACATGGCGGGCCGCGTTCGCCTCTGCCGCCGCGGGGCTGGTGCAGCGCGGAGCCATGGCGATGAAGTGGGCGCCGGAGAGCGGGCTCGGGCCGAACCCGCTGCTGGTGTGGATGTTCGCCGGCGGGGCCCTGATCGGGGCCGGGCTCACGACGCACTTCGTGGTGCGGCGTTGGAAGGAGGGGCTCGGGCAGGAGACCCTCGCCGCGGTGCTGCTCCTGCTGGCAGCGGCCTGCGTGCCGCTCATGGTGCTGCTGCCCGGCGCTGCCTACGTCCTGGTCCTTCCCACGCTCGCCCTGGCGCTGACCGCGCTGGCGCCGAGGCGGGTACGGCCGGTGGTCGGGGCGCTGGCGGCCTTCAGCATCGTGGCGATCCTCGCCCCCGCGGTCCTGCTCATCCACGAGATGCTCAGCCTGGGCGCGGTGTGGGTGACCGTGTTCTTCGCGATCGTGCCGGTGGCGCCGCTGGCGCTTGTGCTCCTGCAGGCCGGTTCCCGGCGCACCGCCAGGGGTGCCGGTACCACATCCGGGGCCGCTCCCAGCGGCACCCCCGTTGCTGGCCAGGTGGCCACGACGGTGTAG","VKATPPLLPRSPPIHVRKADTMTDRRFSTPGLTRRLLAPIAVLLGLVAGLSVLILPSPTPTTADPTTFSAERAMAAINRLADEPHSVLRREAHDRARDDVIGMFTDLGYTPTVHSDPLFDLTNPEDKENFQTLPAELQTEIKDAPAETIVVDVPGKSERTMALMAHYDSSTVEEDEDGVVRKVPGNSYGASDDGYGVAAIVETLRAIKAEGRQPENSLKIVITDGEEVGLVGARNEMRHHRTDYKNVDLVLNLEARGTSGPALMFETSSNNSAVAGYFLSHVKQPVAGSLLPSLYARMPNTTDMAAFIPEGFTVLNIAAIGDAEHYHHPTDAPRYVDHSTLQHYGDQVLDLARAWAFDGQAPTLTADGDLHFFQLWRGLTVRYPAAVGMGLGCLAVIAALGVVAVRARSLRWKRVLGSVWGLTWRAAFASAAAGLVQRGAMAMKWAPESGLGPNPLLVWMFAGGALIGAGLTTHFVVRRWKEGLGQETLAAVLLLLAAACVPLMVLLPGAAYVLVLPTLALALTALAPRRVRPVVGALAAFSIVAILAPAVLLIHEMLSLGAVWVTVFFAIVPVAPLALVLLQAGSRRTARGAGTTSGAAPSGTPVAGQVATTV$","Transmembrane peptidase, M28 family","Membrane, Cytoplasm, Extracellular","putative peptidase","CG33013","peptidase M28","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR007484
Domain

Peptidase M28
PF04389	$\"[159-342]T$	Peptidase_M28

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.10	$\"[82-356]T$	no description
PTHR12147	$\"[186-566]T$	FXNA-RELATED
signalp	$\"[1-49]?$	signal-peptide
tmhmm	$\"[36-56]?$ $\"[383-405]?$ $\"[415-435]?$ $\"[457-477]?$ $\"[489-507]?$ $\"[513-528]?$ $\"[533-555]?$ $\"[561-581]?$	transmembrane_regions

","BeTs to 9 clades of COG2234COG name: Predicted aminopeptidasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2234 is aom-k-yq--r-b-efg-s--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 159 to 342 (E_value = 1.8e-35) place ANA_2077 in the Peptidase_M28 family which is described as Peptidase family M28.Residues 162 to 570 (E_value = 0.0028) place ANA_2077 in the Peptidase_M20 family which is described as Peptidase family M20/M25/M40.","","peptidase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2078","2244594","2245433","840","4.92","-13.17","29905","ATGACACTGCACCCCATTGCCTTAATCACCCTTGTCGCTCCACTCATACTTCCGATACAAAATGCCGGAAACGCAAGTTCGGGCTCCACCACTGTTGAATCTAATGTAACTGCTGGAAATACGGACGCAGGAGTGGAGACCTATGGGGAGGTGACTGAGACCATCCCTCAAGAGAGTGCGTCGGATTCTGGTGAGCCTGCGTCTCAGGAGCGTCCGTCTGTGAGGGCCTCGGATCCGTCGATGTGGGAGGAGCAGTCGCATCGGGAGTGCTCGCCGGAGAAGGACGCCTACGGGCTGGACAAGTACAAGTGCAACCTGTCCACCCTCAACCGCCCCGGCCAGCCCGACCAACCCACCAACACTGACGGTGGTGGCCGTACGGTCACGGTCACCACTCGTCAGGCCGCCACGCTGATCGCCTCGGGCTCGGGCATCACCCGCCAGCCACCCGGTCCCAAGGTCATCATCTCCAAGGCCTTCATCGTCTACACCAGCCCCAGCCCTCAGCACCAGACCACCACCATCCTGGGCACCTCCATCGAGGTGGAGTTCACCCCCGTCTCCTACACCTGGGGCTGGGGAGACGGCACCACCACAACCACCACCGACCCAGGAGCCCCCTACCCCCACCAGACCGTCACCCACCACTACCAGCACACCGCCACCGGAGTCACCACCACTCTGACCACCACCTGGACCACGAGGTTCCGCCCCGCCGGCGAGGACCAGTGGCGGCCCATCGAGGGCACCATCACCACCACCGAGACCTCCACCCCCTACGACCTGGTCCGCATCGTCACCTACCTCACCGACGACGCCGAAGAAGCCCAAGGCCACTAA","MTLHPIALITLVAPLILPIQNAGNASSGSTTVESNVTAGNTDAGVETYGEVTETIPQESASDSGEPASQERPSVRASDPSMWEEQSHRECSPEKDAYGLDKYKCNLSTLNRPGQPDQPTNTDGGGRTVTVTTRQAATLIASGSGITRQPPGPKVIISKAFIVYTSPSPQHQTTTILGTSIEVEFTPVSYTWGWGDGTTTTTTDPGAPYPHQTVTHHYQHTATGVTTTLTTTWTTRFRPAGEDQWRPIEGTITTTETSTPYDLVRIVTYLTDDAEEAQGH$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[440-516]T$	Helicase_C
SM00490	$\"[435-516]T$	HELICc
PS51194	$\"[405-556]T$	HELICASE_CTER

InterPro
IPR004589
Family

ATP-dependent DNA helicase RecQ
PTHR13710	$\"[448-514]T$	DNA HELICASE RECQ FAMILY MEMBER

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[60-265]T$	DEAD

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[55-290]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[67-276]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
PD008161	$\"[835-942]T$	Q8FSS7_COREF_Q8FSS7;
G3DSA:3.40.50.300	$\"[44-280]T$ $\"[413-537]T$	no description
PTHR13710:SF4	$\"[448-514]T$	ATP-DEPENDENT DNA HELICASE

","BeTs to 8 clades of COG1205COG name: Distinct helicase family with a unique C-terminal domain including a metal-binding cysteine clusterFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1205 is a-m-k-y--dr-b-e-----------Number of proteins in this genome belonging to this COG is 1","***** IPB013701 (DEAD/H associated) with a combined E-value of 8.3e-25. IPB013701A 50-93 IPB013701B 120-140 IPB013701D 199-226 IPB013701G 413-433 IPB013701H 466-499***** IPB002121 (HRDC domain) with a combined E-value of 9e-10. IPB002121A 82-91 IPB002121B 123-136 IPB002121F 477-516***** IPB012562 (GUCT) with a combined E-value of 8e-06. IPB012562A 59-98 IPB012562G 460-514","","","No significant hits to the PDB database (E-value < E-10).","Residues 60 to 265 (E_value = 8e-27) place ANA_2080 in the DEAD family which is described as DEAD/DEAH box helicase.Residues 440 to 516 (E_value = 5e-14) place ANA_2080 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","helicase family with a unique C-terminal domain including a metal-binding cysteine cluster","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2081","2249061","2250794","1734","5.18","-11.12","61647","ATGCTCCTTCGATTACTGCGCACGCACCTGCGCCCCTATACCGGGTTGCTGGTGTGCGTCCTGGTGCTTCAGTTCGCACAGGTGATGGCCTCCCTGTACCTCCCCACCCTCAACGCCGACATCATCGACAAGGGTGTGGCCACCGGGGACACCGGCTACATCTGGCGAATGGGCGCGTTCATGCTGGGGGTCAGCCTGGCCCAGGGCGTGTGCTCGGTCGCGGCGACCTACCTCGCGGCGCGCGCGGCGATGAGCATGGGCCGGGACCTGCGCGGCGAGGTCTTCGACCGGGTCAGCGGCTTCTCAGAGCGGGAGATCTCCGCCTTCGGGGCTGGCTCGCTCATCACCCGCAACACCAACGACGTCCAGCAGGTCCAGATGCTGGTGATGATGAGCGCCACGATGCTGGTGACGGCGCCGGTCATGGCGGTGGGCGGCATCGTCATGGCGGTCACGCGCGCCCCGGGCCTTTCGTGGCTCATCGGGGTGTCGGTGCCGGTCCTGCTGGTCGCGGTGGGCCTCATCGTGGGCCGCATGCTGCCCCTGTTCCGCTCCTACCAGGACAAGCTCGACGCCATCAACCGGGTGATGCGCGAGCAGCTCACCGGTATCCGAGTCATCCGCGCCTTCGTGCGCGAGCAGGCCGAGACCGAGCGCTTCGAGGACGCCAACGGCGACATCGCGCGGGTCGGCGAGCGCGTGGGTCAGCTCTTCGTCCTGCTGTTCCCGCTGGTGATGCTGGTGCTGGACGTGACGATCGTTGGCGTCATCTGGTTCGGCGGCCACCGGGTCGGCGACGGCGACGTGGAGGTCGGCACCCTCATCGCCTTCATGTCCTACCTCATGCAGATCCTCATGGGCATCGTCATGGCGAGCTTCATGACGATCATGATCCCGCGCGCCGCGGTGTGCGCCGAGCGCATCAGCGAGGTGCTGGCGACGTCGCCGACCATCACCTCCTCCCCCGACGCCGTCGACACCTTCCCAGCTCCCGGAACGGTTGAGATGCGGGACGTCACCTTCGTCTACCCCGACGCCGACGCCCGCGTCCTGGCGGAGGTGAGCTTCACGGTCCAGCCCGGGACGACGACGGCGATCGTCGGCTCGACGGCGTCGGGCAAGTCCACGGTGGTGCGGCTGCTGGCGAGGCTGCTGGAAGCCAGCAGCGGGCAGGTGCTCATCGGCGGCACCGACGTTCGTGAGGCCGACCCCGAGGCGCTGTGGTCGCAGATGGGGCTCGTGCCTCAGCAGCCCTTCCTGTTCGCCGGGACCGTGGCCTCCAACCTGCGCCTGGGGCGTGAGGAGGCCACCGACGACGAGCTGTGGCAGGCCCTGGAAGTCGCCCAGGCCAAGGACTTCGTCTCCAAGATGGACGGGGGCCTTGAGGCGCCCATAGCCCAGGGCGGCACGAATGTCTCTGGCGGTCAGCGTCAGCGCCTGGCCATTGCCCGGGCCCTGGTGCGCCGGCCCGACATCCTCATCTTCGACGACTCCTTCTCGGCCCTGGACGTGTCCACCGACGCGCGGCTACGCGAGGCCATGGGGCCGGCGACGGTCGGCATCACGAAGGTGATCGTGGCTCAGCGCGTCTCCACGATCGTCGAGGCCGACCAGATCCTCGTCCTGGACGGCGGCCACCTGGTGGGTAGCGGCACGCACACCGAGCTGCTGGCCACCTGCGCCGTCTACCGCGAGATCGTCACCTCCCAGCTCGGAGCGGAGGCCGCAGCATGA","MLLRLLRTHLRPYTGLLVCVLVLQFAQVMASLYLPTLNADIIDKGVATGDTGYIWRMGAFMLGVSLAQGVCSVAATYLAARAAMSMGRDLRGEVFDRVSGFSEREISAFGAGSLITRNTNDVQQVQMLVMMSATMLVTAPVMAVGGIVMAVTRAPGLSWLIGVSVPVLLVAVGLIVGRMLPLFRSYQDKLDAINRVMREQLTGIRVIRAFVREQAETERFEDANGDIARVGERVGQLFVLLFPLVMLVLDVTIVGVIWFGGHRVGDGDVEVGTLIAFMSYLMQILMGIVMASFMTIMIPRAAVCAERISEVLATSPTITSSPDAVDTFPAPGTVEMRDVTFVYPDADARVLAEVSFTVQPGTTTAIVGSTASGKSTVVRLLARLLEASSGQVLIGGTDVREADPEALWSQMGLVPQQPFLFAGTVASNLRLGREEATDDELWQALEVAQAKDFVSKMDGGLEAPIAQGGTNVSGGQRQRLAIARALVRRPDILIFDDSFSALDVSTDARLREAMGPATVGITKVIVAQRVSTIVEADQILVLDGGHLVGSGTHTELLATCAVYREIVTSQLGAEAAA$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","ABC-type transporter, ATPase component andpermease component","K06147 ATP-binding cassette; subfamily B; bacterial","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR000833
Family

Alpha-amylase inhibitor
SM00783	$\"[317-381]T$	no description

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[17-288]T$	ABC_membrane

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[471-514]T$	Q8NRS7_CORGL_Q8NRS7;
PF00005	$\"[361-545]T$	ABC_tran
PS50893	$\"[334-569]T$	ABC_TRANSPORTER_2
PS00211	$\"[472-486]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[360-546]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[20-300]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[299-570]T$	no description
PTHR19242	$\"[3-575]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91	$\"[3-575]T$	LIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[59-79]?$ $\"[128-150]?$ $\"[156-176]?$ $\"[239-259]?$ $\"[273-293]?$	transmembrane_regions

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[102-402]T$	ABC_membrane

InterPro
IPR001482
Domain

Bacterial type II secretion system protein E
PD000739	$\"[508-559]T$	Q8ZUH9_PYRAE_Q8ZUH9;

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[625-668]T$	Q6AH77_BBBBB_Q6AH77;
PF00005	$\"[515-699]T$	ABC_tran
PS50893	$\"[489-723]T$	ABC_TRANSPORTER_2
PS00211	$\"[626-640]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[514-700]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[91-414]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[480-721]T$	no description
PTHR19242	$\"[48-118]T$ $\"[160-438]T$ $\"[480-735]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91	$\"[48-118]T$ $\"[160-438]T$ $\"[480-735]T$	LIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA
tmhmm	$\"[88-108]?$ $\"[168-188]?$ $\"[247-265]?$ $\"[271-291]?$ $\"[360-380]?$	transmembrane_regions

InterPro
IPR012495
Family

TadE-like
PF07811	$\"[67-109]T$	TadE

noIPR
unintegrated

unintegrated
signalp	$\"[1-93]?$	signal-peptide
tmhmm	$\"[75-95]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 67 to 109 (E_value = 0.00021) place ANA_2084 in the TadE family which is described as TadE-like protein.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2085","2252913","2253752","840","11.54","19.53","28792","ATGAGCTCATCGCGGCGGGCGGTGCCTACGCGCGCCTCCACGCGGCCCAGTTCGCGGGCGGCGCCACCGTCGCCGTCGAGGACTGAGGCCCGGGCTGCCCCCGATGTCCGGCGGCGCCGGCCCGAGTGGAGGCCGGTTCTCGCCGGTCCCCACCCTCGAGGATGCACGGTAGGCCTCGCGGACTGTACCCGTGACAGGCGTCGTCGAAGGCTGACGTGCGTCCTCGACGCCTCAGGCGCCCGGGCGCACCGTGTGCACACCCGGGTTTGGGCCGGTTCACGGCTTAGGCGGGGCGTCGACAGGGCCGGCTCGGGCCCGGGCGGAGGCCTGGCGGGGCAGGCCGAGGATCGTCGTCGGGACGACGACGCTGACGGTGACGTCCTCACCGGCCACGGAGCAGGCGCTCACCGAGGCGCCGTTGGCGGCAGCCACGCGCTGCGCCATGGCGCAGGGGTCGCCGGGGGCGATGACCGAGGACAAGACCGTGGCACCGGAGATGGCCGCGAGGTCAGCGGCGGCCCTGGCCCGACCGGCGGCGCTCTGAGCCTGGATGAGGCCCGCGATGCCGACTACCGCGGCGAGCAGCACGGCGATGACGCCGAGCGCGTAGACAGTCCCCGAGCCACGCTCGTCCCACCCGGGGCGGTTTCCTTTGGCGCCCCGGGCGGCCGGTTGCTGCGCCGATCGTCCAGCCGGGCGGCACAACGGCCGGCCGGCCTCCCGGCTGGAGGTCGCGAGCGCGGTGGAAGCCACGGCGGGGAAGGCCAGCGGATCCGGAGCATGGGCCATCTGTCGGCTCCGGTCTCCATGGCGATTCATGGGCTGCTCGGCTCGGTGTAG","MSSSRRAVPTRASTRPSSRAAPPSPSRTEARAAPDVRRRRPEWRPVLAGPHPRGCTVGLADCTRDRRRRRLTCVLDASGARAHRVHTRVWAGSRLRRGVDRAGSGPGGGLAGQAEDRRRDDDADGDVLTGHGAGAHRGAVGGSHALRHGAGVAGGDDRGQDRGTGDGREVSGGPGPTGGALSLDEARDADYRGEQHGDDAERVDSPRATLVPPGAVSFGAPGGRLLRRSSSRAAQRPAGLPAGGRERGGSHGGEGQRIRSMGHLSAPVSMAIHGLLGSV$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2086","2254494","2254243","252","11.47","4.92","8687","ATGAGGAGACCCACCCGGACCACCTTGCGTACCCTGCGCACCAGCGTGATGCTGGCCCGCCCGAGTGACGCCTCAACGCTGCCGGCAGTCCTGCGGCGACTAGCGACCAAGGAGGAGGGCATGGCCACCGCCGAGTACGCCATCGGCACCTTGGCGGCCGCGGCCTTCGCCGGCCTGCTGCTGGCGCTCATGCGCTCGGGCAGCCTGAGCGGGGCGTTGCAGTCCATCATCGAGTCGGCGCTCTCGGTGTGA","MRRPTRTTLRTLRTSVMLARPSDASTLPAVLRRLATKEEGMATAEYAIGTLAAAAFAGLLLALMRSGSLSGALQSIIESALSV$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[42-62]?$	transmembrane_regions

InterPro
IPR000330
Domain

SNF2-related
PF00176	$\"[672-971]T$	SNF2_N

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[1072-1147]T$	Helicase_C
SM00490	$\"[1067-1147]T$	HELICc
PS51194	$\"[1042-1193]T$	HELICASE_CTER

InterPro
IPR007527
Domain

Zinc finger, SWIM-type
PF04434	$\"[68-104]T$	SWIM
PS50966	$\"[64-104]T$	ZF_SWIM

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[665-878]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[681-861]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1038-1180]T$	no description
PTHR10799	$\"[123-128]T$ $\"[250-265]T$ $\"[653-717]T$ $\"[735-972]T$ $\"[1022-1183]T$	ATP-DEPENDENT HELICASE SMARCA (SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN A)-RELATED
PTHR10799:SF72	$\"[123-128]T$ $\"[250-265]T$ $\"[653-717]T$ $\"[735-972]T$ $\"[1022-1183]T$	HELICASE MOT1(YEAST)

","BeTs to 15 clades of COG0553COG name: Superfamily II DNA/RNA helicases, SNF2 familyFunctional Class: K [Information storage and processing--Transcription] Functional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0553 is ao-pkzy-vdrlbcefghs----i-wNumber of proteins in this genome belonging to this COG is 1","***** IPB006576 (Domain in transcription and CHROMO domain helicase) with a combined E-value of 9.5e-56. IPB006576B 669-708 IPB006576D 783-824 IPB006576E 840-874 IPB006576F 886-935 IPB006576J 1097-1137 IPB006576K 1138-1182 IPB006576C 734-757***** IPB000330 (SNF2 related domain) with a combined E-value of 5e-53. IPB000330A 691-703 IPB000330B 737-757 IPB000330C 837-860 IPB000330D 1109-1156***** IPB012958 (CHD, N-terminal) with a combined E-value of 4.4e-14. IPB012958E 643-694 IPB012958G 783-837 IPB012958I 1018-1070 IPB012958J 1088-1134***** IPB002464 (ATP-dependent helicase, DEAH-box) with a combined E-value of 3.6e-07. IPB002464A 809-818 IPB002464B 1138-1155","","","-48% similar to PDB:1Z63 Sulfolobus solfataricus SWI2/SNF2 ATPase core in complex with dsDNA (E_value = 2.0E_34);-48% similar to PDB:1Z6A Sulfolobus solfataricus SWI2/SNF2 ATPase core domain (E_value = 2.0E_34);-57% similar to PDB:1Z5Z Sulfolobus solfataricus SWI2/SNF2 ATPase C-terminal domain (E_value = 3.0E_19);-45% similar to PDB:1Z3I Structure of the SWI2/SNF2 chromatin remodeling domain of eukaryotic Rad54 (E_value = 1.1E_16);-48% similar to PDB:1D9X CRYSTAL STRUCTURE OF THE DNA REPAIR PROTEIN UVRB (E_value = 1.1E_16);","Residues 68 to 104 (E_value = 0.016) place ANA_2087 in the SWIM family which is described as SWIM zinc finger.Residues 672 to 971 (E_value = 8.7e-67) place ANA_2087 in the SNF2_N family which is described as SNF2 family N-terminal domain.Residues 1072 to 1147 (E_value = 2e-24) place ANA_2087 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2088","2254902","2255024","123","8.23","0.89","4214","ATGTCCCCGGCCACGCAGAAGGCCCCCACCCGGGCGCAACCGAGCCGGGCCCCAGTGCAGGACTGTGGTGACGGCCGGCCCACGGCGGCGCCCGACGACGTCGAGCGCCTCAGCCCTCGATGA","MSPATQKAPTRAQPSRAPVQDCGDGRPTAAPDDVERLSPR$","Hypothetical protein","Extracellular","unnamed protein product","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein product","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2090","2258942","2259610","669","9.11","3.16","23641","ATGAACGCGATGCTGACCTGTGAAGAACTGTTCCTACTGCTGACCAAGGACTCCGGTAAGCCGGAGAGCCGCATGACGTATCCGGCCTACGGGCTCACCGGCGCGCTCCTCACCGACCTACTGCTGGCCGGCCGCATCAGCCTGACCGAGGAGCGCAGCCCCCGCGTCTACATCGTCAGCGCCGAGCCGACCGGGCACCCCGTCCTGGACCGGGCCCTGGAGATCCTGCCCGCCAAGGACGGCAAACGATTCTCCTCCCTGGTGTCCTGGGGCAGGCTCAACCCCACCCGCAACATCGCCCAGTCCTTGGAGGCGGCCGGGGTGGTGCGCATCTACACCGGCGGGCTGTTCGGGTCACTGAACCCCAGCTACCCCACGCTCGACCCCCTCCCCGAGCGGCAGCTGCGCGCACGCATCGACGCCGCCCTGCGCGGGGTGCAGCCGCCGACTGCCTCCGACGTCGCCCTGCTGTCGATCCTGCAGGCGCTCAGTGTCGCACCAACCGTCCTGCCGCAGCAGGAGACGGGTCTCAGCCGCGGCGAGCTCAAGCGCCGGATCAAGGAGCTCTCGGGGGAGAACCCCGTGGGGCGTGCGGTGCAGCGGGCCGTGGAAGCCGTGACGATGGCCATCATCGCCGCAGGGAGCGTTGCGGCGGCCTCGTCGAGCTGA","MNAMLTCEELFLLLTKDSGKPESRMTYPAYGLTGALLTDLLLAGRISLTEERSPRVYIVSAEPTGHPVLDRALEILPAKDGKRFSSLVSWGRLNPTRNIAQSLEAAGVVRIYTGGLFGSLNPSYPTLDPLPERQLRARIDAALRGVQPPTASDVALLSILQALSVAPTVLPQQETGLSRGELKRRIKELSGENPVGRAVQRAVEAVTMAIIAAGSVAAASSS$","Hypothetical protein","Membrane, Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-41% similar to PDB:1O4V Crystal structure of phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77 A resolution (E_value = );-45% similar to PDB:1Q16 Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli (E_value = );-45% similar to PDB:1SIW Crystal structure of the apomolybdo-NarGHI (E_value = );-45% similar to PDB:1Y4Z The crystal structure of Nitrate Reductase A, NarGHI, in complex with the Q-site inhibitor pentachlorophenol (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2091","2261419","2259809","1611","10.10","10.10","56471","ATGGCCGAGGTCTTCACCTCCCTGCTACTCATCGTCGCGGTGGCCTTCGTGGCGCCGCTGATCTCCTGGACCATCCCCAAGCGGCTCGTGCCCGAGGTCGTCCTGCTCATCCTGGGCGGGATGCTCATCGGTCCCCACGGCTTGGGGCTGGCCGTCGAGGACTCCTCGATCGAGCTGCTGCGCGAGCTCGGCGTCGCCTTCCTCTTCCTCATGGCCGGCTACGAGATCGACATCAACGAGCTGCGCGGGGCGGGCGGGCGCCACGCCGCCGTCGCCTGGCTGCTCTCGCTGGGGCTGGCCTTCGGTGCGGTCAGCGTCATCGGGGTGACCGGAGGGGCGGCGTCGGCCAACGGCATCGCCATCGCCACCGCCATGACCTCCACGGCCATCGGCACGATTCTGCCGATCCTGCGCGACCGCGGCCTGCTGCCCACGGCGGTGGGCGCCTCGATCCTCAACCACGGCGCCGTCGGCGAGGTCGGGCCGGTCATCGTCATGGCGCTGCTGCTGGGGTCGCGCTCCACCTGGGCGAGCATGGTGATCCTGGGTGTCTTCCTCATCATCACCCTCCTCATCGTTCGCTTCACCAGCCGCGTCAAGCGCGTGGGGCGCCGCCTGGTCGAGGCTATCCACCTGGGGGCCTCGACGACGGCGCAGACCACCATCCGGGCCACCGTCCTGCTCCTGGTGGGGCTGTGCGCCATCGCCGCCATCTTCGACCTTGACGTCATCCTGGGGGCCTTCGCCGCCGGCTTCGTCCTGCGTCATGCCCTGCCCGAGGGGGATGCCGAGTTCGAGGAGAAGCTCGACGGGCTGGCCTACGGGTTCTTCGTGCCGATCTTCTTCGTCACCTCCGGCATGGGCATCGAGGCCGGGCTCAATGCCGGGGACCTGGTCAACCTGCTGGCCTTCTTTGTACTGCTGGTGCTCGTGCGGGGCGTGCCGGTGTGGCTGGCCTCCCGGGCGGAGCGGCGCAGGGACGGCTCGCGCGCCTACTCGATACGTCAGAGCCTCCAGATCGCCGTCTACTCGACGACGGCCCTGCCCATCATCGTGGCCGTCACTCAGGTGGCGGTCAGCGCGGGGGCCATGTCGACCTCCTTCGCCTCCACCCTCGTGCTGGCCGGGGTGCTGTCGGTGCTGGTCCTGCCGGCCGCCGGACTGGCGCTGGGCCACCGGAGCGACCACGTGCCGGCCAACGAGGTGATGCGTGTGGTCCAGGGGCCGGCCGCTCCTGACGGGCGCACCCCCGAGGAGGCCACGGTCCCGGTCGGTGAGCATGTCTCGGAGCCGCGCCGACCGGCGTCGCCGCCTGGCGGCATCAGGCTGCCGGTGGGGGAGCGCACCCCGGCCGCAGGAGTGAAGCGGCCGGCGCAGCCCGACCTCGTGGGCCTGCCGGACCTGCGTGCGCAGACGACGCCGGCGATGGCGCGCCTGGCCGAGCTGGGGATGCACGCACGGGGGCTGTCGCTGGAGGAGTCGCACCGCCTGGCCGCGCGCCTGGTCGAGATCGAGCAGGAGCACGCCCTGTGGCGCGAGCGCTGGCACCGCGCGCGCAGGCACGGCGGTACCTCCCGGGCGGCTCGACGTCGTCGGCCCCGCAGCGAGTGA","MAEVFTSLLLIVAVAFVAPLISWTIPKRLVPEVVLLILGGMLIGPHGLGLAVEDSSIELLRELGVAFLFLMAGYEIDINELRGAGGRHAAVAWLLSLGLAFGAVSVIGVTGGAASANGIAIATAMTSTAIGTILPILRDRGLLPTAVGASILNHGAVGEVGPVIVMALLLGSRSTWASMVILGVFLIITLLIVRFTSRVKRVGRRLVEAIHLGASTTAQTTIRATVLLLVGLCAIAAIFDLDVILGAFAAGFVLRHALPEGDAEFEEKLDGLAYGFFVPIFFVTSGMGIEAGLNAGDLVNLLAFFVLLVLVRGVPVWLASRAERRRDGSRAYSIRQSLQIAVYSTTALPIIVAVTQVAVSAGAMSTSFASTLVLAGVLSVLVLPAAGLALGHRSDHVPANEVMRVVQGPAAPDGRTPEEATVPVGEHVSEPRRPASPPGGIRLPVGERTPAAGVKRPAQPDLVGLPDLRAQTTPAMARLAELGMHARGLSLEESHRLAARLVEIEQEHALWRERWHRARRHGGTSRAARRRRPRSE$","Na+/H+ antiporter","Membrane, Cytoplasm","sodium/hydrogen exchanger family protein/TrkAdomain protein, putative","K03499 trk system potassium uptake protein TrkA","sodium/hydrogen exchanger","","Saenz H.L., Augsburger V., Vuong C., Jack R.W., Gotz F, Otto M. Inducible expression and cellular location of AgrB, a protein involved in the maturation of the staphylococcal quorum-sensing pheromone. Arch. Microbiol. 2000. 174(6):452-455. PMID: 11195102Zhang L., Gray L., Novick R.P., Ji G. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 2002. 277(38):34736-34742. PMID: 12122003","","","

InterPro
IPR006153
Family

Sodium/hydrogen exchanger
PF00999	$\"[8-389]T$	Na_H_Exchanger

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[41-200]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[5-23]?$ $\"[33-51]?$ $\"[93-113]?$ $\"[119-137]?$ $\"[147-167]?$ $\"[173-193]?$ $\"[271-291]?$ $\"[297-319]?$ $\"[340-360]?$ $\"[366-388]?$	transmembrane_regions

","BeTs to 16 clades of COG0475COG name: Kef-type K+ transport systems, membrane componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0475 is a-mpkzyq-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 389 (E_value = 4.3e-42) place ANA_2091 in the Na_H_Exchanger family which is described as Sodium/hydrogen exchanger family.","","exchanger family protein-TrkA domain protein, putative","","1","","","","","","","","","","","Wed Aug 22 22:56:37 2007","","Wed Aug 22 22:56:37 2007","","","Wed Aug 22 22:56:37 2007","","","","Wed Aug 22 22:56:37 2007","Wed Aug 22 22:56:37 2007","","","","","yes","","" "ANA_2095","2261599","2262945","1347","6.08","-10.49","49944","ATGCTCATGCCGTACTCGCCCTCCGCCGAACCACTCACGCGCCTGGCCGACGGGACGGTCAAGCAGATCAGCCCCTTCACCGGCACCGAGGTGTGGACCGTGCCGGGCCGCGCCAACCGCCCCATCTCGCACCCGGTGGCCGAGGTCCGCCCGCTGGAGGAGGCCGACCGCACCCACAGCTGCGCCTTCTGCTCGGCGCGCTACCTGGAGACTCCCCCGGAGAAGGCGCGCCTCGTGCGCGGGGCCGACGGCGGTTTCGAGCGCCTCGACGCCGTCGCCGCCTCCGCCCTGTTCGACACGGTGGCCGAGTTCCGGCGGGTGCCCAACCTCTTTGAGATCCTCTCCTTCGACTACTGGCACATCAACCACGGCTACGAGATCCCCGACGCCGCCCGCGAGCGCATGGAGGCCTACTTGGCCGATCCGGCCGGCGTCGAGCACGTGGAGCGGGTGGCGCGCACCAAACTGGCGGCCGCGGGCGCGGACCCGGACTCCTGGGACTCGATGGACGAGCGGACCCGCCGCACCTTCCTGGCAGCCTTCTTCGCCGGGGGCCACGACGTCATCATCGGCCGGCGCCATTTCACGGACGACGCCGCCGACACCGCCGGCCTGGCCGGCTCGGGGACGCTGAGCGTGGCCGAGCACCGCGCCTACACGCGCCTGGCGATCCACGCGATGCACAGCCTGTACGAGGCCAACCGGTGGGTGCGCTACGTGGCCGTCTTTCAGAACTGGCTGCGGCCGGCCGGGGCGAGCTTCGACCACCTGCACAAGCAGCTGGTGGGCATCGACGAGCGCGGGGTGACCAGCCAGCTGGAGCTGCAGAAGGTGCGGGCCAACCCCAACCTGTACAACGAGATGGCGGTGGACTACGCCGCTTACCAGGGCCTGCTGGTGGCGAGCAACGAGCACGCGGTGGCCTTCGCCGGCTTCGGGCACCGCTACCCGACACTGGAGGTGTACTCGACGTCGGCCATGCCCGAGCCGTGGCTCATGAGCCGCGAGGAGGTCGACGCCGTCTCCGACCTGGTGCACGCCCTGCACGCGGCCACGGGCGCGGACGTGCCCAGCAACGAGGAGTGGCACCACAAGCCGCTCGACGTGGACCAGCCCATGCCCTGGCACATCACGCTCAAGTGGCGGGTCTCCACCCTGGCCGGTTTCGAGGGCGGCACGAAGATCTACCTCAACACCATCGACCCGTGGACGCTGCGCGACCGTGTGGTGGCGCGACTAGAGGACCTGCGGGCCGACCGGCTCATCGCGCCGATGGCCGTGGGTGAGGAGTGCCCGACGACGCCCAACCGGCTCCTGTACAACCCGGTCCTCACCGCCCGGCCGTAG","MLMPYSPSAEPLTRLADGTVKQISPFTGTEVWTVPGRANRPISHPVAEVRPLEEADRTHSCAFCSARYLETPPEKARLVRGADGGFERLDAVAASALFDTVAEFRRVPNLFEILSFDYWHINHGYEIPDAARERMEAYLADPAGVEHVERVARTKLAAAGADPDSWDSMDERTRRTFLAAFFAGGHDVIIGRRHFTDDAADTAGLAGSGTLSVAEHRAYTRLAIHAMHSLYEANRWVRYVAVFQNWLRPAGASFDHLHKQLVGIDERGVTSQLELQKVRANPNLYNEMAVDYAAYQGLLVASNEHAVAFAGFGHRYPTLEVYSTSAMPEPWLMSREEVDAVSDLVHALHAATGADVPSNEEWHHKPLDVDQPMPWHITLKWRVSTLAGFEGGTKIYLNTIDPWTLRDRVVARLEDLRADRLIAPMAVGEECPTTPNRLLYNPVLTARP$","Galactose-1-phosphate uridylyltransferase","Cytoplasm","conserved hypothetical protein","hypothetical protein","Galactose-1-phosphate uridylyltransferase-like","","","","","No hits reported.","No hits to the COGs database.","***** IPB001937 (Galactose-1-phosphate uridyl transferase, class I) with a combined E-value of 2.2e-46. IPB001937A 18-39 IPB001937C 184-231 IPB001937D 239-268 IPB001937E 284-324 IPB001937F 333-366 IPB001937G 370-410","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2096","2263959","2263021","939","5.10","-9.93","33412","TTGGCCATCGCAGTCTCACACCGATTCTCACCCAGCGGCGACCTTCCCGTAGACCCTTCCGGGAGGTACCCCTTGGCCATCGTAGTCTCATACCGATTCGTACCCAGCGGCGACCTTCCCGTAGAGGCGGGGCGCTACCGACTCGTGGCGTCGGGGGCCTGCCCGTGGTGCCGCCGCGTCCTCATCGCCCGGCGCCTGCTGGGCCTGACCGAGGCGATCCCCGTGTCCTGGAGTTACGGCAAGGGCGCGGACGGGTACTGGGAGCTGACCGGCCCCGACGGCGAGCCCGGCGTGGATCCGGCGCTCGGCGCCCGCTCCCTGGCCGAGGTCTTCGAGAAGACCCCCGGCTATACGCCTCCCCCCACGGTCCCGGCCCTCGTGGACACCACCACCGGCCAGGTCGTCAGCGACGACTCCGGCGACCTGCTCTTCGACCTGTCCACCGCCTGGTGGGACCTCCACCGCGAGGGCGCCCCGGACCTCTACCCGCTCAACCGCCGCAACTCCACCGACGCCTGGGACGCCTGGATCGGCTCGCAGATCAACGTCGGCCACGCGGTGGCCACCCACTCCCAGGACCCGGAGAAGGCCGCGGCGGCGGCCAACGGCGTCCTCGTGGGTTTCGACGTCATCGACACTCTCCTGGCCCGGGCCACGCGGATGGAGGCCTCCCGCGAGGACGGCCTGACGATGCTCGACGGGCCGGCCTTGTCCGCCGTCGTCGCCATCGGCCAGTACCTGTGCGGCGACAAGCCCACCGGCAGCGACATCCGCCTGTTCACCACCGTCCAGTCCTACGAGTACGGCGGGCGTCAGCACTACCCCGGCGGGGAGGCGCCGTCGATCTCCTTCTGGCCGGCGCTGGCCCGCTGGTTCCGTGCCCTGGAGGGCCGCTCGGGCTGGGTGGGGCCGGAGGAGCGCAGCGCCCTGGGCTGCTGA","LAIAVSHRFSPSGDLPVDPSGRYPLAIVVSYRFVPSGDLPVEAGRYRLVASGACPWCRRVLIARRLLGLTEAIPVSWSYGKGADGYWELTGPDGEPGVDPALGARSLAEVFEKTPGYTPPPTVPALVDTTTGQVVSDDSGDLLFDLSTAWWDLHREGAPDLYPLNRRNSTDAWDAWIGSQINVGHAVATHSQDPEKAAAAANGVLVGFDVIDTLLARATRMEASREDGLTMLDGPALSAVVAIGQYLCGDKPTGSDIRLFTTVQSYEYGGRQHYPGGEAPSISFWPALARWFRALEGRSGWVGPEERSALGC$","Glutathione S-transferase","Cytoplasm, Membrane","Predicted glutathione S-transferase","K07393 putative glutathione S-transferase","glutathione S-transferase-like","","","","","No hits reported.","BeTs to 6 clades of COG0435COG name: Predicted glutathione S-transferaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0435 is -o----y------cefg----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","glutathione S-transferase (o328)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2097","2267398","2264321","3078","4.99","-51.81","112189","ATGACGGTGCAACGTCAGGCTCCGCCCGGAAGGACAGACTCCATGACCACACGCGAAGACATCCTCGAGCGTCTGGCCTACGCCGATGCCCTCGGCCCCGGCCCCCAGACCTCGGCCCTCATCGCGGAGGCCGTCAGCTGGGCGGACGCACTGGGCGACGAGGACCTGCGGATCGCCACCCGGCTGGCCCTGACCGAGGCCTACCAGCAGGGCAACGAGGCGTGGAAGGCGCTGGCTCCCTTCTCGTGGAACCTCGGCCGCTACCAGCGCCGCCCCGAGGCCTTCGACGACGCCCAGGTGTGCACCCTGCACTGGCACTTCAAGTGGGCGGTGGCCGTGGCGGGCGCCAACCCCAGGGTCTCCAAGGACAAGGTGCGCCAGCTCGAGGCCAGCCTCGAGGAGTTCTACCGCTCCGGGGGCGCCTCCATGCACGTCGTCCACGGAGAGCGCGCCTCGGTTGCCGGCCTGCTGGGCCTGGAGGAGGAGGCCGCCGAGGAGCTGGCCGCCTGGCGGGCCACCCACCGCGACGAGAACGCCGACTGCGAGGGCTGCGACCCCATGCGTCAGGTCGCCTTCGCCTACCGCACCGAGGCCTGGGAGCTGGCCGTGGCCACCGCCGTGCCCGTGCTGACCGGCGCCGTCAGCTGCTCCGTGCAGCCCCAGACCACGCAGTCCCTCGTGCTGCTGCCCCTGTTGGCCTCCGGCCGGCCCCGGGCGGCCTGGGAGGCGCACCTGCGCTCCTACCGGGAGATCCGCCGCAACCCCAAGGCCCTCATCTCCCTGGCCTACCACCTGGAGTACCTGGCCCTCGTGGGGCGGGTGGACCGGGGCCTGGAGCTCCTGCGCCGCCACCTGTCCTGGCTGGCCCAGGCCGAGTCCGCCTACGTGCTGCTGTCGGCCCTGCGCGGCATGAGCCTGGTGCTGCGCGAGGCCGAGCGGGCCGGCCGCGGCGAGGAGGCCCTCGGCGTCGAGGTCCCGGCCGCCGACCTGTGGCACCCGCTGCCGGGACTGGAGGCCTCCACCACCATCTCGCGCGTCTACGCCGAGATGACCGGCTGGGCCCGGCGCCTGGCCCAGCAGTTCGACATGCGCAACGGCAACTCCACCATCTCCGACCACCTGGAGCGCTCCCTGGCCCGGGCCGCCTTCGACGCCGCCCCCGGCGCGGTCCACGGGCTGGGCGTGGAGGTCGACCTCCTGGAGCCCTCCGAGGAGCTGCCCGAGGCGGCCCAGACGAGCCTGACCGTGGACGAGGACGGCGCCGCACCCGATGTCGCCTCCCTCCTGGGCCTGGTGGCCGACGACAACGGCCTGGTCCAGGAGCACGCGCCCCGCACGACGTCGTCGAGCCAGGAAGCGGCCGGCCGACGCGCCCGCGCCGCCACCAGCCACCAGAGCGGCGACGCGCCCTTCCCCCTGGTGGACCTCGTGCGGCCCCGGCCGGTGCGCAACGGCGAGGAGGCGGTGCGCCGCTACGTCGACCACCGCCGCACCATCGGCTCCTCGACGATGGACTACTGGTACGTCGTCGACCAGGTGGCCACGCGCGACCTGCTGCCCCCGCGCGGCGAAGAGATCCCGGGCCTGGAGTACCACACGGGACTGCTGCGGGCCGCCGCCATGACCTGCCGCACCGAGATGGATGAGGCCATCGCCGAGCGCCTGCGGATCCGCCCTCTCATCGAGCTGGTCTTCGGGCCGCTGGGCGCCTACTACGTGGACCTGCTCAACCTCGACAACGAGATCACCGCCGACTCCATTGCCGAGCTATCCCAGGACGTCTTGCGCGATGAGCGCCTGCAGCGGGCCACCTCCCTCATCGGGCAGATCGAGGCCCAGGTCGAGGACCTGGTGTCCACCGAGCTGCTCGACCCCGGGGGTACCGACGCCCTCGTCCTGGCGGCCGACGCCCTGCTCGTGGGGGCCTCGGTCCTCACCGACCTGCACGCCAAGGACGAGGCGCTCGGGGCGATCCAGGTCGTCGCCCGCGCCGCCGAGGCCGTCCCCGAGGACCGCCACGCCGAGCGGATGGACGACATCCTCGACATGGCGCGCGCCGAGGTCCTGGCCGAGTGCGGCGACGTCTACAACGGCTGCCTGCTGGCCGAGGAGGTCATGCGCCGCCACGAGAAGGTCTCCCCGGTCCTGGCCGCCCGCGGTCGGCGCCTGCTGGGCATCTCCTCCATGGAGGTGGGTCAGTTCGATGAGGCCATCGCCCAGTTCCGCGAGCAGGCCAACATCATGCTGGCCGCCGGCATCACCCTGTACGCCGTGGCCTCCCTGCTGTCCCTGGGCTCGGCGCTGGAGGCCTCCGAGCGCTACCTGGAGAGCGCCGAGGTCCTGGAGTCCGCGCTGTCCCTGGCCCAGCGCACCGGGGCCACGAGCATCGCCCTCTACCTGCACCGACTCCTGGCCCAGACCGGCATGGCCATGGGCGAGGAGGAGAGCGTCGCCGAGCACTCGCTGGCCGCCGCCCGCATCCTGCAGGAGCAGGGGCGCCGGGCGCTGGCGGGGGAGTACCTCGCGCACGCGGCGATGGCCGTCTCCAATCTCAAGGACAATGTGCGCGCCGCCGCCCTGTTCCGCCAGGCCGCCGACCTGGAGGACACCCGCACCGACCAGGGCTGCCTGGACCGGGGGCGGGCGCTGCGCCGCTCGGCGCGGGCGCTGGTGGACGACCTCACCCTGCCCATGGCCCGGGGGAGGCTCGACGAGGCCCGCCAGATCATGGAGGAGGCCCGCCAGGCCTTCGCCGGCGTGGCCGACACCGAGGGCTACTCCTCGGCCTGGGAGATCGGCGACTGGCACGACGACATGGCCTGGATCCTCTGGCGCACCGGCCAGAACTGGCAGGCCGTCCAGCACTGCGAGTCCGCCTACGACGGCTACATGGACACCGAGGACCGCGACTCGGCCTCGCGGGCCCTGTGCATGCTGGCCCGCCTGCACGCCGAGCGCGGTGAGCGCGAGGAGGCCCTGGCCGCCTGCGCCCGCGTGCGCGACCTGCTGGGCGAGCCGCACTGGGACGGTCACGACGCCTTGGAGTTCGTGGCCTCCGTGGAGGAGACACTGCGCTGA","MTVQRQAPPGRTDSMTTREDILERLAYADALGPGPQTSALIAEAVSWADALGDEDLRIATRLALTEAYQQGNEAWKALAPFSWNLGRYQRRPEAFDDAQVCTLHWHFKWAVAVAGANPRVSKDKVRQLEASLEEFYRSGGASMHVVHGERASVAGLLGLEEEAAEELAAWRATHRDENADCEGCDPMRQVAFAYRTEAWELAVATAVPVLTGAVSCSVQPQTTQSLVLLPLLASGRPRAAWEAHLRSYREIRRNPKALISLAYHLEYLALVGRVDRGLELLRRHLSWLAQAESAYVLLSALRGMSLVLREAERAGRGEEALGVEVPAADLWHPLPGLEASTTISRVYAEMTGWARRLAQQFDMRNGNSTISDHLERSLARAAFDAAPGAVHGLGVEVDLLEPSEELPEAAQTSLTVDEDGAAPDVASLLGLVADDNGLVQEHAPRTTSSSQEAAGRRARAATSHQSGDAPFPLVDLVRPRPVRNGEEAVRRYVDHRRTIGSSTMDYWYVVDQVATRDLLPPRGEEIPGLEYHTGLLRAAAMTCRTEMDEAIAERLRIRPLIELVFGPLGAYYVDLLNLDNEITADSIAELSQDVLRDERLQRATSLIGQIEAQVEDLVSTELLDPGGTDALVLAADALLVGASVLTDLHAKDEALGAIQVVARAAEAVPEDRHAERMDDILDMARAEVLAECGDVYNGCLLAEEVMRRHEKVSPVLAARGRRLLGISSMEVGQFDEAIAQFREQANIMLAAGITLYAVASLLSLGSALEASERYLESAEVLESALSLAQRTGATSIALYLHRLLAQTGMAMGEEESVAEHSLAAARILQEQGRRALAGEYLAHAAMAVSNLKDNVRAAALFRQAADLEDTRTDQGCLDRGRALRRSARALVDDLTLPMARGRLDEARQIMEEARQAFAGVADTEGYSSAWEIGDWHDDMAWILWRTGQNWQAVQHCESAYDGYMDTEDRDSASRALCMLARLHAERGEREEALAACARVRDLLGEPHWDGHDALEFVASVEETLR$","Tetratricopeptide TPR_4","Cytoplasm","conserved hypothetical protein","hypothetical protein","Tetratricopeptide TPR_4","","Tougu K., Peng H., Marians K.J. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 1994. 269(6):4675-4682. PMID: 8308039","","","

InterPro
IPR011717
Repeat

Tetratricopeptide TPR_4
PF07721	$\"[973-998]T$	TPR_4

InterPro
IPR013026
Domain

Tetratricopeptide region
SM00028	$\"[758-791]T$ $\"[973-1006]T$	TPR

InterPro
IPR013173
Domain

DNA primase DnaG, DnaB-binding
SM00766	$\"[509-618]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 973 to 998 (E_value = 0.028) place ANA_2097 in the TPR_4 family which is described as Tetratricopeptide repeat.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2098","2269049","2268609","441","4.56","-12.87","16014","ATGAGTGCCCAACCGGCTCTGACCCTTCAGCGGGTCGAGACCTGGCTGTCCCAGCACGGCATCACCGCCGGCCCTGAGGAGGACGGTGCCGTCTTCATGGGCTTCCCGGGCTGCGACATTGGCGTCTACCTGCATGACGAGGAGGACGCCCTCGTCGTGGCCGGCATGTGGCGTGGGCGCCCGGCGGCCGAGCGCCTCGATGAGATGCGGGCCTTCATCGACGCCCAGCACCGTTCCACCTACGGCCCGGACCTGGCCGTCACCCCCGCCCACGACCCCGGCCACCTCCTGCTGAGCACCCAAATGGTGGCCTACGTCGGCGCGGGCATGAGTCAGGCCCAGCTCGACGCCTTCATGGACATGGGCCTGGGCATGACCCGCGCGTTCTTCGCCACCGTCCAGGAGCGCTTCCCCGAGCTCGTCACCTGGGAGGAGGACTGA","MSAQPALTLQRVETWLSQHGITAGPEEDGAVFMGFPGCDIGVYLHDEEDALVVAGMWRGRPAAERLDEMRAFIDAQHRSTYGPDLAVTPAHDPGHLLLSTQMVAYVGAGMSQAQLDAFMDMGLGMTRAFFATVQERFPELVTWEED$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2099","2267419","2268717","1299","9.36","11.88","44263","GTGCTGCAAGAACGCACGGAATGCGCTCCGCCGACCCCAGGGATGCCGTGGGTGGAGCGTCGTCCCGCACCGCTCACCGGTGAACGGCGGCATGGGCATCTCGGGCTCCTTTCGTCCAGAGGGCGGTTGTCCGACGTCCAGTGTTACCGAACAGTTATAGAATCCGCTACTGCAACGGCCAGCGGCAACTCGGCCGCGGGGCATGTCGGGGTCGGGCGCCGCCGCCCGCACCAGTCGGCACCAGGGCCGCCCACTCCGACGCGGGCTCCCACCACTCCAGTGTTTCCAACGGATGCCGCCGCACCGGATCTGGGAGCCCGGGGCGCGCTAGGACACCAGCAGAGGCTTGGGGGTGTCGGTTGTCTCAGCCCCGGTTCCGCCCTGAGCATCACCCGGGACACCGGGGACCGGCCCGTCGACGACGGCGGCTATCTCCACAGTCGCATCCGCCATGCCCGCAGCCGTGCCGATAGTCGTGCCGCCAGTCACGCCCTGCATCGTCGCCACGGGAGTCTGCGCACCCTCCTGCCCGGACTGACCTCCCGCAGCCTCAGCAGCGCCGGCGACGTCGGTGGGGTCGTCTGCGGCCCGGGCGGGCCGGGGCGCCTCGGGCAGGGCGATCACGGTCGCCCCGTCGTCCTCTCCCTCAGTGTCGATCTCACCGACGGTCTCCGGCGCGCTCTCAGCCCGGGGCGCGCTCTCAGCCTCCGTCCCAGCGTCGGGCCGCCTGTCGGCAGCGGCGTCCTGGGCGGCCAGAAGGCTGAGGACCTCGCGCAGGGCCTGATCGACGCCGTCGAGGATGAAGTCCAGGGTGCCGGCCAGCTGGGCGTCGTCGAGCCCGGCCCCGATGTTGGTGAGGACCTCGGCGCACAGGCCCAGGCCGGCGTCGTCGACCTCGGTGTAGAAGGCGGGGATGAGCCGGCCGCTGGAGACCTCCTGGGCCACGGAGCGCACCCGCGAGAGCTCCGCGGAACCGGGCAGGGCGGCGGCAAGCCGGTGGTGGGCGCGCACGGCGAGGATCCGGCGGTCCACCACCATGAGCACGTAGTCAAATCCGGCCACCGAGAAGTGCACCACCCCCTCGGACAGGTCGAGGTCGTATCGGTGGCCGCGCTCGGCCATCCAGGCGGCGAGCCGCCTGAGGGTCACGGTCGGGGTCACCGACCCCTCCGGCTGATTCCACCAGGCCATCAGTCCTCCTCCCAGGTGACGAGCTCGGGGAAGCGCTCCTGGACGGTGGCGAAGAACGCGCGGGTCATGCCCAGGCCCATGTCCATGAAGGCGTCGAGCTGGGCCTGA","VLQERTECAPPTPGMPWVERRPAPLTGERRHGHLGLLSSRGRLSDVQCYRTVIESATATASGNSAAGHVGVGRRRPHQSAPGPPTPTRAPTTPVFPTDAAAPDLGARGALGHQQRLGGVGCLSPGSALSITRDTGDRPVDDGGYLHSRIRHARSRADSRAASHALHRRHGSLRTLLPGLTSRSLSSAGDVGGVVCGPGGPGRLGQGDHGRPVVLSLSVDLTDGLRRALSPGRALSLRPSVGPPVGSGVLGGQKAEDLAQGLIDAVEDEVQGAGQLGVVEPGPDVGEDLGAQAQAGVVDLGVEGGDEPAAGDLLGHGAHPRELRGTGQGGGKPVVGAHGEDPAVHHHEHVVKSGHREVHHPLGQVEVVSVAALGHPGGEPPEGHGRGHRPLRLIPPGHQSSSQVTSSGKRSWTVAKNARVMPRPMSMKASSWA$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2101","2270882","2269827","1056","5.89","-6.25","40290","ATGTCCGCCTACGTCCGCTACTACCGGCGGCTTCAGGCACTCACTCAGCGCCTGAGCACCTACCTGGACCGGTTGGAGGCTCGCGCCCGGGAGTTCGGCGTCAGCTCGGCCCGCACCGCGATGGAGATGCAGATCACCGACCCGGCCTCCGTCTCCGCCTTCCGCTCGGAGGTCGAGGCCCAGATCATGTTCCTGCACACCAAGGCCCAGCGGGTCTTCGCCAAGCACTTCGCCCCCTTCCTGGACATCGACGCCGACCTGTCCATCGACGAGGACCGTCAGCTCTCCGCCCGCCTCCAGGATGCGGCCAACCTCGTGGGCGGCTTCGAGGTGCGCCTGCGCAACATCATCGAGGAGGTCTTCGCCCCCGGCCGCGCCGAGCAGGCCCGCGAGGAGTGGAACCGCGCCATGACCGACTGGCGCCAGGCCCAGTTCTCCTTCACCTGCGACAAGTGCGGCGACCCGGTGCCGCTGCCCGAGCTCTACCACATGCCGGTGTTCATCACCTGCCCGCGCTGCAAGTCGCGCGTGGCCTTCCAGCCCACCGAGGCCATGGCGGCCGCGCCCACCTGGGCCAAGGAGGTCGCCAAGACCACCTGCTACGCCGAGTGGCAGAAGTCCGAGTCGGAGCAGGCCGCTGAGGAGGGGGTGGGCCTGGCCTTCTTCTACTACGTCGACTACGCCATCGCCCACCACCTCATGATGAACCGGCTGCTGCCCTTCTACGTGCGCTCCCAGGGCGGCCAGGAGGCCCTGCGCCGCGACGTGCGCAAGGCGCTGGAGACCCGCACCCACCAGCTGCGCCCCGACGAGGTCTCCCCCCAGTACCACGCCATGGAGTACGTCAACTTCATGGGCGGCCTGGGCCGCTCGGCCCAGATCCTGGGCCAGGAGGGCCTCGAGGACCGCCGCGAGCTCATCCTGCAGACGGTGCGCGACATCATGCGCCCCGACGAGCCCCTGGCCCGCTCCATCCTGGACAACACCTTCACCGAGGAGCTGTGGAGCCAGCAGGCCCACGCCGCCGACCAGCTCTCCTGCGAGGTGCCCCGCTAG","MSAYVRYYRRLQALTQRLSTYLDRLEARAREFGVSSARTAMEMQITDPASVSAFRSEVEAQIMFLHTKAQRVFAKHFAPFLDIDADLSIDEDRQLSARLQDAANLVGGFEVRLRNIIEEVFAPGRAEQAREEWNRAMTDWRQAQFSFTCDKCGDPVPLPELYHMPVFITCPRCKSRVAFQPTEAMAAAPTWAKEVAKTTCYAEWQKSESEQAAEEGVGLAFFYYVDYAIAHHLMMNRLLPFYVRSQGGQEALRRDVRKALETRTHQLRPDEVSPQYHAMEYVNFMGGLGRSAQILGQEGLEDRRELILQTVRDIMRPDEPLARSILDNTFTEELWSQQAHAADQLSCEVPR$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2102","2275464","2271769","3696","6.64","-5.86","135667","ATGACGCACATCCCTACACCATCCATAAACCGCATGAACTTCATGATCTCTGACGATCTGCCCGTTTCCAAGGCGCCCACACAGGTCCGAAACTGGCAGTCGAGCCTGCTCGACCTCTCTCGGCGCAACCCCCTCATCAATCGCACCTCTGGCCACGCCGTGGAGCTGCGCGTCCCGCCAGCGCTCATTGGTGAGTTTGAGGACCTTGTTAATGACAAGGAATACATCACGATCGCCTCCGGGCGATACCGCCCGTCGGGGCTGTCCGACGGTGAGCTTCAGCGCGAGCAGGTCCGAGCAGAATCGCTCCTGAGGGAACGAACCGTCGAGGTCGAGCTGGTACCCAAGGACGAGTACGTGCAGCGCCTTCAGTCCCTGGCCACCAGCGCCCGTACCGCCGTTGAGGAAACCGGTGCCAATAATCTGTACCTGGCCATCGGCACCTTGCACTGGGACAGTGACGGTAGCCGCCTGCACTCCCCGCTCATCCTCATCCCGGTCAACCTCGAGCGCACCGGAGACGACTTCAGGCTCATCCTGGATGAGACAGGCGTCTCCACGCCCAACTACTCCTTCCTGGACCGCTTCGCGCGGGACACCGGTATCGAGCTCACCGAGCTGAGGACTCCGAAGCTCGACGAGCACGGCATCGACCTGAGGGCCACTCTTGACGGTGTACGCGACCGTCTGCGACGCGCCGGCTGGGACGACGTCGTCACCCCCACAGTCCATCTGGGCCTGTTCCGCTTCTCCACCTACCGGATGTGGAAAGACCTCGAGGACCACTGGCCGACGATCTCCGCCAACCCGCTGGTCGCCCATCTCATGGTAGGAGGGAGCCGCAACTTCGTGGATCCGGCTGGGCCGGCCGACACGGATCTCGACATTGATGAGGCCACCCAGAACCTACCTTTGGCCGCAGACTCCGCTCAGGCCCGAATCGTGGCCGACGCCGTCGCCGGACGAAGTCTCGTCGTCGAGGGGCCGCCTGGAACAGGTAAATCTCAAACCGTCTCCAACCTCATCTTCCGAGCGTTGGCCACGGGACGGACCATTATGTTCGTCGCAGAGAAGAAGTCCGCCCTCGACGTCGTCGCCCGTCGCCTGCGCGAGGAGACCGGCATCGGGGACCTACTGCTCAATCTGCACGATAACGGCATGAAGCCGACCGAGGTCCGTCGAGCCCTGCGCCGGGCTCTGGCCCTGCGGCGAGAAGAGTCCGGAGACGGTGCCGGTGAGGTGGCCGGCTGCTCCACTCCGGCCGCGCTGCGTGCCGAGTTGGCAGTGATCCGCGCCGAGCTCGACGCCTACCGCCGCGGCCTGTACGAGCCGGCTCCGGGTGGCCCCTCCTACAGTGGAGCCCGAGAGGTGCTCGCCCAGCTCCGGGACTCCGGAGAATCCGGGGACCGTGCCGATTCGGCGGCCTTCGAGGCTCGGTCCGCCCTTGGGGAGCGGGCCCGAGCCACAGGCCTGGACACCTTCGACGCCGCTGCCCACAATCGGCTCATTGAGCGCTACCGCGCCGCTCTGGACAAGCTGCGCCGGGCTCTGACACCTGAGCTGCTCGACGTCGTCCTGGCCCACCGCGACCAGGTCCTTCAGGGCGCCGCCGCCCATGCCGAGGCGCTGCGCAGCGAGGTCAACCGGCGTCGCAGCGTCATGAGCGTGCGCGAGCTGATCCGCACCTACGGCGACCTCATCACCGCCCTGATGCCCTGCCTGCTCGTCTCGCCCGACTCGGTAGCCCGGTTCTTCCCGGCCAACCGCCGCTACGTGGACATCGTCGTCTTCGATGAGGCCTCCCAGATCCGGGTGGCCGACGCAGTCGGCGCCATGGGGCGCGGCCGCAGCGTGGTCGTGGTCGGCGATCCCAAGCAGATGCCGCCGACCCCCAGCGCCGGCGAGACACGAGGGGAGCAGGTGCCCGAGGCCGACTCCATCCTCGCGCGCTGTCTGGACAGCGGCCTGCTTCAGCGCCGACTCACCTGGCACTACCGAAGCCGGGACGAGTCCCTCGTTGCGTTCTCCAACCAGCACTACTACGACGGCCGGCTGCGCACCTTCCCCAGCCCACTGACCATGGCCACCGGTTCCGACGACGGCCCAGGCGGTCACGGGATCTCACTGCGGCGGGTCCAGGGCAGCTACTTCCGTCCGGAGGACCGCGCCCGACACTTCGGTGCGTCTCCGAACACGAACCCCCTCGAGGCCAAACGAGTGGTGGACGAGGTGCTCAGGCACTTCGAGGCCTCCCCCGACCGCCTGCCCTCACTGGGCGTCATCACCTTCAACGATCGCCAGCGCGATCTCATCGAGAACAGCCTGCGCGAGGTTTCCTCGCCCCGAGTCATCGAGGCCCTCGACGCCCGCGACGGCCTGTTCGTCAGGAACCTGGAGAACGTCCAGGGCGAGGAGCGCGACACGATCCTGTTCTCAGCGACCTTCGCCGCCAACTCTCGAGGTGACTTGCCGCTGAACTTCGGGGTGCTCAACCACGTCGGTGGAGAGCGTCGTCTCAACGTGGCCATCACCCGGGCCCGTAGGCAGATCATCGTTTTCACCAGTTTCGACCCTCAGGACCTGCACGCCGAGCGCACGGCCCACCGAGGAGTCAAGGACCTGCGCGCCTACCTCCACCAGGCCGCCGAAGGGCGGGCCCCACGGGCCCTGCCGGCCTCGCAGAGTCCACTCAACTGGCACCGGCGTGAGATCGCCGAGGCGCTGGACGCTGCCGGGCTTACGGTCCACACCGGTGTCGGTCACTCCACCTTCGAGATCGACCTCGTGCTGGCGCGCGCCGGCCAACCTGACCTTCCCGCCGTGGCTGTCCTGCTCGACGGGCCGCAGTGGAACAAGCGGGAGGGCGTCGTCGACCGCGACCTGCTGCCGGTCGACGTCCTGCACACCATGGGCTGGCAGCGGGTCGAGCGGGTCTGGATGCCCGAATGGGTGGCAGATCCGAAGGCCGTCGTCGCCCGACTCGTCACGGCAGCCGGCGGCCACTGGGTGCAGCCGACGGTGTCAACCGTCGTGCTTGAATCGGAGCGGACTGACCATGCCGGGGACGCTGCGCCGCCGATTAAGGACGATGCGAAGGCTGATGGCCGGGACCTCGCGCCTGTGGACGGGGAGACGATGGCGCCTGCTGCCGGCCCGCGTGCCCCGGGGCAGGAGTACACCGCTTGGAGCCCGGCAGGCGTACGCCCCCTGGAGATCCTCAACCGGGCAGGTACTGACCCGGAGGCCAAGAAGGTACTCGTGGAGGTCGCCACCACCATCTGCCAGGTCGAGGCGCCGATCTCCAGGCGCCGGCTCTACGTCAAGATCTCCCGCGCCTTCGGACTGTCGCGAACCGTCAAATCGCGCGAGGAGTCGATCAGGACGGCCCTGGGCGAAGCCTTCGCCTACTTCGACGAGGACGGCTTCGTGTGGGCCACGCGGGACGATGCGCTCGCGGCTCCGACCTACCGTCGCAATGCTCTGGACCATGTGGACTCTATTCAGGAGATCCACCCGCGCGAGCTGGTGGGGCTCATGGCTCAGGCACGTGCTAAGAACCCGGAGTGGGCTTCCCGGGAGGACCTGTTCATGTGGGCGCTCAAGCGTCTGAGTGCGAGGAACCGCAGTCTCGCAGCGCGTGGGGTGGTGGAGGCGCTCACCAAGGCCCTCAAGGACGTGGAAGGCGTGCGCGCGTAG","MTHIPTPSINRMNFMISDDLPVSKAPTQVRNWQSSLLDLSRRNPLINRTSGHAVELRVPPALIGEFEDLVNDKEYITIASGRYRPSGLSDGELQREQVRAESLLRERTVEVELVPKDEYVQRLQSLATSARTAVEETGANNLYLAIGTLHWDSDGSRLHSPLILIPVNLERTGDDFRLILDETGVSTPNYSFLDRFARDTGIELTELRTPKLDEHGIDLRATLDGVRDRLRRAGWDDVVTPTVHLGLFRFSTYRMWKDLEDHWPTISANPLVAHLMVGGSRNFVDPAGPADTDLDIDEATQNLPLAADSAQARIVADAVAGRSLVVEGPPGTGKSQTVSNLIFRALATGRTIMFVAEKKSALDVVARRLREETGIGDLLLNLHDNGMKPTEVRRALRRALALRREESGDGAGEVAGCSTPAALRAELAVIRAELDAYRRGLYEPAPGGPSYSGAREVLAQLRDSGESGDRADSAAFEARSALGERARATGLDTFDAAAHNRLIERYRAALDKLRRALTPELLDVVLAHRDQVLQGAAAHAEALRSEVNRRRSVMSVRELIRTYGDLITALMPCLLVSPDSVARFFPANRRYVDIVVFDEASQIRVADAVGAMGRGRSVVVVGDPKQMPPTPSAGETRGEQVPEADSILARCLDSGLLQRRLTWHYRSRDESLVAFSNQHYYDGRLRTFPSPLTMATGSDDGPGGHGISLRRVQGSYFRPEDRARHFGASPNTNPLEAKRVVDEVLRHFEASPDRLPSLGVITFNDRQRDLIENSLREVSSPRVIEALDARDGLFVRNLENVQGEERDTILFSATFAANSRGDLPLNFGVLNHVGGERRLNVAITRARRQIIVFTSFDPQDLHAERTAHRGVKDLRAYLHQAAEGRAPRALPASQSPLNWHRREIAEALDAAGLTVHTGVGHSTFEIDLVLARAGQPDLPAVAVLLDGPQWNKREGVVDRDLLPVDVLHTMGWQRVERVWMPEWVADPKAVVARLVTAAGGHWVQPTVSTVVLESERTDHAGDAAPPIKDDAKADGRDLAPVDGETMAPAAGPRAPGQEYTAWSPAGVRPLEILNRAGTDPEAKKVLVEVATTICQVEAPISRRRLYVKISRAFGLSRTVKSREESIRTALGEAFAYFDEDGFVWATRDDALAAPTYRRNALDHVDSIQEIHPRELVGLMAQARAKNPEWASREDLFMWALKRLSARNRSLAARGVVEALTKALKDVEGVRA$","DNA helicase-related protein","Cytoplasm","DNA helicase related protein","DNA helicase-related protein","Superfamily I DNA and RNA helicase and helicase subunits-like","","","","","

noIPR
unintegrated

unintegrated
PTHR10887	$\"[1-386]T$ $\"[510-983]T$	DNA2/NAM7 HELICASE FAMILY
PTHR10887:SF7	$\"[1-386]T$ $\"[510-983]T$	DNA2/NAM7 HELICASE FAMILY MEMBER

","BeTs to 15 clades of COG1112COG name: Superfamily I DNA and RNA helicases and helicase subunitsFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1112 is aompk-yqv-r--cef--s-u----wNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","helicase related protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2103","2277079","2275781","1299","10.71","22.79","47853","ATGGGTAACTCGATTTCGCCGTCTCGGCGTGAGCAGGTCATAGGTTTTGACTCCAGGACCAGTGGGATGAGCGTGGAGGAGTTCTGCGCTCAGGTGGGTATCTCGCGGGCCTCGTTCTACCGGATACGCCGACGCGCTGAGCACGAGGGCCTGGCTGCCGCGCTGACACCGCGTTCACGGGCCCCGCGCCACCCGGCGCGGGTGTGGGACCAGGGCACTGATGAGCGCATCGCCCAGGTTCGCGCCGACCTGCTCGCCGCCGGCCGGGAGGCGGGTCCGGCCTCGGTGTGGTGGGTGATGAGCCAGGGCGCCAGCGTTCCGGCTCCTTCGCGCGCGACGATCGCCCGCAGCCTACGCAGAGCCGGCCTGGTGGTCCCCGCCCCGCGCAAGCGGCCCAGGACGTCGTACAAGCGCTTCACCCGCAGCGCGGCCAACGAGCTGTGGCAGATCGACGGCTTCCAGTGGCGCCTGGAGGACCGTCTGGTGACCGTCTACCAGGTCGTTGACGACTGCTCGCGGGTCATCACCGCCCTGAGGGCCTGCTGGGGCGGTGAGAGCGTGGCAGGCGCCCGCATGGTCCTTGAGGAGGCCTTCGCCACCTGGGGGCGTCCGGCGGCGATCCTGTCGGACAACGCGCTGGCGTTCAACACCAGCCGTATCACTGGCCCGGGAGCCACCGAGAAGTGGCTGGCATCCCTGGGGGTGCGTCCCATCAGCGGGCGGGTGGGCCACCCTCAGACCCAGGGCAAGGTCGAGCGCTCCCACCAGCCGGCAGCCGCCTGGCTGCGCGCCCACCCGGCCAGCACCCTTGAGGAGCTCAACGCCGAGCTGGACCGCTTCACCAGCTACTACAACACCGAGCGCCAGCACCAGGGCCACGGCGTCGCACTGACCCCGCTGAGGGTATGGGCTCAGACCCCCAGGGCGCTGGCCAGCCCAGCCCCCATCGACCTGGAGCGCCTACCAGCCGGCGGCGGCCCCATCAGCCTGCCCGACCCCGCCGATCCCGACCAGGCCGTGGACCGCGCCCGACGCACCGTGATGTCCAACGGGTGCGTGTCCTACAAGGACCGTGCACTGTCACTGGGCCAGACCATGCGCGGCGTCGAGGTCACCCTGATCGAGTACACCACGCGCCTGGACCTCTACGACCCCGACGGACGCCGCTTCGTGTCCCTGCCCTGGCCCCAACCCACCCAGAGGCAGCAAGGCAACCGCTCCACCATCGACACCAAGAAACCGCCCTACAGACTCATCCCGCTCCCACCCCGACGCCCCCGAACGTCTCACAGGTCATAA","MGNSISPSRREQVIGFDSRTSGMSVEEFCAQVGISRASFYRIRRRAEHEGLAAALTPRSRAPRHPARVWDQGTDERIAQVRADLLAAGREAGPASVWWVMSQGASVPAPSRATIARSLRRAGLVVPAPRKRPRTSYKRFTRSAANELWQIDGFQWRLEDRLVTVYQVVDDCSRVITALRACWGGESVAGARMVLEEAFATWGRPAAILSDNALAFNTSRITGPGATEKWLASLGVRPISGRVGHPQTQGKVERSHQPAAAWLRAHPASTLEELNAELDRFTSYYNTERQHQGHGVALTPLRVWAQTPRALASPAPIDLERLPAGGGPISLPDPADPDQAVDRARRTVMSNGCVSYKDRALSLGQTMRGVEVTLIEYTTRLDLYDPDGRRFVSLPWPQPTQRQQGNRSTIDTKKPPYRLIPLPPRRPRTSHRS$","Transposase","Extracellular, Membrane","Predicted transposase","integrase; catalytic region","Integrase, catalytic region","","Asante-Appiah E., Skalka A.M. HIV-1 integrase: structural organization, conformational changes, and catalysis. Adv. Virus Res. 1999. 52:351-369. PMID: 10384242Thomas M., Brady L. HIV integrase: a target for AIDS therapeutics. Trends Biotechnol. 1997. 15(5):167-172. PMID: 9161051Katzman M., Katz R.A. Substrate recognition by retroviral integrases. Adv. Virus Res. 1999. 52:371-395. PMID: 10384243","","","

InterPro
IPR001584
Domain

Integrase, catalytic core
PF00665	$\"[140-304]T$	rve
PS50994	$\"[128-307]T$	INTEGRASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[143-310]T$	no description
PTHR10178	$\"[129-291]T$	GAG/POL/ENV POLYPROTEIN

","BeTs to 5 clades of COG1425COG name: Predicted transposaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1425 is a--p-----dr---efgh-n-j----Number of proteins in this genome belonging to this COG is 7","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 140 to 304 (E_value = 5.9e-22) place ANA_2103 in the rve family which is described as Integrase core domain.","","transposase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2104","2278327","2277224","1104","6.21","-2.78","38573","ATGAGCCCGACTGCCAGTGACACCAGTACTTCGACGGGCCTGTCCGTGCGCGGGCTCGCCGTGACCTACGGGGACCTGCACGCCGTCGACGGCGTCGACCTGGAGGTGGCCGCCGGGGAGGTCGTCGCCCTCCTGGGGGCCTCGGGCTCGGGCAAGTCCTCCCTGCTGCGCGCGGTGGCCGGCCTGGAGGATGTGGCCGCAGGCGAGGTCGCTTGGGACGGGCGGAGCATGGTGCGAGTGCCCGTTCACAAGCGCGGCTTCGGCCTCATGTTCCAGGACGGCCAGCTCTTCGAGCACCGCGACGTCGGCAGCAACATCGCCTACGGTCTCACCGGCCTGCCGCGCGCCCAGCGGGGTGAGCGGGTGCGCGAGATGCTTGAGCTCGTCGGCCTGCCCGGCTTCGAGCGGCGGCGCGTGACGACCCTGTCCGGCGGGCAGGCCCAACGGGTGGCTCTGGCCCGGGCGCTGGCGCCGGCGCCGAGGCTCCTCCTGCTCGACGAGCCCCTGTCCGCCCTGGACCGGGCCCTGCGCGAGCAGCTGGCCACCGACGTGCGCACCATTCTGCGTCGGGGTGGCACCACGGCGCTCTACGTCACCCACGACCAGGACGAGGCCATGACCGTGGCCGACCGGGTCGGCGTCATGGAGGCCGGCCGCCTCCTGCGCCTCGACACCCCCCAGCGCCTGTGGGCCGACCCCGGCAGCAGCAAGGTGGCGCGGTTCCTGGGCTTCGACGTCGTCGGCGACCTCGCCCTCGCCCCCGGCGCGCTGCGCGTGGTGGAGGCCGCGGCGGGGGAACCGAGAGAGTCGGACGGGCCCGCGCAGACGGAGACACCGGCGACACCGGAGACTCTGCCGGCCACCGTGCTGGCCTCGCGGCTGCGTCGCGGCCAGTGGGAGGCCGAGGTCGAGCTCGACCCCGAGCGGCTCGCCGGGCTGGTGGGGTCGGACGGGCCGGCTGAGCCGTCCAGCGTCGGGGCTGATGTGGCGGCGGGTCGTGAGCCGGCCCGTGCTACCCGTGCTACCGCCCTGACCCGGCGCCCCCACGCGTCCGGGGCGCGCGTCACCCTGAGTCTCGACCCCGCCCGCACCGCCCGGCTGTAA","MSPTASDTSTSTGLSVRGLAVTYGDLHAVDGVDLEVAAGEVVALLGASGSGKSSLLRAVAGLEDVAAGEVAWDGRSMVRVPVHKRGFGLMFQDGQLFEHRDVGSNIAYGLTGLPRAQRGERVREMLELVGLPGFERRRVTTLSGGQAQRVALARALAPAPRLLLLDEPLSALDRALREQLATDVRTILRRGGTTALYVTHDQDEAMTVADRVGVMEAGRLLRLDTPQRLWADPGSSKVARFLGFDVVGDLALAPGALRVVEAAAGEPRESDGPAQTETPATPETLPATVLASRLRRGQWEAEVELDPERLAGLVGSDGPAEPSSVGADVAAGREPARATRATALTRRPHASGARVTLSLDPARTARL$","ABC-type sugar transport system, ATPase component","Membrane, Cytoplasm","ABC transporter ATP binding protein","ABC transporter related","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[39-218]T$	ABC_tran
PS50893	$\"[14-242]T$	ABC_TRANSPORTER_2
PS00211	$\"[142-156]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[38-219]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[14-251]T$	no description
PTHR19222	$\"[14-264]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF46	$\"[14-264]T$	ABC TRANSPORTER

","BeTs to 3 clades of COG3839COG name: ABC-type sugar transport systems, ATPase componentsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG3839 is -o-pkz-qvdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 2","***** IPB005116 (TOBE domain) with a combined E-value of 1.5e-42. IPB005116A 46-62 IPB005116B 85-102 IPB005116C 142-155 IPB005116D 162-181 IPB005116E 196-209***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3.7e-33. IPB013563A 28-62 IPB013563C 139-166 IPB013563D 194-246***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 2.1e-29. IPB005074C 28-75 IPB005074D 130-173***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.4e-18. IPB010509B 39-64 IPB010509D 137-181***** IPB010929 (CDR ABC transporter) with a combined E-value of 8.6e-08. IPB010929K 26-70 IPB010929M 139-185","","","-52% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 5.1E_27);-52% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 4.5E_23);-52% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 4.5E_23);-52% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 4.5E_23);-52% similar to PDB:2AWN Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg) (E_value = 4.5E_23);","Residues 39 to 218 (E_value = 2e-57) place ANA_2104 in the ABC_tran family which is described as ABC transporter.","","transporter ATP binding protein (AF077856)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2105","2280339","2278324","2016","11.41","25.59","68060","ATGGCGCCGGGCGAGAAGACCCCAGGAGCCGACGCCGCCGCGCGAGCCGACGCCGGAGCCTCCCGGAACGCTGAGCCCGCCGGGACGCCCCGCCGGGCTCGGGCGGTGGCCGGGGGGCCGCGCTCGGCGGACAGCTCGGGAGGCGGTCCGGTCCGGCCCGACGCCGCGCGAGCCGGCGGGCCGGGTGCCGGCGGCCCCCGGCCCGGCTGGGGCGAGCGGGCCGGCTGGACCCTGGCCGTCGTCGGCCCGCTGGCCTTCCTGGCGGTCTTCTTCGCCTGGCCCGTGGCCACGCTCATGGGCCGCGGCCTCGCCCCCGACGGCGCCCTGGACCTGAGCGGCTTCGGCGAGGTCCTGGCCCGCGAGCGCACCTGGCGGATCCTCACCCAGACCCTCACCCAGGCGGTACTCGGCACCGCCGTGTGCGTGGCCCTCGGCATCCCCGGCGCCCTCGTCCTCTACCGGCGCGCCTTCCCCGGACGCGACCTGCTGCGCGGGGTGGTGACCGTGCCCTTCGTGCTGCCCAGTGTCGTCGTCGGCGTCGCCTTCCACGCCCTGGTCACCCGCGGCGGGCCCCTGGAGGCCCTGAACCTGGACGGGACCCTGACCGCGGTGGTGGCCGCGCTGGCCTTCTTCAACTACGGACTCGTGGTGCGCACCGTGGGCACCATGTGGTCGCGGCTCGACCCGCGCGCCGTGGAGGCCGCCCGGGCGCTGGGGGCCTCGCCGATGCGGGCCTTCGCCACCGTCACCCTGCCCGCGTTGGCCCCCGCCATCGCCTCGGCCGCCTCCCTGACCTTCCTGTTCTGTGCCACCGCCTACGGGGTGGTCCTCGTGCTCGGCGGGGTGGGGATCGGCACCATCGAGACCGAGATCTACCGGCTGACCACCCAGTACCTCGACCTGCGGGGCGCCGCCGTCCTGTCCGTGGTTCAGCTCGGCGTCATCGCCCTGGCCCTGTGGGTGGCCGAGCGGGCGCGCGCCGCCACCCAGACGCGCCTGCGCCTGCGCACCGAGGTGCCCGCCCCACGGCTGCGGGCCGCCGACACCCCCGCGCTCGTGGTCACCGCGGTCACGGTCGGGGGGCTGCTGGTGGCGCCGATCGCGGTGCTGGTGGTGCGCTCCCTGCAGCGCGACGGCGCCTGGACCCTGGCGAACTACACCGACTTGGGCTCGACCGGCGGGCGCAGCGCCCTGCTCGTGACCGTGTGGGAGGCGGCCGCCAACTCGGTGTCCGTGGCCGTGGCGGCCGCGGCCATCGCCCTGAGCCTGGGGGTGGCGGTGTGCCTGGTGGTCTCGCGCCGACCCCGCAGCCGGGCGTTGGCCCGGGTCATCACCGGGCTCGACGCCGCCTTCATGCTGCCGCTGGGCGTGTCCGCCGTGACGGTCGGCTTCGGCTTCCTCATCACCCTGGCGCGTCCGCCGCTGGCCCTGACCCGCTCCTGGTGGATCCTGCCGCTGGCGCAGGCCGTCGTGGCCGTGCCGCTCGTGGTGCGCACCCTGCTGCCGGCACTGCGCGCCATCGATCCGCGTCAGCGCGAGGCGGCCGCCGCCCTGGGGGCCGGGCCCGGCCGGGTGCTGGCGACCGTGGATGGGCCCCAGCTACTGCGCGCCGGCGGGCTGGCGGCCGGCTTCGCCCTGGCGACGTCGCTGGGGGAGTTCGGGGCGACGTCGTTCCTGGCTCGGCCCCAGGAGCCGACCCTGCCAGTGGTCGTCTACCGGCTCATCGGCAGCCCCGGCTCCCAGAACCAGGGGATGGCGCTGGCCGGGGGCGTGGTCCTGGCGGTGGGCAGCGCCGCCGTCATGCTCGGCTGCGAGTGGCTCCAGACCCGGTTCGGCTCCGGGCGGGGCGGGAGCGCGGGTACGACGACGAGGCCCGGTGGGGCGTCGGTGCATCGATCCGCCCCGCAGCGCGCAACCTCCGCGGATGCCGGCCAGCATGCGGCGGGCGCGACGGGCGGAAACAACGAGGCGGCCCGGTCGCGCGGGCCCAGGACGGACGGAGGCGAGCGGCCATGA","MAPGEKTPGADAAARADAGASRNAEPAGTPRRARAVAGGPRSADSSGGGPVRPDAARAGGPGAGGPRPGWGERAGWTLAVVGPLAFLAVFFAWPVATLMGRGLAPDGALDLSGFGEVLARERTWRILTQTLTQAVLGTAVCVALGIPGALVLYRRAFPGRDLLRGVVTVPFVLPSVVVGVAFHALVTRGGPLEALNLDGTLTAVVAALAFFNYGLVVRTVGTMWSRLDPRAVEAARALGASPMRAFATVTLPALAPAIASAASLTFLFCATAYGVVLVLGGVGIGTIETEIYRLTTQYLDLRGAAVLSVVQLGVIALALWVAERARAATQTRLRLRTEVPAPRLRAADTPALVVTAVTVGGLLVAPIAVLVVRSLQRDGAWTLANYTDLGSTGGRSALLVTVWEAAANSVSVAVAAAAIALSLGVAVCLVVSRRPRSRALARVITGLDAAFMLPLGVSAVTVGFGFLITLARPPLALTRSWWILPLAQAVVAVPLVVRTLLPALRAIDPRQREAAAALGAGPGRVLATVDGPQLLRAGGLAAGFALATSLGEFGATSFLARPQEPTLPVVVYRLIGSPGSQNQGMALAGGVVLAVGSAAVMLGCEWLQTRFGSGRGGSAGTTTRPGGASVHRSAPQRATSADAGQHAAGATGGNNEAARSRGPRTDGGERP$","ABC-type iron/thiamine transport system, permease component","Membrane, Extracellular","ABC transporter integral membrane protein","K02063 thiamine transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Kota J., Ljungdahl P.O. Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J. Cell Biol. 2005. 168(1):79-88. PMID: 15623581","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[127-331]T$ $\"[406-613]T$	BPD_transp_1
PS50928	$\"[127-323]T$ $\"[406-604]T$	ABC_TM1

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[194-359]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[76-96]?$ $\"[134-152]?$ $\"[167-187]?$ $\"[197-217]?$ $\"[253-287]?$ $\"[301-321]?$ $\"[352-372]?$ $\"[410-430]?$ $\"[451-471]?$ $\"[481-501]?$ $\"[540-560]?$ $\"[584-604]?$	transmembrane_regions

","BeTs to 6 clades of COG1178COG name: ABC-type iron/thiamine transport systems, permease componentsFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1178 is -o--kz---d--bcefgh-nuj--t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 127 to 331 (E_value = 1.4e-08) place ANA_2105 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.Residues 406 to 613 (E_value = 0.0044) place ANA_2105 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","transporter integral membrane protein (III)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2107","2281337","2280339","999","5.19","-8.13","35079","CTGGCCGCCTGCGGCAAGGGCAAGAAGGCCGGCTCCCAGGCCGACTCCAAGACCGTCACCGTCGTCACCCACGACTCCTTCCACGTCTCGGAGAACCTCCAGAAGGCCTTCACCTCCGAGACCGGCTACACCCTCAAGGTCGCCACCTCCGGGGACGCCGGCGCCCTGGTCAACAAGCTCGTCCTGACCAAGGACGCGCCCCTGGGCGACGCCGTCTTCGGCATCGACAACACCTACGCCACCCGCGCCCTCGACCAGGGCGTTATCGACACCTCCGCCACCGTCACCCTGCCCAAGGGCGCCGAGAGCTACGTCGTCGCCGACACCCCGGCCCTGGCGCCCATCGACGTCGGTGACGTCTGCCTCAACATCGACACCGGCTACTTCACCGGCAAGGGCCTGACGCCCCCCGCCACCTTCGAGGACCTGACCAAGCCCGAGTACAAGGGCCTGTTCGTGGCCATCAACCCCACGAACTCCTCACCCGGCATGGCCTGGCTGCTGGCCACCATCGGCCACTTCGGCGCCGGCTCCTTCGCCGACTACTGGAAGCAGCTCATGGCCAACGGCGCCCGGATCGCCGAGGACTGGAGCGCCGCCTATGAGACCGACTTCTCCGGCAGCGGCAAGGGCACCTACCCCATCGTCGTGTCCTACGCCTCCTCGCCCTCCTTCACGGTCTCCAAGGACAAGAGCTCCAGCTCCACCTCCGCCCTGCTGGACACCGCCTTCCGCCAGGTCGAGTACGCCGGCGTCCTCAAGGGCGCCGCCAACCCCGAGGGCGGCAAGGCCTTCGTGGAGTGGATGCTCTCCAAGGCCGTCCAGGAGGACATTCCCGGCCAGATGTACATGTACCCGGTCCTGCCCGACGCCGCCCTGCCCGAGGCCCTCACCAAGTTCGGCCAACTGTCGAAGTCGCCGGTGAAGGTCGACCCCAAGGAGATCACCACCCACCGCGAGGAGTGGCTGAACACCTGGACCGAGGCCGTCGGCAAGTGA","LAACGKGKKAGSQADSKTVTVVTHDSFHVSENLQKAFTSETGYTLKVATSGDAGALVNKLVLTKDAPLGDAVFGIDNTYATRALDQGVIDTSATVTLPKGAESYVVADTPALAPIDVGDVCLNIDTGYFTGKGLTPPATFEDLTKPEYKGLFVAINPTNSSPGMAWLLATIGHFGAGSFADYWKQLMANGARIAEDWSAAYETDFSGSGKGTYPIVVSYASSPSFTVSKDKSSSSTSALLDTAFRQVEYAGVLKGAANPEGGKAFVEWMLSKAVQEDIPGQMYMYPVLPDAALPEALTKFGQLSKSPVKVDPKEITTHREEWLNTWTEAVGK$","ABC-type iron/thiamine transport system, periplasmic component","Extracellular, Periplasm","ABC transporter, periplasmic substrate-bindingprotein, solute-binding family 1","K02064 thiamine transport system substrate-binding protein","ABC transporter, periplasmic binding protein, thiB subfamily","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR005948
Family

Thiamine ABC transporter periplasmic binding protein
TIGR01254	$\"[16-326]T$	sfuA: ABC transporter periplasmic binding p

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[1-276]T$	SBP_bac_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[18-297]T$	no description
tmhmm	$\"[165-183]?$	transmembrane_regions

","BeTs to 12 clades of COG1840COG name: Thiamine-binding periplasmic proteinsFunctional Class: HThe phylogenetic pattern of COG1840 is ---k---Ce--H-----l---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 312 (E_value = 3.2e-10) place ANA_2107 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","transporter, periplasmic substrate-binding protein, solute-binding family 1 (AE005183)","","1","","","Wed Aug 8 10:33:15 2007","","Wed Aug 8 10:33:15 2007","","","Wed Aug 8 10:33:15 2007","Wed Aug 8 10:33:15 2007","Wed Aug 8 10:33:15 2007","","","Wed Aug 8 10:33:15 2007","","","Wed Aug 8 10:33:15 2007","","","","Wed Aug 8 10:33:15 2007","Wed Aug 8 10:33:15 2007","","","","","yes","","" "ANA_2108","2281254","2281760","507","11.57","11.53","16701","GTGGAAGGAGTCGTGGGTGACGACGGTGACGGTCTTGGAGTCGGCCTGGGAGCCGGCCTTCTTGCCCTTGCCGCAGGCGGCCAGGCTCAGGCCGACGGCGCCGGCGGCGGTTCCGGCGATCAGGGCGCGGCGGCTGAGGGCCGGGCGGGGTCGGCCGGGCCGGCCCGAGCGGGGGTTGGACTGGATGCTCATGTGTGCCTCCTGGATGGTTCTCCGGAGGGCCCGGCGACCACCTGCGGCGCGCCGGGGAGATGGTCTCGACTTCCTTCGCCGGTACTAACCGGAGCAGGTTCGAGGGTCTGCGGGTTTCCGCACTCTCAGCGCCGTCGGAGGCGGCCCGTCGGCCAGTGGCGGCCGGGCCGACGACGGGGCGCTCCCCTGTCGTTGCAGGTCAACTGTAGTTCGAGGGCACCCGCCGACACCAACTCCATCCGGCCCGCGCCGCGCGCCCGAGCCCTGCCACGGCCCCGCGCGTTCGCCTCCCCGCGCCATCGCCTTTCCGCGTGA","VEGVVGDDGDGLGVGLGAGLLALAAGGQAQADGAGGGSGDQGAAAEGRAGSAGPARAGVGLDAHVCLLDGSPEGPATTCGAPGRWSRLPSPVLTGAGSRVCGFPHSQRRRRRPVGQWRPGRRRGAPLSLQVNCSSRAPADTNSIRPAPRARALPRPRAFASPRHRLSA$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide

InterPro
IPR001584
Domain

Integrase, catalytic core
PF00665	$\"[140-304]T$	rve
PS50994	$\"[128-307]T$	INTEGRASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[143-310]T$	no description

","BeTs to 5 clades of COG1425COG name: Predicted transposaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1425 is a--p-----dr---efgh-n-j----Number of proteins in this genome belonging to this COG is 7","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 140 to 304 (E_value = 6.4e-21) place ANA_2109 in the rve family which is described as Integrase core domain.","","transposase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2110","2283503","2284642","1140","10.71","17.72","40893","ATGCCGGGAAGGCCCCGCCTTCCCCACATCCAGGACAAACCCACCCCCTGCACCACGAGAGGAAACCACCCCATGAGCACCCCCTGGTTCCTCCCCGCTCCGCTGGTCGACGTCGCCGCCCTGGCGCTGTGGTGGGGGCTCCTCAGGCTCTCGCGGCGCCGCGACAACCGCCGGCTTCGCAACGGACTCCTGTTCCTGCTCCTGGTCGGCACCACGGTCAGAGCACTGCACCACCTGGCCCCCCTCATCCCCGCCCTCAAGCTCCCGGTGGGACTGGGCAGTGTCGCCTTCTTCCTGCTCATCGCCCTCATGCCGTTCCTGCTCATGTTCAACGGCGTCGTCCTCATCCGCCGCGAGGGCCGGCGCCTGAGCAACCTGCTGTGCCTGGCGGCCGGCCTGGGACTCATCGCCACACCGATGGCCGCCGTCGCCCTTGTGGCCACCGGCAGCCCCTGGACCCTGCTGGTCGCCGCGCTCATGTTCTGCGCCTGCGCCTACCTGGGCGTCTTCCTCCTCATCTTCTTGGGCCAGACGGCGGTGCAGCGGATCTGGGGCGGACGCCGAGCCATGCCGCACCCCGACGTCGTCGTGGTCCATGGCGCCGGCCTCATCAACGGGAAGGTCGGGCCGCTGCTGGGCTCGCGGATCGCCGGAGGCATCGATGCCTGGCGCGACGAGGAGGGCCTGCGCCCCGGAGTGCCGCTGCTGGTCATGAGCGGCGGGCAGGGCGCCGACGAGCCGACCAGCGAGGCGCGCGCCATGGCCGACTACGCGATCGCCCGTGGCGTCCCGCCTGAGCGGATCCTCCTGGAGGACCGTTCGACGACGACTCGCACGAACATCTCCTACACGCGCGACCTGTTGGCTGAGCGAGGCATGGTCGATCCGCAGGTGCTGCTGGTGACGAGCTCCTTCCACGCGGTGCGCACCGCGATCCTGGCCTCCGACATGGGGGTGCCGTGGGCGGTCGCGCCGGCGCGCACGGCCTGGTTCTACATCGTCAACGCCTGGCTGCGTGAGTACGTCGCCGTGCTGACCTACCGGCGCCGCCCAGCCTTGGCCTGCGCCGCCGTTGCCGGGGTCTTCGCCGTGCTGTACGCGCTGCTGGTCCTCGGCGCGCAGACGGGGCATATCGGCTGA","MPGRPRLPHIQDKPTPCTTRGNHPMSTPWFLPAPLVDVAALALWWGLLRLSRRRDNRRLRNGLLFLLLVGTTVRALHHLAPLIPALKLPVGLGSVAFFLLIALMPFLLMFNGVVLIRREGRRLSNLLCLAAGLGLIATPMAAVALVATGSPWTLLVAALMFCACAYLGVFLLIFLGQTAVQRIWGGRRAMPHPDVVVVHGAGLINGKVGPLLGSRIAGGIDAWRDEEGLRPGVPLLVMSGGQGADEPTSEARAMADYAIARGVPPERILLEDRSTTTRTNISYTRDLLAERGMVDPQVLLVTSSFHAVRTAILASDMGVPWAVAPARTAWFYIVNAWLREYVAVLTYRRRPALACAAVAGVFAVLYALLVLGAQTGHIG$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","protein of unknown function DUF218","","","","","

InterPro
IPR003848
Domain

Protein of unknown function DUF218
PF02698	$\"[192-344]T$	DUF218

noIPR
unintegrated

unintegrated
signalp	$\"[1-75]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[63-81]?$ $\"[95-115]?$ $\"[125-147]?$ $\"[153-175]?$ $\"[353-373]?$	transmembrane_regions

","BeTs to 8 clades of COG1434COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1434 is -------qvd-l-cefghsn-jx---Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 192 to 344 (E_value = 3.8e-43) place ANA_2110 in the DUF218 family which is described as DUF218 domain.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2112","2284721","2285170","450","5.58","-1.12","15108","ATGGGACGACGACGTACCTTCATCGAGAGCGAGGTCATCGGCTCCGCCACGGCGGTCTTCGCCGAGCGCGGTTTCGCGGGAGCCTCTGTGGACGATCTGGTTCGAGCCACCGGCGTCAATCGCGCCAGCCTCTACGGGGTCTTCGGCTCCAAGGACGGGCTCTTCCAGCGCTGCCTCACTGAGACGCTGGCCGCTCTGAGTCCGACGGCCGCCCCCGGGGATTCCACCGGCGTCGCAAGGGCGGGATGCGGGGAGCTCGACCTGGTCCTCGTGGCGCTCATGGAGATCGCCCCTGGGGACCCGGCCGTGCGCGAGGCCCTCGAGGTCGCCTTGAACCGGGCGGGCATCACCGCCGAGGCGCTGGGCCGACGCCTGCTGGAGCGGGCCGGCATTGCGACGTCGAGCTCGGCCACAGCGACCGGAAAGACATCAGCCTCACCGCCGACGTAA","MGRRRTFIESEVIGSATAVFAERGFAGASVDDLVRATGVNRASLYGVFGSKDGLFQRCLTETLAALSPTAAPGDSTGVARAGCGELDLVLVALMEIAPGDPAVREALEVALNRAGITAEALGRRLLERAGIATSSSATATGKTSASPPT$","Transcriptional regulator, TetR family","Membrane, Cytoplasm","putative membrane protein","putative transcriptional regulator","regulatory protein, TetR","","Mueckler M., Caruso C., Baldwin S.A., Panico M., Blench I., Morris H.R., Allard W.J., Lienhard G.E., Lodish H.F. Sequence and structure of a human glucose transporter. Science 1985. 229(4717):941-945. PMID: 3839598Maiden M.C., Davis E.O., Baldwin S.A., Moore D.C., Henderson P.J. Mammalian and bacterial sugar transport proteins are homologous. Nature 1987. 325(6105):641-643. PMID: 3543693Kayano T., Fukumoto H., Eddy R.L., Fan Y.S., Byers M.G., Shows T.B., Bell G.I. Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues. J. Biol. Chem. 1988. 263(30):15245-15248. PMID: 3170580","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[12-25]T$ $\"[33-56]T$	HTHTETR
PF00440	$\"[12-58]T$	TetR_N
PS50977	$\"[6-66]T$	HTH_TETR_2

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[114-130]?$	SUGAR_TRANSPORT_1

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[3-58]T$	no description

","No hits to the COGs database.","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 7.9e-15. IPB001647 12-54***** IPB013573 (Tetracycline transcriptional regulator YcdC-like, C-terminal) with a combined E-value of 4.4e-06. IPB013573B 33-74","","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 58 (E_value = 1.6e-13) place ANA_2112 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2113","2285252","2285617","366","6.52","-1.62","13284","ATGAGTCGCAACACCGTCACCATCACCGACACCACCTTGAGCGTTGAGCCGCACGGGCTGGACAAGATGTGGTCCTACACCTCCCGGCTGGAGTTCCCGCTGACGCACGTACGCGGCGCCACGCACGACCCCGGCCTGCGCCACGAACCCAAGGGCTGGCGCGGGCCCGGCCTGCAGGCCGGCAGCAAGCTCTCCGGGACCTTCCACGCCGACGGCACCGCGCAGTTCTGGAACATCTCCGGTTACGAGAACACCCTGGTCGTCACCCTGGAGGACGAGCGCTTCACGCACCTCTACCTCACGGTCGACGACCCGGCAGCCTTGGCCGCACAGATCAACGCCGCCATCCGTCCCGCCCAGGCCTGA","MSRNTVTITDTTLSVEPHGLDKMWSYTSRLEFPLTHVRGATHDPGLRHEPKGWRGPGLQAGSKLSGTFHADGTAQFWNISGYENTLVVTLEDERFTHLYLTVDDPAALAAQINAAIRPAQA$","Hypothetical protein","Periplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2114","2287114","2286527","588","6.88","-0.45","19587","GTGTGCGGAGGTCCCTCGCGAACGGTGCTCGGGCGGGAAAAGTCGCCAATCGTGACACGGGACCGCAAAAAAGCGTGCCGACCCCGCACTGGGGCCGGCACTGAGTCCTCAGGCGCTGATGGCGCGCTGCGCGTAGGGGGAGTCGGGGCGGCGGGCGCTGTACCACTTGGCGGCCTGGCGCAGTCCGAGCTCACGCACCAGGGTGACGGTGGCCCCGGAGATGATGGCGAAGGTGACGATCTCGGCCAGCTTGTAGTTGAGGACCTGGTCCTCCTCGCGCGGGGCGGGTTTGCCGGAGATGGCTCGCCAGCCGAGCGCCACGACCTTCTCGGCCACGAACCCGGAGGCGAGCGTGGCCACGGCCGCGGTCGCCTTCCACATGAAGTCGGTGGTCTGGTCGATCTGGGCGGGGTCCTGGTCGCTCATGAGTCCTCCTTGCGCCCGGGTCGGGCGGCGTCGTGGGTACCTGCGTGCTGGCGGCGGACCGATGGTGTCGGCCCGTTCCGCCCCGATCATGCCGTACCTGGGCCGACGGCGCAGCCAGTGCCCGCCCGCGTGGCGCCAACTGCCGGGCCCGCGTGGTCGTAG","VCGGPSRTVLGREKSPIVTRDRKKACRPRTGAGTESSGADGALRVGGVGAAGAVPLGGLAQSELTHQGDGGPGDDGEGDDLGQLVVEDLVLLARGGFAGDGSPAERHDLLGHEPGGERGHGRGRLPHEVGGLVDLGGVLVAHESSLRPGRAASWVPACWRRTDGVGPFRPDHAVPGPTAQPVPARVAPTAGPAWS$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2115","2287391","2289982","2592","5.91","-13.21","91082","ATGAGTGCCGTGCAGATCGCCTGTGTCGTCATCGTCGTCATTGCCACGACGATCGGTATCGCAGTTTTCGCACGCGCCTGTTGCACTATTGGCGCCCGCATGGCCGTGGGCCGCGCAACCGCGCCGGAGCGCCTGCGCCCGGTCGGCCGGCGCCTGGCGCTCACACTGGGGGCGCTCGTGGGCCACACCGCTTTCAAGGGCCGCCCCTTCGTCAAGGCCGCCCACTGGCTGGTCATGGTCTCCTTCCCGCTGCTGTTCCTCACGCTCGTGGCCGGATACGGGCAGGTGCTGGGCGGGCCCGACTTCGCGCTGCCGCTCATCGGGCACGCCGCCTGGTGGGCCTGGGTCGTCGAGATCATCGGCTGGCTGTCCGCTTTCGGGATCGTGGGTCTGACGATCCTACGCTGGCGCCTGACCCGGGCCGGCCGGGCCACCCCGCCCTACGCCCCGGACTCCGACGGCGGTAAGCGTCCACGCACCTCGCGCTTCGCCGGCTCGTCGTCGGCCCAGGCGAAGTTCGTCGAGGCCACCATCATCGGCGTGGTCGCCTGCGTGCTGGCGCTGCGGATGCTGGAGCACGCCCACCTGGCCGCCTCCCCCGACCCGGCGCAGCGGGCCCTGGCCTCCTGGACGCACTTCCCCCTGACGGCCTGGACCGGCCCGCTGCTCACTCCCCTGAGCGCCGGCGCCCTGGCCAACGCGATTCTCGTCGTCGCCACCATCAAGGTGGTGCTGTCGATGACCTGGTTCGTCGTCGTAGGCCTGCAGCCCTCGATGGGCGTGGCCTGGCACCGGTTCCTGGCGATCCTCAACGTCTACGCGCGCCGCGAGGTGGACGGCTCCAAGGCGCTGGGCCCGCTTCAGCCGCTCATGGTCGGCGACGAGCCCCTGACAGAAGCCACCATGGACACGCTGGAGGAGGCCATGGAGGCCGCCGACTCCGGCGAGGGCCCCGAGGTGCGCCTGGGCGTGGGCCGCATCGAGGACTTCACCTGGAAGGGCCTGCTGGACTTCTCCACCTGCACCGAGTGCGGTCGCTGCCAGGACCTGTGCCCGGCGTGGAACACCGGCAAGCCCCTGTCCCCCAAACTGTTCGTCATGGCGCTGCGCGATCACCACGCGGCGGCCGCCCCCTACCTGCGGGCCGCGACCGCCCTGGGGGTCGAGCCCGACGACGTCACCGAGGAGATGGTGGCCTCCCGCCCCACCTCCGGTGGGCTGGTCGGCAAGGCGCTGGGCATGCACGATGGTCTGGCACGCGAGACCAACCTGGGCCTGGAGCCGGGCACCGCCCACACCGGCGACGTGCTCGGCGCGCTGCTGGCGGCCAAGGCGGCCCCCACCGAGACGGGTGTGGCCACACGGCCGGCGCCCCTGGCCGGGGAGGTCATCCCCGCCGACGTCCTGTGGGCCTGCACCACCTGCGGGGCCTGCGTGGACCAGTGCCCGGTGGACATCGAGCACGTCGACCACGTCGTCGATGTGCGCCGCCAGCAGGTGCTCATGGAGTCGGCCTTCCCCAAGGAGCTCGGCGGCATGTTCCGCAAGATGGAGTCCAAGGGGAACCCGTGGGGGCTGCCGGCGCGCAAGCGCCTGGACTGGGCCAAGAACCTGGACTTCGAGGTGCCGGTCATCGGCGACGACGTCGAGAGCGCCGCGGACGTCGACTACCTGTTCTGGGTGGGTTGCGCGGGCGCCTACGAGGACCGCGCCAAGAAGACGACGCGGGCGGTGGCCGAGCTGCTGCACACCGCGGGGGTGAGCTTCGCGGTCCTCGGCGACGCCGAGACCTGCACCGGCGACCCGGCCCGCCGCGCCGGCAACGAGATCCTCTACCAGATGCTTGCCGCGCAGAACGTGGAGACCCTGGGCGAGGTCGAGGCGCAGCGGATCGTGGTGACCTGCGCGCACTGCTTCAACACGATCTCGCGGGAGTACCCGCAGATCGGGGGCCGCTACGAGGTCGTCCACTACACCCAGCTGCTCAACCGGCTCGTGCGCGAGGGCCGGCTGCGTCCGGCGCCGCCGCAGGCCGCGGGTGGTTCGACGGCGCCCGACGCCCCAGCGGCCTCCGCCGCCCTGGCCACGCCGGCACCCGCCACCGGGCAGGACGGCGACTCACGGGCCGGTGATGCCCCGACGTCGAGCACCGAGGCCGCCGAGCCGCAGGCCGAGGCCCCGGCGGCGCCGTCGGGCGAAGAGGAAGCCGGTAAAGCGGCGGGCGAGCCGGTCATCCCGACGGTCACCTACCACGACGCCTGCTACCTGGGCCGCCACAACCAGGTCTACTCCCCGCCGCGCGAGCTGCTGGAGGCGACCGGCGCGACCACGGTGGAGATGCCGCGCAGCCGCGAGCGGGGATTCTGCTGCGGCGGCGGCGGGGCGCGCGCCTTCATGGAGGAGACCATCGGGACGCGCATCGCCGTGGAGCGCTCGCGCGAGGCCATCGGCACCGGCGCGCAGGTCATCGCCACGGCCTGCCCCTTCTGCACCACGATGCTCTCCGACGGCGTCGCCTCCGAGGGCGCCGACGTGCGGGTCACGGACGTGGCCACCCTCATGCTGGAGGCTGTGCGCCGCGGCGGGGAGTAG","MSAVQIACVVIVVIATTIGIAVFARACCTIGARMAVGRATAPERLRPVGRRLALTLGALVGHTAFKGRPFVKAAHWLVMVSFPLLFLTLVAGYGQVLGGPDFALPLIGHAAWWAWVVEIIGWLSAFGIVGLTILRWRLTRAGRATPPYAPDSDGGKRPRTSRFAGSSSAQAKFVEATIIGVVACVLALRMLEHAHLAASPDPAQRALASWTHFPLTAWTGPLLTPLSAGALANAILVVATIKVVLSMTWFVVVGLQPSMGVAWHRFLAILNVYARREVDGSKALGPLQPLMVGDEPLTEATMDTLEEAMEAADSGEGPEVRLGVGRIEDFTWKGLLDFSTCTECGRCQDLCPAWNTGKPLSPKLFVMALRDHHAAAAPYLRAATALGVEPDDVTEEMVASRPTSGGLVGKALGMHDGLARETNLGLEPGTAHTGDVLGALLAAKAAPTETGVATRPAPLAGEVIPADVLWACTTCGACVDQCPVDIEHVDHVVDVRRQQVLMESAFPKELGGMFRKMESKGNPWGLPARKRLDWAKNLDFEVPVIGDDVESAADVDYLFWVGCAGAYEDRAKKTTRAVAELLHTAGVSFAVLGDAETCTGDPARRAGNEILYQMLAAQNVETLGEVEAQRIVVTCAHCFNTISREYPQIGGRYEVVHYTQLLNRLVREGRLRPAPPQAAGGSTAPDAPAASAALATPAPATGQDGDSRAGDAPTSSTEAAEPQAEAPAAPSGEEEAGKAAGEPVIPTVTYHDACYLGRHNQVYSPPRELLEATGATTVEMPRSRERGFCCGGGGARAFMEETIGTRIAVERSREAIGTGAQVIATACPFCTTMLSDGVASEGADVRVTDVATLMLEAVRRGGE$","Iron-sulphur-binding reductase","Membrane, Cytoplasm, Extracellular","ferredoxin, 4Fe-4S","protein of unknown function DUF224; cysteine-rich region","protein of unknown function DUF224, cysteine-rich region domain protein","","Pellicer M.T., Badia J., Aguilar J., Baldoma L. glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein. J. Bacteriol. 1996. 178(7):2051-2059. PMID: 8606183","","","

InterPro
IPR001450
Domain

4Fe-4S ferredoxin, iron-sulfur binding
PF00037	$\"[466-488]T$	Fer4
PS00198	$\"[341-352]?$ $\"[472-483]?$	4FE4S_FERREDOXIN

InterPro
IPR004017
Domain

Cysteine-rich region, CCG
PF02754	$\"[582-643]T$ $\"[770-835]T$	CCG

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[73-93]?$ $\"[112-134]?$ $\"[231-253]?$	transmembrane_regions

","BeTs to 14 clades of COG0247COG name: Fe-S oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0247 is aomp-z-q-drlbcefgh-nuj----Number of proteins in this genome belonging to this COG is 2","***** IPB004017 (Protein of unknown function DUF224) with a combined E-value of 1.8e-08. IPB004017A 341-358 IPB004017C 787-797","","","No significant hits to the PDB database (E-value < E-10).","Residues 466 to 488 (E_value = 0.0075) place ANA_2115 in the Fer4 family which is described as 4Fe-4S binding domain.Residues 582 to 643 (E_value = 4.4e-13) place ANA_2115 in the CCG family which is described as Cysteine-rich domain.Residues 770 to 835 (E_value = 2.7e-20) place ANA_2115 in the CCG family which is described as Cysteine-rich domain.","","4Fe-4S ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2116","2291796","2290207","1590","6.16","-4.41","57330","ATGGTGGGAATTGTCCTGCCCGGCGAGCGGTGCTTGGTCCGCTGGCTGTCTGCTGGCTGTCCGCGTGCGGGGCCGTTTCGCGCGGCCGGTGACATTTCTCTGCGGCCGGGTGCGGTTCGCGCGTTTGGGGACAGGAAGCCGGTCCCCGCACGCGCAGGATGTCCCCGGCTGCGCGGACATGTCACCGTCAGGCCCTACGCTCGAGGCATGGCTCGCCGTACGCCCGAACCGGAATCACCCTCACTGTTCGACGCCGCCGGCCCCGACGGCTCCGGCCTCGTCGACGACCCGGCCCGCCCGCTGGCCGATCGGCTGCGCCCGCGGGTGCTCGACGACGTCGTCGGCCAGGACCAGCTGCTCGCCGACGACGCCCCGCTGGGCCGCATGGTCGCCTCCGGCCGTTTGTCATCGATCATCCTGTGGGGCCCGCCGGGCTGCGGCAAGACGACGATCGCTCGGCTCCTGGCCGACCGCACCGGCCTGGTCTTCGAGCAGGTCTCGGCGACCTTCTCCGGGGTGGCCGACCTGCGCAAGGTCTTCGCCGCAGCGGCCCGCCGCCGCGAGATCGGGCAGGGAACGCTCCTGTTCGTCGACGAGATCCACCGCTTCAACCGGGCCCAGCAGGACTCCTTCCTGCCCTACGTCGAGGACGGGACGGTTGTCCTGGTCGGCGCGACCACCGAGAACCCGAGCTTCGAGCTCAACGGCGCCCTCCTGTCACGCTGCCAGGTCATGGTCCTGCGCCGCCTGGATGAGGCCGCCCTGACCGAGCTGCTGGCGCGCGCCGAGTCCCTGATGGGTCGCAGCCTCGCTCTGACTGAGGATGCCCGCACCGCCCTGCTGTCCATGGCCGACGGCGATGGCCGCTACCTGCTGGGCATGGTCGAGCAGGTCCTCGCCGCCCAGGACGCAGACGGCCCGGAACCACTTGACGTTGAAGGGCTGCGCAGCGTCATCGCCTCCCGGGCACCCCTGTACGACAAGTCCCATGAGGAGCACTACAACCTCATCTCCGCCCTGCACAAGTCGATGCGCGGCTCCGATCCGGACGCCGCCCTGTACTGGCTGACCCGAATGCTAGGTGGGGGCGAGGATCCGCTCTACGTGGCGCGCCGTCTGGTGCGATTCGCCAGCGAGGACGTCGGCATGGCCGACCCGGCCGCCCTTCAGATGACGCTGGCGGCCTGGGACGCCTACGAGCGCCTGGGATCGCCCGAGGGCGAGCTCGCCATCGCGCAGGCGGTCGTCTACCTGGCCACCGCGCCCAAGTCAATCGCTGTCTACCGCGGCTACGGCCGCGCGGTGCGCCTGGCCCGACAGACCGGCTCGCTCATGCCGCCGGCCCACATCCTCAACGCCCCCACCCGACTCATGAAGGAGCTCGGCTACGGCGAGGGCTACGAGTACGACCCGGACACGACCGACGGCTTCTCTGGTGCGGACTACCTGCCCGACGGCGTCGAGCGCCGGCCTCTCTACGAGCCCACCGCCAACGGCCACGAGCGCCGTATCCGTGAGCGGCTGGAGTACTGGGAGGGTCTGCGGGCGCGCAAACGTGGCGAGGACGTCGGTGAGGGAGGCGCCGGCTAA","MVGIVLPGERCLVRWLSAGCPRAGPFRAAGDISLRPGAVRAFGDRKPVPARAGCPRLRGHVTVRPYARGMARRTPEPESPSLFDAAGPDGSGLVDDPARPLADRLRPRVLDDVVGQDQLLADDAPLGRMVASGRLSSIILWGPPGCGKTTIARLLADRTGLVFEQVSATFSGVADLRKVFAAAARRREIGQGTLLFVDEIHRFNRAQQDSFLPYVEDGTVVLVGATTENPSFELNGALLSRCQVMVLRRLDEAALTELLARAESLMGRSLALTEDARTALLSMADGDGRYLLGMVEQVLAAQDADGPEPLDVEGLRSVIASRAPLYDKSHEEHYNLISALHKSMRGSDPDAALYWLTRMLGGGEDPLYVARRLVRFASEDVGMADPAALQMTLAAWDAYERLGSPEGELAIAQAVVYLATAPKSIAVYRGYGRAVRLARQTGSLMPPAHILNAPTRLMKELGYGEGYEYDPDTTDGFSGADYLPDGVERRPLYEPTANGHERRIRERLEYWEGLRARKRGEDVGEGGAG$","ATPase, AAA family","Cytoplasm","ATPase, AAA family","K07478 putative ATPase","AAA ATPase, central domain protein","","","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[134-250]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[137-285]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[87-250]T$	no description
PTHR13779	$\"[109-520]T$	HOLLIDAY JUNCTION DNA HELICASE RUVB-RELATED
PTHR13779:SF1	$\"[109-520]T$	WERNER HELICASE INTERACTING PROTEIN

","BeTs to 14 clades of COG2256COG name: Uncharacterized ATPase related to the helicase subunit of the Holliday junction resolvaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2256 is ------y-vdrlb-efghsnuj---wNumber of proteins in this genome belonging to this COG is 3","***** IPB006642 (Zn-finger Rad18) with a combined E-value of 8.4e-15. IPB006642A 234-246 IPB006642B 400-440 IPB006642C 440-487","","","No significant hits to the PDB database (E-value < E-10).","Residues 110 to 255 (E_value = 0.00044) place ANA_2116 in the Mg_chelatase family which is described as Magnesium chelatase, subunit ChlI.Residues 137 to 304 (E_value = 1.1e-14) place ANA_2116 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).Residues 137 to 250 (E_value = 6.2e-05) place ANA_2116 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).Residues 144 to 163 (E_value = 2.5e-05) place ANA_2116 in the SKI family which is described as Shikimate kinase.","","AAA family (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2117","2292077","2294863","2787","5.15","-37.32","98880","ATGGACCGCGAGGTCGTCGTCACCGACGCCGGTCACCCCCTTCTCGGCTCCGGCCTCGCCCTGCGTCTCATCACCGCGCCCGACGGCGGCGCCGCAGCCATCCACGGCCAGATCCTGGGCGCGGACGGCATGCCCGCCCCGACGGTCACGCCGCTGCGCATCGTCGGGAACCTTCCCGACGAGGTCCTCGCCGCGCACCCCCACCTGGAGGGCTACATCGCCCTGAGCGCGACCGACGCCGCCGGCACCCCCCTGCTCGACGACGCTGCCGTCGCCTCCGCCCTGACCGGCCAGGTCGCCATCGCCCAGTACGTCGGACTCCCGGACCCCACCGAGGCCGCCGACGTCAGCGACGCCCACCTCGACGCCTTCACCGGGGTGCAGACCGCCATCCTCCTGGACCACCTCTACGCCGAGGCCGCCACCCGCGCCGAGCTGGGCGTCACCTTCACCGGCGGCCTGCCCTCCTTCGCCCTGTGGGCGCCCAGCGCGCAGGCCGTCACCCTCCTGACCTGGGAGACCAGCGACCCGCTGGGCTCGGTGCCGGAGGTCCCCGGCCCACCGCGACGCACCCCGGCCGTCCGCAAAGGCGACGGCCGCTGGGTCGTCACCAACCACCCCGACCAGCCGGCCGGCGCCACCTTGAGCACCCCCAGCGGCGAGCCCGGCCCGAGCGCCCCCGGCGCCCCCATCACTGCCGGCTGCCAGTACCTGTGGGAAGTGCGGGTCTACGTGCCCTCCACTCGGCGCGTGGAGACCAACGTCGTCACCGACCCCTACTCGACGACGCTGACAACGGACTCGACCCGCTCAGTTGCCGTCGACCTGGCCGATCCGCGCCTGGCCCCCGAGCAGTGGGCCACCACCCGGGCTCCGGCGGTCCGCAACGACTCGGCCCGCAGCATCTACGAGCTCCACCTGCGGGACTTCTCCGCCGCCGACGACACCGTCCCGCCCGAGCTGCGCGGCACCTACCGGGCCTTCACGGTGGCCGGCTCAGCGGGCGTGCGCCACCTGGCCGAGCTGGCCCGGGCCGGCATGAACACGATCCACCTGCTGCCCACCTTCGACATCGCCACCATCCCCGAGCACCGCGGCTCCCAGCGCCACCCCGACATCCCCGACGGCGCGCACCCGGCCTCGGCCGACCAGCAGGCGGCCATCGCGGAGGTGGCCGACCACGACGCCTACAACTGGGGCTACGACCCGCTCCACTGGGGCGCCCCCGAGGGCTCCTACGCGACCGAGGGCCACCAGGACGGCGGGGCGCGCGTCGTCGAGTTCCGCGAGATGGTGGGGGCCCTGCACGACCTGGGCCTCCAGGTGGTCCTCGACCAGGTCTACAACCACACGGCCGCCTGCGGGCAGGACCCGCGCAGCGTCCTGGACCAGGTGGTGCCGGGCTACTACCACCGTCTCGACGCCGTCGGGCGGGTGACGAGCTCGACCTGCTGCGCCAACACGGCCACGGAGAACGCCCTGTGCGCGCGCCTCATGATCGACTCGGTGGTGCGCTGGGCGCGCTGGTACCGGGTCGACGGCTTCCGCTTCGACCTCATGGGCCACCACCCGCGAGCCGTCATGGAGCGCGTGCGGACGGCCCTGGACGAGCTGACGCTGGAGGCCGACGGCGTCGACGGCCGCTCCATCTACCTGTACGGGGAGGGCTGGAACTTCGGGGAGGTCGCGGGCAACGCCCTGTTCGTGCAGGCCACCCAGGGTCAGCTCGACGGCACCGGGATCGGTGCCTTCAACGACCGTCTGCGTGACGCCGTCCACGGCGGGGGCGCCTTCGACCCCGACCACCGCGTCTTCCAGGGCTTCGGCACCGGCCTGCTCACGCAGCCCAGCGGCCTGGACCATCGAGGCTGGAACGACCAGTCGGCGGACCTGGCCCACCGCACCGACCTGGTGCGCCTAGGTCTGGCGGGCAACCTCAAGGACTATGTCATGACGATCTCGGACGGGTCGGTGCGCCGTGGCATCGACCTCATCCACAACGGGGCGCCGGCGGCCTTCGCCTCCCACCCCCAGGAGAACGTCAACTACGTCGACGCCCACGACAACGAGACGCTCTACGACCTGCTGGCCTACAAGCTGCCCCAGGGCATGCCGGTGGCCGAGCGGGTGCGCATGAACACCGTGTGCCTGGCCACGGTGGCGCTGGCGCAGTCGCCGGCCTTCTGGAGCGCGGGCACCGAACTGCTGCGCAGCAAATCCCTGGACCGGGACTCCTACAACTCGGGGGACTGGTTCAACGCCATTGACTTCACGGGGCAGTCCAACGGTTTCGGGCGGGGTCTGCCGCCGGCCAGCCGCAACGAGGGCTCCTGGGCGATCCAGGGGCCACTGCTGCAGGACGACTGGCTGCGGCCCTCGCCCGAGGAGATCGCGGCGGCCCGCTCCCAGGCCCTGGATCTGCTGCGGCTGCGCGCCTCGACGCCGCTGTTCAGCCTGGGCTCGGCCCGCCTCATCCAGGACAAGTTGAGCTTCCCGGGGGCGGGCTTCGGGGCGCCGGCGGGAGTGATCGTCATGCTCATCGACGACACCCGGGGCGGCAGCGACGTGGACCCCGAGCTCGACGCCGTCCTGGTGGTCTTCAACGCTTCGGGCCAGACGCTCACTCAGCCGCTGCCCGAGCTGGCGGGCCGGGACTTCCGCCTCTGCCCCATTCAGGCCGAGGGGGCCGATGAGGTGGTGCGCCGCACCGGCTTCGACCGTGCCAGCGGGACGATCTCGGTGCCGGCGCGCACCGTGGCCGTCCTGGTAGAGCCCCAGAGCCGCTGA","MDREVVVTDAGHPLLGSGLALRLITAPDGGAAAIHGQILGADGMPAPTVTPLRIVGNLPDEVLAAHPHLEGYIALSATDAAGTPLLDDAAVASALTGQVAIAQYVGLPDPTEAADVSDAHLDAFTGVQTAILLDHLYAEAATRAELGVTFTGGLPSFALWAPSAQAVTLLTWETSDPLGSVPEVPGPPRRTPAVRKGDGRWVVTNHPDQPAGATLSTPSGEPGPSAPGAPITAGCQYLWEVRVYVPSTRRVETNVVTDPYSTTLTTDSTRSVAVDLADPRLAPEQWATTRAPAVRNDSARSIYELHLRDFSAADDTVPPELRGTYRAFTVAGSAGVRHLAELARAGMNTIHLLPTFDIATIPEHRGSQRHPDIPDGAHPASADQQAAIAEVADHDAYNWGYDPLHWGAPEGSYATEGHQDGGARVVEFREMVGALHDLGLQVVLDQVYNHTAACGQDPRSVLDQVVPGYYHRLDAVGRVTSSTCCANTATENALCARLMIDSVVRWARWYRVDGFRFDLMGHHPRAVMERVRTALDELTLEADGVDGRSIYLYGEGWNFGEVAGNALFVQATQGQLDGTGIGAFNDRLRDAVHGGGAFDPDHRVFQGFGTGLLTQPSGLDHRGWNDQSADLAHRTDLVRLGLAGNLKDYVMTISDGSVRRGIDLIHNGAPAAFASHPQENVNYVDAHDNETLYDLLAYKLPQGMPVAERVRMNTVCLATVALAQSPAFWSAGTELLRSKSLDRDSYNSGDWFNAIDFTGQSNGFGRGLPPASRNEGSWAIQGPLLQDDWLRPSPEEIAAARSQALDLLRLRASTPLFSLGSARLIQDKLSFPGAGFGAPAGVIVMLIDDTRGGSDVDPELDAVLVVFNASGQTLTQPLPELAGRDFRLCPIQAEGADEVVRRTGFDRASGTISVPARTVAVLVEPQSR$","Alpha-1,6-glucosidase, pullulanase-type","Cytoplasm, Extracellular","pullulanase","alpha-1;6-glucosidases; pullulanase-type","alpha-1,6-glucosidase, pullulanase-type","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR004193
Domain

Glycoside hydrolase, family 13, N-terminal
PF02922	$\"[145-261]T$	Isoamylase_N

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[427-453]T$	Alpha-amylase

InterPro
IPR011839
Domain

Alpha-1,6-glucosidases, pullulanase-type
TIGR02103	$\"[1-926]T$	pullul_strch: alpha-1,6-glucosidases, pullu

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[286-758]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[258-356]T$ $\"[392-612]T$ $\"[670-757]T$	AMYLASE
PTHR10357:SF22	$\"[258-356]T$ $\"[392-612]T$ $\"[670-757]T$	PULLULANASE

InterPro
IPR000412
Family

ABC-2
PS51012	$\"[20-247]T$	ABC_TM2

InterPro
IPR013525
Domain

ABC-2 type transporter
PF01061	$\"[2-214]T$	ABC2_membrane

InterPro
IPR013526
Family

ABC-2 transporter
PR00164	$\"[22-43]T$ $\"[134-158]T$ $\"[171-190]T$ $\"[191-210]T$	ABC2TRNSPORT

noIPR
unintegrated

unintegrated
PTHR19241	$\"[1-209]T$	ATP-BINDING CASSETTE TRANSPORTER
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[20-40]?$ $\"[54-74]?$ $\"[95-129]?$ $\"[135-157]?$ $\"[162-182]?$ $\"[222-240]?$	transmembrane_regions

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[176-219]T$	Q7M9Z2_WOLSU_Q7M9Z2;
PF00005	$\"[75-252]T$	ABC_tran
PS50893	$\"[50-276]T$	ABC_TRANSPORTER_2
PS00211	$\"[177-191]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[74-252]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[50-267]T$	no description
PTHR19222	$\"[50-265]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[50-265]T$	ABC TRANSPORTER

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[294-386]T$ $\"[702-794]T$	HATPase_c
SM00387	$\"[294-391]T$	HATPase_c

noIPR
unintegrated

unintegrated
tmhmm	$\"[39-59]?$ $\"[65-87]?$ $\"[118-138]?$ $\"[144-164]?$ $\"[440-460]?$ $\"[466-484]?$ $\"[499-519]?$ $\"[525-545]?$	transmembrane_regions

","BeTs to 4 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 294 to 386 (E_value = 0.00012) place ANA_2120 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.Residues 702 to 794 (E_value = 0.00012) place ANA_2120 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","two-component system sensor kinase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2121","2299505","2300218","714","6.26","-5.17","25788","ATGGATCCTCCACACCACCCTCCCCCTCACACCCAAGGACACCCTGTGACGCAGCAGAGCCCAGCCGGAACGATCCGAGTCATCGTCGTCGATGACGACGCCATCGTGCGCGAGACGCTGTCCTCGATCCTCGACTCGGAACCGGACATCGACGTCATCGCCACCGCGGACAATGGCGCCGAGGCAGTCGCCCTCGTCCACGAACGCACCGTCGACGTCGCACTCATGGACATCCAGATGCCCGTGCTCGATGGCGTGGAGGCCACCTCCCGGATTCGGAAGACCAGCGAGAGGACCCGCGTCCTCCTGCTCACCACCTTTGACGAGGACACCTTCCTCGATGGCGGGATTGCCGCCGGGGCCTCCGGCTTCCTGCTCAAGACGACGCGCTCGTCAGAGATTGCGGAAGTGATCCGCACCATCCACGCCGGCGGCAAGGTTCTCTCACCCGGTCCGACGAAGCGGGTCCTGGAGCGATACATCCACGGCCAGACCCCCCATGTCGGCACGATCGCTGACCTGGACCTGTCCGGCCGTGAGCAGCAGGTGCTTCACCTCCTGTGCCAGGCCCACACGAACCATCAGATCGCGCGCGAGATGAACATCGCTGAAACCACCGTGAAAACCTATGTCTCCTCCATCATGCGGAAAATGGATGTGCGCAGCAGGCTCGAGATCGTCGTCGAGGCGCACAAGCGTGGTATCAGCGGTTAA","MDPPHHPPPHTQGHPVTQQSPAGTIRVIVVDDDAIVRETLSSILDSEPDIDVIATADNGAEAVALVHERTVDVALMDIQMPVLDGVEATSRIRKTSERTRVLLLTTFDEDTFLDGGIAAGASGFLLKTTRSSEIAEVIRTIHAGGKVLSPGPTKRVLERYIHGQTPHVGTIADLDLSGREQQVLHLLCQAHTNHQIAREMNIAETTVKTYVSSIMRKMDVRSRLEIVVEAHKRGISG$","Two-component system response regulator","Cytoplasm","two-component response regulator alr2138","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[176-232]T$	Q6REL8_BBBBB_Q6REL8;
PR00038	$\"[176-190]T$ $\"[190-206]T$ $\"[206-218]T$	HTHLUXR
PF00196	$\"[173-230]T$	GerE
SM00421	$\"[173-230]T$	HTH_LUXR
PS50043	$\"[169-234]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[43-141]T$	Q6ABR9_PROAC_Q6ABR9;
PF00072	$\"[25-139]T$	Response_reg
SM00448	$\"[25-138]T$	REC
PS50110	$\"[26-142]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[149-236]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[20-146]T$	no description
PTHR23283	$\"[26-142]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF46	$\"[26-142]T$	OSMOLARITY TWO-COMPONENT SYSTEM PROTEIN SLN1

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[175-229]T$	Q8G5S3_BIFLO_Q8G5S3;
PR00038	$\"[175-189]T$ $\"[189-205]T$ $\"[205-217]T$	HTHLUXR
PF00196	$\"[172-229]T$	GerE
SM00421	$\"[172-229]T$	HTH_LUXR
PS50043	$\"[168-233]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[2-116]T$	Q9RPE7_CORDI_Q9RPE7;
PF00072	$\"[2-116]T$	Response_reg
SM00448	$\"[2-115]T$	REC
PS50110	$\"[3-119]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[148-235]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[2-123]T$	no description
PTHR23283	$\"[30-82]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF45	$\"[30-82]T$	SENSORY TRANSDUCTION HISTIDINE KINASE BACTERIAL

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000673 (CheB methylesterase) with a combined E-value of 1.1e-20. IPB000673B 21-74 IPB000673C 75-105***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 2.1e-17. IPB000792 175-221***** IPB005143 (Autoinducer binding domain) with a combined E-value of 1.7e-10. IPB005143B 175-218***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 1.4e-09. IPB001867A 49-62 IPB001867B 77-121","","","-51% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 1.1E_26);-51% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 1.1E_26);-53% similar to PDB:1DZ3 DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A (E_value = 1.7E_11);-53% similar to PDB:1QMP PHOSPHORYLATED ASPARTATE IN THE CRYSTAL STRUCTURE OF THE SPORULATION RESPONSE REGULATOR, SPO0A (E_value = 1.7E_11);-56% similar to PDB:1S8N Crystal structure of Rv1626 from Mycobacterium tuberculosis (E_value = 1.1E_10);","Residues 2 to 116 (E_value = 1.9e-24) place ANA_2122 in the Response_reg family which is described as Response regulator receiver domain.Residues 172 to 229 (E_value = 5e-18) place ANA_2122 in the GerE family which is described as Bacterial regulatory proteins, luxR family.","","regulator CstA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2123","2300431","2300796","366","8.85","1.90","12693","ATGCTCACAAGCCACGGAGGACCGAGAAGGCGATCAGCCCTAAAAGTCGCCCGCAGTGACACAAACCGGTTCCAGGCGGCTGATTCAAGGAGCTTGCGTGCACCTTCACGCCCGTCCCAGGACGTCATCGAGGCCGATGACGCCGCCGCGCAGGGCCAGCAGCACCAGCTGAACCCGATCTCGGCAGCCGGTCTTGGACAGCAGGTGGCTCACGTGGGTCTTGACCGTGGGCATGGACAGCCACTCCCGGTCGCAGATCTCCTGGTTGGTGAGCCCCAGGGCGATAAGCGCCAGGATCTCGCGCTCACGCTGGGTCAGGCCCGCGACCTGCTGGGAGGCCTCGGCGGCCCGAACCGCCTCGACTGA","MLTSHGGPRRRSALKVARSDTNRFQAADSRSLRAPSRPSQDVIEADDAAAQGQQHQLNPISAAGLGQQVAHVGLDRGHGQPLPVADLLVGEPQGDKRQDLALTLGQARDLLGGLGGPNRLD$","Hypothetical protein","Periplasm, Cytoplasm","putative phosphate transport protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG1869COG name: Uncharacterized components of ribose/xylose transport systemsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1869 is --------v--lb-e-gh---j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","phosphate transport protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2124","2302945","2301398","1548","7.35","1.76","53579","ATGAGAAAGCGGCTGGGGCGTGAGGCGGCGCGGGCCGACTCGGTGGACCCCGCCCCGACCGGGCCGGCGGCGCCGGTGGGATCGACCCCGGTTGCCTGGCGCGACCCGCGCTCGGTCCCGTGGACGAGTGCGTTCGACGTCGTCATCGCTCTGGCCTTCTTCTTCCTGTTGTGCCTTGGCCGGCCCGACTCGGCGTTCTGGCTCGTCGATGGGGCGGGGCCGGTGCTCCACGCCCTGCTGGTGGGGGCCTGCGCCCTGGCTCTGGCCGTCCGGCGCCGCTGCCCGCTGCTCTTCGTTGTGGTGGCCGGCATCTGCCTGAGCGCGCACCTGGTGCTGTTCACGGGGTTCTCCGTCTTCTTCGTCGTGACCGGCCTGATCGCGGTGGAGACGACGCAGTCCCGCCTGGAGGCGCCATGGCGGTGGGTGGCGCTCGTCCTCGAGATCGTGGGCGTGGAGCTGGCGACGGCGCGCGTGTTCCACCTCATCGGCGGCTACGTCCACGCAGGTGAGGCACGGTCCGTGGTCGTCGTCAATATCTGGCTGGTGACGATCGTGGCGGCCTTCGTCGGCGCTGCGCGGCGCCGTAGCCGTGACCGCTACAACCGGGCCCTCGAGCGGGCCTCGGTGCTCGAGGCGCAGCAGGCCACCGAGCGGCGCCTCGCGGTCATCGAGACCCAGCAGCGCATCGCCCGTGACGTCCATGACCTGCTCGGCCACAGTCTCACCGTCATCGCCATGCAGGCCGAGGGCGCCCGGGCCATCCTGGCCACCGATCCGGCGGCCGCCGACGAGGCCCTGGCCGTCATCGGAGAGACCTCCCGCCGCTCCGTCGACGAGGTGCATGCCCTGGTCGACATGCTGCGTTCCGATGCCGGTGCCGCCGGTGTCGATGCGGCCGCCGCGCCCGGTTCCGGCTCCGTTGCTGATAGGGGCTCTGATGCCGGTGCCGCCGGTGGTGCCGGCGGCGGGGCTTCCGGCACTGTTGAGGCCGGAGCCGAGGCTGGCACCGGAACCGGAGAGGCGACGTCGGGACAGCACGTGGAGCTCCTGCGCGAACCCGTGCGTCAGGCGCAGCGGGCGGGACTGCCCGTCACCCTGGAGGCCGACCCGGCCGGCCGGGTTCCCCCGGCGGTGGCGCAGGTCCTTCACCGGGTGGTCCAGGAGTCGCTGACCAACGTGCTGCGCCACGCTCCCGGTGCGGCCACGAGAGTCTCGCTGCGCACCGGGGCGGGGCGCGTCATCCTCGTCGTCGAGAACGCCCCGGTCCCGGCGTTGCCGGCAGGAGATGCGGATCCGATGCCGAGGACCTTCGACCCGCATCGTGAGGACAGGGGTGAACAGGTGGACGCCGTGCCAGGGCGGACGCCACACGCCTCGGCCGCGATGTCTCGTCCCGCGGTGAGCGTCTCCGAAGGTCTGAGGCGCGGCGGCTTCGGTCTCATCGGCATGCGTGACCGGGTTGCCCAGGTCGGAGGCACCTTCACCGCCGGTCCCACGGTTGAGGGCGGATGGAGGGTGACGACAGAGCTCCCCTGTGTTCCACAGTGA","MRKRLGREAARADSVDPAPTGPAAPVGSTPVAWRDPRSVPWTSAFDVVIALAFFFLLCLGRPDSAFWLVDGAGPVLHALLVGACALALAVRRRCPLLFVVVAGICLSAHLVLFTGFSVFFVVTGLIAVETTQSRLEAPWRWVALVLEIVGVELATARVFHLIGGYVHAGEARSVVVVNIWLVTIVAAFVGAARRRSRDRYNRALERASVLEAQQATERRLAVIETQQRIARDVHDLLGHSLTVIAMQAEGARAILATDPAAADEALAVIGETSRRSVDEVHALVDMLRSDAGAAGVDAAAAPGSGSVADRGSDAGAAGGAGGGASGTVEAGAEAGTGTGEATSGQHVELLREPVRQAQRAGLPVTLEADPAGRVPPAVAQVLHRVVQESLTNVLRHAPGAATRVSLRTGAGRVILVVENAPVPALPAGDADPMPRTFDPHREDRGEQVDAVPGRTPHASAAMSRPAVSVSEGLRRGGFGLIGMRDRVAQVGGTFTAGPTVEGGWRVTTELPCVPQ$","Two-component system sensor kinase","Membrane, Cytoplasm, Extracellular","ATPase, histidine kinase-, DNA gyrase B-, andHSP90-like domain protein protein","two-component system sensor kinase","histidine kinase, dimerisation and phosphoacceptor region","","Perego M., Hoch J.A. Protein aspartate phosphatases control the output of two-component signal transduction systems. Trends Genet. 1996. 12(3):97-101. PMID: 8868347Tomomori C., Tanaka T., Dutta R., Park H., Saha S.K., Zhu Y., Ishima R., Liu D., Tong K.I., Kurokawa H., Qian H., Inouye M., Ikura M. Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nat. Struct. Biol. 1999. 6(8):729-734. PMID: 10426948Bilwes A.M., Alex L.A., Crane B.R., Simon M.I. Structure of CheA, a signal-transducing histidine kinase. Cell 1999. 96(1):131-141. PMID: 9989504","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[377-513]T$	HATPase_c
SM00387	$\"[377-514]T$	HATPase_c

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
SM00388	$\"[225-292]T$	HisKA

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[225-292]T$	HisKA_3

noIPR
unintegrated

unintegrated
tmhmm	$\"[39-59]?$ $\"[69-89]?$ $\"[94-128]?$ $\"[142-162]?$ $\"[174-192]?$	transmembrane_regions

","BeTs to 6 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 3.6e-14. IPB011712A 224-241 IPB011712B 382-402","","","No significant hits to the PDB database (E-value < E-10).","Residues 225 to 292 (E_value = 6.3e-18) place ANA_2124 in the HisKA_3 family which is described as Histidine kinase.Residues 377 to 513 (E_value = 5.3e-09) place ANA_2124 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","histidine kinase-, DNA gyrase B-, and HSP90-like domain protein protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2126","2303054","2304247","1194","9.73","6.42","41333","ATGCTCACCAGGTCCAACGCGAGCATCCTTGTTCCCATGACGACCTCGCATCGCATCCCACCAGCGCCTTCAGCACCTCTCCAGGCGAAGGCGGCCGCCTCCAGCACGCCGGCTCAGCCAGTCCGGACCTCCTCTCCGGCTCGCCTCCCGCAGGCCGGCGGGCCGGCCCCGGGAGCGCCTGCCTCCGACGCCGTCGTCCTGACCCACGACCTCACCAAGACCTTCGGCAGGCGCACCGTCGTCGAGGGGCTCAACCTCGTGGTGCCCCGCGGGGCCGTCTACGGCTTCCTGGGCCCCAACGGCTCGGGCAAGTCGACGACGATGAAGATGCTGCTGGGACTCCTGGCGCCCACGCGCGGGCAGATCAGCGTGCTGGGGAGGCCCTTCAGCCCGACCACGCGAGCCGAGATCATGTCGCGCACCGGCTCGATGATCGAGAACCCGCCCGGCTACAGCCACCTCACGGGCGCGGAGAACATGCGGATCGCGGCGAAGATGCAGGCACTGAGCGACCAGCAGATCAGTCGCGCCCTCGCCCTGGTGCGCCTGACCGAGCACAAGGACCGCCTGGTGCGCACCTACTCACTGGGCATGAAGCAGCGCCTCGGGATCGCTCTGGCGCTGGCCCGCCAGCCCGAGCTGCTCATCCTCGATGAGCCCACCAACGGCCTGGACCCGGCCGGTATCGAGGAGGTGCGCCGGCTGCTGGTCGAGCTCTCCGGCGAGGGCGTCACCGTCATGGTCTCCAGCCACCTGCTCGACGAAATCGACCGCATGGCGTCCACGCTCGGCATCCTGTCGGGCGGGCGCCTGGTCTTCCAGGGCACGCGCGCCGAGCTCATGGAGCGCTCGGTGCCGGACGTGCTCGTCGCCACCCCGACGCCGCAGGCCGTCCTGAGCCCTCAGGTCCTGGCCGGGCTCGTACCGGCGCAGGCACTCGCGGCGGCGACGGCGGCCGGCGCCCCCGATGCCTCCGCCTCGCCCAACCCGACCGCTGTTCCCGTCACCGGTTCTGCCACCGGCCCGACGCTGACGCCACAGGGCGTGCGCATCCCGGGAATGTCGAAGGAGGCGGTCGCCGAGCTCATCAACCGTCTGGTGAGCGCCGGCGTCGAGCTGCACGAGGTACGGCGCGAGGCCCAGAGCCTCGAGGACGTCTTCATGGACCTCACCGGTCGCGGAGGTGTGCTGTGA","MLTRSNASILVPMTTSHRIPPAPSAPLQAKAAASSTPAQPVRTSSPARLPQAGGPAPGAPASDAVVLTHDLTKTFGRRTVVEGLNLVVPRGAVYGFLGPNGSGKSTTMKMLLGLLAPTRGQISVLGRPFSPTTRAEIMSRTGSMIENPPGYSHLTGAENMRIAAKMQALSDQQISRALALVRLTEHKDRLVRTYSLGMKQRLGIALALARQPELLILDEPTNGLDPAGIEEVRRLLVELSGEGVTVMVSSHLLDEIDRMASTLGILSGGRLVFQGTRAELMERSVPDVLVATPTPQAVLSPQVLAGLVPAQALAAATAAGAPDASASPNPTAVPVTGSATGPTLTPQGVRIPGMSKEAVAELINRLVSAGVELHEVRREAQSLEDVFMDLTGRGGVL$","ABC-type multidrug transport system, ATPase component","Membrane, Periplasm, Cytoplasm","MrsF protein","ABC transporter; ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[194-236]T$	P94627_CLODI_P94627;
PF00005	$\"[91-269]T$	ABC_tran
PS50893	$\"[66-293]T$	ABC_TRANSPORTER_2
PS00211	$\"[194-208]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[90-277]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[66-284]T$	no description
PTHR19222	$\"[66-293]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[66-293]T$	ABC TRANSPORTER

noIPR
unintegrated

unintegrated
tmhmm	$\"[51-71]?$ $\"[85-107]?$ $\"[139-161]?$ $\"[175-195]?$ $\"[205-225]?$ $\"[259-279]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-40% similar to PDB:2J9I LENGSIN IS A SURVIVOR OF AN ANCIENT FAMILY OF CLASS I GLUTAMINE SYNTHETASES IN EUKARYOTES THAT HAS UNDERGONE EVOLUTIONARY RE-ENGINEERING FOR A TISSUE-SPECIFIC ROLE IN THE VERTEBRATE EYE LENS. (E_value = );-59% similar to PDB:1ZCD Crystal structure of the Na+/H+ antiporter NhaA (E_value = );-55% similar to PDB:1XVQ Crystal structure of thiol peroxidase from Mycobacterium tuberculosis (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2129","2305182","2305922","741","10.26","7.33","25683","CTGCTCGCCGCCGAGGTCATCAAGCTCAAGCGCTCCTCGGTGTGGGTGGTGGCCGTTCTGCTGCCGCTGCTCGCAGTCATCACCGGCACCTTCAACTTCTACCGAAATCTGGGGGTCTTCTCCGCGGAATGGGGAGCTCTGACGTCCCAGATATCCTTGTTCTACTCGATGTTCTTCTGCTCGTTGGGGGTGGCCCTGCTGGCCTCCGCCGCATGGCGGATGGAGCACCGGGGCACGAGCTGGAACGCCATGCGGACCTCCCCGCACTCCCCGGTATCCGTCGTCCTGGCCAAGACCCTGGTCATTGTGCTTCCGGTGCTGGCCATGCAGGTGGCGCTCATCGTGCTGGCCTGGATCTCGGGGGCATTCGTGATGGGTCTCGGTCTCACAATGCCCAGCACCGTCATCGCCTCCAATCTTCTGGCAGTGGTCAGCATCATCCCGCTCATCGCCCTGCAGTCACTGCTGAGCATGCTCATGCGGTCCTTCGCCGCGCCAGTGGCACTGGGATTCGTCGGCTGCGTCCTCGGATTCGGCCTGGGAGCGGCACAGAACCCTCTGGCCTACGCCATCCCCCAAGGGCTTGTCAGCATGACACTGTCTCTGGGATCGACAGCCTTGACGGCCGGGGAACTGGACGCGGCGAGCATGGTTCCTCTCCTGCTCTCCATTGTTGGTGTCGGCGCTGTCATGTGGGGTCTGCTGGTCCTTGTCGCCCGCCGCACCGGCGGCGTGCGCTAG","LLAAEVIKLKRSSVWVVAVLLPLLAVITGTFNFYRNLGVFSAEWGALTSQISLFYSMFFCSLGVALLASAAWRMEHRGTSWNAMRTSPHSPVSVVLAKTLVIVLPVLAMQVALIVLAWISGAFVMGLGLTMPSTVIASNLLAVVSIIPLIALQSLLSMLMRSFAAPVALGFVGCVLGFGLGAAQNPLAYAIPQGLVSMTLSLGSTALTAGELDAASMVPLLLSIVGVGAVMWGLLVLVARRTGGVR$","ABC transporter, peremase protein","Membrane, Extracellular","cdd2 protein, putative","possible MrsE protein","Uncharacterized protein-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[54-74]?$ $\"[95-117]?$ $\"[123-152]?$ $\"[162-182]?$ $\"[218-238]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-56% similar to PDB:2I21 Bacteriorhodopsin/lipid complex, T46V mutant (E_value = );-56% similar to PDB:1PXS Structure of Met56Ala mutant of Bacteriorhodopsin (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","Wed Aug 8 10:40:14 2007","","Wed Aug 8 10:40:14 2007","","","Wed Aug 8 10:40:14 2007","Wed Aug 8 10:40:14 2007","Wed Aug 8 10:40:14 2007","","","","","","Wed Aug 8 10:40:14 2007","","","","Wed Aug 8 10:40:14 2007","Wed Aug 8 10:40:14 2007","","","","","yes","","" "ANA_2130","2306469","2306071","399","6.31","-1.34","14008","GTGCAGCGGCCCGAGAGGCCGGAGAGCGCCGGCCGGGCGGAGGGGTCGGCTGAGTCGGCTGAGTCGGCCGGCGCCGGAGCCGAAGTCCTCGCTGCCGCGACGGTCTCCGCCGTCGATATCGACCCCGTCATTCACGCCCAGGCCCGGCTGCGGATCATGGCGACCCTGGCCGCCGTGCCCGTTGGCGACGAGCTGCACTTCCCGCGGCTGCGCGAGCTGCTGGACATGACGGCGGGCAACCTGTCCACGCACCTGTCCAAGCTGGAGGGGGCGGGCTACGTGCAGCAGAACAAGACCTACTCCGGGCGCAGTCCCGCCACCTACCTGGCACTGACCCCCGAGGGGCGGGTGGCCTTCGAGCGGTACGTGCGCAACCTGCGCGCCCTGCTCGACGCCTGA","VQRPERPESAGRAEGSAESAESAGAGAEVLAAATVSAVDIDPVIHAQARLRIMATLAAVPVGDELHFPRLRELLDMTAGNLSTHLSKLEGAGYVQQNKTYSGRSPATYLALTPEGRVAFERYVRNLRALLDA$","Hypothetical protein","Cytoplasm","Transcriptional regulators","hypothetical protein","hypothetical protein","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[32-132]T$	no description

noIPR
unintegrated

unintegrated
PD463025	$\"[47-130]T$	Q72GL8_THET2_Q72GL8;

noIPR
unintegrated

unintegrated
tmhmm	$\"[39-57]?$ $\"[67-87]?$ $\"[108-128]?$ $\"[142-162]?$ $\"[167-187]?$ $\"[193-211]?$	transmembrane_regions

InterPro
IPR005242
Family

Conserved hypothetical protein 374
PF03706	$\"[764-988]T$	UPF0104
TIGR00374	$\"[694-988]T$	TIGR00374: conserved hypothetical protein

noIPR
unintegrated

unintegrated
tmhmm	$\"[106-126]?$ $\"[150-170]?$ $\"[185-205]?$ $\"[219-241]?$ $\"[256-276]?$ $\"[686-706]?$ $\"[727-747]?$ $\"[761-781]?$ $\"[796-816]?$ $\"[830-850]?$ $\"[883-903]?$ $\"[909-929]?$ $\"[934-954]?$ $\"[960-980]?$	transmembrane_regions

","BeTs to 3 clades of COG0478COG name: RIO-like serine/threonine protein kinase fused to N-terminal HTH domainFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0478 is aom-kzy-------------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 764 to 988 (E_value = 0.0002) place ANA_2132 in the UPF0104 family which is described as Uncharacterised protein family (UPF0104).","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2132.1","2310748","2310323","426","10.13","8.77","15630","ATGAGCCAGATGCTCCCCACCACCCGCCACTCGATCAGCCTGGTCCAGCGCACGAACATCGCCGTGCTGGTCGGCCTGTCCCGCCTCCTGCGCCATCTCAAGCCCCACCGTCTCCAGCGCCTCATGTCCTTCGTCGTGCGGGGCGCGCAGCCCGCCGATTACAGCATCGCCCGCGACGCCAGGGACGACATCCTCTCCGCCAGCGCCGTGTGCCGCGGGGACAGGGCGTGCCTCATCAGGTCGGTGGCCGCGATGCTCCTGTGCAGGCAGCGCGGCTACGCGCCGACGTGGTGCGTCGGCGTCGTCGCCACGCCTCCCTTCGCCGCCCACGCCTGGATCGAGGCCGACGATCGCATCGTCGATGAGCCCATCGACGCGTCCTACCTGCGGACTTTCTACCGCGTGGGCGCCTCCGCCCGGGCGTGA","MSQMLPTTRHSISLVQRTNIAVLVGLSRLLRHLKPHRLQRLMSFVVRGAQPADYSIARDARDDILSASAVCRGDRACLIRSVAAMLLCRQRGYAPTWCVGVVATPPFAAHAWIEADDRIVDEPIDASYLRTFYRVGASARA$","Conserved hypothetical protein","Membrane, Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 12-141 are similar to a () protein domain (PD798253) which is seen in Q82BL7_STRAW.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:04:54 2007","Wed Aug 15 18:04:54 2007","Wed Aug 15 18:04:54 2007","Wed Aug 15 18:02:51 2007","","","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","Wed Aug 15 18:02:51 2007","","Wed Aug 15 18:02:51 2007","","Wed Aug 15 18:02:51 2007","yes","","" "ANA_2133","2311581","2310835","747","9.78","9.51","26084","ATGGGAGTCTTCATTGCGGAGCTGATCAAGATCCGGCGCTCAGCTGCGTGGATTCTCGCCGCACTCGTCCCTTCCGTCACTGCCGTGGCCAGCGCCATGGGAGCCTGGACCTCTGGCGGCTTCGAGGATGGCTGGAACACCCTGTGGATCCGATCGATCGGCCTCTACGGGATGCTGATGCTCGGCGTCGGACTATCCGTCCTGGCCTCCCTCGTCTGGCGCGCCGAGCACACCGGGAACAACTGGAACGCCATGACCGCCCAACCGGTGGCCGCCTGGAGGCTGGCCGCCGCCAAGGTCCTCGCGCTCGCCCTCCTCGCGACCTTCATGCAGGCAGTCCTCCTCCTGACCGTGCTCTTCCTGGGAAAGGTGGTGTTCCACCTGCCCGCTTGGCTCCCGGCTCGCTACTACGCCGTCAGCGTCCTCGTGGTCGTGGCCAGCGTGCCCGTCTGCGCGGCACAGTCCGCTCTGTCAGCAAGGTCCCGCTCGTTCGTTCTTCCCGTCGTGATCGGGTTCGTGCTCACGTGCGTCGGTGCCGTTCTTCTCGCCATCAAGGTCAGGGCGGCCCTGATCTACGCCTACTGCCTCCTGGCTTATACCACTCAGCTCGGATCAGGCTCTGGGGCGGACGCGTCGGCGCTCACGATCCAGTCGGCCACCCTCACCGTCGTTCTGTCCGTCGCGCTGACCGCGCTCTGCGTTCTTGCCACAGCGCGCTACTTCAATCGGACGGACACGCACGCCTGA","MGVFIAELIKIRRSAAWILAALVPSVTAVASAMGAWTSGGFEDGWNTLWIRSIGLYGMLMLGVGLSVLASLVWRAEHTGNNWNAMTAQPVAAWRLAAAKVLALALLATFMQAVLLLTVLFLGKVVFHLPAWLPARYYAVSVLVVVASVPVCAAQSALSARSRSFVLPVVIGFVLTCVGAVLLAIKVRAALIYAYCLLAYTTQLGSGSGADASALTIQSATLTVVLSVALTALCVLATARYFNRTDTHA$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","Uncharacterized protein-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[54-74]?$ $\"[95-127]?$ $\"[133-153]?$ $\"[163-197]?$ $\"[216-236]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[33-53]?$ $\"[67-87]?$ $\"[119-137]?$ $\"[156-176]?$ $\"[185-207]?$ $\"[234-254]?$	transmembrane_regions

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[133-175]T$	P94627_CLODI_P94627;
PF00005	$\"[30-208]T$	ABC_tran
PS50893	$\"[5-232]T$	ABC_TRANSPORTER_2
PS00211	$\"[133-147]?$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[29-216]T$	AAA

InterPro
IPR013173
Domain

DNA primase DnaG, DnaB-binding
SM00766	$\"[140-257]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-221]T$	no description
PTHR19222	$\"[5-287]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[5-287]T$	ABC TRANSPORTER

noIPR
unintegrated

unintegrated
tmhmm	$\"[26-46]?$ $\"[65-85]?$ $\"[111-131]?$ $\"[141-161]?$ $\"[176-196]?$ $\"[235-255]?$	transmembrane_regions

","BeTs to 3 clades of COG2386COG name: ABC-type transport system involved in cytochrome c biogenesis, permease componentFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG2386 is a--------d----efghs--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2137","2315154","2314249","906","6.87","-0.64","33188","ATGCCGCAGATGACTGAAGCCCCTGCAGTCCAGGCCTCACAGCTCACCATGTCGTACGACGACAAGACCGTGCTGGCCGGAACCTCCTTCACCATCCCGCGCGGCTCCGTCCTCGCGCTCCTGGGACCCAATGGCGCAGGCAAGAGCACGACCATCGATATCCTGTGCGGGCTCAAGCGCCGGTCCTCGGGATATGTGCGGGTCCTGGGGATCGATCCCGCCCACGCCGACGAGGCGTGGCGAGCGCGAGTGGGCGTGGTACGTCAGTCCTGGCGTGATCACGAGCGCTGGCGCGTCGGTGACCTCCTGCATCACCTCAGCCAGTACTACGGCGCTTATTCCTCCTCTGAGGCGGGATGGGACCCCGATGAGCTCCTGCGCGTCGTCGGTCTGTCCTCGGTCGCTGCGAAGCGCATCCGTACGCTCTCCGGTGGCCAGAGACGGCGGCTCGACGTCGCCATCGGGCTTGTCGGCAACCCCGACATCCTCTTCCTCGACGAGCCGACCACCGGTTTCGACACCGAGGCGCGCAACGAGTTCCACGCACTCATCCACGCTCTGGTCGCGCGGAAGACCCTGACCATTGTCCTGACCACTCACGACCTCAGGGAGGCCGAGGAGCTCGCCAGTCACGTTATCGTCCTGGCCGAGGGGACGGTGAGGTTCCAGGGCACGGTGGAGGAGTTCGGACAGCGGGTGCAGGTCAAGGACCGCATCAGCTATACGGACCGGGGTGAGTTCCACGTGCTGGAGACACCTCCCGATGCCACCGTCCCCACTCTCAAGACGCTCGTCAACACCGCAGGCGAGTCCCTCGAGAATCTCGAAGTCCGACGCGCCACGCTGGAGCAGCTCTACCTGCGCATCACCAACGAGGCCGCACACTCCCGGAGGGCCGCATCATGA","MPQMTEAPAVQASQLTMSYDDKTVLAGTSFTIPRGSVLALLGPNGAGKSTTIDILCGLKRRSSGYVRVLGIDPAHADEAWRARVGVVRQSWRDHERWRVGDLLHHLSQYYGAYSSSEAGWDPDELLRVVGLSSVAAKRIRTLSGGQRRRLDVAIGLVGNPDILFLDEPTTGFDTEARNEFHALIHALVARKTLTIVLTTHDLREAEELASHVIVLAEGTVRFQGTVEEFGQRVQVKDRISYTDRGEFHVLETPPDATVPTLKTLVNTAGESLENLEVRRATLEQLYLRITNEAAHSRRAAS$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Membrane","ABC-type transporter, ATPase component","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[142-184]T$	Q82FW0_STRAW_Q82FW0;
PF00005	$\"[35-218]T$	ABC_tran
PS50893	$\"[10-242]T$	ABC_TRANSPORTER_2
PS00211	$\"[142-156]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[34-219]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[3-246]T$	no description
PTHR19222	$\"[10-253]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[10-253]T$	ABC TRANSPORTER

","BeTs to 17 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 5.4e-24. IPB005074C 24-71 IPB005074D 130-173***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 2.8e-22. IPB013563A 24-58 IPB013563C 139-166 IPB013563D 194-246***** IPB005116 (TOBE domain) with a combined E-value of 1.8e-15. IPB005116A 42-58 IPB005116C 142-155 IPB005116D 162-181 IPB005116E 196-209***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 9e-13. IPB010509B 35-60 IPB010509D 137-181***** IPB010929 (CDR ABC transporter) with a combined E-value of 4e-08. IPB010929K 22-66 IPB010929M 139-185 IPB010929A 34-53 IPB010929C 124-157","","","-50% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 6.3E_25);-49% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 3.8E_22);-48% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 1.4E_16);-48% similar to PDB:1Q1B Crystal structure of E. coli MalK in the nucleotide-free form (E_value = 1.4E_16);-48% similar to PDB:1Q1E The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form (E_value = 1.4E_16);","Residues 35 to 218 (E_value = 2.9e-39) place ANA_2137 in the ABC_tran family which is described as ABC transporter.","","transporter, ATPase component (drrA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2138","2316009","2315761","249","6.52","-0.59","8597","ATGGCAAACAAGAAAGCCGCCCCTCTGCGGGTGCAGACTGATTACGGCGAGGTGGCGCTGGCCCCGAAGAGCGGGAAGTACTGGCACCTTAATTCCACAGCGGCACAGATACTCGATGAGCTCCAGACCGGGGGCGACGCCAGGAGCGCTACGGATGCTCTTGTGGCCTCATACGGGATCAGTGCCGAGCAGGCCTCACGTGATGTCGCTTCGACCATCGCATCACTTCACCGTGAGGGTCTCGTCTGA","MANKKAAPLRVQTDYGEVALAPKSGKYWHLNSTAAQILDELQTGGDARSATDALVASYGISAEQASRDVASTIASLHREGLV$","Hypothetical protein","Periplasm, Extracellular","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 12-81 are similar to a () protein domain (PD703906) which is seen in Q82BL6_STRAW.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:11:51 2007","Wed Aug 15 18:11:51 2007","Wed Aug 15 18:11:51 2007","Wed Aug 15 18:10:53 2007","","","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","Wed Aug 15 18:10:53 2007","","Wed Aug 15 18:10:53 2007","","Wed Aug 15 18:10:53 2007","yes","","" "ANA_2141","2317960","2316041","1920","6.26","-8.55","69745","ATGACGATCACCGCCCCGGAGATGACGGAATCGGATCACACGGATATCCCGACGATTCACCAGACGATCACCGTCCGGTCCGTCGATCAACAAGATAACTCCATCATCCTGCCTCAGGCATTCGCCATCGCAGTACCGGACACGGCCGAGGCTGACAACGTCATCAGCATCGCCGCCCCGCAGGCGACGATGATCGCCAGGCACGCCTCGGGCAGGCCCTGGCTCATGGTGCGCATGCCGCAGGCGTACGTCACGGCCTCAACAGCTCCCGGCACCAGGATCGTGGCAGTAGGAACGTGCTCCGCCTCAGTCGAGGATCTCAACAGAATCGCGCGACGCGGTGCCTCGCTCTCGGAAACAGCCGCCGAGGTCATGCGGTTCGACGGGAGCTTCACCGTCTACGCGCTGCGGGATGCGACGATCCTCGCCTGCGGGCCGGCGATGCAGACGCATCGCGTCTTCCACGCCCGCATCTTCGGCACCACCATCGTCTCGGATCGCGCCGATACTCTCGCGGCCCTGGGGAGGCTCCCGCTGGACACGGCGGCCGTGGCTCGCTCCCTCCTGGGCAGCCAGCCCAACTTCGACGACGCCCAGCAGCCCATGTGGAAGGGCATCACCCCGGTGTACGGCGGTCACTGTCTCACCGTGGACGCCAGCGCCTCGACATCGACCCATGCCTGGTGGCGGCGGCCGAGTCCGCGTTTGAGCCGCTCCGAGGGTGCGGCATTACTTCGAGAAAGGCTCCAGGCGGCAGTAGCCGCGCGCTCCCAGCAGCATCGCGAGCTGGCATGCGATCTTTCTGGAGGACTCGACTCCACGCCGGTGTGCTACTACGCCTCCACCGCACCTCAGGGGGTCACGGCTCTCACGTTCTACAGCGATGATCCTGGCGGCCGTGAGGACCTCCGCTGGGCTGAGATCGCCGCTCAGGCGATGCCTCGAGTCAGGCATGAAGCACTCTGGCTGGGCGATGCGCCGTCGTTCTACGAGGGAATCGGCGAGATGGACATTCCCGTCGATGAGCCCACTCAGGTGCCACTCACCGCCCCCCGTATCCTCTACGCGCTCGACCGTGATCGCGACCAGGGCGTCACCATGCACCTTCATGGCGCCGGCGGTGACCATCTCTTCCGCGGTGTCCCTGCATGGGACCACAGCATTGCCCGGCGCCACCCCATTCTCGGCTGGAACCGGGCCCGGGCGGAGGCCGCCGCGATGAAGCAGAGCAGCCTCACGGCGCTCCGGCGCCTCATCGACCGGCGATCGTACTCGCGCTGGTTGAAGGACGTGGCGTACGAGTCGGTGCGTCCCTCTGCGGAGACTTTCTGCCTCAGTGCAAGCGACTGGTACATACCGCCCCGCATCCCTGCCTGGATCGCCCAGGAGGCGCGAGAGGAACTCATCGCCTCCATGGTCGCCTCGGCCGAGCATGCCAAGCCGCTCTCCCCTGAACGTGGTGAGCATTTCGATCTGGCGAGCATCATCGACGCCTCGAGAGTGACTCGAGGAATGTCTCAGGTCGGCCTCCACCAAGGTATTGGGTATGAGTCGCCACTCATGGATGACCATGTCGTCGAGGCAGTTCTCAGTGTCGCCTACACAGATCGGGACAGCCCCATCGAGTGGAAGCCCCTCATGAAAGCAGCGATGCGCGGGATCCTCCCCGACGAATACCTGCTCCGAACCACCAAGGTGGGGGGATCGCCACAGGCCGTTCGTGGATACGCACAGAACTTCTCGACAGTGAAGGATCTGCTGGACGAGTCCAGCCTCATGGATCTCGGGATTATTGACCGTCACGCCCTGGAGGATTCGATTCGACCGTCGGAAACCAGTATGCCACCCACTCTGATTTCCCAGCTCATCAACACCGCTCTTTTCCTCAGGAATGCGCCCTCGGTGACGACTGCTTCCTGA","MTITAPEMTESDHTDIPTIHQTITVRSVDQQDNSIILPQAFAIAVPDTAEADNVISIAAPQATMIARHASGRPWLMVRMPQAYVTASTAPGTRIVAVGTCSASVEDLNRIARRGASLSETAAEVMRFDGSFTVYALRDATILACGPAMQTHRVFHARIFGTTIVSDRADTLAALGRLPLDTAAVARSLLGSQPNFDDAQQPMWKGITPVYGGHCLTVDASASTSTHAWWRRPSPRLSRSEGAALLRERLQAAVAARSQQHRELACDLSGGLDSTPVCYYASTAPQGVTALTFYSDDPGGREDLRWAEIAAQAMPRVRHEALWLGDAPSFYEGIGEMDIPVDEPTQVPLTAPRILYALDRDRDQGVTMHLHGAGGDHLFRGVPAWDHSIARRHPILGWNRARAEAAAMKQSSLTALRRLIDRRSYSRWLKDVAYESVRPSAETFCLSASDWYIPPRIPAWIAQEAREELIASMVASAEHAKPLSPERGEHFDLASIIDASRVTRGMSQVGLHQGIGYESPLMDDHVVEAVLSVAYTDRDSPIEWKPLMKAAMRGILPDEYLLRTTKVGGSPQAVRGYAQNFSTVKDLLDESSLMDLGIIDRHALEDSIRPSETSMPPTLISQLINTALFLRNAPSVTTAS$","Asparagine synthetase","Membrane, Cytoplasm","conserved hypothetical protein","putative asparagine synthetase","asparagine synthase","","Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G., Thoden J.B., Holden H.M., Rayment I. Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Biochemistry 1999. 38(49):16146-16157. PMID: 10587437","","","

InterPro
IPR001962
Domain

Asparagine synthase
PF00733	$\"[244-564]T$	Asn_synthase

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[230-562]T$	no description

","BeTs to 6 clades of COG0367COG name: Asparagine synthase (glutamine-hydrolyzing)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0367 is aompkzy---rlb-efg-s--j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","-62% similar to PDB:1VDK Crystal structure of fumarase from thermus thermophilus HB8 (E_value = );-43% similar to PDB:1YGY Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis (E_value = );","Residues 244 to 564 (E_value = 1.4e-11) place ANA_2141 in the Asn_synthase family which is described as Asparagine synthase.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2142","2319197","2318361","837","8.42","1.66","29588","ATGACCGCGATCACCGCATCCGGCACGAAGCTACGTGCCCCCCGCATCAACGGCCACCAGACCTTCGGCCGCGCTCTGCGCTCCGAGTGGATCAAGATCCGCTCTCTGCGCTCCACCTGGGTTACCTCTGCCGTCGCCATGGGCGTCATGGTCCTCTTCGGGGCGGCCACCGCCATCGGCTACCACGACATCCCGGAGCAGGTCGATCAGGCCAAGTACCAGATCACGTCCGCCGCGCCCTTCGGCTATATCATCGTCGCCGTCCTCGGCGCACTCCAAGTCACCGGGGAGTACGCCTCCGGTCAGATCCGCTCCAGCCTCACTGCGACCCCCCACCGGGGTCGACTCCTCATGGCCAAGGCCGCGGTCGTCGCAGTCTTCGCCTTCTTCCTGGGACTACTGTCAACCATGGCGACGTGGGCCGTCACCGTCCCCTTCCTCAAGGATGACGCCGGGAGTATCACCGACAGCGAGTACCTGGGTTTCTTCTGGGGCTCCGGACTCGCCTTCGCCGCCATCGCGCTGATGGGTCTTGCCTACGGATTCCTCCTGCGCTCCACGGCCGGCGCCATTACGACCGTCGTCGTGGTGCTCTTCGTCATCATGGTGCCGTTGCAGATGATGGCCTCGCAGTGGGAGTGGGCCAAAGAGCTCGCGGGTCTGCTCCCGACCTCCGCCGACGCCGCCATCACGGATCCCTTCGCCGTGGCGAACACCTGGGGCGTTGAGGATACGGCGACCTTCCTCTCCCAGGCGCAGACGGCTCTGATATTCCTCGCTTGGACTGTGCTTCCTCTGCCCATCGCGGCGGCAATCTTCCTCACGCGAGACGCCTAA","MTAITASGTKLRAPRINGHQTFGRALRSEWIKIRSLRSTWVTSAVAMGVMVLFGAATAIGYHDIPEQVDQAKYQITSAAPFGYIIVAVLGALQVTGEYASGQIRSSLTATPHRGRLLMAKAAVVAVFAFFLGLLSTMATWAVTVPFLKDDAGSITDSEYLGFFWGSGLAFAAIALMGLAYGFLLRSTAGAITTVVVVLFVIMVPLQMMASQWEWAKELAGLLPTSADAAITDPFAVANTWGVEDTATFLSQAQTALIFLAWTVLPLPIAAAIFLTRDA$","ABC transporter transmembrane protein","Membrane, Cytoplasm, Extracellular","putative ABC transporter transmembrane protein","ABC transporter; integral membrane subunit","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[40-62]?$ $\"[81-101]?$ $\"[122-144]?$ $\"[163-183]?$ $\"[188-208]?$ $\"[254-274]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-49% similar to PDB:1BF2 STRUCTURE OF PSEUDOMONAS ISOAMYLASE (E_value = );","No significant hits to the Pfam 21.0 database.","","ABC transporter transmembrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2144","2320182","2319229","954","7.92","2.32","33324","ATGATCGAGGCACGTGGATTAACGAAGCGCTACGGCGACAAGGTTGCTGTAGACAACATCTCTTTCACCGTCGAGCCGGGCACCGTTACCGGCTTCCTGGGCCCCAACGGCGCAGGCAAGTCCACCACCATGCGCATGATCATGGGCCTGGACAAGCCCACGACCGGCACCGTGACCGTGGCCGGCAAGAAGTACAAGGACCTCAACGCCCCGCTGTGCACCGTCGGTGCCCTGCTGGACGCCAAGGGCCTGCACGGATCGCAAACGGCCCGCACCCACCTGACGCAGCTGGCTGTGTCCAACGGCATCCCCGTCAACCGGGTTGACAAGGTCCTGGACATGACCGGACTCACCTCGGTGGCCAAGAAGCGGGTCAAGGGGTTCAGCCTCGGGATGGGGCAGCGTCTGGGCATCGCCGCCGCCCTCCTGGGAGACCCCGACATCCTCATCTTCGATGAGCCCGTCAACGGTCTGGACCCCGAAGGCGTCATCTGGGTTCGCCAGATCTGCCGCTCCCTGGCGGCCGAGGGGCGCATCGTCTTCATCTCCTCCCACCTCATGGGTGAGATGGCCCAAACAGCCGATCGCCTCATCGTCATCGGCCGCGGCCGCATCCTCAGCACCGGTCCCGTGACCGACGTCATCGCCTCGGCCACCTGCGACACCGTGCGCGTCGCCTCCCCCCAGGCCACCGACCTCGCCGACCTCCTGGCCTCCCAGAGGATCGCCGTCGAGACCCCGGAGCGTGGCGTGCTCACCCTGACCGCCGCCCCTGCCGCTCGCATCGGCGAGCTCGCCGCCGTCCACGGCATCGTCCTGCATGAGCTGACCACCATCAAGGCCAGCCTCGAGGACGCCTACCTCGAGCTCACCGGCGGCAACACCGAGTACAACACCAGCATCCCCAGGGGCCAGGCTGACCAGCCGGTCGCCCAGCAGCACGCGTTGCGTTGA","MIEARGLTKRYGDKVAVDNISFTVEPGTVTGFLGPNGAGKSTTMRMIMGLDKPTTGTVTVAGKKYKDLNAPLCTVGALLDAKGLHGSQTARTHLTQLAVSNGIPVNRVDKVLDMTGLTSVAKKRVKGFSLGMGQRLGIAAALLGDPDILIFDEPVNGLDPEGVIWVRQICRSLAAEGRIVFISSHLMGEMAQTADRLIVIGRGRILSTGPVTDVIASATCDTVRVASPQATDLADLLASQRIAVETPERGVLTLTAAPAARIGELAAVHGIVLHELTTIKASLEDAYLELTGGNTEYNTSIPRGQADQPVAQQHALR$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Membrane","ABC transport protein","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[128-169]T$	Q82JA3_STRAW_Q82JA3;
PF00005	$\"[27-203]T$	ABC_tran
PS50893	$\"[2-227]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[26-204]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-231]T$	no description
PTHR19222	$\"[2-217]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[2-217]T$	ABC TRANSPORTER

","BeTs to 17 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 5.3e-27. IPB013563A 16-50 IPB013563C 125-152 IPB013563D 179-231***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 3.7e-26. IPB005074C 16-63 IPB005074D 116-159***** IPB005116 (TOBE domain) with a combined E-value of 5.1e-11. IPB005116A 34-50 IPB005116D 148-167***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.4e-08. IPB010509B 27-52 IPB010509D 123-167***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.3e-07. IPB010929K 14-58 IPB010929M 125-171 IPB010929A 26-45","","","-54% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 8.4E_28);-50% similar to PDB:1V43 Crystal Structure of ATPase subunit of ABC Sugar Transporter (E_value = 2.9E_20);-50% similar to PDB:1VCI Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3 complexed with ATP (E_value = 2.9E_20);-50% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 2.9E_20);-52% similar to PDB:1Q12 Crystal Structure of the ATP-bound E. coli MalK (E_value = 5.0E_20);","Residues 27 to 203 (E_value = 2.9e-41) place ANA_2144 in the ABC_tran family which is described as ABC transporter.","","transport protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2145","2321560","2320817","744","4.64","-21.29","25906","GTGGGGTGGGTGAGGGTGGTACCTGACCAGCCTGCGGTGCCACTCTCCAAACCCCGCAAGCTGTCAGCACTCCCGACGAGGAACTGGGCTGCCGGTGGTCAGACAAGATCGGTTGCCTCACCCACTATGAAGGCGTGGGGTCAGGGGTGCTCGCGCCCGGGTGTGTCACCGTCGATTGACGGCGCCGAGGGTGACGCTGATGTGGTGGGGCAGGACCGGGTCTGGGGTGGATCGTTGGGTGGCCAGGAAGAGGCCGGCTCCCTTGAGGTCGTTGACGAGGTCCTCGGGCGCGACGAGGTGGTGCTCGGAGACGTGCTCCTGGTCGCGGCAGCGCAGGATGGTGCGTCGCCGGCGACCCACCTGGTCGATCTCCTCGGTGAGGTACGTATCTGGCTGGAGCTGGATGGTGCTGGTTTCAGGCGCCTCTGGGAGTACGTGATCGATGGAGGTGATGAGGGTTCCGCCGATTGCCATGTGGGCGGCCATGCATCGTATGGCTGCTCGTCGCTGCTCAGGATTCAACAGACTGATGGATGCCATGGGGAGGCAGACCGCCTTGAACAACTCCTTGATGTCGAAGGAGACCATGTCCGCCTGCCGGAGTTCGATCCGGTCTGCAGCTCCCGACTGGATGGCCCGCCGTTCTTTCAGCCGGTCGGCGAGGAGGCTGAGCACGTCGATGCTGATGTCTGTGGCGAGCACGTGGTGTCCCGCGGCTGCGATGGGCACAGTGGTGCGTCCTGA","VGWVRVVPDQPAVPLSKPRKLSALPTRNWAAGGQTRSVASPTMKAWGQGCSRPGVSPSIDGAEGDADVVGQDRVWGGSLGGQEEAGSLEVVDEVLGRDEVVLGDVLLVAAAQDGASPATHLVDLLGEVRIWLELDGAGFRRLWEYVIDGGDEGSADCHVGGHASYGCSSLLRIQQTDGCHGEADRLEQLLDVEGDHVRLPEFDPVCSSRLDGPPFFQPVGEEAEHVDADVCGEHVVSRGCDGHSGAS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-47% similar to PDB:1N7D Extracellular domain of the LDL receptor (E_value = );-47% similar to PDB:2FCW Structure of a Complex Between the Pair of the LDL Receptor Ligand-Binding Modules 3-4 and the Receptor Associated Protein (RAP). (E_value = );-52% similar to PDB:2GS9 Crystal structure of TT1324 from Thermus thermophilis HB8 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2147","2321661","2322851","1191","6.73","-2.26","43293","GTGGTGAGTAACTTCCTAGATGCCATCAGAACCCACTCCCACTGGTGGCCGGGCACGCATCTACGGAGCGCCACTCGAACTCAGCGGCGATATGCCGCCATTGGCACTATGGTTGGTGTCATCAACATGACACTCATGCTCACCCTTGTCACATCACCTACCCCAGAGCGCCTCTTTTTTCTTCTCTTAACAGTTGTTGCTCTATTCCTGATCCCCATATTCCCCATATGGGGTTCTCTCGGTTATCTGACCCTATGGATCGTGCTTCTTCAGGTTCCACACGTTCCCGCCAGCGACATGACCATCACCAACGCCGCCTTTTTTTTCTTCTTGGCGACATTTCTTCCCCTACGGGTGGCACTCACTCTCGCGTTAGTCATCCCAGCGGCGCTCATCATACCAACAGGACCCCTTCCGGATGCAGTTTCTTATTTGTTCCTCGCAGCCTGCACCCTTCTTCCCGGATCTATACTGCGTCACACGGAGGCATCGTTAAGAGAAGAAGTATCAACCGCCACAGAGAAGCTGAAGTCCATCCGCTCCGAAATTGCACGGGAAATGCATGATCTCGTCGCCTACTCGATGTCCCAGACCGCCTTGCGGGCGCAACGCGCGGCTGCAGATCCCTCCTATCCCGTCGCCGCTCAGCAGGAGTTCGCCGCGATCGAGTCCACCGCGGCCGACGCACTTCACGAGCTGCGCCTCGTGCTGCGAGCCCTAAGAAGCAACGAGGACGAGCACACCGATCATGCACACACCACCGGATTGGGAACCGTCGTACTGGATCTTGAGGAGTCCGTGCGCGCCGTCGCCGACGACCTCTCCGCGTCCGGCTACTCCGTGACCTACCAGTGCAGGGGAGACGGGCACTACACTCGCCTTCAAGCTGCCATCCTCTCCCGGGTGCTTCGGGAGATGTGCTCCAATGTTCTGAGACATGCGGATCACGATCAACCGGTCACCATCACCCTGAGTCAAGACGCTCACAAGGCTCGCCTGGTTGTGACCAATGGGGTCCTCTCTTCGCATCACAGGTTTCCTTCCTCCGGGATGGGGATTCTTGGTATGAAGGAGAGGCTCTCAACCGTCGGCGGCTCACTGGATACGTTGATGGACAACGGCACCTGGCTGACATCCGCCTCCATCCCTCTCTCACAGCCACCCACCCGAGTCATCGAGGATGAGTCATGA","VVSNFLDAIRTHSHWWPGTHLRSATRTQRRYAAIGTMVGVINMTLMLTLVTSPTPERLFFLLLTVVALFLIPIFPIWGSLGYLTLWIVLLQVPHVPASDMTITNAAFFFFLATFLPLRVALTLALVIPAALIIPTGPLPDAVSYLFLAACTLLPGSILRHTEASLREEVSTATEKLKSIRSEIAREMHDLVAYSMSQTALRAQRAAADPSYPVAAQQEFAAIESTAADALHELRLVLRALRSNEDEHTDHAHTTGLGTVVLDLEESVRAVADDLSASGYSVTYQCRGDGHYTRLQAAILSRVLREMCSNVLRHADHDQPVTITLSQDAHKARLVVTNGVLSSHHRFPSSGMGILGMKERLSTVGGSLDTLMDNGTWLTSASIPLSQPPTRVIEDES$","Two-component system sensor kinase","Membrane, Cytoplasm","putative two-component system sensor kinase","two-component system sensor kinase","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[294-368]T$	HATPase_c
SM00387	$\"[294-388]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[180-245]T$	HisKA_3

noIPR
unintegrated

unintegrated
tmhmm	$\"[31-53]?$ $\"[59-90]?$ $\"[100-134]?$ $\"[140-158]?$	transmembrane_regions

","BeTs to 5 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 1.7e-08. IPB011712A 178-195 IPB011712B 299-319","","","No significant hits to the PDB database (E-value < E-10).","Residues 180 to 245 (E_value = 6.8e-09) place ANA_2147 in the HisKA_3 family which is described as Histidine kinase.Residues 294 to 368 (E_value = 1.2e-05) place ANA_2147 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","two-component system sensor kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2148","2322848","2323552","705","5.42","-6.59","24764","ATGATCAGTATTGGTATTGCGGACGACGACGCCCTGGTTCGTCAGACGCTGACGGATCTTCTCTCCAAGAACGACGACATCGTCGTTGCCTGGACAGCCAAGGACGGCCAGGAGGCGCTCGACCTCTTCCACTCCTCGGAGGTCGAGAGCAGGGTCCAAGCCGTTCTCGTGGACGTCCAGATGCCCAAGATGGATGGCCTCGCACTGGCTCAAGCACTTCTCGAGGAGAAACCAGACATTGCGATCCTCATCCTGACGACTTTTACAGCCGACTCCATCGTTGACAAAGCCATGGCACTGGGGGTACGCGGATTCGTTGCCAAGGAGGATGGTGCCTCATCCTTGGCCGGCGCCATCCACCAGGCGGTCGCAGGCAATCTCGTCCTGTCACCAACATCATCGGCCATCATCAGCGACCAGGCCAGACTGTGGGCAAGCGGCTCCTCCCGCCCCTCGGAGTCCATCCCGGTTCCGACTCACGCGCAGCAGCCCCCTTCCCCCCTCCCCCACGGGGTCACCCTCTCAGAACGAGAACGGGAGGTGCTGACACTTGTCGTGGACGCCAAGACCAACAAGCAGATTGCCACTCGATTGAGAGTCAGTGAGGCCACGGTCAAGACTCACGTATCCGCCATTATCGCCAAGCTCGGAGTCCAAGACCGGGTGGGAGCAGCCGTGTACGCCCTGCAGCACAATCTGGTGTGA","MISIGIADDDALVRQTLTDLLSKNDDIVVAWTAKDGQEALDLFHSSEVESRVQAVLVDVQMPKMDGLALAQALLEEKPDIAILILTTFTADSIVDKAMALGVRGFVAKEDGASSLAGAIHQAVAGNLVLSPTSSAIISDQARLWASGSSRPSESIPVPTHAQQPPSPLPHGVTLSEREREVLTLVVDAKTNKQIATRLRVSEATVKTHVSAIIAKLGVQDRVGAAVYALQHNLV$","Two-component response regulator","Cytoplasm","response regulator CstA","two-component response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[174-231]T$	Q8CNR2_STAEP_Q8CNR2;
PR00038	$\"[174-188]T$ $\"[188-204]T$ $\"[204-216]T$	HTHLUXR
PF00196	$\"[171-228]T$	GerE
SM00421	$\"[171-228]T$	HTH_LUXR
PS50043	$\"[167-232]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[2-119]T$	Q9RPE7_CORDI_Q9RPE7;
PF00072	$\"[2-120]T$	Response_reg
SM00448	$\"[2-119]T$	REC
PS50110	$\"[3-123]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[147-234]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[2-127]T$	no description
PTHR23283	$\"[2-123]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF31	$\"[2-123]T$	SENSOR HISTIDINE KINASE

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 3.3e-22. IPB000792 174-220***** IPB005143 (Autoinducer binding domain) with a combined E-value of 2.3e-13. IPB005143B 174-217","","","-49% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 2.2E_21);-49% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 2.2E_21);-53% similar to PDB:1DZ3 DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A (E_value = 6.7E_10);-53% similar to PDB:1QMP PHOSPHORYLATED ASPARTATE IN THE CRYSTAL STRUCTURE OF THE SPORULATION RESPONSE REGULATOR, SPO0A (E_value = 6.7E_10);","Residues 2 to 120 (E_value = 1e-20) place ANA_2148 in the Response_reg family which is described as Response regulator receiver domain.Residues 171 to 228 (E_value = 3.8e-20) place ANA_2148 in the GerE family which is described as Bacterial regulatory proteins, luxR family.Residues 173 to 216 (E_value = 0.00019) place ANA_2148 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 173 to 218 (E_value = 5.1e-06) place ANA_2148 in the Sigma70_r4 family which is described as Sigma-70, region 4.","","regulator CstA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2149","2325795","2323936","1860","4.76","-27.39","63466","ATGGGGGACACAGGTGGCCTTCGTAAGATGCCGCGCATGACAAGAACACTAAGGCAGCGCCCGGCTGATTCGGGGCGCGCCATCGCGGCGCAGGCGTCCGCGCAGTCCTCGATGACAGGTGGCGCATCGCGCCGTCGTCGCACGAGCATCGGTGTGCTGGCGGTCCTCGTCGGCGGATGCCTGAGCGCCTGCGGGACGGGACTGGCCCCCGCAGCGGGCGGCTCGGCCACCGTCGCGGGCCCGATTCCCTCCGGCCTGGAGTCCTTCTACCGCCAGGCCGTCACCTGGTACCCCTGCGCCGCCACCGACGGCGTGGAGAAGGCCTCGGAGACGACCGCCCGGGCGAGCGCCTCCACGACGGCCGCAACGGCCTCGGCGCAGGCAACCGCCGCCCCGAGCTCCGACGGCGCGACCGGCGCGACCGGGACGGCCGGCTCCTTGGAGGAGGAGACCGACACGGCCACCTTCAGCTGCGCCGTCATCACCGTCCCCCTGGACTACGCCAACCCCAAGGGCGAGACCATCTCGATCGCCGTGAAGAAGCGCGCCGCCACCGGCGGCCACGCCCAGGGCGCCCTGTTCATCAACCCCGGTGGCCCCGGCGACTCCGGGGTCTCCTTCGCCGAGCGGGCGGGCAACGCCTTCAGCCCCGATCTGCTCAACGCCTACGACATCATCGGCTTCGACCCGCGCGGGGTTGGCTCCTCCACGGCCATCACCTGCTCCAGCGACGATGACTCATCCTCCAGCACCGCCGAGCCCTCCACCTCCGCTGGGGCCACGGCCTCGCCATCGGCAGGAACGGAGGCCTCGGGCGGCGAGTCCTACGAGGAGTGGGCGGAGTCAACTCGGCAGTCCTTCCAGGAGCTGACCGAGCAGTGCGCCTCCCACACCGAGCCCGCCGCCCTGCTCGACCACGTCGACACCGTCTCCGCAGCCCGGGACCTCGACATCCTGCGGGCGCTGGCCGGCCAGGAGAAGCTCAACTACCTGGGATTCTCCTACGGCACCTACCTCGCCTCCGTCTACGCTGAGACCTTCCCCGGCAACACGGGCCGCATGGTGCTCGACGGCGCCATCGACCCCTCCCTGTCCCTCGCCGAGCAGGGACTGGGGCAGGCCAAGGGCTTCGAGCAGGCGCTGCGCACCTACGTTGACTACTGCCAGAACTCCACCGGCTGCCCGCTGAGCGGGGGCACCGACGCCGGAGTCCAGCAGATCCGCGACCTCATCACTTCCGCCAACAGCACGCCCCTGGCGACCGGTGACCCGAACCGCACCGTGACCGGCTCGGACATCGTCGCCGCCCTGAGCGAGTACCTCTACACCACCGAGCAGAACTGGGAGCCCCTGAACAAGGCCCTCGACCAGGCCATCAACCACCGCGACGGCTCAGCCTTCGTGGCCTCCGAGGAGCAGGACACCTCCTCGAAGGACGACGGCGGCGGTGCCTTCCAGGCCGTCACCTGCCTGGACTACCCGGTGGAGGGTGACAAGACGACCTGGGCCGCGCAGTACGAGCAGGCTAAGCGCGAGGCCCCGGTCTTTGCGGACTCCGCGGTCGGCATGGACCTGGTGTGCAGCGTGTGGGGGCACAACGGGACCCGCAAGCCCACGCAGATCCATGCCCGCGGGGCTGCGCCGATCCTCGTGGTGGGAACTACCGGGGACCCGGCCACCCCGTACGCCTGGTCGAAGTCCCTGGCCGAGCAGCTCGACTCCGGCCAGCTGCTGACCTGGGAGGGCAATGGGCACACCGCCTACGGCGGCGACGCCTCCTGCGTCAACGACGCCGTCGACGCCTACCTGATCTCCGGCACCATGCCCAAGAAGGGCCTGACCTGCCACGGCAACGAGTAG","MGDTGGLRKMPRMTRTLRQRPADSGRAIAAQASAQSSMTGGASRRRRTSIGVLAVLVGGCLSACGTGLAPAAGGSATVAGPIPSGLESFYRQAVTWYPCAATDGVEKASETTARASASTTAATASAQATAAPSSDGATGATGTAGSLEEETDTATFSCAVITVPLDYANPKGETISIAVKKRAATGGHAQGALFINPGGPGDSGVSFAERAGNAFSPDLLNAYDIIGFDPRGVGSSTAITCSSDDDSSSSTAEPSTSAGATASPSAGTEASGGESYEEWAESTRQSFQELTEQCASHTEPAALLDHVDTVSAARDLDILRALAGQEKLNYLGFSYGTYLASVYAETFPGNTGRMVLDGAIDPSLSLAEQGLGQAKGFEQALRTYVDYCQNSTGCPLSGGTDAGVQQIRDLITSANSTPLATGDPNRTVTGSDIVAALSEYLYTTEQNWEPLNKALDQAINHRDGSAFVASEEQDTSSKDDGGGAFQAVTCLDYPVEGDKTTWAAQYEQAKREAPVFADSAVGMDLVCSVWGHNGTRKPTQIHARGAAPILVVGTTGDPATPYAWSKSLAEQLDSGQLLTWEGNGHTAYGGDASCVNDAVDAYLISGTMPKKGLTCHGNE$","TAP domain protein","Extracellular","proteinase","protease","TAP domain protein","","Brede D.A., Faye T., Johnsborg O. Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii. Appl. Environ. Microbiol. 2004. 70(12):7303-7310. PMID: 15574930","","","

InterPro
IPR013595
Domain

Peptidase S33, tripeptidyl-peptidase C-terminal
PF08386	$\"[513-615]T$	Abhydrolase_4

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[187-603]T$	no description
tmhmm	$\"[52-72]?$	transmembrane_regions

","BeTs to 3 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 223 to 601 (E_value = 3.4e-16) place ANA_2149 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.Residues 513 to 615 (E_value = 7.2e-35) place ANA_2149 in the Abhydrolase_4 family which is described as TAP-like protein.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2150","2327445","2325883","1563","9.92","13.70","53227","GTGAGGCAGACACTCGTCTTGCTGCTGATCTGCACCGCCAGCTTCATGAACGTCCTGGACGTCACGGTCGTCTCCGTCGCGCTGCCTGACATGGGGGCCGCGCTGGGGGCGTCGCTGAGCGAGCTCCAGTGGGTGGTCAACGCCTACACCCTGCCGCTTGGGACACTCCTCATGTCGGCGGCGACGCTGAGCGGATCGATGGGGCGGCTGCGCCTCTTCCGCTGGGGGGTTGTCCTGTTCACGGCCGGCTCCCTGGTCTGCGCGCTGGCGCCGTCGGTCGGTGTCCTGGACTGGAGCCGCTTCATTCAGGGGGTCGGTGGCGCGATCTTCCTGGGCGTCGGCGTCCCCATGATCTCGGACCGCTACCAGGCCGGCCCCGCCCGGGCGCGGGCGATCGGTGTCTACGGCGCGGTCTCCGGTGCGGCGATCGCCCTGGGACCGCTCCTTGGCGGAGGGCTCGTGCTGATGGCGGGCTGGCGCTCGATCTTCTGGGTCAACGTCCCGGTGGGCCTGGCGGTCTGGCTCGGATCGCGCTGGGTTCCCGAGGTCGGCGCGGACCGGGGCGGCGCTGCGGGCAAGGGGACATCCAGGAAGGTCGACTGGCCGGGCACGGTGCTGTGCGTCGCCATGATGGGGGCGCTCACACTGGCGCTCCTCCAGGGCAACACGTGGGGATGGGCCTCGCCCGTGATCGTCTCCCTGCTGGCCGGCTCGGCGGTGCTGCTCGCCGCGTTCTGCCTCGTCGAGAGACGATCGGCCAGCCCCATGGTCGACGTCTCGATCCTCACCGAACCCACCTATGCCGGCAGCGTCCTGGTCGGCTTCATCATCCAGGCGGCCCTCATCGGGCCAATGGCCTTCCTGTCCCTGTACGCGCAGAACATCTACCGGCTCACCCCCGCCCAGACCGGACTGTGCTTCCTGCCCTTCAGCGCCTCCGCCCTCATCGTGGCCGCCACCTGCGGGGGAGCGGTCAGACGCCACGGAGCCAGGGCGAGCCTGCTGGGAATCGTGCTGGGCGGCGTCATCGGCTCCTGCCTGCTCATGCTCCTACGCGGATCGAGTACCTGGCTGGTCCTCATTCCCGGGCTCGTCCTGGCGGGGGCCGCCACCGGGGCCACAGGGACGATCGTCAACCAGCTGGCGGTCTCCTCGGCCGATGAGGACACCGCGGGGATGACCTCGGGCTTCTCCGCGTCGGCCCGGCAGCTCGGCATCGTCATGGGGGTCGCGGTCATGGGTGTGAGCTATGAGCGCGTCATCCGGAGCGTGATGACGATGGCCCCGCAGATCGGTGTCCTGGGGCGGACTGCGGATCGGGAGCGTCTCATCTCCCTGGTGGCCTCCGGCAAGGGGCTGCGGGCACTGGACGGATGGCCCACCGCCATGACGGCTGACATGCGCTCCCACCTGGCACCGCTGGTCCGCTCCGCCACGGATGCGGGGCTCAGCGTCAGCCTGGGGGTGGGGGCCGCGGTGATGCTCGCCGTCGCGATCCACCTGGCCCTGACGGTCCCCGGACGGCGCGCAAAGAGCGAGGTCTCACACCTGTTCGCCTCGTGA","VRQTLVLLLICTASFMNVLDVTVVSVALPDMGAALGASLSELQWVVNAYTLPLGTLLMSAATLSGSMGRLRLFRWGVVLFTAGSLVCALAPSVGVLDWSRFIQGVGGAIFLGVGVPMISDRYQAGPARARAIGVYGAVSGAAIALGPLLGGGLVLMAGWRSIFWVNVPVGLAVWLGSRWVPEVGADRGGAAGKGTSRKVDWPGTVLCVAMMGALTLALLQGNTWGWASPVIVSLLAGSAVLLAAFCLVERRSASPMVDVSILTEPTYAGSVLVGFIIQAALIGPMAFLSLYAQNIYRLTPAQTGLCFLPFSASALIVAATCGGAVRRHGARASLLGIVLGGVIGSCLLMLLRGSSTWLVLIPGLVLAGAATGATGTIVNQLAVSSADEDTAGMTSGFSASARQLGIVMGVAVMGVSYERVIRSVMTMAPQIGVLGRTADRERLISLVASGKGLRALDGWPTAMTADMRSHLAPLVRSATDAGLSVSLGVGAAVMLAVAIHLALTVPGRRAKSEVSHLFAS$","Permease of the major facilitator superfamily","Membrane, Extracellular","drug transporter","integral membrane efflux protein","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR001411
Family

Tetracycline resistance protein TetB
PR01036	$\"[9-33]T$ $\"[69-91]T$ $\"[131-155]T$	TCRTETB

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[6-509]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[10-418]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[1-203]T$ $\"[253-420]T$ $\"[482-513]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57	$\"[1-203]T$ $\"[253-420]T$ $\"[482-513]T$	DRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[5-27]?$ $\"[46-66]?$ $\"[75-95]?$ $\"[99-119]?$ $\"[134-156]?$ $\"[162-180]?$ $\"[201-219]?$ $\"[225-247]?$ $\"[271-291]?$ $\"[305-325]?$ $\"[332-352]?$ $\"[358-378]?$ $\"[399-417]?$ $\"[483-503]?$	transmembrane_regions

","BeTs to 21 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 10 to 418 (E_value = 3.1e-44) place ANA_2150 in the MFS_1 family which is described as Major Facilitator Superfamily.","","transporter ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2151","2328544","2327678","867","4.91","-15.20","29978","GTGAGTGCCGGTGGTGGGTCAGTGACACCGGAGCCGTCGGACGGGCCGACGTCGTCGGCCTGCCTGGAGGAGCTGCTCGCCTGCGGGGTGGCTGCGGTCCGCCAGGCGGCCGCCTTCGCCCTGAACCCGGGTGAGGAGCTGCGCGTCGAGGCCAAGGCGCACCGCAACGACCTGGTCACCCAGGTCGACCGCGGCGTCGAGGAGCGCATCGCCGGCCACCTGGAGGCCACGGGCGTCCCCATCCACGGCGAGGAGGCGCACCGCGTCGAGGACTTCGAGACCTACCGCGGGCGGGCCTGGGTCCTCGACCCCATCGACGGGACCCTCAACTACGTGGCCACCCACCGCGACTGGGCCATCTCCCTGGCCCTGGTCGACGACGGCGCGCCCACGGTCGCCGTCCTCGCCGACCCCGTGGCCGACCGGCTCTACACGGCCATCCGCGGGCGGGGCGCATGGGTGCAGCCGCTTCTGGCGGGCTCGGCGGGCACCGACGACGCGGCGCGGCGACCCCTGGAGCAGCTGGAGGACCTGCCCTTGAGCGAGGGCATGCTCATCGCCCACTACCAGCTCACGCAGGATGCGGGCATCGGCCAGGCCATCGAGGCCTCGCGCGGCATGCGCTGCTACGGGGCGGCCGCCCTGGAGATGGCGGAGGTGGCCGCGGGCGGCGCGGTCGTCTACGCCCAGCCGCGACTCCAGCCCTGGGACGTTGCGGCCGGTGCGCTGCTGTGCGCCGAGACCGGCGCGGCCCTGACCCGGATGGACGGGGCGCCCTTCGACGTGCGCCGCGCCGGCTCGCTCCTCGTGGGCACCCCGACCGCCCACGCCGAGGTGCTGGGGCACCTGCGCGCCGTCGGGGCCTGA","VSAGGGSVTPEPSDGPTSSACLEELLACGVAAVRQAAAFALNPGEELRVEAKAHRNDLVTQVDRGVEERIAGHLEATGVPIHGEEAHRVEDFETYRGRAWVLDPIDGTLNYVATHRDWAISLALVDDGAPTVAVLADPVADRLYTAIRGRGAWVQPLLAGSAGTDDAARRPLEQLEDLPLSEGMLIAHYQLTQDAGIGQAIEASRGMRCYGAAALEMAEVAAGGAVVYAQPRLQPWDVAAGALLCAETGAALTRMDGAPFDVRRAGSLLVGTPTAHAEVLGHLRAVGA$","Inositol monophosphatase family protein","Cytoplasm","extragenic suppressor protein SuhB and tomyo-inositol-1(or 4)-monophosphatase","inositol monophosphatase family protein ","Inositol-phosphate phosphatase","","Neuwald A.F., York J.D., Majerus P.W. Diverse proteins homologous to inositol monophosphatase. FEBS Lett. 1991. 294(1):16-18. PMID: 1660408York J.D., Ponder J.W., Majerus P.W. Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(11):5149-5153. PMID: 7761465Berridge M.J., Downes C.P., Hanley M.R. Neural and developmental actions of lithium: a unifying hypothesis. Cell 1989. 59(3):411-419. PMID: 2553271","","","

InterPro
IPR000760
Family

Inositol monophosphatase
PD023420	$\"[60-113]T$	Q740P9_MYCPA_Q740P9;
PR00378	$\"[95-114]T$ $\"[215-230]T$ $\"[232-250]T$	INOSPHPHTASE
PTHR20854	$\"[44-49]T$ $\"[67-283]T$	INOSITOL MONOPHOSPHATASE
PF00459	$\"[21-288]T$	Inositol_P
PS00630	$\"[236-250]?$	IMP_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.540.10	$\"[20-166]T$	no description
G3DSA:3.40.190.80	$\"[200-285]T$	no description
PTHR20854:SF4	$\"[44-49]T$ $\"[67-283]T$	MYO INOSITOL MONOPHOSPHATASE

","BeTs to 17 clades of COG0483COG name: Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase familyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0483 is aom-kzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB000146 (Inositol phosphatase/fructose-1,6-bisphosphatase) with a combined E-value of 2.2e-07. IPB000146B 96-119 IPB000146D 216-269","","","-43% similar to PDB:1VDW A hypothetical protein PH1897 from Pyrococcus horikoshii with similarities for Inositol-1 monophosphatase (E_value = 7.0E_10);","Residues 21 to 288 (E_value = 3.8e-49) place ANA_2151 in the Inositol_P family which is described as Inositol monophosphatase family.","","suppressor protein SuhB and to myo-inositol-1(or 4)-monophosphatase homolog lin1054","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2153","2330007","2328541","1467","7.90","3.23","52516","ATGCCCCTCACGCCGCCGCCCGCCGATTCCACCTCGGCGGCCGAGTCCTCGCCGCCTCAGCGGCCTGACCTCGACCAGATGGTGGACCACGACGCCGAGCCTCAGCTCCAGCGCCACCTCACCAACCGCCACGTCCAGCTCATCGCCATCGGCGGGGCCATCGGAACCGGGCTGTTCATGGGGTCGGGGAAGACGATCTCCCTGGCCGGCCCCGGTGTGTTCCTCGTCTACGCGGTCATCGGCGGCATCCTCTTCCTGGTCATGCGGGCCCTGGGCGAGGTGCTGCTGTCCAACCTGTCCTACAAGTCCTTCGCCGACGTCGCCCACGACCTCATCGGGCCGTGGGCGGGCTTCTTCGTGGGCTGGACCTACTACGTGTGCTGGCTGGTGACGGCCGTTGCCGAGGTCATCGTCATCACCGGGTACGTGAGGTACTGGTGGCCGGACCTGCCGTTGTGGATCGTGCCGGTGGCCACCGTGGTCCTGCTGTTCAGCCTCAACCTCGCCACCGTCAAGGCCTTCGGGGAGATCGAGTTCTGGTTCTCCATCATCAAGATCGTGGCCATCATGGCGCTCGTCGTCGTCGGTGTCCTCATGGTGCTGCGCGGGTTCACGGCGCCCAACGGCGCCCACGCCCAGTTCTCCAACATCTGGAGCGGCGGATTCTTCCCCAACGGTGCGAGCGGGTTCTTCGGGGCCTTCCAGATCGCCATCTTCGCCTTCGTGGGCACCGAGCTTGTGGGGACCGCGGCCGCCGAGGCCAAGGACCCGGAGGTGACCCTGCCCCGGGCCATCAACGCCATCCCGGTGCGCATCGTCCTGTTCTACCTGGGGGCGCTCGCGGCCATCATGGCCGTCACCCCGTGGCATGAGATCAACCCCGAGGCAAGCCCCTTCGTGGCCATGTTCGCCCTGGCGGGGCTCGGCGTGGCCGCCAGCGTCGTCAACTTCGTGGTGCTCACGGCTGCGGCGTCGTCGGCCAACTCCGGGGTCTACTCCACCTCCCGGATGCTCTTCGGCCTGTCCTGGGCGGACAACGCCCCCCACATCTTCCGCAAGCTGACGGCCCGTTCGGTGCCGGGAGTGTCCCTAGCCGTCACCTGCGCCAGCCTGCTCACCTCGATCCCGCTGCTCTACACCTCCAAGTCCATCATCGCGGCCTTCACGACGGTGACCACGGTGGCCAGCGTCCTGTTCATCCTCGTGTGGTGCGTCATCGTCGTGAGCTACCTGCGCTTCCTCACCCTGCGGCCCGAGCTTCACCGCGCCAGCACCTTCCGCCTGCCCGGTGAGCGTGGGGCGGCCTGGCTGTGCCTGGCCTTCTTCGCCTTCGTCATCTGGACCCTCACCCAGGCCCACGACACCCGCATCGCGGTCTTCGCCTCGCCCCTGTGGCTGGTGGTGCTGGGCGTGGCCTGGCTCGTCCACAGCAGCCGGCTCGCCAGGCAGCAGGAGCTCCAGTCGTGA","MPLTPPPADSTSAAESSPPQRPDLDQMVDHDAEPQLQRHLTNRHVQLIAIGGAIGTGLFMGSGKTISLAGPGVFLVYAVIGGILFLVMRALGEVLLSNLSYKSFADVAHDLIGPWAGFFVGWTYYVCWLVTAVAEVIVITGYVRYWWPDLPLWIVPVATVVLLFSLNLATVKAFGEIEFWFSIIKIVAIMALVVVGVLMVLRGFTAPNGAHAQFSNIWSGGFFPNGASGFFGAFQIAIFAFVGTELVGTAAAEAKDPEVTLPRAINAIPVRIVLFYLGALAAIMAVTPWHEINPEASPFVAMFALAGLGVAASVVNFVVLTAAASSANSGVYSTSRMLFGLSWADNAPHIFRKLTARSVPGVSLAVTCASLLTSIPLLYTSKSIIAAFTTVTTVASVLFILVWCVIVVSYLRFLTLRPELHRASTFRLPGERGAAWLCLAFFAFVIWTLTQAHDTRIAVFASPLWLVVLGVAWLVHSSRLARQQELQS$","D-serine/D-alanine/glycine transporter","Membrane, Cytoplasm","transport protein for D-alanine, D-serine, andglycine","K03293 amino acid transporter; AAT family","amino acid permease-associated region","","Weber E., Chevallier M.R., Jund R. Evolutionary relationship and secondary structure predictions in four transport proteins of Saccharomyces cerevisiae. J. Mol. Evol. 1988. 27(4):341-350. PMID: 3146645Vandenbol M., Jauniaux J.C., Grenson M. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases. Gene 1989. 83(1):153-159. PMID: 2687114Reizer J., Finley K., Kakuda D., MacLeod C.L., Reizer A., Saier Jr M.H. Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria. Protein Sci. 1993. 2(1):20-30. PMID: 8382989","","","

InterPro
IPR002293
Family

Amino acid/polyamine transporter I
PTHR11785	$\"[31-484]T$	AMINO ACID TRANSPORTER

InterPro
IPR004840
Family

Amino acid permease
PS00218	$\"[69-99]T$	AMINO_ACID_PERMEASE_1

InterPro
IPR004841
Domain

Amino acid permease-associated region
PF00324	$\"[44-487]T$	AA_permease

noIPR
unintegrated

unintegrated
PIRSF006060	$\"[34-488]T$	High-affinity amino acid transporter
PTHR11785:SF30	$\"[31-484]T$	AMINO ACID PERMEASE (AAPA)
tmhmm	$\"[67-87]?$ $\"[99-119]?$ $\"[125-143]?$ $\"[153-173]?$ $\"[179-201]?$ $\"[222-242]?$ $\"[272-290]?$ $\"[300-320]?$ $\"[326-344]?$ $\"[359-379]?$ $\"[385-414]?$ $\"[435-453]?$ $\"[457-477]?$	transmembrane_regions

","BeTs to 4 clades of COG1113COG name: Gamma-aminobutyrate permease and related permeasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1113 is ----------rlb-ef----------Number of proteins in this genome belonging to this COG is 2","***** IPB004840 (Amino acid permease) with a combined E-value of 8e-73. IPB004840A 43-71 IPB004840B 167-186 IPB004840C 239-277 IPB004840D 321-360","","","No significant hits to the PDB database (E-value < E-10).","Residues 44 to 487 (E_value = 4e-113) place ANA_2153 in the AA_permease family which is described as Amino acid permease.","","protein for D-alanine, D-serine, and glycine (permease)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2155","2330199","2331770","1572","8.52","4.59","56562","GTGCCCAGCTGGGATCTGGCGATCTTCTCCGAGCTGGCCAAGGCCTACGCCCACTTCCAGACCCCGATCGTGCCGGTCAAGGGTGACGGATACAACCTCCTGGGTGACCACTTCCACCCGATCCTCATTCTGCTGGGGCCGATCTGGAGGCTCTTCCCCACGCCCCTGAGCCTGCTCATCACTCAGGACCTGCTGCTGGCGTTCTCGGCCTGGCCGCTGACCCGCCTGGCCAGCCGCCTGACGAATCAATGGGTGGCCGGCGGGCTGGGGCTCGTCTACGTCCTGTCCTGGGGGATGCAGGGGGCCGTGGCGGCGCAGTTCCACGAGATCGCCTTCGCGATGCCGCTGCTGGCCTATGCCTCGGTGGCCTTCGTGGAGCGGCGCTGGGGGGCGGTGACGGCCTGGTCAGTGCCCCTGGTCCTGGTCAAGGAGGACATGGGGCTGACGGTGCTCATGATCGGGGTGGCCGTCATCCTCACCTCAGCCGTCCCGGCCTGGTACCGCAGCTGCACGGTCATCCGGCCCGGTGACCGTGGGGCCGACGGCCTCAACGCCGCCGCTGGGAACGCTCCCAAGGACGAGGCCACCCGCAACCGGCATCGGGGGCTGCGCCTGGGCGTGGGCATGATCGTCGGCGGGATCGCGGCCTTCCTCTTCGCCATCCAGGTGTTCCTGCCGGCCTTCAACATCAACGGGGTGTGGGACTACGGCCTGGGCTCGCAGGACCAGCCCGCCTCACCCGACGCCCTGACCCAGAAGGCCACGGTGGTCGTCATGCTGATCCTCACCAGTGGGGTCGTCGGGGTCACCTCGCCGTGGCTGCTCGTGGTGCTGCCGACGCTGGCGTGGCGGTTCCTGGGGTCGGTGGAGTTCTACTGGGTGTGGGACAACTGGCACTACAACGCCACCCTCATGCCCATCGCGCTGGGGGCGCTGCTCGACGTCGTCGCCCGGCGCCGGGCCCACGGCTCCTACGTGGCCGACCGCCCCGTCAGGCAGGTGGGGGTCGATGGCCGAGCGGTCGTGGGGCGCTCCGCCCAGGCCGCCCCTGGCGCGAGCAGCCCTGATGAGTCCGACGTCGACGGCCCGCGCCGGAGCCCAACCGCCTTCCCCACCTGGCTCACGGTGCCGCTGCGGCACCGCTTCGTGGTGGCCACGAGCATCCTCACCACGGTGGCCACCGGGGTGCTGACCGCCCCCTACCTCCCGCTGTGGCAGGCCACCAACAAGAACTTCGACCCGCTCGCCGCCGAGGCCAAGCAGAGCGACGAGGCGAAGAGAACCGAGACGCATCGAGTGGCCGTCGCCCACGAGGCCATCGCCACCATCCCCGAGGGGGCCACGGTGGTCACCGACCTGTCCCTGCTGGCCTACCTGGTGCCCCGGGCCGAGGTCTCCTGGGTGGGCACGAGCGGCCCCGACAAGGAGTACATCGTCATGACCCCGACCAGCGCCAACCAGTGGGGCACCACCAATGCCGCCACCTGGGGCGAGCAGCACTCCAAGCAGGGGGCCACCTACACCGTCATCTTCAACAAGGACAACTACCAGATCGCCAAGCGCAATGGCTGA","VPSWDLAIFSELAKAYAHFQTPIVPVKGDGYNLLGDHFHPILILLGPIWRLFPTPLSLLITQDLLLAFSAWPLTRLASRLTNQWVAGGLGLVYVLSWGMQGAVAAQFHEIAFAMPLLAYASVAFVERRWGAVTAWSVPLVLVKEDMGLTVLMIGVAVILTSAVPAWYRSCTVIRPGDRGADGLNAAAGNAPKDEATRNRHRGLRLGVGMIVGGIAAFLFAIQVFLPAFNINGVWDYGLGSQDQPASPDALTQKATVVVMLILTSGVVGVTSPWLLVVLPTLAWRFLGSVEFYWVWDNWHYNATLMPIALGALLDVVARRRAHGSYVADRPVRQVGVDGRAVVGRSAQAAPGASSPDESDVDGPRRSPTAFPTWLTVPLRHRFVVATSILTTVATGVLTAPYLPLWQATNKNFDPLAAEAKQSDEAKRTETHRVAVAHEAIATIPEGATVVTDLSLLAYLVPRAEVSWVGTSGPDKEYIVMTPTSANQWGTTNAATWGEQHSKQGATYTVIFNKDNYQIAKRNG$","Uncharacterized membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","membrane protein-like","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-17]?$	signal-peptide
tmhmm	$\"[54-74]?$ $\"[84-104]?$ $\"[147-167]?$ $\"[205-225]?$ $\"[249-269]?$ $\"[271-291]?$ $\"[297-317]?$ $\"[382-402]?$	transmembrane_regions

","BeTs to 4 clades of COG3463COG name: Uncharacterized membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG3463 is ---pk--------c------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2156","2331886","2332500","615","11.78","9.86","19514","GTGACCCCCTCCCCCTCGGCAGCTGCCGCAGACTCCCCGCCGGCAGCCGGCTCCCCACGGGTGGCCGGGCGGCTGCCAGCCGTGGCTGCGTCCCCCTCTGCAGCCAGCTCCCCGCCGGCAGCCGGCTCCCCATCGGCAGCCGGGCGGGCCCCGTCCGTGACTGCCTCCCTGGCCCTGGTCGCCGCGGGCGGATGCGCGGGCACGCTGGTACGCGCGGCCCTGGAGCGGGCCTGGCCCGCCTCCCCCGGGCACCTGCCGGTCACGACCCTGGCCCTTAACGTCGTCGGGGCCCTCGCCCTGGGGCTGCTGCTCGGGGCGCTCGGCGAAGGCCGCCCCCGCCTGCGACTGGCCCTGGGCACGGGGGTGCTGGGCGGGCTGACGACGCACTCGACCTTCATCCTGGAGAGCCACCGGCTCCTGACCTCCAGCGGGGACGGCGGCCACCCGGTCCTCGGCGCCGCCTACCTGGTGGGGTCGATGGTGGCCGGGCTGGTGGCGGCCGGGCTCGGGCTGTGGCTGGCCGGCCGTCTGCGCCGCACGGGTCGCACGGGCAGTGTGGGCAGTGCAGGCCGAGTGGACCGCGCAGGCAGCGGCCGCCTCCCGGAGGTGTCATGA","VTPSPSAAAADSPPAAGSPRVAGRLPAVAASPSAASSPPAAGSPSAAGRAPSVTASLALVAAGGCAGTLVRAALERAWPASPGHLPVTTLALNVVGALALGLLLGALGEGRPRLRLALGTGVLGGLTTHSTFILESHRLLTSSGDGGHPVLGAAYLVGSMVAGLVAAGLGLWLAGRLRRTGRTGSVGSAGRVDRAGSGRLPEVS$","Camphor resistance CrcB protein","Extracellular","putative integral membrane protein","hypothetical protein predicted by Glimmer/Critica","Camphor resistance CrcB protein","","Hu K.H., Liu E., Dean K., Gingras M., Degraff W., Trun N.J. Overproduction of three genes leads to camphor resistance and chromosome condensation in Escherichia coli. Genetics 1996. 143(4):1521-1532. PMID: 8844142","","","

InterPro
IPR003691
Family

Camphor resistance CrcB protein
PF02537	$\"[57-174]T$	CRCB

noIPR
unintegrated

unintegrated
tmhmm	$\"[53-73]?$ $\"[87-107]?$ $\"[116-134]?$ $\"[153-173]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB003691 (Camphor resistance CrcB protein) with a combined E-value of 2.6e-18. IPB003691A 58-70 IPB003691B 85-101 IPB003691C 115-139","","","No significant hits to the PDB database (E-value < E-10).","Residues 57 to 174 (E_value = 1.1e-20) place ANA_2156 in the CRCB family which is described as CrcB-like protein.","","integral membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2157","2332497","2332994","498","11.57","9.31","16755","ATGAGCGGGGCCGCCGCCGGGCTGGGAACCTGGCTCACCGACTGGCTCCCCCTGGCGCTGGCCGGCGGGGTGGGGGCGGCCTGCCGCTGGGGCGTGGACACCTCGGTCAGCCGCCTCGACAGCCGAGTCGCCCGGGAGGCTGCGGCGGGAGGCCGGCAGCGGCGTCGTTCCGGGCTGCGGGCGCCCTGGATGTCGCGGATGCTGCGAATGCCGTGGGGCACGGTCGTCGTCAACGTGACCGCCTGCCTCCTCATGGGCCTGCTCGTGGGCCGGGCGGCAGACCCGCCGCACTCCGGAACCTGGGCCGCCACCGCGCTGACCGTCCTGGGGACCGGCTTCCTGGGCGGGTACTCGACCTTCTCCACGGCCTGCGTCGAGGGAGCGCGCCTGCTGCTGGCCGGGCGGTGGGGGCCGGCCCTGGCGCACGCGACCCTCATGACGGCGGCGACGCTGGGCGCCGTCGGACTCGGGCTGGCTGCCGGCGCAGCCCTGCGTTAG","MSGAAAGLGTWLTDWLPLALAGGVGAACRWGVDTSVSRLDSRVAREAAAGGRQRRRSGLRAPWMSRMLRMPWGTVVVNVTACLLMGLLVGRAADPPHSGTWAATALTVLGTGFLGGYSTFSTACVEGARLLLAGRWGPALAHATLMTAATLGAVGLGLAAGAALR$","Camphor resistance CrcB protein","Membrane, Extracellular","Protein crcB homolog 2","hypothetical protein predicted by Glimmer/Critica","Camphor resistance CrcB protein","","Hu K.H., Liu E., Dean K., Gingras M., Degraff W., Trun N.J. Overproduction of three genes leads to camphor resistance and chromosome condensation in Escherichia coli. Genetics 1996. 143(4):1521-1532. PMID: 8844142","","","

InterPro
IPR003691
Family

Camphor resistance CrcB protein
PF02537	$\"[15-161]T$	CRCB

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[14-32]?$ $\"[72-92]?$ $\"[98-118]?$ $\"[139-159]?$	transmembrane_regions

","BeTs to 17 clades of COG0239COG name: Integral membrane protein possibly involved in chromosome condensationFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0239 is -om-k-yqvdr-bcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003691 (Camphor resistance CrcB protein) with a combined E-value of 1.3e-19. IPB003691A 16-28 IPB003691B 70-86 IPB003691C 106-130","","","No significant hits to the PDB database (E-value < E-10).","Residues 15 to 161 (E_value = 1.8e-08) place ANA_2157 in the CRCB family which is described as CrcB-like protein.","","crcB homolog 2","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2158","2333286","2334152","867","6.35","-3.18","30305","ATGAGTGTTCAGCCGCCTTCTTCGACGCCGACGCAGACGCAGTCGAAGACCAACCGCGCCACGGTCATCACCCTCGTGGTCATCGCCGTCATCCTGGCCGTCCTCGCCGCAGTGCTGCTGCAGAACGTCGCCTCCCGCCGCCATCAAGCCGCCGCCGCCAGCCAGGCGCCCGCCTCCTCCTCCGATTCGGCCGCCGCGGTCCCCGAGCCCGTACCGGCCCCGCCGGTCGCCGACCAGCAGACCCTGGAGCTCATCCACTCCGAGATCCACCGCGACCCGGCCGACGGCCAGGCCAAGGGCAAGGTCGACGCGCCGGTCGTCATGGTCATCTACTCCGACTTCGCCTGCCCCTTCTGCACCCAGTTCGCCCGGAATGTCGAGCCCGAGCTGAACAAGCTGGTCAAGGAGGGCACGCTGCGCATCGAGTGGCGCGACCTGGCCCAGATCAGCGAGACCTCGCCCCTGGCCGCCCAGGCCGGGCGGGCCGCCGCCAAGCAGGGAAAGTTCTGGGAGTTCCACGACGCCGTCTACGCCGCCGCCGACCCCAAGGGCCACCCGACCTACACCGAGGACTCCCTGGTCGACTTCGCCAAGAAGGCCGGGGTGGCGGACCTGTCGAAGTTCCGCACTGACATGACCGCCGCCGAGACCGTCAAGGCCGTCTCCGAGTCCACCGACCACGTCCATTCCATCGGCATTCAGGGAACCCCGTTCATGATCGTGGGCGAGACCTACATCAACGGGTACCAGGACGTCGACTACATGACATCCGTCGTCAAGAGCCAGGCCGCCAAGGCCAAGGAGGCCAAGGGAGCCCAGGGCACTACCGGGTCCGCGAGCCCCGCGGCACCGGCATCGGCGCACTGA","MSVQPPSSTPTQTQSKTNRATVITLVVIAVILAVLAAVLLQNVASRRHQAAAASQAPASSSDSAAAVPEPVPAPPVADQQTLELIHSEIHRDPADGQAKGKVDAPVVMVIYSDFACPFCTQFARNVEPELNKLVKEGTLRIEWRDLAQISETSPLAAQAGRAAAKQGKFWEFHDAVYAAADPKGHPTYTEDSLVDFAKKAGVADLSKFRTDMTAAETVKAVSESTDHVHSIGIQGTPFMIVGETYINGYQDVDYMTSVVKSQAAKAKEAKGAQGTTGSASPAAPASAH$","Protein-disulfide isomerase","Extracellular, Periplasm, Membrane","putative membrane protein","hypothetical protein","DSBA oxidoreductase","","Hu S.H., Peek J.A., Rattigan E., Taylor R.K., Martin J.L. Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. J. Mol. Biol. 1997. 268(1):137-146. PMID: 9149147Guddat L.W., Bardwell J.C., Martin J.L. Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. Structure 1998. 6(6):757-767. PMID: 9655827","","","

InterPro
IPR001853
Family

DSBA oxidoreductase
PF01323	$\"[107-260]T$	DSBA

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[91-266]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-36]?$	signal-peptide
tmhmm	$\"[20-40]?$	transmembrane_regions

","BeTs to 7 clades of COG1651COG name: Protein-disulfide isomeraseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1651 is ao-----q-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 107 to 260 (E_value = 2.7e-09) place ANA_2158 in the DSBA family which is described as DSBA-like thioredoxin domain.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2160","2334343","2335290","948","5.18","-9.72","32283","ATGGCACTGAGCATCGGAGTGGATGTCGGCGGAACGAAGATCGCGGCCGGCGTCGTCGACGACGAGGGGAAGGTTCTTCAGACGATTCGGCGCGACTCCCCCGCCGCCGACCGCCAGGCGATCATTGACACGATCACGATGGTGGTGCGCCGGCTGCGGGAGGACTTCCCCGACATAGCCACCGTGGGCATCGGGGCGGCGGGCTTCGTGTCCTCCGACCGCAACACGATGGCGCACGGCACCAACCTGGACTGGACTGGGATGCGGATCGGCGACGTCGTCTCCGAGGGCGTGGGCCTGCCCGTCGTCGTCGAGAACGACGCCAATGCCTTCGGGTGGGCCGAGGCCCGCTTCGGGGCGGCCCGCGGCAAGCGCAACGCCCTCATCGTGGCCATCGGCACCGGCGTGGGCGGGGCCATCATCGTCGACGGGCACCTCCTGCGCGGGGCGGCCGGATTCGGCGGGGAGATCGGGCACCTCAACGTCGTTCCCGGCGGACGCCCCTGCGGGTGCGGCCTGCGCGGGTGCCTGGAGCGCTACAGTGCCGGCACGGCCCTGGGCGTCAACGCCTGGGAGCTGGCGCAGTTCCGCCCCGACTACGCGGCCCGCATCATCGAGCTCTCCGGTGGCAACCCGGAGCACATCTCCGGCAAGGCCGTCACCGCCGCCGCCCGCGAGGGGGACCCCGCCGCCCTGGAGTGCTACGAGCAGCTCACCCACTGGCTGGGGGTGGGACTGGCCGACATGTGCGCGCTGCTGGACCCGGAGGTCATCGTCATCGCCGGTGGCCTGGCCGAGGCCGGCGACATCCTGCTCGCCCCCACGCGCAAGGCCTTCGCCGACAACCTCACGGCCGGCACCCACCGCCCCACCATTCCGGTGGTCCTGGCCGAGGGCGGCCAGGAGGCCGGGCTCGTCGGCGCCGCGGACCTGGCCCGCCAGCCCTGA","MALSIGVDVGGTKIAAGVVDDEGKVLQTIRRDSPAADRQAIIDTITMVVRRLREDFPDIATVGIGAAGFVSSDRNTMAHGTNLDWTGMRIGDVVSEGVGLPVVVENDANAFGWAEARFGAARGKRNALIVAIGTGVGGAIIVDGHLLRGAAGFGGEIGHLNVVPGGRPCGCGLRGCLERYSAGTALGVNAWELAQFRPDYAARIIELSGGNPEHISGKAVTAAAREGDPAALECYEQLTHWLGVGLADMCALLDPEVIVIAGGLAEAGDILLAPTRKAFADNLTAGTHRPTIPVVLAEGGQEAGLVGAADLARQP$","Glucokinase ROK","Cytoplasm","Glucokinase (Glucose kinase)","glucokinase ROK ","putative glucokinase, ROK family","","Titgemeyer F., Reizer J., Reizer A., Saier Jr M.H. Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 1994. 140:2349-2354. PMID: 7952186","","","

InterPro
IPR000600
Family

ROK
PF00480	$\"[6-186]T$	ROK
PS01125	$\"[132-159]?$	ROK

InterPro
IPR004654
Family

Glucokinase ROK
TIGR00744	$\"[5-313]T$	ROK_glcA_fam: ROK family protein (putative

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.160	$\"[107-309]T$	no description
G3DSA:3.30.420.40	$\"[4-106]T$	no description
PTHR18964	$\"[65-198]T$ $\"[218-313]T$	ROK FAMILY
PTHR18964:SF37	$\"[65-198]T$ $\"[218-313]T$	GLUCOSE KINASE

InterPro
IPR002549
Family

Protein of unknown function UPF0118
PTHR21716	$\"[94-340]T$	TRANSMEMBRANE PROTEIN
PF01594	$\"[25-343]T$	UPF0118

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[24-42]?$ $\"[46-64]?$ $\"[79-99]?$ $\"[157-177]?$ $\"[209-229]?$ $\"[248-268]?$ $\"[273-293]?$ $\"[312-334]?$	transmembrane_regions

","BeTs to 13 clades of COG0628COG name: Predicted permeaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0628 is aom-k--qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB002549 (Protein of unknown function UPF0118) with a combined E-value of 6.6e-09. IPB002549B 295-332","","","No significant hits to the PDB database (E-value < E-10).","Residues 25 to 343 (E_value = 3.9e-34) place ANA_2161 in the UPF0118 family which is described as Domain of unknown function DUF20.","","membrane protein STY1587 , putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2163","2337960","2337070","891","5.17","-8.86","30786","GTGCTCTGCTGGCTCGTCTCGCTCATGGGCTCAGCCTACGGGGCGGTCACGAGGCAGGATGGGGCCATGACTTCACTGGCGCGCATCGTTACGGGGCCCGACGACGCCCCCACCCTGGTTCTGCTCCACGGCATCACCGGCTCCGCAGTCTCCCTGGCCGAGGCCATCGACCACTGGGTGGGCCGCGGCTACCGGGTCGTGGCGGTTGACGCCCGCGGGCACGGCCTGTCCCCGCGGTGGGAGCCGGCCGAGCTCGAGCGGGCCGGGGAGGTCCTCGTGGAGGACCTCATCGCCGTCCTGGAGGAGTTGGAGGCCGCCTCGTGCGGCCGGGCTGCCCTGGGTCTGCCGACGCCGGCCGCCCCAGTCGTCATCGGTCACTCGATGGGCGCGGCCACCGCCATGGTGGCCGCCGTCCGTCGCCCCGACCTGGTCACCGGCGTCGTCCTGGAGGACCCGGCCCGCTTCGGTACCCGCAGCCCGCGCGAGCTCCTGGCCCGCGGCGCCGCCCGGGAGCGGGCTCGCGCCGCCGAGGTCGCCGACCTGCCGGCCGCCGTCGGCCGCGCCCTGGAGACCATGCCCGACGCTGAGGCCCTCCCGGGCGTATGGGCTTCCCAGCGCACCGACCCTGGCCTGCTGCTCTCCGGCGTCGTCACCCCCGAGGTCCCCTGGGACGAGGCGATGGCGGCGCTCGACGTCCCCGCCCTGCTGCTCACCGGCGACCGGCCTGGCAGCGCCCGCGTGGGCAGCGAGGGCCTGGCCACCGCCTCCCGCAACCCCCGTATCACCCCGGTCCTCGTGCCCGGGGCCGGCCACCAGGTGCGCCGCAGTGACCCACAGGCCTTCTACCGCGCCGTCGACGCCTGGCTGGCCGAGGTCCTGCCAGTGGACTGA","VLCWLVSLMGSAYGAVTRQDGAMTSLARIVTGPDDAPTLVLLHGITGSAVSLAEAIDHWVGRGYRVVAVDARGHGLSPRWEPAELERAGEVLVEDLIAVLEELEAASCGRAALGLPTPAAPVVIGHSMGAATAMVAAVRRPDLVTGVVLEDPARFGTRSPRELLARGAARERARAAEVADLPAAVGRALETMPDAEALPGVWASQRTDPGLLLSGVVTPEVPWDEAMAALDVPALLLTGDRPGSARVGSEGLATASRNPRITPVLVPGAGHQVRRSDPQAFYRAVDAWLAEVLPVD$","Hydrolase, alpha/beta fold family","Cytoplasm, Extracellular","Williams-Beuren syndrome critical region protein21 form A","alpha/beta hydrolase fold","alpha/beta hydrolase fold","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[64-204]T$	Abhydrolase_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[25-289]T$	no description
PTHR10992	$\"[24-289]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF17	$\"[24-289]T$	VALACYCLOVIR HYDROLASE
signalp	$\"[1-14]?$	signal-peptide

InterPro
IPR003815
Family

LuxS protein
PD013172	$\"[7-138]T$	LUXS_HELPJ_Q9ZMW8;
PR01487	$\"[4-22]T$ $\"[27-45]T$ $\"[48-66]T$ $\"[72-90]T$ $\"[112-131]T$	LUXSPROTEIN
PIRSF006160	$\"[1-149]T$	Autoinducer-2 production protein LuxS
PF02664	$\"[1-148]T$	LuxS

noIPR
unintegrated

unintegrated
G3DSA:3.30.1360.80	$\"[1-149]T$	no description

","BeTs to 9 clades of COG1854COG name: LuxS protein involved in autoinducer AI2 synthesisFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1854 is ---------d-lb-e-gh-nu---t-Number of proteins in this genome belonging to this COG is 1","***** IPB003815 (Bacterial autoinducer-2 (AI-2) production protein LuxS signature) with a combined E-value of 1.3e-53. IPB003815A 4-22 IPB003815B 27-45 IPB003815C 48-66 IPB003815D 72-90 IPB003815E 112-131","","","-77% similar to PDB:1J6X CRYSTAL STRUCTURE OF HELICOBACTER PYLORI LUXS (E_value = 1.1E_49);-65% similar to PDB:1INN CRYSTAL STRUCTURE OF D. RADIODURANS LUXS, P21 (E_value = 2.6E_30);-65% similar to PDB:1J6V CRYSTAL STRUCTURE OF D. RADIODURANS LUXS, C2 (E_value = 2.6E_30);-65% similar to PDB:1VGX Crystal structure of a autoinducer-2 synthesis protein (E_value = 2.6E_30);-65% similar to PDB:1VH2 Crystal structure of a autoinducer-2 synthesis protein (E_value = 2.6E_30);","Residues 1 to 148 (E_value = 4.2e-70) place ANA_2165 in the LuxS family which is described as S-Ribosylhomocysteinase (LuxS).","","production protein LuxS (luxS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2168","2339032","2339859","828","6.81","-0.36","29725","GTGTCGGACGCGGCGGCCACGCTCATCGCGCTTGTCGGCCTGTGGCTGGGGCTGCTGCTGGCGGGGTGGATCTTTGAGGAGGGCGACCTGTTCTCGTTCAAGATGCTGGCCACCTCCTGCGGCGTGGCGGTCGTGGTGCTGGTGGCGACCTCCGCAGTGCTGGCGCGCATCCAGCACCATCGCACGCTGCTGCCGATCGCGGAGGTCGCCCAGATGGGCGAGTCCGACCGCCTGGAGTTCAAGTCCTCGGCGCGCTGGAACCTGCGCGCGGACAAGCGCGACGAGGCCATGGAGGAGGTCGTGGCCAAGACGGTGGCGGCCTTCATGAACTCCGCGGGCGGCACGCTCCTGCTCGGCGTCGACGACGGCGGCAACCTCATCGGGCTCGGCCCCGACTACGCGACCCTCAAGCAGCCCGACGCCGACCGTTTCGAGCTGTGGCTGCGCGGCATGTGGCGCACGCGCATGGGCACGAACGCGGCGGCGCTACCGCAGGTGGACTTCGCGCCCACCCCGGACGGGACCGCGGAGGTGTGCCGGGTGACCGCGCCCCCGTCCCCGCTGCCGGTCTACCTCAAGCCGGCCAAGGGTCGCGACGGGGCGGCGCTGTGGGTGCGGGTCGGCAACTCGACGCGGCGCCTGGAGGTGGACGACGCCGTCGACTACGTCATGCTGCGCTGGCCGCGGATCAACCACGTGGCCTGGCCGATCCGGCTGGGGAACTTCCTGCTGCGCCGCGACCAGTCGCGCCGGGCGCTACCCATCAACCCGGCAGCGGCCGTCACCGCCGCCACGGGCTCCCGGGACGACGAGGGCGCGGGTCAGTAG","VSDAAATLIALVGLWLGLLLAGWIFEEGDLFSFKMLATSCGVAVVVLVATSAVLARIQHHRTLLPIAEVAQMGESDRLEFKSSARWNLRADKRDEAMEEVVAKTVAAFMNSAGGTLLLGVDDGGNLIGLGPDYATLKQPDADRFELWLRGMWRTRMGTNAAALPQVDFAPTPDGTAEVCRVTAPPSPLPVYLKPAKGRDGAALWVRVGNSTRRLEVDDAVDYVMLRWPRINHVAWPIRLGNFLLRRDQSRRALPINPAAAVTAATGSRDDEGAGQ$","Hypothetical protein","Membrane, Cytoplasm","predicted protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PTHR12155	$\"[60-128]T$	SCHLAFEN
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[5-25]?$ $\"[31-53]?$	transmembrane_regions

InterPro
IPR000731
Domain

Sterol-sensing 5TM box
PS50156	$\"[240-372]T$	SSD

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[623-792]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-68]?$	signal-peptide
tmhmm	$\"[52-72]?$ $\"[223-243]?$ $\"[245-267]?$ $\"[273-293]?$ $\"[321-341]?$ $\"[351-373]?$ $\"[408-428]?$ $\"[563-583]?$ $\"[598-618]?$ $\"[624-646]?$ $\"[688-708]?$ $\"[714-734]?$	transmembrane_regions

","BeTs to 6 clades of COG2409COG name: Predicted drug exporters of the RND superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2409 is ---p-z---dr-b-------------Number of proteins in this genome belonging to this COG is 1","***** IPB004869 (MMPL domain) with a combined E-value of 2.9e-27. IPB004869B 280-300 IPB004869C 716-753 IPB004869B 639-659 IPB004869C 343-380","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","transport-associated protein homolog ydfJ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2171","2342690","2343298","609","5.29","-3.06","22140","ATGACACCGAGCACCGACCCGCCCGCCGCCGAGCGCACGCTGCGCAAGCGGGAGAACACCCGCGCCCGCCTCATCGAGGCGGCTGCGGACATCGTCGCCTCCAAGGGCATCGCCAGCACTCGCATTGACGACGTCGTCAAACAGGCCGGCTTCACCCGGGGCGCCTTCTACTCCAACTACTCCTCGCTCCAGGACATCCTGACCGAGGCCATCATCATGCGCTCCAACACCTTGCTGTCACGGGTCACGCAGGCCATCGACTCCTTCGAGGGCGCCCCCACGATGGACTCGCTCATGGAGCTGCTCGAGGCCATCCGCCCCGAGGCCCGCACCATCTACCTGCTGACCACCGAGTACTCCCTCTTCCAGCTGCGCAACCCCGACAGCCCGACGATCCCCGGAACGGCGCGCGCCGACTTCACCGCCAGACTGTCCGGAACGGTCGAGAAGGTTCTCGCCCGCATGGGGCGCCGCCCCACCGTCCCCACGGCGAGCCTGGCCGACCTCGTCAGCCTGCTCTTCATGGACTCGATCACTGAGAACACGGACTGCGACAGGCTGCGAGACCTCATCGAGGCGATCATTATCGGGCTAAGCACGCCGACGTAG","MTPSTDPPAAERTLRKRENTRARLIEAAADIVASKGIASTRIDDVVKQAGFTRGAFYSNYSSLQDILTEAIIMRSNTLLSRVTQAIDSFEGAPTMDSLMELLEAIRPEARTIYLLTTEYSLFQLRNPDSPTIPGTARADFTARLSGTVEKVLARMGRRPTVPTASLADLVSLLFMDSITENTDCDRLRDLIEAIIIGLSTPT$","Transcriptional regulator, TetR family","Cytoplasm","putative TetR-family regulator.","transcriptional regulator; TetR family","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[24-37]T$ $\"[45-68]T$	HTHTETR
PF00440	$\"[24-70]T$	TetR_N
PS50977	$\"[18-78]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[2-70]T$	no description

","BeTs to 14 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 5e-11. IPB001647 24-66***** IPB013572 (Tetracycline transcriptional repressor MAATS-type, C-terminal) with a combined E-value of 2.3e-06. IPB013572A 9-29 IPB013572B 45-67","","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 70 (E_value = 6.5e-07) place ANA_2171 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","TetR-family regulator.","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2172","2343568","2344311","744","4.65","-9.88","24670","GTGAGTCGCACCAGTGCCGCACCCGTCATCGTCTCCTGCGCCATGGCCGAGGAGGCCCAGCCCTTCCTGGACGCCCTGCCCGAGCGCGCGGCTGCCCAGGCGCCGCCCCTGCCGGGGTCCGCGCGTGCCTGGTCCCTCCAGCTTCCCGACGGCGAGCGCGAGCTCATCGTCGTGCGCAGCGGCATCGGGCTCGTGGCAGCCGCGAGCGCGCTGGCGACGGTCCTGGCTCAGGTCCGCCCCAGCGCCGTCGTCTCGGCGGGAACCACCGGCGGGCTCGGCCGCCAGGTCGAGGTCGGCGACGTGTGCGCCTCGGCGAGCCTGGCCTACACCGACGCCGACGCCACCGCCTTCGGCTACGCCCGCGGCCAGACCCCGGGTCAGCCGGAGACCTTCGCCGGGGACGCGGCCCTGCTGGAGCGCCTGGAGCAGGTGGGCCAGGAGGCCCTGCGCGGCGCCACGGCGTCGTCGGGCTCGGCGCGACTGCGTGTCGGTCAGATGCTGGCCGGCAACTCCTTCGTGACGGCCGCGAACGTGGCCGACACCCGCGAGGTCTTCCCGGCGGCACTGAGCACGGACATGGAGTCGACGGCGCTGGCGCAGGTGGCGGCGGGCGCCGGCGTCCCCTTCGTCTCGGTGCGCGGCGTGTCCGACCTGTGCGGCCCCGAGGCGGGCCAGGACTTCCACATCGCCGTCGAGGAGGCCGCCGCCCGCAGCGCCGCGGTCGTCCTGGCCCTGCTCGGCTGA","VSRTSAAPVIVSCAMAEEAQPFLDALPERAAAQAPPLPGSARAWSLQLPDGERELIVVRSGIGLVAAASALATVLAQVRPSAVVSAGTTGGLGRQVEVGDVCASASLAYTDADATAFGYARGQTPGQPETFAGDAALLERLEQVGQEALRGATASSGSARLRVGQMLAGNSFVTAANVADTREVFPAALSTDMESTALAQVAAGAGVPFVSVRGVSDLCGPEAGQDFHIAVEEAAARSAAVVLALLG$","5'-methylthioadenosine nucleosidase; S-adenosylhomocysteine nucleosidase","Membrane, Cytoplasm","MTA/SAH nucleosidase","5'-methylthioadenosine nucleosidase / S-adenosylhomocysteine nucleosidase ","purine or other phosphorylase, family 1","","Takehara M., Ling F., Izawa S., Inoue Y., Kimura A. Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp. Biosci. Biotechnol. Biochem. 1995. 59(10):1987-1990. PMID: 8534998Watanabe S., Hino A., Wada K., Eliason J.F., Uchida T. Purification, cloning, and expression of murine uridine phosphorylase. J. Biol. Chem. 1995. 270(20):12191-12196. PMID: 7744869Cacciapuoti G., Porcelli M., Bertoldo C., De Rosa M., Zappia V. Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds. J. Biol. Chem. 1994. 269(40):24762-24769. PMID: 7929153","","","

InterPro
IPR000845
Family

Nucleoside phosphorylase
PF01048	$\"[8-246]T$	PNP_UDP_1

InterPro
IPR010049
Family

MTA/SAH nucleosidase
TIGR01704	$\"[8-246]T$	MTA/SAH-Nsdase: MTA/SAH nucleosidase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1580	$\"[7-247]T$	no description
PTHR21234	$\"[52-246]T$	PURINE NUCLEOSIDE PHOSPHORYLASE
PTHR21234:SF6	$\"[52-246]T$	MTA/SAH NUCLEOSIDASE

","BeTs to 12 clades of COG0775COG name: Nucleoside phosphorylaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0775 is --------vdrlb-efgh-nuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB000845 (Purine and other phosphorylases, family 1) with a combined E-value of 8.3e-07. IPB000845B 46-75 IPB000845C 78-103","","","-46% similar to PDB:1JYS Crystal Structure of E. coli MTA/AdoHcy Nucleosidase (E_value = 3.2E_21);-46% similar to PDB:1NC1 Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH) (E_value = 3.2E_21);-46% similar to PDB:1NC3 Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with formycin A (FMA) (E_value = 3.2E_21);-46% similar to PDB:1Y6Q Cyrstal structure of MTA/AdoHcy nucleosidase complexed with MT-DADMe-ImmA (E_value = 3.2E_21);-46% similar to PDB:1Y6R Crystal structure of MTA/AdoHcy nucleosidase complexed with MT-ImmA. (E_value = 3.2E_21);","Residues 8 to 246 (E_value = 6.8e-14) place ANA_2172 in the PNP_UDP_1 family which is described as Phosphorylase family.","","nucleosidase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2173","2344730","2344422","309","4.88","-4.12","11056","ATGCTTGTCGCCTTCTCCGTGTCCCCGACCACCACTGACGCCCCTGACGGATCTGTCTCCGAGGCGGTGGCCCGGGCTGTGCGCGTGGTGCGCGACTCCGGCCTGCCTTATGAGACGACCTCGATGTTCACCACGGTCGAGGGCGAGTGGGATGAGTGCATGGACGTGGTCAAGCGGGCCTGCGAGGCGGTCGCCGAGGTGAGTCCGCGCGTGGCGCTCGTCCTCAAGGCCGACATCCGCCCGGGCTGGACCGGCCAGATGACCGCGAAGGTCGAGCGCGTCGAGGCCCGCCTGCGCCAGGCCGACTGA","MLVAFSVSPTTTDAPDGSVSEAVARAVRVVRDSGLPYETTSMFTTVEGEWDECMDVVKRACEAVAEVSPRVALVLKADIRPGWTGQMTAKVERVEARLRQAD$","Uncharacterized conserved protein","Periplasm, Cytoplasm","conserved hypothetical protein TIGR00106","hypothetical protein","protein of unknown function DUF77","","","","","

InterPro
IPR002767
Family

Protein of unknown function DUF77
PF01910	$\"[1-95]T$	DUF77
TIGR00106	$\"[1-99]T$	TIGR00106: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.930	$\"[1-95]T$	no description

","BeTs to 5 clades of COG0011COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0011 is aompk-yqv-r-bc------------Number of proteins in this genome belonging to this COG is 1","***** IPB002767 (Protein of unknown function DUF77) with a combined E-value of 3.2e-21. IPB002767A 3-15 IPB002767B 35-52 IPB002767C 70-92","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 95 (E_value = 1.1e-27) place ANA_2173 in the DUF77 family which is described as Domain of unknown function DUF77.","","hypothetical protein TIGR00106","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2174","2344820","2345365","546","6.23","-2.07","19990","ATGACCAGCGCGATTGTTCCAGGCGGCGAGCCCGACGACGCCCAGCTCCGCGAGGCGCTGCGGCTCGCCTCCATCCCACGCAGCGACAACCTCGGGCCTACAGACGGGCCCGGTGCAGCCGGATGGGACATCGCTACCACCGCCGATCGCTTGGGAGTCAGCGCCCACACCCTGCGCTACTACGAGCGGATCGGGCTCGTGCGGGTGGACCGTGACGCCTCGGGACACCGTCATTACGACGCCGCGAGCGTGCGGCGTCTGGTGTTCCTCACCCGGATGCGGACCTCAGGCATGCCGATCCGCGACCTGCGGCGCTACATCGAGCTGGTCGAAGCCGGTCGGGACACGGTGCCCGAGCGCCTGGCTCTGCTCACCGAGCACCGCGACGACCTACGCGCCCGGATCGACGAGCTCCGCCTGGCGCTAGCCGCCACCGAGTACAAGATCGCCGCCTACACGCGGGAGCTGGAAGGGCCGGCCACCCCGGACAACATCAGCACCCCCAACACCAACATTTCCAGCACTGACAAGGAGAATCCCTCATGA","MTSAIVPGGEPDDAQLREALRLASIPRSDNLGPTDGPGAAGWDIATTADRLGVSAHTLRYYERIGLVRVDRDASGHRHYDAASVRRLVFLTRMRTSGMPIRDLRRYIELVEAGRDTVPERLALLTEHRDDLRARIDELRLALAATEYKIAAYTRELEGPATPDNISTPNTNISSTDKENPS$","Transcriptional regulator, MerR family","Cytoplasm","transcriptional regulator, merR family domainprotein","transcriptional regulator; MerR family","regulatory protein, MerR","","Holmes D.J., Caso J.L., Thompson C.J. Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 1993. 12(8):3183-3191. PMID: 7688297Helmann J.D., Wang Y., Mahler I., Walsh C.T. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons. J. Bacteriol. 1989. 171(1):222-229. PMID: 2492496Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 1995. 177(14):3904-3910. PMID: 7608059Nakano Y., Kimura K. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 1991. 109(2):223-228. PMID: 1677938Sadowsky M.J., Cregan P.B., Gottfert M., Sharma A., Gerhold D., Rodriguez-Quinones F., Keyser H.H., Hennecke H., Stacey G. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(2):637-641. PMID: 1988958Helmann J.D., Ballard B.T., Walsh C.T. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. Science 1990. 247(4945):946-948. PMID: 2305262","","","

InterPro
IPR000551
Domain

Bacterial regulatory protein, MerR
PR00040	$\"[43-54]T$ $\"[54-67]T$ $\"[77-97]T$	HTHMERR
PF00376	$\"[43-79]T$	MerR
SM00422	$\"[42-110]T$	HTH_MERR
PS50937	$\"[41-109]T$	HTH_MERR_2

InterPro
IPR015358
Domain

Transcription regulator MerR, DNA binding
PF09278	$\"[84-145]T$	MerR-DNA-bind

noIPR
unintegrated

unintegrated
G3DSA:1.10.1660.10	$\"[42-154]T$	no description

InterPro
IPR003779
Domain

Carboxymuconolactone decarboxylase
PF02627	$\"[48-133]T$	CMD

noIPR
unintegrated

unintegrated
G3DSA:1.20.1290.10	$\"[36-131]T$	no description

","BeTs to 11 clades of COG0599COG name: Uncharacterized ACR, homolog of gamma-carboxymuconolactone decarboxylase subunitFunctional Class: S [Function unknown]The phylogenetic pattern of COG0599 is a-mp--y-vdrlbc-f-hsn-j----Number of proteins in this genome belonging to this COG is 2","***** IPB003779 (Carboxymuconolactone decarboxylase) with a combined E-value of 2.6e-16. IPB003779A 68-77 IPB003779B 102-130","","","-64% similar to PDB:2AF7 Crystal structure of the gamma-carboxymuconolactone decarboxylase from Methanobacterium thermoautotrophicum. Northeast Structural Genomics Consortium target TT747. (E_value = 9.7E_24);","Residues 48 to 133 (E_value = 1.8e-31) place ANA_2175 in the CMD family which is described as Carboxymuconolactone decarboxylase family.","","decarboxylase family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2176","2347615","2346038","1578","7.46","1.11","53896","GTGCTCCATCCCGTCCTCGACGTCCTCGCGCAGGCGCCGATCCTCACCGTCTTCCTCGTCATCGGCCTGGGGACCGCCGCCGGGCAGATCCCGCTGGGGCCGATCCGCTTCGGCGCGGCCGGGGCCCTTTTCGTGGGCCTCGCGGTGGGCGCCCTCGACCCCCGGCTCGGCGCCGACCTCACTCTGCTGCGCAGCCTCGGCCTGGCCCTGTTCTGCTACACGGTGGGACTGGGCGCCGGCAACACCTTCTTCCGCGACCTGCGCCGGCAGCTGCCGCTCATGGCCCTGTGCGTCGTCGCGCTCGTGATCGCCGGCGCGGCGGGCGGCCTCTACTCCCACCTGGCCGGGGTGAGCCCCGCCATGGACTCCGGCGCCTATGCGGGGGCTCTCACCTCACCGGTGCTCGACGCCGCCATCGAGGCGGCCGGGACCCAGGAGCCCGCCGTCGGCTACGCCCTGGCCTACCCCGTGGGCGTCGCCGTCGCCATCCTCATCGTGGCCGGGGTCGTGGGCCGCACCTGGCCCGGGCGGCGCGACCCGCGGCCCGCCAGCGCCGACGGGATCACCGCCACCAGCGTCTACCTCCTGCAGCGGGTGGCCCTGGGCGAGATGAAGGCCTTCAAGGAGGGCCGCATCCGCATCTCCTACCTGGAGCGCGACGGCGAGACGCGGGTCGTGGCCCCCGGTGAGGAGCTGCTGCCCGGGGACAAGGTCGTCATCGTCGGGGCGCCGGCCGCCGTCGAGTCCGCCATGCACGACCTGGGCACCGGGCTCCACAACTGCCTGGCCAAGGACCGCACCGCCGTCGACTTCCGGCGCCTGACCGTCTCTTCGACACGGGTGGCCGGGCGCACGATCGCCGAGGTGGACATGCCCGGGCGCTTCCAGGGCGTCATCACCCGCGTCAAGCGCGGCGACCTGGACCTGCTGGCCCGCGAGGACCTCGTCCTGGAGCTCGGCGACCGGGTGCTGGCGGTCGTCCCCAGTGACGAGCTGGAGAAGGCCGCCGACTGGTTCGGCGACTCCGAGCGCTCCATCGCCCAGATCGACGCCTTCTCCGTCGGGGCAGGCATGGCGCTCGGAGTGCTCCTGGGGCTGGTGGCGATCCCGCTGCCCGGTGGCATCACGCTGCGGCTCGGGGTGGCGGCCGGGCCGCTCGTCGTCGGCATGGTCCTGGGGTGGGTGGGGCGCACCGGACCCTTCGTGTGGGGGCTGCCGCACGCCGCCAACTCCACCATCCGCCAGCTGGGGCTGCTGTTCTTCCTGGCCGCGATCGGGCTGGCCTCGGGGCCGGACTTCGCGGCCTCGGCCTTCTCGATGACGGGACTCAAGGTGGGGGTGCTCGCCGCACTTATTGTGGTGGTCAACGCGATCGTCCTGCTGGCCGGGGCGCGGTGGGCCGGGGTGTCCGCGCAGCGCGCCTCCGGCGGCCTGGCCGGGCTCGTCGGGCAGCCCGCGATCCTCGCCTTCGCCCTGTCCAAACGCGATGACGAGCGCATCGAGGCCGGCTACGCGACCCTGTTCGCCCTGGCCATCGTCGTCAAGATCGTCATGGTTCAGGTCCTCGTGGCGCTGTAG","VLHPVLDVLAQAPILTVFLVIGLGTAAGQIPLGPIRFGAAGALFVGLAVGALDPRLGADLTLLRSLGLALFCYTVGLGAGNTFFRDLRRQLPLMALCVVALVIAGAAGGLYSHLAGVSPAMDSGAYAGALTSPVLDAAIEAAGTQEPAVGYALAYPVGVAVAILIVAGVVGRTWPGRRDPRPASADGITATSVYLLQRVALGEMKAFKEGRIRISYLERDGETRVVAPGEELLPGDKVVIVGAPAAVESAMHDLGTGLHNCLAKDRTAVDFRRLTVSSTRVAGRTIAEVDMPGRFQGVITRVKRGDLDLLAREDLVLELGDRVLAVVPSDELEKAADWFGDSERSIAQIDAFSVGAGMALGVLLGLVAIPLPGGITLRLGVAAGPLVVGMVLGWVGRTGPFVWGLPHAANSTIRQLGLLFFLAAIGLASGPDFAASAFSMTGLKVGVLAALIVVVNAIVLLAGARWAGVSAQRASGGLAGLVGQPAILAFALSKRDDERIEAGYATLFALAIVVKIVMVQVLVAL$","Aspartate:alanine antiporter","Membrane, Cytoplasm","Predicted permease, putative","YidE/YbjL duplication","YidE/YbjL duplication","","Anantharaman V., Koonin E.V., Aravind L. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J. Mol. Biol. 2001. 307(5):1271-1292. PMID: 11292341","","","

InterPro
IPR006037
Domain

TrkA-C
PF02080	$\"[271-340]T$	TrkA_C
PS51202	$\"[256-341]T$	RCK_C

InterPro
IPR006512
Domain

YidE/YbjL duplication
PF06826	$\"[16-171]T$ $\"[353-524]T$	Asp-Al_Ex
TIGR01625	$\"[21-157]T$ $\"[358-510]T$	YidE_YbjL_dupl: YidE/YbjL duplication

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[14-32]?$ $\"[37-57]?$ $\"[61-81]?$ $\"[91-111]?$ $\"[151-171]?$ $\"[351-371]?$ $\"[375-395]?$ $\"[416-438]?$ $\"[444-464]?$ $\"[504-524]?$	transmembrane_regions

","BeTs to 3 clades of COG2985COG name: Predicted permeaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2985 is -o------------e-gh--------Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 16 to 171 (E_value = 4.1e-29) place ANA_2176 in the Asp-Al_Ex family which is described as Predicted Permease Membrane Region.Residues 271 to 340 (E_value = 1.7e-10) place ANA_2176 in the TrkA_C family which is described as TrkA-C domain.Residues 353 to 524 (E_value = 1.4e-27) place ANA_2176 in the Asp-Al_Ex family which is described as Predicted Permease Membrane Region.","","permease, putative","","1","","","","","","","","","","","Tue Aug 14 17:05:21 2007","","Tue Aug 14 17:05:21 2007","","","Tue Aug 14 17:05:21 2007","","","","Tue Aug 14 17:05:21 2007","Tue Aug 14 17:05:21 2007","","","","","yes","","" "ANA_2177","2347895","2350285","2391","7.83","4.67","86365","ATGCCCCAGACAGAAGCCTCTCTGCCGACCTACTCACCGGAGGAGGAGAAGCGGATCATCCGTAACGCCGACGGCGTCCCCGTCGGCATACGTCCTGACAATCGATGGACACCCGTACGGATCGCCACATGGGTGGCCATCACTGCCCTGGGCGTCCTGGGGTGGTGGATGCTGGCGGTCGTGCGCGGCGAGCACGTCAACACCATCTGGTTCGTGGTCACCGCCGTGTGCACCTACGCGATCGGGTACCGCTTCTACGCCCTCTACATCCAGCGGCGCATCATGCGCCCCGACGACACCAACGCCACCCCGGCCGAGCGCATCAACAACGGGCGCGACTTCGACCCCACCCACCGCGTCGTCCTCTACGGCCACCACTTCGCGGCCATCGCCGGCGCCGGCCCGCTGGTCGGCCCGGTCCTGGCCGCCCAGATGGGCTACCTGCCCGGCACCCTGTGGATCATCATCGGCGTGCTCGTGGCCGGCGCCGTCCAGGACATGCTCGTCCTGTTCTTCTCCATGCGCCGCGGCGGCCGCTCCCTGGGCCAGATGGCCACTGACGAGATCGGCCGGATCGGCGGCATCGTGGCGACCATCGTCGTTTTCGTCATGCTCATGATCGTCCTGGCGGTCCTGGCCATGGTCTGCGTCAACGCCCTGGCCGCCTCCCCCTGGGGCGTCTTCTCGGTGGGTATGACCATCCCGATCGCCATCGGGATGGGCCTGTGGCTGCGCTTCGTCCAGCCCGGCAAGATCACGCAGGTCTCCTTCGTCGGTTTCGGCCTGCTCATCGCCGTCATCATCGGCGGGCGCTGGGTGGCCGAGTCACCCCTGGGCCACTACCTGCACCTGTCCCCCAAGACCCTGGTGTGGGCCATGATCATCTACGGCTTCCTGGCCGCGGTCCTGCCGGTGTGGGTCCTGCTCACCCCGCGTGACTACCTGTCGACCTTCATGAAGGTCGGCACGATCACGATCCTGGCCCTGGGCATCATCATCGTGCGCCCCCTGGTGGAGATGTCCGCCGTCACCGAGTTCGCCTTCAACACCGAGGGCCCGGTCTTCGCCGGAACCCTCTTCCCCTTCCTGTTCATCACCATCGCCTGCGGCGCCCTGTCCGGCATGCACGCCATGGTCTCCTCGGGCACCAGCCCCAAGATGGTGGAGAAGGAGACTCAGGTCCGCATGATCGGCTACGGCGGCATGCTCATGGAGTCCTTCGTGGCCATCATGGCGCTGGCCGCCGCGGTCTCGCTGAGCCCGGGCATCTACTTCTCCATGAACACCTCGACGGCGACCATGAACAAGCTCGCCGGCCCCGAGACGGTAGCCGCGGCCCCCTGCAAGACCACCGACGACCCCGAGCACCACTGCGAGAAGCTCGCGGAGGTCGCCGTCGGCAACCTCGGTGTCACCGATGCCCAGGGCCGCAAGCCCACCCCCGAGTGGGACTCCTGGGACGACAACGGCAACCCCAAGACCTACACGGGTGCCGAGGCCCTGGAGCGCCTGGCCAGTGACGTCGGCGAGCCCAACGTCGTCTCGCGCACCGGCGGCGCCCCCACCCTGTCGGTGGGCATCGCCCACATCCTCCACCAGATCGGCGGAGGCCGGGCCATGATGGGCTTCTGGTACCACTTCGCCATCATGTTCGAGGCCCTGTTCATCCTCTCGGCCGTCGACGCCGTCACCCGCGTGGCCCGCTTCCAGCTCTCTGACGCGCTGGGCAACGCCTTCCCCAAGTTCAAGGACCCGTCCTGGCACGTGGGCGCCTGGGGGACCACGGCGGTCGTCGTCGCCTCGTGGGGGGCGCTGCTCCTCATGGGTGTCACCGACCCGCGCGGCGGCATCCAGACGCTCTACCCGCTGTTCGGTATCGCCAACCAGCTCATCGCGGCCGTGGCGCTTCTGGTGGTCACCGTCATGGTGGTGCGCAAGGGCTACACGAAGTGGGTGTGGATCCCCGCGATCCCGCTGGTCTTCGACACGGCCGTCACCTTCACGGCCTCATGGCAGAAGATCTTCTCCACCGACCCGCTCGTGGGCTACTTCCAGCAGCATCGCGAGGCCGTGGCCAAGCTGGGCACGCTCACCGACCCGGCCAAGATCGAGGAGACCCGGGCCATTGTGCGCAACACGATGATTCAGGGGACGCTGTCGATCATCTTCCTGGTCATGGTGGCCTTCGTTATGGTCTGCGCCCTCATCCGTATCGTCCAGACGCTCCGCAACCGGGACACGACGACGTCGGAGGACCCGTACCAGGAGTCCAACTTCTACGCGCCCGAGACGATGATCGCCTCCTCGCTCATGAAGAAGGTCTCCCGGGAGTACGAGCAGGTGGGCGACCCGGCCCTCATCCCGCACAAGGCCCACGCGGAGAAGTCATGA","MPQTEASLPTYSPEEEKRIIRNADGVPVGIRPDNRWTPVRIATWVAITALGVLGWWMLAVVRGEHVNTIWFVVTAVCTYAIGYRFYALYIQRRIMRPDDTNATPAERINNGRDFDPTHRVVLYGHHFAAIAGAGPLVGPVLAAQMGYLPGTLWIIIGVLVAGAVQDMLVLFFSMRRGGRSLGQMATDEIGRIGGIVATIVVFVMLMIVLAVLAMVCVNALAASPWGVFSVGMTIPIAIGMGLWLRFVQPGKITQVSFVGFGLLIAVIIGGRWVAESPLGHYLHLSPKTLVWAMIIYGFLAAVLPVWVLLTPRDYLSTFMKVGTITILALGIIIVRPLVEMSAVTEFAFNTEGPVFAGTLFPFLFITIACGALSGMHAMVSSGTSPKMVEKETQVRMIGYGGMLMESFVAIMALAAAVSLSPGIYFSMNTSTATMNKLAGPETVAAAPCKTTDDPEHHCEKLAEVAVGNLGVTDAQGRKPTPEWDSWDDNGNPKTYTGAEALERLASDVGEPNVVSRTGGAPTLSVGIAHILHQIGGGRAMMGFWYHFAIMFEALFILSAVDAVTRVARFQLSDALGNAFPKFKDPSWHVGAWGTTAVVVASWGALLLMGVTDPRGGIQTLYPLFGIANQLIAAVALLVVTVMVVRKGYTKWVWIPAIPLVFDTAVTFTASWQKIFSTDPLVGYFQQHREAVAKLGTLTDPAKIEETRAIVRNTMIQGTLSIIFLVMVAFVMVCALIRIVQTLRNRDTTTSEDPYQESNFYAPETMIASSLMKKVSREYEQVGDPALIPHKAHAEKS$","Carbon starvation protein A","Membrane, Cytoplasm","carbon starvation protein","carbon starvation protein A","carbon starvation protein CstA","","Schultz J.E., Matin A. Molecular and functional characterization of a carbon starvation gene of Escherichia coli. J. Mol. Biol. 1991. 218(1):129-140. PMID: 1848300","","","

InterPro
IPR003706
Family

Carbon starvation protein CstA
PF02554	$\"[66-465]T$	CstA

noIPR
unintegrated

unintegrated
signalp	$\"[1-63]?$	signal-peptide
tmhmm	$\"[42-62]?$ $\"[68-88]?$ $\"[121-143]?$ $\"[153-173]?$ $\"[194-216]?$ $\"[222-244]?$ $\"[254-274]?$ $\"[288-308]?$ $\"[318-338]?$ $\"[357-377]?$ $\"[406-426]?$ $\"[543-563]?$ $\"[587-607]?$ $\"[621-641]?$ $\"[651-671]?$ $\"[719-739]?$	transmembrane_regions

","BeTs to 12 clades of COG1966COG name: Carbon starvation protein, predicted membrane proteinFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1966 is ----kz-q--rlb-efgh-nu-----Number of proteins in this genome belonging to this COG is 1","***** IPB003706 (Carbon starvation protein CstA) with a combined E-value of 1e-79. IPB003706A 111-162 IPB003706B 296-331 IPB003706C 359-386 IPB003706A 190-241","","","No significant hits to the PDB database (E-value < E-10).","Residues 66 to 465 (E_value = 5.6e-197) place ANA_2177 in the CstA family which is described as Carbon starvation protein CstA.","","starvation protein (cstA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2178","2350282","2350581","300","9.20","5.52","11080","ATGACACCTTCTCCTTCGACGCCGCAGCCGGCGGATCGACCCAGCGCCCGACGTCGGGTCCGCCAGGTCCTGACCCGGGCCCGCACACTGTGGCGGGACATGACCGGCGAGTCCGCCTACGACCGCTACCTGGAGCGCTACGCCCGCGAGCACGCGCAGTGCCCCCACGGGCACGGGGGCGCCCACAGCGCAGGGCACGGTTCTGAGCACGGTTCCGGGCACGGCCCGATGAGTGAGCGCGAGTTCTGGCGCGCCCGGGCCAAGCAGGCCGAGACGGAGATCAACGCCAGCTGCTGCTGA","MTPSPSTPQPADRPSARRRVRQVLTRARTLWRDMTGESAYDRYLERYAREHAQCPHGHGGAHSAGHGSEHGSGHGPMSEREFWRARAKQAETEINASCC$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2179","2350664","2351230","567","6.77","-0.43","19692","GTGAGCGTGCCCGCCCAGCAGCCCGCGCCCGACGCACTGACGTCCGCCGAGTCCCCTGACACCTCCTGGGGGACATCACCGGCGTCGGCCGCTTCGCCGTCGGGCGGCAGAGCCTCCGGGTCGAGGTCCTCTGAGGCCCTCCTGCCGCGCCACGCCTCTCACGAGCGGATCGCCCGCGTCGCGGCGGTCATCCTCCTGGCCATCGTCTGCGTGGCGGTGGTGTGGCCCTCCGGGCGTGAGGTCGCCGAGCTCAAGGACACCGTGGGGCCGGCTTTCCTCAGCTCCGAGGGCAAGGACGTCGTCCTCAACCTGGTGATGCTGGCTCCGGCCACCTTCTGCGCGGTCGCAGGCTGGCGGGACATCCCCTGGTGGATGTGGGCGCTGGTGGGCTGCGTGATCGGGCTGAGCGCCGAGGTGCTCCAGAGCCTCCTGCCGATGCTGGAGCGGCGCCCCTCGCTGGCCAATGTCGGCCAGAACGCCGTCGGCGCCTGGGCCGGGGCCCTGGCCGCCTGGTACCTGCTGCGCCGCCTGCACGCGCGGGTAGTAGAACCCACCTCCGTGGAGTAG","VSVPAQQPAPDALTSAESPDTSWGTSPASAASPSGGRASGSRSSEALLPRHASHERIARVAAVILLAIVCVAVVWPSGREVAELKDTVGPAFLSSEGKDVVLNLVMLAPATFCAVAGWRDIPWWMWALVGCVIGLSAEVLQSLLPMLERRPSLANVGQNAVGAWAGALAAWYLLRRLHARVVEPTSVE$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[57-77]?$ $\"[100-118]?$ $\"[123-143]?$ $\"[153-173]?$	transmembrane_regions

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[155-218]T$	FHA
SM00240	$\"[154-204]T$	FHA
PS50006	$\"[155-204]T$	FHA_DOMAIN

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.20	$\"[144-227]T$	no description
PTHR19241	$\"[152-202]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19241:SF6	$\"[152-202]T$	ABC TRANSPORTER

InterPro
IPR000253
Domain

Forkhead-associated
PF00498	$\"[86-150]T$	FHA
SM00240	$\"[85-135]T$	FHA
PS50006	$\"[86-135]T$	FHA_DOMAIN

noIPR
unintegrated

unintegrated
G3DSA:2.60.200.20	$\"[53-156]T$	no description
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[4-24]?$	transmembrane_regions

","BeTs to 7 clades of COG1716COG name: FHA-domain-containing proteinsFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1716 is ------y--dr-bc----s----i--Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 86 to 150 (E_value = 1.1e-14) place ANA_2182 in the FHA family which is described as FHA domain.","","proteins ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2183","2352842","2354272","1431","5.37","-13.45","50171","ATGACCATCTCCCTGCGCTTCGCCGCACGCTCCGACGTCGGCCTGGTCCGCCAGTCCAACCAGGACTCGGGCTACGCCGGCCCCCACCTGTGCCTTCTGTGCGACGGGATGGGCGGACCTGCGGGCGGAGACATCGCCTCGGCGGTCGCCGTCGAGCACCTCATGCCCCTGGACGCCGACTCCCACCAGGCCGGCGAGCTGCTGGGCCTCATGCGCGACGCCGTCCAGGCCGCCCACACCGAGCTCGTCACCCTGTCCTCGCAGGACCCCGACCTCGCCGGCCTGGGCACCACCTGCATCGGCGTCATGCGCAGCGGCAACAAGCTCGCCATGGTCCACGTGGGCGACTCGCGCGCCTACATGCTGCGCGACGGCACCCTCACCCAGGTCACCACCGACCACACCTTCGTGGAGTACCTCGTGGAGACCGGGCGCCTGACCCGGGACCAGGCCCGCCAGCACCCGCAGCGCTCGGTCCTTCTGCGCGTCCTGGGGGACACCGAGGGCGAGGTCCAGCTCGACGAGTCGATCCGCGAGGCCGTTCCCGGCGACCGCTGGCTGCTGTGCTCCGACGGCCTGAGCGGCCCGGTGACCGCCGAGACCATCGGTGAGGTCCTGGCCGGTGTCGCCGACCCCGGTCAGGCCGCCGACCAGCTCATCGACCTGGCCCTGCGCGCCGGCGGACCGGACAACGTCACCGCCGTCGTCTTCGACGTCGTCAAGGACGACCCCGAGCCCCAGACCGTCCCGCAGGTGGTGGGCAGTGCCGCCACCGAGCGCCTGGCCCAGGAGCGCGCCGCCGCCGCCCACCGTGCCGGTGACGAGCAGTCCGAGGCCCAGGAGCCCGAGGCCGCCAGCCCCGCCGCCAAGGCCGCGGCCCTCATGGCCACCCTGGAGGAGAAGCCCGAGGCCGCCTCCGCCAAGGAGTCCTCCGAGGTCAGCGAGGCCATCGCCGCCGAGGCCGCCACCCAGGAGAAGGCCCGACGCCGTCATCGCCGTCGGGTCCTCGTGGGCAGCATCGTCCTGCTGGCCACGCTCGTCGGTGCCAGCGCCCTGTTCTACCGCTGGACCCAGACCCGCTACTACGTCTCCACCTACAAGGGCGAGGTCGCCATCTACCAGGGGATCCCCCAGTCCGTCGGCCCGCTCAAGCTGAGCCACTCGGTCAAGACCTACGCGGACCTGCCCGTGGAGAGCCTCGACCACAACATCCGCGAGCGCCTCCAGGCCACCGTCACCCAGCCGTCGATGAGCGCCGCGGAGACCTACGTGGACAAGACGGTCCGTTCCTACCGCAAGCAGCCCGCCACCCCGCAGGGCACCTCGAGCCCCACGGCCAAGCCCTCGTCCTCGACCTCCCCGCCCTCCGCCGCCCCGTCGCCGACCTCGGCCGCACCGACCCAGCCCGCCAAGCCCGGGCAGGAGGGGTGA","MTISLRFAARSDVGLVRQSNQDSGYAGPHLCLLCDGMGGPAGGDIASAVAVEHLMPLDADSHQAGELLGLMRDAVQAAHTELVTLSSQDPDLAGLGTTCIGVMRSGNKLAMVHVGDSRAYMLRDGTLTQVTTDHTFVEYLVETGRLTRDQARQHPQRSVLLRVLGDTEGEVQLDESIREAVPGDRWLLCSDGLSGPVTAETIGEVLAGVADPGQAADQLIDLALRAGGPDNVTAVVFDVVKDDPEPQTVPQVVGSAATERLAQERAAAAHRAGDEQSEAQEPEAASPAAKAAALMATLEEKPEAASAKESSEVSEAIAAEAATQEKARRRHRRRVLVGSIVLLATLVGASALFYRWTQTRYYVSTYKGEVAIYQGIPQSVGPLKLSHSVKTYADLPVESLDHNIRERLQATVTQPSMSAAETYVDKTVRSYRKQPATPQGTSSPTAKPSSSTSPPSAAPSPTSAAPTQPAKPGQEG$","Protein serine/threonine phosphatase","Periplasm, Extracellular","possible phosphoprotein phosphatase","protein serine/threonine phosphatases","protein phosphatase 2C domain protein","","Wenk J., Trompeter H.I., Pettrich K.G., Cohen P.T., Campbell D.G., Mieskes G. Molecular cloning and primary structure of a protein phosphatase 2C isoform. FEBS Lett. 1992. 297(1):135-138. PMID: 1312947Maeda T., Tsai A.Y., Saito H. Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae. Mol. Cell. Biol. 1993. 13(9):5408-5417. PMID: 8395005Stone J.M., Collinge M.A., Smith R.D., Horn M.A., Walker J.C. Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Science 1994. 266(5186):793-795. PMID: 7973632Lawson J.E., Niu X.D., Browning K.S., Trong H.L., Yan J., Reed L.J. Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C. Biochemistry 1993. 32(35):8987-8993. PMID: 8396421","","","

InterPro
IPR001932
Domain

Protein phosphatase 2C-related
SM00331	$\"[11-239]T$	PP2C_SIG
SM00332	$\"[2-237]T$	PP2Cc

InterPro
IPR014045
Domain

Protein phosphatase 2C-like
PF00481	$\"[6-232]T$	PP2C

noIPR
unintegrated

unintegrated
G3DSA:3.60.40.10	$\"[1-239]T$	no description
PTHR13832	$\"[71-236]T$	PROTEIN PHOSPHATASE 2C
tmhmm	$\"[336-356]?$	transmembrane_regions

","BeTs to 11 clades of COG0631COG name: Protein serine/threonine phosphatasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0631 is ---p--yq-drlbc-f--s-uj-i-wNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","-70% similar to PDB:1TXO Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A. (E_value = 5.7E_61);-44% similar to PDB:2IQ1 Crystal structure of human PPM1K (E_value = 5.4E_11);","Residues 6 to 232 (E_value = 7e-06) place ANA_2183 in the PP2C family which is described as Protein phosphatase 2C.","","phosphoprotein phosphatase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2184","2354274","2355971","1698","9.69","9.87","59948","ATGACTGCTGCTCCCGGCCCCCTGGGCGCCCCCGCGGGCGTCGCGACCATCCAACCGGCCGGCGTCGCGAAGTACTCGGGACGGTGGGCGGAGGCGGCGCTGCTCGGCGTCGCCCTGGTCCTGGGGCTGGGCGGCTTCGTGCTCACCGCCCTCAACCGCACCGGCTCCTCCCCGGCGCAGACCGTGGGCGTGGCGATCGCCTTCCTCGTCCTGACCGTCCTCATGCACCTGTGTGTGCGCTACGCCGCCCCGTGGGCCGATCCGGTCCTCCTGCCGACGGCGGTGGCGCTCAACGGGATCGGTCTGGCCATGATCCGGCGCCTGGACCTGGCCTACGAGGTCAACGAGCAGTGGCAGTTCTACGTGGGCTCCAAGCAGCTGGTCTGGACGCTGCTGGGCGTCATCCTCTTCGCCGCCACGCTCCTCCTGCTGCGCGACTACCGGCGTCTGAGGCGCTGGGACCGTTGGGCCATGTGGTCCGGCCTGGTCTTCCTCGTCCTGCCCTTCATCCCGGGGATCGGCCAGAGCATCAACGGCGCCCGCATCTGGATCCGGATCGGCCCGATGAGCTTCCAGCCGGCCGAGCTGTCCAAGGTGCTGCTGGCGGTCTTCTTCGCCTCCTACCTGGTGGCCAACCGGGACAACCTGGCTCTGGCGGGTCGCAAGGTCCTGTGGATGAGCCTGCCTCGCGCCCGCCACCTGGGCCCCCTGTTCATCGTGTGGGGCGTGAGCATCGGCGTCCTGGTCCTCCAGAAGGACCTGGGCTCCTCGGTGCTGCTGTTCGGCCTGTTCGTCGTCGTCCTGTACGTGGCCACCGACCGGCCCTCCTGGCTGCTCATCGGCGCCGCCCTGTTCCTCCCAGCGGCCTGGTTCGCGGCCACACACCTCCACCACGTCCAGCAGCGCATCAACGGCTGGCTCCACGCCACCGATGACGCCGTGTACAACGCCGCCGGCGGTTCCTGGCAGCTACTGACGGGCATGTTCGGGATGTCCACCGGCGGGCTCATGGGCGCCGGCTGGGGCAAGGGCTCACCGACCCTGGTCACCTTCGCCAACTCCGACTTCATCTTCGCCTCACTGGGTGAGGAGCTGGGCCTGACCGGCACGCTCGTCCTCCTCGTGCTCTACCTCGTGCTCATCCAGCGGGGACTGCGCACGGCCGTCTCGCTGCGCGACGGCTTCGGCAAGCTCCTGGCCGTGGGCCTGTCCTTCGCCATCGCCCTGCAGATCTTCGTGGTCATCGGCGGCGTCACCCGGCTCATTCCGCTGACGGGACTGACCCTGCCCTTCCTGGCCTATGGCGGCTCCTCGCTCATCGCCAACTGGATCATCCTGGCCCTTCTGCTGCGCCTGTCCGACGCCGCCCGGCGTCCGGCCACCCACGCGCCGCGGATCATCGACACCGCCGAGCTGCCGCTGTCCCTGCGCCGTCGGGTCCAGGACGCCGGAGCCGAGGAGACGACGCCGGAGGCCGCCGGCGACGCGCCCACCGGAACGACACCTGCCGACGCCGGGGGCTACGCGTCCCCATCAGCCGCACCCGGCTTCGGCGACCTGGCGGACGACGCCCGCCCCGCCGTCGCCGTCAGCCCGGAGGCGCCGCCTCCGCCGCACACCGCACCCGACGGGGCGACCCTGCGCTCATCGCGGGCCCCGGGCTTCACTGAGGACTCTGACAGGAGGCAGCTGCCATGA","MTAAPGPLGAPAGVATIQPAGVAKYSGRWAEAALLGVALVLGLGGFVLTALNRTGSSPAQTVGVAIAFLVLTVLMHLCVRYAAPWADPVLLPTAVALNGIGLAMIRRLDLAYEVNEQWQFYVGSKQLVWTLLGVILFAATLLLLRDYRRLRRWDRWAMWSGLVFLVLPFIPGIGQSINGARIWIRIGPMSFQPAELSKVLLAVFFASYLVANRDNLALAGRKVLWMSLPRARHLGPLFIVWGVSIGVLVLQKDLGSSVLLFGLFVVVLYVATDRPSWLLIGAALFLPAAWFAATHLHHVQQRINGWLHATDDAVYNAAGGSWQLLTGMFGMSTGGLMGAGWGKGSPTLVTFANSDFIFASLGEELGLTGTLVLLVLYLVLIQRGLRTAVSLRDGFGKLLAVGLSFAIALQIFVVIGGVTRLIPLTGLTLPFLAYGGSSLIANWIILALLLRLSDAARRPATHAPRIIDTAELPLSLRRRVQDAGAEETTPEAAGDAPTGTTPADAGGYASPSAAPGFGDLADDARPAVAVSPEAPPPPHTAPDGATLRSSRAPGFTEDSDRRQLP$","Cell cycle protein","Membrane, Cytoplasm, Extracellular","protein involved in cell wall formation andstabilization of the FtsZ ring during cell division","cell cycle protein","cell cycle protein","","Ikeda M., Sato T., Wachi M., Jung H.K., Ishino F., Kobayashi Y., Matsuhashi M. Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively. J. Bacteriol. 1989. 171(11):6375-6378. PMID: 2509435Joris B., Dive G., Henriques A., Piggot P.J., Ghuysen J.M. The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures. Mol. Microbiol. 1990. 4(3):513-517. PMID: 2113157","","","

InterPro
IPR001182
Family

Cell cycle protein
PF01098	$\"[88-458]T$	FTSW_RODA_SPOVE

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[32-52]?$ $\"[58-78]?$ $\"[88-108]?$ $\"[127-147]?$ $\"[157-177]?$ $\"[191-211]?$ $\"[232-250]?$ $\"[254-272]?$ $\"[277-299]?$ $\"[318-338]?$ $\"[340-360]?$ $\"[366-381]?$ $\"[396-416]?$ $\"[430-450]?$	transmembrane_regions

","BeTs to 17 clades of COG0772COG name: Bacterial cell division membrane proteinFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG0772 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB001182 (Cell cycle protein) with a combined E-value of 4.5e-35. IPB001182A 178-198 IPB001182B 348-369 IPB001182C 413-438","","","No significant hits to the PDB database (E-value < E-10).","Residues 88 to 458 (E_value = 4.6e-80) place ANA_2184 in the FTSW_RODA_SPOVE family which is described as Cell cycle protein.","","involved in cell wall formation and stabilization of the FtsZ ring during cell division","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2185","2355968","2357470","1503","4.86","-14.57","51824","ATGAACCGACAGATCCGTCAGGTCGCCTTCCTGGTGCTGGTCATGTTCGCCACGCTGGCCCTGTCCGTCACGAGCGTCCAGGGCCTGGCCCGTCCGTCCGTGTGGGAGTCGTGGTCGGCCAATGGGGCCCTCAACTCCGACCCGCGCAACCGCCGCACCGTCAGCCGCAACTTCGACACCGAGCGGGGCCCGATCCTCCTGGCCGGCGGTACCGCGATCGCCAGCACCCAGAAGTCCGACGACGGTCAGGGCGCCGAGGACTACCAGCGCATCTACGCCAACGGGCCGCTCTACGCCCCGGTGACCGGATACTTCTCGCCCGCCTTCGCCTCCATGACCGGCATGGAGAAGGAGGGCAACTCCGTGCTCAACGGGGACGACCCCTCCCTGTTCTCCTCCCGGATCAAGACCCTCATCACCGGTGACTCCCAGCGGGGCGGGGCCGTGGAGCTGACCATCAAGCCCGAGATCCAGCAGGCCGCCTACGACGCCCTGGCCGGCCGCGAGGGCGCCGTCGTGGCCCTGGACCCCAAGACCGGGGCCATCCTCGCCCTGGTCTCCACCCCCTCCTACGACCCCTCGGCCTTCGCGACCCGCAACGGGAACGCCGCCAACGAGGCCAACACGACCCTCAGCCAGGACTCCTCCCGCCCCCTGGACAACCGGGCCATCGCCGGCAACCGCTACCCGCCGGGGTCGACCTTCAAGATCCTCACCACGGCGGCGGCGCTGCGCACCGGCAAGATCACCCCGGATCAGGAGGTCGACGCCCCCGACACCATCACCCTGCCGGGCACCAGCCACTCCCTGGAGAACTACGGCGGGGAGTCCTGCGGCGGCGGTCGGACCACCTTCTCCAAAGCCTTCGCCGAGTCCTGCAACACCCCCTTCGCCCAGCTGGCCATGAACGTCGGCGAGGAGGAGCTCTCCAAGGAGGCGAAGAACTGGGGCTTCGACTCCGAGCTGTCCATCCCGCTGAAGGTCACGCCGTCGACCTACCCGCACAACGACTCCCAGGCCCAGACCGCGATGGCCGGAATCGGTCAGGCCTCGGTGCAGGCGACCCCGCTCATGATGGCGATGGTGGCCGCCACCGTGGCCAACAAGGGCGAGCAGATGACCCCCTATCTGGTCTCGCGCATCCTGGACCCCGACCTCAACGAGGTCAGCTCCACCTCCACGAAGGTGGCCCGCACCCCGATCGACTCGGCCACCGCCAGCTCCCTGACCTCCCTCATGCAGGAGGCCGTGGCCACCGGCACGGGCACCAGCGCCCAGGTCAGCGGGGTCCAGGTCGCCGGCAAGACCGGTACCGCCGAGACCGGCACCGACAGCGGCCCCACCACCTGGTTCGTGGGCTTCGCCGGCACCGACATCAACAAGCCTGAGATCGCTCTGGCCGTCGTGCTCGACGGCAATGCCGAGACCGAGGACGGCGCCACCGGCGGCAAGGTCGCCGGCCCCGTCGCCGCCGCGGTCATCGATGCGGCGGTGAACCAGTGA","MNRQIRQVAFLVLVMFATLALSVTSVQGLARPSVWESWSANGALNSDPRNRRTVSRNFDTERGPILLAGGTAIASTQKSDDGQGAEDYQRIYANGPLYAPVTGYFSPAFASMTGMEKEGNSVLNGDDPSLFSSRIKTLITGDSQRGGAVELTIKPEIQQAAYDALAGREGAVVALDPKTGAILALVSTPSYDPSAFATRNGNAANEANTTLSQDSSRPLDNRAIAGNRYPPGSTFKILTTAAALRTGKITPDQEVDAPDTITLPGTSHSLENYGGESCGGGRTTFSKAFAESCNTPFAQLAMNVGEEELSKEAKNWGFDSELSIPLKVTPSTYPHNDSQAQTAMAGIGQASVQATPLMMAMVAATVANKGEQMTPYLVSRILDPDLNEVSSTSTKVARTPIDSATASSLTSLMQEAVATGTGTSAQVSGVQVAGKTGTAETGTDSGPTTWFVGFAGTDINKPEIALAVVLDGNAETEDGATGGKVAGPVAAAVIDAAVNQ$","Peptidoglycan glycosyltransferase","Extracellular, Periplasm, Membrane","PbpA","peptidoglycan glycosyltransferase ","Peptidoglycan glycosyltransferase","","Pares S., Mouz N., Petillot Y., Hakenbeck R., Dideberg O. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 1996. 3(3):284-289. PMID: 8605631","","","

InterPro
IPR001460
Domain

Penicillin-binding protein, transpeptidase
PF00905	$\"[170-495]T$	Transpeptidase

InterPro
IPR013716
Domain

Adenylate cyclase G-alpha binding
SM00789	$\"[363-415]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.710.10	$\"[152-495]T$	no description
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[10-30]?$	transmembrane_regions

","BeTs to 15 clades of COG0768COG name: Cell division protein FtsI/penicillin-binding protein 2Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0768 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB005311 (Penicillin-binding Protein dimerisation domain) with a combined E-value of 4.3e-10. IPB005311B 81-105 IPB005311E 180-194***** IPB002137 (Beta-lactamase, class D active site) with a combined E-value of 4.1e-08. IPB002137A 224-260","","","-42% similar to PDB:1MWR Structure of SeMet Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r (trigonal form) at 2.45 A resolution. (E_value = 3.2E_22);-42% similar to PDB:1MWS Structure of nitrocefin acyl-Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 2.00 A resolution. (E_value = 3.2E_22);-42% similar to PDB:1MWT Structure of penicillin G acyl-Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 2.45 A resolution. (E_value = 3.2E_22);-42% similar to PDB:1MWU Structure of methicillin acyl-Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 2.60 A resolution. (E_value = 3.2E_22);-42% similar to PDB:1VQQ Structure of Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r at 1.80 A resolution. (E_value = 3.2E_22);","Residues 170 to 495 (E_value = 1.6e-76) place ANA_2185 in the Transpeptidase family which is described as Penicillin binding protein transpeptidase domain.","","(pbp2) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2186","2357467","2358594","1128","9.64","8.39","40191","GTGAAACCTGTTGCCGGGCTCCAGCTCCAGGGCCGCTACGAGCTGGTCGAGCAGATCGCTCTGGGTGGCATGGGCCAGGTGTGGCGCGCCACCGACCTGCGCTCGGGACGTGCCGTGGCCGCCAAGATCCTGCGCCCCGAGCTGACCGGTGACGAGATCTTCCTGTCCCGCCTGCGCGCGGAGGCCAAGAACTCCAAGGGGCTGCGCCACCCGAACCTCGCCGTCGTCCTGGACTCCGGGGAGAAGGACGGGACCGGCTGGCTCATCATGGAGCTCGTCCAGGGGCGCGCCCTGTCCGACATCATCGCCGAGAAGGGGACCCTGTCGCCCGCGGAGATCCTGCCGGTCCTGGCGCAGGTGGCCCGCGCCCTGCAGGTCGTCCACGACTCCGGCGTCGTCCACCGGGACGTCAAGCCCTCCAACATCCTCATCAACCGCGAGGGCCTGGCCAAGCTCACCGACTTCGGCATCTCCACCGGCATCAACCAGCGCCCCCTGACGGCCTCCGGCATGGTCATGGGCACCGCCCAGTACCTCGCCCCCGAGCAGGCCATGGGGAACATGGCCACCCCGGCCGGCGACCTCTACGGGCTGGGCATCATCGCCTACGAGGCCCTGGTGGGGCGACGCCCCTTCAGCGGAGCCACCCAGGTCGATATCGCCTTCGCGCACGTCAACGAGGAGGTGCCCGCCCTCCCCGACGCCGTCCCGCCGCAGGTCCAGGCCATCATTCTCAAGCTGCTCGCCAAGAAGCCCTCCGACCGGCCGCACTCCGCCCGGGAGGTGGCCCGCGCCCTGGACCGGGCGGTGGTGAACCTCCCCACGGACGCGTGGGATCCCCGTGAGGCGCTCAGCTGGGAGGCCACCGGTCGCCGTGGCCCGCAGACCCGTGAGCTGCCCCGGCCGGCCACCGTGCGTCCCGGCCGTCACGCAGCCGAGGAGCCGACGCCGTCGCGCACCGCCCGGCACGCCTCAGGGCGCTCCTTCCTTGGCCTCAACCTGCTGACGCTGAGGGTCGTCATCCCGGCGCTCGCGCTCATCACCCTGCACAGCACGGGTACGCTTGCCCATGCGCATCAGGTCATGCCAGCCTTGATGCTGAGCATCCCTGTCAAGGAGGTACTGTGA","VKPVAGLQLQGRYELVEQIALGGMGQVWRATDLRSGRAVAAKILRPELTGDEIFLSRLRAEAKNSKGLRHPNLAVVLDSGEKDGTGWLIMELVQGRALSDIIAEKGTLSPAEILPVLAQVARALQVVHDSGVVHRDVKPSNILINREGLAKLTDFGISTGINQRPLTASGMVMGTAQYLAPEQAMGNMATPAGDLYGLGIIAYEALVGRRPFSGATQVDIAFAHVNEEVPALPDAVPPQVQAIILKLLAKKPSDRPHSAREVARALDRAVVNLPTDAWDPREALSWEATGRRGPQTRELPRPATVRPGRHAAEEPTPSRTARHASGRSFLGLNLLTLRVVIPALALITLHSTGTLAHAHQVMPALMLSIPVKEVL$","Serine/threonine protein kinase","Cytoplasm, Membrane","serine/threonine-protein kinase","serine/threonine protein kinase ","protein kinase","","Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995. 9(8):576-596. PMID: 7768349Hunter T. Protein kinase classification. Meth. Enzymol. 1991. 200:3-37. PMID: 1835513Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth. Enzymol. 1991. 200:38-62. PMID: 1956325Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988. 241(4861):42-51. PMID: 3291115Knighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991. 253(5018):407-414. PMID: 1862342","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[22-256]T$	Q83H76_TROW8_Q83H76;
PF00069	$\"[13-266]T$	Pkinase
PS50011	$\"[13-271]T$	PROTEIN_KINASE_DOM

InterPro
IPR001220
Domain

Legume lectin, beta domain
PS00307	$\"[73-79]?$	LECTIN_LEGUME_BETA

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[132-144]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[65-255]T$	no description
PTHR22986	$\"[10-260]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES

","No hits to the COGs database.","***** IPB000961 (Protein kinase C-terminal domain) with a combined E-value of 3.7e-27. IPB000961A 12-46 IPB000961C 115-157 IPB000961D 171-212***** IPB003527 (MAP kinase) with a combined E-value of 1e-21. IPB003527A 40-82 IPB003527C 108-158 IPB003527D 189-231***** IPB008266 (Tyrosine protein kinase, active site) with a combined E-value of 6.7e-20. IPB008266A 119-159 IPB008266B 177-213***** IPB000959 (POLO box duplicated region) with a combined E-value of 2e-17. IPB000959A 13-58 IPB000959C 119-158 IPB000959D 175-229***** IPB000861 (PKN/rhophilin/rhotekin rho-binding repeat) with a combined E-value of 7.7e-15. IPB000861D 91-144 IPB000861E 177-226***** IPB001772 (Kinase-associated, C-terminal) with a combined E-value of 4e-14. IPB001772A 10-41 IPB001772B 73-127 IPB001772D 182-221***** IPB013695 (Wall-associated kinase) with a combined E-value of 9.9e-11. IPB013695I 125-161 IPB013695J 162-211***** IPB010513 (Ribonuclease 2-5A) with a combined E-value of 1.4e-08. IPB010513D 123-144 IPB010513E 194-214***** IPB000095 (PAK-box/P21-Rho-binding) with a combined E-value of 2.7e-08. IPB000095D 96-142 IPB000095E 155-199***** IPB000472 (Domain in TGF-beta receptor/activin receptor, type I/II) with a combined E-value of 7.5e-08. IPB000472D 129-159 IPB000472E 172-183***** IPB013896 (Ubiquitin-associated region 2) with a combined E-value of 5.4e-07. IPB013896A 9-40 IPB013896D 114-146***** IPB013543 (Calcium/calmodulin dependent protein kinase II, association-domain) with a combined E-value of 1.6e-06. IPB013543A 3-48 IPB013543D 111-147***** IPB001824 (Receptor tyrosine kinase, class III) with a combined E-value of 5.9e-06. IPB001824F 112-165***** IPB005189 (Focal adhesion targeting region) with a combined E-value of 9e-06. IPB005189K 119-161","","","-55% similar to PDB:1MRU Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB. (E_value = 1.6E_47);-56% similar to PDB:1O6Y CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 3.5E_47);-56% similar to PDB:2FUM Catalytic domain of protein kinase PknB from Mycobacterium tuberculosis in complex with mitoxantrone (E_value = 3.5E_47);-52% similar to PDB:2H34 Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE (E_value = 2.3E_38);-45% similar to PDB:1F3M CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1 (E_value = 2.8E_20);","Residues 13 to 266 (E_value = 1.8e-50) place ANA_2186 in the Pkinase family which is described as Protein kinase domain.Residues 13 to 158 (E_value = 3.2e-11) place ANA_2186 in the Pkinase_Tyr family which is described as Protein tyrosine kinase.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2187","2358591","2360633","2043","5.07","-24.06","70665","GTGACCAGTCAGTTCCCCCAGGTCCTCGCGGGCCGTTACGAGATCCGCGACCTCATCGGACGTGGTGGTATGGCAGAGGTGCACCTCGGCTACGACACTCGCCTGTCGCGGGTCGTGGCCATCAAGTTGCTGCGTTCGGACATCGCCGGCGACCCCACCTTCCAGGCCCGCTTCCGCCGAGAGGCCCAGTCCGCGGCGGCGCTCAACCACCCCGCCGTCGTCGCCGTCTACGACTCCGGGGAGGAGGAGCTCCTCCAGCCCGGTGGCGCCAGCCGCACCGTCCCCTACATCGTCATGGAGTACGTCGAGGGGCACACGGTGCGTGAGCTCCTCAGCGAGGGCGAGGCCGTCCCGATCGCGGAGGCCGCGGAGATCGTCTCCGGGGTCCTGGACGCCCTGGAGTACTCCCACCGGGTGGGGATCGTCCACCGTGACATCAAGCCCGGAAACATCATGCTGACCTCCACCGGCGCGGTGAAGGTCATGGACTTCGGCATCGCGCGGGCCATTGAGGACTCCGCCTCCACGGTCACCCAGACCCACACGGTGGTGGGCACCGCCCAGTACCTCTCCCCGGAGCAGGCTCGCGGCGAGTCCGTGGACGCCCGCTCGGACCTGTACTCCACCGGCTGTCTTCTCTACGAGCTGCTCACCGGCCAGCCGCCTTTCCAGGGCGACTCTGCCGTGGCCATCGCCTACCAGCACGTGCGGGAAATCCCCAAGCGCCCCTCGTCCCTGGCGGCCGATGTGCCCGAGTCCCTGGACCGGGTGATCCTCAAGTCGCTGGCCAAGAGCCGCGAGGACCGCTACCAGGACGCCGCCCACATGCGCGCCGACCTGCAGGCGGCCGTCCGGGGCCTGTCCGTGGCCGCGCCGGCCGCCGACTCCTGGTCCCCGGCCACCTCGGTCATGGCCTCACCGGAGGCCGAGCCGGTTCAGCCCACCTCCACCTTCGCCCAGGTGGCCTCCGGGTCCTCTCCGATGCAGGCGGCCAAGGAAGCCGAGGAGCCCGAGGAGAAGCCCAAAAGCCACGCCTGGGTCTGGATCCTCGTGTTCCTGCTGTTCATGGCCCTGGCCGTCGCCGGCGGGCTGTGGGCCTCCGGGGCCTTCGACTCTCACCCCACCCCGACACCGAGCCCCACCATCAGCAAGGTGGAGGTCCCCGACACCTCCGGTCAGGACGAGGAATCGGCCCGGAAGACCATCGAGGGCGCCGGCCTGAAGTTCGCCAAGGACGAGGTCGCCAACGAGGAGGTCAGCGCGGGCCTGGCCGTCTCCTCCGACCCGGGCAAGGGCACGAAGGTCGAGCCGAACTCCACCGTCACCGTCCACTTCTCCACCGGATCCGCCATGGTCAAGGTTCCCGACTTGACCGGCAAGACCCAGGAGGACGCCCGCAAGGCCCTCAAGGACGCCGGGCTCGAGGGTGGAAACACCTCTCAGGAGGACTCCGCCACGGTCGCCAAGGACCGGGTCATCTACACCAACCCGCCGGCGGGGAACTCCGTTGCGCGCGGCACCACGGTGGACCTGGTGCTCTCCACCGGCAATACCTCCGTCCCCGACGTCTCCGGCCAGGACGAGGCCACGGCGAAGAAGACCATTGAGGACGCCGGCCTGCAGTTCAAGAAGGGCGACGACGTCGCCTCGGCGGAGGTCGAGCGCGGCAAGGCCGTCTCCTCCGACCCGGCCGCGGGCTCCAGCGCCTCCTCCGGAGACACGATCACCGTGCACTTCTCCAGCGGCGCGGCCACGCAGGCGCCGACCGGTCCCGTGACGATTCCCAAGAACCTCAACGGCAAGACCGTCGAGGAGGCAACTGCCGAACTGCAGAAGCTCGGACTCAACGTCACCGTGGACTACAAGTCCTCTGACAAGGTGGATGCCAATAAGGTCATCGGTACGAGCCCGAAGGCCGGAGACCAAGTGCCCGCCGGTTCGACCGTTAACCTCACGGTCTCCAGCGGTAAGGACGGCGGAGGCGGCGACAACCAGCAACCGGGCAACCCCAATCCTGGCGGCGGAGGCGGAGGCGTCAACTGA","VTSQFPQVLAGRYEIRDLIGRGGMAEVHLGYDTRLSRVVAIKLLRSDIAGDPTFQARFRREAQSAAALNHPAVVAVYDSGEEELLQPGGASRTVPYIVMEYVEGHTVRELLSEGEAVPIAEAAEIVSGVLDALEYSHRVGIVHRDIKPGNIMLTSTGAVKVMDFGIARAIEDSASTVTQTHTVVGTAQYLSPEQARGESVDARSDLYSTGCLLYELLTGQPPFQGDSAVAIAYQHVREIPKRPSSLAADVPESLDRVILKSLAKSREDRYQDAAHMRADLQAAVRGLSVAAPAADSWSPATSVMASPEAEPVQPTSTFAQVASGSSPMQAAKEAEEPEEKPKSHAWVWILVFLLFMALAVAGGLWASGAFDSHPTPTPSPTISKVEVPDTSGQDEESARKTIEGAGLKFAKDEVANEEVSAGLAVSSDPGKGTKVEPNSTVTVHFSTGSAMVKVPDLTGKTQEDARKALKDAGLEGGNTSQEDSATVAKDRVIYTNPPAGNSVARGTTVDLVLSTGNTSVPDVSGQDEATAKKTIEDAGLQFKKGDDVASAEVERGKAVSSDPAAGSSASSGDTITVHFSSGAATQAPTGPVTIPKNLNGKTVEEATAELQKLGLNVTVDYKSSDKVDANKVIGTSPKAGDQVPAGSTVNLTVSSGKDGGGGDNQQPGNPNPGGGGGGVN$","Serine/threonine protein kinase","Periplasm, Membrane, Extracellular","serine/threonine protein kinase BH2504","putative serine/threonine protein kinase ","protein kinase","","Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995. 9(8):576-596. PMID: 7768349Hunter T. Protein kinase classification. Meth. Enzymol. 1991. 200:3-37. PMID: 1835513Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth. Enzymol. 1991. 200:38-62. PMID: 1956325Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988. 241(4861):42-51. PMID: 3291115Knighton D.R., Zheng J.H., Ten Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 1991. 253(5018):407-414. PMID: 1862342","","","

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[13-269]T$	Q81ZX9_STRAW_Q81ZX9;
PF00069	$\"[13-280]T$	Pkinase
PS50011	$\"[13-284]T$	PROTEIN_KINASE_DOM
PS00107	$\"[19-42]T$	PROTEIN_KINASE_ATP

InterPro
IPR005543
Domain

PASTA
PF03793	$\"[385-447]T$ $\"[452-515]T$ $\"[518-581]T$ $\"[592-655]T$	PASTA
SM00740	$\"[381-447]T$ $\"[448-515]T$ $\"[516-581]T$ $\"[589-655]T$	PASTA
PS51178	$\"[381-447]T$ $\"[448-515]T$ $\"[516-581]T$ $\"[590-655]T$	PASTA

InterPro
IPR008271
Active_site

Serine/threonine protein kinase, active site
PS00108	$\"[141-153]T$	PROTEIN_KINASE_ST

noIPR
unintegrated

unintegrated
G3DSA:1.10.510.10	$\"[103-286]T$	no description
G3DSA:3.30.200.20	$\"[5-101]T$	no description
PTHR22986	$\"[12-269]T$	MAPKK-RELATED SERINE/THREONINE PROTEIN KINASES
tmhmm	$\"[345-365]?$	transmembrane_regions

InterPro
IPR006139
Domain

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region
PF00389	$\"[25-278]T$	2-Hacid_dh

InterPro
IPR006140
Domain

D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02826	$\"[64-246]T$	2-Hacid_dh_C
PS00065	$\"[112-139]T$	D_2_HYDROXYACID_DH_1
PS00670	$\"[163-185]T$	D_2_HYDROXYACID_DH_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.260	$\"[280-360]T$	no description
G3DSA:3.40.50.720	$\"[56-246]T$	no description
PIRSF000121	$\"[1-360]T$	D-3-phosphoglycerate dehydrogenase with ACT domain
PTHR10996	$\"[1-346]T$	2-HYDROXYACID DEHYDROGENASE
PTHR10996:SF10	$\"[1-346]T$	D-3-PHOSPHOGLYCERATE DEHYDROGENASE

","BeTs to 20 clades of COG0111COG name: Phosphoglycerate dehydrogenase and related dehydrogenasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0111 is aompkzyqvdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is 1","***** IPB006139 (D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain) with a combined E-value of 8.4e-56. IPB006139A 23-61 IPB006139B 106-134 IPB006139C 160-173 IPB006139D 180-233 IPB006139E 237-246","","","-58% similar to PDB:1WWK Crystal structure of phosphoglycerate dehydrogenase from Pyrococcus horikoshii OT3 (E_value = 5.6E_39);-51% similar to PDB:1SC6 Crystal Structure of W139G D-3-Phosphoglycerate dehydrogenase complexed with NAD+ (E_value = 2.1E_38);-51% similar to PDB:2P9C Crystal structure of serine bound G336V mutant of E.coli phosphoglycerate dehydrogenase (E_value = 6.2E_38);-51% similar to PDB:2P9E Crystal Structure of G336V mutant of E.coli phosphoglycerate dehydrogenase (E_value = 6.2E_38);-51% similar to PDB:2PA3 crystal structure of serine bound G336V mutant of E.coli phosphoglycerate dehydrogenase (E_value = 6.2E_38);","Residues 25 to 278 (E_value = 2e-14) place ANA_2188 in the 2-Hacid_dh family which is described as D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.Residues 64 to 246 (E_value = 1.5e-48) place ANA_2188 in the 2-Hacid_dh_C family which is described as D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain.","","specific 2-hydroxyacid dehydrogenase (serA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2189","2363791","2362712","1080","4.87","-13.08","38297","GTGCGCGTCTTCAATTTCTCCGCCGGTCCCGCCCAGCTCCCTCTGCCCGTCCTCGAACAGGCCGCCTCCGAGCTCACCAGCTGGGGCGGATCGGGAATGTCCGTCCTGGAGGTCTCCCACCGCGGAGCCGACTTCGTGGCCTGCGCGGCCGACGCCGAGGCCACCCTGCGCCGCCTCCTGTCCGTTCCCGAGGGCTACCGTGTGCTCTTCCTTCAGGGCGGCGCCAGCGCACAGTTCGCCGGCATCCCCCTCAACCTGACCGCCCCCGGTGACACGGTCGCCTACCTCAACACCGGCCAGTGGTCCGCCAAGGCCATCAAGCAGGCCGGAGCCTACGAGCTCGACGTCGTCGTGCCGGCCGACGAGGCCGCCTCCTCTTACACGACCACCCCCGAGCCCGGCTCCTTCTCGGTGCCCGAGACCGCCCGCTACCTGCACTACACGCCCAACGAGACCATCGGCGGCGTCGAGTTCGACTACGTGCCCGAGGCCGGCGAGGTCCCGCTGGTGGCCGACTTCTCCTCCACGATCCTCTCGAGGCCCATCGACGTCTCCCGCTACGGCCTCATCTACGCCGGGGCTCAGAAGAACATGGGGCCCTCGGGCCTGGCCGTCGTCATCGTGCGCGAGGACCTGCTGGGGCGGGCCCGCCCGGTGACCCCCACCGTCCTGGACTACCAGAAGATGGCCGACGCCGACTCCATGCTCAACACGCCCCCCACCTTCGCCATCTACCTGCTGGGGCTCATCGGCCACTGGATCGAGGACGGCGGCGGCCTGGAGGCAATGGCCGAGCGCAACCGCGCCAAGGCCGAGCTCCTCTACGGCTACATCGACTCCTCCGACTTCTACGCCAACCCCGTTCAGGAGCGCTCGCGGTCCTGGATGAACGTGCCCTTCACCCTGGCCGACCCCGCCCGCGACGCCGACTTCCTGGCCGGCGCCCAGGCCGCCGGGCTCACCAACCTCAAGGGGCACCGCTCCGTGGGCGGCATGCGCGCCTCCATCTACAACGCCATGCCGATTGAGGGCGTGCGCGCCCTCATCGACTACATGACCGACTTCGCCGCCCGGGCCTGA","VRVFNFSAGPAQLPLPVLEQAASELTSWGGSGMSVLEVSHRGADFVACAADAEATLRRLLSVPEGYRVLFLQGGASAQFAGIPLNLTAPGDTVAYLNTGQWSAKAIKQAGAYELDVVVPADEAASSYTTTPEPGSFSVPETARYLHYTPNETIGGVEFDYVPEAGEVPLVADFSSTILSRPIDVSRYGLIYAGAQKNMGPSGLAVVIVREDLLGRARPVTPTVLDYQKMADADSMLNTPPTFAIYLLGLIGHWIEDGGGLEAMAERNRAKAELLYGYIDSSDFYANPVQERSRSWMNVPFTLADPARDADFLAGAQAAGLTNLKGHRSVGGMRASIYNAMPIEGVRALIDYMTDFAARA$","Phosphoserine aminotransferase","Cytoplasm, Extracellular","Phosphoserine aminotransferase (PSAT)","phosphoserine aminotransferase ","phosphoserine aminotransferase","","Ouzounis C., Sander C. Homology of the NifS family of proteins to a new class of pyridoxal phosphate-dependent enzymes. FEBS Lett. 1993. 322(2):159-164. PMID: 8482384","","","

InterPro
IPR000192
Family

Aminotransferase, class V
PF00266	$\"[3-348]T$	Aminotran_5
PS00595	$\"[187-206]T$	AA_TRANSFER_CLASS_5

InterPro
IPR003248
Family

Phosphoserine aminotransferase
PD001544	$\"[240-358]T$	SERC_BORPE_Q7VZG4;
TIGR01364	$\"[3-359]T$	serC_1: phosphoserine aminotransferase

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[2-256]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[257-358]T$	no description

noIPR
unintegrated

unintegrated
PTHR21152	$\"[2-359]T$	AMINOTRANSFERASE CLASS V
PTHR21152:SF1	$\"[2-359]T$	PHOSPHOSERINE AMINOTRANSFERASE

","BeTs to 10 clades of COG1932COG name: Phosphoserine aminotransferaseFunctional Class: H [Metabolism--Coenzyme metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1932 is ------y---rlb-efghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003248 (Phosphoserine aminotransferase) with a combined E-value of 1.6e-159. IPB003248A 3-42 IPB003248B 56-86 IPB003248C 93-112 IPB003248D 141-158 IPB003248E 177-213 IPB003248F 235-284 IPB003248G 311-355","","","-66% similar to PDB:1BJN STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM ESCHERICHIA COLI (E_value = 7.2E_103);-66% similar to PDB:1BJO THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE (E_value = 7.2E_103);-63% similar to PDB:1BT4 PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS SUBSP. ALKALOPHILUS (E_value = 7.0E_90);-63% similar to PDB:1W3U CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS VAR. ALKALOPHILUS (E_value = 7.0E_90);-63% similar to PDB:2C0R CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS VAR. ALKALOPHILUS AT PH 8.5 (E_value = 7.0E_90);","Residues 3 to 348 (E_value = 2.7e-43) place ANA_2189 in the Aminotran_5 family which is described as Aminotransferase class-V.","","aminotransferase (PSAT) (serC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2190","2364188","2365627","1440","6.53","-3.25","51710","ATGTTCGACCGGCTCCGCAGGGGACGCAAGCCGCGCCTGGGCGCCATCCTCATGGCACTGGTCGCCGTGGTGTCCCTGGCCACCGGGTTCCGGGCCTGCAACTGCAACCGGGCCTGGACGGAGGTCTCCGCGGCGGCCACCCCGGAGGCTAACCCGCTCAAGGGCATGATGCCCTTCGCGCCGGCGGACGCCTCCCACTCACCGGCACTGCAGGACAACGCCCCGCCCCACACGATGGAGTGGCTGACGCTGCCGGTCAGCGACGTCGTCACCGGACCCGGCTCGTACGCGTGGGACAAACTCGATGCGCACCTCAACGCCATCGCCTCGCGCGGGCACCAGGCGGTGCTGCGCTTCTACGTCGACTACCCCGGGCGCCCCAGCGGCATCCCGGCCTATCTGCTGAGCTCCCACGCGGTGCCGACCCACGAGTACACGTTCAACGGCAACGCACCGGGCCAGTCGCTGGCGCCGGACTACAACGATCCCGAGATGATGTCGATGCTCACCGGCTTCGTCTCAGCCCTGGGCCAGCAGTACGACGGCGACCCGCGCCTGGCCTTCATCACCCACGGCCTGGTGGGCTTCTGGGGTGAGGGGCACACCTACCCGATGAACGGCAAGGTCTCCGGGGAGAACCCCTCCGGCGAGAACTGGATGCCGTCGGCGGCGAACCAGAACACGCTCATCGACACCTGGGACGGCGCCTTCCAGGTGACGCCGACGCTGGCGCGATACCCGTCCGCGGAGACGGTCAAGCGCGGGGTCGGCTACCACGACGACTCCTTCGGCTACGCCACGATGGACACCGCCGACTGGCACTTCCTGCCGAAGCTGAAGGAGGCCAAGGCGGACCAGGCCTGGCAGCAGCACCCGATCGGCGGCGAGGTCTACCCGGGCATCCAGGAGTGCTCCGTGCGCAACCCGGGCAGCTGCATGGCCTCGGGCTCCAACGGAGGAACGGTGGACATCAACGCCTCCATCAAGGCCACGCACGCGAGCTGGCTGGTGGACAACTGGGCCTTCACCACGACCCTCAACGGCTCCGAGCGCGAGCGGACCGTGCAGGCCTCCGCCGAGACCGGCTACGACCTCGCGGTGGCGCGCTGGCGGATGCGCAACGGCAAGATCGAGGTGCAGATCGCCAACAACGGGGTGGCGCCCTTCTACTACAACTGGAACGTGGAGGCGGTGGCCATCAACACCTCCAACGGCATGGAGGTCGGGCGCACCACGCTCAGCGGCGACCTGCGCAAGGTCGCGGTCGGCAAGACCCAGACCTTCTCCGGGCAGCTCCCGGCGGACCCGGCCGGACAGAACACGATCCTGGTGCGCGTGGTCAACCCGCTCGACTCGGGTCAGCCGCTGCGCTTCTCCAGCGCCGGCCAGGATCAGACGCTGCCCGGCTACCTCACCCTGGGCCGCACCCCCACCAAGTAG","MFDRLRRGRKPRLGAILMALVAVVSLATGFRACNCNRAWTEVSAAATPEANPLKGMMPFAPADASHSPALQDNAPPHTMEWLTLPVSDVVTGPGSYAWDKLDAHLNAIASRGHQAVLRFYVDYPGRPSGIPAYLLSSHAVPTHEYTFNGNAPGQSLAPDYNDPEMMSMLTGFVSALGQQYDGDPRLAFITHGLVGFWGEGHTYPMNGKVSGENPSGENWMPSAANQNTLIDTWDGAFQVTPTLARYPSAETVKRGVGYHDDSFGYATMDTADWHFLPKLKEAKADQAWQQHPIGGEVYPGIQECSVRNPGSCMASGSNGGTVDINASIKATHASWLVDNWAFTTTLNGSERERTVQASAETGYDLAVARWRMRNGKIEVQIANNGVAPFYYNWNVEAVAINTSNGMEVGRTTLSGDLRKVAVGKTQTFSGQLPADPAGQNTILVRVVNPLDSGQPLRFSSAGQDQTLPGYLTLGRTPTK$","Hypothetical protein","Periplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[15-33]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-42% similar to PDB:2TBV STRUCTURE OF TOMATO BUSHY STUNT VIRUS. V. COAT PROTEIN SEQUENCE DETERMINATION AND ITS STRUCTURAL IMPLICATIONS (E_value = );-49% similar to PDB:1OD2 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN (E_value = );-49% similar to PDB:1OD4 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN (E_value = );-49% similar to PDB:1UYR ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN COMPLEX WITH INHIBITOR DICLOFOP (E_value = );-49% similar to PDB:1UYS ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN COMPLEX WITH INHIBITOR HALOXYFOP (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2191","2368488","2367055","1434","7.48","1.98","51398","GTGACCTGGGCCAGGAGATCGGTTGGAACGGCGCCACCGTTGTCACGATCACCCACGACTCCCCGCTGGGAAAGATCATCCTGGACGTCGACGGGCGCAAGACTGACGGACGCAGCGATGAGTGATCTGACCATCACGGCTTCATTCCCCCTCGGAGAGTTCAACGCGCACGATGGAGAGGGGTGCGCTGAATGGCCGCCGGCTCCAGCGCGGGTACTGGCCGCAATGCTGTCTGCCGCCCATGGCCTCGGAGAAGGCGCTTCCGAGGTCGAGGCTCTCTTTCGATGTCGTCCTCCACGGATCACCGCCCCTCCGGCCGGTGAGCGTCAGATCGGTTACCGGCGGTGGGTCCCCGTCAACAATGAGTTGAAGATGGACAAGAACGGTTCGCTGACCGGGATTGTCGACCGGCCCTGGCGATTCCTGGAGAAGCAGGCGAAGGATCCCGAGTGCGGCATGATGGTCGGTACCGGTCCGAGCAACGTCGTGCGATGGGCCTTCGCCGTTGAGGACCAGGTCGATCTGGGCGTTCTGCAGAAGGTGGCGCGGTCCGTGGAGTACCTCGGGCGTCCGACCTCACCTGTGCTGCTCGACGTCGTCGACGGTGCTGTCGAGGTGCCTCCTGGCCATTCCTGTTGGGAACCGGACCCGACGGGCTGGATCCAGCTGCGTGTGGGAACGGAAGGACTCCTGGCTGCTTTGGATGCCCGAGAGGAGGAGCGGCGCCGCAGTACCGTGACGGGGACGCATCCATATATGAGCGTGCGACCCACCGCCCCCTACCGGCTCGTGGGTGTGCAGTACGGTGATAGGGCTGCGCCTGATACTCGGGAGCTGCTGCGCACGTGCTCGCTCTACCGAATGCCCCACAGTGGGCGACAAGGTGCAGTTCTGGTGCATGCCGCTGACGCTGCTCTCGTCACGGAGCAGCTGCGAGACTCCCTTGAAGAAACAGGCTGGATGCTGCCAATCATCGGTGGGTTGGGTCGCCGCCACCTGCCCGTCCTGCGGGGGGTGCTCGTGGCCGGGGGGTCTCGGCTTCCATCCGTGGGGCTCGCGGTGAGAACGGGGGTGGTTGAGGCCAGACTCGCCGAGACCAGGACGATGGCTTCTCTGCCTCGAGTTCTGCGAGCCGCTACGGCTCCTTCGTTACGGTGGACCACTGTTGTGCCGACGGCGGAGGATCCTGAAGGCATTGTGTCCTTGTTGGAGGAATGCGCCTCGGGGCTCGGCTGCAGACTTGTTGGGGCTGAGCGTCACTCCGACTCACGAAGCGACGGAGGTATCGATGTGCAGGAGAACAACGGGCGCTGGCACGTCTCGGTCGCCTTCGACGCGAAAGTGCCCGGGCCGGTGGTCTTTGACGGCGCCCTCATGGTTCCCCTGGGGGCCACCACCTTGGCAGTGAACCCACGGCGACCCCGAACCGACTAA","VTWARRSVGTAPPLSRSPTTPRWERSSWTSTGARLTDAAMSDLTITASFPLGEFNAHDGEGCAEWPPAPARVLAAMLSAAHGLGEGASEVEALFRCRPPRITAPPAGERQIGYRRWVPVNNELKMDKNGSLTGIVDRPWRFLEKQAKDPECGMMVGTGPSNVVRWAFAVEDQVDLGVLQKVARSVEYLGRPTSPVLLDVVDGAVEVPPGHSCWEPDPTGWIQLRVGTEGLLAALDAREEERRRSTVTGTHPYMSVRPTAPYRLVGVQYGDRAAPDTRELLRTCSLYRMPHSGRQGAVLVHAADAALVTEQLRDSLEETGWMLPIIGGLGRRHLPVLRGVLVAGGSRLPSVGLAVRTGVVEARLAETRTMASLPRVLRAATAPSLRWTTVVPTAEDPEGIVSLLEECASGLGCRLVGAERHSDSRSDGGIDVQENNGRWHVSVAFDAKVPGPVVFDGALMVPLGATTLAVNPRRPRTD$","CRISPR-associated protein, GSU0054 family","Cytoplasm, Periplasm","CRISPR-associated protein, GSU0054 family","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
TIGR02165	$\"[43-463]T$	cas_GSU0054: CRISPR-associated protein, GSU

InterPro
IPR013403
Family

CRISPR-associated protein GSU0053
TIGR02570	$\"[19-234]T$	cas_GSU0053: CRISPR-associated protein, GSU

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.1210	$\"[58-164]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-41]?$	signal-peptide

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[339-422]T$	Helicase_C

InterPro
IPR003607
Domain

Metal-dependent phosphohydrolase, HD region
SM00471	$\"[725-796]T$	HDc

InterPro
IPR013444
Family

CRISPR-associated helicase Cas3, Anaes-subtype
TIGR02621	$\"[3-922]T$	cas3_GSU0051: CRISPR-associated helicase Ca

","BeTs to 8 clades of COG1203COG name: Predicted helicasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1203 is a-m-kz-qv--lb-e--h--------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 339 to 422 (E_value = 0.0039) place ANA_2195 in the Helicase_C family which is described as Helicase conserved C-terminal domain.","","CRISPR-associated helicase Cas3","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2196","2374323","2375633","1311","8.98","5.88","47773","ATGACCACCTACCAGCCGCGTCTCATGGACCAGCGCCTCGAGGAGCTGCTGCGGTCGGTCCCGGCGGTCAGCGTCGAGGGAGCCCGCGCCGTCGGGAAGACCCGCACCGCCAGGGCCCACGGCACTACCTTCATTGCCGTTGACGATCCCGATGAACGCGCCCAGCTCGCCGCCATCGGATCGCGCTTCACCACTCTTCCCAGTCCTCTCGTCATCGACGAGTGGCAACGCATGCCCGAGCTGTGGGACCGGGTACGTCGCGCTGTCGACGACGATCCCTCTCCCGGCCGTTTTCTGCTCACTGGGTCCTCCACACCGTCCCAGGCCCCCACCCACACCGGCGCAGGACGGATCATCACTCTCAGGATGCGTCCCTTCAGCCTGGCCGAGCGCGCGATCGAGACTCCAACGGTCTCGGTGGGGCGCCTGTTAGGCAGTGGTCTCGGCACTCAGGATCTCTCCGCCCTGACCCCGATCGAGGGGTACACGAGTGTCACGATCGACCAGTACGTCGATGAGATCTGCCGCTCCGGCTTCCCCGCCATCAGGGAGCAGCCGCCTTTGGGGCGCAAGGCCCAGCTGGACGGATACATCGAGCAAACACTCCGACATGATCTACCGGAGGCGACGGGCGGCAGGCAACGCTCACGAACCGTGAGGGAGTGGCTGACAGCCTACGCCAGCGCAGTGGCCACAACGGCGAGCTTCACCTCCATCGCCGAGCTGGCGACCAGACCCCTGAGCACCGACATGGGCTTGGCGACAGCACGCTCCTACCGAGACCATCTCAGCGGGATGTGGCTGCTGGACCCGGTTCCGGGCTGGAGCCCCAGCGAGAACGAGTTCTCCCGCAACAACCTGACCGACAAGCACCAGCTGTGCGACCCGGCCCTGGCCGCTCGCCTTCTCGGATACGGCCCCGCCGAGGTTCTCGGGGTCGGACACCCGATCCTCACCAGCCCTCGGGGCACCCCGCGCCGCCCCCGAGTACTCGGCTCACTATTCGAGTCCCTGGTGATTCAAAGTCTTCAGGTCTACGCAGAGGTCCTCAGCGCCCGGGTCTTCCACCTGCGCACCAAAGGCGGGCTCCAGGAGATCGACATCATCCTCGAAGGAGCCGACCGTCGGGTCGTCGCCTTCGAGATCAAGGCAAGGGCCACCCCCAAGCCGGAGGACACCAAGCACCTGCGCTGGCTGCGCAAGAAGATCGGCCCGAGGCTCGCAGACGCAGTGCTGGTGACCACCGGCCGTCTGGCCTACCGGGACGAGGACGGGATCGCCGTCGTGCCCGCCGCCCTGCTGGGACCGTAG","MTTYQPRLMDQRLEELLRSVPAVSVEGARAVGKTRTARAHGTTFIAVDDPDERAQLAAIGSRFTTLPSPLVIDEWQRMPELWDRVRRAVDDDPSPGRFLLTGSSTPSQAPTHTGAGRIITLRMRPFSLAERAIETPTVSVGRLLGSGLGTQDLSALTPIEGYTSVTIDQYVDEICRSGFPAIREQPPLGRKAQLDGYIEQTLRHDLPEATGGRQRSRTVREWLTAYASAVATTASFTSIAELATRPLSTDMGLATARSYRDHLSGMWLLDPVPGWSPSENEFSRNNLTDKHQLCDPALAARLLGYGPAEVLGVGHPILTSPRGTPRRPRVLGSLFESLVIQSLQVYAEVLSARVFHLRTKGGLQEIDIILEGADRRVVAFEIKARATPKPEDTKHLRWLRKKIGPRLADAVLVTTGRLAYRDEDGIAVVPAALLGP$","ATPase, AAA+ superfamily","Cytoplasm","conserved hypothetical protein","hypothetical protein","ATPase (AAA+ superfamily)-like","","","","","No hits reported.","BeTs to 4 clades of COG1373COG name: Uncharacterized ATPases of the AAA superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1373 is --mpk---v-r------h--uj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2197","2377185","2375677","1509","5.09","-21.93","55751","ATGATTCACCACATCACCCTGACCGGGCGCAGCATCGCCCTGGCCTGCGACGGCACGGTGACCACCCAGCACGGGGCCGGCGGGGCCACCGGCGCGGTCTACGTCGAGGCCTCCCACCTGACCCTCCTGCACGACATGCGCGATGGCGAGTTCTACCGCACCGGCCAGAACTCTTGGTCGCCGTCGGGCTGGCGCCGCCTGAGCGAGGCGCCCATGCGCATCGCCAACGAGCAGCGCCGCCGGACCGCCGACGACGCCCCCTGGGACGACCCGGCCCGCCACCACTCGGCCTGGATGGCGGTCCTGGAGGACTCCGCCGGGGCGCTGCTCGTGGGCTGCCTGGACGGGCGCACGCCGCGGCTGCGCGCCGACACCGCGGTCCTGGAGGCCTTCACCGAGTCCGGTGACCCGGCGCGCTGGGTGATCCTGCCCGGCCCCGCCACCGCCGTCATGGCCCGCTACGCGCGCGAGCTCGGCGAGAGCCTGGGGAGCCGGGCGATCGAGCCGCAGAGCGTGTGGTGCTCCTGGTACTCCTACTACGAGGGCATCTCGCAGGAGGCCCTCGAGCGCGAGATCCCGCAGGTCGCCGAGCTGGGCTTCAAGACGCTTCAGATCGACGACGGCTGGGAGGTCGCGGTCGGCGACTGGGAGGCCGGCGAGAGCTTCAGCGACGGCATGGAGGCCGCCGCGAGTCGGATCCGGGAGGCCGGCATGCAGCCGGGCCTGTGGGTGGCACCCTTCATCGCCCTGCCCGGCTCACGGGCCGTGCGCGACTACCCGGAGATGTTCGTCCACAATGCCGACGGCGGACTGGCCGTGGCCGGCTCCAACTGGGGCGGCGACTACTACGCGCTGGACACGACCCACCCCACCGCCCAGACCTACGTGCGCAAGCTCATCGCCAAGATCGTCCACCGGTGGGGCTTCAGCTACCTCAAGCTCGACTTCATCAACGCCGCCGCCATCCCCGGCTACCGGCACCGCCAGATCGACCGGGAGGAGGCCTACCGCACCGGGCTGCGGCTCGTGCGCGACACGGCCGGGGAGGAGACCTTCCTCCTGGGGTCCGGGGCGCTCATCATGCCCTCCATCGGGCTGCTCGACGCGGTGCGGGTGGGGCCGGACGTGGCCCCCATGTGGGAGAACTACGCCTCCGACGACTTATCCGACGCCAAGGCCTACAACGCCCTGCACGCCGGCATCAACCGGCTCTGGCTGGGGCGGGTCATCGGGGTCGATCCCGACGTCGTCTTCTTCCGCCACCGCCGCAACCTCCTGGACGACACCCAGATGCAGTGGCTGCGCGACGTGGCCGAGGCCAGCCGCTACCGGTGCCTGTCGGACCAGATGACCTGGCTCGATGAGGAGGAGAAGGAGGCCGTGCGCGCCTACCTGGCCGCCGAGGACGAGCCCCTGGAGATCCTGGGCCGCTACCGCTTCAGCCTGGGTGAGCGCGAGATCGACCTCACCGAGGCCATCGAGGGGACGCCGTCGGCCTACCCGCTGTGA","MIHHITLTGRSIALACDGTVTTQHGAGGATGAVYVEASHLTLLHDMRDGEFYRTGQNSWSPSGWRRLSEAPMRIANEQRRRTADDAPWDDPARHHSAWMAVLEDSAGALLVGCLDGRTPRLRADTAVLEAFTESGDPARWVILPGPATAVMARYARELGESLGSRAIEPQSVWCSWYSYYEGISQEALEREIPQVAELGFKTLQIDDGWEVAVGDWEAGESFSDGMEAAASRIREAGMQPGLWVAPFIALPGSRAVRDYPEMFVHNADGGLAVAGSNWGGDYYALDTTHPTAQTYVRKLIAKIVHRWGFSYLKLDFINAAAIPGYRHRQIDREEAYRTGLRLVRDTAGEETFLLGSGALIMPSIGLLDAVRVGPDVAPMWENYASDDLSDAKAYNALHAGINRLWLGRVIGVDPDVVFFRHRRNLLDDTQMQWLRDVAEASRYRCLSDQMTWLDEEEKEAVRAYLAAEDEPLEILGRYRFSLGEREIDLTEAIEGTPSAYPL$","Alpha-galactosidase","Cytoplasm, Extracellular","alpha-galactosidase","alpha-galactosidase ","glycoside hydrolase, clan GH-D","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR000111
Family

Glycoside hydrolase, clan GH-D
PF02065	$\"[147-468]T$	Melibiase

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[166-380]T$	no description

","BeTs to 3 clades of COG3345COG name: Alpha-galactosidaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG3345 is --------v---b---g---------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-49% similar to PDB:1ZY9 Crystal structure of Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (tm1192) from Thermotoga maritima at 2.34 A resolution (E_value = 6.5E_39);","Residues 147 to 468 (E_value = 0.0018) place ANA_2197 in the Melibiase family which is described as Melibiase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2198","2378541","2377342","1200","5.73","-13.76","43922","GTGCGTGAAGCATCAAGGCAGCTGCGGGTCGGCGTCGTCGGCATCGGGGCCCGCTGCTACCTGGCCGCGCTCGCGGACACCTCACCGGTCCCGGCCCGCCTCGTCGCTGCGGCCGACACCGCCCCCGACGCCGTCGAGCGCGCCCGGCGGCTCCTGCCCGAGGGCGTGGCGGTCGTGGCCGACCACCGCGACCTGCTGGGGCACGGGATCGACGCCGTCGTCCTGACCACGCCCGATGACACGCACGAGGAGCTGGCCTGTTTCTTCCTTGAGGCCGGTATCCCGGTCTACCTGGAGAAGCCCCTGGCCATCACCATCGAGGCCGCCGACCGCATCCTTGAGACCGCCCGGCGCACCGGCACCCGCCTCTACGTGGGCCACAACATGCGCCACATGGAGGTGGTGCGGCTGCTGAAGTCGATCATCGACTCGGGGCGGATCGGCGAGGTCAAGGCCATCTGGTGCCGCCACTTCGTGGGCAACGGCGGCGACTACTACTTCCGCGACTGGCACGCCGAGCGCCGCCACGTCACCGGCCTGCTGCTGCAGAAGGCCGCCCACGACATCGACGTCATGAGCTGGCTGGCTCACTCCGCGCCGGCCCGCGTCGTCGGCATGGGCGGGCTCATGGTCTACGGGGAGGCCGAGCGGCGCCCGGCCGGGACGAGCGCCGGCACCGTTATGCAGGACTGGTTCAGCCTCGATCACTGGCCGTCCGACGAGGTGGACGGGCTCAACCCCGTCATCGACGTCGAGGACCACTCCATGCTCATGATGACCATGCGCAACGGGGTCATGACCTCCTACCAGCAGTGCCACTTCACCCCCGACTACTGGCGCAGCTACACGGTCATCGGCACACGCGGCCGGGCCGAGAACCTCGGTGACGGGGCCGGCGACGTCGTCAAGGTGTGGACCGAGCGCACCGAGCACTACGCCGAGCGCGCCACCCAGGAGTACGTCATCGCCGAGGAGGGCACCGGGCACGACAGCGCTGACCAGCTCGCCATCGACGAGTTCCTGCGCTTCGTGCGCGATGGCGGGGCCACCGAGGTCTCCCCGGTCAGTGCGCGCGACGCCGTCGCGGCGGGGGTGCTGGCCACCCGGTCCCTGCGCTCGGGCTCCGTGCCCTTCGACGTGCCCGAGCTCGACGCGGAGCTGGCGGACTACTTCCACCGTGGACAGCACAACTCTCACTGA","VREASRQLRVGVVGIGARCYLAALADTSPVPARLVAAADTAPDAVERARRLLPEGVAVVADHRDLLGHGIDAVVLTTPDDTHEELACFFLEAGIPVYLEKPLAITIEAADRILETARRTGTRLYVGHNMRHMEVVRLLKSIIDSGRIGEVKAIWCRHFVGNGGDYYFRDWHAERRHVTGLLLQKAAHDIDVMSWLAHSAPARVVGMGGLMVYGEAERRPAGTSAGTVMQDWFSLDHWPSDEVDGLNPVIDVEDHSMLMMTMRNGVMTSYQQCHFTPDYWRSYTVIGTRGRAENLGDGAGDVVKVWTERTEHYAERATQEYVIAEEGTGHDSADQLAIDEFLRFVRDGGATEVSPVSARDAVAAGVLATRSLRSGSVPFDVPELDAELADYFHRGQHNSH$","Oxidoreductase","Cytoplasm","probable oxidoreductase","oxidoreductase","oxidoreductase domain protein","","","","","

InterPro
IPR000683
Domain

Oxidoreductase, N-terminal
PF01408	$\"[8-127]T$	GFO_IDH_MocA

InterPro
IPR004104
Domain

Oxidoreductase, C-terminal
PF02894	$\"[139-287]T$	GFO_IDH_MocA_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[5-162]T$	no description
PTHR22604	$\"[59-216]T$ $\"[250-374]T$	OXIDOREDUCTASES
PTHR22604:SF14	$\"[59-216]T$ $\"[250-374]T$	OXIDOREDUCTASE

","BeTs to 14 clades of COG0673COG name: Predicted dehydrogenases and related proteinsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0673 is --mpk-yqvd-lbcefgh--uj----Number of proteins in this genome belonging to this COG is 5","***** IPB000683 (Oxidoreductase, N-terminal) with a combined E-value of 2.1e-17. IPB000683A 70-103 IPB000683B 187-197","","","-48% similar to PDB:1XEA Crystal structure of a Gfo/Idh/MocA family oxidoreductase from Vibrio cholerae (E_value = 3.2E_14);-41% similar to PDB:1ZH8 Crystal structure of Oxidoreductase (TM0312) from Thermotoga maritima at 2.50 A resolution (E_value = 5.5E_14);-49% similar to PDB:2GLX Crystal Structure Analysis of bacterial 1,5-AF Reductase (E_value = 8.7E_12);","Residues 8 to 127 (E_value = 2.2e-23) place ANA_2198 in the GFO_IDH_MocA family which is described as Oxidoreductase family, NAD-binding Rossmann fold.Residues 139 to 287 (E_value = 2.1e-06) place ANA_2198 in the GFO_IDH_MocA_C family which is described as Oxidoreductase family, C-terminal alpha/beta domain.","","oxidoreductase (1996)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2199","2380138","2378552","1587","6.14","-9.62","57797","GTGACCGATGGTGGCCCGGTGCGGGATGGTCCTCACCACAGGGCGGCTGAGGCCGAGGACGACGGCGCACCGGTGAGGGTTCATGGCAGGCTTGGGCCGATGACTGCGCACCCCGCTCCCGCTGACCCCGCCGACTCCCCGGATGCCGCCGAGAACCGCGGCCTGACGCCCAAGGCCCGTCAGGCCCTCGAGGGCCTGCCCCCCGCCCTGGCGGCCCTGGGCCACGCCTTCGTGCGCGCCGGGCACGAGATCGCGCTCGTTGGCGGGCCGGTGCGGGACGCCTTCCTCGGCGTCGCCCCCCACGACCTGGACCTGACCACCTCGGCCCGCCCCGAGCAGACCGAGAAGATCCTGGCCGCCTGGGGCGAGACCACCTGGGACGTGGGCCGGGCCTTCGGTACCATTGGCGCGCGCAAGGGATCCACCATCGTGGAGGTCACCACCTACCGCACCGAGGCCTACGAGGTCGGCTCGCGCAAGCCCCAGGTGACCTATGGCGACACCCTCACCGGGGACCTCACCCGCCGCGACTTCACCGTCAACGCCATGGCGCTGCGCCTGCCCGACCTCGAGCTCGTCGACCCCTGCGGCGGCCTGGCCGACCTGAGCGCCGGCATCCTGCGCACCCCCGTCAGCGCCGAGCAGTCCTTCGACGACGACCCCCTGCGCATCATGCGGGCCGCCCGCTTCGCCGCCCAGCTCGGCTTCGACGTCGAGATGGACGTCATGACCGCCATGGAGGAGATGGCCCCCCGCCTGGAGATCGTCTCCGCCGAGCGCGTGCGCGCCGAGCTCGAGCGCCTGCTCATCAGCCCCTGGCCCCGGCGCGGACTGGAGCTCATGGTCCACACCGGTGTGGCCGACGTCGTCCTGCCCGAGCTGAGCGCCCTGCGCGAGACCGTCGATGAGCACAAGCGCCACAAGGACGTCTACGAGCACACCCTGACCGTCCTGGACCAGGCCATCGACCTGGAGACCGGGCCCGACGGGCCCGTCCCCGGCCCCGACCTGGTGCTGCGCCTGGCCGCCATCCTCCACGACATCGGCAAGCCCGCCACCCGCCGCTTCCTGCCCGACGGCACCGTCACCTTCCACGGCCACGACCACGTCGGCGCCCGGATGACGGCCAAGCGCCTGCGGGCCCTGCGCTTCGACAAGCAGACCATCAAAGACGTCTCCCGGCTGGTCGAGCTCCACCTGCGCTTCCACGGATACGTCGACGCCGCCTGGTCGGACTCGGCCGTGCGCCGCTACGCCACCGACGCCGGCCCCCTGCTGGAGCGCCTCCACCGGCTCACCCGGGCCGACGTCACCACCCGCAACCGCCGCAAGGCCGCCATGCTGGACCGCGCCTATGACGACCTCGAGGAGCGCATCGAGGCCCTGCGCGCCGCCGAGGAGCTGGCCGCCATCCGCCCCGACCTCGACGGTGGCCAGATCATGGCCGAGCTCGGCGTGGCCCCCGGGCCGGTCGTTGGCGAGGCCTACCGCTTCCTCATGAACCTGCGCATGGAGAAGGGGCCGATCGGCGAGGACCTGGCCCGCCAGGCACTGCGCTCCTGGTGGGCGGCCCGCCAGAAGAGCTGA","VTDGGPVRDGPHHRAAEAEDDGAPVRVHGRLGPMTAHPAPADPADSPDAAENRGLTPKARQALEGLPPALAALGHAFVRAGHEIALVGGPVRDAFLGVAPHDLDLTTSARPEQTEKILAAWGETTWDVGRAFGTIGARKGSTIVEVTTYRTEAYEVGSRKPQVTYGDTLTGDLTRRDFTVNAMALRLPDLELVDPCGGLADLSAGILRTPVSAEQSFDDDPLRIMRAARFAAQLGFDVEMDVMTAMEEMAPRLEIVSAERVRAELERLLISPWPRRGLELMVHTGVADVVLPELSALRETVDEHKRHKDVYEHTLTVLDQAIDLETGPDGPVPGPDLVLRLAAILHDIGKPATRRFLPDGTVTFHGHDHVGARMTAKRLRALRFDKQTIKDVSRLVELHLRFHGYVDAAWSDSAVRRYATDAGPLLERLHRLTRADVTTRNRRKAAMLDRAYDDLEERIEALRAAEELAAIRPDLDGGQIMAELGVAPGPVVGEAYRFLMNLRMEKGPIGEDLARQALRSWWAARQKS$","tRNA nucleotidyltransferase/poly(A) polymerase","Cytoplasm","pcnA","putative RNA nucleotidyltransferase ","HDIG domain protein","","Aravind L., Koonin E.V. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biochem. Sci. 1998. 23(12):469-472. PMID: 9868367","","","

InterPro
IPR002646
Domain

Polynucleotide adenylyltransferase region
PF01743	$\"[84-208]T$	PolyA_pol

InterPro
IPR003607
Domain

Metal-dependent phosphohydrolase, HD region
SM00471	$\"[306-480]T$	HDc

InterPro
IPR006674
Domain

Metal-dependent phosphohydrolase, HD region, subdomain
PF01966	$\"[310-441]T$	HD

InterPro
IPR006675
Domain

HDIG
TIGR00277	$\"[306-394]T$	HDIG: uncharacterized domain HDIG

InterPro
IPR014065
Family

tRNA adenylyltransferase
TIGR02692	$\"[55-523]T$	tRNA_CCA_actino: tRNA adenylyltransferase

noIPR
unintegrated

unintegrated
G3DSA:1.10.3090.10	$\"[207-353]T$	no description
G3DSA:3.30.460.10	$\"[53-205]T$	no description
PTHR13734	$\"[99-523]T$	TRNA-NUCLEOTIDYLTRANSFERASE/POLY(A) POLYMERASE FAMILY MEMBER
PTHR13734:SF7	$\"[99-523]T$	TRNA NUCLEOTIDYLTRANSFERASE

","BeTs to 18 clades of COG0617COG name: tRNA nucleotidyltransferase/poly(A) polymeraseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0617 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB002646 (Polynucleotide adenylyltransferase) with a combined E-value of 2.8e-25. IPB002646A 85-104 IPB002646B 170-183 IPB002646C 217-233","","","-56% similar to PDB:1MIV Crystal structure of Bacillus stearothermophilus CCA-adding enzyme (E_value = 9.0E_31);-56% similar to PDB:1MIW Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with ATP (E_value = 9.0E_31);-56% similar to PDB:1MIY Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with CTP (E_value = 9.0E_31);-49% similar to PDB:1OU5 Crystal structure of human CCA-adding enzyme (E_value = 9.3E_20);-46% similar to PDB:1VFG Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog (E_value = 4.8E_16);","Residues 84 to 208 (E_value = 4.7e-42) place ANA_2199 in the PolyA_pol family which is described as Poly A polymerase head domain.Residues 310 to 441 (E_value = 1.4e-15) place ANA_2199 in the HD family which is described as HD domain.","","(pcnA) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2201","2380235","2380744","510","6.36","-3.66","18611","ATGCCCTCTCCACGCACTCGCACGCCCCGCGCCGGAAACCCGGCCCACCGGGCGAGTGCGCGCGCCCTGCCCATCGTCAACGAGACCAGCGCCGGCGGCCTGGTCGTTGACGTCCAGAACGGGCAGGCCTTCACCGCGGTCATCGCCCGGCGCAACCGGGGCGGGCGCCTGGAGTGGTGCCTGCCCAAGGGGCACCTGGAGGGCGCCGAGACCCCCGAGCAGGCCGCGGTCCGCGAGATCATGGAGGAGACCGGGATCACCGGTCGGGTTCTTCGGCACCTGGCGACCATCGACTACTGGTTCGCCGGCCACGAGCACCGCGTCCACAAGGTGGTGCACCACTTCCTGCTGGAGGCGGTCAGCGGCACGCTGACCACGGAGAACGACCCGGACCATGAGGCCGAGGACGTCGAGTGGGTCGCCCTCGACGACGTCTCCCACCGCCTGGCCTACCCCAACGAGCGCCGTATCGTGGCCGCGGCCTGGGACATCCTGGTGGGGGATGGATGA","MPSPRTRTPRAGNPAHRASARALPIVNETSAGGLVVDVQNGQAFTAVIARRNRGGRLEWCLPKGHLEGAETPEQAAVREIMEETGITGRVLRHLATIDYWFAGHEHRVHKVVHHFLLEAVSGTLTTENDPDHEAEDVEWVALDDVSHRLAYPNERRIVAAAWDILVGDG$","NUDIX hydrolase","Cytoplasm","MutT/nudix family protein","hypothetical protein","NUDIX hydrolase","","Sun Z., Cunningham Jr F.X., Gantt E. Differential expression of two isopentenyl pyrophosphate isomerases and enhanced carotenoid accumulation in a unicellular chlorophyte. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(19):11482-11488. PMID: 9736763","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[59-73]T$ $\"[73-88]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[26-168]T$	no description
PF00293	$\"[27-165]T$	NUDIX
PS00893	$\"[64-85]T$	NUDIX

InterPro
IPR002667
Family

Isopentenyl-diphosphate delta-isomerase
PD004109	$\"[68-143]T$	IDI_RHOCA_P26173;

noIPR
unintegrated

unintegrated
PTHR22769	$\"[35-166]T$	MUTT/NUDIX HYDROLASE

","BeTs to 17 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 3.4e-15. IPB000086 59-86","","","No significant hits to the PDB database (E-value < E-10).","Residues 27 to 165 (E_value = 9.6e-27) place ANA_2201 in the NUDIX family which is described as NUDIX domain.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2203","2380813","2383239","2427","4.88","-24.00","81850","ATGGTGACCATTGCCGCCCTACTGGGGGTGGCCGGCCTGGTGACGTGGCCGGTGGCCGCGCTGCCCGTGGCCGAGGCGGACCAGGGCTCCGGCACGCTCCCGCTCGCGCAGTCCGCCGGACTCTCCGCGGAGGTCGCACCGGCCGCCCCGGCGGCTTCGGCGAAGCCGTCCACGGCGTCGGCCCCGGCGTCGGCCCCCTCAACGGCCCCCTCAACGGCCCCGGCAACGGGCGAGAAGCCCACCAACCAGGTGACTGTGAGCATCGACGCCCTGACCCCCGAGGTGCTCCGCAGCGACCAGGACCTCAACCTGACCGGCACCATCACCAACGGAACTGCTCAGACCATCACCGGGGCGGACCTGGTGACGCGGGTGCAGCGATCCACGGAGTCCACGAGCGGGGGCCTGAGCAAGTGGTTGACTGGGAACGATGAGTCGGGGTTGTCGGACCCGTTCACGGTCCCGCTGGGTCACGACCTCCAGCCGGGGGGCGTCTCCCAGTTCTCCATCACCATCCCCGCCGACGAGCTGCCGCTGAACAGTACCGACCAGTGGGGGCCGCGCGGCGTCTCCGTCGCCCTGGCGACCCAGGACGTCTCCCTGGCCCAGGACCGCAGCATCCTCGTGTGGGACAGCGGCGCATCCGTCTCGCCGTTGCGTATGACCGTCTTTCTGCCGGTCACCGCCTCCGCTCAGGAGATGGCGGTGCTGTCCGGCCCGCACACCCAGGAGCGCACGGAGGCCCTCAGTCGTATCCACAACCGGGTTCTGGGCCTGGTGAGCATGGCCGGCGACGGCGTCGTCGCCGCCGTCGACCCGGCACTGGTCGAGGCCCTCGGTGTCACCACGGCCAGCCTCGAGCAGGCCGCCCGCAACAACGGCTCCCAGCCCTCCTCGCCGGATGCCGTCTCTCAGGCGCCCCAGAGCACCGACTCCTCCGCGTCGTCACCCCCGACTGCTCCGGCGACGACGCCCCCCTCGGCGAGCGCCACCCCGTCCCCGCAGCCGGGGGGCAGCGCCACCGCCTCGCCATCAGGCAAGGCCCCGCAGGTCTCCAACGAGGTCATCCAGCTCTCTGCGGCTCTCGCACGGGCCATCCACTCCGACAGCCTCGTGGCTCTGCCGTGGGGCGACTCCGACACCGCGGCCCTGGCGCACCTGCAGCAGACGAGCCTCATCGAGACGGCCGCGCGGCGCACCCAGGAGTCGGTCATCGTCAAGGCGGGGGCCCCGACGTCGGTGTCCTGGTTGGCATCCAGCGTCGCGGACGCCACCACGGTCAGTGCCCTGGCGCAGCCGGATTCGACCATCATCGCCTCACCGGAGTCCTTGCCTCCGTCCGACGAGCTCACCTACACCCCCTCCGGTCTGGGCGCCTCCGGGGACCATGCGGTCCTCATCCCGGAGCAGTCCCTGTCGGGGGCGCTCACCGGTCAGGACGCCGCACCCACGGCCTCCGATCAGGGGGATCCGACTGCCCAGAGCGCCCCGGCCTCCGCACTCGACACCCGCCAGCTGCTGCGTGGGGACAGTGCCATTCTGGTCCGCCAGGCCCCGGTGCTGGAACGGGACATCATCGTGGCGATGCCCCGCCGGGCGACCTCCGCCGTGCAGTCCTCGGTCGTGCGGGAGCGGGTGGCCGCCCTGCGCTCAGTGCCCTGGGTCCAGTCCCAGTCCCTGGGCGCCCTCCAGGAGCGCGCCCAGCACGAGGTCGCGGCCGTGAACGAGGGCACCTCACGGATCGAGCGCTCCGAGACGCCGGACACGGTGATCGACGACGACGAGCTGTCCGCCGACACCCTCACCGCCGCCGGCCGTACGGCCACGACCCTGCAGTCGATCTCCTCAGTGCTCTCCGAGCCGGCCGCGCTGCTGGGCGACTACACCAGCCTGGAGGCGGTGGTCTCCTCAGCGTCCTGGCGGGCCGACCCCGCGACCCGCAACGCCCAGGTTCCCGCTGCCGAGGCGGCCGGGGCCGGCGTCACCTCCTCGCTGGCCGCGGTGCCGTCGTCGACCATCAACGTCATCAGCTCCGAGGCGCAGCTGCCGGTGCGCATCACCTCCTCCCTGAGTCAGGACGTCACGGTCCAGGTCTACCTGGTCTCGAATAACAAGCGCCTCCAGGTCCCGCGCACCACGACCGTGCGGGTCCCGGCCCACCAACAGGCCAAGGTCACGGTGCCGATCCAGGCCGTCGGCTCGGGCGATGTCGCCCTGACGGTGCAGGTTCTCGCCGCCGACGGCACCACCGTGGGCACCCCCACCACCGTCAACATGCGCGTGCGCGCCGACTGGGAGGGACGCGGCACCGGTGTCATCGTCGGGGTGCTGGTCTCCATCGTGGTGATCGGTACGGTGAGGACAGTAAGACGAGGCCGCCGCACCGCAGTGGCCCCGGCTGCACCGGCTGCACAGGAGACGGCATGA","MVTIAALLGVAGLVTWPVAALPVAEADQGSGTLPLAQSAGLSAEVAPAAPAASAKPSTASAPASAPSTAPSTAPATGEKPTNQVTVSIDALTPEVLRSDQDLNLTGTITNGTAQTITGADLVTRVQRSTESTSGGLSKWLTGNDESGLSDPFTVPLGHDLQPGGVSQFSITIPADELPLNSTDQWGPRGVSVALATQDVSLAQDRSILVWDSGASVSPLRMTVFLPVTASAQEMAVLSGPHTQERTEALSRIHNRVLGLVSMAGDGVVAAVDPALVEALGVTTASLEQAARNNGSQPSSPDAVSQAPQSTDSSASSPPTAPATTPPSASATPSPQPGGSATASPSGKAPQVSNEVIQLSAALARAIHSDSLVALPWGDSDTAALAHLQQTSLIETAARRTQESVIVKAGAPTSVSWLASSVADATTVSALAQPDSTIIASPESLPPSDELTYTPSGLGASGDHAVLIPEQSLSGALTGQDAAPTASDQGDPTAQSAPASALDTRQLLRGDSAILVRQAPVLERDIIVAMPRRATSAVQSSVVRERVAALRSVPWVQSQSLGALQERAQHEVAAVNEGTSRIERSETPDTVIDDDELSADTLTAAGRTATTLQSISSVLSEPAALLGDYTSLEAVVSSASWRADPATRNAQVPAAEAAGAGVTSSLAAVPSSTINVISSEAQLPVRITSSLSQDVTVQVYLVSNNKRLQVPRTTTVRVPAHQQAKVTVPIQAVGSGDVALTVQVLAADGTTVGTPTTVNMRVRADWEGRGTGVIVGVLVSIVVIGTVRTVRRGRRTAVAPAAPAAQETA$","Hypothetical protein","Extracellular, Periplasm, Cellwall","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide

InterPro
IPR000719
Domain

Protein kinase
PD000001	$\"[807-1005]T$	Q9S478_MYXXA_Q9S478;

InterPro
IPR001844
Family

Chaperonin Cpn60
PS00296	$\"[1266-1277]?$	CHAPERONINS_CPN60

InterPro
IPR004268
Family

Virulence factor MVIN-like
PF03023	$\"[47-526]T$	MVIN

InterPro
IPR006162
PTM

Phosphopantetheine attachment site
PS00012	$\"[1052-1067]?$	PHOSPHOPANTETHEINE

noIPR
unintegrated

unintegrated
PTHR11946	$\"[22-201]T$	ISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES
PTHR11946:SF10	$\"[22-201]T$	LEUCYL-TRNA SYNTHETASE
tmhmm	$\"[21-41]?$ $\"[70-90]?$ $\"[105-127]?$ $\"[146-164]?$ $\"[179-199]?$ $\"[218-238]?$ $\"[259-279]?$ $\"[310-330]?$ $\"[351-371]?$ $\"[390-408]?$ $\"[423-445]?$ $\"[451-471]?$ $\"[492-510]?$ $\"[524-542]?$ $\"[1225-1245]?$	transmembrane_regions

","BeTs to 12 clades of COG0728COG name: Uncharacterized membrane protein, putative virulence factorFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0728 is -------qvdr--cefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB004268 (Virulence factor MVIN-like) with a combined E-value of 1.4e-12. IPB004268A 53-87 IPB004268B 302-333","","","No significant hits to the PDB database (E-value < E-10).","Residues 47 to 526 (E_value = 1e-22) place ANA_2204 in the MVIN family which is described as MviN-like protein.","","hypothetical membrane protein in MviN family, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2205","2387606","2388532","927","4.79","-17.67","33064","ATGATTCACGACGTCGTCATCGTCGGCTCCGGTCCCGCCGGCTACACAGCTGCCATCTATGCGGCCCGCGCCCAGCTCAATCCGGTCATCCTGGCCGGTTCGGTGACTGCCGGCGGTGCCCTGATGAATACGACCGAGGTGGAGAACTACCCCGGCTTCGTCACTGGCATCATGGGCCCCGAGCTCATGACCCAGATGCAGGAGCAGGCCGAGCGCTTCGGTACCGACATCCGCTACGAGGACGTCACCGCTCTCGAGCTGGAGGGCGACGTCAAGCGCATCACCACCTCTGACGGCGTCTATGAGGCTCGCACAGTCATCATCTCCACCGGCTCGGAGTACCGGCACCTGGGTATCGACGGGGAGGAGCGCCTCTCCGGCCACGGCGTGTCCTACTGCGCCACCTGCGACGGGTTCTTCTTCAAGGACCAGGACATCGTCGTCGTCGGTGGTGGGGACTCGGCCATGGAGGAGGCCACCTTCCTGACCCGCTTCGCCCGCTCCGTGACGGTGGTCCACCGCCGCGACGAGCTGCGCGCCTCGGCCGTCATGGCCAAGCGCGCCCAGGAGGACCCGAAGATCTCCTTCGCCTGGAACTCGCGAGTCGTCGAGCTTCACGGCGAGGACTCCCTGACCGCCGTCACCCTGGAGGACTCTGTCACCGGGGAGCGCCGCCGGCTTGAGGCCTCGGGTCTGTTCGTCGCCATCGGGCAGGTGCCGCGCAGTGAGCTCGTCGCCGACGTCCTCGACCTCGACGAGGCCGGCTACATCAAGGTCGAAGCGCCTTCTCAGCGCACCCGTATCCCCGGGGTCTTCGCCTGCGGTGACGTCGCCGACCCCACCTACCAGCAGGCGATCACGGCGGCCGGTTCCGGCTGCCGTGCGGCCCTGGACGCCGAGCACTACCTGACAACTCTGCAGGCCTGA","MIHDVVIVGSGPAGYTAAIYAARAQLNPVILAGSVTAGGALMNTTEVENYPGFVTGIMGPELMTQMQEQAERFGTDIRYEDVTALELEGDVKRITTSDGVYEARTVIISTGSEYRHLGIDGEERLSGHGVSYCATCDGFFFKDQDIVVVGGGDSAMEEATFLTRFARSVTVVHRRDELRASAVMAKRAQEDPKISFAWNSRVVELHGEDSLTAVTLEDSVTGERRRLEASGLFVAIGQVPRSELVADVLDLDEAGYIKVEAPSQRTRIPGVFACGDVADPTYQQAITAAGSGCRAALDAEHYLTTLQA$","Thioredoxin reductase","Cytoplasm","thioredoxin-disulfide reductase","thioredoxin reductase ","thioredoxin reductase","","Kuriyan J., Krishna T.S., Wong L., Guenther B., Pahler A., Williams Jr C.H., Model P. Convergent evolution of similar function in two structurally divergent enzymes. Nature 1991. 352(6331):172-174. PMID: 2067578Russel M., Model P. Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 1988. 263(18):9015-9019. PMID: 3288628Cohen G., Argaman A., Schreiber R., Mislovati M., Aharonowitz Y. The thioredoxin system of Penicillium chrysogenum and its possible role in penicillin biosynthesis. J. Bacteriol. 1994. 176(4):973-984. PMID: 8106340Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N. Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 1990. 265(18):10535-10540. PMID: 2191951Xu X.M., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T. Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1. J. Biochem. 1991. 109(5):678-683. PMID: 1917890Mathieu I., Meyer J., Moulis J.M. Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum. Biochem. J. 1992. 285:255-262. PMID: 1637309Waksman G., Krishna T.S., Williams Jr C.H., Kuriyan J. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. J. Mol. Biol. 1994. 236(3):800-816. PMID: 8114095McKie J.H., Douglas K.T. Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett. 1991. 279(1):5-8. PMID: 1995341","","","

InterPro
IPR000103
Domain

Pyridine nucleotide-disulphide oxidoreductase, class-II
PR00469	$\"[4-26]T$ $\"[38-53]T$ $\"[59-69]T$ $\"[104-112]T$ $\"[126-138]T$ $\"[141-165]T$ $\"[193-209]T$ $\"[231-252]T$ $\"[284-303]T$	PNDRDTASEII

InterPro
IPR000759
Family

Adrenodoxin reductase
PR00419	$\"[4-26]T$ $\"[146-160]T$	ADXRDTASE

InterPro
IPR001327
Domain

Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139	$\"[111-177]T$	TRXB_MYCSM_O30973;
PF00070	$\"[145-237]T$	Pyr_redox

InterPro
IPR005982
Domain

Thioredoxin reductase
TIGR01292	$\"[3-303]T$	TRX_reduct: thioredoxin-disulfide reductase

InterPro
IPR008255
Active_site

Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
PS00573	$\"[133-153]T$	PYRIDINE_REDOX_2

InterPro
IPR013027
Domain

FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368	$\"[4-26]T$ $\"[106-115]T$ $\"[145-170]T$ $\"[230-244]T$ $\"[271-278]T$	FADPNR
PF07992	$\"[4-282]T$	Pyr_redox_2

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[2-114]T$ $\"[115-237]T$	no description
PTHR22912	$\"[6-279]T$	DISULFIDE OXIDOREDUCTASE

","BeTs to 26 clades of COG0492COG name: Thioredoxin reductaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0492 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000103 (Pyridine nucleotide-disulphide oxidoreductase, class-II) with a combined E-value of 1.2e-79. IPB000103A 5-23 IPB000103B 38-51 IPB000103C 107-159 IPB000103D 227-242 IPB000103E 266-303 IPB000103A 146-164***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 5.6e-35. IPB013027A 4-26 IPB013027B 106-115 IPB013027C 145-170 IPB013027D 230-244 IPB013027E 271-278***** IPB000759 (Adrenodoxin reductase family signature) with a combined E-value of 3.6e-15. IPB000759A 4-26 IPB000759D 146-160 IPB000759D 5-19***** IPB001100 (Pyridine nucleotide-disulphide oxidoreductase, class I) with a combined E-value of 4.1e-11. IPB001100A 3-28 IPB001100E 256-277***** IPB003042 (Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature) with a combined E-value of 1.8e-06. IPB003042A 4-26 IPB003042A 145-167","","","-71% similar to PDB:2A87 Crystal Structure of M. tuberculosis Thioredoxin reductase (E_value = 2.6E_90);-60% similar to PDB:1VDC STRUCTURE OF NADPH DEPENDENT THIOREDOXIN REDUCTASE (E_value = 6.4E_65);-60% similar to PDB:1CL0 CRYSTAL STRUCTURE OF REDUCED THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI. (E_value = 9.6E_61);-60% similar to PDB:1TDE CRYSTAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN REDUCTASE REFINED AT 2 ANGSTROM RESOLUTION: IMPLICATIONS FOR A LARGE CONFORMATIONAL CHANGE DURING CATALYSIS (E_value = 9.6E_61);-60% similar to PDB:1F6M CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+ (E_value = 1.4E_59);","Residues 4 to 198 (E_value = 0.00085) place ANA_2205 in the DAO family which is described as FAD dependent oxidoreductase.Residues 4 to 282 (E_value = 1.7e-48) place ANA_2205 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 4 to 31 (E_value = 3.5e-07) place ANA_2205 in the FAD_binding_2 family which is described as FAD binding domain.Residues 145 to 237 (E_value = 1.9e-28) place ANA_2205 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase.","","reductase (trxB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2206","2388641","2388967","327","4.91","-4.88","11805","ATGTCCGAGGCTCTCGCCGTCACCGACGCCACCTTCGAGGAGGAGGTCCTCAAGTCCGAGGTGCCCGTCGTCATCGACTTCTGGGCCCAGTGGTGCGGCCCCTGCCGCCAGATGGCGCCGATCGTAGACGAGGTCGCCGCCGACTTCGGTGACAAGGTCAAGTTCGTCAAGGTCGACGTGGACGCCAACCCGGCCACGGCCCGCTCCTACGGCGTGCGTTCCATCCCGACCTTCGCGGTGGTGCGCGACGGCGAGGTCTTCCACCAGTTCGCCGGCTCGCGCCCCAAGGCCTCCTTCAAGGCCGAGGTGGAAAAGGTCCTGGCCTGA","MSEALAVTDATFEEEVLKSEVPVVIDFWAQWCGPCRQMAPIVDEVAADFGDKVKFVKVDVDANPATARSYGVRSIPTFAVVRDGEVFHQFAGSRPKASFKAEVEKVLA$","Thioredoxin","Cytoplasm, Periplasm","thioredoxin","thioredoxin","thioredoxin","","Holmgren A. Thioredoxin. Annu. Rev. Biochem. 1985. 54:237-271. PMID: 3896121Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 1989. 264(24):13963-13966. PMID: 2668278Holmgren A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 1995. 3(3):239-243. PMID: 7788289Martin J.L. Thioredoxin--a fold for all reasons. Structure 1995. 3(3):245-250. PMID: 7788290Saarinen M., Gleason F.K., Eklund H. Crystal structure of thioredoxin-2 from Anabaena. Structure 1995. 3(10):1097-1108. PMID: 8590004","","","

InterPro
IPR005746
Family

Thioredoxin
TIGR01068	$\"[7-107]T$	thioredoxin: thioredoxin

InterPro
IPR006662
Domain

Thioredoxin-related
PR00421	$\"[23-31]T$ $\"[31-40]T$ $\"[71-82]T$	THIOREDOXIN
PS00194	$\"[24-42]T$	THIOREDOXIN

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[2-107]T$	no description

InterPro
IPR013766
Domain

Thioredoxin domain
PF00085	$\"[3-106]T$	Thioredoxin

InterPro
IPR015467
Domain

Thioredoxin family
PTHR10438	$\"[13-107]T$	THIOREDOXIN-RELATED

noIPR
unintegrated

unintegrated
PTHR10438:SF13	$\"[13-107]T$	THIOREDOXIN M(MITOCHONDRIAL)-TYPE

","BeTs to 23 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones] Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB006662 (Thioredoxin type domain) with a combined E-value of 8.1e-28. IPB006662A 23-40 IPB006662B 57-93","","","-63% similar to PDB:1T00 The structure of thioredoxin from S. coelicolor (E_value = 2.3E_22);-58% similar to PDB:1DBY NMR STRUCTURES OF CHLOROPLAST THIOREDOXIN M CH2 FROM THE GREEN ALGA CHLAMYDOMONAS REINHARDTII (E_value = 2.6E_21);-62% similar to PDB:2I4A Crystal structure of thioredoxin from the acidophile Acetobacter aceti (E_value = 6.3E_20);-59% similar to PDB:2I1U Mycobacterium tuberculosis thioredoxin C (E_value = 8.2E_20);-60% similar to PDB:2FCH Crystal Structure of Thioredoxin Mutant G74S (E_value = 9.1E_19);","Residues 1 to 107 (E_value = 0.003) place ANA_2206 in the Redoxin family which is described as Redoxin.Residues 3 to 106 (E_value = 4.1e-42) place ANA_2206 in the Thioredoxin family which is described as Thioredoxin.","","(trx) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2207","2389197","2390636","1440","5.24","-13.10","52040","ATGCAGCACACCCAGTACATCTCCACCCGTGGTCAGATGGCGGCAGCGGGGTTCACGGACGTTCTTGTGGCGGGCCTGGCGCCCGACGGTGGCCTGGCGGTTCCCAGCCGTCTTCCCGCCCTGAGCCCCGAGCAGATCGAGGCCTGGAGGCCCTTGGGCTACGCCGAGCTGGCCACGGAGGTCATCGGCCTGTTCGCCACCGACATTCCCCGGGAGGACCTGGCCGAGCTGACCCGGGCCGCCTATGGCCCGCGGCGGTTCCCACAGCCGGTTGTCCCTGTCACCTGGCTTGACGACGTCGCCGACGGCCTGACCCTCGTGGGCCTGTCCGAGGGACCGACGATGGCCTTCAAGGACCTGGCCATGCAGTTCCTGGGGCAGGCGATTCCCTATGTCCTGGCCAAGCACGGACAGGTCCTTAACATCCTGGGCGCCACCTCCGGCGACACCGGTTCGGCGGCCGAGCACGCCTTCAGGGGGCAGGAGGGCGTCAGCGTCTTCATGCTCTCACCGGCCGGCCGCATGAGCCCGGTGCAGCGCGCCCAGATGTACACCCTCCAGGACGCCAACATCCACAACATCGCGGTGCGCGGTGTCTTCGACGACTGCCAGGCGCTGGTCAAGGCGCTGAGCAACGACGCGGAGTTCAAGGCCGCTCATCACCTGGGCGCCGTCAACTCCATCAACATCGGCCGGATCGCCGCGCAGGCCGTCTACTACGTGTGGTCCTGGCTGCGGGTCACCGACGCGGTGGAGGAGGGGCGCCGCGCCGGCTACCGCATCGATGTCTGCGTGCCCTCGGGCAACTTCGGCAATATCTACGCCGGCTTCCTAGCCCGGTCCATGGGGGTGCCGATCCGCCGCCTCATTCTGGCCACCAATGAGAACAACGTGCTCGAGGAGTTCTTCACCACCGGCATCTACCGACCCCGTTCCGCGGAGGACACCCTGGCCACCTCCAGCCCCTCCATGGACATCTCCAAGGCCTCCAACCTGGAGCGCTTCATCTGGGCACTGCTGGGCCCCGAGGCCTTCGTGCAGCGCTGGGCGGAGTTGGAGACCACCGGCACACTCGACCTGCGCGATCAGCTCCCACGCCTGCGCGAGGAGTTCGGCTTCGTCGCCGGCACGTCCACACACGCCGACCGACTGGAGGCCATCCGCACCGTCAAGGAGCGCTCCGGACGGCTCATCGACCCGCACACCGCCGACGGCGTGACGGTCGCTCTGCGCGTCATGGAGCCCGGTTTCCCCACACTCGTCATGGAGACCGCCAAGGCCGCGAAGTTCCCGCAGACGGTGGCCGAGGCGCTCGGGAGCGAGCCGGAGACCCCCGACGTCGTCGCTGATCTGCTTGCCCGGCCCCAGAAGGTCGAGACGATCGACAACGAGGAGGCTCCTCTGCGCGCCCTCATCGAGGAGCGGGCCCTGACCCGCTGA","MQHTQYISTRGQMAAAGFTDVLVAGLAPDGGLAVPSRLPALSPEQIEAWRPLGYAELATEVIGLFATDIPREDLAELTRAAYGPRRFPQPVVPVTWLDDVADGLTLVGLSEGPTMAFKDLAMQFLGQAIPYVLAKHGQVLNILGATSGDTGSAAEHAFRGQEGVSVFMLSPAGRMSPVQRAQMYTLQDANIHNIAVRGVFDDCQALVKALSNDAEFKAAHHLGAVNSINIGRIAAQAVYYVWSWLRVTDAVEEGRRAGYRIDVCVPSGNFGNIYAGFLARSMGVPIRRLILATNENNVLEEFFTTGIYRPRSAEDTLATSSPSMDISKASNLERFIWALLGPEAFVQRWAELETTGTLDLRDQLPRLREEFGFVAGTSTHADRLEAIRTVKERSGRLIDPHTADGVTVALRVMEPGFPTLVMETAKAAKFPQTVAEALGSEPETPDVVADLLARPQKVETIDNEEAPLRALIEERALTR$","Threonine synthase","Cytoplasm","threonine synthase","threonine synthase ","threonine synthase","","Parsot C. Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase. EMBO J. 1986. 5(11):3013-3019. PMID: 3098560","","","

InterPro
IPR001926
Domain

Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291	$\"[86-405]T$	PALP

InterPro
IPR004450
Domain

Threonine synthase
TIGR00260	$\"[57-446]T$	thrC: threonine synthase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1100	$\"[202-451]T$	no description
G3DSA:3.90.1380.10	$\"[4-88]T$	no description
PTHR10314	$\"[112-340]T$	SER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF1	$\"[112-340]T$	THREONINE SYNTHASE
signalp	$\"[1-33]?$	signal-peptide

","BeTs to 14 clades of COG0498COG name: Threonine synthaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0498 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-52% similar to PDB:1KL7 Crystal Structure of Threonine Synthase from Yeast (E_value = 1.6E_71);-50% similar to PDB:1VB3 Crystal Structure of Threonine Synthase from Escherichia coli (E_value = 1.5E_53);","Residues 86 to 405 (E_value = 7.5e-11) place ANA_2207 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme.","","synthase (thrC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2208","2390749","2392179","1431","5.81","-10.00","52457","ATGTTTCACGTGAAACACCGCGGAATACTCCTGCCCCCGCCGACTGCTGAGCACGGCTGGGTCCATGGCAGACTTAGGGCCACGGACGCATCAGTGGCGACCAAGGAAGGACCGCAGGTGAGTGAGAGCAGTAACCAGGTGAAGGGCAACCGACTCGACCCGTGGCTGGACAGCTATGCGGCACGAGCCCACGGACTGCGTGCCTCGGAGACGCGGTCCCTGTTCGCCGTCGCCTCCCGACCCGAGGTCGTCTCCCTGGCCGGCGGCATGCCCAACCTCAAGGACCTCCCGCTGGAGCGTCTGGCTGAGGCCACTGCACGGATGATCCGCGAGGACGGCGGCCGGGCGCTGCAGTACGGGAACGGGCAGGGACTGCCGCGGCTGCGAGAGCAGATCACCGAGGTCATGGCCCTGGAGGGGATCAGGGCCGATCCCGAGGACGTCATCGTCACCACCGGCTCTCAGCAGGCCGTCGACATCATCACCGAGCTCTTCGTCGACCCCGGCGACGTCGTGCTGACCGAGGCGCCCACCTACGTCGGCTCACTGTCGATCTTCGCGACCTACCAGGCCGATGTGCAGCAGGTGCCCATTGATGCCGGGGGCGTCGTCCCGGAGGCGCTGGAGGAGACGATCGTCCGCCTCGAACGCGAAGGACGCCGTATCAAGTTCTTCTACTGCCTCCCCAACTTCCATAACCCCGCCGGAGTGACCCTCGCCGAAGAGCGCCGTGGACAGGTCGTTGAGATCTGCCGACGCCACCACATCCTCATCGTGGAGGACAATCCCTACGGTCTTCTGGGCTTCGAGGGGCAGACCTACACCGCGCTCAAGACCCTCGCGCCCGACGACGTCGTCTACCTGGGTTCCTTCTCCAAGATCTTCGCCCCGGGTTACCGCGTGGGCTGGGCGGTGGCCCCGCCGGCCGTGCGGGAGAAGATGAAGCTGGCCTCCGAGGCGGCGATCCTGTGCCCGTCATCGGTGGGGCAGTTCTCGATCTCCATGTACCTGGACCAGTTCGACTGGAAGCAGCAGATCGTGGACTTCCGGGCCATGTACCAGGAGCGGCGCGACGCCATGGTCTCGGCACTGGAGGAGTTCCTGCCCATGTGCCACTGGAACGTGCCCGATGGCGGCTTCTACGTGTGGGTACGGCTTCCCGAGGGACTCGATGCCAAAGACATGCTGCCGCGCGCGGTCACGAGCCTGGTCGCCTACGTCTCCGGCACGGCCTTCTACGCCGGCGGCAGGGCGGGGCAGGACCACCTGCGACTGTCCTTCTGCTATCCCGAACCCGCCGAGATCCGTGAAGGGGTGCGCAGGCTGTCCGGCGTCGTGACCCGCGATCTCGAGCTGCTGAGCCTGTTCGGGCCCACCCACAGTCCCCATCCGTCCGAGGGCGTCCACGCGCCCGCACCCGACCAGATCTGA","MFHVKHRGILLPPPTAEHGWVHGRLRATDASVATKEGPQVSESSNQVKGNRLDPWLDSYAARAHGLRASETRSLFAVASRPEVVSLAGGMPNLKDLPLERLAEATARMIREDGGRALQYGNGQGLPRLREQITEVMALEGIRADPEDVIVTTGSQQAVDIITELFVDPGDVVLTEAPTYVGSLSIFATYQADVQQVPIDAGGVVPEALEETIVRLEREGRRIKFFYCLPNFHNPAGVTLAEERRGQVVEICRRHHILIVEDNPYGLLGFEGQTYTALKTLAPDDVVYLGSFSKIFAPGYRVGWAVAPPAVREKMKLASEAAILCPSSVGQFSISMYLDQFDWKQQIVDFRAMYQERRDAMVSALEEFLPMCHWNVPDGGFYVWVRLPEGLDAKDMLPRAVTSLVAYVSGTAFYAGGRAGQDHLRLSFCYPEPAEIREGVRRLSGVVTRDLELLSLFGPTHSPHPSEGVHAPAPDQI$","Aminotransferase, class I and II","Cytoplasm","aspartate aminotransferase","aminotransferase; class I and II","aminotransferase, class I and II","","Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K., Okamoto A., Higuchi T., Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 1991. 266(4):2567-2572. PMID: 1990006","","","

InterPro
IPR004839
Domain

Aminotransferase, class I and II
PF00155	$\"[81-442]T$	Aminotran_1_2

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[118-339]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[341-450]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[100-446]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF17	$\"[100-446]T$	AMINOTRANSFERASE RELATED

","BeTs to 10 clades of COG1167COG name: Transcriptional regulators containing a DNA-binding HTH domain and an aminotransferase domain (MocR family) and their eukaryotic orthologsFunctional Class: K [Information storage and processing--Transcription] Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1167 is ---pkzy-vdrlb-efgh---j----Number of proteins in this genome belonging to this COG is 1","***** IPB001176 (1-aminocyclopropane-1-carboxylate synthase signature) with a combined E-value of 1.7e-06. IPB001176B 113-129 IPB001176C 147-167 IPB001176D 169-190","","","-63% similar to PDB:1X0M a Human Kynurenine Aminotransferase II Homologue from Pyrococcus horikoshii OT3 (E_value = 1.9E_85);-59% similar to PDB:1WST Crystal structure of multiple substrate aminotransferase (MsAT) from Thermococcus profundus (E_value = 5.3E_75);-57% similar to PDB:1VP4 Crystal structure of Aminotransferase, putative (TM1131) from Thermotoga maritima at 1.82 A resolution (E_value = 2.7E_63);-42% similar to PDB:1V2D Crystal Structure of T.th HB8 Glutamine Aminotransferase (E_value = 1.0E_22);-42% similar to PDB:1V2E Crystal Structure of T.th HB8 Glutamine Aminotransferase complex with a-keto-g-methylthiobutyrate (E_value = 1.0E_22);","Residues 81 to 442 (E_value = 5.1e-29) place ANA_2208 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.","","aminotransferase (MsAT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2209","2392188","2393135","948","6.03","-6.44","33493","ATGAACCAGTCTCCACTCCGTATCGCTGTCCTCGCCGGCGGATTGAGCCACGAGCGGGACATCTCCCTGCGCTCGGGGCATCGTGTCGCCCAGGTGCTCAAGCATCTCGGGCACACCGTCCTCGTCCTGGACATCGACGCACGCACCATCGGGTCGCTCAAGACCTTCGGGCCCGACGTCGTGTGGCCCTTGGTTCACGGCGGCCCCGGGGAGGACGGGGGGCTTCAGAATGTCCTCATCTCCCTGGGACTTCCATACGTCGGCACGCACTCCGACGGCTGCCAGCGAGCCTCCTTCAAACCGACGGCCAAGGCAAGCGTTCGCACCGGAGGAGTGATTACTCCTGATTCATTAACGCTTCCACACTCCTATTTCAGTCAACTGGGGGCCCAGGAGGTTCTCACCGTCGTGGCGGGTCATCTGGGACTTCCTGTCGTAGTGAAGCCGCATCAGGGGGGCTCCGGACTTGGTGTCTCCTACGCATCGACGGCGGACGAGCTGCGCTCCGCGATGGTGGCGTGCTTCGCCTACGACGAGCGCGCCCTCATCGAGCGCTACATCGCCGGGACTGAGCTGGCGGTCTCCGTCGTCGACACAGGAGAGGGGCCGCGCGCACTTCCCCCGGTAGAGGTCGTCACCGATGGGCAGTACGACTTCGATGCACGGTACAACCCGGGCCGTTCGGAGTACTTCGTGCCGGCTCGGCTGGATGAGGCGGTCATCGAGAAGGTGAAGAAGACGGCTATCACGGTTCACACCACTCTCGGGCTGGGCAATCTCTCGCGCACCGACCTCATTCTCGATGACAAGGGGACTCCGTGGTTCATCGACGTCAACGTCATTCCAGGAATGACAGAAACGTCCCTGCTGCCTATCGCCGCCAAGGCGGAGGGCTCCCTAGAAGAGCTGTATGACGCGCTGGTGAGGAACCCACTAGTGCATCCGTAA","MNQSPLRIAVLAGGLSHERDISLRSGHRVAQVLKHLGHTVLVLDIDARTIGSLKTFGPDVVWPLVHGGPGEDGGLQNVLISLGLPYVGTHSDGCQRASFKPTAKASVRTGGVITPDSLTLPHSYFSQLGAQEVLTVVAGHLGLPVVVKPHQGGSGLGVSYASTADELRSAMVACFAYDERALIERYIAGTELAVSVVDTGEGPRALPPVEVVTDGQYDFDARYNPGRSEYFVPARLDEAVIEKVKKTAITVHTTLGLGNLSRTDLILDDKGTPWFIDVNVIPGMTETSLLPIAAKAEGSLEELYDALVRNPLVHP$","D-alanine--D-alanine ligase","Cytoplasm","D-ala D-ala ligase","D-alanine--D-alanine ligase ","D-alanine--D-alanine ligase","","Roper D.I., Huyton T., Vagin A., Dodson G. The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA). Proc. Natl. Acad. Sci. U.S.A. 2000. 97(16):8921-8925. PMID: 10908650Fan C., Park I.S., Walsh C.T., Knox J.R. D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant. Biochemistry 1997. 36(9):2531-2538. PMID: 9054558","","","

InterPro
IPR011095
Domain

D-alanine--D-alanine ligase, C-terminal
PF07478	$\"[100-309]T$	Dala_Dala_lig_C

InterPro
IPR011127
Domain

D-alanine--D-alanine ligase, N-terminal
PF01820	$\"[6-88]T$	Dala_Dala_lig_N

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[104-309]T$	ATP_GRASP

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[163-314]T$	no description

InterPro
IPR013817
Domain

Pre-ATP-grasp fold
G3DSA:3.40.50.20	$\"[4-87]T$	no description

noIPR
unintegrated

unintegrated
PTHR23132	$\"[48-312]T$	D-ALANINE--D-ALANINE LIGASE

","BeTs to 17 clades of COG1181COG name: D-alanine-D-alanine ligase and related ATP-grasp enzymesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1181 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB000291 (D-alanine--D-alanine ligase/VANA/B/C) with a combined E-value of 2.1e-45. IPB000291A 8-23 IPB000291B 59-99 IPB000291C 141-184 IPB000291D 213-230 IPB000291E 262-301***** IPB013651 (ATP-grasp fold, RimK-type) with a combined E-value of 2.2e-08. IPB013651C 130-174 IPB013651E 250-300","","","-53% similar to PDB:1IOV COMPLEX OF D-ALA:D-ALA LIGASE WITH ADP AND A PHOSPHORYL PHOSPHONATE (E_value = 3.1E_38);-53% similar to PDB:2DLN VANCOMYCIN RESISTANCE: STRUCTURE OF D-ALANINE:D-ALANINE LIGASE AT 2.3 ANGSTROMS RESOLUTION (E_value = 3.1E_38);-53% similar to PDB:1IOW COMPLEX OF Y216F D-ALA:D-ALA LIGASE WITH ADP AND A PHOSPHORYL PHOSPHINATE (E_value = 8.9E_38);-47% similar to PDB:2FB9 Crystal structure of the Apo form of D-alanine: D-alanine ligase (Ddl) from Thermus caldophilus: a basis for the substrate-induced conformational changes (E_value = 4.1E_27);-43% similar to PDB:1EHI D-ALANINE:D-LACTATE LIGASE (LMDDL2) OF VANCOMYCIN-RESISTANT LEUCONOSTOC MESENTEROIDES (E_value = 1.1E_22);","Residues 6 to 98 (E_value = 1.4e-12) place ANA_2209 in the Dala_Dala_lig_N family which is described as D-ala D-ala ligase N-terminus.Residues 97 to 285 (E_value = 0.0048) place ANA_2209 in the ATP-grasp_3 family which is described as ATP-grasp domain.Residues 100 to 309 (E_value = 3.2e-39) place ANA_2209 in the Dala_Dala_lig_C family which is described as D-ala D-ala ligase C-terminus.","","D-ala ligase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2210","2399021","2397420","1602","5.10","-20.23","57307","ATGGCTCAGAAACGGCGCGGACTGGGACGAGGTCTGCAGGCGCTGATTCCCGAGGCGCAGAAGGAAAAGGTACCGGCTGCGTCTCGTCCTTCCGATGTGTTCTTCCCCGACTCCCGGAAGGACGAGTCGCGTGATGAGGATGCGGCGTCCCAGGCCACGCATGACGCTCCGGAGCCTGAGCCGGCCGCCGAGGCGCGCAGTACTCGCGATCTGGCCGCTACTCTCCTGGCTCCGTCTCAGCGGAAGCGTGGCTCCAAGAGCCGTTCGACTCGTTCGACGACAGCTTCCAAGACCGCTGCCTCAAAGACCGCTGCGCAGAGTAGGCAGACGAAGCCGGTTTCACGTGAAACCACGCCAGACTCGGAGACTGCTGCTCAGGTGACGGAGAAAAAGTCCACGAAGAAATCGTCCTCTGCTGCCACGAAGCGGACATCGTCGGCGGCGCCGAAGCGAGCGACCACAAAGGCGACAAAGGAAGCGTCTGTCGCGGTGGAAAAGCCTTCGCATGAGGCCTCCACGGTCGAGGATCCCCAGGAGGAGATTGCGCCGACGTCTGTTGCTCAGCCGGACGAAACGCCCGTGGTCCCCGAGGTTTCACGTGAAACGGCAGAGGAGCAGCCTGTCGCTGCCGATCTCGGAAGCTCCGATGCCGAGGAGGAGAGGACCGAGGAAGACCTGGCGGCGGTTTCATCTGACGCTGGCACTGAGGCGTCGGACGCGACCGTTGCTGAGGAGGAGACGGCGGATACAGGCGCGGACGACCTCGTTCCCGTTCCGGGTGCTCGCTTCGCTGAGATTCCAGTGGGGCTGATTCACCCGAATCCCCGTCAGCCCCGTCAGGTCTTCGACGAAGAGGACATCGCCGAACTGGCGGCTTCGATTGCTGAAGTGGGTCTGCTGCAGCCGATCGTGGTGCGCCAGGTGCCGACCGCTCCGGGAGAGGAGCTTCGGTACGAGCTCATTATGGGTGAGCGGCGTCTTCGCGCTTCCAAGGAAGCTGGACTGGAGACCATTCCGGCGGTCGTTCGGGACACCGACGACGTCGACCTGCTGCGTGACGCACTGCTGGAGAACCTGCACCGCGTCCAGCTCAATCCCTTGGAAGAGGCCGCGGCCTACCAGCAGTTGCTGGAGGACTTCCAGTGCACTCACGCGGAGCTCTCCGAGCGGATCGCCCGGTCTCGTTCCCAGATCTCCAACACGCTGCGTCTCATGAAGCTGCCACCGTTGGTGCAGCGCCGGCTTGCTGCGAATGTCATTTCCGCAGGACATGCCCGCGCACTTCTGGGTCTTCCCAATGCGGCGGAGATGGAACGACTTGCTCAGCGTGTGGTTGCCGAGGGACTGTCAGTGCGCGCCACGGAGGAGCTCGTGGCCCTTCATGAGGAACCTGAGCCGGGACCGGATCAGCCGAGGGTCTTACGCGCTCGAAGCACCCCTCTCCCGGCGCTCTCGACTCGGCTGTCCGATGCCTTCGACACTCGCGTGAAGGTGACACGGGGAGCGAAGAAGGGGCGCATCACCATTGAGTTCGCGGGTGATGAGGACCTCGCCCGCCTGGTCGATGCGCTGGCGCCGGGAACGTCTCTTGACGAGGAGTAG","MAQKRRGLGRGLQALIPEAQKEKVPAASRPSDVFFPDSRKDESRDEDAASQATHDAPEPEPAAEARSTRDLAATLLAPSQRKRGSKSRSTRSTTASKTAASKTAAQSRQTKPVSRETTPDSETAAQVTEKKSTKKSSSAATKRTSSAAPKRATTKATKEASVAVEKPSHEASTVEDPQEEIAPTSVAQPDETPVVPEVSRETAEEQPVAADLGSSDAEEERTEEDLAAVSSDAGTEASDATVAEEETADTGADDLVPVPGARFAEIPVGLIHPNPRQPRQVFDEEDIAELAASIAEVGLLQPIVVRQVPTAPGEELRYELIMGERRLRASKEAGLETIPAVVRDTDDVDLLRDALLENLHRVQLNPLEEAAAYQQLLEDFQCTHAELSERIARSRSQISNTLRLMKLPPLVQRRLAANVISAGHARALLGLPNAAEMERLAQRVVAEGLSVRATEELVALHEEPEPGPDQPRVLRARSTPLPALSTRLSDAFDTRVKVTRGAKKGRITIEFAGDEDLARLVDALAPGTSLDEE$","ParB-like partition protein","Cytoplasm, Periplasm","ParB","ParB-like partition proteins","parB-like partition protein","","","","","

InterPro
IPR003115
Domain

ParB-like nuclease
PF02195	$\"[264-359]T$	ParBc
SM00470	$\"[264-359]T$	ParB

InterPro
IPR004437
Family

ParB-like partition protein
TIGR00180	$\"[259-445]T$	parB_part: ParB-like partition proteins

","BeTs to 14 clades of COG1475COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1475 is aom-kz-q-drlb-efg-snujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003115 (ParB-like nuclease) with a combined E-value of 2.3e-26. IPB003115A 289-305 IPB003115B 318-329 IPB003115C 357-370 IPB003115D 395-404","","","-57% similar to PDB:1VZ0 CHROMOSOME SEGREGATION PROTEIN SPO0J FROM THERMUS THERMOPHILUS (E_value = 4.7E_35);-41% similar to PDB:1W79 CRYSTAL STRUCTURE OF THE DD-TRANSPEPTIDASE-CARBOXYPEPTIDASE FROM ACTINOMADURA R39 (E_value = 4.7E_35);-41% similar to PDB:1W8Q CRYSTAL STRUCTURE OF THE DD-TRANSPEPTIDASE-CARBOXYPEPTIDASE FROM ACTINOMADURA R39 (E_value = 4.7E_35);-41% similar to PDB:1W8Y CRYSTAL STRUCTURE OF THE NITROCEFIN ACYL-DD-PEPTIDASE FROM ACTINOMADURA R39. (E_value = 4.7E_35);-38% similar to PDB:2IYA THE CRYSTAL STRUCTURE OF MACROLIDE GLYCOSYLTRANSFERASES: A BLUEPRINT FOR ANTIBIOTIC ENGINEERING (E_value = 4.7E_35);","Residues 264 to 359 (E_value = 1e-37) place ANA_2210 in the ParBc family which is described as ParB-like nuclease domain.","","(parB) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2211","2399923","2399021","903","4.79","-16.88","32290","TTGTCCGGATCGTCTATCTTCGATCAGCTCCAGGCCGAGCACCTCGCATTAGACGAGGTAGCGGGTGGAGAGTTCCCACATCCCGAACGGACTCGTGTCATCGCAGTCGCCAATCAGAAAGGCGGCGTCGGAAAAACATCGACGGCGGTGAATCTTGCAGCGGCTTTAGCTGAAGGCGGGTTGCACGTCCTGCTCATTGATGCCGACTCTCAAGGTAATGCCTCTACGGCACTGGGGGTGGAGCATGATGAGGACAGTGCCTCCATCTACGACGTCCTCGTTGACGCCATGCCGATCAAGGATGTCGTCGCCAAGACGCGATTCTGTGAGTCCCTGTGGTGCGTACCGGCGACCATTGACGTGGCTGCGGTTGAGATAGAGCTCATCTCCACGGCCGAGCGTGAGTCGCGGCTGCGGCGTGCCCTGGTGGACTACCTGGTTTCACGTGAAACCGACGGTCTGGAGCCTCTCGACTACGTCATCATCGATTGCCCTCCGAGCCTCGGCATTATGACGATCAACGCCTTCGTCGCTGCGGACGAGGTTCTCATTCCGATGCAGGCCGAGTACTACGCTCTCGAAGGTCTCGCCCTGTTGACGCGCTCCATTGACAGGATCGCGCGTATTCACAATCCGGGGCTGGGAGTCTCCATGATTGTGCTCACCATGTTTGACGGACGTACCACCCTGGCTCGTGAGGTGGAGTCTGAAGTTCGTTCCTATTTCCCTGATGCGACGCTGGACACCAAGGTGCCACGTTCCATCCGTGTTGCCGAGGCCCCCTCCTTCGGTGCTCCTGTGGTGTTCTGGGATCCCCGGTCCACCGGCGCAATTGCGTACAAGAAAATGGCTCGTGAGGTCGCTCTGCGGGGCGCTCCCCGAATTGAAGGCGAGGAAGCCTGA","LSGSSIFDQLQAEHLALDEVAGGEFPHPERTRVIAVANQKGGVGKTSTAVNLAAALAEGGLHVLLIDADSQGNASTALGVEHDEDSASIYDVLVDAMPIKDVVAKTRFCESLWCVPATIDVAAVEIELISTAERESRLRRALVDYLVSRETDGLEPLDYVIIDCPPSLGIMTINAFVAADEVLIPMQAEYYALEGLALLTRSIDRIARIHNPGLGVSMIVLTMFDGRTTLAREVESEVRSYFPDATLDTKVPRSIRVAEAPSFGAPVVFWDPRSTGAIAYKKMAREVALRGAPRIEGEEA$","Cobyrinic acid a,c-diamide synthase","Cytoplasm","ParA","cobyrinic acid a;c-diamide synthase","Cobyrinic acid a,c-diamide synthase","","Pollich M., Klug G. Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus. J. Bacteriol. 1995. 177(15):4481-4487. PMID: 7635831Roth J.R., Lawrence J.G., Rubenfield M., Kieffer-Higgins S., Church G.M. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. J. Bacteriol. 1993. 175(11):3303-3316. PMID: 8501034","","","

InterPro
IPR002586
Domain

Cobyrinic acid a,c-diamide synthase
PF01656	$\"[34-259]T$	CbiA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[32-287]T$	no description
PTHR23264	$\"[33-57]T$	NUCLEOTIDE-BINDING PROTEIN NBP35(YEAST)-RELATED
PTHR23264:SF1	$\"[33-57]T$	gb def: Mus musculus 9 days embryo whole body cDNA, RIKEN full-length enriched library,

InterPro
IPR003682
Family

Glucose inhibited division protein
PD004441	$\"[15-93]T$	GIDB_STRCO_O54571;
PF02527	$\"[8-190]T$	GidB
TIGR00138	$\"[12-195]T$	gidB: methyltransferase GidB

InterPro
IPR013838
Binding_site

Beta tubulin, autoregulation binding site
PS00228	$\"[1-4]?$	TUBULIN_B_AUTOREG

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[3-195]T$	no description
PTHR13369	$\"[63-122]T$	UNCHARACTERIZED

","BeTs to 17 clades of COG0357COG name: Predicted S-adenosylmethionine-dependent methyltransferase involved in bacterial cell divisionFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0357 is -------qvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 1","***** IPB003682 (Glucose inhibited division protein) with a combined E-value of 1.6e-33. IPB003682A 15-36 IPB003682B 60-90 IPB003682C 120-131 IPB003682D 145-160","","","-52% similar to PDB:1JSX Crystal Structure of the Escherichia coli Glucose-Inhibited Division Protein B (GidB) (E_value = 1.6E_14);-48% similar to PDB:1XDZ Crystal Structure of Gram_Positive Bacillus subtilis Glucose inhibited Division protein B (gidB), Structural genomics, MCSG (E_value = 1.6E_14);","Residues 8 to 190 (E_value = 2.6e-58) place ANA_2212 in the GidB family which is described as Glucose inhibited division protein.Residues 52 to 85 (E_value = 8.9e-05) place ANA_2212 in the MTS family which is described as Methyltransferase small domain.","","GidB (gidB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2213","2401289","2400678","612","4.26","-31.05","21691","ATGAGTGAGCAGCACAGTAACGACTCCTCCCAGCAGACAGCGGAGGAGGCCTCGAGCAGCCCCGTGAGCAACACCGTCTCGCGCCTCGAGGAGGAGGGCGAGATCGGTGCCGACTACCTCGAGGAGCTTCTCGACATCGCCGATCTGGGCGGTGACATCGACATCGACATCGATCACGGGCGCGCCTCGATTGCCGTGGTCGCCTCCGAGGAGGGTGACGAGCGCGAGCTCGCCGACCTCGTTGGACGCGACGGTGAGGTTCTCGAGGCCGTTCAGGAGCTGACCCGTCTCGCCGTCCAGGCGCGCACCGGTAACCGCTCCCGGCTCATGCTCGACATCAACGGCTACCGCGCGGACCGACGCACCGAGCTGACCAAGGTGGCCCAGGAGGCGGTCACCAAGGTCCTCACCTCAGGAGAGGCCGTCAGTCTTGAGCCGATGAACCCCTTCGAGCGCAAGGTGTGCCACGACGTTGTCGCCGCCGCCGGACTGGTCTCCGAGTCTGAGGGCGCCGAGCCGCACCGCTACGTCGTGGTCCTGCCCGCCGACGAGGAGGGCGTGGACGACGCTGCCGAGGACGCGGCCGACGACTCCGCTTCGGAGCAGGCCTGA","MSEQHSNDSSQQTAEEASSSPVSNTVSRLEEEGEIGADYLEELLDIADLGGDIDIDIDHGRASIAVVASEEGDERELADLVGRDGEVLEAVQELTRLAVQARTGNRSRLMLDINGYRADRRTELTKVAQEAVTKVLTSGEAVSLEPMNPFERKVCHDVVAAAGLVSESEGAEPHRYVVVLPADEEGVDDAAEDAADDSASEQA$","SpoIIIJ-associated protein","Cytoplasm","SpoIIIJ-associated protein","K06346 spoIIIJ-associated protein","single-stranded nucleic acid binding R3H domain protein","","Grishin N.V. The R3H motif: a domain that binds single-stranded nucleic acids. Trends Biochem. Sci. 1998. 23(9):329-330. PMID: 9787637","","","

InterPro
IPR001374
Domain

Single-stranded nucleic acid binding R3H
PF01424	$\"[128-182]T$	R3H
SM00393	$\"[104-182]T$	R3H
PS51061	$\"[118-183]T$	R3H

","BeTs to 7 clades of COG1847COG name: Predicted RNA-binding proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1847 is --------vdrlbc----------t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 128 to 182 (E_value = 2.7e-15) place ANA_2213 in the R3H family which is described as R3H domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2216","2402527","2401343","1185","10.06","19.66","44029","ATGGACACGTTGCTGTGGCCCCTCAAGGTGGCCGTGGCCTGGGTCATGGTCACGATCCACAAGGCCCTGGTCCTCATCGGGTTCCCCGACGGACCGGGTATTGCCTGGGTGCTGTCCATCATCGGTCTGACGATCGTGGTGCGGCTACTCATCATGCCGCTGTTCGTCAAGCAGATACGAGCCTCCCGCGGGATGCAGCTCCTCCAGCCCGAGCTGCAGGCCCTTCAGGCCAAGTACAAGGGCAAGAAGGATCCCGAGTCGCGCCAGCGCATGAACGAAGAGATGATGGCGCTCTACCGCAAGCACGGGACCAACCCCATGGCCTCCTGCCTGCCGATTCTGGTGCAGATGCCCATCTTCTTCGCCCTGTTCCGGGTTCTGGCCTCCCTGGGCGCCGTCGCCGGTGGCACCTACGGACGTCCCTCGATCGGTCCGCTCACGCAGCAGCTGGCCGAACAGGTCCAGGCCTCCAGCGTCTTCGGCGCCAGTCTGTCCTCCTCCTTCCTGGGCAGCTCCGACACGCAGGTCAAGATCGTCACGGTCGCCATGATCATCATCATGTCGGTGACGCAGTGGTACACCATGGCGCAGCTGTCGATGAAGAACATGTCGACGGACTCCCTCAACTCCGACAACCCCATGATCCGTTCCCAGCGGATGATGCTGTACGTGATGCCGGTGATCTTCGCAGTCTCCGGCGTCAACTTCCAGATCGGTGTGCTCGTCTACTGGGTCGTCTCCAACCTGTGGACCATGGGCCAGCAGTTCTTCACCATCCGCAACATGCCCGCACCCGGCAGCGAGGCGGAGAAGAAGTACCGCGCCCGGATCAACGCCAAGCGGGCGCGCAAGGGCCTGCCCTCCCTGGAGGAGGAGGAACGGGCCGAGGCGATCGCCAAGGCCGAGGCCGAGGGACGTACCGGCGGCCAGCGGGTGCAGCCGGTGCGCAAGAACCGGCAAAAGAAGTCAGGCGGTCAGGGCGAGTCCCGCAGTGAGGCCTTCACTGACGACTTCGATGTCGAGCAGCTCGAGGACGCCGATGAGGACAGGGACTCGACGTCGGCCAAGAACGGTGGCCTCAGCGATGAGGAGATCGCTCGACGTCGTTATGAGCGCCGAGCTCGCCAGCGTCGAGAGGCGGCGGCTCGACGCAAGGCCCAGGCCAAGAAGAAGCACAACCGCTGA","MDTLLWPLKVAVAWVMVTIHKALVLIGFPDGPGIAWVLSIIGLTIVVRLLIMPLFVKQIRASRGMQLLQPELQALQAKYKGKKDPESRQRMNEEMMALYRKHGTNPMASCLPILVQMPIFFALFRVLASLGAVAGGTYGRPSIGPLTQQLAEQVQASSVFGASLSSSFLGSSDTQVKIVTVAMIIIMSVTQWYTMAQLSMKNMSTDSLNSDNPMIRSQRMMLYVMPVIFAVSGVNFQIGVLVYWVVSNLWTMGQQFFTIRNMPAPGSEAEKKYRARINAKRARKGLPSLEEEERAEAIAKAEAEGRTGGQRVQPVRKNRQKKSGGQGESRSEAFTDDFDVEQLEDADEDRDSTSAKNGGLSDEEIARRRYERRARQRREAAARRKAQAKKKHNR$","Preprotein translocase YidC subunit","Periplasm, Membrane","60 kDa inner-membrane protein homolog","K03217 preprotein translocase YidC subunit","60 kDa inner membrane insertion protein","","Novoseler M., Hershkovits G., Katcoff D.J. Functional domains of the yeast chromatin protein Sin1p/Spt2p can bind four-way junction and crossing DNA structures. J. Biol. Chem. 2005. 280(7):5169-5177. PMID: 15563464","","","

InterPro
IPR001708
Family

60 kDa inner membrane insertion protein
PTHR12428	$\"[4-155]T$ $\"[179-277]T$	OXA1
PF02096	$\"[36-263]T$	60KD_IMP

InterPro
IPR013256
Family

Chromatin SPT2
SM00784	$\"[317-387]T$	no description

noIPR
unintegrated

unintegrated
PTHR12428:SF9	$\"[4-155]T$ $\"[179-277]T$	gb def: Membrane protein oxaA
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[34-56]?$ $\"[108-128]?$ $\"[178-196]?$ $\"[222-244]?$	transmembrane_regions

","BeTs to 18 clades of COG0706COG name: Preprotein translocase subunit YidCFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0706 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001708 (60Kd inner membrane protein signature) with a combined E-value of 1.2e-19. IPB001708G 102-125 IPB001708I 226-249","","","No significant hits to the PDB database (E-value < E-10).","Residues 36 to 263 (E_value = 1.6e-70) place ANA_2216 in the 60KD_IMP family which is described as 60Kd inner membrane protein.","","kDa inner-membrane protein homolog","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2217","2402905","2402621","285","10.00","7.79","10839","ATGGGCAGATGGTTGACACGAGTCCTTGTGGCTCCGGTGCGTTTCTATCAGCGCTTCATCTCGCCCGCCCTGCCGGCCTCCTGTCGCTACTACCCCACATGCTCGGCTTACGCCGTCACGGCGCTGGAGGTGCACGGTCCGATCAAGGGCCTGCTGCTGGCCCTGTGGCGTCTGCTGCGATGCAACCCATTGACCCGCGGTGGAGTCGATCATGTCCCGGACAGGGGGCAGTGGCGATACCACCATCCCCGTGACGTTCCGAGGTTCACGGTCGAGGACCCCTGA","MGRWLTRVLVAPVRFYQRFISPALPASCRYYPTCSAYAVTALEVHGPIKGLLLALWRLLRCNPLTRGGVDHVPDRGQWRYHHPRDVPRFTVEDP$","Alpha-hemolysin","Membrane, Cytoplasm, Extracellular","alpha-hemolysin homolog","K08998 hypothetical protein","protein of unknown function DUF37","","","","","

InterPro
IPR002696
Family

Protein of unknown function DUF37
PD004225	$\"[9-73]T$	YJ13_ENTFA_Q833N1;
PF01809	$\"[5-72]T$	DUF37
TIGR00278	$\"[9-83]T$	TIGR00278: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide

","BeTs to 17 clades of COG0759COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0759 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB002696 (Protein of unknown function DUF37) with a combined E-value of 5.3e-37. IPB002696 13-63","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 72 (E_value = 5.9e-40) place ANA_2217 in the DUF37 family which is described as Domain of unknown function DUF37.","","homolog ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2218","2403399","2402929","471","11.68","18.54","16673","GTGCCAAGGTGCACGGCTTCCGTAAGCGCATGTCCACCCGCGCAGGCCGCGCCGTCCTCGCTTCGCGGCGCCGCAAGGGCCGCGTTCGCCTCGCCGCCTGAGGTGCTCGGCGCGGCGCACCGATTAGCGCGGGGTGAGGACTTCACTACCGCGATTCGTCGGGGTACGCGCTGCGGGAACCGCAGGCTGGTCGTGCACTACCACGCCGGCGGGAGAGGGGATGACTCCCCGGCTCTCGTCGGCGTCGTCGTGCCCAAGAAGCAGGTCCCGCTGGCGACTCGCCGCAACCGCGTCAAGCGCCGGGTGCGAGCCCTCATGGCGCAGCGGGTCGGTTCCCTCGAACCGGGCGCCCGCGTCGTCGTACGCGGACTGGCAGGTGCCGACGGCGCCGACAGCAACACCCTGGGACGGGACCTGGACCGGCTGCTGAGCCGGTGCCGGGAGCGTCAGGACGAAGGGCGTCGGCGGTGA","VPRCTASVSACPPAQAAPSSLRGAARAAFASPPEVLGAAHRLARGEDFTTAIRRGTRCGNRRLVVHYHAGGRGDDSPALVGVVVPKKQVPLATRRNRVKRRVRALMAQRVGSLEPGARVVVRGLAGADGADSNTLGRDLDRLLSRCRERQDEGRRR$","Ribonuclease P protein component","Extracellular, Cytoplasm","Ribonuclease P protein component (RNasePprotein) (RNaseP protein) (Protein C5)","putative ribonuclease P component ","ribonuclease P protein component","","Pace N.R., Smith D. Ribonuclease P: function and variation. J. Biol. Chem. 1990. 265(7):3587-3590. PMID: 1689306Altman S. Ribonuclease P. Postscript. J. Biol. Chem. 1990. 265(33):20053-20056. PMID: 1700778Brown J.W., Pace N.R. Ribonuclease P RNA and protein subunits from bacteria. Nucleic Acids Res. 1992. 20(7):1451-1456. PMID: 1374553","","","

InterPro
IPR000100
Family

Bacterial ribonuclease P protein
PF00825	$\"[36-147]T$	Ribonuclease_P
TIGR00188	$\"[36-150]T$	rnpA: ribonuclease P protein component
PS00648	$\"[89-103]T$	RIBONUCLEASE_P

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[36-155]T$	no description

","No hits to the COGs database.","***** IPB000100 (Bacterial ribonuclease P protein) with a combined E-value of 2.7e-06. IPB000100 86-107","","","No significant hits to the PDB database (E-value < E-10).","Residues 36 to 147 (E_value = 2.8e-20) place ANA_2218 in the Ribonuclease_P family which is described as Ribonuclease P.","","P protein component (RNaseP protein) (RNaseP protein) (Protein C5)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2219","2403898","2405703","1806","6.70","-2.49","64630","ATGATGGGACGCCTGGTCAAGACCTTCCGGTTCGCCAGTTCCACACAACCCTGTCATCATCGACACAGGGCCCCGGCCGGCGTCGGTCGGGCTGCAGTCACCGGGTTCACCAACCATGCCGATCAGGAGTCCGTCGTGCCCGACGCCGCCAATACCAAATGGCTCTCAGCCCTTGAGGTGCTCTCCAGCTCCGGAGAACTGGGCCAGGGCAAGATGTCCATGATCCGCATGACCCACCTCATCGACGTCGACGGCACGCTCGTCCTCGTCGTCGGCTCGGCCTTCGCCAAGGACATCGTCGAGCAGGCACGTGCCCCCATCAGCGCCGCCATCACCCAGGTCTGGGGCCGCCCCATGCCCATGGAGGTCACGGTCGACACCTCCTCGGAGGCCTCGCGCGCACCGATGACTCCCATGGCTCCCGAACCCGTCAACCTGGCGACCGTCGCCCCCGCACCGGCATCCTCCCCGTCCCCCTCGGTCCCGCCCCAACCCTCGGGGCCCTCCACCGTGCCGGCTGCGCCCGCTCCACCCACGGTGCCCGCCTACAGCGAGCAGCTCGCCGAGCCCTCGCCCTACTCGGCGACCGCCCCCTCACCGATGCCCTACTCCCAGGCCTCCGCCGCCTCGGCGCCGTCGACGATGTCGGGTTCCCTTCCCACGAGGTCAGCACATCCCGGCACCTACAGCCCCGGGGGCACCGGCCCCCAGAATCCCACCGGGCTGCTGACGCCCACCGCGGCCCACGACGTCTCCCAGCTCAATCCGAGATACACCTTCGACACCTACGTCACCGGCTCCTCCAACCGGTTCGCCCACGCCACCGCGCTGGCCGTGGCCGAGGCCCCGGCCCGTGCCTACAACCCCCTATTCATCTACGGCGGCTCCGGCCTGGGCAAGACGCACCTCCTGCACGCCATCGGCCACTACGCCCAGACCCTCAACCCGGGGATCCGCGTCAAGTACGTCAACTCCGAGGTCTTCGTCTCCGACTTCATCGCCTGCGTGCGCGACGGCAACCAGGACGACGGCCGCATGGAGGGCTTCAAGCGCCGCTACCGCGAGGTCGACATCCTCCTGGTAGACGACATCCAGTTCCTCCAGGGCAAGGAGTCGACCCTCGAGGAGTTCTTCCACACCTTCAACTCCCTGCACTCCTCGGGCAAGCAGGTGGTCCTCACCTCCGACCAGCCCCCCAAGGCCCTCGGTGGGCTCGACGAGCGCCTGCGCTCCCGCTTCGAGTGGGGCCTGCTGGCCGACGTCCAGCCCCCGGACCTGGAGACCCGCATCGCGATCCTCTCCCGCAAGGGCACCGCCGAGGGCCTCGACCTGCCCTTCGACGTCCTGGAGTACATCGCCTCACGCATCACCACCAACATCCGCGAGCTCGAGGGCGCCCTCATCCGGGTCACGGCCTTCGCCTCCCTCAACAAGCAGCCCGTCGACCAGACCCTGGCCGAGATGGTCCTCAAGGACATCATCTCCGACCCCGAGGGCCAGGAGATCACGACCTCCCTCATCATGGCGCAGACCGCCGACTACTTCGGCATCACCATCGACGACCTGTGCTCGGCCAACCGCTCACGCACCATGGTCTCGGCCCGCCACATCGCCATGTACCTGTGCCGCGAGCTCACCGACCTCTCCCTTCCCAAGATCGGGCGGGAGTTCGGCGGGCGCGACCACACCACCGTCATGAGCGCCGACAAGAAGATCCGCACCCTCATGGCCGAGCGGCGCTCGACCTTCAACCAGGTCACCGAGCTGACCAGCCGCATCAAGCAGGCCGCCCAGTCTCCCGCCTAA","MMGRLVKTFRFASSTQPCHHRHRAPAGVGRAAVTGFTNHADQESVVPDAANTKWLSALEVLSSSGELGQGKMSMIRMTHLIDVDGTLVLVVGSAFAKDIVEQARAPISAAITQVWGRPMPMEVTVDTSSEASRAPMTPMAPEPVNLATVAPAPASSPSPSVPPQPSGPSTVPAAPAPPTVPAYSEQLAEPSPYSATAPSPMPYSQASAASAPSTMSGSLPTRSAHPGTYSPGGTGPQNPTGLLTPTAAHDVSQLNPRYTFDTYVTGSSNRFAHATALAVAEAPARAYNPLFIYGGSGLGKTHLLHAIGHYAQTLNPGIRVKYVNSEVFVSDFIACVRDGNQDDGRMEGFKRRYREVDILLVDDIQFLQGKESTLEEFFHTFNSLHSSGKQVVLTSDQPPKALGGLDERLRSRFEWGLLADVQPPDLETRIAILSRKGTAEGLDLPFDVLEYIASRITTNIRELEGALIRVTAFASLNKQPVDQTLAEMVLKDIISDPEGQEITTSLIMAQTADYFGITIDDLCSANRSRTMVSARHIAMYLCRELTDLSLPKIGREFGGRDHTTVMSADKKIRTLMAERRSTFNQVTELTSRIKQAAQSPA$","Chromosomal replication initiator protein dnaA","Cytoplasm, Periplasm, Membrane","Chromosomal replication initiator protein dnaA","chromosomal replication initiator protein DnaA","chromosomal replication initiator protein DnaA","","Skarstad K., Boye E. The initiator protein DnaA: evolution, properties and function. Biochim. Biophys. Acta 1994. 1217(2):111-130. PMID: 8110826Yoshikawa H., Ogasawara N. Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial replication origins. Mol. Microbiol. 1991. 5(11):2589-2597. PMID: 1779750Georgopoulos C. The E. coli dnaA initiation protein: a protein for all seasons. Trends Genet. 1989. 5(10):319-321. PMID: 2558436Skovgaard O. Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli. Gene 1990. 93(1):27-34. PMID: 2172087","","","

InterPro
IPR001957
Family

Bacterial chromosomal replication initiator protein, DnaA
PR00051	$\"[287-307]T$ $\"[319-333]T$ $\"[356-370]T$ $\"[390-417]T$ $\"[553-572]T$	DNAA
TIGR00362	$\"[121-593]T$	DnaA: chromosomal replication initiator pro
PS01008	$\"[553-572]T$	DNAA

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[286-421]T$	AAA

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
PF08299	$\"[503-572]T$	Bac_DnaA_C
SM00760	$\"[503-572]T$	no description

InterPro
IPR013317
Domain

Chromosomal replication initiator, DnaA
PF00308	$\"[254-477]T$	Bac_DnaA

noIPR
unintegrated

unintegrated
G3DSA:1.10.1750.10	$\"[490-598]T$	no description
G3DSA:3.40.50.300	$\"[251-423]T$	no description

","BeTs to 18 clades of COG0593COG name: ATPase involved in DNA replication initiationFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0593 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001957 (Bacterial chromosomal replication initiator protein, DnaA) with a combined E-value of 4.8e-132. IPB001957A 287-306 IPB001957B 349-391 IPB001957C 393-438 IPB001957D 444-470 IPB001957E 507-555 IPB001957F 557-572***** IPB013317 (Chromosomal replication initiator, DnaA) with a combined E-value of 5.3e-97. IPB013317A 259-269 IPB013317B 287-308 IPB013317C 353-399 IPB013317D 405-433 IPB013317E 458-467 IPB013317F 559-568***** IPB010921 (Trp repressor/replication initiator) with a combined E-value of 7.1e-88. IPB010921A 287-308 IPB010921B 357-366 IPB010921C 389-436 IPB010921D 527-568","","","-57% similar to PDB:1L8Q CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR (E_value = 6.3E_52);-57% similar to PDB:2HCB Structure of AMPPCP-bound DnaA from Aquifex aeolicus (E_value = 6.3E_52);-64% similar to PDB:1J1V Crystal structure of DnaA domainIV complexed with DnaAbox DNA (E_value = 9.8E_13);-45% similar to PDB:1HQC STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8 (E_value = 9.8E_13);-45% similar to PDB:1IXR RuvA-RuvB complex (E_value = 9.8E_13);","Residues 254 to 477 (E_value = 9.8e-140) place ANA_2219 in the Bac_DnaA family which is described as Bacterial dnaA protein.Residues 503 to 572 (E_value = 1.3e-39) place ANA_2219 in the Bac_DnaA_C family which is described as Bacterial dnaA protein helix-turn-helix domain.","","replication initiator protein dnaA (dnaA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2220","2406359","2407489","1131","4.88","-16.60","39610","GTGAAGCTCAGGGTTGACCGAGACATCCTCGCTGAAGCCGTCACCTGGACTGCACGATCCGTGCCCGCCCGCCCGCCGGTACCCGTGCTCGCCGGAGTCAGGCTGGAGGCCAAGGGCTCCAGCCTCGTCCTGGCCTCCTTCGACTATGAGGTCTCCGCCCACTGCGAGGTGGCCGCCGATGTCGAGGAGGACGGCGTCGTCCTCGTCTCTGGACGCCTCCTGGCCGATATCGCCAAGGCGCTGCCGAACAAGCCCGTCGACCTGGAGGTCGAGGGCAACAAGGTCGCCGTCTCCTGCGGATCGGCCCGCTTCTCCCTGGCGGCCATGGCCGCCGACGACTACCCGGCGCTGCCGGTCATGCCCGCCGTCGCCGGCACGATCGACGCCCACGACCTGGCCCGCGCCGTCGGCCAGGTCTCCATCGCCGCCTCCCGCGACGACACCCTGCCGCTGCTCACCAGTGTCCAGATCGAGGTCGAGGGCAGCTCGTTGGTCCTCATGGCCACCGACCGCTACCGCCTGGCCATGCGGGAGCTGACCTGGTCGCCGTCCAACACCGAGCTGTCCACCACGGCCCTGCTCAAGGCCCGCACTCTCTCCGACGTCGCCAAGTCCCTGACCTCTTCCGGAGACGTGACCGTGGCCCTCAGCAGCGAGTCGGCCGCCTCCAGCCTCATCGGCTTCGAGGCCGGCGGCCGGCGCACCACCTCCCTGCTCACCGACGGCGACTACCCGCCGGTGCGCCGCCTCTTCCCGGAGTCCACCTCGATCCACGCCACCGTGGGCACCGACGAGCTCATGGCCGCCGTGCGCCGCGTCAGTCTCGTCGCGGACCGCTCCACCCCCATCCACATGTCCTTCACCCAGGGCAACCTGGAGCTCGACGCCGGACAGGGCGACGACGCCCAGGCCACCGAGCAGCTCGTCGCCCACCTCGAGGGCGATGACATCTCCACCGCCTTCAACCCCGGCTACCTCCTCGACGGCCTGGGCGCCCTCAACCAGCCCTACGTCCGCCTCGACTTCACCCACGCCTCGAAGCCCGCGGTGCTCACCGGCATGGACTCCATCGGGGGCACCGAGGACTCCTCCTTCCGCTACCTGCTCATGCCGATCCGCTTCGGGGCCTGA","VKLRVDRDILAEAVTWTARSVPARPPVPVLAGVRLEAKGSSLVLASFDYEVSAHCEVAADVEEDGVVLVSGRLLADIAKALPNKPVDLEVEGNKVAVSCGSARFSLAAMAADDYPALPVMPAVAGTIDAHDLARAVGQVSIAASRDDTLPLLTSVQIEVEGSSLVLMATDRYRLAMRELTWSPSNTELSTTALLKARTLSDVAKSLTSSGDVTVALSSESAASSLIGFEAGGRRTTSLLTDGDYPPVRRLFPESTSIHATVGTDELMAAVRRVSLVADRSTPIHMSFTQGNLELDAGQGDDAQATEQLVAHLEGDDISTAFNPGYLLDGLGALNQPYVRLDFTHASKPAVLTGMDSIGGTEDSSFRYLLMPIRFGA$","DNA polymerase III, beta subunit","Cytoplasm, Membrane","DNA polymerase III, beta subunit","DNA polymerase III; beta chain ","DNA polymerase III, beta subunit","","","","","

InterPro
IPR001001
Family

DNA polymerase III, beta chain
G3DSA:3.10.150.10	$\"[1-117]T$ $\"[118-251]T$ $\"[252-375]T$	no description
PF00712	$\"[1-118]T$	DNA_pol3_beta
PF02767	$\"[126-246]T$	DNA_pol3_beta_2
PF02768	$\"[248-373]T$	DNA_pol3_beta_3
SM00480	$\"[17-370]T$	POL3Bc
TIGR00663	$\"[1-374]T$	dnan: DNA polymerase III, beta subunit

","BeTs to 18 clades of COG0592COG name: DNA polymerase sliding clamp subunit (PCNA homolog)Functional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0592 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001001 (DNA polymerase III, beta chain) with a combined E-value of 4.2e-49. IPB001001A 5-53 IPB001001B 65-82 IPB001001C 97-115 IPB001001D 132-155 IPB001001E 167-176 IPB001001F 237-252 IPB001001G 319-331","","","-48% similar to PDB:1VPK Crystal structure of DNA polymerase III, beta subunit (TM0262) from Thermotoga maritima at 2.00 A resolution (E_value = 2.9E_25);-46% similar to PDB:2AWA Crystal structure of DNA polymerase III, beta chain (EC 2.7.7.7) (np_344555.1) from STREPTOCOCCUS PNEUMONIAE TIGR4 at 2.50 A resolution (E_value = 4.0E_19);-43% similar to PDB:1MMI E. COLI DNA POLYMERASE BETA SUBUNIT (E_value = 2.0E_18);-43% similar to PDB:1OK7 A CONSERVED PROTEIN BINDING-SITE ON BACTERIAL SLIDING CLAMPS (E_value = 2.0E_18);-43% similar to PDB:1UNN COMPLEX OF BETA-CLAMP PROCESSIVITY FACTOR AND LITTLE FINGER DOMAIN OF POLIV (E_value = 2.0E_18);","Residues 1 to 118 (E_value = 7.2e-45) place ANA_2220 in the DNA_pol3_beta family which is described as DNA polymerase III beta subunit, N-terminal domain.Residues 126 to 246 (E_value = 5.2e-26) place ANA_2220 in the DNA_pol3_beta_2 family which is described as DNA polymerase III beta subunit, central domain.Residues 248 to 373 (E_value = 5.8e-34) place ANA_2220 in the DNA_pol3_beta_3 family which is described as DNA polymerase III beta subunit, C-terminal domain.","","polymerase III, beta subunit (dnaN)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2221","2407503","2408720","1218","6.39","-3.08","43360","ATGTACGTCTCTGACCTCTCCCTGGACGACTTCCGCTCCTACCGCAGCCTGGTGCTGTCCCTGGAGCCGGGCCCCAGCGCCTTCGTCGGCTCCAACGGGCAGGGCAAGACCAACCTGGTCGAGGCCATCGTCTACCTGGCGACCCTCTCCTCCCACCGGATCGGCGCGGACACCGCCCTCGTCCGACGGGCGGCACCGGGGCAGGCCCAGCCGGCCGGCGCCGTCGTGCGCGCCCGCGCCGTCCACGGGGAAAGACCCAGCGTCCTGGAGATCGAGATCATCGCCGGCAAGGCGAACCGGGCCCGCCTCAACCGGGGCGGCTGCCGGCCCCGCGACCTGCTCGGGGTGCTGCGCGCGGTCGTCTTCGCCCCCGAGGATCTCTCCCTGGTGCGCGCCGAGCCCGGGGTCCGCCGGGGCTTCCTCGACGACCTGGCGGTCACGCTGCGCCCGGGCCTGGCCGGGGTGCGCGCCGAGCACGACAAGATCCTCGCCCAGCGCGCCAGCCTCCTGAAGTCCGCGCGCGCGGCCCGCTCCTCGACCTCCTCCATGCTCTCCACCCTGGAGGTCTGGGATGCCCAGCTCGCCGCGGCGGCCGCCCGGCTCATCGCCGCCCGGGTCGACGTCGTGCGGCGCCTGCGCCCCTGGGTGGCCTCCGCCTACGAGACCGTCTCGGGGACCTCCGGGCAGCGTTCCCGCGCCCAGATCGCCTATCGCTCCAGCCTGCTGACTCACGAGGGAGTCCCGGAGCCCGACCCCCACGACGAGACGGCCTGGCTCGCCGGCGAGGAGATGCTCCTTGATGAGACCGCCCTGGCCGCGCGCCTGGAGAGCGCCATGGGTGAGCTCCACGCCCGCGAGATCGACCGCGGCGCCAACCTCGTCGGGGCGCACCGCGACGACCTGAGTCTGTTCCTCACCGGTCTGCCCGCCCGTGGATTCGCCTCCCACGGGGAGCAGTGGTCCTTGGCCCTGGCGCTGCGCCTGGCCTCCTACGACATGCTGCGCACTGACATCGACGCCTACGGCGGGGACGGCGAGCCGGTCCTCATCCTCGACGACGTCTTCGCCTCCCTCGACGAGCAGCGCCGCCGCGCCCTGGCCCAGATGGTCGCCGGCGCCCAGCAGGTCCTGCTGACCGCCGCCGTCGACGACGACGTCCCCGCCGAGCTCGCCGGCGCCCGGTACCGCGTGGCCGACGGTGAGGTCACCCGTGGCTGA","MYVSDLSLDDFRSYRSLVLSLEPGPSAFVGSNGQGKTNLVEAIVYLATLSSHRIGADTALVRRAAPGQAQPAGAVVRARAVHGERPSVLEIEIIAGKANRARLNRGGCRPRDLLGVLRAVVFAPEDLSLVRAEPGVRRGFLDDLAVTLRPGLAGVRAEHDKILAQRASLLKSARAARSSTSSMLSTLEVWDAQLAAAAARLIAARVDVVRRLRPWVASAYETVSGTSGQRSRAQIAYRSSLLTHEGVPEPDPHDETAWLAGEEMLLDETALAARLESAMGELHAREIDRGANLVGAHRDDLSLFLTGLPARGFASHGEQWSLALALRLASYDMLRTDIDAYGGDGEPVLILDDVFASLDEQRRRALAQMVAGAQQVLLTAAVDDDVPAELAGARYRVADGEVTRG$","DNA replication and repair protein recF","Cytoplasm, Membrane","DNA replication and repair protein recF","DNA replication and repair protein RecF","DNA replication and repair protein RecF","","Jessberger R. The many functions of smc proteins in chromosome dynamics. Nat. Rev. Mol. Cell Biol. 2002. 3(10):767-778. PMID: 12360193Haering C.H., Lowe J., Hochwagen A., Nasmyth K. Molecular architecture of SMC proteins and the yeast cohesin complex. Mol. Cell 2002. 9(4):773-788. PMID: 11983169","","","

InterPro
IPR001238
Family

RecF protein
TIGR00611	$\"[1-402]T$	recf: DNA replication and repair protein Re

InterPro
IPR003395
Domain

SMC protein, N-terminal
PF02463	$\"[2-403]T$	SMC_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-131]T$	no description

","BeTs to 12 clades of COG1195COG name: Recombinational DNA repair ATPase (RecF pathway)Functional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1195 is ---------drlbcefghs--jxit-Number of proteins in this genome belonging to this COG is 1","***** IPB001238 (RecF protein) with a combined E-value of 2.8e-35. IPB001238A 6-53 IPB001238B 122-142 IPB001238C 159-170 IPB001238D 350-359","","","-60% similar to PDB:2O5V Recombination mediator RecF (E_value = 1.2E_13);","Residues 2 to 403 (E_value = 4.5e-07) place ANA_2221 in the SMC_N family which is described as RecF/RecN/SMC N terminal domain.","","replication and repair protein recF","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2222","2408821","2409390","570","11.45","12.16","20132","GTGCCGGCCCGCCGCCTGCGCGAGCCGGCCGGCGGTTCCGGGGGCAAGAACGCACAGCCGGCAGCGCCCTGGGACCAACGCCGCGAGCTGGCCCGGGCCCTGGGCCAGAACCCCGACGATCCGGCCGACCGCGGCCCCGGACTGGCGCGGGGACGCGACCGGCCCGGACCCACCCCCTTCGACCCCCGCACCGGGCAGCGCGAACTGCGCCGCATGGTGGCCGACAACGGCTGGGCGGGAAAGCTCGCGGTGGCCGGCGTCGTCGCCCGGTGGCGAGCCATCGTGGGCGATCAGGTCGCCGAGCACTGCACCATCGAGTCCTTCGACGCCGGGCGTATCACCCTGCGCGCCTCGTCCTCGAGCTGGGCCCAGCAGCTCCGGCTCCTCCAGCCCACCATCGAAGCCAGGATCGTCGAGGCCCTGCGCTCGGGGCCCGGCGGCCGCCAGGCCGGAGGGATCAGTACCGGCGACGCGGTGGAGCTGCGGATCCTGGGGCCGGCCGGCCCATCCTGGAAGCGCCGCGGAGTCGGCCTGCGCGGCACCCGTGGTCCGCGCGATACCTACGGATAG","VPARRLREPAGGSGGKNAQPAAPWDQRRELARALGQNPDDPADRGPGLARGRDRPGPTPFDPRTGQRELRRMVADNGWAGKLAVAGVVARWRAIVGDQVAEHCTIESFDAGRITLRASSSSWAQQLRLLQPTIEARIVEALRSGPGGRQAGGISTGDAVELRILGPAGPSWKRRGVGLRGTRGPRDTYG$","Conserved hypothetical protein","Cytoplasm, Extracellular","alpha-1 type 2 collagen (714 AA)","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR007922
Family

Protein of unknown function DUF721
PF05258	$\"[77-173]T$	DUF721

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 77 to 173 (E_value = 2.3e-17) place ANA_2222 in the DUF721 family which is described as Protein of unknown function (DUF721).","","type 2 collagen (714 AA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2223","2409717","2411744","2028","5.29","-26.16","74225","GTGTCTGACCAGGACGCCACTGTGAATCACGATTACGGAGCCTCGGACATCACCGTCCTCGAAGGGCTCGAAGCGGTCCGGAAGCGCCCCGGCATGTACATCGGTTCCACCGGTGAGCGGGGCCTGCACCACCTCGTCTACGAGGTCGTCGACAACTCCGTCGACGAGGCCCTGGCCGGCTACTGCGACCACATCGAGGTCACCATCCTGGCCGACGGCGGCGTGCGCGTCAGCGACAACGGCCGCGGCATCCCGGTCGACGAGCACCCCACCGAGCACAAGCCCACCGTCGAGGTCGTCATGACGATCCTGCACGCCGGCGGCAAGTTCGGGGGCGGCGGCTACGCCGTCTCCGGCGGTCTGCACGGCGTGGGCATCTCCGTGGTCAACGCCCTGTCCACCCGGGTGGACACCGAGGTCCGCCGGCAGGGCTTCGTGTGGCGCATGTCCTTCGCCGACGGCGGCCGCCCCATCACCGAGCTCGTCAAGGGCGAGGCCACCGAGTCCACCGGCACCACCCAGACCTTCTACCCGGACCCGACCATCTTCGAGACGGTCGACTTCGACTACGAGACGCTGCGCCGTCGCTTCCAGCAGATGGCTTTCCTCAACAAGGGCCTGCGCATCACCCTGACCGACGAGCGTCTCGGCGTCCAGGACGCCGGCGACGAGATCGCCGGGGACGACTCCGCCCCCGACGCCCCCGAGGTCGGCTTCCGCACCGACTCCTACTGCTACGAGCACGGCCTGCGCGACTACGTCGCCTTCCTCAACAAGTCCAAGAAGGCCGAGCTCATCCACCCCGAGATCATCGACTTCGAGGCCGAGCAGTCCCTGGGCGAGAACCACTCCATCAGCCTGGAGATCGCCATGCAGTGGACCAGCGCCTACTCGGAGTCGGTCCACACCTACGCCAATACGATCAACACCACCGAGGGCGGCACCCACGAGGAGGGCTTCCGCACGGCCCTGACCACCCTGGTCAACAAGTACGCCCGGGACAAGGGCCTGCTCAAGGAGCGCGACGACAACCTCACCGGTGACGACATCCGTGAGGGGCTGACCGCCGTCATCTCCGTCAAGCTCTCCGAGCCGCAGTTCGAGGGCCAGACCAAGACCAAGCTCGGCAACACCGAGGCGCGCACCTTTGTCCAGCAGACGGTTTACGCCCAGCTCGGCGACTGGCTGGACTCCCACCCCGGTGACGCCCGCGCCATCATCACCAAGGCCTCCCAGGCCGCCGCCGCGCGCCTGGCCGCCCGCAAGGCCCGCGAGGCCACCCGCCGCAAGGGCGTCCTGGAGTCGGCCTCCATGCCCGGCAAGCTGCGCGACTGCTCCTCGAAGAACGCCGCGGACTCCGAGATCTTCATCGTTGAGGGAGACTCCGCCGGTGGCTCCGCCGTCGGCGGCCGCGACCCCGAGCACCAGGCGATCATGCCGATCCGCGGCAAGATCCTCAACGTGGAGAAGGCGCGCCTGGACCGGGCCCTGTCCTCCGACACGATCCGCAGCCTCATCACCGCCTTCGGCACCGGAATCGGCGAGGACTTCGACATCGCCAAGCTGCGCTACGGCAAGATCGTCATCATGGCCGACGCCGACGTCGACGGCCAGCACATCGCCACCCTCCTGCTGACCCTCCTGTTCCGCTACATGCGGCCCCTCATCGAGCACGGCCACACCTACATCGCCATGCCGCCGCTCTACCGGCTCAAGTGGTCCAACGCCGAGCACGAGTTCGCCTACTCCGACGCCGAGCGCGACAAGCTCCTGGCCGCCGGACAGGAGAAGGGCCGCCGCCTCCCCAAGGACGGCGGGATCCAGCGCTACAAGGGTCTGGGCGAGATGAACGACCACGAGCTGTGGGAGACGACCATGGACCCCACCACCCGGATCCTCAAGCAGGTCACGCTCGATGAGGCGGCCGACGCCGACGAGACCTTCGCGATCCTCATGGGCGACGACGTCGAGCAGCGGCGCTCCTTCATCCAGCGCAACGCCTCCGACGTCCGTTTCCTGGACATCTGA","VSDQDATVNHDYGASDITVLEGLEAVRKRPGMYIGSTGERGLHHLVYEVVDNSVDEALAGYCDHIEVTILADGGVRVSDNGRGIPVDEHPTEHKPTVEVVMTILHAGGKFGGGGYAVSGGLHGVGISVVNALSTRVDTEVRRQGFVWRMSFADGGRPITELVKGEATESTGTTQTFYPDPTIFETVDFDYETLRRRFQQMAFLNKGLRITLTDERLGVQDAGDEIAGDDSAPDAPEVGFRTDSYCYEHGLRDYVAFLNKSKKAELIHPEIIDFEAEQSLGENHSISLEIAMQWTSAYSESVHTYANTINTTEGGTHEEGFRTALTTLVNKYARDKGLLKERDDNLTGDDIREGLTAVISVKLSEPQFEGQTKTKLGNTEARTFVQQTVYAQLGDWLDSHPGDARAIITKASQAAAARLAARKAREATRRKGVLESASMPGKLRDCSSKNAADSEIFIVEGDSAGGSAVGGRDPEHQAIMPIRGKILNVEKARLDRALSSDTIRSLITAFGTGIGEDFDIAKLRYGKIVIMADADVDGQHIATLLLTLLFRYMRPLIEHGHTYIAMPPLYRLKWSNAEHEFAYSDAERDKLLAAGQEKGRRLPKDGGIQRYKGLGEMNDHELWETTMDPTTRILKQVTLDEAADADETFAILMGDDVEQRRSFIQRNASDVRFLDI$","DNA gyrase, B subunit","Cytoplasm","DNA gyrase, B subunit","DNA gyrase; B subunit ","DNA gyrase, B subunit","","Bergerat A., de Massy B., Gadelle D., Varoutas P.C., Nicolas A., Forterre P. An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 1997. 386(6623):414-417. PMID: 9121560Versalovic J., Lupski J.R. The Haemophilus influenzae dnaG sequence and conserved bacterial primase motifs. Gene 1993. 136(1):281-286. PMID: 8294018Aravind L., Leipe D.D., Koonin E.V. Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Nucleic Acids Res. 1998. 26(18):4205-4213. PMID: 9722641","","","

InterPro
IPR000565
Family

DNA topoisomerase, type IIA, subunit B
PR01159	$\"[12-22]T$ $\"[187-202]T$ $\"[202-215]T$ $\"[248-270]T$ $\"[277-295]T$ $\"[347-363]T$ $\"[395-409]T$ $\"[409-429]T$ $\"[505-514]T$ $\"[628-640]T$ $\"[644-660]T$	DNAGYRASEB

InterPro
IPR001241
Domain

DNA topoisomerase, type IIA, subunit B or N-terminal
PR00418	$\"[41-56]T$ $\"[76-89]T$ $\"[119-133]T$ $\"[303-316]T$ $\"[455-469]T$ $\"[521-537]T$ $\"[539-556]T$ $\"[559-571]T$ $\"[607-623]T$	TPI2FAMILY
SM00433	$\"[41-668]T$	TOP2c
PS00177	$\"[457-465]T$	TOPOISOMERASE_II

InterPro
IPR002288
Domain

DNA topoisomerase, type IIA, subunit B, C-terminal
PF00986	$\"[600-664]T$	DNA_gyraseB_C

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[9-220]T$	no description
PF02518	$\"[37-181]T$	HATPase_c
SM00387	$\"[37-182]T$	HATPase_c

InterPro
IPR006171
Domain

TOPRIM
PF01751	$\"[483-564]T$	Toprim

InterPro
IPR011557
Family

DNA gyrase, subunit B
TIGR01059	$\"[12-675]T$	gyrB: DNA gyrase, B subunit

InterPro
IPR011558
Domain

DNA topoisomerase, type IIA, subunit B, conserved region
PD149633	$\"[460-581]T$	Q83WB7_STRSH_Q83WB7;

InterPro
IPR013506
Domain

DNA topoisomerase, type IIA, subunit B, region 2
PF00204	$\"[249-426]T$	DNA_gyraseB

InterPro
IPR013759
Domain

DNA topoisomerase, type IIA, subunit B or N-terminal, alpha-beta
G3DSA:3.40.50.670	$\"[419-632]T$	no description

InterPro
IPR014721
Domain

Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10	$\"[278-419]T$	no description

noIPR
unintegrated

unintegrated
PTHR10169	$\"[31-219]T$ $\"[241-674]T$	DNA TOPOISOMERASE/GYRASE
PTHR10169:SF3	$\"[31-219]T$ $\"[241-674]T$	DNA GYRASE SUBUNIT B

InterPro
IPR002205
Domain

DNA topoisomerase, type IIA, subunit A or C-terminal
PD000742	$\"[62-137]T$	Q6AHN0_BBBBB_Q6AHN0;
PF00521	$\"[47-498]T$	DNA_topoisoIV
SM00434	$\"[26-483]T$	TOP4c

InterPro
IPR005743
Family

DNA gyrase, subunit A
TIGR01063	$\"[23-835]T$	gyrA: DNA gyrase, A subunit

InterPro
IPR006691
Repeat

DNA gyrase/topoisomerase IV, subunit A, C-terminal beta-pinwheel
PF03989	$\"[521-570]T$ $\"[571-623]T$ $\"[627-679]T$ $\"[680-731]T$ $\"[735-785]T$ $\"[786-835]T$	DNA_gyraseA_C

InterPro
IPR013757
Domain

DNA topoisomerase, type IIA, subunit A, alpha-helical
G3DSA:1.10.268.10	$\"[388-477]T$	no description

InterPro
IPR013758
Domain

DNA topoisomerase, type IIA, subunit A or C-terminal, alpha-beta
G3DSA:3.90.199.10	$\"[45-314]T$	no description

noIPR
unintegrated

unintegrated
PTHR10169	$\"[47-205]T$	DNA TOPOISOMERASE/GYRASE
PTHR10169:SF2	$\"[47-205]T$	DNA TOPOISOMERASE II

noIPR
unintegrated

unintegrated
signalp	$\"[1-68]?$	signal-peptide
tmhmm	$\"[46-66]?$ $\"[99-119]?$ $\"[125-143]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[29-49]?$ $\"[81-99]?$ $\"[114-134]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[15-33]?$ $\"[43-63]?$ $\"[78-96]?$ $\"[106-126]?$	transmembrane_regions

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[12-66]T$	HTH_3
SM00530	$\"[11-66]T$	HTH_XRE
PS50943	$\"[12-66]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[7-72]T$	no description

","BeTs to 9 clades of COG1476COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1476 is aom-k----d-lb--f-----j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 66 (E_value = 1.2e-16) place ANA_2230 in the HTH_3 family which is described as Helix-turn-helix.","","DNA-binding protein (pXO1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2231","2416679","2417197","519","10.46","9.66","19136","ATGACGAGGCCTCCTAGGATGAGTACCGTGAGCCGCTCCGTTGACATTCCGCCCCCGAGGCGAGGACGTCGCGAGCTCGTCGAGGACACCGGGGTGCGGCTCGGCCTGCACATCAAGTCGGCCGAGCAGGCCATGATGGCCGCCAAGACCGAGGCCCTGAGGCGCTTTGGCCTCACCGTGGCCCAGTACGCGGCCATGCTCTCCCTGTACTACGTGCCCGAGCAGTCCTCGGCCCAGCTGGCCAGGGCCGCCGCGGTCACTCCGCAGACGATGGCCACCGTCATCGCCAAACTGGAGCAGAAACGACTCGTCACCCGTCACCCCTCCTCCGACCACGCCAAGGTCCTCATCGCCTCACTCACGACCGAGGGTGAGGCCCTGCTACTGCGCGCCGACAAGGTTGCACGCCGCATCGAGCAGCGTATGGCCGAGTCCTTCACCGCCAAGGAGCGTCAGCAGCTCACCGAGATGCTCGGGCGCGTCACCTCCCTCCTGCGCGACAACCTCATCGCCGAGTAG","MTRPPRMSTVSRSVDIPPPRRGRRELVEDTGVRLGLHIKSAEQAMMAAKTEALRRFGLTVAQYAAMLSLYYVPEQSSAQLARAAAVTPQTMATVIAKLEQKRLVTRHPSSDHAKVLIASLTTEGEALLLRADKVARRIEQRMAESFTAKERQQLTEMLGRVTSLLRDNLIAE$","Transcriptional regulator, MarR family","Cytoplasm","Hypothetical transcriptional regulatorRv2887/MT2955/Mb2911","MarR-family protein transcriptional regulator","regulatory protein, MarR","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631Lai E., Clark K.L., Burley S.K., Darnell J.E. Hepatocyte nuclear factor 3/fork head or \"winged helix\" proteins: a family of transcription factors of diverse biologic function. Proc. Natl. Acad. Sci. U.S.A. 1993. 90(22):10421-10423. PMID: 8248124Cicero M.P., Hubl S.T., Harrison C.J., Littlefield O., Hardy J.A., Nelson H.C. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res 2001. 29(8):1715-1723. PMID: 11292844Yamada K., Miyata T., Tsuchiya D., Oyama T., Fujiwara Y., Ohnishi T., Iwasaki H., Shinagawa H., Ariyoshi M., Mayanagi K., Morikawa K. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002. 10(3):671-681. PMID: 12408833Liu J., Smith C.L., Deryckere D., Deangelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000. 6(3):637-648. PMID: 11030343Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997. 388(6637):97-100. PMID: 9214510Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M. The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(3):1146-1150. PMID: 8577730","","","

InterPro
IPR000835
Family

Bacterial regulatory protein, MarR
PR00598	$\"[75-91]T$ $\"[92-107]T$ $\"[111-127]T$ $\"[141-161]T$	HTHMARR
PF01047	$\"[58-127]T$	MarR
SM00347	$\"[51-151]T$	HTH_MARR
PS50995	$\"[31-163]T$	HTH_MARR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[58-131]T$	no description

","BeTs to 10 clades of COG1846COG name: Transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1846 is aompkz--vdrlb-efg-sn-j----Number of proteins in this genome belonging to this COG is 6","***** IPB000835 (Bacterial regulatory protein, MarR family) with a combined E-value of 4.6e-06. IPB000835 91-124","","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 127 (E_value = 5e-13) place ANA_2231 in the MarR family which is described as MarR family.","","transcriptional regulator Rv2887-MT2955-Mb2911","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2232","2417334","2418305","972","4.88","-13.56","33248","ATGAAGGCCATGCAGATCGTCAGCTTCGATGGTCCGGCGTCCGGTTTGCGGTACCAGGAGGCTCCGACCCCTGAGCCCGGACCGGGCGAGATCGCCGTGGATGTGGACCATGCCGGCGTCGGCTACGTCGAGGCGCTCTTCACCGAGGGCCTCGTGCCCATCGACCTGCCCTGGACTCCCGGGCTGGAGGTGAGTGGTCGAGTCCGCGCCCTCGGCGACGGGGTGGATGGCTACCGGGTCGGGGACGCCGTCGTCGCCCTGACCATCACCGGAGGTGGCGGCTACGGGCAGGTCGCCGTGGCCCCCGCGGAGCTCGTCGTACCGCTCCCCGCGGGACTCGATCCGATCCTGGCCGCCGCAGTTCCGGCCAACTCGACGACGGCGCTCGTCGCCCTGGAGGAGATCGCCCACCTGCGCCGCGGCGAGAGCGTGCTGGTCCACGCCGCCGCCGGCGGCCTCGGATCGCAGATGGGTCAGGTGGCCCGGCTGCTCGGTGCGGGCCGCGTCGTCGGCGCCACCCGCAGCGAGGCCAAGCGCCAGGAGATCCTGGACCTGGGCTATGACGAGGCCTGGCTGCCCGAGGAGCTCGCGGAGGTCGAACCCGCCCAGTTCGATGTCGTCGCCGACCCGGTGGCCGGCCCGGCCAGGCTGCGCAGCCTCGACCTGCTGCGTACGGGAGGACGGCTCCTCGCGCTGGGGGACGCCTCCCAGGCGGAGGTCCAGCAGGTGAGCACCACGTCGCTGTGGCTGCGGGGCATTGGCGTCATCGGCTTTAACCTCGGGGCCTTCAGCCAGGCGAACCCGGCGCTCGTCGGAGGCCACCTGAGGCGCGCGATGGAGCTTGTGGCCTCCGGAGAGCTCCAGGTCCACGTCATCGACCGCCTCCCGATCCAGGAGGCCGCTCAGGCCGTTACCGCGGTGCGCGCGGGAACCACCACCGGCAAGATCGTTCTGACCCACTCGCAGGACTGA","MKAMQIVSFDGPASGLRYQEAPTPEPGPGEIAVDVDHAGVGYVEALFTEGLVPIDLPWTPGLEVSGRVRALGDGVDGYRVGDAVVALTITGGGGYGQVAVAPAELVVPLPAGLDPILAAAVPANSTTALVALEEIAHLRRGESVLVHAAAGGLGSQMGQVARLLGAGRVVGATRSEAKRQEILDLGYDEAWLPEELAEVEPAQFDVVADPVAGPARLRSLDLLRTGGRLLALGDASQAEVQQVSTTSLWLRGIGVIGFNLGAFSQANPALVGGHLRRAMELVASGELQVHVIDRLPIQEAAQAVTAVRAGTTTGKIVLTHSQD$","Quinone oxidoreductase","Cytoplasm, Extracellular","enoyl reductase","quinone oxidoreductase","Alcohol dehydrogenase, zinc-binding domain protein","","Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Taneja B., Mande S.C. Conserved structural features and sequence patterns in the GroES fold family. Protein Eng. 1999. 12(10):815-818. PMID: 10556240","","","

InterPro
IPR002085
Family

Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695	$\"[16-322]T$	ALCOHOL DEHYDROGENASE RELATED

InterPro
IPR002364
Family

Quinone oxidoreductase/zeta-crystallin
PS01162	$\"[141-162]T$	QOR_ZETA_CRYSTAL

InterPro
IPR013149
Domain

Alcohol dehydrogenase, zinc-binding
PF00107	$\"[140-284]T$	ADH_zinc_N

InterPro
IPR013154
Domain

Alcohol dehydrogenase GroES-like
PF08240	$\"[28-109]T$	ADH_N

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[103-295]T$	no description
PTHR11695:SF31	$\"[16-322]T$	QUINONE OXIDOREDUCTASE, BACTERIA AND PLANT

","BeTs to 9 clades of COG0604COG name: NADPH:quinone reductase and related Zn-dependent oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0604 is -o-p-zyq-drlb-efghs--j----Number of proteins in this genome belonging to this COG is 4","***** IPB002364 (Quinone oxidoreductase/zeta-crystallin) with a combined E-value of 3.5e-29. IPB002364B 56-76 IPB002364C 93-120 IPB002364D 139-162***** IPB011597 (GroES-related) with a combined E-value of 7.1e-21. IPB011597B 57-84 IPB011597C 92-129 IPB011597D 142-186***** IPB002328 (Zinc-containing alcohol dehydrogenase) with a combined E-value of 1.7e-11. IPB002328A 15-46 IPB002328B 57-84","","","-47% similar to PDB:1YB5 Crystal structure of human Zeta-Crystallin with bound NADP (E_value = 4.5E_16);-44% similar to PDB:1IYZ Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH (E_value = 3.0E_12);-44% similar to PDB:1IZ0 Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH (E_value = 3.0E_12);-44% similar to PDB:2CF2 ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE (E_value = 3.0E_12);-45% similar to PDB:2J8Z CRYSTAL STRUCTURE OF HUMAN P53 INDUCIBLE OXIDOREDUCTASE (TP53I3,PIG3) (E_value = 3.9E_12);","Residues 28 to 109 (E_value = 4.8e-07) place ANA_2232 in the ADH_N family which is described as Alcohol dehydrogenase GroES-like domain.Residues 140 to 284 (E_value = 2e-19) place ANA_2232 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase.","","reductase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2233","2418362","2418820","459","4.73","-9.33","16481","ATGGTGCGCATGAGAGAAACGATCGGCTCCTTCGACGTTGTTGGCCTGCCTCTTCGGACGACGAACCGAGAGGCAGCCCGAACCATCCCTCCTCACTGGCAGGCCGCTGCCGACGCCGGGCTCCTCGCACCCGAGAAGCCCGGCGTCGGCCCCGGCATCTATGCGGTCTACACCGACTACGAGACTCCCGGTGACGATGTCGACGGTGTCTACACCCTCGTCATCGGTAGGCGCATCGAGGCCGGAGGTCCGGTTCCCCCTGGCCAGGTGACTGTGACGGTCCCGGCCTCTACTCACGAGATCGTCACGCTGGCTGATGCTCGGCCGGAGAGTGTCTATGACGCGTGGGTGGATGTCTGGGCCCGCGAGGACCTGACCCGTGACTATCGGGCCGACTACGAGTACTACGCTCCGGACGGCTCGACCCACCTGTCCATCGGGGTCCTTCCGAACACATGA","MVRMRETIGSFDVVGLPLRTTNREAARTIPPHWQAAADAGLLAPEKPGVGPGIYAVYTDYETPGDDVDGVYTLVIGRRIEAGGPVPPGQVTVTVPASTHEIVTLADARPESVYDAWVDVWAREDLTRDYRADYEYYAPDGSTHLSIGVLPNT$","Transcriptional regulator","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","transcription activator, effector binding","","Kwon H.J., Bennik M.H., Demple B., Ellenberger T. Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA. Nat. Struct. Biol. 2000. 7(5):424-430. PMID: 10802742","","","

InterPro
IPR010499
Domain

Bacterial transcription activator, effector binding
PF06445	$\"[4-149]T$	AraC_E_bind

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 149 (E_value = 2.7e-05) place ANA_2233 in the AraC_E_bind family which is described as Bacterial transcription activator, effector binding domain.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2234","2418817","2419665","849","7.12","0.59","31428","ATGAGGGCCGAGCAGTACCTGCACCACCTCGACGTTGTCACCGACTACATCTACGCGCATCTTGATGAGGACCTCAGCCTGGAGACTCTCGCTCACGTCTCCGGGTTCTCCCGCTATCACTGGCACCGCATCTACCGGGCGGTGCGCGGGGAGACGGCCGCTCAGACCGTACGTCGTCTCCGCCTGGAGCGAGCGGCCGCCATGCTCACAGAGACCTCGTGGCCGGTGGAACGGATCGCCTGGAAAGCCGGGTTCACCGGCACCGAAGTGTTCAGTCGGGCCTTTCTCCGCTCCTATGGGACGACTCCCAGCCGATTCCGCATCGGTGGACGCCCGGTGTCGATCAATTCACCGGCGATGAGCTGCGGTTCGGGATCGACGTCGTCGGTGAGTCAGGACCCGGGGTGGGCGGTGCGCGTGGAGACTCGCCGCGGCTATCGACTTGCCGTATCCGAGCACCGTGGTTCCTACCTGGATATCGGCTGGGCCTTCAGCCGAGTCAGAGACCGTGTGGGCTCCGGGAGTCTGATGGTTGCCATCTATGAGGACGATCCCGACGCCGTTCCCCCGGCTGATCTGCGCTCGGCGGCTGGAACCGTCGTCGACCCCGGTATGAAGATTCCCCACGGCCTTGCTGAGAGGATGGTGCCGGCTGGCCGATACGCGATCATGCGTCACATCGGCCCGTACTCGTCGATGCATGCCGCCTACCTGTGGCTCTACGGTCAGTGGCTGCCGAGCTCGGGCGAGGAGCCGCGAGACCATCCGGTCATCGAGGAGTACCTCACCGACCCGGCGACCACCCCGCCCGTCGACGCTGTCACCGACATCCTTCTCCCGCTCCTGTGA","MRAEQYLHHLDVVTDYIYAHLDEDLSLETLAHVSGFSRYHWHRIYRAVRGETAAQTVRRLRLERAAAMLTETSWPVERIAWKAGFTGTEVFSRAFLRSYGTTPSRFRIGGRPVSINSPAMSCGSGSTSSVSQDPGWAVRVETRRGYRLAVSEHRGSYLDIGWAFSRVRDRVGSGSLMVAIYEDDPDAVPPADLRSAAGTVVDPGMKIPHGLAERMVPAGRYAIMRHIGPYSSMHAAYLWLYGQWLPSSGEEPRDHPVIEEYLTDPATTPPVDAVTDILLPLL$","Transcriptional regulator, AraC family","Cytoplasm","AraC-family transcriptional regulator","K07506 AraC family transcriptional regulator","transcription activator, effector binding","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR000005
Domain

Helix-turn-helix, AraC type
PR00032	$\"[76-91]T$ $\"[91-107]T$	HTHARAC
PF00165	$\"[64-108]T$	HTH_AraC
SM00342	$\"[24-107]T$	HTH_ARAC
PS01124	$\"[11-109]T$	HTH_ARAC_FAMILY_2
PS00041	$\"[61-103]T$	HTH_ARAC_FAMILY_1

InterPro
IPR010499
Domain

Bacterial transcription activator, effector binding
PF06445	$\"[136-282]T$	AraC_E_bind

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[2-61]T$ $\"[62-107]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.20.80.10	$\"[136-281]T$	no description
PTHR11019	$\"[10-109]T$	THIJ/PFPI
PTHR11019:SF11	$\"[10-109]T$	ARAC FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN

","BeTs to 6 clades of COG2207COG name: AraC-type DNA-binding domain-containing proteinsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2207 is --------v-rlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000005 (Helix-turn-helix, AraC type) with a combined E-value of 1.1e-08. IPB000005 76-107","","","No significant hits to the PDB database (E-value < E-10).","Residues 64 to 108 (E_value = 8.7e-07) place ANA_2234 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, AraC family.Residues 136 to 282 (E_value = 2.6e-29) place ANA_2234 in the AraC_E_bind family which is described as Bacterial transcription activator, effector binding domain.","","transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2235","2422601","2419755","2847","7.02","0.10","99654","ATGCTTCGCCGATTCTTTGTCCGCTCACACCGGCGGGAACTGACGTCATCACGTCAACCCTCACGCCAGTCTCGTCGGAGACTGAGGAGCGGCGCCGCCATCTCGACATTTGCCCTGATTGCCGGCGCACTGGGCACAGCGACGCTCCCGGCTCCCCCGGCTGAGGCCGTTCACGGCAATCCTGCCGGAGGATCGGGAAAATACACCCAGGTGATCGACTGGATCGACTGGACCGAGATGACTAATACCTTACCCGGGAAAGGCACGAGAATCCTTCCCGACGGAAGCACCGGCGTGGTCTGGTCGACTCCCTCACGGATCTCCGGCGATAAGTGGCGAACCAGTCGATGCACCCTATCCAATGTGCGCACCACTGCCGTGGGAAAGAATGAGACGGGGCTGCCCACGGACCGGGGCCTGAGTGTCGGATACTATCCGGGTAACTGGAGGGGAGACGGCCTGGCTCGCCTTTACAACGACGGCACCAACTACACCGCCGGGGTTGCCAAGAAGCCCTATGCGACCTCATCGAACCTGCCTCTGGGCATTGCCAACCTGAGGGACTCCTCTACACAGCAGTTCCAGATCGAGTGCAGCGCCTACCTGGTGACCTCCGCCTCCCAGCCTGCGAAGAGCCAGCTGGAGCACTTCCCCAACAAGGTGGAGGTTCCGATGGAGGGTATCGTCTTCGCCGATGCTGAGGCCTCGAGCTGGCACATCCCGAACGGCCAGAAGGAGTACATCTCCGTTTCCCCGATCCCCTACGTCGCCTCCCAGAACGTCACCTACCGCCTGTTGGAGAGCGCCCGGCCACCGGGATGCATCACGAACTCCGTCGTGGGCAAGGTCTCCGTCTCCACCCCTGTTGGTAACCGGCCCGGCGTCAAGCTGCGCCCGGACGACGCCGAGTGCAGCGCCAAGGTTCCCAACGGCTACGGCCCCTCCTCGGTCATGCTGCTGAGCAACATGCGCACCGGCTACGTCGAGATCCACGGAGGCGGTCGAGGCGCCGTCGCCTTCGGTGTCGTCTCCTACATGGACTACGGCGACGCGCCTGAGAGCTACGGTGTTGCCGGCAGCGCGTTCCAGCCGGCCTGGAGCGGTGGGGAGCTGTCTGACAGCGGAGAGCGCAACATCGCCCGCGGCAAGGCACCGTATGAGGGCGACGCCGGAGACTGGTACAACCTGAGTGCGGCAACGGACCAGGGCAACGTGGCCACCACGAACTCCGCCGTCGTGCGTCTGGGTGCCCTGACGGACCACGATGACACCATCACCCACAGCGCTGACGCCTCGAGGGACAACACCACGGATATTGATGACGAGGACGCCCTGCCCGCCGGCTGGGACCGCGTCATCTGGACCGATATCGGCCAGAAGTGGAGCCAGGAGATCACCTGCTCGGGCAGCAACACCAAGATTGCCGGCTGGGTGGACTGGAACCGGGACGGCACCTTCTCCGCCGGTGAGCGCTCCGCGGTGACCTCCTGCTCCAGCGCCGGTAAGGCCACTGTGACCTGGACCGTCCCCCAGGACGCCAAGCGGAGCACCATCAATGGCAACGGTGCGGCCACCTTCATGCGTCTGCGCATCACCGGCGCCCCGCCCAACGGACGGGAAGCCGAGGACCCTCAGCCCACTGGCATCGCTGTCAACGGTGAGGTCGAGGACCACCAGGTACAGGTCCAGCTGCCCAACCTGTCCCTGGCCAAGCAGGTGGACAACACCGCGGCCGGGTCTCTGGGTCTGTCCGCCAAGGACTGGACGCTCACGGCAACTCCCAAGCGCGGTAAGACCGCCTCAGGCGCCGGCGGCTTCGACTCCGCTTACCTGCCCCAGGGCCAGACGGTGCTGTCGGAGTCCTCATCGTCTCCCAAGTCGGCCGGGTACAAGGCCTCCGTCTCCTGCGTGCCGCACCCGAACTCGGATATCAGGACTCCGTCGTCGACGGTCAACTCCGCCTCCAAGACCCTGGATCTGGCCACCGGTGAGTGGATGCAGTGCACGATGGTCAACACGGCTCAGCCCGGTCAGGTCGTCTGGAGCAAGGTCGACGACGCCGGCAACCCGCTGGCGGGGACCGTGTTCACGCTGGCCTCCCCGGCGCTCAACGGCGGTCAGAAGGAAGTGACCGACTGCGTCGTCACCGGTGGGAAGGCCACGTGCCCCAATGGCTCGGTGGACCAAGACCCTCGTGCCGGGTTCTTCAGGGTCTCCGGGCTCACCTGGGGCAACTACTCCATCACTGAGACCCAGGCGCCGGCCGGCTACCACCTGTCCTCCACCACCCTGACCAAGACCCTGGACGGATCGGCGCCGGCCGCGGGCACCGACGACGACACTCCCACCCTCGACCTGGGTCAGGTCACCAACACCCGGATCAAGGGGTCGGCCACCTGGACCAAGACCGATGAGCGGGGCAACCCCATCAAGGGTGCCCAGTGGTCGCTGGTTCCCCTCGACTCCAACGGTCGGCCCCAGCCGGACCAGGCCCGCACCATCACCGACTGCGTGGGCACCTGCGCCCAGGGCAGCCTGGACACCGATGGGAACCCCGGCGCCTTCAAGCTGGCGGAGCTGGGCTACGGCTCCTACGGGCTCATGGAGACCAAGCCACCGACCGGCTACATCCTGGACGCCACCCCCCGCACCATCACCATCTCCTCCCAGGGGCAGGTCGTGGCGCTGGGCAAGATCTCCAACCGCAAGTCGGCGGTGCCCGCCATCCCCTTCACCGGAGGGAGCGCGGCCGACACCTTCCTCATCGCCGGTGGGGCGGTGCTGGGGATCACGGCCCCGGTCATGATGATCCAGGCCTACCGACGCCGGCGGGCCCTGGACTCATGA","MLRRFFVRSHRRELTSSRQPSRQSRRRLRSGAAISTFALIAGALGTATLPAPPAEAVHGNPAGGSGKYTQVIDWIDWTEMTNTLPGKGTRILPDGSTGVVWSTPSRISGDKWRTSRCTLSNVRTTAVGKNETGLPTDRGLSVGYYPGNWRGDGLARLYNDGTNYTAGVAKKPYATSSNLPLGIANLRDSSTQQFQIECSAYLVTSASQPAKSQLEHFPNKVEVPMEGIVFADAEASSWHIPNGQKEYISVSPIPYVASQNVTYRLLESARPPGCITNSVVGKVSVSTPVGNRPGVKLRPDDAECSAKVPNGYGPSSVMLLSNMRTGYVEIHGGGRGAVAFGVVSYMDYGDAPESYGVAGSAFQPAWSGGELSDSGERNIARGKAPYEGDAGDWYNLSAATDQGNVATTNSAVVRLGALTDHDDTITHSADASRDNTTDIDDEDALPAGWDRVIWTDIGQKWSQEITCSGSNTKIAGWVDWNRDGTFSAGERSAVTSCSSAGKATVTWTVPQDAKRSTINGNGAATFMRLRITGAPPNGREAEDPQPTGIAVNGEVEDHQVQVQLPNLSLAKQVDNTAAGSLGLSAKDWTLTATPKRGKTASGAGGFDSAYLPQGQTVLSESSSSPKSAGYKASVSCVPHPNSDIRTPSSTVNSASKTLDLATGEWMQCTMVNTAQPGQVVWSKVDDAGNPLAGTVFTLASPALNGGQKEVTDCVVTGGKATCPNGSVDQDPRAGFFRVSGLTWGNYSITETQAPAGYHLSSTTLTKTLDGSAPAAGTDDDTPTLDLGQVTNTRIKGSATWTKTDERGNPIKGAQWSLVPLDSNGRPQPDQARTITDCVGTCAQGSLDTDGNPGAFKLAELGYGSYGLMETKPPTGYILDATPRTITISSQGQVVALGKISNRKSAVPAIPFTGGSAADTFLIAGGAVLGITAPVMMIQAYRRRRALDS$","Cna B domain protein","Extracellular, Periplasm, Cellwall","Cna protein B-type domain family","probable surface-anchored fimbrial subunit","Cna B domain protein","","Deivanayagam C.C., Rich R.L., Carson M., Owens R.T., Danthuluri S., Bice T., Hook M., Narayana S.V. Novel fold and assembly of the repetitive B region of the Staphylococcus aureus collagen-binding surface protein. Structure 2000. 8(1):67-78. PMID: 10673425","","","

InterPro
IPR008454
Domain

Cna B-type
PF05738	$\"[734-767]T$ $\"[853-894]T$	Cna_B

noIPR
unintegrated

unintegrated
tmhmm	$\"[31-51]?$ $\"[920-940]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 691 to 781 (E_value = 0.034) place ANA_2235 in the Cna_B family which is described as Cna protein B-type domain.Residues 810 to 894 (E_value = 0.0067) place ANA_2235 in the Cna_B family which is described as Cna protein B-type domain.","","protein B-type domain family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2237","2423032","2423730","699","5.87","-3.17","24857","GTGCGCACAGCGGGACAGGGGCCACGCTGGAGCCGCGTCCTCAACTCCGCCGGCGGCGTCGGCACGGCCTGGACCATGGATGTGCGCAGCCGCCCGGCCCTCAACGACGGGCCGCTCGAGGGACGGCCACTGCGCGACGTCGGCGCCCTGGCGAAGTCCTGGAACCTGGCTGAGGCCAGCATCGGCCAGGCCGCCATCAACTCCTGGTACTCGCGCGAGCAGACGGCTGCGGCCAACGGATTCGAACCCACCGGGGAGGGACTGACCTGGCGCCAGGTCTTCGACCCCTACCGGGAGATGATCGTCGGCAAGAGAGTCGCAGTCATCGGGCACTTCCCCTTCGCCGAGGCCGCCCTGGCCGGCGCCGGCGAGTACATCTGCCTCGAGCGCAACCTTCAGCCCGGCGACTGGCCGGACAGCGCCTGCGAGTACGTCCTGCCCGAGTGCGACCTCGTCTTCATCTCCTCATCGAGCTTCGTCAACAAGACCGCGCCGCGTCTCATCGAGCTCTCCCGCCAGGCGCACACCGTCCTGGTGGGGCCATCGACGCCACTCAACCCGGTGCTCCTCGACTACGGCGTGGACACCATCACCGGTTTCATCGCGGCGAGTTCACTGAGCGACCCCGCCTCCCTGGCTGAGATGATTCCGGCCGGCGACATCGGCCCCGGATTCCGGGTCCACCGTCATCGGGCCTGA","VRTAGQGPRWSRVLNSAGGVGTAWTMDVRSRPALNDGPLEGRPLRDVGALAKSWNLAEASIGQAAINSWYSREQTAAANGFEPTGEGLTWRQVFDPYREMIVGKRVAVIGHFPFAEAALAGAGEYICLERNLQPGDWPDSACEYVLPECDLVFISSSSFVNKTAPRLIELSRQAHTVLVGPSTPLNPVLLDYGVDTITGFIAASSLSDPASLAEMIPAGDIGPGFRVHRHRA$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","K09138 hypothetical protein","conserved hypothetical protein","","","","","

InterPro
IPR007161
Family

Protein of unknown function DUF364
PF04016	$\"[104-199]T$	DUF364

","BeTs to 3 clades of COG2014COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2014 is --m-k---------------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-59% similar to PDB:2H1Q Crystal structure of hypothetical protein (ZP_00559375.1) from Desulfitobacterium halfniense DCB-2 at 2.01 A resolution (E_value = 6.6E_34);-42% similar to PDB:1Y4I Crystal structure of Citrobacter Freundii L-methionine-lyase (E_value = 6.6E_34);-38% similar to PDB:1TQY The Actinorhodin Ketosynthase/Chain Length Factor (E_value = 6.6E_34);-56% similar to PDB:1TQJ Crystal structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 angstrom resolution (E_value = 6.6E_34);","Residues 104 to 199 (E_value = 7.2e-09) place ANA_2237 in the DUF364 family which is described as Domain of unknown function (DUF364).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2238","2424412","2423867","546","8.26","2.82","19231","ATGTCCTGCCTGACGAAGACATGCTGCGACAAGAAGCTCGACACCACTCATCTGCGCAAGGAGGCAGCATCCCTTGCCGGATCCGTCGTCGGCCAGGCTGAGAAGGCCGCCCTGTGGGCTGCTCCGCACGTGAGCAAGGCCGCCGGGGGCGTGGCCCGCGCCGCCAAGGACGCACAGGAGCGTCTGGAGCCCGTGGTCCACGAGGCCCGCTACCGGGTTGTCGAGGACTACATCCCGCGTGCGCAGCGCGCCGCCGTGGCTGCCCAGGCTGCTGCAGGTACGGACGGTACCCTGACAGAGCGCGCCCAGCGCGTGGCTGTTGCCGCAAAGTCCGCCGCATTGGAGGTTCCCGTGAAGAAGCAGAAGAAGCACCGCGTGCTCAAGACCCTGGGTTGGCTCGCCGTCGCCGGCGCGGCCGCTGCCGGCGCCTACGTCGTGTGGCGTCGTAGCCAGCCCGTTGAGGACCCGTGGGCCGAGGAGTACTGGGCCGACTCCACCGAGGATGAGGCCGGCTACGGCATCAGCCCCGAGGACGCTCAGGCCTGA","MSCLTKTCCDKKLDTTHLRKEAASLAGSVVGQAEKAALWAAPHVSKAAGGVARAAKDAQERLEPVVHEARYRVVEDYIPRAQRAAVAAQAAAGTDGTLTERAQRVAVAAKSAALEVPVKKQKKHRVLKTLGWLAVAGAAAAGAYVVWRRSQPVEDPWAEEYWADSTEDEAGYGISPEDAQA$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[129-147]?$	transmembrane_regions

InterPro
IPR002130
Domain

Peptidyl-prolyl cis-trans isomerase, cyclophilin-type
PR00153	$\"[16-31]T$ $\"[57-69]T$ $\"[101-116]T$ $\"[116-128]T$ $\"[129-144]T$	CSAPPISMRASE
G3DSA:2.40.100.10	$\"[3-172]T$	no description
PF00160	$\"[2-172]T$	Pro_isomerase
PS50072	$\"[6-171]T$	CSA_PPIASE_2
PS00170	$\"[52-69]T$	CSA_PPIASE_1

noIPR
unintegrated

unintegrated
PTHR11071	$\"[1-171]T$	CYCLOPHILIN
PTHR11071:SF35	$\"[1-171]T$	PEPTIDYL-PROLYL CIS-TRANS ISOMERASE (CYCLOPHILIN)

","BeTs to 16 clades of COG0652COG name: Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin familyFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0652 is -om---y--drlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB002130 (Peptidyl-prolyl cis-trans isomerase, cyclophilin type) with a combined E-value of 4.5e-46. IPB002130A 10-34 IPB002130B 52-91 IPB002130C 101-140","","","-58% similar to PDB:1W74 X-RAY STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, PPIA, RV0009, FROM MYCOBACTERIUM TUBERCULOSIS. (E_value = 9.3E_39);-51% similar to PDB:2A2N Crystal Structure of the peptidylprolyl isomerase domain of Human PPWD1 (E_value = 7.7E_25);-52% similar to PDB:1XWN solution structure of cyclophilin like 1(PPIL1) and insights into its interaction with SKIP (E_value = 1.4E_23);-52% similar to PDB:2FU0 Plasmodium falciparum cyclophilin PFE0505w putative cyclosporin-binding domain (E_value = 9.4E_23);-52% similar to PDB:1CYN CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN (E_value = 1.8E_21);","Residues 2 to 172 (E_value = 2.6e-57) place ANA_2239 in the Pro_isomerase family which is described as Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD.","","cis-trans isomerase B (PPIase B)(Rotamase B) (Cyclophilin ScCypB) (S-cyclophilin) (rotamase)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2242","2425299","2426153","855","9.08","9.85","30549","ATGAGCTCGACGAACTCGTTTCCGCAGCAGGCACCGCCGGTGTGCCCGCGGCACCCGGACACGGTGGCCTACGTGCGCTGCCAGCGCTGCGACCGACCCACCTGTCCCGCCTGCCAGGTGCCCAGCTCGGTGGGGGTCCACTGTGTGGACTGTGCTCGTCAGTCTCAGGCCGGCCGACGTCAGGCGCGCACGCTGCTGGGCGGGAACGTCACCTCCGGGGCCCTGGTCACCAAGATCCTCGTCGGCCTGTGCGTCGTCGTCTACGCGCTTCAGGTCCTCATCCCCGAGGTGACGATGCAGTCGCTGGAGCTCCGCCTGGGCTTCGTCCCGGCACTGGCCGTCTACGAGCCCTGGCGGTTCCTGACCACCGCCTTCCTGCATGCGAACTACATGCACCTCGGCTTCAACATGTGGGCTCTGTGGGTGCTGGGCACTGCTCTTGAGCCGGTGCTCGGGCGGTGGCGCTTCACCTGCGTCTACCTGCTCAGTGCTCTGGGCGGCTCGACGATGATCTACTGGCTCTCCTGGCCGGACACAGAGTCCTGGCTCACGCTGACAGTGGGCGCTTCGGGAGCGGTCTTCGGCCTGTTCTCGGCCATGTTCATCGTGCAACGGCGCTTTGGGCGAGACACCTCGGGAATCGTGGCGCTGGTGGCGGTCAATGCCGTCATCTCCTTCCTGGGGGCCAATATCTCCTGGCAGGGGCACCTCGGTGGGCTTGTCGTCGGCGGGATCGTCTCGGCGATCTACGCCTGGGCGCCACGGGGGAAGCGACAGGTCGTGGGGATCGCTGGAACCGTTGCGGTCGCGGTGGCCCTGGTGGGGCTCGATCTGCTTCGGGCCCTTCTCACCTGA","MSSTNSFPQQAPPVCPRHPDTVAYVRCQRCDRPTCPACQVPSSVGVHCVDCARQSQAGRRQARTLLGGNVTSGALVTKILVGLCVVVYALQVLIPEVTMQSLELRLGFVPALAVYEPWRFLTTAFLHANYMHLGFNMWALWVLGTALEPVLGRWRFTCVYLLSALGGSTMIYWLSWPDTESWLTLTVGASGAVFGLFSAMFIVQRRFGRDTSGIVALVAVNAVISFLGANISWQGHLGGLVVGGIVSAIYAWAPRGKRQVVGIAGTVAVAVALVGLDLLRALLT$","Rhomboid family protein","Membrane, Cytoplasm","Rhomboid family protein","rhomboid family protein","Rhomboid family protein","","Bier E., Jan L.Y., Jan Y.N. rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster. Genes Dev. 1990. 4(2):190-203. PMID: 2110920Urban S., Lee J.R., Freeman M. Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 2001. 107(2):173-182. PMID: 11672525","","","

InterPro
IPR002610
Family

Peptidase S54, rhomboid
PTHR22936	$\"[99-255]T$	RHOMBOID-RELATED
PF01694	$\"[111-255]T$	Rhomboid

noIPR
unintegrated

unintegrated
tmhmm	$\"[70-90]?$ $\"[124-144]?$ $\"[159-177]?$ $\"[183-203]?$ $\"[212-230]?$ $\"[236-254]?$ $\"[259-279]?$	transmembrane_regions

","BeTs to 17 clades of COG0705COG name: Uncharacterized membrane protein (homolog of Drosophila rhomboid)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0705 is aompkzyqvdrlbcefghs-uj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB002610 (Rhomboid-like protein) with a combined E-value of 8.4e-36. IPB002610A 118-162 IPB002610B 187-199 IPB002610C 235-244","","","No significant hits to the PDB database (E-value < E-10).","Residues 111 to 255 (E_value = 2.7e-36) place ANA_2242 in the Rhomboid family which is described as Rhomboid family.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2243","2426640","2426212","429","10.62","8.28","14755","ATGATTTCCGCTGGGTGCTTCGACGGCAGGCTCGTCAATGTCAGCGCTGTGGACACCGGGCCGCGCAGGAGTGAGTCCGGGGTTCTTGCGGCAGAGCCCGGCGCCTCCGTCACAGGTCCGCCCCCACCGACTCCTGCCCACCATCTGCGCAGGGTCCCGGTGGTCATGGTTCGACGCCGGCCCCGCTCTCGAGTCTTACCTCGAGTTGGTCTGATCCACGAGGGTCGGGATCCACTGACCAAGGGTTGTGCGTACTGCACGAAGGCCCCACCTACCCTCAGTACCCCCGACCCTCGACCAGTAACACCCACCCCTCGTGCAGTGCACCCAGCCGACGCCGGAAGCCACCACAGTGACCGGGCCAGCCCCCTCCAGCAGGCCGAAGCAGCAGCTCCCCCAGCTGGCAGCCCCACCCCACCGATGTCTTGA","MISAGCFDGRLVNVSAVDTGPRRSESGVLAAEPGASVTGPPPPTPAHHLRRVPVVMVRRRPRSRVLPRVGLIHEGRDPLTKGCAYCTKAPPTLSTPDPRPVTPTPRAVHPADAGSHHSDRASPLQQAEAAAPPAGSPTPPMS$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2244","2427832","2427320","513","9.87","15.64","18823","GTGGCCTTGGAGAAGAAGTCCACAGCGGACGACGCCGACAAGAGCTCGGAGAAGGTCTCGAAGAAGAGCTCTGAGAAGAACAGCGCGAAGAGCGCTGAGAAGGACAAGGGCTCGACGAAGGACTCTGCTGCCTCTGAGAAGACAGAGAAGAAGAGCAAGGCGGACAAGGGTTCGAAGAAGAACTCGTCGAAGAAGAAGCACCCTGAGCGCTCCGGCAACCCGGCCAAGGCCGCCAAGGCCCTCGAGGAGGAGTCGCGCGCCGCAGCGAACCGGGTCTCACGCACCCCCAAGAAGATCAAGGACACCGCCTCACCGCGCTGGTACGCCCCCACCATGGTGACGCTCCTGGTCATCGGGCTGCTGTGGGTTGTCACCACCTACCTCTTCCAGGGCAAGTACCCGCTGCCCTACTTCGTCGAGCACCATGTCGGCGACTGGCTGTTCAACGGCAACCTCTACATCGGCTTCCTCATCATGATGTCAGGCTTCCTCGGCCTGCTGCGCTGGAAGTGA","VALEKKSTADDADKSSEKVSKKSSEKNSAKSAEKDKGSTKDSAASEKTEKKSKADKGSKKNSSKKKHPERSGNPAKAAKALEEESRAAANRVSRTPKKIKDTASPRWYAPTMVTLLVIGLLWVVTTYLFQGKYPLPYFVEHHVGDWLFNGNLYIGFLIMMSGFLGLLRWK$","Membrane protein","Periplasm, Membrane","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

InterPro
IPR009619
Family

Protein of unknown function UPF0233
PF06781	$\"[77-170]T$	UPF0233

noIPR
unintegrated

unintegrated
tmhmm	$\"[108-128]?$ $\"[147-167]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB009619 (Protein of unknown function UPF0233) with a combined E-value of 6.4e-14. IPB009619B 107-128 IPB009619C 147-170","","","No significant hits to the PDB database (E-value < E-10).","Residues 77 to 170 (E_value = 6e-10) place ANA_2244 in the UPF0233 family which is described as Uncharacterised protein family (UPF0233).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2245","2428028","2428801","774","6.64","-1.42","28207","ATGACTAGAGGAGGTCTTGTGCGACACCGAGCACCCGGCCAGAGTCGTGCTGTCCGAATCTTCAACGGCACCTTGACCGGAATCGGTGAGCTGCTGATCACCGCCGGCCTCGTCGTCGCCCTCTTCCTGTGCTGGCAGCTGTGGTGGACCGGCATTGACGCCAACGCCAGCGCGCAGGCGGTGGCCACGCAGTTCCACGAGAAGCAGGTCCAGTCGCCTCAGAAGGCGGGTACGAAGCGCACTGACGCTCCGCCCGTCATGGAGCAGGTTGGCTACGGGGAGACCATCGGGATGCTCGTCGTCCCCAAGTGGTACGGCGTCACCAACAACAACATGCCCATCATGGAGGGCACCGGCTCCGACGTTCTGGACCAGGCCGCAGCGGGCCACTACACCAACACCCAGCAGCTCGGTGAGGTCGGTAACTTCGCGATCGCCGGGCACCGCCGTACCTACGGCAACTCCTTCCGCCGCATTGACCTGCTCCAGGAGGGCGACGAGATTATCGTCTCCACCGCCAAGACCTGGTACGTGTTCAAGGTGACTGGTCACGAGCTCGTCAAGCCCGAGCAGGTCGAGGTCATCGCCCCGGTCCCCAACCAGCCGGACGCCCAGCCCACGGACCGGTACATCACGCTGACCACCTGTCACGGATCGACCGCCGGTGAGTTCGGTAATGACCTGCGCTGGATCGTCCACGCGAAGTTCGCCTACTGGATGGATCGCTCCGAGGGCCGTCCGGAGTCCGTGCTCAACGACCCGGGGGTCAACTGA","MTRGGLVRHRAPGQSRAVRIFNGTLTGIGELLITAGLVVALFLCWQLWWTGIDANASAQAVATQFHEKQVQSPQKAGTKRTDAPPVMEQVGYGETIGMLVVPKWYGVTNNNMPIMEGTGSDVLDQAAAGHYTNTQQLGEVGNFAIAGHRRTYGNSFRRIDLLQEGDEIIVSTAKTWYVFKVTGHELVKPEQVEVIAPVPNQPDAQPTDRYITLTTCHGSTAGEFGNDLRWIVHAKFAYWMDRSEGRPESVLNDPGVN$","Sortase","Cytoplasm, Periplasm","hypothetical transmembrane protein with unknownfunction","K07284 sortase A","sortase family protein","","Barrett A.J., Rawlings N.D. Evolutionary lines of cysteine peptidases. Biol. Chem. 2001. 382(5):727-733. PMID: 11517925Mazmanian S.K., Liu G., Ton-That H., Schneewind O. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 1999. 285(5428):760-763. PMID: 10427003Mazmanian S.K., Ton-that H., Schneewind O. Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus. Mol. Microbiol. 2001. 40(5):1049-1057. PMID: 11401711Pallen M.J., Chaudhuri R.R., Henderson I.R. Genomic analysis of secretion systems. Curr Opin Microbiol 2003. 6(5):519-527. PMID: 14572546","","","

InterPro
IPR005754
Family

Peptidase C60, sortase A and B
PF04203	$\"[99-237]T$	Sortase
TIGR01076	$\"[97-245]T$	sortase_fam: sortase family protein

noIPR
unintegrated

unintegrated
G3DSA:2.40.260.10	$\"[94-223]T$	no description
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[31-49]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide

InterPro
IPR001264
Domain

Glycosyl transferase, family 51
PD001895	$\"[299-342]T$	Q82ID3_STRAW_Q82ID3;
PF00912	$\"[207-374]T$	Transgly

InterPro
IPR001460
Domain

Penicillin-binding protein, transpeptidase
PF00905	$\"[481-760]T$	Transpeptidase

noIPR
unintegrated

unintegrated
G3DSA:3.40.710.10	$\"[455-786]T$	no description
tmhmm	$\"[170-190]?$	transmembrane_regions

","BeTs to 16 clades of COG0744COG name: Membrane carboxypeptidase (penicillin-binding protein)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0744 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB001264 (Glycosyl transferase, family 51) with a combined E-value of 1.3e-71. IPB001264A 229-281 IPB001264B 302-345 IPB001264C 354-388 IPB001264D 507-530 IPB001264E 715-743***** IPB001285 (Synaptophysin/synaptoporin) with a combined E-value of 4.6e-09. IPB001285F 880-923 IPB001285F 862-906 IPB001285F 875-919 IPB001285F 866-910 IPB001285F 879-923 IPB001285F 874-918 IPB001285F 861-905 IPB001285F 870-914 IPB001285F 876-920 IPB001285F 867-911 IPB001285F 871-915 IPB001285F 857-901 IPB001285F 858-902***** IPB000817 (Prion protein) with a combined E-value of 2.5e-08. IPB000817A 875-916 IPB000817A 868-909 IPB000817A 857-898 IPB000817A 871-912 IPB000817A 872-913 IPB000817A 877-918 IPB000817A 866-907 IPB000817A 876-917 IPB000817A 865-906 IPB000817A 863-904 IPB000817A 873-914 IPB000817A 858-899 IPB000817A 859-900 IPB000817A 861-902 IPB000817A 870-911 IPB000817A 879-920 IPB000817A 874-915 IPB000817A 884-923 IPB000817A 856-897 IPB000817A 864-905 IPB000817A 862-903 IPB000817A 867-908 IPB000817A 881-922 IPB000817A 860-901 IPB000817A 855-896 IPB000817A 869-910 IPB000817A 853-894 IPB000817A 880-921 IPB000817A 850-891 IPB000817A 878-919 IPB000817A 854-895 IPB000817A 883-923 IPB000817A 847-888 IPB000817A 882-923***** IPB008021 (Phage Coat A) with a combined E-value of 3e-07. IPB008021E 868-903 IPB008021E 886-921 IPB008021E 881-916 IPB008021E 877-912 IPB008021E 863-898 IPB008021E 872-907 IPB008021E 880-915 IPB008021E 873-908 IPB008021E 862-897 IPB008021E 876-911 IPB008021E 871-906 IPB008021E 870-905 IPB008021E 864-899 IPB008021E 865-900 IPB008021E 867-902 IPB008021E 882-917 IPB008021E 858-893 IPB008021E 890-923 IPB008021E 854-889 IPB008021E 869-904 IPB008021E 875-910 IPB008021E 883-918 IPB008021E 887-922 IPB008021E 885-920 IPB008021E 878-913 IPB008021E 859-894 IPB008021E 850-885 IPB008021E 884-919 IPB008021E 860-895 IPB008021E 874-909 IPB008021E 866-901 IPB008021E 857-892 IPB008021E 853-888 IPB008021E 856-891 IPB008021E 844-879 IPB008021E 879-914","","","-47% similar to PDB:2OLU Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme (E_value = 3.4E_44);-47% similar to PDB:2OLV Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex (E_value = 3.4E_44);-66% similar to PDB:2OQO Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis (E_value = 7.7E_36);-40% similar to PDB:2BG1 ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA PENICILLIN-BINDING PROTEINS (PBPS) (E_value = 6.6E_11);-40% similar to PDB:2FFF Open Form of a Class A Transpeptidase Domain (E_value = 6.6E_11);","Residues 207 to 374 (E_value = 9.2e-83) place ANA_2248 in the Transgly family which is described as Transglycosylase.Residues 481 to 760 (E_value = 4.4e-14) place ANA_2248 in the Transpeptidase family which is described as Penicillin binding protein transpeptidase domain.","","protein 1 (PBP1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2249","2435867","2436154","288","5.53","-1.82","10842","ATGCGTCACTACGAGATCATGATCATCCTCGACCCCGAGACGGACGAGCGCACCGCCAACGCGACGCTCGAGAAGCTGCTGCAGGTCGTCCCCAGCAACGGGGGCACCGTGGACAAGGTCGACATCTGGGGCAAGCGCCGGCTGGCCTACGACATCAAGAAGAAGTCCGAGGGCTTCTACGCCGTCGTGGACATGACCACCACGCCCGAGATCGCCCAGGAGCTCGACCGCCAGCTCGGCCTCAACGAGACCGTCCTGCGCACCAAGCTGCTGCGTCCCGAGGCCTGA","MRHYEIMIILDPETDERTANATLEKLLQVVPSNGGTVDKVDIWGKRRLAYDIKKKSEGFYAVVDMTTTPEIAQELDRQLGLNETVLRTKLLRPEA$","Ribosomal protein S6","Cytoplasm","ribosomal protein S6","ribosomal protein S6","ribosomal protein S6","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000529
Family

Ribosomal protein S6
PD003809	$\"[39-87]T$	RS6_STRCO_Q9X8U2;
PF01250	$\"[2-93]T$	Ribosomal_S6
TIGR00166	$\"[1-95]T$	S6: ribosomal protein S6
PS01048	$\"[44-53]T$	RIBOSOMAL_S6

InterPro
IPR014717
Domain

Translation elongation factor EF1B/ribosomal protein S6, conserved
G3DSA:3.30.70.60	$\"[1-94]T$	no description

","BeTs to 18 clades of COG0360COG name: Ribosomal protein S6Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0360 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000529 (Ribosomal protein S6) with a combined E-value of 2.6e-14. IPB000529A 4-17 IPB000529B 41-60","","","-57% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 3.5E_10);-57% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 3.5E_10);-57% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.5E_10);-57% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 3.5E_10);-57% similar to PDB:2AVY Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 30S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 3.5E_10);","Residues 2 to 93 (E_value = 6.7e-27) place ANA_2249 in the Ribosomal_S6 family which is described as Ribosomal protein S6.","","protein S6 (rpsF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2250","2436182","2436787","606","5.13","-3.08","20618","ATGGCCGGAGACACCATCATCACCGTCATCGGGAACCTCACCGCGGACCCCGAGATGCGCTTCACGCCCTCCGGGGCAGCGGTGGCCTCCTTCACGGTCGCCTCCACGCCGCGTACCTTCGACCGCCAGGCCGGCGAGTGGAAGGACGGGGAGACCCTGTTCATGCGCTGCTCGATCTGGCGCGACGCCGCGGAAAACGTGGCCGAGTCGCTGACCAAGGGCACGCGCGTCATCGTCCAGGGCCGGCTGGTCCAGCGCTCCTACACCACCCGTGAGGGCGAGAACCGCACGGTCGTGGAGATGCAGGTCGATGAGATCGGTCCGTCCCTGCGCTACGCCAAGGCCCAGGTCACCCGCCAGCCGCGCGGCGGCGGCCAGGGTGGCTTCGGCGGAGGTCAGGGCGGCCCCCAGGGCGGCGGCTTCGGCGGCAACCAGGGCGGTCAGGGCGGATACAACCAGGGCGGCCCCCAGCAGAGCGGCTACAACGGCGGTGGCGGCTTCGGTGGCCAGGGCCAGTCCGGGTACAACGCCCCCGCCGGCGGCGCCGCGGACGACCCGTGGGCCACGGGCGGCTCCACCTCCTTCGGTGACGAGCCCCCGTTCTAA","MAGDTIITVIGNLTADPEMRFTPSGAAVASFTVASTPRTFDRQAGEWKDGETLFMRCSIWRDAAENVAESLTKGTRVIVQGRLVQRSYTTREGENRTVVEMQVDEIGPSLRYAKAQVTRQPRGGGQGGFGGGQGGPQGGGFGGNQGGQGGYNQGGPQQSGYNGGGGFGGQGQSGYNAPAGGAADDPWATGGSTSFGDEPPF$","Single-stranded DNA-binding protein","Extracellular, Cytoplasm","single-stranded DNA-binding protein","single-strand binding protein","single-strand binding protein","","Meyer R.R., Laine P.S. The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev. 1990. 54(4):342-380. PMID: 2087220","","","

InterPro
IPR000424
Family

Single-strand binding protein/Primosomal replication protein n
PF00436	$\"[4-109]T$	SSB
PS50935	$\"[1-110]T$	SSB

InterPro
IPR011344
Family

Single-strand binding protein
PTHR10302	$\"[39-187]T$	SINGLE-STRANDED DNA-BINDING PROTEIN, SSB
TIGR00621	$\"[2-201]T$	ssb: single-strand binding protein

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[4-145]T$	no description

","BeTs to 18 clades of COG0629COG name: Single-stranded DNA-binding proteinFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0629 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB011344 (Single-strand binding protein) with a combined E-value of 7.8e-36. IPB011344A 4-36 IPB011344B 50-102***** IPB000424 (Single-strand binding protein) with a combined E-value of 3.1e-27. IPB000424A 4-41 IPB000424B 63-91***** IPB000817 (Prion protein) with a combined E-value of 2.7e-06. IPB000817A 120-161 IPB000817A 128-169 IPB000817A 135-176 IPB000817A 106-147 IPB000817A 124-165 IPB000817A 134-175 IPB000817A 117-158 IPB000817A 118-159 IPB000817A 126-167 IPB000817A 132-173 IPB000817A 116-157 IPB000817A 108-149 IPB000817A 121-162 IPB000817A 119-160 IPB000817A 109-150 IPB000817A 112-153 IPB000817A 138-179 IPB000817A 125-166 IPB000817A 143-184 IPB000817A 133-174 IPB000817A 130-171 IPB000817A 129-170 IPB000817A 123-164 IPB000817A 136-177 IPB000817A 115-156 IPB000817A 131-172 IPB000817A 122-163 IPB000817A 140-181 IPB000817A 127-168 IPB000817A 139-180 IPB000817A 141-182 IPB000817A 110-151 IPB000817A 150-191 IPB000817A 152-193 IPB000817A 146-187 IPB000817A 137-178","","","-91% similar to PDB:1X3E Crystal structure of the single-stranded DNA-binding protein from Mycobacterium smegmatis (E_value = 1.9E_52);-91% similar to PDB:1X3F Crystal structure of the single-stranded DNA-binding protein from Mycobacterium SMEGMATIS (E_value = 1.9E_52);-91% similar to PDB:1X3G Crystal structure of the single-stranded DNA-binding protein from Mycobacterium SMEGMATIS (E_value = 1.9E_52);-89% similar to PDB:1UE1 Crystal structure of the single-stranded dna-binding protein from mycobacterium tuberculosis (E_value = 9.5E_52);-89% similar to PDB:1UE5 Crystal structure of the single-stranded dna-binding protein from mycobacterium tuberculosis (E_value = 9.5E_52);","Residues 4 to 109 (E_value = 4.3e-30) place ANA_2250 in the SSB family which is described as Single-strand binding protein family.Residues 31 to 109 (E_value = 109) place ANA_2250 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.","","DNA-binding protein (SSB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2251","2436872","2437108","237","11.35","16.91","8749","ATGGCGAAGCCCCAACTTCGCAAGCCGAAGAAGAAGGTCAGCCCCGTCAAGGCCATCAAGGTCGGCACCATCGACTACAAGGACACCGCCACGCTGCGGAAGTTCATCTCCGACCGCGGCAAGATCCGCGCCCGTCGCGTCACCGGCGTCTCCGTCCAGGAGCAGCGCAAGATCGCCAAGGCCGTGAAGAACGCCCGCGAGATGGCTCTGCTGCCCTACTCGAGCTCGGCTCGCTGA","MAKPQLRKPKKKVSPVKAIKVGTIDYKDTATLRKFISDRGKIRARRVTGVSVQEQRKIAKAVKNAREMALLPYSSSAR$","Ribosomal protein S18","Periplasm, Cytoplasm","ribosomal protein S18","K02963 small subunit ribosomal protein S18","ribosomal protein S18","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498Mueller F., Brimacombe R. A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data. J. Mol. Biol. 1997. 271(4):545-565. PMID: 9281425McDougall J., Choli T., Kruft V., Kapp U., Wittmann-Liebold B. The complete amino acid sequence of ribosomal protein S18 from the moderate thermophile Bacillus stearothermophilus. FEBS Lett. 1989. 245(1):253-260. PMID: 2647521Agafonov D.E., Kolb V.A., Spirin A.S. Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique. Proc. Natl. Acad. Sci. U.S.A. 1997. 94(24):12892-12897. PMID: 9371771Otaka E., Suzuki K., Hashimoto T. Examination of protein sequence homologies. VII. The complementary molecular coevolution of ribosomal proteins equivalent to Escherichia coli L7/L12 and L10. Protein Seq. Data Anal. 1990. 3(1):11-19. PMID: 2179947","","","

InterPro
IPR001648
Family

Ribosomal protein S18
PD002239	$\"[24-73]T$	Q6ABW9_BBBBB_Q6ABW9;
PR00974	$\"[31-41]T$ $\"[41-48]T$ $\"[49-63]T$ $\"[63-73]T$	RIBOSOMALS18
G3DSA:4.10.640.10	$\"[2-73]T$	no description
PTHR13479	$\"[1-78]T$	30S RIBOSOMAL PROTEIN S18
PF01084	$\"[18-71]T$	Ribosomal_S18
TIGR00165	$\"[7-76]T$	S18: ribosomal protein S18
PS00057	$\"[24-47]T$	RIBOSOMAL_S18

noIPR
unintegrated

unintegrated
PTHR13479:SF16	$\"[1-78]T$	30S RIBOSOMAL PROTEIN S18

","BeTs to 19 clades of COG0238COG name: Ribosomal protein S18Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0238 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB001648 (Ribosomal protein S18) with a combined E-value of 7.4e-24. IPB001648 31-73","","","-68% similar to PDB:1P6G Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the EF-G.GTP state of E. coli 70S ribosome (E_value = 2.0E_10);-68% similar to PDB:1P87 Real space refined coordinates of the 30S subunit fitted into the low resolution cryo-EM map of the initiation-like state of E. coli 70S ribosome (E_value = 2.0E_10);-68% similar to PDB:1VS5 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5A resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 2.0E_10);-68% similar to PDB:1VS7 Crystal structure of the bacterial ribosome from escherichia coli in complex with the antibiotic kasugamyin at 3.5a resolution. this file contains the 30s subunit of one 70s ribosome. the entire crystal structure contains two 70s ribosomes and is described in remark 400. (E_value = 2.0E_10);-68% similar to PDB:2AVY Crystal structure of the bacterial ribosome from Escherichia coli at 3.5 A resolution. This file contains the 30S subunit of one 70S ribosome. The entire crystal structure contains two 70S ribosomes and is described in remark 400. (E_value = 2.0E_10);","Residues 18 to 71 (E_value = 1e-26) place ANA_2251 in the Ribosomal_S18 family which is described as Ribosomal protein S18.","","protein S18 (rpsR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2252","2437124","2437579","456","10.14","8.14","16232","ATGACCACCAAGCTCATCCTCACGCACGACGTCTCCCACCTCGGCTCCGCCGGCGAGGTCGTGGAGGTCAAGGACGGCTACGCCCGTAACTACCTCCTGCCCCGCAAGCTGGCCACCCCGTGGACCAAGGGCGCCCAGCGCCAGATCGACCAGATGGCCGAGGCGCGCCGCAAGCGCTCCATCGAGTCCCTCGAGCACGCCCAGACCGCTCGCGCCTGGCTGCAGGAGAACGTTGTGACCGTCTCCGCGACCGCCGGTGACAACGGCCGCCTCTTCGGCGCCATCACCACCGCGACCCTGGCCGACGCCGTCAAGGCCGCTGGCGGCCCCGCCGTCGACCGCCGCAAGATCCAGGTCGTGCCGCCGATCAAGTCTACCGGCCGTCACAGCGCCTCCGTGCGCCTGCACGCCGACGTCGTGGCCCCCCTCGAGGTCAACGTCGTCCCCGCGCGCTGA","MTTKLILTHDVSHLGSAGEVVEVKDGYARNYLLPRKLATPWTKGAQRQIDQMAEARRKRSIESLEHAQTARAWLQENVVTVSATAGDNGRLFGAITTATLADAVKAAGGPAVDRRKIQVVPPIKSTGRHSASVRLHADVVAPLEVNVVPAR$","Ribosomal protein L9","Cytoplasm","ribosomal protein L9","K02939 large subunit ribosomal protein L9","ribosomal protein L9","","Ramakrishnan V., Moore P.B. Atomic structures at last: the ribosome in 2000. Curr. Opin. Struct. Biol. 2001. 11(2):144-154. PMID: 11297922Maguire B.A., Zimmermann R.A. The ribosome in focus. Cell 2001. 104(6):813-816. PMID: 11290319Chandra sanyal S., Liljas A. The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 2000. 10(6):633-636. PMID: 11114498","","","

InterPro
IPR000244
Family

Ribosomal protein L9
PTHR21368	$\"[1-150]T$	50S RIBOSOMAL PROTEIN L9
PF01281	$\"[3-50]T$	Ribosomal_L9_N
PF03948	$\"[64-150]T$	Ribosomal_L9_C
TIGR00158	$\"[3-150]T$	L9: ribosomal protein L9
PS00651	$\"[15-42]T$	RIBOSOMAL_L9

noIPR
unintegrated

unintegrated
G3DSA:3.10.430.100	$\"[62-151]T$	no description
G3DSA:3.40.5.10	$\"[3-61]T$	no description
PTHR21368:SF17	$\"[1-150]T$	50S RIBOSOMAL PROTEIN L9

","BeTs to 18 clades of COG0359COG name: Ribosomal protein L9Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0359 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000244 (Ribosomal protein L9) with a combined E-value of 4.7e-44. IPB000244A 3-42 IPB000244B 84-108 IPB000244C 123-147","","","-60% similar to PDB:1DIV RIBOSOMAL PROTEIN L9 (E_value = 1.8E_21);-60% similar to PDB:1GIY CRYSTAL STRUCTURE OF THE RIBOSOME AT 5.5 A RESOLUTION. THIS FILE, 1GIY, CONTAINS THE 50S RIBOSOME SUBUNIT. THE 30S RIBOSOME SUBUNIT, THREE TRNA, AND MRNA MOLECULES ARE IN THE FILE 1GIX (E_value = 1.8E_21);-60% similar to PDB:1YL3 Crystal structure of 70S ribosome with thrS operator and tRNAs. Large subunit. The coordinates for the small subunit are in the pdb entry 1YL4. (E_value = 1.8E_21);-60% similar to PDB:2B66 50S ribosomal subunit from a crystal structure of release factor RF1, tRNAs and mRNA bound to the ribosome. This file contains the 50S subunit from a crystal structure of release factor RF1, tRNAs and mRNA bound to the ribosome and is described in remark 400 (E_value = 1.8E_21);-60% similar to PDB:2B9N 50S ribosomal subunit from a crystal structure of release factor RF2, tRNAs and mRNA bound to the ribosome. This file contains the 50S subunit from a crystal structure of release factor RF1, tRNAs and mRNA bound to the ribosome and is described in remark 400. (E_value = 1.8E_21);","Residues 3 to 50 (E_value = 3.4e-23) place ANA_2252 in the Ribosomal_L9_N family which is described as Ribosomal protein L9, N-terminal domain.Residues 64 to 150 (E_value = 9.1e-24) place ANA_2252 in the Ribosomal_L9_C family which is described as Ribosomal protein L9, C-terminal domain.","","protein L9 (rplI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2253","2439091","2437793","1299","10.54","21.79","47890","ATGGGTAACTCGATTTCGCCGTCTCGGCGTGAGCAGGTCATAGGTTTTGACTCCAGGACCAGTGGGATGAGCGTGGAGGAGTTCTGCGCTCAGGTGGGTATCTCGCGGGCCTCGTTCTACCGGATACGCCGACGCGCTGAGCACGAGGGCCTGGCTGCCGCGCTGACACCGCGTTCACGGGCCCCGCGCTACCCGGCGCGGGTGTGGGACCAGGGCACTGATGAGCGCATCGCCCAGGTTCGTGCCGACCTGCTCGCCGCCGGCCGGGAGGCGGGTCCGGCCTCGGTGTGGTGGGTGATGAGCCAGGGCGCCAGCGTTCCGGCTCCCTCGCGCGCGACGATCGCCCGCAGCCTGCGCAGAGCCGGCCTGGTGGTCCCCGCCCCGCGCAAGCGGCCCAGGACGTCGTACAAGCGCTTCACCCGCAGCGCGGCCAACGAGCTGTGGCAGATCGACGGCTTCCAATGGCGCCTGGAGGACCATCTGGTGACCGTCTACCAGGTCGTTGACGACTGCTCGCGGGTCATCACCGCCCTGAGGGCCTGCTGGGGCGGTGAGAGCGTGGCAGGCACCCGCATGGTCCTTGAGGAGGCCTTCGCCACCTGGGGGCGTCCGGCGGCGATCCTGTCGGACAACGCACTGGCGTTCAACACCAGCCGTATCACTGGCCCGGGAGCCACCGAGAAGTGGCTGGCATCCCTGGGGGTGCGTCCCATCAGCGGGCGGGTGGGCCACCCTCAGACCCAGGGCAAGGTCGAGCGCTCCCACCAGCCGGCAGCCGCCTGGCTGCGCGCCCACCCGGCCAGCACCCTTGAGGAGCTCAACGCCGAGCTGGACCGCTTCACCAGCTACTACAACACCGAGCGCCAGCACCAGGGCCACGGCGTCGCACTGACCCCGCTGAGGGTATGGGCTCAGACCCCCAGGGCGCTGGCCAGCCCAGCCCCCATCGACCTGGAGCGCCTACCAGCCGGCGGCGGCCCCATCAGCCTGCCCGACCCCGCCGATCCCGACCAGGCCGTGGACCGCGCCCGACGCACCGTGATGTCCAACGGGTGCGTGTCCTACAAGGACCGTGCACTGTCACTGGGCCAGACCATGCGCGGCGTCGAGGTCACCCTGATCGAGTACACCACGCGCCTGGACCTCTACGACCCCGACGGACGCCGCTTCGTGTCCCTGCCCTGGCCCCAACCCACCCAGAGGCAGCAAGGCAACCGCTCCACCATCGACACCAAGAAACCGCCCTACAGACTCATCCCGCTCCCACCCCGACGCCCCCGAACGTCTCACAGGTCATAA","MGNSISPSRREQVIGFDSRTSGMSVEEFCAQVGISRASFYRIRRRAEHEGLAAALTPRSRAPRYPARVWDQGTDERIAQVRADLLAAGREAGPASVWWVMSQGASVPAPSRATIARSLRRAGLVVPAPRKRPRTSYKRFTRSAANELWQIDGFQWRLEDHLVTVYQVVDDCSRVITALRACWGGESVAGTRMVLEEAFATWGRPAAILSDNALAFNTSRITGPGATEKWLASLGVRPISGRVGHPQTQGKVERSHQPAAAWLRAHPASTLEELNAELDRFTSYYNTERQHQGHGVALTPLRVWAQTPRALASPAPIDLERLPAGGGPISLPDPADPDQAVDRARRTVMSNGCVSYKDRALSLGQTMRGVEVTLIEYTTRLDLYDPDGRRFVSLPWPQPTQRQQGNRSTIDTKKPPYRLIPLPPRRPRTSHRS$","Transposase","Extracellular, Membrane","Predicted transposase","integrase; catalytic region","Integrase, catalytic region","","Asante-Appiah E., Skalka A.M. HIV-1 integrase: structural organization, conformational changes, and catalysis. Adv. Virus Res. 1999. 52:351-369. PMID: 10384242Thomas M., Brady L. HIV integrase: a target for AIDS therapeutics. Trends Biotechnol. 1997. 15(5):167-172. PMID: 9161051Katzman M., Katz R.A. Substrate recognition by retroviral integrases. Adv. Virus Res. 1999. 52:371-395. PMID: 10384243","","","

InterPro
IPR001584
Domain

Integrase, catalytic core
PF00665	$\"[140-304]T$	rve
PS50994	$\"[128-307]T$	INTEGRASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[143-310]T$	no description

","BeTs to 5 clades of COG1425COG name: Predicted transposaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1425 is a--p-----dr---efgh-n-j----Number of proteins in this genome belonging to this COG is 7","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 140 to 304 (E_value = 2e-21) place ANA_2253 in the rve family which is described as Integrase core domain.","","transposase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2254","2440660","2439242","1419","8.84","3.13","46975","GTGCCCAACACCAGTCGCCCCGCCTCCTCCGGCCTCAACCATCAGGTCCTGTCCCTGGCCGTCCCCGCTCTGGGAGCTCTCATCGCCGAGCCGCTCTTCATCCTGGCGGACTCGGCCATGGTCGGCCACCTCGGCGCGGTGAGCCTGGCGGGCCTGTCCCTGGCCTCGACGATCCTGACGACGACGGTGGGCCTGTTCGTCTTCCTGGCCTACGCCACCACGGCGACGACGGCGCGTCTATTCGGGGCCGGCCGGCGCACCGAGGGCCTGCGGGCCGGCGTCGACGGCATGTGGCTGGCACTCCTGCTGGGACTGGGCGCGGGCGCCTTCCTGGGACTGACCGCCCCCTGGCTGACCGCTGCGATGGGCGCCGACGGCGCGGTGGCTCAGGCGGCCGTCGCCTACCTGCGCGCCTCCTGCCCGGGGTTGCCAGGCATGTTCGTCGTCCTGGCCGCCACTGGTGTGCTGCGCGGTCTGTTGGACACGCGCACGCCCTTCGTCGTGGCCACGGGCGGGGCGGTCTTCAACGTCGTCGTCAACGCGATCCTGCTCTACGGCGTCGGAATGGGGATCGCGGGCTCGGGTGCCGGAACCGCGATCGCGCAGACGGCCATGGCGCTGGCGCTGGCCGGTCCGATCACCCGGGCGGCCCGGGCAGCCGGAGTGGGTCTGCTCCCCCACCGCGAGGGCCTGCGGGCCTCCCTGGGCAGTGGGGCGCCGCTACTCATCCGCTCACTGAGCCTACGGGTGGCGATCCTGGTGACCGTGTGGGCGGCAACCGCGCTCGGGGAGGTGTCGCTGGCCGCCCACCAGGTGGTCAACGCCCTGTGGACCTTTGCGGCCTTCGCCCTGGACGCACTGGCTGTGGCGGCGCAGGCCCTCATCGGCACCGCCCTGGGACAGGCCCAGCGAGCGGACGCGGACTCGGCCGCACCGGAGGCTGAGGCCCTCACCGAGGAGGAGGCCGGGGCTGCTGCGGCGACCGCCGGCTGGTCCATTGACGAGCTCCTCAAGCGGATGCTGGCCTGGGGCGCTGGGACGGGGGCCCTTATCGGCGTGCTCATGGCAGCGGGCGCCGCCTGGCTGCCCCGCGCCTTCACCTCCGACCCAGGCGTCATCGCGGCCGCGACTCCAACGCTCCTGGTCGCGGCGAGCGCGCAGCCACTCGCCGGGGTCGTCTTCCTGCTCGACGGCGTGCTCATGGGCGCCGGCGACGGCCGCTACCTGGCCCGGGCGGGCCTGGTGACGCTGCTGCCCTATGTGCCACTCGCACTACTCATCGGGGGCGGCGTGCTGCCGGGGGCTGACGGGGCGACGTCGGGCCTGGTGCTGCTGTGGATCGCCTTCGCCTGGGTCTTCATGGCCGCCCGCGGCGCCACCACCTACCTGCGCTCGCGCGGTACCGCCTGGCGCCACTGA","VPNTSRPASSGLNHQVLSLAVPALGALIAEPLFILADSAMVGHLGAVSLAGLSLASTILTTTVGLFVFLAYATTATTARLFGAGRRTEGLRAGVDGMWLALLLGLGAGAFLGLTAPWLTAAMGADGAVAQAAVAYLRASCPGLPGMFVVLAATGVLRGLLDTRTPFVVATGGAVFNVVVNAILLYGVGMGIAGSGAGTAIAQTAMALALAGPITRAARAAGVGLLPHREGLRASLGSGAPLLIRSLSLRVAILVTVWAATALGEVSLAAHQVVNALWTFAAFALDALAVAAQALIGTALGQAQRADADSAAPEAEALTEEEAGAAAATAGWSIDELLKRMLAWGAGTGALIGVLMAAGAAWLPRAFTSDPGVIAAATPTLLVAASAQPLAGVVFLLDGVLMGAGDGRYLARAGLVTLLPYVPLALLIGGGVLPGADGATSGLVLLWIAFAWVFMAARGATTYLRSRGTAWRH$","MATE efflux family protein","Membrane, Extracellular","POSSIBLE DNA-DAMAGE-INDUCIBLE PROTEIN F DINF","DNA-damage-inducible protein F","MATE efflux family protein","","","","","

InterPro
IPR002528
Family

Multi antimicrobial extrusion protein MatE
PTHR11206	$\"[36-308]T$ $\"[335-471]T$	MULTIDRUG RESISTANCE PUMP
PF01554	$\"[22-182]T$ $\"[240-426]T$	MatE
TIGR00797	$\"[22-446]T$	matE: MATE efflux family protein

noIPR
unintegrated

unintegrated
PTHR11206:SF3	$\"[36-308]T$ $\"[335-471]T$	DNA-DAMAGE-INDUCIBLE PROTEIN F
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[21-43]?$ $\"[49-69]?$ $\"[90-110]?$ $\"[116-136]?$ $\"[165-185]?$ $\"[191-211]?$ $\"[253-273]?$ $\"[279-299]?$ $\"[341-361]?$ $\"[380-400]?$ $\"[412-432]?$ $\"[438-456]?$	transmembrane_regions

","BeTs to 10 clades of COG0534COG name: Na+-driven multidrug efflux pumpFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG0534 is aom-kzyqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002528 (Multi antimicrobial extrusion protein MatE) with a combined E-value of 1.2e-11. IPB002528A 190-203 IPB002528B 372-421","","","No significant hits to the PDB database (E-value < E-10).","Residues 22 to 182 (E_value = 9.5e-32) place ANA_2254 in the MatE family which is described as MatE.Residues 240 to 426 (E_value = 7.3e-09) place ANA_2254 in the MatE family which is described as MatE.","","DNA-DAMAGE-INDUCIBLE PROTEIN F DINF","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2256","2443665","2442874","792","10.44","6.67","28033","ATGAGCACCTCACCTGACCAGTCCACGCCACAGACCGAGTGGGACCGCTCCGAGGGCGCCCGGTTCCGGTCGAAGGCCGCGACCACGGGCCTGGTCGCACTCGTCACCCTGCGGGAGCTCGCCCGACGGCGCGGCGCCCTCGCACTGGCGACCCTCCTGCCGCTGACCTTCTACCTGGTGCGCCTGGAGACGCACTGGACCGCCATCCGGCTCCTGTCGATCGGCCTGGGCTGGGCGACGGCGACGCTGGCGCTGTTCACACAGGTCTCGTCCCGCTCAGTGGACCGCCGCCTCGCCGTGAGCGGGGCTCGGCCCGCAAGCCTGCTGCTGGGCCGCTACCTCGCGGTGCTCGGGCTCGGGTGGATTATCGGCCTGCTCTACAGCGGCCTCGTCCTGGCCACGATCGGCGACGAGCTCACCCACCCGAGTGCGGTGCCGGTCATGCTGCTGCTGACCGCCACCGTGGCCACTCCCCTGGGCTCCCTGGCCGCCGCCCTGGTTCCACGGGACCTCGAGGGAGCACTTCTGCTGCTGTCAGTGATGGCGGTGCAGGTACTGGTGGATCCTTCAGAGGGCTGGACCCGAGTGCTGCCGCTGTGGTCGACCCGGGAGCTCGCGAGCGTCATCGTGGAGAACCTGGGACCCGAGACCGCCGACTACCTCCGCCGCGGGCTGGCGCATGGCGTCGCCATGACCGTCCTGCTGACCACGGCGAGCTGGGCCGTGGGCGTCCAGCGCCTGCGCACGGTCCGCCTCCCGACCCCGTCCCCAGCCGGGCCGGCCTACTCGTAG","MSTSPDQSTPQTEWDRSEGARFRSKAATTGLVALVTLRELARRRGALALATLLPLTFYLVRLETHWTAIRLLSIGLGWATATLALFTQVSSRSVDRRLAVSGARPASLLLGRYLAVLGLGWIIGLLYSGLVLATIGDELTHPSAVPVMLLLTATVATPLGSLAAALVPRDLEGALLLLSVMAVQVLVDPSEGWTRVLPLWSTRELASVIVENLGPETADYLRRGLAHGVAMTVLLTTASWAVGVQRLRTVRLPTPSPAGPAYS$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[67-87]?$ $\"[108-128]?$ $\"[147-167]?$ $\"[224-244]?$	transmembrane_regions

InterPro
IPR007692
Family

DnaB helicase
TIGR00665	$\"[25-460]T$	DnaB: replicative DNA helicase

InterPro
IPR007693
Domain

DnaB-like helicase, N-terminal
G3DSA:1.10.860.10	$\"[30-132]T$	no description
PF00772	$\"[29-131]T$	DnaB

InterPro
IPR007694
Domain

DnaB-like helicase, C-terminal
PD332834	$\"[312-420]T$	Q6A5L6_PROAC_Q6A5L6;
PF03796	$\"[205-403]T$	DnaB_C
PS51199	$\"[202-467]T$	SF4_HELICASE

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[192-451]T$	no description

","BeTs to 18 clades of COG0305COG name: Replicative DNA helicaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0305 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB007693 (DnaB-like helicase, N-terminal) with a combined E-value of 5.7e-114. IPB007693A 41-94 IPB007693B 208-246 IPB007693C 257-289 IPB007693D 338-349 IPB007693E 356-403 IPB007693F 434-462","","","-59% similar to PDB:1JWE NMR Structure of the N-Terminal Domain of E. Coli Dnab Helicase (E_value = 3.8E_17);-57% similar to PDB:1B79 N-TERMINAL DOMAIN OF DNA REPLICATION PROTEIN DNAB (E_value = 1.6E_15);","Residues 29 to 131 (E_value = 3.2e-42) place ANA_2257 in the DnaB family which is described as DnaB-like helicase N terminal domain.Residues 205 to 403 (E_value = 1.1e-106) place ANA_2257 in the DnaB_C family which is described as DnaB-like helicase C terminal domain.","","DNA helicase (dnaB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2258","2444651","2443662","990","8.72","3.16","35051","ATGAGCCGGCCCGAGGAAGCCAGGGACCCAGCACAGAACACAACGGCCGAGTGGTACCGAAGCTTCACGGTAGAGCTTGCCTCCCGCGGTCTGCCGTCCTCCGAGGTCGAGCGCACGGCCGCCTCGACCCGGGCGGAGGCCGAGGCGGCCGGGGTGCCGCCCGGCGACCTGTACGGTCCGGCAGTCCTCTACGCCCGCGAGGTCGCCTCTGCACTACGGGACTACCAGGCGGCAGCACCCGCCCCGGCCCCACACAGCTCGTCGCCCCACGCCACTGCTGACCTCGGCACCACCGACTTCGCCACCACATCTGCCAAGACTCCGCCCGCAACCCCCGTGGTCCTGCGCCTGACGGACGTCTCCGCGCGCCGCGGCAGGCGCACGGTCCTGTCCGGAATCAACCTCACCATCCACCGGGGCGAGGTCGTCGCCGTCGTCGGGGCCAACGGCGCCGGCAAGTCGACTCTGCTTCAGCTTTGCGCGGGCCTGCTGCGCGCAAGCGGTGGGCGCATCGAGAGGACGCCGAACTTCGGCTATGCGCCTCAGCTCGACTCCTTGGCGCCGCTGCTGACGGTGGACGAGCACCTCCGGCTCTTCGGGGCGGCGCGTGGGATCCGGCAAGGCCGCTCCATCTCGACCGGCCGCCGTCTCCTGACCCGCCTGGGCTGGACCGCCCGCGGAGACCAGACCGCCGGGACGCTCTCGGGCGGGACCCAGCAGAAGCTCAACGTCGCTCTCGCCCAGCTCGACGCGCCCGACCTGCTCCTGCTGGATGAGCCCTACCAGGGCCTGGACGCCCTGGCCTACGAGGATCTGTGGGCCCTCATCTCGGCCTGGCGCACCTCGGGCGCGGGCGTCCTGCTGGTCACCCACCTGCTGCGCGACGTCGACCTGGTCGACCGCGTCGTCGAGCTGCCGGCCCCGCAGGAGGACGCAAGCCGGACTGTCCTCCGAATGCCCCGGCGGGTACAGCGAAAGGAGTCCGCATGA","MSRPEEARDPAQNTTAEWYRSFTVELASRGLPSSEVERTAASTRAEAEAAGVPPGDLYGPAVLYAREVASALRDYQAAAPAPAPHSSSPHATADLGTTDFATTSAKTPPATPVVLRLTDVSARRGRRTVLSGINLTIHRGEVVAVVGANGAGKSTLLQLCAGLLRASGGRIERTPNFGYAPQLDSLAPLLTVDEHLRLFGAARGIRQGRSISTGRRLLTRLGWTARGDQTAGTLSGGTQQKLNVALAQLDAPDLLLLDEPYQGLDALAYEDLWALISAWRTSGAGVLLVTHLLRDVDLVDRVVELPAPQEDASRTVLRMPRRVQRKESA$","ABC-type multidrug transport system, ATPase component","Membrane, Periplasm","ABC-type transport system ATP-binding protein","putative ABC transporter ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PF00005	$\"[140-309]T$	ABC_tran
PS50893	$\"[115-329]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[139-309]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[77-305]T$	no description
PTHR19222	$\"[115-305]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 11 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 21","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 9.2e-28. IPB005074C 129-176 IPB005074D 222-265 IPB005074E 285-305***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 4.9e-18. IPB013563A 129-163 IPB013563C 231-258***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 7.7e-12. IPB010509B 140-165 IPB010509D 229-273***** IPB005116 (TOBE domain) with a combined E-value of 4.9e-09. IPB005116A 147-163 IPB005116C 234-247 IPB005116D 254-273","","","No significant hits to the PDB database (E-value < E-10).","Residues 140 to 309 (E_value = 1.3e-36) place ANA_2258 in the ABC_tran family which is described as ABC transporter.","","transport system ATP-binding protein (III)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2259","2444998","2444648","351","8.20","1.39","12529","ATGGACTCATCAGCGGCGCGCCTCCTGCGCGGATTCCTGGAACCCTGTCTGCTCTCACTGCTGGCCGAGCACGCCGACTACGGGCTGTCCCTGGCCCAGCGGCTCGCCGCCGCCGGATTGGACGAGGTACCCGGCGGCACGCTCTACCCGGCTCTCATGCGCCTGGAGAAGCGCGGCCTCGTCGCGGTCTCCTGGCGCCCCTCCACCTCCGGGCCCGCCCGCAAGTACTACGAGCTGACGGACGCCGGACACACTGAGCTCGCCGCACGTCGGACCGAATGGCGCACCTTCTCCACGGCGGTCGGCGCTCTCATCGAGGGCCGCAGGGTAAGCACGGAGGCCCCCTCATGA","MDSSAARLLRGFLEPCLLSLLAEHADYGLSLAQRLAAAGLDEVPGGTLYPALMRLEKRGLVAVSWRPSTSGPARKYYELTDAGHTELAARRTEWRTFSTAVGALIEGRRVSTEAPS$","Transcriptional regulator, PadR family","Cytoplasm, Periplasm","transcriptional regulator, PadR family","transcriptional regulator; PadR family","transcriptional regulator PadR family protein","","Gury J., Barthelmebs L., Tran N.P., Divies C., Cavin J.F. Cloning, deletion, and characterization of PadR, the transcriptional repressor of the phenolic acid decarboxylase-encoding padA gene of Lactobacillus plantarum. Appl. Environ. Microbiol. 2004. 70(4):2146-2153. PMID: 15066807","","","

InterPro
IPR005149
Family

Transcriptional regulator PadR-like
PF03551	$\"[7-90]T$	PadR

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[13-97]T$	no description

","BeTs to 12 clades of COG1695COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1695 is aompkz--vdrlb-e-g----j----Number of proteins in this genome belonging to this COG is 4","***** IPB005149 (Transcriptional regulator PadR-like family) with a combined E-value of 1e-07. IPB005149A 27-41 IPB005149B 44-52 IPB005149C 73-82","","","No significant hits to the PDB database (E-value < E-10).","Residues 7 to 90 (E_value = 1.1e-31) place ANA_2259 in the PadR family which is described as Transcriptional regulator PadR-like family.","","regulator, PadR family (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2260","2445223","2445071","153","11.70","6.61","5657","GTGCGTCATCTACGCCCAGATCTGTCACGGATGGCGACTTTTCAGGCGGACCGCCGCGGCCACCAACCCATCCGCACCGCCCTGACCTGCGTAGATGCCCCTGGCCCACCGACGCGACGCAGCACAGACACACTTAAAAGTCGCCATCCGTGA","VRHLRPDLSRMATFQADRRGHQPIRTALTCVDAPGPPTRRSTDTLKSRHP$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2261","2446119","2445313","807","4.89","-12.74","28059","ATGACTGCCATTGCCCTGACCATCGCCGGCTCCGAGGCCTCGGGCGGCGCCGGCGCCCAGACCGACCTCAAGACCTTCCACACCCTCGGCGTCTACGGTTGCACGGCCCTGACCTGCATCGTGTCCATGGACCCCAAGGACGGGTGGAACCACCGCTTCGTCCCCGTGGACCCCGGCGTCATCGCCGACCAGATCGAGACCTGCGCCGCCGTCCACTCGCGCATCGACGCCGTCAAGATCGGAATGCTGGGTACGGCGCCCACCATCGACGTCGTTGAGCAGGCCCTGGAGACCTACGACTTCCCCACCGTGGTGCTCGACCCGGTCCTCATCTGCAAGGGCCAGGAGTTCGGGGGCGCCCTCGAGGTGGACAACGCCCTGCGCACCAAGATCCTGCCGCGCGCCACGATGACCACTCCGAACCTCTTCGAGGCCGCCACGCTGGCGGGCATGGAGGAGATCACCTCCGTCGAGCAGCTCAAGGACGCCGCCAAGCGCATCCACGACCAGGGCGTCCCCAATGTCCTGGCCAAGGCCGGCCCGTCGCTGGGCACCGGCACCGCGCTGGACGTCTTCTACGACGGCACCACCCTGGAGGTCCTCGAGGTTGAGGCCGTCGGCACCGAGCGCGTCCACGGCGCCGGCTGCACCCTGGCCGCCGCGGTGACCGCCGAGCTCGCCAAGGGCGCCTCCCCGCTTGAGGCCGCCGTCACCGCCAAGGAAGTCGTCTCCTCCTCCATCCGGCACGGCCTGCGCGGCAACATGCCCTTCCTCTACGTCTACCAGGGCGAGTACCGGCAGGACTGA","MTAIALTIAGSEASGGAGAQTDLKTFHTLGVYGCTALTCIVSMDPKDGWNHRFVPVDPGVIADQIETCAAVHSRIDAVKIGMLGTAPTIDVVEQALETYDFPTVVLDPVLICKGQEFGGALEVDNALRTKILPRATMTTPNLFEAATLAGMEEITSVEQLKDAAKRIHDQGVPNVLAKAGPSLGTGTALDVFYDGTTLEVLEVEAVGTERVHGAGCTLAAAVTAELAKGASPLEAAVTAKEVVSSSIRHGLRGNMPFLYVYQGEYRQD$","Phosphomethylpyrimidine kinase","Cytoplasm","phosphomethylpyrimidine kinase","phosphomethylpyrimidine kinase ","phosphomethylpyrimidine kinase","","Petersen L.A., Downs D.M. Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis. J. Bacteriol. 1997. 179(15):4894-4900. PMID: 9244280","","","

InterPro
IPR004399
Domain

Phosphomethylpyrimidine kinase type-2
TIGR00097	$\"[5-257]T$	HMP-P_kinase: phosphomethylpyrimidine kinas

InterPro
IPR013749
Domain

Phosphomethylpyrimidine kinase type-1
PF08543	$\"[14-252]T$	Phos_pyr_kin

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[2-262]T$	no description
PTHR20858	$\"[1-251]T$	PHOSPHOMETHYLPYRIMIDINE KINASE

","BeTs to 21 clades of COG0351COG name: Hydroxymethylpyrimidine/phosphomethylpyrimidine kinaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0351 is aompkzyqvdrlb-efghsnuj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB013749 (Phosphomethylpyrimidine kinase type-1) with a combined E-value of 3.9e-52. IPB013749A 5-45 IPB013749B 75-90 IPB013749C 105-115 IPB013749D 131-150 IPB013749F 201-224","","","-60% similar to PDB:2I5B The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parralel emergence of enzyme activity during evolution (E_value = 1.1E_51);-49% similar to PDB:1UB0 Crystal Structure Analysis of Phosphomethylpyrimidine Kinase (ThiD) from Thermus Thermophilus Hb8 (E_value = 4.1E_25);-47% similar to PDB:1JXH 4-Amino-5-hydroxymethyl-2-methylpyrimidine Phosphate Kinase from Salmonella typhimurium (E_value = 2.7E_21);-47% similar to PDB:1JXI 4-Amino-5-hydroxymethyl-2-methylpyrimidine Phosphate Kinase from Salmonella typhimurium complexed with 4-Amino-5-hydroxymethyl-2-methylpyrimidine (E_value = 2.7E_21);","Residues 14 to 252 (E_value = 3.6e-77) place ANA_2261 in the Phos_pyr_kin family which is described as Phosphomethylpyrimidine kinase.","","kinase (thiD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2262","2446827","2446216","612","4.85","-10.83","20836","ATGAAGATCGCCGTCATCGGAGGAACCGGCATGGTCGGCTCGGCCACCGTCACCGAGGCCGCCGGCCGCGGCCACGAGGTCGTCTCCGCCTCGCGCTCGGGCCGTCACGCCGAGGGAGCCGCGCAGGACGTCACCCTCACCCTGACCGACACGCAGGCCGTCGTCGACCTCGTCAACGGCTCCGACGCCACCGTCATCACCGTCTCCGCCGGCCGCGGAGAGCCCGCCCAGCCCGTCATTGACGCCCACCGCGCCCTTATCGCGGCTGCTCCCACCGGCCGGCTCATCGTCGTCGGCGGCGCCGGCTCCCTGCTCACCCCCGACGGCACCCGCCTGGTGGACACCCCCGGGTTCCCCGAGGAATACAAGGCCGAGGCCCTGGCCTTCACCGAGGTCCTCGACCTCTATCGCGAGGCCGGCAGCGCCCTGACCTGGACCTTCCTCTCCCCCGCCCCGGAGTTCACCGACAAGCCGCGCACCGGCACCTACACCGAGGGCGGCGACCAGCCCGCGGGCAGCGAGATCTCCGTGGCCGACTTCGCCGTCGCTCTGGTGGACGAGGCCGAGAAGGACGCGCACCGCGGCCACCGCTGGACCATCGCCAACGCCTGA","MKIAVIGGTGMVGSATVTEAAGRGHEVVSASRSGRHAEGAAQDVTLTLTDTQAVVDLVNGSDATVITVSAGRGEPAQPVIDAHRALIAAAPTGRLIVVGGAGSLLTPDGTRLVDTPGFPEEYKAEALAFTEVLDLYREAGSALTWTFLSPAPEFTDKPRTGTYTEGGDQPAGSEISVADFAVALVDEAEKDAHRGHRWTIANA$","NAD-dependent epimerase/dehydratase","Cytoplasm","conserved hypothetical protein","hypothetical protein","NAD-dependent epimerase/dehydratase","","Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 1997. 36(21):6294-6304. PMID: 9174344","","","

InterPro
IPR001509
Family

NAD-dependent epimerase/dehydratase
PF01370	$\"[3-63]T$	Epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[2-202]T$	no description
PTHR15020	$\"[1-202]T$	FLAVIN REDUCTASE-RELATED
PTHR15020:SF10	$\"[1-202]T$	CHARACTERIZED

","BeTs to 5 clades of COG2910COG name: Putative NADH-flavin reductaseFunctional Class: RThe phylogenetic pattern of COG2910 is ---k---Ce--H-----l---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 126 (E_value = 1.8e-06) place ANA_2262 in the F420_oxidored family which is described as NADP oxidoreductase coenzyme F420-dependent.Residues 59 to 257 (E_value = 0.0021) place ANA_2262 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.","","hypothetical protein","","1","","","Wed Aug 8 13:39:43 2007","","Wed Aug 8 13:39:43 2007","","","Wed Aug 8 13:39:43 2007","Wed Aug 8 13:39:43 2007","Wed Aug 8 13:39:43 2007","","","Wed Aug 8 13:39:43 2007","","","Wed Aug 8 13:39:43 2007","","","","Wed Aug 8 13:39:43 2007","Wed Aug 8 13:39:43 2007","","","","","yes","","" "ANA_2263","2447067","2447522","456","5.30","-5.17","16415","ATGGAGCTGTCCTCAGGCGAGTCAGGAGAGGTAACTCCTCAGGAGAGCGCCCCATGCTGCGAGGTTGCTGTCGGGGAGGGAACCCAGGCGCCGGTCTTCGACTTCGACATCCTCTCGCCCGCCTGCCCGTCGCGCACGGTGCTGCGTCACGTCGTTGACCGCTGGACCCCGCTGGTGGTCACGGTCCTGGCCGACGGGCCGAGCCGCTTCGGCGAGCTGCGCGCTCGGGTCGGCGGGGTGACGCCCAAAGTCCTCACCCAGACGCTGCGATCCATGGAGCGCGACGGCCTGGTGACGCGCACCCAGCTGCCGGGTGTGCCGCCGCGGGTCGACTACGAGCTGACCGACCTGGGCCGCAGCCTCCAGGCGCCTATCGACGCGCTGCGCACCTGGATCCACACCCACTCAGCCCAGATCCTGGCCCACCGCGAGTCCTACGACGCCGTCGAATCCTGA","MELSSGESGEVTPQESAPCCEVAVGEGTQAPVFDFDILSPACPSRTVLRHVVDRWTPLVVTVLADGPSRFGELRARVGGVTPKVLTQTLRSMERDGLVTRTQLPGVPPRVDYELTDLGRSLQAPIDALRTWIHTHSAQILAHRESYDAVES$","Transcriptional regulator, HxlR family","Cytoplasm, Periplasm","transcriptional regulatory protein","putative transcriptional regulator","helix-turn-helix, HxlR type","","Yasueda H., Kawahara Y., Sugimoto S. Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression. J. Bacteriol. 1999. 181(23):7154-7160. PMID: 10572115Huffman J.L., Brennan R.G. Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr. Opin. Struct. Biol. 2002. 12(1):98-106. PMID: 11839496","","","

InterPro
IPR002577
Domain

Helix-turn-helix, HxlR type
PD004032	$\"[69-106]T$	Q98I26_RHILO_Q98I26;
PF01638	$\"[50-140]T$	DUF24
PS51118	$\"[42-140]T$	HTH_HXLR

","BeTs to 13 clades of COG1733COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1733 is Amt----ceBR----------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-64% similar to PDB:1YYV Putative transcriptional regulator ytfH from Salmonella typhimurium (E_value = 7.1E_24);-57% similar to PDB:2HZT Crystal Structure of a putative HTH-type transcriptional regulator ytcD (E_value = 4.3E_13);-56% similar to PDB:1Z7U Crystal Structure of the Putitive Transcriptional Regulator of MarR Family from Enterococcus faecalis V583 (E_value = 1.5E_10);-56% similar to PDB:2FSW Crystal Structure of the Putative Transcriptional Regualator, MarR family from Porphyromonas gingivalis W83 (E_value = 2.0E_10);","Residues 82 to 172 (E_value = 4.5e-31) place ANA_2263 in the DUF24 family which is described as HxlR-like helix-turn-helix.Residues 120 to 157 (E_value = 9.1e-05) place ANA_2263 in the PadR family which is described as Transcriptional regulator PadR-like family.","","regulatory protein","","1","","","Wed Aug 8 13:45:11 2007","","Wed Aug 8 13:45:11 2007","","","Wed Aug 8 13:45:11 2007","Wed Aug 8 13:45:11 2007","Wed Aug 8 13:45:11 2007","","","Wed Aug 8 13:45:11 2007","","","Wed Aug 8 13:45:11 2007","Wed Aug 8 13:45:11 2007","","","Wed Aug 8 13:45:11 2007","Wed Aug 8 13:45:11 2007","","","","","yes","","" "ANA_2264","2447947","2449950","2004","4.87","-38.64","74172","ATGAGCGCCGCCACTTCCCTCCCGCCATCCCTCAACGACATCGTCTTCCACGTCCTGGACCCGCTTGAGGCCGTGGAGCGGGACATCTTCCTCACGCGCGCCGAGGCCTGGTACCCCGACCTTCTCGACGGGCTCACCACCCTCTACGGCGACGCCGCCGAGGAGGAGGTCCTCAACCTGCTGGCCCTGGCCGCCCGGGCCTACGCGGAGCGCGACTACGAGCTGCGCCGCCTGGATCTGGCCCGTACCCTCGACCCCGCCTGGGCCCAGCACCCGGGCCGCGTCGGATACGCCGCCTACACCGAGCGCTTCGCCGGCACCCTGCGCGGCGTGGAGGACCGCATCGACTACCTGCGCGAGCTGGGTGTCACCTATCTCCACCTCATGCCCCTGCTCACCCCGCGCCCTGGCGACTCCGACGGCGGCTACGCGGTCGCCGACTACCGCACCGTGCGCCCGGACCTGGGCTCCATGGAGGACCTTGAGCACCTGGCCGGCGAACTGCGCGCCGAGGGCATCTCCCTGGTGGTGGACCTCGTCCTCAACCACGTGGCCGCCGAGCATGAGTGGGCGGCGCGGGCCCGCGCCGGCGAGCAGCGCTACCGCGACTACTTCCTCATCTTCCCTGACCGCACTGAGCCCGACGCCTACGAGCGCACCCTGCCGGAGGTCTTCCCCGACTTCGCCCCCGGCAACTTCACCTGGGACGACGGTGTGGGCGGCTGGGTGTGGACCACCTTCAACTCCTTCCAGTGGGACCTCAACTGGCGCAACCCCCACGTCATGGCCGAGTTCGCCGGCATCGTTCTGGACTTGGCCAACCGCGGCGTCGAGGTGCTGCGCCTGGACGCCATCGCCTTCACCATCAAGCGCAAGGGCACCGACTGCCAGGGCCAGCCCGAGGTCCACGCCATCACCGAGGTCCTGCGCGCCCTGACTCGCATCGTCTGCCCCGCCGTCGACCTCAAGGCCGAGGCGATCGTCGCCCCCACCGAGCTCCTCCAGTACCTGGGCCAGGGCAAGTACACCGGCAAGGTCTCCGACCTGGCCTACCACAACTCCCTCATGGTCCAGATCTGGTCCATGCTCGCGGCGCGCGACACGACGCTGGCCGTCGAGGCCCTCCAGAACCTGCCGGTCGAGCCCTCCACCGCCACCTGGATCACCTACCTGCGCTGCCACGACGACATCGGCTGGGCCATTGACGACGACGACGCGGCCGCAGTCGGCCTGAGCGGTTACGACCACCGCTCCTTCCTGGCCGACTGGTACAGCGGCGAGTACCCCACCTCCGACGCCGCGGGCCTGGTCTTCCAGCACAACCCGGCCACCGGGGACCGGCGCATCGCCGGGACGGCCGCCTCGCTCATCGGGATTGAGGCCGCCGACCAGGCCTGGGAGGGCGTCACCGACGAGACTCCCGAGCACGAGGTCGAGGCGTTGTGGACCTGGCGCGAGGAGCGGATCCATGCCCTGCGCATGGCCCACGCCATCGTCTACGGCTGGGGCGGCATCCCCGTCCTGTGGAGCGGGGACGAGCTCGCCCAGCCCAACGACCCCAACTGGGACACCGAGCCGGGCCACGAGGCCGACTCGCGCTGGGCCGGTCGCCCCCGCCTCAATGAGGCCCGGCTGGCCAACCGCCGCGACCGCTCCACCGTCGAGGGGCGCGTCTTCACCGACCTGGCGCGAATGGCGCAGGTGCGCGCCGGCCTGCCCCAGCTCGACGCCGCGGTGCGTACCCAGGTCCAGGACGTCGACGACCACGGGGTGCTGGTGACCTACCGCGACCACCCGCGCGGCAGCTTCGTGGGCGTGTACAACGTGACGCCGCAGTGGCGCTCGGTGGCCGCGTACCAGCTCGCCCGGCTCGGGGTCATGGGGGCCACTGACGTCCTGACTGACACGGTCCCCTTCGGCTCCACCACGCTGGACGGGGCGGGGGACGGGCGCGTGCCCGTGCCGCCCTACGCCGCCTGGTGGCTGGTGCGCCCCACGGACTGA","MSAATSLPPSLNDIVFHVLDPLEAVERDIFLTRAEAWYPDLLDGLTTLYGDAAEEEVLNLLALAARAYAERDYELRRLDLARTLDPAWAQHPGRVGYAAYTERFAGTLRGVEDRIDYLRELGVTYLHLMPLLTPRPGDSDGGYAVADYRTVRPDLGSMEDLEHLAGELRAEGISLVVDLVLNHVAAEHEWAARARAGEQRYRDYFLIFPDRTEPDAYERTLPEVFPDFAPGNFTWDDGVGGWVWTTFNSFQWDLNWRNPHVMAEFAGIVLDLANRGVEVLRLDAIAFTIKRKGTDCQGQPEVHAITEVLRALTRIVCPAVDLKAEAIVAPTELLQYLGQGKYTGKVSDLAYHNSLMVQIWSMLAARDTTLAVEALQNLPVEPSTATWITYLRCHDDIGWAIDDDDAAAVGLSGYDHRSFLADWYSGEYPTSDAAGLVFQHNPATGDRRIAGTAASLIGIEAADQAWEGVTDETPEHEVEALWTWREERIHALRMAHAIVYGWGGIPVLWSGDELAQPNDPNWDTEPGHEADSRWAGRPRLNEARLANRRDRSTVEGRVFTDLARMAQVRAGLPQLDAAVRTQVQDVDDHGVLVTYRDHPRGSFVGVYNVTPQWRSVAAYQLARLGVMGATDVLTDTVPFGSTTLDGAGDGRVPVPPYAAWWLVRPTD$","Alpha-amlyase","Cytoplasm","alpha-amlyase","alpha amylase; catalytic region","alpha amylase, catalytic region","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[98-285]T$	Alpha-amylase

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[86-575]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[97-397]T$ $\"[441-458]T$ $\"[489-662]T$	AMYLASE
PTHR10357:SF11	$\"[97-397]T$ $\"[441-458]T$ $\"[489-662]T$	ALPHA-AMYLASE

","BeTs to 9 clades of COG0366COG name: GlycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0366 is ---p--y-vdrlbcefg----j----Number of proteins in this genome belonging to this COG is 7","***** IPB006589 (Alpha amylase, catalytic subdomain) with a combined E-value of 1.1e-13. IPB006589A 113-130 IPB006589B 155-183***** IPB004185 (Glycoside hydrolase, family 13, N-terminal Ig-like domain) with a combined E-value of 8.2e-12. IPB004185B 102-135 IPB004185C 142-173","","","-57% similar to PDB:1G5A AMYLOSUCRASE FROM NEISSERIA POLYSACCHAREA (E_value = 5.3E_108);-57% similar to PDB:1JG9 Crystal Structure of Amylosucrase from Neisseria polysaccharea in Complex with D-glucose (E_value = 5.3E_108);-57% similar to PDB:1MW1 Amylosucrase soaked with 14mM sucrose. (E_value = 5.3E_108);-57% similar to PDB:1MW2 Amylosucrase soaked with 100mM sucrose (E_value = 5.3E_108);-57% similar to PDB:1MW3 Amylosucrase soaked with 1M sucrose (E_value = 5.3E_108);","Residues 98 to 544 (E_value = 2e-19) place ANA_2264 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2265","2450195","2451670","1476","5.32","-12.09","50443","CTGAGCGTCTTCGACCTCATGCGCATCGGCATCGGCCCCTCCTCCTCCCACACCGTGGGCCCCATGCGGGCCGGCCGCGCCTTCAGCCGGGCCCTGGCCGAGGCGGTCCGCCCAGGCGGCGCGGGGGCCTCCGACGCCGAGTGCGCCTCACCGGCCCCCGGCTCCGGCCTGCCGCATCCCACCCGCGTCACCGTCGAGCTCTACGGCTCGCTGGGCGCTACCGGCCGCGGGCACGCCACCGACCGCGCCACCGTCATGGGCCTGGCCGGCTACGAGCCCGAGACCGTCCCCGCCGTCGTGTGCGAGTCCCTCATGGAGGAGGTCGAGGCCGCCGGCGAGCTGGTGGTCGACGGCGTCGGTCCCATCCCCTTCAGCCCGAGCGCCGACATCCACTTCCTGCCCGGGCGGGTCCTGCCCTACCACGTCAACGGCATGACCCTGACCGCCTACTGCGCCAGCGGCGCCGAAATCCTGCGCCGCACCTACTACTCCGTGGGCGGCGGCTTCGTCATGGAGGACGTCGGCACCCCCGGGGCACCGTCGATCCAGGCCCTGGCGACCGCCTCCGCCTCTCAGGCGCACGCCACCCCGGCGCCCTTCCCCTTCACCACCTCGGCCGCGATGCTGGCGATCTGTGAGCGCGAGGGCCTGAGCGTGTCCGACGTCGTCTTGGCCAACGAGCTCTCCGCCCGCAGCCGCGAGGAGGTCATGGCCTACCTGGACCGGCTGCGGGCCACGATGCGGGCCTGCATCGAGGCCGGCATGAACGCCGAGGGCATCCTGCCCGGCGGGCTCGGGGTGCGACGGCGTGCCAAAGCCCTCCATGAGCGGCTGCGCGCCCAGTCGACCGGCCCGGGTGCCGCCTTCACCATGGCCGACCCCCTGCGCGGCATGGACTGGGTGGACCTGTTCGCGCTCGCGGTCAACGAGGAGAATGCCGCCGGGCGTCGCGTGGTCACCGCCCCCACCAACGGCGCGGCCGGCATCGTCCCGGCGGTCCTGGCCTACTACGAGCGCTTCATCCCCGGGGCCGACGACGACGGCGCCCGCCGCTTCCTGCTGGCCGCCACGGCCGTGGGCGGGCTCATCAAGACCAATGCATCGATCGCGGGGGCCGAGGTGGGCTGCCAGGGGGAGGTCGGCTCGGCCTCCTCGATGGCGGCCGCCGGCCTGGCCGAGGCCTTGGGTGGGACGCCCGCCCAGGTTGAGAACGCCGCCGAGATCGCCATGGAGCACAACCTGGGGCTCACCTGCGACCCGGTGGGCGGGCTGGTCCAGATCCCCTGCATCGAGCGCAACGCGGTGGCCGCGGTCAAGGCCATCAACGCTGCCCGTATGGCCCTGTGGGGCGAGGGCCGGCACGCCGTCAGCCTCGACACCGTCATTGAGACGATGCGCCAGACCGGCGAGGACATGCTCGCCAAGTACAAGGAGACCTCCCGCGGCGGCCTGGCCGTCAACGTCGTGGAGTGCTGA","LSVFDLMRIGIGPSSSHTVGPMRAGRAFSRALAEAVRPGGAGASDAECASPAPGSGLPHPTRVTVELYGSLGATGRGHATDRATVMGLAGYEPETVPAVVCESLMEEVEAAGELVVDGVGPIPFSPSADIHFLPGRVLPYHVNGMTLTAYCASGAEILRRTYYSVGGGFVMEDVGTPGAPSIQALATASASQAHATPAPFPFTTSAAMLAICEREGLSVSDVVLANELSARSREEVMAYLDRLRATMRACIEAGMNAEGILPGGLGVRRRAKALHERLRAQSTGPGAAFTMADPLRGMDWVDLFALAVNEENAAGRRVVTAPTNGAAGIVPAVLAYYERFIPGADDDGARRFLLAATAVGGLIKTNASIAGAEVGCQGEVGSASSMAAAGLAEALGGTPAQVENAAEIAMEHNLGLTCDPVGGLVQIPCIERNAVAAVKAINAARMALWGEGRHAVSLDTVIETMRQTGEDMLAKYKETSRGGLAVNVVEC$","L-serine dehydratase","Cytoplasm","L-serine ammonia-lyase","L-serine dehydratase ","L-serine dehydratase 1","","","","","

InterPro
IPR004644
Family

Iron-sulfur-dependent L-serine dehydratase single chain form
TIGR00720	$\"[1-491]T$	sda_mono: L-serine ammonia-lyase

InterPro
IPR005130
Domain

Serine dehydratase alpha chain
PF03313	$\"[203-487]T$	SDH_alpha

InterPro
IPR005131
Domain

Serine dehydratase beta chain
PF03315	$\"[2-179]T$	SDH_beta

","BeTs to 10 clades of COG1760COG name: L-serine deaminaseFunctional Class: EThe phylogenetic pattern of COG1760 is --------EBrhuj-------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-52% similar to PDB:2IQQ The Crystal Structure of Iron, Sulfur-Dependent L-serine dehydratase from Legionella pneumophila subsp. pneumophila (E_value = 1.8E_26);-51% similar to PDB:2IAF Crystal structure of a fragment (residues 11 to 161) of L-serine dehydratase from Legionella pneumophila (E_value = 8.5E_24);","Residues 63 to 240 (E_value = 6.3e-53) place ANA_2265 in the SDH_beta family which is described as Serine dehydratase beta chain.Residues 264 to 548 (E_value = 9.5e-158) place ANA_2265 in the SDH_alpha family which is described as Serine dehydratase alpha chain.","","ammonia-lyase (sdaA)","","1","","","Wed Aug 8 14:01:45 2007","","Wed Aug 8 14:01:45 2007","","","Wed Aug 8 14:01:45 2007","Wed Aug 8 14:01:45 2007","Wed Aug 8 14:01:45 2007","","","","","","Wed Aug 8 14:01:45 2007","Wed Aug 8 14:01:45 2007","","","Wed Aug 8 14:01:45 2007","Wed Aug 8 14:01:45 2007","","","","","yes","","" "ANA_2266","2453684","2451684","2001","6.01","-9.01","76476","ATGATAAGCAAAATCAACGACACAGTTAAAAAATTAACACAAAACTGCATAGAACGGGCGAGAAAGCACCCAACTGGAGTTTCAATCGCCTTTATGTCGATTATCGTCGTCACATTATGCTGTAAGCGCAACCTAATGCCAAATTATTTTTCCGATAAAGATGACGCTGACATCGCCGTCAGAGCGATGTTAACAAACGCTGTCGGACTGCTGGCCTTACTTACATTCACAACCGATAGGTTGTCAAACATTTCCAAGAAGAACCACAATGAAAACTTCATTTTGGGCAATGATGTTGACAGCTTTATGATATTGCGATCGGCTCACACTAGAGTTATTTCTGGGCGCTTTTTTAAATGGGGAGTAATCCTCATTTTTATTCTCCCAATATTAGTCTTCGAATTTCATGCTTCTATATTCTGGGTCGCACCATTCTGGTGGGGACTATTTTCCGTAATCGCATCGCTTCTTGTTTGGAATCTTGTTAGCGTGTTAGAGATATTTGGCACCAATGCGCTATACCCAGAAAACGTGAAATCAAGAATTGCTTCACACCAGCTCGGGAGATGGCTTGAGTTTATTGACAACGCCGTCAAGAATAAAGGAGACGATCCACTATATTCCTATAGTATGCATTCACAGTACTTGGAAACAGCTAGCGGCGCCAAACCGGAGTTTCGGAAAAAATATTTCGAAATTATTAACAACCTAGTGTATGCCGATTATGTTTTCATCGTTTCCAGACAATATACCTCCGATCCTGAACAGCAAGATAATAGAGTAAATGCGTTGCTCGGCTTCATTGCAGGCCGACAAAAGGCTCTCGTTGAACACCTACTCGCTACTCCAAATCTATCCATACAGGCGAAATTATTGGAGTTGATCTGCGATACGGATTCAAAATACTGGAATTACACAACGTTGGCTGACTCTGTCGCTCAAGACCGCAGCAGACCCATCTGCACTGAGGACGAAGTTCCCGAAATCGATCTTACTGCAATTGGGGTATGGCAGTCAAAGGAATCACACGATGAGGTGGATTTAATACCTGCTTTTGTTTACCATAAAATTTCACATGAATTCTCTACGGGTAAAATAAGGCTCACAGCAAACGAAGTGGAAAGGATTGTTAGATCAATCGACAATATCAAGCACCGAAGAACAAAAGAGTACGCAGCACAGCAGTTCGCGGAAGCGCTCATAAAGGCAACAGTTAGTCATAGAACCAGCGACCAGTCGCTACCTAGCGACATCTCTAAAATTTCAACTTTCCGCTTTCTAAACTTCCCGGAATTCATGGATGAGGACGAGAAAATGTGGAAGAATGCCGTGCAATCCGTTAGTGAACGTGCAGTAATTACGAAAAACAAACTTCCAAGTGAAGCAAAAAAGGCTCTTCTACAGAACACCTCTAAAGAATTTCGAATTGCATACCTGTTTTTGACACTGTTTCAACAATCTACATTCTCAATCTCAGAAAACAAGGACCTTCTAGAGTGCCTGTCCAGTATTATTTTGGAGGATTCTAGTGGAAGTACTGGTGAGTGTTTTGAGTGGCTCGATCCAGAAACTCAGGGAATATTCGGCATTCAAAAGATCGACTTCGAAAAAACTAAGGAAGTCGTTTCAAGTTTTCCTACAACTTCAGACAATTTTGATAAGGTGCGTTCTGAGGAATCGCTTGTGTGGCTCTTTGAAGTTTTGACTCGACCTGTCACCTATGACTGGCATGAAGAATTTGAAAGCCGGGGTTTCGGGTCGCTATTCGAATTTAGTACGGTTATACTGTGGAAGGAAGTGGTCTCTAAGGATCAATGGGCAGATTTTGATTTTATGGAAGAGTTTTTAGTTGGCGATTTTTTTAACGATAGTCAAATCAAACCAAACCGCCAAAAAATGGGCGACGCAAAGATGGAAGTAAATAAGGCAGCAAGTACGCTCGAACGACTCGGGAGAACAGAGGATGCTAAAAGACTGCGCCGGTCTATCGACTTGAAGTGA","MISKINDTVKKLTQNCIERARKHPTGVSIAFMSIIVVTLCCKRNLMPNYFSDKDDADIAVRAMLTNAVGLLALLTFTTDRLSNISKKNHNENFILGNDVDSFMILRSAHTRVISGRFFKWGVILIFILPILVFEFHASIFWVAPFWWGLFSVIASLLVWNLVSVLEIFGTNALYPENVKSRIASHQLGRWLEFIDNAVKNKGDDPLYSYSMHSQYLETASGAKPEFRKKYFEIINNLVYADYVFIVSRQYTSDPEQQDNRVNALLGFIAGRQKALVEHLLATPNLSIQAKLLELICDTDSKYWNYTTLADSVAQDRSRPICTEDEVPEIDLTAIGVWQSKESHDEVDLIPAFVYHKISHEFSTGKIRLTANEVERIVRSIDNIKHRRTKEYAAQQFAEALIKATVSHRTSDQSLPSDISKISTFRFLNFPEFMDEDEKMWKNAVQSVSERAVITKNKLPSEAKKALLQNTSKEFRIAYLFLTLFQQSTFSISENKDLLECLSSIILEDSSGSTGECFEWLDPETQGIFGIQKIDFEKTKEVVSSFPTTSDNFDKVRSEESLVWLFEVLTRPVTYDWHEEFESRGFGSLFEFSTVILWKEVVSKDQWADFDFMEEFLVGDFFNDSQIKPNRQKMGDAKMEVNKAASTLERLGRTEDAKRLRRSIDLK$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[27-47]?$ $\"[57-77]?$ $\"[120-140]?$ $\"[146-164]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PS51257	$\"[1-34]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB001285 (Synaptophysin/synaptoporin) with a combined E-value of 1.8e-09. IPB001285F 546-590 IPB001285F 538-582 IPB001285F 537-581 IPB001285F 552-596 IPB001285F 547-591 IPB001285F 532-576 IPB001285F 543-587 IPB001285F 553-597 IPB001285F 541-585***** IPB000817 (Prion protein) with a combined E-value of 8.3e-07. IPB000817A 538-579 IPB000817A 537-578 IPB000817A 539-580 IPB000817A 529-570 IPB000817A 536-577 IPB000817A 547-588 IPB000817A 540-581 IPB000817A 545-586 IPB000817A 528-569 IPB000817A 531-572 IPB000817A 544-585 IPB000817A 542-583 IPB000817A 532-573 IPB000817A 534-575 IPB000817A 523-564 IPB000817A 543-584 IPB000817A 546-587 IPB000817A 530-571 IPB000817A 516-557","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2268","2456717","2455704","1014","10.17","14.59","35897","ATGACCACGACGACAACCTCAACGACGATCTCAACGGCAACCGTGAGCACCTCCCCGGCAGCCTCCTCCGCAGGGTCTCAGGCTCCGACGTCGGACCCCCTGAACACCGGCCGCCTGGCTCCGACCAGTCTCGCCGAGCTCAACGGCGCCGCGGGCCTGCTCACCCGGGTGGACCACAAGTACCTGGTGCCGCTGGAGCGTGCGCAGGAGCTCGTGGGCGGTCTCACCTCCGAGGCTCGGGTCCTGGACATCGACGGGAGGCGCCGCTTCTCCTACGCCTCGACCTACTTCGACACCCCGGGGCTGGAGGCCTTCATGCTCACGGCCCGCAAGCGGCGTCGGCGCTTCAAGGTGCGCACCCGCACCTACCTGGATTCCGGCCTGTGCTTCCTGGAGGTCAAGACCCGCGGCGCGCGCGGCACCACCGTCAAGCGACGCATGGGCTACCACCCCGACGACGCCTCCCGCCTGACCGGCTCGGGTCGTGCCTTCGTGGCCGCCTGCCTGGCGAGCACAGGGGTCACCGGTCCGGCTGCTGCCCGGGATGTCGCCGCCGCGCTGCGGCCGGTGCTGGCCACCACCTATGAGCGCACCACCTTGCACCTGCCTGAGGCTGAGGCCCGGGCCACCATCGACACGTCCCTGACCTGGCGGCGCCTGACTCCGGCGGCACGCGAGAGGACTGCCATCGTTGCTGGTACCCCTCAGGCCCTGCGCCCGGCCCACCTGACCGCGGCCATCGACGACGGCGAGCCGGTGGCGGTGACGGGCCTCGCCGTCGTCGAGACGAAGAATCCGGCCACGCCCTCGCCCGCGGACCGGGCCCTGTGGGATGCCGGGCATCGCCCCGCCCGCATTTCGAAGTACGCCACCGGCATGGCGCTGCTTCACCCCAAGCTCCCCGCCAACCGGTGGTACCGGACCCTGACCCACGAGCTCGCCGACCTGTTCGGCACCGACCGCTCCAGCCTGGAGAGCATCGGCGCCACGAGCCCCACCGTGAGCGCCGCCTGA","MTTTTTSTTISTATVSTSPAASSAGSQAPTSDPLNTGRLAPTSLAELNGAAGLLTRVDHKYLVPLERAQELVGGLTSEARVLDIDGRRRFSYASTYFDTPGLEAFMLTARKRRRRFKVRTRTYLDSGLCFLEVKTRGARGTTVKRRMGYHPDDASRLTGSGRAFVAACLASTGVTGPAAARDVAAALRPVLATTYERTTLHLPEAEARATIDTSLTWRRLTPAARERTAIVAGTPQALRPAHLTAAIDDGEPVAVTGLAVVETKNPATPSPADRALWDAGHRPARISKYATGMALLHPKLPANRWYRTLTHELADLFGTDRSSLESIGATSPTVSAA$","Hypothetical protein","Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2270","2457592","2456783","810","6.90","-0.36","28142","ATGAGCCTGACCACCCTGACCTACATCGCCGCCGACCTGATCGCCCTCGCCGTCCTGGTCGGGGCCCTCTACGCCCCCCGCCACGCACGCAAGGACCTCATGGCCGCCTATATCGGCGTCAACGTGGGCGTCCTGGCAGTCACCCTGCTGCTGTCGACGGCGAGCGTCGCGGCCGGCCTGGGCCTGGGGCTCTTCGGCGTCCTGTCCATCATCCGCCTGCGCTCCACCGAGCTGGCCCAGCACGAGGTCGCCTACTTCTTCGCGGCCCTGGCCCTGGGCCTGCTCGGCGGCATCCAGACCGCACCCATCGGGATGGTGGCGGCCCTCATGGGCACCGTCGTCGCCGCCCTGTGGGTCGGCGACCACCCCGCGCTCATGCGCCGCAACCGTCACCAGGTGATCGTCCTCGACCACGCCATCACCAACGAGACCGCGCTCATCGCGCACCTGGAGCGCACCCTGGGCGGGCAGGTCCGCTCGGTGGAGGTCCAGCGCCTCGACCTGGTCGACGACACCACCACCGTTGACGTCCGCTTCCGGGTGCCGCGCCACACTCCCGCTGAGCTTGAGATCGCTACGGCCTTCGACGACGTCGCCCCTGCCGCGCAGCCTGCCACCGAGCCGACCGCTGCCGTCGCCCGCGAGGCGCAGACCGCCCAGCCCTGGAGCGGCACGCGCCTGAACGCCGCGCAGGCCGGCTCCCGCCCTGAGCCCGTCGAGGCCCAGCCCCTCACCGTGGCGCCGGCCGCCCAGTACGTCACCCGCTCCAGCAGTCAGGTGGCCTCGCCCGCCGCCGTGGCCTCGCGCTGA","MSLTTLTYIAADLIALAVLVGALYAPRHARKDLMAAYIGVNVGVLAVTLLLSTASVAAGLGLGLFGVLSIIRLRSTELAQHEVAYFFAALALGLLGGIQTAPIGMVAALMGTVVAALWVGDHPALMRRNRHQVIVLDHAITNETALIAHLERTLGGQVRSVEVQRLDLVDDTTTVDVRFRVPRHTPAELEIATAFDDVAPAAQPATEPTAAVAREAQTAQPWSGTRLNAAQAGSRPEPVEAQPLTVAPAAQYVTRSSSQVASPAAVASR$","Membrane protein","Membrane, Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[9-27]?$ $\"[37-71]?$ $\"[86-120]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[39-57]?$ $\"[63-83]?$ $\"[92-126]?$	transmembrane_regions

InterPro
IPR002109
Domain

Glutaredoxin
PF00462	$\"[65-123]T$	Glutaredoxin

InterPro
IPR011909
Family

Glutaredoxin-like protein NrdH
TIGR02194	$\"[65-135]T$	GlrX_NrdH: Glutaredoxin-like protein NrdH

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[63-143]T$	no description

","BeTs to 11 clades of COG0695COG name: Glutaredoxin and related proteinsFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0695 is aom-k-y-vdrlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB002109 (Glutaredoxin) with a combined E-value of 1.8e-09. IPB002109A 65-83 IPB002109B 104-138","","","-80% similar to PDB:1R7H NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer (E_value = 4.9E_23);-68% similar to PDB:1H75 STRUCTURAL BASIS FOR THE THIOREDOXIN-LIKE ACTIVITY PROFILE OF THE GLUTAREDOXIN-LIKE PROTEIN NRDH-REDOXIN FROM ESCHERICHIA COLI. (E_value = 4.9E_15);","Residues 65 to 123 (E_value = 2.7e-16) place ANA_2277 in the Glutaredoxin family which is described as Glutaredoxin.","","to [SwissProt Accession Number P47472]","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2278","2460706","2461116","411","8.46","2.11","14776","GTGAGTAGCGGGCCTCTGCTGGTCTACTTCTCCTCCACCTCGGAGAACACGCACCGATTCGTGGGCAAGCTCGGCTTCCCGACGGCGCGCATCCCCTTGAGGCGCACGGACCCGCCGCTGACCGTGGATGAGGAGTACGTCCTAGTCGTGCCCACCTACGGTGGCGGCTCCGTCAAGGGAGCGGTGCCCAAGCAGGTCATCGCCTTCCTCAACAACCCGGACAACCGGGCCCTGTGCCGGGGCGTCATCGCCTCGGGCAACACCAACTTCGGCCAGGCCTACTGCCTGGCGGGTGACATCATCGCCAGCAAGCTGGGGGTGCCGTTCCTGTACCGCTATGAGCTGCTCGGCACCCCCACGGACGTCGCACGCGTCAAAGAAGGATTGGAAGACTTTTGGCAGACACGCTGA","VSSGPLLVYFSSTSENTHRFVGKLGFPTARIPLRRTDPPLTVDEEYVLVVPTYGGGSVKGAVPKQVIAFLNNPDNRALCRGVIASGNTNFGQAYCLAGDIIASKLGVPFLYRYELLGTPTDVARVKEGLEDFWQTR$","NrdI protein","Periplasm, Membrane","nrdI protein","K03647 protein involved in ribonucleotide reduction","NrdI protein","","Torrents E., Roca I., Gibert I. Corynebacterium ammoniagenes class Ib ribonucleotide reductase: transcriptional regulation of an atypical genomic organization in the nrd cluster. Microbiology 2003. 149:1011-1020. PMID: 12686643","","","

InterPro
IPR004465
Family

Ribonucleotide reductase Class Ib, NrdI
PF07972	$\"[8-127]T$	Flavodoxin_NdrI
TIGR00333	$\"[8-135]T$	nrdI: nrdI protein

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[7-136]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 127 (E_value = 1.2e-74) place ANA_2278 in the Flavodoxin_NdrI family which is described as NrdI Flavodoxin like.","","protein (nrdI)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2279","2461137","2463257","2121","5.85","-13.75","79751","GTGTCCTCCCCGGAGCTGGACTACCACGCGCTCAACGCGAAGCTGAACCTCTACGACGCGGAGGGCAGAATCCAGTTCGACGCCGACCATGAGGCGGCTCGGCAGTACTTCCTCCAGCACGTCAACCAAAACACGGTCTTCTTCCACGACCTGGAGGAGAAGCTCGAGTACCTGGTTGAGGAGGGCTACTACGAGGGTCACATCCTGGACAAGTACTCCCCGGAGTTCGTCAAGTCCGCCTTCAAGGCCGCCTACGCCCACAAGTTCCGCTTCGAGACCTTCCTGGGCGCCTTCAAGTACTACACGTCCTACACGCTCAAGACCTTCGACGGGAAGCGCTACCTGGAGCGTTTCGAGGACCGCGTCACCATGGTGGCCCTCACCCTGGCCAACGGCGTTGAGCGGCTGGCCCTCGACCTCGTCGACGAGATGATGTCCGGCCGCTTCCAGCCGGCCACCCCCACCTTCCTCAACGAGGGCAAGGCCCAGCGAGGGGAGCCCGTCTCCTGCTTCCTCGTGCGCATCGAGGACAACATGGAGTCGATCGCCCGTGGCATCAACTCCGCCCTCCAGCTGTCCAAGCGCGGCGGGGGAGTGGCCCTCCTGCTGAGCAACCTGCGGGAGATGGGCGCCCCCATCAAGCGCATCGAGAACCAGTCCAGCGGCGTCATCCCCGTCATGAAGCTGCTGGAGGACTCCTTCTCCTACGCCAACCAGCTCGGTGCCCGCCAGGGTGCGGGGGCTGTGTACCTGCACGCCCACCACCCCGACATCATGCGCTTCCTGGACACCAAGCGTGAGAACGCCGACGAGAAGATCCGCATCAAGACCCTCTCGCTGGGCGTCGTCATCCCGGACATCACCTTCGAGCTGGCCCGCAACAACGAGGACATGTACCTCTTCAGCCCCTACGACGTCGAGCGCGTCTACGGCATGCCCTTCGCGGACATCAACGTCACCGAGAAGTACCGCGAGATGGTGGACGACGGGCGCATCAAGAAGAAGAAGATCAACGCCCGCACCTTCTTCCAGACTCTGGCCGAGATCCAGTTCGAGTCCGGCTACCCGTACGTCATGTTCGAGGACACGGTCAACAAGGCCAACCCCATCAAGGGCAAGGTCGTCATGTCCAACCTGTGCTCCGAGATCCTGCAGGTCTCCGAGCCCAGCGAGCTCAACGAGGACCTCACCTACGCCCACGTGGGTAAGGACATCTCCTGCAACCTGGGCAGCCTCAACATCGCCAAGACGATGGACTCCCCGGACTTCGCCCGCACGATCCGCACCGCCGTGCGCGGCCTGACCGCCGTCAGCGACCAGACCCACCTGCCCAGCGTGCCCTCCATTGACCGGGGCAACCACGAGTCGCACGCCATTGGCCTGGGGCAGATGAACCTCCATGGTTTCCTGGCGCGCGAGCGCATCCACTACGGCTCCGAGGAGGGCCTGGACTTCACCAACGTCTACTTCGCCAGCGTCCTGTTCGCCGCCCTGACGGCGTCGAACGAGATGGCCGTGGAGCGCGGGGAGAGCTTCGTGGGCTTCGAGGACTCGACCTACGCCAGCGGCGAGTTCTTCGAGAAGTACGTAACCCAGGACTTCGTGCCGGTCACCGAGCGCGTCAAGGAGATCTTCGCAGCCTCCAGCGTGCACGTTCCCACGCGTGAGGACTGGGCCGAGCTGGCGGAGAAGATCAAGAAGGGCGGCCTGTACAACCGCAACCTGCAGGCCGTGCCGCCCACCGGCTCGATCTCCTACATCAACAACTCCACCTCCTCGATCCACCCGATCGTGGCCAAGGTGGAGATCCGCAAGGAGGGCAAGATCGGCCGCGTCTACTACCCGGCGCCCTTCATGACGAATGACAACCTCGAGTACTACCGGGACGCCTACGAGATCGGCCCGGAGAAGATCATCGACACCTACGCCGTGGCCACCCAGCACGTGGATCAGGGGCTGAGCCTCACGCTGTTCTTCCCGGACACGGCCACCACCCGCGACGTCAACCGCGCCCAGATCTACGCCTGGCGCAAGGGAATCAAGACCCTCTACTACATCCGCCTGCGTCAGGCCGCCCTAACCGGAACCGAGGTCGAGGGCTGCGTCTCCTGCATGCTGTGA","VSSPELDYHALNAKLNLYDAEGRIQFDADHEAARQYFLQHVNQNTVFFHDLEEKLEYLVEEGYYEGHILDKYSPEFVKSAFKAAYAHKFRFETFLGAFKYYTSYTLKTFDGKRYLERFEDRVTMVALTLANGVERLALDLVDEMMSGRFQPATPTFLNEGKAQRGEPVSCFLVRIEDNMESIARGINSALQLSKRGGGVALLLSNLREMGAPIKRIENQSSGVIPVMKLLEDSFSYANQLGARQGAGAVYLHAHHPDIMRFLDTKRENADEKIRIKTLSLGVVIPDITFELARNNEDMYLFSPYDVERVYGMPFADINVTEKYREMVDDGRIKKKKINARTFFQTLAEIQFESGYPYVMFEDTVNKANPIKGKVVMSNLCSEILQVSEPSELNEDLTYAHVGKDISCNLGSLNIAKTMDSPDFARTIRTAVRGLTAVSDQTHLPSVPSIDRGNHESHAIGLGQMNLHGFLARERIHYGSEEGLDFTNVYFASVLFAALTASNEMAVERGESFVGFEDSTYASGEFFEKYVTQDFVPVTERVKEIFAASSVHVPTREDWAELAEKIKKGGLYNRNLQAVPPTGSISYINNSTSSIHPIVAKVEIRKEGKIGRVYYPAPFMTNDNLEYYRDAYEIGPEKIIDTYAVATQHVDQGLSLTLFFPDTATTRDVNRAQIYAWRKGIKTLYYIRLRQAALTGTEVEGCVSCML$","Ribonucleoside-diphosphate reductase, alpha subunit","Cytoplasm","Ribonucleoside-diphosphate reductase alphachain(Ribonucleotide reductase R1 subunit)","ribonucleoside-diphosphate reductase alpha chain ","ribonucleoside-diphosphate reductase, alpha subunit","","Uhlin U., Eklund H. Structure of ribonucleotide reductase protein R1. Nature 1994. 370(6490):533-539. PMID: 8052308","","","

InterPro
IPR000788
Domain

Ribonucleotide reductase large subunit, C-terminal
PR01183	$\"[243-262]T$ $\"[374-385]T$ $\"[418-441]T$ $\"[457-479]T$ $\"[485-508]T$ $\"[569-596]T$	RIBORDTASEM1
PTHR11573	$\"[148-706]T$	RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN
PF02867	$\"[168-690]T$	Ribonuc_red_lgC
PS00089	$\"[558-580]T$	RIBORED_LARGE

InterPro
IPR013346
Domain

Ribonucleoside-diphosphate reductase, alpha subunit
TIGR02506	$\"[94-689]T$	NrdE_NrdA: ribonucleoside-diphosphate reduc

InterPro
IPR013509
Domain

Ribonucleotide reductase large subunit, N-terminal
PF00317	$\"[90-164]T$	Ribonuc_red_lgN

InterPro
IPR013554
Domain

Ribonucleotide reductase N-terminal
PF08343	$\"[8-89]T$	RNR_N

noIPR
unintegrated

unintegrated
G3DSA:3.90.244.10	$\"[398-691]T$	no description
PTHR11573:SF4	$\"[148-706]T$	RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE, ALPHA SUBUNIT, GROUP I INTRON- CONTAINING

","No hits to the COGs database.","***** IPB013554 (Ribonucleotide reductase N-terminal) with a combined E-value of 0. IPB013554A 25-68 IPB013554B 84-132 IPB013554C 133-172 IPB013554D 173-212 IPB013554E 236-281 IPB013554F 282-316 IPB013554G 317-344 IPB013554H 366-420 IPB013554I 453-497 IPB013554J 512-546 IPB013554K 571-610 IPB013554L 630-669 IPB013554M 670-697***** IPB000788 (Ribonucleotide reductase large subunit) with a combined E-value of 6.8e-40. IPB000788D 192-237 IPB000788E 238-274 IPB000788G 374-383 IPB000788J 557-596 IPB000788K 676-685***** IPB013678 (Ribonucleotide reductase class II vitamin B12-dependent) with a combined E-value of 1.2e-06. IPB013678D 178-227 IPB013678H 442-492 IPB013678L 631-674","","","-44% similar to PDB:4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI (E_value = 3.5E_41);-44% similar to PDB:2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI (E_value = 1.0E_40);-44% similar to PDB:3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI (E_value = 1.0E_40);-41% similar to PDB:1ZYZ Structures of Yeast Ribonucloetide Reductase I (E_value = 1.3E_40);-41% similar to PDB:1ZZD Structures of Yeast Ribonucleotide Reductase I (E_value = 1.3E_40);","Residues 8 to 89 (E_value = 1.1e-43) place ANA_2279 in the RNR_N family which is described as Ribonucleotide reductase N-terminal.Residues 90 to 164 (E_value = 1.4e-24) place ANA_2279 in the Ribonuc_red_lgN family which is described as Ribonucleotide reductase, all-alpha domain.Residues 168 to 690 (E_value = 1.1e-206) place ANA_2279 in the Ribonuc_red_lgC family which is described as Ribonucleotide reductase, barrel domain.","","reductase alpha chain(Ribonucleotide reductase R1 subunit) (l34407)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2279.1","2463290","2463829","540","8.45","4.51","20703","GTGAACGAGTGGGATGAGAGTCAGCCCTACCGGGTGTTTGTTGACGAATCTGAGGTCAGTGGATACTCCATAACGGCTGTCTATGTGCGACCGCAAGATGTTCACAAGATCAGGACTGTGCTTCGTAAGCATCTGCGTTCGGGACAGCGCTCCATCCACTTCACTAAAGAGCGGCCGGAAGTACGTAAGGCCGTGATAGCAGACATAGCTAAGATGCCGATCAAGGCTGAACTTTACAAAGTCGCGGAGAAACATCGGGAAGCTCGTTCAATATGCCTGCAAGCGTTGGCTGAGACTCTGCGGGACGGGAAGTGCCAACAACTGGTTCTCGACCAGAATGACTCGGTTTGTCAGTCTGACCGGAGAGTCCTACGCAGTGCCCTTGGCCCTGGCTGGAGCGGTACGTACGACCACTTCCACGATCATGAGGAGGCTCTCCTGTGGCTACCGGATGCCATCAGCTGGTGCTGGAATAAGGGAGGGAACTGGCGAGCCAGGCTCTCTGAGATGGATCTCAAGATTGTGCCGTTGGCTAGATGA","VNEWDESQPYRVFVDESEVSGYSITAVYVRPQDVHKIRTVLRKHLRSGQRSIHFTKERPEVRKAVIADIAKMPIKAELYKVAEKHREARSICLQALAETLRDGKCQQLVLDQNDSVCQSDRRVLRSALGPGWSGTYDHFHDHEEALLWLPDAISWCWNKGGNWRARLSEMDLKIVPLAR$","Hypothetical protein","Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:14:21 2007","Wed Aug 15 19:14:21 2007","Wed Aug 15 19:14:21 2007","Wed Aug 15 19:13:22 2007","","","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","Wed Aug 15 19:13:22 2007","","Wed Aug 15 19:13:22 2007","","Wed Aug 15 19:13:22 2007","yes","","" "ANA_2280","2465066","2464020","1047","9.35","6.81","36531","ATGACACCCCCGACAGACACTGACGTAGTCACCGATGCAGCCGCCGAGAAGAGACAGGACCGCAGCGCCCGCATTGCGGTGACGGTCTTCCCGCTCATCATGTTCGGCGCCTTCCTCGCCGCCTTCTTCTCGCCCTCCACCTTCGTGCCGCTGGCCGGCTACATGACGCCGTTGCTGGCCGTCACGATGCTGGGAATGGGGATGACCCTGTCCATCCCGGACTTCACGATGATCGCTCGTCACCCGAAGCCGGTCATTCTGGGTGTGCTCAGCCAGTACGCGGTCATGCCGCTGGTTGGTTGGAGCGTGGCGAACCTGCTGCCGCTGTCCCCCGAGCTCAAGGTGGGCATCATCCTCATCGGCTGCGTGCCCGGAGGGACGACGTCGAACGTGGTCAGCTACCTGGCCAAGGGCAACACGGCCCTTTCGGTGTCGATGACCGCCTTCTCCACGATGCTCGCCCCGATCGTCACCCCGTTGCTGACCCTGTGGCTGGCCGGGACCTACATGCAGGTGCCAGCCGGGTCGATGGCACTGTCGATTGTGCAGATCGTGCTGCTGCCGGTGGGTGCGGGCCTGGCCTGCAATGTCTTCTTCCACCGGCAGGTGGCACGGATCCAGCCGGCGATGCCGTGGGTCTCGGTTGTGGCGATCGCCGCGGTGGTGGCGGCCGTGGCCTCCAAGAGCCAGCCGCTCATCGCCACCGCGGGGCCGCTCATGTTCGCAGCGATCGCCTTGGAGAATGCGACCGGCTACGCCCTGGGTTACGCCGTGGCGCGGGCCTTCGGCGTCTCGCGGGCCGACCGACGCACGATCGGTATCGAGGTGGGCCTGCAGAACGCGGGGCTCGGTTCGACGCTTGCCCTGCAGTACCTGAGCGCGGCGGTGGCCGCGCCCTGCGCGGTGGCGACCTTCTGGCACACGATCACCGGTTCCCTGCTGGCCATGTACTGGCGCCTGCGCGGGTTCCCGGCCGGAGAGGATCCGCACGCCACCGTGCGCGAACTGCGCCGTCGTGCCGAGGAGTCGTCACCTGCAGAACGTTGA","MTPPTDTDVVTDAAAEKRQDRSARIAVTVFPLIMFGAFLAAFFSPSTFVPLAGYMTPLLAVTMLGMGMTLSIPDFTMIARHPKPVILGVLSQYAVMPLVGWSVANLLPLSPELKVGIILIGCVPGGTTSNVVSYLAKGNTALSVSMTAFSTMLAPIVTPLLTLWLAGTYMQVPAGSMALSIVQIVLLPVGAGLACNVFFHRQVARIQPAMPWVSVVAIAAVVAAVASKSQPLIATAGPLMFAAIALENATGYALGYAVARAFGVSRADRRTIGIEVGLQNAGLGSTLALQYLSAAVAAPCAVATFWHTITGSLLAMYWRLRGFPAGEDPHATVRELRRRAEESSPAER$","Bile acid:sodium symporter","Membrane, Cytoplasm, Extracellular","Predicted Na+-dependent transporter","K03453 bile acid:Na+ symporter; BASS family","Bile acid:sodium symporter","","Hagenbuch B., Stieger B., Foguet M., Lubbert H., Meier P.J. Functional expression cloning and characterization of the hepatocyte Na+/bile acid cotransport system. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(23):10629-10633. PMID: 1961729Bobrowicz P., Wysocki R., Owsianik G., Goffeau A., UBaszewski S. Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Yeast 1997. 13(9):819-828. PMID: 9234670","","","

InterPro
IPR002657
Family

Bile acid:sodium symporter
PTHR10361	$\"[21-320]T$	SODIUM-BILE ACID COTRANSPORTER
PF01758	$\"[56-236]T$	SBF

noIPR
unintegrated

unintegrated
signalp	$\"[1-41]?$	signal-peptide
tmhmm	$\"[25-45]?$ $\"[51-73]?$ $\"[85-105]?$ $\"[115-135]?$ $\"[145-165]?$ $\"[179-199]?$ $\"[209-227]?$ $\"[287-309]?$	transmembrane_regions

","BeTs to 6 clades of COG0385COG name: Predicted Na+-dependent transporterFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0385 is ------yq--r-bcef---n-j----Number of proteins in this genome belonging to this COG is 1","***** IPB002657 (Bile acid:sodium symporter) with a combined E-value of 2.7e-16. IPB002657A 92-105 IPB002657B 173-208 IPB002657C 270-287","","","No significant hits to the PDB database (E-value < E-10).","Residues 56 to 236 (E_value = 4.9e-52) place ANA_2280 in the SBF family which is described as Sodium Bile acid symporter family.","","Na+-dependent transporter (E1117)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2281","2465958","2465263","696","4.87","-14.59","24910","GTGGGCGAGACCTCCGCCCTTGTCAGCAACCTCGTCAACCAGCTCGTACAGCGGTTGGCGGCCGACGACGCGCCCGAGCGCCTCGTCGTCGGGCTCGCGGGTGCTCCCGGTTCGGGAAAATCAACGATTGCCGAGCAGCTGAAGACCGGGTTGAAAGCAGCGGGCATTTTCGCTGGGCTGGTTGCCATGGACGGCTTCCACCTGTCCAACGCCGTCCTGGACGAGCTGGGGCGCCGCAACCGCAAGGGTGCGCCGGACACCTTCGACGTCGAGGGCTACCTGACGATCCTGGACCGGGTGCGGACCGACGGCGCCCCTCGGGTCCTCGTCCCGGTGTACCGGCGCGATCTTCACGAGGCCGTGGCAGCCGGGAGCATCGTCAGCGGCACCGGCGTCGTCGTCACTGAGGGCAACTACCTCGCGCTGGAGACGCGCGGTTGGGGTGCGGCGCGTGAGCGGATCGACCTGCTCATCCACATTGACGTGCCCGAGGAGGTGCTCGTGCCGCGGCTCATCAACCGGCACGAGGACTTCGGTAAGAACCCGATCGCGGCCGGCCACTGGGTGCGCACCGTGGACCTGCCCAATGCTCGCCTCATCGCCACAAGCGTCCACCGCTGCGACGAGGTCTGGCGTGACCCCGAGGACGACGACGAGTCCGACGTCGTCGACGACGCCGACGACGACCTCGAGTAG","VGETSALVSNLVNQLVQRLAADDAPERLVVGLAGAPGSGKSTIAEQLKTGLKAAGIFAGLVAMDGFHLSNAVLDELGRRNRKGAPDTFDVEGYLTILDRVRTDGAPRVLVPVYRRDLHEAVAAGSIVSGTGVVVTEGNYLALETRGWGAARERIDLLIHIDVPEEVLVPRLINRHEDFGKNPIAAGHWVRTVDLPNARLIATSVHRCDEVWRDPEDDDESDVVDDADDDLE$","Panthothenate kinase","Cytoplasm","frcK protein","hypothetical protein","Panthothenate kinase-like","","Attwood T.K., Findlay J.B. Fingerprinting G-protein-coupled receptors. Protein Eng. 1994. 7(2):195-203. PMID: 8170923Birnbaumer L. G proteins in signal transduction. Annu. Rev. Pharmacol. Toxicol. 1990. 30:675-705. PMID: 2111655Casey P.J., Gilman A.G. G protein involvement in receptor-effector coupling. J. Biol. Chem. 1988. 263(6):2577-2580. PMID: 2830256Attwood T.K., Findlay J.B. Design of a discriminating fingerprint for G-protein-coupled receptors. Protein Eng. 1993. 6(2):167-176. PMID: 8386361","","","

InterPro
IPR000276
Family

Rhodopsin-like GPCR superfamily
PS00237	$\"[194-210]?$	G_PROTEIN_RECEP_F1_1

noIPR
unintegrated

unintegrated
PD135248	$\"[28-96]T$	Q750K6_ASHGO_Q750K6;
G3DSA:3.40.50.300	$\"[10-226]T$	no description

","BeTs to 5 clades of COG1072COG name: Panthothenate kinaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1072 is ----------rlb-e-gh---j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein (AF196574)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2282","2466251","2469202","2952","4.90","-32.88","100749","ATGAGATTTTCGCCATTGATACCAGTAAATATAGAACTTAAGTTCGCCACCGCATCAATTGAGTGCCGGACTTCTCCCGAAAGGTTTGCCGTGTCAAAGATCCCTGCCCCCAGAGCGCTCAGAGCGCCTGTGCGTGCCACAGGTGCTCTCCTCCTGCTCGTGGTCATGGTTGCCGCGATGCTGACGGTCCTGCCCATGCAGGCCCGAGCCGCCATCAACCCGAAGATCACCATCTCCGACCTGTCACTGACCCCCTCCAACGCCACCGGCGAGGAGGACCCGAGCAAGACCGCGATCCAGAGCGGTGACTACCTCAAGCTGAAGTTCAGCTGGGATGCCAGCAAGGCCAACGCCAAGAGTGGGGACTCCTTCGAGATCGCACTGCCCGAGCAGGTCCGCAGCAAGGACAAGCTCACCGAGCCGATGATGCTCAACCACGATGGCGTCAGCACGAAGGTGGGTGAGTGCTCGGTGGCTGAGCGCACGATCACCTGCACCTTCAACAGTGAGCTCGACAAGATCGTCGCCCAGGGCTTCAAGGACCTGCGTGGAAACGGGGCGTCGCTGGTGGTGGCTAACGGGGCCTCGGATCTGCCCAACCTGCCGGTCAAGGCCAACGGTGCGGACACTACTGTGGCCGTTCCCGGCGGGAAGATTGCCCCCTACGTCGAGGGCCCCTACAAGCCGGAGAAGGTCACCAAGTGGGCCAGCGACCTGAATGTCGACTCCGACAAGATTGCCTGGCAGCTGATCTTCGGCCCCGACCAGATCAAGGCGGCGCTGGAGGAGAACGGCCAGTCTCTGAGCGTGGACGGCAAGACCCGCTCGACCATCATGTTCACCGACGAGCTCGGCCCCGGACAGAAGTACGTTGCCGACAAGGCGAAGTGGAGGCTGGAGACCGGCACCGCTGAGGGCAAGAACGCCAGTTCCGTCCAGCTCACGGACGCTGCCGGAACGGACCAGAACACCAGCGCGGGCGACTTCGACCTCGATGTCACCTTCAACGGCGACGTCGCCTTCATCAAGGTGACCGGTCCCTTCGCGCCGCGTAGCAACTACATCGTCCGCTACGAGTCGACCCCTGAGACCGGCAACGGCAAGGTGCAGCCCGGTGTGCGGTACAAGAACGACGCCACCGCGCTGGGAACCAGCTTGCGGGGCTCCTACGCGGTGCACTACGCCTCGTCCTTCTCCATCAACGTCGAGATGAAGCCCGGATTCGGTGGATTCGAGATCACCAAGCTCCTCACCGGAACGCAGACCGGCAAGGTGCCGGCGGACACCACCTTCAAGGTCAGTGTCCACTACGACCTGCCCGGCGGTGCGAAGGCCAGCGCCTACCCGGACTGGAAGGCCCCGGGCACCCTCAACCAGGAGGGTACTGGTGGCGACCTCGAGATGACCCTTGGCATCGGTGCCAAGACCGTGTTCAAGGACATCTTCCCCGTTGGAACGGTCCTCACATTCAACGAGGACCCCACGAATGCCTCGGCTACTCCCGAAGGTGTCGTCTGGGGCAAGCCGGCCTTCACGGTGAACGGTCAGAGCGCCAGCACCGCGACCATCGCGGACCAGGAGCTCACGCCCGTGACACTGAGCAACTCCGCTGACGCCGTGCCCGTGGATCACGGTGACTTCACGATCACGAAGGCCCTGGCCGGCGAAGGCGACTTCAGCAACTCCACCTTCCTGTTCACCTACAGCTGCACTGACAACACCACGGGCTTCCTGATGGTGAAGGGCGGGAAGACCTCGGAGCACTCCGAGGAGGTCCAGGCGGGCTCGACCTGCACCGTCACCGAGATCACCGACTCCGCCTTCCGGGCGGGGTACACGCTGACCGCCCCGGAGCCGCAGACCGTCGCCATCGTCAAGGATGAGACGGCTGAGGTGACGATGACCAACACCTACACGAAGGCCAAGGGCTCGTTCTCGGTGACCAACACAGTCAAGGGCGCCGAGGTCGGGGACAAGGAGTTCACCTTCACCTACACCTGCGACAACGGGCAGAAGGGCGACCTCAAGGTCAAGGCCGATGGCACGGCAGTGAACGGTCCGGAGCTGCCCGTGGGCACTGAGTGCACCATTGAACAGGACGTGGACAAGGCTCAGGTCGACGGGTACACCCTCAAGGCCCCCGCGTCTCAGAAGGTGACTATTGGCGAGAAGGTGCTGGACCTGAAGTTCGCTGGTATGTACGCCTCTCTCAATGTTCCGACGCCGAGCGCTGAGGCGACTGCGAAGCCTTCCGCCGAGCCGAGTGCTGCGCCGAGTGCCGCTCCGACTGAGAAGCCGGCCGCTGACGCCAGTGCGGACCCGAACGCCAAGCCCAGTGCTGAGGCGAGCGCCAAGCCGAGTGCTGAGGCCAGTGCGGACCCGGCTGACAAGCCCGCTGCCGACGCCAGCGCGGACCCGAACGCCAAGCCCAGTGCTGAGGCGAGCGCCAAGCCGAGTGCTGAGGCCAGTGCGGACCCGGCTGACAAGCCCGCTGCCGACGCCAGCGCGGACCCGAACGCCAAGCCCAGTGCTGAGGCGAGCGCCAAGCCGAGTGCTGAGGCCAGTGCGGACCCGGCTGACAAGCCGGCCGCAGACGCCAGCGCAGACCCGAACGCCAAGCCCAGTGCTGACGCGACTGCTGAGTCGACTGAGAAGCCAGCCGATGACGCGAGTGCGGGCTCGACGGACAAGCAGGCCGCTGACGCGGACCCGAACGCCGCGCCCAGCGCCAGTGCGAGCAGCTCCACCGCTGCGGGTGACTCGTCGTCGGACGGCGCGCCTGCACCGGTGACGTCCACTAGCTCGGCGGTGCCGGCCCCGGCTGATGGGGCACCCGGCGGTCCTGCGGGGGGCCCGTTGGCCAGCACCGGTGTCAGGATCGGCCTGCCTCTGGGCATCGCCGTGGTCGCCGTGATGGGAGGGGCTCTGCTGGTGAGCCGCCGCCGCGCCTGA","MRFSPLIPVNIELKFATASIECRTSPERFAVSKIPAPRALRAPVRATGALLLLVVMVAAMLTVLPMQARAAINPKITISDLSLTPSNATGEEDPSKTAIQSGDYLKLKFSWDASKANAKSGDSFEIALPEQVRSKDKLTEPMMLNHDGVSTKVGECSVAERTITCTFNSELDKIVAQGFKDLRGNGASLVVANGASDLPNLPVKANGADTTVAVPGGKIAPYVEGPYKPEKVTKWASDLNVDSDKIAWQLIFGPDQIKAALEENGQSLSVDGKTRSTIMFTDELGPGQKYVADKAKWRLETGTAEGKNASSVQLTDAAGTDQNTSAGDFDLDVTFNGDVAFIKVTGPFAPRSNYIVRYESTPETGNGKVQPGVRYKNDATALGTSLRGSYAVHYASSFSINVEMKPGFGGFEITKLLTGTQTGKVPADTTFKVSVHYDLPGGAKASAYPDWKAPGTLNQEGTGGDLEMTLGIGAKTVFKDIFPVGTVLTFNEDPTNASATPEGVVWGKPAFTVNGQSASTATIADQELTPVTLSNSADAVPVDHGDFTITKALAGEGDFSNSTFLFTYSCTDNTTGFLMVKGGKTSEHSEEVQAGSTCTVTEITDSAFRAGYTLTAPEPQTVAIVKDETAEVTMTNTYTKAKGSFSVTNTVKGAEVGDKEFTFTYTCDNGQKGDLKVKADGTAVNGPELPVGTECTIEQDVDKAQVDGYTLKAPASQKVTIGEKVLDLKFAGMYASLNVPTPSAEATAKPSAEPSAAPSAAPTEKPAADASADPNAKPSAEASAKPSAEASADPADKPAADASADPNAKPSAEASAKPSAEASADPADKPAADASADPNAKPSAEASAKPSAEASADPADKPAADASADPNAKPSADATAESTEKPADDASAGSTDKQAADADPNAAPSASASSSTAAGDSSSDGAPAPVTSTSSAVPAPADGAPGGPAGGPLASTGVRIGLPLGIAVVAVMGGALLVSRRRA$","PT repeat-containing protein","Extracellular, Periplasm, Membrane","PT repeat family","putative surface-anchored membrane protein","PT repeat-containing protein","","Sivaraman J., Li Y., Larocque R., Schrag J.D., Cygler M., Matte A. Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate. J. Mol. Biol. 2001. 311(4):761-776. PMID: 11518529","","","

InterPro
IPR001917
Binding_site

Aminotransferase, class-II
PS00599	$\"[548-557]?$	AA_TRANSFER_CLASS_2

InterPro
IPR006970
Repeat

PT repeat
PF04886	$\"[741-776]T$ $\"[785-820]T$ $\"[821-852]T$	PT

noIPR
unintegrated

unintegrated
tmhmm	$\"[48-68]?$ $\"[960-978]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 741 to 776 (E_value = 0.0049) place ANA_2282 in the PT family which is described as PT repeat.Residues 777 to 812 (E_value = 812) place ANA_2282 in the PT family which is described as PT repeat.Residues 785 to 820 (E_value = 9.8e-05) place ANA_2282 in the PT family which is described as PT repeat.Residues 817 to 852 (E_value = 0.0026) place ANA_2282 in the PT family which is described as PT repeat.","","repeat family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2283","2470470","2471414","945","7.89","2.09","34352","ATGAGTGTGCGACGTCGTCAGGTCCTGGCCGTAACGGCCGCATCCCTTGCTCTCGCAGTGGCCGGGTGCTCGCCCATGGCCATGGCGCGCAAGAGACGGAAGCGGAAGGTGCAGCAGTACCTCTCCGGGCTCGACGCCGTGGCATCCGCACGGGTGGAGGTGCACCCGGAGTTCTCAGAGCCGGATCGTTGGATTGTGGACGTGCGGCTCAAGGATGATCCGTCTGTGGGATCGGTGTCGTCAGTTGTGCGGGACGCCTACGCCGAGGTGCTGCGCCTGACCGGGGCCAGTGAGGTGAGGATGGTTGTCACCTGGGCCCAGGCTAAGGTCTCCGTCTTCTGCTACCTGCCGATGAAGGATGCCGATAAGGCTGCCTCCGCCACGGTGGAGGCGTTATCGCCCGGCATGGAGCGAGTCCAGATCGAGGAGGAAAGAATCTCCTTCGAGTACCGGACTACTGAGACCCTCCCGGATCATTTTATCCTGCCGCCCAGCTCTGCGGTGCTGCGCCTCGGCTCCCTGAGGGTCGAGCAGAGCATTCTGATTGGACGGTCTCACTGCTTCATCTCCCACGCCAAGGGTAAGGACCTCACATCTGTGCCGGTCAAGCGTGCACTGGAAACCATTCCCTCCGACAAGCGGTACGGAGCGGTCCTGAGCCTGGAGGCGGAGGATTATAACAGTCACCAGGCCCGTCTCATATTCAAGAAATGGGTCAATGACTGGCAGGATGAGGATGTTCAGGCCGACGCTGCGGTTCTTGCCACAGTCCTCGGTAACCAGGTGCTCCAGAGGGTGGAGCTGCTTACCTCGGTGGAAAGCAAGGTCCAGCCCAGGGTGGTTGGCTTTGACATGAAGTCCGGCACTGTGGTCGGCCAGGGAGATCCGCCTGAGAAGGGGGCGCCCATCCTTGCCGCGGCCCAGCAGCCGGACGCTTCGTCGTAA","MSVRRRQVLAVTAASLALAVAGCSPMAMARKRRKRKVQQYLSGLDAVASARVEVHPEFSEPDRWIVDVRLKDDPSVGSVSSVVRDAYAEVLRLTGASEVRMVVTWAQAKVSVFCYLPMKDADKAASATVEALSPGMERVQIEEERISFEYRTTETLPDHFILPPSSAVLRLGSLRVEQSILIGRSHCFISHAKGKDLTSVPVKRALETIPSDKRYGAVLSLEAEDYNSHQARLIFKKWVNDWQDEDVQADAAVLATVLGNQVLQRVELLTSVESKVQPRVVGFDMKSGTVVGQGDPPEKGAPILAAAQQPDASS$","Hypothetical protein","Periplasm, Membrane, Cytoplasm","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[9-29]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[83-103]?$	transmembrane_regions

InterPro
IPR000358
Family

Ribonucleotide reductase
PTHR23409	$\"[7-321]T$	RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN
PF00268	$\"[8-286]T$	Ribonuc_red_sm
PS00368	$\"[102-118]T$	RIBORED_SMALL

InterPro
IPR012348
Family

Ribonucleotide reductase-related
G3DSA:1.10.620.20	$\"[1-296]T$	no description

InterPro
IPR013233
Family

PIG-X/PBN1
SM00780	$\"[179-317]T$	no description

noIPR
unintegrated

unintegrated
PTHR23409:SF5	$\"[7-321]T$	RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN

","BeTs to 19 clades of COG0208COG name: Ribonucleotide reductase beta subunitFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0208 is -o----yq-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000358 (Ribonucleotide reductase) with a combined E-value of 2.4e-82. IPB000358A 20-73 IPB000358B 87-120 IPB000358C 162-208 IPB000358D 233-245 IPB000358E 258-281 IPB000358F 298-309","","","-86% similar to PDB:1KGN R2F from Corynebacterium Ammoniagenes in its oxidised, Fe containing, form (E_value = 3.8E_140);-86% similar to PDB:1KGO R2F from Corynebacterium Ammoniagenes in its reduced, Fe containing, form (E_value = 3.8E_140);-86% similar to PDB:1KGP R2F from Corynebacterium Ammoniagenes in its Mn substituted form (E_value = 3.8E_140);-86% similar to PDB:1OQU A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes (E_value = 3.8E_140);-88% similar to PDB:1UZR CRYSTAL STRUCTURE OF THE CLASS IB RIBONUCLEOTIDE REDUCTASE R2F-2 SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS (E_value = 1.3E_137);","Residues 8 to 286 (E_value = 1.1e-85) place ANA_2285 in the Ribonuc_red_sm family which is described as Ribonucleotide reductase, small chain.","","reductase, beta subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2286","2473878","2474306","429","4.87","-6.59","15525","ATGACTTCGATCCGGTCGTCCCTCCAGGAGCGGGGCTTCGATGAGTTGGTTGAGCACTCGGCGCGACTCACTCAAGCCGATGACGAGATGCGCTGGGCGCTCATCCAAGCCCGCAAGGAGTCTGGCCTCTCGCAGCGCGACGTTGCCGAGATGATGGGCGTCAAGCAGCCGACAGTTGCCGCCTTCGAGAGTCAAGATAACGATCCTCGGCTCTCCACCCTGCGTCGCTACGCGCTTGCTGTTGGAGCGAGCGTGGAGCATCGCGTCACAACCTGGGGGAGTACGACCTTCGACTCGGAGAGTTGGACGCCCATTCAGACACTTGGTAAAGGGTGGCCTATGGCGGTAGAGGCGAGCGCTGGCGATCCGCTTCTGATCCAAGCCGGGTGCACAGTTCCGCTTGTCGACGACTTTTCTGTGGCTGCATGA","MTSIRSSLQERGFDELVEHSARLTQADDEMRWALIQARKESGLSQRDVAEMMGVKQPTVAAFESQDNDPRLSTLRRYALAVGASVEHRVTTWGSTTFDSESWTPIQTLGKGWPMAVEASAGDPLLIQAGCTVPLVDDFSVAA$","Transcriptional regulator, XRE family","Periplasm, Cytoplasm","Predicted transcriptional regulators","hypothetical protein predicted by Glimmer/Critica","helix-turn-helix domain protein","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[34-88]T$	HTH_3
SM00530	$\"[33-88]T$	HTH_XRE
PS50943	$\"[34-88]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[25-87]T$	no description

","BeTs to 6 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 34 to 88 (E_value = 2.4e-10) place ANA_2286 in the HTH_3 family which is described as Helix-turn-helix.","","transcriptional regulators","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2287","2474303","2474758","456","4.90","-6.82","16735","ATGAGTGCTGATCGGTGTTACGAGACTGCTCGAGACCTGCTCCCAGTTCTCGATCTGAATCGTGTGACGCCCTACGAGGTTGCGGGTAGGCGCGTTTCCGCCCCCGAGGTCACCGAGATAACCAGTTCGATGGAGTCGATGATCGGTGGAGAGGAGGGGAAGTCCTTCGTCTTCAGGGTGCGGCAGCGGGTGAGGACCAGTGAGGCTGAGATTGCCGCTGACTTCGAAGCGGAGTACCGGTTCAGTGAGCCAGGTGGTCGGATCTCGGAGGAGGCTCAGGTCGAGTTCGCTGAGAAGGTGGCTTTCATGGCACTCGTTCCCTACCTCAGGGAGTCAGTCCATACGACTGCCATGCGTCTGGGTGTGCAGCCGCCCCTCCTTGGGATGGTGCGTCAAGGTGAGTTCCGGCTGCGTGCCGACGGCGACGCCGGCTCGAGCGCTGACGTTCAGAATTGA","MSADRCYETARDLLPVLDLNRVTPYEVAGRRVSAPEVTEITSSMESMIGGEEGKSFVFRVRQRVRTSEAEIAADFEAEYRFSEPGGRISEEAQVEFAEKVAFMALVPYLRESVHTTAMRLGVQPPLLGMVRQGEFRLRADGDAGSSADVQN$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","Wed Aug 8 14:31:54 2007","","Wed Aug 8 14:31:54 2007","","","Wed Aug 8 14:31:54 2007","Wed Aug 8 14:31:54 2007","Wed Aug 8 14:31:54 2007","","","","","","Wed Aug 8 14:31:54 2007","","","","Wed Aug 8 14:31:54 2007","Wed Aug 8 14:31:54 2007","","","","","yes","","" "ANA_2288","2474871","2475728","858","5.01","-11.41","30327","GTGCCGCAGGCGACCGGGCGGAGACGGGGAGCGCTCCCCCGGGTAGCCTCCCCATGGCCGAGGGTTCGTGCCTGGCGCACACTTTCGTTGTCCCCAGCGTGCCAGAAAGGAATCCCCATGCGCTCCTCCGTCAAAGCTCTCTCCGTCGTCGCCGCCCTCGCCATGGCTGTCGGACTGTCCGCCTGCGATGAGGAGGAGGTCTCTCAGCCCTCCTCCGGTGGCGCCTCCGCGTCCAGCTCCGCCAAGGCGGACTCGGACGAGTCGGATGCATCCCCCTCTGATGACTCTCAGGAGGACAAGGACTCCAAGGGCTCCAAGGATGACAAGAAATCTCAGGACTCCAAGGGCAAGAGTGGTGAGACCACCAAGTCCGGCTCCACCATTCAGAACATCCAGCCGGTGACCTTCAAGGACGAGGAGATCGGCCTCACCCAGACCTGCGACAAGGTGATCGAGGACTACGCCGCACCGAAGTACAAGGCAAGTCGTGATTCAGACACGGTCTACCTGCTTCACTGCACGCTCGACTTCAGTGGAGATATTGCTTTCAGCAACACGATCGTGGACTCCACCTCGCTCCAGGACAAAACGGAATCCAGGCACAAGGCGGATGAGTACGGGGCGCTGCTGGCCGACGACCTGAAGGATGACGGACTTGAGGTGTTCGACTCCGAGGACTCCGGATCCACGCATGTTGAGGGCTGGGTCTCCATGGCTACCGTCACGGAGTCGACCAAGCTGAAGCCCTTCTCCGAGGGCACCACCAGCATCGTCTACGACCGCGCAGCCGGAAAGGGCATCCAGTCCGGCAAGCAGTACGCGGCCTACTCCGACACCCAGGACCTCGTGCTCAAGTAG","VPQATGRRRGALPRVASPWPRVRAWRTLSLSPACQKGIPMRSSVKALSVVAALAMAVGLSACDEEEVSQPSSGGASASSSAKADSDESDASPSDDSQEDKDSKGSKDDKKSQDSKGKSGETTKSGSTIQNIQPVTFKDEEIGLTQTCDKVIEDYAAPKYKASRDSDTVYLLHCTLDFSGDIAFSNTIVDSTSLQDKTESRHKADEYGALLADDLKDDGLEVFDSEDSGSTHVEGWVSMATVTESTKLKPFSEGTTSIVYDRAAGKGIQSGKQYAAYSDTQDLVLK$","Hypothetical protein","Periplasm, Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2290","2475845","2476657","813","5.04","-8.64","28165","TTGCTCCGTGTCGAAGGAACGAAAGGTACTGTCATGAAATCCACGATCAAGGCTGTTGCAGCGGTGGCCGCCCTGGCCCTGTCTCTTGGCCTGTCAGCCTGCGGAGACCAGGAAGCCGGGACGGACTCGGAGAAATCAAGCCGGGCAACGGCCTCGCAGGCGAGCGATGACAAGTCCCCCGAGGCTGAATCCGACGCGTCAGAGTCAGCCTCGAGCAAGGCATCGAGCAAGGAATCGTCTGCACCCACCGGCTCGGCGTCGAGCTCGAGCAGCGCGAAGGCATCCTCGCCTCAGGGCGGTGAGACGCTGCCCACCGGTGAGAAGGTGGAGAGCATTGATCCCATCGTCATCAAGGACCAGGCGATCGGGCTGACCCAGACCTGCGACAAGATCGTCTACGACTACTCGGCCCCCACCTTCAAGGGGACGGAGAAGGGCAGCCAGGACAAGATCATCCTGCTTCACTGCAAGATGGAGTTCAGCGGCGAGGTCTCCTTCAGCGGCAAGGTCACCGCCTACCAGGAAATCCAGTCCAAGGAGAAGGACTACCTCAACGCTGGAGTGGCGGCGTCCCTGGTCGAGCAGGACCTCAAGGACGCCGGTCTCGAGCCGGTGGGGGCCGGCACGGCATCCACGGGCTCCAAGAGCGTTGACGGATGGGTCCCCTTCGTGGCCCAGCCGGTGCGGGGCAAGAACGACTACCTGACGCGGGACAACATGGTGTTCGTCTACAACCGTGAGGCAACGACCTTCGACGGTACCGGGAAGACCTACGAGGCCTACTCCGACCGGCACGACATCGTCATCAAGTAG","LLRVEGTKGTVMKSTIKAVAAVAALALSLGLSACGDQEAGTDSEKSSRATASQASDDKSPEAESDASESASSKASSKESSAPTGSASSSSSAKASSPQGGETLPTGEKVESIDPIVIKDQAIGLTQTCDKIVYDYSAPTFKGTEKGSQDKIILLHCKMEFSGEVSFSGKVTAYQEIQSKEKDYLNAGVAASLVEQDLKDAGLEPVGAGTASTGSKSVDGWVPFVAQPVRGKNDYLTRDNMVFVYNREATTFDGTGKTYEAYSDRHDIVIK$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide

","No hits to the COGs database.","***** IPB005028 (Herpes virus intermediate/early protein 2/3) with a combined E-value of 4e-07. IPB005028B 44-92 IPB005028B 52-100 IPB005028B 64-112 IPB005028B 40-88 IPB005028B 56-104 IPB005028B 43-91 IPB005028B 48-96 IPB005028B 60-108 IPB005028B 47-95 IPB005028B 24-72 IPB005028B 32-80 IPB005028B 42-90 IPB005028C 48-98 IPB005028C 32-82 IPB005028C 44-94 IPB005028C 40-90 IPB005028C 52-102 IPB005028C 56-106 IPB005028C 64-114 IPB005028C 36-86 IPB005028C 60-110***** IPB008408 (Brain acid soluble protein 1) with a combined E-value of 1.1e-06. IPB008408C 52-101 IPB008408C 41-90 IPB008408C 44-93 IPB008408C 54-103 IPB008408C 40-89","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2292","2476787","2478202","1416","6.68","-2.13","51541","ATGACGTCATCCGAGGTGACTCGCCCCCGTCCGACGGCGCCGCCCGTCTACCGGGACGGCCCGTCCAAGATGTCGGAGGTCGATGCCCGCTCCTGGAGCATCGATGACGTCCTGGACGCCGTCTTCTTCGCCATCGCCGCCGTCGCCACGCTGTGGCTGGCCTGGTTGCTCATCGGCTCAGGCTGGCACCTCGATCCGGTCCTCGTGGTCAACTCCCTGCTGTTCTGGGCGGTCCTGGCCTACCTCGCCCTGCCACGCCTCCACCAGGTCCTCACCTGGCTCTACGTCCCCGACTACTTCATCGGCCGCACCCGCACCCCCGACGGGCTCCTGGGCGACCCCGTCAACCTCGCCGTCAAGGGCGACGAGGAGGACATTCACGAGGCGATGATCGCGGCCGGCTGGGTGCGCGCCGACCCCATCACCCTGCGCACCTCCTGGCGCATCATCGTCTCCTCGCTGCTGCGCCGCTCCTACCCGGCCGCCCCGGTCTCCAGCCTCATGCTCTTCGGGCGCAAGCAGAGCTTTGCCTACCAGAAGGAGGTTGAGGGCAACCCCGCCCAGCGCCACCACATCCGCTTCTGGTACTGCCCGCCCGGCTGGTCGCTGCCCGGCGGCGGACACGTGGACTGGCTGGCCGCCGCCACCTACGACCGCGCCGTCGGCCTGAGCGCCCTCACCCTCCAGGTCACCCACAAGATCGACGCCGATATCGACATCGAGCGCAACTACGTCGTCGACGACGTCCGCTGGGCCAACGAGGCCGCCGACCTGGAGATCTGGCCGGACTTCTTCGCCTCCTACCACGACAAGAACGGGGGAGGGGACCGGGTGGTCACCGACGGCGCCCTTCACGTGCTCGACCTTAACGAGGTGGTTCCCGGATCCGACGCCGGGCTCTCCCTGCGGCAGGCCCGCCTGGCCGACCACCAGGCCCGCCGCCGTCGCCCCAGCCAGCTCGTCATCGCCCTGGCGCTCATCGGGCTCGCGATGACGGTCGAGATCCTGCGCGTGGCCCGCATCGACATCACCCAGGTGCTGGAGGCCGCTCCGTTCCCGGAGGAGGACCCGGGGGCGGTTACCGCCGTCGTCGCTCTCATCGCCACGGTCTCTGCCGGCCTGATGCTCCTCACCGCCGCCCTGGGGATCGCAGCCTGGCGCGGGCACCCGCGCAGCCGCATCGCCCTCATGGCGACCCTCGTCCTGGGTGTCGCCACTGACATGGTTCAGGTCTCCAGCCTCGGGGTTCGGCAGGCGACTCTCGGCCTGGTCGTCACCAGCGCGCTCCAGGTCCTGGCCCTGCTGGCGCTCTCGGCCCGGCAGGTCCGCGAGTGGGAGCACGCCCGCAAGGAGGAGCGGCTTGCCGACCGTGCGAACGCACGGGGCGACCGGGCGGCAGTTAGGCTGGGCTCATGA","MTSSEVTRPRPTAPPVYRDGPSKMSEVDARSWSIDDVLDAVFFAIAAVATLWLAWLLIGSGWHLDPVLVVNSLLFWAVLAYLALPRLHQVLTWLYVPDYFIGRTRTPDGLLGDPVNLAVKGDEEDIHEAMIAAGWVRADPITLRTSWRIIVSSLLRRSYPAAPVSSLMLFGRKQSFAYQKEVEGNPAQRHHIRFWYCPPGWSLPGGGHVDWLAAATYDRAVGLSALTLQVTHKIDADIDIERNYVVDDVRWANEAADLEIWPDFFASYHDKNGGGDRVVTDGALHVLDLNEVVPGSDAGLSLRQARLADHQARRRRPSQLVIALALIGLAMTVEILRVARIDITQVLEAAPFPEEDPGAVTAVVALIATVSAGLMLLTAALGIAAWRGHPRSRIALMATLVLGVATDMVQVSSLGVRQATLGLVVTSALQVLALLALSARQVREWEHARKEERLADRANARGDRAAVRLGS$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[37-57]?$ $\"[67-85]?$ $\"[320-340]?$ $\"[359-379]?$ $\"[394-414]?$ $\"[420-440]?$	transmembrane_regions

InterPro
IPR004923
Family

Iron permease FTR1
PF03239	$\"[2-283]T$	FTR1

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[145-308]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide
tmhmm	$\"[39-57]?$ $\"[71-91]?$ $\"[118-140]?$ $\"[154-172]?$ $\"[182-204]?$ $\"[255-273]?$	transmembrane_regions

","BeTs to 10 clades of COG0672COG name: High-affinity Fe2+/Pb2+ permeaseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0672 is a----zy-v---bcef-h-nu-x-t-Number of proteins in this genome belonging to this COG is 1","***** IPB004923 (Iron permease FTR1) with a combined E-value of 1.8e-34. IPB004923A 6-28 IPB004923B 121-138 IPB004923C 167-198 IPB004923B 3-20","","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 283 (E_value = 2.4e-54) place ANA_2295 in the FTR1 family which is described as Iron permease FTR1 family.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2296","2480670","2481998","1329","5.01","-14.36","46862","ATGCCCACCATCAAGCGACGCAATGTCCTCACCCTGCTCCCCCTGACCGCCATGGGCCTGGGCCTGGCCGCCTGCGCCGACAACCCCAAGAACGCCAAGGGCAGCGCCTCCGGCTCCGGGGCGCCCCAGGAGATCACGGTGACCCTCACCGACGACGCCTGCAAGCTCTCCTCGACCTCCTTCCCCTCGGGCGTGGTCACCTTCACCATCACCAACTCCGGCACGGCCCCCAACGAGCTGGAGATCCTCACCGAGGACAAGCTCCAGATCGTCTCCGAGCAGGAGAACATCGGCCCCGGCACCACCACGAAGCTCACCACCTCCCTCAAGGAGGGCACCTACTACGCCGCCTGCAAGCCCAACATGGTCGGCGAGCTCAAGGGCGTCACCGAGCTGAAGATCACCAAGGGCGCCGCCGTCGACATCAGTGCCGACGAGGCCAAGGCGCGCGAGGCCGCCGTCACCAACTACACCGCCTACGTGCGCGACCAGACCGGCCAGCTGCTCACCGCCACCCAGGGCTTCGTCACCGCTTACACCTCCGGCGACACTGACACCGCCAAGAGCCTCTATCCGCTGGCGCGCCAGTACTACGAGCGCATCGAGCCCACCGCCGAGTCCTTCGGCCTCAAGGAGGCCGGCGACCTCGACGCCGCCCTGGACACCCGCGTCCAGGACCTCGCCGCCGGCGCCGGCAAGGCCGTCACCGACAAGGACGTCCTCGCCGGATGGACCGGCTGGCACCGTATCGAGGCCGACCTGTGGGCCCAGGACTCCTCCAGCCCCTTCAAATTCGCCGACGACGCCTCCCGCAAGAAGGTCGCCGACCAGCTCAACGCCGACACCAAGTCGCTCTACGACCTCGTCTACGGGAACATCACCGGCGCCAGCGGCAAGAAGTTCGAGCTCGGGCTCGAGGATGTCGCCAAGGGCGCCTCCGGCCTCCTTGAGGAGGTCGCCAGCTCCAAGATCGTCGGCGAGGAGGAGACCTTCTCCCACACCGACCTCTACGACTTCCAGGCCAACGTCGAGGGTGCCAAGGTCGCCTACGGCAACGTCGAGGACCTCATGAAGAAGAAGGACTCCAAGCTCGCCGAGAAGATCACCGGCCAGTTCACGGCGGTTGAGAAGCTCATCGCGAACCACGTCTCCGGGAAGGCCTCCAACGGCCAGCCCACCTACGTGGACTACTCCACCATCGCCTCGGTCCAGAAGGACGCCGGCGAGACCCCGGACAAGAACGCCTACACCGACACCCAGCGCAAGTTCTCCGACGCCGTCAACGCCCTGAGCGAGTCGCTGTCCAAGGTCGCCGGAACCGTCCTCTAA","MPTIKRRNVLTLLPLTAMGLGLAACADNPKNAKGSASGSGAPQEITVTLTDDACKLSSTSFPSGVVTFTITNSGTAPNELEILTEDKLQIVSEQENIGPGTTTKLTTSLKEGTYYAACKPNMVGELKGVTELKITKGAAVDISADEAKAREAAVTNYTAYVRDQTGQLLTATQGFVTAYTSGDTDTAKSLYPLARQYYERIEPTAESFGLKEAGDLDAALDTRVQDLAAGAGKAVTDKDVLAGWTGWHRIEADLWAQDSSSPFKFADDASRKKVADQLNADTKSLYDLVYGNITGASGKKFELGLEDVAKGASGLLEEVASSKIVGEEETFSHTDLYDFQANVEGAKVAYGNVEDLMKKKDSKLAEKITGQFTAVEKLIANHVSGKASNGQPTYVDYSTIASVQKDAGETPDKNAYTDTQRKFSDAVNALSESLSKVAGTVL$","Periplasmic lipoprotein involved in iron transport","Extracellular, Periplasm","Protein ycdO","K07224 putative lipoprotein","protein of unknown function DUF451","","","","","

InterPro
IPR007399
Family

Protein of unknown function DUF451
PF04302	$\"[138-441]T$	DUF451

noIPR
unintegrated

unintegrated
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-25]?$	signal-peptide

","BeTs to 3 clades of COG2822COG name: Predicted periplasmic lipoprotein involved in iron transportFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2822 is ------------b-e----n------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 138 to 441 (E_value = 1.1e-55) place ANA_2296 in the DUF451 family which is described as Protein of unknown function (DUF451).","","ycdO ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2297","2482044","2483582","1539","5.02","-19.32","54858","GTGAGTGGCAAGCCGGCCCACGAGTCGGGCACCTCCCCGGTCGCCGACGAAGCGGCCCAGGACGAGACCCTGGACGAGCCTCAGGACAAGACCGCGCGGGCGCAGCAGGAGTCGCAGGCACCGACGTCGGAGGGCCCGGGTGACAGCTCCTCGGCCTCCGACGCGGCCGAGCAGTCCGAGGGGGCGAGCACCCCCGACGGGGCTGACCAGCCGGAGAAGACCGAGAAGCCGGATGAGGCCGGGAAGCCCGGCGCCAAGGGCACCAGCCGCCGCGCCATGTTCACCGGTGCGGGCCTGGGCGCCGCGCTCGCGGGCCTGGCCGGTGTGGCCGGGGGCCGCGCCTGGGAGGCCTCCCGCCGTCCCGAGGAGGCCATCCTCACGACCTACCCCTTCCGGGGTGACCACCAGGCGGGGATCACCACCCCCGCCCAGGACAACATGTTCACCGCGGCCTTCGACGTCTCTGCCACCGACGTCGAGGAGCTCAAGACCCTCCTGTCCGAATGGGCCGTGGCCGCCGAGCAGATGACCGCCGGCGAGCTCATCGGCGGCCAGCCCAGCTCCAACAAGCAGCTGCCGCCCAAGGACACCGGCGAGGCCTGGGGCTACAAGCCCAACGGCCTGACCATCACCTTCGGCGTGGGCAAGGGCCTGTTCGTCGACGCCGACGGCAAGGACCGCTTCGGCCTGGCCGCTAAGATGCCCGCCGTCCTCAAGGAGGGCATGCCCTCCTTCGCCGGAGACCAGCTCCACGCCGCCCAGTCCGACGGCGACCTGCTCATCCAGGCCTGCTCCAACGACGCCCAGGTGTGTGTCCACGCGATCCGCAACCTCACCCGCATCGCCTTCGGGACCGCCACACTGCGGTGGAGCCAGGTCGGCTACGGGCGCACGTCGTCGACCTCCGTGGACCAGGAGACGCCGCGCAACCTCTTCGGCTTCAAGGACGGCACCAACAACATCAAGGCCGAGGACTCCACCGACCAGCTCAATGAGCACCTGTGGGTCCAGAAGGGCGACGACGCCGCAGCCGCGTGGATGACGGGCGGCACCTACTACGTGGCCCGGCGCATCCGCATGCTCGCCGAGATCTGGGACCGGCTGCGGCTCATTGAGCAGGAGCAGACCATGGGGCGCGACAAGCGCTACGGGGCGCCGCTGAGCATCACCAACCCCACGAAGTCCTCCGAGGAGTTCACGGCCGTGGACTACAAGGCAAAGGACGACAAGGGCGAGACGCTCGTACCGGCCGACGCGCATATCGCCGTCGTCTCACCGGAGCAGAACCAGGGGCGCCGGATGCTGCGCCGCGGCTACAACTACACCGACGGCTCCGACTCCCTGGGGCAGCTGCAGACCGGCCTGTTCTTCATCGCCTTCGTGCGTGACCCACGCACGAACTTCTACCCGATCCTGGACCGCATGACCAAGACCGACGCCCTCCAGGAGTACCTCAAGCACGAGGCCTCGGCGCTGTTCGCGATCCCCCCGGGCATCAAGGAGGGCGACACCATGGTGGCCGCCTCGCTCTTCAGCTGA","VSGKPAHESGTSPVADEAAQDETLDEPQDKTARAQQESQAPTSEGPGDSSSASDAAEQSEGASTPDGADQPEKTEKPDEAGKPGAKGTSRRAMFTGAGLGAALAGLAGVAGGRAWEASRRPEEAILTTYPFRGDHQAGITTPAQDNMFTAAFDVSATDVEELKTLLSEWAVAAEQMTAGELIGGQPSSNKQLPPKDTGEAWGYKPNGLTITFGVGKGLFVDADGKDRFGLAAKMPAVLKEGMPSFAGDQLHAAQSDGDLLIQACSNDAQVCVHAIRNLTRIAFGTATLRWSQVGYGRTSSTSVDQETPRNLFGFKDGTNNIKAEDSTDQLNEHLWVQKGDDAAAAWMTGGTYYVARRIRMLAEIWDRLRLIEQEQTMGRDKRYGAPLSITNPTKSSEEFTAVDYKAKDDKGETLVPADAHIAVVSPEQNQGRRMLRRGYNYTDGSDSLGQLQTGLFFIAFVRDPRTNFYPILDRMTKTDALQEYLKHEASALFAIPPGIKEGDTMVAASLFS$","Tat-translocated enzyme","Periplasm, Cytoplasm, Extracellular","Tat-translocated enzyme","Tat-translocated enzyme","Dyp-type peroxidase family","","Sugano Y., Nakano R., Sasaki K., Shoda M. Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1. Appl. Environ. Microbiol. 2000. 66(4):1754-1758. PMID: 10742277","","","

InterPro
IPR006313
Family

Tat-translocated enzyme
TIGR01412	$\"[81-512]T$	tat_substr_1: Tat-translocated enzyme

InterPro
IPR006314
Family

Dyp-type peroxidase
PF04261	$\"[136-501]T$	Dyp_perox
TIGR01413	$\"[136-501]T$	Dyp_perox_fam: Dyp-type peroxidase family

","BeTs to 5 clades of COG2837COG name: Predicted iron-dependent peroxidaseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2837 is ---------dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is 2","***** IPB006314 (Dyp-type peroxidase) with a combined E-value of 8.1e-25. IPB006314A 136-167 IPB006314C 310-320 IPB006314D 349-386","","","No significant hits to the PDB database (E-value < E-10).","Residues 136 to 501 (E_value = 1.3e-113) place ANA_2297 in the Dyp_perox family which is described as Dyp-type peroxidase family.","","enzyme ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2298","2485022","2483772","1251","10.07","11.00","42234","ATGTCTCCCGAACACCGACCCGATCAGCATCCCGACGTCACTCACTTCCCCGAGCCATCAGGCCAGTCGGCGACTCGGTCACCCTCCCCCACCTACCCCGCCGACAGCGGAGCTACCGCGGCCCTCGTGGTCACCGCACTGCTCGTCCTGACCCAGCTGTACGCCGCCATCCCCCTGCTCACCCCGATCTCGACCGGCCTCCACGGCAGTGCCACCGTCGCCCTGTCGACGGCCTTCAGCCTCACCTACGCCGCAGGCTTCCTCATCTGGGGGCCAGTCTCTGACCACTACGGCAGGAGGAGAACCATGGCGCTCGCGCTGGGTACCCTCACCATCTCCACCGCCTGCTGCGCCCTGGCCCCGTCCCTACCGGCACTCGCGGCCCTGCGCGCGATCCAGGGTCTGAGCGCCTCCGGTTTCGCACCCGTGGCCCTGGCCTACTTGTCCGAGGCGCTGGCACCATCCAGGCGGGCCGGGGCGATCGGGGCAATGTCGACGTCGTTCCTCGTGGCGGGCATCTTTGGCCAGGTCCTGGCCTCGCTGGTCGCGCTGCACCTGGGGTGGCGGTGGTTCTTCCCCCTGTGTGGCGGACTGCTGGCCGTGGCCCTGGCGGCCGTGCTCGCCGTCGTGCACGACGCCGCTTCCACCTCCGGCCCCTCGGGCTCCTCCCTGCGGGGGCAGTTCGCATCCCTGGGGCGCCTCGCGCTCAGGCCTGCGGTTGTGGCGCTGAGCCTGGCGCATGTCACGCTGCTCATGGTGTTCGTCGCCATGTACACAGGGATCGGCGGGCACCTGGAGTCGCAGGGCATGCGGCCGTCGACGATCGTTCTCATTCGCCTGGCAGCCCTGCCGGTCATGTTCCTCAGCCTCGTTGCGGGCCGGATCGCGGCTAGGTGGTCCTGGGCGCAGACGGCCCGGCTGGGCTTCGGGGTGTCGGCGCTGGGCATGCTCGGCGAGGCACTGCTGGCGCAGAGCCTGGCGGGCCTGGTGGCCGGCAGCATCGTGTACGTCGCAGGGGTCGCGCTGGCTGTGCCGGCGATGATCAGCCTCTACGGGCAGGTGTCCGCCCCCAACCGCGGCAGCGGCATGGCACTCAACGGATTCATCCTGTTCGTCGGCACGAGCGCCGGCCCGCTCCTGGCGACGTCGTCGCCCACCTTCCGGACGCTGGCTCTCACCCTGAGCGGCATCCTGGCCGTGGCACTGGCCGCGATCACCGGTTTCAAGGCTCTGGCCGACGTCGACCGCTGA","MSPEHRPDQHPDVTHFPEPSGQSATRSPSPTYPADSGATAALVVTALLVLTQLYAAIPLLTPISTGLHGSATVALSTAFSLTYAAGFLIWGPVSDHYGRRRTMALALGTLTISTACCALAPSLPALAALRAIQGLSASGFAPVALAYLSEALAPSRRAGAIGAMSTSFLVAGIFGQVLASLVALHLGWRWFFPLCGGLLAVALAAVLAVVHDAASTSGPSGSSLRGQFASLGRLALRPAVVALSLAHVTLLMVFVAMYTGIGGHLESQGMRPSTIVLIRLAALPVMFLSLVAGRIAARWSWAQTARLGFGVSALGMLGEALLAQSLAGLVAGSIVYVAGVALAVPAMISLYGQVSAPNRGSGMALNGFILFVGTSAGPLLATSSPTFRTLALTLSGILAVALAAITGFKALADVDR$","Drug resistance transporter","Membrane, Extracellular","TcaB protein, putative","membrane transport protein","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[1-413]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[42-386]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[20-381]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF29	$\"[20-381]T$	MAJOR FACILITATOR FAMILY TRANSPORTER
tmhmm	$\"[36-68]?$ $\"[74-94]?$ $\"[104-124]?$ $\"[130-148]?$ $\"[163-183]?$ $\"[189-209]?$ $\"[239-261]?$ $\"[275-293]?$ $\"[303-323]?$ $\"[329-351]?$ $\"[361-381]?$ $\"[387-407]?$	transmembrane_regions

","BeTs to 19 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 42 to 386 (E_value = 4.9e-38) place ANA_2298 in the MFS_1 family which is described as Major Facilitator Superfamily.Residues 78 to 174 (E_value = 1.7e-05) place ANA_2298 in the Sugar_tr family which is described as Sugar (and other) transporter.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2300","2485138","2485731","594","6.03","-2.36","22437","ATGGCCTGGGACACCGAGGGGACCAAGCGCAAGATCAAGGACGCCGCCACCGCCGAGTTCACCCGCCGTGGGCCCGCTGGGACCACCGTCGAGCGGATTGCCAGGCGGGCGGGGGTCAATAAGGAGCGCATCTACAACTACTTCGGCTCCAAGGACCGCTTGTTCTCCGCAGTCCTGCGCGACGAGCTGACCAGGGTGGCCGAGGCTGTGCCGCCCGCCTTCGACGCAGGAGAGGACGTGGGGGACTACGCCGGGCGCCTCTACGACTACCACCGACAACGCCCCGAGCTCATCCGGCTGCTGTGCTGGGAGGCCCTCACCTTCGACGACGAGGTACCCGAGGAGGAGCTGCGGCGCGAGCACTACCAGCGCAAGATCGCCGGGGTGCGCAGCGGTCAGGATGTCGGCTTCCTGACCCGGGACGTCGATCCCGGTGCGCTCATGCTCATGCTCATGTCACTGACCGGCTGGTGGTCCACCGTGCCCCAGGTGGCGCGGATGCTGTGCGGACCCCTCGATGATGAGGAGGCTCACGAGCGTCAGCGCGCCGTCGTCGTCGATGCGGCCCGTCGGCTTGCCGTACCCCGCGACTGA","MAWDTEGTKRKIKDAATAEFTRRGPAGTTVERIARRAGVNKERIYNYFGSKDRLFSAVLRDELTRVAEAVPPAFDAGEDVGDYAGRLYDYHRQRPELIRLLCWEALTFDDEVPEEELRREHYQRKIAGVRSGQDVGFLTRDVDPGALMLMLMSLTGWWSTVPQVARMLCGPLDDEEAHERQRAVVVDAARRLAVPRD$","Transcriptional regulator, TetR family","Cytoplasm","transcriptional regulatory protein","transcriptional regulator; TetR family","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[12-25]T$ $\"[33-56]T$	HTHTETR
PF00440	$\"[12-58]T$	TetR_N
PS50977	$\"[6-66]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[6-58]T$	no description

","BeTs to 15 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 2.3e-16. IPB001647 12-54***** IPB013573 (Tetracycline transcriptional regulator YcdC-like, C-terminal) with a combined E-value of 1.6e-11. IPB013573B 33-74 IPB013573D 127-181","","","-61% similar to PDB:2D6Y Crystal Structure of transcriptional factor SCO4008 from Streptomyces coelicolor A3(2) (E_value = 5.6E_33);","Residues 12 to 58 (E_value = 5.4e-14) place ANA_2300 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulatory protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2301","2485766","2487169","1404","5.23","-20.72","49095","ATGCGCGACCTGAACGACCTGACCCGCCCCACCGTCCCCTCCGGCGCCATCCAGGAGCGCATGCTCGCCGAGACCGAGGAGCGCCGCGGCGTCGTCGGCCCGGCACCGGCCCTGCCCGACGACGCCGGAGCCCCCACCGCTCTGCGCGCCGCCCTGGGTCAGGCCGTCGCCGAGCTGGCCCCGCAGATCGTCGAGCTCTCCCACGACATCCACGACCACCCCGAGACCGGCTACGAGGAGCACCACGCCGTGGCCACGGTCGCCGAGCTCCTGCGCCGCCACGGCATTGAGCCCGAGGTCGGCGTCTACGGTATGGACACCGCCCTGCGCGCCGAGATCCCCGCGGCCGGCAGCACCGGCGGTGCAGACGCGGCGGCCGCGGGCTCCGGTGAGTCCGCCGGCACCATCGCCATCCTCGCCGAGTACGACGCCCTGCCCGGCATCGGCCACGGCTGCGGCCACAACGTCATGTGCGCCAACTCCGTGGGTGCCTTCCTCGCCCTGGCCGCCCTGGCCCGCACCCGCCCAGGCGCCCTGCCCGGCCGCGTCGTCCTGCAGACCACGCCCGCCGAGGAGAACTCGACCGCCAAGGAGATCCTGGCCGTGCGCGGCATGCTCGACGGCGTCGACGCCGCCATCCAGACCCACTCCTACGCCCACGACGTCACCCACCAGACCTGGCTGGGCGTGCGCCGCCTGCGCGTCATCTTCCACGGCGTGCCGGCCCACGCCGCCTCCCAGCCCTTCATGGGCCGCAACGCCCTGGATGCCGCCACCCTGGCCCTGACCGGTATCGGCCTGCTGCGCCAGCAGATGCTCCCCATGGACCGCCTCCACGCCATCATCACCGACGGCGGCCAGGTCCCCAACATCATCCCCGAGCGCACCGAGCTGTCCATCATGGTGCGCTCGAAGTACCTCGAGACCCTCAAGGAGATCGCCGAGCGGGTCGAGGAGGTCCTCCACGGCGCCGCCCTCATGACCGGCACAGGCGTTGAGATCCTCACCTCCGAGTACTGCAACGAGGTCCCCGTCCGCGACAACGGCCCCCTGCTGACCTCCTGGGTGCGCTCCCAGCGCGAGCGCGGCCGCGACCCCCTGGCCGCCGGGGTCCTGCCCGAGACCATCGCCGCCGGCACCGACTTCGGCAACGTTTCCCAGCGGATCCCCGGCATCCACCCGCTCATCAAGGTCACCGACCGGCCCGACGTCGCCCTCCACACCCCCGCCATGACCGAGGCCGCCGGCGCCCCCACCGGGGATGCGGCCGCGCTCGACGGCGCCTACGGGCTGGCCGCCGTTGCCCTGGACTGGCTGCACGACGCCGAGCTGCGCCGGGCCGTGCGCGCCGACTTCGAGGCCAGTGGCGGGACGATCGACGTCGCCGGCTTCTGGGAGGAGTGA","MRDLNDLTRPTVPSGAIQERMLAETEERRGVVGPAPALPDDAGAPTALRAALGQAVAELAPQIVELSHDIHDHPETGYEEHHAVATVAELLRRHGIEPEVGVYGMDTALRAEIPAAGSTGGADAAAAGSGESAGTIAILAEYDALPGIGHGCGHNVMCANSVGAFLALAALARTRPGALPGRVVLQTTPAEENSTAKEILAVRGMLDGVDAAIQTHSYAHDVTHQTWLGVRRLRVIFHGVPAHAASQPFMGRNALDAATLALTGIGLLRQQMLPMDRLHAIITDGGQVPNIIPERTELSIMVRSKYLETLKEIAERVEEVLHGAALMTGTGVEILTSEYCNEVPVRDNGPLLTSWVRSQRERGRDPLAAGVLPETIAAGTDFGNVSQRIPGIHPLIKVTDRPDVALHTPAMTEAAGAPTGDAAALDGAYGLAAVALDWLHDAELRRAVRADFEASGGTIDVAGFWEE$","Metal-dependent amidase/aminoacylase/carboxypeptidase","Cytoplasm, Extracellular","Metal-dependentamidase/aminoacylase/carboxypeptidase","hydrolase; Ama/HipO/HyuC family","amidohydrolase","","Rowsell S., Pauptit R.A., Tucker A.D., Melton R.G., Blow D.M., Brick P. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Structure 1997. 5(3):337-347. PMID: 9083113Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR002933
Family

Peptidase M20
PF01546	$\"[137-409]T$	Peptidase_M20

InterPro
IPR010168
Family

Peptidase M20D, amidohydrolase
TIGR01891	$\"[63-420]T$	amidohydrolases: amidohydrolase

InterPro
IPR011650
Domain

Peptidase M20, dimerisation
PF07687	$\"[225-329]T$	M20_dimer

InterPro
IPR013838
Binding_site

Beta tubulin, autoregulation binding site
PS00228	$\"[1-4]?$	TUBULIN_B_AUTOREG

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.10	$\"[34-455]T$	no description

","BeTs to 11 clades of COG1473COG name: Metal-dependent amidohydrolases/aminoacylasesFunctional Class: RThe phylogenetic pattern of COG1473 is ---K--vCEBRh---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 160 to 460 (E_value = 5.2e-05) place ANA_2301 in the Peptidase_M20 family which is described as Peptidase family M20/M25/M40.Residues 248 to 352 (E_value = 2.1e-05) place ANA_2301 in the M20_dimer family which is described as Peptidase dimerisation domain.","","amidase-aminoacylase-carboxypeptidase (HmrA)","","1","","","Wed Aug 8 15:03:12 2007","","Wed Aug 8 15:03:12 2007","","","Wed Aug 8 15:03:12 2007","Wed Aug 8 15:03:12 2007","Wed Aug 8 15:03:12 2007","","","Wed Aug 8 15:03:12 2007","","","Wed Aug 8 15:03:12 2007","","","","Wed Aug 8 15:03:12 2007","Wed Aug 8 15:03:12 2007","","","","","yes","","" "ANA_2302","2488226","2487177","1050","10.73","8.67","35701","ATGCAGGCGCGCCTGGCCCTGGCGGCCGGGGCGAAGCTGGTGGTGGCCGCCGGCGGTGACGGAACGGTGCGCTCGGTGGCGGCCGGCCTGGCCGGCACCGGCGCCCAGATGGGCATCGTCCCGCTGGGCACGGCGAACCTGGCGGCCCGCAACCTCGGGGTGCCGGTCGGGGACGCCCGGGCCGCGGCCCGGGTGGTGGCCCACGGCGTCGATCTTGCCGCCGATCTGGCCTGGGTGCGCACCGAGCCCTGGACCGATCCCAACATCCTCTCCGACCCGGCGTCATCGGGCGCCCCCCGCGGACGGACCGGCTCCACACCCTCCACACCCCTGACGAGCCCAGCCGCAGCAGCGCCGCCGGACTCCCCGCCCACTCCTGCCGACCCGGCCAACCCGGCCAACCCAGCCGACTCCCGGCAGCTGTCGGCTGAGGCGGTCCGGGCCGTGCGCACGATCCAGAGAGCGACCCGCCGGCCGCATCAGTGGACCCGGCCCACACTCGGCGACGAGCACGCCTGCATGGTGGTGGCCGGGATCGGTTTCGACGCCGGGCTGGTGGCCTCCACGCGCCCGGCCCTCAAGGCGCGGGTCGGCTGGGGCGCCTATGCGCTGGCGGCCATGGAGAACCTGGGATCGCCGCGCATGGACCTGGTCCTCAGCCTCCTGGACGAGGCCGGCGCGCGGCGCGTGGAGCGCCTGCGGGCCCGCAACCTGCTGGTGGCCAACGGCGGCCGCCTGCCGGCAGGGATCAACCTGCTGCCGCAGGCCCGCACCGATGACGGCCTGCTCGACGTCGCCGCCATCGACACGGTGGCGGGTTTGGCGGGCTGGAGCTCGCTGGCGCGCCAGGTGCTGCCGCCTTACGCGGCGCGCTACTCGGAGTCGGGCCGCTCGCTGGGGCGGGTGGTGATGCGCCGCGGCGGGGAGGTGGCCGTCCAGCTCTCGGCACCGGCCCTGGTGGAGGTCGACGGCGACCTGCTGGCGCCCACGCAGGGCATGCGGGTGCGCATCGACCCCGGGGCGCTGCTCATCCGCCGCCCGGCGGCCTGA","MQARLALAAGAKLVVAAGGDGTVRSVAAGLAGTGAQMGIVPLGTANLAARNLGVPVGDARAAARVVAHGVDLAADLAWVRTEPWTDPNILSDPASSGAPRGRTGSTPSTPLTSPAAAAPPDSPPTPADPANPANPADSRQLSAEAVRAVRTIQRATRRPHQWTRPTLGDEHACMVVAGIGFDAGLVASTRPALKARVGWGAYALAAMENLGSPRMDLVLSLLDEAGARRVERLRARNLLVANGGRLPAGINLLPQARTDDGLLDVAAIDTVAGLAGWSSLARQVLPPYAARYSESGRSLGRVVMRRGGEVAVQLSAPALVEVDGDLLAPTQGMRVRIDPGALLIRRPAA$","Diacylglycerol kinase","Cytoplasm, Membrane","conserved hypothetical protein","diacylglycerol kinase; catalytic region","Sphingosine kinase and enzymes related to eukaryotic diacylglycerol kinase-like","","Staub E., Fiziev P., Rosenthal A., Hinzmann B. Insights into the evolution of the nucleolus by an analysis of its protein domain repertoire. Bioessays 2004. 26(5):567-581. PMID: 15112237","","","

InterPro
IPR001206
Domain

Diacylglycerol kinase, catalytic region
PD005043	$\"[20-52]T$	Q6A8S5_PROAC_Q6A8S5;
PF00781	$\"[3-82]T$	DAGK_cat

InterPro
IPR012948
Domain

AARP2CN
SM00785	$\"[144-214]T$	no description

noIPR
unintegrated

unintegrated
PTHR12358	$\"[8-84]T$ $\"[169-269]T$	SPHINGOSINE KINASE
PTHR12358:SF4	$\"[8-84]T$ $\"[169-269]T$	BMRU PROTEIN
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 7 clades of COG1597COG name: Predicted kinase related to diacylglycerol kinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1597 is ---p--y-vdrlbcef-----j----Number of proteins in this genome belonging to this COG is 3","***** IPB000756 (Diacylglycerol kinase accessory domain (presumed)) with a combined E-value of 5.2e-06. IPB000756E 13-27 IPB000756F 35-58","","","No significant hits to the PDB database (E-value < E-10).","Residues 3 to 82 (E_value = 5.4e-13) place ANA_2302 in the DAGK_cat family which is described as Diacylglycerol kinase catalytic domain (presumed).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2305","2489663","2488539","1125","6.09","-5.72","40050","GTGCACCCTATCGTTCCCGACGGTGTTTCCGAGCCGCCACGTTGGAGGCTCGTCCACACCCCACCGCATCGTCCTCCCCACTCCTCCCGGCTAGTCGTCTGTCCCCGATTTTCTGTCACTCCGTCATATCAGGCTCGCCGACCGCCACGCATGCGGGCCCCGACCACAGGACCACCACTCATGCCGACCACATCATCTCCGTCCTTCTCCCAGCTGAGGGCCTTCGTAGCGCTGTGCGACCACCAGCACTTCGGCGAGGCCGCCGCGGCGCTCGGAGTCAGCCAGCCCAGCCTGTCCCAGGCCATCACCGCACTGGAGAAGCGCGTCGGCGGCGAGCTGGTGGAGCGCACCACCCGTCGTGTCCTGGTCACCTCCCTGGGCGAGGCCCTACTGCCCTACGCCCGGGACGCCGTCCTGGCCGCCGAGGCCTTCAACGAGGCCGCCTCCAGCCAGGGCGCCGCCCTGAGCGGCACGATGCGCCTGGGCGTCATCCCCACCATCGCGCCCTACCTGGCCCCCGTTCTCATCGATGGTCTGCGCGAGGCCCTGCCCCAGATGGACCTGGACCTACGCGAGATGGTCACCGGCGACAACCTCGACCAGCTCGCCCAGGGGCGCCTCGACGCCGCCATCATCGCCCTGGAGGACGACCTCCAGCGCACCACCGCGATCCCGATGTTCGACGAGCGGCTCGTCGTCCTCACCGCCGCCGACCACCCCTGGGCCGGCCGCACGGACGTGAGCCCCGCCGAGCTCGACGACCAGCCCCTCCTCCTGCTCGACGAGGGCAACTGCCTGCGCGACCAGACCCTGGCCCTGTGCCAGCGCTACGGCTCCCAGCCCCCGGTCGCGGTGGCCACCACGCTGTCCACGGTCACCCGCATGGTCGCCCACGGCTCCGGCGTGACGATCATCCCCGAGGGGGCGCTCCAGCTGCTGACCCCCTCCTCGGAGTACGGCGTCGCCCGTTTCGGCGACGAGGCGCCGATGCGCCGCATGGGCCTGGTGCACCGGGTCTCCTCCTCCCGCGGCGCCGACTTCGCCCAGCTGGCCGAGCTCATCTCGCACCTGGTGCGAGAGGCCGATCTGCCCGTGGCCCCCGTCACGGCTCTGGCTGTGGCCTGA","VHPIVPDGVSEPPRWRLVHTPPHRPPHSSRLVVCPRFSVTPSYQARRPPRMRAPTTGPPLMPTTSSPSFSQLRAFVALCDHQHFGEAAAALGVSQPSLSQAITALEKRVGGELVERTTRRVLVTSLGEALLPYARDAVLAAEAFNEAASSQGAALSGTMRLGVIPTIAPYLAPVLIDGLREALPQMDLDLREMVTGDNLDQLAQGRLDAAIIALEDDLQRTTAIPMFDERLVVLTAADHPWAGRTDVSPAELDDQPLLLLDEGNCLRDQTLALCQRYGSQPPVAVATTLSTVTRMVAHGSGVTIIPEGALQLLTPSSEYGVARFGDEAPMRRMGLVHRVSSSRGADFAQLAELISHLVREADLPVAPVTALAVA$","LysR family transcriptional regulator; hydrogen peroxide-inducible genes activator","Cytoplasm, Membrane","Transcriptional regulator","K04761 LysR family transcriptional regulator; hydrogen peroxide-inducible genes activator","LysR, substrate-binding","","Viale A.M., Kobayashi H., Akazawa T., Henikoff S. rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum. J. Bacteriol. 1991. 173(16):5224-5229. PMID: 1907267Sung Y.C., Fuchs J.A. The Escherichia coli K-12 cyn operon is positively regulated by a member of the lysR family. J. Bacteriol. 1992. 174(11):3645-3650. PMID: 1592818Kondorosi E., Pierre M., Cren M., Haumann U., Buire M., Hoffmann B., Schell J., Kondorosi A. Identification of NolR, a negative transacting factor controlling the nod regulon in Rhizobium meliloti. J. Mol. Biol. 1991. 222(4):885-896. PMID: 1840615Henikoff S., Haughn G.W., Calvo J.M., Wallace J.C. A large family of bacterial activator proteins. Proc. Natl. Acad. Sci. U.S.A. 1988. 85(18):6602-6606. PMID: 3413113Thony B., Hwang D.S., Fradkin L., Kornberg A. iciA, an Escherichia coli gene encoding a specific inhibitor of chromosomal initiation of replication in vitro. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(10):4066-4070. PMID: 2034653","","","

InterPro
IPR000847
Domain

Bacterial regulatory protein, LysR
PR00039	$\"[84-95]T$ $\"[95-105]T$ $\"[105-116]T$	HTHLYSR
PF00126	$\"[69-128]T$	HTH_1
PS50931	$\"[67-124]T$	HTH_LYSR

InterPro
IPR005119
Domain

LysR, substrate-binding
PF03466	$\"[152-359]T$	LysR_substrate

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[67-153]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[153-267]T$	no description

","BeTs to 12 clades of COG0583COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000847 (Bacterial regulatory protein LysR, HTH motif) with a combined E-value of 4.1e-18. IPB000847 72-116***** IPB005119 (LysR substrate binding domain) with a combined E-value of 7.9e-12. IPB005119A 84-106 IPB005119B 113-124","","","-54% similar to PDB:1I6A CRYSTAL STUCTURE OF THE OXIDIZED FORM OF OXYR (E_value = 4.3E_29);-53% similar to PDB:1I69 CRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYR (E_value = 6.2E_28);","Residues 69 to 128 (E_value = 3.4e-20) place ANA_2305 in the HTH_1 family which is described as Bacterial regulatory helix-turn-helix protein, lysR family.Residues 152 to 359 (E_value = 5.1e-43) place ANA_2305 in the LysR_substrate family which is described as LysR substrate binding domain.","","regulator (oxyR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2306","2489890","2491323","1434","5.81","-7.19","51523","TTGCGCCCTCCAGTGTCGGCTCGGCCACGTACCCGTGACTTTGGTCGTCCCCGACTCGCTCCGCCTCCGCAGCCCGCCGCGCTCGCGGCCCGGATCGGACCGGGGCGCTGCCCGAATGCTGTCCGGGGCGCGGTCCTGACTACACTCGGGACCATGATCGACCTGCGTGCGCTTCGTGAGAACCCCGAGCCCTTCCGCGCCAGCCAGCGAGCCCGTGGAGCCGACGTCGATCTCGTCGACCGCGTCATCGCCGCCGACGAGACCCGCCGTCAGGCGCTGGCCGCCTTCGAGAACCTCCGCGCCGAGCAGAAGCAGGTCTCCCGGTCCGTGGGGAAGGCCTCCCCGGAGGAGCGCCCGGCGATCCTGGCCAACGCCAAGGAGCTGGCCGAGCAGGTCAAGGCCGCCGAGGCCGCCTCCTCGGCCGCCGCCGCCGAGCTCGACGACCTGGCCCGCCAGTTCGCCAACCTCATCGAGGGGGCGCCCTCGGGCGGCGAGGAGGACTACGTCGTCCTGCGCCATGAGGGCGGCGAGCCCCGCGACTTCGCCGCCGAGGGCTTCGAGCCCGCCGACCACCTGGCGATCGGCGAGGGCCTGGACATCATTGACACCCGCCGCGGCGCCAAGGTCTCCGGCGCCCGCTTCTACTACCTCAAGGGCTGGGGCATGCGCCTGGAGCTGGCGCTCATGACGGCCGCCCTGGACGCCGCCGTCGCCCACGGCTTCACCCCGATGACCACCCCCACCCTCGTCACCCCGCAGGTCATGGGTGGCACCGGCTTCCTGGGCGCCCACAGCGACGAGATCTACTACCTGCCCGCCGACGACCTCTACCTCACCGGCACCTCCGAGGTGGCCCTGGCCGGCTACCACGCCGACGAGATCCTCGACCTGTCCGCCGGCCCCAAGCGCTACATGGGTTGGTCCACCTGCTACCGGCGCGAGGCCGGGGCCGCCGGCAAGGACACCCGTGGCATCATCCGCGTCCACCAGTTCAACAAGGCGGAGATGTTCTCCTACTGCCGCCCCGAGGACGCCGAGGCCGAGCACGCCCGGCTCCTGGCCATGGAGGAGGAGATGCTGGCCCTGGTCGAGCTGCCCTACCGGGTCATCGACACCGCCGCCGGGGACCTGGGCTCCTCCGCCGCCCGCAAGTTCGACTGCGAGGCCTGGCTGCCCACCCAGCAGCGCTGGATGGAGGTCACCTCCACCTCCAACTGCACCACCTACCAGGCCCGCCGCCTGGCCGTGCGCGAGCGCCGCGAGGGCGGCACGAGCCCCGTGGCCACCCTCAACGGGACCCTGGCCACCACCCGCTGGATGGTCGCCATCCTGGAGAACCACCAGCAGGCCGACGGCTCGGTGCGCGTGCCCGCGGGCCTGCGCCCCTACCTGGGCGGCCTGGAGGTCATCGAGCCCGCCGGGGCCACCGCCTGA","LRPPVSARPRTRDFGRPRLAPPPQPAALAARIGPGRCPNAVRGAVLTTLGTMIDLRALRENPEPFRASQRARGADVDLVDRVIAADETRRQALAAFENLRAEQKQVSRSVGKASPEERPAILANAKELAEQVKAAEAASSAAAAELDDLARQFANLIEGAPSGGEEDYVVLRHEGGEPRDFAAEGFEPADHLAIGEGLDIIDTRRGAKVSGARFYYLKGWGMRLELALMTAALDAAVAHGFTPMTTPTLVTPQVMGGTGFLGAHSDEIYYLPADDLYLTGTSEVALAGYHADEILDLSAGPKRYMGWSTCYRREAGAAGKDTRGIIRVHQFNKAEMFSYCRPEDAEAEHARLLAMEEEMLALVELPYRVIDTAAGDLGSSAARKFDCEAWLPTQQRWMEVTSTSNCTTYQARRLAVRERREGGTSPVATLNGTLATTRWMVAILENHQQADGSVRVPAGLRPYLGGLEVIEPAGATA$","Seryl-tRNA synthetase","Cytoplasm","seryl-tRNA synthetase","seryl-tRNA synthetase ","seryl-tRNA synthetase","","Eriani G., Delarue M., Poch O., Gangloff J., Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 1990. 347(6289):203-206. PMID: 2203971Sugiura I., Nureki O., Ugaji-Yoshikawa Y., Kuwabara S., Shimada A., Tateno M., Lorber B., Giege R., Moras D., Yokoyama S., Konno M. The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. Structure 2000. 8(2):197-208. PMID: 10673435Perona J.J., Rould M.A., Steitz T.A. Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry 1993. 32(34):8758-8771. PMID: 8364025","","","

InterPro
IPR002314
Domain

tRNA synthetase, class II (G, H, P and S)
PF00587	$\"[224-394]T$	tRNA-synt_2b

InterPro
IPR002317
Family

Seryl-tRNA synthetase, class IIa
PR00981	$\"[314-326]T$ $\"[326-339]T$ $\"[366-379]T$ $\"[383-399]T$ $\"[401-417]T$	TRNASYNTHSER
PTHR11778	$\"[149-472]T$	SERYL-TRNA SYNTHETASE
PF02403	$\"[52-157]T$	Seryl_tRNA_N
TIGR00414	$\"[52-464]T$	serS: seryl-tRNA synthetase

InterPro
IPR006195
Domain

Aminoacyl-transfer RNA synthetase, class II
PS50862	$\"[190-457]T$	AA_TRNA_LIGASE_II

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.40	$\"[52-154]T$	no description
G3DSA:3.30.930.10	$\"[154-473]T$	no description

","BeTs to 24 clades of COG0172COG name: Seryl-tRNA synthetaseFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0172 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB002317 (Seryl-tRNA SYNTHETASE signature) with a combined E-value of 9e-40. IPB002317A 314-326 IPB002317B 326-339 IPB002317C 366-379 IPB002317D 383-399 IPB002317E 401-417","","","-51% similar to PDB:1SER THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH TRNA SER (E_value = 1.3E_60);-51% similar to PDB:1SES CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE (E_value = 1.3E_60);-51% similar to PDB:1SET CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE (E_value = 1.3E_60);-51% similar to PDB:1SRY REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION (E_value = 1.3E_60);-46% similar to PDB:1WLE Crystal Structure of mammalian mitochondrial seryl-tRNA synthetase complexed with seryl-adenylate (E_value = 1.6E_47);","Residues 52 to 157 (E_value = 1.1e-30) place ANA_2306 in the Seryl_tRNA_N family which is described as Seryl-tRNA synthetase N-terminal domain.Residues 224 to 394 (E_value = 8.3e-54) place ANA_2306 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T).","","synthetase (serS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2307","2491607","2492467","861","4.88","-16.13","30151","ATGCGGGACCTCGACGCCCTGGAGGCCGCCGGCGGCGCCCGGCTCGCGCCCGGCCACGGGCTCGTCGTCGCCCTCGACGTCGACGGCACCATCCTGGACATGGACGGGCACGTCTCGGAGCGGGTCTTGGCCTCCGTCGCCCGCCTGCGCGCCCACGAGGTCCCCGTGGTCATCTCCACCGGCCGCGGGATCGCCGCCGCCATGCCGGTGGTGCGCCACCTGGGGCTGTCCGCCGGCTGGATGGTGTGCGCCAATGGCGCCATGACCCTGCGGCTCGACCCTGACGCCCCCGGCGGCTACGAGGTCGTCGACTCGCGCACCTTCGACCCGCGCGCCGCCATCGAGACCCTCCACGCCGCCGTGCCCGACGGGATCCTCGCCGTGGAGGACCCCGGTGTCGGCTTCAAGGTCTCCCGGCTCTTCCCCGACGGCGAGCTCATTGAGGACCAGCGGGTCGTCACCTTCGACGAGCTCGTCTCCCAGTCGGTCACCCGCGTGGTCCTGCGGGCCCCGGGCATGCCGGTGGAGCGCTTCTCCCAGATCGTGGCCGACTCCGGGCTGCACTCGGTGGAGTACGCCATCGGCTGGACGGCCTGGCTCGACGTCGCCCCCGAGGGCGTCACCAAGGCCTCCGCCCTTGAGGCGCTCATCGCCCGCCTGGGCACCGACTCCGCCCACGTCCTGGCGGTCGGGGACGGCTCCAACGACGTCGAGATGATCGAGTGGGCCGGGGCCGGCGTCGTCATGGGCAGCGCGCCGCCGTGGGTGCGCGACCGCGGCGATATCCTGACCGAGCCCGTGTGGCGGGACGGCTGCGCGGCCGTCCTGGACGCCCTCATCGAACGAGTAAGGCACCCCTGA","MRDLDALEAAGGARLAPGHGLVVALDVDGTILDMDGHVSERVLASVARLRAHEVPVVISTGRGIAAAMPVVRHLGLSAGWMVCANGAMTLRLDPDAPGGYEVVDSRTFDPRAAIETLHAAVPDGILAVEDPGVGFKVSRLFPDGELIEDQRVVTFDELVSQSVTRVVLRAPGMPVERFSQIVADSGLHSVEYAIGWTAWLDVAPEGVTKASALEALIARLGTDSAHVLAVGDGSNDVEMIEWAGAGVVMGSAPPWVRDRGDILTEPVWRDGCAAVLDALIERVRHP$","HAD-superfamily hydrolase, subfamily IIB","Cytoplasm","HAD-superfamily hydrolase, subfamily IIBsubfamily, putative","hypothetical protein","HAD-superfamily hydrolase, subfamily IIB","","Koonin E.V., Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994. 244(1):125-132. PMID: 7966317","","","

InterPro
IPR000150
Family

Cof protein
PS01229	$\"[230-252]T$	COF_2

InterPro
IPR006379
Family

HAD-superfamily hydrolase, subfamily IIB
TIGR01484	$\"[22-249]T$	HAD-SF-IIB: HAD-superfamily hydrolase, subf

InterPro
IPR013200
Domain

HAD superfamily hydrolase-like, type 3
PF08282	$\"[23-276]T$	Hydrolase_3

InterPro
IPR013838
Binding_site

Beta tubulin, autoregulation binding site
PS00228	$\"[1-4]?$	TUBULIN_B_AUTOREG

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[22-280]T$	no description
PTHR10000	$\"[205-253]T$	PHOSPHOSERINE PHOSPHATASE

","BeTs to 17 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: RThe phylogenetic pattern of COG0561 is a-tky-vCEBrH--GPOlin-Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-45% similar to PDB:1RKQ Crystal structure of NYSGRC target T1436: A Hypothetical protein yidA. (E_value = 1.1E_13);-44% similar to PDB:1YMQ HAD Superfamily Phosphotransferase Substrate Diversification: Structure and Function Analysis of the HAD Subclass IIB Sugar Phosphatase BT4131 (E_value = 4.5E_10);","Residues 110 to 371 (E_value = 8e-06) place ANA_2307 in the S6PP family which is described as Sucrose-6F-phosphate phosphohydrolase.Residues 111 to 344 (E_value = 2.1e-06) place ANA_2307 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.Residues 114 to 367 (E_value = 7e-32) place ANA_2307 in the Hydrolase_3 family which is described as haloacid dehalogenase-like hydrolase.","","hydrolase, subfamily IIB subfamily, putative","","1","","","Wed Aug 8 15:12:17 2007","","Wed Aug 8 15:12:17 2007","","","Wed Aug 8 15:12:17 2007","Wed Aug 8 15:12:17 2007","Wed Aug 8 15:12:17 2007","","","Wed Aug 8 15:12:17 2007","","","Wed Aug 8 15:12:17 2007","Wed Aug 8 15:12:17 2007","","","Wed Aug 8 15:12:17 2007","Wed Aug 8 15:12:17 2007","","","","","yes","","" "ANA_2308","2492608","2494104","1497","5.03","-15.98","50962","CTGGCTGCGGCCAGCACCCTGACCCTGGCGGCCGCCGCCACCGCCGCCTGCTCAGCCCGTGGGACGGGCTCGGCCTCGGCCACCGGCTGCGCCGCCTACCAGGCCTACCAGGGCCACAAGGGCGCCACCGTCACCATCTCCAGCAGCCTGACCGGCACCGAGGCCGAGCGTTTCGAGGCCTCCGTGGCCGAGTTCGAGAGCTGCACGGGCATCAACATCGAGCACACCGGCACCACCGAGCTGCGCTCCCAGCTGCTCAACGGCTCGGGAGCCAACCTGTCCACCAGCTCGGGGGCCTCGCCGTCGAGCCAGGACAACCCCGAGAACCTGCCCGACCTGGCTATCGTGCCTCAACCCGCCATGGTGGCCGAGCTCGTCGACACCGGCGTCGTCCACCCGCTGCCCAACAAGGTCAACAGCAACGTGGAGGCCGGCTGGGACCGGCACTGGATCCAGGTCGGCATCCACGCCTCCGTGCCCTACGGCGCCCCGCTCATGGTCTCGCTGAAGTCCCTCGTGTGGTACTCGCCGGACGCCTTCGCCAAGGCCGGCTACGAGGTGCCCGACACGTGGGCCGAGCTGGAGGCCCTCACCAGCAAGATCCGCTCCGACCACCCCGACGGCTCCGTAACGCCCTGGTGCGTGGGCGCCGCCGATGGCGAGTCCACTGGCTGGGTTCTCACCGACTGGCTCGAGGACGCCCTGCTGGCCACCCAGGGGCCCGGCGTCTACGAGACCTGGGCCTCGCACCGGGTTCCCGTCGACTCCTCGAACGCGGTGGAGGCCCTCGGCGCTGTCAACTCCCTGGTTCTGGACAACGGGCGCGTCGCCGGTGGGCGCGGCTCGGTCATCTCCCGCACCCCCGTGCAGGCCGGGGCCGAGCTGGTCAAGGGCAGCTGCCTCATGCTGCACGCCTCCTCCTCCTTCGAGAGCCGCTTCCCCGAGGGCACTGTCATCACCGACGCCGACGGCGCCAACCCGGTGACGGTCCAGGCCCCCCACCCGACCGCGAGTGCCACCGCCAGTGGGGCGGCCGGGGCGACGGCGTCGGCCAAGGGTACGGCGGGTGCGACGACTCAGGCGGGTTCGGCTGGAACGAAGGTCTCGGCCTTCGTCACTCCGGCGGCGGACCGCGGCTCGGACTCGGTGCTGGTGGGCACCGACTACCTCGTGGCCTTCACCCGCTCGGACGCGGTCAGCGCGGTCATGGAGTACCTGACCTCCCAGGAGTGGGCCCGCACGCGGATGGCACTGGGTGGGGTGGCGACCGCCAACCAGGGTGTTGACCCGGACCTGGCGCCCAGCGACGTCGGCCGGCGCGCCACCAGGATGCTCCAGTCGCGCCAGACGACCGTTGAGATGGACGCCTCGGACTCCATGCCGGTGGGCGTGGGCAGCAGCGCCCTGTGGGTCGGGCTGAGCCGGTGGGCGACCGGGACGGTGACCCCCAAGGAGGCGCTCAAGCAGGCCGAGGCCGCCTGGCCCAAGCAGAAGTAG","LAAASTLTLAAAATAACSARGTGSASATGCAAYQAYQGHKGATVTISSSLTGTEAERFEASVAEFESCTGINIEHTGTTELRSQLLNGSGANLSTSSGASPSSQDNPENLPDLAIVPQPAMVAELVDTGVVHPLPNKVNSNVEAGWDRHWIQVGIHASVPYGAPLMVSLKSLVWYSPDAFAKAGYEVPDTWAELEALTSKIRSDHPDGSVTPWCVGAADGESTGWVLTDWLEDALLATQGPGVYETWASHRVPVDSSNAVEALGAVNSLVLDNGRVAGGRGSVISRTPVQAGAELVKGSCLMLHASSSFESRFPEGTVITDADGANPVTVQAPHPTASATASGAAGATASAKGTAGATTQAGSAGTKVSAFVTPAADRGSDSVLVGTDYLVAFTRSDAVSAVMEYLTSQEWARTRMALGGVATANQGVDPDLAPSDVGRRATRMLQSRQTTVEMDASDSMPVGVGSSALWVGLSRWATGTVTPKEALKQAEAAWPKQK$","ABC-type multiple sugar transport system, substrate-binding component","Extracellular, Periplasm","Bacterial extracellular solute-binding proteindomain protein","K02027 multiple sugar transport system substrate-binding protein","extracellular solute-binding protein, family 1","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR002155
Family

Thiolase
PS00099	$\"[12-25]?$	THIOLASE_3

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[1-413]T$	SBP_bac_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[171-270]T$	no description
signalp	$\"[1-19]?$	signal-peptide

","BeTs to 7 clades of COG1653COG name: Sugar-binding periplasmic proteins/domainsFunctional Class: GThe phylogenetic pattern of COG1653 is ---K--VCEBR------l---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 81 to 493 (E_value = 0.0015) place ANA_2308 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein.","","extracellular solute-binding protein domain protein","","1","","","Wed Aug 8 15:19:07 2007","","Wed Aug 8 15:19:07 2007","","","Wed Aug 8 15:19:07 2007","Wed Aug 8 15:19:07 2007","Wed Aug 8 15:19:07 2007","Tue Aug 14 17:08:17 2007","","Wed Aug 8 15:19:07 2007","","","Wed Aug 8 15:19:07 2007","","","","Wed Aug 8 15:19:07 2007","Wed Aug 8 15:19:07 2007","","","","","yes","","" "ANA_2309","2494392","2495741","1350","5.72","-16.03","50514","ATGGGACTGGGATGGTTCGGCGCCCCCGAGCACAAGCGTTGGCTGGCCTACGAGACGCACGCGCTGCTGCACTACGCGCGCGCCGCGCAGGTGCCTACAGGATTCGGGTGGATCGGTCAGGACGGCGAGGTGGACCCCGCCCATCCCGTCGAGCTGTGGATCACTGGCCGCATGACCTTCGCCTTCTCCCTGGGGGCGCTCATGGGGATCCCCGGCTGCCGCCGCTATGCCGACCACGGCGTGCGCGCCCTCAACGGACCCTTGCGCGACCCGGTCAACGGCGGCTGGTACTCGGCGATCGGCCCTGAGCCCGACGCCGAGGGGCGGGGCCTCCCGGTGGACCGCGACGCCCGCAAGGAGTGCTACCAGCACGCCTTCGTGCTCCTGGCCGCCGCCACCGCGACGGCCGCCGACCGGCCCGGTGGCCACGAGCTGCTGCGCGACGCCATCGAGATCCAGGACCGCTACTGGTGGGATGAGGGCCAGCAGATGCCGGTGGAGTCCTACGCCGCCGACTTCACCGACTCCGAGGACTACCGGGGCATCAACGCCGCCATGCACACGGTGGAGGCCTACCTGGCCACCGCCGACGTCACCGGTGAGGTGCGTTGGCTGGAGCGGGCCCTGAAGATCACCGACTTCGCCGTCAACGTCCAGGCCCGCGAGCACGGCTGGCGCCTGCCCGAGCACTACTCCGCCTCCTGGGAACCGCGCCTGGACTACAACCGCGACGAGCCCGCCCACCCCTTCCGGCCCTACGGCGTCACGCCGGGCCACGGGCTGGAGTGGGCGCGCCTGACGGTGCAGCTGCGCGGGGCGCTCATCAACCGCTCCATGAGCGCGCCGGAGTGGATGCTGGAGGCCGCCGAGCACATCTTCGATCAGGCCCGCATCGATGGCTGGCGGGTCGACGGCGCCCCCGGCTTCGTCTACACCACGGACTTCGACGGCAAGCCCGTGGTGCATGAGCGCATGCACTGGGTGGTCTGCGAGGGCATCTCGGCGTCGGCCGCCATCCGCCAGGCCCTGCTCGACGACGGGCGTGGGGAGATCGACGTCGAGCACTACGAGCACTGCTATCGGGCCTGGATCGACTACGCCGAGGAGTTCCTCATCGAGGCGCCCGGCGTGTGGACCCATGAGCTCGACCGCGACAACCGGCCCTCGACCCGCACTTGGGCTGGGCACCCGGACATCTACCACGCCCTGCAGGCCACCCTCATGGCGCGCCTGCCGGTGTGGCCGGCGATCGGGCAGGCCCTGGCCGAGGGGCGGCTCGACGAGCCGAACTCGCTGCTGCCGGCGCGCGCCAGCAAACCGCACCGGCGCGGGTTCTTCGGGCGGGCCTAG","MGLGWFGAPEHKRWLAYETHALLHYARAAQVPTGFGWIGQDGEVDPAHPVELWITGRMTFAFSLGALMGIPGCRRYADHGVRALNGPLRDPVNGGWYSAIGPEPDAEGRGLPVDRDARKECYQHAFVLLAAATATAADRPGGHELLRDAIEIQDRYWWDEGQQMPVESYAADFTDSEDYRGINAAMHTVEAYLATADVTGEVRWLERALKITDFAVNVQAREHGWRLPEHYSASWEPRLDYNRDEPAHPFRPYGVTPGHGLEWARLTVQLRGALINRSMSAPEWMLEAAEHIFDQARIDGWRVDGAPGFVYTTDFDGKPVVHERMHWVVCEGISASAAIRQALLDDGRGEIDVEHYEHCYRAWIDYAEEFLIEAPGVWTHELDRDNRPSTRTWAGHPDIYHALQATLMARLPVWPAIGQALAEGRLDEPNSLLPARASKPHRRGFFGRA$","N-acylglucosamine 2-epimerase","Cytoplasm","putative isomerase","hypothetical protein","N-acylglucosamine 2-epimerase","","Itoh T., Mikami B., Maru I., Ohta Y., Hashimoto W., Murata K. Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution. J. Mol. Biol. 2000. 303(5):733-744. PMID: 11061972","","","

InterPro
IPR010819
Family

N-acylglucosamine 2-epimerase
PF07221	$\"[34-405]T$	GlcNAc_2-epim

InterPro
IPR012341
Domain

Six-hairpin glycosidase
G3DSA:1.50.10.10	$\"[35-421]T$	no description

","No hits to the COGs database.","***** IPB010819 (N-acylglucosamine 2-epimerase) with a combined E-value of 3.3e-10. IPB010819B 97-149 IPB010819C 251-300 IPB010819C 227-276","","","-57% similar to PDB:2AFA Crystal Structure of putative NAG isomerase from Salmonella typhimurium (E_value = 2.2E_99);-75% similar to PDB:1EA9 CYCLOMALTODEXTRINASE (E_value = 2.2E_99);","Residues 34 to 405 (E_value = 2.5e-114) place ANA_2309 in the GlcNAc_2-epim family which is described as N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase).","","isomerase (AF220438)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2311","2496285","2497754","1470","8.75","4.32","51212","ATGACCAAGAGAGACACCTTCCGCGATACCGAACTGACGAACGGGGGGGGGGAGATGACGGAAGATTCTCTAGACATAACAGTCAGCGCTCGGCAGTGGATCGGGTTGTGCGCGTTGGCTGGTGGGTACTTCATCGCTCTCCTCGATCTGACAATTATTAACCTCGCAGTTCCCTCGCTGACACGGGACCTGGGCGCGTCCACAGCACAGGTTTTCTGGGCGGTCAACAGCTACGGTCTCGTCCTCGCACTGGCGATCATCCCGTCAGGTCGTTTAGGTGACCGATTCGGGCACCGACGCCTCTTCCTCCTGGGAACGATCGTCTTGGCAGTTGCCAGCCTCGCCTGCGGTGCCGCGACCTCTCCGTTCGTCTTGATCGCCAGCCGGTTCCTTCAGGGGCTCGGTGCCGGCATGCTGGTACCGCAGACTCTCACGCTCATCGGCGTCACCTTCCCTGAAAATATCCGTGGGCGCGCAGTCGGCATCTGGGGGTCAATTGCAGGAACTGCGTCCGTCGTCGGCCCCCTTGCTGGCGGAGTATTGATTGATGGGCTCAGCTGGCGCTGGGTCTTCCTCGTCAACCTTCCGATTGCTGTTCTTGTCGTGATTCTGGGCATGAGAAGTCTTCCGATCGAGGTGGTCCGGTCCGTGAGGGTTGATTTCGTGGGAACCTTTCTTGCGGGCATCGGCCTTGTGGCACTTCTCTATGGAAGCCTGCAAGGCCCCCATGCGGGCTGGGACCCGCTGACCATTGCTTGCCTGCCGTTCGCTGTGCTCTGCCTGTTTGCTTTCTTCCGGTATGAACGTCGTGCGGATCCGGCGTACGCAGTTTTTCCGCAGTCTCTTCGCAAGAATCCGCGGTTCCTCACTGCTGCCGTATTCGGTCTAATTGTGGCCCTTGGTGTATTCGCCTTGACATTTCTCGTATCGAACTACATTCAGTCCGTGATGGGGCAAGCGGCAGTCTGGGCGGGGGCTGCTCTTGCGCCGGCGTCGATTGCTTCTGTGGTCACAGCACCTATCGCGGGTTACTGGGTTGATGAAGGAAAGGCCCGCCTCGTGCTACAGATCGGCTTCGGGGCGTCCGCGATGGGAACCGCCCTGAGCATGCTGATTGCCGCTACTGGGGTTTCTTGGATGTGGTTCCTGGGGGCGACTATCGTTTTCGGTGTCGGAAATGGCTTCTTGATGGCGCCACTGACAACAGTAGGTATGGCCGCACTGAGGAGTGACGAGTTCGGTGCTGCATCCTCCCTTCTCAACGTCCTTCGCCAAGCCGGTCCCGTGCTAGGGGGAGCTGTTGTCGGGCTCTTGATACAGGTGCTCGCTGCCGCGCCTACTGATGTCGACCCGCTGGGGCTATCGAGGTCGACCGTTGCCTGGGTGTTGAGTGTTCCATTGCTGCTGTTTTTTATCGGTCTCTTTGTGTATTCGTTCGTTCCGAGGTCGCTGGTGTCGGCAATGGACTGA","MTKRDTFRDTELTNGGGEMTEDSLDITVSARQWIGLCALAGGYFIALLDLTIINLAVPSLTRDLGASTAQVFWAVNSYGLVLALAIIPSGRLGDRFGHRRLFLLGTIVLAVASLACGAATSPFVLIASRFLQGLGAGMLVPQTLTLIGVTFPENIRGRAVGIWGSIAGTASVVGPLAGGVLIDGLSWRWVFLVNLPIAVLVVILGMRSLPIEVVRSVRVDFVGTFLAGIGLVALLYGSLQGPHAGWDPLTIACLPFAVLCLFAFFRYERRADPAYAVFPQSLRKNPRFLTAAVFGLIVALGVFALTFLVSNYIQSVMGQAAVWAGAALAPASIASVVTAPIAGYWVDEGKARLVLQIGFGASAMGTALSMLIAATGVSWMWFLGATIVFGVGNGFLMAPLTTVGMAALRSDEFGAASSLLNVLRQAGPVLGGAVVGLLIQVLAAAPTDVDPLGLSRSTVAWVLSVPLLLFFIGLFVYSFVPRSLVSAMD$","Puromycin:H+ antiporter","Membrane, Cytoplasm","Puromycin resistance protein pur8","drug transporter","drug resistance transporter, EmrB/QacA subfamily","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR001411
Family

Tetracycline resistance protein TetB
PR01036	$\"[38-62]T$ $\"[129-149]T$ $\"[159-183]T$ $\"[323-347]T$ $\"[381-401]T$	TCRTETB

InterPro
IPR004638
Family

Drug resistance transporter EmrB/QacA subfamily
TIGR00711	$\"[33-480]T$	efflux_EmrB: drug resistance MFS transporte

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[35-484]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[39-440]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[20-223]T$ $\"[274-482]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57	$\"[20-223]T$ $\"[274-482]T$	DRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
tmhmm	$\"[33-53]?$ $\"[72-92]?$ $\"[101-121]?$ $\"[131-151]?$ $\"[161-181]?$ $\"[187-206]?$ $\"[221-239]?$ $\"[249-267]?$ $\"[288-308]?$ $\"[322-344]?$ $\"[354-374]?$ $\"[380-400]?$ $\"[426-446]?$ $\"[460-480]?$	transmembrane_regions

","BeTs to 22 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 39 to 440 (E_value = 4.7e-59) place ANA_2311 in the MFS_1 family which is described as Major Facilitator Superfamily.","","resistance protein pur8","","1","","","","","","","","","","","Tue Aug 14 17:11:36 2007","","Tue Aug 14 17:11:36 2007","","","Tue Aug 14 17:11:36 2007","","","","Tue Aug 14 17:11:36 2007","Tue Aug 14 17:11:36 2007","","","","","yes","","" "ANA_2312","2498387","2498139","249","11.48","4.90","9377","GTGCGAGTGAGAACCGCCAACATTGACAGACCCCGCCCACAGTGCGGAGGTCGGTCAACGAGAGAGCGCTCGGTGGCCTTCCAGCCCCAAGCCACGGGCGCGATGCGCCTCCAGCGCCTGCCTGCCGAGATGCTCACTACCCAGCAGCTCACCGACGATACGGACAGCCTCGTCCCAGTCGATCGCCTCCGGCGCATACGCCTTGGCCAGGGCTGGATAGTCTTCCCGGAGTTCTTCACGAACCCTTGA","VRVRTANIDRPRPQCGGRSTRERSVAFQPQATGAMRLQRLPAEMLTTQQLTDDTDSLVPVDRLRRIRLGQGWIVFPEFFTNP$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2314","2498864","2498478","387","4.50","-10.36","14000","ATGACGACCTTCGTTCCCAACAGCGTCATCCTCTACGTCTCCGACGTCGAGGCGAGTACCACCTTCTACAGCCAGATTCTCGGTCATGAACCGATCAAGACCTATCCAGGATTCAGCGTCTTCGCATTGTCCGACGACGTCACTCTCGGCCTGCAGGCAGCCGACGAGATTGAACCCACTGCCGAGCCATACGTAGGCGGGACCGAACTGAGTCTCAGCAACGTCGAGCGTGCCGACGTCGATCGTCTTCACGCGCAATGGAAGAAGCTGGGCATTCCGATGGTTCTGGAGCCGACCGTCCTCGAATTCGGCTACACCTTTGTGGCAACAGACCCCGATGGGCACCGCCTGCGTGTGTGCGCCACTGATACCTCGAGCTTCGTCTGA","MTTFVPNSVILYVSDVEASTTFYSQILGHEPIKTYPGFSVFALSDDVTLGLQAADEIEPTAEPYVGGTELSLSNVERADVDRLHAQWKKLGIPMVLEPTVLEFGYTFVATDPDGHRLRVCATDTSSFV$","Glyoxalase/bleomycin resistance protein/dioxygenase","Cytoplasm","EhpR","hypothetical protein","Glyoxalase/bleomycin resistance protein/dioxygenase","","Kim N.S., Umezawa Y., Ohmura S., Kato S. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 1993. 268(15):11217-11221. PMID: 7684374Harayama S., Rekik M. Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J. Biol. Chem. 1989. 264(26):15328-15333. PMID: 2670937Asturias J.A., Eltis L.D., Prucha M., Timmis K.N. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases. J. Biol. Chem. 1994. 269(10):7807-7815. PMID: 8126007Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 1995. 270(5238):976-980. PMID: 7481800","","","

InterPro
IPR004360
Domain

Glyoxalase/bleomycin resistance protein/dioxygenase
PF00903	$\"[5-119]T$	Glyoxalase

InterPro
IPR011588
Domain

Glyoxalase/extradiol ring-cleavage dioxygenase
PD002334	$\"[11-115]T$	Q764R8_BBBBB_Q764R8;

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.10	$\"[7-119]T$	no description

","BeTs to 10 clades of COG0346COG name: Lactoylglutathione lyase and related lyasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0346 is aom-kzy--drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB000486 (Extradiol ring-cleavage dioxygenase) with a combined E-value of 5.3e-07. IPB000486A 7-28 IPB000486C 98-118","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 119 (E_value = 2.2e-10) place ANA_2314 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2315","2498942","2499952","1011","6.01","-5.99","37732","GTGTCACGTACGTGCGAGGATGAGCCGGTGCGTGCTGACCGCTTGCTGTCCATGATCTGGCTGCTGCGTACCCATGGTCGTCTGTCCGCCTCGGATCTGGCTCAGCGGCTGGAGGTCTCACGGCGCACCGTGCTGCGGGACGTTGAGGCGCTGTCGGCTGCGGGCGTGCCCGTATGGTGCGAGCGAGGACCTCATGGGGGAGTGAGAATCGACCCCGGCTTTCGCATTGATGTGACGGGACTGAACCGTGAGGAGAGCCGGGCTCTCTTCGCAGGTCTCACCAGCTGGGGTGCTGTGCCACTGGGCCTTGGCGACGCCCTCGCCTCCGCGTCTCGCAAACTGCTCGCCGCCGTGCCCGACAGCCATCGAAGCCGGTCCATTGGCATTGCCTCGCGCGTCGTGGTCGATCCTCAAGGGTGGCTTCCCCTTCCCGAGAGCGAGCGGGCCGACGCCGTCTTCCAAGCTGTTCAGGAAGCGGTCTTGACGCGCCATCGACTGCGTATGGTCTTCCGTCACAAGTCGAGGACGACGACGCAGGACGTCGTCGATCCGCACGGAATAGTTGCCGCTGGTCGCAGCTGGTACCTGTGTGCCTCACACGGCACCGAGGTTCGCTTCACCAGGCTCTCTCGGATCGAAGAGGCTGATGTACTCGCTGAGGAGTGTGCTGACGACTCCGGCTTCGATATGGCCGCGGCATGGCGGAAACAGCGTGAGGAGTTTCTTGAAAGGTTCGAGGCGATCACAGCCACTGTCTGGGTGCGGGACGAGCGTTGGAGTGATGTGCAGGAGTGGACGTTGCGCGCAACGACGACCGAGGCAGAGGGTGAACCTCCCGGAGATGACGGATGGACCTGTCTCCAGCTGGAGTTCATGGACCACCTGCATGCCATGACGATTCTGCTTCGGCTCGGTCCGGATGCCTGCGTCGTCACCCCCAAGCGCCTGCGTCAGGACCTCCTCGACTACGTGGACCTTATGCGTGAGCGTTACCGTGCCGATGGGAACTGA","VSRTCEDEPVRADRLLSMIWLLRTHGRLSASDLAQRLEVSRRTVLRDVEALSAAGVPVWCERGPHGGVRIDPGFRIDVTGLNREESRALFAGLTSWGAVPLGLGDALASASRKLLAAVPDSHRSRSIGIASRVVVDPQGWLPLPESERADAVFQAVQEAVLTRHRLRMVFRHKSRTTTQDVVDPHGIVAAGRSWYLCASHGTEVRFTRLSRIEEADVLAEECADDSGFDMAAAWRKQREEFLERFEAITATVWVRDERWSDVQEWTLRATTTEAEGEPPGDDGWTCLQLEFMDHLHAMTILLRLGPDACVVTPKRLRQDLLDYVDLMRERYRADGN$","Transcriptional regulator, DeoR family","Cytoplasm","transcription regulator","hypothetical protein","Helix-turn-helix, type 11 domain protein","","Gajiwala K.S., Burley S.K. Winged helix proteins. Curr. Opin. Struct. Biol. 2000. 10(1):110-116. PMID: 10679470Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(19):9257-9261. PMID: 1409631","","","

InterPro
IPR001034
Domain

Bacterial regulatory protein, DeoR N-terminal
SM00420	$\"[14-70]T$	HTH_DEOR
PS51000	$\"[11-70]T$	HTH_DEOR_2

InterPro
IPR013196
Domain

Helix-turn-helix, type 11
PF08279	$\"[14-69]T$	HTH_11

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide

","BeTs to 6 clades of COG2378COG name: Predicted transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2378 is ---------dr-b-efg-snuj----Number of proteins in this genome belonging to this COG is 3","***** IPB013196 (Helix-turn-helix, type 11) with a combined E-value of 3.3e-09. IPB013196 33-55","","","No significant hits to the PDB database (E-value < E-10).","Residues 14 to 69 (E_value = 1.1e-17) place ANA_2315 in the HTH_11 family which is described as HTH domain.Residues 14 to 74 (E_value = 0.00083) place ANA_2315 in the HTH_DeoR family which is described as DeoR-like helix-turn-helix domain.","","regulator ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2316","2500764","2500054","711","7.21","0.64","26737","ATGGCGGAGAGCGGGCAGGCGGATGCGCGGGTCGCGGAGTTCATCACCGATCTGCGTCGGGCCCTGGCGGAGGCGGGCGACCCTGCCCGCGCCGAGCAGCAGCGGGCGTACCTGAAGTCCGAGATGGCGATGTACGGCGTCGGGGTCCCGGACACGCGGCGCCTCGCGCAACGGATCGCCGCCGCCCACAGCGATGTGTGGGCTGAGGCCGCCACCTGGGAGGTGACGCTGCGGCGCCTGTGGGACGGGGCGGCTCGCCGCGAGGAGCGCTATGCGGCGCTGGCCGTCATCCGTGCCAAGCTCTCCGCGACGCATGCCGGACGCATGGAGTCCCTGGCGCTCTACGAGCACTTTCTGCGCACGGGGCAGTGGTGGGATCTGGTCGATGAGACCTCCCACGCCGTCGGGCTGGTGGTGCGTGAGCATCCGGCTGCGGTGGCGCGCATACGTGTGTGGGCCACCGACCCGGACATGTGGGTGCGGCGCAGCGCCATCCTCTGCCAGCTCCAGCACAAGGCCGACACGGACCTCGACCTGCTCACCAATGTCATCGAGGTCAACCAGGAGGACCCGGAGTTCTTCATCCGCAAGGCCATCGGCTGGGCGCTGCGCGACTACGCGCGCACGGACGGCGACTGGGTGCGTGCCTTCGTCCAGGCGCATCCGGGCCTGTCCCCACTCAGCCGACGCGAGGCCCTCAAGCGCCTGTGA","MAESGQADARVAEFITDLRRALAEAGDPARAEQQRAYLKSEMAMYGVGVPDTRRLAQRIAAAHSDVWAEAATWEVTLRRLWDGAARREERYAALAVIRAKLSATHAGRMESLALYEHFLRTGQWWDLVDETSHAVGLVVREHPAAVARIRVWATDPDMWVRRSAILCQLQHKADTDLDLLTNVIEVNQEDPEFFIRKAIGWALRDYARTDGDWVRAFVQAHPGLSPLSRREALKRL$","DNA alkylation repair enzyme","Cytoplasm","DNA alkylation repair enzyme","hypothetical protein","DNA alkylation repair enzyme-like","","","","","

InterPro
IPR014825
Family

DNA alkylation repair enzyme
PF08713	$\"[26-236]T$	DNA_alkylation

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-46% similar to PDB:2B6C Predicted DNA alkylation repair enzyme from Enterococcus faecalis. (E_value = 4.9E_16);-54% similar to PDB:1S9H Crystal Structure of Adeno-associated virus Type 2 Rep40 (E_value = 4.9E_16);-54% similar to PDB:1U0J Crystal Structure of AAV2 Rep40-ADP complex (E_value = 4.9E_16);","Residues 26 to 236 (E_value = 5.9e-63) place ANA_2316 in the DNA_alkylation family which is described as DNA alkylation repair enzyme.","","alkylation repair enzyme","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2318","2501122","2502639","1518","5.16","-8.90","51204","GTGCGCAGCAGCGTGCCGGGGCTTCGTCGTTGCCGGAGCACCCGTCGCGGCGGCCCGGAGACCTCCCAACGGCCGGCCGAGACCGCGAATCGGCCCTGCGGTCGCAGCGTTCGCCTCTGGCCGATCGGGGTGCCTGTGTGTCTTCCGGCGCAGATCCGGGATAGCGTGATGCTGTACTCGACTGAGAGGGACCTCATGTCTGACCACGACGCAACCCAGCCGCCGACCTCCGGCTCGCCCCGCCCCAACCAGGGCGATGAGTTCAACGCCCGGACCGTCCTCATCAACCAGGACATGCTCGACGCCGCGCGCGCCGAGCAGCAGACCCCGGGGCAGGCTCCCGGCGCCGTCCCTGGTGCGGTTCCCGGCGCCCAGGCCGGATCATGGCGCCCGGCGCAGCCCGACCTGCCCGCTGGGCCGCCCCCTGAGGAGCAGACGCGCGCCTTCTCCGCAGGTGCCGCGCAGGCGGCCGCCCAGCCCGGTGCGGCGTCCGCCGACCCCTACATTCAGGCCAACCCCTTCGCTCAGCAGAGCGGGGCCACCCAACCGGCGCCCTACAACCCGCCGACCCAGTTCGGCCAGGCCGACTCGACCGGCAGCGGCGGCCTCGGTACTGCTCAGCCCGGTGCGGCGTCGGCCGACCCCTACGCGCAGGCCAGCCCCTTCGCTCAGCAGAGCGGGGCCGCCCAGCCGGCGCCCTACAACCCGCCGGCGCAGCCCGCCTGGGGTGGGGCACCCGCCGACGACGGCGCCGCAGCCGCGTCGTCGCCCTTCGCCCAGTCCGCCCCCGGGATCCCCTCGGCCCCGGGCACCTCCTCGGCCTCCGCCGCCGGTGCGGCCGCAGGCGGCGAGGCGAGTCGGGGGGCCTCGCAGTGGCCCGGTCAGCAGCCGCAGGGCCAGCCGTCGGGCCTGCAGGACCAGCACCCCTTCGCCCAGCAGCCCGCCCAGCACTCGCACCCCTTCAGCGGGGGCCGTCAGGACGGCGAGGTCGGCATGTCCTCGGTCTTCCCCACGGCGACCGCACGCGCTGAGACCGAGCAGGCCACGGAGGCCTTCGTCCCCGACGCGACTCAGGCGGTCGCCTCGTCCGCGCCGTCGTCCTCAGCTTTCCCGTCGCAGAGCTCGGCCCCCCAGTGGGGCTCGGCCCCCTCCTCCGACGCCGCAGCCGGGCAGGCCCCGTCCTTCTCCGACATGGTTCCTACCGCAGCTGGCTCGCCCTTCGATCGGCCGGCAGGAGGCGGAGCCCTGGCAGCAGCCCGCTCCGAGGAGGTCGAGACCGCGGACTCCGTGGGCAGCTGGATGCTGACGCTGTTCCTCATGGCCATCCCCGTCGTCAACCTCGTCTGGCTGCTCATGCTCGTCTTCGGCAGCGGCCACTCCGCCAGCAAGAGGAACTGGGCTAAGGCCTCTCTCATCTGGATGGTGATCAGTCTCGTCCTGAGCATCGCCTTCTTCTTTGTGCTCAGCATGCTCGGTTACTCGCTCTTCGCTATCAACCAGAGCGCCAGCGTCGGATAG","VRSSVPGLRRCRSTRRGGPETSQRPAETANRPCGRSVRLWPIGVPVCLPAQIRDSVMLYSTERDLMSDHDATQPPTSGSPRPNQGDEFNARTVLINQDMLDAARAEQQTPGQAPGAVPGAVPGAQAGSWRPAQPDLPAGPPPEEQTRAFSAGAAQAAAQPGAASADPYIQANPFAQQSGATQPAPYNPPTQFGQADSTGSGGLGTAQPGAASADPYAQASPFAQQSGAAQPAPYNPPAQPAWGGAPADDGAAAASSPFAQSAPGIPSAPGTSSASAAGAAAGGEASRGASQWPGQQPQGQPSGLQDQHPFAQQPAQHSHPFSGGRQDGEVGMSSVFPTATARAETEQATEAFVPDATQAVASSAPSSSAFPSQSSAPQWGSAPSSDAAAGQAPSFSDMVPTAAGSPFDRPAGGGALAAARSEEVETADSVGSWMLTLFLMAIPVVNLVWLLMLVFGSGHSASKRNWAKASLIWMVISLVLSIAFFFVLSMLGYSLFAINQSASVG$","Hypothetical protein","Extracellular, Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[430-450]?$ $\"[471-491]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB007758 (Nsp1-like, C-terminal) with a combined E-value of 1.3e-06. IPB007758B 147-184 IPB007758C 240-284 IPB007758B 261-298 IPB007758B 243-280 IPB007758B 266-303 IPB007758C 246-290","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2320","2504899","2502971","1929","5.26","-17.88","66769","ATGACGCCGGGTCGGGCTACCCCGACATCATCCGTCCAGTCAACCGCATGGTCTATTCTTCCTGGAGGCGGGAGAATCGTAGCCATGAGACACCTACGAACATCCTCGCCACCCCAGACCACCTCACGACTGACCCTCCTCACCCTGCTCGGTGCGCTCACCGCCTGCAGCATGCTCGGCACAAGCGCCACAGCCGTCGCCACACCACCCGCGCAAGGAGCCCAGCACGCCGTCGTGCTGGACAACAGCACCAACGCCGGCAGTGCCGCCGGCACCTCCCAGACCACCGGCAGCAACAGCTCCAGCGGCTCATCGAACGGTTCCGGCGGTTCCAGCGGTTCCCATGGATCCAACGGGTCAACGGGGGCCACGATCCCCAAGGGGCTGGAGTCCTTCTACCGTCAGAATCTCACCTGGACCGACTGCCCCGACGGCGCCACCGGCACCGCCTTCAAGTGCGCCACCGTGACCGTGCCCCTGGACTACGACCACCCGCAGGGCAAGACCATCACGGTGGCCCTCAAGAAGCTGCCCTCGACGAGCTCCTCCCCTCGGGGCTCGGTCTTCCTCAACCCCGGAGGCCCCGGGGGAAGCGGTATCTCCCTCATCAATGCCCAGGCCGGGCTCTACACGAGCGGCGGCCTGTCGGGGGTCCTGGAGAACTACGACGTCATCGGCTTCGACCCGCGCGGCATCGGCCAGTCCACCCCCATCACCTGCTGGTCCCCCGACGACGTTCAGGCGATTATGGCCGGGCGGGCCGAGGCCCCCTCCCAGCTGACGCCGGGCAGCGCCACTGACATCGTTGCGAAGGGATCGCGCGAGGCCGCGGCCTGCCAGAAGTACACGGAGGTCCCTGAGATCCTCGACCACATGGACACCCGTTCGGTGGCCCGTGACATGGATGTCATGCGGGCCCTGGTGGGAGACCGGGACCTCAACTTCTTCGGGTACTCCTACGGCACCTACCTGGGGGCCGTGTACACCGAGCTCTTCCCCGACAACGTCGGGCGCGTCGTGCTGGACAGCGCCATGGACCCCACCCTGTCCCGGCAGGAGGCCTTCGAAGGCGATGCGGCGGCCGGGGAGCAGATACTGCGCACCTATATCGAGTCTCAGCACGGCCAGGCCGGGTTCCCCCTGAGCGGCACAACGGATGAGGCCGTCTCCCGGCTCGCGACCTTCCTCGACGGCCTGGACGCCAAGCCGCTGACCGTCTCCGACGGCGGAGACCCCGTGGACCGGGCCGAGGCCACTACGGCGATCAGAACGCTCGTCGTCGCCTCACCTGAGAACTGGCCACTGCTCAACGAGGGACTGGCCCAGGCCATGAGCTCACACGACGGCACCACTCTGATGAAGAATGCCGAGTCCCTCTCGGGCGGTGAGGAGTCTCCTGGGACCGAGGAGCAGACCGTCGAGCTGCTCCAATCCGTGTACGCCTTCTCGGCCAACCGGTGCCTCGACTTCCCCGACACCGGGAACCAGGCGAGCTGGGATGCGGCACTGTCCTCCTACCGCCGCGACTACCCGGTCTTCCACCCCCTGCTGCCCCAGCACGACGCCTACTGCCACGGCTGGGGGCACACCAGTAAGACCAAGCCCGTCGATGTCGACGTCGACGCCACGAACCCGGTGCTCGTCATCGGCATCCTGCACGACCCGCAAACGCCTTACGCGTGGTCCAAGGCGCTGGTGTCGAGGCTCCGTAACAGTCACCTGCTGAGCGTCGACATGTACGGCCATGGCGCGACCGGCCCCAATTCCTGCACAACCGCGAAGGTGAACGACTACTTCGTCAAGGGAGCGCTTCCCTCCGACGGCGAGGTCTGTGCGGCGAACCCGAAGCCCCAGGCCGGTCAGGAGACTCCGGCCGGAGTTGCGCGTCCAGCTGGACGTGAGCGTCCGTCCGGCTTTGAGGCCGGCTGA","MTPGRATPTSSVQSTAWSILPGGGRIVAMRHLRTSSPPQTTSRLTLLTLLGALTACSMLGTSATAVATPPAQGAQHAVVLDNSTNAGSAAGTSQTTGSNSSSGSSNGSGGSSGSHGSNGSTGATIPKGLESFYRQNLTWTDCPDGATGTAFKCATVTVPLDYDHPQGKTITVALKKLPSTSSSPRGSVFLNPGGPGGSGISLINAQAGLYTSGGLSGVLENYDVIGFDPRGIGQSTPITCWSPDDVQAIMAGRAEAPSQLTPGSATDIVAKGSREAAACQKYTEVPEILDHMDTRSVARDMDVMRALVGDRDLNFFGYSYGTYLGAVYTELFPDNVGRVVLDSAMDPTLSRQEAFEGDAAAGEQILRTYIESQHGQAGFPLSGTTDEAVSRLATFLDGLDAKPLTVSDGGDPVDRAEATTAIRTLVVASPENWPLLNEGLAQAMSSHDGTTLMKNAESLSGGEESPGTEEQTVELLQSVYAFSANRCLDFPDTGNQASWDAALSSYRRDYPVFHPLLPQHDAYCHGWGHTSKTKPVDVDVDATNPVLVIGILHDPQTPYAWSKALVSRLRNSHLLSVDMYGHGATGPNSCTTAKVNDYFVKGALPSDGEVCAANPKPQAGQETPAGVARPAGRERPSGFEAG$","Protease","Extracellular, Periplasm","tripeptidylaminopeptidase","protease","TAP domain protein","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[222-350]T$	Abhydrolase_1

InterPro
IPR013595
Domain

Peptidase S33, tripeptidyl-peptidase C-terminal
PF08386	$\"[510-611]T$	Abhydrolase_4

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[198-584]T$	no description

","BeTs to 3 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 222 to 596 (E_value = 1.8e-09) place ANA_2320 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.Residues 510 to 611 (E_value = 5.3e-19) place ANA_2320 in the Abhydrolase_4 family which is described as TAP-like protein.","","(AE005334) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2321","2506138","2504930","1209","5.11","-16.96","42539","ATGACCAGCCCGTCCGCACCCCAGCCCACTGCTCAGACCGAGTGTTCCCAGCCGCCGGCCGCCCGCACCTTCCCCGTCCACCACCACCCGACGTCGTCGGCCCCTGACCCGCAGCTCCGCCTGGAGACGCTGCTGGTGCGCTCGGGCACCGGGACCGACCCGGCCACGGGGGCGATCACGACGCCGATCCACCTGTCGACCGCCTACGGTCACCCGGGTCTGGGCGAGTCGACGGGCTACGACTACACGCGCACGGCCAGCCCGACCCGCGACGTCCTGCAGGACGCCCTGGCCCGCCTGGAGGGCGGGACGGCGGCCTTCGCCCTGTCCTCGGGGATGGCGGCCCTGGAGCTGGTGACCCGCACGCTGGCGCCGCACGGCAGCCGGATCGTGGCGCTGCGCGACCTGTACGGCGGCTCCTTCCGCTTCCTGGAGGTCCTGGCCGAGGAGGGGGCGGCGCGCATCGACTTCGTGCTGGGCCTTGAGGGGCTACGCGGGGCCCTGGCCGACCCGGCCGACCTGGTCATCATCGAGACCCCCACGAACCCGATGATGGAGGAGATCTCCATCCCCGAGGCGGCCGAGCTGGCCCATGCGGCCGGGGCGAGGCTGGTCGTGGACAACACCTTCTACACCCCGGTGGTGCAGCGGCCCCTGGAGCTGGGGGCCGACGTCGTCGTCCACTCGGGCACGAAGTACCTCGGCGGGCACAACGACGTCATGGCGGGCGTGGCCGTGGTGGCCGACGACGCCCTGGCCGAGCAGCTGAACTACCGGCTCAACACAACCGGGGCGACGCTGGGTCCCTTCGACTGCTTCCTGCTGCTGCGCGGGCTGAAGACCCTGGCGCTGCGCATGGAGCGTCACGAGGCCAACGCCACCGCGATCGCGCAGTTCCTGCGCTCGAGCCCCTACGTGACGCGGGTGCTCTACCCGGGGCACTCGGGCATGGTGAGCTTCGATCTGGCCGAGTCGGTGGACGTCGCCCGCTTCCTGGCATCGGTGCGGGTGTTCACCTTCGCCGAGTCCCTGGGCGGCGTGGAGTCGCTGGTGACGTGCCCGTCGGTGCAGACGCACGCGGACGTGCCCGTCGAGGTGCGCGCCTCCTACGGGCTGACCGACCAGCTCATGCGCCTGAGCGTCGGCATCGAGCACGTGGACGACCTCATCGCGGACCTGGCCCAGGCCTTCGAGGCCGCCACGGTCTGA","MTSPSAPQPTAQTECSQPPAARTFPVHHHPTSSAPDPQLRLETLLVRSGTGTDPATGAITTPIHLSTAYGHPGLGESTGYDYTRTASPTRDVLQDALARLEGGTAAFALSSGMAALELVTRTLAPHGSRIVALRDLYGGSFRFLEVLAEEGAARIDFVLGLEGLRGALADPADLVIIETPTNPMMEEISIPEAAELAHAAGARLVVDNTFYTPVVQRPLELGADVVVHSGTKYLGGHNDVMAGVAVVADDALAEQLNYRLNTTGATLGPFDCFLLLRGLKTLALRMERHEANATAIAQFLRSSPYVTRVLYPGHSGMVSFDLAESVDVARFLASVRVFTFAESLGGVESLVTCPSVQTHADVPVEVRASYGLTDQLMRLSVGIEHVDDLIADLAQAFEAATV$","Cystathionine gamma-synthase","Cytoplasm","cystathionine gamma-synthase","cystathionine gamma-synthase ","Cystathionine gamma-synthase","","Bork P. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?. Proteins 1993. 17(4):363-374. PMID: 8108379Gorina S., Pavletich N.P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 1996. 274(5289):1001-1005. PMID: 8875926Luh F.Y., Archer S.J., Domaille P.J., Smith B.O., Owen D., Brotherton D.H., Raine A.R., Xu X., Brizuela L., Brenner S.L., Laue E.D. Structure of the cyclin-dependent kinase inhibitor p19Ink4d. Nature 1997. 389(6654):999-1003. PMID: 9353127Batchelor A.H., Piper D.E., de la Brousse F.C., McKnight S.L., Wolberger C. The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA. Science 1998. 279(5353):1037-1041. PMID: 9461436Jacobs M.D., Harrison S.C. Structure of an IkappaBalpha/NF-kappaB complex. Cell 1998. 95(6):749-758. PMID: 9865693","","","

InterPro
IPR000277
Family

Cys/Met metabolism pyridoxal-phosphate-dependent enzymes
PTHR11808	$\"[121-400]T$	TRANS-SULFURATION ENZYME FAMILY MEMBER
PF01053	$\"[42-398]T$	Cys_Met_Meta_PP
PS00868	$\"[224-238]T$	CYS_MET_METAB_PP

InterPro
IPR002110
Repeat

Ankyrin
PR01415	$\"[59-71]T$ $\"[211-223]T$	ANKYRIN

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[37-282]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[283-401]T$	no description

noIPR
unintegrated

unintegrated
PIRSF001434	$\"[43-402]T$	Cystathionine gamma-synthase
PTHR11808:SF15	$\"[121-400]T$	CYSTATHIONINE GAMMA-LYASE (GAMMA-CYSTATHIONASE)

","BeTs to 15 clades of COG0626COG name: Cystathionine beta-lyases/cystathionine gamma-synthasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0626 is -o-pkzy-vdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000277 (Cys/Met metabolism pyridoxal-phosphate-dependent enzymes) with a combined E-value of 1e-111. IPB000277A 79-103 IPB000277B 134-145 IPB000277C 170-203 IPB000277D 207-245 IPB000277E 264-306 IPB000277F 331-352 IPB000277G 376-393","","","-55% similar to PDB:1CS1 CYSTATHIONINE GAMMA-SYNTHASE (CGS) FROM ESCHERICHIA COLI (E_value = 2.7E_69);-55% similar to PDB:2NMP Crystal structure of human Cystathionine gamma lyase (E_value = 6.0E_61);-54% similar to PDB:1IBJ Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana (E_value = 9.6E_59);-50% similar to PDB:1Y4I Crystal structure of Citrobacter Freundii L-methionine-lyase (E_value = 1.4E_54);-49% similar to PDB:1N8P Crystal Structure of cystathionine gamma-lyase from yeast (E_value = 6.0E_53);","Residues 42 to 398 (E_value = 5e-170) place ANA_2321 in the Cys_Met_Meta_PP family which is described as Cys/Met metabolism PLP-dependent enzyme.Residues 84 to 323 (E_value = 0.001) place ANA_2321 in the Beta_elim_lyase family which is described as Beta-eliminating lyase.","","gamma-synthase (thiol)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2322","2507668","2506268","1401","5.17","-16.56","49626","ATGCATACCCGCCTCACCTCCGTCTCCAGCTCCGCCGACTCCACCGACTCCGCCTGTCCGGCCCGCCCTGACCTCACAGCCCCCCACGCGCCCACCGCCTCCTCCCCCGCGGCCGCCCTCACCTCGGCGGACCGCTCCGCCTTCTTCAACGCCACCGCCGTCGACCCGGCCGTCTTCGATGCGGTCCCCGACCGCCGCGGCACGGCTAGCCTCAAGTGGGACTCCGCCGTCAAGCGCGGCCGCCCCGAGGATGTCCTGCCCCTGTGGGTGGCGGACATGGACCACGCCACCGCACCGGCGGTCACCAGCGCCCTGCTGTGGCGCACCCGCCACGGCATTTTCGGCTACTCCGAGCCCGACGACGCCTACAACGCCGCCCTGACCGGCTGGTTCTCCCGCCGCTACGGCTGGCAGGTGGAGGCCGAGTGGAACACCGTGACCCCCGGCGTCGTTCCGGCCCTGGCCCTGGCGGTACGGGCCCTGACCGCACCGGGCGAGGCGGTCCTCATCGAGGAGCCCGTCTACTACCCCTTCCGCGACGTCGTCGAGGTCAACGAGCGCACCGTGGCCGCCGTCCCCCTCGTGCGTGACGCCGACGGCGTCTACCGCCGCGACCTGGCCGCCCTGGAGTCCACCATCGAGGCGACCGGTGCGCGCCTGCTGCTCCTGTGCAACCCGCACAACCCGGTGGGCCGGGTCTGGAGCCGGGAGGAGCTCGCCGCGCTGGAGGAGGTCACGGCCCGCCACGGCGTCGTCGTCGTGGCCGATGAGATTCACGCGGACCTGGCCCTGCCGGGTTGCGCGACGACGCCCTTCGCCTCCCTGAGCGAGGCGGCCGCCGCCCACACGATCACCTGCACCTCGCCGTCGAAGTCCTTCAACCTCGCCGGTCTGCAGGTCGCCAACATCCTCATCTCTGATGCCCGTCTGCGCAGGGCCTTCCGCCGAGAGCTGGCCACCACCGGCTACTCCCAGCCCAATACCCTGGGCCTGACGGCCTGCCGGGCCGCCTACGAGAGCGGGGACGCCTGGCTCGATGCCCTGCGCGAGCACATCGCGGCAGCCCGCGCCCATGTCGAGGCGCGCCTGGAGCGGATCGAGGGGATCGAGGCCGCCCCCTGCGAGGGCACCTACCTGCTGTGGCTGGACTGCTCGGGATTCCTGAAGGCCGCCGGGCTCGAGCCCGAGCAGCTCGACGAGGTCATGCTCAACGAGGCCGGGCTCTGGCTCGACGACGGCCGGATCTTCGGGGCCGGCGGCGAGGGCTTCACCCGCATCAACGTCGCCTGCCCCCGCGCCACCCTCGATGCCGCCCTGGACCGGTTGGAGGTGGCCGTGGTCGCCGTGACCGCCCGCTCCACCGCCCAGGCCGGGCACGGCCCCACCACCCTGTCCGCCTGA","MHTRLTSVSSSADSTDSACPARPDLTAPHAPTASSPAAALTSADRSAFFNATAVDPAVFDAVPDRRGTASLKWDSAVKRGRPEDVLPLWVADMDHATAPAVTSALLWRTRHGIFGYSEPDDAYNAALTGWFSRRYGWQVEAEWNTVTPGVVPALALAVRALTAPGEAVLIEEPVYYPFRDVVEVNERTVAAVPLVRDADGVYRRDLAALESTIEATGARLLLLCNPHNPVGRVWSREELAALEEVTARHGVVVVADEIHADLALPGCATTPFASLSEAAAAHTITCTSPSKSFNLAGLQVANILISDARLRRAFRRELATTGYSQPNTLGLTACRAAYESGDAWLDALREHIAAARAHVEARLERIEGIEAAPCEGTYLLWLDCSGFLKAAGLEPEQLDEVMLNEAGLWLDDGRIFGAGGEGFTRINVACPRATLDAALDRLEVAVVAVTARSTAQAGHGPTTLSA$","Aminotransferase","Cytoplasm","aminotransferase","putative aminotransferase ","aminotransferase, class I and II","","Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K., Okamoto A., Higuchi T., Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 1991. 266(4):2567-2572. PMID: 1990006","","","

InterPro
IPR004839
Domain

Aminotransferase, class I and II
PF00155	$\"[83-442]T$	Aminotran_1_2

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[97-341]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[100-450]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF21	$\"[100-450]T$	AMINOTRANSFERASE RELATED

","BeTs to 5 clades of COG1168COG name: PLP-dependent aminotransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1168 is ---------drlb-e--h--------Number of proteins in this genome belonging to this COG is 1","***** IPB001176 (1-aminocyclopropane-1-carboxylate synthase signature) with a combined E-value of 3.6e-14. IPB001176D 165-186 IPB001176E 215-239 IPB001176F 251-274 IPB001176G 282-306***** IPB011715 (Tyrosine aminotransferase ubiquitination region) with a combined E-value of 1.2e-06. IPB011715E 222-259 IPB011715C 145-188***** IPB004839 (Aminotransferase, class I and II) with a combined E-value of 2.7e-06. IPB004839A 212-232 IPB004839C 290-301","","","-51% similar to PDB:1C7N CRYSTAL STRUCTURE OF CYSTALYSIN FROM TREPONEMA DENTICOLA CONTAINS A PYRIDOXAL 5'-PHOSPHATE COFACTOR (E_value = 2.8E_57);-51% similar to PDB:1C7O CRYSTAL STRUCTURE OF CYSTALYSIN FROM TREPONEMA DENTICOLA CONTAINS A PYRIDOXAL 5'-PHOSPHATE-L-AMINOETHOXYVINYLGLYCINE COMPLEX (E_value = 2.8E_57);-49% similar to PDB:1D2F X-RAY STRUCTURE OF MALY FROM ESCHERICHIA COLI: A PYRIDOXAL-5'-PHOSPHATE-DEPENDENT ENZYME ACTING AS A MODULATOR IN MAL GENE EXPRESSION (E_value = 2.7E_52);-43% similar to PDB:2O0R The three-dimensional structure of N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis (E_value = 1.6E_15);-43% similar to PDB:1GD9 CRYSTALL STRUCTURE OF PYROCOCCUS PROTEIN-A1 (E_value = 8.6E_14);","Residues 83 to 442 (E_value = 6.5e-42) place ANA_2322 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2322.1","2508276","2508479","204","7.26","0.15","6981","ATGGATATGATGAGTCAAGCCCTCCAGCTTTTCGTGAAGTTCGCCACCATTGGAGGTGGCCTGTGGACCGTTTGGGGGGTTATCACGCTGGCGGGAGGCCTGCGTGACCACCAGGGTCCGCAGATTCAGTCTGGTGTTTGGCAGGCTGTTGGTGGCGGCCTGATTGTGGCTGCGGCGCAGCTCTTCTCGAATATCGCCCTGTAG","MDMMSQALQLFVKFATIGGGLWTVWGVITLAGGLRDHQGPQIQSGVWQAVGGGLIVAAAQLFSNIAL$","Permease of the major facilitator superfamily","Extracellular","","","","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[10-32]?$ $\"[46-66]?$	transmembrane_regions

InterPro
IPR013212
Domain

Mad3/BUB1 homology region 1
SM00777	$\"[530-630]T$	no description

InterPro
IPR007921
Domain

Cysteine, histidine-dependent amidohydrolase/peptidase
PF05257	$\"[305-429]T$	CHAP
PS50911	$\"[300-444]T$	CHAP

noIPR
unintegrated

unintegrated
tmhmm	$\"[254-274]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 305 to 429 (E_value = 0.00014) place ANA_2325 in the CHAP family which is described as CHAP domain.","","TraG-related protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2325.1","2514979","2515797","819","6.01","-1.58","29685","ATGGATGACATGATAATCTACATGTTTAAAAAGCTGTTTGAGTTCGACACAAGTGAGGCAACAGGACTTAAACAGACGCTATCGGAGTACAGCAATGAAACATACAATGTTGTCACGTCATTGCACAACACAGGCATCAAGCCGGTAGCGTCTGTGATCATTTCGATGCTACTGGTGCTAGAGTTGGCGAGGAATGCCAGCCGAATCGAAGCGGACCAGCAGCTCGGCGTTAAAATTATTGCGGCCACGATGTTTAAGTCAGTGCTCCTTGTGTGGGCTGCCCAGAACGCCATGATGTTTCTTGATGCAATTAATCAGGTCGTTCAGAGTGTCGCTAAAAATATAGAAGCGGCTCAAAAGTCGTTACCGCAGCTTCCTGACATTTCCGATAAAGTGTCCAATGCAGAGATGATGGACAAGGCGGGAATGGTGATGCTGCTCATTATTCCATTCATTGTCGCAATGGCTGCCGTCCTAGTTGTTAAGCTCATGGTGGTGCTGCGCTTTATTGAGCTATACATTATGACCGCATTCGCATCATTGCCGATTGCGTTCCTGGGGCACCCGGACACGAAGTCGATGGGTATCGGATACCTTCAAAAGTATGCCGCCGTCTCGATGCAAGCTGCCACATTAATGCTGGCGACTAAAATCTATTCGTACCTACCTGTGGTAAATGCGATTAATGTCGGTGAGCCTGACGATTCTCTGAGTGGGTGGATCGTTCAGAATTATGCGACGTTCCTTTTGGCGCCAGTGCTCTTGATAATGCTTGTGATGAGCAGCGGTAAGGTGGCCAAAGCGCTGGTTGGTCAGTGA","MDDMIIYMFKKLFEFDTSEATGLKQTLSEYSNETYNVVTSLHNTGIKPVASVIISMLLVLELARNASRIEADQQLGVKIIAATMFKSVLLVWAAQNAMMFLDAINQVVQSVAKNIEAAQKSLPQLPDISDKVSNAEMMDKAGMVMLLIIPFIVAMAAVLVVKLMVVLRFIELYIMTAFASLPIAFLGHPDTKSMGIGYLQKYAAVSMQAATLMLATKIYSYLPVVNAINVGEPDDSLSGWIVQNYATFLLAPVLLIMLVMSSGKVAKALVGQ$","Membrane protein","Membrane, Cytoplasm","","","","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[141-161]?$ $\"[165-187]?$ $\"[202-222]?$ $\"[241-259]?$	transmembrane_regions

","BeTs to 3 clades of COG0840COG name: Methyl-accepting chemotaxis proteinFunctional Class: NThe phylogenetic pattern of COG0840 is A--K--VCEB--UJ--OL---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 190-272 are similar to a () protein domain (PD940805) which is seen in Q6AG12_BBBBB.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:29:01 2007","Mon Jul 16 15:29:01 2007","Mon Jul 16 15:29:01 2007","Mon Jul 16 15:36:55 2007","","","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","Mon Jul 16 15:28:10 2007","","Mon Jul 16 15:28:10 2007","","Mon Jul 16 15:28:10 2007","yes","","" "ANA_2326","2516220","2519732","3513","4.35","-104.04","125309","ATGATTACGATCACGGTGAATCCCGACGGAAGTGGCCAACTTTCCGGTGAAGGGGGAGAACAGCGTGTCAATGCCGGGAGCGTATTCCAAGCACGTGAAGAGCTTCTGCGTCTCGTTGCGTCGATTGCCGCAAAGAAGGGGAGCAGCGTCACTGTAGCGGCCGTCGACGAGAACGGAACGCAGTACATTTCTGTCGACGCCTTCGGCGCAGTGACGCTACTTGATGAAACGTTGGTTGTCCAAGAGTATAATGAGCTGTTCGCCTCAGATCTGACAGTGGCGGGAGATGTTGAGCCTCCAGCCCTGCAGCCAGAGGAAGGTGCTTCAACGAGTGAGAATTCGTTGGTGTCAGAGATCGGTGGCTCTGTCGATTCGGTCGCTTACTCACGTCAATCTCCGTTCGTGGCAGAGCTTGAGGGGGACAGTCCGTTCAACTCGCGAGTGTCGAATATTGACGAAGGTGAAGGTGGTCCCGAATTTTCACATAACGACGGCGCCTATGAGATGGATTCGCAGCCTCCACGAATCTATCCGAAGCGAACTCGCGTAGCTCAAAGCGCCTCGTCACCGTATCGGGTTTTGTCTCCACAATCCGTATCGCCTGATGGCGATGAGCGACTATATGAAGATCCGGGTCGCCTATCCCATACCTCTGTTCCGAGTGAGCCCACGTCCAAGTCGACTCCGTCTAGCATTATCGACTACTCTTCCCTGCTGGGTGTCGATGGCCACAAGAGTAATGATTCTGACATTGACCCTGGTGCTGCTGGAGCTGACAGTGAGGCTGATCCGAGTAATGTGGGAGAGGGTGTCCCGGGCTCTGCATTCCGGATGGACCTTTCAGTGTTTGGTTTGCCAGGAATGGGAGAGAATACCGTGGGGCACGATGACGCACAGAGTAGTTTCCCCGATGCCTTTGTGGCATACGATGATGTTGAAGTACCTTCCATTTCCTCGTCGGGGCAACGTGCGGAACTTTCCGGTTTTGTGAGGGATGAGGATCTTGAGTGGGGTCCGGAGTGGATCGAGGAGCGTATCCGGGAGGACATGATTGAGTCGGTGGATCCGATGCCTCCTTTGGGTGTGGGTCGGGTGGTGCCGGAGGGGTACTTTGAGCGGTTTGGGGGTGTGTTTCCTGAGTCGGTTTTGTATATCTGGAGGCGTTTCGGGTTTGATGGTTTTGGGCAGGGGCGCTCGTGGATCACGGATCCGGTTGAGTGGGCCCCGGTGGTGGATGCCTGGCTGGAGGGGATCGAGCTGCCCTTCCCGGCTCAGCGCTGGCACTGCCTGACGCGCACTGCCTTGGGCACCATGCGTCTGTGGGGGGAGATCTCCGGTCCGGCACTGAAGGTCGACGTCATCGACGGGGCCATCTATCCCAACGTCTCTGCTGCTGAGGATATGACGGATCCGGTTGTCAGGGAGCGTAGCGGCTGCATCACCTTCACCGATCCGCTCGTTGATTTTGATGAGGATGAGGTGACGGGTCGGTCTTTGGCTGTGGAGGGGATTGAGCGTCTGGGGGTGCCTGGGGCTGACGAGGTGCTGGGGTTTGTGCCTGCGTTGAGCTTTGGTGGCCAGGTGAGCGCCGATCGGTTGAGTGTGCAGAAGGCTGTGCCCTACCTGCTGGGCCTGGCGCAGTCCACACCCAGGTACCTGGGGGTCGATCTCATGGCTGCCTGGGGCGGGGCGGCCACGCAGTTCCTCATCGACCAAGGAGCCATACCTGCCAACAGCACAAACACAGACACGTCCGGTGGTGCAAGCACTCCCAACACCCCCGGCGACCCCGAAGACCTTGGAAGTCCTGGTGGCCATGGTGGTTCCACTGGGCTTGGTGGCCAGGATGGTGCTGTTGGTTTTGCTAAAGATGACGATTTTGAGTGGGGTCCGGAGTGGATCGAGCAGCAGATCCAGGAGGAGTTACTCGACTTTCATAACATGCCTCCTTTGGGTGTGGGTCGGGTGATGCCGGAGGAATACTTTGAGCGGTTTGGGGGTGTGTTTCCTGAGTCGGTTTTGTATATCTGGAGGCGTTTCGGGTTTGATGGTTTTGGGCAGGGGAGATCGTGGATCACGGATCCGGTTGAGTGGGCTCCGGTGGTGGAGGCCTGGTTGGAGGGTGTTGAGCTGCCGTTCCCGCCTCAGCGCTGGCACTGCGTAGCACGTACCACCCTGGGGTGCATGCTTCTGTGGGGTGAGATTTCCGGCCCCGCACTGCATGTTGACGTCATCTCCGGGGAGATCTGCCCGGACTCGTTGGCTTCTAGGGACATGGCTGATTCGGTTCTCAGGCAGAGCATGGGCTGTAATATTTTCACCCGTCCGCTTATGGATCATGGAATGGATGGGGTGACGGGTCGGCCTTTGGTTGTGGAGGGGATTGAGCGTCTGGGGGTGCCTGGGGCTGACGAGGTGTTCGGGTTCGTGCCGCCGTTGAATTCCGGCGACCAGGTCAGCGCGGATCGGTTGAGTGTGCACAAGGCTGTGCCTTACCTGGTGGGGCTGGCGCAGTCCACGCCCAGGTACCTGGGGGTCGATCTCATCACTTTCTGGGCTGGGGCGGCCACCCAGTTTTTCGCCGACCAAGAAACCATACGCAACAGCACAGACGCCTCTGGCGACCTCCGTGGCCAGGATGGTCTCAATGGGCTTGGTGGCCAGGGTAATTCTGTTGGTTTTGTGAGGGATGAGGATCTTGAGTGGGGTCCGGAGTGGATTGAGCAGCAGATTCAGGAGGATCTGCTTGACTATCAGGGCATGCCTCCTTTGGGTGTGGGTCGGGTGGTGCCGGAGGAGTATTTTGAGCGGTTTGGGGGTGTGTTTCCTGAGTCTGTTTTGTATTTCTGGAGGCGTTTTGGGTTTGATGGTTTTGGGCAGGGGAGGTCGTGGATCACGGATCCTGTTGAGTGGGCGCCGGTGGTGGACGCCTGGTTGGAGGGGATCGAGCTGCCGTTCCCGCCTCAGCGCTGGCACTGCGTGGCACGCACGACCCTGGGCACCATGCGTCTGTGGGGGGAGATCTCCGGGCCTGCGCTGAAGGTCGACGTCATTGACGGGGCCATCTACCCCAATGCCTCTGAGGCGCAGAAGATGACTGATCCGGTTGTCAGGGAGCGCAGCGGCTGCACTACCTTCACCAGCCCGACTGAGGACCTGGATGAGGATGAGGTGTCGGGTCGGCCTTTGGCTGTGGAGGGGATTGAGCGTCTGGGGGTGCCTGGTGCTGACGAGGTGCTGGGGTTCGTTCCGCCGTTGAGCTTTGGTGGCCAGATCAGTGCGGATCGGTTGAGTGTGCAGAAGGCTGTGCCCTATCTGGTGGGGCTGGCGCAGTCCACGCCCAGGTACCTGGGCGTGGATCTCATGGCTGCCTGGGGCGGGGCCGCCACCCAGTTCCTCATCGACCAAGGAGCCATACCCAACAGCACAAGCACAGACACCTCCGGTGACCCCGACGGCCAGGATGGCCCGGGTGGTCCTGCTGGTGCTGGTGGTTTTGGGGGTGGGTTGTGA","MITITVNPDGSGQLSGEGGEQRVNAGSVFQAREELLRLVASIAAKKGSSVTVAAVDENGTQYISVDAFGAVTLLDETLVVQEYNELFASDLTVAGDVEPPALQPEEGASTSENSLVSEIGGSVDSVAYSRQSPFVAELEGDSPFNSRVSNIDEGEGGPEFSHNDGAYEMDSQPPRIYPKRTRVAQSASSPYRVLSPQSVSPDGDERLYEDPGRLSHTSVPSEPTSKSTPSSIIDYSSLLGVDGHKSNDSDIDPGAAGADSEADPSNVGEGVPGSAFRMDLSVFGLPGMGENTVGHDDAQSSFPDAFVAYDDVEVPSISSSGQRAELSGFVRDEDLEWGPEWIEERIREDMIESVDPMPPLGVGRVVPEGYFERFGGVFPESVLYIWRRFGFDGFGQGRSWITDPVEWAPVVDAWLEGIELPFPAQRWHCLTRTALGTMRLWGEISGPALKVDVIDGAIYPNVSAAEDMTDPVVRERSGCITFTDPLVDFDEDEVTGRSLAVEGIERLGVPGADEVLGFVPALSFGGQVSADRLSVQKAVPYLLGLAQSTPRYLGVDLMAAWGGAATQFLIDQGAIPANSTNTDTSGGASTPNTPGDPEDLGSPGGHGGSTGLGGQDGAVGFAKDDDFEWGPEWIEQQIQEELLDFHNMPPLGVGRVMPEEYFERFGGVFPESVLYIWRRFGFDGFGQGRSWITDPVEWAPVVEAWLEGVELPFPPQRWHCVARTTLGCMLLWGEISGPALHVDVISGEICPDSLASRDMADSVLRQSMGCNIFTRPLMDHGMDGVTGRPLVVEGIERLGVPGADEVFGFVPPLNSGDQVSADRLSVHKAVPYLVGLAQSTPRYLGVDLITFWAGAATQFFADQETIRNSTDASGDLRGQDGLNGLGGQGNSVGFVRDEDLEWGPEWIEQQIQEDLLDYQGMPPLGVGRVVPEEYFERFGGVFPESVLYFWRRFGFDGFGQGRSWITDPVEWAPVVDAWLEGIELPFPPQRWHCVARTTLGTMRLWGEISGPALKVDVIDGAIYPNASEAQKMTDPVVRERSGCTTFTSPTEDLDEDEVSGRPLAVEGIERLGVPGADEVLGFVPPLSFGGQISADRLSVQKAVPYLVGLAQSTPRYLGVDLMAAWGGAATQFLIDQGAIPNSTSTDTSGDPDGQDGPGGPAGAGGFGGGL$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR014983
Domain

GAD-like
PF08887	$\"[347-457]T$ $\"[636-747]T$ $\"[909-1021]T$	GAD-like

InterPro
IPR015002
Domain

Domain of unknown function DUF1851
PF08906	$\"[467-550]T$ $\"[764-841]T$ $\"[1009-1114]T$	DUF1851

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 347 to 457 (E_value = 5.6e-08) place ANA_2326 in the GAD-like family which is described as GAD-like domain.Residues 467 to 550 (E_value = 7.8e-05) place ANA_2326 in the DUF1851 family which is described as Domain of unknown function (DUF1851).Residues 636 to 747 (E_value = 3.6e-06) place ANA_2326 in the GAD-like family which is described as GAD-like domain.Residues 764 to 841 (E_value = 5.2e-05) place ANA_2326 in the DUF1851 family which is described as Domain of unknown function (DUF1851).Residues 909 to 1021 (E_value = 7.8e-07) place ANA_2326 in the GAD-like family which is described as GAD-like domain.Residues 1009 to 1114 (E_value = 7.4e-05) place ANA_2326 in the DUF1851 family which is described as Domain of unknown function (DUF1851).","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2327","2519892","2520692","801","4.38","-19.59","27983","ATGCCTCCTTTGGGTGTGGGTCGGGTGGTGCCGGAGGAGTACTTTGAGCGGTTTGGGGGCGTGTTTCCTGAGTCGGTTCTGTATATCTGGAGGCGTTTCGGGTTTGATGGTTTTGGGCAGGGACGCTCCTGGATCACGGATCCTGTTGAGTGGGCGCCGGTGGTGGACGCCTGGCTGGAGGGGATCGAGCTGCCGTTCCCACCCCAGCGCTGGCACTGCGTGGCACGTACCGCCCTGGGGTACATGCTTCTGTGGGGGGAGATCTCCGGGCCGGCCGTGGACATCGACGTCATCAATGGTGAGATCTCCCCGAATGCCAATGAGGCGGAGAACATGACTGATCCGGTTGTCAGGGAGCGCAGCGGCTGCACTGTTTTCACCAGCCCGCTTGAGGATGTGTATGACGATGAGGTGTCGGGGCGGCCTTTGGCTGTGGAGGGGATTGAGCGTCTGGGGGTGCCGGGTGCTGACGAGGTATTGGGGTTTGTGCCGCCGTTGAGCTTTGGTGGCCAGATCCGTGGGGATCGGTTGAGTGTGCAGAAGGCTGTGCCCTACCTGGTGGGTCTGGCGCAGTCCACGCCCAGGTACCTGGGCGTGGATCTCATGGCTGCCTGGGGCGGGGCCGCCACCCAGTTCCTCATCGACCAAGGCGCCATACCCAACAGCACAAACACAGACACGTCCGGTGGTGGCGCAAGCACCCCCGGCGACTCTGACCCCCACAGTGGCCCCGACAGCCAGGATGGTCCTGGTGGCCCGGGTGGTCCTGCTGGTCCTGGTGGTTTTGGGGGTGGGTTGTGA","MPPLGVGRVVPEEYFERFGGVFPESVLYIWRRFGFDGFGQGRSWITDPVEWAPVVDAWLEGIELPFPPQRWHCVARTALGYMLLWGEISGPAVDIDVINGEISPNANEAENMTDPVVRERSGCTVFTSPLEDVYDDEVSGRPLAVEGIERLGVPGADEVLGFVPPLSFGGQIRGDRLSVQKAVPYLVGLAQSTPRYLGVDLMAAWGGAATQFLIDQGAIPNSTNTDTSGGGASTPGDSDPHSGPDSQDGPGGPGGPAGPGGFGGGL$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR014983
Domain

GAD-like
PF08887	$\"[1-100]T$	GAD-like

InterPro
IPR015002
Domain

Domain of unknown function DUF1851
PF08906	$\"[117-194]T$	DUF1851

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 100 (E_value = 1.6e-05) place ANA_2327 in the GAD-like family which is described as GAD-like domain.Residues 117 to 194 (E_value = 0.00051) place ANA_2327 in the DUF1851 family which is described as Domain of unknown function (DUF1851).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2328","2520818","2522854","2037","10.20","15.70","69338","GTGCTGGTGTGGGAGGGGCCTGCCGCCTTGAGGACGGCTGGTGCCCAGGTGGGGGCCGACCAGTGGTGTGACAAGGTGGACCCGGTGGTGGTGTCGTACCACACGGGTGGGAAGAATCGGTCCTCGAGTGGGTTGCCGCAGGAGATGACGCGTCAGCTTGATGGGCAGTTCACGGCTCTGAGCCTGATGAGTGCCAAGGAGATCCTGGCTGGTATGGCCACCTTCGACGAGCGCAAGCGCTCCCCAGCCAGCCACACCGCCATCCGCCAGAAGTTCCAGAAGAAGCTCGCCAAGGATCTGAAAGACCGTCATGGGTTTCCTGAGGAGGTGGCGGGGTTGTGGGCTTCTCGGGCGATGGGTGAGCTGGCGGTGCTGCACAATCCTGATCAGCTGTTGTCTGGTCCGCAGGGTCCTTCCTTGGTGGGGGGTGTGGTGGCTCTGGGGGACCGGGCGACGAACTCGGCGGTGGGGGCGCAGACGGCTCAGGGTCCTAGGGAGCTGATTCGTGATGCGGCTCAGGCGGCGGTGGACGCGGGTCAGGGGGACCGGTTGCTGCAGATGCGGGTGGTGCTGACTGACTCCCCGAAGCTGTCTAGGGACCTGAACGAGAGGTTGGAGGCGTTGGAGCCGCGGAGCCTGGCTGAGCAGTGGGAGGCGGTCTCCCCTCGCGGGCCCCCACTGACCCCTCAGGTGCTGTCTGATCGTCTGGCCCAGGCCCTGGGCGGTGATGGTGGGCTGGAGGACCTCACCCGTGATGAGCTGCGGCAGGCCCTGACCCAACCACCAGGACCCACCCCAGACCACCCAGACACCCCCACCCCAGATGCACCCGCTCCAGACGGGCTGGACACACCAACCCCAGACGGACTGGGTACGGATGCCCCGGAGACGGGCGTACCCGATCGGGGTGCCCCGGGGGTGCCGGTTTCGACTCCGCAGGCGCCGGCTCCGGTGGAGCCGGTTGCCCGGCCCACGGACACCTCGCCCTCCATGTCGGCTCCAACCCCCGACCTCAACGCCCCAGACAGGAACCCCTTAGACAAGGCGGCCCCTGACAGGAGCGCCCCTGAGCAGAACGCCCCAGACAGGGCAGCCCCAGAGGTGAGCGCTCCTGAGCAGAGCGCCCCCGAGCAGAACCGGCCAGACAAGGGCACCCCAGACGGGCGCGCGCCGGGCGGGCCTGGTCGCAGTGCCCCGAACGCGGGTGCACCCGATGGGGGCACACCGAGCGGGCCTACCCAGGCGCAGGCGCCTGGGGCCGGGCGGACCACGCCGCCTTCTGCGCCGCCGGTGTCTGCGGAACCGCCGGTCCGCTCGCAGCGGACTGCCTCGCCCGCGACCCCCAAGCAACCAGCCCAACCAGCCCAGCAGAACCAGCCGGGCCAACCAGGCCAGCCGAGTGGTCAGCCGGGCAGGCCAGCTCAGCCGGGCAAGCCAGGCCGGCCGAGTGGTCAGCCGGGCAGGCCAGCTCAGCCAGGCCAGCCAGGCAGGCAGAGCCAACCAGGCCAGCCAGTTCGGTCGGGCCGGTCTGGTCGGTCGGGTGTGCCGGGTCGGGGTGCTGCTGGGGCGGGCACCTCAGGTGCCCCGGGGGCTACTGCCCGGCCTGAGGCCCCCTCACGCCTGCAGGCCGGCCAGGGAACAGGCACACCTCCTGCCCCGACCCGCTCAGTGCCCCAGACTGGGCCGGCTCAGCCGGCGCCGCGTCGCAGCACCAGCGGGCCCGGCGCGGGGGACGCCCCCAGTCGTAGTGCTGGTGGGCGCGGCACCGACATCACGCCCAGGACAGCGCCCAGGTCCACGTCTCGTTCGGCATCCCGGTCGGCGTCCCGTTCCTCGTCGCGTTCGGCCGGTGCCACCGCCTCTGGCGCACGCACGAGGGCCCAGGACCCGATCAAGGCCCGCCTGGCCCCCACCGGCGACTCCCAACGAGACGGCGCCATAGCCGGCATCTCCTCCAAGCTCGACAAGCTCCGCCAGAACAACCAGCAACGCCAACCCACCCAAGCCCCCACCCGCACCCACCACCCACGCCGATAA","VLVWEGPAALRTAGAQVGADQWCDKVDPVVVSYHTGGKNRSSSGLPQEMTRQLDGQFTALSLMSAKEILAGMATFDERKRSPASHTAIRQKFQKKLAKDLKDRHGFPEEVAGLWASRAMGELAVLHNPDQLLSGPQGPSLVGGVVALGDRATNSAVGAQTAQGPRELIRDAAQAAVDAGQGDRLLQMRVVLTDSPKLSRDLNERLEALEPRSLAEQWEAVSPRGPPLTPQVLSDRLAQALGGDGGLEDLTRDELRQALTQPPGPTPDHPDTPTPDAPAPDGLDTPTPDGLGTDAPETGVPDRGAPGVPVSTPQAPAPVEPVARPTDTSPSMSAPTPDLNAPDRNPLDKAAPDRSAPEQNAPDRAAPEVSAPEQSAPEQNRPDKGTPDGRAPGGPGRSAPNAGAPDGGTPSGPTQAQAPGAGRTTPPSAPPVSAEPPVRSQRTASPATPKQPAQPAQQNQPGQPGQPSGQPGRPAQPGKPGRPSGQPGRPAQPGQPGRQSQPGQPVRSGRSGRSGVPGRGAAGAGTSGAPGATARPEAPSRLQAGQGTGTPPAPTRSVPQTGPAQPAPRRSTSGPGAGDAPSRSAGGRGTDITPRTAPRSTSRSASRSASRSSSRSAGATASGARTRAQDPIKARLAPTGDSQRDGAIAGISSKLDKLRQNNQQRQPTQAPTRTHHPRR$","Hypothetical protein","Extracellular, Cellwall","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Akira T., Komatsu M., Nango R., Tomooka A., Konaka K., Yamauchi M., Kitamura Y., Nomura S., Tsukamoto I. Molecular cloning and expression of a rat cDNA encoding 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Gene 1997. 197(1):289-293. PMID: 9332377","","","

InterPro
IPR013982
Domain

AICARFT/IMPCHase bienzyme, formylation region
SM00798	$\"[64-239]T$	no description

","No hits to the COGs database.","***** IPB001359 (Synapsin) with a combined E-value of 3.6e-07. IPB001359H 466-516 IPB001359G 551-562 IPB001359H 475-525 IPB001359H 459-509 IPB001359H 450-500 IPB001359H 472-522 IPB001359H 436-486 IPB001359H 453-503 IPB001359H 463-513 IPB001359H 456-506 IPB001359H 460-510 IPB001359H 469-519 IPB001359H 447-497 IPB001359H 446-496 IPB001359H 478-528 IPB001359H 437-487 IPB001359H 386-436 IPB001359H 434-484 IPB001359H 462-512 IPB001359H 433-483 IPB001359H 492-542***** IPB002486 (Nematode cuticle collagen, N-terminal) with a combined E-value of 2.3e-06. IPB002486 484-520 IPB002486 481-517 IPB002486 487-523 IPB002486 472-508 IPB002486 466-502 IPB002486 475-511 IPB002486 478-514 IPB002486 493-529 IPB002486 490-526 IPB002486 450-486 IPB002486 447-483 IPB002486 469-505 IPB002486 459-495 IPB002486 456-492 IPB002486 431-467 IPB002486 453-489","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2329","2523703","2525652","1950","5.03","-23.96","72448","ATGAGTAGAATTCGATATGTCATTCTCGCGTCAGTGACCCTGATTTCCTGGTGGGTTGGAGACAAGATATCCTGGCAGATACGAACTGACCGTTCCGCCGGGCGCACTCTCAGTGACGTGATGGACAGATTCTGGTTCGACCTCCAGAGTCCTTTTCACATCTCCTGGAATACGACCGATATGCTCGTCGGAGCGGGATTCGCTGCGGCGATCCTCATGATGTGGGCCTATCATGTGGGTGCCAGAAAAGCCACGCGCCCAGGGGAGGAGCACGGGTCAGCCAAATGGGCGAGCCCCAGAGACATTCGTCCTTACGTTGGGAATCGGTCGAATGATATTCTATTCACTCGTACCGAATCTTTGAGTCTCGATTCTCGGAAGACACAGCGAAACCTTAATGTCCTTGTCATTGGTAGCTCCGGTTCGGGTAAGTCGCGCTACTTCGTCATGCCTAATCTTCATCAGGGAAACACCTCCTACGTTGTGACGGACCCCAAAGGTGAAGTTCTCGCGGCAACGGGAAACAAACTCCTTGAGCTCGGGTATGAAATACGGTGCCTCAACCTTGTTGACTTCGCTCGATCTGACACTTTCAATCCTCTTGCGTACTTCAACCCTGACCAGGCGGAAGTCGACTGCGCCATTCTGACAGAGAACTTCATCACGAACACGACAGGAAAGAAGCCTTCCGATGGTGGCGATTTCTGGGAGAAGGCGGAAAGGGCCCTGCTCACCGCCCTCGTTGCGATGGTGTACTTCACCAAGGGTGAGAAGGGGACACTTCTTGATGTTGTCGAGCTTTTGTCGATGATGACAGCTTCTGAGCAAAATGAGGAAGCACTTAGCCCAGTCGACGAGCTGTTCCTTGCCACGAAGGAGTACATTGCCGATTGTGACAATAATCCAGACTCCGACCCGGACGGCAACAAGATAATCGAAGGTCTTCGGTTCGCATGCTCTCAGTACAATGTGTACACGCAGGGCGCTGGAGAGACCAAGAAGTCGGTGATCATCTCTCTGGGGGTGAGAATGGCACCCCTCCACATGGCGCCCATGCGGAGAATACTGGGGTCAGATACGATCAAGGCGGATCAGATTGGAATGCGTCCGACGGCACTGTTCCTTGTGATCCCCGATACCCATCAGGCATTCAACTTCCTGGCGTCCATCTTCTATGAGACGTTCTTTGAGAAGAACATTTATATTGCGGATCATTCTGGTGGCCGACTCCCGGTTCCAGTGCAGTGCTACATGGATGAGTTCGCCAATATCGGCAAAATGCCCAGCTTTGAGCGTAAAATTGCCGTGATGCGCTCTCGTGGTATCTCCACCTCTGTCATCCTGCAGAACTACTCTCAGGGGAAAGCTCTCTATAAGGATGACTGGGAGACTATTGTCGGGAACTGTGACTCCCTGCTCTTCTTAGGAGGAAATGAGGGGTCCACAACCGAGTTCATCTCCAAGAGGCTGGGTAAGGAGACTATCACCCAGGAAGATAACTCGGATCAGCGAGGAGCTCAGGGATCCTGGTCCCGATCATATCGCTCGTCAGGTCGCGAGCTCATGACGGCAGATGAGATCTCTCGTCTGCCGGGCAACGAATGTCTTTACTTCCTGCGAGGCGTTCCTCCGTTCCGCTCGCGGAAGTTGGCGGCCCCGCCCGAGGGTTACTTCGAATACATGCCAGCAGAGGTTCCGCAAGCCCTGTCTCCGGAGGAGAACCTCCTTTTGGCCCCTTGGGAGAGCCGGCCTGAGTACAACGAGATCGACAGTCATGACGGTGAGTTCGCGGACGTAGGAGACGATCCCGAGCTTGCCGAGCTCGCTTCCATGAGTCCGTCGGATCTTGATGAGTTCGGCGGCGAAGGTGACGTCGAGATCACCGTCGTTCTGAGTGACGGTCGGCAGGATCGGCAGGTCATTCACTTCAAGGATCTTGACGTCTTCTGA","MSRIRYVILASVTLISWWVGDKISWQIRTDRSAGRTLSDVMDRFWFDLQSPFHISWNTTDMLVGAGFAAAILMMWAYHVGARKATRPGEEHGSAKWASPRDIRPYVGNRSNDILFTRTESLSLDSRKTQRNLNVLVIGSSGSGKSRYFVMPNLHQGNTSYVVTDPKGEVLAATGNKLLELGYEIRCLNLVDFARSDTFNPLAYFNPDQAEVDCAILTENFITNTTGKKPSDGGDFWEKAERALLTALVAMVYFTKGEKGTLLDVVELLSMMTASEQNEEALSPVDELFLATKEYIADCDNNPDSDPDGNKIIEGLRFACSQYNVYTQGAGETKKSVIISLGVRMAPLHMAPMRRILGSDTIKADQIGMRPTALFLVIPDTHQAFNFLASIFYETFFEKNIYIADHSGGRLPVPVQCYMDEFANIGKMPSFERKIAVMRSRGISTSVILQNYSQGKALYKDDWETIVGNCDSLLFLGGNEGSTTEFISKRLGKETITQEDNSDQRGAQGSWSRSYRSSGRELMTADEISRLPGNECLYFLRGVPPFRSRKLAAPPEGYFEYMPAEVPQALSPEENLLLAPWESRPEYNEIDSHDGEFADVGDDPELAELASMSPSDLDEFGGEGDVEITVVLSDGRQDRQVIHFKDLDVF$","TraG family protein","Cytoplasm, Membrane, Extracellular","TraG family protein","TraG family protein","TRAG family protein","","","","","

InterPro
IPR003688
Family

TRAG protein
PF02534	$\"[95-574]T$	TraG

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[126-550]T$	no description
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[61-81]?$	transmembrane_regions

","BeTs to 4 clades of COG3505COG name: Type IV secretory pathway, VirD4 componentsFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG3505 is ------------------s-ujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003688 (TRAG protein) with a combined E-value of 3.1e-17. IPB003688A 143-165 IPB003688B 411-441","","","No significant hits to the PDB database (E-value < E-10).","Residues 95 to 574 (E_value = 3.8e-27) place ANA_2329 in the TraG family which is described as TraG/TraD family.","","family protein (traK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2330","2528581","2525816","2766","5.37","-15.67","92419","ATGAGTACGACCAGCCAGGAATCCGGCGGGCAGCTGCGCACCGTCAACCTCTCCATCGGGGGCATGACCTGCGCCAGCTGCGTGGCCCGGGTGGAGAAGAAGCTGAACAAGCTCGACGGCGTGAGCGCCTCGGTCAACCTTGCCACCGAGTCGGCCCGCGTCACCGCCCCAAGCGCAGTGAGCGTCGATGACCTCCTGGCCACAGTCGCTCGCGCCGGCTACACCGGCGCCCTGCTGGACGCCGCCTCACCAGATGAGTCGGCGCAATCGGAGGCGTCACCGGCCGGGGAGCCCGCGTCGGCGACGCCGGCAGCACCGGCGTCGGGACCGTCCACGCCCGGTTCGGCCGAGGGTGGACGCGGCACCAAGGGCACAGGCGGCCGCGCGTCACTGTCCATGGCTGCGGCGCCGGCCACGCGCCCGGGCGCCCCCGCCGGCACCAACAGCACGAACGGCACCACCGGCACCTCCCCCCGCTCCGCCTCCGGGAGTGGGGCAAAGTCTCTGGGCGCCTCGCATATGGAGCGGGCCGCCGACCTGCGCCTGCGGCTCATCTACTGCCTCATCCTGTCGGTGCCGATCATGGCGATCTCCATGGTGCCGGCGCTCCAGCTGCCGGGCTGGCAGTGGACGGTGGCGCTCATGGCGCTGCCGGTGGCGGTCTGGGGGGCCTGGCCCTTCCACAAGGCGGCCTTCCGGGCGCTGCGCCACGGGGCCTTCACGATGGACACGCTCGTATCCCTCGGGGTGATCGCCGCGACTGGATGGAGCCTGTGGGCGCTGGTGCTCGGCGGGGCCGGGCACATCGGCATGCGGATGAGCATGGAGCTGCTGCCCCGCTCCCAGGGGCATGCCGCCCACATGTACTTCGAGTCGGCCGCCTGGGTGACCACCTTCCTCCTGGCGGGCCGCTACGCGGAGGCGCGCGCCAAGTACCGTTCCGGCGACGCCCTGCGCGCCCTGCTGGAGCTGGGCGCCAAGGAGGTGACCCGAGTCGTCCTCACCTCGCCGTCGGGCAGCCGCGACGCCGTCGACGTCTTGGATGAGGACGGCTCGCCGCGCGCGGAGGCCACCCGCACTGAGGAGCGCATCAGTGTTGAGGATCTGGCGGCCGGGGACCTGTTCCTCGTGCGGCCGGGTGAGAAGGTGGCCGCCGACGGCGTCGTCGTCGAGGGCCGCTCGGCCGTGGACGCCTCACTGCTCACCGGGGAGTCCGTGCCCACCGAGGTCGAGGCGGGACAGACCGTCACCGGGGCGACCGTCAACACCTCCGGCGTCCTGCTGGTGCGGGCCACGGCCGTGGGCGAGGGCACGACGCTGGCGCGGATCGGCCGGATGGTGACGGCCGCGCAGGCGGGTAAGGCCCCCGTCCAGCGCCTGGCGGACCGGATTTCGGGGGTGTTCGTGCCCATCGTCCTGGTGCTGGCGGCAGCGACCCTGGCGGGGTGGCTGCTCACCGGGCACAGCCCGCAGGCGGCCTTCACCGCGGCGGTGGCCGTGCTCGTCATCGCCTGCCCCTGCGCGCTGGGGCTGGCCACGCCGACGGCGCTGCTGGTCGGTTCGGGCCGGGCCGCCCAGCTGGGCGTAGTCATCAAGGGCCCCGAGGTGCTGGAGTCGACGCGGGCTCTGGACACGATGGTCATGGACAAGACCGGCACCGTCACCCAGGGGCGCATGAGCCTGGAGGTTGAGGCCTGCCAGGAGGTGGGCGCCGGCGCTGGTACCGGCGCAGATACCAGTGCAGACTCCGCCGCGGGCCTGAGCCCGCTCGGGGATGAGGCGCTGCGCCTGGCCGGGGCGGTCGAGTCCGCCTCGGAGCACCCGGTGGCCACAGCGATCACGGCGGCCGCCCGCGAGCGACTGGGAGACCTGCCGACGCCGGCCGACTTCTCCAACCACGAGGGCCGGGGCGTCTCCGCCACCGTGGAGGGGCGCCGGGTCGCGGTGGGACGGCCGGGCTGGCTCGCCGGTGAGTTGGGCGCCGAGGTTCCCGAGGCTCTCAGCGCCGCCGTGGAGCAGGCCCAGGACTCCGGGGCGACGGCCGTCGTCCTGGCCGTGGGCGGGGCCGGTGAGGCCGCGAACGTTGAGACCGAGGCGCCTGACGGGGCCGCCGCGGACAGCACCGCTGACGCCTCCGCCACCTCTGACGCCTCCGCCGACGCTGGCACTGCGGCGCCGGATGCGCGGCCACTGAAGGCTATCGCGGTTCTCGTGGTGCGGGACACCGTGCGGCCCTCCTCGCGGGCGGCGGTGGCGGCGCTGCGCGAGCTGGGGATCCGGCCGGTACTGCTGACCGGGGACAACGTCCGGGCCGCCGAGCACGTGGCGGCCCAGGTGGGGATCGATGCCGCCGACGTGCGCGCCGAGGTGCTGCCCGCCGACAAGCGCGACGTCGTCGCCGACCTGCAGGCCCAGGGCGCGGTGGTCGGCATGGTGGGTGACGGGGTCAACGACGCCGCCGCCCTGGCCCAGGCCGGCACGCAGGGGCTGGGATTCGCCATGGGCTCGGGGGCGGACGTGGCCATCGAGGCCGCCGACATCACCCTGGTGCGCACGGACCTGGATGCGGCGGTGGCCGCGGTGCGGGTGTCGCGGGCAACCCTGCGGATCATCCGCCAGAACCTGTTCTGGGCCTTTGCCTACAACGTGGCCGCGATCCCGCTGGCGGCCGCCGGGCTGCTCAACCCGATGATCGCGGGGGCCGCCATGGCCGCCTCCAGCGTCATCGTGGTCACCAACTCCCTGCGGCTGCGCCGCGCCGGCTGA","MSTTSQESGGQLRTVNLSIGGMTCASCVARVEKKLNKLDGVSASVNLATESARVTAPSAVSVDDLLATVARAGYTGALLDAASPDESAQSEASPAGEPASATPAAPASGPSTPGSAEGGRGTKGTGGRASLSMAAAPATRPGAPAGTNSTNGTTGTSPRSASGSGAKSLGASHMERAADLRLRLIYCLILSVPIMAISMVPALQLPGWQWTVALMALPVAVWGAWPFHKAAFRALRHGAFTMDTLVSLGVIAATGWSLWALVLGGAGHIGMRMSMELLPRSQGHAAHMYFESAAWVTTFLLAGRYAEARAKYRSGDALRALLELGAKEVTRVVLTSPSGSRDAVDVLDEDGSPRAEATRTEERISVEDLAAGDLFLVRPGEKVAADGVVVEGRSAVDASLLTGESVPTEVEAGQTVTGATVNTSGVLLVRATAVGEGTTLARIGRMVTAAQAGKAPVQRLADRISGVFVPIVLVLAAATLAGWLLTGHSPQAAFTAAVAVLVIACPCALGLATPTALLVGSGRAAQLGVVIKGPEVLESTRALDTMVMDKTGTVTQGRMSLEVEACQEVGAGAGTGADTSADSAAGLSPLGDEALRLAGAVESASEHPVATAITAAARERLGDLPTPADFSNHEGRGVSATVEGRRVAVGRPGWLAGELGAEVPEALSAAVEQAQDSGATAVVLAVGGAGEAANVETEAPDGAAADSTADASATSDASADAGTAAPDARPLKAIAVLVVRDTVRPSSRAAVAALRELGIRPVLLTGDNVRAAEHVAAQVGIDAADVRAEVLPADKRDVVADLQAQGAVVGMVGDGVNDAAALAQAGTQGLGFAMGSGADVAIEAADITLVRTDLDAAVAAVRVSRATLRIIRQNLFWAFAYNVAAIPLAAAGLLNPMIAGAAMAASSVIVVTNSLRLRRAG$","Heavy metal translocating P-type ATPase","Membrane, Cytoplasm","Cation transport ATPases","heavy metal translocating P-type ATPase","heavy metal translocating P-type ATPase","","Smith D.L., Tao T., Maguire M.E. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 1993. 268(30):22469-22479. PMID: 8226755Fagan M.J., Saier Jr M.H. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 1994. 38(1):57-99. PMID: 8151716","","","

InterPro
IPR001757
Family

ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
PR00119	$\"[397-411]T$ $\"[547-561]T$ $\"[757-767]T$ $\"[812-831]T$	CATATPASE
PTHR11939	$\"[15-65]T$ $\"[148-312]T$ $\"[341-572]T$ $\"[591-685]T$ $\"[722-917]T$	CATION-TRANSPORTING ATPASE
TIGR01494	$\"[361-562]T$ $\"[734-903]T$	ATPase_P-type: ATPase, P-type (transporting
PS00154	$\"[549-555]?$	ATPASE_E1_E2

InterPro
IPR001877
Family

Copper-transporting ATPase 1
PR00942	$\"[14-39]T$ $\"[205-225]T$ $\"[225-250]T$	CUATPASEI

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[543-835]T$	Hydrolase

InterPro
IPR006121
Domain

Heavy metal transport/detoxification protein
PF00403	$\"[16-78]T$	HMA
PS50846	$\"[14-78]T$	HMA_2
PS01047	$\"[19-47]T$	HMA_1

InterPro
IPR006403
Family

ATPase, P type cation/copper-transporter
TIGR01511	$\"[223-918]T$	ATPase-IB1_Cu: copper-translocating P-type

InterPro
IPR006416
Family

Heavy metal translocating P-type ATPase
TIGR01525	$\"[242-917]T$	ATPase-IB_hvy: heavy metal translocating P-

InterPro
IPR008250
Domain

E1-E2 ATPase-associated region
PF00122	$\"[295-539]T$	E1-E2_ATPase

noIPR
unintegrated

unintegrated
G3DSA:2.70.150.10	$\"[318-440]T$	no description
G3DSA:3.30.70.100	$\"[11-88]T$	no description
G3DSA:3.40.50.1000	$\"[730-859]T$	no description
PTHR11939:SF35	$\"[15-65]T$ $\"[148-312]T$ $\"[341-572]T$ $\"[591-685]T$ $\"[722-917]T$	COPPER-TRANSPORTING ATPASE P-TYPE ATPASE
tmhmm	$\"[182-201]?$ $\"[207-225]?$ $\"[246-266]?$ $\"[285-303]?$ $\"[467-487]?$ $\"[493-513]?$ $\"[875-893]?$ $\"[899-917]?$	transmembrane_regions

InterPro
IPR006121
Domain

Heavy metal transport/detoxification protein
PF00403	$\"[14-80]T$	HMA
PS50846	$\"[12-75]T$	HMA_2
PS01047	$\"[17-46]T$	HMA_1

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.100	$\"[10-85]T$	no description

","BeTs to 9 clades of COG2608COG name: Copper chaperoneFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2608 is ao-p-zyqvd-lbc-f-h-nu----wNumber of proteins in this genome belonging to this COG is 1","***** IPB000428 (Copper ion binding protein signature) with a combined E-value of 2.6e-13. IPB000428A 12-24 IPB000428B 24-37 IPB000428C 37-50***** IPB006121 (Heavy metal transport/detoxification protein) with a combined E-value of 3.6e-08. IPB006121A 17-39","","","No significant hits to the PDB database (E-value < E-10).","Residues 14 to 80 (E_value = 1.2e-05) place ANA_2332 in the HMA family which is described as Heavy-metal-associated domain.","","reductase (merP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2333","2529316","2529035","282","6.29","-1.40","10172","ATGGCCGGCTACACCGGATCCAAGGAGGACTACCTCAAGCGCTTGCGCCGCATCGAGGGGCAGGTTCGGGGCATCTCCCGCATGGTTGAGGAGGACATCTACTGCATCGACGTCCTCACCCAGATCTCCGCCGCCACCAAGGCCCTCCAGGCCGTCAGCCTCGGCCTGCTGGAGGACCACATGAGCCACTGCGTCCTGCACGCCGCCCAGGCCGGCGACGAGGAGGGCACCGCCAAGATCCGCGAGGCCTCCGACGCCATCGCCCGGCTCGTGCGGTCCTGA","MAGYTGSKEDYLKRLRRIEGQVRGISRMVEEDIYCIDVLTQISAATKALQAVSLGLLEDHMSHCVLHAAQAGDEEGTAKIREASDAIARLVRS$","Uncharacterized conserved protein","Cytoplasm","Uncharacterized BCR","hypothetical protein","protein of unknown function DUF156","","","","","

InterPro
IPR003735
Family

Protein of unknown function DUF156
PF02583	$\"[5-90]T$	DUF156

","BeTs to 7 clades of COG1937COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1937 is ---------drlbcef----u-----Number of proteins in this genome belonging to this COG is 1","***** IPB003735 (Protein of unknown function DUF156) with a combined E-value of 5.2e-15. IPB003735 34-63 IPB003735 7-36","","","-54% similar to PDB:2HH7 Crystal Structure of Cu(I) bound CsoR from Mycobacterium tuberculosis. (E_value = 2.6E_10);","Residues 5 to 90 (E_value = 4.9e-40) place ANA_2333 in the DUF156 family which is described as Uncharacterised BCR, COG1937.","","BCR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2335","2529463","2530467","1005","6.70","-0.85","32979","ATGACCGCCGTTGCCCATGCCTCGCCCGGCCCCGCCGACTCCGACGCGGCGCCCCAGATGCCAGATGACCCCGATCTCCAGCTCGCCCGGGACCCCAGGGCGGGCGCTGGGCGCCTCATGGTGCTGGCCGGCAACCGACCCGACCTGCGCGGTGTCATTGTGGACAACCCGGGCTGCTCCCCGGAGCTGCGCGCCTGGGTGAGCCGCATGGGGGGAGCCTCCGCCGGTCCTGGTGGCGGCGGGCACGGTGGGCGTGGCGGACCTGAGGCCGCGGTGGCTCGGACGGGCGGCTCTGGAGGCGTCGACGACGCGGATGATGCGGTGTCTCTGGCGCCCACGGGCTGGGAGCCCTCCGACATCGGCCTGGGTGAGGACCCCTTCGGCTCCGTCCTGGGCGACCCGCTCATGGGCTCACCGCTGTTCGACGACGACAACGGCCCGGGCCGCGAGCCCGCCGACGCCGAGGCCACCGAGCCTGCCGGTGCGACCGGTCGCGACGACAGGGGCGGGCGGCATTTGTCGTCGAGCCGGCGTACGGCCAGGCCGCACACCGCCTCCGCCCATACCGCCTCGCGCACAGCCGCGGCCCGGGTCTCGCAGACCCCCGCCCCGCCCCCGCAGCGGCCGGCAGTGACGAGGCCTGCACCGCCGGCTCCGATGCCGCCTGGACGCTTCGCGCCCGCGGCGCCCTACCCGGTGCCGGGGATCGCCGGGCCCGTTGGGATCGCCGGGCCGGTCGGGGCCGCCCCGGGTCGCGTAGAGGCCGACCCCTGGGCCGTGGGAGGAGCGCCCGCCGTCGGCCTGCCGACCGCACCTCCGCCGCCCTCCGGTGCACCGGGGATCCCCGGCGCCTCCTTCGGGATGGGGCGCTACAACGCCCCGGCCTCCTCGCGCAGCGCCAGGAGGTCGGCCCCGTCGTCGCCGTCCAGCACGAGCCCGGCCAAGATCATTGGCTGGATCCTCTTCGTCCTGCTGTTCATCGTCATCCGGGCCCTCAACGGCTGA","MTAVAHASPGPADSDAAPQMPDDPDLQLARDPRAGAGRLMVLAGNRPDLRGVIVDNPGCSPELRAWVSRMGGASAGPGGGGHGGRGGPEAAVARTGGSGGVDDADDAVSLAPTGWEPSDIGLGEDPFGSVLGDPLMGSPLFDDDNGPGREPADAEATEPAGATGRDDRGGRHLSSSRRTARPHTASAHTASRTAAARVSQTPAPPPQRPAVTRPAPPAPMPPGRFAPAAPYPVPGIAGPVGIAGPVGAAPGRVEADPWAVGGAPAVGLPTAPPPPSGAPGIPGASFGMGRYNAPASSRSARRSAPSSPSSTSPAKIIGWILFVLLFIVIRALNG$","Hypothetical protein","Extracellular, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[309-329]?$	transmembrane_regions

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[158-215]T$	Q9XAU5_PSEST_Q9XAU5;
PR00038	$\"[158-172]T$ $\"[172-188]T$ $\"[188-200]T$	HTHLUXR
PF00196	$\"[155-212]T$	GerE
SM00421	$\"[155-212]T$	HTH_LUXR
PS50043	$\"[151-216]T$	HTH_LUXR_2

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[33-126]T$	Q8P408_XANCP_Q8P408;
PF00072	$\"[10-124]T$	Response_reg
SM00448	$\"[10-123]T$	REC
PS50110	$\"[11-127]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[131-218]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[10-131]T$	no description
PTHR23283	$\"[14-112]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[14-112]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

InterPro
IPR003776
Domain

YcaO_like
PF02624	$\"[54-430]T$	YcaO

noIPR
unintegrated

unintegrated
signalp	$\"[1-17]?$	signal-peptide

","BeTs to 5 clades of COG1944COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1944 is -om-------r---ef-h---j----Number of proteins in this genome belonging to this COG is 1","***** IPB003776 (Protein of unknown function DUF181) with a combined E-value of 8.7e-09. IPB003776B 186-204 IPB003776C 281-303 IPB003776C 188-210","","","No significant hits to the PDB database (E-value < E-10).","Residues 54 to 430 (E_value = 2.5e-14) place ANA_2338 in the YcaO family which is described as YcaO-like family.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2339","2532982","2533701","720","5.58","-5.77","25392","ATGAGCACGACGCCGCCCGCACCGGCCGCACTGCCGGCACAGCACCCGGCGCCGCAGGCCCCCACGGGGCCGGTGACGGCCTACCTGACCCAGGGCGGGTTCGCGCGCGCCGTCGCCACGCGCCTGGCCGGGCCCGGCGACGTCATCATCCCGGTCGACCACGGGCTGGTCAGCGCCTACATCCCCTACGCCGACCGCGCGGTCCTCATCGCCGACCCCGACCAGACCGGCCTGCGCGAGGATCTCGACACCCTGTCCTTCACCCGGGGGATGCCCTCCCTGGGTCTGGAGCTCTTCCCCACCGAGCTGCGCTGCGGGCCACTCGTGGTCCCCGGCCGCAGCGCCTGCTACCGCTGCTACGACCGGCGCCGCCGCCAGCACGGCTACCGCCCCCTGCCCCCCGAGGTCGCCTCCGAATACGGCCCGCTGGAGCAGGCCTACGCCCACCACCACGTGCTCCTGGGCGTCGGCCTCATCTCCCTGGCCCTGCAGACCCTCGATGCCCCCGGCCCCCAGGACCCGGCCACGACAGACTCCGACGACGTCGCCCCGATCGGCGGCCGGGTGTGGACCATCGACCTCGTCTCCGGCATCACCACCTGCTCGCCGACCGTGGCCGTGGACCGCTGCGAGACCTGCTCGGGCCGCTACGAGGGGCGCCGCGACGGCCTGCCCGCGCTCGCGGCCCTCCTGCCCGAGCGGCGTGAGGAGGTGGCCTGA","MSTTPPAPAALPAQHPAPQAPTGPVTAYLTQGGFARAVATRLAGPGDVIIPVDHGLVSAYIPYADRAVLIADPDQTGLREDLDTLSFTRGMPSLGLELFPTELRCGPLVVPGRSACYRCYDRRRRQHGYRPLPPEVASEYGPLEQAYAHHHVLLGVGLISLALQTLDAPGPQDPATTDSDDVAPIGGRVWTIDLVSGITTCSPTVAVDRCETCSGRYEGRRDGLPALAALLPERREEVA$","Hypothetical protein","Cytoplasm, Membrane","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2342","2533703","2535514","1812","5.28","-15.32","63753","ATGGCCGGGGACGCCACAGGCTCCGTCATGCGCGCCGGCGACGTCGGCCGCGCCGCCCGCCGCGACCTGCAGTTCCGTATCCCCCGCAAGCCCGTGGTACGCCTGGGCCTGCGCGCCCGGCCCGAGGAGACCGGCTGGATCATCGACGGCGCCCGCAAGAGCCAGGTCCTGGGCGGCGCCTTCGCCCGCGAGCACATGGGCGCCCTGCTCCAGGCCTGCGACGGCACCCGCGCCCTCGACGAGATCGGCGAGGTCACCGGCATCGGCCCCCAGGCCGCCTTCGAGGCCGTCTCCCTGCTGTGGACCGGCGGCATCGTCGAGGAGGGCGACACCGAGCCCGCCCCTGGCGACCCGCCGCCCGAGCTGGCGCGGCTGCTCTCCCGCCTGGGCGACTCCACCGGTGTCAACGACTCCTGGCAGGACGCTGCCCGCCGCCTGGCCGCCGCCCGGGTCGCCGTCGTCGGGGACGCCGAGCTGGCCGGGGAGATGGTCGCCGCCCTGGAGCCCACCCTGCCCGAGGTGAGGCTCGACAGCGCCCCCCGCCGCGGGGACACCCTCACCGTCCTGGTCGAGACCGCCGACTCCGTGGCCCGCTCCCCGGAGGTGGCGCGCCGCTGCCGGGAGGAGGACATCGCGCTGCTGCGGGTGCGCGCCGAGCAGGAGGCGGTGACGGTGGGCCCTTACGTCGACGAGTCCTTCTCACCCTGCCTGGCCTGCGCCTGCGCCGACGAGCCCGAGATCGGCCCGCGCCCCGAGCCCGTCCGCCACGACATCATCGTCGGCCTGGCCGCCCGGGCCGTGGCCGCCCTCATCGCCCGCGCGACCGTCACCCACCTGCCCGGGGACGCGCGGCGCACCGACCTGGCCACCTTCACCTACTCCGACCGCCCGGTCGTCTCCCGCCCCGGCTGCCCCATCTGCTCGGTGGCCGGTGCTGGCGAGGAGCCGGTGCCGGTGGCGCCCTCGGCCCCCGTGGGGGCCCGCTACGAGCAGTCCGTGGCCATCCCGCCGGCCGCCTTCGTCGACTCCAAGGGCCACCAGCAGCACTACAAGCCCTCCAACCTGCGCCTCCAGCGCGAGTTCCGCGACTGGCCGGTCTGCCCGCGCACGCCCCTGCCGCCGGCCGACCTCGAGCGCCTCGACCAGCCCTGGCCGATCGCGCACCCGCTCACCGACGCCGGCGCGGAGCCCGACGTCCTCGCCCGCCCCACCCTGAGCGAGCTCGCCACGATCCTGGCCCTGTCGGTGGGTGTGCGCGAGCCGCTCGGTGCCGAACCCACCGGCCCGGAGTCGGCCGAGGCCCCCCAGGCCCCGCCCAGCGCCAAGCTGCGCCGCTGGACGGCCGCCGGCGGCAACATCGGCTCGGTGACCGCCTACGTGCTCGTCCCCGAGTACGAGCAGAGCGGCCCGGAGGTCACGGGGGTGGCGGCCGGGCAGCGGCTCGCCCCCGGCACCTACGTCTACATCGAGCGTGACCACGCCCTGGCCCTCATCGGCCCCGCCCCCTCGGCGGCGGATTCGGGGGAAGGCGCGGAGACGGATCTCCTGCCCGACGGCGTCGGCGCCCGGATCGTCCTGACCGGCAACGTGGACAAGGTGGCCCGTAAGTACTTCTCCTTCGCCCTGCGCATCGCGGTCCAGGACTGCGGCTGCTCCTTCGAGGTGCTCCGTCTGGTCGCCGAGGCCCTGGGGGTGCCGCTGCGCGCCCGGGCCCGCTGGGACGAGCAGCGCATCGCCCGGGCGCTGGGCACCGACCCGGCCCGGGAGCCGGCCTGCATCGTCGTCGACCTGGGAGGCCGCCGTGCGCACTGA","MAGDATGSVMRAGDVGRAARRDLQFRIPRKPVVRLGLRARPEETGWIIDGARKSQVLGGAFAREHMGALLQACDGTRALDEIGEVTGIGPQAAFEAVSLLWTGGIVEEGDTEPAPGDPPPELARLLSRLGDSTGVNDSWQDAARRLAAARVAVVGDAELAGEMVAALEPTLPEVRLDSAPRRGDTLTVLVETADSVARSPEVARRCREEDIALLRVRAEQEAVTVGPYVDESFSPCLACACADEPEIGPRPEPVRHDIIVGLAARAVAALIARATVTHLPGDARRTDLATFTYSDRPVVSRPGCPICSVAGAGEEPVPVAPSAPVGARYEQSVAIPPAAFVDSKGHQQHYKPSNLRLQREFRDWPVCPRTPLPPADLERLDQPWPIAHPLTDAGAEPDVLARPTLSELATILALSVGVREPLGAEPTGPESAEAPQAPPSAKLRRWTAAGGNIGSVTAYVLVPEYEQSGPEVTGVAAGQRLAPGTYVYIERDHALALIGPAPSAADSGEGAETDLLPDGVGARIVLTGNVDKVARKYFSFALRIAVQDCGCSFEVLRLVAEALGVPLRARARWDEQRIARALGTDPAREPACIVVDLGGRRAH$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG0778COG name: NitroreductaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0778 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2343","2535504","2536241","738","5.64","-4.88","25966","GTGCGCACTGACTTCGAGACGCTGCGCGAGCTCATCTCCGGGTTCTCCGCCGGAACGGACACTCCCCCCGCCGAGCCGACCTCCGACGGCCTGGCCGCGCGCCGCCCGCGCCCGCCGCTGGACTGCCGGCTGCCGGACGCGCTTGTCCCCGGCCCCCAGGGCCCCTACCCCCACAGCCTGCACGAGACCTTCGAGCGCCGCTCGTCGTCGACCAGCTACGGCACCGAGCCGGTCGAGGCCGAGGCCCTCCTGGGCATGGTCCGCGACGCCCTGGCCGACGACGCACGCACCTGGGGGGCGGACGCGGTGGCCTGCCCCCTGGAGCCCTTCGTGCTCCTGCTGCGTCCGCGCGGCGCCGAGCCCGGCATCTACCGGGTGCGGCTCGACGGCGTCGACCTCGTCCGTCCCCTGCCGCCGGCCGAGGCGATCGAGGGCATGGCGGTGCAGAAGGAGTTCGCTCGCGCCGGGGCCATCGTCTCGGTGGCCGCCAACCTCGATGAGGCCGACGCCTGGGGCGGGGCCGCCGGCTACCGCTTCACCATGAGCCGCAGCGCCGCCCTCATCTACTCGCTGCACCTGCGCGCCGCCGCTCGGGGACTGGTGGGGACGGTCTTCGCCGGCTTCGCCACCTCGGCGGTGCGCCACCTGCTGGACTCCGACGGCGTCAGCCGCCACCAGATGTTCGCCGTCACCATCGCCAGACCGCAGACAGAACCGCCAGGTCAGGCGGCCGGCTAG","VRTDFETLRELISGFSAGTDTPPAEPTSDGLAARRPRPPLDCRLPDALVPGPQGPYPHSLHETFERRSSSTSYGTEPVEAEALLGMVRDALADDARTWGADAVACPLEPFVLLLRPRGAEPGIYRVRLDGVDLVRPLPPAEAIEGMAVQKEFARAGAIVSVAANLDEADAWGGAAGYRFTMSRSAALIYSLHLRAAARGLVGTVFAGFATSAVRHLLDSDGVSRHQMFAVTIARPQTEPPGQAAG$","Nitroreductase","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG0778COG name: NitroreductaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0778 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2345","2536881","2537996","1116","10.48","20.23","39911","ATGCTGTTCGACTCCGACTCGGGCAAGTACCACCGGCTCGGTGCGGCCGCCGCCTTCATCGTGGGCCAGTTCGACGGGGTGCGCCCCCTGCCGACCATCATCGAGGAGCTGCCCCAGGACATCGACGAGGCGGGTGCCAAGCGCATCACGGGCCTGGTCGACAACCTGCGCGACAAGGGCCTCCTGGCGGGCGGCGACCCCGCCTCCGCCGACCCCGCCGCCCCCGACGCTTCGGCGGCCCCGGTGCGCACCAGGCGCAGCCGCGGACGCCACACCGCCCAGCCCCGCCGGGCCCGCCACCTCAAGGTCGAGAGGCCCCGCCGCAGCGGGGGCTGGTGGCTGCCCCGCATCATCATTGCCCGCAAGTACCACCGGATCGTCGCTCCTGTTGTCACCCTGCTCCAGCGCCTGCCGGCCCCCGCGCTCAGCTGGGTCTTCTTGGCGCTGGCCGCCTGCGGGTATGCGGCCGGGGCCATGGCGCTCAGCTCCCTGGCCGGAGGCCCCCGCCCGGGGGTCCTGGTCTTCGTCACGGCGGTGGCGATCCAGCTGGTGAGCATCCTGCTGCACGAGTCCTGGCACGCCATCGTCGCCGGCTACCTGGGCACCCCCATCCGCGGATTGGGGGTGGCGCTCATGTTCTGGGCGATCCCCATCGCCTACGTCGACCGCACCGACTCCTACCGGGTGCGCTCCCGGCGCGGTCTGACCATGCTGGCCCTGGCCGGCATCTTCTCCGACGGCGTCGTCTGCGGCCTGGAGGCGGCCGTCGCCTGGGCCTCGACGGGAACGGTGCGCCAGGTGGCCCTGACCCTGTGCGCCTTCCAGCTCACCATGCTCGTCACCAACCTCAACCCCCTCACCCAGTCCGACGGCGTCGCCGCGGTCGAGGCGGCCACCGGCTCGGTCAACCTGCGCGGGCGCTCCATGTTCGTGCTGCGCTGCGTCCTGAGGCGCCAGCCGCTGCCGCCGGGGCTGGCCGTCATGCGGCCCGCGGTGCGCTGGGGCTACTTCATCTACGGGCTGGCGTGCTCTCTTCTCGGACTGCTGGCCTTCGTGATGAGCGTTGTATGGATAGGCTACTGGCTGTACGCCCTCGTGAAAGGTTTCCTCCTATGA","MLFDSDSGKYHRLGAAAAFIVGQFDGVRPLPTIIEELPQDIDEAGAKRITGLVDNLRDKGLLAGGDPASADPAAPDASAAPVRTRRSRGRHTAQPRRARHLKVERPRRSGGWWLPRIIIARKYHRIVAPVVTLLQRLPAPALSWVFLALAACGYAAGAMALSSLAGGPRPGVLVFVTAVAIQLVSILLHESWHAIVAGYLGTPIRGLGVALMFWAIPIAYVDRTDSYRVRSRRGLTMLALAGIFSDGVVCGLEAAVAWASTGTVRQVALTLCAFQLTMLVTNLNPLTQSDGVAAVEAATGSVNLRGRSMFVLRCVLRRQPLPPGLAVMRPAVRWGYFIYGLACSLLGLLAFVMSVVWIGYWLYALVKGFLL$","Peptidase M50","Membrane, Cytoplasm","hypothetical protein","membrane zinc metallopeptidase; M50 family","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[144-164]?$ $\"[169-189]?$ $\"[195-215]?$ $\"[235-257]?$ $\"[263-283]?$ $\"[338-358]?$	transmembrane_regions

","BeTs to 4 clades of COG0750COG name: Predicted membrane-associated Zn-dependent proteases 1Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0750 is aompkz-qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","Wed Aug 8 15:36:40 2007","","","","","Wed Aug 8 15:36:40 2007","","","","Wed Aug 8 15:36:40 2007","Wed Aug 8 15:36:40 2007","","","","","yes","","" "ANA_2347","2538065","2540629","2565","5.61","-18.45","92222","GTGACCCCCGGGGAGCCCATCCCATCCGCTCCGACCTCCGCCGTACCAGCGCCGGTACCGGCACCGGAGCCCCCGGCCCTGGCCCAGCCCGCCGTGGCCCTGCCGACCCTCGTGCGCCTGGGCGGGCTGCCGGTGCGGGCCGTCCCCGAGACCAGCGCCGCCGTCATCGGCACCCTGGACTACCTGCGTCGGCTCGACGAGGTGCTCGACGGCGCCGCCGACCAGCTGCTCGACCCGCTCTACGAGATCGTCCCCACCCTGGACAAGGCCGAGCGCCGCCCGGTCCTGCGCGCCAAGCGCTGCGTCTTCCAGGGGCGCGCCACCGACCTGTCCGAGGAGGTCCTGGCGGCCCTGCCCGCCGAGCTGCGCGCGCTGCTGGAGCGCTGGGACGCCCTGGTGGCCCGTAAGGAGGAGACCCGAGCCCGCCTGGCCGTCCTGGTCGACGTCGACCTGGACCGCAGCCGCGAGCTGCTGGCGGCCGGCCTCGACGAGCCCGGCTACCAGGAGGCCCTGGCGATCGCCGCCCCGGCCCTGGTCTCCACCCTGGCCGCCCGCGGCCGTCGGCTCGAGGACCCCCGAGTCCTGCGCACCCTCTACACCCTGGCCACCCGGGCCGCCCTCAAGACCAGCCCGTTCTCGGGACTGACCACCGTCAACGAGGCGGGCCAGCCCTCCACCGGGCGCAGCCACCGCATGGTGGCCACCCACCTGGCCTACCGCATCCTGAGCGCCACCGCCCAGGACCTGGCCGCCGACGGCGCCCTCTACCTCGAGCCCGCCCCCGTGCGCCGGTCCTACAGCGCCGCCCCCGGCCCGGACGCGGCCGGCGTCTACGGCCAGTACCCCTCCCGGGAGGTCGAGGCGGAGGCGCTGACCGTCGTCGGCGAGCACGAGTACGGCAACGGCATGGTCTTCCGCCAGGAGACCATCCAGCCCGCCCGCTGGCTCCAGGAGACCCACGACGCCCTCACTGGCGGCGGCATGCACGCCGTGCTCAGTGTGCGCGACGCCTGCGAGCGCGTGGGCGGAGCCGACCCGCGCCTGCGCCTGGAGCGGCTGCTGGCCTCCGGCGCCATCGTGCCGCACGTGCCCTGGTACCGCGGGGAGAACCCCTTCCCGCTGCTGGCCGCCTCGCTCTCACCGGAGCAGCAGCGCCAGTGGGGCAAGGACCTGGCCTGGCTGGCCCGGCTCGACGACGCCGTCGGCGCCGCTGACGGGCCCGGCCGCGCCGAGCTCCTCAACCGCACGGTGCGCCTGGCCGAGCGGGTCTTCCCCGACGGCGAGCTCGGTGAGCGGCCCAGCGGCTTCCTCTACGAGGACCGCGAGTCGACCCGCAGCTGGGTCGACCCTCTCGAGGACGCCCCCTTCGAGCAGGACGTCAAGACCCTGGGCGAGCTCGCCGACCCCTGGGTGGCCCGCTCCCACATCTACGACCTCATGGTGGCCCGCTTCGTCTCCCTGTTCGGCAACGGCGGGGTGTGCAAGGACCCGCTGGCCTTCTTCATGACCATCGCCCACGCCCCCGACGGCGACCAGGAGATGCTGCGTGCCGCCGGGCTCGACTACGCCGCCGGCCCCGACGAGGAGCGGGCCGCCCTGTCCGGCGGGCTCTCCGGCTCTCCCAGGCACCTGGGTGCCTTCCTCCAGCCGGTGGCCCCCAGCGCCCGGACTTACGCCGCCGGCGGGGGCCTGACCGTCGTCAACGCCTTCACCAACGCCAACGGCTCCCTCCAGGCCCGCTTCCACCGGCTCCTGGGCTCCGGCTTCCGGGAGCGCCTGGCCACGCGGATCCGCACCTCCTGGGGCACCGAGCGGGTCCTGGAGATCCAGGCCAGCACCGAGTGCAACACCGGTCAGGCCGTCTCCTGCGGGCTCCTACCGCCGCTGGGACTGCCCGGTGAGCCGGGGGCGCCGGAGGCGGTCCCCCTCAGCTCCCTGCGGCTCGTCCACGACCCGGCCACGAGCACCCTGTTCCTGGCCGACGACGCCGGGCCCGTTGGGCTGGCCTACCTGGGCCTGACCCCCCAGTACCTCCTGGGCGGCTACCTGTCCTGGCTGGTGCTGCTGAGCGACCCCTGGTCCCGGCTGCCCCCCTTCGCGGACCACTGGACCAGCCGCCGTCGGGACCTGAACGGCCCCCTGCCCGACGAGGTGATGCACTCCGAGCGGACCGTGGCCGGCCGTCTGGTGACCCGCCGCGAGTCCTGGACCTTCCCGGCCCACCAGATCGCCCCGCTCATGGACCGCGACCTGACCACGACCCTGCTGCACATGGACGACCTGCGCAAGCAGTGGGGCATACCCACGGAGGTGTTCGTCCACCAGCACATGCCCTCCCAGGGTGCCACCTTCGACCAGCACAAGCCCCGCTACGTGGATCTCACCTCACCGGTGTCACTGCTGGCGCTGCGCGGCTGGATCGACTCCGGCGCCGCCCACATCAGCTTCGTCGAGGCCCTGCCGGCCCGCGGCGAGGCCCTGGGGCTCACCCAGGATGGTGAGCCGACGGTGGCCGAGTACCTGGTGGGACTCCAGTGGCCCAAGAACCTGGGAGGCATGGCATGA","VTPGEPIPSAPTSAVPAPVPAPEPPALAQPAVALPTLVRLGGLPVRAVPETSAAVIGTLDYLRRLDEVLDGAADQLLDPLYEIVPTLDKAERRPVLRAKRCVFQGRATDLSEEVLAALPAELRALLERWDALVARKEETRARLAVLVDVDLDRSRELLAAGLDEPGYQEALAIAAPALVSTLAARGRRLEDPRVLRTLYTLATRAALKTSPFSGLTTVNEAGQPSTGRSHRMVATHLAYRILSATAQDLAADGALYLEPAPVRRSYSAAPGPDAAGVYGQYPSREVEAEALTVVGEHEYGNGMVFRQETIQPARWLQETHDALTGGGMHAVLSVRDACERVGGADPRLRLERLLASGAIVPHVPWYRGENPFPLLAASLSPEQQRQWGKDLAWLARLDDAVGAADGPGRAELLNRTVRLAERVFPDGELGERPSGFLYEDRESTRSWVDPLEDAPFEQDVKTLGELADPWVARSHIYDLMVARFVSLFGNGGVCKDPLAFFMTIAHAPDGDQEMLRAAGLDYAAGPDEERAALSGGLSGSPRHLGAFLQPVAPSARTYAAGGGLTVVNAFTNANGSLQARFHRLLGSGFRERLATRIRTSWGTERVLEIQASTECNTGQAVSCGLLPPLGLPGEPGAPEAVPLSSLRLVHDPATSTLFLADDAGPVGLAYLGLTPQYLLGGYLSWLVLLSDPWSRLPPFADHWTSRRRDLNGPLPDEVMHSERTVAGRLVTRRESWTFPAHQIAPLMDRDLTTTLLHMDDLRKQWGIPTEVFVHQHMPSQGATFDQHKPRYVDLTSPVSLLALRGWIDSGAAHISFVEALPARGEALGLTQDGEPTVAEYLVGLQWPKNLGGMA$","Goadsporin biosynthetic protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Onaka H, Nakaho M, Hayashi K, Igarashi Y, Furumai T.Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp. TP-A0584.Microbiology. 2005 Dec;151(Pt 12):3923-33.PMID: 16339937","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","Wed Aug 8 15:42:27 2007","","Wed Aug 8 15:42:27 2007","","","Wed Aug 8 15:42:27 2007","Wed Aug 8 15:42:27 2007","Wed Aug 8 15:42:27 2007","Wed Aug 8 15:39:02 2007","","Wed Aug 8 15:42:27 2007","","","Wed Aug 8 15:39:02 2007","","","","Wed Aug 8 15:39:02 2007","Wed Aug 8 15:39:02 2007","","","","","yes","","" "ANA_2350","2540626","2541915","1290","7.06","0.29","45894","ATGAGCACGCACGACGACGTCCAGTCCAGCCGGCGCGAGCAGCGCAACCAGCCCAGCCGGCTCATCCGCTCCCGCAGGCTGCGCTGGCTCGGGGGGCGCTCGCGGGCCAGTGAGCAGGCGGAGCGCACCGGGCCGGCGAGCCAGATGGATCAGGTGGGCCAAGTGGGCCAGGTGGGCCAGATGGATCAGGTGGGCCAAGTGGGCCAGGCGGGCCAGATGGATCAGGTGGGCCAGCCCAGTCAGGGCGGTCAGGCCGGCCAGGCCGGAATGGTTGGCCTGGGGGGCGCGACGTCGCAGGATGGCGGCTCGATCCCGGGGATCCAGCCCCTGGAGATGGCGGCCGCCGACTTCGGCAACCTGCGCGCCCAGCACAGCGCGATGCGCCAGCGGGGTGCGGCGATGGCCGGTCAGCGTGAGGGGGTCGGCTGGCTGTATGCGCGGATCTACTGCGCCGGCGGGGACGACACCGACGCCCTGCTGCCCGAGGTCGCCCAGTGGCTGGATCGGGCCCGCGGCCAGTGGGACATCCGCTCAGCGCACTTCCTGCGCTTCGTCGACCTGCGCGGCCACCACATCCGGCTGCGGCTCAAGGCCGTCGAGGGCGTCCTGGACGAGGCCTACGCGAGCATGCGCGAGCTGGGGGCCGTGGCCCAGCGGACCGAGGCGCGCACGGTCGAGCGCCTCGTCTCCGATCCGATGACCGGGGGGATCGGCGCGAGCCGGCCCGGCATCACCTTCGGCGTCTACGGCCCCGAGTACGACAAGTACGGGGGAGTGGCCGGCGTCGAGGAGGCCGAGCGGCACTTCTACGTCTCCAGCCGCTGGTGCCTGGACCACCAGGTCTGGCAGATCCCGAGGCCGGTGCCGCGGGCGGCCCTGGCGGCGCGGTTCCTGGCGCTGGCGGCCCGCAGCGCGCCGCTGCCCGAGGCCGAGCTGCTCTCCGCCCACCTGCGGATGTGGGGCTCTCGGCTCCCCGCGCACCTGCGCGACGGCAGCGCCCTGGGGCCGATCGTTCAGCAGCTGCTGGAGGTCATCGAGTTCCAGTTCGATGAGATCCCGTCCTGGAGCCAGGCGGCGGCTGCCGTGGGTGAGCTGGCCGACGACGCCGGGCGCGCCATCGGCGTCATGGGGGCGGGCACCGGCGGGCGCCGGGCCTTGGACCTGCTGCACATCGACGTCAACCGGCTCGGTCTCAACCCGGCCGAGGAGTGCATTGCCGGGCTGTGCGCCCGCCAGCTCCTGACCGGGGGCGCCGTACCCCCGGCCCAGCCCTCAGCCGCCGTCGGGTAG","MSTHDDVQSSRREQRNQPSRLIRSRRLRWLGGRSRASEQAERTGPASQMDQVGQVGQVGQMDQVGQVGQAGQMDQVGQPSQGGQAGQAGMVGLGGATSQDGGSIPGIQPLEMAAADFGNLRAQHSAMRQRGAAMAGQREGVGWLYARIYCAGGDDTDALLPEVAQWLDRARGQWDIRSAHFLRFVDLRGHHIRLRLKAVEGVLDEAYASMRELGAVAQRTEARTVERLVSDPMTGGIGASRPGITFGVYGPEYDKYGGVAGVEEAERHFYVSSRWCLDHQVWQIPRPVPRAALAARFLALAARSAPLPEAELLSAHLRMWGSRLPAHLRDGSALGPIVQQLLEVIEFQFDEIPSWSQAAAAVGELADDAGRAIGVMGAGTGGRRALDLLHIDVNRLGLNPAEECIAGLCARQLLTGGAVPPAQPSAAVG$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PTHR10499	$\"[8-109]T$	COLLAGEN ALPHA CHAIN
PTHR10499:SF50	$\"[8-109]T$	COLLAGEN ALPHA 1(IX) CHAIN-RELATED

InterPro
IPR000362
Domain

Fumarate lyase
PR00149	$\"[180-196]T$ $\"[312-328]T$	FUMRATELYASE
PF00206	$\"[134-332]T$	Lyase_1
PS00163	$\"[312-321]T$	FUMARATE_LYASES

InterPro
IPR013539
Domain

Adenylosuccinate lyase C-terminal
PF08328	$\"[349-469]T$	ASL_C

noIPR
unintegrated

unintegrated
G3DSA:1.20.200.10	$\"[138-418]T$	no description
PTHR11444	$\"[8-113]T$ $\"[130-477]T$	ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF2	$\"[8-113]T$ $\"[130-477]T$	ADENYLOSUCCINATE LYASE

","BeTs to 21 clades of COG0015COG name: Adenylosuccinate lyaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0015 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB013539 (Adenylosuccinate lyase C-terminal) with a combined E-value of 1.7e-174. IPB013539A 5-40 IPB013539B 70-103 IPB013539D 179-220 IPB013539E 230-276 IPB013539F 277-315 IPB013539G 317-337 IPB013539H 338-366 IPB013539I 367-408 IPB013539J 415-448 IPB013539K 449-479 IPB013539C 117-150***** IPB003031 (Delta crystallin signature) with a combined E-value of 1.8e-15. IPB003031B 175-195 IPB003031E 312-328***** IPB009049 (Argininosuccinate lyase) with a combined E-value of 1.4e-11. IPB009049C 181-218 IPB009049E 295-349***** IPB000362 (Fumarate lyase) with a combined E-value of 5.3e-07. IPB000362 312-337","","","-50% similar to PDB:2HVG Crystal Structure of Adenylosuccinate Lyase from Plasmodium Vivax (E_value = 8.3E_76);-43% similar to PDB:1DOF THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY (E_value = 1.1E_14);-43% similar to PDB:2PFM Crystal Structure of Adenylosuccinate Lyase (PurB) from Bacillus anthracis (E_value = 4.2E_11);-46% similar to PDB:1F1O STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES (E_value = 2.7E_10);","Residues 18 to 328 (E_value = 2.8e-18) place ANA_2351 in the Lyase_1 family which is described as Lyase.Residues 134 to 332 (E_value = 3.7e-25) place ANA_2351 in the Lyase_1 family which is described as Lyase.Residues 349 to 469 (E_value = 9.7e-66) place ANA_2351 in the ASL_C family which is described as Adenylosuccinate lyase C-terminal.","","lyase (purB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2352","2544527","2544042","486","11.37","6.36","16965","ATGCCACAAGGATCCGGCAGGATTTTGCCCGGTCATACCATTCCCCACCATGTCCGCCCTAGAAGGTCATCTACCATGCGACTCCTCCCACCAGTCGTCTTCACGCTTGCCACGACCGTCCTGGCCCTGACGGTCGGCGGCGGCCTGTTCGGCTGGGAAACCTCCCTCCTGACGCCTCTGAGCCTGCTCACGGTGAGTCTCATCCTCCTCCAGGCCCAGCACGTTCAGCGCGCCGAGCCGTCCCAGCGGATCCCGGGCCCCTCGATCCTCGCGCTGGCCGTCATCGGCCTGGGGCTGGCGGCCGCACTGCTCGGCCACGGCCTCTACAGCCATGAGCCCGCCGCCGCCATCAACCTGCCGTCGGCCGGCATCCTGCTGTTCGTCGTCGTGACCGCCTACCGCCGACGCCGCCCCGAGGCGCAGCCCGTCCTCGTCTCGACCCAGGAGGCCCCACTCGCAGAGATCGGTGCCAACCTGCCACAATGA","MPQGSGRILPGHTIPHHVRPRRSSTMRLLPPVVFTLATTVLALTVGGGLFGWETSLLTPLSLLTVSLILLQAQHVQRAEPSQRIPGPSILALAVIGLGLAAALLGHGLYSHEPAAAINLPSAGILLFVVVTAYRRRRPEAQPVLVSTQEAPLAEIGANLPQ$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[28-50]?$ $\"[56-74]?$ $\"[89-109]?$ $\"[115-133]?$	transmembrane_regions

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[54-124]T$	Acetyltransf_1
PS51186	$\"[10-145]T$	GNAT

","BeTs to 4 clades of COG0456COG name: AcetyltransferasesFunctional Class: RThe phylogenetic pattern of COG0456 is amtkYqvcebrh---------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 12-143 are similar to a (GNAT CGL0178 TRANSFERASE FAMILY ACETYLTRANSFERASE) protein domain (PD640873) which is seen in Q8NTX3_CORGL.","","","Residues 54 to 124 (E_value = 6e-07) place ANA_2352.1 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","","","1","","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:14:12 2007","Mon Jul 16 16:14:12 2007","Mon Jul 16 16:14:12 2007","Mon Jul 16 16:17:38 2007","","","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","Mon Jul 16 16:13:14 2007","","Mon Jul 16 16:13:14 2007","","Mon Jul 16 16:13:14 2007","yes","","" "ANA_2354","2545674","2545303","372","11.55","8.89","13053","ATGCGACTCATCAAGCCCGCCATTGTTGTCCTTGCCCTGACCGTCCTGGTCAACTCGATCGGAAGCCTGCTGCTCGGGTGGCAGCTCAACAGCCTCACCTCATCGCTGTGCATGCTCCTGCTCGGCCTCATCCTGCTGCAAGCCCAGAACTCGGGTCCGGGCGAGCGCAGCCTGCCGCCGTCGGGCGTTCGGCTGCTGGGGGCCGTCGGAGTCATCCTCTCCGGGCTCATGGTCGCGCGCGGCCTGTACCGGTCCGACGTCGACGTGCTCCTCGCCCTGCCCGCGCTGGGCCTACTGGGCTACGTCCTGGCGCGCAGTCTGAGGGACCGGCGGACCCGCGAGGTCACCGCGCGCAAGACCTCGGCCCGATAG","MRLIKPAIVVLALTVLVNSIGSLLLGWQLNSLTSSLCMLLLGLILLQAQNSGPGERSLPPSGVRLLGAVGVILSGLMVARGLYRSDVDVLLALPALGLLGYVLARSLRDRRTREVTARKTSAR$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[2-22]?$ $\"[28-48]?$ $\"[63-83]?$ $\"[89-107]?$	transmembrane_regions

InterPro
IPR007037
Domain

Siderophore-interacting protein
PF04954	$\"[127-243]T$	SIP

InterPro
IPR013113
Domain

FAD-binding 9, siderophore-interacting
PF08021	$\"[24-120]T$	FAD_binding_9

","BeTs to 3 clades of COG2375COG name: Siderophore-interacting proteinFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2375 is ---------dr---efg---------Number of proteins in this genome belonging to this COG is 1","***** IPB007037 (Siderophore-interacting protein) with a combined E-value of 6.8e-14. IPB007037B 96-107 IPB007037C 114-166 IPB007037D 201-223","","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 120 (E_value = 1.3e-11) place ANA_2355 in the FAD_binding_9 family which is described as Siderophore-interacting FAD-binding domain.Residues 127 to 243 (E_value = 1.6e-06) place ANA_2355 in the SIP family which is described as Siderophore-interacting protein.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2356","2548276","2546819","1458","5.19","-17.43","53356","GTGAGCGGCGTCGGACTGCTGATCGGAGTGCTGCTGGCGGGGCTGCGTCATGACTGGATCCTACCGACGCCGGGTCACCCGGCAGGCGGTTCGGTGACGGCGCCCGGCGGCCCGGTGGGGACGCGAGCGCTCCGCCCGATCTATCCTCTGCCCATGACAATCGACACCTCCTGGGTCGCCCAGCGCAATGCCGCCTTCCTCGCCGACCCCGCCGCCCGCCTGGCCGGCAACGCCGTCGCCACCACGGACGTGGAGCAGGTCTCCCTGGACCGGACCACGGTGACCGCCATCGACACCTCCGTGTCCGACCTCGTCCCGGACGCCTCGATCACCGACCAGAAGCAGTCGGGACGCTGCTGGGCCTTCGCCGGCCTCAACGTGCTGCGCGCCTCCATGCTCAAGGAGCTCGAGCTCGACTCCCTGGAGCTGAGCCAGGCCTTCCCCTTCTTCTACGACAAGCTGGAGAAGGCCAACGCCTTCCTCACGCGCGTCATCGCCGAGGCGGACCGCCCCCTGGATGACCGCGAGGTCGTCGACTCCCTGTACTCCCCCATTCCCGACGGCGGCTGGTGGCCGGAGTTCGCGCGTCTGGTGGCCAAGTACGGGATCGTCCCGGCCTACGCCATGCCGGACACCGTCTCGGCCGGTAACTCCGAGGCGATGAACGAGCACCTGGCCACGCTGCTGCGGCGCACGGCCCTGCGACTGCGGGCCGCGGTGGCCGACGGCGTCGACCCTGAGCCGCTGCGGCTCACGGCCCTGGAGCAGGTTCACCGGATGCTGTGCATCCATCTGGGGACCCCGCCCGAGGAGTTCGTGTGGCAGTACCGCGATAAGAACAAGGAATTCCACCGGGTCGGGACGCTCACGCCGCGACAGTTCGCGCAGCGCTATGTCACCGGGGTGGAGGAGTTCGTGGTCGTGGCCCACGACCCGCGCCCGGAGATCGCGGTCAACACGCGCTACGGCATGGGCCGCAGCGACGTCATGGTGGGCGAACCGGTCCAGGATCACGTCACCGCCGAGCTCGAGGTGCTCAAGGCCGCCGCGATCGCCGCGATCCAGGACGGCGAGCCTGTGTGGTTCGCCTGCGACGTCGCCAAGCAGCGGGACAAGAAGGCCGGAATCTGGGACGCCGCCCTGCACGACTACGAGGGCCTGTACGGGGTGGACCTGTCGATGACGAAGGCCGAGCGGCTGGTGGCGCGCGAGTCGGCGCTCACCCACGCCATGTGCCTGACCGGCGTCGACCTGGTCGACGGCGCTCCACGGCGCTGGCGGGTGGAGAACTCCTGGGGCGACAAGTTCGGGGACAAGGGCTTCCACACGATGAGCGACTCCTGGTTCGACGAGTACGTCTTCGAGGTCGTCGTGCGCGCGAGCCGCCTGCCCGAGGAGGTCCGCGCCGCCCTGGAGACCGAGCCCATCATGCTGCCCAGCTGGGACCCGATGGCCTGA","VSGVGLLIGVLLAGLRHDWILPTPGHPAGGSVTAPGGPVGTRALRPIYPLPMTIDTSWVAQRNAAFLADPAARLAGNAVATTDVEQVSLDRTTVTAIDTSVSDLVPDASITDQKQSGRCWAFAGLNVLRASMLKELELDSLELSQAFPFFYDKLEKANAFLTRVIAEADRPLDDREVVDSLYSPIPDGGWWPEFARLVAKYGIVPAYAMPDTVSAGNSEAMNEHLATLLRRTALRLRAAVADGVDPEPLRLTALEQVHRMLCIHLGTPPEEFVWQYRDKNKEFHRVGTLTPRQFAQRYVTGVEEFVVVAHDPRPEIAVNTRYGMGRSDVMVGEPVQDHVTAELEVLKAAAIAAIQDGEPVWFACDVAKQRDKKAGIWDAALHDYEGLYGVDLSMTKAERLVARESALTHAMCLTGVDLVDGAPRRWRVENSWGDKFGDKGFHTMSDSWFDEYVFEVVVRASRLPEEVRAALETEPIMLPSWDPMA$","Bleomycin hydrolase","Cytoplasm, Extracellular","Bleomycin hydrolase (BLM hydrolase) (BMH) (BH)","bleomycin hydrolase ","Bleomycin hydrolase","","Dufour E. Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidin. Biochimie 1988. 70(10):1335-1342. PMID: 3148320Rawlings N.D., Barrett A.J. Families of cysteine peptidases. Meth. Enzymol. 1994. 244:461-486. PMID: 7845226King T.P., Hoffman D., Lowenstein H., Marsh D.G., Platts-mills T.A., Thomas W. Allergen nomenclature. WHO/IUIS Allergen Nomenclature Subcommittee. Int. Arch. Allergy Immunol. 1994. 105(3):224-233. PMID: 7920024","","","

InterPro
IPR000169
Active_site

Peptidase, cysteine peptidase active site
PS00139	$\"[113-124]?$	THIOL_PROTEASE_CYS
PS00639	$\"[407-417]?$	THIOL_PROTEASE_HIS

InterPro
IPR004134
Family

Peptidase C1B, bleomycin hydrolase
PIRSF005700	$\"[50-484]T$	Aminopeptidase C (bleomycin hydrolase)
PTHR10363	$\"[22-484]T$	CYSTEINE PROTEASE C1B
PF03051	$\"[53-485]T$	Peptidase_C1_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.70.10	$\"[100-484]T$	no description
signalp	$\"[1-17]?$	signal-peptide

","No hits to the COGs database.","***** IPB004134 (Peptidase C1-like family) with a combined E-value of 2.6e-137. IPB004134A 110-133 IPB004134B 138-168 IPB004134C 169-211 IPB004134D 253-291 IPB004134E 308-333 IPB004134F 342-382 IPB004134G 394-417 IPB004134H 425-458 IPB004134I 475-485","","","-54% similar to PDB:1CB5 HUMAN BLEOMYCIN HYDROLASE. (E_value = 3.0E_78);-54% similar to PDB:2CB5 HUMAN BLEOMYCIN HYDROLASE, C73S/DELE455 MUTANT (E_value = 4.4E_77);-49% similar to PDB:1GCB GAL6, YEAST BLEOMYCIN HYDROLASE DNA-BINDING PROTEASE (THIOL) (E_value = 8.9E_54);-49% similar to PDB:1A6R GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A (E_value = 9.8E_53);-49% similar to PDB:3GCB GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A/DELTAK454 (E_value = 9.8E_53);","Residues 53 to 485 (E_value = 8e-174) place ANA_2356 in the Peptidase_C1_2 family which is described as Peptidase C1-like family.","","hydrolase (BLM hydrolase) (BMH) (BH) (pepC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2357","2548226","2548897","672","5.08","-12.68","23867","ATGACGCAGCCCCGCCAGCAGCACTCCGATCAGCAGTCCGACGCCGCTCACTCCGCCTCCCGCTGGGAGGAGCGTTACGCCTCGGTCGAGCAGCTCTGGTCGGGGCGCCCCAACGACTGGCTGCCGGAGCTCGCCACCGACTGGAGCCCCGGGACCGCCCTGGAGATCGGCTGCGGCGAGGGCGCCGACGTCCTGTGGCTGGCCGAGCGCGGCTGGCAGGTGGTCGGGCTGGATCTGTCCGCCACCGCCATCGGGCGCCTGACCGGGCAGGCCGAGTGGCTCGGGGTCGCCTCGCGCGTGACCGGCCGCGTGCACGACGCCGGAGACGGCCTGCCGGCCGGACCCTTCGACCTGGTGACGAGCTTCTACGTCCACGGCGGGCGCGAGCCGGGCTCCCTGGACCTCGTGGCCCTCCTTTCCGACGCCGCTACCCGCGTCGCTCCCGGCGGGCACCTGCTCGCCGCGGTGCACGCCGTCAACCCGCCCTGGCACACCCACCACGCCCGCACCTACACGGCCGCCGAGCTCCTCGAGGGTCTGGCCGAGGCGACGGACGGCTGGGAGGTCGTCGTCGGCGAGGAGCGGGACCGGCAGGTCACGGGGCCCGACGGCCAGGAGGGGCACCGGGCCGATGCCGTCGTGTGCCTGCGCAGGCCACCGGCCTCGGTTTGA","MTQPRQQHSDQQSDAAHSASRWEERYASVEQLWSGRPNDWLPELATDWSPGTALEIGCGEGADVLWLAERGWQVVGLDLSATAIGRLTGQAEWLGVASRVTGRVHDAGDGLPAGPFDLVTSFYVHGGREPGSLDLVALLSDAATRVAPGGHLLAAVHAVNPPWHTHHARTYTAAELLEGLAEATDGWEVVVGEERDRQVTGPDGQEGHRADAVVCLRRPPASV$","Methyltransferase","Cytoplasm","methyltransferase homolog","methyltransferase","Methyltransferase type 12","","Poon W.W., Barkovich R.J., Hsu A.Y., Frankel A., Lee P.T., Shepherd J.N., Myles D.C., Clarke C.F. Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. J. Biol. Chem. 1999. 274(31):21665-21672. PMID: 10419476Ogawa H., Gomi T., Fujioka M. Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers. Comp Biochem Physiol B 1993. 106(3):601-611. PMID: 8281755","","","

InterPro
IPR013217
Domain

Methyltransferase type 12
PF08242	$\"[54-152]T$	Methyltransf_12

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[39-154]T$	no description
PTHR10108	$\"[20-119]T$	METHYLTRANSFERASE
PTHR10108:SF15	$\"[20-119]T$	2-HEPTAPRENYL-1,4-NAPHTHOQUINONE METHYLTRANSFERASE

","BeTs to 17 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 6","***** IPB008854 (Thiopurine S-methyltransferase) with a combined E-value of 2e-13. IPB008854A 43-92","","","No significant hits to the PDB database (E-value < E-10).","Residues 54 to 154 (E_value = 3.9e-11) place ANA_2357 in the Methyltransf_11 family which is described as Methyltransferase domain.Residues 54 to 152 (E_value = 2.1e-14) place ANA_2357 in the Methyltransf_12 family which is described as Methyltransferase domain.Residues 57 to 84 (E_value = 2.5e-07) place ANA_2357 in the TPMT family which is described as Thiopurine S-methyltransferase (TPMT).","","homolog ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2358","2549676","2551622","1947","4.82","-27.90","66976","ATGGACGGGGACAGTCCGTACCCCGTCTGGAAGCAGGATCCCCACGCGACGAAATCACCGGCCTCTTCATCGGCGCCCCCGAAGCCCACGACTCCTCCCGCCTCGACCGCCCCACAAGATAGCGGCCACACCTGGACCATGTGGGGTGTGGGCCCTGCGGTGGTGGTGGGGGGCGGCTCCGTCTCCGTGAACACGACCGACCTCGACTCCCTGGCCAGCAGCCTCACCTCGGCGGCAGGCACCCTGGATGACGCGCGAACCCTCATTGCCAACGTGGTCACTGAAGTGAATGAGGCGCCGGCTCCGCCGGTATCCCCACCCAGCGTCCCATACCCGATCCTGGGTGGATTCGATCTGGAGAAGTCCGTCGCTCTTCAGTCCCTGGATGCGTTGAGCATGGGGCCGGGGTCGCTCCAGGACGTCGCCGACACTATGCGCGGCCTCGCCTCCGACGTCACCGCCTGCTCCCAGGCCCACGCCCTGGCCGATGGGAAGGCCACTCCCGCCAATGGTCTGGTAGGTCCCGTGGACGTTCGGGCCTTCGACTCCGGTCTCCTCAAGATGGCGCTGGGGTCCGTCGCAATCGCCTCTCAGTTCCCCACGATCGCAACTCTGCTGGCGTCCTCACCGGCGACGAGCTGGCTGCTCTATGAGCTGGTGAAGGACAACGAGGACGGGCAGGCCGCCGTCGAGGCCCTCCAGCTCCTGCTCAACGACCCGACCACCGAGCAGTGGGTCAAGGAGGACCTCGTCAGGATCGTCCTGCTGACGCGCTGGCTCAAGAACGCCAAGACCGGGCGGGAGGCCGCCACGGTCCAGACCTACCTCCAGCAGGTCTCCCAGCGCCTCGACCCCTGGGCGACACACCGCCTGCCCGGGCAGGTCGCCGTCGGGACGCAGACCGTCGACACCACGAGCCTGACGCCCATGCAGCGCGTCGCCATGGTCCTGGGTGCGAACGCCGCCGCGATAGGGGCGGGGGTCTACGGAACCCAGAGCGGCGTCACGGTCACCCCCGTCGGCGGCAACGGGGCCACCGTGCTCCCGCCCGCCGCCAAGGATCCCTTCGGGCTCGCCAGTGCCGTGAATCCCGGTATGACCGGCAAGGGCAAGGAGGCCAAGTCCCCGCAGAGCATCTCCGAGACCATCACCCACTGCCAGGAGGTGCAGTCCTCGAAGAACTCCCTGGGGCAGGGCTACGAGGAGGCCGGGGTCATCTCCATCCAGCGGGTCGAGCATGCCGACGGGCGAGTCTCCTGGGTCGTCTACGTCCCCGGCACCACCGACTGGACCGTCGGCGACGGCGAACCGCAGGACCTGCTCACCAACCTCGAGGCCGTGGGCGGCACGCCCACGGACATGGAAAGCGGCGTCGTCACCGCCATGCGCCAGGCCGGCATCCAGCCAGGTGAGGAGGTCGCCCTCTACGGCCACTCCCAGGGCGGAATCACGGTCTCCAACATTGCCGCCGACCCCGCCATCCAGGAGCGTTACAACATCACCACGGTCCTCACCGCCGGCTCCCCCACCGCGGGAGCCGACATCCCCGACGACGTCCACGCCCTCCACCTGGAGAACACCGGCGACGCCGTCCCGGGGCTCGACGCCGCCCCCACACCCACCGGCCCCAACCGGCAGGTCGCCATGCTCGACACCCACCAGATGAGCACGAACGGCTACCCCCACTCCTCCAGTGTCTACGCCCAGGCCACCGAAGGGCTGGAGGACAAGGCTCCCGAGCTGGCCGAATGGAACAAGTCCTTCTCACACGCCTCGGGCGCCGGCGAGCAGGGGACGACCACCACCGAGTACACCTTCGCGATCCAGCGCAACACCGACCCCAACGGGGTCTACAAGGGCGGCGCCACCTACCAGGGCAAGGTGCCCTCGGCACAACCCTCCTACCCCCGGCCCACCCCGAGCCCGCAGACGACGGGCGAGCACTAG","MDGDSPYPVWKQDPHATKSPASSSAPPKPTTPPASTAPQDSGHTWTMWGVGPAVVVGGGSVSVNTTDLDSLASSLTSAAGTLDDARTLIANVVTEVNEAPAPPVSPPSVPYPILGGFDLEKSVALQSLDALSMGPGSLQDVADTMRGLASDVTACSQAHALADGKATPANGLVGPVDVRAFDSGLLKMALGSVAIASQFPTIATLLASSPATSWLLYELVKDNEDGQAAVEALQLLLNDPTTEQWVKEDLVRIVLLTRWLKNAKTGREAATVQTYLQQVSQRLDPWATHRLPGQVAVGTQTVDTTSLTPMQRVAMVLGANAAAIGAGVYGTQSGVTVTPVGGNGATVLPPAAKDPFGLASAVNPGMTGKGKEAKSPQSISETITHCQEVQSSKNSLGQGYEEAGVISIQRVEHADGRVSWVVYVPGTTDWTVGDGEPQDLLTNLEAVGGTPTDMESGVVTAMRQAGIQPGEEVALYGHSQGGITVSNIAADPAIQERYNITTVLTAGSPTAGADIPDDVHALHLENTGDAVPGLDAAPTPTGPNRQVAMLDTHQMSTNGYPHSSSVYAQATEGLEDKAPELAEWNKSFSHASGAGEQGTTTTEYTFAIQRNTDPNGVYKGGATYQGKVPSAQPSYPRPTPSPQTTGEH$","Hypothetical protein","Periplasm, Extracellular","gp340, putative","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2359","2552174","2551767","408","8.74","1.16","13780","ATGGAGATCGTGGCACGAACTGTCGGAAATGCGGCCGGCCTGTGGCTGGCCACGCGCCTCCTGTCCGGGCTGAGTGTGCCCGAGGGGGCGGGGGCCGGCCCGATGTGGCTGAACCTGCTGGTCCTGGGCTTGATACTGGCGCTGGTGAACTCGCTCATCAAGCCGGTGGCGAAGTTCGTGACCTTTCCGCTCTACATTGTCACCTTCGGACTGTTCGCCCTGGTGGTCAACGGTGCGATGCTCTCGCTGACGGGCCGGCTCACCGACCACATTGCGGCGCTGGGCGCCGGCGGGTCGGTGCCGCTGGGGCTGGAAGTGGCCTCCTTCGGCTCGGCGGTGGTCGGCTCGATCATCATCTCGGTGATCTCCTCGATCATCGCCGCAATGCTCGTGCGCCGCGAGGACTGA","MEIVARTVGNAAGLWLATRLLSGLSVPEGAGAGPMWLNLLVLGLILALVNSLIKPVAKFVTFPLYIVTFGLFALVVNGAMLSLTGRLTDHIAALGAGGSVPLGLEVASFGSAVVGSIIISVISSIIAAMLVRRED$","Membrane protein","Membrane, Cytoplasm","membrane spanning protein","hypothetical protein predicted by Glimmer/Critica","membrane protein of unknown function","","","","","

InterPro
IPR007165
Family

Membrane protein of unknown function
PF04020	$\"[1-134]T$	DUF360

noIPR
unintegrated

unintegrated
signalp	$\"[1-51]?$	signal-peptide
tmhmm	$\"[35-55]?$ $\"[61-81]?$ $\"[83-101]?$ $\"[107-127]?$	transmembrane_regions

","BeTs to 5 clades of COG1950COG name: Predicted membrane proteinFunctional Class: SThe phylogenetic pattern of COG1950 is -------c-br----------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 47 to 180 (E_value = 7.4e-17) place ANA_2359 in the DUF360 family which is described as Membrane protein of unknown function.","","spanning protein","","1","","","Wed Aug 8 15:56:40 2007","","Wed Aug 8 15:56:40 2007","","","Wed Aug 8 15:56:40 2007","Wed Aug 8 15:56:40 2007","Wed Aug 8 15:56:40 2007","","","","","","Wed Aug 8 15:56:40 2007","","","","Wed Aug 8 15:56:40 2007","Wed Aug 8 15:56:40 2007","","","","","yes","","" "ANA_2360","2552305","2553378","1074","5.16","-10.67","37534","GTGCGCATCCGCCCCGACGTCGCCGCCCTGCCCGCCTACGTGCCCGGGGCCCGCCCCGACGAGGACGCCGCGGCGCAGATCGCCAAGCTCTCCTCCAACGAGCTGCCCTATCCGCCGCAGGACGCGGTCGTCGAGGCCATCACCCGGGCCGCCGCCGGAGTCAACCGCTACCCGGAGATGACCGGGGAGAGCCTCGCGCATGCCCTCGCCCGCCGCTGGGGCGTGGAGGCCGAGCAGGTCGTCGTCGGCAACGGCTCGGTCGCCCTCATCCAGCACCTGCTCGACGCCGTCTGCGAACCCGGCGACGAGGTCGTCATCCCCTGGCGGTCCTTCGAGGCCTACCCGATCTGCGTTGCCGTCGCCGGGGCCCGGGCCGTACGCGTCCCGCTGACCCCCGACGCCCGCCACGACGTGCCCGCCATGCTGGCGGCCATCACCGCCCGCACCCGCGTGGTCATGGCCTGCACCCCCAACAACCCCACCGGGACGATCCTGACCGCCGAGGAGCTGGCCGAGCTCGTGGCCGGGGTGCCACGCGACGTCGTCGTCCTCATCGACGAGGCCTACCTCGACTTCGTCACCGACCCGCGGGCCGGTGACGCCCTCACCCTCCTGGCCGGAGCCCCCAACCTCGTGGTCTCACGGACCTTCTCCAAGGCCCACGCCCTGGCCGGGATGCGCGTGGGCTACCTCGTGTGCGAGCCGGGCCTGGCCGCCGCCATCCGCTCGGTGACCACACCCTTCGGGGTCAACCTGCCCGCGCAGGCCGCCGCCACCGCGGCCCTGGGGGAGGGAGAACTGGCCCGAACCGCCGAGCGCTCGGCCGCCGTCGCCGCCGAGCGGGACCGGGTCGTGGAGGTACTGCGCACCCAGGGCTGGCAGGTCCCCGAGGCTCAGGGCAACTTCTTCTGGCTCGGCGTGGACGAGCAGACGACGGCGCTGGCCGAGCACTTCCGCGGCGCCGGCATCCTCGTGCGGCCCTTTGCCGGTGAGGGCGTGCGGATCTCGGTGGGGACGACGTCGGACAACGAGAGGGTCCTGGCCGCCGCAGCCGCCTGGCGCGCCGAGCACTGA","VRIRPDVAALPAYVPGARPDEDAAAQIAKLSSNELPYPPQDAVVEAITRAAAGVNRYPEMTGESLAHALARRWGVEAEQVVVGNGSVALIQHLLDAVCEPGDEVVIPWRSFEAYPICVAVAGARAVRVPLTPDARHDVPAMLAAITARTRVVMACTPNNPTGTILTAEELAELVAGVPRDVVVLIDEAYLDFVTDPRAGDALTLLAGAPNLVVSRTFSKAHALAGMRVGYLVCEPGLAAAIRSVTTPFGVNLPAQAAATAALGEGELARTAERSAAVAAERDRVVEVLRTQGWQVPEAQGNFFWLGVDEQTTALAEHFRGAGILVRPFAGEGVRISVGTTSDNERVLAAAAAWRAEH$","Histidinol-phosphate aminotransferase","Cytoplasm","histidinol-phosphate aminotransferase","histidinol-phosphate aminotransferase","histidinol-phosphate aminotransferase","","Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K., Okamoto A., Higuchi T., Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 1991. 266(4):2567-2572. PMID: 1990006","","","

InterPro
IPR004839
Domain

Aminotransferase, class I and II
PF00155	$\"[25-350]T$	Aminotran_1_2

InterPro
IPR005861
Family

Histidinol-phosphate aminotransferase
TIGR01141	$\"[4-353]T$	hisC: histidinol-phosphate aminotransferase

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[39-264]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[41-356]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF3	$\"[41-356]T$	HISTIDINOL-PHOSPHATE AMINOTRANSFERASE

","BeTs to 19 clades of COG0079COG name: Histidinol-phosphate aminotransferase/Tyrosine aminotransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0079 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB001176 (1-aminocyclopropane-1-carboxylate synthase signature) with a combined E-value of 1.4e-16. IPB001176C 79-99 IPB001176E 146-170 IPB001176F 181-204 IPB001176G 210-234***** IPB004839 (Aminotransferase, class I and II) with a combined E-value of 7.5e-14. IPB004839A 143-163 IPB004839B 186-193 IPB004839C 218-229***** IPB001917 (Aminotransferase, class-II) with a combined E-value of 8.9e-13. IPB001917A 182-194 IPB001917B 212-229***** IPB004838 (Aminotransferase, class-I) with a combined E-value of 2.2e-07. IPB004838C 152-164 IPB004838D 216-229","","","-51% similar to PDB:1FG3 CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH L-HISTIDINOL (E_value = 9.9E_20);-51% similar to PDB:1FG7 CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE WITH PYRIDOXAL-5'-PHOSPHATE (E_value = 9.9E_20);-51% similar to PDB:1GEW CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE (E_value = 9.9E_20);-51% similar to PDB:1GEX CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH HISTIDINOL-PHOSPHATE (E_value = 9.9E_20);-51% similar to PDB:1GEY CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH N-(5'-PHOSPHOPYRIDOXYL)-L-GLUTAMATE (E_value = 9.9E_20);","Residues 25 to 350 (E_value = 6.7e-59) place ANA_2360 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.","","aminotransferase (hisC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2361","2554350","2553442","909","11.25","18.56","33397","CTGGCCACCGGCAAGCCCCGGCAGGCCGAGCACCCCAAGCCGCCCACCCAGGAGCAGATCCGCCGCCAGCCCGGTCGCAAGGCCTGGGTGCCCAACCAGCACGGGGCCTGGTCGATGCTGGTGCTGCCGCCGATCGTCGGCTGGATCGTGGGCGGCTTCAGCTGGGTGAACCTCCTGTTCCTTCCCGCCTGGTGGGGCGGCTACCTCACCTACTGGTCCTGGTCGCAGTGGCTGCGCACCCGCTCGGCCCGCAAGCGCGCCCTCATCATGCTGCCGCTCCTGGTCTACACCGGCTGGACGGCCTCCCTGGCCCTCATCACTTTGCTGGTGGCGCCCTACCTCATCCAGTGGGCAGTGCCTCTGGCGCCACTGTTCGCCATCGCGTTGCACCAGGTGTGGCGCGGTCACGAGCGCTCACTGCTCTCGGGGCTGTCGACGACGATGGCCGCTTCCCTCATGGCGGCCGTCACCTACAGCCTGGCGGTGCGCGGCGACGGCGGCTTCCTGGGCCTGGGGACACCGAGCTCCCCCCTGCCCGGGGCCTCCCCCAGCGGCGCACTGACGGGCTGGTCCTGGATGTGGCTGGTCACGGCGCTGACGGCCGCCTACTTCGGCGGGACGGTCCCCTACATCAAGTCGATGATCCGCGAGCGCTTCAACTACACGCTGCTGGCCGGCACGGTGGTAGCGCACACGCTGGTGGCGGCGGCGACGTGGTGGCTGGCGTCGTCGGGCATGCTGCCGTGGGGGCACGCCGTCCTGTGGGTGGTGCTGACGGTGCGGTCGCTGGTCATGCCGCTGTGGCAGTGGCAGCTGGTGCGCACCCGCCACCGCCCGCTGCGCCCGGGGACGATGGGCATCGTCGAGGTCGTCATGTGCGTGGCCTTCCTGGTGACCATCTCCGTATGA","LATGKPRQAEHPKPPTQEQIRRQPGRKAWVPNQHGAWSMLVLPPIVGWIVGGFSWVNLLFLPAWWGGYLTYWSWSQWLRTRSARKRALIMLPLLVYTGWTASLALITLLVAPYLIQWAVPLAPLFAIALHQVWRGHERSLLSGLSTTMAASLMAAVTYSLAVRGDGGFLGLGTPSSPLPGASPSGALTGWSWMWLVTALTAAYFGGTVPYIKSMIRERFNYTLLAGTVVAHTLVAAATWWLASSGMLPWGHAVLWVVLTVRSLVMPLWQWQLVRTRHRPLRPGTMGIVEVVMCVAFLVTISV$","Hypothetical protein","Periplasm, Membrane","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[45-65]?$ $\"[86-104]?$ $\"[110-130]?$ $\"[140-162]?$ $\"[190-210]?$ $\"[222-242]?$ $\"[248-268]?$ $\"[283-301]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","Wed Aug 8 16:07:28 2007","","Wed Aug 8 16:07:28 2007","","","Wed Aug 8 16:07:28 2007","Wed Aug 8 16:07:28 2007","Wed Aug 8 16:07:28 2007","","","","","","Wed Aug 8 16:07:28 2007","","","","Wed Aug 8 16:07:28 2007","Wed Aug 8 16:07:28 2007","","","","","yes","","" "ANA_2362","2555447","2554878","570","5.06","-10.96","20346","ATGCTCGACGTCGATCTACCGACTGGTGAAAATATGGCCATGGGTACCTCCGACTCCCCCGTCCTCCACATCCGCACGGCCCGGACAGCCCGGGCAGAGCGGGCGCAGGACGCGGCCATGGCCGCCGCCCTGGAGGCCATCTGCTTCCCACCCGAGCAGGCTGCCAGCCCGACAACGATCGCCGAGCGGATGGCTACTTACGCCGACCACTTCTGGCTCATCGAGGACGAGGGCGGCATGCTGCTGACGCTGGTCAACGGACCGTGCACCCACGCGCGCGATCTGAGCGACGAGATGTACGAGGCGCCCACGATGCACGACCCCGACGGGGCCTGGCAGATGATCCTCGGCGTCGCCACGGCTCCCGCAGCTCAAGGGCAGGGGCTGGCCACCCGACTGCTGCACACTGTCATCGAGACAACGCGCGTCCACGGCCGCCAGGGCCTGGTGCTCACCTGCCTCGACGACCTCGTGGGCTTCTACGCGCGCCTGGGTTTCGTCGACGAGGGCCTGTCCGCCTCCCACCACGGCGGCGTGCCCTGGCACCAGATGCGGCTCACCCTGGCCTGA","MLDVDLPTGENMAMGTSDSPVLHIRTARTARAERAQDAAMAAALEAICFPPEQAASPTTIAERMATYADHFWLIEDEGGMLLTLVNGPCTHARDLSDEMYEAPTMHDPDGAWQMILGVATAPAAQGQGLATRLLHTVIETTRVHGRQGLVLTCLDDLVGFYARLGFVDEGLSASHHGGVPWHQMRLTLA$","GCN5-related N-acetyltransferase","Cytoplasm","acetyltransferase, GNAT family family","hypothetical protein","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[72-167]T$	Acetyltransf_1
PS51186	$\"[22-189]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[23-188]T$	no description
PTHR10908	$\"[99-188]T$	ARYLALKYLAMINE N-ACETYLTRANSFERASE

","BeTs to 7 clades of COG0454COG name: Histone acetyltransferase HPA2 and related acetyltransferasesFunctional Class: K [Information storage and processing--Transcription] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0454 is aompkzyqvdrlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 72 to 167 (E_value = 4.9e-09) place ANA_2362 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","GNAT family family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2363","2557341","2555659","1683","4.90","-29.36","58744","ATGCACGCACGCGCAGGACAGCCAGCACAGCCCGAAGACCTCATCGACGTCGACGAGGTCGTCTCCGCCTACTACGACCTCGTCCCCGACCCCGCCGTCCCGGCCCAGAAGGTCGTCTTCGGCACCTCCGGGCACCGCGGCTCCTCTCTGGACACCGCCTTCAACGAGGCCCACATCGTGGCCACGACCGCCGCCATCGTGGAGTACCGCCGCTCCCAGGGCACCGACGGCACCCTCTACCTGGGCCGTGACACGCACGCCCTGTCCGAGCCGGCCTGGCGCACCGCCGTCGAGGTGCTTGCCGGGGCCGGGGTGACCACCGCCGTCGACTCCCGGGGTGCCTACACGCCCACCCCGGCGGTCTCGCACTCCATCCTCCTGGCCAACGGCGCCGGGACCGAGGCGGGGGTGCGCACGAGCGGGCCCGGCCTGGCCGACGGCATCGTCGTGACCCCCTCCCACAACCCGCCGCGCGACGGCGGCTTCAAGTACAACCCGCCCACCGGCGGTCCGGCCGGCTCGGAGGCCACCACGTGGATCGCCAATCGCGCCAACGAGCTGCTCGCCTCCGGATGGCAGGACGTCCCGCGTATCCCGGTCCCCGAGGCGCTCGACGGCCCCCACATCATCAAGCACGACTACCTGGAGACCTACGTCAACGACCTGGAGAGCGTTATCGACCTCGAGGCGATCCGCAAGGCCGGCGTGCGCATCGGGGCCGACCCGCTGGGCGGCGCCTCGGTGGACTACTGGGGCGCGATCGGTGAGCGCTACGGCCTGGAGCTCACGGTGGTCAACCCCGAGGTGGACCCGGCCTGGCACTTCATGACCCTGGACTGGGACGGCAAGATCCGCATGGACTGCTCCTCCCCCAACGCCATGGCCTCGCTGCGCTCCACGATGACGCCCGACGCCGAGGGTAAGACCCCCTACGACGTCGCCACCGGGAACGACGCCGACTCCGACCGCCACGGCATCGTCACCCCCGACGGCGGGCTGATGAACCCCAACCACTTCCTGGCCGTGGCCATCGAGTACCTCTTCACCCACCGGCCCGGCTGGCCCGCCGACGCAGCCGTCGGCAAGACCCTGGTCTCCTCCAGCCTCATCGACCGGGTGGCGGCCGCGATCGGGCGCACCCTCATCGAGGTGCCGGTGGGCTTCAAGCACTTCGTGCCCGGGCTGCTCGACGGCTCGATCGGCTTCGGCGGCGAGGAGAGCGCGGGGGCCTCCTTCCTGCGCAAGGACGGCACCGTGTGGACCACGGACAAGGACGGCATCATCCTGGCCCTGCTGGCCAGTGAGATCATCGCCGTCACCGGCAAGTCCCCCTCCCAGTTGCACGAGGAGCAGGTGGAGCGCTTCGGCGCCAGCGCCTACGCACGCATCGACGCCGCCGCCTCCAAGGAGGAGAAGGCCAAGCTCGCCGCCCTGGCCGCCGAGGACGTGACCGCCACCGAGCTGGCCGGCGAGGAGATCACCGCCCGCCTGGTCGACGCGCCCGGCAACGGGGCCCCCATCGGCGGGCTCAAGGTCACCACCGAGGACGCCTGGTTCGCCGCGCGTCCCTCGGGCACGGAGGACGTCTACAAGATCTACGCCGAGTCCTTCAAGGGCGCCGACCACCTGGCGCAGGTGCAGGAGGAGGCCAAGAAGGTGGTCGCCGCGGCCCTGGGCGACTGA","MHARAGQPAQPEDLIDVDEVVSAYYDLVPDPAVPAQKVVFGTSGHRGSSLDTAFNEAHIVATTAAIVEYRRSQGTDGTLYLGRDTHALSEPAWRTAVEVLAGAGVTTAVDSRGAYTPTPAVSHSILLANGAGTEAGVRTSGPGLADGIVVTPSHNPPRDGGFKYNPPTGGPAGSEATTWIANRANELLASGWQDVPRIPVPEALDGPHIIKHDYLETYVNDLESVIDLEAIRKAGVRIGADPLGGASVDYWGAIGERYGLELTVVNPEVDPAWHFMTLDWDGKIRMDCSSPNAMASLRSTMTPDAEGKTPYDVATGNDADSDRHGIVTPDGGLMNPNHFLAVAIEYLFTHRPGWPADAAVGKTLVSSSLIDRVAAAIGRTLIEVPVGFKHFVPGLLDGSIGFGGEESAGASFLRKDGTVWTTDKDGIILALLASEIIAVTGKSPSQLHEEQVERFGASAYARIDAAASKEEKAKLAALAAEDVTATELAGEEITARLVDAPGNGAPIGGLKVTTEDAWFAARPSGTEDVYKIYAESFKGADHLAQVQEEAKKVVAAALGD$","Phosphoglucomutase, alpha-D-glucose phosphate-specific","Cytoplasm","phosphoglucomutase, alpha-D-glucosephosphate-specific","phosphoglucomutase ","phosphoglucomutase, alpha-D-glucose phosphate-specific","","Dai J.B., Liu Y., Ray Jr W.J., Konno M. The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution. J. Biol. Chem. 1992. 267(9):6322-6337. PMID: 1532581Zielinski N.A., Chakrabarty A.M., Berry A. Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase. J. Biol. Chem. 1991. 266(15):9754-9763. PMID: 1903398","","","

InterPro
IPR005841
Family

Phosphoglucomutase/phosphomannomutase
PS00710	$\"[147-156]?$	PGM_PMM

InterPro
IPR005843
Domain

Phosphoglucomutase/phosphomannomutase C-terminal
PF00408	$\"[470-557]T$	PGM_PMM_IV

InterPro
IPR005844
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I
PF02878	$\"[37-191]T$	PGM_PMM_I

InterPro
IPR005845
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II
PF02879	$\"[216-333]T$	PGM_PMM_II

InterPro
IPR005846
Domain

Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III
PF02880	$\"[335-455]T$	PGM_PMM_III

InterPro
IPR005852
Family

Phosphoglucomutase, alpha-D-glucose phosphate-specific
TIGR01132	$\"[1-559]T$	pgm: phosphoglucomutase, alpha-D-glucose ph

noIPR
unintegrated

unintegrated
G3DSA:3.40.120.10	$\"[20-228]T$ $\"[333-460]T$	no description
PTHR22573	$\"[96-556]T$	PHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF2	$\"[96-556]T$	PHOSPHOGLUCOMUTASE

","BeTs to 6 clades of COG0033COG name: PhosphoglucomutaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0033 is ------y--dr--ce-g----j----Number of proteins in this genome belonging to this COG is 1","***** IPB005841 (Phosphoglucomutase/phosphomannomutase) with a combined E-value of 1.8e-18. IPB005841C 111-126 IPB005841D 146-156 IPB005841E 159-181 IPB005841F 209-232 IPB005841I 312-323 IPB005841K 385-423 IPB005841M 516-528","","","-63% similar to PDB:2FUV Phosphoglucomutase from Salmonella typhimurium. (E_value = 2.2E_152);-38% similar to PDB:1TUO Crystal structure of putative phosphomannomutase from Thermus Thermophilus HB8 (E_value = 2.3E_24);-39% similar to PDB:1C47 BINDING DRIVEN STRUCTURAL CHANGES IN CRYSTALINE PHOSPHOGLUCOMUTASE ASSOCIATED WITH CHEMICAL REACTION (E_value = 8.4E_11);-39% similar to PDB:1C4G PHOSPHOGLUCOMUTASE VANADATE BASED TRANSITION STATE ANALOG COMPLEX (E_value = 8.4E_11);-39% similar to PDB:1JDY RABBIT MUSCLE PHOSPHOGLUCOMUTASE (E_value = 8.4E_11);","Residues 37 to 191 (E_value = 8.7e-34) place ANA_2363 in the PGM_PMM_I family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I.Residues 216 to 333 (E_value = 1.9e-17) place ANA_2363 in the PGM_PMM_II family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II.Residues 335 to 455 (E_value = 2e-28) place ANA_2363 in the PGM_PMM_III family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III.Residues 470 to 557 (E_value = 1.1e-15) place ANA_2363 in the PGM_PMM_IV family which is described as Phosphoglucomutase/phosphomannomutase, C-terminal domain.","","alpha-D-glucose phosphate-specific (pgm)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2365","2557620","2558126","507","6.11","-0.85","17146","ATGGGTAGTCTGGCCCGGGCGTCGGCGCCACTGCGCTGTCACCCGGGCCGCCGCTCCGCCCGCCGGGGACGCGGCCGAACCCCAGCGTCCAGCAGGAACGAGGAACCCATGACCGTCAGCCGTATCGCCACGACCAACGCCCCCGCCGCCGTCGGCCCCTACTCCCAGGGCGTCTCCACCGGTCAGGAGGCCGGCTCGCTCGTCTTCGTCTCCGGGCAGGTGCCGCTCGACCCGGCCACCGGTGCGCTCGTCGAGGGCGACATCCAGGCCCAGGCCGAGCAGGTCCTCAAGAACGTGGGTGCCATCCTGGCCGAGGCCGGGCTCGGGTACGACGACGTCGTCAAGACCACGGTCCTGCTCGCCGACATCGCCGACTTCGCCGCCGTCAACGAGGTCTACGCCCGCTACTTCACCGGTGAGACCCTCCCGGCCCGGGCCGCCTTCGGGGTGGCCGCCCTGCCGCTGGGGGCCGGCGTTGAGATCGAGGCCATCGCCGCCCGGTCCTGA","MGSLARASAPLRCHPGRRSARRGRGRTPASSRNEEPMTVSRIATTNAPAAVGPYSQGVSTGQEAGSLVFVSGQVPLDPATGALVEGDIQAQAEQVLKNVGAILAEAGLGYDDVVKTTVLLADIADFAAVNEVYARYFTGETLPARAAFGVAALPLGAGVEIEAIAARS$","Endoribonuclease L-PSP","Cytoplasm, Extracellular","Heat-responsive protein 12","K07567 TdcF protein","putative endoribonuclease L-PSP","","Sinha S., Rappu P., Lange S.C., Mantsala P., Zalkin H., Smith J.L. Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(23):13074-13079. PMID: 10557275","","","

InterPro
IPR006056
Family

YjgF-like protein
TIGR00004	$\"[39-167]T$	TIGR00004: endoribonuclease L-PSP, putative
PS01094	$\"[143-161]T$	UPF0076

InterPro
IPR006175
Domain

Endoribonuclease L-PSP
PF01042	$\"[44-167]T$	Ribonuc_L-PSP

InterPro
IPR013813
Domain

Endoribonuclease L-PSP/chorismate mutase-like
G3DSA:3.30.1330.40	$\"[38-168]T$	no description

noIPR
unintegrated

unintegrated
PTHR11803	$\"[42-168]T$	TRANSLATION INITIATION INHIBITOR

","BeTs to 18 clades of COG0251COG name: Putative translation initiation inhibitorFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0251 is -o--kzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB006175 (Endoribonuclease L-PSP) with a combined E-value of 5.3e-34. IPB006175A 51-78 IPB006175B 113-137 IPB006175C 143-165***** IPB006056 (YjgF-like protein) with a combined E-value of 1.6e-33. IPB006056A 51-78 IPB006056B 113-137 IPB006056C 143-165 IPB006056A 47-74","","","-71% similar to PDB:1QAH CRYSTAL STRUCTURE OF PERCHLORIC ACID SOLUBLE PROTEIN-A TRANSLATIONAL INHIBITOR (E_value = 6.7E_31);-71% similar to PDB:1NQ3 Crystal structure of the mammalian tumor associated antigen UK114 (E_value = 4.4E_30);-70% similar to PDB:2DYY Crystal structure of putative translation initiation inhibitor PH0854 from Pyrococcus horikoshii (E_value = 4.4E_30);-70% similar to PDB:1ONI Crystal structure of a human p14.5, a translational inhibitor reveals different mode of ligand binding near the invariant residues of the Yjgf/UK114 protein family (E_value = 7.4E_30);-67% similar to PDB:2CSL Crystal structure of TTHA0137 from Thermus Thermophilus HB8 (E_value = 2.4E_28);","Residues 44 to 167 (E_value = 2.4e-60) place ANA_2365 in the Ribonuc_L-PSP family which is described as Endoribonuclease L-PSP.","","protein 12","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2366","2558538","2559497","960","6.35","-3.19","34459","ATGACGGCGGGCCTGGCGGCGGCGCTCTCACCGGTGGCCGTAGCGGTGTGGGCGCCCTCGCTCGCCGCCCTCACGCTCCTGCCGGCCCTGCTGGGCGCCGGCGGCGTCGGCTACTACCTGTGGCGCGGTCTGTCCGCACGGCGCATGTTCGAGCAGGCGCTGCGGCACTACGCGCAGGTCACCGACGACTACGAGGTCACCGAGCTCCATGCCCGTCTCATCCCTGAAGGCGAGACCCGCGGCGCCCACGTCATGGCCCACTACCGCTGGTTCCGCGACGAGTACGAGAGCCTGACCCGCTCCTGGCAGGACCTGGGCAGCCCCCGGGGCGCCCAGTGGTTCGAACCGGGAGTGTTCCAGCGGGTCCGTGAGATCAAACGACGCTCGGCCGCGCTGGAGTCGACCGACGACATCATCGCCAGCAACGCCGCGTTCCTGAGCCTGTCCTCCAACTGGGAGAGGCTCTGGCGCCAGGAGCAGCAGCCGGTTCTTCATGAGCTCGACCTGCTCCTGGGCCAGTGCCAGTGGATCGACTCCTGCGCGTTCACTCCCCGGGGCACGGTGGAGGTGCGCGAGCTGGTGCGGGCCTACCACCAGCGCCTCAGCGAGATGACCGCGGAGCTGTCGGCCGGCTTGCTGCAGCCCTCGGCGGCGCTTGACGAGCTCGCCTGGATGGTGGCTGATGCTCGCCGGGCGGGGCATGGCCTGTCGCTCAGTGCGGCCGGTGCGGAGCCTGCCCTCAGCAGCTCTCTCGGTTCTCTCGACGGCGAAGCCTCCGCCCGCCCGGGTCCCCACGCCCTGCTGGACGTCGTCGGACCCGGAAGGAACGCCGGCTACTGGAAACCGGTCAGCCCTGGTGCCAATGGGAGAGCCGTCGTGCCTGTCGGCTACGCCGGGCCGCCACGGTTCCTGAATGCCGGTGCGGGATATCTCGGGGACGGGACCTTCCCGGGATGCTGA","MTAGLAAALSPVAVAVWAPSLAALTLLPALLGAGGVGYYLWRGLSARRMFEQALRHYAQVTDDYEVTELHARLIPEGETRGAHVMAHYRWFRDEYESLTRSWQDLGSPRGAQWFEPGVFQRVREIKRRSAALESTDDIIASNAAFLSLSSNWERLWRQEQQPVLHELDLLLGQCQWIDSCAFTPRGTVEVRELVRAYHQRLSEMTAELSAGLLQPSAALDELAWMVADARRAGHGLSLSAAGAEPALSSSLGSLDGEASARPGPHALLDVVGPGRNAGYWKPVSPGANGRAVVPVGYAGPPRFLNAGAGYLGDGTFPGC$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-33]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[41-75]?$ $\"[226-246]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[19-39]?$ $\"[196-218]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[15-37]?$ $\"[189-209]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[16-36]?$ $\"[206-224]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[27-45]?$	transmembrane_regions

InterPro
IPR003680
Family

Flavodoxin-like fold
PF02525	$\"[12-141]T$	Flavodoxin_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.360	$\"[13-201]T$	no description

","BeTs to 5 clades of COG2249COG name: Putative NADPH-quinone reductase (modulator of drug activity B)Functional Class: R [General function prediction only]The phylogenetic pattern of COG2249 is ------------b-efgh-nuj---wNumber of proteins in this genome belonging to this COG is 3","***** IPB003680 (NAD(P)H dehydrogenase (quinone)) with a combined E-value of 1.5e-10. IPB003680 83-128","","","-49% similar to PDB:1D4A CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION (E_value = 1.8E_13);-49% similar to PDB:1DXO CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,3,5,6,TETRAMETHYL-P-BENZOQUINONE (DUROQUINONE) AT 2.5 ANGSTROM RESOLUTION (E_value = 1.8E_13);-49% similar to PDB:1GG5 CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AND A CHEMOTHERAPEUTIC DRUG (E09) AT 2.5 A RESOLUTION (E_value = 1.8E_13);-49% similar to PDB:1H66 CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,5-DIAZIRIDINYL-3-HYDROXYL-6-METHYL-1,4-BENZOQUINONE (E_value = 1.8E_13);-49% similar to PDB:1H69 CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,3,5,6,TETRAMETHYL-P-BENZOQUINONE (DUROQUINONE) AT 2.5 ANGSTROM RESOLUTION (E_value = 1.8E_13);","Residues 12 to 202 (E_value = 2.6e-10) place ANA_2376 in the Flavodoxin_2 family which is described as Flavodoxin-like fold.","","dehydrogenase [quinone]","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2377","2571692","2571111","582","5.76","-4.69","20719","GTGAACTTGATTAACCTATCCAGTGTGAAGATAGACCGGCGCAGTACGGACACCCGTCAGCGGCTCATCGACACCACCCTGGACCTCATTGACTCCAACGGGTGGCATGCGGTGACACTGAGCGGGGTGGCCCGCGCCTGCGGAGTGACCACGCCCGCGTGCTACAAACACTTCCCGTCCAAGACGAGCCTTTTCGAGGCCGCGGCGCGCCGGCTGTCGGCCTCACTGGGCGAGCGCGCGGACGCCCTCATCCAGGACGATCCGCTCGAGTCACTCGTCGGCATCGGGACTCTTCTGGTCGACTTGGCCGCAGAGCACCCGCATCTCTTCGAGTTCAATCAGATCAGCCCCGCGGCCATCGCGGCACTCGACCGCCTCGACGACCACCCACTGCTGGCACTGACCCGCGGCGAGGTGGAGCGTCTGGCTGCACAGCAGGGAACCGATCCGACGGCGCTTCACCTCCTGGTGTGGTCCTGCCTGCAGGGCTACACCCAGCTCATCGCCGTCGGCGCCACCACCGCCGACACCACCTTCATCCGCGCAGCCCTGCGCGCCATCGTCACGATTGGAGACAACTGA","VNLINLSSVKIDRRSTDTRQRLIDTTLDLIDSNGWHAVTLSGVARACGVTTPACYKHFPSKTSLFEAAARRLSASLGERADALIQDDPLESLVGIGTLLVDLAAEHPHLFEFNQISPAAIAALDRLDDHPLLALTRGEVERLAAQQGTDPTALHLLVWSCLQGYTQLIAVGATTADTTFIRAALRAIVTIGDN$","Transcriptional regulator, TetR family","Cytoplasm","putative TetR-family transcriptional regulator","transcriptional regulator","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[22-35]T$ $\"[43-66]T$	HTHTETR
PF00440	$\"[22-68]T$	TetR_N
PS50977	$\"[16-76]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[15-79]T$	no description

","BeTs to 13 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 3.1e-11. IPB001647 22-64","","","No significant hits to the PDB database (E-value < E-10).","Residues 22 to 68 (E_value = 9.8e-13) place ANA_2377 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","TetR-family transcriptional regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2379","2572496","2574520","2025","6.37","-10.28","72175","ATGTCCGATCACTCCTCGAAGCACTCTCCAGTCGGACCCGCTGCATCCGCGACCGGCTCCCATGCGCAGGACGCCCGCGCCGACACGGCGGACGTCGCACCCGCCCCCGCCACCAGCCCGGTGAGCACCGGGCCGCCCGAGCGGCCGCCGGTCCACCCGCAGCATCCGAGCTCAGGGACCTGGCGGGCCGTCCGCACGGCCGGCGCCCCCTTGAGCGTGCGCGAGGTCGAGGCGGCATCCTCCGCGGCGCCCGCCGCTCACACCTCCGCCCAGGCCGCCACCCGCTCCTCGGTCCGCTCCCCCTCGGAGACCGCGGCCGCCGGCGTCGTCCTGCGCGACCTTGCCGACGAGTACGCCCAGCTCCTGTGTGCCCACGATCCCGAGGCGGCCGCCCGCACCGGACTGCCCGGCGGGACCATCCTGCCCGACTACTCGCCCGCGGGACTGGCCGAGCGTCTCAGTGCCGAGCGCTCCCTGCGTCACCGCGTGGCCGCCGTCGAGCACTCGACCGGCTCCGACGAGCTCCTGCGCCGCCACCTCCTGGAGCGCCTGGAGACCTCCATCCAGTTCATCTCCGCCGGGGAGGAGGGCGGAAACCTCGGTTTCCTCTCCTCGCCGTTCCAGCAGATCGCCCGCCAGCTGCACCGGCCCCCCGAGGCCCCCGACCGTGCCGGCTCCGAGGAGGCGGACCTCGCCGAGGCCGAGGCCAAGTGGGAGGACGCCTGGAACCTGCACCGCACCCGCCTGGAGGCGCTGCCCACCGCACTGGAGGGGCTGGCCGCCTCCCTGGCCGCCTCCGCCGAGGCCGGTGCGATTGCCCCGCTCAGTCAGGTCGACGTCGTCGCCGGGCAGGCGCGCGACCTCGCCCGACGCCGGACCCAGGGGCTGCCCGAGGACCTGCCGGCCACTCTGCACGTCCAGCTCCAGGAGGCGGACATCGTCGCCCGCCGCGCCGCGCTGGACTTCGCCTCGCACCTGCGCACGACGCTCTCGCCGCGGGCGCCCCAGGCCGAGGGGGTCGGCCCGCAGCGCCACGCCCTGTGGATGCGCCGCGTCCTGGGCACCCGGGTGGACCCCGAGGAGACCTACGCCTGGGCCACGGAGGAGCTGGGGCGGGTCATCGCCGAGCAGGACGCCATCGCCGTCGACATCCTGGGGTCCGGCGCCGATGCCGGCAGCCTCAACCGGCACCTGCGCGCCGACCCGACCCGCGCTGTGCGCGCGCAGGACTACACGATCTGGGCGCAGGAGGTCGCCGACGAGGCCTGGGACGCCGTCGTCGGCCGGATCCTCGACCCGCCCGACGGCCTGGGCCGCCCCCGGGTGCGCCTCGGGGAGCCCGGCGACGGCGCCGTCCACTACGAGGAGCCGCGCGGTACCGGCGGGGAGCGTCGGCCCGGCGTCGTCATGCGCTCCCTGGCTGCCGGCGAGCAGCTGGTGTGGCCGTGGATGGAGCGGACCACGGTCCTGCATGAGTCGGTTCCGGGCCACCACGTCCACGTCGGCGCGCATGCCACCAGTACGCGCCTGACCGCCTGGCAGCGCTACTTGGGCTCCGTGCCCGGCTGCGATGAGGGCTGGGGCCTGTATGCCGAGTCCCTCGCCGACGAGCTCGGGCTCATGCCTACGCCCGAGGACCGTTTCGGCTGCCTGGCGGCACGCCGCTGGCGCCTGGCCCGGGTCCTCGTGGACCTGGGCGTCCACTCCCGGCTCCCCGTGCCCGACGACGTCGCCGCGCTCCCGGGGGCCTGCCGCGAGTGGAACCGGGCGACCGTCACCGCCGTGCTGCGCCACCACACCGTGATCTCCGAGGGGCGCCTGCGCTTCGAGGTCTCCCGGCACCTGGGGTGGCCGTCCCAGCCGCTGGCCTACGCGGTGGGGGAGCGGGTCTGGCAGGCCGGTCGGCGCAGTGCCCGGGCTCAGGCCCGCACCGAGGGCGGTGAGCTGGATTTGCGCGCCTTCCACAACCGGGGCATCGACCTGGGCAGCGTGGGGCTCGATCTGCTCGCAAGCGCCTTGCACTGA","MSDHSSKHSPVGPAASATGSHAQDARADTADVAPAPATSPVSTGPPERPPVHPQHPSSGTWRAVRTAGAPLSVREVEAASSAAPAAHTSAQAATRSSVRSPSETAAAGVVLRDLADEYAQLLCAHDPEAAARTGLPGGTILPDYSPAGLAERLSAERSLRHRVAAVEHSTGSDELLRRHLLERLETSIQFISAGEEGGNLGFLSSPFQQIARQLHRPPEAPDRAGSEEADLAEAEAKWEDAWNLHRTRLEALPTALEGLAASLAASAEAGAIAPLSQVDVVAGQARDLARRRTQGLPEDLPATLHVQLQEADIVARRAALDFASHLRTTLSPRAPQAEGVGPQRHALWMRRVLGTRVDPEETYAWATEELGRVIAEQDAIAVDILGSGADAGSLNRHLRADPTRAVRAQDYTIWAQEVADEAWDAVVGRILDPPDGLGRPRVRLGEPGDGAVHYEEPRGTGGERRPGVVMRSLAAGEQLVWPWMERTTVLHESVPGHHVHVGAHATSTRLTAWQRYLGSVPGCDEGWGLYAESLADELGLMPTPEDRFGCLAARRWRLARVLVDLGVHSRLPVPDDVAALPGACREWNRATVTAVLRHHTVISEGRLRFEVSRHLGWPSQPLAYAVGERVWQAGRRSARAQARTEGGELDLRAFHNRGIDLGSVGLDLLASALH$","Uncharacterized conserved protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","protein of unknown function DUF885","","","","","

InterPro
IPR010281
Family

Protein of unknown function DUF885, bacterial
PF05960	$\"[126-674]T$	DUF885

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 126 to 674 (E_value = 3.1e-22) place ANA_2379 in the DUF885 family which is described as Bacterial protein of unknown function (DUF885).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2380","2578287","2575882","2406","9.88","11.83","80008","ATGATCCTGGCGGTGGTGGGGCCGGCCCTCGCCACCGCGGCCCCGACGGCGCCGGAATCCGAGGCAGCGCCGGCGTCCCAGCAGGCCTCCCAGCCGGCCTCCGATGTCGCCTCGGCCTCGCACTCATCTTCGCGGCCGGCGCCGGTGGTCGTCCTGGCGACGAACAATCTCACCTGGGCGGACCTGCAAGAACAGGCCTCCCGCGAAGGCGCCGGTGCGAGCTCCGACTCTTCCGGCATCGGCTCGGCGGCCGACCGCCTGCTGGCCTTCGCCCAGCGAGGCGAGCCGATGAACCTGTCCGTGCGCACCCCGGCGGACCACACCTGCCCGGCCGATGCCTGGCTCACCCTGGGCCGGGGCAAGCGCGCGAGCGCCGTCGAGGCGGCCGCTTCCTGCGCCGGCCCCACTGCCGCGATCCCCCGCAGCACCCCACTGGTCGGGGCGCTCGGGCAGGACGTCTCGGTCAAGACCGTCGGCCCCAGTACGCAGCTGGCCACAGGCGCACCAGGGGGCTCAGCGAACAGGCCCGCCCCCGTGGCGCCGTCGGTGGCCGATGCCCTGGTCGCCGACGCGGACCTCACCATCGTCGACACCGCGAGCGCCGCCTCCACCGACGCCGAGCGGATCGCCGCCCTCGACGAGGCCCTGCGCATGGTCCAGGAGCAGTCGCGCCCTGGCACTCGCATCATCGTTGCCTCCCTGGCCGACGACGAGGCCCCCGGCCCCCAGATGGCGGTCCTGCCCGCGGGCACGAGGAGCTCACGCGGCACCTCCGGGGGTCTTGTCGTCGGCGACTCCACGCACCAGGCGGGCCTGGTCCAGCTGACTGACCTCACCCCGACTCTCGTCTCCGCCCTGGCCGGCCGCCGCGACCCAGCCTTCGACGGCCACGCGCTCACGCTGCCCGAGACCGGCCGCGCGGGCGTGGCAACGACCAACACAAGCGCCGCCACCGGGGACGCCCGCATCTCGCGGCTCGCCGACGACGCCCTGCACGCCCGTGCCTCTCAGGCCACGGTCATGCGGGCCGGCGCCCTGCTCATGGGCCTGGCCGTGGCGCTCCTGGTCTGGGCGGCCGTCGCGCTGCGTAGCCCGAAGGCGAGTCGGCGCGAGGCTCTCCGCCGCCGGGTCACGTGGGTGGCCGTCTGCCTCAGCGGCCTGCCGACGGCGTTGCTGCTGGTCAATGCTGCCCCGTGGTGGCGGGTGGGGGCCCGGGCCGGCTCGCCTTCGGGGTTGACCTCACTCGTCGCCGTGGTCGCGGCCGTGCCGGTCGCAGCCGGGATCGTGGGACTGGCCGCCGGGATCGCGGCGCTGGTACGACGGCGCAAGCGGCCCCACCCTGCCGTCTCACCGAGTCCGTCGCCCTCAGCGCTTGGTGCCGCAGCCGCTGAAACGGTCGGATCCCCCAAAACCACCTCCGCCCGAGGGGAGGCCGCGGTCGAGCCGCCACCGGACGAGGCCGACGGCCCCGAGCCCGCCTTACCGTCTCCACCCCGTAACGGGACGAGCCTGACGGCCCTGCTGGTGGCGGCGGCGATCCCGCTGGCCTGGCTGGTCGACGCCGCCGCGGGCGCACCTCTGGCCTTCAACAACCCTCTGGGCATGAACGCGGTGGTGGCGGGCCGTTTCTACGGGGTGTCGAATACGGCTTTCGCGCTGGTGGCCGGCGCGCTCGTCGTCGTCATCGCCGGCGTCTGGGAGGTTCTGGGCGGCGGCCGGCGGAGCGCGCTGCTGGTGACAGCCCTGCTGGGCGGGGCGGCGCTGCTCGTCGATGGGGCCCCGCAGCTGGGCGCGGACGTGGGTGGTGCGCTGACACTGGTGCCGACGCTGGCCTTCCTCACTGCGGGCCTGGCGAATCTGCGCCTGAGCTGGCGGCGCTGGTTGGCCATCGGGGCCGCGACGGTCCTGGTGGTGGGCGGCTTCGCCGTCGTCGACCTCCTCCGACCCGGTGAGCCCACGCACCTGGGGCGCTTCGCCCGTCAGGTGGCCGACGGCTCGGCCGCCGGCGTGCTGGGACGCAAGGCCTACGCGCTGGTCGGCCCCTTCGTCACGAAGCCGATCATGGCGGCAGCCCTGGCCTGCGCCGTGGTCGTCGTGGCAGCGACCCTGTGGTGGGGACGCCGGCAGGTGCGGGCCTGGCGCAATGGCACGAGCCCCTACGCCTGGCTCGCCCCCACCGCCCACGGGGACAATCCACGCGTGGGGGGACAGGAATCCGGTTCCCCAACGCGTGGAATGTCCCCCTCCGCGCGATGGGTGACAACGGCGCTGAAGTCCCTGGGGGTACTGACGCTCGTGGCCGTCCTGGTCAACGACTCCGGTGTCACGATGGCCGGCTTCATCCTGGCGGCAGCGGCTCCCGCCCTGCTGGCGCTGACGCTGGCCGGGAGTGAGTCGGCGCGCTAG","MILAVVGPALATAAPTAPESEAAPASQQASQPASDVASASHSSSRPAPVVVLATNNLTWADLQEQASREGAGASSDSSGIGSAADRLLAFAQRGEPMNLSVRTPADHTCPADAWLTLGRGKRASAVEAAASCAGPTAAIPRSTPLVGALGQDVSVKTVGPSTQLATGAPGGSANRPAPVAPSVADALVADADLTIVDTASAASTDAERIAALDEALRMVQEQSRPGTRIIVASLADDEAPGPQMAVLPAGTRSSRGTSGGLVVGDSTHQAGLVQLTDLTPTLVSALAGRRDPAFDGHALTLPETGRAGVATTNTSAATGDARISRLADDALHARASQATVMRAGALLMGLAVALLVWAAVALRSPKASRREALRRRVTWVAVCLSGLPTALLLVNAAPWWRVGARAGSPSGLTSLVAVVAAVPVAAGIVGLAAGIAALVRRRKRPHPAVSPSPSPSALGAAAAETVGSPKTTSARGEAAVEPPPDEADGPEPALPSPPRNGTSLTALLVAAAIPLAWLVDAAAGAPLAFNNPLGMNAVVAGRFYGVSNTAFALVAGALVVVIAGVWEVLGGGRRSALLVTALLGGAALLVDGAPQLGADVGGALTLVPTLAFLTAGLANLRLSWRRWLAIGAATVLVVGGFAVVDLLRPGEPTHLGRFARQVADGSAAGVLGRKAYALVGPFVTKPIMAAALACAVVVVAATLWWGRRQVRAWRNGTSPYAWLAPTAHGDNPRVGGQESGSPTRGMSPSARWVTTALKSLGVLTLVAVLVNDSGVTMAGFILAAAAPALLALTLAGSESAR$","Hypothetical protein","Membrane, Cytoplasm, Extracellular","membrane protein, putative","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR013222
Domain

Glycosyl hydrolase family 98, putative carbohydrate-binding module
SM00776	$\"[269-364]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-13]?$	signal-peptide
tmhmm	$\"[344-362]?$ $\"[377-397]?$ $\"[416-438]?$ $\"[507-527]?$ $\"[546-566]?$ $\"[576-594]?$ $\"[600-618]?$ $\"[627-647]?$ $\"[686-706]?$ $\"[752-770]?$ $\"[776-796]?$	transmembrane_regions

InterPro
IPR001173
Domain

Glycosyl transferase, family 2
PF00535	$\"[12-175]T$	Glycos_transf_2

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[10-101]T$	no description
PTHR10859	$\"[19-218]T$	GLYCOSYLTRANSFERASE RELATED

","BeTs to 19 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 9","***** IPB001173 (Glycosyl transferase, family 2) with a combined E-value of 6.5e-06. IPB001173A 39-51","","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 175 (E_value = 3.9e-13) place ANA_2381 in the Glycos_transf_2 family which is described as Glycosyl transferase family 2.","","involved in cell wall biogenesis","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2382","2579240","2578389","852","5.60","-7.91","29831","ATGGCCGACGGCGGGGCACACGTGGTGCCGGTGACCAGTGGCCCGGGCTGGCTGGAGGAGCCACGGCTGACGACGACCGGCGTGACGCTGGCCGGGGCGGAGGCCTTCGGTCGGGCACTGGCCGTTACCCACGCCGCGGGCGCCCCGGCCTTCGGGGCGGCGCCTCCCGGGTGGGACGGCCGGGCGCAGATGGGCCGCTCGGACATCCGGCTGCGGCCGCACGCCGTCGAGGAGGGCGAGCCGCGCCGCTGGGGCGAGTTCTACGCCGAGGACCGGATCCTGCCCTACCTGCAGCCCAGTCGGGACAACGGCTCGATCAGCGCCGGCGGGGCCGGAGTCGTCGAGCGGCTGTGCGAACGCCTGCGCGACGGCGACTTCGACACCGACCAGCCGGCCCTCGTGCGCGCCGGCGCCCGCGAGCGCGGCGCGCGGGTCGCGGTGGCCCGCACGCACGGGGACCTGTGGTGCGGCAATGTCCTGTGGACCCCAGCCGATGAGGCCGCCCAGTGGGCGCCGCCGCGGGCCGGGCTCGGGCCGCAGGAGCCTGACCCCGGGCAGACACCCGTGAGCGGGGCGGCTGACGGGCCAGCCGGCGGGCCGACGGTGGTCGGCGTGCTCATTGACCCGATGGCGCAGGGCGCGCACGCAGAGACCGACCTGGCGGCCCTGGGCGTGTTCGGGCAGCGCTACCTGGATCGCATCTACGCGGCCTACCACGAGGTCTCGCCGCTGGTAGAGGGCTGGCGCGAGCGGGTGGGCCTGCACTCCTGGCACATCCTCATGATTCACGCCTTCCTCTTCGGCGGGGGCTATGGCGGGGAGGCGGTCGCCGTGGCCCGCCAGTACCTGTGA","MADGGAHVVPVTSGPGWLEEPRLTTTGVTLAGAEAFGRALAVTHAAGAPAFGAAPPGWDGRAQMGRSDIRLRPHAVEEGEPRRWGEFYAEDRILPYLQPSRDNGSISAGGAGVVERLCERLRDGDFDTDQPALVRAGARERGARVAVARTHGDLWCGNVLWTPADEAAQWAPPRAGLGPQEPDPGQTPVSGAADGPAGGPTVVGVLIDPMAQGAHAETDLAALGVFGQRYLDRIYAAYHEVSPLVEGWRERVGLHSWHILMIHAFLFGGGYGGEAVAVARQYL$","Fructosamine kinase","Cytoplasm","Uncharacterized BCR","hypothetical protein","Uncharacterized protein-like","","","","","No hits reported.","No hits to the COGs database.","***** IPB005581 (Fructosamine kinase) with a combined E-value of 9.3e-09. IPB005581A 187-238 IPB005581B 248-269***** IPB002575 (Aminoglycoside phosphotransferase) with a combined E-value of 6.5e-07. IPB002575B 151-160 IPB002575C 201-221","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","BCR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2384","2579513","2580457","945","5.99","-5.21","33471","ATGACTGCTCCCGCACCGCTCTGGTCCTTCCTGGGGCCGGCCGGCACCTTCACCGAGATGGCGCTGCGCCAGGTCGCCCCCGTCGATGTCGAGCTCGATCCCTGCCCGGACGTGCCCACCGCCCTGGACCACCTGCGCGAGCGCACGGTGGAGGCCGCCGTCGTGCCCATTGAGAACTCCGTCGAGGGCGGGGTCAACGCCACGCTGGACAACCTCGTGGCCTCCACGCCCCTGGTCATCGCTGCCGAGATGGCCGTGCCGATCACCTTCGTCCTGGCCGGCCGCCCCGGCACCCGCCTGGAGGACGTGCGCGCCATCTCCACCCACCCGCACGCCTGGGCCCAGTGCCGCGGCTGGGTCCACCAGAACCTCCCCGAGGCCGTGTACGTCGCCGGGACCTCCACCTCGGCGCCCGCCCGCGCGCTGGCCACCACCGAGGGGGACACCGGATTCCAGGCCGTCCTGTGCAACCCGCTGGCCGCCAAGCAGTACGGGTTGGAGGTCATCGCCGGGGGCGTGGCGGACAACCCCGACGCCGTCACCCGCTTCGTCAAGGTGACCCGGCCCGGCCGCGTGGGCGAGCCCACCGGCGCCGACAAGACCACCCTGCTCGTCCACCTCCCGCACGACCGCTCCGGCGCCCTGCTGGACATGCTCGAGCAGTTCAGCGCCCGCGGCGTCAACCTCTCGCGCATCGAGTCCCGGCCCGTGGGCGACTCCCTGGGGCGCTACCGCTTCTCCATCGACGTCGAGGGGCACGTGCGCGAGGAGCGGGTCCAGGCCGCCCTCATCGGGCTGCACCGCACCTGCCCGGTGGTGCGGTTCCTGGGCTCCTACCCGCGGCTGGACGCCCGCCCGACGGCGGTCCTGGCCGGCACCAGCGACAAGGACTTCGTCGTGGCCCGGTCCTGGGTCGCCGACGTCCTCGACGGCCGCGCGCTCTAG","MTAPAPLWSFLGPAGTFTEMALRQVAPVDVELDPCPDVPTALDHLRERTVEAAVVPIENSVEGGVNATLDNLVASTPLVIAAEMAVPITFVLAGRPGTRLEDVRAISTHPHAWAQCRGWVHQNLPEAVYVAGTSTSAPARALATTEGDTGFQAVLCNPLAAKQYGLEVIAGGVADNPDAVTRFVKVTRPGRVGEPTGADKTTLLVHLPHDRSGALLDMLEQFSARGVNLSRIESRPVGDSLGRYRFSIDVEGHVREERVQAALIGLHRTCPVVRFLGSYPRLDARPTAVLAGTSDKDFVVARSWVADVLDGRAL$","Prephenate dehydratase","Cytoplasm","prephenate dehydratase","prephenate dehydratase ","Prephenate dehydratase","","Schnappauf G., Krappmann S., Braus G.H. Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase. J. Biol. Chem. 1998. 273(27):17012-17017. PMID: 9642265","","","

InterPro
IPR001086
Domain

Prephenate dehydratase
PF00800	$\"[10-191]T$	PDT
PS51171	$\"[7-188]T$	PREPHENATE_DEHYDR_3
PS00857	$\"[164-186]?$	PREPHENATE_DEHYDR_1
PS00858	$\"[229-236]?$	PREPHENATE_DEHYDR_2

InterPro
IPR002912
Domain

Amino acid-binding ACT
PF01842	$\"[201-268]T$	ACT

InterPro
IPR008237
Family

Prephenate dehydratase with ACT region
PIRSF001424	$\"[6-287]T$	Prephenate dehydratase

noIPR
unintegrated

unintegrated
PTHR21022	$\"[10-289]T$	PREPHENATE DEHYDRATASE (P PROTEIN)
signalp	$\"[1-16]?$	signal-peptide

","BeTs to 19 clades of COG0077COG name: Prephenate dehydrataseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0077 is aomp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001086 (Prephenate dehydratase) with a combined E-value of 1.8e-57. IPB001086A 8-20 IPB001086B 51-72 IPB001086D 103-120 IPB001086E 153-186 IPB001086F 210-253","","","-47% similar to PDB:2IQ8 The crystal structure of putative prephenate dehydratase from Staphylococcus aureus subsp. aureus Mu50 (E_value = 9.8E_21);-49% similar to PDB:1G5G FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS (E_value = 9.8E_21);-52% similar to PDB:1NNW hypothetical protein from Pyrococcus furiosus Pfu-1218608 (E_value = 9.8E_21);-53% similar to PDB:1PHZ STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE (E_value = 9.8E_21);-53% similar to PDB:2PHM STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED (E_value = 9.8E_21);","Residues 10 to 191 (E_value = 3.3e-58) place ANA_2384 in the PDT family which is described as Prephenate dehydratase.Residues 201 to 268 (E_value = 6.9e-06) place ANA_2384 in the ACT family which is described as ACT domain.","","dehydratase (PDT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2385","2580643","2581941","1299","10.62","22.04","47864","ATGGGTAACTCGATTTCGCCGTCTCGGCGTGAGCAGGTCATAGGTTTTGACTCCAGGACCAGTGGGATGAGCGTGGAGGAGTTCTGCGCTCAGGTGGGTATCTCGCGGGCCTCGTTCTACCGGATACGCCGACGCGCTGAGCACGAGGGCCTGGCTGCCGCGCTGACACCGCGTTCACGGGCCCCGCGCCACCCGGCGCGGGTGTGGGACCAGGGCACTGATGAGCGCATCGCCCAGGTTCGCGCCGACCTGCTCGCCGCCGGCCGGGAGGCGGGTCCGGCCTCGGTGTGGTGGGTGATGAGCCAGGGCGCCAGCGTTCCGGCTCCCTCGCGCGCGACGATCGCCCGCAGCCTACGCAGAGCCGGCCTGGTGGTCCCCGCCCCGCGCAAGCGGCCCAGGACGTCGTACAAGCGCTTCACCCGCAGCGCGGCCAACGAGCTGTGGCAGATCGACGGCTTCCAATGGCGCCTGGAGGACCATCTGGTGACCGTCTACCAGGTCGTTGACGACTGCTCGCGGGTCATCACCGCCCTGAGGGCCTGCTGGGGCGGTGAGAGCGTGGCAGGCACCCGCATGGTCCTTGAGGAGGCCTTCGCCACCTGGGGGCGTCCGGCGGCGATCCTGTCGGACAACGCACTGGCGTTCAACACCAGCCGTATCACTGGCCCGGGAGCCACCGAGAAGTGGCTGGCATCCCTGGGGGTGCGTCCCATCAGCGGGCGGGTGGGCCACCCTCAGACCCAGGGCAAGGTCGAGCGCTCCCACCAGCCGGCAGCCGCCTGGCTGCGCGCCCACCCGGCCAGCACCCTTGAGGAGCTCAACGCCGAGCTGGACCGCTTCACCAGCTACTACAACACCGAGCGCCAGCACCAGGGCCACGGCGTCGCACTGACCCCGCTGAGGGTATGGGCTCAGACCCCCAGGGCGCTGGCCAGCCCAGCCCCCATCGACCTGGAGCGCCTACCAGCCGGCGGCGGCCCCATCAGCCTGCCCGACCCCGCCGATCCCGACCAGGCCGTGGACCGCGCCCGACGCACCGTGATGTCCAACGGGTGCGTGTCCTACAAGGACCGTGCACTGTCACTGGGCCAGACCATGCGCGGCGTCGAGGTCACCCTGATCGAGTACACCACGCGCCTGGACCTCTACGACCCCGACGGACGCCGCTTCGTGTCCCTGCCCTGGCCCCAACCCACCCAGAGGCAGCAAGGCAACCGCTCCACCATCGACACCAAGAAACCGCCCTACAGACTCATCCCGCTCCCACCCCGACGCCCCCGAACGTCTCACAGGTCATAA","MGNSISPSRREQVIGFDSRTSGMSVEEFCAQVGISRASFYRIRRRAEHEGLAAALTPRSRAPRHPARVWDQGTDERIAQVRADLLAAGREAGPASVWWVMSQGASVPAPSRATIARSLRRAGLVVPAPRKRPRTSYKRFTRSAANELWQIDGFQWRLEDHLVTVYQVVDDCSRVITALRACWGGESVAGTRMVLEEAFATWGRPAAILSDNALAFNTSRITGPGATEKWLASLGVRPISGRVGHPQTQGKVERSHQPAAAWLRAHPASTLEELNAELDRFTSYYNTERQHQGHGVALTPLRVWAQTPRALASPAPIDLERLPAGGGPISLPDPADPDQAVDRARRTVMSNGCVSYKDRALSLGQTMRGVEVTLIEYTTRLDLYDPDGRRFVSLPWPQPTQRQQGNRSTIDTKKPPYRLIPLPPRRPRTSHRS$","Transposase","Extracellular, Membrane","Predicted transposase","integrase; catalytic region","Integrase, catalytic region","","Asante-Appiah E., Skalka A.M. HIV-1 integrase: structural organization, conformational changes, and catalysis. Adv. Virus Res. 1999. 52:351-369. PMID: 10384242Thomas M., Brady L. HIV integrase: a target for AIDS therapeutics. Trends Biotechnol. 1997. 15(5):167-172. PMID: 9161051Katzman M., Katz R.A. Substrate recognition by retroviral integrases. Adv. Virus Res. 1999. 52:371-395. PMID: 10384243","","","

InterPro
IPR001584
Domain

Integrase, catalytic core
PF00665	$\"[140-304]T$	rve
PS50994	$\"[128-307]T$	INTEGRASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[143-310]T$	no description

InterPro
IPR000106
Family

Low molecular weight phosphotyrosine protein phosphatase
PTHR11717	$\"[57-166]T$ $\"[183-234]T$	LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE
PF01451	$\"[51-233]T$	LMWPc
SM00226	$\"[51-233]T$	LMWPc

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.270	$\"[44-235]T$	no description
PTHR11717:SF7	$\"[57-166]T$ $\"[183-234]T$	LOW MOLECULAR WEIGHT PROTEIN-TYROSINE-PHOSPHATASE

","BeTs to 11 clades of COG0394COG name: Protein-tyrosine-phosphataseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0394 is aom---yq-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000106 (LMW phosphotyrosine protein phosphatase signature) with a combined E-value of 1.5e-24. IPB000106A 53-70 IPB000106B 100-116 IPB000106C 147-162 IPB000106E 205-220","","","-43% similar to PDB:1U2P Crystal structure of Mycobacterium tuberculosis Low Molecular Protein Tyrosine Phosphatase (MPtpA) at 1.9A resolution (E_value = 2.6E_12);-43% similar to PDB:1U2Q Crystal structure of Mycobacterium tuberculosis Low Molecular Weight Protein Tyrosine Phosphatase (MPtpA) at 2.5A resolution with glycerol in the active site (E_value = 2.6E_12);","Residues 51 to 233 (E_value = 1.7e-18) place ANA_2386 in the LMWPc family which is described as Low molecular weight phosphotyrosine protein phosphatase.","","molecular weight protein-tyrosine-phosphatase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2387","2584003","2583059","945","6.77","-2.01","34638","GTGGCCCGCCGTATCCCGGTGACCGAGTCACCCACGAAGGCGCCCGGCGCCGACCACGCCGTGCTCGTCTTCCAGCGTGAGGCGGCGGGCCGGGCCAGTCGGCCCCGGCACTCGCGCGCGGTCCTCTACCTGCACGGCCGCAGCGACTACTTCTTCCAGACCCACCTGGCCCAGGCCTACCTCGACGCCGGCTTCGAGTTCTACGCGCTGGACTTGCGGGCCTGCGGGCGGGCCGGCGTCGGGCACGCCTCCCCGCACGACGTGCGCGACCTGCGCGTCCATGACGAGGAGATCGCCGAGGCCCTGCGCATCATCCGCTCCGAGCACGGGCACGACGTCGTTGTCCTCAACGGGCACTCGACCGGCGGGCTGCAGGCGGTCATCTGGGCGGCCGATCACCCCGGGACCGTGGATGCGCTCGTCCTCAACTCCCCGTGGCTGGATCTGCGCGGGTCGGCGCTGGTGCGCTCCTACGGCTCGGCCTTCGTGGACCTCCTCTCGCGGCGGGACCCCGAGCGCGTCATCGGTGAGCCGGGCAGCGGCGATGAGGACAACTACGTGGCGGCCCTGCACCGGCGCTGGCACGGCGAGTGGGACTGGGACCTGGCGCTCAAGCCGGCGCCGTCCTTCCCGGTGCGGGCCGGGTTCCTGGCGGGGATCCGGCGTCTGCAGCGCGAGGTCCACCACGGGCTGGGGATCCGGGTGCCGATCCTCGTGTGCTGCTCAACGGCCAGTGGCGGCGTCAAGGCGAGCCTGGAGGAGGCGCAGCGCTCCGACGTCGTCCTCGACGTGGAGCAGATCATCGACCGCTCCCAGTATCTGGGCGACGACGTGACCGTCCGCCAGATCCCCGAGGGCGTCCACGACCTGGCCCTGTCCGGGCCGCTGGCGCGCGCCGAGTACCTTCAGGCCGTCATGCGCTGGCTGGACAACCGCCTGCACTGA","VARRIPVTESPTKAPGADHAVLVFQREAAGRASRPRHSRAVLYLHGRSDYFFQTHLAQAYLDAGFEFYALDLRACGRAGVGHASPHDVRDLRVHDEEIAEALRIIRSEHGHDVVVLNGHSTGGLQAVIWAADHPGTVDALVLNSPWLDLRGSALVRSYGSAFVDLLSRRDPERVIGEPGSGDEDNYVAALHRRWHGEWDWDLALKPAPSFPVRAGFLAGIRRLQREVHHGLGIRVPILVCCSTASGGVKASLEEAQRSDVVLDVEQIIDRSQYLGDDVTVRQIPEGVHDLALSGPLARAEYLQAVMRWLDNRLH$","Hydrolase, alpha/beta fold family","Cytoplasm","conserved hypothetical protein","hypothetical protein","alpha/beta hydrolase fold","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[65-167]T$	Abhydrolase_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[39-309]T$	no description
PTHR10992	$\"[41-148]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF12	$\"[41-148]T$	PROLINE IMINOPEPTIDASE

","BeTs to 5 clades of COG2267COG name: LysophospholipaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG2267 is a---k-y-vdrlb-efgh---j----Number of proteins in this genome belonging to this COG is 3","***** IPB000639 (Epoxide hydrolase signature) with a combined E-value of 3.3e-07. IPB000639B 64-79 IPB000639C 116-129 IPB000639D 130-143","","","No significant hits to the PDB database (E-value < E-10).","Residues 65 to 304 (E_value = 0.00049) place ANA_2387 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2388","2584361","2585428","1068","6.02","-5.17","37210","GTGACAATCAGTGAACAGTCGACCGCCGAGCCCGGCCGGTCCGAAGACGGTGACGTGCCCGGCTCTCCAGGCGAGCCCATGATCTCCTTGCGCGACGTCCACAAGGTCTACCGCCTGCGCAGCGGCAAGGAGGTGCGCGCCCTGGACGGGCTCAGCCTCGACGTCGCCGCCGGCTCCATCCACGGCATCGTCGGCACCTCCGGGGCCGGCAAGTCCACGCTCGTGCGCTGCCTGACCTCCCTGGAGCGCCCCACCAGTGGCCACGTGAGCGTCGCCGGCCAGGACATGACCGCCCTGTCGCCCAGTCAGCTGCGCGAGGCCCGACGCCGCATCGGCATGGTCTTCCAGCACGCCAACCTCCTGGACCAGCGCACCACGGCGCAGAACATCGCCTACCCGCTGGCGCTCGCGGGTGTCCCCGGCGGGAGGCGCCACCCGGTCGTCAAGCGCATGCTCGACCTCGTGGGGCTGGCCGACCGCGGCGGCTCCTATCCTTCCCAGCTCTCCGGCGGCCAGAAGCAGCGCGTCGGCATCGCCCGGGCGTTGGCCGATGACCCGGCCGTCCTCCTGTGCGACGAGCCCACCTCGGCCCTGGACCCGGAGACCACCCGCTCCATCCTCGACCTCATCAAGAACGTCCGCGACACCCTGGGCTTGACCGTCATCATCATCACCCACGAGATGAGCGTGGTCCGCCAGGTCTGCGACTCCGTCAGCCTGCTTGAGGCCGGACAGATCGTCGAGAGCGGCCGCCTGGAGGACATCGTGCTCGACGTCGACTCCCGGCTCTCGCGCGAGATCGTGCCCTTCCCGAAGGTGCCCGAGGCCGCCGTCGCCCACGGGGAGAGCGTCATCGACGTCTCCATCACCGCCCACCCGGGCCAGCCGGCTGCCGTCGCCCTCATGTCGATGGTGGCCGAGCTCGGCGGGGACATCGCCGCCGGCGTCTTCGAGACGATCGGGCAGGCCCAGATCGGGCGCCTGGCCGTCACCGTCCCCGCGTCCGACACCGAACAGGCCGTGAGCACCCTGCGCAAGGCCGGTATTGCTGCGGAGGTCCGCTCATGA","VTISEQSTAEPGRSEDGDVPGSPGEPMISLRDVHKVYRLRSGKEVRALDGLSLDVAAGSIHGIVGTSGAGKSTLVRCLTSLERPTSGHVSVAGQDMTALSPSQLREARRRIGMVFQHANLLDQRTTAQNIAYPLALAGVPGGRRHPVVKRMLDLVGLADRGGSYPSQLSGGQKQRVGIARALADDPAVLLCDEPTSALDPETTRSILDLIKNVRDTLGLTVIIITHEMSVVRQVCDSVSLLEAGQIVESGRLEDIVLDVDSRLSREIVPFPKVPEAAVAHGESVIDVSITAHPGQPAAVALMSMVAELGGDIAAGVFETIGQAQIGRLAVTVPASDTEQAVSTLRKAGIAAEVRS$","ABC-type D-methionine transport system, ATP-binding component","Cytoplasm, Membrane","ABC transporter (ATP-binding protein) BH3481","K02071 D-methionine transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[167-210]T$	Q87UV4_PSESM_Q87UV4;
PF00005	$\"[58-244]T$	ABC_tran
PS50893	$\"[28-268]T$	ABC_TRANSPORTER_2
PS00211	$\"[168-182]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[57-253]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[25-271]T$	no description
PTHR19222	$\"[28-268]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF34	$\"[28-268]T$	METHIONINE ABC TRANSPORTER

","BeTs to 12 clades of COG1135COG name: Uncharacterized ABC-type transport system ATPase componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1135 is ---------d-lbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 1.3e-40. IPB013563A 47-81 IPB013563C 165-192 IPB013563D 220-272***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 5.4e-34. IPB005074C 47-94 IPB005074D 156-199 IPB005074E 220-240***** IPB005116 (TOBE domain) with a combined E-value of 3.5e-24. IPB005116A 65-81 IPB005116B 109-126 IPB005116C 168-181 IPB005116D 188-207***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.7e-16. IPB010509B 58-83 IPB010509D 163-207***** IPB010929 (CDR ABC transporter) with a combined E-value of 1.1e-08. IPB010929K 45-89 IPB010929M 165-211 IPB010929C 150-183","","","-57% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 7.2E_39);-51% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 7.5E_36);-59% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 9.1E_34);-59% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 2.0E_33);-51% similar to PDB:1OXS Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus (E_value = 1.1E_31);","Residues 58 to 244 (E_value = 5.4e-63) place ANA_2388 in the ABC_tran family which is described as ABC transporter.","","transporter (ATP-binding protein) BH3481 (atp_bind)","","1","","","","","","","","","","","Tue Aug 14 17:14:17 2007","","Tue Aug 14 17:14:17 2007","","","Tue Aug 14 17:14:17 2007","Tue Aug 14 17:14:17 2007","","","Tue Aug 14 17:14:17 2007","Tue Aug 14 17:14:17 2007","","","","","yes","","" "ANA_2389","2585425","2586141","717","9.70","5.13","25252","ATGAACCCGATCCTCCTTCCGCTGACCCAGGCCGCCGCCGCGCCGACCAGCCGCACCTGGTTCGACAACCCGGCCATCCAGAACAAGCTCGGCTACGCCCTCGTTGAGACCCTGGCGATGACCTTCGTCTCCGGGGCCATCACAGTCATCCTCGGGCTTCTGCTGGGGCTCGCCCTGGTCTCCACCGGCAAGCGGGGCCAGTTCCGCAACCCGACCCTGTACTGGGTGCTCTCCCAGATCGTTAACATCGGGCGCTCCATGCCCTTCATCATCCTCATGGTGGCCCTCATCCCGCTCACCCGGTTGCTCGTGGGCACCTCCCTGGGGTGGCAGGCGGCCTGCGTGCCGCTGACCATCGGCGCGATCCCGTTCTACGCGCGCCTGGTGGAGACGGCCATCAACGACGTCGACCGCGGCAAGGTCGAGGCGGCCCTCATGATGGGGGCCTCCGGGCGGCAGATCACCTGGGGGGTCCTCGTGCGGGAGGCCCTGCCGATCCTCATCCAGTCGGCCACCGTCACCATCATCACCCTCCTGGGCTACTCCGCCATGGCCGGCGCCGTGGGCGGCGGTGGCGTGGGTGACCTCGCCATCCAGTACGGCTACCAGCGCAACCAGGTCGACGTCATGGTCATCACCGTGGTCGTCATTGTCGGCATCGTCGGCGTCATCCAGCTGGTCGGCGACATGCTCAGCCGGCTGGTGAACCACCGCTGA","MNPILLPLTQAAAAPTSRTWFDNPAIQNKLGYALVETLAMTFVSGAITVILGLLLGLALVSTGKRGQFRNPTLYWVLSQIVNIGRSMPFIILMVALIPLTRLLVGTSLGWQAACVPLTIGAIPFYARLVETAINDVDRGKVEAALMMGASGRQITWGVLVREALPILIQSATVTIITLLGYSAMAGAVGGGGVGDLAIQYGYQRNQVDVMVITVVVIVGIVGVIQLVGDMLSRLVNHR$","ABC-type D-methionine transport system, permease component","Membrane, Cytoplasm","ABC-type metal ion transport system, permeasecomponent","K02072 D-methionine transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[34-237]T$	BPD_transp_1
PS50928	$\"[34-228]T$	ABC_TM1

noIPR
unintegrated

unintegrated
tmhmm	$\"[38-60]?$ $\"[81-101]?$ $\"[107-125]?$ $\"[166-188]?$ $\"[207-227]?$	transmembrane_regions

","BeTs to 12 clades of COG2011COG name: Permease component of an uncharacterized ABC transporterFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2011 is ---------d-lb-efghsnuj-it-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-51% similar to PDB:1XIO Anabaena sensory rhodopsin (E_value = );","Residues 34 to 237 (E_value = 2.9e-12) place ANA_2389 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component.","","metal ion transport system, permease component (membrane)","","1","","","","","","","","","","","Tue Aug 14 17:14:37 2007","","Tue Aug 14 17:14:37 2007","","","Tue Aug 14 17:14:37 2007","","","","Tue Aug 14 17:14:37 2007","Tue Aug 14 17:14:37 2007","","","","","yes","","" "ANA_2391","2586270","2587127","858","6.41","-1.34","30636","ATGTCCTCCGTCATCTCCCGGCGCACCGTCATCGCCGGTGGCCTGGCCACCGCCGCCGCCCTCACCCTGGCCGCCTGCTCCAAGTCCGGTAAGGGCGAGGTCAAGGGCATCAAGGTCGACGGCGACACCGCCACGATCACCATCGGTGCCACCCCCAAGCCCCACGTCGAGATCCTCAAGTGGGTTCAGGACAACCTCACCAAGGGCTCCGGCATCAAGCTGGACATCAAGGAGATCAACGACTACCAGACGCCCAACTCCTCGCTGGAGGACGGCTCGCTGGCCGCCAACTTCTACCAGACCCCCAACTTCCTGGCTCAGCAGAACAAGGAGAAGGGCTACGACTTCGTCTCCATCGCCGACGTCCACATCGAGCCCATGGGTATCTACACCTCCAAGGGCTACAAGGACGTCAAGGAGATCAAGGAGGGCGGCACGATCGTCCTCAACAACGACCCGGCCAACACGGCCCGCGGCCTCAAGCTCCTGGCCCAGGCCGGGCTCATCGAGCTGGACAAGTCCGCCGAGCTGCCCAGCGACACCGACGTGACCTCCAACCCCAAGAAGCTGAAGTTCACCACGGTTGACGGCGCCCAGGTCTACAAGTCGATGCCGGACGCCGAGGCCGCGGTCATCAACGGCAACTACGCCATCGATGCCGGGCTGAACCCCAAGAAGGACGCGCTCGTCCTGGAGAAGGGCGGCAAGGACTCGGAGTACCCCAACCAGCTCGTCGTGCGCAAGGACGACAAGGACAACGAGCACCTCAAGAAGCTCGCCAAGCTCCTCAACGACGACAAGCTGCGTGACTACATCAACAAGACCTGGCCCGACGGGGCGGTCGTCGCGGCGTTCTGA","MSSVISRRTVIAGGLATAAALTLAACSKSGKGEVKGIKVDGDTATITIGATPKPHVEILKWVQDNLTKGSGIKLDIKEINDYQTPNSSLEDGSLAANFYQTPNFLAQQNKEKGYDFVSIADVHIEPMGIYTSKGYKDVKEIKEGGTIVLNNDPANTARGLKLLAQAGLIELDKSAELPSDTDVTSNPKKLKFTTVDGAQVYKSMPDAEAAVINGNYAIDAGLNPKKDALVLEKGGKDSEYPNQLVVRKDDKDNEHLKKLAKLLNDDKLRDYINKTWPDGAVVAAF$","ABC-type D-methionine transport system, substrate-binding component","Periplasm, Membrane, Extracellular","ABC transporter substrate-binding protein","K02073 D-methionine transport system substrate-binding protein","NLPA lipoprotein","","","","","

InterPro
IPR004872
Family

NLPA lipoprotein
PF03180	$\"[46-285]T$	Lipoprotein_9

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[45-176]T$	no description
PS51257	$\"[1-26]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 12 clades of COG1464COG name: ABC-type uncharacterized transport systems, periplasmic componentFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1464 is ---------d-lb-efghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB004872 (NLPA lipoprotein) with a combined E-value of 1.3e-47. IPB004872A 64-107 IPB004872B 116-165 IPB004872C 165-201 IPB004872D 205-254 IPB004872D 206-255","","","-58% similar to PDB:1P99 1.7A crystal structure of protein PG110 from Staphylococcus aureus (E_value = 1.5E_33);-51% similar to PDB:1XS5 The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum (E_value = 9.5E_28);","Residues 46 to 285 (E_value = 5.5e-93) place ANA_2391 in the Lipoprotein_9 family which is described as NLPA lipoprotein.","","transporter substrate-binding protein","","1","","","","","","","","","","","Tue Aug 14 17:14:58 2007","","","","","Tue Aug 14 17:14:58 2007","Tue Aug 14 17:14:58 2007","","","Tue Aug 14 17:14:58 2007","Tue Aug 14 17:14:58 2007","","","","","yes","","" "ANA_2393","2587618","2588481","864","8.05","1.88","29504","ATGGCAGCTCGACGTGAACGGACGCAGTCGGACCGGTCGGCTCAACCGGTGCGGGGACGCACAGCTGAAGGCCTCGGGGGCCCGGGCGGCGCGGCTGGGGAGGGAGGCATCGCCGGCGTTGGGGGCGCAGGTGGCCCGGCCGCTGTGGAAGCGCGCGATCTTCACAAGTCCTTCCCGACCCTCGGTGGGGAACCGATCGAGATCCTGCACGGCATCTCCTGCGCCATGATGCCGGGGCGGATGACGGCGCTGGTCGGACCCAGTGGCTCGGGCAAGTCCACAGCGCTGCTGTGCCTGGCCGGGCTGGAGCCGGCGACGTCGGGGCGCGTCTCGCTCATGGGGCGCGACCTCGGCGGGCTCCCGGCGGCGCGAGTGGCCGAGCTCTACCGCGACCGGGTCGGCTTCGTCTTCCAGGCCTACAACCTCGTGCCCTACCTGACGGTGCGGGAGAACATCACGATCTCCGACACCCTGGCCGGCCGGCGCCCCGACTCGGCACGGGTGCGGGAGGTCCTGGCCGGACTGGGACTGGAGTCGCGCGCCGACGCGGTCGCGACCACGCTCTCGGGCGGTGAGCAGCAGCGCGTCGCCCTGGGGCGGGTCCTCTACCGCCGTCCACCGGTCGTCTTCGCCGACGAGCCCACCGGGGCCCTCGACACCCGCTCGGCCGCCTTCGTCCTGGCCGAGCTGCGGCGCCTGGCCGACGACGGGGCCGCCGTCATCCTCGTGACGCACGACCTGGGGGCCGCGGCCCTGGCCGAGAGCGTGCTCATCATGCGCGACGGCCGCATCGTCGACCACCGCCGCGGCGCCACCCCCGACGAGCTGCTGGCCGCCGTCAACCAGACGGGAGCTGCGGCATGA","MAARRERTQSDRSAQPVRGRTAEGLGGPGGAAGEGGIAGVGGAGGPAAVEARDLHKSFPTLGGEPIEILHGISCAMMPGRMTALVGPSGSGKSTALLCLAGLEPATSGRVSLMGRDLGGLPAARVAELYRDRVGFVFQAYNLVPYLTVRENITISDTLAGRRPDSARVREVLAGLGLESRADAVATTLSGGEQQRVALGRVLYRRPPVVFADEPTGALDTRSAAFVLAELRRLADDGAAVILVTHDLGAAALAESVLIMRDGRIVDHRRGATPDELLAAVNQTGAAA$","ABC-type transport system, involved in lipoprotein release, ATPase component","Cytoplasm, Membrane","ABC transporter ATP-binding protein","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[188-230]T$	Q82CC1_STRAW_Q82CC1;
PF00005	$\"[79-262]T$	ABC_tran
PS50893	$\"[49-286]T$	ABC_TRANSPORTER_2
PS00211	$\"[188-202]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[78-263]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[43-286]T$	no description
PTHR19222	$\"[49-279]T$	ATP BINDING CASSETE (ABC) TRANSPORTER

","BeTs to 20 clades of COG1136COG name: ABC-type transport systems, involved in lipoprotein release, ATPase componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1136 is aom--z-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 10","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 7.9e-30. IPB005074C 68-115 IPB005074D 176-219 IPB005074E 239-259***** IPB005116 (TOBE domain) with a combined E-value of 8.4e-25. IPB005116A 86-102 IPB005116B 131-148 IPB005116C 188-201 IPB005116D 208-227***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 9e-19. IPB013563A 68-102 IPB013563C 185-212***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 2.3e-18. IPB010509B 79-104 IPB010509D 183-227***** IPB010929 (CDR ABC transporter) with a combined E-value of 2.2e-14. IPB010929K 66-110 IPB010929L 120-172 IPB010929M 185-231","","","-56% similar to PDB:1F3O Crystal structure of MJ0796 ATP-binding cassette (E_value = 9.9E_33);-56% similar to PDB:1L2T Dimeric Structure of MJ0796, a Bacterial ABC Transporter Cassette (E_value = 2.2E_32);-57% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 3.3E_28);-55% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 8.1E_27);-53% similar to PDB:2D62 Crystal structure of multiple sugar binding transport ATP-binding protein (E_value = 4.5E_25);","Residues 79 to 262 (E_value = 1e-60) place ANA_2393 in the ABC_tran family which is described as ABC transporter.","","transporter ATP-binding protein","","1","","","","","","","","","","","","","Tue Aug 14 17:15:23 2007","","","Tue Aug 14 17:15:23 2007","Tue Aug 14 17:15:23 2007","","","Tue Aug 14 17:15:23 2007","Tue Aug 14 17:15:23 2007","","","","","yes","","" "ANA_2394","2588478","2589869","1392","11.53","21.97","47404","ATGACCCGCTACACACTGCGCGCCCTGGCTACCCAGTGGCGGGCCTGGTCGGGAACGGTGGCGGTACTGGCCCTCGCCGCAGGGCTCATCAACGTCTGCCTGGTGCACCGCATGACCGTCACTCGTTCCGACGTCGTCGCCGCGGCGCGGGCGGCGGGAGTGGACCCGGCCGAGCTCACGGTTCCGGGCGTCTCGGTGGCCTTCTACACGGCGATGGTGACGGTTCCGGTGGTGGCCGTCGTCGGGCAGTCCTGCGTGCAGGCACTGCGCACGAGCTGGGCCCTGTGGCGGCTGGCTGGCGCCCTGCCCCGCCAGGTGCTCGCCGCCGTCCTCGCCACCGTGGCGGTGCTGGGCCTGGTGGCCTGTGTGCCCGGGATCTTGCTGGGGATGGTGGCGGCCCAGCCCTTCGCCTCGGTGCTCACCCGCCTGGCGGCCGCGCGCATGGGGCGGATCGAGGTCGCCCAGACACCGACGACACTTCTGCTCACCGTGGTGGTCGTGGTCGCCGTCGCGGTCCTGGGGGCCGTGGGCCCGGCACGCGCCGCCGTGAGAACGCCAGCCGTGGAGGCAGTGCGGGACACCGCATCGGAAGGCCGACGCCGCATGGGGGTGGGGCGATGGATCCTGGCCGGAGTGTGGGCGCTTGCGTGTGCGGGGCAGCTGTTCGTCGCTTTTCTGGCCCCACCCGGAAGGAAGATCGACGGATTGCCGACCGGTGGGGGCCAGGCGATCCTGGCGTCGCTCCTGCTCGCGGTCCTCGTGGTGCTGCTGGCGCCCGCGCTCATCCCGCGGCTGCTGCGGCTGTGGTCGGCGCCGCTGGCGCGGCTGGGTGGACCGTGGCTCATCGCGCGGCGTTCGGCGCTGTGGCGCAGCGAGTCGTCGGCAAGTGCCATCGGCCTGCTGGCCCTGGCGATCTCCTTCACCGCGGCACTCACGACCAGTCTCGCCACGGGGCAGGCGGTGGTGGAGGCGGCGCGCCTGAACGTGGCGATCAACCAGGTGGACTCGCTGGTGCTGGCGGCGATCCTCGGGGCGATGGCGCTGCTGGGGGCCGTGGCCGTCGTCGGCATGTCCTCCCGGTCCCGGCAGTGTGAGTTCGCGGTGCTGCGCTGCGCCGGGAGCACGGTGCGCGGCGTGTGCCGGCAGGTGGTCGTCGAGGCGGCGCTGTACGTGGGGACGGCCCTGCTGATCTCGCTCGTGCCACTGGTGGTGACAACGGCCGGCGAGTCCCTTTTCTACGCCAGGGCGGGGATGCCGCTGGTAGTGCGCCCCGGCGTCGGGCCAGTGCTGCTGGTGGCCCTCCTGTCCTTCCTGGCCCTGGTCGCGGTGCTACTCGCTCCGATCCGGGGCGCCACCCGGACCCCGATCGGCACTGTCCTGGCGGCCGAGTGA","MTRYTLRALATQWRAWSGTVAVLALAAGLINVCLVHRMTVTRSDVVAAARAAGVDPAELTVPGVSVAFYTAMVTVPVVAVVGQSCVQALRTSWALWRLAGALPRQVLAAVLATVAVLGLVACVPGILLGMVAAQPFASVLTRLAAARMGRIEVAQTPTTLLLTVVVVVAVAVLGAVGPARAAVRTPAVEAVRDTASEGRRRMGVGRWILAGVWALACAGQLFVAFLAPPGRKIDGLPTGGGQAILASLLLAVLVVLLAPALIPRLLRLWSAPLARLGGPWLIARRSALWRSESSASAIGLLALAISFTAALTTSLATGQAVVEAARLNVAINQVDSLVLAAILGAMALLGAVAVVGMSSRSRQCEFAVLRCAGSTVRGVCRQVVVEAALYVGTALLISLVPLVVTTAGESLFYARAGMPLVVRPGVGPVLLVALLSFLALVAVLLAPIRGATRTPIGTVLAAE$","Permease","Membrane, Cytoplasm, Extracellular","permease, putative domain protein","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF214","","","","","

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[35-187]T$ $\"[295-456]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[66-86]?$ $\"[107-127]?$ $\"[158-176]?$ $\"[207-227]?$ $\"[243-263]?$ $\"[297-317]?$ $\"[336-356]?$ $\"[387-407]?$ $\"[426-446]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 35 to 187 (E_value = 0.0016) place ANA_2394 in the FtsX family which is described as Predicted permease.Residues 295 to 456 (E_value = 0.0011) place ANA_2394 in the FtsX family which is described as Predicted permease.","","putative domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2397","2590035","2591306","1272","7.09","0.30","44233","ATGAGGATGCGGATCGACTGGCGGACGTTGGGGGAGTGGGTGCGCCAGCCGGCGCCCGCGCAGGCCGGCCCCGGCATCCTGTCCACGCTGCTCCTCATCCTGTGCGCCACCTACCAGGGCGGCATGATTGGCAGCGCGGTGCTGACCGGCCGCGTCGGCGACGGCGGCCTGGTTGCAGGGATCGCCCCGACCAGAATCGGTTCTGCGATTCTCATTCTGGCGGCCATGGGGTCCACGGCGCTCCTTACTGCGCGACGCAGGTACCCGCTGGGGGTCTTCCTGATCGAGTGTGCCGTGTACGTGGTGGCCTCGGCGCTGGGGCTCAACAACTTCTTTCTCTTCCCGATGCTGGTGGCACTGGGGAGTGCGGTGAGCCGGCTCCCGCTGTGGCAGCACCTCGCGGTGATCGGCGCGGCCTGCCTCATGGCGACGGCCAGCGCGGTCCTGGTGGCCCCGCCCGGGGTCCTGATGGAGGAGTGGCTCAGCCAGGTGGTCGCGGTCCTGCTGACGGTCATCGCGGCAATGATGGCGCGCAGCGTCGCGAACTGGCGAGCGGCGCAAGCCGGGGCCAAAGCCGAGCGGGAGCGCTTCCGGGCGCTTCGGGCCGAGCGCGACCGCGCAGTGAGCCGGGCCGGTATCGCCGCCGAGCTGCACGACTCCGTGGGGCACGGCCTGACCACGATCATCGCCCTGTCCGAGGGGCTGGCCGGTGGCGCCGACCCGGAGATCGATGAGGCGCTCGGCGGCATCAACGAGGTGGCGCGGGAGTGCCTGGAGCAGACGCGCCGGGCGGTGAGAGCGTTGGCCGACGGCGAGGGTGAGCTGGCGGACTCACCGGGCCGGGACGGTGCCGGGCACCGATCCTGGGATGAGATCAGGAGCGTCGTCGGCAGGGTGAGATCACTGGGCGTCACGGTCGTCTTCACTGAGACCGGGCAGCGGGCCGACGACGCCGGGCAGGCCGACCTGTGCTTCGCGCTCACCCGGGAGGCGCTTACCAACGCGGTGCGGCACGCGCCCGCGCTGTCGCAGGCGCAGGTGTCCTGGGACCACGGCGAGTCGGCGGTCACGGTGATGGTTAGCAACGACGGTTTCTCAGGTGGTAGAGGCAGGGGCGACGATGGCCGCCGTGGTGGACCCGTGGAGGGGACCGGTCTGCTGCGGCTGCGGAACCGGGTCGAGGCGGCGGGAGGCTCGCTGGACTGGGGGCCCGAGTCCGACGGCGGCTGGCGGGTCGCGGCGATAGTGCCGAGAACTCGCGGTGAGGGCTGA","MRMRIDWRTLGEWVRQPAPAQAGPGILSTLLLILCATYQGGMIGSAVLTGRVGDGGLVAGIAPTRIGSAILILAAMGSTALLTARRRYPLGVFLIECAVYVVASALGLNNFFLFPMLVALGSAVSRLPLWQHLAVIGAACLMATASAVLVAPPGVLMEEWLSQVVAVLLTVIAAMMARSVANWRAAQAGAKAERERFRALRAERDRAVSRAGIAAELHDSVGHGLTTIIALSEGLAGGADPEIDEALGGINEVARECLEQTRRAVRALADGEGELADSPGRDGAGHRSWDEIRSVVGRVRSLGVTVVFTETGQRADDAGQADLCFALTREALTNAVRHAPALSQAQVSWDHGESAVTVMVSNDGFSGGRGRGDDGRRGGPVEGTGLLRLRNRVEAAGGSLDWGPESDGGWRVAAIVPRTRGEG$","Two-component system sensor kinase","Membrane, Cytoplasm","putative two-component system sensor kinase","two-component sensor kinase","histidine kinase, dimerisation and phosphoacceptor region","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
PF02518	$\"[319-419]T$	HATPase_c
SM00387	$\"[319-420]T$	HATPase_c

InterPro
IPR011712
Domain

Histidine kinase, dimerisation and phosphoacceptor region
PF07730	$\"[209-273]T$	HisKA_3

noIPR
unintegrated

unintegrated
signalp	$\"[1-40]?$	signal-peptide
tmhmm	$\"[25-45]?$ $\"[51-73]?$ $\"[88-108]?$ $\"[130-150]?$ $\"[160-180]?$	transmembrane_regions

","BeTs to 7 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB011712 (Histidine kinase, dimerisation and phosphoacceptor region) with a combined E-value of 1.3e-09. IPB011712A 208-225 IPB011712B 324-344","","","No significant hits to the PDB database (E-value < E-10).","Residues 209 to 273 (E_value = 1.2e-13) place ANA_2397 in the HisKA_3 family which is described as Histidine kinase.Residues 319 to 419 (E_value = 6.3e-07) place ANA_2397 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","two-component system sensor kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2398","2591349","2592002","654","9.03","2.21","23700","ATGATCGTGGATGACCAGCGCTACGCGCGCCTGGGGCTGGCGCTCATGATCCGCAAGGCGCCGGACCTGTACGTGGTGGCGGAGGCCGGTGACGGGCAGGAGGCGCTGGAGGTTCTGGAGGGGCTGAACCGGTCGTTGGGGCTGCCCGACGTCGTGCTCATGGATGTGCGCATGCCGGGGATGGATGGGATCAGCGCAACCCGGGCGATGGCGCGGCGGTTCCCGACGGTGAAGGTTCTGGTGCTGACCACCTACGACGAGGATGACTACGCCTTCGGGGCTCTGGAGGTGGGGGCCTCGGGGTTCCTGCTCAAGGATGTGCGCGCGGCGCAGCTGGCTCAAGCGGTGCGGGCGGTGGCGCAGGGCGATGCGGTGCTCACGCCGCGCGTCACCAAGGAGCTCATCGCGCGTGGGGTCCCGCGGGCGCTGCCCGCGGCGCAGCGTGAGGGGCTGCGGGAGAGGTTCGGGGTGCTGACGCCCAGGGAGCTCGACGTGGCTCGGCTCATTGCGGAAGGCATGTCGAACGAGGAGATTGCCGAGCGGCTCGTGCTGCAGCCCGCCTCCGTGCGCCGCAACGTCAGCCGAATCCTGGCCAAGCTCCACTTGCGTGACCGCGTCCAAATCGCCGTCGCCTGGTACAAGAGCGGCGGTTGA","MIVDDQRYARLGLALMIRKAPDLYVVAEAGDGQEALEVLEGLNRSLGLPDVVLMDVRMPGMDGISATRAMARRFPTVKVLVLTTYDEDDYAFGALEVGASGFLLKDVRAAQLAQAVRAVAQGDAVLTPRVTKELIARGVPRALPAAQREGLRERFGVLTPRELDVARLIAEGMSNEEIAERLVLQPASVRRNVSRILAKLHLRDRVQIAVAWYKSGG$","Two-component system response regulator","Cytoplasm","chitinase two-component response regulator","two-component system response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[158-214]T$	Q9ZBU8_STRCO_Q9ZBU8;
PR00038	$\"[158-172]T$ $\"[172-188]T$ $\"[188-200]T$	HTHLUXR
PF00196	$\"[155-212]T$	GerE
SM00421	$\"[155-212]T$	HTH_LUXR
PS50043	$\"[151-217]T$	HTH_LUXR_2
PS00622	$\"[172-199]T$	HTH_LUXR_1

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[1-106]T$	Q8FPY0_COREF_Q8FPY0;
PF00072	$\"[1-117]T$	Response_reg
SM00448	$\"[1-116]T$	REC
PS50110	$\"[1-120]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[147-216]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[1-124]T$	no description
PTHR23283	$\"[22-120]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF41	$\"[22-120]T$	TWO COMPONENT SENSOR AND REGULATOR HISTIDINE KINASE BACTERIA

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 3.5e-18. IPB000792 158-204***** IPB001789 (Response regulator receiver) with a combined E-value of 1.8e-11. IPB001789A 50-63 IPB001789B 98-108***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 1.6e-10. IPB001867A 50-63 IPB001867B 78-122***** IPB000673 (CheB methylesterase) with a combined E-value of 1e-07. IPB000673A 1-10 IPB000673B 22-75 IPB000673C 76-106***** IPB005143 (Autoinducer binding domain) with a combined E-value of 1.4e-07. IPB005143B 158-201","","","-54% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 4.6E_26);-54% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 4.6E_26);-59% similar to PDB:1S8N Crystal structure of Rv1626 from Mycobacterium tuberculosis (E_value = 4.9E_12);-59% similar to PDB:1SD5 Crystal structure of Rv1626 (E_value = 4.9E_12);-55% similar to PDB:1TMY CHEY FROM THERMOTOGA MARITIMA (APO-I) (E_value = 7.8E_10);","Residues 1 to 117 (E_value = 1.9e-30) place ANA_2398 in the Response_reg family which is described as Response regulator receiver domain.Residues 148 to 200 (E_value = 0.00018) place ANA_2398 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 155 to 212 (E_value = 1.8e-13) place ANA_2398 in the GerE family which is described as Bacterial regulatory proteins, luxR family.","","two-component response regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2399","2592393","2593163","771","7.06","0.14","28736","GTGGAAGGAGGATTTCAGACCGTTCTGGCCGACCCTCCGTGGCGTTTCGCCAATCGAACCGGCAAGGTCGCTCCCGAGCACCGCCGTCTGGGCAGGTACGGGACGATGTCCCTCGAGGAGATCAAGGATCTCCCGATCGGTGACGTGACCGCAGCGAATGCCCACCTGTACCTGTGGGTTCCCAACGCCTTGCTTCCGGAGGGCCTGGAGGTCATGCAGGCGTGGGGATTCCGCTACGTCTCGAACATCATCTGGGCCAAGCGCCGCAAAGACGGCGGGCCGGACGGCCGCGGCGTCGGCTTCTACTTCCGCAATGTCACCGAGCCGATCCTGTTCGGTGTTAAAGGATCCATGAGAACGCTGGCGCCGGGGCGCTCAACGGTCAATATGATCGAGACGCGCAAGCGTGAGCACAGCCGCAAACCCGACGAGCAGTATGACCTCATCGAATCCTGCTCGCCGGGTCCGTACCTGGAGATGTTCGCCCGCTACGCGCGACCGGGCTGGTCCGTGTGGGGCAATGAGTCGGATGAAGAGATCACGCCGCAGGGGAAGGCTCAGCGGGGATACGCTGGCGGCGACATCGACCCCCTGCCGCACCTGGAACCCAATGAGCAGATGAGCGACTGGCTCTCGGATCGCGTCGCCCGGATCCTGGCTGATGAGTACGCGAAGGGAGCGTCGATTCAGCAGATCTCGACTCAATCGGGCTACTCCACCACGCGGGTACACAGCCTCCTGACCAGGGCAGGCGTGGAGCTGCGAGAGTGA","VEGGFQTVLADPPWRFANRTGKVAPEHRRLGRYGTMSLEEIKDLPIGDVTAANAHLYLWVPNALLPEGLEVMQAWGFRYVSNIIWAKRRKDGGPDGRGVGFYFRNVTEPILFGVKGSMRTLAPGRSTVNMIETRKREHSRKPDEQYDLIESCSPGPYLEMFARYARPGWSVWGNESDEEITPQGKAQRGYAGGDIDPLPHLEPNEQMSDWLSDRVARILADEYAKGASIQQISTQSGYSTTRVHSLLTRAGVELRE$","MT-A70 family protein","Cytoplasm","adenine-specific DNA methyltransferase","MT-A70","MT-A70 family protein","","Cheng X. Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 1995. 24:293-318. PMID: 7663118Loenen W.A., Daniel A.S., Braymer H.D., Murray N.E. Organization and sequence of the hsd genes of Escherichia coli K-12. J. Mol. Biol. 1987. 198(2):159-170. PMID: 3323532Narva K.E., Van Etten J.L., Slatko B.E., Benner J.S. The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases. Gene 1988. 74(1):253-259. PMID: 3248728Lauster R. Evolution of type II DNA methyltransferases. A gene duplication model. J. Mol. Biol. 1989. 206(2):313-321. PMID: 2541254Timinskas A., Butkus V., Janulaitis A. Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases. Gene 1995. 157(1):3-11. PMID: 7607512Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E., Schildkraut I., Saenger W. Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(23):10957-10961. PMID: 7971991","","","

InterPro
IPR002052
Domain

N-6 Adenine-specific DNA methylase
PS00092	$\"[8-14]?$	N6_MTASE

InterPro
IPR007757
Family

MT-A70
PF05063	$\"[5-175]T$	MT-A70
PS51143	$\"[1-195]T$	MT_A70

noIPR
unintegrated

unintegrated
PTHR12829	$\"[3-177]T$	N6-ADENOSINE-METHYLTRANSFERASE

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 5 to 175 (E_value = 3.8e-35) place ANA_2399 in the MT-A70 family which is described as MT-A70.","","DNA methyltransferase (AL049481)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2400","2595291","2593294","1998","5.22","-12.89","70468","ATGACGACGGGGCACTCACCTTCTGCTGGCGACTACGACGCGACGACGGCGCTCAGCAGGTTCGCCTCGCCGCAGGACCTCGAGCGGATCGCCGAGACCCGTCCCGATCTGCACTCGATCCTGGCGACCAACCCGTCGATCCCACCTCGGGTCCGCGAGATACTGGAGCAGTCCGACGACGCTGTCGTCCAGGAGGTGCTGGCGCGCCAGGCTGGTCGTGGTGCTCAGCCGGCGCCACCGACGCCGTCTCCTGTCCCGGGCGACATCGGTCCGATGGCTCCGACGATGGCGGTGGGAACAGCTGCTGGGACGATGGGGGCGCCGCCCCAGCAGGCAGCGTCCACCAGCTCCGGGTACGCACAGGTTCCCCAGGAGTATGGCGGCAACCAGCAGGGGGCGCCCGGAGAGGCACCGCGGGGAGGGGCGCTTCAAGGGTCCTCCCCTCAGGGGTATGCGGCCGTCGCGCCGCCGCCAACCGCCCAGCCGTATTCGGCGTCCGCGATGCAGGCAGCGGCTCAGCCCGTGGATCAGCAGACTGCGATGCCGCCCGGGGTGCCGAGCCGGGCGCCGTCGGAATACGTACTGGGCCACGGCCAGGCTTATGACTCAGGGCAGGCATACGGTCCGGAGCAGCCGGCCGCACCGGCCTATGGGACACCGATGTATGCACCACCGGCGCAGGCGCCGAAGAAGCGCCGCCTGCTCAAAGTGGTCGCCGTCGTTCTGCCGATCATTCTTGTTCTGGGCGCTGGAGGTGCGGCCGCCTGGTACTTCTTGGGGCGCAGCGAGGTCTCCTTGGCATCTCCATTCGTGACCCCATCAGAGGCATGGCTGAAGGGTGCGAGCAAAGCCTGGAGTGCCGATGTCGCAGCCAACAAGGACCCCTACGTGATCGGTGGTCATTTTCTTACTCTCGACACGTCCGACGGCACTCTGACCGGCTACACACCTCTGGGCGACAACATGGAGGAGGTGTGGCAAGCGACCCTCGACGACGAGGACCTGACATCCAGCCACCGACCCACGCCGGGCTTTCAGACCTGGGGCAACAACACGCTCGTCTACAAGTCGACCCTCATCGACATGAAAACTGGAAAAGTTTCTTCAGCCCCCTGGAAAGAGGGGAAGTCAGCGATTATCGCCGACAACATCGCCATCTCCTGCAACTCGAGCGACAAGTGCACCGCCTGGGACTCCCCGGCGAAGCAGAAGTGGACACGCGAGATCCCCGGGACTGGAGAGATGTCCTCCAAAACCTACTATCGCAATGATTCCACCCTTACCAGAGGAGGTCGGCGCTACGCCTGGGTGTACAACGCCATCATCAACATCGACAACGGCGAGACACTCATCCTGGGCGGAGGATCCAAGGTCGACTCTGACCTCACCAGCACCTTCTTCAAGGATGGTTGGGGGACCTTCGAGGTAAAGAATGGCGAGTCCGAGGCTGACGACACCGATAGCGATTCACCATGGTCAACCACGTACAAAGTGACGATATACGACTTTACCGGCAAGAAGCGGAGCAGCTTCACCGAGACAATAACATTGGGCGAACAAGTTGTCATAGGCGAGAGCGAGCTCATCACCGCCGAAGAGTACCGCACGTACTTCAAGGACCAGGACTACAGCAAAGCAAAACTGACATCAAAAGTCAACGCGAATGGGTGCATCACGAAACTCAAACCCAAAGATGGAAAGCCTATCAGCATCCAGCCACCCGACAACAGTAGCGGCTTATCCTACGACTGGATTTCACCATCCTGCGCATCCGTCGCAACAAGCCCTCAGGGCAGCGACATCGTTAGATTGGCAACATTGGGCCGTGGTGACATCAACGGGCTGACTATGCTTATGAACATCAAGACCGGCGAAGAGATCACCTTCAATGGGATCGACTGGAAAAACGGAGACTCGCTCATCATCGCCAAGCCCGATCTCATCATCGGCTACAACAAGTTTGACGGCAAGGTCATCGGCTTCAAACCAGGCTCCTAG","MTTGHSPSAGDYDATTALSRFASPQDLERIAETRPDLHSILATNPSIPPRVREILEQSDDAVVQEVLARQAGRGAQPAPPTPSPVPGDIGPMAPTMAVGTAAGTMGAPPQQAASTSSGYAQVPQEYGGNQQGAPGEAPRGGALQGSSPQGYAAVAPPPTAQPYSASAMQAAAQPVDQQTAMPPGVPSRAPSEYVLGHGQAYDSGQAYGPEQPAAPAYGTPMYAPPAQAPKKRRLLKVVAVVLPIILVLGAGGAAAWYFLGRSEVSLASPFVTPSEAWLKGASKAWSADVAANKDPYVIGGHFLTLDTSDGTLTGYTPLGDNMEEVWQATLDDEDLTSSHRPTPGFQTWGNNTLVYKSTLIDMKTGKVSSAPWKEGKSAIIADNIAISCNSSDKCTAWDSPAKQKWTREIPGTGEMSSKTYYRNDSTLTRGGRRYAWVYNAIINIDNGETLILGGGSKVDSDLTSTFFKDGWGTFEVKNGESEADDTDSDSPWSTTYKVTIYDFTGKKRSSFTETITLGEQVVIGESELITAEEYRTYFKDQDYSKAKLTSKVNANGCITKLKPKDGKPISIQPPDNSSGLSYDWISPSCASVATSPQGSDIVRLATLGRGDINGLTMLMNIKTGEEITFNGIDWKNGDSLIIAKPDLIIGYNKFDGKVIGFKPGS$","Hypothetical protein","Extracellular, Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[239-259]?$	transmembrane_regions

","BeTs to 3 clades of COG1197COG name: Transcription-repair coupling factor - superfamily II helicaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1197 is --------vdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2401","2596030","2595392","639","4.99","-10.90","23259","ATGCGCCTCCACGTAGCCGACCACCCCCTCATCGACCACAAGCTCTCCGTCCTGCGTGACGAGAGGACACCGTCGGCGGTCTTCCGCCAGCTGGTGGACGAGCTCGTCACCCTGCTCGCCTACGAGGCCACCCGCGAGGTGCGCACCGAGGAGGTCGAGATCCGCACCCCCGTGGCGCTGGCCCAGTGCCGCCGCCTGGCCGACCCGAGGCCGATCGTGGTGCCGATCCTGCGCGCGGGCCTGGGGATGCTGGAGGGCATGACCCGCCTGCTGCCCACGGCGGAGGTCGGCTTCCTGGGGATGAAGCGCGACGAGGACACCCTGGAGGTGGAGACCTACGCCAACCGCCTGCCCGACGACCTCTCGGGCCGCCAGTGCTTCGTCGTCGACCCCATGCTCGCCACCGGTCACACCCTCGTGGCCGCCATCGACTACCTGCTGGAGCGCGGGGCGCGCGACGTCACCGCGCTGTGCCTCATCGCCGCGCCCGAGGGGGTCAAGACGCTGGAGGATGCGGTTGGCGAGCGCGCGAACGTCACGGTGGTGACCGCCGGGGTCGACGAGCGCCTCAACGAGCACGCCTACATCGTGCCCGGTCTCGGCGACGCCGGCGACCGCCTCTACGGCATCGTCGACTGA","MRLHVADHPLIDHKLSVLRDERTPSAVFRQLVDELVTLLAYEATREVRTEEVEIRTPVALAQCRRLADPRPIVVPILRAGLGMLEGMTRLLPTAEVGFLGMKRDEDTLEVETYANRLPDDLSGRQCFVVDPMLATGHTLVAAIDYLLERGARDVTALCLIAAPEGVKTLEDAVGERANVTVVTAGVDERLNEHAYIVPGLGDAGDRLYGIVD$","Uracil phosphoribosyltransferase","Cytoplasm","uracil phosphoribosyltransferase","uracil phosphoribosyltransferase ","uracil phosphoribosyltransferase","","","","","

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[34-178]T$	Pribosyltran

InterPro
IPR005765
Family

Uracil phosphoribosyl transferase
TIGR01091	$\"[2-211]T$	upp: uracil phosphoribosyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2020	$\"[4-211]T$	no description
PTHR10285	$\"[4-211]T$	URIDINE KINASE RELATED
PTHR10285:SF1	$\"[4-211]T$	URACIL PHOSPHORIBOSYLTRANSFERASE

","BeTs to 19 clades of COG0035COG name: Uracil phosphoribosyltransferaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0035 is -om-kzyqvdrlbcefgh-nuj--twNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-67% similar to PDB:1I5E CRYSTAL STRUCTURE OF BACILLUS CALDOLYTICUS URACIL PHOSPHORIBOSYLTRANSFERASE WITH BOUND UMP (E_value = 3.3E_50);-63% similar to PDB:1V9S Crystal structure of TT0130 protein from Thermus thermophilus HB8 (E_value = 3.6E_44);-62% similar to PDB:1O5O Crystal structure of Uracil phosphoribosyltransferase (TM0721) from Thermotoga maritima at 2.30 A resolution (E_value = 6.7E_43);-49% similar to PDB:1BD3 STRUCTURE OF THE APO URACIL PHOSPHORIBOSYLTRANSFERASE, 2 MUTANT C128V (E_value = 8.8E_19);-49% similar to PDB:1BD4 UPRT-URACIL COMPLEX (E_value = 8.8E_19);","Residues 34 to 178 (E_value = 3.3e-12) place ANA_2401 in the Pribosyltran family which is described as Phosphoribosyl transferase domain.","","phosphoribosyltransferase (upp)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2402","2596726","2597589","864","5.11","-12.09","31723","ATGGCCAACGGCTCCGCCCCCACCATCACTCTGAACAATGGCGTCGACATCCCCCAGATCGGCTACGGCGTCTTCCTGACCCCGCCGGAGGAGACCGAGCGCGCCGTGCTCGAGGCCTTCGAGGTCGGCTACCGCCACATCGACACCGCCCAGGCCTACCGCAACGAGGAGGGCGTGGGCGCGGCCGTTGCCGCCAGCGGACTGCCCCGCGAGGACATCTTCCTGACCACCAAGGTGTGGATCTCCAACGCAGGGGAGGAACGTGCCGCCCGCTCCATCGACGGCTCCCTGCGCCGCCTGGGCGCCGACTACATCGACCTGCTGCTCGTCCACCAGCCCTTCGGCGACTACTACGGCACCTACCGCGCCATGGAGAAGGCCCTGGCCGCCGGCAAGGTCCGCGCCATTGGCGTCTCCAACTTCTTCCCCGACCGGTTCGTGGACCTGGCGCAGCACGTCGAGGTGCCGCCGGCCGTCAACCAGATGGAGACTCACGTCTTCAACCAGCAGGCCGACAACCGCGCCTGGTACACCAAGTACGACACCGCCCTGGAGTCCTGGGGGCCGCTCGCTCAGGGCCGCAACAACATCTTCACCCACCCGGTGCTCACCTCCGTCGGCGAGAAGCACGGCAAGACCGCCGCCCAGGTGGCCCTGCGCTACCTCATCCAGCTCGACATCATCGTCATCCCCAAGACGGTCCACCGCGAGCGCATGGTCACCAACCTCGACGTCACCGACTTCCAGCTCGACGACGCCGACATGCGGGCCATCGCCGCCCTCGACGAGGGGCAGGGCGTCGTCAACCACTACGACCCCGCCTTCCAGGAGCGCCTCGCCTCCTACACGGTCGAGGCGGACTGA","MANGSAPTITLNNGVDIPQIGYGVFLTPPEETERAVLEAFEVGYRHIDTAQAYRNEEGVGAAVAASGLPREDIFLTTKVWISNAGEERAARSIDGSLRRLGADYIDLLLVHQPFGDYYGTYRAMEKALAAGKVRAIGVSNFFPDRFVDLAQHVEVPPAVNQMETHVFNQQADNRAWYTKYDTALESWGPLAQGRNNIFTHPVLTSVGEKHGKTAAQVALRYLIQLDIIVIPKTVHRERMVTNLDVTDFQLDDADMRAIAALDEGQGVVNHYDPAFQERLASYTVEAD$","Oxidoreductase, aldo/keto reductase","Cytoplasm","oxidoreductase, aldo/keto reductase","hypothetical protein","aldo/keto reductase","","Bohren K.M., Bullock B., Wermuth B., Gabbay K.H. The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 1989. 264(16):9547-9551. PMID: 2498333Schade S.Z., Early S.L., Williams T.R., Kezdy F.J., Heinrikson R.L., Grimshaw C.E., Doughty C.C. Sequence analysis of bovine lens aldose reductase. J. Biol. Chem. 1990. 265(7):3628-3635. PMID: 2105951Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A. An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 1992. 257(5066):81-84. PMID: 1621098Borhani D.W., Harter T.M., Petrash J.M. The crystal structure of the aldose reductase.NADPH binary complex. J. Biol. Chem. 1992. 267(34):24841-24847. PMID: 1447221Gulbis J.M., Zhou M., Mann S., MacKinnon R. Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. Science 2000. 289(5476):123-127. PMID: 10884227","","","

InterPro
IPR001395
Family

Aldo/keto reductase
PD000288	$\"[11-262]T$	Q8A7Z1_BACTN_Q8A7Z1;
PR00069	$\"[39-63]T$ $\"[95-113]T$ $\"[124-141]T$ $\"[158-187]T$ $\"[197-221]T$	ALDKETRDTASE
G3DSA:3.20.20.100	$\"[5-285]T$	no description
PTHR11732	$\"[1-234]T$	ALDO/KETO REDUCTASE
PF00248	$\"[11-263]T$	Aldo_ket_red
PS00062	$\"[124-141]T$	ALDOKETO_REDUCTASE_2
PS00063	$\"[230-245]?$	ALDOKETO_REDUCTASE_3
PS00798	$\"[43-60]T$	ALDOKETO_REDUCTASE_1

noIPR
unintegrated

unintegrated
PTHR11732:SF34	$\"[1-234]T$	ALDO-KETO REDUCTASE

","BeTs to 12 clades of COG0656COG name: Aldo/keto reductases, related to diketogulonate reductaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0656 is -o-pkzy-v-rlbcefg----j----Number of proteins in this genome belonging to this COG is 1","***** IPB001395 (Aldo/keto reductase) with a combined E-value of 2.8e-75. IPB001395A 17-29 IPB001395B 39-63 IPB001395C 68-80 IPB001395D 96-113 IPB001395E 120-155 IPB001395F 156-191 IPB001395G 201-255","","","-67% similar to PDB:1VP5 Crystal structure of 2,5-diketo-D-gluconic acid reductase (TM1009) from Thermotoga maritima at 2.40 A resolution (E_value = 1.7E_72);-58% similar to PDB:1A80 NATIVE 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE A FROM CORYNBACTERIUM SP. COMPLEXED WITH NADPH (E_value = 1.2E_57);-58% similar to PDB:1HW6 CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE (E_value = 1.2E_57);-57% similar to PDB:1M9H Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor (E_value = 6.4E_56);-59% similar to PDB:1VBJ The crystal structure of prostaglandin F synthase from Trypanosoma brucei (E_value = 1.2E_46);","Residues 11 to 263 (E_value = 2.8e-102) place ANA_2402 in the Aldo_ket_red family which is described as Aldo/keto reductase family.","","aldo-keto reductase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2403","2600125","2597915","2211","5.67","-10.30","80036","GTGAGCCGGTCCCCCGAATCGAGCGATGAGAGCGAGTCCGCGCCAGGCGGTTCCGTTCCGGGAGCCTCCCGGCCGGCCCCGTCGTCGGACCGATTCTCAGTGCTGCGACTCCCCGCCGGCTCCCTGCCCGGCAAGGAGCCCCTCAACCCGGTGGTGTTCTTCGTGTCGGCCACCATCATCGCGATCGTCGCCCTGGCCGCGCTCATCGCCCCCGACCTCGTCAAGAGCGCCTTCGGGGCGGCCGTGACCTGGACGAGCCGATGGTTCGGCTCCTTCTACATCCTGCTCATCACAGCCGCGCTGGTCTTCATCCTGGGGCTGGCCTTCTCCCGCTTCGGGCGCATCCGCCTGGGCCCGGACAACTCGACGCCGGACTTCTCCACCTTCGCCTGGACGGCCATGCTCTTCGCCGCCGGCATCGGCACCGAGATCCTGTTCTTCGCCGTCGCCGAGCCGGTCGACCAGTACGTGCACCCGCCCACCGGCGACGCCCAGACCATCCCCCCGGCCGCCCGCGCCCGCGAGGCCATCGTCCTATCCCTGTTCCACTACGGCATCTCCGGCTGGGGCCTGTACGCCCTGGTGGGCCTGGCCATGGCCTACTTCGCCTACCGACGCCGCGACACGCTCACGCTGCGCTCCACCCTGCGCCCGCTGCTGGGGCGGCACACCGAGGGCGTCATCGGTGACATCGTCGACGCCGCAGCCCTGGTCGGCGGGGTTTTCGGCATCGCGGCCTCGCTGGGGGTCGGCGTCGTCCAGCTGAACGTGGCCCTCAACATCCTGTTCGGGCTGCCGCAGGGCTTCCCCACCCAGATCGGGCTGACCGCCCTGGCCGTCATCATGGCCACCGTCTCGGCCGTCTCCGGCGTCGACCGGGGCGTGCGCGTCCTGTCCACCATCAACGTGCTGCTGGCCATCGGCCTGGCCCTGTGGGTGCTCGTCACCGGTGACGCCGCCTTCCTCATCGACGCGCTCATCGGCTCCATCGGCGACTTCTTCACCCGCTTCCCGCAGCTGACGCTGGAGACCTACGCCTACAACCGCCCCGATGACTGGCTCAACGCCTGGACCCTGTTCTTCTGGGCGTGGTGGATCGCCTGGGCGGCCTTCGTGGGCATGTTCCTGGCCCGCATCTCACGCGGGCGCACCATCCGGCAGTTCGTGCTCGGCAGCCTCCTGCTGCCCTTCAGCTACATCCTCATGTGGGTGGCGATCTTCGGCAACCACGCCCTGGACCTGGTCATCCGCGGCAACGGCGAGTTCCGGGACATCACCCTGGAGCGCCCCGAGCAGGGGCTGTACTGGATCCTGGAGCACCTGCCGGGCCAGAAGATCCTCATCGCCCTGGCCCTGTTCGTGGGGATCCTCTTCTACGTCACCAGCGCCGACTCCGGCGCCCTGGTCATGGCCAACCTCTCCAGCCGCATCCGCTCGGCGCGTCAGGACGCCGCCGCCTGGTTGCGGATCTTCTGGGCCGCCCTGACCGGGATTCTCACCATCGCGATGCTCGTGGCCGGCGGCATCCCCATCCTGCAGCAGGCCACCATCGTCATGGCGCTGCCCTTCTCCGGGGTCCTCATCCTCATCATGTACACCCTGTGGCGCTCCCTGAGCACCGAGGACACCTACAACCAGGCCCTGAGCCGGGCCGACCGCAACCGGGCCCTGGGCTTCAACGGCTCGGCCGCGGGGCTGGAGCAGACGCCCTGGCGCGAGCGCCTGACGCACACCCTCAACTCGGTCTCCCCCGACGAGGCCGGCAACGCCATGGAGCGGCGCATCGTGCCGGCCCTGGAGGCGGTGGCCACCGAGCTGCGCAAGGAGAACGTCTCCGCCGAGGTCTTCGTCGAGGGCCCCGAGGCCCAGGACCCCGACGACGAGCGCACCTTCCTGGGGCGTGCCAGCCTGGTGGTCTCCTCCCACCCGGCCACCGACAGCGGCGAGGAGCAGTCCAGCTCCATCGACTCCTTCCGCTACGTGGTGCGCATGGTGGTCACACCGGTACCCGCCTACGGTTTCGCCGTCCACGAGGCCGACGACCTCACGGTGCGCCTCGAGGTACGCCCGCACAGCGGCGGCCAGGGCTACGACGTCGTCGACTGGAACTCCGACCAGGTGGCCCACGACGTCCTCGACCACTACGAGCGCTGGCTGGAGTACGTGGGCACCTCCGAGAAGAGCGAGTCCCGGTTCTCCCGCCGGCTGTGA","VSRSPESSDESESAPGGSVPGASRPAPSSDRFSVLRLPAGSLPGKEPLNPVVFFVSATIIAIVALAALIAPDLVKSAFGAAVTWTSRWFGSFYILLITAALVFILGLAFSRFGRIRLGPDNSTPDFSTFAWTAMLFAAGIGTEILFFAVAEPVDQYVHPPTGDAQTIPPAARAREAIVLSLFHYGISGWGLYALVGLAMAYFAYRRRDTLTLRSTLRPLLGRHTEGVIGDIVDAAALVGGVFGIAASLGVGVVQLNVALNILFGLPQGFPTQIGLTALAVIMATVSAVSGVDRGVRVLSTINVLLAIGLALWVLVTGDAAFLIDALIGSIGDFFTRFPQLTLETYAYNRPDDWLNAWTLFFWAWWIAWAAFVGMFLARISRGRTIRQFVLGSLLLPFSYILMWVAIFGNHALDLVIRGNGEFRDITLERPEQGLYWILEHLPGQKILIALALFVGILFYVTSADSGALVMANLSSRIRSARQDAAAWLRIFWAALTGILTIAMLVAGGIPILQQATIVMALPFSGVLILIMYTLWRSLSTEDTYNQALSRADRNRALGFNGSAAGLEQTPWRERLTHTLNSVSPDEAGNAMERRIVPALEAVATELRKENVSAEVFVEGPEAQDPDDERTFLGRASLVVSSHPATDSGEEQSSSIDSFRYVVRMVVTPVPAYGFAVHEADDLTVRLEVRPHSGGQGYDVVDWNSDQVAHDVLDHYERWLEYVGTSEKSESRFSRRL$","High-affinity choline transport protein","Membrane, Cytoplasm","BetT","high-affinity choline transport protein","choline/carnitine/betaine transporter","","Kappes R.M., Kempf B., Bremer E. Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD. J. Bacteriol. 1996. 178(17):5071-5079. PMID: 8752321","","","

InterPro
IPR000060
Family

BCCT transporter
PD010111	$\"[45-204]T$	Q8FKI6_ECOL6_Q8FKI6;
PF02028	$\"[52-541]T$	BCCT
TIGR00842	$\"[90-541]T$	bcct: transporter, betaine/carnitine/cholin
PS01303	$\"[356-365]T$	BCCT

noIPR
unintegrated

unintegrated
tmhmm	$\"[50-70]?$ $\"[89-109]?$ $\"[130-150]?$ $\"[186-204]?$ $\"[232-252]?$ $\"[271-291]?$ $\"[301-321]?$ $\"[357-377]?$ $\"[387-407]?$ $\"[448-470]?$ $\"[491-511]?$ $\"[517-535]?$	transmembrane_regions

InterPro
IPR002125
Domain

CMP/dCMP deaminase, zinc-binding
PF00383	$\"[48-150]T$	dCMP_cyt_deam_1
PS00903	$\"[101-138]?$	CYT_DCMP_DEAMINASES

noIPR
unintegrated

unintegrated
G3DSA:3.40.140.10	$\"[54-197]T$	no description
PTHR11079	$\"[55-197]T$	CYTOSINE DEAMINASE
PTHR11079:SF9	$\"[55-197]T$	CYTIDINE/DEOXYCYTIDYLATE DEAMINASE-RELATED

","BeTs to 14 clades of COG0590COG name: Cytosine/adenosine deaminasesFunctional Class: F [Metabolism--Nucleotide transport and metabolism] Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0590 is ------yq-drlbcefghsn-jxi--Number of proteins in this genome belonging to this COG is 1","***** IPB002125 (Cytidine/deoxycytidylate deaminase, zinc-binding region) with a combined E-value of 2e-06. IPB002125A 101-107 IPB002125B 125-134","","","-66% similar to PDB:1Z3A Crystal structure of tRNA adenosine deaminase TadA from Escherichia coli (E_value = 1.2E_22);-65% similar to PDB:2B3J Crystal Structure of Staphylococcus aureus tRNA Adenosine Deaminase, TadA, in Complex with RNA (E_value = 8.4E_21);-55% similar to PDB:2A8N Biochemical and Structural Studies of A-to-I Editing by tRNA:A34 Deaminases at the Wobble Position of Transfer RNA (E_value = 8.1E_16);-63% similar to PDB:1WWR Crystal structure of tRNA adenosine deaminase TadA from Aquifex aeolicus (E_value = 6.9E_15);","Residues 48 to 150 (E_value = 1.1e-34) place ANA_2404 in the dCMP_cyt_deam_1 family which is described as Cytidine and deoxycytidylate deaminase zinc-binding region.","","cytidine and deoxycytidylate deaminase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2405","2601437","2601898","462","7.12","0.32","16959","ATGAGTCGCCGTCCCCACGAATCCCGAACCCTGTCCCGTTCCCGCACTCAGGTCCCGCACCCCCACGCCTCCGAGATCGCGCCGCGTGCGGCCGCTGACCTCTACTCGCTCCTGTGCGACGCCATGGTCGCCGCTGATACCAAGGCGATCGACGCCCTGCTCACCGACTACTGTGTCCTGACCCACATGACCGGCTACCCCCAGCCCAAGGTCGAGTGGCTCGGCGACATCGCCAACGGCGCCATGCGCTACCACGACCATGAGGTGGTCTCCGTCCAGCCCGACACCATCGCCGGATTCCCGGTGGTGCGCGGCCGCACCCGCACCACGGCCACCCTGTGGGGAGGGCGCGGCACCTGGAACCTCCAGATCGTCGGATACGTCGTGCCCGACGCTGACCCCGACACTGAGCGCAACCCCACCGGCTTCCGCTTCAGCCGCCTGGACGCCTCCACCTGGTGA","MSRRPHESRTLSRSRTQVPHPHASEIAPRAAADLYSLLCDAMVAADTKAIDALLTDYCVLTHMTGYPQPKVEWLGDIANGAMRYHDHEVVSVQPDTIAGFPVVRGRTRTTATLWGGRGTWNLQIVGYVVPDADPDTERNPTGFRFSRLDASTW$","Hypothetical protein","Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:35 2007","Wed Aug 15 19:42:35 2007","Wed Aug 15 19:42:35 2007","Wed Aug 15 19:42:17 2007","","","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","Wed Aug 15 19:42:17 2007","","Wed Aug 15 19:42:17 2007","","Wed Aug 15 19:42:17 2007","yes","","" "ANA_2406","2605016","2601921","3096","6.80","-1.60","105420","ATGACTCGCACCGGGCCGCAGGGCCGCACGCTGCCTCCGCAGACCGGCCCCATCAGGGCGCTGCTCGCCTCGCCCCCGGATCTGCCGGTGGTCGAGGTGCTGACCGATCTGCGCGAGCTCCTCTCCGCCGCTCCCTCCGCCTCCGACAACGCAGGCGCCGGCGCCTGCCTGGTCCTCACCGCCCCGCCCGGCACCGGTAAGACGACGCTCGTCCCACCGCTTCTGGCCGACGTCCTTGCAGACGTCCCTGCCGACGCCCCACAGCGCGCCCAGGAACGCCGGCCGGGCCGCGTCGTCGTCACCCAGCCGCGGCGCATCGCCGCCCGCGCGGCCGCCCGCCGCCTGGCCGACCTCCTGGGAGAGGAGGTCGGCGGCACCGTCGGATACGCGGTGCGCGGGGAGCGGCGCGCCGGCCCGGACATGCGGATCGAGGTGGTCACCGCCGGGCTCCTCCTGCGCCGCCTCCAGCGGGACCCGGAGCTGAGCGGCGTCGACGCCGTTATCCTCGACGAGGTCCACGAGCGCTCCTTGGACAGCGACCTCCTCCTGGCCCTCCTGGCGGACGCACGCGCCGCCCTGCGCGAGGACCTCACCCTCGTGGCCATGTCAGCCACGCTCGACGCCGATCGCCTGCGCCGCATCCTGGGCGGCTCCTCGGGCGGAGCCTCGCACGGCTCGTCGGACGGAGCCGCGCCGCTGGTGGAGGTGCCTGGGCGCCTCCACCCCCTAGAGGAGGTGTGGGCGCCGCCGGGGCGCACCGGCCGCCTGGGGCCGCGCGGGGTGCCGCGGGAGTTCCTCGCCCACGTCGCCGCCACCGTGGAGCGGGCCCTGGCCGAGCGCTCCGGCGACGTGCTGGTCTTCCTGCCCGGGGCCCGCGAGGTCGACGACGTCGTCTCCCGCCTGCGCGGTGCAGTTCACGAGGGCGTGGACGTCCTGCCGCTGCACGGCCGCCTGCCCGCGAGCGCCCAGGACGCGGCCCTGGCCCCGAGCCCGGCGGGGCGGCGGCGCGTCGTGGTGGCCACGAACGTGGCCGAGTCCTCGCTGACGGTGCCCGGGGTGCGGGTGGTGGTGGACTCCACGCTGGCGCGTGAGCCGCGCCTGGACGTGGCCCGCTCCATGAGTGGCCTGGTGACGGTGGGGGTCTCGCGGGCGGCCGGGGTGCAGCGGGCCGGGCGGGCGGGGCGCGAGGGGCCCGGCGTCGTCTACCGCTGCTGCTCGCCGACGGACTGGGCGCGTTCGCCGCTGGCTCCGACCCCGGAGATCCTCTCGGCCGACCTCACCGGTGCGGCCCTGGAGCTGGCCGTGTGGGGCGTGCCCGACGGCGCGGGGCTGGCCTGGGTCGATGAGCCACCGGCTGCGGCGCTGGCGGCCGCCCGGGAGGCGTTGGAGCGCCTGGGCCTGGCCGGCGCCGATGGCGTGACGCCCCTGGGTCGGGCGGTGGCCGGGCTGCCGGCGGGCGTGCGTGAGGCACGCGCCCTGCTGGCGACGGCACCGGTGCTGGGGGCGCGGCGGGCGGCGCGGGCGACGGCTCTGCTGACCGCCGACCTGCGCGCGCCTGGTGGGGACCTGACGGCCCTGGCCCGACAGGTCCGGGGCGGTGGGGCCGGGTCGGGGGCGTGGAAGGCGGAGGCGCACCGACTGGAGCAGGCCTGCCGGCGCGCCGCCGCTGAGCAGTCGGGGTCCTCTGAGGCCCCGGGTTCCGCGAGCGGTGGACCACAGGCGCCGGGCGCAACAGGGGCGGCCGGTTCGCCGGGCACCGGGCGCGGCCGCGAGACTGCCGGACGGCCTGAGGATCCGGCCGCCGCGAACGGTGGACCACAGGCGCCGAGCGCGTTGGGGACCTCCGGCTCGCCGGCCACGGGCCGGGAGGGTGCGGGCCGTCCTGACCGCGTCGGCGGGGACGCTCTCGGGGGCGGCGATGGCGCCGGGGCGCACGACCTGGAGTCGGCGGTGGCGCTGGTGGCCGGGACGGCGCAGCCGCAGTGGATCGCGCGACGTCGGGGGCCGGCCCCACAGGCGGGCAAGGAGGCGCACTACGCGAGCGTCGCCGGGACCGGTCTGCGCCTGCCGTCGGGCTCGGCGCTGGCGGAGTCCGAGTGGCTGGCGGTGGCCGGCGTGGACCTGACCAGTGGGCGCGGCGACGCACTCATCCGGGCCGCCGCGCCCCTCGACGAGCAGGCGGCCCTGGAGCTGGCCGGGGCCTGGCTGACCGAGGAGGAGCGCACCGTCTGGGAGGGCGGGCGGCTGCGCACGGAGCGCCTGCGCCGCCTGGGGGCCATCACACTCACCACCACCCCGGGGCCGCCGCCGGGTCCGACGGCGGTGGCGGAGGCCGTCGTCGCGCGGGTGCGCGCTGAGGGGGCCGATGCCGGCCTGGGCGTGCTGCCGTGGGATGAGGAGGCGCTCGGCCTGCGCGCCCGACTGGCCCTGCTGCACGAGCACCTGGGTGAGCCCTGGCCGGATATGAGCGATGCGGCCCTGGCGGAGCGGGCCGAGGAGTGGCTGGCACCGGCGGTGACGAGCCTGGCCGGGCGGGCTGGAGGGTCACACGGAGTAGACGGGCCGGGTGGGGCGGCGTCGGGTAGGCCCGGTGAGTCGGCGGCGTCGGGCTCGGGGGGCCGGCGTTTCAGCCTGGAGCGGCTGGACGTGGCTCAGGCGCTGCGGGCGCTGCTGCCGTGGCCGCAGGCGTCGCGCCTGGACGAGCTGGTGCCCGAGCGCCTGGAGGTCCCCTCAGGCTCGCAGGTGCGGGTGGACTACACGGGGGCGGTCGGCGGGGCGGCCGGGGCCGCTGGCTCGGTGGGTTCAGCGGGCTTGATTGAGGCCGGGCAGGTGGGTCGGCCGGTGCTGGCGGTGCGGGTCCAGGAGTGCTTCGGCTGGGAGGCCACGCCGCGAATCGTGGAGGGCCGGGTGGCGGTGCTGCTGCACCTGCTCTCTCCGGCGCGCCGTCCGGTGGCGGTCACCGACGACCTGACCTCCTTCTGGGAGCAGGGCTACCCGCAGGTGCGCGCCGAGATGCGGGGCCGCTACCCCAAGCACGCCTGGCCGGAGGACCCGTGGAACGCGCCCGCGACGAGGGGGACCGGACGACGTCGGTAG","MTRTGPQGRTLPPQTGPIRALLASPPDLPVVEVLTDLRELLSAAPSASDNAGAGACLVLTAPPGTGKTTLVPPLLADVLADVPADAPQRAQERRPGRVVVTQPRRIAARAAARRLADLLGEEVGGTVGYAVRGERRAGPDMRIEVVTAGLLLRRLQRDPELSGVDAVILDEVHERSLDSDLLLALLADARAALREDLTLVAMSATLDADRLRRILGGSSGGASHGSSDGAAPLVEVPGRLHPLEEVWAPPGRTGRLGPRGVPREFLAHVAATVERALAERSGDVLVFLPGAREVDDVVSRLRGAVHEGVDVLPLHGRLPASAQDAALAPSPAGRRRVVVATNVAESSLTVPGVRVVVDSTLAREPRLDVARSMSGLVTVGVSRAAGVQRAGRAGREGPGVVYRCCSPTDWARSPLAPTPEILSADLTGAALELAVWGVPDGAGLAWVDEPPAAALAAAREALERLGLAGADGVTPLGRAVAGLPAGVREARALLATAPVLGARRAARATALLTADLRAPGGDLTALARQVRGGGAGSGAWKAEAHRLEQACRRAAAEQSGSSEAPGSASGGPQAPGATGAAGSPGTGRGRETAGRPEDPAAANGGPQAPSALGTSGSPATGREGAGRPDRVGGDALGGGDGAGAHDLESAVALVAGTAQPQWIARRRGPAPQAGKEAHYASVAGTGLRLPSGSALAESEWLAVAGVDLTSGRGDALIRAAAPLDEQAALELAGAWLTEEERTVWEGGRLRTERLRRLGAITLTTTPGPPPGPTAVAEAVVARVRAEGADAGLGVLPWDEEALGLRARLALLHEHLGEPWPDMSDAALAERAEEWLAPAVTSLAGRAGGSHGVDGPGGAASGRPGESAASGSGGRRFSLERLDVAQALRALLPWPQASRLDELVPERLEVPSGSQVRVDYTGAVGGAAGAAGSVGSAGLIEAGQVGRPVLAVRVQECFGWEATPRIVEGRVAVLLHLLSPARRPVAVTDDLTSFWEQGYPQVRAEMRGRYPKHAWPEDPWNAPATRGTGRRR$","ATP-dependent helicase HrpB","Cytoplasm","ATP-dependent helicase HrpB","ATP-dependent helicase HrpB","ATP-dependent helicase HrpB","","Skarstad K., Boye E. The initiator protein DnaA: evolution, properties and function. Biochim. Biophys. Acta 1994. 1217(2):111-130. PMID: 8110826Yoshikawa H., Ogasawara N. Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial replication origins. Mol. Microbiol. 1991. 5(11):2589-2597. PMID: 1779750Georgopoulos C. The E. coli dnaA initiation protein: a protein for all seasons. Trends Genet. 1989. 5(10):319-321. PMID: 2558436Skovgaard O. Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli. Gene 1990. 93(1):27-34. PMID: 2172087","","","

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[303-397]T$	Helicase_C
SM00490	$\"[295-397]T$	HELICc
PS51194	$\"[264-437]T$	HELICASE_CTER

InterPro
IPR010225
Family

ATP-dependent helicase HrpB
TIGR01970	$\"[28-1031]T$	DEAH_box_HrpB: ATP-dependent helicase HrpB

InterPro
IPR011545
Domain

DEAD/DEAH box helicase, N-terminal
PF00270	$\"[38-214]T$	DEAD

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[71-134]T$	no description

InterPro
IPR013689
Domain

Helicase ATP-dependent, C-terminal
PF08482	$\"[873-1018]T$	HrpB_C

InterPro
IPR014001
Domain

DEAD-like helicases, N-terminal
SM00487	$\"[6-237]T$	DEXDc

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[48-212]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[251-409]T$	no description
PTHR18934	$\"[13-495]T$	ATP-DEPENDENT RNA HELICASE

noIPR
unintegrated

unintegrated
tmhmm	$\"[47-62]?$ $\"[76-94]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[116-136]?$ $\"[142-162]?$ $\"[191-211]?$ $\"[221-241]?$	transmembrane_regions

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[17-71]T$	HTH_3
SM00530	$\"[16-71]T$	HTH_XRE
PS50943	$\"[17-71]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[12-74]T$	no description

","BeTs to 9 clades of COG1476COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1476 is aom-k----d-lb--f-----j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-76% similar to PDB:1UTX REGULATION OF CYTOLYSIN EXPRESSION BY ENTEROCOCCUS FAECALIS: ROLE OF CYLR2 (E_value = 3.2E_11);-76% similar to PDB:2GZU High-resolution structure determination of the CylR2 homodimer using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings (E_value = 3.2E_11);","Residues 17 to 71 (E_value = 3.1e-17) place ANA_2410 in the HTH_3 family which is described as Helix-turn-helix.","","DNA-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2411","2607044","2606700","345","4.91","-11.91","12124","GTGTGCGGGGCGGCGGGCCGGGCAGGGCGGGCCGAGCGGCGGCAGGCTCGGACACACCTCCACGATCTACATGGTGCGGTTGAAGTAGATGTTCCCTCCGATGAAGCTGACCAGCTGGAGCCACAGGACAACCACCAGGGCCAGCTTCATCGACCCCCCGAAGGCACCCACGGCGCCTACGACAACGTTGCCGAACAACCCGACGACGCCGGCCAGAGCCCAGGCCCGCTGCGAGGTGGCCCTGTCCCGCTCATCCTTCCGCCTCTCGAGCCCACGGACGGCGAAGGTGTCGTGCCCACGTCTCTTCGCGATGATCAGGGCGATGTACACGAGCATCACGACTGA","VCGAAGRAGRAERRQARTHLHDLHGAVEVDVPSDEADQLEPQDNHQGQLHRPPEGTHGAYDNVAEQPDDAGQSPGPLRGGPVPLILPPLEPTDGEGVVPTSLRDDQGDVHEHHD$","Hypothetical protein","Cytoplasm","Unknown (protein for MGC:64703)","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","(protein for MGC:64703)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2412","2607238","2608059","822","7.54","0.69","27660","ATGGTCCAGCAGTCCGCCCCACCAGGAATCTGGGACGAGGACCCCGACGGCGCCTCCATCCTCCTGGCCACCGGGCGCGCTCGCCACGACCTCCTCGTCGTCGCCGAGCCCGTCTTCCTGCGCGATCTCGACCAGGCATGGGGGCGCCCCTCGGCCCGGGTGCGCCTGTCCTTCCTGCCCGGCGTCGAGGCTCCCAGTGCCCCGGGCCACGAGGACGCGCTCATGTCCTACGAGCGCGGTGGCCTCGGCGTCCTCGTCGCCCGTGGTCGCACCAGCGTGTATGAGGGCGAGGCCGCCCGTAGTGCGACGGCGCTGGCCCGGATCGCCAGCGGGGCCCGCCTGCGCGCCGCGCTGCTCGTCACCCGCGCCACCCCGCTGCGTGGCTCCGGTGACGTGGCCGGCGGCTCGGCGCCAGGACAGGTGCGCGTCGTCGCCGACCACCTCAACCTCTCCGGTGGCTCTCTCTTCCCGGCCCCCGGCATGGTCTCGGCTGGCTGGGACGCGACGCTTACCGAGCGCCTGGGGAGCCTTCGCGGCGTGAGCGGTAGCTCCGTGGTCGCCCTCGTGCCCGGGCCGCTGCGTCCGAGCCCGGCCGAGTCCCGTGCCCTGGTCTCCCTGGGGGCCGACGCCGCCGTCACCGACTCCGTGGCCGAGGCCATGATCCTGGCCGCGAGGGGAGTGGCGGTCTCCGCCCTGACCTACCTCGACGCCCCGGCCGCCGGCGGCAACCTCGGGCGGGCGCAGCTCTCCCTGAGGCAGGCCTCCGGAGTCACTCTGGCCGCCGTCGAGGAGATCCTCAGAAGCCTGCGGGCCGGTTCCTGA","MVQQSAPPGIWDEDPDGASILLATGRARHDLLVVAEPVFLRDLDQAWGRPSARVRLSFLPGVEAPSAPGHEDALMSYERGGLGVLVARGRTSVYEGEAARSATALARIASGARLRAALLVTRATPLRGSGDVAGGSAPGQVRVVADHLNLSGGSLFPAPGMVSAGWDATLTERLGSLRGVSGSSVVALVPGPLRPSPAESRALVSLGADAAVTDSVAEAMILAARGVAVSALTYLDAPAAGGNLGRAQLSLRQASGVTLAAVEEILRSLRAGS$","Purine nucleoside phosphorylase","Cytoplasm, Membrane","Purine nucleoside phosphorylase (Inosinephosphorylase)(PNP), putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1580	$\"[40-269]T$	no description

","BeTs to 3 clades of COG0005COG name: Purine nucleoside phosphorylaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0005 is aompkzyqv-rlbcef--s--j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","nucleoside phosphorylase (Inosine phosphorylase)(PNP), putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2413","2608127","2608861","735","4.87","-14.46","26488","GTGAAACCCTTCCTCTTCCTGGCCACCCGCAGCGACGACGAGCCTGCCGACGCCGAGTACGAGGCGTTCCTCAAGCGCACCGGCCTGGAGGAGTCCACGCTCCGCCGCCTGCGCCTGGAGTCCCAGTCCCTGCCGCAGATCGACCTGGACGACTGGTCCGGCATCCTCGTGGGCGGCTCCCCCTTCAACGCCTCCACCCCGCCGGAGAAGAAGTCCGCCACCCAGAAGCGCGTCGAGGCCGAGCTCTCCGGCCTGCTCGACCGCGTCGTCGAGGCCGACTTCCCCTTCTTCGGCGCCTGCTACGGCGTCGGTACGCTCGCCTGCCACCAGGGCGCCGTCGTCGATACCACCTACGGTGAGGCCGTCACCGCCCCTGAGGTCACTCTCACCGAGGCCGGCCTGGCCGACCCGATCTGCGCGGGCGTCCCGAAGGTCTTCCAGGCCTTCGTCGCCCACAAGGAGGCGGTGACGACGCTGCCGCCCCACGCCGTCGTCCTAGGAACCGGTGAGGCGTGCCCGGTCCAAATGTTCCGGATCGGGTCCAACCTGTACGCCACCCAGTTCCATCCCGAGCTCGACGGCGACTACCTCGCCCACCGGCTCGGCTTCTACTCCGGTCACGGCTACTTCGCCGACGACGAGCTCGCCGAGCTTCAGGCCCGCGTGCGCCTCGACGACGTCTCCGACTCCTGGAAGCTCCTGGCCAACTTCGTGGCCGTCCACGCCCGCGACTGA","VKPFLFLATRSDDEPADAEYEAFLKRTGLEESTLRRLRLESQSLPQIDLDDWSGILVGGSPFNASTPPEKKSATQKRVEAELSGLLDRVVEADFPFFGACYGVGTLACHQGAVVDTTYGEAVTAPEVTLTEAGLADPICAGVPKVFQAFVAHKEAVTTLPPHAVVLGTGEACPVQMFRIGSNLYATQFHPELDGDYLAHRLGFYSGHGYFADDELAELQARVRLDDVSDSWKLLANFVAVHARD$","Glutamine amidotransferase","Cytoplasm","GMP synthase - Glutamine amidotransferasedomain, putative","glutamine amidotransferase","GMP synthase - Glutamine amidotransferase domain-like","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[22-240]T$	no description

","BeTs to 24 clades of COG0518COG name: GMP synthase - Glutamine amidotransferase domainFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0518 is aompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 3","***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 2.9e-06. IPB000991A 95-112 IPB000991B 182-192","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","synthase - Glutamine amidotransferase domain, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2414","2609010","2609696","687","5.24","-6.84","23407","ATGTCCCGCATCGTCATGATCGGAGGTCACGGCAAGGTCGCGCTGCTGGCCGCCCCGCTGCTCGTGGACGCCGGCCACGAGGTCGTCTCCCTCATCCGCAACCCTGACCACTCCGCCGACGTCGCCGCCACCGGAGCCACCCCGCTGGTCCTGTCCGTCGAGGAAGCCGACGTCGCTGAGCTCACCCGGGTCTTCGCCGGTGCTGACGCGATCGTCTGGTCCGCCGGGGCCGGCGGCAAGGGAGGCCCGGAGCGTACCGACGCCGTCGACCGCGCCGCCGCCATCCGCTCCATGGAGGCCGCCGCCGCAGCCGGGGTCACGCGCTACGTCATGGTCTCCTTCCTCACCGCCTACGGCGAGGTTCCCGACGACCACCCGCTGCGCGCCTACGCCATTGCCAAGATCGTGGCAGACCGACACCTGCAGACCACCGACCTGGCCTGGACGATCTTGGGGCCGGGCCTGCTGACCCTGGATGAACCCACCGGTGCCATCACCGTGGCTCGCGTCCCCAAGGGCACCCCGACCTCGAAGGCGCCGACGTCGCGTGGGAACGTCGCCCGCGTTATCACCGCCGTGCTCGCCGAGCCGGCCAGTATCGGTAAGGTCATCCCCTTCTACGACGGCGACACCCCCATAGCCCAGGCTGTTGCTGACGTACCGCAGGAGTACGCCGACCTGTCATGA","MSRIVMIGGHGKVALLAAPLLVDAGHEVVSLIRNPDHSADVAATGATPLVLSVEEADVAELTRVFAGADAIVWSAGAGGKGGPERTDAVDRAAAIRSMEAAAAAGVTRYVMVSFLTAYGEVPDDHPLRAYAIAKIVADRHLQTTDLAWTILGPGLLTLDEPTGAITVARVPKGTPTSKAPTSRGNVARVITAVLAEPASIGKVIPFYDGDTPIAQAVADVPQEYADLS$","NAD-dependent epimerase/dehydratase","Cytoplasm","Predicted nucleoside-diphosphate-sugarepimerases","hypothetical protein","NAD-dependent epimerase/dehydratase","","Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 1997. 36(21):6294-6304. PMID: 9174344","","","

InterPro
IPR001509
Family

NAD-dependent epimerase/dehydratase
PF01370	$\"[4-201]T$	Epimerase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[4-224]T$	no description
PTHR15020	$\"[1-214]T$	FLAVIN REDUCTASE-RELATED
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 5 clades of COG0702COG name: Predicted nucleoside-diphosphate-sugar epimerasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0702 is -o----yq-d-lbcefghs--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 201 (E_value = 0.00017) place ANA_2414 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.","","nucleoside-diphosphate-sugar epimerases (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2415","2610090","2609788","303","5.51","-1.10","10165","ATGCGTACTCGCAAGATCGTGTCAGCCGCCCTGCTCGTTGCCGCCCTCGCCGTCGGCACCGCCGCCTGCGGCTCCATGAATGCCGACAAGGACAAGATGGAGCAGACCTCCACCCCGAACGGCACCATGAGCGACGGCAAGATGTCCGATGGAAAGATGAGCGACGGAAAGACCGAGGACGGGAAGATGTCGGATAACAAGATGTCCGACAGCCCCACCTCCGGCAGCATGTCGGACGGCAAAATGAGCGACGACAAGATGTCGGCCGCCCCCTCGGCCAGCGCTATGAGCGACGGCAAGTAG","MRTRKIVSAALLVAALAVGTAACGSMNADKDKMEQTSTPNGTMSDGKMSDGKMSDGKTEDGKMSDNKMSDSPTSGSMSDGKMSDDKMSAAPSASAMSDGK$","Hypothetical protein","Extracellular, Periplasm","probable vegetatible incompatibility proteinHET-E-1, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[10-28]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[158-176]?$ $\"[200-222]?$ $\"[227-247]?$ $\"[253-273]?$ $\"[283-303]?$ $\"[341-361]?$ $\"[376-398]?$ $\"[417-437]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[19-37]?$ $\"[47-67]?$ $\"[105-127]?$ $\"[137-157]?$ $\"[167-187]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[26-186]T$	no description

","BeTs to 20 clades of COG0518COG name: GMP synthase - Glutamine amidotransferase domainFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0518 is aompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2419","2614576","2614052","525","8.36","2.56","17842","GTGCGCGGACCGGGCTTCTCACAGGCACCGACGGGCACCGCGGGCACCGGAGGGGGCTCTTCGCGGACATCTGCCGGGCAGCGCCCAATTCGTCCGCGGGAAGGATGTCAGCGGCAGGTGCCGACAGTGCATGATGTGGGCATGAGCACCGTCGGAACCTCCCCTCCAGGACAGAGCGCACCGCGCTTCTCGCCGGGCGCGGAGCAGTACGCCGACGGGCTCCCCCAGGGATTCGTCTTCCCCGGCACCGAGAACCTCGACCCAGCAGAAATCTTCTCCGGCCCCGGCTACACGGCACCCCGCCCCCGCAGCGACTCCGGGGCGACGGCCGCCCTGGTATGCGGACTGCTCAGCTTCATCCCCCTCATCGGCGTCGCCGCGATCATCCTGGGCATCAACGCGCTGCGGCGCCTGCATCACAGCTATAACTCCGGCGAGGGGCTGGCCTGGCTGGGGCTCATTCTGGGAGCCGTCTTCGTCATCCTGTGGCTCTGCGTCCTCATCCTCGTACTGCTCGTGGGCTAG","VRGPGFSQAPTGTAGTGGGSSRTSAGQRPIRPREGCQRQVPTVHDVGMSTVGTSPPGQSAPRFSPGAEQYADGLPQGFVFPGTENLDPAEIFSGPGYTAPRPRSDSGATAALVCGLLSFIPLIGVAAIILGINALRRLHHSYNSGEGLAWLGLILGAVFVILWLCVLILVLLVG$","Hypothetical protein","Membrane, Extracellular","probable integral membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[110-132]?$ $\"[151-173]?$	transmembrane_regions

InterPro
IPR006042
Family

Xanthine/uracil permease
TIGR00801	$\"[68-457]T$	ncs2: uracil-xanthine permease

InterPro
IPR006043
Family

Xanthine/uracil/vitamin C permease
PTHR11119	$\"[46-430]T$	XANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER
PF00860	$\"[72-440]T$	Xan_ur_permease

InterPro
IPR013248
Family

Shr3 amino acid permease chaperone
SM00786	$\"[326-505]T$	no description

noIPR
unintegrated

unintegrated
PTHR11119:SF3	$\"[46-430]T$	XANTHINE-URACIL PERMEASE
tmhmm	$\"[69-91]?$ $\"[97-117]?$ $\"[122-142]?$ $\"[161-181]?$ $\"[191-211]?$ $\"[217-237]?$ $\"[355-375]?$ $\"[381-403]?$ $\"[418-438]?$ $\"[444-464]?$	transmembrane_regions

","BeTs to 9 clades of COG2233COG name: Xanthine/uracil permeasesFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG2233 is ----k---vd-lb-efgh-n------Number of proteins in this genome belonging to this COG is 1","***** IPB006042 (Xanthine/uracil permease family) with a combined E-value of 3.7e-43. IPB006042A 188-204 IPB006042B 324-353 IPB006042C 365-408","","","No significant hits to the PDB database (E-value < E-10).","Residues 72 to 440 (E_value = 3.8e-79) place ANA_2420 in the Xan_ur_permease family which is described as Permease family.","","permeases ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2421","2617226","2616609","618","5.98","-1.64","21441","GTGAGTAGTCCCGCAGATCCGCGTGCCGAGTACCGGCGGCACATGCAGCACCGTCAGGCCACCGTCATCGGCGCCATCCTGGCCGTCATGGTGGTCGCGGTCGCCGTGAGCCTCCTGGTATCGCTGGGCATCCTGCCCGCCTACAACCCGGGCTTCTCGCAGCCCAAGAGCACGGCGACCTACGTGCCCCAGACCTGCCCGCCGAGCGGCGCCAAGACCGTCGACGTCACCACGATCGAGAAGATCAACGTCTACAACGGCTCGGAGACAGTGGGTCTGGCCGCCACGGTGCAGCAGGAGCTGGAGGAGGCGGGCCTGACCGTCACCTCGGCGAATGACTGGCCGGGGGGCATCTACAACGGCGAGGTCCAGATCATGGCCTCCAAGGGCGGCCTGACCAATGCCTACTCCCTGGCCCAGATCTTCCCCAAGTCCACGGTGCAGCTCGACAAGAGCCTGTCCGACGACGACACCACGGTCTCGGTGGTCCTGGGCAAGGAGTACCTACAGAACGCCCTGAAGGCGGACGAGATCAAGCTGCTCGGCGCCGGCAAGCCCATCACTGCGCCCAGCGACTGCGTTCCGGCGGACAAGGCCGCCACGAAGAAGCCCAGCTGA","VSSPADPRAEYRRHMQHRQATVIGAILAVMVVAVAVSLLVSLGILPAYNPGFSQPKSTATYVPQTCPPSGAKTVDVTTIEKINVYNGSETVGLAATVQQELEEAGLTVTSANDWPGGIYNGEVQIMASKGGLTNAYSLAQIFPKSTVQLDKSLSDDDTTVSVVLGKEYLQNALKADEIKLLGAGKPITAPSDCVPADKAATKKPS$","Hypothetical protein","Membrane, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PS51257	$\"[1-29]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[9-29]?$	transmembrane_regions

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[50-63]T$ $\"[71-94]T$	HTHTETR
PF00440	$\"[50-96]T$	TetR_N
PS50977	$\"[44-104]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[28-96]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[53-73]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PS51257	$\"[1-24]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-22]?$	signal-peptide

InterPro
IPR001765
Domain

Carbonic anhydrase, prokaryotic and plant
G3DSA:3.40.1050.10	$\"[6-167]T$	no description
PF00484	$\"[25-164]T$	Pro_CA

noIPR
unintegrated

unintegrated
PTHR11002	$\"[2-96]T$	CARBONIC ANHYDRASE

","BeTs to 14 clades of COG0288COG name: Carbonic anhydraseFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0288 is -om---y--drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001765 (Carbonic anhydrase, prokaryotic) with a combined E-value of 3.5e-28. IPB001765A 23-66 IPB001765B 68-97 IPB001765D 128-163","","","-73% similar to PDB:1YLK Crystal Structure of Rv1284 from Mycobacterium tuberculosis in Complex with Thiocyanate (E_value = 6.9E_44);-56% similar to PDB:1G5C CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM (E_value = 1.1E_17);","Residues 25 to 164 (E_value = 2.3e-13) place ANA_2428 in the Pro_CA family which is described as Carbonic anhydrase.","","anhydrase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2430","2622842","2626492","3651","4.76","-53.79","117390","ATGGCGGCGCTGCGGGCCGACCGCGTCACCCACGCCTACCTCTTCTCCGGCCCGCGCGGCTGCGGCAAGACGACGTCGGCGCGCATCCTGGCCCGCTGCCTCAACTGCGCCCAGGCCCCCACCGACACCCCCTGCGGTACCTGCCCCTCCTGCCGGGACCTCGCCACCGGCGGCCCCGGCAGCCTCGACGTCGTCGAGATCGATGCCGCCAGCCACAACGGTGTCGACGACGCCCGCGACCTGCGTGAGCGCGCCGCCTTCGCCCCGGCCCGCGACCGCTACAAGATCTTCATCCTCGACGAGGCCCACATGGTCACCGCGCAGGGCTTCAACGCGCTGCTCAAGCTCGTCGAGGAGCCGCCGGCGCACGTGAAGTTCATCTTCGCCACCACCGAGCCGGAGAAGGTCATCGGCACCATCCGCTCGCGCACCCACCACTACCCCTTCCGTCTCGTCCCGCCCGACGTCCTCGAGGGCTACCTCGCCCACCTGTGCCAGGCCGAGGGCGTCGAGATCGGCCCCGGCGTCTTCCCCCTCGTGGTGCGCGCCGGCGGCGGCTCGGTGCGCGACACCCTCTCGGTCATGGACCAGCTCATCGGCGGGGCGCATGACGGCGGCGTCAACTACCAGCGGGCCGTCGCCCTGCTGGGCTACACCGACACCACCATGCTCGACCAGTGCGTTGACGCCATCGCGGCGGGCGACGGCGCCGGCGTCTTCCGGGTGGTGGACCGGGTCGTCTCCTGCGGGCACGACCCGCGCCGCTTCGTGGAGGATCTGCTGGCTCGGCTGCGCGACCTGCTCGTCATCGCCCTGGCCGGTTCCGAGGCCGGTGCGGCGCTGGGTTCTCTGCCGGTCGATGAGTTCGAGCGCATGGACCTGCAGGCCCGCACCATGGGGGCCGCCGTTCTCTCGCGGGCCGCCGACACCACCGCCCAGGCCCTGACCGCCATGGTTGGCGCCACCTCCCCGCGCCTCCAGCTCGAGCTGCTCGTGGCCCGCCTGCTCATCCCCGCCGGCGGCGCCGCCAGAGCGGGGGGTGCTGTCGGCGCAGCTGCGGCGGGAGGCCCGGCTGGAGCAGCCGGGAGCGCCGGACCGATGGCCTCGCCCGCCCCCGGTGGTGCGGGCGCCGGCGCGGGCACGGGAGCGGCCGGCAGCACCGCCGGTGCCGTGCCCGCCGGGTCCGGACGCGAGATGGCCGCCCAGATCGCCCGCCAGGCCTCCGCAGAGGCCGCCGGGCGGCGTGGAGGCCAGCGGCCCGAGAACGCCGGAGGACCAGAGGGAGTCGGGAGCGCGGTGCCCACCGCTCCGCAGGCGCCCCACTCCGACGCTGGTTGGGGAACGGCCCCTGCCGCGCCCTCAGCGCCCGCCGCGGGCCCGACGTCGACCGCACCGGCCTCACAGGCCGGCCCCGCCGTCAGCTGGGACGGCCCCGAGGGTGGCGCCGTCGCCTCGCCAGGGCCCTCCGCACCCTCGGCCGCGGCGGCCTCACGACCGGTCGAGCAGCCGCCACGCGCAGCCGAGCCGGCCAGCGCCCCAGCCGCCCCGAGCGCGCCCGTCGCTCCCTCGGCCCCCGCTGCCCAGGCAGGCGCCGGTTGGGGGGCAGCCCCTGCTGCGGCCTCAGCACCCGTCGCCCAGGGAGGTGTCGCTGCTGGCAGCTCGGGCGGGGGCGAGGCGGCTGACGCGGAGATGATCCGCACCCGCTGGGAGGAAGTCCTCGAGGCGGCCAAGCGCTCGCGGCGCGCCACCTGGGCGCTGGTCGGCCCCAACTCCCGACCGGGCACCGTCTCCGGGGGCGTCTTCACGCTCCTGTTCGCCGCCCCCGGCCTCGTGGGCGCCTTCGAGAACGGCGGACACGGCCCCATCTTCTCCGCGGCCCTCCACCAGGCCCTCGGCCTGCGCCTCGAGGTGCATGCCATCGTTGCCGGCGACGACGGGCCGGGCGGTTCCGGAGGCCCTGGCGGCCCGCGTGGACCGCAAGGCATGGGTGGCCCCGGCGCTGCCCCCTCCGGAGCGGAGGCGGCGCACAACCCCGGCCCCAGCGTCAGCTCCGCCGTCGGCCACGACGCCGGTCACGGCGGGCCGCAGGGCTTCGACGGTGGCGGCGCCCCGGGCGCAGGCCCGAGCGGACCGGGACCACAGGCCGGCGCTTTCGACTCGGCGGGCTCGGCCGCCAGCAGCGTGGCGCAGGACGTCAACGGCGCCGGGACGCACGCCGGTGGCCTGGGCGCGGTCGAGGCCGACGTGGCGGTTCCTGTCGTCGGCAGTGGCGCTGACAGTTCAGGCTCCGGTGTTGCAGATGCGGGGCTGCACGGCTCCACCGGTGAGCCGGTCGCCGCATCCGCTCCCGACCCCCAGGCGCTTGCCACCCACGACCCCAGTAGCGCTGTCCATGACGTCGGCCGCCCCGCCCAGGACCCGGCCGCCCAGTCGCCCGCTGCAGCACCTTCGCGGCCAACCGACGTCGAGCCGGCCGACCGCCCCGGTGCGCACCGGCCCGTCTCCACCACCTGGGACGACGGCTCCCCGATCCCCGAGCCCCCGCCCGAGGACGACTGGGGTGCCGATCCCTACGCCGAGGACTTCGGGTACGTCAGTGGGGCTCTCAGTGTCGATGAGCCCAGCGGCTCTGCTGGGTACTCCGCCGCTCCAGCCCCGGCCGCCGTCGCCCAGGAGGCCGCGACCTCGCCCGAGCCGCAGCCGGCCCAGGTCGGCGTCGATCCCGCCGCCCCCACCGAGTTCCAGGCGGTCTCCCCGGCATCCCCGACCGCCTCCAAGTCCCCGGCGCCCGCCGCTGCTCCCATGGCGCCGCCGGCATCCCCCGCTCCCGCGAACCCCACCGATCCCGACGACGGCTGGGGGCCCGTCGCGATCCCCGGCGGGGGCTCGGCCCCGGTCTCCGCGCCCGCCGCCGGCGGCACCGACCCGGACGACGGTTGGGGCCCGGTCGCCGTCCCCGGCGGCGGAACCGTGCCCGCCCAGTCGGCATCCGCCTCCGGGCCCTCCTCAGGCGCAGGTTCAGGAGTGCCTGCGTCCCCCGCCCCCACCGACCCCCAGTCCGCTCCGGCCCCCACCTCGGCCCCGGCGGCCTCAGCCTCACCCGCCCAGTCCCGCTCCGCCCCCGCCGCGCAGGCGCCCGACGAGGCGCCCCTGGCCACCGTCCACCGTCTGCGCGCCCTGCCGGAGATTCCCGGCGGGGCCGCGTCCGCTCCGGCTGCCCCCCAGTCCTTCCAGCAGGCTCCCTCCTCCCCGTCCCCGCAGGCGTCCGGAGCCGGCAGCGCACCACGCGCCCCCGGCTCCTCGGAGACCACTGCCGGATCCCCCGGCCTGGCCCCCGTCACCTGGGAGGGGACGACGTCGAGCCCCTTCAGCCCAGGCCCGCCCCCCGAGGAGCCCAGCGCCTCGAGCGCCCCACCCGAGGATGAGTCCACCTGGGCGCCGTCGGGTATCGCCGGCTCGCGCCTGGCCGCCGCCATGGCCGCCGCCCGCGCCGCCGCCCAGGAGGCCGACACCGACTCCCTGGCCGACGACACCCCCAGCGAGGACGACCCCGACGCCGAGGACGCCGGCGTCGTCGGGCTCGAGGTCGTCAAACGGATCCTTGGCGCCCAGGTCATCGAAGAGGTCACCGTGACCCAGGAAGGACGCTGA","MAALRADRVTHAYLFSGPRGCGKTTSARILARCLNCAQAPTDTPCGTCPSCRDLATGGPGSLDVVEIDAASHNGVDDARDLRERAAFAPARDRYKIFILDEAHMVTAQGFNALLKLVEEPPAHVKFIFATTEPEKVIGTIRSRTHHYPFRLVPPDVLEGYLAHLCQAEGVEIGPGVFPLVVRAGGGSVRDTLSVMDQLIGGAHDGGVNYQRAVALLGYTDTTMLDQCVDAIAAGDGAGVFRVVDRVVSCGHDPRRFVEDLLARLRDLLVIALAGSEAGAALGSLPVDEFERMDLQARTMGAAVLSRAADTTAQALTAMVGATSPRLQLELLVARLLIPAGGAARAGGAVGAAAAGGPAGAAGSAGPMASPAPGGAGAGAGTGAAGSTAGAVPAGSGREMAAQIARQASAEAAGRRGGQRPENAGGPEGVGSAVPTAPQAPHSDAGWGTAPAAPSAPAAGPTSTAPASQAGPAVSWDGPEGGAVASPGPSAPSAAAASRPVEQPPRAAEPASAPAAPSAPVAPSAPAAQAGAGWGAAPAAASAPVAQGGVAAGSSGGGEAADAEMIRTRWEEVLEAAKRSRRATWALVGPNSRPGTVSGGVFTLLFAAPGLVGAFENGGHGPIFSAALHQALGLRLEVHAIVAGDDGPGGSGGPGGPRGPQGMGGPGAAPSGAEAAHNPGPSVSSAVGHDAGHGGPQGFDGGGAPGAGPSGPGPQAGAFDSAGSAASSVAQDVNGAGTHAGGLGAVEADVAVPVVGSGADSSGSGVADAGLHGSTGEPVAASAPDPQALATHDPSSAVHDVGRPAQDPAAQSPAAAPSRPTDVEPADRPGAHRPVSTTWDDGSPIPEPPPEDDWGADPYAEDFGYVSGALSVDEPSGSAGYSAAPAPAAVAQEAATSPEPQPAQVGVDPAAPTEFQAVSPASPTASKSPAPAAAPMAPPASPAPANPTDPDDGWGPVAIPGGGSAPVSAPAAGGTDPDDGWGPVAVPGGGTVPAQSASASGPSSGAGSGVPASPAPTDPQSAPAPTSAPAASASPAQSRSAPAAQAPDEAPLATVHRLRALPEIPGGAASAPAAPQSFQQAPSSPSPQASGAGSAPRAPGSSETTAGSPGLAPVTWEGTTSSPFSPGPPPEEPSASSAPPEDESTWAPSGIAGSRLAAAMAAARAAAQEADTDSLADDTPSEDDPDAEDAGVVGLEVVKRILGAQVIEEVTVTQEGR$","DNA polymerase III, subunits gamma and tau","Extracellular, Cytoplasm","DNA polymerase III subunit gamma","DNA polymerase III subunit gamma ","DNA polymerase III, subunits gamma and tau","","","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[9-157]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[12-143]T$	AAA

InterPro
IPR012763
Domain

DNA polymerase III, subunits gamma and tau
TIGR02397	$\"[1-336]T$	dnaX_nterm: DNA polymerase III, subunits ga

noIPR
unintegrated

unintegrated
G3DSA:1.20.272.10	$\"[217-336]T$	no description
G3DSA:3.40.50.300	$\"[1-152]T$	no description
PTHR11669	$\"[71-340]T$	REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT

","BeTs to 18 clades of COG2812COG name: DNA polymerase III, gamma/tau subunitsFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2812 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","***** IPB013748 (Replication factor C) with a combined E-value of 2.5e-11. IPB013748C 94-144***** IPB007758 (Nsp1-like, C-terminal) with a combined E-value of 6.1e-07. IPB007758B 357-394 IPB007758C 511-555 IPB007758C 351-395 IPB007758C 348-392***** IPB009464 (PCAF, N-terminal) with a combined E-value of 2.7e-06. IPB009464A 348-392 IPB009464A 504-548 IPB009464A 511-555 IPB009464A 512-556 IPB009464A 333-377 IPB009464A 355-399 IPB009464A 339-383 IPB009464A 342-386 IPB009464A 363-407 IPB009464A 337-381 IPB009464A 344-388 IPB009464A 494-538 IPB009464A 509-553 IPB009464A 499-543 IPB009464A 353-397 IPB009464A 500-544 IPB009464A 690-734 IPB009464A 338-382 IPB009464A 498-542 IPB009464A 350-394 IPB009464A 334-378 IPB009464A 345-389 IPB009464A 481-525 IPB009464A 490-534 IPB009464A 515-559 IPB009464A 336-380 IPB009464A 486-530 IPB009464A 351-395 IPB009464A 520-564 IPB009464A 921-965 IPB009464A 917-961 IPB009464A 517-561 IPB009464A 648-692 IPB009464A 340-384 IPB009464A 346-390 IPB009464A 518-562 IPB009464A 502-546 IPB009464A 514-558 IPB009464A 341-385 IPB009464A 1027-1071","","","-57% similar to PDB:1JR3 Crystal Structure of the Processivity Clamp Loader Gamma Complex of E. coli DNA Polymerase III (E_value = 8.1E_49);-57% similar to PDB:1XXH ATPgS Bound E. Coli Clamp Loader Complex (E_value = 8.1E_49);-57% similar to PDB:1XXI ADP Bound E. coli Clamp Loader Complex (E_value = 8.1E_49);-63% similar to PDB:1NJF Nucleotide bound form of an isolated E. coli clamp loader gamma subunit (E_value = 5.2E_48);-63% similar to PDB:1NJG Nucleotide-free form of an Isolated E. coli Clamp Loader Gamma Subunit (E_value = 5.2E_48);","Residues 12 to 204 (E_value = 6.4e-06) place ANA_2430 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).","","polymerase III subunit gamma (dnaH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2431","2626494","2627102","609","4.93","-9.69","21989","ATGCCCGCCGTCTACGAAGGCGCCGTCCAGGACCTCATCGACGAGTTCGGCGAGCTGCCCGGTATCGGCCCCAAGTCCGCCCAGCGCATGGCCTTCCACGTCCTGGCCGCCGACGCGGCCGCCGTCGAGCGCCTCATCGAGGCCCTGCGCGCCGTCAAGGCCAAGGTCCGCTTCTGCGAGACCTGCGGCAACATCGCCGAGGCTCCCCAGTGCGCCATCTGCCGCGACCCCCGCCGCGACCAGCGCGTCATCTGCGTCGTCGAGGAGCCCAAGGACGTCGTCGCCATCGAGCGCACCCGCGAGTACCGGGGGCTCTACCACGTGCTCGGCGGTGCCATCGACCCCATCAACGGCGTCGGCCCCGACGACCTGCGCGTGCGCGAGCTCTTCAGCCGTCTGGGGGACGGCGAGGTCGAGGAGGTCATCCTGGCCACCGACCCCGACGTCGTCGGAGAGGCGACCGCCGCCTACCTCACCCGCATGCTGCGCACCATGGCCGTGCCCGTCTCCCGGCTCGCCTCCGGCCTGCCCGTGGGCGCCGACCTGGAGTACGCCGACGAGGTCACCCTCGGGCGGGCCTTCGAGGGCCGACGCCGCGTCGAGGACTGA","MPAVYEGAVQDLIDEFGELPGIGPKSAQRMAFHVLAADAAAVERLIEALRAVKAKVRFCETCGNIAEAPQCAICRDPRRDQRVICVVEEPKDVVAIERTREYRGLYHVLGGAIDPINGVGPDDLRVRELFSRLGDGEVEEVILATDPDVVGEATAAYLTRMLRTMAVPVSRLASGLPVGADLEYADEVTLGRAFEGRRRVED$","Recombination protein RecR","Cytoplasm","recombination protein RecR","recombination protein RecR","recombination protein RecR","","Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Aravind L., Walker D.R., Koonin E.V. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res. 1999. 27(5):1223-1242. PMID: 9973609Provvedi R., Dubnau D. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol. Microbiol. 1999. 31(1):271-280. PMID: 9987128Doherty A.J., Serpell L.C., Ponting C.P. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 1996. 24(13):2488-2497. PMID: 8692686","","","

InterPro
IPR000093
Family

RecR protein
PF02132	$\"[40-81]T$	RecR
TIGR00615	$\"[3-198]T$	recR: recombination protein RecR
PS01300	$\"[59-80]T$	RECR

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[14-33]T$	HhH1

InterPro
IPR006154
Domain

Toprim subdomain
SM00493	$\"[82-167]T$	TOPRIM

InterPro
IPR006171
Domain

TOPRIM
PF01751	$\"[82-175]T$	Toprim

","BeTs to 17 clades of COG0353COG name: Recombinational DNA repair protein (RecF pathway)Functional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0353 is -------q-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000093 (RecR protein) with a combined E-value of 1.6e-80. IPB000093A 12-35 IPB000093B 59-108 IPB000093C 140-158 IPB000093D 167-197 IPB000093B 58-107","","","-67% similar to PDB:1VDD Crystal structure of recombinational repair protein RecR (E_value = 4.9E_56);-51% similar to PDB:1MZJ Crystal Structure of the Priming beta-Ketosynthase from the R1128 Polyketide Biosynthetic Pathway (E_value = 4.9E_56);-51% similar to PDB:1SH0 Crystal Structure of Norwalk Virus Polymerase (Triclinic) (E_value = 4.9E_56);-51% similar to PDB:1SH2 Crystal Structure of Norwalk Virus Polymerase (Metal-free, Centered Orthorhombic) (E_value = 4.9E_56);-51% similar to PDB:1SH3 Crystal Structure of Norwalk Virus Polymerase (MgSO4 crystal form) (E_value = 4.9E_56);","Residues 40 to 81 (E_value = 8.9e-13) place ANA_2431 in the RecR family which is described as RecR protein.Residues 82 to 175 (E_value = 1.3e-15) place ANA_2431 in the Toprim family which is described as Toprim domain.","","protein RecR (recR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2432","2628817","2627393","1425","7.39","1.66","52422","ATGGGCCACGACGACATCGATACGCTACTCAACCTCCCGATCAACGAACGCGGTGAGCGACTGGCTCAGACGCAGGAGAACCAGTGGTTCGAACGCAAATCCATCCGCGTTGACCAGAAGAGCTTCGCCAAGGCCATCATCGGGATGGCGAACGCGGAAGGTGGAACCGTCGTCGTCGGCTTGAGCGAGAAGCGAGTCGAGGGGACCAACTCCACACCCTCTCAAACCAACAGGCTTCGCCAGGTACCGATGACCATGGTGGCTCCACCACTGCGCGTCCACTTCCGGGAGGTCCCGGTGATGAACGACGACGGCACGCAAGACCATCTTCTCGTCGCCCAGGTACCTCCCAGCCGACACGCACACCGGCGCAGTGACGGAACAGCCTTCCTGCGCATGGGCGACTCCACCGTGAAGCTTGACGGCCCGATGTGGGAAGAGCTCGTCTACGACCGGGAGGCCGAGACATATGAGGCCCAGCCCGCCGGTATCACGATGGCTGACCTGAGCGGGAAGGCAATCGATCGACTACGAGCGGAGATCGGCGCACACGGAGACGACAGCCACGTCTTACGCAGCCGCAGCCTCCTGACACAGGACGGCAAGCCCACCATCGCCGCACTCCTGCTCTTCGGCGCTGCACCCGAGCAGCTTCTGCCGCAGGCACTGGTGCGCGTCCTACGCTACCGAGAGGACGAGACAGGCACCGGAGCGCGCCAAACCATGGAGGCCGACGGTGATCGACGCCTCGAGGGCACTATCCCAGACGTCATCGCCAGAGCAGCTGAGCTCATCGATCAGTGGGCCCCCAAGCGCAGGGCCCTGAAGAACGAGGGGACCTTCGGCCCCACGGACATCATCCCCCGGGACGCCTGGCTGGAGGCCGTGGTGAACGCCGTCGTCCACCGCTCTTACTCGATGGCTGGAGACCACATCCGCGTGTCGATCTTCCCCCACCGCATCGAGGTTTCCAGTCCGGGCCGTTTTCCCGGAATGAGCGATCCGAGTCGCCCGCTCGAGATCGCGCGATACGCACGCAACCCGCGCATCGCGAGGGTGTGCGCGGACCTCGGGATCACACAGGAGCTCGGCGAGGGTATTCGACGCATGGTTGACGACATGCGCCGGGCCGGCCTCGCGGACCCTCGCTACCGTCAGACCTCAACCAGTGTCATCGTGAGGCTGGATGCGACGTCGGCCATCTCGAGCGACGTCATGGAGAGGCTGCCTCACGGCTCGCTCGAGGTCGTCACGCTCCTGCGAAGCACCGGACCATTGGGCACGGGGGAGATTGCGTCGGGCGTCAACGCATCCCGCCCTACGGTCCTGCGGTGGCTCAAGACACTGCGCGACGAGGGACTGGTGGAGCGAAGAGGGCAGTCACCCCGAGACCCGCGAGCCACATGGTACGTCCCCGGCACGTGA","MGHDDIDTLLNLPINERGERLAQTQENQWFERKSIRVDQKSFAKAIIGMANAEGGTVVVGLSEKRVEGTNSTPSQTNRLRQVPMTMVAPPLRVHFREVPVMNDDGTQDHLLVAQVPPSRHAHRRSDGTAFLRMGDSTVKLDGPMWEELVYDREAETYEAQPAGITMADLSGKAIDRLRAEIGAHGDDSHVLRSRSLLTQDGKPTIAALLLFGAAPEQLLPQALVRVLRYREDETGTGARQTMEADGDRRLEGTIPDVIARAAELIDQWAPKRRALKNEGTFGPTDIIPRDAWLEAVVNAVVHRSYSMAGDHIRVSIFPHRIEVSSPGRFPGMSDPSRPLEIARYARNPRIARVCADLGITQELGEGIRRMVDDMRRAGLADPRYRQTSTSVIVRLDATSAISSDVMERLPHGSLEVVTLLRSTGPLGTGEIASGVNASRPTVLRWLKTLRDEGLVERRGQSPRDPRATWYVPGT$","ATP-dependent DNA helicase recG","Cytoplasm","ATP-dependent DNA helicase recG, putative","putative transcriptional regulator","AAA-4 family protein","","Poland B.W., Silva M.M., Serra M.A., Cho Y., Kim K.H., Harris E.M., Honzatko R.B. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 1993. 268(34):25334-25342. PMID: 8244965Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 2000. 296(2):569-577. PMID: 10669609","","","

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[55-243]T$	no description

InterPro
IPR001845
Domain

Bacterial regulatory protein, ArsR
PF01022	$\"[414-457]T$	HTH_5

InterPro
IPR007421
Family

ATPase associated with various cellular activities, AAA-4
PF04326	$\"[49-143]T$	AAA_4

","BeTs to 4 clades of COG2865COG name: Predicted transcriptional regulator containing an HTH domain and an uncharacterized domain shared with the mammalian protein SchlafenFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2865 is ----k----d----------u----wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-48% similar to PDB:2FBI The crystal structure of transcriptional regulator PA4135 (E_value = );-54% similar to PDB:1CLQ CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION (E_value = );-54% similar to PDB:1IG9 Structure of the Replicating Complex of a Pol Alpha Family DNA Polymerase (E_value = );-54% similar to PDB:1IH7 High-Resolution Structure of Apo RB69 DNA Polymerase (E_value = );-54% similar to PDB:1Q9X Crystal structure of Enterobacteria phage RB69 gp43 DNA polymerase complexed with tetrahydrofuran containing DNA (E_value = );","Residues 49 to 143 (E_value = 1.3e-06) place ANA_2432 in the AAA_4 family which is described as Divergent AAA domain.Residues 409 to 471 (E_value = 0.0021) place ANA_2432 in the MarR family which is described as MarR family.Residues 410 to 457 (E_value = 5e-05) place ANA_2432 in the HTH_5 family which is described as Bacterial regulatory protein, arsR family.","","DNA helicase recG, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2433","2629192","2630691","1500","4.97","-19.85","51270","ATGGCACTGGTCGTCCAGAAGTACGGCGGCTCGTCCGTCAGCGACGTCGACGCGATGCGGCGCGTCGCCCGGCGCATCGTCGCCACCCGCCAGGCCGGTAACACGGTCGTCGTCGTCGTCTCCGCGATGGGGGACACGACCGACGAGCTCCTTGACCAGGCCGCCGCCCTGACCACCGACGCCCCCGCCCGCGAGATGGACATCCTGCTGTCCGCCGGTGAGCGCATCTCCGTGGCCCTGCTCGCCATGGCCGTCTCCGAGCTCGGAGTCCCGGCGCGCGCCTACACCGGCGCCCAGGCCGGCGTCCTCACCGACTCCAAGTACGGCAAGGCCTCCATCGTCGGCGTGCTGCCCGAGCGCGTGGCCCGCTCCATCCAGACCGGCTCGGTCGCCATCGTCGCCGGCTTCCAGGGCATCAACGAGGTCGAGGACACCACCACCCTGGGCCGCGGCGGCTCCGACACGACCGCGGTCGCCCTGGCCGCGGCCCTCAACGCCGACGTCTGCGAGATCTACACCGACGTCGACGGCCTGTTCACCGCCGACCCCCGCATCGTCCCCACCGCCAAGCGCATCGAGTCCCTCTCCAGCGAGGAGACCCTGGAGCTGGCCGCCCACGGCGCCAAGATCCTCCACCTGCGCGCCGTGGAGTACGCCCGCCGCTTCGGGGTGCCGCTGCACGTGCGCTCCTCCTTCTCCGACAAGACCGGGACCTGGATCTACGACGGCCGCCGCGAGGGCGCCTTCGTGCCCTCGGTCGTGGCCGCCCAGCTTGACGACGTCGTCGCCGCCGACACCGACAGCGCGCCCAGCGCCCCCAGCGCCGCGAGCCCTGCTGCCCCGGCCGCCTCCGCCTCGCCCTCAGACCCCGCCGGGCTCGACGAGGGGCCCTCGGCCTCCGTCGTCGACACCGCGCACCGCAACGCCATCGCAGCGCGGGCCCAGGCCCGCCCCCGCCCGTCCGCCAAGGAGGACCACGTGGAAGCCCCCGTCATCTCCGGAATCGCCCACGACCGCAGCCAGGACAAGATCACGCTCGTGGGCGTGCCCGACGTCCCCGGCGCCGCCGCCCGCATCTTCGCGATCGTGGCCGGCACCGACGCCAACATCGACATGATCGTCCAGGACGTCTCCGCCGAGGGGACGGGCCTGACCAACATCTCCTTCACCTGCCCCGACGGCGACTCCGCCGCCGCCCGCGAGGCCCTCGAGGCCGCCCGCGAGGAGCTGGGCTTCCGAAGCCTGCACTTCAACCCCGACATCGGCATCCTGTCCCTGGTGGGGGCCGGCATGCGCTCCAACCCGGGAGTCTCGGCGCGCCTGTTCGGCTCGCTGAGCGAGGCCGGGGTCAACATCCACATGATCTCCACCTCCGAGATCCGCATCTCGGTGGTGGTCGACGACGCCGTACTCGACGAGGCCGTGCGCGCCGTCCACTCCGCCTTCGGCCTCGACGCCCAGGCCGCCGAGGCGGTCGTCTACGGAGGGACCGGACGATGA","MALVVQKYGGSSVSDVDAMRRVARRIVATRQAGNTVVVVVSAMGDTTDELLDQAAALTTDAPAREMDILLSAGERISVALLAMAVSELGVPARAYTGAQAGVLTDSKYGKASIVGVLPERVARSIQTGSVAIVAGFQGINEVEDTTTLGRGGSDTTAVALAAALNADVCEIYTDVDGLFTADPRIVPTAKRIESLSSEETLELAAHGAKILHLRAVEYARRFGVPLHVRSSFSDKTGTWIYDGRREGAFVPSVVAAQLDDVVAADTDSAPSAPSAASPAAPAASASPSDPAGLDEGPSASVVDTAHRNAIAARAQARPRPSAKEDHVEAPVISGIAHDRSQDKITLVGVPDVPGAAARIFAIVAGTDANIDMIVQDVSAEGTGLTNISFTCPDGDSAAAREALEAAREELGFRSLHFNPDIGILSLVGAGMRSNPGVSARLFGSLSEAGVNIHMISTSEIRISVVVDDAVLDEAVRAVHSAFGLDAQAAEAVVYGGTGR$","Aspartate kinase","Cytoplasm, Membrane","aspartokinase","aspartate kinase ","aspartate kinase","","Rafalski J.A., Falco S.C. Structure of the yeast HOM3 gene which encodes aspartokinase. J. Biol. Chem. 1988. 263(5):2146-2151. PMID: 2892836","","","

InterPro
IPR001048
Domain

Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10	$\"[4-250]T$	no description
PF00696	$\"[2-230]T$	AA_kinase

InterPro
IPR001341
Domain

Aspartate kinase region
TIGR00657	$\"[1-484]T$	asp_kinases: aspartate kinase
PS00324	$\"[5-13]T$	ASPARTOKINASE

InterPro
IPR002912
Domain

Amino acid-binding ACT
PF01842	$\"[343-408]T$ $\"[425-483]T$	ACT

InterPro
IPR012150
Family

Aspartate kinase
PIRSF000726	$\"[3-488]T$	Aspartate kinase

noIPR
unintegrated

unintegrated
PTHR21499	$\"[58-240]T$ $\"[321-495]T$	ASPARTATE KINASE
PTHR21499:SF1	$\"[58-240]T$ $\"[321-495]T$	ASPARTATE KINASE

","BeTs to 24 clades of COG0527COG name: AspartokinasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0527 is aompkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB001341 (Aspartate kinase) with a combined E-value of 2.5e-82. IPB001341A 5-15 IPB001341B 38-48 IPB001341C 67-89 IPB001341D 146-192 IPB001341E 421-458***** IPB001057 (Glutamate 5-kinase) with a combined E-value of 7.3e-11. IPB001057D 150-183","","","-60% similar to PDB:2DTJ Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum (E_value = 1.9E_30);-44% similar to PDB:2HMF Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate (E_value = 1.9E_27);-46% similar to PDB:2CDQ CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA ASPARTATE KINASE COMPLEXED WITH LYSINE AND S-ADENOSYLMETHIONINE (E_value = 1.4E_14);-40% similar to PDB:2J0W CRYSTAL STRUCTURE OF E. COLI ASPARTOKINASE III IN COMPLEX WITH ASPARTATE AND ADP (R-STATE) (E_value = 1.4E_14);-40% similar to PDB:2J0X CRYSTAL STRUCTURE OF E. COLI ASPARTOKINASE III IN COMPLEX WITH LYSINE AND ASPARTATE (T-STATE) (E_value = 1.4E_14);","Residues 2 to 230 (E_value = 1.9e-74) place ANA_2433 in the AA_kinase family which is described as Amino acid kinase family.Residues 343 to 408 (E_value = 1.6e-09) place ANA_2433 in the ACT family which is described as ACT domain.Residues 425 to 483 (E_value = 5.8e-11) place ANA_2433 in the ACT family which is described as ACT domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2434","2630718","2631767","1050","4.97","-13.11","36530","GTGGCCGACGGCGTCTGTGTCGCCGTCGTGGGGGCCACCGGCCAGGTCGGCCGCGTCATGCGCGCCATGCTGGCCGAGCGCGACTTCCCTGCCCGCTCGGTGCGCTTCTTCTCCTCGGCCCGCAGCGCCGGGACCGTCGTGGACTTCCGCGGCGCCCAGGTCGAGGTTGAGGACGTCGCCACCGCGGACCTGAGCGGCATCGACGTCGCTATCTTCTCCGCCGGGGGCGCGGCCTCGCGCGAGCACGCCCCGCGTTTCGCCGAGGCGGGGGCCGTCGTCGTCGACAACTCCTCGGCCTGGCGCAAGGACCCCGAGGTGCCGCTCGTGGTCAGCGAGGTCAACCCGCAGGCGCTGCGCGAGCGCCCCAAGGGCATCATCGCCAACCCCAACTGCACCACCATGGCGGCCATGCCGGCCCTCAAGGTGCTGCACGAGGAGGCCGGGCTCATCCGCCTCATCGTCTCCACCTACCAGGCCGTCTCCGGATCGGGTCGGGCCGGGGTGGCCGAGCTGGCCGGGCAGGTACGCGCCGTCGTGAACGAGGACATGGAGGGCCTGGCCCTGGACGGGCGGGCCGTCGAGTTCCCCGCGCCGGAGGTCTACGTCGACACCATCGCCTTCAACGCCGTGGCCTGGGCCGGGAATGACGCCGGTGACGGCTCCGGTGAGACCGACGAGGAGCAGAAGCTACGCAACGAGTCCCGCAAGATCCTGGGGATCCCGGACCTGCTGGTCTCCGGGACCTGCGTGCGCATCCCGGTGTTCTCCGGCCACGGGCTCAGCATCAACGCCGAGTTCGAGCGCGAGATCAGCGTCGAGCGTGCCCGCGAGCTGCTGGAGGCGGCGCCCGGCGTCACCTACGAAGACGTGCCCAGCCCCCTCAAGGGCGCCGGCCGCGACGGCACCTTCGTGGGGCGCCTGCGCGCCGACCAGGCCTTCGCACCGGGCCACGGCCTGCAGTTCTTCGCCGTGGGGGACAACCTGCGCAAGGGCGCGGCCCTCAACGCCGTCGAGCTGGCTGAGTTGGTGGCCGCCGAGCTGCGGGGCTGA","VADGVCVAVVGATGQVGRVMRAMLAERDFPARSVRFFSSARSAGTVVDFRGAQVEVEDVATADLSGIDVAIFSAGGAASREHAPRFAEAGAVVVDNSSAWRKDPEVPLVVSEVNPQALRERPKGIIANPNCTTMAAMPALKVLHEEAGLIRLIVSTYQAVSGSGRAGVAELAGQVRAVVNEDMEGLALDGRAVEFPAPEVYVDTIAFNAVAWAGNDAGDGSGETDEEQKLRNESRKILGIPDLLVSGTCVRIPVFSGHGLSINAEFEREISVERARELLEAAPGVTYEDVPSPLKGAGRDGTFVGRLRADQAFAPGHGLQFFAVGDNLRKGAALNAVELAELVAAELRG$","Aspartate-semialdehyde dehydrogenase","Cytoplasm","aspartate-semialdehyde dehydrogenase","aspartate-semialdehyde dehydrogenase ","aspartate-semialdehyde dehydrogenase","","Hadfield A., Kryger G., Ouyang J., Petsko G.A., Ringe D., Viola R. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. J. Mol. Biol. 1999. 289(4):991-1002. PMID: 10369777","","","

InterPro
IPR000534
Domain

Semialdehyde dehydrogenase, NAD - binding
PF01118	$\"[6-121]T$	Semialdhyde_dh

InterPro
IPR005986
Family

Aspartate-semialdehyde dehydrogenase, bacterial
TIGR01296	$\"[6-346]T$	asd_B: aspartate-semialdehyde dehydrogenase

InterPro
IPR012080
Family

Aspartate-semialdehyde dehydrogenase
PIRSF000148	$\"[4-349]T$	Aspartate-semialdehyde dehydrogenase

InterPro
IPR012280
Domain

Semialdehyde dehydrogenase, dimerisation region
PF02774	$\"[140-330]T$	Semialdhyde_dhC

noIPR
unintegrated

unintegrated
G3DSA:3.30.360.10	$\"[130-344]T$	no description
PTHR10174	$\"[7-170]T$ $\"[203-348]T$	RETINALDEHYDE BINDING PROTEIN-RELATED
PTHR10174:SF2	$\"[7-170]T$ $\"[203-348]T$	ASPARTATE SEMIALDEHYDE DEHYDROGENASE

","BeTs to 24 clades of COG0136COG name: Aspartate-semialdehyde dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0136 is aompkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB000319 (Aspartate-semialdehyde dehydrogenase) with a combined E-value of 7e-69. IPB000319A 7-18 IPB000319B 94-114 IPB000319C 149-170 IPB000319D 213-239 IPB000319E 245-268 IPB000319F 290-310 IPB000319G 322-333***** IPB012280 (Semialdehyde dehydrogenase, dimerisation region) with a combined E-value of 1.2e-22. IPB012280A 94-114 IPB012280B 126-143 IPB012280C 154-164***** IPB000173 (Glyceraldehyde 3-phosphate dehydrogenase) with a combined E-value of 2e-06. IPB000173B 66-102 IPB000173C 125-167","","","-55% similar to PDB:2GYY Structure of aspartate semialdehyde dehydrogenase (ASADH) from Streptococcus pneumoniae (E_value = 7.0E_47);-55% similar to PDB:2GZ1 Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with NADP (E_value = 7.0E_47);-55% similar to PDB:2GZ2 Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with 2',5'-ADP (E_value = 7.0E_47);-55% similar to PDB:2GZ3 Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with NADP and aspartate-semialdehyde (E_value = 7.0E_47);-46% similar to PDB:2HJS The structure of a probable aspartate-semialdehyde dehydrogenase from Pseudomonas aeruginosa (E_value = 8.4E_24);","Residues 6 to 121 (E_value = 2.6e-46) place ANA_2434 in the Semialdhyde_dh family which is described as Semialdehyde dehydrogenase, NAD binding domain.Residues 140 to 330 (E_value = 5.9e-63) place ANA_2434 in the Semialdhyde_dhC family which is described as Semialdehyde dehydrogenase, dimerisation domain.","","dehydrogenase (asd)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2435","2632666","2631884","783","6.52","-2.17","27769","ATGAAGAGCAACGAGTCGCTTCAACAGGTGCGACCCCCATTCGCTATGGCGCTCACAGCAGTTTTCGCGTCGCTACTCGCCTCCACGACAAGCGCGGATCACCCCGGAAACCCATTGATCCTCATCCCTCTTCTGATGCTTCTCCCATGGGTCACCTGGAATCACCCACCCAGCCTGGCAACCTCTGGGGCGATGCTGTTGACAGTGAGCATCCTGGCACCGTACAGCAGCGACGGGCCGAGCGACCTTTATCTCGCTTACAGGACTCTATGGTTCTTCGCCGGCCTGCTCCTGGGAGCGGCGCTCGCTCTCATTATGGGAGAGCGCATACGCTCGTGGCACCCGCACATACGTGGGTGGCGATACGCTCTTCATCCTGCACGGATCGCCGCAGCCGCAACCGGAATCATCGTCGTTCTCGCCCTCTTTAAACCATCACCCCAGTCATCGCAGATCGAACAGACTCAGGCAGCCACGAACAACGATACAGTAATATTTTGGCTCGCAGCCGGCCTGTTCATCACTTTACTGGCGTCCATCTCCCCCACAGCGACCATGATCTGCTTGATCGCCTTCATCTCCATTCACGGTGTCACTACCCATGCACCTTTTCCAAACGCAAGCGCCGTCTTCGTTCTCATTCTCTTCACGCCAGCGATCATCGGCCCCCTGTTCCTTCCTCGGGACCTCACCGCGCATGAGGCCGAGGAATCCGACACCAGCACCGATGCCTCGGTTATCCCGCCCCCCACCTCCGAGGCCTCACCAAAGGAGGCATCGTGA","MKSNESLQQVRPPFAMALTAVFASLLASTTSADHPGNPLILIPLLMLLPWVTWNHPPSLATSGAMLLTVSILAPYSSDGPSDLYLAYRTLWFFAGLLLGAALALIMGERIRSWHPHIRGWRYALHPARIAAAATGIIVVLALFKPSPQSSQIEQTQAATNNDTVIFWLAAGLFITLLASISPTATMICLIAFISIHGVTTHAPFPNASAVFVLILFTPAIIGPLFLPRDLTAHEAEESDTSTDASVIPPPTSEASPKEAS$","Hypothetical protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[15-49]?$ $\"[55-75]?$ $\"[84-104]?$ $\"[123-143]?$ $\"[164-193]?$ $\"[207-227]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-54% similar to PDB:1QS0 CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA 2-OXOISOVALERATE DEHYDROGENASE (BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE, E1B) (E_value = );-54% similar to PDB:2BP7 NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1) (E_value = );-54% similar to PDB:1E15 CHITINASE B FROM SERRATIA MARCESCENS (E_value = );-54% similar to PDB:1E6N CHITINASE B FROM SERRATIA MARCESCENS INACTIVE MUTANT E144Q IN COMPLEX WITH N-ACETYLGLUCOSAMINE-PENTAMER (E_value = );-54% similar to PDB:1E6P CHITINASE B FROM SERRATIA MARCESCENS INACTIVE MUTANT E144Q (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2436","2633827","2633072","756","6.04","-1.56","27113","ATGCCGACTGACATCAGCCCGGGCACTCGGCTGCGGGCGTGGGAGCGGGCCGCGGAGTGGCCGCTGGCCGGTGCCGCCGTCGTCTTCCTGGGCGCCTATGCCTGGGAGGTACTCACCAACGCACAGGGCGGCGCCAAGGAGACGGCCGAGTTCGTGATCGGCGCCGTGTGGGCACTGTTCGGCCTCGACTATCTTGTCCGCCTGGTCCTGGCGCCGAGCCGGGGCCGCTGGTTTTTCCGCCACCTGCCCGACCTGGCGATCATTGTCCTGCCGATCCTGCGGCCGCTCAGGCTCCTGCGCCTGGTGACGCTCGTGAGCATCATGCAGCGCAGCGCCGGCACCGCGCTGCGCGGGCGGATCACCCTGTACACGGCCGGCAGCGCCGCCCTGCTCGTCTTCACCTCGGCACTGGCCGTGCTGGATGCGGAGCGTCATGAGCCGGGCTCCTCGATCCAGTCCTTCGGCCGGGCCCTGTGGTGGGCGCTGACGACGATCACCACCGTCGGCTACGGCGACACCTTCCCGGTCTCCACGCAGGGTCGTTTCATCGCGGCGCTGCTCATGATCGGTGGGGTGGCACTGGCCGGCGTCGTCACGGCGACCCTGGCCTCGTGGATCGTCTCGCTGGTCGAGGAGGAGAACGCCGAGCAGGAGGCCGCCACGCAGGCGCAGGTGGCAGCCCTGCAGCAGCAGGTCAGTGAGCTGAGCGAGCGCATCGACCGTCTTCTGGCGGAACGCGACTCGGACCGTGGATAG","MPTDISPGTRLRAWERAAEWPLAGAAVVFLGAYAWEVLTNAQGGAKETAEFVIGAVWALFGLDYLVRLVLAPSRGRWFFRHLPDLAIIVLPILRPLRLLRLVTLVSIMQRSAGTALRGRITLYTAGSAALLVFTSALAVLDAERHEPGSSIQSFGRALWWALTTITTVGYGDTFPVSTQGRFIAALLMIGGVALAGVVTATLASWIVSLVEEENAEQEAATQAQVAALQQQVSELSERIDRLLAERDSDRG$","Voltage-gated potassium channel protein","Membrane, Cytoplasm","possible voltage-gated potassium channelprotein","putative ion transport integral membrane protein","Ion transport 2 domain protein,","","Choe S. Potassium channel structures. Nat Rev Neurosci 2002. 3(2):115-121. PMID: 11836519","","","

InterPro
IPR013099
Domain

Ion transport 2
PF07885	$\"[127-208]T$	Ion_trans_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.70	$\"[114-216]T$	no description
PTHR11537	$\"[14-220]T$	VOLTAGE-GATED POTASSIUM CHANNEL
PTHR11537:SF13	$\"[14-220]T$	gb def: Putative ion transport integral membrane protein
tmhmm	$\"[21-41]?$ $\"[51-71]?$ $\"[120-140]?$ $\"[156-176]?$ $\"[186-206]?$	transmembrane_regions

","BeTs to 16 clades of COG1226COG name: Kef-type K+ transport systems, predicted NAD-binding componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1226 is aompkzyqvdrlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is 1","***** IPB003091 (Potassium channel signature) with a combined E-value of 7.7e-15. IPB003091C 51-74 IPB003091G 151-173 IPB003091H 180-206***** IPB013821 (KCNQ voltage-gated potassium channel, C-terminal) with a combined E-value of 4.3e-09. IPB013821D 150-180***** IPB013099 (Ion transport 2, bacterial) with a combined E-value of 4.2e-08. IPB013099 159-175***** IPB011996 (SK channel region) with a combined E-value of 6.9e-06. IPB011996D 153-204","","","-56% similar to PDB:2ATK Structure of a mutant KcsA K+ channel (E_value = 3.1E_11);-56% similar to PDB:1J95 KCSA potassium channel with TBA (tetrabutylammonium) and potassium (E_value = 4.0E_11);-56% similar to PDB:1JVM KCSA POTASSIUM CHANNEL WITH TBA (TETRABUTYLAMMONIUM) AND RUBIDIUM (E_value = 4.0E_11);-56% similar to PDB:1K4C Potassium Channel KcsA-Fab complex in high concentration of K+ (E_value = 4.0E_11);-56% similar to PDB:1K4D Potassium Channel KcsA-Fab complex in low concentration of K+ (E_value = 4.0E_11);","Residues 51 to 206 (E_value = 0.0013) place ANA_2436 in the Ion_trans family which is described as Ion transport protein.Residues 127 to 208 (E_value = 2e-17) place ANA_2436 in the Ion_trans_2 family which is described as Ion channel.","","voltage-gated potassium channel protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2438","2637221","2636157","1065","8.06","4.18","38094","ATGGGCGTGAGGCACCCGCCACCCCCAGACTTGACTCGCCAGCCACAACCGACCCGCCATCAGTCCTCAGGAGGGCACCCCATGGCGATCTATCTCCGTTCGCGCCCCACCACGAAGACCAGGGCGCTCGGGTGCCTGTGTGCTCTCACTACCATCGGCATGACGCTCCTCTACCCGGCCGCCCTGCTCCTGACCCCCTCCATCCCGAACCCTCTGACCGAACTCGTCGCCAACGAAAACGGGAATCTGGAGTTGCAGTCCTTATCCGTTCTGATCGGCGTCATGACCGTCTACAATTTCATACTGTTCGCCACGATCTTCGGTGCACTCTCCGGATTCAGGGGCATGGACCAGCGCTTACCCAAGGACTCGACGGTCACCCATCGCGATATCGCATCGGCACGGTTCCTTCACATCTCCCAGAGCCCAAGCAGGCGCATCGTGGGCATGCTGTTGGCGGTGCTTGCGGTCATGCTGGGCGAGGTATGTCCAGCTATCGCAATAACCATCCCACACCTCCTGATCACCGACGATTCAACCCCAGCGCTGGAGCAGGCTGCCGTCATAGGCACGGTCTGCCTTACCATCGGACTGTTTGCGGCATTGGTGTCGGCCGCCTCGCGTCGGGAGAAGATCGCGGTGTGCCTGACGCCGCAGTGCATGGCGGTTGTCAAATCATTTCCTCTCTTCCTCCCCCTGCCTTCCGGCCGCAACGACCTCAGCATCCAGGAGGTCCCGGCATACTGGGGTCGCGTGAAGATCCAAGCCGTCTATGCCCCACCCACCGGAGGCGCCCAGCCGGCCAGACCAGTTCTCCTCTCGCAGCTCGGCCTGACGGTGAAGTCCTCACAGCTCAACGACGCCCGTTCCCGGGTCGAGGCCCGGCTCGACGAGGTCTGGCGGGCCGCACAGCTGATACGCACCCCGCCCGAGCGGGAGGAGACGGCCGACGCCCCGACATCGGAGGCTGAGACGAATCCGACTCACCAGTTATCACCCGCACCACCGCACCACGATGCAGCCCCTGAGCACATCCAGTCCCAGGCAGAGAACCCTCTCACTTGA","MGVRHPPPPDLTRQPQPTRHQSSGGHPMAIYLRSRPTTKTRALGCLCALTTIGMTLLYPAALLLTPSIPNPLTELVANENGNLELQSLSVLIGVMTVYNFILFATIFGALSGFRGMDQRLPKDSTVTHRDIASARFLHISQSPSRRIVGMLLAVLAVMLGEVCPAIAITIPHLLITDDSTPALEQAAVIGTVCLTIGLFAALVSAASRREKIAVCLTPQCMAVVKSFPLFLPLPSGRNDLSIQEVPAYWGRVKIQAVYAPPTGGAQPARPVLLSQLGLTVKSSQLNDARSRVEARLDEVWRAAQLIRTPPEREETADAPTSEAETNPTHQLSPAPPHHDAAPEHIQSQAENPLT$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[42-62]?$ $\"[88-110]?$ $\"[147-167]?$ $\"[186-206]?$	transmembrane_regions

InterPro
IPR005746
Family

Thioredoxin
TIGR01068	$\"[50-148]T$	thioredoxin: thioredoxin

InterPro
IPR006662
Domain

Thioredoxin-related
PR00421	$\"[65-73]T$ $\"[73-82]T$ $\"[112-123]T$	THIOREDOXIN
PS00194	$\"[66-84]T$	THIOREDOXIN

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[45-148]T$	no description

InterPro
IPR013766
Domain

Thioredoxin domain
PF00085	$\"[46-147]T$	Thioredoxin

InterPro
IPR015467
Domain

Thioredoxin family
PTHR10438	$\"[55-148]T$	THIOREDOXIN-RELATED

noIPR
unintegrated

unintegrated
PTHR10438:SF11	$\"[55-148]T$	gb def: Thioredoxin

","BeTs to 21 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones] Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","***** IPB006662 (Thioredoxin type domain) with a combined E-value of 6.9e-24. IPB006662A 65-82 IPB006662B 98-134","","","-58% similar to PDB:1RQM SOLUTION STRUCTURE OF THE K18G/R82E ALICYCLOBACILLUS ACIDOCALDARIUS THIOREDOXIN MUTANT (E_value = 1.3E_16);-58% similar to PDB:1NSW The Crystal Structure of the K18G Mutant of the thioredoxin from Alicyclobacillus acidocaldarius (E_value = 1.6E_16);-57% similar to PDB:1NW2 The crystal structure of the mutant R82E of Thioredoxin from Alicyclobacillus acidocaldarius (E_value = 1.1E_15);-57% similar to PDB:1QUW SOLUTION STRUCTURE OF THE THIOREDOXIN FROM BACILLUS ACIDOCALDARIUS (E_value = 1.4E_15);-57% similar to PDB:2GZY solution structures of the reduced form of thioredoxin from Bacillus subtilis (E_value = 2.4E_15);","Residues 46 to 147 (E_value = 1.3e-24) place ANA_2439 in the Thioredoxin family which is described as Thioredoxin.","","isomerase and thioredoxins (TRX2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2440","2638114","2639052","939","6.80","-1.29","33512","ATGGCCCGCGTGAAGTTGGAGTCCCACGTCAGCCACGCTGTCAGAGCCCGATGGGCGGTCCCCGTCGGTGCCTCGGGCCGCGACGCGTTGGTGCGCCACCTCGTCTATGCCTTCCTGCGCTCCGACCCCGAGGGGGCCACGGACTGGATCGACTCGACGGTCCCCACCGACCCCGACGAGCTGCGCACCATGCTCGACTTCCTCCTCACTGCCCGCCCCCCGGCCCCCCTGCCCGAGGACATTGCCGCCGACCTCGACACCCTCCTGGAGGCTGAGGCCGCCGAGCGCGGCATGGTCGACGCCACCGAGATCCCGCCCCTGGCCATCACCGATCACGTTCCCGGCCTGCTGGGCCGCAACGTGGCCTTCTGGCGCGGCGACCTCACCCGGCTGCGCGCCGGCGCCGTCCTCAATGCCGCGAACTCCGGGATGCTCGGCTGCTTCGCCCCCGGGCACCGCTGCATCGACAACATCATCCACGCCGTCGCCGGGCCGGCCCTGCGCGCCGAGTGCGCCCGCTACATGACCTGGGCGGAGACCTTCGACCCCACCCGTCGCCAGGGCGGGGAGCCCGCCGGCCGGGCCGTCTTCACCGGCGGATACCACCTGCCGGCCCAGCACGTCATCCACTCGGTGGGGCCCGTCATCGAGGACGGGCGCAAACCGACCCTGCATGACCGGCGCCTGCTGTCCTCGTGCTACACGAGCGTCCTCAACGTCGCGCACGCCGCCGGGCTGGGCAGCGTCGGCCTGTGCTCGCTGTCCACGGGCGTCTTCGGCTACCCCAAGCGGCAGGCCGCGCTGGTGACCCTGGAGACGATCGGCCGCTGGCTGGCGGCCCACCCCGACTCCCGGATGCGCATCGTCATCAGCCTCAACGCCGACGTCGACGTCGCCGCCTACGAGGCCGCCCTCGCCCCGCCGCCCTGGCGGCCGTAG","MARVKLESHVSHAVRARWAVPVGASGRDALVRHLVYAFLRSDPEGATDWIDSTVPTDPDELRTMLDFLLTARPPAPLPEDIAADLDTLLEAEAAERGMVDATEIPPLAITDHVPGLLGRNVAFWRGDLTRLRAGAVLNAANSGMLGCFAPGHRCIDNIIHAVAGPALRAECARYMTWAETFDPTRRQGGEPAGRAVFTGGYHLPAQHVIHSVGPVIEDGRKPTLHDRRLLSSCYTSVLNVAHAAGLGSVGLCSLSTGVFGYPKRQAALVTLETIGRWLAAHPDSRMRIVISLNADVDVAAYEAALAPPPWRP$","Appr-1-p processing domain protein","Cytoplasm","Unknown","hypothetical protein","Appr-1-p processing domain protein","","","","","

InterPro
IPR002589
Domain

Appr-1-p processing
PF01661	$\"[137-270]T$	A1pp
PS51154	$\"[108-309]T$	MACRO

noIPR
unintegrated

unintegrated
G3DSA:3.40.220.10	$\"[117-305]T$	no description
PTHR11106	$\"[120-305]T$	GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED

","BeTs to 10 clades of COG2110COG name: Uncharacterized ACR related to the C-terminal domain of histone macroH2A1Functional Class: S [Function unknown]The phylogenetic pattern of COG2110 is a--pkzyqvdrl--ef-----j----Number of proteins in this genome belonging to this COG is 2","***** IPB002589 (Protein of unknown function Appr-1) with a combined E-value of 1.7e-14. IPB002589A 126-154 IPB002589B 205-214 IPB002589C 249-262","","","-53% similar to PDB:1SPV Crystal Structure of the Putative Phosphatase of Escherichia coli, Northeast Structural Genomoics Target ER58 (E_value = 9.1E_19);","Residues 137 to 270 (E_value = 2.9e-38) place ANA_2440 in the A1pp family which is described as Appr-1-p processing enzyme family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2441","2640800","2639262","1539","5.68","-8.65","52035","TTGGGAATCAGTTCCGCCCGGTACGGCTCACCGGCCCGAACCGGCCCTGACCAGTTCATCGACAGGATCACCGTGACTCAGCAACCGCAGCCCGCCGGCCGGCCCTCCAGTGCCACCGCCTCCACCAACACCTCCCTGTTCGAGGCGGCTCGCGCCGTCATCCCCGGGGGCGTCGACTCCCCCGTGCGCGCCTTCGGCTCGGTGGGTGGCACGCCGCGGTTCATCGCCTCGGCGAGCGGTGCCCACGTCACCGATGCCGAGGGCCGCAGCTACGTGGACCTGGTGGGCTCGTGGGGCCCGGCACTCCTGGGCCACGCCCACCCGGAGGTCGTCGCCACGGTACAGGCCGCCGCCGCCCGCGGCCTGTCATTCGGTGCCCCCACCGCCACAGAGACGCTCCTGGCCGAGGAGGTGCGCCGCCGGGTGCCGGCCGCACAGAAGGTGCGCTTCGTGTCCACCGGCACCGAGGCGACGATGACGGCCGTGCGCCTGGCCCGCGGCGCCACGGGCCGCGACCTGGTGGTGAAGTTCGCCGGCTGCTACCACGGGCACAGTGACGGCCTGCTCGCGGCGGCCGGCTCGGGCCTGGCCACCGGCGGCCTGCCGGGCAGCGCCGGCGTACCCGCGGCGGTGGCCGCCCAGACCATCGTCCTGCCCTATAACGACGTCGCCGCCCTGGAGGCCTGCTTCGCCGAGCGCGGCGCCGAGATCGCCGCGGTCATCACCGAGGGCGCCCCGGCCAACATGGGGATCGTGCCACCGGCGCCCGGCTTCAACGCCGCGATCCGCCGAGTGACCGCCGAGCACGGCGCGCTCATGATCCTCGATGAGGTCCTCACTGGCTTCCGCGTGGGCCCGGCCGGCTGGTGGGGCCTGGAGGCCGTCGACGGCTGGACCTCGGACCTGCCGGTCTTCGCCACCGCCGGCGCCGCTGCTTCTGAGCGCGCCGGCGCCGGCACCCCCTCCTGGCCGGGCGCCGAATGGCGCGAGCGCGCTACCTGGGTGCCGGACCTGGTGACCTTCGGGAAGGTCGTGGGCGGCGGGATGCCGCTGGCCGCCGTCGGCGGGCGCACGGAGGTCATGGACCTGCTGGCGCCGGACGGCCCCGTCTACCAGGCGGGCACGCTCTCGGGGAACCCGCTGGCCACGGCGGCCGGCCTGGCCACGCTCCAGCTGGCCGACGACGCCATCTACGCCTCGGTGGCCGAGCATGCCCGGACCATCGGCGAGGTGGTCTCGGCGGCCCTGAACGAGCAGGGCGTGCCCCACCGCGTGCAGCGGGCGGGCTCGCTGTTCTCCTTCATGTTCGGGCAGCGGGCCGCCGAGCAGGGCGTGAGCGACTACGAGGCCGCTCGCGCCCAGGAGACCTGGCGCTACGGGCCCTTCTTCCACGCCTTCCTCGAGGCGGGGGTGGGCCTGCCGCCGTCGGTCTTCGAGGCCTGGTTCGTCTCGGCCGCGCACGGCGAGGCGGAGCTGGAGGCGATCGCGTCTGCGGCCCCGGCGGCCGCCCGCGCCGCGGCCCGGGCCCAGGCGAGCTGA","LGISSARYGSPARTGPDQFIDRITVTQQPQPAGRPSSATASTNTSLFEAARAVIPGGVDSPVRAFGSVGGTPRFIASASGAHVTDAEGRSYVDLVGSWGPALLGHAHPEVVATVQAAAARGLSFGAPTATETLLAEEVRRRVPAAQKVRFVSTGTEATMTAVRLARGATGRDLVVKFAGCYHGHSDGLLAAAGSGLATGGLPGSAGVPAAVAAQTIVLPYNDVAALEACFAERGAEIAAVITEGAPANMGIVPPAPGFNAAIRRVTAEHGALMILDEVLTGFRVGPAGWWGLEAVDGWTSDLPVFATAGAAASERAGAGTPSWPGAEWRERATWVPDLVTFGKVVGGGMPLAAVGGRTEVMDLLAPDGPVYQAGTLSGNPLATAAGLATLQLADDAIYASVAEHARTIGEVVSAALNEQGVPHRVQRAGSLFSFMFGQRAAEQGVSDYEAARAQETWRYGPFFHAFLEAGVGLPPSVFEAWFVSAAHGEAELEAIASAAPAAARAAARAQAS$","Glutamate-1-semialdehyde-2,1-aminomutase","Cytoplasm, Extracellular","glutamate-1-semialdehyde-2,1-aminomutase","glutamate-1-semialdehyde-2;1-aminomutase ","glutamate-1-semialdehyde-2,1-aminomutase","","Yonaha K., Nishie M., Aibara S. The primary structure of omega-amino acid:pyruvate aminotransferase. J. Biol. Chem. 1992. 267(18):12506-12510. PMID: 1618757","","","

InterPro
IPR004639
Family

Tetrapyrrole biosynthesis, glutamate-1-semialdehyde aminotransferase
TIGR00713	$\"[42-509]T$	hemL: glutamate-1-semialdehyde-2,1-aminomut

InterPro
IPR005814
Family

Aminotransferase class-III
PTHR11986	$\"[60-294]T$ $\"[334-510]T$	AMINOTRANSFERASE CLASS III
PF00202	$\"[74-438]T$	Aminotran_3

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[108-306]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[369-506]T$	no description

noIPR
unintegrated

unintegrated
PTHR11986:SF5	$\"[60-294]T$ $\"[334-510]T$	GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE

","BeTs to 19 clades of COG0001COG name: Glutamate-1-semialdehyde aminotransferaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0001 is aomp-z-q-dr-bcefghsnuj-i--Number of proteins in this genome belonging to this COG is 2","***** IPB005814 (Aminotransferase class-III) with a combined E-value of 1.1e-51. IPB005814A 77-114 IPB005814B 152-166 IPB005814C 258-286 IPB005814D 336-350 IPB005814E 372-390","","","-51% similar to PDB:2GSA CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE, WILD-TYPE FORM) (E_value = 3.1E_81);-51% similar to PDB:3GSB CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE IN COMPLEX WITH GABACULINE (E_value = 3.1E_81);-51% similar to PDB:4GSA CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE (E_value = 3.1E_81);-51% similar to PDB:2HOY Inter-subunit signaling in GSAM (E_value = 5.4E_81);-51% similar to PDB:2HOZ Inter-subunit signaling in GSAM (E_value = 5.4E_81);","Residues 74 to 438 (E_value = 3.3e-70) place ANA_2441 in the Aminotran_3 family which is described as Aminotransferase class-III.","","(hemL) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2442","2641886","2640837","1050","4.99","-15.42","37085","ATGACTGACGCCCTCCGACCGGCCGCCGACTTCCTGTCGCGCCGCTCCGTCCCCGACCCGCAGGCCCCCACGGTCCGCCCCCGGCGCCTGCGCACCACTCCCGCGATGCGGCGCCTGGCGCGCGAGCACGTCGTGGACCCGGCCGCCCTCATCCTGCCGGTGTTCGTGCGCGAGGACATCGACACCCCCCGCCCCGTGGAGGCGATGCCAGGCGTCGTCCAGCACACGCTGGACTCGCTGCGCAGGGAGGCCGCCGCCTGCGCCGAGGCCGGCATCGGCGCCATCGACCTGTTCGGCGTTCCCGCCACCCGCGACGAGGCCGGCACGGCGGCCTGGGCCGAGGACGGCATCCTCAACCGCGGGATCGCGGCCGTGCGCGCGGAGGTGGGGGACGAGGTCGTCGTGTGCGCGGACACCTGCCTGGACGAGTTCACCAGCCACGGCCACTGCGGCCTCATCCGCCCCGACGGCCCGCGCGCCGGCGAGGTAGACAACGACGCCACCCTGGCCACCTACCAAGCCATGGCCGTCTCCCAGGCGGAGGCCGGGGCGCACATGGTCTCACCCTCGGGGATGATGGACGGGCAGGTCGCCGCGATCCGCGCCGCCCTGGACGCCACCGGCCACGACGACGTCGCGATCCTGGCCTACTCGGCGAAGTACGCCTCGGCCTACTTCGGGCCGTTCCGGGAGGCCGTGGGCTCCACGCTCACCGGGGACCGGCGCGCCTACCAGCAGGATCCGGCCAACCGCCGCGAGGGCATGCGCGAGGTGATGCTCGACGTCGCCGAGGGGGCGGACATCGTCATGGTCAAGCCGGCCGGCCCCTACCTGGACGTGCTGGCCGACGTCGCCGCCGCCTCCCCGGTGCCGGTGGCGGCCTACCAGGTCAGCGGCGAGTACGCGATGGTGGAGGCGGCCGCGCAGCGCGGGTGGATCGACCGCGAGCGCGTCATCGCCGAGTCGGTGCTGGGCATCGTGCGGGCGGGCGCCGACATGGTTCTGACCTACTGGGCCCGGGAGATCGCCGAGAACTCGGCCCTGCACTGA","MTDALRPAADFLSRRSVPDPQAPTVRPRRLRTTPAMRRLAREHVVDPAALILPVFVREDIDTPRPVEAMPGVVQHTLDSLRREAAACAEAGIGAIDLFGVPATRDEAGTAAWAEDGILNRGIAAVRAEVGDEVVVCADTCLDEFTSHGHCGLIRPDGPRAGEVDNDATLATYQAMAVSQAEAGAHMVSPSGMMDGQVAAIRAALDATGHDDVAILAYSAKYASAYFGPFREAVGSTLTGDRRAYQQDPANRREGMREVMLDVAEGADIVMVKPAGPYLDVLADVAAASPVPVAAYQVSGEYAMVEAAAQRGWIDRERVIAESVLGIVRAGADMVLTYWAREIAENSALH$","Delta-aminolevulinic acid dehydratase","Cytoplasm","delta-aminolevulinic acid dehydratase","delta-aminolevulinic acid dehydratase ","Porphobilinogen synthase","","","","","

InterPro
IPR001731
Family

Tetrapyrrole biosynthesis, porphobilinogen synthase
PD002304	$\"[35-343]T$	Q8FSE1_COREF_Q8FSE1;
PR00144	$\"[141-155]T$ $\"[176-195]T$ $\"[214-233]T$ $\"[265-281]T$ $\"[290-305]T$ $\"[320-339]T$	DALDHYDRTASE
PIRSF001415	$\"[25-349]T$	Porphobilinogen synthase
PTHR11458	$\"[26-344]T$	PORPHOBILINOGEN SYNTHASE
PF00490	$\"[22-346]T$	ALAD
PS00169	$\"[265-277]T$	D_ALA_DEHYDRATASE

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[15-347]T$	no description

","BeTs to 21 clades of COG0113COG name: Delta-aminolevulinic acid dehydrataseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0113 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB001731 (Delta-aminolevulinic acid dehydratase) with a combined E-value of 6.5e-112. IPB001731A 26-53 IPB001731B 80-101 IPB001731C 131-148 IPB001731D 163-213 IPB001731E 239-282 IPB001731F 311-339","","","-60% similar to PDB:1B4E X-RAY STRUCTURE OF 5-AMINOLEVULINIC ACID DEHYDRATASE COMPLEXED WITH THE INHIBITOR LEVULINIC ACID. (E_value = 1.2E_67);-60% similar to PDB:1I8J CRYSTAL STRUCTURE OF PORPHOBILINOGEN SYNTHASE COMPLEXED WITH THE INHIBITOR 4,7-DIOXOSEBACIC ACID (E_value = 4.7E_67);-60% similar to PDB:1L6S Crystal Structure of Porphobilinogen Synthase Complexed with the Inhibitor 4,7-Dioxosebacic Acid (E_value = 4.7E_67);-60% similar to PDB:1L6Y Crystal Structure of Porphobilinogen Synthase Complexed with the Inhibitor 4-Oxosebacic Acid (E_value = 4.7E_67);-59% similar to PDB:1W1Z STRUCTURE OF THE PLANT LIKE 5-AMINO LAEVULINIC ACID DEHYDRATASE FROM CHLOROBIUM VIBRIOFORME (E_value = 1.7E_64);","Residues 22 to 346 (E_value = 1.3e-175) place ANA_2442 in the ALAD family which is described as Delta-aminolevulinic acid dehydratase.","","acid dehydratase (hemB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2443","2643376","2642195","1182","7.77","2.60","39867","ATGGCGCAGTCCACCTCACGCACTGACTCGGCCGGGGGCGTGCCGGGCCTGCCCCGGGAAGACGGCGGAGCACCGCTGTCGGGGCGGGTGGTTCTGCTGCCGCGCCTCAAGGAGCGCGACCGCATCGCCTCGGCGCTGGAGCGGGCCGGGGCTCGGGTGCTGCGCGCCGCCGTGACGCGGACGGTTCCGGGTGAGGCGGCGGCGCTGGGGGCGACTGCGCGCAGGATCGCGGCGGGCAAGGCGGCCTGGCTGGTGCTCACCTCGGCCCGGACGGTTGAGGCGCTGGCGCCGTACCTGCTTGCGGAAGCCGCCTCGGCGACCGGAGACCAGGCCCTCCATCAGGAAGCCGGCACGTCCGGCCCCCACGACGGCTCCGTGCCTCCCCACACCCCAATCACCCCACCGGGACAGCACCAACCACGCTCAAGCATCCCGCCGATGCGGGTGGCTGTCGTCGGTCCAGCGACAGCACGTGCGTGGACCAAGTTCACCGGGACCGCCCCCGACCTGGTGGCCCGAGGATCGGCCGCCGCCCTCCTGAAGGAGCCCGCGTTCGCCGGAAGCCCAGCAACCGGAGACCACGCGCCCTACCAGGAACCCGACATTCCCAACACCCACCACGGCACCCCGCCACCCCACGCCCCAGCACGGATCCCGGAATCGAAGACAGCCCCTCGAGGCCTCCCCGGGGGTGTCACCGGCCCGCATGACTCCAGCTGGAGGGCTCATGCCTCCGACGATTCTCCCGCTCGGCTTCGAACCGCTCCGGAGGCGGCACGGCGCGTGCTGCTGCCGGCCTCGGCTCTGGCCGACCCGGCACTGGCGGACGGCCTGCGTCGAGCGGGCTGGGAGGTGGAGCAGGTGGCCGCCTACACGACCGTCACGGCTGACGCCTGCAACCTGCCCCCGGACCTGGAGCACAGGTGGGCCACTGGCGGTGTGGACGCGGTCGTGCTCACCGCCCCGTCCACGACGCGGGCCGTCCTGGAGCTGCTCGGCCCACCGCCGCAGGGAACCGGGCTGGTGGCCATTGGCGCCACCACGGCGGCGGCCACCCGCGAGCTCGGTCTGACGGTTGCTGCCGTCGCCCCCTCCCCCACGCCCGAGGGGGTCCTCCAGGCCACCATCGACGCCATCCGGGCCACCGCGGGCCCCACCCCTCCCCCTCAGGAGCCGCCGTGA","MAQSTSRTDSAGGVPGLPREDGGAPLSGRVVLLPRLKERDRIASALERAGARVLRAAVTRTVPGEAAALGATARRIAAGKAAWLVLTSARTVEALAPYLLAEAASATGDQALHQEAGTSGPHDGSVPPHTPITPPGQHQPRSSIPPMRVAVVGPATARAWTKFTGTAPDLVARGSAAALLKEPAFAGSPATGDHAPYQEPDIPNTHHGTPPPHAPARIPESKTAPRGLPGGVTGPHDSSWRAHASDDSPARLRTAPEAARRVLLPASALADPALADGLRRAGWEVEQVAAYTTVTADACNLPPDLEHRWATGGVDAVVLTAPSTTRAVLELLGPPPQGTGLVAIGATTAAATRELGLTVAAVAPSPTPEGVLQATIDAIRATAGPTPPPQEPP$","Uroporphyrinogen-III synthase","Periplasm, Cytoplasm, Extracellular","uroporphyrinogen-III synthase","uroporphyrinogen-III synthase; HemD ","Uroporphyrinogen-III synthase-like","","","","","

InterPro
IPR003754
Domain

Tetrapyrrole biosynthesis, uroporphyrinogen III synthase
PF02602	$\"[261-374]T$	HEM4

","BeTs to 6 clades of COG1587COG name: Uroporphyrinogen-III synthaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1587 is aomp--yq-dr-bcefghsnu-xi--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 261 to 374 (E_value = 9.7e-08) place ANA_2443 in the HEM4 family which is described as Uroporphyrinogen-III synthase HemD.","","synthase (hemD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2444","2644676","2643381","1296","4.99","-18.40","44168","ATGACCACGACGGAGACGGACTCCCGGCGGCTTCGCCTGGGCACGCGCGGCTCGCGCCTGGCGCTGACCCAGTCCGGGCAGGTCGCTGAGGCACTGATGGCGGCCGGCGGGGGCGGTGCGGCCGCCGCGGCCGGCAAGGCCAGCGAGGGTTCCGGCGGCCTGGGCATCGACCTGGTCACCGTTCGCACGGATGGCGACGGCGACCGCACACCCCTGCGGCAGCTCGGCGGGGTAGGGGTCTTCGCGGCCCGGCTGCGTCACGCGCTCCTGGATGGCGAGGTGGACCTGGTGGTCCACTCCTTCAAGGACCTGCCCACGCAGCCGGTCGAAGGTCTGGAGGTCATCTGCGTGCCGCCGCGCGAGGACCCGCGCGACGCCCTATGCGCCCGCGACAGCCTGACCCTGGCCGACCTGCCCGAGGGGGCCCGCGTGGGCACCGGCTCGCCGCGTCGGGCCGCCCAGCTGCTGGCGGCCCGCCCCGACCTGGAGGTGGTGGACCTGCGCGGCAACGTGCCCACGCGCCTGGCACGGGTGCGGGGGCTGGAGGTGGTCGGCGTCGGCACCGATGAGCCGGTGGCGCCGAGCCGAGCCGATGCCGCCGGCGACCTGGACGCGGTGGTCCTGGCCCTGTCGGGGCTACGGCGTCTGGGGCTGGAGCACTGTGCGAGCGAGGTGCTGGACCTGGAGACGATGCTGCCCGCACCGGCACAAGGGGCCCTGGCCGTGGAGGCGCGAACCGGCGAGGACTCCGTGGAGCTGGCCCGGGCGGTGGCGGCGCTCGACGACGAGCCCACGCGCCTGGCGGTGACGGCCGAGCGGGCGCTCATGGCCCGGCTCGGGGCCGGCTGCGCGGCGCCGGTGGGGGCCTGGGCGCACCTGCGGGGCGGCGGTCAAGAGCAGCGGGAGGAGCACGCCGAACACGGAACCGGGTGGAACGAGGGCTTCCGCGACGATGACACCGCCGTGACCGGGGGCAAGCAAGGGGCTGGGGCCGCGAACGGCGATCCGCGGCCAGTCGGGGTCTCCGAGGTAGGACCGCACGATTCAGCGGCCTCGCGCCGCTCGCCGCGGGTGCTCGTGCTGCGAGCAGTGGTCACCTCGCTCGATGGCGGCCAGGAGGTCGGCTGCGAGCTAAGTACTGAGCTGCCCGAGGCCTCTGGGGTGCCAGGGGCTCCCGGGGACACGGCGGCGGTTCGGGCGGCCGAGGCACTGGGGGTCAGGGCGGCCGAGGTCCTGCTGGAGGACGGCGCCGACCAGATCGTCGACCTGTACGCCAACAAGCCCCGGCGGGACTGA","MTTTETDSRRLRLGTRGSRLALTQSGQVAEALMAAGGGGAAAAAGKASEGSGGLGIDLVTVRTDGDGDRTPLRQLGGVGVFAARLRHALLDGEVDLVVHSFKDLPTQPVEGLEVICVPPREDPRDALCARDSLTLADLPEGARVGTGSPRRAAQLLAARPDLEVVDLRGNVPTRLARVRGLEVVGVGTDEPVAPSRADAAGDLDAVVLALSGLRRLGLEHCASEVLDLETMLPAPAQGALAVEARTGEDSVELARAVAALDDEPTRLAVTAERALMARLGAGCAAPVGAWAHLRGGGQEQREEHAEHGTGWNEGFRDDDTAVTGGKQGAGAANGDPRPVGVSEVGPHDSAASRRSPRVLVLRAVVTSLDGGQEVGCELSTELPEASGVPGAPGDTAAVRAAEALGVRAAEVLLEDGADQIVDLYANKPRRD$","Porphobilinogen deaminase","Cytoplasm, Extracellular","porphobilinogen deaminase","porphobilinogen deaminase ","porphobilinogen deaminase","","","","","

InterPro
IPR000860
Family

Tetrapyrrole biosynthesis, hydroxymethylbilane synthase
PD002745	$\"[112-245]T$	Q6AB05_PROAC_Q6AB05;
PR00151	$\"[95-114]T$ $\"[143-160]T$ $\"[162-179]T$	PORPHBDMNASE
G3DSA:3.30.160.40	$\"[262-296]T$	no description
PTHR11557	$\"[97-178]T$ $\"[198-296]T$	PORPHOBILINOGEN DEAMINASE
PF01379	$\"[10-255]T$	Porphobil_deam
PF03900	$\"[266-416]T$	Porphobil_deamC
TIGR00212	$\"[11-328]T$	hemC: porphobilinogen deaminase
PS00533	$\"[272-288]T$	PORPHOBILINOGEN_DEAM

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[119-238]T$	no description

","BeTs to 21 clades of COG0181COG name: Porphobilinogen deaminaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0181 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB000860 (Porphobilinogen deaminase) with a combined E-value of 1.3e-80. IPB000860A 11-32 IPB000860B 74-128 IPB000860C 144-196 IPB000860D 233-245 IPB000860E 256-291","","","-51% similar to PDB:1AH5 REDUCED FORM SELENOMETHIONINE-LABELLED HYDROXYMETHYLBILANE SYNTHASE DETERMINED BY MAD (E_value = 3.7E_32);-51% similar to PDB:1GTK TIME-RESOLVED AND STATIC-ENSEMBLE STRUCTURAL CHEMISTRY OF HYDROXYMETHYLBILANE SYNTHASE (E_value = 3.7E_32);-51% similar to PDB:1YPN REDUCED FORM HYDROXYMETHYLBILANE SYNTHASE (K59Q MUTANT) CRYSTAL STRUCTURE AFTER 2 HOURS IN A FLOW CELL DETERMINED BY TIME-RESOLVED LAUE DIFFRACTION (E_value = 3.7E_32);-51% similar to PDB:2YPN Hydroxymethylbilane synthase (E_value = 3.7E_32);-50% similar to PDB:1PDA STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE (E_value = 1.9E_31);","Residues 10 to 255 (E_value = 3.6e-65) place ANA_2444 in the Porphobil_deam family which is described as Porphobilinogen deaminase, dipyromethane cofactor binding domain.Residues 266 to 416 (E_value = 1.2e-14) place ANA_2444 in the Porphobil_deamC family which is described as Porphobilinogen deaminase, C-terminal domain.","","deaminase (PBG)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2445","2646491","2644806","1686","5.75","-9.39","57134","ATGAGCGGGGAGGCCGTCGAGGAGCGACGGTGGGACGCGCTCGTCATCGGCGGCGGGATCGCGGGTCTGACGGCCGCCTGGGACCTGGTGCGCGCCGGGCTGCGGCCGCTGCTCATTGAGGCGCGCGGCTACACCGGCGGGCTCGTCGCGGCCGGGCCGATCGGCGGAGCACGCATGGACCTGGGGGCTGAGGGCTTCGTCGTGCGCGGCCAGGCGGCCACCTCGATGCTCGCCGAGCTGGGGCTGCACACCGCCGCCCCGCACGGCCGGCCCCGGCTCTTCCTGCCGCCCCTCGCGCCGGGCACCGGCGGCGAGCCGCCCCAGTGGGGGCTGCACCGGTTCCCCGACCACGCCTACCTGGGGATCCCGGCGGACCCACTGGCTCCCGACGTCGTCGCCATCATCGGGCAGGAGGCGGCGCGCCGGGCCGCGCAGGACGCCGACCTGCCCGGCACCGTGGGCACCGGCCCGGAGGATCCGGCCGACCTGGCCTCCTTCGTCACCGCGCGGATGGGGGCCGGCGTCCTGGAGCGCCTCGTGCGGCCCATCGTCGCGGGCATCCACTCGGCCGACCCGGCGGACCTGGCGGCCGATGTCGTCATGCCCGGGCTGCGGCGGGCCACGGCGGAGCTGGGGTCGCTCAGTGCCGCTGTGGCGGCGGTGCTGGAGCGGCGTCGGGCCCGTCAGGACGGGGCGGGTGGTCGGAGCGTGGACGCGGCCGTCGAGGGCGGGCTGTTCCGGCTCACCGACGCGCTGCGCGAGGCCATCGAGGCCGGCGGCGGGAGCGTGCGCACCCGCACCGGTGCCCAGTGGCTGCGGCCCAGCGGCGGCCAGGACTGCGCGGACAGGGAGGCACCGGCCGCCTGGCGGGTGGGGATCGCCCCGACGCGCCGGGGTCCGACGCCGTCGGACGAGCCGGTGCCCGATGGCGCGCAGGAGGTCGTGGCCACCGACCGCGTCATCCTGGCCTGCTCGGCAGGGGCCGCGCTGCGGCTGCTGCGGGGGATTCCCGGCCTGCCCGCGAGCGCGACGGAGCTGACCGTGCCGGTGGGGGCGCCGATCGCCCGCTTCACGCTGGTGGCGCGGGCGCCGGAGCTCAGTGATGAGCCGGTGGGCTCGGGGCTGCTCGTGGCGCCCGCCGGCGTTGCTGAGCCCGGTGAAGTCGCCGGCCCGGCTGGGCCCGACACTGCGGCGTCGTCGGCCGGCACCGGGGCCTCTGACCTGGTCTCTGACGGGATGGTTCCCAGTGGAGGGTCTGCGAGCCCGACGGCCTGCCCGGTGCAGGCCAAGGCGCTGTCGCACCTGAGTGCCAAGTGGCCGTGGGTCGGTGCCGAGCTGCGGGCGCTGCACGGCCCGGATGTCCACGCGCTGCGCCTGTCGTACGGTCGGCCCGGGCAGCCGCGACCGCAGGTAGATCTGCAGGTGGCGCTGGATGATGTGGCGGCCCTGACGGGGGTGCGGATCGAGCCGGAGGCGGTCATCGACCACATGCTGGTGCGGTGGGACGGGACGCTGCCGCCAGTGACGCCCGTCTACCGGGAGCGCACGAGGCGCCTGGAGGAGCAGCTGGCGCCGGTGACGGGACTGGAGGTCACCGGGGCATGGGTGGCCGGGACCGGGATCGCGGCCGTCGTCGAGCACGCCCGCGCCGCGGTCGGGCGCCTGATGGGCTCCCATGGCGGGTGA","MSGEAVEERRWDALVIGGGIAGLTAAWDLVRAGLRPLLIEARGYTGGLVAAGPIGGARMDLGAEGFVVRGQAATSMLAELGLHTAAPHGRPRLFLPPLAPGTGGEPPQWGLHRFPDHAYLGIPADPLAPDVVAIIGQEAARRAAQDADLPGTVGTGPEDPADLASFVTARMGAGVLERLVRPIVAGIHSADPADLAADVVMPGLRRATAELGSLSAAVAAVLERRRARQDGAGGRSVDAAVEGGLFRLTDALREAIEAGGGSVRTRTGAQWLRPSGGQDCADREAPAAWRVGIAPTRRGPTPSDEPVPDGAQEVVATDRVILACSAGAALRLLRGIPGLPASATELTVPVGAPIARFTLVARAPELSDEPVGSGLLVAPAGVAEPGEVAGPAGPDTAASSAGTGASDLVSDGMVPSGGSASPTACPVQAKALSHLSAKWPWVGAELRALHGPDVHALRLSYGRPGQPRPQVDLQVALDDVAALTGVRIEPEAVIDHMLVRWDGTLPPVTPVYRERTRRLEEQLAPVTGLEVTGAWVAGTGIAAVVEHARAAVGRLMGSHGG$","Protoporphyrinogen oxidase","Cytoplasm","putative protoporphyrinogen oxidase","protoporphyrinogen oxidase ","FAD dependent oxidoreductase","","Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S. The primary structure of the flavoprotein D-aspartate oxidase from beef kidney. J. Biol. Chem. 1992. 267(17):11865-11871. PMID: 1601857Miyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M., Miyake Y. Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization. J. Biochem. 1991. 109(1):171-177. PMID: 1673125","","","

InterPro
IPR006076
Family

FAD dependent oxidoreductase
PF01266	$\"[12-47]T$	DAO

noIPR
unintegrated

unintegrated
G3DSA:1.10.3110.10	$\"[122-219]T$	no description
G3DSA:3.50.50.60	$\"[7-84]T$	no description
PTHR10742	$\"[8-41]T$	AMINE OXIDASE
PTHR10742:SF11	$\"[8-41]T$	gb def: Putative amino oxidase
tmhmm	$\"[10-30]?$	transmembrane_regions

","BeTs to 6 clades of COG1232COG name: Protoporphyrinogen oxidaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG1232 is ao--k-yq-dr-b--------j-i--Number of proteins in this genome belonging to this COG is 1","***** IPB000759 (Adrenodoxin reductase family signature) with a combined E-value of 3.4e-06. IPB000759A 12-34 IPB000759D 13-27***** IPB013027 (FAD-dependent pyridine nucleotide reductase signature) with a combined E-value of 4.9e-06. IPB013027A 12-34 IPB013027C 12-37***** IPB003042 (Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature) with a combined E-value of 7.9e-06. IPB003042A 12-34","","","No significant hits to the PDB database (E-value < E-10).","Residues 10 to 42 (E_value = 0.0002) place ANA_2445 in the FAD_binding_3 family which is described as FAD binding domain.Residues 12 to 554 (E_value = 0.00052) place ANA_2445 in the DAO family which is described as FAD dependent oxidoreductase.Residues 12 to 47 (E_value = 5e-07) place ANA_2445 in the FAD_binding_2 family which is described as FAD binding domain.Residues 12 to 42 (E_value = 0.0002) place ANA_2445 in the GIDA family which is described as Glucose inhibited division protein A.Residues 12 to 54 (E_value = 4.1e-05) place ANA_2445 in the Pyr_redox_2 family which is described as Pyridine nucleotide-disulphide oxidoreductase.Residues 20 to 66 (E_value = 1.2e-07) place ANA_2445 in the Amino_oxidase family which is described as Flavin containing amine oxidoreductase.","","protoporphyrinogen oxidase (PPO)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2446","2647855","2646488","1368","5.85","-7.65","47683","ATGTCTCACATTCAGTTCCCTTATCGCAGGGAAAGCACGCGGCGTCAGCATTCTTCGCCCGATAACGGCGATTTCGTCACCGGCAGTTCACACAATGATTCAATGACTTCCGAGCCGGCGGCGCAGGCTGCCGAGGCGGCGGGGCCTGCCGGGACCACGACGGGACCGGCTCCGTCGCCGGCGCTCCTGGAGGCGCTGGCGGGGCGGAGGCCCGCGCGCACACCGGTGTGGTTCATGCGTCAGGCGGGACGGTCGCTGCCGGAGTACCGGGCGCTGCGGGCGCGCGCCGGCGTGCCGATGCTGGATGCCTGCCTGGATCCTGCGCTGGCGGCGGAGGTGACGCTGCAGCCGGTGCGGCGCCACGGCGTCGACGCCGCCGTCTTCTTCTCCGACATCATGGTGCCGCTGCGCCTGGCGGGCGTGGGGGTACGGATCGAGGAGGGCGTCGGGCCGGTCCTCGACGCCCCGGTGCGCAGCGGTCGCGAGGTGGTCGAGCTGGTGGCCCGCCGCTTCGGTGACGGCCCCGACGCCGAGGGGGTCGGGGCGATCGAGGAGGCGGTGCGGCGCGTCGTCGTCGAGCTGGGCAGTCCGCAGGCGCCGGGCGTGCGCGAGGGGCTGAGCGAGCGGGCGCGCGCCGGGCTGGAGCACAGTGCCGGGTCGGCGGGGTGGACGCCGGTGCTCGCCTTCGGCGGGGCGCCCTTCACGCTGGCGGCCTACCTGGTGGAGGGCCGGCCCAGTCGCGACCACCTGGCGGCGCGCACGCTCATGCGCGCCGACCGCGACTCCTGGGACCGGCTCATGACGTGGTGCGCGCGCCTGACCGGCGAGTTCATCGCCACCCAGGTGCGTGCCGGGGCGGTCGCGGCCCAGCTCTTCGACTCCTGGGCGGGCTCGCTGTCCCCGCGCGCCTACCGCGAGCGCGTGGCCCCCTACTCGGCGCTCGCGCTGGATGTCGCCCGCCAGGCCGTCTCCCCCACCACCGGTGAGAGCGCGCCGCTCATCCACTTCGGGACCGGGACCGCCCGGCTGCTGGGGCTCATGCGGCAGGCGGGGGCCGACGCCGTCGGCGTAGACGAGCGCATCGAGCTGGGCGAGGCCATTGAGGCGCTGGCCGAGGCCGACCCGCAGGCGGGGGCCTGCCCGGTTCAGGGCAACCTGGACCCGGCGCTGCTGGCGGCGCCATGGCCGATCCTGGCTGAGGAGCTCGACGCAGTGCTGGCCGCCGGGCGCGCGGCGCCGGGGCACGTCGTCAACCTGGGGCACGGGGTCCCTCCGGCCACCGACGCGAATGTCCTCTCCCGGATCGTGGCGCGGGTGCACGGCTCCGCGGACTGGGAGTCCGTGGCCCTGGCCGGGTGGGAGGCATGA","MSHIQFPYRRESTRRQHSSPDNGDFVTGSSHNDSMTSEPAAQAAEAAGPAGTTTGPAPSPALLEALAGRRPARTPVWFMRQAGRSLPEYRALRARAGVPMLDACLDPALAAEVTLQPVRRHGVDAAVFFSDIMVPLRLAGVGVRIEEGVGPVLDAPVRSGREVVELVARRFGDGPDAEGVGAIEEAVRRVVVELGSPQAPGVREGLSERARAGLEHSAGSAGWTPVLAFGGAPFTLAAYLVEGRPSRDHLAARTLMRADRDSWDRLMTWCARLTGEFIATQVRAGAVAAQLFDSWAGSLSPRAYRERVAPYSALALDVARQAVSPTTGESAPLIHFGTGTARLLGLMRQAGADAVGVDERIELGEAIEALAEADPQAGACPVQGNLDPALLAAPWPILAEELDAVLAAGRAAPGHVVNLGHGVPPATDANVLSRIVARVHGSADWESVALAGWEA$","Uroporphyrinogen decarboxylase","Cytoplasm","uroporphyrinogen decarboxylase","uroporphyrinogen decarboxylase ","Uroporphyrinogen decarboxylase","","Whitby F.G., Phillips J.D., Kushner J.P., Hill C.P. Crystal structure of human uroporphyrinogen decarboxylase. EMBO J. 1998. 17(9):2463-2471. PMID: 9564029","","","

InterPro
IPR000257
Family

Uroporphyrinogen decarboxylase (URO-D)
PD003225	$\"[68-440]T$	Q6NJJ4_CORDI_Q6NJJ4;
PF01208	$\"[57-442]T$	URO-D
PS00906	$\"[75-84]T$	UROD_1
PS00907	$\"[227-243]T$	UROD_2

InterPro
IPR006361
Family

Uroporphyrinogen decarboxylase HemE
PIRSF001349	$\"[59-445]T$	Uroporphyrinogen-III decarboxylase/methylcobamide:CoM methyltransferase
PTHR21091:SF2	$\"[72-186]T$ $\"[207-440]T$	UROPORPHYRINOGEN DECARBOXYLASE

InterPro
IPR014670
Family

Uroporphyrinogen-III decarboxylase
PIRSF500079	$\"[59-445]T$	Uroporphyrinogen-III decarboxylase

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.210	$\"[44-440]T$	no description
PTHR21091	$\"[72-186]T$ $\"[207-440]T$	METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED

","BeTs to 16 clades of COG0407COG name: Uroporphyrinogen-III decarboxylaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0407 is ---p--yq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB000257 (Uroporphyrinogen decarboxylase (URO-D)) with a combined E-value of 8.5e-63. IPB000257A 75-89 IPB000257B 104-150 IPB000257C 209-257 IPB000257D 353-364 IPB000257E 382-392 IPB000257F 415-440","","","-47% similar to PDB:2INF Crystal Structure of Uroporphyrinogen Decarboxylase from Bacillus subtilis (E_value = 8.0E_49);-41% similar to PDB:1JPH Ile260Thr mutant of Human UroD, human uroporphyrinogen III decarboxylase (E_value = 2.3E_27);-41% similar to PDB:1JPI Phe232Leu mutant of human UROD, human uroporphyrinogen III decarboxylase (E_value = 2.3E_27);-42% similar to PDB:1J93 Crystal Structure and Substrate Binding Modeling of the Uroporphyrinogen-III Decarboxylase from Nicotiana tabacum: Implications for the Catalytic Mechanism (E_value = 3.0E_27);-41% similar to PDB:1R3Q Uroporphyrinogen Decarboxylase in complex with coproporphyrinogen-I (E_value = 3.0E_27);","Residues 57 to 442 (E_value = 1.8e-92) place ANA_2446 in the URO-D family which is described as Uroporphyrinogen decarboxylase (URO-D).","","decarboxylase (UPD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2448","2647977","2649542","1566","5.92","-11.80","53160","ATGTCGGGTGTGTGTCGCCACGCCGCTATTGTGCCCGCTCACCACGGTGATGTTTCAATAGCCCACGTTGTGACTACTCATCTTCTCTCCGCAGACCATCGACTGCCGGGCCTCGACGTCGTTGCCCGGCTCGGTGCGGTCGCCCCGGGGCTGGGGCCGGACCTCCTGGAGGCGGTCCCGGCGCTACGCGGGGTTCTGGTGCTGTCCACCTGCAACCGCCTGACCCTGCTCATCGATGCCGACTCCTGGGCCGACACCGGCTGCCCGGCGGCCCTGCACCCGGACCTCTCTCCGGCGGACGCGAGCCAGTCGGCCGCGGCGTCGGACCTGGGGGAGACCATCACCGCCTTCCTGGCCGAGCGCGCCGGGCTCCCTGCGAGCGGACTCCTGCTGACCCACCTGGTCGGGGCGGCCGCCCGCAGGGAGATGCTCGCCATCGCTGCGGGCCTGAGCTCGATGGTGGTCGGCGAGGCCCAGATCGTCGGCCAGGTCCGCCGCGCTGCCGAGACCGCCGCCGCCGAGGGCACGCTTAGCCCCGAGCTCGTGCGGGTCGTCGAGCGCGCCTCGGCCACCGCCCGCCGGGTGGCCCACGAGACCGAGCTGTCCGGTCAGGGGCGCAGCGTCGTCGCCGTCGGCGTGGATCAGGCCGCAGCGCACCTGCCGCCGCTGGAGGACTGCCGCGCCCTCATCGTCGGCACCGGCTCCTACGCCGGCGCCACCGTCGCCGACCTGCGCGCCCGAGGCCTGAGCGACATCGCCGTCTACTCCGCCTCCAACCGCGCCGAGGCTTTCGCCGTCGGCCACGGCCTGCGCGCCGTCCCCACCGGCGCCCTGAGTGGGGCCATGAGCCGCGCTGACCTCGTGGTCACCTGCCGCGGCACCGGCGGGCCGATCCTCACCGCCGACGTCGTCGCCCCCGTCGCCGCCGAGCGAGCCGGCTCGGCCGGGGGAGACGCCCGCCCGCTCGTCATCCTCGACCTGGCCCTGACCCGCGACGTCGACGAGTCCGTCGGTGCCCTACCCGGCGTCGTCCACCTCGACCTGGCCCGCGTGCGCGACGCCGTTCCCGAGGCCGAGGCCCAGCAGGTGACCGCCGCCCGCGCCATCGTCGAGGCCGAGGCCGCTGACTTCGAGCGCACCCTGGCCGGCCGGGCCATGGACCCCCTCATCACCGCCCTGCGCGCCCAGGTGGGTCGCGTCGTCGCCGAGGAGGCCGCCCGCCTGCGCCCCCAGCCCGCCCGCCGCCTCGCCCTGGCCGTCCCCGCCGTCGACGGGCGCGCCGGAACCGGCGTCAGCGGTGTCAACAGCGCCGACGCCGCCGCAGGGGCCTGCCCCCACCATCTCCTCGCTGCCAAGCCCGGCTTCGAGGCCGCCAGCGAGATCGACGGCGAGCCTATGGTGCCCCTGGCGCAGGCCGAGCGGGCCCTGCACCACCTGGCCGCCCGCCTCCTCCACCAGCCCACCGTCATGGCCCGCCGCGCCGGCCAGGAGGGCCGCGAGGAGGCCTACCGTCAGGCCCTCGAGCTCGTCTGGGGCCTGGAAAGCACAGGAGAGAACCATGACTGA","MSGVCRHAAIVPAHHGDVSIAHVVTTHLLSADHRLPGLDVVARLGAVAPGLGPDLLEAVPALRGVLVLSTCNRLTLLIDADSWADTGCPAALHPDLSPADASQSAAASDLGETITAFLAERAGLPASGLLLTHLVGAAARREMLAIAAGLSSMVVGEAQIVGQVRRAAETAAAEGTLSPELVRVVERASATARRVAHETELSGQGRSVVAVGVDQAAAHLPPLEDCRALIVGTGSYAGATVADLRARGLSDIAVYSASNRAEAFAVGHGLRAVPTGALSGAMSRADLVVTCRGTGGPILTADVVAPVAAERAGSAGGDARPLVILDLALTRDVDESVGALPGVVHLDLARVRDAVPEAEAQQVTAARAIVEAEAADFERTLAGRAMDPLITALRAQVGRVVAEEAARLRPQPARRLALAVPAVDGRAGTGVSGVNSADAAAGACPHHLLAAKPGFEAASEIDGEPMVPLAQAERALHHLAARLLHQPTVMARRAGQEGREEAYRQALELVWGLESTGENHD$","Glutamyl-tRNA reductase","Cytoplasm","Glutamyl-tRNAGlu reductase, N-terminal domainprotein","glutamyl-tRNA reductase ","Glutamyl-tRNA reductase","","","","","

InterPro
IPR000343
Family

Tetrapyrrole biosynthesis, glutamyl-tRNA reductase
PF00745	$\"[364-411]T$	GlutR_dimer
PF05201	$\"[29-200]T$	GlutR_N

InterPro
IPR006151
Domain

Shikimate/quinate 5-dehydrogenase
PF01488	$\"[204-351]T$	Shikimate_DH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[204-361]T$	no description

","BeTs to 17 clades of COG0373COG name: Glutamyl-tRNA reductaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0373 is aomp-z-q-dr-bcefghsnu--i--Number of proteins in this genome belonging to this COG is 1","***** IPB000343 (Glutamyl-tRNA reductase) with a combined E-value of 2.9e-41. IPB000343B 56-77 IPB000343C 139-165 IPB000343D 181-216 IPB000343E 227-262 IPB000343F 286-305 IPB000343G 329-383 IPB000343H 478-488","","","-45% similar to PDB:1GPJ GLUTAMYL-TRNA REDUCTASE FROM METHANOPYRUS KANDLERI (E_value = 1.1E_12);","Residues 29 to 200 (E_value = 5e-11) place ANA_2448 in the GlutR_N family which is described as Glutamyl-tRNAGlu reductase, N-terminal domain.Residues 204 to 351 (E_value = 3.6e-06) place ANA_2448 in the Shikimate_DH family which is described as Shikimate / quinate 5-dehydrogenase.Residues 364 to 411 (E_value = 1.8e-06) place ANA_2448 in the GlutR_dimer family which is described as Glutamyl-tRNAGlu reductase, dimerisation domain.","","reductase, N-terminal domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2449","2649535","2650974","1440","4.87","-26.00","49269","ATGACTGACACCGCCGCGCCCGTGCCCGGGCCCACCCAGGAGGCTCCCGCGCGCCTGGACGCACGCTCGGATGCCCTCCCGGGCGCCGACCTCGCCGGAGCCCCAGCCACTGTCCCGGCCCTCGACCCGCTGGCCCCCTACGACGCCATTCTCCTGCAGTCCTACGGCGGGCCCCGCCGCCCCGAGGACGTCCTGCCCTTCATGCGCAACGCCACAGCCGGCCGCGGCGTGCCCGACTCCCGCCTCGTAGAGGTCTCCGGCCACTACCAGAGTGTCGGCGGCGCCTCCCCGATCAACGCGTGCAACGCCGAGCTGCGCGACTCCCTCCAGGCCCGCCTGGCCGAGCGCGGCTCGACGCTGCCGATCATCGTCGGCAACCGCAACTGGCACCCCTTCGTCAGCCAGGCCCTGCGCGAGCTGGCCGACGCCGGGGCCCGCCGCGTTCTGGCCCTGCCCACCGCGGCCTTCGGCTCCTACTCCGGGTGCCGCCAGTACCGCGAGGACCTGGCCGGCGCCGTCGCCCTGCTCGCCGACGGCGCGGACGGCTCCACCGGTGAGGGATTCGAGGCCGACGCCGCCGCCCGGGTCGGCGGGGACGGGGGCGGTCCCGTGGAGCTCACCGCGGACAAGACGCGCCCCTACTACAACACCCCCGGCCTGCTGCAGGCCAACATTGACGCCATCGTCGAGGCCTACGGCGCCCTGGCCGAGCAGGGAGTGGCGGCCGCGGACGCGCGCCTCGTGCTCGTCACCCACTCCATCCCCCTGGGCATGGAGGCCGGTTCCGCCCCTGGGGAGGGCACTGAGAGCGCACCCGGCGCCTCCGGCGCTTCTGACGCGCACGACCCGACCGGCGCCGGGCGGCGAGAGCCGGGCGTGGCCGCCGACCTGTCCACGGAGGTCTCCTACGTCGCCCAGCACGAGGCGCTGGCCGCCGTCCTCGTGCCCGAGGTCGCCCGCCGCCTCGGCCTGGAGACGGTCGAGGCCGACCTCGTCTACTGCTCGCGCTCCGGCCCGCCGCAGGCCCGCTGGCTCGAACCGGACGTCAACGACCACCTCGAGGCCCTGGCCGCCGGGCACCTGACCGACGGCAGCCCCGTGAGCAGGCCCGAGGGCGTCGTCGTGGCCCCCTTCGGCTTCATCTCCGACCACATGGAGGTCGTCTTCGACCTCGACACCGAGGCCGCCCAGACCGCCCGCGACCTGGGGATGCCGTATGCGCGCGCTGCCACTGTCGGCACCCACCCGGCCTTCATCGACTCCCTCGTCGACATCCTCTTCGAGCGGGCCGCCGCCGCCCGCGGTGAGGACGTCCGGCCCGACTCGACCACCGGCGTCGGCCCGTTCCACACGGTCTGCCCGGACTCCTGCTGCCGGAACGGGGCCAGCCACCCCGGCCGGCCCGCTCACCACGGGACCGACGGCGAAGGCTCTCGATAG","MTDTAAPVPGPTQEAPARLDARSDALPGADLAGAPATVPALDPLAPYDAILLQSYGGPRRPEDVLPFMRNATAGRGVPDSRLVEVSGHYQSVGGASPINACNAELRDSLQARLAERGSTLPIIVGNRNWHPFVSQALRELADAGARRVLALPTAAFGSYSGCRQYREDLAGAVALLADGADGSTGEGFEADAAARVGGDGGGPVELTADKTRPYYNTPGLLQANIDAIVEAYGALAEQGVAAADARLVLVTHSIPLGMEAGSAPGEGTESAPGASGASDAHDPTGAGRREPGVAADLSTEVSYVAQHEALAAVLVPEVARRLGLETVEADLVYCSRSGPPQARWLEPDVNDHLEALAAGHLTDGSPVSRPEGVVVAPFGFISDHMEVVFDLDTEAAQTARDLGMPYARAATVGTHPAFIDSLVDILFERAAAARGEDVRPDSTTGVGPFHTVCPDSCCRNGASHPGRPAHHGTDGEGSR$","Ferrochelatase","Cytoplasm","ferrochelatase","ferrochelatase ","Ferrochelatase","","Labbe-Bois R. The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption, and expression of its structural gene HEM15. J. Biol. Chem. 1990. 265(13):7278-7283. PMID: 2185242Brenner D.A., Frasier F. Cloning of murine ferrochelatase. Proc. Natl. Acad. Sci. U.S.A. 1991. 88(3):849-853. PMID: 1704134Al-Karadaghi S., Hansson M., Nikonov S., Jonsson B., Hederstedt L. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure 1997. 5(11):1501-1510. PMID: 9384565Wu C.K., Dailey H.A., Rose J.P., Burden A., Sellers V.M., Wang B.C. The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat. Struct. Biol. 2001. 8(2):156-160. PMID: 11175906","","","

InterPro
IPR001015
Family

Ferrochelatase
PD002792	$\"[52-440]T$	HEMZ_STRCO_O50533;
PTHR11108	$\"[45-164]T$ $\"[187-260]T$ $\"[303-474]T$	FERROCHELATASE
PF00762	$\"[47-430]T$	Ferrochelatase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1400	$\"[44-234]T$	no description

","BeTs to 10 clades of COG0276COG name: Protoheme ferro-lyase (ferrochelatase)Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0276 is ---p--yq-drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 2","***** IPB001015 (Ferrochelatase) with a combined E-value of 4.6e-26. IPB001015A 49-59 IPB001015C 125-157 IPB001015D 247-265 IPB001015E 335-351 IPB001015F 379-392","","","-36% similar to PDB:2C8J CRYSTAL STRUCTURE OF FERROCHELATASE HEMH-1 FROM BACILLUS ANTHRACIS, STR. AMES (E_value = 8.9E_14);-34% similar to PDB:1AK1 FERROCHELATASE FROM BACILLUS SUBTILIS (E_value = 2.2E_12);-34% similar to PDB:1C1H CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN (E_value = 2.2E_12);-34% similar to PDB:1C9E STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE (E_value = 2.2E_12);-34% similar to PDB:1DOZ CRYSTAL STRUCTURE OF FERROCHELATASE (E_value = 2.2E_12);","Residues 47 to 430 (E_value = 3.5e-52) place ANA_2449 in the Ferrochelatase family which is described as Ferrochelatase.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2450","2651015","2651824","810","6.04","-8.46","30969","ATGAGTACCGACACCCACGGCCAGCACGGACATCCCGGCGGTCACCCCGGTGAGGGCGGCCTGCACCGCTTCGAGGACGAGGAGCGCCGCCCCCACCGCGACCCACGCGACGCCACCGACGTCGACCTGGAGGCCATCAACAACCAGTACCACTACACCCTTTACGCCGTCTTCCGCCTGGCCCGCCCGCTGCCCGCCTCCCAGCCCGAGCGCGAGCAGCTCCTGGGGGAGAGCGCCAACTTCGTCGAGGCCGGCGGCGTGACGACGCGCGGCTGGTACGACGTCGGGGGCCTGCGCGCCGACGCCGACCTGCTCGTGTGGTGGCTCGACGACGACCCCGAGGTCCTTCAGGACGCCTACCACCGCCTGCGCGGCAGTGCGCTGGGTCGCTATCTGGAGCCGGTGTGGTCCTGCATGGGGATGCACACGCCCGCCGAGTTCAATCCCCGCCATGTGCCGGCCTGCCTGGCCGGGGTGGCGCCGCGCGACTGGGTCATGGTCTACCCCTTCGTGCGCTCCTACGAGTGGTACCTGCTCGAGCCCGAGGAGCGCTCGCGCATGATGGCCCAGCACGGGCGCCACGGCTTCTCCAAGTACCCCGACGTCAAGGGCTCGACCCTGTCCACCTTCGGCCTGAGCGACTACGAGTGGATCCTCGGCTTCGAGGCCGACAGCCTCGACCGGCTCGAGGGGGTCCTGCACCACCAGCGCTACACGGAGGCGCGCATGCACGTGCGCGTGGACACGCCCTTCTACACCGGGCGCCGCGTCAGCCCGCAGGAGTGGGCTCAGCGCCAGCCCTGGGCCTGA","MSTDTHGQHGHPGGHPGEGGLHRFEDEERRPHRDPRDATDVDLEAINNQYHYTLYAVFRLARPLPASQPEREQLLGESANFVEAGGVTTRGWYDVGGLRADADLLVWWLDDDPEVLQDAYHRLRGSALGRYLEPVWSCMGMHTPAEFNPRHVPACLAGVAPRDWVMVYPFVRSYEWYLLEPEERSRMMAQHGRHGFSKYPDVKGSTLSTFGLSDYEWILGFEADSLDRLEGVLHHQRYTEARMHVRVDTPFYTGRRVSPQEWAQRQPWA$","Chlorite dismutase","Cytoplasm","Uncharacterized ACR","hypothetical protein","Chlorite dismutase","","Van ginkel C.G., Rikken G.B., Kroon A.G., Kengen S.W. Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme. Arch. Microbiol. 1996. 166(5):321-326. PMID: 8929278","","","

InterPro
IPR010644
Family

Chlorite dismutase
PF06778	$\"[69-254]T$	Chlor_dismutase

noIPR
unintegrated

unintegrated
G3DSA:3.30.70.1100	$\"[162-268]T$	no description

","BeTs to 7 clades of COG3253COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3253 is -o-p-z---dr-b-------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 69 to 254 (E_value = 3.2e-58) place ANA_2450 in the Chlor_dismutase family which is described as Chlorite dismutase.","","ACR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2451","2651939","2652250","312","5.44","-3.37","11412","GTGCGAAATGTCCCCGGCCATGAGGGTGGGCGACGGCGCAACCTGACCAACCTGGTTGACCAGGTCGCTTTCTCCTGGGACCATCAATGCATGAAGACGGTGAAGGTTCAGGAGGCGAAGACGCATCTGTCGGCGCTGTTGGTGGAGGTCGAGCAGGGGGCGACCATCAACATCGCCCGAGGGCGTCAGACAGTGGCGCGCTTGGTTCCGGTCGGGGGCGAGCGCGAGCTGGGCTTCGGCGGATACCAGCTGCCGGACACGTTCTTCGACGAGCTGCCGGAGGAGGAGCTGAGTGCCTGGGAGGGTGCATGA","VRNVPGHEGGRRRNLTNLVDQVAFSWDHQCMKTVKVQEAKTHLSALLVEVEQGATINIARGRQTVARLVPVGGERELGFGGYQLPDTFFDELPEEELSAWEGA$","Antitoxin of toxin-antitoxin stability system","Cytoplasm","hypothetical protein","antitoxin of toxin-antitoxin stability system","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2452","2652247","2652639","393","6.69","-0.85","14567","ATGAAGGGCTACCTGCTCGATACGCACGCGCTCATGTGGGCGATCAATGAGCCCTCGCGACTGGGCGGAAGGGCTGTCGAGGTGCTGCGAGACCGAGGGAATCTCCTGGTGGTCTCCGCCGCCAGTGCATGGGAACTGCATACCAAGAACCGCATCGGGAAACTGCCTGGAGCGGGGCCGTGGCTGGATGCTCTCGAGGGGCACGTGCGACGGCTCGGAGCGGAGTTCTTGCCCATCGAGTGGTCGCACGCGCGCCTGAGCGGGCAGCTTGAGTGGTCGCATCGCGATCCCTTTGATCGGATGCTGGCGGCGCAAGCGATGTACGAGTCGCTTGCGCTGGTGACGCGCGATCCGGCCTTCGAGGAACTGTCCGGTGTGACGATCCTGTGGTGA","MKGYLLDTHALMWAINEPSRLGGRAVEVLRDRGNLLVVSAASAWELHTKNRIGKLPGAGPWLDALEGHVRRLGAEFLPIEWSHARLSGQLEWSHRDPFDRMLAAQAMYESLALVTRDPAFEELSGVTILW$","PilT protein domain protein","Cytoplasm","PIN domain, putative","hypothetical protein","PilT protein domain protein","","Wall D., Kaiser D. Type IV pili and cell motility. Mol. Microbiol. 1999. 32(1):1-10. PMID: 10216854Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N., Yanagida M., He X., Mueller U., Sazer S., Nishimoto T. Dis3, implicated in mitotic control, binds directly to Ran and enhances the GEF activity of RCC1. EMBO J. 1996. 15(20):5595-5605. PMID: 8896453","","","

InterPro
IPR002716
Domain

PilT protein, N-terminal
PF01850	$\"[4-128]T$	PIN

","BeTs to 3 clades of COG3744COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3744 is ----------r--c-----n------Number of proteins in this genome belonging to this COG is 1","***** IPB002716 (PilT protein, N-terminal) with a combined E-value of 9.6e-07. IPB002716A 5-12 IPB002716B 99-117","","","No significant hits to the PDB database (E-value < E-10).","Residues 4 to 128 (E_value = 1.5e-10) place ANA_2452 in the PIN family which is described as PIN domain.","","domain, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2453","2653543","2652902","642","4.89","-9.37","22473","ATGTTGACTCGTGAGGACGTTCCTGGGGCCACTGACGTGAAGTGGTCGGATGAGACGGGATATCTGAGTATTTGCCCCGCCGCGGATGATGACATCGATCTGTCGTTGTCATCGGATCCTGAGACTCAGATGAGTGTCGAACGCCTCGAGGGCGATGGGATGTCCGTCACCCAGGCACTGATCTTCAATCTCATAGAAAGCGACAAGGGTGGACGTGTTCGTGCTCTACATACGGATGTCATAGCCTGCGACGGTGCAGAGACGACTGAGAGTCGCCCCTGGCCTGACAGGCCCGCACCCGCCCCTGGGGAGCGAGTGAGCGTGGCGATATCGACGCTGGAACCAGGCTCCCTACCCAAGGGCGCCTTCGGTTTCAGGCAGCGGGCCACCACACGAGCCAGCGTCGTCGTCGTGGACATGGTCTACGCACCTGTGAAACGCGGCGACCAGCAGGGCATCCTCATGATCCGCACCGCCACAACCGAAGGCAAGACCAGTCCGCAAGACGCCGTCGGGCTGCTGAACAAGGCGCTCCACCGCGCCAACGCCCACATCGACCCCGACCAGCTGACCGCGCCGGCACAGCCGACACCGACATCAGGCAGCGCCACCGCAACACCAACGTCGCCGCCAACACCCTGA","MLTREDVPGATDVKWSDETGYLSICPAADDDIDLSLSSDPETQMSVERLEGDGMSVTQALIFNLIESDKGGRVRALHTDVIACDGAETTESRPWPDRPAPAPGERVSVAISTLEPGSLPKGAFGFRQRATTRASVVVVDMVYAPVKRGDQQGILMIRTATTEGKTSPQDAVGLLNKALHRANAHIDPDQLTAPAQPTPTSGSATATPTSPPTP$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2454","2654253","2654957","705","8.43","3.30","23861","GTGGCACATGCCGAGAACCGCCCCGCGAGTCGAGCTGGGGGTCGTCGTCGAGCTGCCGCACTGGGCTGCCTGCTGCTCGCCGGCTCACTGGCCCTGACCGGCTGCTCCTCCAAGGACTCCAAGCCCGACGCCAAGGCGCCCGCCAGCAGGGCTGGTTCCACGGGGAGGCCGACGTCGGCCCCCTCGGCTTCCGCTACGGCGTCGGGCACTGCTGGCACCGTCACGGCGGCCTCCCTGTCCGACGCCCAGCTCGGGTACACCGTCACCGCGATCCCCGCCGGCCTCGACGTCAAGCGGGTCGCGATCCTCCAGGACTTCGTGGCCTACGATCAGATGTCCTGGAAGCTGTGGGTCGGCGGCGGGCAGGACACGAGCAAGGTACCCACTGTCACCACCGGCAACCTCCAGCAGCAGCTCCTCAATGACGCCGCCACCTTGAAAAACGCGGGGCAGAAGGCCAAGACCCCCGTCAAGGTGGCGATCTCCGAGGTCGCCATGAGCGCCGACGGTCAGAGCGCCACCGTCTCCTACTGCGTGGACATGACGCAGGTGACCTATGTCGACGCGCAGGGCAAGGACGTCACCGAACCCACCAACAAGGCGCGCATCCCGGCGAAGAACACCATGGTGCCCGGTAGTAACGGACACTGGCTCGCCTCCGAGGAGGAGGAGACCGGTGAGCCGAACACCTGCAAGGTCGGCTGA","VAHAENRPASRAGGRRRAAALGCLLLAGSLALTGCSSKDSKPDAKAPASRAGSTGRPTSAPSASATASGTAGTVTAASLSDAQLGYTVTAIPAGLDVKRVAILQDFVAYDQMSWKLWVGGGQDTSKVPTVTTGNLQQQLLNDAATLKNAGQKAKTPVKVAISEVAMSADGQSATVSYCVDMTQVTYVDAQGKDVTEPTNKARIPAKNTMVPGSNGHWLASEEEETGEPNTCKVG$","Hypothetical protein","Extracellular, Periplasm","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide

InterPro
IPR002177
Family

DNA-binding protein Dps
PD149803	$\"[38-74]T$	Q6A5X2_PROAC_Q6A5X2;
PR01346	$\"[38-54]T$ $\"[62-78]T$ $\"[133-151]T$	HELNAPAPROT
PIRSF005900	$\"[6-158]T$	Ferritin-like protein, Dps type
PS00818	$\"[38-54]T$	DPS_1

InterPro
IPR008331
Family

Ferritin and Dps
PF00210	$\"[21-159]T$	Ferritin

InterPro
IPR012347
Family

Ferritin-related
G3DSA:1.20.1260.10	$\"[6-155]T$	no description

InterPro
IPR013188
Domain

Influenza matrix M1, C-terminal
SM00759	$\"[68-159]T$	no description

","BeTs to 13 clades of COG0783COG name: Starvation-inducible DNA-binding proteinFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0783 is -o-------d-lbcefghs-ujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB002177 (DNA-binding protein Dps) with a combined E-value of 5.6e-27. IPB002177A 20-60 IPB002177B 61-78 IPB002177C 130-153","","","-45% similar to PDB:1UVH X-RAY STRUCTURE OF DPS FROM MYCOBACTERIUM SMEGMATIS (E_value = 1.4E_11);-45% similar to PDB:1VEI Mycobacterium smegmatis Dps (E_value = 1.4E_11);-45% similar to PDB:1VEL Mycobacterium smegmatis Dps tetragonal form (E_value = 1.4E_11);-45% similar to PDB:1VEQ Mycobacterium smegmatis Dps Hexagonal form (E_value = 1.4E_11);","Residues 21 to 159 (E_value = 0.0001) place ANA_2456 in the Ferritin family which is described as Ferritin-like domain.","","induced DNA-binding protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2457","2655834","2657141","1308","5.14","-20.41","46999","ATGAGCCGATCCGCCGCCCCCGCCTGGATCGACCACGCCATCTGGTGGCAGGTCTACCCCCTCGGCGCCACCGGCGCCCCCATCCGCCCCGAACCGGATGCGCCCCTGACCGAGCCCGGCGCCCCCGCGCGCCTTGACCGCCTGGAGCCCTGGCTCGACTACGCCGTCGAGCTCGGCGCCAACGGCCTGTCGCTCGGGCCGATCTTCGCCTCCTCCACCCACGGCTACGACACCACCGACCACCTGCGCATCGACCCCCGCCTGGGGGACGACTCCGCCTTCGACCGCCTCGCCGAAGCCTGCCGCGCCCGGGGCCTGGCCCTCATGCTCGACGGCGTCCTCGGGCACGTCGGCACCGAGCACCCCCTCTTCCGGGCCGCCCGCGCCGGGGGAGAGGAGCGCGGCCTCTTCCGCTTCGACGACGCCGCCGTCGGGGATGGTGCTGGCGGGAGCGATGCCGGACCGACCGGTCCCGGCTACGCCACCTTCGAGGGGCACGAGTCCCTGGCCGCCCTCAATCACGACTCCGCCGAGGTGCGCGACCTGGCCGTGCGGGTACTCACCCACTGGCTCGACCGCGGCGCGAGCGCCTGGCGCCTGGACGCCGCCTACGCCGTCGACCCCGCCTTCTGGGCGAGCGTCCTACCCGCCGTGCGCGAGCGCCACCCCGACGCCTGGTTCATGGGCGAGGTCATCCACGGCGACTACGCCGGCTTCGTGGAGGCCTCCACCGTGGACGCCGTCACCCAGTACGAGCTGTGGAAGGCGACTTGGAGCTCGCTGGCCGACGTCAACTTCTACGAGCTCGACTGGTGCCTCAAGCGCCACAACGAGCTGCTGGACCGGTTCATCCCGGCCACCTTCGTCGGCAACCACGACGTCACCCGCATCGCCAGCAAGGTCGGGGCCGGCGGGGCGGCGCTCGCCGTCGTCCTGCTCATGACCGTGGGCGGCGTGCCCAGCGTCTACTACGGGGACGAGCAGGCTTTCCGCGGGGTGAAGACCGAGACTCTCGGCGGCGACGACGAGGTCCGCCCCGCCCTGCCGGCCGCGCCGTCCGGGCTCGCGCCGCAGGGTGCCTGGATGCTGCGGCTCCACCAGGACCTCATCGGGCTGCGACGCCGCCACCCCTGGCTCGTGCGCGCCCGCACCGAGGTCACCGAGCTGGACAATCCGCGACTGTCCTACGACGCCGTCGGCGAGGAGGGCCAGCGGTTGCACGTGAGCCTGGCCCTGGAGCCGGCACCCCGCGCCGAGGTGCGCGCCCCCGGCGAGGCACCGCTCGTCGTCGAGCCGCCCGCGGAGTGA","MSRSAAPAWIDHAIWWQVYPLGATGAPIRPEPDAPLTEPGAPARLDRLEPWLDYAVELGANGLSLGPIFASSTHGYDTTDHLRIDPRLGDDSAFDRLAEACRARGLALMLDGVLGHVGTEHPLFRAARAGGEERGLFRFDDAAVGDGAGGSDAGPTGPGYATFEGHESLAALNHDSAEVRDLAVRVLTHWLDRGASAWRLDAAYAVDPAFWASVLPAVRERHPDAWFMGEVIHGDYAGFVEASTVDAVTQYELWKATWSSLADVNFYELDWCLKRHNELLDRFIPATFVGNHDVTRIASKVGAGGAALAVVLLMTVGGVPSVYYGDEQAFRGVKTETLGGDDEVRPALPAAPSGLAPQGAWMLRLHQDLIGLRRRHPWLVRARTEVTELDNPRLSYDAVGEEGQRLHVSLALEPAPRAEVRAPGEAPLVVEPPAE$","Alpha amylase","Cytoplasm, Extracellular","possible cyclomaltodextrinase or neopullalanase","cyclomaltodextrinase ","alpha amylase, catalytic region","","Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(15):7090-7094. PMID: 7624375Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995. 3(9):853-859. PMID: 8535779","","","

InterPro
IPR006047
Domain

Glycosyl hydrolase, family 13, catalytic region
PF00128	$\"[17-366]T$	Alpha-amylase

InterPro
IPR013781
Domain

Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80	$\"[5-382]T$	no description

noIPR
unintegrated

unintegrated
PTHR10357	$\"[52-260]T$ $\"[285-396]T$	AMYLASE
PTHR10357:SF11	$\"[52-260]T$ $\"[285-396]T$	ALPHA-AMYLASE
signalp	$\"[1-25]?$	signal-peptide

InterPro
IPR002716
Domain

PilT protein, N-terminal
PF01850	$\"[12-130]T$	PIN

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 12 to 130 (E_value = 6e-06) place ANA_2458 in the PIN family which is described as PIN domain.","","domain, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2459","2658094","2657762","333","5.28","-3.57","11971","GTGCGGGGCGGCCTACTCCGCGGGCGGCTCGACGACGAGTGGCGCCTTACCGGGGGCACGCACCTGGGCACAGGGCGTCTTCGCCACCCTTGGTATGATTCGGGTATGACTCAGAAGATCGCGGTGAGCCTCCCGGACGAGCAGGTCGTCTCGATCCGTCGCGCGGTCGAGCAGGGCAGGGCTCCGTCGGTGTCGGGCTTCATCAGCGCGGCGGTCGCCCGTGTGCAGCGGGAGGACGACCTCGCCCAGCTGCTGGACGATCTTGATCGCGAGCTCGGCCCCGTCGACGACGCCGACCTGGCTTGGGCGGATAAGGCACTGGGGCTGGCGTGA","VRGGLLRGRLDDEWRLTGGTHLGTGRLRHPWYDSGMTQKIAVSLPDEQVVSIRRAVEQGRAPSVSGFISAAVARVQREDDLAQLLDDLDRELGPVDDADLAWADKALGLA$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2459.1","2658285","2658812","528","4.76","-8.38","18961","ATGAGGCTGCCCCACATGAGCACCTTCAACGCATTCGAGATGAGCCCCGTCCCCGCGCCCAGCGAGGACGCCCAACCGCCCGAGCCCTTCCACGGCATCTACGGCATGCCGATGTTCGTCACCGTCCCGACGTCGGACCTGGACGCCTCGGTCGACTTCTGGACCGAGGCGCTGGGCTTCTTCACTCTGTTCAGCATTCCCGGCCAGCTGGTGCACCTGCGCCGCTGGGCCTTCCAGGACGTCCTCCTGGTGCCGGCGCCGCAGGCACCCGCCCCGGCCGATGGCCCCTCGATGAGCGTCAGCTTCTCCTGCGTCCTGTCCCAGATCGACGAGATCGCCGCGGCCTGCGAGCAGCGCCGACCGGGCAGCGTCACCGGCCCGCGCATCACGCCGTGGAACTCCCGCGAGGTCGAGGTCGTCACCCCCGAGGGCGTGCGTGTCATCCTCACCGCCGCCAGGCCCCTGGACCCGAACGGCCCGCAGGCCGAGGGCCTCCGGCGCATCGGCATCGAGGCGCCCGAGGCCTGA","MRLPHMSTFNAFEMSPVPAPSEDAQPPEPFHGIYGMPMFVTVPTSDLDASVDFWTEALGFFTLFSIPGQLVHLRRWAFQDVLLVPAPQAPAPADGPSMSVSFSCVLSQIDEIAAACEQRRPGSVTGPRITPWNSREVEVVTPEGVRVILTAARPLDPNGPQAEGLRRIGIEAPEA$","Glyoxalase/bleomycin resistance protein/dioxygenase","Periplasm, Membrane","","","","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.10	$\"[39-154]T$	no description

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[46-60]T$ $\"[60-75]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[9-140]T$	no description
PF00293	$\"[20-153]T$	NUDIX

InterPro
IPR000633
Family

Vinculin
PS00664	$\"[146-156]?$	VINCULIN_2

InterPro
IPR002667
Family

Isopentenyl-diphosphate delta-isomerase
PD004109	$\"[25-79]T$	IDI_STRAW_Q82MJ7;

noIPR
unintegrated

unintegrated
PTHR22769	$\"[26-136]T$	MUTT/NUDIX HYDROLASE

","BeTs to 14 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 3.2e-08. IPB000086 46-73","","","No significant hits to the PDB database (E-value < E-10).","Residues 20 to 153 (E_value = 9.3e-23) place ANA_2460 in the NUDIX family which is described as NUDIX domain.","","pyrophosphohydrolases including oxidative damage repair enzymes (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2463","2661852","2659753","2100","5.34","-11.62","74735","ATGAGTGACCACTGCGCAGCCTCCGAGGTCCCCGGCGCCCCCGACTGCCACTGCGGGTCCTCCAGCTCCAAGACCCTGGTGTCCGGCGCCCTGAGGGTTGCCCTGGCCGGCGCCCCCAACGCCGGCAAGACCTCCATCTACAACGCCCTGACCGGTCTGCACGCCAAGACCGGCAACTACCCCGGCGTCACCGTGGCGCGGTCGCTGGGGACCTGCCGGATCGGCGAGACCAGCCTGACCATCGAGGACCTGCCGGGCGCCTACTCCCTGAACCCGATCAGCCCCGACGAGCAGGTGGTGCGTGACGTCCTCACCGACGCCTCACAGAGCATCACCGTGCCCGACGCCCTCGTGGTCGTCGTCGACGCCACGACGCTACGGCGCGGACTGAACTTCGTCGCTGAGGCCCTCGCCCTGGAGCTGCCCACCTGCCTGGTGGTCACCATGACCGACGAGCTCACGCGGCGCGCCGGGCGCCTGGACGTGGCGGCCCTCGGGCAGGCCCTGGGGATCCCGGCGGTGCGGGTGGTCGGCAACCGCAGCATCGGCATCCCCGAGCTGCGCGAGCGCCTCACCGAGCTCTCCTCCTGGCAGCGCCCACCGCTGCCCGCGCCGACGGAGCCCACCGAGGTGGCCTCCTGGGCCGACTCCATCCTGGAGGCCGCCGACTACCAGGCACCCCAGCAGGACCGCATCACGACCGCCGTCGATAAGGTCCTGCTCAACCCCGTCCTGGGATCCCTGGTGTTCTTCGCCATCATGTACATCTTCTTCCAGGCGATCTTCACCTGGGCGGCACCTTTCCAGGACGCCGTCGAGGGAGGTTTCGGGTACCTGGGGGAGCTGGTGCACGGCTGGCTCGACGAGTCCCACCCGCTGCTGGCCGGGCTCCTGGGGGACGGTCTCATCGGGGGTGTGGGCTCGGTGCTCACCTTCGTGCCCCAGATCATCATCATGTTCCTCATCATCGCCTTCCTCGAAGGCGTGGGGTACATGTCGCGCGCCGCCTTCCTCATGGACCGGATCATGAGTCGGGCCGGACTGGAGGGGCGGGCCTTCGTGGCACTGCTGTCGTCCTTCGCCTGCGCGATCCCCGGGATCATGGCCACTCGCACGCTGCCCAGCGCCAAGGACCGGGTGGCCACGATGCTGGCCGCCCCCCTCATGACCTGCTCGGCACGGTTGCCCGTCTACGTCCTGCTCACCTCCATCATGGTGCCCGCCGACACGAAGATCGGGCCGCTGAACGCGCGCGGCACCGTCATGTTCGCCCTCTACCTGCTGGGGGCGGTCTCCGCGATGGTGGCCGCCTGGGTGGTCAAGCGCCTCACCGACCGCGGCGGGGTGCTGCTGCCCTTCTACATGGAGATGCCGCCCTACCGGCTGCCGCGGCCGCGCACGGTTCTCATCATGGTGTGGGACGCCTGCAAGGGCTTCGTGAAGAAGGCCGGGACCGTCATCGCCCTGACCACGCTCATCCTGTGGGTGCTGCTCAACGTTCCGATGCGCTCCGATGAGCAGTTCAACGCCCACTGCTCCGCCAGCGCCGAGTGCGCGGCCGTGTCCGCGGCGGTGGAGGACCCGGCGTCGTCGACCATCAAGGGCGATGACGGGCAGGTCATCACCGACCCCGAGGAGCTCGGCAAGCTGCTGGAGGCCCAGAAGACCTCCTACACGATGGACAACTCCTGGGCGGCCGCCATCGGCAAGACGGTGCAGCCGGTCTTCGAGCCCCTGGGCTTCGAGTGGCGCGTCAACGTGGCGATCCTGTCCTCGCTGGCGGCGCGCGAGACCTTCGTGGCCACCATCGGCCAGATCGCCGCAGCCGAGGACCCCGAGGAGCCCAGCGCGCACCTGGCCACGATGACGTACCAGCAGGACACACTCACCAACAAGGCCGGCGACCAGCTGTTCAACCCGGCCACGATCGCGGCGATCCTGGTGTTCTTCGTCTACGCCCTGCAGTGCATGGCCACGGCTGCGGCGATGCGCCGCGAGACCGGCACCTGGAAGTGGCCGATCATCGCCTACACCTACATGTTCGTCACGGCGTGGGTCATGGCGGCCCTCACGAGGGTCATCGTCGCCATGCTCATGTAG","MSDHCAASEVPGAPDCHCGSSSSKTLVSGALRVALAGAPNAGKTSIYNALTGLHAKTGNYPGVTVARSLGTCRIGETSLTIEDLPGAYSLNPISPDEQVVRDVLTDASQSITVPDALVVVVDATTLRRGLNFVAEALALELPTCLVVTMTDELTRRAGRLDVAALGQALGIPAVRVVGNRSIGIPELRERLTELSSWQRPPLPAPTEPTEVASWADSILEAADYQAPQQDRITTAVDKVLLNPVLGSLVFFAIMYIFFQAIFTWAAPFQDAVEGGFGYLGELVHGWLDESHPLLAGLLGDGLIGGVGSVLTFVPQIIIMFLIIAFLEGVGYMSRAAFLMDRIMSRAGLEGRAFVALLSSFACAIPGIMATRTLPSAKDRVATMLAAPLMTCSARLPVYVLLTSIMVPADTKIGPLNARGTVMFALYLLGAVSAMVAAWVVKRLTDRGGVLLPFYMEMPPYRLPRPRTVLIMVWDACKGFVKKAGTVIALTTLILWVLLNVPMRSDEQFNAHCSASAECAAVSAAVEDPASSTIKGDDGQVITDPEELGKLLEAQKTSYTMDNSWAAAIGKTVQPVFEPLGFEWRVNVAILSSLAARETFVATIGQIAAAEDPEEPSAHLATMTYQQDTLTNKAGDQLFNPATIAAILVFFVYALQCMATAAAMRRETGTWKWPIIAYTYMFVTAWVMAALTRVIVAMLM$","Ferrous iron transport protein B","Membrane, Cytoplasm","Ferrous iron transport protein B","ferrous iron transport protein B","Ferrous iron transport protein B domain protein","","Vernet C., Ribouchon M.T., Chimini G., Pontarotti P. Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm. Genome 1994. 5(2):100-105. PMID: 8180467","","","

InterPro
IPR002917
Domain

GTP-binding protein, HSR1-related
PF01926	$\"[31-151]T$	MMR_HSR1

InterPro
IPR005289
Domain

GTP-binding
TIGR00650	$\"[36-86]T$	MG442: GTP-binding conserved hypothetical p

InterPro
IPR006073
Domain

GTP1/OBG
PR00326	$\"[33-53]T$ $\"[54-72]T$	GTP1OBG

InterPro
IPR011619
Domain

Ferrous iron transport protein B, N-terminal
PF02421	$\"[213-305]T$	FeoB_N

InterPro
IPR011640
Domain

Ferrous iron transport B, C-terminal
PF07664	$\"[421-475]T$	FeoB_C

InterPro
IPR011642
Domain

Nucleoside recognition
PF07670	$\"[309-405]T$ $\"[480-670]T$	Gate

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[29-189]T$	no description
PTHR11702	$\"[33-86]T$	DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED
tmhmm	$\"[248-268]?$ $\"[292-312]?$ $\"[318-338]?$ $\"[353-373]?$ $\"[383-401]?$ $\"[422-440]?$ $\"[483-501]?$ $\"[636-656]?$ $\"[675-695]?$	transmembrane_regions

","BeTs to 14 clades of COG0370COG name: Fe2+ transport systemFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0370 is a-m-k--qvd-l-cefg-s-uj----Number of proteins in this genome belonging to this COG is 2","***** IPB003373 (Ferrous iron transport protein B) with a combined E-value of 1.2e-143. IPB003373A 33-63 IPB003373B 64-91 IPB003373C 94-116 IPB003373D 122-155 IPB003373E 233-265 IPB003373F 323-373 IPB003373G 379-425 IPB003373H 452-489 IPB003373I 582-607 IPB003373J 641-666***** IPB006073 (GTP1/OBG GTP-binding protein family signature) with a combined E-value of 2.3e-11. IPB006073A 33-53 IPB006073B 54-72***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 4e-07. IPB002917 35-67","","","No significant hits to the PDB database (E-value < E-10).","Residues 31 to 151 (E_value = 3.1e-20) place ANA_2463 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 184 to 305 (E_value = 6.8e-24) place ANA_2463 in the FeoB_N family which is described as Ferrous iron transport protein B.Residues 309 to 405 (E_value = 9.2e-15) place ANA_2463 in the Gate family which is described as Nucleoside recognition.Residues 421 to 475 (E_value = 6.6e-17) place ANA_2463 in the FeoB_C family which is described as Ferrous iron transport protein B C terminus.Residues 480 to 670 (E_value = 2.2e-07) place ANA_2463 in the Gate family which is described as Nucleoside recognition.","","iron transport protein B (feoB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2465","2662283","2661849","435","7.04","0.10","15715","GTGCTGCCCCGCATCGCGGCCGAGAACAGACTCAAGGATCCGAGGAACTCCGAGGTCAACATGGCGACTGCAGTCCCACACCACCGCACGACGCCGGCCGGCACCGGCGGCGCCCCCTCTTCCGCCCACCCATCCCTGTCCGATCTGCGTCTGGGGACCAGCTGCCGGGTCGTCGGCCTGCAGGAGGACACGGCCGACGACCCCATCGCCAAGCGGCTGAGCAACCTGGGCTTCGTGCCCGGCCGGACCGTGACGCCCCTGCGCCGCGCCCCGCTGGGCGACCCGGTGGTCTACCGCGTCGCCGACTACGAGCTGTGCCTGCGCCGCCACGAGGCCCGCATGGTTCACGTCGAGGTCCTCACCGAGGCCGACGTCGTCGAACCCCTCACCGGGCAGCGGGCCGACACTACCGACCGTGAGGAGCAGCGCCCATGA","VLPRIAAENRLKDPRNSEVNMATAVPHHRTTPAGTGGAPSSAHPSLSDLRLGTSCRVVGLQEDTADDPIAKRLSNLGFVPGRTVTPLRRAPLGDPVVYRVADYELCLRRHEARMVHVEVLTEADVVEPLTGQRADTTDREEQRP$","Ferrous iron transport protein A","Cytoplasm","putative ferrous iron transport protein","hypothetical protein predicted by Glimmer/Critica","FeoA family protein","","Kammler M., Schon C., Hantke K. Characterization of the ferrous iron uptake system of Escherichia coli. J. Bacteriol. 1993. 175(19):6212-6219. PMID: 8407793","","","

InterPro
IPR007167
Family

FeoA
PF04023	$\"[44-119]T$	FeoA

","BeTs to 8 clades of COG1918COG name: Fe2+ transport systemFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1918 is a-m-k---vd-l-cefg-s-uj----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 44 to 119 (E_value = 3.9e-17) place ANA_2465 in the FeoA family which is described as FeoA domain.","","ferrous iron transport protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2466","2663011","2662475","537","5.88","-5.96","18960","GTGCCCGTCGTTCCCACGCACCCGACAACCACGCCGGACCCCGACGTGCTGCGGTGGGTCATTCCCGACGGCCTGCTGCCCTTTACCGGGGAGGTCGCCCACGCCCCGGCGCTTCTCCAACAGCTCCTGGATGATGGCACCCTGCGCTCGGTGAGAGTCGACGGCGGCGGGGTGCTCACCCTCCTGGGCACCGGCCACGACTGGCGCACGGAGGGGGCCCGAGTGCGATCCGCCCTGGTGGACGCCCTGGGCGCCCCGAAGTCGTGGAGGGGTGCCGACACCGCCCACGCCTCCGGCCCCGACGACGCCCTGGAGGCGGCCGCCCGGCAGATCGCCGACGGTTCCCTGGGGACCTTCGTTAACAGCCACGGGGGCGCGCTCGTGGTGCACTCGGTGCGCGACGGCGTCGTCGAGATCGCCATGGAGGGCGCCTGCGACCACTGCCCGGCCGCGGAGATCACGATGCACGCGCGCTTCGAGCACCTGCTGCGGCGCCGGTGCCCCTGGCTGGTCGAGGTCCGCCGGATCGACGAGTAG","VPVVPTHPTTTPDPDVLRWVIPDGLLPFTGEVAHAPALLQQLLDDGTLRSVRVDGGGVLTLLGTGHDWRTEGARVRSALVDALGAPKSWRGADTAHASGPDDALEAAARQIADGSLGTFVNSHGGALVVHSVRDGVVEIAMEGACDHCPAAEITMHARFEHLLRRRCPWLVEVRRIDE$","Nitrogen-fixing NifU-like protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

InterPro
IPR001075
Domain

Nitrogen-fixing NifU, C-terminal
PD002830	$\"[116-176]T$	Q8CPV7_STAEP_Q8CPV7;
PF01106	$\"[108-176]T$	NifU

","BeTs to 11 clades of COG0694COG name: Thioredoxin-like proteins and domainsFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0694 is ao----y-----bcefghs-ujxi--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 108 to 176 (E_value = 0.0018) place ANA_2466 in the NifU family which is described as NifU-like domain.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2467","2665223","2663094","2130","5.76","-8.91","75635","GTGAGCACCCACGACACCACGAGACACGCCTCCGGGCAGTCGCAGCACTGCGAGCAGCCCTACGACGGCGCCGACTGCCACTGCGGCTCAGGAAGCTCCAAGACCCTGGTGGCCGGCGCCCCCCGTGTCGCCCTGGCCGGCGCCCCCAACGCCGGCAAGACCTCCATCTACAACGCCCTGACCGGCCTGCACGCCAAGACCGGCAACTACCCCGGCGTCACCGTCCAGCGGTCGATGGGAACCTGCAAGGTCGGCGGCAAGACCCTGACCATCGAGGACCTGCCGGGCGCCTACTCCCTGGACCCGATCAGCCCCGACGAGCAGATCGTCCACGACGTCCTCACCGGGACCTCGACCACGGTCAGCGCCCCGGACGCCCTGGTCATCGTCGTCGACGCCACGACCCTGCAGCGCGGCATGAACTTCATCGCCGAGGCCCTCGCCCTGGAGCTGCCCACCTGCCTGGTGGTCACCATGACCGACGAACTCAGCCGCCGCACGGGTCGGCTCAACGTCGCCGCTCTCGGACAGGCCCTGGGCATCCCGGCCGTGCGAGTCATCGGACACCGCGGCGTCGGCATGCCTGACCTGCGCGCCCAGCTCGCCCAGGTCGAGAACTGGCAGCGCACCCCGCTGCCGCCGCCCACCGACCCCGACGAGATCACCTCCTGGGCCGACTCGGTGCTGGCCGCGGCGGACTACCAGGCGCCCCAGAACGACCAGATCACCTCTGCCGTGGACAAGGTCCTGCTGCGCCCCATCCCCGGCACCATCGTGTTCTTCACGATCATGTTCCTCTTCTTCCAGGCGATCTTCACCTGGGCGGCCCCCTTCCAGGACGCCGTCGAAGGAGGTTTCGGGTATCTGGGGCAGCTGGTGCACGGCTGGCTCGATGAGTCCCATCCGCTCATCGCCGGGCTCCTGGGCGACGGCATCATCGGGGGTGTGGGCGCCGTGCTCACCTTCATCCCCCAGATCATCATCATGTTCCTCATCATCTCCGTCCTGGAGGGCGTGGGGTACATGTCGCGTGCCGCCTTCCTCATGGACAAGGTCATGAGTATCGCCGGCCTGGAGGGGCGGGCCTTCGTGGCCCTGCTGTCCTCGCTGGCCTGCGCGATCCCCGGGATCATGGCCACCCGCACGCTGCCCTCCACGAAGGACCGGGTGGCCACGATGCTGGCCGCCCCCCTCATGACCTGCTCGGCCCGCCTGCCCGTCTACGTCATCATGATCTCCTTGACGGTCGACGGCGACGCCAAGGTCGGCCCCTTCGGGACGCGCGGTGTGGTCATGTTCGCCCTCTACCTGCTGGGCGCGGTCTCCGCGATGGCGGCCGCCTGGGTGGTCAAGCAGCTCACCGACCGCGGCGGGGTGCTGCTGCCCTTCTACATGGAGATGCCGCCCTACCGCATGCCCCGCCTGCGCACCGTCTTCATCATGGTGTGGGACGCCTGCAAGGGCTTCCTGAAGAAGGCCGGCACGATCATCACCCTGACCACCGTCATCCTGTGGGTGCTGCTCAACGTCCCCATGCGCTCGGACGCCCAGTTCGAGGCCTTCTGCGCCTCCGACAAGCAGTGCGCCGCCATCGCGGCGGCCGTGGACAAGCCGGAGTCCTCCACCGTCAAGGGCGATGACGGGCAGGTCATCACCGACGCCGAGGAGCTCGGCAAGCTGTTGGATGCCCAGAAGACCTCCTACACGATGGACAACTCCTGGGCGGCCAAGGGGGGCAAGGTGGTCCAGCCGGTCTTCGAGCCCCTGGGCTTCGACTGGCGCATCAATGTCGCCACCCTGTCCTCGCTGGCGGCGCGCGAGACCTTCGTGGCCACCCTGGGACAGATCGCCGCCGCCGAGGACCCCGAGGACCCCGGCGCCCACCTGGCCACGATGACCTACCAGCAGGACACCCTGACCAACAAGGCCGGTGACCAGCTGTTCAACCCGGCCACCGTCATCGCGATCCTCGTGTTCTTCGTCTACGCCCTGCAGTGCATGGCCACGGCCGGTGCGATGCGCCGCGAGACCGGCACCTGGAAGTGGCCGGTCATCGCCTTCACCTACATGTTCGTCATGGCCTGGGTCATGGCGGCGCTCAGCCGCGCACTCGTGGCCGCCTTCATGTAG","VSTHDTTRHASGQSQHCEQPYDGADCHCGSGSSKTLVAGAPRVALAGAPNAGKTSIYNALTGLHAKTGNYPGVTVQRSMGTCKVGGKTLTIEDLPGAYSLDPISPDEQIVHDVLTGTSTTVSAPDALVIVVDATTLQRGMNFIAEALALELPTCLVVTMTDELSRRTGRLNVAALGQALGIPAVRVIGHRGVGMPDLRAQLAQVENWQRTPLPPPTDPDEITSWADSVLAAADYQAPQNDQITSAVDKVLLRPIPGTIVFFTIMFLFFQAIFTWAAPFQDAVEGGFGYLGQLVHGWLDESHPLIAGLLGDGIIGGVGAVLTFIPQIIIMFLIISVLEGVGYMSRAAFLMDKVMSIAGLEGRAFVALLSSLACAIPGIMATRTLPSTKDRVATMLAAPLMTCSARLPVYVIMISLTVDGDAKVGPFGTRGVVMFALYLLGAVSAMAAAWVVKQLTDRGGVLLPFYMEMPPYRMPRLRTVFIMVWDACKGFLKKAGTIITLTTVILWVLLNVPMRSDAQFEAFCASDKQCAAIAAAVDKPESSTVKGDDGQVITDAEELGKLLDAQKTSYTMDNSWAAKGGKVVQPVFEPLGFDWRINVATLSSLAARETFVATLGQIAAAEDPEDPGAHLATMTYQQDTLTNKAGDQLFNPATVIAILVFFVYALQCMATAGAMRRETGTWKWPVIAFTYMFVMAWVMAALSRALVAAFM$","Ferrous iron transport protein B","Membrane, Cytoplasm","Ferrous iron transport protein B","K04759 ferrous iron transport protein B","GTP-binding protein, HSR1-related","","Vernet C., Ribouchon M.T., Chimini G., Pontarotti P. Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm. Genome 1994. 5(2):100-105. PMID: 8180467","","","

InterPro
IPR002917
Domain

GTP-binding protein, HSR1-related
PF01926	$\"[41-161]T$	MMR_HSR1

InterPro
IPR006073
Domain

GTP1/OBG
PR00326	$\"[43-63]T$ $\"[64-82]T$	GTP1OBG

InterPro
IPR011619
Domain

Ferrous iron transport protein B, N-terminal
PF02421	$\"[210-315]T$	FeoB_N

InterPro
IPR011640
Domain

Ferrous iron transport B, C-terminal
PF07664	$\"[431-485]T$	FeoB_C

InterPro
IPR011642
Domain

Nucleoside recognition
PF07670	$\"[319-415]T$ $\"[490-680]T$	Gate

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[41-216]T$	no description
PTHR23305	$\"[45-71]T$	GTP-BINDING PROTEIN-RELATED
PTHR23305:SF1	$\"[45-71]T$	GTP-BINDING PROTEIN-RELATED
tmhmm	$\"[258-278]?$ $\"[302-322]?$ $\"[328-348]?$ $\"[363-383]?$ $\"[393-415]?$ $\"[430-450]?$ $\"[493-511]?$ $\"[646-666]?$ $\"[685-705]?$	transmembrane_regions

","BeTs to 14 clades of COG0370COG name: Fe2+ transport systemFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0370 is a-m-k--qvd-l-cefg-s-uj----Number of proteins in this genome belonging to this COG is 2","***** IPB003373 (Ferrous iron transport protein B) with a combined E-value of 6.6e-139. IPB003373A 43-73 IPB003373B 74-101 IPB003373C 104-126 IPB003373D 132-165 IPB003373E 243-275 IPB003373F 333-383 IPB003373G 389-435 IPB003373H 462-499 IPB003373I 592-617 IPB003373J 651-676***** IPB006073 (GTP1/OBG GTP-binding protein family signature) with a combined E-value of 2e-11. IPB006073A 43-63 IPB006073B 64-82***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 4.2e-08. IPB002917 45-77","","","No significant hits to the PDB database (E-value < E-10).","Residues 41 to 161 (E_value = 2.2e-20) place ANA_2467 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 172 to 315 (E_value = 4.3e-17) place ANA_2467 in the FeoB_N family which is described as Ferrous iron transport protein B.Residues 319 to 415 (E_value = 9.9e-15) place ANA_2467 in the Gate family which is described as Nucleoside recognition.Residues 431 to 485 (E_value = 3.1e-16) place ANA_2467 in the FeoB_C family which is described as Ferrous iron transport protein B C terminus.Residues 490 to 680 (E_value = 1.4e-07) place ANA_2467 in the Gate family which is described as Nucleoside recognition.","","iron transport protein B (feoB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2468","2665693","2665220","474","8.53","3.31","16878","TTGACCTGCTGCGAGACAGAGAAGCGTTCCCTTAGACTCCTATTGACGAAGCCCTCTTCATGTCGACCCGAGGACACCATGGATTCTGCTGTTCCACGACACCGCGCCCCCGCCAGCACCACTAACCTTCCCGAACCGGGTGCTGCCACCTTCGCACTGTCGGACCTGAGCCCCGGCACCAGCGGACGCATCACCGGCCTGGCCGACGACGGCGTCGGCGGCGTCCTGGTCAAGCGCCTGCGCAACCTGGGCTTCGTCCCCGGCCGGATCGCCACGCCGCTGCGCCGTGCCCCGATGGGGGACCCGGTGGTCTACCGCGTCTCCGACTACGAGCTGTGCCTGCGTCGCCAGGAGGCCAGGCTCATCCAGGTCACCACCGTGGAGGCCGAGAACCGCATCATCCTCCAACCCCGGCCGGCCGGACGGCATGCGGCCGACGACCCCGCAGCACCGAACACGGGAGAGACTCTGTGA","LTCCETEKRSLRLLLTKPSSCRPEDTMDSAVPRHRAPASTTNLPEPGAATFALSDLSPGTSGRITGLADDGVGGVLVKRLRNLGFVPGRIATPLRRAPMGDPVVYRVSDYELCLRRQEARLIQVTTVEAENRIILQPRPAGRHAADDPAAPNTGETL$","Ferrous iron transport protein A","Cytoplasm, Periplasm","putative ferrous iron transport protein","hypothetical protein predicted by Glimmer/Critica","FeoA family protein","","Kammler M., Schon C., Hantke K. Characterization of the ferrous iron uptake system of Escherichia coli. J. Bacteriol. 1993. 175(19):6212-6219. PMID: 8407793","","","

InterPro
IPR007167
Family

FeoA
PF04023	$\"[51-126]T$	FeoA

","BeTs to 8 clades of COG1918COG name: Fe2+ transport systemFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG1918 is a-m-k---vd-l-cefg-s-uj----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 51 to 126 (E_value = 1.4e-15) place ANA_2468 in the FeoA family which is described as FeoA domain.","","ferrous iron transport protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2469","2666213","2666013","201","9.46","2.88","7354","ATGACAGCACAGAATTCTACTGGTTTCGATTGGCCCGCCCGTTCCGCCAACAAGATCTGGCTCGGCGTCTGCGGAGGCCTGGCCAACAAATGGAACGTCAATGCCTGGCTGGTCCGCGCCGCCTTCTTCTTCTTTGTGGTGCCGCTCGGCTACGTCTACTACCTGGGCGCCCAGAACATGCCCGATCCCGCCACCCGCTGA","MTAQNSTGFDWPARSANKIWLGVCGGLANKWNVNAWLVRAAFFFFVVPLGYVYYLGAQNMPDPATR$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[35-55]?$	transmembrane_regions

","BeTs to 4 clades of COG1983COG name: Putative stress-responsive transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription] Functional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG1983 is ----k---v--lb-e-g---------Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2470","2667306","2666551","756","5.74","-6.90","27043","ATGACCGCGCGCTATGAGCACACCACTGACGGCCCCGCCCGCGGGCACCTGCGCCTGCTCCAGCTCTACCCGCGGGACATGAACATCTACGGCGACTGGGGCAACACGCTCGTGCTGGCGCGGCGCGCCCAGTGGCAGGGCTACGACGTCGAGCTCCTCTCCTACGACCCGGGCGACGAGCTGCCCGGCGACATCGACATCCTCGTGGGCGGCGGCGGCCAGGACTCCGGCCAGGACCGCATCAAGGAGGATCTGGTCAAGGTCGGCCCCACCCTCAAGGCCTGGGCGGCCGACGGCGTCCCGATGCTGGCGATCTGCGGCCTCTACCAGCTCTTCGGGCACGGCTTCACCACTGCCAAGGGCCAGGAGATCCCCGGCATCAGCCTCATGGACGCCCACACGGTGGCCGGAGACACCCGCCTCATCGGCAACATCACCCTGAACACCGAGAACTTCGGCGCGGTGGTCGGCTACGAGAACCACTCCGGCCTGACCACCCTGGGGTCGGGCGCGCGCCCCTTCGGCACCGTGAAGATGGGCGACGGCAACAACGGCAAGGACTCCACCGAGGGCGGGCGCGTCCACCACGTCATCGGCACCTACCTGCACGGCTCCCTGCTGCCCAAGAACCCGACCGTGGCCGACTGGTTGCTGGCCCGCGCCGCCGAGCACGCCGGCACCACCTGGGAGCCCGAGCCGCTCGACGACACCTGGGCCGAGCGCGCCCGCGCCGTGGCCATGTCCCGGCCCCGCTGA","MTARYEHTTDGPARGHLRLLQLYPRDMNIYGDWGNTLVLARRAQWQGYDVELLSYDPGDELPGDIDILVGGGGQDSGQDRIKEDLVKVGPTLKAWAADGVPMLAICGLYQLFGHGFTTAKGQEIPGISLMDAHTVAGDTRLIGNITLNTENFGAVVGYENHSGLTTLGSGARPFGTVKMGDGNNGKDSTEGGRVHHVIGTYLHGSLLPKNPTVADWLLARAAEHAGTTWEPEPLDDTWAERARAVAMSRPR$","Glutamine amidotransferase; CobB/CobQ family","Cytoplasm, Periplasm","possible cobyric acid synthase CobQ","glutamine amidotransferase; CobB/CobQ family","CobB/CobQ domain protein glutamine amidotransferase","","Galperin M.Y., Grishin N.V. The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase. Proteins 2000. 41(2):238-247. PMID: 10966576","","","

InterPro
IPR011698
Domain

CobB/CobQ-like glutamine amidotransferase
PF07685	$\"[58-211]T$	GATase_3

","BeTs to 3 clades of COG3442COG name: Predicted glutamine amidotransferaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG3442 is ----------rl-c------------Number of proteins in this genome belonging to this COG is 1","***** IPB011698 (CobB/CobQ-like glutamine amidotransferase) with a combined E-value of 7.3e-20. IPB011698A 21-61 IPB011698B 64-80 IPB011698C 99-113","","","No significant hits to the PDB database (E-value < E-10).","Residues 58 to 211 (E_value = 1.1e-34) place ANA_2470 in the GATase_3 family which is described as CobB/CobQ-like glutamine amidotransferase domain.","","cobyric acid synthase CobQ (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2471","2668613","2667303","1311","5.30","-9.82","46671","ATGCGTTCTCGTCTTACGGTCGCTCTCGGCCGCACAGCGCGCCTGGCCGCCCGCGTGCGCGGCGGCGGCAGCGGCGGCACCGCCTTCCCCGGCCTGGTCATGGAGCGCACCGACCCCGGTTTCCTGGAGCGCACCCTTGGCCGTCTGCCCCGCGGCGTTATCGTGGTCTCGGGCACCAACGGCAAGACCACGACCACCAAGATGGTCGTCCAGCTCCTGCGCGAGCAGGGCCTGAAGGTCTTCACCAACCGGACCGGCTCGAACTTCGTGCGCGGCGTGCTCGCCTCCCTGCTCACCGAGGTCGACGCCGCCGGCAACCTGGACGCCGACATCGCCATCCTCGAGCTCGACGAGGCCCACGCCGTGCACTTCGTGGCCCGGGTCCGCCCGCGCGCCTGCCTCCTGCTCAACGTCATGCGCGACCAGCTCGACCGCTTCGGCGAGATCGACTACACCGCCTCCCTGCTGCACTCGATCGCCCAGGCCACCAGCGACGTCGTCGTGCTCAACGGTGACGACCCGCGCCTGGCCGCCCCCGCCTTCCTGGAGGGCGTCAGCGCCCGCGTCGTCTCCTTCGGCGCCGGGGAGGACCTGCGCTCCCTGTTCCTGTCCGACGACGACCTGCGCACCGGCCTGGTCAGCCCCCGTCAGGCCGGCCAGGCCCCCGGACCGCGAGTCACCCTGGAGGCCATCGACGGCCAGCGCGCCACCGTGCGCGTGGACGGGGTCTCCCACGAGGTCGACTTCACCATCCCGGGCGTTCACAACCTGCTCAACGCCTGCGCCGCCCTCGGGGTGGTACTGGAGGTGCTGGGCGAGGACGCCGACCTGCCCGGACTGCTGACCACCCTGGGCACCGTGCAGGCCGCCTTCGGCCGCGGCGAGGTCCTTACCCTGGACGGCCGCCCCATCCAGCTGTCCCTGGTCAAGAACCCGGCCGGCTTCCGCATGGGCCTGCTCTCGGCAGCCTCCCAGGCGCAGGACGGCGAGGTCGTGGTCGTGGCCATCAACGACGAGTACGCCGATGGCCGGGACATGTCCTGGCTGTGGGACGTGGACTTCTCGGCCCTGCGCGCCGGCGGGGTCGCTGTCGTCACCGGGGTGCGGGCCTGGGACATGGCCCTGCGGCTGCGCTACGACGAGGTCGAGGTCGCCGAGGTCGAACCCGACCTGCGCCGGGCCGTGGCCCTCATGCGCCGGGTGGCCGCCGACACCGACCGCCCCATGCGGATCTTCACCACCTACACCGCGATGCTGGCCCTGCGCTCGATCCTGGGCGAGATGACGGACGTTGAGGAGGTCATGTCATGA","MRSRLTVALGRTARLAARVRGGGSGGTAFPGLVMERTDPGFLERTLGRLPRGVIVVSGTNGKTTTTKMVVQLLREQGLKVFTNRTGSNFVRGVLASLLTEVDAAGNLDADIAILELDEAHAVHFVARVRPRACLLLNVMRDQLDRFGEIDYTASLLHSIAQATSDVVVLNGDDPRLAAPAFLEGVSARVVSFGAGEDLRSLFLSDDDLRTGLVSPRQAGQAPGPRVTLEAIDGQRATVRVDGVSHEVDFTIPGVHNLLNACAALGVVLEVLGEDADLPGLLTTLGTVQAAFGRGEVLTLDGRPIQLSLVKNPAGFRMGLLSAASQAQDGEVVVVAINDEYADGRDMSWLWDVDFSALRAGGVAVVTGVRAWDMALRLRYDEVEVAEVEPDLRRAVALMRRVAADTDRPMRIFTTYTAMLALRSILGEMTDVEEVMS$","UDP-N-acetylmuramyl tripeptide synthetase","Cytoplasm","UDP-N-acetylmuramyl tripeptide synthetasehomolog murC","hypothetical protein","domain of unknown function DUF1727","","Sun X., Bognar A.L., Baker E.N., Smith C.A. Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(12):6647-6652. PMID: 9618466","","","

InterPro
IPR001645
Family

Folylpolyglutamate synthetase
PS01011	$\"[54-77]?$	FOLYLPOLYGLU_SYNT_1

InterPro
IPR013221
Domain

Mur ligase, middle region
PF08245	$\"[54-267]T$	Mur_ligase_M

InterPro
IPR013564
Domain

Domain of unknown function DUF1727
PF08353	$\"[308-418]T$	DUF1727

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.10	$\"[53-285]T$	no description
PTHR23135	$\"[56-276]T$	MUR LIGASE FAMILY MEMBER
PTHR23135:SF2	$\"[56-276]T$	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 5 clades of COG0769COG name: UDP-N-acetylmuramyl tripeptide synthaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0769 is --m----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 2","***** IPB013221 (Mur ligase, middle region) with a combined E-value of 7.6e-09. IPB013221A 56-65 IPB013221C 253-263***** IPB001645 (Folylpolyglutamate synthetase) with a combined E-value of 9.5e-07. IPB001645A 53-95","","","No significant hits to the PDB database (E-value < E-10).","Residues 54 to 267 (E_value = 8.2e-14) place ANA_2471 in the Mur_ligase_M family which is described as Mur ligase middle domain.Residues 308 to 418 (E_value = 1.9e-40) place ANA_2471 in the DUF1727 family which is described as Domain of unknown function (DUF1727).","","tripeptide synthetase homolog murC (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2472","2670436","2668808","1629","6.74","-1.16","57130","GTGACCGAGCCTCCATGCGACTCCGCCGCCCCTACCGCCGCCTCCCCCTCCCCCCGAGCCCCCCGACGCCTGAAGTACGTCGAGGCCATCCTGTGCATCGGCTTCACCCTGGCCTTCCTCGTGTGGACCTACTTGAGCGCCCCGGGACCGCTCGCCCCCGGCGACACACACCGCTCCCCCGCCATCGACGCCCTCCTGCCGACCCCCGACGCCCAGCTGCGGTCGGCCGCCGGCCAGCTCGCCGAGGCCTTCGCGACCCTCACCCACCCCATCCTCATCCTCGGGCTCATCGTGGCCGGGGTCGCCTACGCCTACACGGCCCGCATGCGCCGCCTGAGCGTCTCGCTGGCCATCGCCGCCGCCGGCATCCCCACGCAGTACCTCATCGCCCTGTACCTGGCCCGCCCCGCCCCGGGCTCCACCTTCTCCGACTCCATCGCCGCCTTCGAGTACTCCTACCCCAACGCGCACATCACGGCGATGACCCTGGCCTCCTGGGTCCTGGTGACCCTCGCGCGCGCCCACCACCGCAGCACCATGGTCGCCGCCGGCACCGTCCTGGGCTACGCGGCCGTCGCCGTGACAGCCGTCAGCCAGTGGTACATGGGCCTAGCTGCGCTCAGCGACCTCATCGGCGGCTTCCTCCTGGGTGCCGCCTTCGCGAACCTGGCCCTGCGGGTCGGCGGCATCGACGCGATCCTCACCAGCTGGGTCAATCGCCGCCTGTCGCGCTCCAGCAGCGAGAAGCGCGCCGCCGTCATCTACAACCCCACCAAGTTCGACGACCTCTCGCTCCTGCGCCGTCGGGTCGCCGCCGAGGTGCGCGCCGCCGGCTGGCTGCCCACCGTCTGGCTGGAGACCACCCCCGACGACCCCGGCCGCTCCATGGCCCACCGCGCCCTGGAGGCCGGCGTCGACCTGGTCATGGTGGCCGGCGGCGACGGCACCGTGCGCGCCGTCTCCTCCGAGCTGGCCGGCACCGAGATGCCGATGGCCCTCATCCCCGCCGGCACCGGCAACCTCCTGGCCCGGAACCTGTCCATCCCCCTGGACACCGACGCCGCCATCCGCCTGGCCCTGCACGGCCGCCTCCAGGCCATCGACATGGTCACTTGCGCCTTCGACGACGGCCAGGAGCGCTTCGTCGTCATGGCCGGTATGGGCCTGGACGCCCAGATCATGGAGTCCACCGACCTGGGCCTGAAGAAGGTCATCCGCTCGGGCGCCTACGCGGTGGCCGCCGTCCAGAACGCGGTCCCCGACCCCTTCACCGCCACCATCACGCTCGACGACGCTCCCCCGGTGCGCCGTCGGATGGTCATGGCCCTCATGGGCAATGTCGGCACCATCACCGGCGGCATGACGCTCTTCCCGCGGGCCACCCCCTCCGACGGCCTGGTCGACCTGCTCCTGGCCAGCCCCGGCAAGGTCGTGGACTGGGCGCGCCTGGGGGCGCAGATCCTCACTGGCCAGGAGATGGAGGGCTTCACCCTCACCCGGGCCCGGAAGGTCCTCATCGAGGCCGACCGTCCCGTCCCCTTCGAGCTCGACGGCGACACGGCCGGCTCCACCCGCACCCTGCGCGCCGAGGTCGAGGACGGCGCCCTGCACGTCGTCGTCCCCCAGTGA","VTEPPCDSAAPTAASPSPRAPRRLKYVEAILCIGFTLAFLVWTYLSAPGPLAPGDTHRSPAIDALLPTPDAQLRSAAGQLAEAFATLTHPILILGLIVAGVAYAYTARMRRLSVSLAIAAAGIPTQYLIALYLARPAPGSTFSDSIAAFEYSYPNAHITAMTLASWVLVTLARAHHRSTMVAAGTVLGYAAVAVTAVSQWYMGLAALSDLIGGFLLGAAFANLALRVGGIDAILTSWVNRRLSRSSSEKRAAVIYNPTKFDDLSLLRRRVAAEVRAAGWLPTVWLETTPDDPGRSMAHRALEAGVDLVMVAGGDGTVRAVSSELAGTEMPMALIPAGTGNLLARNLSIPLDTDAAIRLALHGRLQAIDMVTCAFDDGQERFVVMAGMGLDAQIMESTDLGLKKVIRSGAYAVAAVQNAVPDPFTATITLDDAPPVRRRMVMALMGNVGTITGGMTLFPRATPSDGLVDLLLASPGKVVDWARLGAQILTGQEMEGFTLTRARKVLIEADRPVPFELDGDTAGSTRTLRAEVEDGALHVVVPQ$","Diacylglycerol kinase","Membrane, Cytoplasm","conserved hypothetical protein TIGR00147,putative","hypothetical protein","diacylglycerol kinase, catalytic region","","Kanoh H., Yamada K., Sakane F. Diacylglycerol kinases: emerging downstream regulators in cell signaling systems. J. Biochem. 2002. 131(5):629-633. PMID: 11983067","","","

InterPro
IPR001206
Domain

Diacylglycerol kinase, catalytic region
PD005043	$\"[283-349]T$	Q6A8S5_PROAC_Q6A8S5;
PF00781	$\"[250-382]T$	DAGK_cat

InterPro
IPR005218
Family

Conserved hypothetical protein 147
TIGR00147	$\"[246-542]T$	TIGR00147: conserved hypothetical protein T

noIPR
unintegrated

unintegrated
PTHR12358	$\"[241-510]T$	SPHINGOSINE KINASE
PTHR12358:SF4	$\"[241-510]T$	BMRU PROTEIN
signalp	$\"[1-38]?$	signal-peptide
tmhmm	$\"[26-46]?$ $\"[87-107]?$ $\"[112-132]?$ $\"[151-171]?$ $\"[186-204]?$ $\"[210-230]?$ $\"[440-460]?$	transmembrane_regions

","BeTs to 8 clades of COG1597COG name: Predicted kinase related to diacylglycerol kinaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1597 is ---p--y-vdrlbcef-----j----Number of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-46% similar to PDB:2BON STRUCTURE OF AN ESCHERICHIA COLI LIPID KINASE (YEGS) (E_value = 1.3E_11);-46% similar to PDB:2JGR CRYSTAL STRUCTURE OF YEGS IN COMPLEX WITH ADP (E_value = 1.3E_11);-46% similar to PDB:1ND4 Crystal structure of aminoglycoside-3'-phosphotransferase-IIa (E_value = 1.3E_11);","Residues 250 to 382 (E_value = 1.5e-20) place ANA_2472 in the DAGK_cat family which is described as Diacylglycerol kinase catalytic domain (presumed).Residues 299 to 343 (E_value = 0.00022) place ANA_2472 in the NAD_kinase family which is described as ATP-NAD kinase.","","hypothetical protein TIGR00147, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2474","2670486","2670758","273","11.41","8.10","10172","GTGCGCCTGTGGGCGGCATATGTCCCGGCTGTGGGTGGCGAGGAGGGCGGGCGGCGTGAGTGCATCGACGTCGAGCATCCCGGGCGCCTGGAGCAACGTGGCTACGTGTGGTGGCCTTGGGTGTCTGAACGTCCGGTGAGCGCCTGGTGGCCCTCGCGCCCCAGGCCGCGGGCGCGGTGGGCCTCGAGTGCCTGCGCGCCGAGGCGTTCACTTCCCAGGACCTCTCCGACGATGCGGATGGCCTCGTCGTCGTCGATCGGTTCGGGCAGGTAG","VRLWAAYVPAVGGEEGGRRECIDVEHPGRLEQRGYVWWPWVSERPVSAWWPSRPRPRARWASSACAPRRSLPRTSPTMRMASSSSIGSGR$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Bohren K.M., Bullock B., Wermuth B., Gabbay K.H. The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 1989. 264(16):9547-9551. PMID: 2498333Schade S.Z., Early S.L., Williams T.R., Kezdy F.J., Heinrikson R.L., Grimshaw C.E., Doughty C.C. Sequence analysis of bovine lens aldose reductase. J. Biol. Chem. 1990. 265(7):3628-3635. PMID: 2105951Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A. An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 1992. 257(5066):81-84. PMID: 1621098Borhani D.W., Harter T.M., Petrash J.M. The crystal structure of the aldose reductase.NADPH binary complex. J. Biol. Chem. 1992. 267(34):24841-24847. PMID: 1447221Gulbis J.M., Zhou M., Mann S., MacKinnon R. Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels. Science 2000. 289(5476):123-127. PMID: 10884227","","","

InterPro
IPR001395
Family

Aldo/keto reductase
PS00063	$\"[71-86]?$	ALDOKETO_REDUCTASE_3

InterPro
IPR002589
Domain

Appr-1-p processing
PF01661	$\"[19-136]T$	A1pp
SM00506	$\"[2-136]T$	A1pp
PS51154	$\"[1-181]T$	MACRO

noIPR
unintegrated

unintegrated
G3DSA:3.40.220.10	$\"[1-177]T$	no description
PTHR11106	$\"[1-141]T$	GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED
PTHR11106:SF3	$\"[1-141]T$	UNCHARACTERIZED

","BeTs to 10 clades of COG2110COG name: Uncharacterized ACR related to the C-terminal domain of histone macroH2A1Functional Class: S [Function unknown]The phylogenetic pattern of COG2110 is a--pkzyqvdrl--ef-----j----Number of proteins in this genome belonging to this COG is 2","***** IPB002589 (Protein of unknown function Appr-1) with a combined E-value of 4e-30. IPB002589A 8-36 IPB002589B 75-84 IPB002589C 115-128","","","-65% similar to PDB:1SPV Crystal Structure of the Putative Phosphatase of Escherichia coli, Northeast Structural Genomoics Target ER58 (E_value = 2.5E_29);-52% similar to PDB:2DX6 Crystal structure of conserved hypothetical protein, TTHA0132 from Thermus thermophilus HB8 (E_value = 3.0E_14);-48% similar to PDB:1HJZ CRYSTAL STRUCTURE OF AF1521 PROTEIN CONTAINING A MACROH2A DOMAIN (E_value = 1.5E_10);-48% similar to PDB:1VHU Crystal structure of a putative phosphoesterase (E_value = 1.5E_10);-48% similar to PDB:2BFQ MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES (E_value = 1.5E_10);","Residues 19 to 136 (E_value = 4.9e-51) place ANA_2477 in the A1pp family which is described as Appr-1-p processing enzyme family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2478","2672776","2673720","945","5.37","-9.96","32743","GTGGAATGTCCCCGGCCGCAAGAAAAAGTCCCCGGACGCGCGGACCGTCCTCCTACACTCGCCTGCATGACCACCGACGCTGACCATGGACACCCCTCGACCGTTCCGGTCGGCCCGGCCGGCCGCGACCCGCTGCCCCTGGCGGGGCGCACCGTCCTGGTCACCGGGGTCAGCCGCCGCATCGGCATCGGCCACGCCATTGCCTGCCGCGCCGCCGACTACGGGGCGAGCATCGTCGCCCACCACTACCGCCCGCACGACGCCTCCCAGTCCTGGGGCGCCGACGACATCGACGCCGTCATGGACTCCATCCGCAGCCACCTGGTCGGCCCCGCCCGGCTCATCGACATCCCCGCCGACCTGGCCGCCCCCGGGGAGCCGGCCCGCGTCGTCGAGCAGGCCGCGGCCGCCGCCGGCCACCTCGACGCCCTCGTGTGCAACCAGGCCATGAGCAGCCCCGACGGGTCGCTCAGCGAGATGACCGAGGCCGTCCTGGATGCCCACTGGGCCGTCGACGCCCGCGCCTCCATCCTCCTGGCGCAGGCCTTCGCTGCTCAGGAGGGCTTCGCCTCGCCCGCCCCGTCCGGCTCCGCGCGCCGCCGTGGGTCGATCGTCTTCCTCACCTCGGGCCAGGGCCTGGCTCCCCTGCCCGGGGAGATCGCCTACGCCGCAGCCAAGGCCGCCATCGCCGGCCTCACCCCGACCATCTCCGAGGAGCTCATCGACGCCGGCATCACCGTCAACACGGTCAACCCCGGCCCCGTCGACACCGGCTACATCACCGAGGCGGACCGGGAGGCGACGGCCGTCATGTTCCCCCAGGGGCGCTGGGGCGAGCCCGACGACGCCGCCCGCCTCATCACCTGGCTGCTCACCGATGAGGCCCGCTGGATCACCGGGCAGGTCATCAACTCCGAGGGCGGCTTCGCCCGCTGGCGCCGCTGA","VECPRPQEKVPGRADRPPTLACMTTDADHGHPSTVPVGPAGRDPLPLAGRTVLVTGVSRRIGIGHAIACRAADYGASIVAHHYRPHDASQSWGADDIDAVMDSIRSHLVGPARLIDIPADLAAPGEPARVVEQAAAAAGHLDALVCNQAMSSPDGSLSEMTEAVLDAHWAVDARASILLAQAFAAQEGFASPAPSGSARRRGSIVFLTSGQGLAPLPGEIAYAAAKAAIAGLTPTISEELIDAGITVNTVNPGPVDTGYITEADREATAVMFPQGRWGEPDDAARLITWLLTDEARWITGQVINSEGGFARWRR$","3-oxoacyl-[acyl-carrier protein] reductase","Cytoplasm","3-oxoacyl-[acyl-carrier protein] reductase","oxidoreductase; short-chain dehydrogenase/reductase family ","short-chain dehydrogenase/reductase SDR","","Jornvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 1995. 34(18):6003-6013. PMID: 7742302Villarroya A., Juan E., Egestad B., Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 1989. 180(1):191-197. PMID: 2707261Persson B., Krook M., Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 1991. 200(2):537-543. PMID: 1889416Neidle E., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 1992. 204(1):113-120. PMID: 1740120Benyajati C., Place A.R., Powers D.A., Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 1981. 78(5):2717-2721. PMID: 6789320","","","

InterPro
IPR002198
Family

Short-chain dehydrogenase/reductase SDR
PTHR19410	$\"[50-307]T$	SHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106	$\"[50-241]T$	adh_short
PS00061	$\"[209-237]?$	ADH_SHORT

InterPro
IPR002347
Family

Glucose/ribitol dehydrogenase
PR00081	$\"[51-68]T$ $\"[139-150]T$ $\"[196-212]T$ $\"[222-241]T$ $\"[243-260]T$ $\"[273-293]T$	GDHRDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[41-309]T$	no description
PTHR19410:SF51	$\"[50-307]T$	3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE

","BeTs to 21 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 4","***** IPB002347 (Glucose/ribitol dehydrogenase family signature) with a combined E-value of 3.1e-29. IPB002347A 51-68 IPB002347B 139-150 IPB002347C 196-212 IPB002347D 222-241 IPB002347E 243-260 IPB002347F 273-293***** IPB002198 (Short-chain dehydrogenase/reductase SDR) with a combined E-value of 1.4e-15. IPB002198B 202-250***** IPB002424 (Insect alcohol dehydrogenase family signature) with a combined E-value of 3.7e-07. IPB002424E 201-215 IPB002424F 221-239 IPB002424G 244-257","","","-45% similar to PDB:2UVD THE CRYSTAL STRUCTURE OF A 3-OXOACYL-(ACYL CARRIER PROTEIN) REDUCTASE FROM BACILLUS ANTHRACIS (BA3989) (E_value = 1.4E_19);-43% similar to PDB:2PH3 Crystal structure of 3-oxoacyl-[acyl carrier protein] reductase TTHA0415 from Thermus thermophilus (E_value = 8.6E_17);-41% similar to PDB:1JA9 Crystal structure of 1,3,6,8-tetrahydroxynaphthalene reductase in complex with NADPH and pyroquilon (E_value = 4.3E_16);-46% similar to PDB:2HQ1 Crystal Structure of ORF 1438 a putative Glucose/ribitol dehydrogenase from Clostridium thermocellum (E_value = 1.2E_15);-42% similar to PDB:1X1E Crystal Structure of TT0495 protein from Thermus thermophilus HB8 (E_value = 6.2E_15);","Residues 50 to 241 (E_value = 1e-06) place ANA_2478 in the adh_short family which is described as short chain dehydrogenase.","","protein] reductase (AL132824)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2479","2674976","2673957","1020","7.13","0.73","36687","ATGACAACTGCACAGAAGAGGACCCGACTCCCCATGACGCCCTGCTCTGCCGGCCGTGCCGCCCTGTCCGTCATCGGCACCACCGCCGCTCTGGGGACGGCCACGCTGGCCTACAGCCTCATTGAGGCCAGGTGCCCCGTACTGCGGCGCATCGACGTGCCAGTGCTCGCCACCGACGAGGAGCCCCTCACGGTGCTGCACCTGGCCGACCTTCACCTGACGGACCACACCGAGGCGCGGGTCTCCTGGGTGCGGCAGCTGGCGCAGCTGCAGCCCGACGTCGTTGTCAACACCGGCGACAACCTCTCCCTGGCATCCGGCCTGGAGCCGCTGCGACGGGCACTCGAACCGCTGACGGGCCTGCCCGGGGCCTTCGTCATGGGCGACCACGACTACCGCTCCACCGTCTTCCGCCTGCCGACGCGCTATCTGCACCGGGACCCGCGCAAGGCCTCCAGCCGCGTGCGCGACGAGGACATCGAGGCCCTGCCCTGGGAGGAGGTCCGCGACCTGCAGGCCGCCGGCGGCTGGGTGGACCTGACCAACCGACGCGGCTCGCTGACCGTGCGCGGGCGGCGCATCGAGCTGGTCGGCGTCGATGACCCGCACGCCAACCGCGATGTCCTGCCCCTCCCCGAGGCCGCCGGCTCAGCGGAGTCGGCCACCTCCCTGCCGGCGATCCGTGACCACGAGGGCCGGGCTCTGCGGCTGGGACTCACGCACGCCCCCTACCGGCGGGTCCTGGAGGCGATGTCAGCCGACGACGTCGACCTGGTGCTGGCCGGGCACACCCACGGCGGGCAGCTGTGCGTGCCCGGGGTCGGGGCACTGGTGACCAACTGCGACCTGGACCGGGGGCGCGCCTCGGGACTGTCGCAGTGGCCGGGCCGGTTCGGGGACCCGCGGGCCGCCGACCACATGTACCTGCACGTCTCCGCCGGGCTCGGCACGAGCCCCTACACGCCCGTGCGCCTGGCCTGCCGGCCCGAGGCCACGCTGCTGCGGCTGCTGCCGGCCTGA","MTTAQKRTRLPMTPCSAGRAALSVIGTTAALGTATLAYSLIEARCPVLRRIDVPVLATDEEPLTVLHLADLHLTDHTEARVSWVRQLAQLQPDVVVNTGDNLSLASGLEPLRRALEPLTGLPGAFVMGDHDYRSTVFRLPTRYLHRDPRKASSRVRDEDIEALPWEEVRDLQAAGGWVDLTNRRGSLTVRGRRIELVGVDDPHANRDVLPLPEAAGSAESATSLPAIRDHEGRALRLGLTHAPYRRVLEAMSADDVDLVLAGHTHGGQLCVPGVGALVTNCDLDRGRASGLSQWPGRFGDPRAADHMYLHVSAGLGTSPYTPVRLACRPEATLLRLLPA$","Metallophosphoesterase","Cytoplasm","Predicted phosphohydrolases","hypothetical protein","metallophosphoesterase","","Stone S.R., Hofsteenge J., Hemmings B.A. Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A. Biochemistry 1987. 26(23):7215-7220. PMID: 2827745MacKintosh R.W., Haycox G., Hardie D.G., Cohen P.T. Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A. FEBS Lett. 1990. 276(1):156-160. PMID: 2176161","","","

InterPro
IPR004843
Domain

Metallophosphoesterase
PF00149	$\"[63-267]T$	Metallophos

noIPR
unintegrated

unintegrated
G3DSA:3.60.21.10	$\"[63-265]T$	no description
signalp	$\"[1-37]?$	signal-peptide
tmhmm	$\"[21-41]?$	transmembrane_regions

","BeTs to 8 clades of COG1408COG name: Predicted phosphohydrolasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG1408 is --m----q-drlb-e-----uj-i--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-37% similar to PDB:1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS (E_value = );-37% similar to PDB:1BXR STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP (E_value = );-37% similar to PDB:1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S (E_value = );-37% similar to PDB:1C3O CRYSTAL STRUCTURE OF THE CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTANT C269S WITH BOUND GLUTAMINE (E_value = );-37% similar to PDB:1CE8 CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP (E_value = );","Residues 63 to 267 (E_value = 2.1e-10) place ANA_2479 in the Metallophos family which is described as Calcineurin-like phosphoesterase.","","phosphohydrolases ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2480","2677028","2674995","2034","5.28","-14.03","71834","ATGCTCGTGGTCTTCCTGACTCTCTCGTGCGTCGGCGGCGTCCTGTCAGCGGGCTTCGCCGCCCCCTTCGTGGGCGCCACGGCAGCACTGACCAAGGCGTCGGCCGAGCTCTTCGAGGAGCTCCCCAGCGACTTCAACGTCCAGCAGCCCAGCCAGATCTCCACCCTCCTGGCGGCCGACGGCACCGAGATCACCAAGTTCTACGCGGAGAACCGCATCGTGGTGCCCCTGAACTCGATCTCGGTCAACATGCAGAACGCCATCGTCGCCGTCGAGGACCAGCGCTTCTACCAGCACCAGGGCGTCGACCCCACCGGCATGGTGCGGGCCCTGGTGTCCAACAACGCCGGCGGCTCGCGTCAGGGCGCCTCAACACTGACCCAGCAGTACGTGCGCAACACGCTCATCGAGACCGGCCTGAAGAACGATGACCACAAGATCATCAGGGACGCCACCGAGAGCACCGTGGCCCGCAAGCTGCGGGAGATGAAGTTCGCCCTCAGCCTGGAACAGAAGTACTCCAAGCAGCAGATTCTCGAGGGCTACCTCAACATCGCCGCCTTCAGCCCCTCCACCTACGGGGTCGAGGCCTCCGCCCGGCACTACTTCAGCAAGTCGGCCAAGGACCTGACGGTGGCCGAGGCCGCCCTCATGGCCGGCACCACCAACGCTCCCAGCGCCTACGACCCCGTCACCCAGCCGGAGCTGGCCAAGAACCGCATGGACTGGGTGCTCTCCAAGATGCTGGAGGAGAAGTTCATCACCAAGCAGCAGTACGACGAGGCGGTCGCCACTCCGATCGCAAGCATGCTGCACGTCTCGGAGTCCCCGGCCGGCTGCGGCGCCGCGGGAAACGCCGCCTACTTCTGCACCTACGTGGTCAACGAAATCCTCGGGTCGGAGAACTTCGGCCCCGATATCGCCTCCCGCCGTCAGCTCCTGACGCGCGGAGGGCTGAAGATCACCACCACCTTGAACCTCGAGCGTCAGAGCGCCGCGGACAACGTCATCCAGTCCAACGTCCCCACCGGCGACGCCTCGGGAACCGACACGACCATCGTCTCCATCGAGCCCGGTACGGGCCGAATTCAGGCGCTGGCCCAGAACAGCAACTACGGCGACGGCGGCCCCGACAGCACCGACACCCAGCTCGTCTACGCCGCGGACGCCAAGCACGGCGGTATCGAGCTCAGTGACGGAACCGTCGGCTTCCAGCCGGGGTCCACCTTCAAGGCCCTCATCCTGGCCGAGTGGTTCAAGAACGGGAACTCCCCCAGCGCCAGGCTCAGCGCCGTCCCCAGAACCTTCCACTGGGACATCCCCTGCGCCCCGGAGAACAACGACCCGACCTGGGCCCCGAAGAACGTTGACCCCTTACTCAACCGAGCCACCAACGTCACCGAGGCCACGAAGCTGTCCATCAACGTCGCCTACGCCGAGATGCTCAGCCGCCTCAACGTCTGCGACGTCACCAGCTTCGCCGCCTCCATCGGAGTGACGAAGGCCGACGGGACCCAGCTGGACCCGCGTCCCTCCATCGTGCTGGGCTCCCAGAACGTGCCGCCGCTGAGCATGGCCAACGCCTACGCCACCTTCGCCTCCGGCGGCAAGTACTGCAAGCCCATCGCCATCGACCAGATCCTGGATGCCAGCGGCACCTCGATGGCCGTGCCCAGCGCCGACTGCACCCAGGCCATGGACCAGGGGGCCGCGGACCTGACCGCGACCACCTTGACCGCCACGTCGCAGAGAGGCGGAACAGCTCAGTTCGCCACATTCGGTCGACCAATCGGCGGCAAGACCGGAACCACGGACGACAACAACGACGCCTGGTTCGTGGGCTTCACTCCGCAGCTGGCCACCGCCGTCTGGATCGGTCACGCCGGCAGCCCCAGGACCCTCAACTACCAGCAGATCGGTCCGCACTCCATTGGCATCATGTACGGTAGCGACGTGGCTGTGCCGATGTGGCGCGACTACATGTCCCAGGCCGTGGCCAACGACCCGGCTCTGCCCATTCCCTCCCACGGGTGA","MLVVFLTLSCVGGVLSAGFAAPFVGATAALTKASAELFEELPSDFNVQQPSQISTLLAADGTEITKFYAENRIVVPLNSISVNMQNAIVAVEDQRFYQHQGVDPTGMVRALVSNNAGGSRQGASTLTQQYVRNTLIETGLKNDDHKIIRDATESTVARKLREMKFALSLEQKYSKQQILEGYLNIAAFSPSTYGVEASARHYFSKSAKDLTVAEAALMAGTTNAPSAYDPVTQPELAKNRMDWVLSKMLEEKFITKQQYDEAVATPIASMLHVSESPAGCGAAGNAAYFCTYVVNEILGSENFGPDIASRRQLLTRGGLKITTTLNLERQSAADNVIQSNVPTGDASGTDTTIVSIEPGTGRIQALAQNSNYGDGGPDSTDTQLVYAADAKHGGIELSDGTVGFQPGSTFKALILAEWFKNGNSPSARLSAVPRTFHWDIPCAPENNDPTWAPKNVDPLLNRATNVTEATKLSINVAYAEMLSRLNVCDVTSFAASIGVTKADGTQLDPRPSIVLGSQNVPPLSMANAYATFASGGKYCKPIAIDQILDASGTSMAVPSADCTQAMDQGAADLTATTLTATSQRGGTAQFATFGRPIGGKTGTTDDNNDAWFVGFTPQLATAVWIGHAGSPRTLNYQQIGPHSIGIMYGSDVAVPMWRDYMSQAVANDPALPIPSHG$","Penicillin-binding protein","Extracellular, Periplasm","possible penicillin-binding protein","penicillin-binding protein","glycosyl transferase, family 51","","Pares S., Mouz N., Petillot Y., Hakenbeck R., Dideberg O. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 1996. 3(3):284-289. PMID: 8605631","","","

InterPro
IPR001264
Domain

Glycosyl transferase, family 51
PD001895	$\"[155-210]T$	Q82EN1_STRAW_Q82EN1;
PF00912	$\"[54-234]T$	Transgly

InterPro
IPR001460
Domain

Penicillin-binding protein, transpeptidase
PF00905	$\"[522-629]T$	Transpeptidase

noIPR
unintegrated

unintegrated
G3DSA:3.40.710.10	$\"[324-672]T$	no description
signalp	$\"[1-16]?$	signal-peptide

InterPro
IPR003482
Family

Transcription factor WhiB
PF02467	$\"[8-70]T$	Whib

","No hits to the COGs database.","***** IPB003482 (Transcription factor WhiB) with a combined E-value of 6.3e-08. IPB003482A 35-45 IPB003482B 45-61 IPB003482C 67-74","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 70 (E_value = 9.6e-24) place ANA_2481 in the Whib family which is described as Transcription factor WhiB.","","protein whiB","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2482","2677993","2678184","192","5.08","-1.84","6850","ATGACAGCATCATCTGAGCCCGTATCCGCCTCGCCGACCACCTGGGAGTACGTCACCGTCCCCCTCATCACTCACGCCACCAAGCAGATCCTCGACCAGTGGGGTGCTGACGGCTGGGAGCTCGTCCAGGTCGTGCCTGGTCCCTCCGGCACGGACAACCTCATCGCCTACCTCAAGCGCCCCCGGTCCTGA","MTASSEPVSASPTTWEYVTVPLITHATKQILDQWGADGWELVQVVPGPSGTDNLIAYLKRPRS$","Hypothetical protein","Periplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2483","2679019","2678342","678","5.51","-5.81","24742","GTGGAAGACAGCATTATCTCCAGGATCCCGCTCTTCGAGGGCCTGAGCCCGGAAGAGCAGGAGGAACTGCGCGCCATGATGACGCAGACGACTCTGCGCCGTGGCGAGACCCTCTTCAACGAGGGCGACTCAGGCGACCGCCTCTACATTCTCCTCTCCGGGAAGGTGAAGCTCGGCCACGCCAGCGCCGACGGCCGCGAGAACCTGCTCGCGGTGCTCGGCCCCGGCGAGATCGTCGGCGAGCTGACCCTGTTCGACCCGGGCCCGCGCTCCACCACCGCCACCGCCGTGGCCCCCACCGAGCTCCTGACGCTGGACCACAACCAGCTCATGACCTTCGTGGAGTCCCACCCGCAGCTGGCCAAGGACATGCTGCGCGCCCTGGCCCAGCGCCTGCGCCGCACGAACACCGCGCTGGCGGACCTCGTCTTCTCCGACGTGCCCGGCCGCGTGGCCAAGGCCCTGCTGGACCTGGCCGACCGCTTCGGCTCGCCCACCGACGACGGCGTCCACGTCCCCCACGACCTCACCCAGGAGGAGCTCGCCCAGCTGGTGGGCGCCTCGCGCGAGACGGTCAACAAGTCGCTGGCCGAGTTCGTCTCCCGCGGCTGGATCCGCCTGGAGGGCCGGGCCGTCACGCTGCTCGACGTCGACCGCCTGCGCCGTCGCGCCCGCTGA","VEDSIISRIPLFEGLSPEEQEELRAMMTQTTLRRGETLFNEGDSGDRLYILLSGKVKLGHASADGRENLLAVLGPGEIVGELTLFDPGPRSTTATAVAPTELLTLDHNQLMTFVESHPQLAKDMLRALAQRLRRTNTALADLVFSDVPGRVAKALLDLADRFGSPTDDGVHVPHDLTQEELAQLVGASRETVNKSLAEFVSRGWIRLEGRAVTLLDVDRLRRRAR$","Transcriptional regulator, Crp/Fnr family","Cytoplasm","cAMP-binding domains - Catabolite gene activatorand regulatory subunit of cAMP-dependent protein kinases","transcriptional regulator; Crp/Fnr family","cyclic nucleotide-binding","","Korner H., Sofia H.J., Zumft W.G. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol. Rev. 2003. 27(5):559-592. PMID: 14638413Busby S., Ebright R.H. Transcription activation by catabolite activator protein (CAP). J. Mol. Biol. 1999. 293(2):199-213. PMID: 10550204Kaupp U.B. The cyclic nucleotide-gated channels of vertebrate photoreceptors and olfactory epithelium. Trends Neurosci. 1991. 14(4):150-157. PMID: 1710853","","","

InterPro
IPR000595
Domain

Cyclic nucleotide-binding
PF00027	$\"[29-119]T$	cNMP_binding
SM00100	$\"[11-129]T$	cNMP
PS50042	$\"[11-131]T$	CNMP_BINDING_3

InterPro
IPR001808
Domain

Bacterial regulatory protein, Crp
PF00325	$\"[175-205]T$	Crp
SM00419	$\"[168-216]T$	HTH_CRP

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[145-224]T$	no description

InterPro
IPR012318
Domain

Helix-turn-helix motif, Crp-type
PS51063	$\"[145-218]T$	HTH_CRP_2

InterPro
IPR014710
Domain

RmlC-like jelly roll fold
G3DSA:2.60.120.10	$\"[9-145]T$	no description

noIPR
unintegrated

unintegrated
PTHR10217	$\"[4-136]T$	VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL

","BeTs to 16 clades of COG0664COG name: cAMP-binding domains - Catabolite gene activator and regulatory subunit of cAMP-dependent protein kinasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0664 is ------yqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB001808 (Bacterial regulatory protein, Crp family) with a combined E-value of 6.9e-35. IPB001808A 38-76 IPB001808B 142-155 IPB001808C 172-214***** IPB002373 (cAMP-dependent protein kinase signature) with a combined E-value of 3.6e-15. IPB002373A 32-46 IPB002373B 47-61 IPB002373C 77-86 IPB002373D 89-100 IPB002373E 144-156***** IPB000595 (Cyclic nucleotide-binding domain) with a combined E-value of 4.3e-10. IPB000595 35-58","","","-55% similar to PDB:1CGP CATABOLITE GENE ACTIVATOR PROTEIN (CAP)/DNA COMPLEX + ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (E_value = 1.2E_19);-55% similar to PDB:1G6N 2.1 ANGSTROM STRUCTURE OF CAP-CAMP (E_value = 1.2E_19);-55% similar to PDB:1I5Z STRUCTURE OF CRP-CAMP AT 1.9 A (E_value = 1.2E_19);-55% similar to PDB:1J59 CATABOLITE GENE ACTIVATOR PROTEIN (CAP)/DNA COMPLEX + ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (E_value = 1.2E_19);-55% similar to PDB:1LB2 Structure of the E. coli alpha C-terminal domain of RNA polymerase in complex with CAP and DNA (E_value = 1.2E_19);","Residues 29 to 119 (E_value = 1.2e-30) place ANA_2483 in the cNMP_binding family which is described as Cyclic nucleotide-binding domain.Residues 175 to 205 (E_value = 8e-05) place ANA_2483 in the Crp family which is described as Bacterial regulatory proteins, crp family.","","domains - Catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases (CAP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2484","2679264","2679905","642","7.37","0.99","23197","ATGACGACCGAGCCGGCCCGGCGTGCGGGCGCCGTCGACGACGAGCTCATGACCCTCTACCCTGACGCCGCCTGCGCCCTGGATCATGACGGCCCCTTCCAGCTGCTCGTGGCCACCGTCCTGTCGGCGCAGACCACTGACGCGCGCGTCAACACCGTCACCCCCGAGCTCTTCGAGCGCTACCCAGACGCCGCGGCCCTGGGGGCGGCCCGGCGCGAGGACCTCGAGGCGATCCTGCGGCCGCTCGGCTTCCAGCGCGCTAAGGCCGGCCATCTGCTCGGCATCGGTCAGGCGCTCACCGAGCGCTTCGAGGGGCGGGTGCCGCGCAGCCGCGAGGAGCTCGTGGCCCTGCCGGGCGTGGGGCGCAAGACCGCCAACGTCGTGCTCGGCAACGCCTTCGGTCAGCCCGCCATCACCGTGGACACCCACGTGGGCAGGCTCTCGCGCCGCCTGGGGTGGACGACGTCGAAAGACCCGCTGCGCGTGGAGAAGGACATCGCGGCCCTGTGGGAGCCGTGGCGCTGGACCGACGGCTGCCACCGGCTCATCGAGCACGGGCGCCAGGTGTGCTCGGCCCGCTCACCCCGCTGCGGCCAGTGCACACTGCTCGAGGCCGGCCTGTGTCCGCAAGTGGGGGTCTGA","MTTEPARRAGAVDDELMTLYPDAACALDHDGPFQLLVATVLSAQTTDARVNTVTPELFERYPDAAALGAARREDLEAILRPLGFQRAKAGHLLGIGQALTERFEGRVPRSREELVALPGVGRKTANVVLGNAFGQPAITVDTHVGRLSRRLGWTTSKDPLRVEKDIAALWEPWRWTDGCHRLIEHGRQVCSARSPRCGQCTLLEAGLCPQVGV$","Endonuclease III","Cytoplasm, Extracellular","endonuclease III","endonuclease III","endonuclease III","","Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Aravind L., Walker D.R., Koonin E.V. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res. 1999. 27(5):1223-1242. PMID: 9973609Provvedi R., Dubnau D. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol. Microbiol. 1999. 31(1):271-280. PMID: 9987128Doherty A.J., Serpell L.C., Ponting C.P. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 1996. 24(13):2488-2497. PMID: 8692686","","","

InterPro
IPR000445
Domain

Helix-hairpin-helix motif
PF00633	$\"[102-131]T$	HHH

InterPro
IPR003265
Domain

HhH-GPD
PF00730	$\"[37-172]T$	HhH-GPD
SM00478	$\"[41-188]T$	ENDO3c

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[112-131]T$	HhH1

InterPro
IPR003651
Domain

Iron-sulfur cluster loop
SM00525	$\"[189-211]T$	FES

InterPro
IPR004036
Domain

Endonuclease III, HhH
PS01155	$\"[105-134]T$	ENDONUCLEASE_III_2

InterPro
IPR005759
Family

Endonuclease III/Nth
TIGR01083	$\"[6-197]T$	nth: endonuclease III

noIPR
unintegrated

unintegrated
G3DSA:1.10.340.30	$\"[23-135]T$	no description
PTHR10359	$\"[25-209]T$	A/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III
PTHR10359:SF2	$\"[25-209]T$	ENDONUCLEASE III

","BeTs to 24 clades of COG0177COG name: Predicted EndoIII-related endonucleaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0177 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB004036 (Endonuclease III, HhH) with a combined E-value of 9.3e-48. IPB004036A 33-47 IPB004036B 75-89 IPB004036C 103-134 IPB004036D 140-150 IPB004036E 182-206***** IPB011257 (DNA glycosylase) with a combined E-value of 1.1e-17. IPB011257A 117-126 IPB011257B 140-150 IPB011257C 186-200","","","-63% similar to PDB:1P59 Structure of a non-covalent Endonuclease III-DNA Complex (E_value = 3.0E_43);-63% similar to PDB:1ORN Structure of a Trapped Endonuclease III-DNA Covalent Intermediate: Estranged-Guanine Complex (E_value = 6.8E_43);-63% similar to PDB:1ORP Structure of a Trapped Endonuclease III-DNA Covalent Intermediate: Estranged-Adenine Complex (E_value = 6.8E_43);-55% similar to PDB:2ABK REFINEMENT OF THE NATIVE STRUCTURE OF ENDONUCLEASE III TO A RESOLUTION OF 1.85 ANGSTROM (E_value = 2.7E_31);-48% similar to PDB:1KEA STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE (E_value = 4.7E_12);","Residues 37 to 172 (E_value = 1e-20) place ANA_2484 in the HhH-GPD family which is described as HhH-GPD superfamily base excision DNA repair protein.Residues 102 to 131 (E_value = 1.8e-07) place ANA_2484 in the HHH family which is described as Helix-hairpin-helix motif.","","III (nth)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2485","2680023","2680862","840","8.60","4.07","29244","ATGACTGCTCACTCGCCCCTGGCCCCCTCCGACCCGACCGCCGCCCCCGCCTCATTCCTGCCGTCCGCCACTCCGCCTGCCGGGCCGGGCCCGACGTCGCCCATCGCCATCCGGCTGCGCGGCCTGACCCGCGTCTACGAGGTCCCCGGACGCCAGGACGCCCGCGTCACCGCCCTGGACCATGTCGACGCCGACCTGCCCGAGGGCAGCTTCACCGCCGTCGTCGGGGCCTCCGGGTCGGGCAAGTCCACGCTGCTGCACTGCATGGCCGGCCTCGATGAGCCCACCAGCGGACAGGTGACCATGCTCGGTGCCCTCACCTCCGGGATGCGGGCCGCCGAGCGGGCCCGGTTCCGCGCCCGCCACGTCGGCTTCGTCTTCCAGGAGTACAACCTCATCGCCTCCCTGAGCGCCGCCGACAACGTCTCCATGCCCTCGCGCCTGGCCGGGCGTCCCCTGAGCAGCGCCCAGACCCGGGAGGCCCTCGACGCCGTCGGGCTCGCTCACCGTGCCGGACTCAAGCCCCACCAGCTCTCCGGCGGGGAGCGCCAGCGCGTGGCCATCGCCCGCGTCATGGCCAGCCGGCCCCGGATCGTCTTCGCCGACGAGCCCACCGGTGCCCTCGACCTGGACTCCGCCGCCCTCGTCCTGGACTGGCTGCGCCGGCTCACCGAGCAGGGCACCACTGTGGTCATGGTGACCCACGACGTCGAGGCCGCCGCCAGGGCTGACGCGGTCGCCGTCATGAGTCAGGGGCACCTGGTGCAGTGGACCGGCTGCCGTGACGCCCGCCAGATCGCCGAGCTCGTCCACTCGGCGCGAGCCACGCGCGCCGCCTGA","MTAHSPLAPSDPTAAPASFLPSATPPAGPGPTSPIAIRLRGLTRVYEVPGRQDARVTALDHVDADLPEGSFTAVVGASGSGKSTLLHCMAGLDEPTSGQVTMLGALTSGMRAAERARFRARHVGFVFQEYNLIASLSAADNVSMPSRLAGRPLSSAQTREALDAVGLAHRAGLKPHQLSGGERQRVAIARVMASRPRIVFADEPTGALDLDSAALVLDWLRRLTEQGTTVVMVTHDVEAAARADAVAVMSQGHLVQWTGCRDARQIAELVHSARATRAA$","ABC-type transport system involved in lipoprotein release, ATPase component","Membrane, Cytoplasm","ABC transporter ATP-binding protein","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[177-206]T$	Q9XAA7_STRCO_Q9XAA7;
PF00005	$\"[69-252]T$	ABC_tran
PS50893	$\"[37-276]T$	ABC_TRANSPORTER_2
PS00211	$\"[178-192]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[68-253]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[31-265]T$	no description
PTHR19222	$\"[37-255]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32	$\"[37-255]T$	ABC TRANSPORTER

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[25-183]T$ $\"[300-455]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[63-85]?$ $\"[106-135]?$ $\"[149-169]?$ $\"[199-217]?$ $\"[245-265]?$ $\"[303-323]?$ $\"[337-357]?$ $\"[378-407]?$ $\"[413-447]?$	transmembrane_regions

","BeTs to 11 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","","","-57% similar to PDB:1OD2 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN (E_value = );-57% similar to PDB:1OD4 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN (E_value = );-57% similar to PDB:1UYR ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN COMPLEX WITH INHIBITOR DICLOFOP (E_value = );-57% similar to PDB:1UYS ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN COMPLEX WITH INHIBITOR HALOXYFOP (E_value = );-57% similar to PDB:1UYT ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN (E_value = );","Residues 25 to 183 (E_value = 2.9e-07) place ANA_2486 in the FtsX family which is described as Predicted permease.Residues 300 to 455 (E_value = 0.00066) place ANA_2486 in the FtsX family which is described as Predicted permease.","","membrane protein","","1","","","","","","","","","","","Tue Aug 14 17:19:53 2007","","","","","Tue Aug 14 17:19:53 2007","","","","Tue Aug 14 17:19:53 2007","Tue Aug 14 17:19:53 2007","","","","","yes","","" "ANA_2487","2683285","2682380","906","9.69","6.82","31983","GTGCCTGTTGACGTCAATCGCCCCGGCCCCTGGGCCCACCGCAACCTCACCGCCCGCGGCACTCGTTTCCATGTCGCGCTGGCGGGCCCCGAGGCCCCGGCCGGAGCCGGTCCCCTTACCCTCCTGGTGCACGGCTTCCCCGAGTGCTGGTGGACCTGGCGTCACGTCATCCCCGCCCTGGCACAGGCCGGGCACCGCGTGGCGGCCCTCGACCTGCGTGGCTTCGGCGGCTCGGACCGGCCGCCGTCGGGCTACGACCTGGTGACGCTCGCCCAGGACCTGGCCGCCGTGGTCCGCTCCCTGGGGCACGAGCGCGCCGTGGTCGTCGGCGCAGGGCTCGGCGGTCAGATCGCCTGGGCGCTGCCGAGCCTGGCGCCGGACCTGACGACGGCGATCGTCCCGGTCGGCGCCCCCCACCCGCTCGCGCTGCGCTCGCTGCGGGCCCGGGCCCTGTCCGGGCCGGCGCTGCAGTACGTGAGCCTGCGGATCCCGGGCCTGGCCGAGCGCCGCCTGCGCAGCCGCAGCGCCCTGGAGGGCCTGCTGCGCTCCTGGGCCGGGCCGCACACGCGCGAGGTGCTGGCCGAGGAGGCCCCCTACTACGCCGAGCTCCTGTCCCGGCCCGGCGCCGCCCGCAGCGCCCTGGAGCCGCTGCGCAACCTCGTGCTATCCCGGGCGGAAACGGCGGCCCTGGACAAGCCGGTGGCGGTGCCCGTCCTGTCGATGCAGGGCGAACTCGACCCGGTCCAGCCCGCCCAGGCCTACGCACGCGACACCCACCACGTGGCCGGCAACCTGCGCCAGGTGACGATCCACCGCTCCGGCCACTTCCCCCAGGAGGAGACCCCGGCCGGGTTCGTCCAGGCCCTGCTGCCCTTCCTGGCCGACGTCGCCCCGCCCACCACCTGA","VPVDVNRPGPWAHRNLTARGTRFHVALAGPEAPAGAGPLTLLVHGFPECWWTWRHVIPALAQAGHRVAALDLRGFGGSDRPPSGYDLVTLAQDLAAVVRSLGHERAVVVGAGLGGQIAWALPSLAPDLTTAIVPVGAPHPLALRSLRARALSGPALQYVSLRIPGLAERRLRSRSALEGLLRSWAGPHTREVLAEEAPYYAELLSRPGAARSALEPLRNLVLSRAETAALDKPVAVPVLSMQGELDPVQPAQAYARDTHHVAGNLRQVTIHRSGHFPQEETPAGFVQALLPFLADVAPPTT$","Putative hydrolase","Membrane, Cytoplasm, Extracellular","hydrolase","putative hydrolase","alpha/beta hydrolase fold","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539Beetham J.K., Grant D., Arand M., Garbarino J., Kiyosue T., Pinot F., Oesch F., Belknap W.R., Shinozaki K., Hammock B.D. Gene evolution of epoxide hydrolases and recommended nomenclature. DNA Cell Biol. 1995. 14(1):61-71. PMID: 7832993Verschueren K.H., Seljee F., Rozeboom H.J., Kalk K.H., Dijkstra B.W. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 1993. 363(6431):693-698. PMID: 8515812Pinot F., Grant D.F., Beetham J.K., Parker A.G., Borhan B., Landt S., Jones A.D., Hammock B.D. Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase. J. Biol. Chem. 1995. 270(14):7968-7974. PMID: 7713895","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[65-291]T$	Abhydrolase_1

InterPro
IPR000639
Family

Epoxide hydrolase
PR00412	$\"[44-62]T$ $\"[64-79]T$ $\"[108-121]T$ $\"[236-252]T$ $\"[270-292]T$	EPOXHYDRLASE

InterPro
IPR003089
Family

Alpha/beta hydrolase
PR00111	$\"[64-79]T$ $\"[108-121]T$ $\"[238-252]T$	ABHYDROLASE

InterPro
IPR013982
Domain

AICARFT/IMPCHase bienzyme, formylation region
SM00798	$\"[82-225]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[3-293]T$	no description
PTHR10992	$\"[20-294]T$	ALPHA/BETA HYDROLASE RELATED
PTHR10992:SF22	$\"[20-294]T$	EPOXIDE HYDROLASE

InterPro
IPR008407
Family

Branched-chain amino acid transport
PIRSF003203	$\"[2-105]T$	Branched-chain amino acid transport protein, AzlD type
PF05437	$\"[7-104]T$	AzlD

noIPR
unintegrated

unintegrated
signalp	$\"[1-22]?$	signal-peptide
tmhmm	$\"[10-28]?$ $\"[49-69]?$ $\"[88-106]?$	transmembrane_regions

","BeTs to 3 clades of COG1687COG name: Predicted branched-chain amino acid permeases (azaleucine resistance)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1687 is ------------b----h--u-----Number of proteins in this genome belonging to this COG is 1","***** IPB008407 (Branched-chain amino acid transport) with a combined E-value of 6e-11. IPB008407A 12-54 IPB008407B 75-104 IPB008407A 33-75","","","-43% similar to PDB:1VIM Crystal structure of an hypothetical protein (E_value = );-59% similar to PDB:2F93 K Intermediate Structure of Sensory Rhodopsin II/Transducer Complex in Combination with the Ground State Structure (E_value = );-59% similar to PDB:2F95 M intermediate structure of sensory rhodopsin II/transducer complex in combination with the ground state structure (E_value = );-71% similar to PDB:2EVU Crystal structure of aquaporin AqpM at 2.3A resolution (E_value = );-71% similar to PDB:2F2B Crystal structure of integral membrane protein Aquaporin AqpM at 1.68A resolution (E_value = );","Residues 7 to 104 (E_value = 3.2e-17) place ANA_2488 in the AzlD family which is described as Branched-chain amino acid transport protein (AzlD).","","amino acid transport protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2490","2685343","2684804","540","9.45","3.86","18463","GGCGAGCCACTGGCGGCCATCGCCCTGTCCACCGGTTTCGTCTCGGGCCGGCACGTCTTCTACGGGCTGGGCTTCCCCCTGGAGCGGGTGCGGGGCAGGGCGCTCACGCGCCTCTACGCCGTCCACGCGATCACCGACGAGGTCTACGCGCTGCTGGCGGCGCGCGACCGGCGGGCCATGAGCGGGCGCTACCTGGTGGGCGTGGAGGCGATCAGCCACGCCTCCTGGGTGTCGGGCACGACCGTCGGGGCACTGGCCGGCACCGCGCTGGCCTCCGTGGTGGGTGAGCGCATCGAGCTGCTGGGCTTCGTGCTTACCTCCCTGTTCGTGGTCCTGGCCATTGAGAACTGGCGCAATCACCCCGACATCGGAGTGCTGTGCGTGGGGCTGGTGGCCGGCGGGATCGGCCTGGCGATCGGTGGTTCGGCGGCACTGCTGACCGCGCTGGTGATCCTCGGCGCCGGCCTGGTGGGGCTGTACGCCTGGCGCGGCCGCCGCCCCGGGGCGAGCGCGCCGACGTCGGAGCGGGGGGACAGCTGA","GEPLAAIALSTGFVSGRHVFYGLGFPLERVRGRALTRLYAVHAITDEVYALLAARDRRAMSGRYLVGVEAISHASWVSGTTVGALAGTALASVVGERIELLGFVLTSLFVVLAIENWRNHPDIGVLCVGLVAGGIGLAIGGSAALLTALVILGAGLVGLYAWRGRRPGASAPTSERGDS$","Branched-chain amino acid permease (azaleucine resistance)","Membrane, Cytoplasm","Predicted branched-chain amino acid permease(azaleucine resistance)","probable branched-chain amino acid transporter","AzlC family protein","","Belitsky B.R., Gustafsson M.C., Sonenshein A.L., Von Wachenfeldt C. An lrp-like gene of Bacillus subtilis involved in branched-chain amino acid transport. J. Bacteriol. 1997. 179(17):5448-5457. PMID: 9287000","","","

InterPro
IPR011606
Family

AzlC-like
PF03591	$\"[3-91]T$	AzlC

noIPR
unintegrated

unintegrated
tmhmm	$\"[126-160]?$	transmembrane_regions

","BeTs to 6 clades of COG1296COG name: Predicted branched-chain amino acid permease (azaleucine resistance)Functional Class: EThe phylogenetic pattern of COG1296 is a-------eb-huj-------Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 28 to 124 (E_value = 4e-07) place ANA_2490 in the AzlC family which is described as AzlC protein.","","branched-chain amino acid permease (azaleucine resistance)","","1","","","Thu Aug 9 09:21:13 2007","","Thu Aug 9 09:21:13 2007","","","Thu Aug 9 09:21:13 2007","Thu Aug 9 09:21:13 2007","Thu Aug 9 09:21:13 2007","","","Thu Aug 9 09:21:13 2007","","","Thu Aug 9 09:21:13 2007","Thu Aug 9 09:21:13 2007","","","Thu Aug 9 09:21:13 2007","Thu Aug 9 09:21:13 2007","","","","","yes","","" "ANA_2491","2685633","2685163","471","9.99","5.07","16039","GTGACTGAGCCCGGCGCCGCCCCGCCGCCCACCGGGGCCGAAGAGGCAGGAGCGCCGTCGGCTCGGCGGATGCAGACCCTCGCCGATGCGGCCCGGGACGCGGTGCCCATTGTCGTGGGATACGTGACGCTGGGGCTGGCGGCCGGGATGCTTCTGGTCGCCGAGGGCCTGGCCTGGTGGTGGGCGCCGGTGTGGAGCCTGGTCATCTACTCCGGGACCATGCAGATGCTGCTGGTGCCGCTGGCCGGTGCCGGCGAGCCACTGGCGGCCATCGCCCTGTGGCCGGTGCCGGCGAGCCACTGGCGGCCATCGCCCTGTCCACCGGTTTCGTCTCGGGCCGGCACGTCTTCTACGGGCTGGGCTTCCCCCTGGAGCGGGTGCGGGGCAGGGCGCTCACGCGCCTCTACGCCGTCCACGCGATCACCGACGAGGTCTACGCGCTGCTGGCGGCGCGCGACCGGCGGGCCATGA","VTEPGAAPPPTGAEEAGAPSARRMQTLADAARDAVPIVVGYVTLGLAAGMLLVAEGLAWWWAPVWSLVIYSGTMQMLLVPLAGAGEPLAAIALWPVPASHWRPSPCPPVSSRAGTSSTGWASPWSGCGAGRSRASTPSTRSPTRSTRCWRRATGGP$","Branched-chain amino acid permease (azaleucine resistance)","Extracellular","Predicted branched-chain amino acid permease(azaleucine resistance)","hypothetical protein predicted by Glimmer/Critica","AzlC family protein","","Belitsky B.R., Gustafsson M.C., Sonenshein A.L., Von Wachenfeldt C. An lrp-like gene of Bacillus subtilis involved in branched-chain amino acid transport. J. Bacteriol. 1997. 179(17):5448-5457. PMID: 9287000","","","

InterPro
IPR011606
Family

AzlC-like
PF03591	$\"[35-138]T$	AzlC

noIPR
unintegrated

unintegrated
tmhmm	$\"[38-58]?$ $\"[64-84]?$	transmembrane_regions

","BeTs to 6 clades of COG1296COG name: Predicted branched-chain amino acid permease (azaleucine resistance)Functional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1296 is a--------d-lb-efgh-nuj----Number of proteins in this genome belonging to this COG is 2","***** IPB011606 (AzlC-like) with a combined E-value of 2.5e-12. IPB011606A 42-82","","","-47% similar to PDB:1F0N MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85B (E_value = );-47% similar to PDB:1F0P MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85B WITH TREHALOSE (E_value = );","Residues 35 to 138 (E_value = 0.00024) place ANA_2491 in the AzlC family which is described as AzlC protein.","","branched-chain amino acid permease (azaleucine resistance)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2492","2688631","2685626","3006","4.05","-112.06","98939","GTGAGCACCGACAACACAGACCGCACCACACCGCAGACACCCGTCGCCTCCGACGACGTCGCCCCGTCCTCTGAGGCGGCCCCGACGCCCACCGCACGGACAGCGGCCACGGACGCCCGCTCGGGAGAGGCGACGGTCAACCTGGTCGATGAGGGTCTCGTCTCGGCCTCCCTCGCGAGCCTCGCCAGCAAGGTCACCCAGGTCTCTCCATCCGCCTCCCCCACGCCCCGGGCGACGGCGGCCCAGGACGGCGAGGCCGGTGCGGTCAGTGCTGCCGCCGGCGCCGATGTGGACCAGACGACCGATGACGCAGCCCACGACTGGGCCGACGAGCAGGACGCGGCCGATGACGACGAGGCCGACACCCTCAACCTCCGCGAGCACGCGTCCTTCCCCGGCGCCGCCGGGAGCCGGGCCGCCGAGGCGGAGTCGGCCGTCGGGCCCGCTGCGGCCGCCGACGTGCCGCCGTCGATTCCTCCGTCGTCGGAGCCCGGCGAGGTCGAGGAGGAGCCCGCGCCGGTCACTGACGCCGCCCCGGTCTCCGTGGAGACCGCAACCGAGCCGGCGGCCCCCGAGGTCGTCGACGTCTCGCAGGCCCGTGCCGACACTGCTGAGGACGCCGCCGCCCAGGTGTCCGTACAGGCTGTGACTCCTGAGCCCGCCCGCGCCGAGGAGCCTCAGGGCGCCGGGGCCACCGCCGCAGTCGCTCCGGCAGCCACCGCAGCCACCACCAACAGCACGACCAGCAGCACGACCAGCACAGCCAGCACAGCGGCAGTCCTCAGCAGCTCCGCCGGCTCCGCCCCGGAGGCGCTCTCACCCGTTTCGGCGGACGATGGCGACGATGAGGACGAGGCCCCGGCAGTGAGCGCCGAGTCCACCCGTCAGCAGGACGGCGCACCGCTCACCTGGCCGACCAGCCAGCCGACCACAGCGTCCGCCGCAGTGCCTGCGACAGCAGCGGCCGCGGACGGTCAGGGACGCTTGCCCGTGGCCGACACCGCCGATGCCGCCGATGCCCCTGCGGCGCCGCAGAGCCTCATCGAGGCTGAGGACTTCGAAGACTTCGAGGACTTTGAGGACTTTGACGAGCTCGAGGACTTCGAGGACTCGTCGCAGTCGGAGCAGCCGGCCGGGGCCGATGACCTCGACACCCCTGAGGCGCAGGCCGACCTCACCCCCGCGACCCCGGCGATCCCCACGCCCGTGACCGGCTCCCCTGCCATGAGGGCCGTGCCCGTCTCAGTGGCCACCGGCGCCGCCCGCGCCGCGAACGAGACCGCGGGCGCCACCCCGCAGACCCCCTCCGCCGCGACCGGCACCGCGGATGCCGCCGTCGGCGTGGACGACACTGACGACTCCACCATCGACAGCCTCGACGACATCTCCGACGACTTCGACGGCGAGCTCGACGCGGAAGACGTCGAGGTCGGCGAGGCCGAGCGGGAGGCCGGAGCCGGCGAGGAGTCCGAGGACGATGCTCAGAACGTGACCGAGAGCGTTGCCGAGGAGGTTACGCAGCCGGCAGCCGCCTCGACACCCGCCTCAGCATCTGTCTCGACGGCCGCCGCTCAGCCCTGGACGCCGGTTCCACCGGCCTCCGGCTCCCAGACGTTTGCCAGCACGGCCGAGGCAGCCGACGTCGATGACCGTGAGGAGGGTGATGGCGGTGAGGGCGCCGCTGAGACCGATGACGGCTTCGCGCCCGTTGAGGCCCCCGCCGTCTCGGCGGCCTTCGCGGCTCCCTCAGCGCCGTCGGTAGCCGTGACGACACCGGCCGCCCCGTCAGCGGACTCACCGGAGCCCACCTCATCGAGCCGGTCCGAGTTCGAGCCGCAGGTGCCGGCGTCGGCACCGTCAGCGACCTCGGGGCCATCGGTGGCCGCTTCGACGTCACCGGCCGAGCCGGAGGCGGCAGCGCCGGTGAACGCCGACGCGGACAACCGCCCCTCGGCCCCGTCCTGGCCGGCGACCCCCGCGGCCCAGCTGGCCCGGACGGGCTCCGCGGCCAGCGCCTCCTCGGCGCGTTCCTCCGAGTCGGCGACCTCCGCCCGCCCCACCTTCTCCGCTGGCGCCCCGGCTCCCACCCCCTCAACGCAGCCGATGGGAGGAGCGCCCCGAGCCGCTTCGTCCCCGTACATCGGGCTCTCCGACCTCCGCCCGGAGGCCCCCGCCGACGCGCCGGCCCCCGCCCCGGCGGGAACGACACCGCAGTCCGAGTGGGCACCGTCAACCCAGCCGGCCCCGTCAACCCAGCCGGCCCCCGCCTCCGCGGACACCCGGGACTATCACCCGACGCCGGCAGCCTCGCCGTCGGCCCCCTCCCCGCAGCAGACGCCCGACTGGTTCGCAGCCGCCCCCACCGGGCGGGGCCTGTCCGCGAGCGCCGACGCCGGGGAGAGCGACGACCCGGAGGAGCGCGGCCGCTCGCGGGCCCGGCAGGCCGCCATGGCCATGACCGGTGCCGACGAGGACGACGATTCCATCCTCCTCAAGGGCGCCAGCGTGCTGAGCGCCCCGGGCTCGCGCGTCGAGACCCACTGGGCCGGGGTGCTCGTCGCCGTCGTCCTGTTCCCCCTGGCCTGGTTCCTCGTGCACGACGGCGCCGCCACCCTGACCGGCGGCAACCCCTCGGCCTGGCCGTCGGCCGCCTCCCCCATGGGTGCGCTGGAGATTCTGGGCGGGACCGCGGCCTGCGCCGCCGCCCTGTTCATGATCTCGCGATCCTCGCTGGGGGCCTTCGTCGTCGGCGCCTTCAGCACGGTCATCGGGCTGCCCTTCGTCCTCCTGCCGGGGGTCACCAAGTCGATCCTGGGGCCCACGGTGGATCGGCTTCAGGCCCACTCCGACCTGGGTAAGGCCCTGTCCACCTATGTCATGGACGACGGCCTCTCGGGCCGCTTCATCCTCATGGGCGTACTCACGATCATGGTCGCCGTCGTCGGCCACCTGGCGCGCCGGGCCGGGCAGCGCAAGGTGACCGACGGTCGGGGACCGCGTGACTGA","VSTDNTDRTTPQTPVASDDVAPSSEAAPTPTARTAATDARSGEATVNLVDEGLVSASLASLASKVTQVSPSASPTPRATAAQDGEAGAVSAAAGADVDQTTDDAAHDWADEQDAADDDEADTLNLREHASFPGAAGSRAAEAESAVGPAAAADVPPSIPPSSEPGEVEEEPAPVTDAAPVSVETATEPAAPEVVDVSQARADTAEDAAAQVSVQAVTPEPARAEEPQGAGATAAVAPAATAATTNSTTSSTTSTASTAAVLSSSAGSAPEALSPVSADDGDDEDEAPAVSAESTRQQDGAPLTWPTSQPTTASAAVPATAAAADGQGRLPVADTADAADAPAAPQSLIEAEDFEDFEDFEDFDELEDFEDSSQSEQPAGADDLDTPEAQADLTPATPAIPTPVTGSPAMRAVPVSVATGAARAANETAGATPQTPSAATGTADAAVGVDDTDDSTIDSLDDISDDFDGELDAEDVEVGEAEREAGAGEESEDDAQNVTESVAEEVTQPAAASTPASASVSTAAAQPWTPVPPASGSQTFASTAEAADVDDREEGDGGEGAAETDDGFAPVEAPAVSAAFAAPSAPSVAVTTPAAPSADSPEPTSSSRSEFEPQVPASAPSATSGPSVAASTSPAEPEAAAPVNADADNRPSAPSWPATPAAQLARTGSAASASSARSSESATSARPTFSAGAPAPTPSTQPMGGAPRAASSPYIGLSDLRPEAPADAPAPAPAGTTPQSEWAPSTQPAPSTQPAPASADTRDYHPTPAASPSAPSPQQTPDWFAAAPTGRGLSASADAGESDDPEERGRSRARQAAMAMTGADEDDDSILLKGASVLSAPGSRVETHWAGVLVAVVLFPLAWFLVHDGAATLTGGNPSAWPSAASPMGALEILGGTAACAAALFMISRSSLGAFVVGAFSTVIGLPFVLLPGVTKSILGPTVDRLQAHSDLGKALSTYVMDDGLSGRFILMGVLTIMVAVVGHLARRAGQRKVTDGRGPRD$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[846-866]?$ $\"[910-930]?$ $\"[965-985]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-53% similar to PDB:1TQY The Actinorhodin Ketosynthase/Chain Length Factor (E_value = );-48% similar to PDB:2UV8 CRYSTAL STRUCTURE OF YEAST FATTY ACID SYNTHASE WITH STALLED ACYL CARRIER PROTEIN AT 3.1 ANGSTROM RESOLUTION (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2494","2689660","2688722","939","11.81","15.85","31787","GTGAGTGACTCCCCCTCCCACTACGCCCCGGGCTCCGGCCCGCCACCCGCGACCCCTGGCGCATCGGGTCGGCCACCGCGCAGTCGCCGCCCCGACTACGTGCTCACCGCTGTCGTCGGAGTCCTCTTCGCCCTGGGTGCCTCCGCCCTCCTGGGCCTGGCCGCCGACCAGACCTCGATCCTGCGCACCGGCCTGCTGCTCGGCACCCTCCTGCTGCTGTCCTCAGCCGCCGCCGTCCTGTTCGCCAGCCGTTCCTCGCTGGGCGCGCTCGCCACCGGGCTGACCGCGTTGACCGCCCAGTCGATGGTCTTCCTGGCTCCTATTCACGCGGCCTCCTTGACTGAGCCCTGGCTTCAGCACCTCGTCAGCACCGGTTTCATGCTCGTCCTGGCGGGCCTGTGGCTGGGCGGGTCCTGGGGGATGCGCCTGGCACGCCGCGCCGGCCAGGCCCAGGGGCACGCCGCCTTCCGCCTCACCGAGGCCGACCGGACCGTGGGTACCACTCCGACGCCGCCGCCCTCACGCCGTCGCGATCACCTCCTGTCCCTGCCCTGGGTCATCGCCGGACTGGCGCTGACGGCCTATCTGTTGCCGCGCGCCTACCTGCATGCAGTCGCCCCCGGCGTCCAGACCGGGCCACTGCTGCTGGCAGCCGTCCTCATCTCCCTCCTGGCCCTGGCCGCGGCCGGCGCCTCGACGGCCCGCTCCACCCTCGGCGCGCGCGTCATCGGCCCGGTTCTTGTTCTTGCCGCGGTGCCCGCGCTCAGTAACGATATGATCCCTGGCGGCCATCTGGTCTCCAGGCTCCTGCCGAACGGCCCGAACGCCGTCGTGCTCGCCGCCATCGGCATCGAGCTCATGGCGATCGGCTGGGGAGTACATGTGGCTCGCCGGCAGGGCCGTGCCAACGCGCTGGCCAGGCTGCGCTCCGCCGCCTGA","VSDSPSHYAPGSGPPPATPGASGRPPRSRRPDYVLTAVVGVLFALGASALLGLAADQTSILRTGLLLGTLLLLSSAAAVLFASRSSLGALATGLTALTAQSMVFLAPIHAASLTEPWLQHLVSTGFMLVLAGLWLGGSWGMRLARRAGQAQGHAAFRLTEADRTVGTTPTPPPSRRRDHLLSLPWVIAGLALTAYLLPRAYLHAVAPGVQTGPLLLAAVLISLLALAAAGASTARSTLGARVIGPVLVLAAVPALSNDMIPGGHLVSRLLPNGPNAVVLAAIGIELMAIGWGVHVARRQGRANALARLRSAA$","Membrane protein","Membrane, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[33-55]?$ $\"[61-81]?$ $\"[91-111]?$ $\"[117-137]?$ $\"[180-198]?$ $\"[212-232]?$ $\"[237-257]?$ $\"[276-296]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-41% similar to PDB:1Y0F The structure of collagen type I. Single type I collagen molecule (E_value = );-41% similar to PDB:1YGV The structure of collagen type I. Single type I collagen molecule: rigid refinment (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","Thu Aug 9 10:52:12 2007","","Thu Aug 9 10:52:12 2007","","","Thu Aug 9 10:52:12 2007","Thu Aug 9 10:52:12 2007","Thu Aug 9 10:52:12 2007","","","","","","Thu Aug 9 10:52:12 2007","","","","Thu Aug 9 10:52:12 2007","Thu Aug 9 10:52:12 2007","","","","","yes","","" "ANA_2496","2689991","2690821","831","8.59","2.88","28512","GTGCGCGCCGCTGAGGACGCAGTGCGTGAGGCCTGCTCCGAGCTGCGCTGGAACGAGGCCCTGCGGCGCCGATGGCGCGAGGCCCGCGCCGAGGCCGCGATCCGGGGCGCCATCGCCTCGGGCGGCGTCGAGGGCGCCGTGGTCTCCGCCGAGGTGCTGCGCGAGCAGGTGGCCGCCGGCTCCCTCACCCAGGCCGCCACAGGGGACCCGGGCCTGGACGCCGTGGCCGGGCTGTGGCGCGCCGGGACCCGCCTGGTGAGCTGGATGCCGGACCTGGTGGGGCGAGGTCGGCCGGTGGCGCCCTCGGCGCGCTCGCTGCTGGCGGCGCTGCACCGCGACGTCGTCGGTCCCCTGGCGGCGGGCGGCCGGTTGGGCCTGGGGGAGGTCGGAGTGCCGCGCGCCCGGCAGGTGCATGCCCGCGAGGGCGGTCCTGGGGTCGCGCCGCAGGGTGAGGAACTGGTGGCGAGGCTGGCGGGGCTGGTCGATCTCATTGAGGCGCCGCAGGCGCCGGCGCTGGTGCGGGCGGCCATCGTGCATGCCGAGATGCTGGCCGCCCGCCCCTTCACCGCCGGGAACGCCGCCGTGGGGCGCCTGCTGGTGCGTCACCTCCTGGTGCGTGACGGGCTCGAGCCGACGGGCACGGCCGTCACCGACCTCTATCCCGGGCGGGTGCCGGCGGCCTACGCCGAGGCCGCCGGGGCCTACGCCTCGGGCACCATGGACGGGGTGGTGGCCTGGGTGGTGTGGCAGGCCGAGGCGGTGCTCGCGGGGGTTCAGGAGGCCCAGCGCCTGTGCCGGGCGGTGCAGGCCGGCACCTGGCGGGCCGGGTAA","VRAAEDAVREACSELRWNEALRRRWREARAEAAIRGAIASGGVEGAVVSAEVLREQVAAGSLTQAATGDPGLDAVAGLWRAGTRLVSWMPDLVGRGRPVAPSARSLLAALHRDVVGPLAAGGRLGLGEVGVPRARQVHAREGGPGVAPQGEELVARLAGLVDLIEAPQAPALVRAAIVHAEMLAARPFTAGNAAVGRLLVRHLLVRDGLEPTGTAVTDLYPGRVPAAYAEAAGAYASGTMDGVVAWVVWQAEAVLAGVQEAQRLCRAVQAGTWRAG$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","Thu Aug 9 09:59:08 2007","","Thu Aug 9 09:59:08 2007","","","Thu Aug 9 09:59:08 2007","Thu Aug 9 09:59:08 2007","Thu Aug 9 09:59:08 2007","","","","","","Thu Aug 9 09:59:08 2007","","","","Thu Aug 9 09:59:08 2007","Thu Aug 9 09:59:08 2007","","","","","yes","","" "ANA_2497","2691797","2690877","921","7.69","2.32","32262","ATGAGCGCGCAGGACCGCGCAAGCGACCTCTCCCGACTGCCAGCGGCGTCACCGGTGACGGCATCGTCCGCCCCACCGGCTGCGCCGGCGCGCGCCCCTGCCGGTCCGTCCCCCACCGGGCACCGAGCGGCGGCCTACTTCGACCTGGACAAGACGATCCTGGCGACGTCGTCGACCTGGGCGCTGGGCACCCCGATGCGGCGCAGCGGCCTCATCTCCTCCCGCGCCCTGGCCTACGGGCTCATCGCCCAGATCCCCTACCTCCTGGTGGGCGCCGGTACCCAGCGCTCCAGCACCCTCATGGAGCACCTGGCCCTCATGTCCGCCGGCATCAGCCGCCGGGACCTGATGGAGGTCGTCGAGGGCGCCCTGACCACGGCGATCGAGCCGGCCGTCTACGCCGAGGCCCTCGACCTCATTGAGGGCCACCGTCGGGCCGGGCACGACGTCGTGGTGGTCTCGGCCTCCATCTCCGAGATGGTCGCCCCCATCGCCCGCCTCGTCGGGGCCGACCGGGCGGTGGCCACCCACATGGAGGTCGGCGAGGACGGCCTGTTCACCGGGCGCATCTCCCGCTCCATGCTGCACTCGGAGAAGGTGGTGGCGCTGCATGAGGACGCCGCCGCCCACGGCATTGACCCGGCCCGGTGCTGGGCCTACTCCGACTCCATCTCCGATGAGCCGATGCTCAGCGCCGTCGGTCATCCGGTCGCCGTCAACCCCGATAGGGACCTGCGGCGCCTGGCGCAGGAGCAGGACTGGCCGGTGCGCGACTTCGCCCGCCCGGTGCGGCTGCGGCCGCGCTGGGAGCCGCCGAGCCTGTCGACCCGGGCCTCGGTCATCGCCCACGTGGCCGGCGTGCTGGCCGTCGGGGGCACCGCCGCCTGCCTTGTTGCCCGACGCAGCCCGCGCGGCAGCTGA","MSAQDRASDLSRLPAASPVTASSAPPAAPARAPAGPSPTGHRAAAYFDLDKTILATSSTWALGTPMRRSGLISSRALAYGLIAQIPYLLVGAGTQRSSTLMEHLALMSAGISRRDLMEVVEGALTTAIEPAVYAEALDLIEGHRRAGHDVVVVSASISEMVAPIARLVGADRAVATHMEVGEDGLFTGRISRSMLHSEKVVALHEDAAAHGIDPARCWAYSDSISDEPMLSAVGHPVAVNPDRDLRRLAQEQDWPVRDFARPVRLRPRWEPPSLSTRASVIAHVAGVLAVGGTAACLVARRSPRGS$","Phosphoserine phosphatase","Membrane, Cytoplasm","Inhibition of morphological differentiationprotein","hypothetical protein","HAD-superfamily subfamily IB hydrolase, TIGR01490","","","","","

InterPro
IPR006383
Domain

HAD-superfamily hydrolase, subfamily IB, PSPase-like
TIGR01488	$\"[44-233]T$	HAD-SF-IB: HAD-superfamily hydrolase, subfa

InterPro
IPR006385
Domain

HAD-superfamily hydrolase, subfamily IB, PSPase-like, bacterial
TIGR01490	$\"[44-245]T$	HAD-SF-IB-hyp1: HAD-superfamily subfamily I

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1000	$\"[132-249]T$	no description
PTHR10000	$\"[100-296]T$	PHOSPHOSERINE PHOSPHATASE
tmhmm	$\"[279-299]?$	transmembrane_regions

","BeTs to 11 clades of COG0560COG name: Phosphoserine phosphataseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0560 is aompkzy---rl--efghsnuj----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","of morphological differentiation protein (PSPASE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2499","2692175","2693398","1224","6.44","-1.91","42021","ATGCCTGTGAGGCAGGCGCCTGTTCCAGCGGGGCGCCGCAGGGGACAGCCGGGCCAGTGGGAGCAGTCGGAGGAGACGCTGACCATCCCGGCACTGGAGGGGCTCGGGGAGGAGGCGGTGCAGGAGCCCGGGGAGGAGGCCCCGGCCTCGGGGGCGACGGGAGGATCGCAGGTGTGGGACGGCCGGGACGTCTCCTTCCCTCCCCTGAGGCCCTCCGCCGGCCGGCCTGTGCGTCCCGGTGGAGAGATACAGCTGGGGGAGAGGGGGACGAGCCAGGGACGGGCACGCTCGGGCTGCTCACTGTCGGAGTCACCGCCGGAACCACCGTCGGAGCCGCTGTGGGCGTCCGCCCCCGTTGGGAGTGGCCGCGGACGTCGTGCCGCACAGGTCCTGGCCGTCACCGGTGCCCGTGGGGGACTGGGGGCCAGCGTCCTGCTGCTGCACCTGGCGTGGGCGCTGGGACGGGCGGGTAGGCGGGTGGCGATGATGGACCTCGACCCCACCGGCGGCCTGGACCTCCTGTGCGGGCAGAGCGTCCTGACCGGGCTGCGCTGGGCGGACCTGCCGGCAGAGGAGTCGGCCTTCCGGCCCGGTCACCTCGTCGGGGCTCTGCCCGTGTGGCACGCCATGCCGGTCCTCACCGGGGACGTGCGTGGAGGCCCCCTGCCGTGTGCGGAGGCGGTCCTGGAGGCGATGCGGGCCGAGCACGACGTCGTGCTGGTGGACCTGCCCCGCGGGGCGTCTCCGCCCCCGGGCGCCGGGGTCCTCATCGTCACCGGGCTCGACCTGCGCTCGGCCGTCGCCGCCGAGAGCATCGTCTCGCGACTGCGGGGTACGGCGCCCGCCGCTGTCGTGGCCGCCGATGCTGAAGCCTCCGCGGCCGTCGCCGCTGCTGCAGAGGTGCCGGTCTGGCTCGTGGCGCGCCAGGTGGGCGAGGACGTCGTCGTCGAGGACCTCGAGCTCATCACCGGCTGCCCGGTCCTGGGGCAGGTCCCCACCGACCGGGTCCTGGCCAAGCGGCTGGCCCTCGGGGAGGACCCGGTGCGGGCCCGCTCAGCCTTCCGGCGCGCCGCGAGCGCCCTGGCCCGGGAGCTGCTGCCCCGGCTCGCCGACGCCGCAGCGCCGGTGAACCGGTCAGTCAGCCAGTCAGTCAGCCAGACAGCGAGACAGACAGGGAATCAGTCCGTCCATCAATCCGGCAATCAGCTGAGGAGGCAGTCATGA","MPVRQAPVPAGRRRGQPGQWEQSEETLTIPALEGLGEEAVQEPGEEAPASGATGGSQVWDGRDVSFPPLRPSAGRPVRPGGEIQLGERGTSQGRARSGCSLSESPPEPPSEPLWASAPVGSGRGRRAAQVLAVTGARGGLGASVLLLHLAWALGRAGRRVAMMDLDPTGGLDLLCGQSVLTGLRWADLPAEESAFRPGHLVGALPVWHAMPVLTGDVRGGPLPCAEAVLEAMRAEHDVVLVDLPRGASPPPGAGVLIVTGLDLRSAVAAESIVSRLRGTAPAAVVAADAEASAAVAAAAEVPVWLVARQVGEDVVVEDLELITGCPVLGQVPTDRVLAKRLALGEDPVRARSAFRRAASALARELLPRLADAAAPVNRSVSQSVSQTARQTGNQSVHQSGNQLRRQS$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[129-365]T$	no description

","BeTs to 4 clades of COG1192COG name: ATPases involved in chromosome partitioningFunctional Class: D [Cellular processes--Cell division and chromosome partitioning]The phylogenetic pattern of COG1192 is -ompk--q-dr-bcefg-snujxitwNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2500","2695936","2694551","1386","12.32","75.74","47744","ATGACGAAGGCCGGCAGGTGGCAGGCGCCCAGCGGCAGGACCAGGCGCACCGCCAGGCGCTCAGCGGCCTCCTCGTCACGGGCGTGCCGCCCCGCGCGCAGGCTCGCCGCCGTCGCCGCCAGGAGGGCGGCCGGTGAGGCCCCGTCCTCCCAGCCGGGGCGCAGGCAGGACTCCAGGCGGGAGCGCCGTGCCCTCCACTGCTCGTCCTCGGGCGCCTGCCAGGCCTCCTCCCACGGGGCGCCCAGCAGCAGGGCCCGCCCCACGACGCCGGCCCCCTTCTCCTCCAGAGCCTCACCCAGGGCGGTGAGTACCCCGGGCACCGAGGCTCCGGCGCTCAGGGCGGCGGAGGCCAGGTCCAGGACCAGGGCCTCATCGACGACGTCGCCCTCAGCAGTCGCGGCGCGGACGAGGCGCCGGGTCACCAGGTGCCCCACGACCATGAGCCCGATGCCCAGCACCCCCACGGCGCTGCCGAGACCGCCGTCGAGCAGGAGGGAGGCGGGGTCGGCGCCCACGAGCATCCCCAGCGCCAGGCCGACCACGGGCAGGCAGGCCAGGAGCCGGGCGGTGCTGCGGGGCCCGGCCAGGGCGGCCCGGCGGGAGGCCTCGGCGCGACCGGACTCAGCCACCCCACCGGCCACGGTCTGGAGGATGTCGGCCAGGGGCGCTCCCAAAGCGGTCGACAGGCGGCAGGAGGCGACGGCGCCCGGCACCCCGGCGGCGGTGGCCCGCCTCTGCCGGGCCCGCCGGCCCCGCGGGGGCGGATGCCAGTGCAGGCGCCCGCAGCTCCATCGAGGCAGCCACGAGTCGTGCTGGAGGTCCGCGAGCGCGCACAGCACGGGTGGGACGCCGTCCTCGTCGGGCTCAGCACCCTCGGTGAGGCCGGCGCGCCGACAGGCGCGTGTCCAAGCCCGCTGCGGGGTGGCGCCGGCGCGCAGGAGACTGGCGACCTCGGTGAGCAGCAGGCCGAGGTCCGGTTCAGGCACCCCGGTGCGTCGGGAGCGCAGCGCGGCGAGCGCCGCCTGCCGCATCGTCGGGCGAGCCTGGGCCGCGGGGGCGCCCGAGGTCCAGCCGCGGGGCAGACCGCGACGGGCCGGCAGCAGGAGCACGGCGGCGGCCAGGGCGACCAGGACCGCTGCGATCCAGGCGCCCGGCACCAACCCGACCGCCGACCCACCCAGCTGCCCAGGCAGCTGCCCGGCCAGGTGCCCCGCCGGGGGCGGGATCGCAGCCGTGCCCGTCACGCCAGCCATGTCCACTCCGCAGGTCGCGTCAGTCATCACGGTCTCCTCTCCCCCGCCCAGGGCAGTGCGTCAAGGCCGGCGCGGGCGAAGGCCTGCGGGCCGATCCGCTCCCGCAGCGCCGCCGCAGCCGGGCCGGACCTGA","MTKAGRWQAPSGRTRRTARRSAASSSRACRPARRLAAVAARRAAGEAPSSQPGRRQDSRRERRALHCSSSGACQASSHGAPSSRARPTTPAPFSSRASPRAVSTPGTEAPALRAAEARSRTRASSTTSPSAVAARTRRRVTRCPTTMSPMPSTPTALPRPPSSRREAGSAPTSIPSARPTTGRQARSRAVLRGPARAARREASARPDSATPPATVWRMSARGAPKAVDRRQEATAPGTPAAVARLCRARRPRGGGCQCRRPQLHRGSHESCWRSASAHSTGGTPSSSGSAPSVRPARRQARVQARCGVAPARRRLATSVSSRPRSGSGTPVRRERSAASAACRIVGRAWAAGAPEVQPRGRPRRAGSRSTAAARATRTAAIQAPGTNPTADPPSCPGSCPARCPAGGGIAAVPVTPAMSTPQVASVITVSSPPPRAVRQGRRGRRPAGRSAPAAPPQPGRT$","Hypothetical protein","Extracellular, Cytoplasm","ppg3, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2501","2693395","2694657","1263","6.31","-3.96","43357","ATGACCCCGGAGAGTCCCAATCAGCCCAGAGTTCCCGGCCCTCCCGGCGAGGGTGGGACGGACGATCCCGAGCTGGTCCGCGTCCGCAGCGCCCTGGCTCGCGGCGTGGGCCTGGAGGAGGCCCTCAACGATGCCGCCGCCCCCGCCACCGGACAGGTGGGGATGGCGCGCCTGGGTCAGCGGGTGCGCGCCGACGTCGACGGCGCCGGGCCGCTCCTCCAACCCCTCATCGAGTCCGACGGTGTCACCGATGTCCTCGTCAGTGGCGGGCGCACCTGGATCGACCGGGGACACGGCCTCGAACCCGTCCCCGCGGCCACCATGGATGAACCCGAGGTGCGGGCCCTGGCCGTGCGCATGGCCGCATCCGCCCACAAGCGCCTCGACGACGCCTGCCCCGTCGTCGACGCCACCCTGCCCGACGGCACCCGACTCAACGCGGTGCTGCCGCCCCTGAGCGCCGATGGCACTCTCATCAGTCTGCGCACCAAGCGCCGCCGCGGCTTCACCTTGGACGAGCTGACCGCCGCCGGCACGATCGCCCCCGGTCTGGACGAGGTCCTGGCCGCCCTGGTGGCCGGCCGCGCCAGCTGTCTGGTCACCGGCGCCACCGGTACCGGCAAGACCACCCTCCTGGCCGCTCTGCTCTCACTCGTCCCGGACACTGAGCGCATCGTGTGCATCGAGGAGGCCAGCGAGCTGCGCCCCGATCACCCCCACGTCGTCCACCTCCAGGAGCGCGGCGCCAACGTCCAGGGAGTCGGGGCGGTCTCGATGACCTCTCTGGTGCGCACCGCCCTGCGCATGCGGCCCGACCGGATCGTCCTGGGCGAGTGCCGCGGCCCCGAGGTGCGAGACGTCCTCACCGCCCTCAACACCGGCCACGAGGGCGGCTGGGCCACCCTCCACGCCAACTCTCCCGCCGACGTCCCCGCCCGCCTGACCGCCCTGGGGGCGCTCGCGGGACTCGACGAGGCCGCCGTCGCCGCCCAGGCGGCCAGCGCCCTCGACGCCGTTGTCCACCTGCGCCGGCAGGCCGGGGCCGCCGGTGCGCGCCGGTACGTGGCCTCCGTCGGCGTGCTGCGGCGTGAGGCGTCCCCGACCGGAGCGGTCCTCATCTGCGAGGAGGCCCTGCACGTGACGGGCGACGGCCGCCTCAGGTCCGGCCCGGCTGCGGCGGCGCTGCGGGAGCGGATCGGCCCGCAGGCCTTCGCCCGCGCCGGCCTTGACGCACTGCCCTGGGCGGGGGAGAGGAGACCGTGA","MTPESPNQPRVPGPPGEGGTDDPELVRVRSALARGVGLEEALNDAAAPATGQVGMARLGQRVRADVDGAGPLLQPLIESDGVTDVLVSGGRTWIDRGHGLEPVPAATMDEPEVRALAVRMAASAHKRLDDACPVVDATLPDGTRLNAVLPPLSADGTLISLRTKRRRGFTLDELTAAGTIAPGLDEVLAALVAGRASCLVTGATGTGKTTLLAALLSLVPDTERIVCIEEASELRPDHPHVVHLQERGANVQGVGAVSMTSLVRTALRMRPDRIVLGECRGPEVRDVLTALNTGHEGGWATLHANSPADVPARLTALGALAGLDEAAVAAQAASALDAVVHLRRQAGAAGARRYVASVGVLRREASPTGAVLICEEALHVTGDGRLRSGPAAAALRERIGPQAFARAGLDALPWAGERRP$","Type II secretion system protein E","Cytoplasm","Predicted ATPases involved in pili and flagellabiosynthesis, VirB11 family","K02283 pilus assembly protein CpaF","type II secretion system protein E","","Salmond G.P., Reeves P.J. Membrane traffic wardens and protein secretion in gram-negative bacteria. Trends Biochem. Sci. 1993. 18(1):7-12. PMID: 8438237Hobbs M., Mattick J.S. Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes. Mol. Microbiol. 1993. 10(2):233-243. PMID: 7934814","","","

InterPro
IPR001482
Domain

Bacterial type II secretion system protein E
PD000739	$\"[173-272]T$	Q82EK8_STRAW_Q82EK8;
PF00437	$\"[59-346]T$	GSPII_E

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[160-344]T$	no description

InterPro
IPR013991
Domain

PhnA protein N-terminal, proteobacterial
SM00782	$\"[128-165]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-42]?$	signal-peptide
tmhmm	$\"[24-46]?$ $\"[52-72]?$	transmembrane_regions

InterPro
IPR003779
Domain

Carboxymuconolactone decarboxylase
PF02627	$\"[93-174]T$	CMD

InterPro
IPR004674
Family

Alkylhydroperoxidase AhpD
TIGR00777	$\"[2-176]T$	ahpD: alkylhydroperoxidase, AhpD family

InterPro
IPR004675
Domain

Alkylhydroperoxidase AhpD core
TIGR00778	$\"[111-161]T$	ahpD_dom: alkylhydroperoxidase AhpD family

noIPR
unintegrated

unintegrated
G3DSA:1.20.1290.10	$\"[119-176]T$	no description

","BeTs to 4 clades of COG2128COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG2128 is ---------dr-b-ef---n-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-67% similar to PDB:1ME5 Crystal Structure of Mycobacterium Tuberculosis Alkylperoxidase AhpD H132Q Mutant (E_value = 1.9E_42);-67% similar to PDB:1GU9 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ALKYLPEROXIDASE AHPD (E_value = 3.2E_42);-67% similar to PDB:1KNC Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity. (E_value = 3.2E_42);-66% similar to PDB:1LW1 Crystal Structure Of Mycobacterium Tuberculosis Alkylperoxidase Ahpd H137F mutant (E_value = 3.5E_41);","Residues 93 to 174 (E_value = 1.3e-10) place ANA_2503 in the CMD family which is described as Carboxymuconolactone decarboxylase family.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2504","2697879","2697301","579","4.58","-14.43","21282","ATGGCCGTTCTCTCCATCGGAGACCAGTTCCCCGCCTACGAGCTCACCGCCGTCGTCCCCGGCAACCTCAAGGAGGTTGAGGCCAGCAAGCCCGAGGACTACTTCACCACCGTCTCCTCCCAGGTCCCCGCCGGCACCTGGCGCGTCGTCTTCTTCTGGCCCAAGGACTTCACCTTCGTGTGCCCCACCGAGATCGCCGCCTTCGGCGACCTCTACCAGGACTTCAAGGACCGCGACTGCGAGGTCGTGGGCGTCTCGGTGGACAACGAGTACACCCACTACGCCTGGCGCCGCAGCCACGACAAGCTCCAGGACCTGCCCTTCCCCATGGCCAGCGACCTGAACCGCGAGCTCACCGAGGCCCTGGGCATCAAGCGCCCCACCGGTGAGGCCGACCGCGCCACCTTCATCATCGACCCCCACAACGTCATCCAGTCGGTCTCCGTGACCGCCGACTCCGTGGGCCGCAACACCGAGGAGGTCCTGCGCCAGCTCGACGCCCTCCAGTCCGACGAGCTGTGCGCCTGCAACTGGCAGGCCGGCGCCGCCACCATCGACGCCCTGGGCCAGATGGGCTGA","MAVLSIGDQFPAYELTAVVPGNLKEVEASKPEDYFTTVSSQVPAGTWRVVFFWPKDFTFVCPTEIAAFGDLYQDFKDRDCEVVGVSVDNEYTHYAWRRSHDKLQDLPFPMASDLNRELTEALGIKRPTGEADRATFIIDPHNVIQSVSVTADSVGRNTEEVLRQLDALQSDELCACNWQAGAATIDALGQMG$","Alkyl hydroperoxide reductase","Cytoplasm","alkyl hydroperoxide reductase C","alkyl hydroperoxide reductase ","alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen","","Wood Z.A., Schroder E., Robin harris J., Poole L.B. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 2003. 28(1):32-40. PMID: 12517450","","","

InterPro
IPR000866
Domain

Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
PF00578	$\"[6-147]T$	AhpC-TSA

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[4-185]T$	no description

noIPR
unintegrated

unintegrated
PTHR10681	$\"[4-186]T$	PEROXIREDOXIN
PTHR10681:SF6	$\"[4-186]T$	gb def: Alkyl hydroperoxide reductase

","BeTs to 22 clades of COG0450COG name: PeroxiredoxinFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0450 is aompkzyqvdrlbcefghs-ujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000866 (Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen) with a combined E-value of 1.2e-17. IPB000866A 45-64 IPB000866B 82-96","","","-79% similar to PDB:2BMX MYCOBACTERIUM TUBERCULOSIS AHPC (E_value = 4.0E_68);-56% similar to PDB:1QMV THIOREDOXIN PEROXIDASE B FROM RED BLOOD CELLS (E_value = 2.5E_30);-56% similar to PDB:1YEP Structural and biochemical analysis of the link between enzymatic activity and olgomerization in AhpC, a bacterial peroxiredoxin. (E_value = 3.1E_28);-55% similar to PDB:1YF1 Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin. (E_value = 1.2E_27);-56% similar to PDB:1QQ2 CRYSTAL STRUCTURE OF A MAMMALIAN 2-CYS PEROXIREDOXIN, HBP23. (E_value = 1.5E_27);","Residues 5 to 168 (E_value = 2.5e-07) place ANA_2504 in the Redoxin family which is described as Redoxin.Residues 6 to 147 (E_value = 9.7e-44) place ANA_2504 in the AhpC-TSA family which is described as AhpC/TSA family.","","hydroperoxide reductase C","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2506","2698201","2699211","1011","5.71","-10.70","36687","ATGAGTCCTCGTCTCAGCCGGATCAGCATCCTCGAGCAGGTCCCTCTCTTCGAGGGAGGAGACGTTCGCCAGACCCTGGGGGATCTCGTCCACCTGGGGCGCGGCCTGGAGGAGTCCGGCTACCACCGCCTCTGGCTGGCCGAACACCACAACACCGGCTCCTTCCTGTCCTCGGCGCCTGACCTGCTCATGATGCACATCCTGGACGCCACCAACCGCATCCGGGTGGGCTCGGGCGGCGTCATGGCCATGCACTACGGCTCGCTCCAGATGGCCGAGCGCTTCGCCACCCTGGCCACCCTCCACCCCGGCCGCGTCGACATGGGCCTGGGCCGCGCTCCCGGCGGGGACATGCGCGCGGCCGCAGCCCTCAACCAGGGCCGCGTCATCGACCCCGACGCCATCAACGCCCTCATCGAGGAGACGGTCGCCCTCCTGCGCGACGACCTTCCCGCCACCCACCCCTACGCCTCTGTCGAGGTCCGTCCTCTCCCGGCCCAGATGCCGGAGGTCTGGCTCCTGGGCTCCTCAGGTCAGTCGGCCGCCTGGGCCGGCGTCCACGACCTCAACTACGCCTACGCCCAGTTCTTCACTGGCCGCCAGCAGGTCGAGATCATGAACCACTACCGCGCCCACCTCCCCGAGGGGTCCGGCCGCGGCTCCATCCACGGGGGTCAGACCCTCTCCGCCCTGTGCGTCAGCGCCGCCGCCACCCGCGAGGAGGCCCGCGAGCAGGCCCTCGTGGCCGCCGACGCCCGCTTCAGCCTGCGCACCGGCCGACCCATGTGCTTCCGCGACCCGTCCACCCTCGATGCCGCCTACCGCGCCGAGGTCGAGCGCTACCTCGAGCGCGACACCGCCATCATCGTGGGCACCTACGACGAGGTCGCCCAGGCCCTGTCCTCCTTCGCCGAGAACCACGGCACCGAGGAGGTCATGCTCATCAGCTACATCGACGACGTCGAGGTCAAGAACCACCAGTACGCCGAGCTCGCCGCCCGCCTCCTGTGA","MSPRLSRISILEQVPLFEGGDVRQTLGDLVHLGRGLEESGYHRLWLAEHHNTGSFLSSAPDLLMMHILDATNRIRVGSGGVMAMHYGSLQMAERFATLATLHPGRVDMGLGRAPGGDMRAAAALNQGRVIDPDAINALIEETVALLRDDLPATHPYASVEVRPLPAQMPEVWLLGSSGQSAAWAGVHDLNYAYAQFFTGRQQVEIMNHYRAHLPEGSGRGSIHGGQTLSALCVSAAATREEAREQALVAADARFSLRTGRPMCFRDPSTLDAAYRAEVERYLERDTAIIVGTYDEVAQALSSFAENHGTEEVMLISYIDDVEVKNHQYAELAARLL$","Bacterial luciferase family protein","Cytoplasm","bacterial luciferase family protein","bacterial luciferase family protein","luciferase family protein","","Fisher A.J., Thompson T.B., Thoden J.B., Baldwin T.O., Rayment I. The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 1996. 271(36):21956-21968. PMID: 8703001Moore S.A., James M.N. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 1995. 249(1):195-214. PMID: 7776372Eichhorn E., Davey C.A., Sargent D.F., Leisinger T., Richmond T.J. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J. Mol. Biol. 2002. 324(3):457-468. PMID: 12445781Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J. Mol. Biol. 2000. 300(4):935-950. PMID: 10891279","","","

InterPro
IPR011251
Family

Bacterial luciferase-like
G3DSA:3.20.20.30	$\"[7-335]T$	no description
PF00296	$\"[16-335]T$	Bac_luciferase

","BeTs to 10 clades of COG2141COG name: Coenzyme F420-dependent N5,N10-methylene tetrahydromethanopterin reductase and related flavin-dependent oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG2141 is aom------drlb-ef--s--j----Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 16 to 335 (E_value = 1.5e-08) place ANA_2506 in the Bac_luciferase family which is described as Luciferase-like monooxygenase.","","luciferase family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2508","2699297","2700976","1680","4.88","-26.33","57686","ATGAGCCCCGCGAGCGCCCGGTCCGCCTCTGAGTCCTCCTCCTTCCCGCCTCCGGCGGCCACGCCCGAGCAGGCGGCGCGCCTGCGGGCGGACCTGGCCGACTCCGGCTGGGGTGTGGAGGCGGTGGCCGCCCTCCTGGGCGAGGCCGCCGACGCCGCCCTGCGCCGCGAGATCCGCCTGCCCGCCCTGCGAGCCGTGCGCGCCGCCCTGGCCGCCGGGCCCGCCCCCTCACCCGTGGCCGTCCTGACCGCCCTGTTCATGCTCGGTGAGCCGGTCCCCGCCGCCGCCCTCGACGCCGCTCTGCCCCGCACGACAGCGGCGGGCGCCGCTGCTATCGGCCTGGTCGGCGAGCCCGATGGGGCCGGATATGTCCGTGCCCTGGTCGACCTGCGTCCCCACGAGGCCGTCGACGACGCCGGTGAGGTCCGCTGGTGGGTGGCCTCCGACCTGGGTGAGCTCGTCACCGGCCGGGCGCTGGCCCCCGATCATGTCCTGGGTGTCGGCGGCGCCGGCCTCACCCTGGCGGGCCTGACCCCGCGCAGGCGGGTGGGCACCGCCCTGGACCTGGGCTGCGGCTGCGGCATCCAGACCCTCTACCTGCTGCGTCACGCCGAGCACGTGGTGGCCACCGACATCTCCGCGCGCGCCCTGGCCTTCACCGCCTTCAACGCTGCCCTGGCCGGCGTGAGCGTCACCGGTGCTCCAGGCGCCGATTCCGGAGCTGACGCCGCGTCCGAGGCCGACGTTGAGCCCGGCTCCGCTTCGGGCGCGGGCCGCCTGGAGCTCCTGCGCGGCTCCCTCCTGGAGCCGGTAGCCGGTCGCCGCTTCGACCTCATCGCCTCCAACCCGCCCTTCGTCCTCACCCCGCCGGCGGTACGCGAGGCCGGCCTGCCCCTCATGGAGTACCGCGACGCCGGCGGCCCCATCCTGCCGGGGCTCGTCGCCGGGCTCGGCGAGCACCTCGAGCTCGGGGCGAGCGCCGTCATGCTCGGCAACTGGGAGCACCGTGGCGCCGGCTCGTGGCGCGACGCCGTGGCCGCATGGCTCCCCGAGGGGCTCGACGCCTGGGTCATTGAGCGCGAGCTCCAGGACCCGGTGGAGTACGCCACCATGTGGCTGCGCGACGGCGGCCTGACCCCCGAGCGCGACCCGGAGGCCTTCGACGCCGCCCTGGAGGCGTGGATCGACGACTTCGAGGTCCGCGACGTGCGGGGCGTCGGCTTCGGCTACCTCATCGTCCACCGTCCCCGGCATCCCCGCGAGCCCTGGCGCCTCCTGGAGGAGGTGACCACCTCCGGTCAGGGGGTCCTGGGCCCCCATGTCGCCGAGGTGCTGGAGGTGCGCGAGCGCCTCGCCGGCCTCGACGACGACGCCGTCGCCGACCTGCGCCCGCTCCTGGCCCCCGACGTCACTGAGGAGCGTCACCTCATTCCGGGCGCCGCCGAGCCCACGGTCATCCTGCTGCGTCAGGGCGGAGGGCTGGGGCGCACGCTGCAGGCCTCCACGGCGGTGGCCGCCCTGGCCGGGGTGGCCGACGGTGAGCTGAGCGTCGGGCAGGTCGCCTCCGCGGTCGCCGCCCTTAGTGAGCTGAACGCAGTCGATGCGCTCGCGCTGCGCGCGGAGATGGTCGAGGCGGCCCGTCATCTTCTGACCACAGGATTCCTGCGCCCAGGAAAGTGA","MSPASARSASESSSFPPPAATPEQAARLRADLADSGWGVEAVAALLGEAADAALRREIRLPALRAVRAALAAGPAPSPVAVLTALFMLGEPVPAAALDAALPRTTAAGAAAIGLVGEPDGAGYVRALVDLRPHEAVDDAGEVRWWVASDLGELVTGRALAPDHVLGVGGAGLTLAGLTPRRRVGTALDLGCGCGIQTLYLLRHAEHVVATDISARALAFTAFNAALAGVSVTGAPGADSGADAASEADVEPGSASGAGRLELLRGSLLEPVAGRRFDLIASNPPFVLTPPAVREAGLPLMEYRDAGGPILPGLVAGLGEHLELGASAVMLGNWEHRGAGSWRDAVAAWLPEGLDAWVIERELQDPVEYATMWLRDGGLTPERDPEAFDAALEAWIDDFEVRDVRGVGFGYLIVHRPRHPREPWRLLEEVTTSGQGVLGPHVAEVLEVRERLAGLDDDAVADLRPLLAPDVTEERHLIPGAAEPTVILLRQGGGLGRTLQASTAVAALAGVADGELSVGQVASAVAALSELNAVDALALRAEMVEAARHLLTTGFLRPGK$","SAM-dependent methyltransferase","Cytoplasm","Predicted rRNA or tRNA methylase","methyltransferase small","hypothetical protein","Chen P, Cisar JO, Hess S, Ho JT, Leung KP.Amended Description of the Genes for Synthesis of Actinomyces naeslundii T14V Type 1 Fimbriae and Associated Adhesin.Infect Immun. 2007 Aug;75(8):4181-5.PMID: 17485454","Cheng X. Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 1995. 24:293-318. PMID: 7663118Loenen W.A., Daniel A.S., Braymer H.D., Murray N.E. Organization and sequence of the hsd genes of Escherichia coli K-12. J. Mol. Biol. 1987. 198(2):159-170. PMID: 3323532Narva K.E., Van Etten J.L., Slatko B.E., Benner J.S. The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases. Gene 1988. 74(1):253-259. PMID: 3248728Lauster R. Evolution of type II DNA methyltransferases. A gene duplication model. J. Mol. Biol. 1989. 206(2):313-321. PMID: 2541254Timinskas A., Butkus V., Janulaitis A. Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases. Gene 1995. 157(1):3-11. PMID: 7607512Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E., Schildkraut I., Saenger W. Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. U.S.A. 1994. 91(23):10957-10961. PMID: 7971991","","","

InterPro
IPR002052
Domain

N-6 Adenine-specific DNA methylase
PS00092	$\"[279-285]?$	N6_MTASE

InterPro
IPR013216
Domain

Methyltransferase type 11
PF08241	$\"[187-231]T$	Methyltransf_11

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[171-338]T$	no description
PTHR18895	$\"[169-230]T$ $\"[260-401]T$	METHYLTRANSFERASE
PTHR18895:SF6	$\"[169-230]T$ $\"[260-401]T$	RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE D (RRNA (GUANINE-N(2)-)-METHYLTRANSFERASE)

","BeTs to 7 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 184 to 231 (E_value = 5.4e-07) place ANA_2508 in the MTS family which is described as Methyltransferase small domain.Residues 187 to 231 (E_value = 1.6e-06) place ANA_2508 in the Methyltransf_11 family which is described as Methyltransferase domain.","","rRNA or tRNA methylase","","1","","","","","","","","","","","","Thu Jul 26 15:12:33 2007","","","","Thu Jul 26 15:12:33 2007","","","","Thu Jul 26 15:12:33 2007","Thu Jul 26 15:12:33 2007","","","","","yes","","" "ANA_2509","2701300","2705541","4242","7.09","0.67","149202","ATGTCCCAGTCATCACGTCGCCCGCAGCGCGGGCGTGAAGGACTACTGCGCAGATTCTGTGCGGTGGTCGGTTCTCTTGCGATCGTCCTGGTGACCATGGTGTCGCTGCCGTGGACGGCGCCTCCCGCGGATGCCTCCACCAGTGACCTCAGTATTCCCCTGGGGGACACTGCGGTGCAGATCTCCTATGTGCGCACCATTGACACTATTGATCGGGTGTACGACACGGTGAACGGAGTCGGCTACGACTCCTACCCGTGGGAGTGGGCATACGCGCGTGCCTGCACTCGCTACTCGCCGGGGGCCAATAACTACTGGACTGACTATGTTCGCGGCAGCAGCGGCCAGTACGCGGCGGTCGGTTATGGACGCAAGGTGGATGAGGGTGCCTGCCCCACCTACTACCAAGGCGAGCCGGGTGATGTGCAGACCTCGCTGGGTTTCCAGCCCTCCAACACCACGAGCGTCAAGGCCGGAAACGTCTTCCTCGTGGGGCGGATGCGCCACGTCAACAGCCCGATCTACTCCGACAACAGCGCCGTGACCAACCCCTCCGAGGGTAAGGGCACCACCTACTACGGCAGCTTCAACATCAACACCGCCCAGACGATTCAGGCCGACTTCCCGTGGACCGAGTTCGACACCACGAACGTCTGCACCGGGAAGCTCGACTCGAACGGCAAGCTCATCATCGGCGACTACGGCACTGAAAATCAGACGGTCAGGACGCAGTACGCCTATGACCGGAACGGGAGGGTTGGCCGTTACGACGGGTCCACCTACACCTACCTGTACAAGAACGGCTCCCTGGTCTGGTTCAACGGTGTCATGACCCAGGACTTCACCGACAAGATCGGACACAGCTGCGCCGACGACATCCTCGACATCAAGTCTGACCGCTCCGACACTGCCTGGACGGACCCCAACACCGGCATCAAGTACAAGCTCAAGCTGTGGGGATTCGTCAACAACGGAGACAACCAGCAGTGCCGCCCCGACATGGAGAAGGCGGAGACCTCCAACCTGGAGGAGCGCTTCATCACCCGTGAGCGGGCCGTCTCCTACGGCTGCCTCTACGGCTCCATCGAGCAGGAGCGCCCGGTGACCTTCGCCAAGGACGTCAAGGCGGACTCATCGGTTCAGGGATCGTTGACGATCCCCACCTTCAACTACGTTAACGTCTCACCGGAAGGAACCTTCGGCGCAAGGACCTGGGGGACCCCCAAGTCCCTGACCCCCTCCTGGAACTCTGAGGACGTCGACCCCAAGAGCTACACCCTGCTGGCTCCCAACGACGCCGCCACGGTGCAGGAGGCGGGCACCACCCCGCAGGCCTCCGTTGACCGCAGGACCGGTGACGTGTGGACCACCGGCTGGTTCCTGCGCGACGTCAGCTGCACGGTGGGGAACGGCAGCGCTCCCCTGCTGCGCCGTGACGGAACCACCCACCTGGACAAGTCCGACTCCGTGAACCTCGAGCAGCGCACCATCCGCCTCGATGAGACTCAGCTGGCTGAGCGCCAGGAAGAGGTCGCCGTCAAGTGCGTCTGGCACAACGAGTACGTCGTCGGCCGTGGGCGCGTCACCCTCGTCAACATTGTCGACGGCGGCAGCGCCAGGCCCGAGCAATGGACCCTGACCGCCAAGCCCGCCACCGATGGGCTCTTCGGGCAGAAGACCATCACCGGCGCCAGCGGCACGCCCGCCGTCAGCAAGGTCTACACCGCCGGCGGCACCTACGGCCTGTCCGCGGGCAACGGCCCCGAGGGCTACTCGCAGAACGGCCCCTGGGTCTGCACCAACGACGACGGCAGTAACGTGCCCGTCAGCGCGGACAACAAGTTCGTGCTGGGGGAGGGCAAGAACGTCACCTGCGTCGTGCACCAGAAGCCTCAGCAGACCCCCGTCAGCGCGGTCAAGAGCGTTGAGGGCGCCTCCGACGCCGCCACGGCCGGCTCCTACTCCCTGAGCTACACCTGCACCCCGGGTCCCGACGGCAAGGGCTCCTCCACCGGCAAGATCACCGTGGACGCCCAGGGCAATGCCGCGAACCTGCCCGCCCAGCGCGTGGGTGCCACCTGCACCGTCACCGAGGATGCTCGTGACGCCAGGGGACTCAAGCAGCCCGGAACCGCCGCCGGCGGAAGCGTCAGCTGGAAGGACCCGGCCGCCTTCAAGGTGGTCACCAACCCGGGCAACCAGGAGAGGGAACTCGCCTCCACCGCCGTGGCCCCGACCAACGGCAACGCAGGCGGTGTCACCTTCACCGTGCCCGACTCCACGCAGGGAGCCGTGCGGGTCAAGGTCGTCAACTCCGTCGTCCCGCACGCCGGTATCGACAAGACCTTCAGCAAGGTCACCAAGAGCACCGAGAAGGTCAACGGTCGCACCACCTTCGACCAGACCTACACCATCACGGTGACCAACCCCTCCGCCAAGGCGGGCCTCACCTACGACCTCAACGACGCCTGGCAGGTCCCCACCGGGGTCACCGTCCACAAGGTCAGCATCTCAGGTGGCGCCATCAACGGCACCGAGACGCCTCAGGCCGGAGTGCCCTACGTCAAGACCGGCATCTCCCTGCCCGCGGGCCAGAAGCACACCTACACGGTGGTGCTCAACGTCTCCGGTCCCGACGCCGGACTGCCCGGCATCCAGGGAACCTGCACCCCGGGCGCCGTCGGTCAGGGCAAGGCCATCTACAACAAGGCCTCAGTGACCACCAAGGGCGACGGGCAGCCCAAGGAGGCCGCGGCCTGCGGCACCCTGCCCGCCAACCCCCAGTTCAAGGCCTCCAAGAGCCCGCTCGACGTGGTCCGCAACAGTGATGGCACCTTCACCTCCAGCTACACGGTGACGGTCACCAACACCTCCCTGGTCGCCAGCCCGGTGGCCGCCGACCTCACCGACACCCCGCAGATGCCCACCGGCACCCGCCTGAGCCGGATCAAGGTCCTGGAGAAGGGAGTCGACGCCCAGGGCGTCACCCTGCCCGCCATTAACCCTGCCAACGGAACCCTCAACGGCTCGATCACCCTCATCAAGGGCGGAACCGGCGAGCGCCTCGCCGCCGCTCCCCGGGCCGGGGCCGACGGAGGCAGCCGCACCTTCACGATGCAGATGACCTTCACGGTCCGTGAGAACACCCCGGGCTTCAATGAGGCCGACTTCCAGTGCGGTCACCAGCGCGCCGACGGCAAGCCCTCCGGCCTGGTCAACACCATCGCCATGGAAGGTGACACCGACGGTGACGGGAACAACCACGGTTGCCTCTCCACCGACGGCAAGCTGAAGTTCTCCAAGGAGGTCACCACCCAGCCCGGCAACGGCTCGACCTTCGATGTCGTCTACACCGTGAGCGTGGTCAACGAGGGATCGCTGTCGGTGTCCACCGGACCGATCAACGACAAGCCCTCCTTCGCCCCCGGGCTCAACCCGACCCTGGTCAAGGTGCAGCGTGAGATGGGACCGACCCGGACAGTCAATGCCCAGGCCGACGGCTCCTACCGCCTGTCCGACAACGAGACCCTCTACTCGGGCCTGACGATCCGCTACACCGTCACCTTCACGGTGAAGATCGACCCGTCAGTTACCGGATACCGCGATGAGCTGCTGTCCTGCACCACGGACAAGGGGCGCCTCGTTCCCGGCCACGGCCTCTACAACAAGGTCGTGCCTCAGACGGGCAAGGACTCCGACACCCGGCCCGACCACGACGTGGCCTGCGCCAACGTCTCGCCCAATGCCGGCAAGCGCATCCTGTCGATCGTCAAGACCGGCAGCCAGGGTCCCCTGGACGACGCGGCCTTCGACATCTACCCGATGGACCCCTCCACCCCGGGTGCCAAGCCCCTGACCGACGGTGTGACCTTCACCGGCGGCAAGGGAACCGGAACCTTCACCACCACGGGACTGGCCATCAACCGCGAGTACTGGCTGGTGGAGACCAAGGCTCCCGCCGGGCACCAGCTCATGGCCAAGCCGGCCCGCTTCAAGGTGACCGACACGGGCATCGAGCTCATCACCGCCACTCCCGGCGGCTCGGCCCTGACGGTCTCGCGCAGCGGTGCCAGCAAGTCCGACGACACCATCACCGTCCGAGACCTCCAGATCGGCACCCTGCCGCTGTCCGGTGGACGCGGAATCGGCATGAACATCGCCGTCGGAATCGCGGCCATCACCGGCGCCGGCCTGCTGGCACTGCGTCAACGAAAGACTTCCTCGTTCGGGCGCTCAGCCTGA","MSQSSRRPQRGREGLLRRFCAVVGSLAIVLVTMVSLPWTAPPADASTSDLSIPLGDTAVQISYVRTIDTIDRVYDTVNGVGYDSYPWEWAYARACTRYSPGANNYWTDYVRGSSGQYAAVGYGRKVDEGACPTYYQGEPGDVQTSLGFQPSNTTSVKAGNVFLVGRMRHVNSPIYSDNSAVTNPSEGKGTTYYGSFNINTAQTIQADFPWTEFDTTNVCTGKLDSNGKLIIGDYGTENQTVRTQYAYDRNGRVGRYDGSTYTYLYKNGSLVWFNGVMTQDFTDKIGHSCADDILDIKSDRSDTAWTDPNTGIKYKLKLWGFVNNGDNQQCRPDMEKAETSNLEERFITRERAVSYGCLYGSIEQERPVTFAKDVKADSSVQGSLTIPTFNYVNVSPEGTFGARTWGTPKSLTPSWNSEDVDPKSYTLLAPNDAATVQEAGTTPQASVDRRTGDVWTTGWFLRDVSCTVGNGSAPLLRRDGTTHLDKSDSVNLEQRTIRLDETQLAERQEEVAVKCVWHNEYVVGRGRVTLVNIVDGGSARPEQWTLTAKPATDGLFGQKTITGASGTPAVSKVYTAGGTYGLSAGNGPEGYSQNGPWVCTNDDGSNVPVSADNKFVLGEGKNVTCVVHQKPQQTPVSAVKSVEGASDAATAGSYSLSYTCTPGPDGKGSSTGKITVDAQGNAANLPAQRVGATCTVTEDARDARGLKQPGTAAGGSVSWKDPAAFKVVTNPGNQERELASTAVAPTNGNAGGVTFTVPDSTQGAVRVKVVNSVVPHAGIDKTFSKVTKSTEKVNGRTTFDQTYTITVTNPSAKAGLTYDLNDAWQVPTGVTVHKVSISGGAINGTETPQAGVPYVKTGISLPAGQKHTYTVVLNVSGPDAGLPGIQGTCTPGAVGQGKAIYNKASVTTKGDGQPKEAAACGTLPANPQFKASKSPLDVVRNSDGTFTSSYTVTVTNTSLVASPVAADLTDTPQMPTGTRLSRIKVLEKGVDAQGVTLPAINPANGTLNGSITLIKGGTGERLAAAPRAGADGGSRTFTMQMTFTVRENTPGFNEADFQCGHQRADGKPSGLVNTIAMEGDTDGDGNNHGCLSTDGKLKFSKEVTTQPGNGSTFDVVYTVSVVNEGSLSVSTGPINDKPSFAPGLNPTLVKVQREMGPTRTVNAQADGSYRLSDNETLYSGLTIRYTVTFTVKIDPSVTGYRDELLSCTTDKGRLVPGHGLYNKVVPQTGKDSDTRPDHDVACANVSPNAGKRILSIVKTGSQGPLDDAAFDIYPMDPSTPGAKPLTDGVTFTGGKGTGTFTTTGLAINREYWLVETKAPAGHQLMAKPARFKVTDTGIELITATPGGSALTVSRSGASKSDDTITVRDLQIGTLPLSGGRGIGMNIAVGIAAITGAGLLALRQRKTSSFGRSA$","Usher-like protein precursor","Extracellular, Periplasm","usher-like protein precursor","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","Li T, Johansson I, Hay DI, Strmberg N.Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins.Infect Immun. 1999 May;67(5):2053-9.PMID: 10225854Chen P, Cisar JO, Hess S, Ho JT, Leung KP.Amended Description of the Genes for Synthesis of Actinomyces naeslundii T14V Type 1 Fimbriae and Associated Adhesin.Infect Immun. 2007 Aug;75(8):4181-5.PMID: 17485454","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[1381-1401]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein precursor","","1","","","Wed Aug 15 20:11:01 2007","","Wed Aug 15 20:11:01 2007","","","Wed Aug 15 20:11:01 2007","Wed Aug 15 20:11:01 2007","Wed Aug 15 20:11:01 2007","","Wed Aug 15 20:11:01 2007","","","","Thu Jul 26 15:13:23 2007","","","","Thu Jul 26 15:13:23 2007","Thu Jul 26 15:13:23 2007","","","","","yes","","" "ANA_2510","2705631","2707226","1596","5.62","-8.42","56793","ATGCACTCCCTCAACACGCGCCGGGGCCTCGGCCTCGCCGCTGCGATGACGCTCGCCGCCGGCGCGCTCGTCGCCCCGACCGGCGCGGCGGCACCCGCTGACCCGAACGGCTCCACCATCGACCCCCAGGCGGCCACCACGCTGACCGTCCACAAGTGCGAGCAGACCGACACCAACGGCGTCAAGGAGGGGACCGGTAACGAGGACCCCCAGGCCGAGTGCAAGCCCGTCTCCGACGTCGAGTTCACCATCACCAAGCTGAACGTGGACCTGACCACCTACGACGGCTGGAAGACCCTCGCCGACCTCAAGGGGAACGTTTTCGCAGCCGGTGACCTCAAGACCGACACCGTCCAGAAGATCACCACCGGTGCTGACGGCCTGGCCTCCTTCACCGACGCCCAGACCGAGGTCGGCGCCTACCTCGTCAGCGAGACGCGCACCCCCGACAAGGTCATCCCGGCCGAGGACTTCGTCGTCACCCTGCCGATGACCAACCCGGAGCGCACCAGCGAGTGGAACTACAACGTCCACGTCTACCCCAAGAACACCCTCTCCGGTGTGGACAAGCAGGTGACCGACAAACCGGCCCCCGGCTCCGGGCGCGACATCACCTACACCATCACCACCTCCATCCCGAAGGTGGACTACCCCGGCGGTGCGCGCATCAAGCGCTACGAGGTCGTTGACCAGCTCGACAAGCGCATCAAGAAGGACGCCCTGGCCCCAGTCGTCAAGATTGTCGGCAAGAAGGAGGTGACCCTGGCGGAGACCACCGACTACACCGTCATCACCGCTGAGGGCACCGACCACAACTGGGCCACCATCCAGCTCACCGAGGAGGGCCGCCGCAAGGCCTCCGAGGAGCGCTACAACGGCACCGGCGAGACCAAGCTCCAGGTGACCCTGACCGCCAAGTTCGACGCCAACGTCAACCTCGAGGGCGACCTGTCCAACACCGCGGGCCTCATCCCCAACGACAGCCCCAACTTCACCTGGGACCCGAGCCACCCCGGCACGAAGGTCCCCGGCATTCCCACCACCCCCGTGCTCTCCAAGTACGGCAAGGTGGTTCTCACCAAGACCGGTACGGACCAGCTGGCCGACAAGACCAAGTACAACGGCGCCCAGTTCCAGGTCTACGAGTGCACCAAGACCGCCAGCGGTGCCACGCTGCGTGACTCCGACCCCAGCACCCAGACCGTCGACCCGCTGACCATCGGTGGGGAGAAGACCTTCACCACCGCCGGCGAGGGCAAGGTGGAGATCAACTACCTGCGCGCCAACGACTACGTCAACGGCGCGAAGAAGGACCAGCTGACCGACGAGGACTACTACTGCCTCGTGGAGACCAAGGCCCCCGAGGGCTACAGCCTCCAGGCCGACCCGCTCCCCTTCCGGGTCCTGGCTGAGAAGGCCGAGAAGAAGGCCGCGACCGAGGTCACCGTCACCGACATCCCGAAGAACGCGGGCTTCCGCCTGCCGCTGACCGGTGCCAACGGCGTCATCTTCCTGACCGTTGCCGGCGCCCTGCTGGTGGCCGGTGGCGCGGTGGTCGCCTACGCCAACAAGCGCCGTCACGTTGCCAAGCACTGA","MHSLNTRRGLGLAAAMTLAAGALVAPTGAAAPADPNGSTIDPQAATTLTVHKCEQTDTNGVKEGTGNEDPQAECKPVSDVEFTITKLNVDLTTYDGWKTLADLKGNVFAAGDLKTDTVQKITTGADGLASFTDAQTEVGAYLVSETRTPDKVIPAEDFVVTLPMTNPERTSEWNYNVHVYPKNTLSGVDKQVTDKPAPGSGRDITYTITTSIPKVDYPGGARIKRYEVVDQLDKRIKKDALAPVVKIVGKKEVTLAETTDYTVITAEGTDHNWATIQLTEEGRRKASEERYNGTGETKLQVTLTAKFDANVNLEGDLSNTAGLIPNDSPNFTWDPSHPGTKVPGIPTTPVLSKYGKVVLTKTGTDQLADKTKYNGAQFQVYECTKTASGATLRDSDPSTQTVDPLTIGGEKTFTTAGEGKVEINYLRANDYVNGAKKDQLTDEDYYCLVETKAPEGYSLQADPLPFRVLAEKAEKKAATEVTVTDIPKNAGFRLPLTGANGVIFLTVAGALLVAGGAVVAYANKRRHVAKH$","Type-1 fimbrial major subunit precursor","Extracellular, Periplasm, Cellwall","type-1 fimbrial major subunit precursor","putative type 1 fimbrial protein","LPXTG-motif cell wall anchor domain","Li T, Johansson I, Hay DI, Strömberg N.Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins.Infect Immun. 1999 May;67(5):2053-9.PMID: 10225854Chen P, Cisar JO, Hess S, Ho JT, Leung KP.Amended Description of the Genes for Synthesis of Actinomyces naeslundii T14V Type 1 Fimbriae and Associated Adhesin.Infect Immun. 2007 Aug;75(8):4181-5.PMID: 17485454","Schneewind O., Jones K.F., Fischetti V.A. Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci. J. Bacteriol. 1990. 172(6):3310-3317. PMID: 2188957Fischetti V.A., Pancholi V., Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol. Microbiol. 1990. 4(9):1603-1605. PMID: 2287281","","","

InterPro
IPR001899
Domain

Surface protein from Gram-positive cocci, anchor region
PF00746	$\"[486-525]T$	Gram_pos_anchor
TIGR01167	$\"[493-527]T$	LPXTG_anchor: LPXTG-motif cell wall anchor
PS50847	$\"[494-531]T$	GRAM_POS_ANCHORING

noIPR
unintegrated

unintegrated
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[502-522]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 486 to 525 (E_value = 2.3e-09) place ANA_2510 in the Gram_pos_anchor family which is described as Gram positive anchor.","","fimbrial major subunit precursor","","1","","","","","","","","","","","","Thu Jul 26 15:17:51 2007","","","","Thu Jul 26 15:17:51 2007","","","","Thu Jul 26 15:17:51 2007","Thu Jul 26 15:17:51 2007","","","","","yes","","" "ANA_2511","2707289","2708812","1524","7.63","2.13","54704","TTGTGGGGGAGGCGGGAGAACCCGTCTCCCCCACACGGGCGTCGCAGGGATCCTCCCTGCCAATCGTTAAAGCCACAACTGATCCCCACCCGTCTTTCGCAGCGAGCTCCGCAGACAACCCGACGCAGGAAGGCACGGTTCTCCGTGACAGCGCTACTCCCATCACTTCGCGACCGCATCTCCCAGTCCCGCACCAGCCAGGCCCAGAGGGAGCCCGACTCCGCGGCCCCGCAGCCCGGCCCGGACGGCCCCGCCTCCCCGGCGACCGACCCGAAGAAGGCGGCCCGCCGCAAGATCCTGCGTGAGCGCTTCCTGACCTGGCTGCCGCTGGTCCTGGTCCTGGTCGGCGTCGCCGTCCTCCTGTACCCGGTCATGGCGACCCAGCACAACAACGACGAGCAGCAGCGCCTGGCCAAGATGTACACCGCCACCGTGAACTCGGCCGGACCGGAGACCATCGCCAAGGAGCGCGCCTCCGCCGAGACCTACAACAACAACCTGGAGAGCGCGCCGATCCTCGACCCCTGGCTCGAGTCGCAGCGCCCCGACACCCCCCAGTACCAGGCCTACCTCCACGAGATGGACATCGACCCGGTCATGGCCCGGATCGTCATCCCCTCCATCCACGTGAGCCTGCCCATCTATCACGGCACCGACAGCCGCACCCTGACGGAAGGCGTCGGGCACCTGTTCGGCACGAGCCTGCCGATCGGCGGCCCCTCCACCCACGCAGTCCTCACCGGCCACACCGGGCTGTCCACCGCGACCATGTTCGACAACCTCAACCAGCTCGAGAAGGGCGACGTCTTCTACGTCTCCTCCCTGGGGCAGACCCTCAAGTACGAGGTCAACGACATCACCGTCGTCAAGCCCGAGGAGACCGACTCCCTGCGCAAGGTCCCCGGACGCGACCTGGTCACCCTCATCACCTGCACGCCCTACGGCGTCAACTCCCACCGCCTCCTGGTCACCGGCGAGCGCGTCCCCATGGACCCCACGGCCGCCGCGGCCGAGGAGGCCAAGGCCCTGCCCGCCCCCATGCAGACCTGGATGAAGGCCATCATCGTGGCCGTCGTCATCATCCTGGCCGTCGTCGTCGGAATCCTCGTGCGCCTGTGGTGGACGCGCCGTCGTCGCTCCCGGGGTGCCGGCCGGCAGGCCGCCAAGGGCTCAGCCGCCCGCGAGGCAGGCCGCGGTGAGGTCCGCAGTGACGACGCGGCCGACGACGTCGGCGCGCCGGAGCGCTGGCCCGGACGCCCCCTGCAGGACGTCGTCGGCGCTGTCGGGGCCGCCGAGGCCGCCGGAGCGGATGCGCAGTTCACCGACGAGACCAGCGAGCTCGAGGTCATCAGCCCATCGGCCGCCGCAGGGCAGAGCGCCGGAAGCGACGCCTCCCAGGACCCGAAGGCCGCGCCCTCCGAGACGCAGGAACCGCGGACCGCCTCCCCCTACGGGCCGATCACCCCGGCCGCAGGGGGCCAGGGGGAGAACCCGTTCAGCGACCTGGAGGCACGCGAGTCGTGA","LWGRRENPSPPHGRRRDPPCQSLKPQLIPTRLSQRAPQTTRRRKARFSVTALLPSLRDRISQSRTSQAQREPDSAAPQPGPDGPASPATDPKKAARRKILRERFLTWLPLVLVLVGVAVLLYPVMATQHNNDEQQRLAKMYTATVNSAGPETIAKERASAETYNNNLESAPILDPWLESQRPDTPQYQAYLHEMDIDPVMARIVIPSIHVSLPIYHGTDSRTLTEGVGHLFGTSLPIGGPSTHAVLTGHTGLSTATMFDNLNQLEKGDVFYVSSLGQTLKYEVNDITVVKPEETDSLRKVPGRDLVTLITCTPYGVNSHRLLVTGERVPMDPTAAAAEEAKALPAPMQTWMKAIIVAVVIILAVVVGILVRLWWTRRRRSRGAGRQAAKGSAAREAGRGEVRSDDAADDVGAPERWPGRPLQDVVGAVGAAEAAGADAQFTDETSELEVISPSAAAGQSAGSDASQDPKAAPSETQEPRTASPYGPITPAAGGQGENPFSDLEARES$","Sortase","Membrane, Periplasm","sortase-like protein","putative fimbrial associated sortase-like protein","sortase family protein","Li T, Johansson I, Hay DI, Strömberg N.Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins.Infect Immun. 1999 May;67(5):2053-9.PMID: 10225854Chen P, Cisar JO, Hess S, Ho JT, Leung KP.Amended Description of the Genes for Synthesis of Actinomyces naeslundii T14V Type 1 Fimbriae and Associated Adhesin.Infect Immun. 2007 Aug;75(8):4181-5.PMID: 17485454","Barrett A.J., Rawlings N.D. Evolutionary lines of cysteine peptidases. Biol. Chem. 2001. 382(5):727-733. PMID: 11517925Mazmanian S.K., Liu G., Ton-That H., Schneewind O. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 1999. 285(5428):760-763. PMID: 10427003Mazmanian S.K., Ton-that H., Schneewind O. Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus. Mol. Microbiol. 2001. 40(5):1049-1057. PMID: 11401711Pallen M.J., Chaudhuri R.R., Henderson I.R. Genomic analysis of secretion systems. Curr Opin Microbiol 2003. 6(5):519-527. PMID: 14572546","","","

InterPro
IPR005754
Family

Peptidase C60, sortase A and B
PF04203	$\"[203-328]T$	Sortase
TIGR01076	$\"[201-336]T$	sortase_fam: sortase family protein

noIPR
unintegrated

unintegrated
G3DSA:2.40.260.10	$\"[189-333]T$	no description
tmhmm	$\"[104-124]?$ $\"[353-373]?$	transmembrane_regions

InterPro
IPR000326
Family

Phosphoesterase, PA-phosphatase related
PF01569	$\"[59-175]T$	PAP2
SM00014	$\"[57-167]T$	acidPPc

noIPR
unintegrated

unintegrated
PTHR14969	$\"[48-176]T$	SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE
signalp	$\"[1-46]?$	signal-peptide
tmhmm	$\"[31-51]?$ $\"[60-80]?$ $\"[99-119]?$ $\"[124-142]?$ $\"[152-172]?$ $\"[216-238]?$ $\"[252-272]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB000326 (PA-phosphatase related phosphoesterase) with a combined E-value of 7.4e-06. IPB000326A 98-105 IPB000326B 140-159","","","No significant hits to the PDB database (E-value < E-10).","Residues 59 to 175 (E_value = 3.7e-16) place ANA_2513 in the PAP2 family which is described as PAP2 superfamily.","","peptidase-like protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2514","2711787","2710036","1752","5.20","-23.08","61639","ATGAGCGCCGCTGAGCGCCCGCCGATGTCCCAGCAGCCGGCACCGCCCCGGCGGCGGATCAGCCTGAGCTCGTGGAGACCCGGCTCGCTGCTCACGCCTCCTCGCAGTCTGCGCACTCGGCTGGTGGTCGGGGTGCTCGGGCTGGTGCTGGTCATGGCGGCGGTCATGAGCGCCTTCTCCACCGTCAGCCTGCGCCACACGCTCATGGCGCGCACGGACAGCCAGCTGATGGCGGCTGCCCAGCGCGCCGCCGACAAGCGCCATGACCTGACGCAGGAGGCCAGGAAGGCCTCCGATGAGGCGGCCCAGGAGGGTGCGGACAAGCCGGGCGATCAGCCCGACGGGGCCGGCGGGGCCGACGGGGCCGACGGGGCCGGCGGGGCCGACGGGGCCGACGGCGGCCCCGGCAAGGAGGGGGTCCCTCCGGGCCTCGACGCCGCCGGGCAGTCGACCGGCACGCTGACGCTCATCACCACGCAGGCATCGTCCTCCGACACTGCGAGCAGTGAGACCGCCGCTTACATCGACAAGAACGGCCACTACGCGTCCATCTCCAAGGAGGACTGCCGGCTGCTGCTGTCCCAGGCCACGGAGGACCACCCCGTCACCGTGCACCTGCACCACCTGGGCAGCTACCGGGTGGTGGCTACCCGCGACGAGGCCTCGGGCAGCACGGTCATCACCGGGCTCTCCCTGGAGGGCGACAAGGGGCTCATCCGCACCCAGCTGCTCATCGAGCTGACGGTGGCCCTGCTGGGCGCCCTCGTGGTGGCCCTGGCCGGGCGGACCATGGTGCGCTCCTCGCTGGCGCCCCTGGAGCGGGTGGCCCGCACCGCGCAGCGCGTGGCCTCCCAGCCGCTGGAGCGCGGTGAGGTGAGCATCGAGGACCGCGTGGAGAAGGCGGACCTGGACTCCTCAGCGGAGGTCGGTCAGGTCGGCGGCGCCCTTAACACGCTGCTGGGGCACGTGGAGTCCGCCCTGACCGCGCGCCAGCGCTCGGAGACGCAGGTGCGCCAGTTCGTGGCCGACGCCTCTCACGAGCTGCGCACGCCGCTGGCCTCGATCCGCGGCTACACCGAGCTCATCCGCCGCGAGGGGGCCGACGCCGACCTGCCGGAGGAGGCCACCTACGCCCTGGAGCGCGTGCACTCCGAGTCGGTGCGAATGACGGCGCTCGTCGAGGACCTGCTGCTGCTGGCCCGCCTGGACGCCGGGCGCGAGCTGCGCCGAGAGGAGGTGGACCTGGTCGGCCTCCTGGTGGACACGGTGGCCGACGCCCGCGCGGCCGGCCCCGACCACGACTGGCAGCTGGATCTGGCCGTCCTGGAGCCGCCGGCCGACGCCACGCCGGAGGAGGCCGAGGACTTCCTGCCCGAGCCTCCGCTGGTCATCGGCGATGAGGCCCGCCTGCGCCAGGTCGTCGTCAACCTCCTGGCCAACGCCCGGGTGCACACGCCGGCCGGCAGCCACGTGACCACGACGCTGGCCCGAGAGGGGGACACGCTCATCGTGCGCATCCACGACGACGGCCCGGGGATCGCCCCCGAGGTGCGCGACCGCCTCTTTGAGCGCTTCGCCCGGGGGGACTCCTCACGTGAGCGGCGCACCGGCTCCACAGGTCTGGGCATGTCGATCGCTCTGGCCATCGTCCAGTCCCACGGCGGGAGCATCGACGTCGACTCCTCCACCGCGCCCGAGGACCACGGCACCACCTTCAGCGTCAGGCTCCCGGCCGCCGTCGTCGAGGAGTAG","MSAAERPPMSQQPAPPRRRISLSSWRPGSLLTPPRSLRTRLVVGVLGLVLVMAAVMSAFSTVSLRHTLMARTDSQLMAAAQRAADKRHDLTQEARKASDEAAQEGADKPGDQPDGAGGADGADGAGGADGADGGPGKEGVPPGLDAAGQSTGTLTLITTQASSSDTASSETAAYIDKNGHYASISKEDCRLLLSQATEDHPVTVHLHHLGSYRVVATRDEASGSTVITGLSLEGDKGLIRTQLLIELTVALLGALVVALAGRTMVRSSLAPLERVARTAQRVASQPLERGEVSIEDRVEKADLDSSAEVGQVGGALNTLLGHVESALTARQRSETQVRQFVADASHELRTPLASIRGYTELIRREGADADLPEEATYALERVHSESVRMTALVEDLLLLARLDAGRELRREEVDLVGLLVDTVADARAAGPDHDWQLDLAVLEPPADATPEEAEDFLPEPPLVIGDEARLRQVVVNLLANARVHTPAGSHVTTTLAREGDTLIVRIHDDGPGIAPEVRDRLFERFARGDSSRERRTGSTGLGMSIALAIVQSHGGSIDVDSSTAPEDHGTTFSVRLPAAVVEE$","Two-component system sensor kinase","Membrane, Cytoplasm","sensor histidine kinase","sensor histidine kinase","Histidine kinase","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[423-577]T$	no description
PF02518	$\"[465-579]T$	HATPase_c
SM00387	$\"[465-580]T$	HATPase_c

InterPro
IPR003660
Domain

Histidine kinase, HAMP region
PF00672	$\"[246-325]T$	HAMP
SM00304	$\"[266-328]T$	HAMP
PS50885	$\"[266-328]T$	HAMP

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[336-405]T$	HisKA
SM00388	$\"[336-405]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[502-516]T$ $\"[520-530]T$ $\"[537-555]T$ $\"[564-577]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[343-580]T$	HIS_KIN

noIPR
unintegrated

unintegrated
PTHR23283	$\"[29-162]T$ $\"[250-578]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23	$\"[29-162]T$ $\"[250-578]T$	SENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
tmhmm	$\"[41-61]?$	transmembrane_regions

","BeTs to 14 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB004358 (Bacterial sensor protein C-terminal signature) with a combined E-value of 3.8e-19. IPB004358A 502-516 IPB004358B 520-530 IPB004358C 537-555 IPB004358D 564-577***** IPB003661 (Histidine kinase A, N-terminal) with a combined E-value of 2.8e-17. IPB003661A 340-352 IPB003661B 506-525","","","-42% similar to PDB:2C2A STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN (E_value = 1.6E_15);-53% similar to PDB:1BXD NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ (E_value = 2.6E_10);","Residues 246 to 325 (E_value = 6.9e-08) place ANA_2514 in the HAMP family which is described as HAMP domain.Residues 336 to 405 (E_value = 3.2e-25) place ANA_2514 in the HisKA family which is described as His Kinase A (phosphoacceptor) domain.Residues 465 to 579 (E_value = 2e-42) place ANA_2514 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","histidine kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2515","2712472","2711774","699","5.23","-7.28","26250","TTGCGCGTCCTGGTCGTCGACGACGAGCAGATGCTCGCCGACCTGCTCGCCTCCGCCCTGCGTTACGAGGGCTGGGAGGTCACCACTGCCGGGACCGGGATCGCAGCCGTGCGCTCCGCCCAGGAGATCGACCCCGACGTCATCGTCCTGGACATCATGCTGCCCGATTTCGACGGCCTGGAGGTCATGCGCCGGGTGCGCGGCCACCGCCCGAACGTGCCGGTCCTGTTCCTGACGGCCAAGGACGCCGTCGAGGACCGGGTGGCCGGACTGACCGCCGGCGGCGACGACTACGTCACCAAGCCCTTCTCCCTGGAGGAGGTCGTGGCCCGGCTGCGTGCCCTGTTGCGGCGCTCCGGGGCCAGCGAGGAGAAGCAGGCCTCCCTGCTGGAGGTCGGGGACCTGCGCATGGACGAGGACTCCCACGAGGTCTGGCGCGGCGAGGACGAGATCCAGCTGACCGCCACCGAGTTCGAGCTGCTGCGCTACCTCATGCGCAACCCCCGCCGGGTCCTGTCCAAGCCGCAGATCCTGGACCGGGTGTGGAACTACGACTTCGGCGGGCAGGCCAATATCGTCGAGCTGTACATCTCCTACCTGCGCCGCAAGATCGACAAGGGCCGCGAGCCCATGATCCACACGATGCGCGGCGTCGGATACGTCCTCAAGCCGGCCGCCGGCACCGATGAGCGCCGCTGA","LRVLVVDDEQMLADLLASALRYEGWEVTTAGTGIAAVRSAQEIDPDVIVLDIMLPDFDGLEVMRRVRGHRPNVPVLFLTAKDAVEDRVAGLTAGGDDYVTKPFSLEEVVARLRALLRRSGASEEKQASLLEVGDLRMDEDSHEVWRGEDEIQLTATEFELLRYLMRNPRRVLSKPQILDRVWNYDFGGQANIVELYISYLRRKIDKGREPMIHTMRGVGYVLKPAAGTDERR$","Two-component system response regulator","Cytoplasm","DNA-binding response regulator","K02483 two-component system; OmpR family; response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[1-104]T$	Q7WSY5_PROFR_Q7WSY5;
PF00072	$\"[1-113]T$	Response_reg
SM00448	$\"[1-112]T$	REC
PS50110	$\"[2-116]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[134-220]T$	Q97SI5_STRPN_Q97SI5;
PF00486	$\"[148-222]T$	Trans_reg_C

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00217	$\"[88-113]?$	SUGAR_TRANSPORT_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[1-152]T$	no description
PTHR23283	$\"[2-118]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[2-118]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 1.1e-44. IPB001867A 46-59 IPB001867B 74-118 IPB001867C 212-222***** IPB000673 (CheB methylesterase) with a combined E-value of 9.1e-14. IPB000673B 18-71 IPB000673C 72-102***** IPB001789 (Response regulator receiver) with a combined E-value of 3.1e-11. IPB001789A 46-59 IPB001789B 94-104","","","-58% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 7.8E_43);-58% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 7.8E_43);-59% similar to PDB:1KGS Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima (E_value = 5.7E_38);-58% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 1.7E_37);-67% similar to PDB:1MVO Crystal structure of the PhoP receiver domain from Bacillus subtilis (E_value = 3.4E_22);","Residues 1 to 113 (E_value = 2.4e-39) place ANA_2515 in the Response_reg family which is described as Response regulator receiver domain.Residues 148 to 222 (E_value = 4.5e-21) place ANA_2515 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","response regulator","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2516","2712827","2714179","1353","5.01","-21.59","49381","ATGGAATACGTCGATGGCAACGAGCGCCGCTTCGGTGCCGAGGACCTGTTCTTCTCGACGACGGATACCAAGGGTGTCATTCGCAGGACCAACCGGGTCTTCGATTCGCTGTCCCGTCACAGCTCCGAGGAGCTCGTCGGCTCTCCGCACAACATTATTCGGCACGACGACATGCCCGCCGGGGCCTTCAAGCTCATGTGGGACGAGCTCGAGCAGGGGCGCTCCTCCTGCGTCTACGTGCTCAACCGGGCCAAGGACGGGCGGGACTACTGGGTCTTCGCCACGATCGCCCCGCTGGCCGACGGCTACCTGTCCGTACGCGTGCGTCCCACCAACCACGCCATGTTCACTCCCGTCAAGGAGATCTACGCCCGTGTGCGGGCCGCCGAGCGCGCCTACGCCGAGGAGGGTCACGGGCGCCGGGAGGTTGCCGAGCACGGGGCCGCGCTGCTGACCGAGGAGCTGGCGAAGCTTCAGTACCACGACCTGCACAACTTCGCCCGGGCCGCCCTCCCGCGGGAGCTGGCCCTGCTGGTCGTCGAGGGGGTGCGGGTGCCGCTCCGTGCCGAGTCGGACAATCCCATGTCCGCCGTTCTCCAGGCCGTCGCCGCCATCGAGCGGGACACCGACGAGCTCATCTACCAGCTCGGCGAGTACCAGGAGCTCATCAACGGCCTGGGCTCCTGGGCCGGCGGGGTGCGCTCGGTCATCGACCGGGCCGACCGCGTGGGCTCCCTCATGGGGGAGGTGACCAGCCCCGACGCCGAGTCCTCCGTTCCCAACGTCTCCGAGCGCGTCAAGGAGCGTGGGGCTCAGGCCGTCGAGGTGCTGCGCCAGCTCAACTCCTCCCTCGTGGCGCTCTACGAGGCGGCCTCCGAGGTGCGCTTCCGCAGCTCGATGATGCGTCTGCACACCCTCATGGCCGGCATCTTCGCCGCCGCCGTCCTGGACGGCCAGGAGGGGGAGTCCGCCGACGCTATCGGCGACCTCGCCGAGGCGATGCTCTCCGACCTGGAGGAGCTCGTGCCCTCCTGCCAGGAGGCGGCCAACCTGGCCGAGCGCCTGGAGGGCGACCTGCGCTCCGTGGTCAGCAACCTCGACCGCGTCAAGAGGCCCTTCCAGCGCTGGATCCGCGCTCTTCAGGACGAGGGGGCCCAGGCGCTCGTCGAGGGCGTCGACGCCGAGGCCGCCCTGAGTGAGGCCGTCGCCGTGGGTGAGCAGGGCTTCCCGGAGACGGCCTCGCTGGCCGAGCTGGCTGCCAAGGCCCGCGGCGTGGTCGTGACCTTGGACGAACCCGTCATCCGCCAGCGGGTGGCGACCGTCCGCGAGACCCTGAGTCACCTGGGGGAGTAA","MEYVDGNERRFGAEDLFFSTTDTKGVIRRTNRVFDSLSRHSSEELVGSPHNIIRHDDMPAGAFKLMWDELEQGRSSCVYVLNRAKDGRDYWVFATIAPLADGYLSVRVRPTNHAMFTPVKEIYARVRAAERAYAEEGHGRREVAEHGAALLTEELAKLQYHDLHNFARAALPRELALLVVEGVRVPLRAESDNPMSAVLQAVAAIERDTDELIYQLGEYQELINGLGSWAGGVRSVIDRADRVGSLMGEVTSPDAESSVPNVSERVKERGAQAVEVLRQLNSSLVALYEAASEVRFRSSMMRLHTLMAGIFAAAVLDGQEGESADAIGDLAEAMLSDLEELVPSCQEAANLAERLEGDLRSVVSNLDRVKRPFQRWIRALQDEGAQALVEGVDAEAALSEAVAVGEQGFPETASLAELAAKARGVVVTLDEPVIRQRVATVRETLSHLGE$","Signal-transduction sensor protein","Cytoplasm","probable sensory protein","putative signal-transduction sensor protein","PAS sensor protein","","Kerres A., Vietmeier-decker C., Ortiz J., Karig I., Beuter C., Hegemann J., Lechner J., Fleig U. The fission yeast kinetochore component Spc7 associates with the EB1 family member Mal3 and is required for kinetochore-spindle association. Mol. Biol. Cell 2004. 15(12):5255-5267. PMID: 15371542","","","

InterPro
IPR000014
Domain

PAS
TIGR00229	$\"[1-126]T$	sensory_box: PAS domain S-box

InterPro
IPR013253
Family

Kinetochore Spc7
SM00787	$\"[11-297]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.450.20	$\"[10-101]T$	no description

","BeTs to 8 clades of COG2202COG name: PAS/PAC domainFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG2202 is aom----qvdr-bcefg-s-uj-it-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","sensory protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2518","2714349","2715683","1335","6.48","-3.41","48396","ATGGAGTCGCAGGTCGGTTACGAGCGTTTGTTCGATCCGCAGGACATCTTCTTTTCCACCACGGATCTCAAAGGCGTCATTCAGAACACGAACCGGACGTTCGATACGTTATCGCGCTACTCGCGCGAGCGTCTCATCGGGGCTCCGCACAACATCATTCGTCACCTGGACATGCCGGCGGGTCTGTTCCGCCTCATCTGGGACGACCTGCAGACCCGGCGCCCCGCCTGCGGCTACATCACCAACCGTGCCGTGGACGGCCTGGACTACCGGGTCTTCGCCACCATCGTGCCGCTGCGCCAGGGCTTTCTGTCGGTGCGGATCAAGCCGATGGACATTGCGACTAGAGACCGGGTCGAGGAGGCCTACCGCCGGGTGCGCACCAAGGAGCGCGACCTTCAGGCCCGGGGCGCCTCGCGCCACCAGCTCGGTGAGTTCGGCGGCCGTGAGCTGGCCGCGGAGCTGGCGGCCCTGGGCTTCCCCTCCCTGCACGACATGACCCTGGTGACCCTGCCGCGTGAGGTGGCCGCCCTGGTCGCCGCCGGGGTGCGCGTCCCGGCGGCCGCCCCCGAGGGACTGGGTGCCGTGGCCCGGATCCTCAACGCGGTGGCCGCCATGGAGAAGGACACCGACGCCCTGGTCTTCGAGCTCGACGAGTACCTGCGCCTCATCACCACCATGGAGGCCACCCACGACTCGGCCCGGGCGGTGGAGGCGCGAGTGGGGCGCATCGGCCAGCTCGTCTCCCACGACGTCGGCGACAGCGCCCAGACCAAGGTGCTCATGCTCGGTGAGCGCATCGCCGAGCTCACCGGCGTCGCGGGCGCCGAGCTGCACGGGCTGCCCTCACGGCTCAAGGTCCTGCACCAGTCGGTCACCGAGCTGCGTTTCTCCGTGGCCCTCATGCGCCTGATCACCCTCATGGTGGGGCGCTTCGCCCAGTCCATCCTCGATGGCACTGAGGTGGACGCCGTGCACTCCCTGACGGACCTGTGCGAGGCGCTCGAGTCCGGCATCCGCGGCCTGGGCCCCGTGCTGCAGGCCGTGAGCACCCAGGTCGCCCAGCTTAACGACGCCCTGCACACCGTGACCTCCAGCCTGGACCGTGCGGCCCGGCGCCTGGGGCAGTGGGTGGACCTGCGTGGCGGCGGGGCCGGCTCCTCAGGCTCGCCGATCATCGACGAGGTCGCCCAGCTCACCTCCCGAGGCTTCCCCGAGGTCCGCTCCCTGGCCGAGCTGGCCGCCGAGTGCCGCGGACTGCACCTGCCCTACGACGAGAACATCGCCGCTCAGCGCCTGGCCGCTGTGCGCAGCGCCCTGGCCGAGCTCATCTGA","MESQVGYERLFDPQDIFFSTTDLKGVIQNTNRTFDTLSRYSRERLIGAPHNIIRHLDMPAGLFRLIWDDLQTRRPACGYITNRAVDGLDYRVFATIVPLRQGFLSVRIKPMDIATRDRVEEAYRRVRTKERDLQARGASRHQLGEFGGRELAAELAALGFPSLHDMTLVTLPREVAALVAAGVRVPAAAPEGLGAVARILNAVAAMEKDTDALVFELDEYLRLITTMEATHDSARAVEARVGRIGQLVSHDVGDSAQTKVLMLGERIAELTGVAGAELHGLPSRLKVLHQSVTELRFSVALMRLITLMVGRFAQSILDGTEVDAVHSLTDLCEALESGIRGLGPVLQAVSTQVAQLNDALHTVTSSLDRAARRLGQWVDLRGGGAGSSGSPIIDEVAQLTSRGFPEVRSLAELAAECRGLHLPYDENIAAQRLAAVRSALAELI$","PAS sensor protein","Cytoplasm","aerotaxis receptor Aer PA1561","hypothetical protein","PAS sensor protein","","Hefti M.H., Francoijs K.J., De vries S.C., Dixon R., Vervoort J. The PAS fold. Eur. J. Biochem. 2004. 271(6):1198-1208. PMID: 15009198Amezcua C.A., Harper S.M., Rutter J., Gardner K.H. Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation. Structure 2002. 10(10):1349-1361. PMID: 12377121Zhulin I.B., Taylor B.L., Dixon R. PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 1997. 22(9):331-333. PMID: 9301332","","","

InterPro
IPR000014
Domain

PAS
TIGR00229	$\"[1-123]T$	sensory_box: PAS domain S-box

noIPR
unintegrated

unintegrated
G3DSA:3.30.450.20	$\"[10-100]T$	no description

","BeTs to 7 clades of COG2202COG name: PAS/PAC domainFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG2202 is aom----qvdr-bcefg-s-uj-it-Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","receptor Aer PA1561","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2520","2715905","2718841","2937","8.59","6.57","106242","GTGTCCACCAAGCTCGTCATCGTGGAGTCCCCCAACAAGGTGCGCTCCATCGCCGGCTACCTGGGTCCGGAGTTCGACGTCGAGGCCTCCGTGGGGCACATTCGCGACCTGCCGCAGCCCTCCGAGCTGCCCGCCACCATGAAGAAGGGCCCCTACGGGAAGTTCGCGGTCGACGTCGAGGACGACTTCACCCCCTACTACGTCGTCAACCCTGACAAGAAGAAGACGGTCGCCCAACTCAAGAAGGCCCTCAAGGAGGCCGACGAGCTCTACCTGGCCACCGATGACGACCGCGAGGGCGAGGCCATCGCCTGGCACCTCCAGCAGGTCCTCAAGCCCAAGGTGCCGGTGCGCCGTATGGTCTTCACCGAGATCACCCGCGAGGCCGTCACCCGGGCCCTGGACAACACCCGCGAGCTGGACATCCACCTCGTCGACGCCCAGGAGACCCGACGCATCCTGGACCGCCTCGTGGGCTACGAGGTCAGCCCGGTCCTGTGGCGCAAGGTCCGCGCCGGCCTGTCCGCCGGGCGCGTGCAGTCAGTGGCCACCCGACTCGTCGTCGAGCGCGAGCGCGAGCGCATGGCCTTCCGCTCCGCCTCCTACTGGGGGGTGGAGGCCACCTTCTCCACCGTCCTGTCCGCCGTGGACGTCACCGCCCGCCAGGAGGCCTCCTTCACCGCCCGGCTCGTCACCCTCGACGGGCGGCGCGTGGCCACCGGGCGCGACTTCAACGACGACGGCCAGCTGCGCCCGGCCGCGCTCAAGGCCTCCGCCGTCCACCTCCACCAGGTGGGGGCCACCGCCGTGGCCGAGGCCATCGGCCGGGGAGAGCCGCGCGTGGTCGGCGTGGAGGACAAGCCCTACAAGCGCCGCCCGGCCGCCCCCTTCACCACCTCCACCCTCCAGCAGGAGGCCTCCCGCAAGCTGCGCATGAACCCGCGCGAGACCATGCGCGTGGCGCAGGGCCTCTACGAGAACGGCTTCATCACCTACATGCGTACCGACTCCACGGTCCTGTCCGGTCAGGCCGTGGCCGCAGCCCGCTCGCAGGTGGCCGAGCTCTACGGGGCCGAGTACGTCCCCGAGCGCCCCCGCGTCTACGCCTCCAAGTCCAAGGGCGCCCAGGAGGCCCACGAGGCGATCCGCCCCGCCGGCGACCACTTCCGCACCCCGGCCCAGGTCTCCGGTGAGCTCACCGGCGCCCAGTTCCGCCTCTACGAGCTCATCTGGAAGCGGACCGTGGCCTCCCAGATGGCCGACGCCGTCGGCTCGACCGCCACGGTCACCGTCGAGGTGCCGCTGACACCCGTGGCCGGCGAGTCGCGCGACTCCGGCCCCACCTTCTCCACGGCCGGCCTGACGGCGTCGGGCACCGTCATCACCTTCCGCGGCTTCCTGGCCGCCTACGAGGAGGGGCGCGACGCCGAGCGCTACCAGGACGACGCCGGAGCCGCCGCCAAGGACTCCAAGGACGTGCGCCTGCCCGCGATGATCGCCGGGCAGGAGCTGGCCGCCCTGGACGCCGAGGCCTCCGGCCACGAGACCACGCCGCCGCCGCGCTACACCGAGGCCTCCCTGGTCAAAGCCCTTGAGGAGCGCGAGATCGGCCGCCCCTCGACGTATGCGGCCACCATGTCCACCATCTCCGACCGCGGCTACGTCGACCACCGAGGCCAGGCCCTGGTGCCGACCTGGCTCGCCTTCGCCGTCACTCGGCTGCTGGAGGAGAACTTCGCCGAGCTCGTCGACTACGACTTCACCGCCTCCATGGAGCGCGACCTGGACCGGATCGCCGCCGGCGAGGAGGACCGGGTCGCCTGGCTGCGGCGCTTCTACAACGGGCAGGGTGGGGCCGGCACCGAGCAGGCCGTCCAGGCCGCCTCGAACGAGCTTGAGGCCGCGGCGGCTGCGCTGCGCGCCCAGGGGCTCAAGGGCCTGGTGGACAACCTCGGTGAGATCGATGCCCGCGCCGTCAACTCCATCGAGATCGGCGAGGGCATCACCCTGCGCGTGGGGCGCTACGGCCCCTACCTGGAGGACGCCGAGGGCAAGCGTGCCAACGTCCCGGCCGACCTCGCCCCCGACGAGCTGACCGTGGACAAGGCCCGCGAGCTCTTCACCCGCGCCGCCGACGACGGCCGCGAGCTCGGCGTCGACCCGGCCAGCGGGCACGTCATCATCGCCAAGGATGGCCGCTACGGCCCCTACGTCACCGAGGTCCTGCCCGAGCCGGAGGAGACGGCCGAGGCGGAGGCGACCAAGACTGCGAAGACGGCCAAATCGACGAAGGCGAAGAAGACCGCGAAGGCAGCCAAGCCCAAGCCCCGTACCGCCAGCCTCCTGCGCTCCATGGACCTGTCCACCGTGACCCTGGAGCAGGCCCTGGACCTGCTGAGCCTGCCGCGCGTCGTCGGCCAGGACCCGGAGTCGGGGGAGGACATCACCGCCCAGAACGGCCGCTACGGGCCCTACCTCAAGAAGGGCACGGACTCGCGCTCCCTGGAGACCGAAGAGCAGATCTTCACCGTCACCCTGGAGCAGGCCCTGGAGATCTTCGCCCAGCCCAAGCGGCGTCGAGGTCAGGCGGCCGCTCGTGGACCGCTGCGCGAGCTGGGGCAGGACCCGGCCACTGAGAAGCCGGTGGTCATCAAGGACGGTCGCTTCGGCCCCTACATCACTGACGGGCAGACCAACGTCACCGTGCCCCGCAGCGAGGACCCGGCCACCATCAGCGCCGAGCGGGCCTTCGAGCTGCTCGCGGACAAGCGCGCCAAGGGCCCGGCCAAGAAGCGCACCACCCGCAAGACCACCGCCAAGAAGACCACGACGAAGAAGACCACCACGAAGAAGGCCGCCACGAAGAAGGCCGCCGCCACTAAGAAGACCGCCGCCAAGACGGCGTCGAGCAAGGCGGCCGCCTCGAAGGAGGGCTGA","VSTKLVIVESPNKVRSIAGYLGPEFDVEASVGHIRDLPQPSELPATMKKGPYGKFAVDVEDDFTPYYVVNPDKKKTVAQLKKALKEADELYLATDDDREGEAIAWHLQQVLKPKVPVRRMVFTEITREAVTRALDNTRELDIHLVDAQETRRILDRLVGYEVSPVLWRKVRAGLSAGRVQSVATRLVVERERERMAFRSASYWGVEATFSTVLSAVDVTARQEASFTARLVTLDGRRVATGRDFNDDGQLRPAALKASAVHLHQVGATAVAEAIGRGEPRVVGVEDKPYKRRPAAPFTTSTLQQEASRKLRMNPRETMRVAQGLYENGFITYMRTDSTVLSGQAVAAARSQVAELYGAEYVPERPRVYASKSKGAQEAHEAIRPAGDHFRTPAQVSGELTGAQFRLYELIWKRTVASQMADAVGSTATVTVEVPLTPVAGESRDSGPTFSTAGLTASGTVITFRGFLAAYEEGRDAERYQDDAGAAAKDSKDVRLPAMIAGQELAALDAEASGHETTPPPRYTEASLVKALEEREIGRPSTYAATMSTISDRGYVDHRGQALVPTWLAFAVTRLLEENFAELVDYDFTASMERDLDRIAAGEEDRVAWLRRFYNGQGGAGTEQAVQAASNELEAAAAALRAQGLKGLVDNLGEIDARAVNSIEIGEGITLRVGRYGPYLEDAEGKRANVPADLAPDELTVDKARELFTRAADDGRELGVDPASGHVIIAKDGRYGPYVTEVLPEPEETAEAEATKTAKTAKSTKAKKTAKAAKPKPRTASLLRSMDLSTVTLEQALDLLSLPRVVGQDPESGEDITAQNGRYGPYLKKGTDSRSLETEEQIFTVTLEQALEIFAQPKRRRGQAAARGPLRELGQDPATEKPVVIKDGRFGPYITDGQTNVTVPRSEDPATISAERAFELLADKRAKGPAKKRTTRKTTAKKTTTKKTTTKKAATKKAAATKKTAAKTASSKAAASKEG$","DNA topoisomerase I","Cytoplasm","DNA topoisomerase I (Omega-protein) (Relaxingenzyme)(Untwisting enzyme) (Swivelase)","DNA topoisomerase I ","DNA topoisomerase I","","Podobnik M., Mcinerney P., O'Donnell M., Kuriyan J. A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases. J. Mol. Biol. 2000. 300(2):353-362. PMID: 10873470","","","

InterPro
IPR000380
Family

DNA topoisomerase, type IA
PR00417	$\"[90-103]T$ $\"[174-192]T$ $\"[327-336]T$ $\"[406-422]T$ $\"[535-549]T$	PRTPISMRASEI
PTHR11390	$\"[12-213]T$ $\"[249-738]T$	PROKARYOTIC DNA TOPOISOMERASE
PS00396	$\"[322-336]T$	TOPOISOMERASE_I_PROK

InterPro
IPR003601
Domain

DNA topoisomerase, type IA, domain 2
SM00436	$\"[116-204]T$	TOP1Bc

InterPro
IPR003602
Domain

DNA topoisomerase, type IA, DNA-binding
SM00437	$\"[285-572]T$	TOP1Ac

InterPro
IPR005733
Domain

DNA topoisomerase I, bacterial-type
TIGR01051	$\"[5-694]T$	topA_bact: DNA topoisomerase I

InterPro
IPR006154
Domain

Toprim subdomain
SM00493	$\"[3-116]T$	TOPRIM

InterPro
IPR006171
Domain

TOPRIM
PF01751	$\"[3-124]T$	Toprim

InterPro
IPR013497
Domain

DNA topoisomerase, type IA, central
PF01131	$\"[137-598]T$	Topoisom_bac

InterPro
IPR013824
Domain

DNA topoisomerase, type IA, central region, subdomain 1
G3DSA:1.10.460.10	$\"[147-207]T$ $\"[489-620]T$	no description

InterPro
IPR013826
Domain

DNA topoisomerase, type IA, central region, subdomain 3
G3DSA:1.10.290.10	$\"[293-420]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.140	$\"[1-146]T$	no description

","BeTs to 24 clades of COG0550COG name: Topoisomerase IAFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0550 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB013263 (Topoisomerase I, zinc-ribbon-like) with a combined E-value of 2.4e-117. IPB013263A 45-86 IPB013263B 87-133 IPB013263C 138-166 IPB013263D 167-208 IPB013263E 285-336 IPB013263F 337-369 IPB013263H 491-523 IPB013263I 524-551 IPB013263J 557-588 IPB013263K 589-616***** IPB000380 (DNA topoisomerase I) with a combined E-value of 6.8e-103. IPB000380A 19-41 IPB000380B 90-107 IPB000380C 119-127 IPB000380D 145-170 IPB000380E 174-205 IPB000380F 320-344 IPB000380G 373-385 IPB000380H 405-416 IPB000380I 519-555***** IPB009435 (Acid shock) with a combined E-value of 8.5e-06. IPB009435A 939-965 IPB009435A 944-970 IPB009435A 950-976 IPB009435A 940-966 IPB009435A 945-971 IPB009435A 934-960 IPB009435A 929-955 IPB009435A 949-975 IPB009435A 744-770 IPB009435B 949-978 IPB009435B 945-974 IPB009435B 944-973 IPB009435B 939-968 IPB009435B 929-958 IPB009435B 746-775 IPB009435B 924-953 IPB009435B 744-773 IPB009435B 934-963 IPB009435B 950-978 IPB009435B 940-969 IPB009435B 743-772 IPB009435B 749-778","","","-56% similar to PDB:1CY0 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3'-5'-ADENOSINE DIPHOSPHATE (E_value = 2.1E_108);-56% similar to PDB:1CY1 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPT (E_value = 2.1E_108);-56% similar to PDB:1CY2 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH TPTPTP3' (E_value = 2.1E_108);-56% similar to PDB:1CY4 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'pTpTpTp3' (E_value = 2.1E_108);-56% similar to PDB:1CY6 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3' THYMIDINE MONOPHOSPHATE (E_value = 2.1E_108);","Residues 3 to 124 (E_value = 1.7e-34) place ANA_2520 in the Toprim family which is described as Toprim domain.Residues 137 to 598 (E_value = 2.8e-167) place ANA_2520 in the Topoisom_bac family which is described as DNA topoisomerase.","","topoisomerase I (Omega-protein) (Relaxing enzyme)(Untwisting enzyme) (Swivelase) (omega-protein)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2521","2719237","2719854","618","4.46","-15.34","20523","ATGCATCTGCCCAAGATCGCTCTCGCCGGTACCGCCGCTCTGGCCCTGTCCCTGACCCTGGGCGCCTGCTCCTTGTCCGTCAACGGCTCCGGCTCCGGGGACTCCGGCACGCCGGCCACCCAGTCCGAGCAGAAGGACTCGCAGAGCGCCGACTCCAAGGATGCGTCCAAGGCTGATGCCAAGGGGGCCGCGACGGCCGACTCCCAGTCCTCCTCCGGTGGCTCGGCCCAGGCCTCCACGGCCCCCAGCAACAAGGCCGGGGACACGGATGACGACAAGGACGGCGACGACGCCCCCATCACGGACCCCACCTGGAAGGACATCCAGAGCACCGGTCAGCGCACCGAGGTCTCCGGTACCTATACCGTCCAGGGAGCCGGAACGACCCTCAACCTGGTCGGCGACCTCGACACGCTGGCGGTTCAGGGCTCTGACGTCAAGGTTGCCGCGGAGGATGTCGACACCCTCACCGTTCAGGGCTCCAACGTCACCGTCTACGCCCGCGACATCGACCACCTGACCATCCAGGGCTCCAACGTCACCGTCCACTGGCTGGGCGACGACCCGACGATCCAGGACCTCGGCGCCGGCAACACCACCGGGAAGCTCTCCCAGTGA","MHLPKIALAGTAALALSLTLGACSLSVNGSGSGDSGTPATQSEQKDSQSADSKDASKADAKGAATADSQSSSGGSAQASTAPSNKAGDTDDDKDGDDAPITDPTWKDIQSTGQRTEVSGTYTVQGAGTTLNLVGDLDTLAVQGSDVKVAAEDVDTLTVQGSNVTVYARDIDHLTIQGSNVTVHWLGDDPTIQDLGAGNTTGKLSQ$","Hypothetical protein","Extracellular, Periplasm","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-39% similar to PDB:1Y8Q SUMO E1 ACTIVATING ENZYME SAE1-SAE2-MG-ATP COMPLEX (E_value = );-39% similar to PDB:1Y8R SUMO E1 ACTIVATING ENZYME SAE1-SAE2-SUMO1-MG-ATP COMPLEX (E_value = );-49% similar to PDB:1NYO Solution structure of the antigenic TB protein MPT70/MPB70 (E_value = );","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2522","2719862","2720590","729","7.07","0.18","26625","GTGACCCATCCCGCCGCACCGGTTCCGTCCGCCACCGTCCTGCTCGTCGACGACGAGGCCCCCATCCGCCGCTCCCTGGGCCCTTACCTGGAGCGCGGCGGGTACCGGGTGCTGCTCGCCTCGGACGGGATGGAGGCCCTGGACATCCTGGCCTCCTACCAGGTGGACATCATCGTCTCCGACGTCCTCATGCCCAGGATGGATGGGCGCGAGCTGGTGCGGCGGGTCAGGGCCGGTGGGGCCTGGACCCCCATCATCCTGCTCACCCAGGTGGACGCCTCCTATGAGCGGGTCTCGGCCCTCGACGACGGCGCTGACGACTACCTGTCCAAGCCCTTCGACCCCGCCGAGCTCGCCTCCCGGATCCGCGCGGTGCTGCGCCGTACCCGCGGCGTGGCCCAGCCGCTGACCTCCGCCGCCCGGCTCACGGCCGGACAGCTCATCCTGGAGCGGACCTCGCGGCGAGTGACCCTGTCGGGACGCGAGGTGACGCTCACCCCGAAGGCCACGATGCTCCTGGACTACCTCATGAGCCATCCCGGCGAGCTCCACACCCGGGACGCCCTGCTGGCCTCCCTGTGGGGCATCGACTTCGCCACCTCCACGCGCGCCGTCGACCACCGCATCCGCGAGATCCGCCAGGCTCTGGGCGACGACGCCACCCACCCCACCTACATCGAGACGGTCCCCTCCGTCGGCTACCGCTTCCGGGCCGAGGTCCGGGCATGA","VTHPAAPVPSATVLLVDDEAPIRRSLGPYLERGGYRVLLASDGMEALDILASYQVDIIVSDVLMPRMDGRELVRRVRAGGAWTPIILLTQVDASYERVSALDDGADDYLSKPFDPAELASRIRAVLRRTRGVAQPLTSAARLTAGQLILERTSRRVTLSGREVTLTPKATMLLDYLMSHPGELHTRDALLASLWGIDFATSTRAVDHRIREIRQALGDDATHPTYIETVPSVGYRFRAEVRA$","Two-component system response regulator","Cytoplasm","MYCOBACTERIAL PERSISTENCE REGULATOR MRPA (TWOCOMPONENT RESPONSE TRANSCRIPTIONAL REGULATORY PROTEIN)","DNA-binding response regulator","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[13-127]T$	Q84BX0_BBBBB_Q84BX0;
PF00072	$\"[11-123]T$	Response_reg
SM00448	$\"[11-122]T$	REC
PS50110	$\"[12-126]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[142-236]T$	Q8G780_BIFLO_Q8G780;
PF00486	$\"[160-236]T$	Trans_reg_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[8-162]T$	no description
PTHR23283	$\"[12-130]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[12-130]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is 11","***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 6.4e-30. IPB001867A 56-69 IPB001867B 84-128 IPB001867C 226-236***** IPB001789 (Response regulator receiver) with a combined E-value of 2e-13. IPB001789A 56-69 IPB001789B 104-114***** IPB000673 (CheB methylesterase) with a combined E-value of 2.2e-11. IPB000673B 28-81 IPB000673C 82-112","","","-54% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 1.2E_30);-54% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 1.2E_30);-55% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 1.2E_30);-54% similar to PDB:1KGS Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima (E_value = 4.4E_28);-68% similar to PDB:1MVO Crystal structure of the PhoP receiver domain from Bacillus subtilis (E_value = 5.6E_23);","Residues 11 to 123 (E_value = 1.6e-35) place ANA_2522 in the Response_reg family which is described as Response regulator receiver domain.Residues 160 to 236 (E_value = 6e-18) place ANA_2522 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","PERSISTENCE REGULATOR MRPA (TWO COMPONENT RESPONSE TRANSCRIPTIONAL REGULATORY PROTEIN)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2523","2720707","2721843","1137","6.45","-2.32","39601","ATGCCGGTCACCTGGCCCACAGAGCAGGCTGGGCAGCCGACGCAGACTGAGCAGTCCGGACAGCCGGTCGCCCACCCGCTGGCCGGCCAGCCGGCGAACCCGCCGCAGCCGGCGGTCGAGCCACGCCCCGCCGAGCCCTCGGCCGGGGTCGTTGCCGAAGCCGTCGCCGAAGCCGCCCCGGCACCTCTAGACCCCACGACGGAGACGCCCCGGCGGGCCGGCTGGATCGGATGGGTGCTGGCGGCGGCGGTCGTGGCCGTCGCGGCGGCGGCCTCCTATGCGGCTTTCGGACTGGTCCCGGTGGTCATCTCCACGGCAGTGCCGCTGGCGGTGGCGCAGACCGGGATCGTGCTGCTGCTGCTCGCCCTGGCAGTGGCTGTGATCCGCCGCAGGCTGCGTCTGGCCGAGCAGCGGGGGCGACGTCAGGCCCAGGAGGAGGCGTGGTCTCGTCACCAGCAGTTCCTGCGCCGGCTGGACCACGAGCTGAAGAACCCGCTGACGGCGGTGCGGGCTGCCGTCGCCGACCTGCCGCAGGCCCCGCCCCACGAGCTGCAGGCCCGGGTCGACGTCGTCGACGCTCAGGCCCGCCGCATGGGGCGCTTGGTGACGGACCTGCGCAAGCTGGCCGACCTGGAGACGGCCGCGCTCTCACTGGAGGACGTCGATATCGCCGAGACCGTCCACGACGCCGCCCAGGCGGTCGGCGAGGAGGGGGCGGCGCGTGGCGGCGGGCCCAAGATCCGTCTGGATCTGCCGCAGGTGCCATGGCCGTTGTCGCATGTGCGCGGCGACGGCGACCTGCTGTACTCGGCCGTCTACAACGTCATCTCCAACGCCTCCAAGTACACCCAGCCCGGCGGGACCGTGGAGGTGCGCGGTCGGGAGGAGTCGGGCACTGTCACCATCGAGGTGGCCGACACCGGGATCGGGGTGCCGCAGGCCGACCTGCCGGCCGTGTGGAGCGAGCTGGCCCGGGCCGGCAACGCCCGGGGCCTGCCGGGCTCGGGTCTGGGGCTGGCGCTGGTGTCCACGATCGTGCGCCGCCACGGCGGCAGCGTGCGCATGGCCTCCCGGGAGGGCGTGGGCACCCGGGTGTGGCTGAGCCTGCCCGTCGCGGGCCCAGCGGAGACGCCGTGA","MPVTWPTEQAGQPTQTEQSGQPVAHPLAGQPANPPQPAVEPRPAEPSAGVVAEAVAEAAPAPLDPTTETPRRAGWIGWVLAAAVVAVAAAASYAAFGLVPVVISTAVPLAVAQTGIVLLLLALAVAVIRRRLRLAEQRGRRQAQEEAWSRHQQFLRRLDHELKNPLTAVRAAVADLPQAPPHELQARVDVVDAQARRMGRLVTDLRKLADLETAALSLEDVDIAETVHDAAQAVGEEGAARGGGPKIRLDLPQVPWPLSHVRGDGDLLYSAVYNVISNASKYTQPGGTVEVRGREESGTVTIEVADTGIGVPQADLPAVWSELARAGNARGLPGSGLGLALVSTIVRRHGGSVRMASREGVGTRVWLSLPVAGPAETP$","Two-component system sensor kinase","Membrane, Cytoplasm","sensor histidine kinase","two-component sensor histidine kinase","ATP-binding region, ATPase domain protein domain protein","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[217-372]T$	no description
PF02518	$\"[263-372]T$	HATPase_c
SM00387	$\"[263-373]T$	HATPase_c

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[150-214]T$	HisKA
SM00388	$\"[150-214]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[300-314]T$ $\"[333-351]T$ $\"[357-370]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[157-373]T$	HIS_KIN

noIPR
unintegrated

unintegrated
PTHR23283	$\"[67-78]T$ $\"[140-371]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF34	$\"[67-78]T$ $\"[140-371]T$	TWO COMPONENT SENSOR HISTIDINE KINASE (PHOR)
signalp	$\"[1-90]?$	signal-peptide
tmhmm	$\"[76-96]?$ $\"[106-128]?$	transmembrane_regions

","BeTs to 16 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB004358 (Bacterial sensor protein C-terminal signature) with a combined E-value of 2e-17. IPB004358A 300-314 IPB004358C 333-351 IPB004358D 357-370***** IPB003660 (Histidine kinase, HAMP region) with a combined E-value of 4.6e-06. IPB003660C 336-354","","","-47% similar to PDB:2C2A STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN (E_value = 3.0E_14);","Residues 150 to 214 (E_value = 4.9e-07) place ANA_2523 in the HisKA family which is described as His Kinase A (phosphoacceptor) domain.Residues 263 to 372 (E_value = 3.8e-34) place ANA_2523 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","histidine kinase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2525","2721963","2723273","1311","4.70","-16.38","42877","ATGACAAAAGCACACATCTCCCTGCCCTCCCTCGCCCTCATCACCACCCTCGCGCTGAGCGGCTGCTCCCTGTCCATCGGAGGCGGCTCGTCCTCACAGGCTCAGGGGCAGCAGACCCAGGCCAGTCAGGCCGGCTCGGACTCCGCCGGTTCCGCGGGAAGCGCCCAGGGCGCCGCCTCCGCCTCGGCGTCGGGAACGGCCGCCTCCGCGGGACAGGCCGTCGCCGGCTACGAACCCGGACAGATCCCCCCGATCCCCATGATCTCCCTGCCCGATCTCAGCCTGCTCACCCAGTCCACGGGCGCCTTCACCCCGGACCTCACGCGCTCCATCACCTCCCAGCCCGGCATCACGGTCAGGCCCGCCCGCTGCGATGCGAGCGGATCGCTCGTCTCCGGCTCCACGGTCTTGGGCGGGGACGGTTCGCTGACCACGAGCTCAGGCGCCACGGCGGTCACCAACAATGGTGATGGTTCGGGCACCTTCAGTGACGGGAAGGTCTCCATCACCAACAACGGGGACGGCTCAGGCACTTACTCCGACGGCAAGGTCTCCATCACGATCAATGGTGATGGCTCGGGCACTTACAGCGACGACCACCTCTCCGTCACCGTCAATGGTGACGGCTCGGGCACCTACAGCGACTCCGCCACGGGGGAGGCCATCACCCTCGACGGCAAGGGCTCGGGCACCTACAGCGACTCCGCCACGGGGGAGGCCATCACCCTCGACGGCAAGGGCTCGGGCACCTACAGCCGCGGCGGGGTCTCCATCACCAACAACGGTGACGGCTCGGGCAGCTACAGCGACGGCACGATCTCCATCACCAACCTCGGCGACGGCAGCGCCGTCGTCAACGACGCCACGGTCTCGGCCAAGCCCGTCCCCAAGGCCGGCAAGGTCGGCACCTTCCCCTCCATCGACGCCGCCAAGCCCGTGCAGTCCTGCGGCACCGTCATCACCCTGGAGGACAGCGTCCTGTTCGACTTCGGCTCATCCGACCTGCGTGGCGAGGCCTCGACCACGCTCACCAACCTGGCTACCGTCATCAAGGACTCCAAGGCCCCCAAGGTTCAGGTTCAGGGCCACACCGATTCCGTCTCCGACGACGCCTTCAACCAGAAGCTCTCCGAGCAGCGGGCGCAGGCCGTCTCAAGCGCCCTGAAGTCCAACGGCGTCACCGCTGATCTGGAGGCCGTCGGCTACGGCGAGACCAAGCCGGTGGCTCCCAACGAGAACCCCGACGGCTCCGACAATCCCGGCGGCCGCCGCCTCAATCGCCGCGTCGAGGTCTTCGTCCCGGCTTTCTGA","MTKAHISLPSLALITTLALSGCSLSIGGGSSSQAQGQQTQASQAGSDSAGSAGSAQGAASASASGTAASAGQAVAGYEPGQIPPIPMISLPDLSLLTQSTGAFTPDLTRSITSQPGITVRPARCDASGSLVSGSTVLGGDGSLTTSSGATAVTNNGDGSGTFSDGKVSITNNGDGSGTYSDGKVSITINGDGSGTYSDDHLSVTVNGDGSGTYSDSATGEAITLDGKGSGTYSDSATGEAITLDGKGSGTYSRGGVSITNNGDGSGSYSDGTISITNLGDGSAVVNDATVSAKPVPKAGKVGTFPSIDAAKPVQSCGTVITLEDSVLFDFGSSDLRGEASTTLTNLATVIKDSKAPKVQVQGHTDSVSDDAFNQKLSEQRAQAVSSALKSNGVTADLEAVGYGETKPVAPNENPDGSDNPGGRRLNRRVEVFVPAF$","Outer membrane porin F","Extracellular, Cellwall","Outer membrane porin F","K03286 OmpA-OmpF porin; OOP family","OmpA/MotB domain protein","","Freudl R., Klose M., Henning U. Export and sorting of the Escherichia coli outer membrane protein OmpA. J. Bioenerg. Biomembr. 1990. 22(3):441-449. PMID: 2202726Bouveret E., Benedetti H., Rigal A., Loret E., Lazdunski C. In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J. Bacteriol. 1999. 181(20):6306-6311. PMID: 10515919De Mot R., Proost P., Van Damme J., Vanderleyden J. Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. aeruginosa and P. syringae. Mol. Gen. Genet. 1992. 231(3):489-493. PMID: 1538702","","","

InterPro
IPR006664
Domain

Bacterial outer membrane protein
PR01021	$\"[328-350]T$ $\"[358-373]T$ $\"[373-389]T$	OMPADOMAIN

InterPro
IPR006665
Domain

OmpA/MotB
PD000930	$\"[319-383]T$	Q7NJK4_GLOVI_Q7NJK4;
PF00691	$\"[327-421]T$	OmpA
PS51123	$\"[315-436]T$	OMPA_2

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.60	$\"[310-433]T$	no description
PS51257	$\"[1-22]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[10-30]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PS51257	$\"[1-29]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

InterPro
IPR000524
Domain

Bacterial regulatory protein GntR, HTH
PF00392	$\"[15-78]T$	GntR
SM00345	$\"[19-78]T$	HTH_GNTR
PS50949	$\"[13-81]T$	HTH_GNTR

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[8-78]T$	no description

","BeTs to 5 clades of COG1725COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1725 is ---p----v-rlbc------------Number of proteins in this genome belonging to this COG is 1","***** IPB000524 (Bacterial regulatory protein, GntR family) with a combined E-value of 4.4e-13. IPB000524 38-78***** IPB011663 (UbiC transcription regulator-associated) with a combined E-value of 3.7e-10. IPB011663 38-78","","","No significant hits to the PDB database (E-value < E-10).","Residues 15 to 78 (E_value = 6.5e-14) place ANA_2527 in the GntR family which is described as Bacterial regulatory proteins, gntR family.","","regulator, gntR family (MOCR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2528","2724677","2725504","828","5.37","-9.09","29732","GTGAACCCCGTCGAGATCTCCCACCTGACCAAGCACTACCCGGACTTCAGTCTCAACGATGTCACCTTCTCCGTCCCCGCCGGCTACGTGACGGGCTTCGTCGGGGCCAACGGCTCGGGGAAGACCACCACGATCAAGGCCGCCCTGGGCATGATCCACCCCGATTCCGGCTCGGCCACCACTGTGGGACACGAGCGCATCGGCGTCGTCTTCGACGCCCCGCCCTACAACCCCGAATGGCGCCTGAAGGACCTGGGCCGCGGCATCGGGCGTTTCTTCCCCACCTGGTCCCAGGAGCGCTACGACGCCGAGCTCCAGGCCGCGGGCTTGGCCCCCACTAAGAAGGTCAAGGAGCTCAGCCGAGGCATGGGCATGCGCCTGCAGATGGCGGTGGCCCTGGCTCACGATCCCGAGCTGCTCATCCTCGATGAGCCCACCGGCGGGCTGGACCCCTTGGCCCGCAGCGAGATGGTGGACATGGTCGCCCAGTTCATGGTGGAGGAGGGCCGCACCATCCTGTTCTCCACCCACATCACCTCCGACCTCGATCGGCTGGCCGACTACCTGGTCATCCTCAGTCGGGGCAGGGTCGTGGCCAACGGCACGGCTGAGGAGATCCTCGGCTCCTTCCGGCTTGTGCGCGGCACCCCTGAGCACCTGACCGACGCCGTGCGCCAGGCCGGCCTCGGGCTGCGCAGCACGTCGCTGGGCTGGGAGGCCATGATGCCGGCCGACGCCGCTGAGGTGCTGGCCGACCGCGTCGTCGTCGAGACCCCCACCATTGAGGACCTCGCCGTGCACATCGCCAAGGAGGCGGGCCGTGAATGA","VNPVEISHLTKHYPDFSLNDVTFSVPAGYVTGFVGANGSGKTTTIKAALGMIHPDSGSATTVGHERIGVVFDAPPYNPEWRLKDLGRGIGRFFPTWSQERYDAELQAAGLAPTKKVKELSRGMGMRLQMAVALAHDPELLILDEPTGGLDPLARSEMVDMVAQFMVEEGRTILFSTHITSDLDRLADYLVILSRGRVVANGTAEEILGSFRLVRGTPEHLTDAVRQAGLGLRSTSLGWEAMMPADAAEVLADRVVVETPTIEDLAVHIAKEAGRE$","ABC-type multidrug transport system, ATPase component","Cytoplasm, Membrane","ABC transporter ATP-binding protein","K01990 ABC-2 type transport system ATP-binding protein","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[119-161]T$	Q8G5H2_BIFLO_Q8G5H2;
PF00005	$\"[28-195]T$	ABC_tran
PS50893	$\"[1-219]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[27-196]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-217]T$	no description
PTHR19222	$\"[4-226]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16	$\"[4-226]T$	ABC TRANSPORTER

","BeTs to 19 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: RThe phylogenetic pattern of COG1131 is AmTKy-VCEBR-uJ-pol--xNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-50% similar to PDB:1VPL Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga maritima at 2.10 A resolution (E_value = 3.6E_19);-43% similar to PDB:1Z47 Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius (E_value = 7.8E_14);-44% similar to PDB:1B0U ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM (E_value = 3.8E_13);-44% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 4.3E_12);-44% similar to PDB:2FF7 The ABC-ATPase of the ABC-transporter HlyB in the ADP bound state (E_value = 4.3E_12);","Residues 178 to 345 (E_value = 2.9e-31) place ANA_2528 in the ABC_tran family which is described as ABC transporter.","","transporter ATP-binding protein","","1","","","Thu Aug 9 12:42:45 2007","","Thu Aug 9 12:42:45 2007","","","Thu Aug 9 12:42:45 2007","Thu Aug 9 12:42:45 2007","Thu Aug 9 12:42:45 2007","Tue Aug 14 17:21:51 2007","","Thu Aug 9 12:42:45 2007","","","Thu Aug 9 12:42:45 2007","Thu Aug 9 12:42:45 2007","","","Thu Aug 9 12:42:45 2007","Thu Aug 9 12:42:45 2007","","","","","yes","","" "ANA_2529","2725509","2726210","702","10.82","8.60","23823","ATGACCACGGATCGACGCGAGCACCCCGCCGAGGCGGCCGCAGTGGCCAAGATGCCGGCCGGCGTGACGATGAGGGGTGCCGCGGGCGGGCCCGGACGGGTCGGTCGGCTGCTCTTGCTGGTGCGGTTGCACCTCCTGGGCCTGCGGGGTCCTCTGCCCTCCCTCCTCGGCCTTCTCCTCATTGTCGGCGCCGCCGGCATCGTCTCCGGCAGTATCGCCCCGGTCAGTGGATTCCTCGCGGGGACCGCCCTGGTCGGGGGCCTCTCGGGAGTGATGGCCGAGCACTCCGACATCAACCGTCTGCTGGCCTCCCTGCCCGTCTCCCGGGCCGACGTCGTCAACTCCTACTGGGCGCTCGCGATGCTGCATCTTCTGGCCGCTTCGGCCCTCTATGCGGCCATAGGCCTCCCTCTGGGCGTACACCCGTGGCGGCTGCTCGTCCTTCCTCTCGTCCTCATCGTGGGGCAGGCCCTGGGAATTCCCGTGTTCCTGCACTTCAGGCGTGGGCTCGGTCTGCTCGTCTGGACGGTTTCGATTCTCGCCATCGGGGCGCTGGGCCTGCTGGTATCCAGCGTCGGGCCGATCCGGGACCTCCCTGCGGGGACGACGACGGGAGGCGGCCTGCTCCTGGCCCTGGGGGCCGGCGCCCTCATCGGCCTGTGGGTGTTGAGCCACTACCTCTACCTCAAGCAGGACCAGTGA","MTTDRREHPAEAAAVAKMPAGVTMRGAAGGPGRVGRLLLLVRLHLLGLRGPLPSLLGLLLIVGAAGIVSGSIAPVSGFLAGTALVGGLSGVMAEHSDINRLLASLPVSRADVVNSYWALAMLHLLAASALYAAIGLPLGVHPWRLLVLPLVLIVGQALGIPVFLHFRRGLGLLVWTVSILAIGALGLLVSSVGPIRDLPAGTTTGGGLLLALGAGALIGLWVLSHYLYLKQDQ$","Hypothetical protein","Membrane, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-66]?$	signal-peptide
tmhmm	$\"[45-65]?$ $\"[71-91]?$ $\"[112-134]?$ $\"[144-164]?$ $\"[169-189]?$ $\"[208-228]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-50% similar to PDB:1MT3 Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1 (E_value = );-50% similar to PDB:1MTZ Crystal Structure of the Tricorn Interacting Factor F1 (E_value = );-50% similar to PDB:1MU0 Crystal Structure of the Tricorn Interacting Factor F1 Complex with PCK (E_value = );-50% similar to PDB:1XQV Crystal structure of inactive F1-mutant G37A (E_value = );-50% similar to PDB:1XQW Crystal structure of F1-mutant S105A complex with PHE-LEU (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2530","2726219","2726932","714","6.74","-0.52","24016","ATGATGGAGACGACGACGGGGGTGGCGCCGGATGGCAGCCGGGGCAGCGGAGCGGCCGCGGCGACTGGGCCGGCCGGCCCTGAGGGCAGCGGCGAGACGGCGCTCGCCGGGGTGGGGGCGGTGCTGCGACTCGACCTCATCGTGCTGCGCCGGCGTGGTCCACTGCTCTTCCTGCCCTTGGCGCTGGCGCTGTTCATCGCCATGGACGTCCTGGCCGGCCGTCTGCAGACGACGGTGATGGCGGGGGTCGCCCTGGGACTGTGCGCCCAGTACGCCCAGGGGGCCGTCGAGTCCGCTCACCACATGGAGCGCCTCTATGGGGCACTGCCGCTGCGGCGTAGCGAGCTGGTCGGTGCCCGCTGGGTCGAGGGGGTCGCCCTGGCGCTCCTCTCCGGCCTGGTCTGCGTGCTGGTGGCCGCTCTCACCGGTGACTGGGGCGGCCTCATGGCCGGCCTGCTCGTCATCTGCCTGTCCGCGGCCCTCGGGCTGCCCCTGTTCCTATGCCTGGCCCCCGAGCGGGCCCTGTGGGTGTGGGGGCTGTGCCTGGGGGTGGGAGCTGGCGCCCTTTACAGCGCTATTCCGCTGCTGGCAGGACCCGTGGCCGAGGTGCTGCGCGAGCCGGCACCCGCCGCCCTGGCGGCCCTGGCCTGCCCCGCCCTCCTGGGCGCCTCCCTGGTGGTGGCCCTCCGCTGGTACGGGCGCCAGGACCACTGA","MMETTTGVAPDGSRGSGAAAATGPAGPEGSGETALAGVGAVLRLDLIVLRRRGPLLFLPLALALFIAMDVLAGRLQTTVMAGVALGLCAQYAQGAVESAHHMERLYGALPLRRSELVGARWVEGVALALLSGLVCVLVAALTGDWGGLMAGLLVICLSAALGLPLFLCLAPERALWVWGLCLGVGAGALYSAIPLLAGPVAEVLREPAPAALAALACPALLGASLVVALRWYGRQDH$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[53-73]?$ $\"[121-141]?$ $\"[147-165]?$ $\"[174-194]?$ $\"[208-228]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-42% similar to PDB:1FX8 CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITH SUBSTRATE GLYCEROL (E_value = );-42% similar to PDB:1LDA CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITHOUT SUBSTRATE GLYCEROL (E_value = );-42% similar to PDB:1LDI CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITHOUT SUBSTRATE GLYCEROL (E_value = );-42% similar to PDB:1LDF CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) MUTATION W48F, F200T (E_value = );-50% similar to PDB:1YBE Crystal Structure of a Nicotinate phosphoribosyltransferase (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2532","2726976","2727794","819","8.29","3.94","28351","ATGCCCGAGTCCGTGCCCACGTCCGAGTCCGTTGTGTCCGCTGCGCGGACCGTACCCACTCTGCCCACTGCCGCCGAGTCCTGCGGCACTCAGGTTCCCAGTGCGCCTGCGGCGGTGCGGGGGCCAGGTGCCCTGAGCCGGTGGGAGACGGTGCGTGCCGTCATGCACCTGGAGCTGGTTGCCTGGAATCAGGCGTACCTGACGGCGATGATCGGGCTGATCCTCATCGCGCAGGCCGGTCTCGTCGTGCACCGCTGGCTGGGGGTGGTGCTCCCGCTTCCGCTGGTGCTCGTCCTGGCGATCCTCCCGCCCTTCCTCCTCCTGACCCTGTGCGGGGTGGTGTGCCTGACCCTGTGGGATCCTTCGCGCTCCTCAGGGGCCCTGCGGCTCTACGGGGCGCTGCCCGTGACCCGCGCCGAGGTGCTTGCCGGCCACTACCTGCTCAGCCTGGCCTACGGTGGTGCCTCCGTCCTCCTGGCCGCCATCCACATGCTCGGTGCGTTCGGCGGTGCCGATCCCCTGGTCTGGGCGACAGTACTGGCGTGGGTGGCGGCAGTGTTGGGGATCTGCGCAGTGATGCCCCCAGTGCTCGCCAGGTACCGCAGCCCCCTCACAGGGATTGTGGTCATGATGCTGGTGATTGCAGTCCTGGGCCTGCTCGGCGGGTTCGTCAAGGGATCCGAAGCGGTATCCCTGACCGCCGTCTCCCAGTCCGGGATGCTCCTGGCCCTGACAGCCCTGCTCCTCGTGCTCGTCCCAGTGGGGCTGGGCGCCTCCTGGTGGACCTGCTGCCGTATCTACCTCCGCCAGGACCACTGA","MPESVPTSESVVSAARTVPTLPTAAESCGTQVPSAPAAVRGPGALSRWETVRAVMHLELVAWNQAYLTAMIGLILIAQAGLVVHRWLGVVLPLPLVLVLAILPPFLLLTLCGVVCLTLWDPSRSSGALRLYGALPVTRAEVLAGHYLLSLAYGGASVLLAAIHMLGAFGGADPLVWATVLAWVAAVLGICAVMPPVLARYRSPLTGIVVMMLVIAVLGLLGGFVKGSEAVSLTAVSQSGMLLALTALLLVLVPVGLGASWWTCCRIYLRQDH$","Membrane protein","Membrane, Cytoplasm","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Saenz H.L., Augsburger V., Vuong C., Jack R.W., Gotz F, Otto M. Inducible expression and cellular location of AgrB, a protein involved in the maturation of the staphylococcal quorum-sensing pheromone. Arch. Microbiol. 2000. 174(6):452-455. PMID: 11195102Zhang L., Gray L., Novick R.P., Ji G. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 2002. 277(38):34736-34742. PMID: 12122003","","","

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[58-250]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[64-84]?$ $\"[90-119]?$ $\"[148-168]?$ $\"[174-194]?$ $\"[204-224]?$ $\"[243-263]?$	transmembrane_regions

InterPro
IPR000062
Domain

Thymidylate kinase
PF02223	$\"[26-213]T$	Thymidylate_kin
TIGR00041	$\"[21-213]T$	DTMP_kinase: thymidylate kinase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[20-226]T$	no description
PTHR10344	$\"[19-225]T$	THYMIDYLATE KINASE

","BeTs to 26 clades of COG0125COG name: Thymidylate kinaseFunctional Class: FThe phylogenetic pattern of COG0125 is AmTkyqvceBrhujgpolinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-63% similar to PDB:2CCG CRYSTAL STRUCTURE OF HIS-TAGGED S. AUREUS THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE (TMP) (E_value = 3.7E_38);-63% similar to PDB:2CCJ CRYSTAL STRUCTURE OF S. AUREUS THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE (E_value = 3.7E_38);-63% similar to PDB:2CCK CRYSTAL STRUCTURE OF UNLIGANDED S. AUREUS THYMIDYLATE KINASE (E_value = 3.7E_38);-52% similar to PDB:4TMK COMPLEX OF E. COLI THYMIDYLATE KINASE WITH THE BISUBSTRATE INHIBITOR TP5A (E_value = 8.9E_24);-52% similar to PDB:5TMP COMPLEX OF E. COLI THYMIDYLATE KINASE WITH THE BISUBSTRATE INHIBITOR AZTP5A (E_value = 8.9E_24);","Residues 61 to 248 (E_value = 1.7e-54) place ANA_2533 in the Thymidylate_kin family which is described as Thymidylate kinase.","","kinase, transmembrane","","1","","","Thu Aug 9 14:52:04 2007","","Thu Aug 9 14:52:04 2007","","","Thu Aug 9 14:52:04 2007","Thu Aug 9 14:52:04 2007","Thu Aug 9 14:52:04 2007","","","Thu Aug 9 14:52:04 2007","","","Thu Aug 9 14:52:04 2007","Thu Aug 9 14:52:04 2007","","","Thu Aug 9 14:52:04 2007","Thu Aug 9 14:52:04 2007","","","","","yes","","" "ANA_2535","2730693","2729923","771","7.32","1.64","26211","ATGAACCGACCAGCAGGTGCATGCTCCCTCTCAGGGATGAGATGGGCCGCGTCCCTCTCCCCCACGAGTCCCGTTGCCCTCCGGGTCCTCAGCGGGCACCAGGTTCCAGGAGGCGGCCCAGGCCCAGATCTGGTCGAGCTCGCCCTCCATGAGGTAGCGGGCCCTGGGCTCGGTGAGTGCCCGAGCGGTCATTCCTCCCAGCGCCACCGTGCCCGCCTCGCTGTGTACTGTCGCCTGCACGCTCGGGCCTGCCTCGCGGAGGCGCAGAGCGGATCGGGGTTGCCGGGCGATGTCGAAGTCGTCCCGGGAACCGGGCCAGGCGAGGTTGTGGGAGCGCAGCAGCGTCCTGCTGTGGATGCCGCTGCGGTCGAAGACGGTCCGCGGCCGCAGGGTCAGGTAGCCCATGAGGAGGCACAGTGCCGCCGCGGCGAGGCAGGCGAGCATTCCCCGGTACTGCCCAAAGGTCATGATTGCCAGCCCGATGGCCAGCCCCAGGAGGCCGACGGCGGTCAGCCCCCAGGCGATGACTCGCTCCTGCGGGCTCGATCTGCGGATGATCGGCTCGAACCGAGCGGCGTGGTCGGCGTCCTCGGCCCCGGACTGTGTCACGGTCATGTCACGACTCTTGCACACCTGTCCAAAGCCGTCCTGGTTTTGGAGGTCGCTCCGGCAGTGACCCGCGCCCGACGACGGCGACCTCATGCCCCGCCGCAGCTCGGGCGGGACAGGGTGCTCACCGTCCTTCGGCCTGGGGTCGCAGCTGCACCATGA","MNRPAGACSLSGMRWAASLSPTSPVALRVLSGHQVPGGGPGPDLVELALHEVAGPGLGECPSGHSSQRHRARLAVYCRLHARACLAEAQSGSGLPGDVEVVPGTGPGEVVGAQQRPAVDAAAVEDGPRPQGQVAHEEAQCRRGEAGEHSPVLPKGHDCQPDGQPQEADGGQPPGDDSLLRARSADDRLEPSGVVGVLGPGLCHGHVTTLAHLSKAVLVLEVAPAVTRARRRRPHAPPQLGRDRVLTVLRPGVAAAP$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-16]?$	signal-peptide

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[57-197]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[4-197]T$	no description
PTHR11669	$\"[114-206]T$	REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT

","BeTs to 10 clades of COG0470COG name: ATPase involved in DNA replicationFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0470 is aompkzyqvdrlbcefghsnu-xitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-48% similar to PDB:1A5T CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III (E_value = 3.2E_17);-48% similar to PDB:1JR3 Crystal Structure of the Processivity Clamp Loader Gamma Complex of E. coli DNA Polymerase III (E_value = 3.2E_17);-48% similar to PDB:1XXH ATPgS Bound E. Coli Clamp Loader Complex (E_value = 3.2E_17);-48% similar to PDB:1XXI ADP Bound E. coli Clamp Loader Complex (E_value = 3.2E_17);-50% similar to PDB:1NJF Nucleotide bound form of an isolated E. coli clamp loader gamma subunit (E_value = 8.3E_13);","No significant hits to the Pfam 21.0 database.","","polymerase III, delta subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2537","2730706","2732391","1686","5.78","-8.15","58490","ATGGAAACGAGAATGAAGCATCCTCCCCAGAATCGTCCTGATCGTCCCTTGTCCACGGGTGTGAGCGACGCAAGAGGCTCCGGTGGCCTTCGACGTCGTCGGGTGTCTGCCGGGGTGTTGGCGGCTGTGGCGGGCGTGTGCCTGGGGGTGGGGGCCGGTGTGGTTCCTGCTGCTGCGGCGCCCGCTGCGGGGTCGGCTCCGGCTGCGTCGTCCAAGGCGGCGGTGCCCAAGGGGCTGGAGTCCTTCTACGGTCAGAAGGTCGCGTGGTATGACTGCGTGGCCTCTGCCGGAGTGGAGAAGTCTGCCGAGAAGACCGGTTTTCAGTGCGCTAAGGTCAAGGTTCCGCTGGACTACTCCAAGCCCGATGGGCAGACCATTGAGATCGCGATGAAGAAGCACCAGGCCACCGGCTCGGTGCGCCAGGGCACCCTCTTCATGAACCCCGGTGGCCCCGGCGGATCCGGCGTGGACGACGTCGGCGCGATGGTGGACTCGACCTTCGCCGGCGTCCAGAAGTCCTACGACATCATCGGCTTCGACCCCCGCGGCGTCGGCTCCTCCACCGCCGTGAACTGCACCTCCGACACCGAGCTGGAGGCGAAGACGGAAGACGCTCCGGTCAATGCCGGAGAAGGTGCCGCGACATTCGAGCAGCGGGCCGCCGTCATCTCCGCACAGTTCAAGCAGTTCGAGGCCAGCTGCGCGGCGGGCACCAAGCCTGCCGAGCTGCTCGACCACGTGGATACCGTCTCGGTGGCCCGGGATCTTGACGTGCTGCGGGCACTGTCCGGGGACCAGAAGCTCAACTACGCGGGCTTCTCCTACGGCACCTTCCTGGGGGCTCACTACGCCGAGCTCTTCCCCGCCAACACCGGCCGCATGGTCCTCGACGGCGCCCTCGACCCCAGCCTGAGCCTCAGCGAGCACATTCTCGGGCAGGCCCGGGGCTTCGAGCGGGCGCTGCGCAACTATGTCTCCTGGTGCCAGTCGGGGCAGAACTGCCCCCTCTCCGGTGACGCCGACGCCGGCGTCAAGCAGATCGGGGACATCTTCAACTCGGCCGACCAGTCGCCCGTGCCCTCCTCGGACGCGAACCGTCCGGTCACGGGTGACGACATGAAGCAGGTCGTGTCGGTCATGCTCTATTCTCCGGAATCCTCTTGGGACGTCCTGAACGAGGCATTTGGGCAGGTTGTGAACCAGAAAGACGCCTCGGCCTTCAGGGCTATCGCGGACCGGCTCGAAGCTCAGCCCCTGGTCAACACCGGTGCGAACATTGCCATCAACTGCCGGGACTACCAGGTCGAGGGTGACATGGCCACCTGGAAGGCGCAGAGTGAGAAGGTGCAGAAGGCCTCACCTCGCTTCGCGTCCACGTTCGATGGTGCGGAACTGGGGTGCCAGGCCTGGGGGCACACCAACCCCCAGCCGTCCAAGAAGCTCCACGCCAAGGGAGCCGCGCCGATCCTCGTGATCGGGACGACCGGTGACCCGGCCACGCCGTACGAGGATGCCGTGTCCCTGGCCGATCAGCTGGACTCCGGCCAGCTCCTCACCTGGGAGGGCAACGGGCACACGGCTTACGCCAGCTCCGGGCGCGGCCCCTGTGTCATCAAGGCGGTCGACACCTACCTGCTGAGCGGCACCATGCCCAAGAAGGGGCTGACGTGCCACGGCACGGAGTGA","METRMKHPPQNRPDRPLSTGVSDARGSGGLRRRRVSAGVLAAVAGVCLGVGAGVVPAAAAPAAGSAPAASSKAAVPKGLESFYGQKVAWYDCVASAGVEKSAEKTGFQCAKVKVPLDYSKPDGQTIEIAMKKHQATGSVRQGTLFMNPGGPGGSGVDDVGAMVDSTFAGVQKSYDIIGFDPRGVGSSTAVNCTSDTELEAKTEDAPVNAGEGAATFEQRAAVISAQFKQFEASCAAGTKPAELLDHVDTVSVARDLDVLRALSGDQKLNYAGFSYGTFLGAHYAELFPANTGRMVLDGALDPSLSLSEHILGQARGFERALRNYVSWCQSGQNCPLSGDADAGVKQIGDIFNSADQSPVPSSDANRPVTGDDMKQVVSVMLYSPESSWDVLNEAFGQVVNQKDASAFRAIADRLEAQPLVNTGANIAINCRDYQVEGDMATWKAQSEKVQKASPRFASTFDGAELGCQAWGHTNPQPSKKLHAKGAAPILVIGTTGDPATPYEDAVSLADQLDSGQLLTWEGNGHTAYASSGRGPCVIKAVDTYLLSGTMPKKGLTCHGTE$","Proteinase","Extracellular, Periplasm, Cytoplasm","proteinase","protease","TAP domain protein","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[174-320]T$	Abhydrolase_1

InterPro
IPR013595
Domain

Peptidase S33, tripeptidyl-peptidase C-terminal
PF08386	$\"[453-557]T$	Abhydrolase_4

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[140-528]T$	no description
tmhmm	$\"[35-55]?$	transmembrane_regions

","BeTs to 5 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","***** IPB002410 (Prolyl aminopeptidase (S33) family signature) with a combined E-value of 5.2e-07. IPB002410A 144-152 IPB002410B 176-187 IPB002410C 270-284","","","No significant hits to the PDB database (E-value < E-10).","Residues 174 to 541 (E_value = 2e-12) place ANA_2537 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.Residues 453 to 557 (E_value = 4.9e-29) place ANA_2537 in the Abhydrolase_4 family which is described as TAP-like protein.","","(AE005334) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2538","2732692","2734320","1629","5.06","-16.38","56513","GTGGTTCCTGCTGCTGCGGCGCCCGCTGCGGGGTCGGCTCCGGCTGCGTCGTCCAAGGCGGCGGTGCCCAAGGGGCTGGAGTCCTTCTACGGTCAGAAGGTCGCGTGGTACGACTGTGCGGCCACTGGCGGGATGGAGAAGTCGGCCGAGAAGACCGGTTTTCAGTGTGCCAAGGTCAAGGTTCCGCTGGACTACTCCAAGCCCGATGGGCAGACCATTGAGATCGCGATGAAGAAGCACCAGGCCACCGGCTCGGTGCGCCAGGGCACCCTCTTCGTCAACCCCGGCGGACCCGGCTACTCCGGGGTGGAGATGGTGGAGAACAACGAGATCCAGTTCTCTCCCGCCCTCAACCAGGCCTACGACATCATCGGCTTCGACCCCCGCGGTGTCGGCTCCTCCACCCCGATCACCTGCGATGACGGCGCGGGCCAGCAGCCCGCCAAGGCCGCCCAGGGGGGCATGGGCGTCAACGACCCCCAGCCCGGCTCCCTCGTCGCCGACGTCGCCGGCGGGGACGACCCCACCCCCTTCCGGGATGCTGAGAATCCTGCTGCCGACGGCGGAGCGGAGGCCAACGTCGGCTTCCCGACCCTGATCGACGAGATCACCAAGGACTTCAAGCAGGAGGAGGCCAACTGCGCCGCCCACACCAAGCCGGCCGGGCTGCTCGACCATGTGGACACCGTCTCGGTGGCCCGGGATCTTGACGTGCTGCGGGCACTGTCCGGGGACCAGAAGCTCAACTACCTGGGCTTCTCCTACGGCACTTACCTGGGGGCTCACTACGCCGAGCACTTCCCCGCCAACACCGGCCGCATGGTCCTCGACGGCGCCCTCGACCCCTCCCTGTCACTGGGCGACCGGGCCGCCGGGCAGGCCCAGGGCTTCGAGGCCGCGCTGCGCACCTACGTCCAGCAGTGCCAGTCCGGCCAGGCCGTCCAGGAAGGCCAGAGCTGCCCCCTGACCGGTGACGCCGACGCCGGAGTCCAGCAGGTTCGCGCCCTCATCGCCTCGGCGGACCAGACACCGCTGAAAACCGCGGATCCGAACGTCACCGTGGACGGCAGCACGATCCGCAGCGCCATCCGCCGACTCCTGTACTCCTCCGAATATTGGCCCCTCCTCACCTATGCCCTCGACCAGGCCATCACCCAGAAGGACGGCTCCTACATCCAGGTGCTCTACGGCAAGGTGACCGCCGGAGGCAGCGCCCCGACCTTCTACGCCGTCAACTGCCAGGACATCCCCGTCCAGGGCGACATGACCAGCTGGGAGAAGGAGTACCAGCAGATCCTCCAGAGCTCGCCCACCTTCGGCGCCTCCTTGGGCAACCAGGATGCGCGCTGCCAGGCCTGGGGGCACAACGGGACCCGCAAGCCCGCTCCCATCCACGCCAAGGGGGCGGCCCCCATCCTGGTGGTGGGCACCACCGGTGACCCGGCCACGCCCTACGCCTGGTCCCAGGCCATGGCCGATCAGCTCGAGTCCGGCCGGCTCCTGACCTGGGAGGGCAACGGCCACACCGCCTACGGGCGCGCGGGGGCCTGCGTCCAGAAGGCCGTCGACACCTACCTCACGAGCGGGACCCTGCCCAAGGAGGGCCTGACCTGCACAAGCGGTCAGTAA","VVPAAAAPAAGSAPAASSKAAVPKGLESFYGQKVAWYDCAATGGMEKSAEKTGFQCAKVKVPLDYSKPDGQTIEIAMKKHQATGSVRQGTLFVNPGGPGYSGVEMVENNEIQFSPALNQAYDIIGFDPRGVGSSTPITCDDGAGQQPAKAAQGGMGVNDPQPGSLVADVAGGDDPTPFRDAENPAADGGAEANVGFPTLIDEITKDFKQEEANCAAHTKPAGLLDHVDTVSVARDLDVLRALSGDQKLNYLGFSYGTYLGAHYAEHFPANTGRMVLDGALDPSLSLGDRAAGQAQGFEAALRTYVQQCQSGQAVQEGQSCPLTGDADAGVQQVRALIASADQTPLKTADPNVTVDGSTIRSAIRRLLYSSEYWPLLTYALDQAITQKDGSYIQVLYGKVTAGGSAPTFYAVNCQDIPVQGDMTSWEKEYQQILQSSPTFGASLGNQDARCQAWGHNGTRKPAPIHAKGAAPILVVGTTGDPATPYAWSQAMADQLESGRLLTWEGNGHTAYGRAGACVQKAVDTYLTSGTLPKEGLTCTSGQ$","Proteinase","Extracellular, Periplasm","proteinase","peptidase","TAP domain protein","","Brede D.A., Faye T., Johnsborg O. Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii. Appl. Environ. Microbiol. 2004. 70(12):7303-7310. PMID: 15574930","","","

InterPro
IPR013595
Domain

Peptidase S33, tripeptidyl-peptidase C-terminal
PF08386	$\"[436-538]T$	Abhydrolase_4

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[90-526]T$	no description

","BeTs to 6 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 121 to 524 (E_value = 5.3e-14) place ANA_2538 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.Residues 436 to 538 (E_value = 8.7e-38) place ANA_2538 in the Abhydrolase_4 family which is described as TAP-like protein.","","(AE005334) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2539","2734421","2736016","1596","4.85","-18.63","55072","GTGACTACTGCAACCTCTCCTCGGCCTCGTATCAAGCCCCTGTTCGTGGCGCTCGCTGCGCTTCTGGCGTGCGGGGGTCTGACCGCCTGCCAGGACGAAGCCGATATCAAGGCAACCCCAGCAACGGCGTCGGCCTCGGCGGCGGTCCCGGCCGGGCTGGAGAGCTTCTACACCCAGAAGGTCTCCTGGTACGCCTGCGACAAGAAGGGGATGGGGGAGGCGAAGTCGGGGAAGGACACCGGCTTCACCTGCGCCAAGGTCAAGGTGCCGCTGGACTACGACAACCCCGGCGGTGAGACGATCGAGATCGCGGTGAAGAAGCGGACCGCCAGCGGGGACTCGGTCGGCTCACTGTTCGTCAACCCGGGCGGGCCGGGAGGGTCGGGCATCGAGCTGGTCGAAAGCGCCGGCTCCTACTTCTCCAAGAACCTCACCAGCTCCTACGACGTCGTCGGTTTCGACCCGCGCGGCGTGGGCGCCTCCACAGCGGTCGACTGCCTGACCGACGCCGAGCTCGATGCCGAGCGCGCCGGGGCGAACGACCCGGCGACCCCCTCGGCCGCGGCCACCCAGGAGCGGGCCCAGAAGATGGGGGAGGCCTGTGCGGCGAAGACCAGCCCCGCGGGGCTCCTGGACCACATCGACACCATCAGCGCGGCCAAGGACCTCGACATCCTGCGGGCGGTCGACGGCCAGCAGACGCTGACCTACCTGGGTTTCTCCTACGGCACCTACCTGGGGGCCACCTACGCCGAGCTGTTCCCGGCCAACACCGGGCGGCTGGTCCTCGACGGCGCCGTCGACCCCTCCCTGAGCGCCGAGGAGCTGACCCTGGGGCAGGCCAAGGGCTTCGAGGCGTCGCTTCGGGCCTACGTGCAGAGCTGCCAGAGCTCCAAGCTGGGCTGCCCCCTGAGCGGCGACGTCGACTCCGGTGTCTCCCAGATCCGCGAGCTCCTGGAGTCCACGAAGGCGGCGCCGCTGCCGACCTCCGACGACAAGCGGCCGCTGACCTACGACCTGGCCGTCTACGGGGTGCTGGGATCGATGTACCAGACCCAGCTGTGGCCCTCGCTCACCCTGGCGCTGTCTCAGGCGATGGGCAAGATGGGCAACCCGGACGGAAGCGCGCTGCTGGCCATCGCCGACGCCGTCTCCTCCCGCCAGAGCGACGGCAGCTACTCCGGTAACGGCGCCGAGGCCCTCATGGCGGTCAACTGCCTGGACTATCCGGTCCAGGGGGACAACACCTCCTGGGAGGAGAACGCCAAGGCCGTCAACGAGGCCTCGCCCACCTTCGGCTCCCAGCTGCTCTACCCCGACGCCTACTGCCAGGGCTGGGGCCACACGTCGAGCCGCAAGCGCGAGAAGATCACGGCCTCCGGCGCCGCACCGATCCTCGTGGTGGGCACCACCGGCGACCCGGCCACGCCCTACGCCTGGTCCGAGTCGCTGGCCGATCAGCTCGAGTCCGGTCAGCTCATGACCTGGAAGGGCGACGGACACACCGCCTACGGGCGCTCCAACGACTGCGTCAAGAAGGCCGTGGACACCTACCTGCTCAACGGGACGATGCCGGACAAGGGACTCACCTGCTGA","VTTATSPRPRIKPLFVALAALLACGGLTACQDEADIKATPATASASAAVPAGLESFYTQKVSWYACDKKGMGEAKSGKDTGFTCAKVKVPLDYDNPGGETIEIAVKKRTASGDSVGSLFVNPGGPGGSGIELVESAGSYFSKNLTSSYDVVGFDPRGVGASTAVDCLTDAELDAERAGANDPATPSAAATQERAQKMGEACAAKTSPAGLLDHIDTISAAKDLDILRAVDGQQTLTYLGFSYGTYLGATYAELFPANTGRLVLDGAVDPSLSAEELTLGQAKGFEASLRAYVQSCQSSKLGCPLSGDVDSGVSQIRELLESTKAAPLPTSDDKRPLTYDLAVYGVLGSMYQTQLWPSLTLALSQAMGKMGNPDGSALLAIADAVSSRQSDGSYSGNGAEALMAVNCLDYPVQGDNTSWEENAKAVNEASPTFGSQLLYPDAYCQGWGHTSSRKREKITASGAAPILVVGTTGDPATPYAWSESLADQLESGQLMTWKGDGHTAYGRSNDCVKKAVDTYLLNGTMPDKGLTC$","Proteinase","Extracellular, Periplasm","proteinase","protease","TAP domain protein","","Hempel J., Harper K., Lindahl R. Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. Biochemistry 1989. 28(3):1160-1167. PMID: 2713359","","","

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PS00070	$\"[194-205]?$	ALDEHYDE_DEHYDR_CYS

InterPro
IPR013595
Domain

Peptidase S33, tripeptidyl-peptidase C-terminal
PF08386	$\"[429-531]T$	Abhydrolase_4

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[118-519]T$	no description
signalp	$\"[1-29]?$	signal-peptide

","BeTs to 4 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: R [General function prediction only]The phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is 11","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 148 to 517 (E_value = 1.4e-11) place ANA_2539 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.Residues 429 to 531 (E_value = 2e-39) place ANA_2539 in the Abhydrolase_4 family which is described as TAP-like protein.","","(AE005334) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2540","2737148","2736150","999","5.18","-10.92","34254","ATGCACGTTCACATCACCTACACCGGGGGCACCATCGGGATGGTGGACTCCCCCCACGGCCTCGTTCCCGGTGCGGATCTGGAGGGGTGGCTCGACTCGCTGCTGAAGGGCACGCCCCTGGCTCGCTCGGTGTCCGTGACCTCGCTGGAGCCGCTCATCGACTCCTCGAACGCCACCCCGCTGTCCTGGCAGGCGATCGTGGACGACCTGCGCGCCCACGCCGCGGCCGACCCGCAGACCGCCTTCGTCATCCTGCACGGGACCGACACGATGGCCTACACCAGTGCCGCTCTGTCCTATGCGCTGACGGATCTGAGCGTTCCGGTCGTCGTCACCGGTTCCCAGCTCCCCCTCGGAGAACTGGGAACCGACGCCGCAGCGAACGTCACCGGGGCGCTCAAGGCCGCCACCTCCGGGCGCCTGAGCGGGGTGGCGCTGTTCTTCGGACATCGGCTCCTGGCCGGGAACCGGGTGACGAAGTCCTCCTCGTGGGCCTTCACCGGTTTCGAGTCCCCCAATGCGGCCCCTCTGGCCACCACTGGCGCCCCGTGGCAGTGGGCTCCATGCACCCGGGGCGGGGCCGGTTGGAAGGATGCCGCCCCCTACGCCCGTCACGACGTCGTCGTGGTCGACCTGGTCCCGGGCATCACCGCGGCCCGCCTGGAGGCGCTGCTGACACCGCTGCCCGAGGCCGTGATCTTGCGTGCCTTCGGAGTCGGCAACGTGCCGTCCCAGGAGCCGGGGCTGACCGACGTCGTCGAGCGGGTGATCACCGCCGGAACGCCCGTCATCGTCACCTCCCAGTGCCACGAGTCCGAGGTCCTCCTGGGGCACTACGAGGCCGGTGATGCACTGGCCCGCAGTGGCGCCGTCGGCAGCCGCGACATGACCCTGGAGGCCGCCTACGCCAAGGTCCAGTTCCTGCTCTCGCAGGGACTGGCGGGAGACGACCTGGCCGGCTGGATGGGACGCTCCATCGCCGGCGAGCTGAGCCAGTGA","MHVHITYTGGTIGMVDSPHGLVPGADLEGWLDSLLKGTPLARSVSVTSLEPLIDSSNATPLSWQAIVDDLRAHAAADPQTAFVILHGTDTMAYTSAALSYALTDLSVPVVVTGSQLPLGELGTDAAANVTGALKAATSGRLSGVALFFGHRLLAGNRVTKSSSWAFTGFESPNAAPLATTGAPWQWAPCTRGGAGWKDAAPYARHDVVVVDLVPGITAARLEALLTPLPEAVILRAFGVGNVPSQEPGLTDVVERVITAGTPVIVTSQCHESEVLLGHYEAGDALARSGAVGSRDMTLEAAYAKVQFLLSQGLAGDDLAGWMGRSIAGELSQ$","L-asparaginase I","Cytoplasm, Membrane, Extracellular","L-asparaginase I","L-asparaginase I ","Asparaginase","","Minton N.P., Bullman H.M., Scawen M.D., Atkinson T., Gilbert H.J. Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 L-asparaginase gene. Gene 1986. 46(1):25-35. PMID: 3026924Jennings M.P., Beacham I.R. Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins. J. Bacteriol. 1990. 172(3):1491-1498. PMID: 2407723Tanaka S., Robinson E.A., Appella E., Miller M., Ammon H.L., Roberts J., Weber I.T., Wlodawer A. Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi. J. Biol. Chem. 1988. 263(18):8583-8591. PMID: 3379033","","","

InterPro
IPR006034
Family

Asparaginase/glutaminase
PD003221	$\"[5-172]T$	Q6AAU5_PROAC_Q6AAU5;
PR00139	$\"[3-14]T$ $\"[80-98]T$ $\"[256-274]T$	ASNGLNASE
PIRSF001220	$\"[1-330]T$	L-asparaginase/Glutamyl-tRNA(Gln) amidotransferase subunit D
PTHR11707	$\"[50-330]T$	L-ASPARAGINASE
PF00710	$\"[2-319]T$	Asparaginase
PS00144	$\"[5-13]?$	ASN_GLN_ASE_1
PS00917	$\"[81-91]T$	ASN_GLN_ASE_2

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1170	$\"[2-180]T$	no description
G3DSA:3.40.50.40	$\"[206-325]T$	no description
PIRSF500176	$\"[1-328]T$	L-asparaginase/L-glutaminase
PTHR11707:SF3	$\"[50-330]T$	L-ASPARAGINASE I

","BeTs to 19 clades of COG0252COG name: L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit DFunctional Class: E [Metabolism--Amino acid transport and metabolism] Functional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG0252 is aompkzy--drlb-efghsnu-----Number of proteins in this genome belonging to this COG is 1","***** IPB006034 (Asparaginase/glutaminase) with a combined E-value of 1.8e-35. IPB006034A 7-14 IPB006034B 80-98 IPB006034C 107-136 IPB006034D 158-171 IPB006034E 231-241","","","-56% similar to PDB:2OCD Crystal structure of L-asparaginase I from Vibrio cholerae O1 biovar eltor str. N16961 (E_value = 1.6E_56);-55% similar to PDB:2P2D Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I (E_value = 1.6E_56);-55% similar to PDB:2P2N Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I (E_value = 1.6E_56);-55% similar to PDB:2HIM Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I (E_value = 6.0E_56);-48% similar to PDB:1WLS Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii (E_value = 1.9E_30);","Residues 2 to 319 (E_value = 2.2e-85) place ANA_2540 in the Asparaginase family which is described as Asparaginase.","","I (ansA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2541","2738715","2737168","1548","7.34","1.34","54531","ATGAGCGAGTCTCCGTCCAGCCACTCCCCCACCTCTCCCTCACCGCACTCGGGTGCTTCGCCGTCACCCTCCCCCGCTTCCCAGCCCGACCAGATCCGGGACCGCGGCGACGCCGGTTACAACAAGTCGCTGAAGAACCGCCACCTGCAGATGATCGCCATCGGCGGCTCCATCGGCACAGGTCTTTTCATGGGTGCCGGCGGGCGGCTCAAGGACGGCGGGGCGGGCCTGATGTTCGCCTATGCCGTCTGCGGAATCTTCGCCTTCCTCATGGTGCGCGCTCTGGGCGAGCTCGCCATCCGCCGCCCCTCCTCGGGAGCATTCGTCTCCTACGCCCGTGAGTTCCTCGGCGAGAAGGGCGCCTACATCACCGGCTGGTTCTTCTTCCTGGACTGGTCGGTCACCGTGATGGCCGACATCACGGCCGTGGCCCTCTACCTCCACTACTGGACGGCTCTGAAGGTTGTTCCACAGTGGGTCTTCGCGCTCGTGGCACTCGTCCTGGTCTTCATCCTCAACATGCTCAACGTCAAGATGTTCGGCGAGGCGGAGTTCTGGTTCGCGCTCATCAAGGTCGCCGCCATCGTGTCCTTCATGGTGGTGGCCATCGTCGCCATTGTTCTCGGGCTTCACACCGGAACGGATCCCGACGGTGGCGCGATCACCGCAGGGGCTCACAACATCCTCGAAAACGGCGGCTTCTTCCCCGAGGGATTGCCAATCGTCTTCGCCCTGACCCTCGGCGTCGTCTTCGCCTTCGGTGGCACGGAGATGGTGGGCGTGGCCGCCGGAGAGGCGAAGGACGCGGAGAAAATCCTGCCCAAGGCGATCAACTCGATGATTCTGCGCATCTTCGTCTTCTACGTCGGCTCGGTCATGCTGCTGGCTCTGGTCCTGCCCTATACCTCCTACTCGAAGGACCAGTCGCCCTTCGTCACCTTCTTCTCCGGGATCGGTGTGCCCTATGCCGGCGACATCATCCAGGTCGTGGTCCTCACCGCCGCGCTGTCCTCCCTCAACGCCGGCCTGTACGCCACCGGACGCACCCTGCGCTCCATGGCCGTGGCCGGTGAGGCCCCTCGGGTGGCGGCCGGGCTCAACAAGCACCAGGTTCCTGCCGGGGGCATCATCATTACCTCCGCCCTGGGGCTGCTCGGCGTCGTCCTCAACGCCTACCTGCCCGGCGATGCCTTCAACATCGTCATGAACCTGGCCGGCATCGGCATCGCCGGGACCTGGGGAGCCATCCTCGTCACCCACCTCGCCTTCCTGCGCCGGGTGCACGAGGGCAAGGAGGTGCGCCCGACCTACCGGATGCCCTGGGCCCCCTGGTCCAACTACGCGGCCCTGGCCTTCTTCACCATCGTCGTCGTCTCCAACGTGACCAGCCCGGCCGGACGTTGGACCCTGGTCCTGTTCGCCATCGTCGCCGTCATGATGGTGGCAGGCTGGTACGCGGTGCGGGGACGCATTCGGGGCGACCTGCTCGACGAGGTCCTCGCCGACGAGGTGGAGGAAGCCGCATCCGCCCCGTCGCACGAGGCCTAA","MSESPSSHSPTSPSPHSGASPSPSPASQPDQIRDRGDAGYNKSLKNRHLQMIAIGGSIGTGLFMGAGGRLKDGGAGLMFAYAVCGIFAFLMVRALGELAIRRPSSGAFVSYAREFLGEKGAYITGWFFFLDWSVTVMADITAVALYLHYWTALKVVPQWVFALVALVLVFILNMLNVKMFGEAEFWFALIKVAAIVSFMVVAIVAIVLGLHTGTDPDGGAITAGAHNILENGGFFPEGLPIVFALTLGVVFAFGGTEMVGVAAGEAKDAEKILPKAINSMILRIFVFYVGSVMLLALVLPYTSYSKDQSPFVTFFSGIGVPYAGDIIQVVVLTAALSSLNAGLYATGRTLRSMAVAGEAPRVAAGLNKHQVPAGGIIITSALGLLGVVLNAYLPGDAFNIVMNLAGIGIAGTWGAILVTHLAFLRRVHEGKEVRPTYRMPWAPWSNYAALAFFTIVVVSNVTSPAGRWTLVLFAIVAVMMVAGWYAVRGRIRGDLLDEVLADEVEEAASAPSHEA$","L-asparagine permease","Membrane, Cytoplasm","L-asparagine permease (L-asparagine transportprotein)","putative L-asparagine permease","amino acid permease-associated region","","Weber E., Chevallier M.R., Jund R. Evolutionary relationship and secondary structure predictions in four transport proteins of Saccharomyces cerevisiae. J. Mol. Evol. 1988. 27(4):341-350. PMID: 3146645Vandenbol M., Jauniaux J.C., Grenson M. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases. Gene 1989. 83(1):153-159. PMID: 2687114Reizer J., Finley K., Kakuda D., MacLeod C.L., Reizer A., Saier Jr M.H. Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria. Protein Sci. 1993. 2(1):20-30. PMID: 8382989","","","

InterPro
IPR002293
Family

Amino acid/polyamine transporter I
PTHR11785	$\"[37-206]T$ $\"[226-490]T$	AMINO ACID TRANSPORTER

InterPro
IPR004840
Family

Amino acid permease
PS00218	$\"[73-103]?$	AMINO_ACID_PERMEASE_1

InterPro
IPR004841
Domain

Amino acid permease-associated region
PF00324	$\"[48-496]T$	AA_permease

noIPR
unintegrated

unintegrated
PIRSF006060	$\"[38-510]T$	High-affinity amino acid transporter
PTHR11785:SF25	$\"[37-206]T$ $\"[226-490]T$	L-ASPARAGINE PERMEASE
tmhmm	$\"[49-69]?$ $\"[75-95]?$ $\"[129-149]?$ $\"[159-177]?$ $\"[187-209]?$ $\"[241-263]?$ $\"[284-304]?$ $\"[323-343]?$ $\"[374-394]?$ $\"[404-424]?$ $\"[439-459]?$ $\"[465-487]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
PD026347	$\"[1-102]T$	Q6AB31_PROAC_Q6AB31;

InterPro
IPR001345
Active_site

Phosphoglycerate/bisphosphoglycerate mutase
PS00175	$\"[53-62]T$	PG_MUTASE

InterPro
IPR005952
Family

Phosphoglycerate mutase 1
PTHR11931	$\"[47-291]T$	PHOSPHOGLYCERATE MUTASE
TIGR01258	$\"[49-291]T$	pgm_1: phosphoglycerate mutase

InterPro
IPR013078
Domain

Phosphoglycerate mutase
PF00300	$\"[50-233]T$	PGAM

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1240	$\"[45-287]T$	no description
PIRSF001490	$\"[49-291]T$	Cofactor-dependent phosphoglycerate mutase
signalp	$\"[1-19]?$	signal-peptide

","BeTs to 8 clades of COG0588COG name: Phosphoglycerate mutase 1Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0588 is ------y---rl--e--hsn-j-it-Number of proteins in this genome belonging to this COG is 1","***** IPB001345 (Phosphoglycerate/bisphosphoglycerate mutase) with a combined E-value of 1.2e-77. IPB001345A 51-79 IPB001345B 97-109 IPB001345C 123-163 IPB001345D 191-209 IPB001345E 218-261***** IPB013079 (6-phosphofructo-2-kinase) with a combined E-value of 6.9e-07. IPB013079F 100-112 IPB013079H 218-265","","","-80% similar to PDB:1RII Crystal structure of phosphoglycerate mutase from M. Tuberculosis (E_value = 6.3E_91);-75% similar to PDB:1BQ3 SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE (E_value = 2.6E_81);-75% similar to PDB:1BQ4 SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH BENZENE HEXACARBOXYLATE (E_value = 2.6E_81);-75% similar to PDB:4PGM SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE (E_value = 2.6E_81);-75% similar to PDB:5PGM SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE (E_value = 2.6E_81);","Residues 50 to 233 (E_value = 5.5e-44) place ANA_2545 in the PGAM family which is described as Phosphoglycerate mutase family.","","mutase (gpmA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2546","2741700","2741020","681","4.95","-12.59","24892","ATGCGCGCCATCTTCAACCAGGAGCTCAAGCAGCTGGGCTCCGACCTCGAGTCCATGGCCAACCAGGTCGCCACCGCGATCGAGCGGGCCGCGGAGTCCCTGCGCCAGGGGGACATCGTCATCGCCGAGCAGGTGATCGACGCCGACGAGCGCATCAACGACCTCCAGCGCGACATCGACGACCTGTGCGTCATGCTGCTGGCCCGTCAGCAGCCGGTGGCCGGGGACCTGCGCAACGTCCTGTCCGCGCTGCGCATGGCCCAGACCCTGGAGCGCCAGGGCGACCTGGCCCGCCACGTGGCGGCCATCGCCCGCGGCCGCTACCCCGAGCCGCCGCTGCCCGAGCCGGTCCTGGGGCTCATCCTGGAGATGGCGGACCTGGCGGTGCGCGCCGGTAAGGACGTTGCCCGCCTCATCTCGACGCGGGACCTGGAGCTGGCCTCCGTCATTCAGACCAACGACGCCGAGCTCGATGCCCTGCACCGCCGCTCCTTCCAGATGATCCTGGACCCGGCTCACGACCTGAGCCGCCAGCAGGTCATCGACGCCGTCCTCATGGGCCGCTTCCTGGAGCGCTTCGGCGACCACTCCACGTCGGTGGCCAGCCGCGTGGCCTACCTCGTCTCGGGCGCCTCCATGCCCGAGACGCATGACGCCGAGGACGCCGACGCGCTCCACTGA","MRAIFNQELKQLGSDLESMANQVATAIERAAESLRQGDIVIAEQVIDADERINDLQRDIDDLCVMLLARQQPVAGDLRNVLSALRMAQTLERQGDLARHVAAIARGRYPEPPLPEPVLGLILEMADLAVRAGKDVARLISTRDLELASVIQTNDAELDALHRRSFQMILDPAHDLSRQQVIDAVLMGRFLERFGDHSTSVASRVAYLVSGASMPETHDAEDADALH$","Two-component system response regulator","Cytoplasm","response regulator of two-component system","putative phosphate transport system regulatory protein","phosphate transport system regulatory protein PhoU","","Steed P.M., Wanner B.L. Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon. J. Bacteriol. 1993. 175(21):6797-6809. PMID: 8226621","","","

InterPro
IPR008170
Family

PhoU
PF01895	$\"[16-104]T$ $\"[121-204]T$	PhoU
TIGR02135	$\"[3-213]T$	phoU_full: phosphate transport system regul

noIPR
unintegrated

unintegrated
G3DSA:1.20.58.220	$\"[5-113]T$ $\"[121-223]T$	no description
PTHR10010	$\"[48-210]T$	SODIUM-DEPENDENT PHOSPHATE TRANSPORTER-RELATED

","BeTs to 17 clades of COG0704COG name: Phosphate uptake regulatorFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0704 is aompkz-qvdrlbcefg-s--j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB008170 (PhoU) with a combined E-value of 6.5e-37. IPB008170A 16-55 IPB008170B 66-102 IPB008170C 188-210 IPB008170A 121-160 IPB008170A 9-48","","","-46% similar to PDB:1T72 Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus (E_value = 1.9E_17);-46% similar to PDB:1T8B Crystal structure of refolded PHOU-like protein (gi 2983430) from Aquifex aeolicus (E_value = 1.9E_17);-47% similar to PDB:1XWM The crystal structure of PhoU (phosphate uptake regulator), Structural genomics (E_value = 5.4E_17);-41% similar to PDB:2I0M Crystal structure of the phosphate transport system regulatory protein PhoU from Streptococcus pneumoniae (E_value = 5.8E_11);","Residues 16 to 104 (E_value = 3.5e-21) place ANA_2546 in the PhoU family which is described as PhoU family.Residues 121 to 204 (E_value = 3.3e-11) place ANA_2546 in the PhoU family which is described as PhoU family.","","regulator of two-component system (phoU)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2547","2741902","2743152","1251","5.20","-12.54","43592","GTGGGCCTGACCGTCACCGTTCTCCTCATCATCGCCGCTGGCCTCCTGTGCCTGGGGGTGGGGATCGGTGTCGCGCTGTCCCGGCGCGAGCGCAGAGCGGCCACGAGCGCCGCCGACCTGGCCGGCCTGGCCGGGACCGACACGGCCGTCCCGGTGCTGGCGGCACTGCGCTCGACCGTCGTCGTCCTCGATGATGACGACGAGGTCCTGCGAGCCTCGGCGTCGGCCTACACCTTCAACATCGTGCGCGACGACGCCGTCATCGAGCCGACCGTGGTGGCGATGGTGGGGCGCGTGCGGGCCTCGGGCCAGGCGCAGGACGCGGCCGTCACCGTCGCCCGGGGGCGGGTACCTGGCGCGGGCCAGTTCCACCTGCAGGTGCGGGTGGCCGGTATCGGTCAGGGGCGCGTCCTCATCCTCATTGAGGACCACACCGCCGCCCGCCGGGTGGAGGCCATGCGCCGTGACTTCGTCGCCAACGTCTCCCACGAGCTCAAGACCCCGGTCGGTGCGATCCAGCTGCTGGCCGAGACCGTCGAGGCCGGCGCCGACGACCCCGACTTCGTGCGCGACTACTCCGGGCGCATGCGCAAGGAGGCCCGCCGCCTGGGCGTCCTGGTCCAGGAGATCATCGAGCTCACCCGCCTCCAGGAGGGCGACGCCCTGGCCGAGCCCGAGGTCGTTGACATCGACGACGTCGTCGCCGAGGCCGTGGACCGGGTGCGCGTCGAGGCCGAGGGCCGCCAGATCGCCCTCGTGGCCGGCGGGACCAAGGGGCTGCGGGTGCGTGGCGACGCCGCCCTCATCACCACCGCCGTGCGCAACCTGCTGGACAACGCCATCCGCTACTCCGAGCCGCGCACCCGGGTCTCGGTGGGCGTCTCGCTGGATGCGGAGGACCCCGATATCGTGCGCATCGCCGTGGTCGACCAGGGCATCGGCATCCCCAAGGAGGAGCAGGAGCGCGTCTTCGAGCGCTTCTACCGCGTGGACAAGGCCCGCTCGCGCGCCACCGGGGGCACTGGCCTGGGCCTGAGCATCGTCAAGCACGTGGCCGCCGACCACGGCGGCACCGTCGAGCTGTGGTCCGCCCCGGGACGCGGCTCTACCTTCACCCTCGTGCTGCCGCGCCTGGGCGAGGGCGAACCGGTGGAGGGTGAGTCGGTCGGGTCTGGTTCGGTCGGGGTCGGTTCGGCCCAGGACGAGCCCGCCGACGCCGCGGCGGAGCACATCCCTGGGAGCGGTTCATGA","VGLTVTVLLIIAAGLLCLGVGIGVALSRRERRAATSAADLAGLAGTDTAVPVLAALRSTVVVLDDDDEVLRASASAYTFNIVRDDAVIEPTVVAMVGRVRASGQAQDAAVTVARGRVPGAGQFHLQVRVAGIGQGRVLILIEDHTAARRVEAMRRDFVANVSHELKTPVGAIQLLAETVEAGADDPDFVRDYSGRMRKEARRLGVLVQEIIELTRLQEGDALAEPEVVDIDDVVAEAVDRVRVEAEGRQIALVAGGTKGLRVRGDAALITTAVRNLLDNAIRYSEPRTRVSVGVSLDAEDPDIVRIAVVDQGIGIPKEEQERVFERFYRVDKARSRATGGTGLGLSIVKHVAADHGGTVELWSAPGRGSTFTLVLPRLGEGEPVEGESVGSGSVGVGSAQDEPADAAAEHIPGSGS$","Two-component system sensor kinase","Membrane, Cytoplasm","sensor protein","putative two-component system sensor kinase ","Histidine kinase","","West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001. 26(6):369-376. PMID: 11406410Foussard M., Cabantous S., Pedelacq J., Guillet V., Tranier S., Mourey L., Birck C., Samama J. The molecular puzzle of two-component signaling cascades. Microbes Infect. 2001. 3(5):417-424. PMID: 11369279","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[225-385]T$	no description
PF02518	$\"[264-378]T$	HATPase_c
SM00387	$\"[264-379]T$	HATPase_c

InterPro
IPR003661
Domain

Histidine kinase A, N-terminal
PF00512	$\"[153-219]T$	HisKA
SM00388	$\"[153-219]T$	HisKA

InterPro
IPR004358
Domain

Histidine kinase related protein, C-terminal
PR00344	$\"[304-318]T$ $\"[322-332]T$ $\"[339-357]T$ $\"[363-376]T$	BCTRLSENSOR

InterPro
IPR005467
Domain

Histidine kinase
PS50109	$\"[160-379]T$	HIS_KIN

noIPR
unintegrated

unintegrated
G3DSA:1.10.287.240	$\"[143-215]T$	no description
PTHR23283	$\"[122-377]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF34	$\"[122-377]T$	TWO COMPONENT SENSOR HISTIDINE KINASE (PHOR)
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","BeTs to 15 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","***** IPB004358 (Bacterial sensor protein C-terminal signature) with a combined E-value of 1.5e-25. IPB004358A 304-318 IPB004358B 322-332 IPB004358C 339-357 IPB004358D 363-376***** IPB003661 (Histidine kinase A, N-terminal) with a combined E-value of 2e-16. IPB003661A 157-169 IPB003661B 308-327","","","-51% similar to PDB:2C2A STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN (E_value = 6.2E_24);-54% similar to PDB:1BXD NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ (E_value = 8.6E_10);","Residues 153 to 219 (E_value = 4e-19) place ANA_2547 in the HisKA family which is described as His Kinase A (phosphoacceptor) domain.Residues 264 to 378 (E_value = 7.3e-44) place ANA_2547 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","protein (PhoR1)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2548","2743242","2743958","717","5.48","-5.31","26805","GTGGGCGGCCCGACGCGGATCCTCCTGGTCGAGGACGAGGAGAACTTCCGCGACCCACTCGCCTACGGGCTGCGGCGCGACGGCTTCGAGGTGGTCGAGGCCGAGGACGGCCAGCGCGCCGTCGAGATCTTCGAGGCCTCCCGGCGCCCCGGCGGCGTCGGCCCCATTGACCTGGTCCTGCTGGACCTCATGCTGCCCCGCCTGGACGGGACCGAGGTGTGCACCCGGATCCGGCGCTCCTCCTCCGTGCCGGTCATCATGCTCACCGCCAAGGACACCGAGCTGGACAAGATCGTCGGCCTGGAGATCGGGGCCGACGACTACGTCACCAAGCCCTACTCCTACCGGGAGCTCCTGGCGCGCCTCAAGGCGGTTCTGCGTCGTAGCCGCGCGGCCGCCCCGGAGCCCGAGCCGGTGCTGGTCGCCGGCGGGGTGCGGATGGACGTCGAGCGCCACGAGGTCAGGGTCGACGGCGAGGTGGTCGCCATGCCGCTGCGGGAGTTCGAGCTCCTCGAGCTGTTTCTGCGTCACCCCGGCCGCGTGCTCACCCGCAGCCAGATCCTGGAGCGGCTGTGGGGGCCCGATTACGAGGGCGACACGAAAACTCTGGACGTCCATATCAAACGGCTCCGGGGCCGGATTGAGGTCGACGCCTCCAAACCGGTTCTCATCACCACGGTCAGGGGTCTCGGCTATCGCCTGGACTGGGATTCGTAG","VGGPTRILLVEDEENFRDPLAYGLRRDGFEVVEAEDGQRAVEIFEASRRPGGVGPIDLVLLDLMLPRLDGTEVCTRIRRSSSVPVIMLTAKDTELDKIVGLEIGADDYVTKPYSYRELLARLKAVLRRSRAAAPEPEPVLVAGGVRMDVERHEVRVDGEVVAMPLREFELLELFLRHPGRVLTRSQILERLWGPDYEGDTKTLDVHIKRLRGRIEVDASKPVLITTVRGLGYRLDWDS$","Two-component system response regulator","Cytoplasm","response regulator of two-component system","DNA-binding response regulator RegX3","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[6-127]T$	Q8G7F0_BIFLO_Q8G7F0;
PF00072	$\"[5-123]T$	Response_reg
SM00448	$\"[5-122]T$	REC
PS50110	$\"[6-126]T$	RESPONSE_REGULATORY

InterPro
IPR001867
Domain

Transcriptional regulatory protein, C-terminal
PD000329	$\"[147-233]T$	Q6NJL0_CORDI_Q6NJL0;
PF00486	$\"[157-234]T$	Trans_reg_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[6-139]T$	no description
PTHR23283	$\"[6-130]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21	$\"[6-130]T$	TWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)

","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a HTH DNA-binding domainFunctional Class: T,KThe phylogenetic pattern of COG0745 is -----QVCEBRHUJ----inXNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-55% similar to PDB:2GWR Crystal structure of the response regulator protein mtrA from Mycobacterium Tuberculosis (E_value = 1.8E_33);-51% similar to PDB:1YS6 Crystal structure of the response regulatory protein PrrA from Mycobacterium Tuberculosis (E_value = 8.0E_29);-51% similar to PDB:1YS7 Crystal structure of the response regulator protein prrA comlexed with Mg2+ (E_value = 8.0E_29);-68% similar to PDB:1NXO MicArec pH7.0 (E_value = 3.1E_25);-68% similar to PDB:1NXP MicArec pH4.5 (E_value = 3.1E_25);","Residues 36 to 154 (E_value = 1.2e-37) place ANA_2548 in the Response_reg family which is described as Response regulator receiver domain.Residues 188 to 265 (E_value = 1.2e-24) place ANA_2548 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal.","","regulator of two-component system","","1","","","Thu Aug 9 14:59:55 2007","","Thu Aug 9 14:59:55 2007","","","Thu Aug 9 14:59:55 2007","Thu Aug 9 14:59:55 2007","Thu Aug 9 14:59:55 2007","","","Thu Aug 9 14:59:55 2007","","","Thu Aug 9 14:59:55 2007","Thu Aug 9 14:59:55 2007","","","Thu Aug 9 14:59:55 2007","Thu Aug 9 14:59:55 2007","","","","","yes","","" "ANA_2549","2744107","2744589","483","5.20","-5.55","17921","ATGACCTATGAAGTCGGTGAGACTGTCGTTTACCCGCACCACGGGGCCGCCCGGATCATTGACATCCGGCAGCGCAAGGTACGCGGTGAGGAGAAGACGTATCTGCAGCTCGAGGTGGCCCAGGGTGACCTGACCATCTTGGTTCCCGCCGAAAGCGTTGAGCTCATCGGTGTCCGTGACGTGGTTGATGAGACCGGCTTGGAAAAGGTCTTCGAGGTGCTGCGGGCACCGCTGACCGAGGAGCCCACGAACTGGTCTCGCCGTTTCAAGGCCAACCAGGAGAAGATCGCCTCCGGGGACGTCATCAAGGTCGCCGAGGTCGTGCGGGACCTATCCCGCCGGGACACGGACCGCGGCCTGTCCGCCGGCGAGAAGCGCATGCTCGCCAAGGCCCGCCAGATTCTCGTCTCCGAGCTGGCTCTGGCCCAGAAGACCCCTGAGGAGGAGGCCGAGTCCCGCCTGGACGAGGTCCTCGCCTCCTAG","MTYEVGETVVYPHHGAARIIDIRQRKVRGEEKTYLQLEVAQGDLTILVPAESVELIGVRDVVDETGLEKVFEVLRAPLTEEPTNWSRRFKANQEKIASGDVIKVAEVVRDLSRRDTDRGLSAGEKRMLAKARQILVSELALAQKTPEEEAESRLDEVLAS$","Transcriptional regulator, CarD family","Cytoplasm","Transcriptional regulators, similar to M.xanthus CarD","K07736 CarD family transcriptional regulator","transcription factor CarD","","Nicolas F.J., Cayuela M.L., Martinez-argudo I.M., Ruiz-vazquez R.M., Murillo F.J. High mobility group I(Y)-like DNA-binding domains on a bacterial transcription factor. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(14):6881-6885. PMID: 8692912","","","

InterPro
IPR003711
Domain

Transcription factor CarD
PF02559	$\"[2-112]T$	CarD_TRCF

","BeTs to 7 clades of COG1329COG name: Transcriptional regulators, similar to M. xanthus CarDFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1329 is -------q-dr-b--------jx-t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-46% similar to PDB:2EYQ Crystal structure of Escherichia coli transcription-repair coupling factor (E_value = );-50% similar to PDB:1EG0 FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME (E_value = );-50% similar to PDB:1QD7 PARTIAL MODEL FOR 30S RIBOSOMAL SUBUNIT (E_value = );-50% similar to PDB:1RIP RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR (E_value = );-48% similar to PDB:1RKT Crystal structure of yfiR, a putative transcriptional regulator from Bacillus subtilis (E_value = );","Residues 2 to 112 (E_value = 7.1e-32) place ANA_2549 in the CarD_TRCF family which is described as CarD-like/TRCF domain.","","regulators, similar to M. xanthus CarD (carD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2550","2744641","2745486","846","5.51","-5.08","28116","GTGAGCATCAGCCCTTCATCCCAAGCATCCGCCCCGCCCGAGTCCGCTCCGGGTGGGGCGGTCGCTGTTCTCACCGCGGCGGGCTCCGGGTCTCGCCTGGGCGCCGGGGTCCCCAAGGCCCTCGTCCCGGTGGGTGGTGTCAGCCTCCTGCGGCGGGCGGCGGCCGGGCTTATCGCCTCGGGCGCCGTCAGCCACGTCGTCGTCACCGCCCCCGCTGAGGAGGTCGACCGGTTCCGCGCCGAGCTCGAGGGCCTGCCGGACGGATCGGTCGGGGCCTCGGCGGGCCGACGTGGTGAGATCGAGGTTGTTGCCGGCTCGCCCCGCTCCCGGCAGGCCTCTGTGGCCCTTGGGCTCGCAGCGGCCCTGGCCGCCGTGCCGCAGGCCGACGTCGTCATCGTTCACGACGCCGCGCGGGCGCTGACACCGCCGGAGGTGACGCAGCGGGTGGTCGCGGCCGTGCGGGCCGGACACGAGGCCGTGGTCCCGGCGCTGCCCGTGACCGATACCGTCAAGGAGGTCGAGGTCCGCCGGGCGGGGGAGCCCGAGCCCGTCGTCGGCACCCCCCGACGCGACCGGCTCCGGGCGGTCCAGACCCCCCAGGGATTCTCGACCCCCGTGCTCGTCGCCGCCCACCGGGCTGGGGCCGAGCGGGCCGGAGATGAGACGCTCGCCGCCTCCGACGACGCCGGTCTGGTCGAGGCCTGCGGCGGCAGCGTCGTCGTCGTCGCCGGTGACGAGCGCGCCATGAAGGTGACCACGCCCATGGATCTGGCCCTGGCTGAGCTGCTCCTGGAGCGGCAGTCCGCTCAGGAGAAGCGCCCTACCGAGACCGGTGGGGAGAACTGA","VSISPSSQASAPPESAPGGAVAVLTAAGSGSRLGAGVPKALVPVGGVSLLRRAAAGLIASGAVSHVVVTAPAEEVDRFRAELEGLPDGSVGASAGRRGEIEVVAGSPRSRQASVALGLAAALAAVPQADVVIVHDAARALTPPEVTQRVVAAVRAGHEAVVPALPVTDTVKEVEVRRAGEPEPVVGTPRRDRLRAVQTPQGFSTPVLVAAHRAGAERAGDETLAASDDAGLVEACGGSVVVVAGDERAMKVTTPMDLALAELLLERQSAQEKRPTETGGEN$","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","Cytoplasm, Membrane","2-C-methyl-D-erythritol 4-phosphatecytidylyltransferase","4-diphosphocytidyl-2C-methyl-D-erythritol synthase ","2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","","","","","

InterPro
IPR001228
Domain

4-diphosphocytidyl-2C-methyl-D-erythritol synthase
PF01128	$\"[20-266]T$	IspD
TIGR00453	$\"[21-264]T$	ispD: 2-C-methyl-D-erythritol 4-phosphate c
PS01295	$\"[131-138]T$	ISPD

InterPro
IPR008233
Family

4-diphosphocytidyl-2-methyl-D-erythritol synthase
PIRSF006765	$\"[20-271]T$	4-diphosphocytidyl-2-methyl-D-erythritol synthase

noIPR
unintegrated

unintegrated
G3DSA:3.90.550.10	$\"[13-273]T$	no description

","BeTs to 15 clades of COG1211COG name: 4-diphosphocytidyl-2-methyl-D-erithritol synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1211 is ----k--qvdr-bcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB001228 (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) with a combined E-value of 2.5e-49. IPB001228A 23-39 IPB001228B 106-118 IPB001228C 131-141 IPB001228D 159-173 IPB001228E 187-207 IPB001228F 226-261","","","-41% similar to PDB:1VGW Crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol synthase (E_value = 7.7E_14);-41% similar to PDB:1VGZ Crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol synthase (E_value = 7.7E_14);-40% similar to PDB:1I52 CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS (E_value = 4.2E_12);-40% similar to PDB:1INI CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHETASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS, COMPLEXED WITH CDP-ME AND MG2+ (E_value = 4.2E_12);-40% similar to PDB:1INJ CRYSTAL STRUCTURE OF THE APO FORM OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHETASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS (E_value = 4.2E_12);","Residues 20 to 266 (E_value = 5.6e-53) place ANA_2550 in the IspD family which is described as Uncharacterized protein family UPF0007.","","4-phosphate cytidylyltransferase (ispD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2551","2745473","2746993","1521","9.20","5.38","53292","GTGGGGAGAACTGACGATCAGGTCGGTTCCCTTTTCGGTACCGCCACCGGCCCGAATGGCCCTATCGTCTCTCCCATGAGCACGACAGTGACTGCTCCGACGCAGGCCGGCTCCCGCACCCGGCTCCTGTCCTGGCCCGTCATCGCCTGGGGCCTGTGGGACTGGGGGTCGGCGGCCTTCAACGCGGTCATCACCACCTTCGTCTTCACCGTCTACCTGGTCAGCGACGCCTTCGGGGCCAAGGCGGACAACGAGTCGGCGCTGTCCCTCGGGCTGGCCATCGCCGGCCTGTTCATCGCCCTGCTGGCGCCGGTGACCGGGCAGCGCTCGGACCGGGGCGGGCGAACCGTCTTCTGGCTCGGGGGCTACACCGCGGTGGTGGTGGCGGTCTCGGCGGCCCTGTTCCTGGTGCGGCCCGAGCCCGGCTACCTGTGGTTCGGCATCGTCCTGCTGGGGGTCGGCAACATCTTCTTCGAGCTGGCCTCGGTCAACTACAACGCCATCCTCAACCACCTGGCCCCCAAGGACCGCATCGGTGCCGTCAGCGGGCTGGGGTGGGGGATGGGCTACCTCGGTGGCATCGTCCTGCTGCTCATCCTCTACGTCGCTCTCGTGGGGCCGAGTCCCCTGGTCTCCTTCGCGGCCGGAAGCGGGATGGGGGTACGCGTCGCCATGCTCGTGTCGGCGGCCTGGTTCGGCCTGTCCGCCCTTCCCGTCCTCATCAACCGCTCCCGCAGGCTCGGGCGCTCCCGCGCCGAGCACGTCGCGGAGGTCGGTGAGGGGATGGCGACTGCCGAACCGGGACGGGACCGGGCCGCCATGGAGGCCGAGCCGGTGGAGGCCGTCTCCCACCAGGGCAGGCGCAAGGAGTCGATCCTGACCTCCTACAAGCTGCTGTGGCGCACCCTGCTCCAGCTGCACCACTTCCAGCCGCGCCTGCTGTGGTTCCTGCTGGCCGCCGCCGTCTTCAGGGACGGGCTGGCCGGGGTCTTCACCTACGGCGGCATCATTGCCCAGAACACCTTCGGCTTCTCATCGGGCGACGTCATCATCTTCGCCATCGTGGCCAACATCGTGGCCGGCATCGCCACCATCTGGGCCGGGCGGCTCGATGACCGCTTCGGGCCGCGCAACGTCATCATGGCCAGCCTCAGCATTCTGGTGGTGGCTGGACTGCTGGTGTTCTTCCTGCACTCCGCCGGGACCGTGGCCTTCTGGGGGCTGGGCCTGCTCCTGTCGGCCTGCGTGGGGCCGGCCCAGTCAGCCGCCCGGTCCTTCCTGGCCCGCCTCATCCCCGAGGGGCAGGAGGGCGAGATCTTCGGGCTCTACGCGACCACCGGGCGGGCGGTGTCCTTCATGGCGCCCGCGATGTACGGCATCTTCATCTATCTGGGCACGCGCATCGTCGGGCCGGGGGCGAACTACTGGGGGATCCTCGGGATCGTCGCGGTGCTGGCCACGGGACTGCTCCTCATGCTGCGCGTGGGCAACCCCGTCGCCGAGGAGGAGTCGGCCGCGTAG","VGRTDDQVGSLFGTATGPNGPIVSPMSTTVTAPTQAGSRTRLLSWPVIAWGLWDWGSAAFNAVITTFVFTVYLVSDAFGAKADNESALSLGLAIAGLFIALLAPVTGQRSDRGGRTVFWLGGYTAVVVAVSAALFLVRPEPGYLWFGIVLLGVGNIFFELASVNYNAILNHLAPKDRIGAVSGLGWGMGYLGGIVLLLILYVALVGPSPLVSFAAGSGMGVRVAMLVSAAWFGLSALPVLINRSRRLGRSRAEHVAEVGEGMATAEPGRDRAAMEAEPVEAVSHQGRRKESILTSYKLLWRTLLQLHHFQPRLLWFLLAAAVFRDGLAGVFTYGGIIAQNTFGFSSGDVIIFAIVANIVAGIATIWAGRLDDRFGPRNVIMASLSILVVAGLLVFFLHSAGTVAFWGLGLLLSACVGPAQSAARSFLARLIPEGQEGEIFGLYATTGRAVSFMAPAMYGIFIYLGTRIVGPGANYWGILGIVAVLATGLLLMLRVGNPVAEEESAA$","Permease of the major facilitator superfamily","Membrane, Cytoplasm","Permeases of the major facilitator superfamily","K06902 MFS transporter; UMF1 family","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[313-506]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[218-463]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[22-41]T$ $\"[89-202]T$ $\"[218-257]T$ $\"[297-502]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
tmhmm	$\"[60-80]?$ $\"[86-106]?$ $\"[116-136]?$ $\"[146-168]?$ $\"[183-215]?$ $\"[221-241]?$ $\"[314-336]?$ $\"[342-364]?$ $\"[379-399]?$ $\"[405-425]?$ $\"[440-462]?$ $\"[472-492]?$	transmembrane_regions

","BeTs to 3 clades of COG2270COG name: Permeases of the major facilitator superfamilyFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2270 is ------yq--r-b--------j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-47% similar to PDB:1RE5 Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida (E_value = );","Residues 53 to 463 (E_value = 5.9e-17) place ANA_2551 in the MFS_1 family which is described as Major Facilitator Superfamily.","","of the major facilitator superfamily (AL133213)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2552","2748426","2747842","585","9.10","4.11","21152","GTGGGACCTCGCGAGGCTTGGGCCCGCGGTTCGGATTTCCGAACCGCGGGCCGAGTCCTTTCTCGGACCCGGTGGCACACCCCTTCCAGGCCCCGCTCTCGCGCTATGAGAGAACTCGTGGGGACCGCGGCCGGCCAAGCGCGTCAGGATAGGGGCATGACTGACTCCGCCGACTCAGCACAGCCCGTCTTCTCCTGTCGCTCCACCGCTCGTGTGAGCACGGACCGCCCCTCCCGATACGGCAAGCAGCTGGCCTCTCACATGGGCCGCAAGATCACCGCCGCTTGGGATGAGGCCGCCCAGACCGGCTCCCTGTCCTTTGACCGTGAGGGGGCAGTCACCGGCGTCGTCGAGATCTCCTGTCACGATGGCATCCTCCAGCTCGACCTGGCCGCCGACGACGCGCACCTCGAACGCCTCGAGCAGGTCACCGGAATCCACCTGGCCCGCTTCGGAGCCAAAGAGGGTCTTGTCGTGAGCTGGATCCGTCAGGACGGGAGTCCCGGGACCACCCAGGGGCCGCTGACTCCGGAGGATCTTGAGCGCATGCGCGCCGAGCGCGAGGCCCGCCAGGCCTCCTCGTGA","VGPREAWARGSDFRTAGRVLSRTRWHTPSRPRSRAMRELVGTAAGQARQDRGMTDSADSAQPVFSCRSTARVSTDRPSRYGKQLASHMGRKITAAWDEAAQTGSLSFDREGAVTGVVEISCHDGILQLDLAADDAHLERLEQVTGIHLARFGAKEGLVVSWIRQDGSPGTTQGPLTPEDLERMRAEREARQASS$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG3553COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3553 is ---------------fg----j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-41% similar to PDB:1N8J Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S) (E_value = );-41% similar to PDB:1YEP Structural and biochemical analysis of the link between enzymatic activity and olgomerization in AhpC, a bacterial peroxiredoxin. (E_value = );-41% similar to PDB:1YEX Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin. (E_value = );-41% similar to PDB:1YF0 Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin. (E_value = );-41% similar to PDB:1YF1 Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin. (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2553","2749031","2748702","330","4.47","-6.09","11487","ATGCTCGTGACCACCACCCCCACCGTCGAGGGATACCCCGTGACCCAGTACCTGCGAGTCGTCTGCGGTGAGACCATCGCCGGAGTCAACGCCCTCAAGGACATGGCGGCCGGGTTCCGCAACCTTGTGGGCGGTCGTTCCCAGACCTATGAGGCCGAGCTCGTCCAGGCCCGTGAGAGCGCCCTGGCGGAAATGGTGCAGCGCGCCCAGGAGCTCGGCGCTGAAGGCATCGTCGGCGTCGACATCGACTACGAGACGCTGGGCTCTGATAACGGCATGCTCATGGTGACCGCCTCGGGCACCGCAGTGCGGTTCTCCCCAGTCTCCTGA","MLVTTTPTVEGYPVTQYLRVVCGETIAGVNALKDMAAGFRNLVGGRSQTYEAELVQARESALAEMVQRAQELGAEGIVGVDIDYETLGSDNGMLMVTASGTAVRFSPVS$","Uncharacterized conserved protein","Cytoplasm, Periplasm","Domain of unknown function DUF74","hypothetical protein","protein of unknown function DUF74","","","","","

InterPro
IPR002765
Family

Protein of unknown function DUF74
G3DSA:3.30.110.70	$\"[1-105]T$	no description
PF01906	$\"[1-106]T$	DUF74

","BeTs to 12 clades of COG0393COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG0393 is aompk---v-rlbce-gh---j----Number of proteins in this genome belonging to this COG is 1","***** IPB002765 (Protein of unknown function DUF74) with a combined E-value of 9.1e-39. IPB002765A 1-23 IPB002765B 41-82 IPB002765C 93-103","","","-70% similar to PDB:1Y2I Crystal Structure of MCSG Target APC27401 from Shigella flexneri (E_value = 2.6E_26);-72% similar to PDB:1VR4 Crystal Structure of MCSG TArget APC22750 from Bacillus cereus (E_value = 1.8E_22);-72% similar to PDB:2GTC Crystal structure of the hypthetical protein from Bacillus cereus (ATCC 14579). Northeast structural genomics Target BcR11 (E_value = 1.8E_22);-62% similar to PDB:1BSH SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX (E_value = 1.8E_22);-62% similar to PDB:1BSN SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX (E_value = 1.8E_22);","Residues 1 to 106 (E_value = 4.1e-53) place ANA_2553 in the DUF74 family which is described as Domain of unknown function DUF74.","","of unknown function DUF74 (pXO2)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2554","2749741","2749076","666","10.75","13.96","24766","ATGCACGGCCCGAAGACCCCAGCGTCCCGCAGCCACTGCCCGATCAGGAGCCGACGGGAGGCGATACGCCCCACAGCACCGCCGTCGTCCGGGAAGACCGCCGTCGCATACCGTGGGCCCGTGAATCTTCCCGACGTCCTGAGCCTGGCGCATTCCCTCATGGAGGAGGCCGACGTCGGCGACTGGGACCTGGCCTTCGACCGGGCGCGTCGGCGGGCCGGCCAGACGGATCATGCTCGACGTCGGATCACGCTCAGCCGCCACCTCATGAGCCTGTACGACGAGACCCAGGTCCGCGAGACGATCCTGCACGAGATCGCCCACGCCCGCGTCGGCCCCAGCCACGGGCACGACGCCGTCTGGGCCGCCGAGGCGACCCGGTTGGGGGCGACGGGCCGGCGGCTCATTGACGCCCAGGCCCCGCGACTGCGGGGACGCTGGGTGGGCAGGTGCCCGGCGGGCCACGAGGTGGACCGCATGCGCCGCCCGGCCTCACCCGTCTCCTGCTCGCGCTGCTCCCCTCGATTCAACCTGGAGCACCTCCTGACGTGGAGCCTCGACGGAGAACCTGTCCCCCATGCGCGGATCAGCGATCGCTACAGCCGCCTGCTGCATCTGGCCAGGCAGGCCGCCACCAGGTCACAAGAAGATTTCACCACCCTGTAG","MHGPKTPASRSHCPIRSRREAIRPTAPPSSGKTAVAYRGPVNLPDVLSLAHSLMEEADVGDWDLAFDRARRRAGQTDHARRRITLSRHLMSLYDETQVRETILHEIAHARVGPSHGHDAVWAAEATRLGATGRRLIDAQAPRLRGRWVGRCPAGHEVDRMRRPASPVSCSRCSPRFNLEHLLTWSLDGEPVPHARISDRYSRLLHLARQAATRSQEDFTTL$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-52% similar to PDB:2AO2 The 2.07 Angstrom crystal structure of Mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions (E_value = );-52% similar to PDB:2F6L X-ray structure of Chorismate Mutase from Mycobacterium Tuberculosis (E_value = );-52% similar to PDB:2FP1 Secreted Chorismate Mutase from Mycobacterium tuberculosis (E_value = );-52% similar to PDB:2FP2 Secreted Chorismate Mutase from Mycobacterium tuberculosis (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2555","2749770","2750888","1119","9.20","11.16","39407","ATGTCCCACCATCCCTCCGGCCGGCGTCCGCGGCCCCAACGAAGCACTGTAGGATCCGGATCGCCCCAGCCCGCACGAGCTCCGCGCAGCGGCCGTCCGACCGCGCAGCGCGGTACTGACCGTGCCCGGCGGGAGGATGCGAGTCACCGTCCCGGGCGGGGGAAGGGGAGTCGAGGAGGCCGTGGGCGCCTCGGGCTCCTGCGTGCCGGTGTCAGATGGCGGCGGGGGCGCAGGGGCGGTTCCGTTCGGTCCTTCCTGAGAAGCCCGATCGGCGTTGTCCTGGCCGCCTTCCTGGTCACGCTCCTGGTGGGACTCCTCGTGCTGCGTACCACCGGTTCCTCCCTCGGCGGCCTCGCACTGGGGTGGGGGCGGGACGCTGATGCCGGGACGCGTTCCGCTCCGGCACCCCTGGTGCCCGACGCCAGCGGCTTCAACGCCGCCCGCATCATCGATGACGAGGTCTTCTACGACTCCCAGGCCATGACGCGCGAGGAGATCGCCGCTTTCGTTACCAAGGTCAATGCCGGCTGCCAGCCGGGCAGTGATGGCACCCAGTGCCTGGCCGCCGCCACCTTCTCCGTGCAGGCCCGCCAGGCCAGCACCTTCTGCCCCGGTGACATCAAGGCCGCCTCCGGCGTCAGTGCGGCCGACGTCATCTGGGAGGTCTCCCAGGCCTGCGACATCAATCCCCAGGTGCTCCTCGTGCTCATTCACAAGGAGCAGGGACTGCTCACCGCCTCCGGCGAGAACCTGAGTGCTCGCGACTACGAGGCCGCAGCCGGGTACGCCTGCCCTGACTACGGGGCCTGCGACCCCCAGTGGGCAGGCTTCCCCTCCCAGCTCTACGGGGCGGCCTCCCAGTTCCATCGCTACCGTCTTGATCCGGGTGGCTACGACGTCGTGGCGCAGCAGCCCAGACGTATCGCCTACTCGCCAGATGTGCTGTGCGGCAGCGGTGAGGTGACGGTGGCCAATCAGGCGACCGCCGGCCTGTACAACTACACGCCCTTCCAGCCCAATGAGGCCGCCGCACATGGTGGGGACCAGTGCACCTCGTGGGGCAACTGGAACTTCTACGGCTACTTCAAGACGCTCTTCGGAAGTCCGACATCAGATTAA","MSHHPSGRRPRPQRSTVGSGSPQPARAPRSGRPTAQRGTDRARREDASHRPGRGKGSRGGRGRLGLLRAGVRWRRGRRGGSVRSFLRSPIGVVLAAFLVTLLVGLLVLRTTGSSLGGLALGWGRDADAGTRSAPAPLVPDASGFNAARIIDDEVFYDSQAMTREEIAAFVTKVNAGCQPGSDGTQCLAAATFSVQARQASTFCPGDIKAASGVSAADVIWEVSQACDINPQVLLVLIHKEQGLLTASGENLSARDYEAAAGYACPDYGACDPQWAGFPSQLYGAASQFHRYRLDPGGYDVVAQQPRRIAYSPDVLCGSGEVTVANQATAGLYNYTPFQPNEAAAHGGDQCTSWGNWNFYGYFKTLFGSPTSD$","Hypothetical protein","Membrane, Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[85-105]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-40% similar to PDB:1VRQ Crystal Structure of Heterotetrameric Sarcosine Oxidase from Corynebacterium sp. U-96 in complex with Folinic Acid (E_value = );-40% similar to PDB:1X31 Crystal Structure of Heterotetrameric Sarcosine Oxidase from Corynebacterium sp. U-96 (E_value = );-38% similar to PDB:1HD5 ENDOGLUCANASE FROM HUMICOLA INSOLENS AT 1.7A RESOLUTION (E_value = );-38% similar to PDB:2ENG ENDOGLUCANASE V (E_value = );-38% similar to PDB:3ENG STRUCTURE OF ENDOGLUCANASE V CELLOBIOSE COMPLEX (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2556","2751315","2752841","1527","7.36","1.77","56855","ATGACGCTACCGCCGGTACTGGCGACCACCTGGGTCGTCATCGAGTACCTCATCAAGATCGCCGCGCTGGGCACGGTTCCGGAGAACCGCCGCCCGTCGTCGTCGACCGCCTGGCTGCTGCTCATCTTCCTGCTGCCCCTCGTGGGACTCCCGCTCTACCTGCTCATCGGCAGCCCGTGGGTCCACGGCACGCGCCGCCGCCAGCAGCACACCGTCAACGAGATCACCCTCGACTACACCCGCGCCATGCCCGACCTGCCCAAGGGGGCCCGGCCCTCGACCTACCTGGCCGGAGCGCTGCGCATGAACCGCCAACTCACTGGCCTGCCCTGCGTCAGCGGTGAAGTGGTGGCCGTCCACGCCGACCCCCGCAGCGCCTACGAAGCCATGGCCCGAGCCATTGACTCCGCCACCGACCACGTCCACGTCGAGTTCTACATCATGAGCTGGGACGAGGTCACCGACGTCTTCTTCACCGCCCTGGAGCGCGCGGTGGCCCGCGGAGTCACGGTGCGACTCCTCCTGGACCACCTGGGCAGCCGCAAGTACCCCGGCTGGAAGCAGTTCTGCCAGCGCATGACCGACGCCGGCATCCGCTGGCGCCTCATGATGCCGCTGCTTCCGCTCAAGCGCCGCTGGCGCCGCCCGGACCTGCGCAACCACCGCAAGATCCTGGTCATCGACGGCGAGAAGGGCTTCATCGGCAGCCACAACGTCATCGACCCCTCCTACCGGACCCGGCGCAACGTGCGGGCCGGGCGCCGCTGGGAGGACCTGTCCGTGGAGGTCACCGGCGAGATCGTCCTGGAGGCCCAGGCCATCTTCGCCATGGACTGGTTCTTCGAGGCCGGCGAGCAGCTCGAGGCCTTCGACCTGGCGCTGGGAACTCCGGCCGAGACCCTGCCGGAGATGGCGGGACTGCCGGGAATCCCGGTGGGCACACCGGCCCCCAGACCCGGGCGCCCGGGCGCCGTCGTCAACGCCATGCAGCTCATTCCCTCCGGGCCGGGGTACCCCACCGAGCCGAACCTGCGGATGTTCCTGGCCCTCATCCACGGGGCCAAGCGGCACGTGTCCATCACCAGCCCCTACTTCATTCCCGACGAGGCGCTGCTGGCGGCGATGACCTCGGCCGCCTACCGGGGGGTGGAGGTCGAGCTGTTCGTGGGCAAGGAGTCCGACCAGTTCATCGTCAGTCACGCCCAGCGCTCCTACTACTCGGCGCTCCTGGCGGCAGGGGTGCGGATCTACCTCTACCCCTCGCCGATCGTCCTGCACTCGAAGTACATGACGGTCGACGACGAGGTCGGGGTCATCGGCTCGTCCAACATGGACTTCCGTTCCTTCGCCCTCAACTACGAGGTCATGCTGCTGGCCTTCGGCGGGGACCTCGACGACCTGCTGCGCAACAACGACGCCGCCTACCGGGCTGCCTGCACCGAGCTGACCCCCGAGCTGTGGGCCACCGAGCCCTGGTACAACCGCTACGTGGACAACGTCTGCCGCCTCATGTCCGCAGTGTTGTGA","MTLPPVLATTWVVIEYLIKIAALGTVPENRRPSSSTAWLLLIFLLPLVGLPLYLLIGSPWVHGTRRRQQHTVNEITLDYTRAMPDLPKGARPSTYLAGALRMNRQLTGLPCVSGEVVAVHADPRSAYEAMARAIDSATDHVHVEFYIMSWDEVTDVFFTALERAVARGVTVRLLLDHLGSRKYPGWKQFCQRMTDAGIRWRLMMPLLPLKRRWRRPDLRNHRKILVIDGEKGFIGSHNVIDPSYRTRRNVRAGRRWEDLSVEVTGEIVLEAQAIFAMDWFFEAGEQLEAFDLALGTPAETLPEMAGLPGIPVGTPAPRPGRPGAVVNAMQLIPSGPGYPTEPNLRMFLALIHGAKRHVSITSPYFIPDEALLAAMTSAAYRGVEVELFVGKESDQFIVSHAQRSYYSALLAAGVRIYLYPSPIVLHSKYMTVDDEVGVIGSSNMDFRSFALNYEVMLLAFGGDLDDLLRNNDAAYRAACTELTPELWATEPWYNRYVDNVCRLMSAVL$","Cardiolipin synthase","Cytoplasm, Membrane, Extracellular","cardiolipin synthetase","cardiolipin synthase ","phospholipase D/Transphosphatidylase","","Thatcher T.H., Gorovsky M.A. Phylogenetic analysis of the core histones H2A, H2B, H3, and H4. Nucleic Acids Res. 1994. 22(2):174-179. PMID: 8121801Doenecke D., Gallwitz D. Acetylation of histones in nucleosomes. Mol. Cell. Biochem. 1982. 44(2):113-128. PMID: 6808351Ebralidse K.K., Grachev S.A., Mirzabekov A.D. A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA. Nature 1988. 331(6154):365-367. PMID: 3340182","","","

InterPro
IPR001736
Domain

Phospholipase D/Transphosphatidylase
PF00614	$\"[216-243]T$ $\"[421-448]T$	PLDc
SM00155	$\"[216-243]T$ $\"[421-448]T$	PLDc
PS50035	$\"[216-243]T$ $\"[421-448]T$	PLD

InterPro
IPR001951
Family

Histone H4
PS00047	$\"[353-357]?$	HISTONE_H4

InterPro
IPR015679
Family

Phospholipase D
PTHR18896	$\"[422-452]T$	PHOSPHOLIPASE D

noIPR
unintegrated

unintegrated
G3DSA:3.30.870.10	$\"[112-256]T$ $\"[340-461]T$	no description
PIRSF006046	$\"[1-508]T$	Cardiolipin synthase
PTHR18896:SF10	$\"[422-452]T$	PHOSPHOLIPASE D
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[37-57]?$	transmembrane_regions

","BeTs to 11 clades of COG1502COG name: Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthases and related enzymesFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1502 is a--p--y-v--lbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 1","***** IPB001736 (Phospholipase D/Transphosphatidylase) with a combined E-value of 3.2e-16. IPB001736A 161-171 IPB001736B 228-246 IPB001736D 424-449","","","No significant hits to the PDB database (E-value < E-10).","Residues 216 to 243 (E_value = 2.4e-05) place ANA_2556 in the PLDc family which is described as Phospholipase D Active site motif.Residues 421 to 448 (E_value = 8.4e-07) place ANA_2556 in the PLDc family which is described as Phospholipase D Active site motif.","","synthetase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2556.1","2753598","2752981","618","9.97","7.41","22961","ATGAGTCTACGCCCGATCATGGACGCTGGCCCTGGACTCAATTTTCTCTCCCTCAACAAGGAACGACTTCTTTTTGATACAGTCGGACCTCTCAGGGTACCCGAAAAAGTTGAGGAAGAAATTCTTCGCAAGTCACGTCAAGATCGTCGATTCTCTGCAGCCGAAAATGTCTGGCGAAGACTACCTGAGCGACTCCTTCAGGTACTTTCCGACGACTCCACTAACGAGGACCTCAGCCGAGCAGTTGGACGCATCAGCGGAACGTCGTTCGAACAGCGCATCCGCATTTCAAAGAATCTCGGAGAAGTCATGGTCATCTCACACGCCTCGGTCGCAGCTGAATCCGGAGAAAACGTCATCATTCTCATAGACGATTCAGGTGGTCGTCAGATCGCAGCAGTTGAAGCTAGAAGATTGGACCGGTTGCGCTTAATGGGAAAACCTGCAGGAAGCATTCGCTTGATTAGCACACTCACCGTACTCCAGAAGGCTGCAGGCAGGGAACACATCCCAAACAAGAAATCAATGAGAACATTATATTCACGGCTCAGGCAACTGGATGACGGCCTCGTCCCTATTGAACAAACCGGCCTATTGTCTTTACCGTGCTGGAAATGA","MSLRPIMDAGPGLNFLSLNKERLLFDTVGPLRVPEKVEEEILRKSRQDRRFSAAENVWRRLPERLLQVLSDDSTNEDLSRAVGRISGTSFEQRIRISKNLGEVMVISHASVAAESGENVIILIDDSGGRQIAAVEARRLDRLRLMGKPAGSIRLISTLTVLQKAAGREHIPNKKSMRTLYSRLRQLDDGLVPIEQTGLLSLPCWK$","Hypothetical protein","Cytoplasm, Periplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:21:17 2007","Wed Aug 15 20:21:17 2007","Wed Aug 15 20:21:17 2007","Wed Aug 15 20:19:25 2007","","","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","Wed Aug 15 20:19:25 2007","","Wed Aug 15 20:19:25 2007","","Wed Aug 15 20:19:25 2007","yes","","" "ANA_2556.2","2753921","2753595","327","4.40","-7.82","11959","ATGCAGATTTCGACACCACAGTTGGCAATACGCTTCGGCTGGAACGATCAGTACCGAGCACTCCAAAACAGCTCAGATTACACCCGCCCACCACAGCGCCTTCTGGCGCGAGCAATCGAGGGTTACGCTGAAGGCGTCATATCGTTGCAAACCCTCGCTACCCTCCGAGGTACTGCCATCGAAGTCGTCCAAGAAGACATCGCCTCGGCGGGGATCACTCCAGAACATATTACCATTCCTCAAATAGACGCAGATTATCTTTCTTCCACTCCAATCGACTGGGACGACATCTACGGAAATAGCATCCCACAGGACTCTATACAATGA","MQISTPQLAIRFGWNDQYRALQNSSDYTRPPQRLLARAIEGYAEGVISLQTLATLRGTAIEVVQEDIASAGITPEHITIPQIDADYLSSTPIDWDDIYGNSIPQDSIQ$","Hypothetical protein","Cytoplasm, Periplasm","","","","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-2]?$	signal-peptide

","BeTs to 3 clades of COG1482COG name: Phosphomannose isomeraseFunctional Class: GThe phylogenetic pattern of COG1482 is a---y-v-eBr-----o----Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:55 2007","Wed Aug 15 20:23:55 2007","Wed Aug 15 20:23:55 2007","Wed Aug 15 20:23:08 2007","","","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","Wed Aug 15 20:23:08 2007","","Wed Aug 15 20:23:08 2007","","Wed Aug 15 20:23:08 2007","yes","","" "ANA_2557","2754171","2754353","183","4.62","-4.74","6174","GTGAGCCAATTCGTGCGCCAATGTGCTGCGTTGGCGCATGGGGTTGCGTGTGCGTGCAATTCCGATGAAGGTGACATTGCGTGCGGGATCAGTCATGGTCAGCCCGTGTTCGTCGCGGTCAACGTCGAGGACTGCGACATCGTGGCCGGTGGTCTGTTCGACGAGCGCAATAAGATCGCCTAG","VSQFVRQCAALAHGVACACNSDEGDIACGISHGQPVFVAVNVEDCDIVAGGLFDERNKIA$","Hypothetical protein","Cytoplasm, Extracellular","lipoprotein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2558","2755516","2754809","708","10.14","10.54","26074","CTGCACCCATGCAGCGAGAGGCGGCAGGAAGATGAATATCGAGGACATCGAGGTCTTCATCGGCACCGGGCGTCGGCAAGGAGCGAGCACTGGGCCACTGCCCTGAGCCGGGAGGGTCGGAAGGTCTTCGACAGGGCCCTGCCCAACGATGAGGAGCGCCTGCGTGCTCTCTATGAGAAGCTGGCCGATCACGGGAGCCTGCTGGTGGTGGTCGATCAGCCGGCCACCATCGGGGCCCTGGCCGTGGCAGTGGCTCAGGACATGGGCATCACCGTGGGCTATCTGCCGGGACTGTCGATGCGACGCATCGCCGACCTGACACCGGGCAGCGCCAAGACCGATGCCAAGGACGCGGCCGTCATCGCCGGCGCGGCCAGGAGCATGCCTCACACCCTGAGAGCCATCAACGCCTCGGACGAGCACGCCGCGGCGCTGAGCATGCTGACTGGATTCGACCTGGACCTGGCCCACCAGGTCAACCAGAGCGCTAACCGGCTCCGGGGCCAGTCGTTCACGCAAGACCCCGCCCAGCCCTCGAGGCCGTGGTGGGGCCCTGGCCGGGCGCACGACGCCGTCTTGGAGGCCCGTCGTCGCCTGGCCCACCGCCGCTTGACACACCACATAGGGGCACCCCACCATCGGTTGCTGCTTCGTGATCCACCTGTCAGATACGGAACTAGAAGCCGCAGCGACCTCCAGCTAGAATGA","LHPCSERRQEDEYRGHRGLHRHRASARSEHWATALSREGRKVFDRALPNDEERLRALYEKLADHGSLLVVVDQPATIGALAVAVAQDMGITVGYLPGLSMRRIADLTPGSAKTDAKDAAVIAGAARSMPHTLRAINASDEHAAALSMLTGFDLDLAHQVNQSANRLRGQSFTQDPAQPSRPWWGPGRAHDAVLEARRRLAHRRLTHHIGAPHHRLLLRDPPVRYGTRSRSDLQLE$","Transposase","Cytoplasm","ISSfl4 orf","transposase","transposase, IS111A/IS1328/IS1533","","","","","

InterPro
IPR002525
Family

Transposase, IS111A/IS1328/IS1533
PF01548	$\"[85-170]T$	Transposase_9

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 153 to 247 (E_value = 6.4e-18) place ANA_2558 in the Transposase_9 family which is described as Transposase.","","orf ","","1","","","Thu Aug 9 15:08:38 2007","","Thu Aug 9 15:08:38 2007","","","Thu Aug 9 15:08:38 2007","Thu Aug 9 15:08:38 2007","Thu Aug 9 15:08:38 2007","","","","","","Thu Aug 9 15:08:38 2007","","","","Thu Aug 9 15:08:38 2007","Thu Aug 9 15:08:38 2007","","","","","yes","","" "ANA_2559","2760154","2755805","4350","6.62","-5.35","156529","GTGACCGGGATGATCGGCCACACCCAGCCGCGGCGCATTGCCGCGCGCAGCGTGGCCGAGCGGATCGCCTCCGAACTGGGCACCCCGATCGGACGTGACGGCGTCGTCGGCTACCAGGTGCGTTTCACCGAGGAGATCGGCGAGAACACCCTGGTCAAGCTCATGACCGACGGCATCCTGCTGGCGGAGATCCAGTCCGACCCCCAGCTGCGCCGCTATGACACGATCATCGTGGACGAGGCCCACGAGCGCAGCCTCAATATCGACTTCATCCTGGGCTACCTGGCGCGCCTGTTGCCCGAGCGCCCCGACCTCAAAGTCATCATCACTTCGGCCACCATCGACTCCGAGCGCTTCGCCGAGCACTTCGGCCGCGAGCAGATCGGCGACCGCGGGCAGCCCTTCACCGTCCCTGCCCCGGTCATCGAGGTCTCCGGACGCACCTACCCCGTTGAGGTGCGCTACCGCCCGCTAGCTCCCGACGACGCCCCTCCTGCCTCCGACGACGCCGGCAGCGAGCCGGCCAAGCCCGCCGCCGCGCCCCAGCCCGGCCCGGCGGGACCCGGAGAGCTGAGCGAGGCCGAACTGGAGGCCCTGACCTCGCCTGACCCGGCGGTGCGCGCCGCGGCCCGGGCCCGCCGCGAGGCCATCCGCTCCGGCGCCGGCCCCGCCGCGCTCGCGCCCCGCAACCAGGGGGCTCGTGGCAAGGGCCGGGGCCGAGCCGCCTCAACGGCCGCCGAGTCCGGAGAGCCCAAGGATCAGGTGACCGGGATCCTCGACGCCGTCGACGAGCTCCTGGGCGAGCCCAGCGGCGACATCCTCATCTTCCTGGCCGGTGAGCGCGACATCCGCGACACCGAGGCGGCCCTCATCGACCATTTGGGGGCGCGCTACACGCCCGACGGGCGCTCACGCACGCCGGGTGCCATTGAGGTCGTCCCCCTGTACTCGCGCCTGAGCGCCGCCGAGCAGCACCGGGTCTTCGAGACCCACCAGGCGCGCCGCATCGTCCTGGCCACGAACGTGGCCGAGACCTCCCTGACGGTTCCCGGGATCCGGTACGTCATCGACCCGGGCCTGGCGCGCATCTCCCGCTACTCCAACCGCACCAAGGTTCAGCGCCTGCCGATCGAGCCGGTCAGCCGGGCCAGCGCCAACCAGCGGGCGGGCCGTTGCGGGCGCGTGGCCGACGGCATCGCCATCCGCCTGTACTCGCAGGCCGACTTCGAGGCGCGCCCGGAGTACACCGAGCCGGAGATCCTGCGCACCTCGCTGGCCAGCGTCATTCTGCAGATGGCGGCCCTGGGGCTGGGGGCGGTGGAGGACTTCCCCTTCCTGGACGCCCCCGACTCCCGTCAGGTCCGCTCCGGCCTGCAGCTGCTCACGGAGATCGGCGCCATCGAGCCGGCCGGGGCCGCCTCCGCCCGCTCCGACGACGCCCCCGACCGGGGCCGGCGCGGGCCGCGCCTGACGGAGATCGGGCGGCGCCTGGCGCGCCTGCCCATCGACCCGCGTCTGGGGCGCATGCTCCTGGAGGCCGGTGAGCTGGGCTGTGTCGGGGAGGTCATGGTCATCGTGGCGGCCCTGTCCATCCAGGACGTGCGCGAGCGCCCGGCGGACAAGCAGGAGGCCTCCGACGCCCTGCACCGGCGCTTCGCGGACCCGACGAGTGACTTTCTGACCTACCTGAACCTATGGCGCTACCTGCGCACGCAGAGCCGCGAACTGTCCGGCTCGGCCTTCCGGCGCATGTGCCGGGCCGAGTTCCTGCACTACCTGCGGGTGCGCGAGTGGCAGGACGTCCACACCCAGCTGCGCCAGCTGGCCCGACCGCTGGGCCTGGACGCGGCCCCGGTGGAGCTGCCGACGGCCCGTTCGATCCGGGCGGCAACCGAGGCCCTGGAGCCGGGCAGCCATGCCGCCCAGATCGCCAACGGGGGTGTGGCGGCCGCTGTCGTGGCCCTGGGGCGCAGTGCGGACACGCCCGACGCCGATGCGATCCACCGCTCGCTGCTGGTGGGGCTGCTGTCCAATGTGGGGAACTGGGATGAGCGTCGTCGGGAGTACGCCGGCGCGCGCGGGACCCGTTTCACGATCTGGCCGGGCTCGGGCCTGCGCCGCAAGACCTACGACTGGGTGATGACCGCCGAGCTGGTGGAGACCTCCCGGCTCTTCGCCCGCACGGTGGCCAAGGTGGACTCCCGGTGGATCGAGCAGGTGGCGGACCGGGCGGGCCTGACCCGCCACGTCTTCGGTGAGCCCTACTGGTCGACCCGCCAGGGGGCGGCCATGGTTCACGAGAAGGTGCTGCTCTACGGGATGACGCTGGTGGCGGACCGGCCGGCGACGCTGGCGAGCGTGGGGACGGACTCGGCCCGCCAGGTGGCCCGGGAGATGTTCATCCGCTCGGGCCTGGTGGAGGGCGGCTGGCACGCCCGGCACGGCTTCGTGGAGCGCAACCGGGAGCTCATCGAGGAGCTTCAGGACGTGGAGCGGCGTCGGCGCGAGCACGGGCTGCTGGCCGACGACGCCGCCCTGTTCGACTTCTATGACGACCGGATCCCCGAGGAGGTGACCTCCGCGGCGGCCTTCGACGCCTGGTGGAAGGAGCAGCGGCGCACCACCCCGGACCTGCTGGACTTCACCCGCGAGCTGCTGCTGCCCGGCGGGGGCGACGCGAGCGGCTTCCCGGACACGTGGGTGCAGGGGGACCTGACCCTGGGCCTGGACTACGTGTTCGAGCCGGGCCACCCCGAGGACGGGGTCAGTGTCCAGGTGCCGGTGGAGGTGCTGGGGCGCCTGAGCCCGGAGGGCTTCGACTGGCTGGTGCCGGGGATGCGCCCCGAGCTGTGCGTGGCCACGATCCGGGCGCTGCCCAAGCGGGTGCGCCGCCAGCTGGTGCCGGCACCGGACGTGGGCGCCCAGGTGTGGGCACAGATCGCCCAGGAGTTCCCGACGCCGCCGGGCGCGAGCTGCCCCGAGGCGCCCTTCGAGGAGGCCTTCAGCCGGGTGGTGTTCCGCCTCAAGGGCGTGGAGATCACGGAGGAGGACTGGGCCGAGGCGGCCGAGCGGCTGCCGGATCACCTGGCGATGGGCTTCGCGGCCCTGGATGCGCAGGGCCGGGTCATTGGCCGTGGCCGGGACCTGGTTGCGCTCCAGCAGCGGCTGTCGGGCAAGACGGAGGCCGCCGTGCGCTCAGTGGTGCGCGGCGCGCTGGCCCAGGCGATGGCCGAGGCTCAGGAGCGCCAGGGCGCGCAGGGCGGGAAGCCCGGCCGCAAGGGCCGCAAGAAGAAGGGCGGGCGGCCGGCGGCCGCCCAGCGTCCGGGTGGCGCCGCTGGGACCACAGGGGTCGTAGGAGGCTCAGGGACCGGAACTGGGGCCGCTGCTGGAGGCGGCGCCGGCCTGGAGGAGCGCCAGGGACTGACCGACTGGCCCCGGGGCGTGCCGGGCCTGGGTGACCCGGATGCTTCGACGATCCCGGCCTCGGTGGAGTCCGCGGGCCGGGCCGGCCTGGTGGTGCGCGGCTACCCCGCCCTGGTGGCGGTCTCAGCCAGGAGCGCAGACTTGAGGATCCTGCCCGACGCCGCCGCGCAGCTGAGTGCCCATGACGCCGGGGTGACGGCGCTGGCCCTGGCTCGCACGGCCTTGCCGACGGCCCGGGTGACGAGCCGGTGGAGTGCCCAGGAATCGCTCATCCTGGCGGCCAGTCCCTACCGGACGACGGAGGCTCTCGTGGAGGACGTGCAGGCGGCTGCCGCACGGATCGTGGCCGGGCGCTGGGCGGCGTCGGCCTCCGGCTGCGCGCTTGCGGAGGTGCGCAGGCGGGAGGTCTTCGAGGCACTGGTCGGTGTCATGCGCAGTGAGCTCGAGGACGAGGTCTACCGGGTGGCCCGGTATGCGGCGGCGGCGCTCAAGGCGGCCCGGGAGGTGGAGCGCGTGGTGGGTGAGCACACCTCCCTGACGTTGCTGAACACGCTGCAGGAGGTGCGCGAGCACGCGGCCTCCCTGGTTCCGGAGGGTTTCATCACCGCCACCCCGCCGGAGCACCTGGCGCATCTGGAGCGCTACCTACGGGCCCTGGTGATGCGGGTGGAGAAGGCGGCCTCCTCGCCGTCGGCCGCCTCTCAGGACGCGGCCCTGGCCTTCCAGGTCTCCCAGGCCCGGGAGGTGGTGGACAAGGCCCGCGCCAAGGCGGCCTCGCTGCCGGCCGACCCGCAGCGCGAGGCCCTCCTGGAGGAGGCCCGTTGGATGGTGGAGGAGCTGCGGGTGAGTCTGTTCGCCCAGACTCTGGGGACGAGCCGCAAGGTGAGCCTCCAGCGCATCACCAAGCTCTGCGCCCAGATCGCCTGA","VTGMIGHTQPRRIAARSVAERIASELGTPIGRDGVVGYQVRFTEEIGENTLVKLMTDGILLAEIQSDPQLRRYDTIIVDEAHERSLNIDFILGYLARLLPERPDLKVIITSATIDSERFAEHFGREQIGDRGQPFTVPAPVIEVSGRTYPVEVRYRPLAPDDAPPASDDAGSEPAKPAAAPQPGPAGPGELSEAELEALTSPDPAVRAAARARREAIRSGAGPAALAPRNQGARGKGRGRAASTAAESGEPKDQVTGILDAVDELLGEPSGDILIFLAGERDIRDTEAALIDHLGARYTPDGRSRTPGAIEVVPLYSRLSAAEQHRVFETHQARRIVLATNVAETSLTVPGIRYVIDPGLARISRYSNRTKVQRLPIEPVSRASANQRAGRCGRVADGIAIRLYSQADFEARPEYTEPEILRTSLASVILQMAALGLGAVEDFPFLDAPDSRQVRSGLQLLTEIGAIEPAGAASARSDDAPDRGRRGPRLTEIGRRLARLPIDPRLGRMLLEAGELGCVGEVMVIVAALSIQDVRERPADKQEASDALHRRFADPTSDFLTYLNLWRYLRTQSRELSGSAFRRMCRAEFLHYLRVREWQDVHTQLRQLARPLGLDAAPVELPTARSIRAATEALEPGSHAAQIANGGVAAAVVALGRSADTPDADAIHRSLLVGLLSNVGNWDERRREYAGARGTRFTIWPGSGLRRKTYDWVMTAELVETSRLFARTVAKVDSRWIEQVADRAGLTRHVFGEPYWSTRQGAAMVHEKVLLYGMTLVADRPATLASVGTDSARQVAREMFIRSGLVEGGWHARHGFVERNRELIEELQDVERRRREHGLLADDAALFDFYDDRIPEEVTSAAAFDAWWKEQRRTTPDLLDFTRELLLPGGGDASGFPDTWVQGDLTLGLDYVFEPGHPEDGVSVQVPVEVLGRLSPEGFDWLVPGMRPELCVATIRALPKRVRRQLVPAPDVGAQVWAQIAQEFPTPPGASCPEAPFEEAFSRVVFRLKGVEITEEDWAEAAERLPDHLAMGFAALDAQGRVIGRGRDLVALQQRLSGKTEAAVRSVVRGALAQAMAEAQERQGAQGGKPGRKGRKKKGGRPAAAQRPGGAAGTTGVVGGSGTGTGAAAGGGAGLEERQGLTDWPRGVPGLGDPDASTIPASVESAGRAGLVVRGYPALVAVSARSADLRILPDAAAQLSAHDAGVTALALARTALPTARVTSRWSAQESLILAASPYRTTEALVEDVQAAAARIVAGRWAASASGCALAEVRRREVFEALVGVMRSELEDEVYRVARYAAAALKAAREVERVVGEHTSLTLLNTLQEVREHAASLVPEGFITATPPEHLAHLERYLRALVMRVEKAASSPSAASQDAALAFQVSQAREVVDKARAKAASLPADPQREALLEEARWMVEELRVSLFAQTLGTSRKVSLQRITKLCAQIA$","ATP-dependent helicase HrpA","Cytoplasm","ATP-dependent helicase HrpA","ATP-dependent helicase HrpA ","ATP-dependent helicase HrpA","","Poland B.W., Silva M.M., Serra M.A., Cho Y., Kim K.H., Harris E.M., Honzatko R.B. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 1993. 268(34):25334-25342. PMID: 8244965Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 2000. 296(2):569-577. PMID: 10669609","","","

InterPro
IPR001114
Family

Adenylosuccinate synthetase
SM00788	$\"[1166-1380]T$	no description

InterPro
IPR001650
Domain

Helicase, C-terminal
PF00271	$\"[310-396]T$	Helicase_C
SM00490	$\"[284-396]T$	HELICc
PS51194	$\"[257-436]T$	HELICASE_CTER

InterPro
IPR007502
Domain

Helicase-associated region
PF04408	$\"[456-563]T$	HA2

InterPro
IPR010222
Family

ATP-dependent helicase HrpA
TIGR01967	$\"[1-1447]T$	DEAH_box_HrpA: ATP-dependent helicase HrpA

InterPro
IPR011709
Domain

Domain of unknown function DUF1605
PF07717	$\"[603-745]T$	DUF1605

InterPro
IPR014021
Domain

Helicase superfamily 1 and 2 ATP-binding
PS51192	$\"[1-132]T$	HELICASE_ATP_BIND_1

noIPR
unintegrated

unintegrated
PTHR18934	$\"[3-177]T$ $\"[261-472]T$ $\"[490-614]T$ $\"[656-741]T$	ATP-DEPENDENT RNA HELICASE

","BeTs to 9 clades of COG1643COG name: HrpA-like helicasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1643 is ------y--d----efghsn-j--t-Number of proteins in this genome belonging to this COG is 3","***** IPB007502 (Helicase-associated region) with a combined E-value of 2.8e-112. IPB007502B 5-42 IPB007502C 50-96 IPB007502D 271-283 IPB007502E 334-367 IPB007502F 380-406 IPB007502G 481-531***** IPB002464 (ATP-dependent helicase, DEAH-box) with a combined E-value of 2.1e-11. IPB002464A 76-85 IPB002464B 387-404","","","No significant hits to the PDB database (E-value < E-10).","Residues 305 to 396 (E_value = 1.1e-11) place ANA_2559 in the Helicase_C family which is described as Helicase conserved C-terminal domain.Residues 456 to 563 (E_value = 7.5e-27) place ANA_2559 in the HA2 family which is described as Helicase associated domain (HA2).Residues 603 to 745 (E_value = 6.5e-12) place ANA_2559 in the DUF1605 family which is described as Domain of unknown function (DUF1605).","","helicase HrpA (hrpA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2560","2760747","2760151","597","12.39","27.85","20602","GTGGCCCGGACGCTGGGGAGTTTCCGTCATGTCGGTGAGTATTTCACGCAGGACCCCCACCGGCTTGGCCTGTCGCCGGCGGTCCTGTCGCGGGGTGATCGGGCGCCGGCGCGCCCATGGGGGACAATGGGCCACCTATGGAACAGGGCGAGCACCTCACGCACAACCAGGGCGACGATCACGCCGATGGACATCACGGCCAGCAGGACGGCGATCTCGGCGCGCGCAGCACCGAGAACACTCAGGCGTCCCCTGGCGGGCCGGACGGGCACGCCGCCGATCGTGCGCGGGGCGGCGCCCCGGACCGCCAGAAGTCACGATCCCCGCGCGGTGGCGGCAGGCGTCGGGGCCGGCGCCCGGGCCGCACCGAGGGCAGGCGCCGCAACGCCTGGAAGGGCTACTCCCCCGAGCAGCTCGCCGCCCGCGCCGCCGCCGTCCCGGCGATCGTCTACCCCGAGGAGCTGCCGGTCTCCGCCCGCCGTGAAGAGATCGCCGCCGCCATCGGTGAGCACCAGGTCGTCATCGTCGCCGGTGAGACCGGCAGCGGTAAGACCACCCAGCTACCCAAGATCTGCCTGGAGCTGGGGCGGGGCGTGA","VARTLGSFRHVGEYFTQDPHRLGLSPAVLSRGDRAPARPWGTMGHLWNRASTSRTTRATITPMDITASRTAISARAAPRTLRRPLAGRTGTPPIVRGAAPRTARSHDPRAVAAGVGAGARAAPRAGAATPGRATPPSSSPPAPPPSRRSSTPRSCRSPPAVKRSPPPSVSTRSSSSPVRPAAVRPPSYPRSAWSWGGA$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2561","2760718","2762211","1494","5.36","-12.17","54454","ATGACGGAAACTCCCCAGCGTCCGGGCCACCCTTCAGGGCCTGTGGCGCATGGTGCGGCCGAGCCTCAGCCTCCCTACGATCCGCAGAGCCCCGCGGATACACCAGGCTCGTATGCTCCGCCCGACTTCTCCACCCAGCGGACCGCACTCGACCAGGGGCAGTTCCCATCCGTCCTGGGTGGTGACGGTGATCAGGGCGGTACTGCTGGAAGAAGGCCCCGACGTCGACGTGCCGAGATTGTCGTGGCGGTCGTGACGGTGCTGGTCCTCGCAGTCGCTGGAGGGGGCGCGGCCTACTGGTGGCTGCGCGGCACGAAGGTCGACGGTCTTGTCTACCGGGCAGTGCCGGCGGATGCCAGCTGGAACAAGAGGTGGGTCAACGGCTACCGGCAGATCTGGTCTCTCAAGGCGACGAATGGTTTCATTCAAGGTCGGTTCGCCTCAGTGAAGTATGCCGAGGGCAAGCTCATCCGGGCGACGCCCGATGAGGACTTCGTTGACGTCGAGGTCTACTCGCTGACGAGTAAGACTCCCACACTGCTTTTCAAGGACAGATTTGAGGGCGGTGACGGCTCTTATGAGGCGAATGTATGGCAGGGGTGGCTCATAGAGAAAGGTGAGCTCGTCAACCTGGAGTCCCAGAAACGCCGGGATGCCCCGTGGGATGACGATGCGAAGGTGTCGGTAGTCGGCAGCTACGCCATAGCCTGCGAGAAGGCGCAGTGCTCGATGTGGTCGTCCTCGAAGGAGCGTGTGTGGAAGAAGACCCTGTCTTTCCTGCGTTCCGATGAAGTCGATGACGTGATCTTCGATCATCCCATCGGGCCTTATGTGAGTGCTCATACCGGATTTCGGGCCCAGGCCGTGCAATCCCTCATTGTCGACCTCAGGGACGGGTCGAGTAAGTCGATCAAGCAGGAGGCGGCGGGTGTCTACCCGCGCCCCCTTGCCGATGGGTGGCTGCTCTATGACCCGTACAAGAGTCTCGAGGGCCCTGCGACAGTGACTCTGCTGAAGGCCGATGGGTCTGTCCAGGAGACCTTCGAAGAAGGAATACCTCAAGGCTTCAAGAACTACCCCTGGTCTCCGGGCTACTGGACCTTGGACCAGGCCCGGGCCTGGTTCAAGCGCGGCGATACCTCGTGGGCCCCCTATACCTTCTCCATCGATGTCAGCGATACGGAATGCAGTCATATCATCGTCGGCGGGAAGAAAATCCATGTGTCCACACACAGTCCGCTCATCAATGGGGACTCACGCTTCGGCTGCGTGGGGGATCCGATTGAGGGGCTGGAGCACTCGGGTCGGGGGGATATTGGAGTCTTCACGGACCGGACAGGTGATGACTACTCTCTGCGTCTTGTTGACATGTCGAACGGGAACAGTCCCGATCCCGTCCCGGAGGGGATCGATGAGAACTATCGCATCGCAGTAGGTGACCTGCTCATCTCCTACCAAGGCGATGGTGAGCTGACGGTCTACCGAGCATCCTGA","MTETPQRPGHPSGPVAHGAAEPQPPYDPQSPADTPGSYAPPDFSTQRTALDQGQFPSVLGGDGDQGGTAGRRPRRRRAEIVVAVVTVLVLAVAGGGAAYWWLRGTKVDGLVYRAVPADASWNKRWVNGYRQIWSLKATNGFIQGRFASVKYAEGKLIRATPDEDFVDVEVYSLTSKTPTLLFKDRFEGGDGSYEANVWQGWLIEKGELVNLESQKRRDAPWDDDAKVSVVGSYAIACEKAQCSMWSSSKERVWKKTLSFLRSDEVDDVIFDHPIGPYVSAHTGFRAQAVQSLIVDLRDGSSKSIKQEAAGVYPRPLADGWLLYDPYKSLEGPATVTLLKADGSVQETFEEGIPQGFKNYPWSPGYWTLDQARAWFKRGDTSWAPYTFSIDVSDTECSHIIVGGKKIHVSTHSPLINGDSRFGCVGDPIEGLEHSGRGDIGVFTDRTGDDYSLRLVDMSNGNSPDPVPEGIDENYRIAVGDLLISYQGDGELTVYRAS$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[80-102]?$	transmembrane_regions

InterPro
IPR005627
Family

CutC
G3DSA:3.20.20.380	$\"[27-268]T$	no description
PTHR12598	$\"[9-81]T$ $\"[101-137]T$ $\"[161-269]T$	COPPER HOMEOSTASIS PROTEIN
PF03932	$\"[28-273]T$	CutC

","BeTs to 3 clades of COG3142COG name: Uncharacterized protein involved in copper resistanceFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG3142 is -----------l--e-ghs--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-41% similar to PDB:1TWD Crystal Structure of the Putative Copper Homeostasis Protein (CutC) from Shigella flexneri, Northeast Structural Genomics Target SfR33 (E_value = 2.8E_20);-41% similar to PDB:1X7I Crystal structure of the native copper homeostasis protein (cutCm) with calcium binding from Shigella flexneri 2a str. 301 (E_value = 2.8E_20);-41% similar to PDB:1X8C Crystal structure of the SeMet-derivative copper homeostasis protein (cutCm) with calcium binding from Shigella flexneri 2a str. 301 (E_value = 2.8E_20);-40% similar to PDB:2BDQ Crystal Structure of the Putative Copper Homeostasis Protein CutC from Streptococcus agalactiae, Northeast Strucural Genomics Target SaR15. (E_value = 2.1E_12);-56% similar to PDB:1IO1 CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN (E_value = 2.1E_12);","Residues 28 to 273 (E_value = 2.6e-23) place ANA_2564 in the CutC family which is described as CutC family.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2566","2766974","2766009","966","6.07","-5.61","34339","ATGCGAAACCTCAGGTGGTCAGGGAGCAGCGGCCCACGCCATGATCGGGGCGTGTCCTCCCGCTACTCACCCCCCAAGGACCTGAGCCGCTACGCGTGGCTGTCCATCGGTGCCGCACTGGCCACGATCGCGCTCAAGGGCGCCTCAGCCTGGCTGACCGGCTCCGTGGGTCTGCTCTCCGACGCCGCCGAGTCCGTGGTCAACCTCATCGCCGCCGTCGTCGCCCTCATCGTGCTGAAGATCGCGGCCAAGCCCGCCGACGCCGACCACCAGTTCGGGCACTCCAAGGCCGAGTACTTCTCGGCCGTCGTCGAGGGCGTCATGATCTTCGTGGCCGCCGCCGTCATCATCATCTCCGCCATCGAGCGCCTCATCGACCCACAGATGCCCGAGCAGCTGGGGGTGGGCCTGGCGGTCTCGGTCATCGCCTCGCTCCTCAACGGCGCGTTGGCGTGGGTGCTCTACCGGGCCGGGCGCCGCGAGCGCTCCATGACCCTGGTGGCCGACGCCAAGCACCTGGCCACCGACGTCGTCACCTCCGCCGCAGTCCTGGTCGGGGTGGCGCTGGTGGCCGTCTTCAACTCGGCCGTGCTCGACGCCGTCGTCGCCCTGGGGGCCGGCCTCAACATCATGTGGACCGGCTTCACGCTCATCCGCGACTCGGTGGGCGGTCTCATGGACATCGCCCCGTCCGCTGAGGTGCTCCAGCGCGTGGAGGAGGTTCTGGCGCACCACCGCCAGACGGGCATGATCGACTTCCACGCGGTGCGGGTGCGCGAGGCCGGCAACCGGCGTTTCATGGAGCTGCACGTGCTGGTTCCGGCGGCCTGGAGCGTCAAGAAGGGCCACGACTTCACCGAGCAGGTCATCGACGAACTCATCGAGGCCGACACCAGCCTGCGCATCTCGGCGCACCTGGAGCCCATCGAGGACCCCAAGTCCTACGAGGATGTGGAGGACATCTGA","MRNLRWSGSSGPRHDRGVSSRYSPPKDLSRYAWLSIGAALATIALKGASAWLTGSVGLLSDAAESVVNLIAAVVALIVLKIAAKPADADHQFGHSKAEYFSAVVEGVMIFVAAAVIIISAIERLIDPQMPEQLGVGLAVSVIASLLNGALAWVLYRAGRRERSMTLVADAKHLATDVVTSAAVLVGVALVAVFNSAVLDAVVALGAGLNIMWTGFTLIRDSVGGLMDIAPSAEVLQRVEEVLAHHRQTGMIDFHAVRVREAGNRRFMELHVLVPAAWSVKKGHDFTEQVIDELIEADTSLRISAHLEPIEDPKSYEDVEDI$","Cation diffusion facilitator family transporter","Membrane, Cytoplasm","CzrB protein","cation diffusion facilitator family transporter","cation diffusion facilitator family transporter","","Xiong A., Jayaswal R.K. Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus. J. Bacteriol. 1998. 180(16):4024-4029. PMID: 9696746Kunito T., Kusano T., Oyaizu H., Senoo K., Kanazawa S., Matsumoto S. Cloning and sequence analysis of czc genes in Alcaligenes sp. strain CT14. Biosci. Biotechnol. Biochem. 1996. 60(4):699-704. PMID: 8829543Conklin D.S., Mcmaster J.A., Culbertson M.R., Kung C. COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae. Mol. Cell. Biol. 1992. 12(9):3678-3688. PMID: 1508175","","","

InterPro
IPR002524
Family

Cation efflux protein
PTHR11562	$\"[30-316]T$	CATION EFFLUX PROTEIN/ ZINC TRANSPORTER
PF01545	$\"[32-313]T$	Cation_efflux
TIGR01297	$\"[28-311]T$	CDF: cation diffusion facilitator family tr

noIPR
unintegrated

unintegrated
tmhmm	$\"[30-50]?$ $\"[56-78]?$ $\"[99-121]?$ $\"[135-155]?$ $\"[176-194]?$ $\"[200-218]?$	transmembrane_regions

","BeTs to 17 clades of COG0053COG name: Predicted Co/Zn/Cd cation transportersFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0053 is aom-kzyqvdrlbcefgh--ujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB002524 (Cation efflux protein) with a combined E-value of 6.7e-32. IPB002524A 42-82 IPB002524B 84-123 IPB002524C 172-185","","","No significant hits to the PDB database (E-value < E-10).","Residues 32 to 313 (E_value = 2.7e-78) place ANA_2566 in the Cation_efflux family which is described as Cation efflux family.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2567","2767151","2767930","780","9.69","10.23","27183","ATGCCGGCCTCCCTGACCGACACCTTCCGGCTGCTGGACCTGTGCGGGGTCCTGCTCAATGGGATCCTGGGCGGGCTCATCGCCCGGCGCAAGAACTTCGACTTGGTGGGCTTCGTCGTCCTGGCCATGCTCACGGCCACCGCCGGCGGCATCCTGCGCGACGTCATGATCCAGGCCGGCCCGCCCTTCGCCCTGACCGACCCCTACTACCTCTACACGGCCTGCCTGGGGGCGACGGTGGCCTGGTTCGTGCCGCTGACCTCGCGGCCCACCCGTCGCCTGCTCGTGGTGGCCGACGCCGTCATCCTGGGCTGCTGGGCCGCCACCGGGGCCTCGAAGGCCCTCACCCACGGGCTCGGCGTCATGCCGGCGCTCCTGCTGGGCTGCCTGACCGCCATCGGCGGCTCTATGATCCGCGACGTCGCGGTGGGGGAGACCCCGGCCGTCTTCGGGGGCAACAAGCTCTACGCGATCCCGGCGCTCATCGCCGCCGGCACCCAGGTCGTGGCCGTCAAGGCGGGGGTGGCCGACGCGCACGCCATGCTCGTGTCCACCGTGGTCGGTGCGGGCCTGTGCGTGCTCGCCTACTGGCGCTCCTGGCAGCTGCCGGTCATCTCCGATAGGGAACGGCGCCGGGCCGGACGGCGCGAGGTCAACGGCGCGCTCGTGGGCTGGCGCCGGGGGCTCATGATGGGGCCGCTCAAGGCCCCCTCCTGGCGCGGCCGCGGCGGGCGGACGGCGCAGGAGGACGCCTCCTGCCAGCAGCCCGAGCAGGGCTAG","MPASLTDTFRLLDLCGVLLNGILGGLIARRKNFDLVGFVVLAMLTATAGGILRDVMIQAGPPFALTDPYYLYTACLGATVAWFVPLTSRPTRRLLVVADAVILGCWAATGASKALTHGLGVMPALLLGCLTAIGGSMIRDVAVGETPAVFGGNKLYAIPALIAAGTQVVAVKAGVADAHAMLVSTVVGAGLCVLAYWRSWQLPVISDRERRRAGRREVNGALVGWRRGLMMGPLKAPSWRGRGGRTAQEDASCQQPEQG$","Membrane protein","Membrane, Cytoplasm","Predicted membrane protein","hypothetical protein","protein of unknown function UPF0126","","","","","

InterPro
IPR005115
Domain

Protein of unknown function UPF0126
PF03458	$\"[9-94]T$ $\"[95-181]T$	UPF0126

noIPR
unintegrated

unintegrated
signalp	$\"[1-49]?$	signal-peptide
tmhmm	$\"[10-28]?$ $\"[35-55]?$ $\"[69-84]?$ $\"[94-112]?$ $\"[118-138]?$ $\"[153-173]?$ $\"[179-197]?$	transmembrane_regions

","BeTs to 8 clades of COG2860COG name: Predicted membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2860 is -o-------d-lb-efgh--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB005115 (Domain of unknown function UPF0126) with a combined E-value of 1.7e-39. IPB005115A 16-68 IPB005115B 97-130 IPB005115C 132-156 IPB005115B 11-44 IPB005115C 46-70","","","No significant hits to the PDB database (E-value < E-10).","Residues 9 to 94 (E_value = 1.1e-19) place ANA_2567 in the UPF0126 family which is described as UPF0126 domain.Residues 95 to 181 (E_value = 1.1e-10) place ANA_2567 in the UPF0126 family which is described as UPF0126 domain.","","membrane protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2568","2768316","2767999","318","10.08","6.16","10850","ATGGCCGGCAAGATCCCCTTCATCCTCGGACTCGGCGCGGGATACGTGCTCGGGACCCGCGCGGGGCGCGCCCAGTACGAGCGCATCAAGACCGCGGCCTCCAAGGTCGCCGAGCAGCCCTTCGTGCGCACCCGGGTCGACGCCGCCTCCAGTCACGTCAAGCAGGCCGTGCGCACCCAGGGCGAGGCCGTCACTGAGAAGGTCGCCGACGCCGTCAAGGAGCGGCTCTTCGGGGCACCCTCGAGCAAGGGCGGCGCCCAGTCCCAGCCCGTAGACGCCGGCCAGGCCAGCGTGCGCCCGGTCGGCGAGAGTTCCTGA","MAGKIPFILGLGAGYVLGTRAGRAQYERIKTAASKVAEQPFVRTRVDAASSHVKQAVRTQGEAVTEKVADAVKERLFGAPSSKGGAQSQPVDAGQASVRPVGESS$","Membrane protein","Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide

noIPR
unintegrated

unintegrated
tmhmm	$\"[45-65]?$	transmembrane_regions

InterPro
IPR013209
Domain

LNS2, Lipin/Ned1/Smp2
SM00775	$\"[124-278]T$	no description

noIPR
unintegrated

unintegrated
tmhmm	$\"[16-34]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[44-66]?$ $\"[131-151]?$ $\"[161-179]?$ $\"[185-203]?$ $\"[240-260]?$ $\"[299-319]?$ $\"[340-358]?$ $\"[364-382]?$ $\"[387-407]?$ $\"[426-444]?$	transmembrane_regions

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[229-417]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[17-376]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[3-410]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF7	$\"[3-410]T$	PERMEASE-RELATED
tmhmm	$\"[21-43]?$ $\"[49-69]?$ $\"[79-99]?$ $\"[105-125]?$ $\"[172-192]?$ $\"[224-244]?$ $\"[265-283]?$ $\"[297-331]?$ $\"[352-372]?$ $\"[382-402]?$	transmembrane_regions

","BeTs to 9 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G [Metabolism--Carbohydrate transport and metabolism] Functional Class: E [Metabolism--Amino acid transport and metabolism],P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 19","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 376 (E_value = 2.8e-25) place ANA_2576 in the MFS_1 family which is described as Major Facilitator Superfamily.","","membrane prootein","","1","","","","","","","","","","","Tue Aug 14 17:24:21 2007","","Tue Aug 14 17:24:21 2007","","","Tue Aug 14 17:24:21 2007","","","","Tue Aug 14 17:24:21 2007","Tue Aug 14 17:24:21 2007","","","","","yes","","" "ANA_2577","2779301","2777994","1308","5.00","-11.76","43847","ATGTCTCAGGCCAAGGACGAGCTTGTCGCGCGAGCGCAGGATCCCAATGCAGAGTTGGAGACCCTCCACCAGCTGGCGCAGAACTACCCCGGCCTGCGCCCCTACATCGCCGCCAACCCACGCACCTATCCCGCCCTCCTGGAGTGGCTGGGAACCCTGGGAGACCCCGCGGTCGATGCAGCCCTGGCCTCTCGCGACAGCCAGCCCCAGTCGGCGCCGTCGGCGCAGTCATCGCCTCGTCTGGCGGTGGTCTCGCCCCCCGGCGCCCAGCCGGGCACGCCGTCGGCCAGGTCCTCCGAGGCGCCCACGCAGGTGACCCTGCCCCGTTCCCTCCAGCCGGGCAGCGCAGTCTCCGGCACCTCCGCGGTCTCCGGGGCATCGGCGATCTCCGCCGCCAGCTCGAGGAGCGCCCAGAGCGCACCAAGCGCCTTCAACACGGCCGGTGCGAACACGCAGGTTGACGGCTTCCAGGCCGCGGGCGCCCCGGCCGTCCCCGTCCCCACGTCCCACCCCGCCCCAGCGATGGCCTCCCAGTCACCGGCTCGGCCGGTTCAGCCCGCCCTGCAGCAGACCTTCCAGCAGTCCGCGAACGTCTCTCAGGCGCAGAGCCCGGTCATTCCGACTCCCGCGCAGCAGGCCCCCGCGGTGACCGGCGACGACGGCGTCTTCGGCGTCGGCACCGAGGACGACGACTCCGAGCCCCCCTCCTCCTTCCTGACCTCCAACCGCATCCTGCTCATCCTGGCGCTCCTGGTGGCCACCGTCCTGGTCTTCCTGGCGACCTGGTACCTCTCCGGGGGCAGCGACAAGGGCTCGGTCGCCGACTCGGGCACCGAGGCCCCGGCCGACTCCGGCCAGGCTGCGGCTGAGGACGGCTCCTCCCCGGCCCCCCATTCGGCCTCCCCCAAGGCCTCGGCCACCCCGAGCGCCTCGGCGACGCCCGCGCTCAAGGCGCCGGCACCCCAAGAGGCTCAGGAGCTGTCCGGCTTCGACGCCCCCAGCGGCAACATCAGCTGCACCCTGAACGACAACAACCTCACCTGCGTCATCAACGAGCACGCCAAGGTCGATTCCTGTGATTCCTCGAAGCCGTTGACGGTCACGATCGACGCTGACGGGAACATGAGCAAGAGCTGCGGGTCGCCCTTCACCACCAAGGGTGTCAGCCTCAGTTACGGTTCCTCGGCCAAGCACTCCACCTTCGCCTGCAAGTCAACCGATAAAGGCATGCAATGCTGGAGCCAGGTCACCGGCAAGGGCTTCATCCTCAGCCGCGACAGCGTCGTCGACACCCACGGCGGCAACTGA","MSQAKDELVARAQDPNAELETLHQLAQNYPGLRPYIAANPRTYPALLEWLGTLGDPAVDAALASRDSQPQSAPSAQSSPRLAVVSPPGAQPGTPSARSSEAPTQVTLPRSLQPGSAVSGTSAVSGASAISAASSRSAQSAPSAFNTAGANTQVDGFQAAGAPAVPVPTSHPAPAMASQSPARPVQPALQQTFQQSANVSQAQSPVIPTPAQQAPAVTGDDGVFGVGTEDDDSEPPSSFLTSNRILLILALLVATVLVFLATWYLSGGSDKGSVADSGTEAPADSGQAAAEDGSSPAPHSASPKASATPSASATPALKAPAPQEAQELSGFDAPSGNISCTLNDNNLTCVINEHAKVDSCDSSKPLTVTIDADGNMSKSCGSPFTTKGVSLSYGSSAKHSTFACKSTDKGMQCWSQVTGKGFILSRDSVVDTHGGN$","Hypothetical protein","Extracellular, Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[244-264]?$	transmembrane_regions

InterPro
IPR001932
Domain

Protein phosphatase 2C-related
SM00331	$\"[31-264]T$	PP2C_SIG
SM00332	$\"[16-262]T$	PP2Cc

InterPro
IPR001969
Active_site

Peptidase aspartic, active site
PS00141	$\"[191-202]?$	ASP_PROTEASE

InterPro
IPR014045
Domain

Protein phosphatase 2C-like
PF00481	$\"[26-257]T$	PP2C

noIPR
unintegrated

unintegrated
G3DSA:3.60.40.10	$\"[21-263]T$	no description
PTHR13832	$\"[134-263]T$	PROTEIN PHOSPHATASE 2C

","BeTs to 11 clades of COG0631COG name: Protein serine/threonine phosphatasesFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0631 is ---p--yq-drlbc-f--s-uj-i-wNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","-52% similar to PDB:1TXO Crystal structure of the Mycobacterium tuberculosis serine/threonine phosphatase PstP/Ppp at 1.95 A. (E_value = 2.7E_30);","Residues 26 to 257 (E_value = 7.5e-06) place ANA_2580 in the PP2C family which is described as Protein phosphatase 2C.","","phosphatase (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2581","2782078","2782911","834","5.15","-7.32","29722","ATGAGCGACCTGACATGGACGGAGATGCCGGAGGTCAGTCCTGAGCAGCCCGACGAGCTTGTCCTGGACTTCTCCGGAGAGATTTACCGGGTCGCCCCGGCCGACACCTTCGTCATCGGTCGAGGCGGAGACCTCGATATTGACGACAATCCCTACCTCCACCGCCGCTTCCTGGTCTTCGCCCACTCCGAGAACCTCTGGTGGATCGCCAACGAGGGGTCGCGGTTGTCGGCCACCCTGACCGACGGCGAGGGGCTGGTCCAGTCCCGGCTGGCCCCCGGCGCCCGCATGCCGCTGGTCTTCCCCCGGGTCATCCTCACCTTCTCCGCCGGTCCGACCACCTACGAGATCAACCTCATCACCTCCGGGGAGGACCGTTTCTCCGGGATCGACGGCGTGCGTCAGTCCTCCGGCCAGACCACCATCGGGGTGACCCCGATGACCCGCTCCCAGCTGCTGCTCGTCCTGGCGCTGTCCGAGCCGGTGCTCAAACGGGCCGGGACCGGGGCCGCCGAGATCCCCTCCTCCGCGGCGGCCGCGGCGCGCCTGGGCTGGCCGCTGACCAAGTTCAACCGCAAGCTCGACAACGTCTGCGAGAAGCTCGACCGGGTGGGGGTGCGCGGGCTGCGCGGCGGCCGCGTGGCCGGAGCCGCCTCCAACCGGCGTACTGCCCTGGTGGAGCACGCCGTGTCCACCCTCATGGTCACCGCCGAGGACCTCTACATGCTTGACGAGGAGCTGGCCGCCAACCAGGCCCCCGCAGACCAGACGGCTGAGCGCTCGGTGAGCACCGCCCCGGTGGCCCAGAGCTCGCCGTCGGCGTCGGGGCGATGA","MSDLTWTEMPEVSPEQPDELVLDFSGEIYRVAPADTFVIGRGGDLDIDDNPYLHRRFLVFAHSENLWWIANEGSRLSATLTDGEGLVQSRLAPGARMPLVFPRVILTFSAGPTTYEINLITSGEDRFSGIDGVRQSSGQTTIGVTPMTRSQLLLVLALSEPVLKRAGTGAAEIPSSAAAAARLGWPLTKFNRKLDNVCEKLDRVGVRGLRGGRVAGAASNRRTALVEHAVSTLMVTAEDLYMLDEELAANQAPADQTAERSVSTAPVAQSSPSASGR$","Hypothetical protein","Periplasm, Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2582","2782913","2783872","960","8.38","2.18","33246","GTGACGCGAGCAGTGAGGAGTCACCGGGGCGACGCGGACTCGCCTCGAGCGAAGGCGGATGTCGCGGGCAAGGAGTTCCCCAACCGGGCGCTCCTCGACGAGGTCCTGGCGAACGATCCCGAGGAGGGCGACTTTCTCGAGGACCGGCTCGTCGAGGACTCCTCGCAGGGGAAGCTCTCAGACGGCAACCGTCCCCGTCCCGCCAGACGGCGTCACGCGCGACGGTGGCTGGCGGTCCTGGTGGTGCTCGTCGTCATCCTGAGCGCCGGGGCCGTCGGGGCGGAGTACCTCGTGCGCGGGCAGGTCGACGCCGCCGTCCGCTCCGCCCTGCCGGGGCTCAACCCGGACGCCCGCATCGCCACCAAGGGAATCCTCCTGCGTCAGGTTATCGGCGGCTCACTGGACAGCCTGAGCGTGGACTCCTCGAGCCTGACGATCACCTCCAAGAGCCAGGGAAACGCCTCGGTCACGCTCAGCGACGTCGACGTCGACCTCAGCCACATCAGCCTGCACAAGCCCTATCAGACCGACACGGTGGCGGCGTCGGGCACTATCAGCTGGCAGCAGGTGGGCGAGCTCGCCGCGGTATCGCACCCCAAGCTCAAGGGCGTCACCCTCCAGGCCAAGCGCACTGGGACCAGCGCGCAGGATCCGGGATCCATCCAGGCCTCGATGTCCCTGCTCGGTCTGAGCGGTGAGGCGGAGATCACCCCGTCGCTGGGCTCCGACGGCAGCCTGATCCTGACCATCACCTCCACCCGGATGGGTGGGAAGAAGGTCGGCGTCGACGTCGCCACGGGCCAGGACAGCATGCTCAGCTATATCGGGCTGGACTCCCCGCAGATCACGGTCCCCGCGAAGTCCCTGCCGCCGGGGCTGCGCCCGACCAGCGTCATTGTCACCAGTGATGGGCTCCGGCTGAGCCTGGCCGGGAGCAGGGTGAACCTCGGCCAGCTCTGA","VTRAVRSHRGDADSPRAKADVAGKEFPNRALLDEVLANDPEEGDFLEDRLVEDSSQGKLSDGNRPRPARRRHARRWLAVLVVLVVILSAGAVGAEYLVRGQVDAAVRSALPGLNPDARIATKGILLRQVIGGSLDSLSVDSSSLTITSKSQGNASVTLSDVDVDLSHISLHKPYQTDTVAASGTISWQQVGELAAVSHPKLKGVTLQAKRTGTSAQDPGSIQASMSLLGLSGEAEITPSLGSDGSLILTITSTRMGGKKVGVDVATGQDSMLSYIGLDSPQITVPAKSLPPGLRPTSVIVTSDGLRLSLAGSRVNLGQL$","Hypothetical protein","Membrane, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-94]?$	signal-peptide
tmhmm	$\"[76-98]?$	transmembrane_regions

InterPro
IPR001208
Family

MCM
PTHR11630	$\"[224-273]T$	DNA REPLICATION LICENSING FACTOR

InterPro
IPR011703
Domain

ATPase associated with various cellular activities, AAA-3
PF07726	$\"[160-290]T$	AAA_3

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[140-295]T$	no description
PTHR11630:SF47	$\"[224-273]T$	DNA REPLICATION LICENSING FACTOR MCM8

","BeTs to 18 clades of COG0714COG name: MoxR-like ATPasesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0714 is aompkzyqvdr-bcefg-s--j--t-Number of proteins in this genome belonging to this COG is 3","***** IPB011703 (ATPase associated with various cellular activities, AAA_3) with a combined E-value of 8.5e-94. IPB011703A 165-199 IPB011703B 231-279 IPB011703C 280-291 IPB011703D 373-396 IPB011703E 400-442 IPB011703B 232-280***** IPB000523 (Magnesium chelatase, ChlI subunit) with a combined E-value of 3.6e-12. IPB000523A 141-183 IPB000523E 377-421","","","No significant hits to the PDB database (E-value < E-10).","Residues 160 to 290 (E_value = 4.2e-75) place ANA_2583 in the AAA_3 family which is described as ATPase family associated with various cellular activities (AAA).Residues 160 to 296 (E_value = 2.3e-07) place ANA_2583 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).","","conserved MoxR-like protein in magnesium chelatase family (moxR)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2584","2785444","2786445","1002","6.47","-2.30","36642","ATGAGCACGGAGGTACATGGCGCTCCCGGGGCGCCCGAGTCCGATTCCGGCGAGGGCCGGCGCGGTTCGCGGATCGAGCGTCTGCGCGCGGCTCTGAGCCTGCCGACCCTGCGCCGCGCCACGGGGCTGCTCGACGGGCGCCACAAGTCGGTGTTCGTCGGGCGCGGGCAGGACTTCGACGACATGTCCTTCTACCGGCCCGGCGACGACATCTCCGACATCGACTGGAAGTCCTCGGCCCGTCTGGGGCAGCCGGTCATCAAGCGCTACCAGCGCGAGTCCATGATGCCCATGGTGCTGGCCGTGGACACGGGCCGGACCATGGCGGCGATGACCCCCTCGGGCGAGGACAAGCGCGACCTGGCCCTGGGAGTGGCGGAGGTCTTCGCCTACCTGGCCCGGATGCGGGGGGACTCGGTGGCGCTCGTGGCCGGTGACGCCGGCCGGATGATCTCGCGTCCGGCCCGTTCCGGGGCCAAGCACGTGGAGACCCTGCTGGCGCTGCTGGCCCGCACCTACGAGGACCTCGACGCTCCCGTCGAGGGGGCGCCCGGCGTCTACGAGCTGGCCCCCGGGGCACCTCCCTCCAGCCTGCCGCGCCTCATGGAGCGGGTGAGCACCTGGCACCGCCGACGCAGCCTGGTCATCCTCATCACCGACACCGCCCACCCCGGCCCCGATGCCGCGACCTGGCTGCGGCGCCTGTCGATCCAGCACGAGATGATCGTCGTCCAGATCGAGGACGACGATCCGCTGCGACCGGACGGCGGCCGCGGGCGGGACATCGACCTGCCCTTCGAGATCCCCGCCTTCCTGCGCGCGGACTCCTACCTGGCCGCTCAGGCGGCCGTGGTGCGCGAGCAGTGGCGCACCAGCGTCGAGCAGGTGCTCGACGCCCGGCACCTGGAGTACGGCGTCGTCTCCTCCGAGGAGACGCTCATCGACTCCATCGCCGAGCTCCTCCAGCGTGAGCGCGCCGCCGTGGCCAGAGGGAGGCGGTGA","MSTEVHGAPGAPESDSGEGRRGSRIERLRAALSLPTLRRATGLLDGRHKSVFVGRGQDFDDMSFYRPGDDISDIDWKSSARLGQPVIKRYQRESMMPMVLAVDTGRTMAAMTPSGEDKRDLALGVAEVFAYLARMRGDSVALVAGDAGRMISRPARSGAKHVETLLALLARTYEDLDAPVEGAPGVYELAPGAPPSSLPRLMERVSTWHRRRSLVILITDTAHPGPDAATWLRRLSIQHEMIVVQIEDDDPLRPDGGRGRDIDLPFEIPAFLRADSYLAAQAAVVREQWRTSVEQVLDARHLEYGVVSSEETLIDSIAELLQRERAAVARGRR$","Uncharacterized conserved protein","Cytoplasm","Protein of unknown function family","hypothetical protein","protein of unknown function DUF58","","","","","

InterPro
IPR002881
Domain

Protein of unknown function DUF58
PF01882	$\"[1-93]T$	DUF58

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

InterPro
IPR002035
Domain

von Willebrand factor, type A
PF00092	$\"[117-327]T$	VWA
SM00327	$\"[115-307]T$	VWA
PS50234	$\"[117-327]T$	VWFA

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[80-100]?$	transmembrane_regions

","BeTs to 5 clades of COG3035COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3035 is -----z----r----fg-------t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 117 to 327 (E_value = 0.0003) place ANA_2586 in the VWA family which is described as von Willebrand factor type A domain.","","Willebrand factor type A domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2588","2788074","2789177","1104","5.63","-5.04","39422","ATGAAGCCGGTTCCAATCATCGGGGACTTCGCGTTCATCCCGGTCACCTGGTGGCTCCTCGTCCTGCTCCTGGCGGCCGCCCTGACGGGGCTGCTCGTCGTGGCCCGACGCCGCCTGGTCCGTGACGATGCCGAGCCTGCCGCCCGCCGAGCCTGGTGGAGGCGCCTGGCCATCGTCGTCGTCATCGTGCTGGCGCTGGCGGGGCCGGCGATCCGCGGCAGCGAGGCGATCAGCGTCTCCAACGTGGAGATCTACATGGTGGTGGACCGCACCGGCTCCATGGCCGCGGAGGACTACCAGGGCAAGGGGCCCGACGGCGTCGACCAGTCGGCCTCCACCAGGCTCGACGGCGTGCGCGCGGACATGCGGGCCATCCGCGAGGCCTTCCCGGACTCGCGCTTCTCCATCATCGCCCTGGACAACACCGCGGCCCGGGAGCTGCCGCTGACTCACGACACCAACGCCGTCGACGCCTGGATCGGCTCCTTCAAGCAGGAGGTCTCAGGCCACGCCACCGGCTCCTCGCTGGAGGTGGCGCTTCCGATGCTGGGGCTCACGCTGGCACAGGCCCGCCAGTCCGACCCCAAGGACATCCGCCTCGTCTACATCTTCTCCGACGGGGAGGCCACCGACAACGGCCGCGGCGCTCAGGCGGCCGACAACGCCGGCATCTCCTGGCAGTCCCTGGCCGGGCTCGTCGACGGCGGCGCGGTGCTGGGCTACGGCTCGACCGAGGGCGGCAAGATGCGCAGCTACGACGGCTCGCCGTCCACCGGCGAGCACACCCAGTCCGACTACATCACCGACGGCCAGGGCGGGCAGCCCGGGGTGTCGAAGATCGACGCCGACGAGCTCCAGAAGGTGGCCAAGGACCTGGGGCTGCCCTACTTCCACCGCACCGGCGGCTCGGGGGATGACCCGACGAGCAAGTTCACCAACCTCGACATCGAGGCCGTCACCTCCGACGGGCGGGCCAAGACCAACGCCCGGGTGTACCTGACCTGGCCACTGGGACTCATCGCCTTCGGTCTGCTGTTGTGGGAGATCCTCGACCTCATGCGAGCCGACCGTCGCCTGCGTCTTCTCATGGGAAGGGGACGATGA","MKPVPIIGDFAFIPVTWWLLVLLLAAALTGLLVVARRRLVRDDAEPAARRAWWRRLAIVVVIVLALAGPAIRGSEAISVSNVEIYMVVDRTGSMAAEDYQGKGPDGVDQSASTRLDGVRADMRAIREAFPDSRFSIIALDNTAARELPLTHDTNAVDAWIGSFKQEVSGHATGSSLEVALPMLGLTLAQARQSDPKDIRLVYIFSDGEATDNGRGAQAADNAGISWQSLAGLVDGGAVLGYGSTEGGKMRSYDGSPSTGEHTQSDYITDGQGGQPGVSKIDADELQKVAKDLGLPYFHRTGGSGDDPTSKFTNLDIEAVTSDGRAKTNARVYLTWPLGLIAFGLLLWEILDLMRADRRLRLLMGRGR$","Von Willebrand factor; type A","Membrane, Cytoplasm","conserved hypothetical protein","von Willebrand factor; type A","hypothetical protein","","Ruggeri Z.M., Ware J. von Willebrand factor. FASEB J. 1993. 7(2):308-316. PMID: 8440408Colombatti A., Bonaldo P., Doliana R. Type A modules: interacting domains found in several non-fibrillar collagens and in other extracellular matrix proteins. Matrix 1993. 13(4):297-306. PMID: 8412987Perkins S.J., Smith K.F., Williams S.C., Haris P.I., Chapman D., Sim R.B. The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. Its occurrence in collagen types VI, VII, XII and XIV, the integrins and other proteins by averaged structure predictions. J. Mol. Biol. 1994. 238(1):104-119. PMID: 8145250Bork P. Shuffled domains in extracellular proteins. FEBS Lett. 1991. 286(1):47-54. PMID: 1864378Edwards Y.J., Perkins S.J. The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted beta-sheet flanked by alpha-helices found in human ras-p21. FEBS Lett. 1995. 358(3):283-286. PMID: 7843416Lee J.O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 1995. 80(4):631-638. PMID: 7867070Qu A., Leahy D.J. Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(22):10277-10281. PMID: 7479767","","","

InterPro
IPR002035
Domain

von Willebrand factor, type A
PR00453	$\"[82-99]T$ $\"[200-208]T$	VWFADOMAIN
SM00327	$\"[81-267]T$	VWA

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[55-73]?$ $\"[332-350]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
tmhmm	$\"[77-97]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB005028 (Herpes virus intermediate/early protein 2/3) with a combined E-value of 7.2e-09. IPB005028B 245-293 IPB005028B 253-301 IPB005028B 257-305 IPB005028B 241-289 IPB005028B 249-297 IPB005028B 233-281 IPB005028B 244-292 IPB005028B 237-285 IPB005028B 261-309 IPB005028B 252-300 IPB005028B 256-304 IPB005028B 229-277 IPB005028B 269-317 IPB005028B 248-296 IPB005028B 268-316 IPB005028B 240-288 IPB005028B 260-308 IPB005028C 253-303 IPB005028C 245-295 IPB005028C 249-299 IPB005028C 241-291 IPB005028C 237-287 IPB005028C 261-311 IPB005028C 233-283 IPB005028C 257-307 IPB005028C 265-315 IPB005028C 229-279***** IPB001359 (Synapsin) with a combined E-value of 5.5e-07. IPB001359H 233-283 IPB001359H 237-287 IPB001359H 225-275 IPB001359H 243-293 IPB001359H 227-277 IPB001359H 259-309 IPB001359H 256-306 IPB001359H 226-276 IPB001359H 229-279 IPB001359H 244-294 IPB001359H 235-285 IPB001359H 257-307 IPB001359H 241-291 IPB001359H 247-297 IPB001359H 255-305 IPB001359H 245-295 IPB001359H 239-289 IPB001359H 253-303 IPB001359H 231-281 IPB001359H 251-301 IPB001359H 230-280 IPB001359H 250-300 IPB001359H 254-304 IPB001359H 234-284 IPB001359H 228-278 IPB001359H 249-299 IPB001359H 238-288 IPB001359H 242-292","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2590","2790202","2790699","498","5.03","-8.09","17838","GTGAGCGACTCCGATACGGGGCGGGCCTCCCGACTCGTCGTGGCGGCCGCGGTCCTGGACGACCTGGAGCATCCGACCACCCTGCTGTGCGCGGCCCGCTCCTACCCGCCTGAGCACGCCGGTCAGTTCGAGCTGCCCGGCGGCAAGGTCGAGCCCGCAGAGCGGCCCGAGCAGGCCCTGGCCCGCGAGCTGGACGAGGAGATCGGCCTGAGCGCCCGCCTCGGGGCCGAGCTCGTCGTTCCCCGACAGCTGGCGGTTCCGCCGCCGCCGGACGGCGCTCCCGGTGACGACGCCCCGGCCTGGCCGGCCATGCACGGCTTCAGGATGCGAGTGTGGCTGGCCGAGCCCGCCCGCCCCGGGGACCGGGGCAGGGTCGGAGGCGACCACCAACGCCTGGAGTGGGTGCGCCTGGACCCTCCCGACCAGCTGCGCCGACTGCCGTGGCTGGAGGCGGACCTGCCGATCATCGACGCGCTCGTAGGCGCCCTGGGACGCTGA","VSDSDTGRASRLVVAAAVLDDLEHPTTLLCAARSYPPEHAGQFELPGGKVEPAERPEQALARELDEEIGLSARLGAELVVPRQLAVPPPPDGAPGDDAPAWPAMHGFRMRVWLAEPARPGDRGRVGGDHQRLEWVRLDPPDQLRRLPWLEADLPIIDALVGALGR$","NUDIX hydrolase","Cytoplasm, Extracellular","NTP pyrophosphohydrolase","putative mutT-like protein ","NUDIX hydrolase","","Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 1992. 174(20):6321-6325. PMID: 1328155Koonin E.V. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 1993. 21(20):4847-4847. PMID: 8233837Mejean V., Salles C., Bullions L.C., Bessman M.J., Claverys J.P. Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydrolases. Mol. Microbiol. 1994. 11(2):323-330. PMID: 8170394Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 1993. 268(31):23524-23530. PMID: 8226881McLennan A.G. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int. J. Mol. Med. 1999. 4(1):79-89. PMID: 10373642Bessman M.J., Frick D.N., O. Handley S.F. The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes. J. Biol. Chem. 1996. 271(41):25059-25062. PMID: 8810257","","","

InterPro
IPR000086
Domain

NUDIX hydrolase
PR00502	$\"[43-57]T$ $\"[57-72]T$	NUDIXFAMILY
G3DSA:3.90.79.10	$\"[8-162]T$	no description
PF00293	$\"[10-162]T$	NUDIX
PS00893	$\"[48-69]T$	NUDIX

noIPR
unintegrated

unintegrated
PTHR22769	$\"[18-70]T$	MUTT/NUDIX HYDROLASE

","BeTs to 19 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 7","***** IPB000086 (NUDIX hydrolase) with a combined E-value of 8.5e-12. IPB000086 43-70","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","pyrophosphohydrolase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2592","2790849","2791541","693","7.37","1.37","24860","ATGCCGAAGATTCTGGGTTCCTCGCTGGCCGAGCATCGAGAGCGCACGCGCACCGCCCTGTTCGGGGCACTGTCCGAGCTCATGAGCCAGCGCAGCTTCGACAAGATCACCCTGTCCGACGTCGCCAATCACGCGGGTGTGGGGCGCACGGCCGTCTACAACCACTTCGCGGACAAGGAGGACCTCCTCCTGGCCTTCATGGAGCATGAGGCCGGCCGCTACGCCGAGGAGCTCTCCCGGGCGCTGGCCGGCACCCAGGACCCGATCGACCGCCTGCGCATCTACGTGCGCCAGCAGGCCCTCATCGCCCGGCACTTCCACTTCCCCGCCTCGGGGCCGCTGTCCGAGGTGGTCTCGCGTGGGACCGCCGGTCGTCTCAAGGCCCACGGGGCGCTCGTGGCCCAGATGCTTGCCTCAATCCTCACCGACGCCATGGACCAGGGGCTCATCCCCGCCCAGGAGCCCGAGCAGGTCATCCCCCTCATCCACGCCACCGTCATGGGCGGGCGCCCAACCCCCACGGATCCGGAGCAGCGCCGGGCCTACCTGGAGAGCCTGGACGCCTTCGTGCTGCGGGCGGTGGGGGCCCGCCAGCCCGCCCACGCGGTACCGACCATTGCCCAGCCCCGCGCCACCGAGCCGCTGGAGGGTGCCCAGGCCCCCGGTTCGCTTCGTCACAGCGCGGTCGGCTGA","MPKILGSSLAEHRERTRTALFGALSELMSQRSFDKITLSDVANHAGVGRTAVYNHFADKEDLLLAFMEHEAGRYAEELSRALAGTQDPIDRLRIYVRQQALIARHFHFPASGPLSEVVSRGTAGRLKAHGALVAQMLASILTDAMDQGLIPAQEPEQVIPLIHATVMGGRPTPTDPEQRRAYLESLDAFVLRAVGARQPAHAVPTIAQPRATEPLEGAQAPGSLRHSAVG$","Transcriptional regulator, TetR family","Cytoplasm","A-factor receptor homolog SC9B1.18 cprB","hypothetical protein","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[20-33]T$ $\"[41-64]T$	HTHTETR
PF00440	$\"[20-66]T$	TetR_N
PS50977	$\"[14-74]T$	HTH_TETR_2
PS01081	$\"[32-63]?$	HTH_TETR_1

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[13-77]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-47]?$	signal-peptide
tmhmm	$\"[19-39]?$ $\"[95-115]?$ $\"[121-139]?$ $\"[144-162]?$ $\"[168-188]?$ $\"[209-231]?$	transmembrane_regions

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[9-324]T$	SBP_bac_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[143-343]T$	no description
PS51257	$\"[1-23]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 8 clades of COG1653COG name: Sugar-binding periplasmic proteins/domainsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1653 is -o-pkz--vdrlbcefghs--j--t-Number of proteins in this genome belonging to this COG is 6","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","periplasmic proteins-domains, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2595","2794412","2793957","456","6.00","-5.71","16415","GTGCGCGTGGAGTGGACGGGCAACCTGGGCACGGGCACATCCGGATACCGCGACTACTCGCGCGACCACGATGTCCGGGGAATCACCGCCGACCTGCCGGCGATCCACGGATCGGCGGATCCAGCATTCCGAGGGGACGCTCGCAGATGGAACCCGGAACAGCTCCTGCTCGCCTCGCTCTCACAGTGCCACATGCTGTGGTACCTCCACGTCGCGGCGGACGCGGGTCTCACCGTCACCGCCTACTCGGATACCCCTACTGGCCTCATGGCCGAGCACCCGGGCGGTACCGGGGAGTTCACGTTAGTCACCCTTCACCCCACAGTGACCATCGCTCCCGGCAACGATCCTGAGAGTGCCGCCACGCTCCACGACCGCGCCGCCGAGTACTGCTTCATTGCTCGATCGGTGAGATTCCCGGTTCACCACGACGTCATCATCACGACCGAGCACTAG","VRVEWTGNLGTGTSGYRDYSRDHDVRGITADLPAIHGSADPAFRGDARRWNPEQLLLASLSQCHMLWYLHVAADAGLTVTAYSDTPTGLMAEHPGGTGEFTLVTLHPTVTIAPGNDPESAATLHDRAAEYCFIARSVRFPVHHDVIITTEH$","OsmC family protein","Cytoplasm","Predicted redox protein","hypothetical protein","OsmC family protein","","Wimberly B.T., Brodersen D.E., Clemons W.M., Morgan-warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V. Structure of the 30S ribosomal subunit. Nature 2000. 407(6802):327-339. PMID: 11014182Chen X., Court D.L., Ji X. Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(15):8396-8401. PMID: 10411886Worbs M., Bourenkov G.P., Bartunik H.D., Huber R., Wahl M.C. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol. Cell 2001. 7(6):1177-1189. PMID: 11430821","","","

InterPro
IPR003718
Family

OsmC-like protein
PF02566	$\"[25-146]T$	OsmC

InterPro
IPR009019
Domain

KH, prokaryotic type
G3DSA:3.30.300.20	$\"[51-149]T$	no description

","BeTs to 5 clades of COG1764COG name: Predicted redox protein, regulator of disulfide bond formationFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1764 is ---p-----d-lb-efg-s--j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB003718 (OsmC-like protein) with a combined E-value of 1.1e-06. IPB003718 51-67","","","-53% similar to PDB:2D7V Hypothetical protein VCA0330 from Vibrio cholerae O1 biovar eltor str. N16961 (E_value = 1.1E_10);","No significant hits to the Pfam 21.0 database.","","redox protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2597","2794965","2795441","477","4.70","-4.63","16113","ATGACTGATCCCTTCAACTCTCATGAGCCGACTGATCCCGCTGCGAGTCCTGGTATGGACGCGCCGGCACTGCCCGCGGGGCCCGCCCCCACGGACTACCCGTCAGGCGGGTACCCGCCCTACAGCGGTCCCTACGCTTCCGGTGCCCAGCCGGGGTATGACCCGCAGTGGGCCTACGCGCCCCCGCCCGGTTATGGCATGCCTCCTGGATACGGTGTGCCTCCCGGCTACGGGGGCAAGTCCAGGGTGGCCGCCGGCGTCCTGGCCCTGCTCCTGGGAACCTTCGGGATCCACAACTTCTACCTGGGCTACACGGGCAAGGCGCTCTTCCAGCTCCTGGGCACGTTCTTGAGCTGCGGGATGCTGGCCCTTCCGATCGCCATCTGGGCCTTCGTCGAGGGCATCCTCATCCTCGTGGCCCGCCCCGGCGAGGCGCCGTGGGGCGTTGACGCCTCCGGTATGCCGCTGAGCGGCTGA","MTDPFNSHEPTDPAASPGMDAPALPAGPAPTDYPSGGYPPYSGPYASGAQPGYDPQWAYAPPPGYGMPPGYGVPPGYGGKSRVAAGVLALLLGTFGIHNFYLGYTGKALFQLLGTFLSCGMLALPIAIWAFVEGILILVARPGEAPWGVDASGMPLSG$","TM2 domain containing protein","Extracellular","TM2 domain family","narrowly conserved hypothetical protein","TM2 domain containing protein+B7201","","","","","

InterPro
IPR007829
Domain

TM2
PF05154	$\"[78-128]T$	TM2

noIPR
unintegrated

unintegrated
tmhmm	$\"[84-102]?$ $\"[112-132]?$	transmembrane_regions

","BeTs to 3 clades of COG2314COG name: Predicted membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG2314 is --m------drlbc-f--------t-Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","domain family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2598","2795490","2796161","672","5.94","-5.14","24068","GTGACGCCTCCGGGAGGACCTGGCACAATCGGGCCCGTGCTGCTCTCAGACCGCGATATCCGCACCGAGCTCGACGCCGGACGGGTCGTCCTCGACCCCTACGACCCCGAGATGATTCAGCCGGCCTCCATTGATGTGCGCCTGGACCGCTGGTTCCGTCTCTTCGACAACCACCGCTACCCGGTCATCGACCCGGCCGCCGACCAGGAGGGGCTGACCCACCTGGTCGACGTCGGGGCCGATGAGCCCTTCGTTCTGCATCCCGGGGAGTTCGTCCTGGGGGCCACCTACGAGCGCATCACCCTGCCCGACGACGTCGCCGCCCGCCTGGAGGGCAAGTCGAGCCTGGGGCGCCTGGGGCTGCTGACCCACTCCACCGCCGGATTCATCGACCCGGGCTTCACCGGGCACGTCACCCTGGAGCTGTCCAACACGGCCACCATGCCCATCAAGCTCTGGCCGGGGATGAAGGTGGGGCAGCTGTGTTTCTTCCGCCTGTCCAGCCCCGCCGAGGCCCCCTATGGCTCGGGCGCCACCGGCTCGCGCTACCAGGGCCAGCGCGGACCGACGGCATCGCGCTCCCACCAGTCCTTCCACCGCACCCGCATCCCCGACACCCCGGCGGTCCCCGCCGACGGCGCCGCTCCCATCTCCCAGGAGAAGCACATATGA","VTPPGGPGTIGPVLLSDRDIRTELDAGRVVLDPYDPEMIQPASIDVRLDRWFRLFDNHRYPVIDPAADQEGLTHLVDVGADEPFVLHPGEFVLGATYERITLPDDVAARLEGKSSLGRLGLLTHSTAGFIDPGFTGHVTLELSNTATMPIKLWPGMKVGQLCFFRLSSPAEAPYGSGATGSRYQGQRGPTASRSHQSFHRTRIPDTPAVPADGAAPISQEKHI$","Deoxycytidine triphosphate deaminase","Cytoplasm","Deoxycytidine triphosphate deaminase (dCTPdeaminase)","deoxycytidine triphosphate deaminase ","deoxycytidine triphosphate deaminase","","Wang L., Weiss B. dcd (dCTP deaminase) gene of Escherichia coli: mapping, cloning, sequencing, and identification as a locus of suppressors of lethal dut (dUTPase) mutations. J. Bacteriol. 1992. 174(17):5647-5653. PMID: 1324907","","","

InterPro
IPR003232
Domain

dCTP Deaminase
PD004900	$\"[88-190]T$	Q6AC71_BBBBB_Q6AC71;

InterPro
IPR008180
Domain

DeoxyUTP pyrophosphatase
PF00692	$\"[82-193]T$	dUTPase

InterPro
IPR011962
Family

Deoxycytidine triphosphate deaminase
TIGR02274	$\"[14-194]T$	dCTP_deam: deoxycytidine triphosphate deami

noIPR
unintegrated

unintegrated
G3DSA:2.70.40.10	$\"[13-197]T$	no description

","BeTs to 20 clades of COG0717COG name: Deoxycytidine deaminaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0717 is aompkz-q--r-bcef-hsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB003232 (dCTP Deaminase) with a combined E-value of 1e-15. IPB003232A 93-117 IPB003232B 130-144***** IPB008180 (DeoxyUTP pyrophosphatase) with a combined E-value of 8.8e-13. IPB008180A 102-117 IPB008180B 128-144 IPB008180C 179-188","","","-57% similar to PDB:1XS1 dCTP deaminase from Escherichia coli in complex with dUTP (E_value = 9.0E_33);-57% similar to PDB:1XS4 dCTP deaminase from Escherichia coli- E138A mutant enzyme in complex with dCTP (E_value = 4.5E_32);-57% similar to PDB:1XS6 dCTP deaminase from Escherichia coli. E138A mutant enzyme in complex with dUTP (E_value = 4.5E_32);-53% similar to PDB:1OGH STRUCTURE OF THE BIFUNCTIONAL DCTP DEAMINASE-DUTPASE FROM METHANOCALDOCOCCUS JANNASCHII (E_value = 5.5E_22);-53% similar to PDB:1PKH STRUCTURAL BASIS FOR RECOGNITION AND CATALYSIS BY THE BIFUNCTIONAL DCTP DEAMINASE AND DUTPASE FROM METHANOCOCCUS JANNASCHII (E_value = 5.5E_22);","No significant hits to the Pfam 21.0 database.","","triphosphate deaminase (dCTP deaminase) (dcd)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2599","2798061","2797282","780","6.17","-5.46","27595","ATGCCCTTCTACCACCGCCCGCCCACCGACCGCGGCCCGCTGCGCCCCCGCTCCCCCATGGCCCCCGGCCAGACGTCCGGCGTCCCCACGGCAGATGAGATGGCTGAGGCCGCCGAGGTCGGCTACGCCGTCGTCGACCTGGAGACCACCGGCCTGTCCCCCACGACGGACTCGATCCTGGAGGTCGCGCTCGTGCTCACCGACGCCGCCGGGCGCGTCGAGCGCAGCTGGTCCACGCTCATCGACCCCGGCGCGGGCGTGGGCGTGGGCCCCACCCATATCCACGGTCTTGTCGCCGAGGAGCTCATCGGGGCGCCCGGCTTCGATGAGGTCGCCGACCTTCTGGTGGCCGACCTGGCCGGACGGGCGGTGGTGGCCCACAATGCCCGCTTCGACGTCGGCTTCCTCACCCAGGCGCTGGGAACGCGGGGGCTGCTCGACCGCGGCGCGCGGGTGCCGCGGGTGTGCACGATGGAGTGGGCGCGCCATTTCATGACGACGCCGTCGCGCCGGCTGACCACCTGCTGCGAGGTGGCCGGGGTGGAGATCGGCCACCACCACAACGCGCTCGACGACGCCCTCGCCGCTGCCGGACTGCTGCGCCACTACCTGGCGGTGGGAGCTCAGCGCGGCGAGGAGCCGGTGGCCTGGGCCCGCTCGCTCATTGAGGCTCGCCGGTTCACCGGCTGGCACTGGGACGCGGCAAGGGCTCAGGCCGGCGTCGAGCATCTCACGGAGCGCACCACGCCCGGCGCCGAGCGAGCCCGGCCTGGGACTTAG","MPFYHRPPTDRGPLRPRSPMAPGQTSGVPTADEMAEAAEVGYAVVDLETTGLSPTTDSILEVALVLTDAAGRVERSWSTLIDPGAGVGVGPTHIHGLVAEELIGAPGFDEVADLLVADLAGRAVVAHNARFDVGFLTQALGTRGLLDRGARVPRVCTMEWARHFMTTPSRRLTTCCEVAGVEIGHHHNALDDALAAAGLLRHYLAVGAQRGEEPVAWARSLIEARRFTGWHWDAARAQAGVEHLTERTTPGAERARPGT$","DNA polymerase III, epsilon subunit","Cytoplasm","DNA polymerase III, epsilon subunit","DNA polymerase III; epsilon subunit","Exonuclease, RNase T and DNA polymerase III","","Koonin E.V., Deutscher M.P. RNase T shares conserved sequence motifs with DNA proofreading exonucleases. Nucleic Acids Res. 1993. 21(10):2521-2522. PMID: 8506149","","","

InterPro
IPR006055
Domain

Exonuclease
SM00479	$\"[41-209]T$	EXOIII

InterPro
IPR013520
Domain

Exonuclease, RNase T and DNA polymerase III
PF00929	$\"[42-200]T$	Exonuc_X-T

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[35-204]T$	no description

","BeTs to 16 clades of COG0847COG name: DNA polymerase III epsilon subunit and related 3'-5' exonucleasesFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0847 is a--p--yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB006055 (Exonuclease) with a combined E-value of 2.4e-08. IPB006055A 43-53 IPB006055B 186-200","","","-45% similar to PDB:2P1J Crystal structure of a polC-type DNA polymerase III exonuclease domain from Thermotoga maritima (E_value = 3.5E_10);","No significant hits to the Pfam 21.0 database.","","polymerase III, epsilon subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2600","2796158","2797285","1128","4.41","-32.26","39919","ATGAGCGACTCGACCGACTTCGCCGTCTCCCTGCCCACCGACACCGGCACCTTCACCGCCGCCTCCATGCTGCCGGTCGGGCTGCTGGACACCAACCACGTCCTGCTCCTGGCCGACGACGTCGCCCCCGACGAGGTGGAGGCCCTGGCCCTGTCCCAGGACATCCAGTCCGGCTGGGTGGGGGTCTCCAGCCTCCAGCTCTTCCCCGGGGTCTCCCTGCTGGGGCCCTGGAAGGTCGACGCCGAGATGCGCAGCCTCCTGGGTGCGCCGGAGTGGACCACCCAGCTGATGATCCTGGACTGCCCCCGCATCCGTGCCGGCGCCCTGCCGGCCGAGCTCGCCGGCCTGGACCCGCTCTCCGACGCCTTCCCTCACGCCCAGCCCACGGGGGCCGAGCTGGTGGCCCTCACCCGCCTGCGCGCCATCGCCCGACGCCTGGCCGGGGCCCTGCGGCTCATTCCCGGAGGGGACACCGAGGAGCCGGTGCTGGTCGAGCCCAGCCCGGAGGTCTCGGCCTCCCTGACCATCTACGCCCCGGTGTGGCTCGGCCCGGAGGACCTGGTGGCCGTCCTGCAGCCCGTGGCCCCCGAGGTGAGCGCCGCGCTGGAGGCTGTTCAGCCCCGCGGCGCCGTCGGGCTGGACGCCATCGACCCCGAGCAGCTGGAGAGCCTCGTCGAGCGCATCGGCCCGGACGTCTTCGAGAAGGCCTGGCGCGGCTCGGAGAAGGTCCGCCAGGACACGATGCGTCAGGAGATCGTCGCCGCCGCCACCGGCAACGTCATTGAGGAGGTGCGTGACGGCTACGCGGTCGTCACCCCGGTCGACCCCGAGCACGAGGGCTGGGGGCGCATCGAGGTGCGGGCCGGCGCCACCGACGGGCTGCCCCTGGCCGTGCGCGGCGAGCCGTGGGCGCGCGGGGCGGTCCTGTCCTACGACCTGCGTTGGATCCCCCTGGACCAGGCTGACGCCTACGCCGAAGTGGTCTCCCGCTCCCGACGCCGCGAGCGCCAGACCGCCCGGGACCTGGTCGAGGAGCTCGCCACCGTCCTGGTGGCCGCCGTCTCCGGGGTGGCCGTGGACGACGACGGGTTCCTCGTCTCCCTGGGTGAGGACGCCGAGGAGGCCTAA","MSDSTDFAVSLPTDTGTFTAASMLPVGLLDTNHVLLLADDVAPDEVEALALSQDIQSGWVGVSSLQLFPGVSLLGPWKVDAEMRSLLGAPEWTTQLMILDCPRIRAGALPAELAGLDPLSDAFPHAQPTGAELVALTRLRAIARRLAGALRLIPGGDTEEPVLVEPSPEVSASLTIYAPVWLGPEDLVAVLQPVAPEVSAALEAVQPRGAVGLDAIDPEQLESLVERIGPDVFEKAWRGSEKVRQDTMRQEIVAAATGNVIEEVRDGYAVVTPVDPEHEGWGRIEVRAGATDGLPLAVRGEPWARGAVLSYDLRWIPLDQADAYAEVVSRSRRRERQTARDLVEELATVLVAAVSGVAVDDDGFLVSLGEDAEEA$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2602","2798298","2799149","852","5.08","-8.85","29442","ATGACTACCCCGGACACCCCTCAGGCGCCGGCCCCGGCCCTGCCGGCGCTGGCCGCCTTCCCCTTCCCGACTGCCCTCGTCGTGACCGGCAGGTCCGCCGCCGGTGACGGTGTGCTCCTCGAGGCCGGGGAGGTCGATGAGGTCTTCCCCTTCGCCTCGGTGACTAAGCCGATCGTCGCCTGGGCGGCCCTGGTCGCCGTCGACCGGGGACTGCTGGACCTGGAGGCCCCCGCCGGTGCGCCCGCGCCCGACGGCGCGACCATCGAGAACCTGCTGTCCCACTCCTCGGGAATCGCGGCCAACTCCGACGAGCGCCTGGCGGCTCCGGGCACGCGCCGCATCTACTCCAACCGCGGCATCGAGATCCTGGGGGAGCGCCTTGAGGAGGCCACCGGCACGCCCCTGGAGACCTGGGTGGAGACCACCGTGCTCGAGCCCCTGGGGATGGCCAGTGTCCTCATCCCCGGCTCGCCCGCCCACTCCGGGGAGGGCAGCGCCCGCGACCTGTCCCTGTTCGCCCGCGAGCTGGCCGCGCCCAGGCTCGTCTCGCCCGCGCTCGCGCAGCGCGCCCGCACGCCGGTCCTGCCCGGCCTCGACGGCGTCCTACCCGGCTACGGGCGACAGACCCCCAACCCCTTCGGGCTGGGGGTCGAGGTGCGCGGAGCCAAGTCCCCGCACTGGACGGGGGTCGGCAACAGCGAGCAGACCTTCGGGCACTTCGGCCAGTCGGGCTCCTTCATCTGGGTGGATCCGGTCGCCGAGCGTCAGGCCGTCTTCCTGGGGGCCAAGCCCTTCGGGGCGGTTCACCGGCGGAACTGGTCCGAGCTCTGCGACCAGATCCTGGCCTTGTAG","MTTPDTPQAPAPALPALAAFPFPTALVVTGRSAAGDGVLLEAGEVDEVFPFASVTKPIVAWAALVAVDRGLLDLEAPAGAPAPDGATIENLLSHSSGIAANSDERLAAPGTRRIYSNRGIEILGERLEEATGTPLETWVETTVLEPLGMASVLIPGSPAHSGEGSARDLSLFARELAAPRLVSPALAQRARTPVLPGLDGVLPGYGRQTPNPFGLGVEVRGAKSPHWTGVGNSEQTFGHFGQSGSFIWVDPVAERQAVFLGAKPFGAVHRRNWSELCDQILAL$","Beta-lactamase","Cytoplasm, Membrane, Extracellular","beta-lactamase","hypothetical protein","beta-lactamase","","Knox J.R., Moews P.C. Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration. J. Mol. Biol. 1991. 220(2):435-445. PMID: 1856867Campbell J.I., Scahill S., Gibson T., Ambler R.P. The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an indigenous class A beta-lactamase. Biochem. J. 1989. 260(3):803-812. PMID: 2788410Joris B., Ghuysen J.M., Dive G., Renard A., Dideberg O., Charlier P., Frere J.M., Kelly J.A., Boyington J.C., Moews P.C. The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family. Biochem. J. 1988. 250(2):313-324. PMID: 3128280","","","

InterPro
IPR001466
Family

Beta-lactamase
PF00144	$\"[15-280]T$	Beta-lactamase

noIPR
unintegrated

unintegrated
G3DSA:3.40.710.10	$\"[39-283]T$	no description
PTHR22935	$\"[20-188]T$	PENICILLIN-BINDING PROTEIN
PTHR22935:SF4	$\"[20-188]T$	gb def: Hypothetical protein SCO2380

","BeTs to 9 clades of COG1680COG name: Beta-lactamase class C and other penicillin binding proteinsFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG1680 is ----kz---drlbcef--s--jx---Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2603","2800044","2799235","810","4.97","-12.83","30062","ATGCGCCTGGCCACCTGGAACGTCAACTCCATCCGTACCCGCGTCGACCGCGTCCTGGCCTTCCTGGAGCGTGAGGACATCGACGCCCTGGCGATGCAGGAGATAAAGTGCCGCCCCGACCAGTTCCCGGTCGAGCCCTTCGAGGCGGCCGGCTACGAGCTGGCCATCCACGGCCTCAACCAGTGGAACGGGGTGGCGATCGCCTCACGCGTGGGCCTCGACGACGTCGCCACCTCCTTCCCGGGTCAGCCCGCCTGGGCGGCCAAGCCCGAGGCCGAGCCGGTCGTGGAGGCCCGGGCGCTCGGGGCGACGGTGGGTGCGGCCTCGGATGCGACGCCGGTGCGCCTGTGGAGCCTGTACGTGCCCAATGGCCGCGAGCTCACCCACCCGCACTACACGTACAAGCTCGACTGGCTGCGGGTGCTGCGCGACGACGTCGCCGCCTGGCTCGAGGCCGAGCCCGACCTGCCGCTGGCGCTGGTGGGCGACTGGAACGTGGCGCCCCGGGATGAGGACGTGTGGGACATGAGCGTCTTCGAGGGCGCCACCCACGTCTCCGCACCGGAGCGGGAGGCCTTCGCCGCCTTCGCCGAGGCGGGCATGCGTGAGGTCACGCGCGAGCGGGTCACCAACTACACGTACTGGGACTATCAGAAGCTGCGCTTCCCGAGGAACGAGGGCATGCGCATTGACTTCATCTATGCCTCGCCGGCCCTGGCGGGCCGCGTCACTGGCGCCGCCATCGACCGCGACGAGCGCAAGGGCAAGGGCGCCTCCGACCACGTCCCCGTCATCGTCGAGCTCGACTGA","MRLATWNVNSIRTRVDRVLAFLEREDIDALAMQEIKCRPDQFPVEPFEAAGYELAIHGLNQWNGVAIASRVGLDDVATSFPGQPAWAAKPEAEPVVEARALGATVGAASDATPVRLWSLYVPNGRELTHPHYTYKLDWLRVLRDDVAAWLEAEPDLPLALVGDWNVAPRDEDVWDMSVFEGATHVSAPEREAFAAFAEAGMREVTRERVTNYTYWDYQKLRFPRNEGMRIDFIYASPALAGRVTGAAIDRDERKGKGASDHVPVIVELD$","Exonuclease III","Cytoplasm, Extracellular","Exonuclease III","exodeoxyribonuclease III ","exodeoxyribonuclease III Xth","","Dlaki M. Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases. Trends Biochem. Sci. 2000. 25(6):272-273. PMID: 10838565","","","

InterPro
IPR004808
Family

Exodeoxyribonuclease III xth
PTHR22748	$\"[52-269]T$	AP ENDONUCLEASE
TIGR00633	$\"[1-269]T$	xth: exodeoxyribonuclease III (xth)

InterPro
IPR005135
Domain

Endonuclease/exonuclease/phosphatase
PF03372	$\"[1-268]T$	Exo_endo_phos

noIPR
unintegrated

unintegrated
G3DSA:3.60.10.10	$\"[1-268]T$	no description

","BeTs to 18 clades of COG0708COG name: Exonuclease IIIFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG0708 is a-mp--y--drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB000097 (AP endonuclease, family 1) with a combined E-value of 3.4e-51. IPB000097A 1-13 IPB000097B 27-36 IPB000097C 59-96 IPB000097D 156-190 IPB000097E 212-259","","","-44% similar to PDB:2JC4 3'-5' EXONUCLEASE (NEXO) FROM NEISSERIA MENINGITIDIS (E_value = 3.2E_30);-40% similar to PDB:1AKO EXONUCLEASE III FROM ESCHERICHIA COLI (E_value = 1.1E_17);","No significant hits to the Pfam 21.0 database.","","III (PA4172)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2604","2800109","2800882","774","9.34","5.59","27548","ATGGGAACAGCACTTGTCACCGGGGCCACGAGCGGCCTCGGCCTGGAGATCGCCTGGCAGCTCGCCCAGGCCCGTCATGACCTCGTCCTCGTGGCGCGCACCCCCGAGCGGCTGCGGCAGGTGGCCGAGGAGATGCGCCAGTTCGCAGGCATCCAGGTGGAGACTCTGCAGGCCGACCTATCCAAGCGTGATGAGCTCGAGCGCGTTGCCGAGCGCCTGCGGGAGAAGAGCAAGCCTGTCGGGCTCCTGGTCAACAACGCCGGCTTCGGGCTGGGGCAGCGCTTCGTCGGGGGAGACCTGGCCCGTGAGGAGGATGCCCTCAACGTCATGGTCCGTGCCGTCATGGTGGCCTCCCACGCGGCGGCCGGCGCCATGGTGGAGCGCGGCCGCGGCGCCATTCTCAACGTCTCCTCCATGACCGCGCACACCGCCATGGGAACCTACGCCGCCCACAAGGCCTGGGTGCTGCGCTTCACCGAGGGGCTGGCCAGTGAGCTCGCCGGCACCGGGGTGACCGCCACGGCGCTGTGCCCGGGGCTGGTGCACACCGGCTTCCACGCCGCGGCCGGCATCGACGAGACCCAGTGGAAGGCGCCGCTGTGGCTGGACGCCGAGCGAGTGGCCATCGACGGCCTGGCGGCGGTGCGGCGCGGCCAGGTCATCTGCACCCCGAGCCTGCGCTACCGCAGCGCCAACGCCGTGCTGCGGCTGGCGCCCCGCTGGTTCGTGCGCCGGGCGGTCGGGCCGGAACGCTCCGGCCAGGGGCACGACTGA","MGTALVTGATSGLGLEIAWQLAQARHDLVLVARTPERLRQVAEEMRQFAGIQVETLQADLSKRDELERVAERLREKSKPVGLLVNNAGFGLGQRFVGGDLAREEDALNVMVRAVMVASHAAAGAMVERGRGAILNVSSMTAHTAMGTYAAHKAWVLRFTEGLASELAGTGVTATALCPGLVHTGFHAAAGIDETQWKAPLWLDAERVAIDGLAAVRRGQVICTPSLRYRSANAVLRLAPRWFVRRAVGPERSGQGHD$","Short-chain dehydrogenase/reductase SDR","Cytoplasm","dehydrogenase","short-chain dehydrogenase/reductase SDR","short-chain dehydrogenase/reductase SDR","","Jornvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 1995. 34(18):6003-6013. PMID: 7742302Villarroya A., Juan E., Egestad B., Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 1989. 180(1):191-197. PMID: 2707261Persson B., Krook M., Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 1991. 200(2):537-543. PMID: 1889416Neidle E., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S. cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 1992. 204(1):113-120. PMID: 1740120Benyajati C., Place A.R., Powers D.A., Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 1981. 78(5):2717-2721. PMID: 6789320","","","

InterPro
IPR002198
Family

Short-chain dehydrogenase/reductase SDR
PR00080	$\"[78-89]T$ $\"[131-139]T$ $\"[148-167]T$	SDRFAMILY
PTHR19410	$\"[3-208]T$	SHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106	$\"[2-167]T$	adh_short

InterPro
IPR002347
Family

Glucose/ribitol dehydrogenase
PR00081	$\"[3-20]T$ $\"[78-89]T$ $\"[125-141]T$ $\"[148-167]T$ $\"[169-186]T$	GDHRDH

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[3-242]T$	no description
PTHR19410:SF38	$\"[3-208]T$	17-BETA HYDROXYSTEROID DEHYDROGENASE
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 10 clades of COG0300COG name: Short-chain dehydrogenases of various substrate specificitiesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0300 is -o----y---rlb-ef-hsnuj----Number of proteins in this genome belonging to this COG is 3","***** IPB002347 (Glucose/ribitol dehydrogenase family signature) with a combined E-value of 1.8e-25. IPB002347A 3-20 IPB002347B 78-89 IPB002347C 125-141 IPB002347D 148-167 IPB002347E 169-186***** IPB002424 (Insect alcohol dehydrogenase family signature) with a combined E-value of 8.4e-07. IPB002424E 130-144 IPB002424F 147-165 IPB002424G 170-183","","","-48% similar to PDB:1W4Z STRUCTURE OF ACTINORHODIN POLYKETIDE (ACTIII) REDUCTASE (E_value = 3.7E_20);-48% similar to PDB:1X7G Actinorhodin Polyketide Ketoreductase, act KR, with NADP bound (E_value = 3.7E_20);-48% similar to PDB:1X7H Actinorhodin Polyketide Ketoreductase, with NADPH bound (E_value = 3.7E_20);-48% similar to PDB:1XR3 Actinorhodin Polyketide Ketoreductase with NADP and the Inhibitor Isoniazid bound (E_value = 3.7E_20);-49% similar to PDB:2C07 OXOACYL-ACP REDUCTASE OF PLASMODIUM FALCIPARUM (E_value = 5.3E_19);","No significant hits to the Pfam 21.0 database.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2605","2801157","2801654","498","4.40","-9.90","16780","ATGGCTTCCATTACCTTCCACGGAGACCCCGTTAGCACCGTCGGCGAGCTGCCCGCTGTGGGCTCGACCGCGCCCGCCTTCGACCTCGTAGGCGCCGACCTCGCCCCGGTCACCAGCCAGTCCCTGGCCGGCCGCCGCGTGGTCCTCAACATCTTCCCCTCGGTGGACACCGGGGTGTGCGCCGCCTCCGTGCGCCAGTTCAACAAGCTGGCCTCCGAGCTGGACAACACGACCGTGGTCTGCGTCTCCGCCGACCTGCCCTTCGCCGGAGCCCGCTTCTGCGGTGCCGAGGGCCTCACCAACGTGGTCACCGGCTCGACCTTCCGCTCCACCTTCGGCGCCGACTACGGCGTCACCCTGGCCGACGGCCCGCTGGCCGGCCTGCTGTCGCGTGCTGTCGTGGTCCTCGACGAGTCCGGCAAGGTCATCTACACCGAGCAGGTCCCCGAGGTCGGCCAGGAGCCCGACTACGACGCCGCCGTGGCCGCCCTGTCCTGA","MASITFHGDPVSTVGELPAVGSTAPAFDLVGADLAPVTSQSLAGRRVVLNIFPSVDTGVCAASVRQFNKLASELDNTTVVCVSADLPFAGARFCGAEGLTNVVTGSTFRSTFGADYGVTLADGPLAGLLSRAVVVLDESGKVIYTEQVPEVGQEPDYDAAVAALS$","Peroxiredoxin","Cytoplasm, Extracellular","20 kDa protein","thiol peroxidase ","Redoxin domain protein","","Cha M.K., Kim H.K., Kim I.H. Thioredoxin-linked \"thiol peroxidase\" from periplasmic space of Escherichia coli. J. Biol. Chem. 1995. 270(48):28635-28641. PMID: 7499381","","","

InterPro
IPR002065
Family

Antioxidant Tpx
PTHR10681:SF3	$\"[9-164]T$	PEROXIREDOXIN RELATED
PS01265	$\"[83-94]T$	TPX

InterPro
IPR012335
Domain

Thioredoxin fold
G3DSA:3.40.30.10	$\"[2-165]T$	no description

InterPro
IPR013740
Domain

Redoxin
PF08534	$\"[19-164]T$	Redoxin

noIPR
unintegrated

unintegrated
PTHR10681	$\"[9-164]T$	PEROXIREDOXIN

","BeTs to 9 clades of COG2077COG name: PeroxiredoxinFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG2077 is -------q--rlb-efgh--u-----Number of proteins in this genome belonging to this COG is 1","***** IPB000866 (Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen) with a combined E-value of 7.9e-07. IPB000866A 44-63 IPB000866B 79-93","","","-75% similar to PDB:1XVQ Crystal structure of thiol peroxidase from Mycobacterium tuberculosis (E_value = 4.7E_53);-74% similar to PDB:1Y25 structure of mycobacterial thiol peroxidase Tpx (E_value = 5.7E_51);-76% similar to PDB:1QXH Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State (E_value = 7.5E_51);-70% similar to PDB:1Q98 Structure of a Thiol Peroxidase from Haemophilus influenzae Rd (E_value = 1.4E_44);-61% similar to PDB:1PSQ Structure of a probable thiol peroxidase from Streptococcus pneumoniae (E_value = 3.3E_30);","No significant hits to the Pfam 21.0 database.","","kDa protein (P20)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2606","2801778","2802347","570","4.99","-10.58","19734","GTGAGCACCAACGACTCCCACATCACCCGCCTGGCCGAGCTCGTCAACGAGCTGTCCGTCGTCCGTGGCAAGGTCACCCTCGCCTCCGGCCTCGAGTCCGACTTCTACGTGGACATGCGCCGCGCCACCCTCCACCACGAGGCCGCCCCTCTCATTGGCCACGTCATGCTCGACATGCTCGAGGAGGCGGGCCTGGGCACCGACGAGATCGATGCCGTCGGCGGCCTGACCATGGGGGCCGACCCCGTGGCCGCCGCCATGCTGCACGCCGCGGCCTCGCGCGGCCTGGACCTGGACGCCTTCGTCGTGCGCAAGGCCGCCAAGGACCACGGCATGCGCCGGCGCATCGAGGGACCCGACGTCGCCGGGCGCTCCGTGGTGGTCCTGGAGGACACCTCCACCACCGGCGGCTCACCCCTGGAGGCCGTCGAGGCCCTGCGCGAGGCGGGTGCCGACGTGCGGGCCGTGGCCGTCATCGTGGACCGGGCCACCGGCGCGCGCGAGCGCATCGAGGCCGCTGGCCTGCCCTACTACGCGGCGCTCGGTCTGGCCGACCTCGGCCTGGAGTGA","VSTNDSHITRLAELVNELSVVRGKVTLASGLESDFYVDMRRATLHHEAAPLIGHVMLDMLEEAGLGTDEIDAVGGLTMGADPVAAAMLHAAASRGLDLDAFVVRKAAKDHGMRRRIEGPDVAGRSVVVLEDTSTTGGSPLEAVEALREAGADVRAVAVIVDRATGARERIEAAGLPYYAALGLADLGLE$","Orotate phosphoribosyltransferase","Cytoplasm","orotate phosphoribosyltransferase","orotate phosphoribosyltransferase ","orotate phosphoribosyltransferase","","","","","

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[38-169]T$	Pribosyltran

InterPro
IPR004467
Domain

Orotate phosphoribosyl transferase
TIGR00336	$\"[13-186]T$	pyrE: orotate phosphoribosyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2020	$\"[3-186]T$	no description

","BeTs to 21 clades of COG0461COG name: Orotate phosphoribosyltransferaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0461 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-71% similar to PDB:2P1Z Crystal structure of phosphoribosyltransferase from Corynebacterium diphtheriae (E_value = 9.0E_41);","No significant hits to the Pfam 21.0 database.","","phosphoribosyltransferase (pyrE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2607","2802401","2803099","699","5.96","-5.16","25045","CTGCCTGAGGGGGAGCACCTGTCCGCGGCGTCCCCAGCGGATTCTGTGTCGGGTCTGGAGGAGGACCGGCCGGCCGACATCCGTCAGGTGGGCGTCGGCCCCTGGCCCGGCGGCCCCGAGGCGTGGCCCGCCGACCCCCGCTACGACCGCGAGCTGCTCGCCGACGGCGACCGGCGCAATGTCGTCGACCGCTACCGCTACTGGACCGTCGCGGCCATCCGCGCCGACCTGGCCGCCCGCGCCCACCGGCTGCACATCGCCATCGAGAACGTCAGCCAGGACCTCAACATCGGCTCCATCGTGCGCAGTGCCAACGCCTTCAATGTGGCCGGCGTCCACATCATTGGCCGACGCCGCTGGAACAAGCGCGGCGCCATGGTCACCAACCGCTACCTGGACGTGCGCCACCACCCCGAGCCCGGCGAGCTGCTCGCCTGGGCGCAAGCCGAGGGCTACGAGGTCGTCGGCATCGACAACGGCCCCGGGGCCCAGCCCCTGGAGTCCGCCGACCTGCCCGAGCGCTGCCTCATGGTCTTCGGCTCCGAGGGGGAGGGCATCAGCGCCGAGCTGAGCGCCGGCTGCTCCCGACTGCTGCGCATCGGTCAGTACGGCTCCACCCGCTCCATCAACGTGGCGGCCGCCGCGGCCGTGGCCATGCACTCCTGGATCCTCCAGCACGCGGGACCGGCGCCCGACTGA","LPEGEHLSAASPADSVSGLEEDRPADIRQVGVGPWPGGPEAWPADPRYDRELLADGDRRNVVDRYRYWTVAAIRADLAARAHRLHIAIENVSQDLNIGSIVRSANAFNVAGVHIIGRRRWNKRGAMVTNRYLDVRHHPEPGELLAWAQAEGYEVVGIDNGPGAQPLESADLPERCLMVFGSEGEGISAELSAGCSRLLRIGQYGSTRSINVAAAAAVAMHSWILQHAGPAPD$","tRNA/rRNA methyltransferase (SpoU)","Cytoplasm","rRNA methylases","tRNA/rRNA methyltransferase (SpoU)","tRNA/rRNA methyltransferase (SpoU)","","Persson B.C., Jager G., Gustafsson C. The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity. Nucleic Acids Res. 1997. 25(20):4093-4097. PMID: 9321663Koonin E.V., Rudd K.E. SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases. Nucleic Acids Res. 1993. 21(23):5519-5519. PMID: 8265370Sirum-Connolly K., Mason T.L. Functional requirement of a site-specific ribose methylation in ribosomal RNA. Science 1993. 262(5141):1886-1889. PMID: 8266080","","","

InterPro
IPR001537
Domain

tRNA/rRNA methyltransferase, SpoU
PD001243	$\"[96-210]T$	Q6A685_PROAC_Q6A685;
PF00588	$\"[83-220]T$	SpoU_methylase

noIPR
unintegrated

unintegrated
G3DSA:3.40.1280.10	$\"[62-226]T$	no description
PTHR12029	$\"[47-225]T$	RNA METHYLTRANSFERASE
PTHR12029:SF7	$\"[47-225]T$	RRNA METHYLASE

","BeTs to 18 clades of COG0566COG name: rRNA methylasesFunctional Class: JThe phylogenetic pattern of COG0566 is a---YQvCEBRHujgpOLinxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","methylases ","","1","","","Thu Aug 9 15:22:58 2007","","Thu Aug 9 15:22:58 2007","","","Thu Aug 9 15:22:58 2007","Thu Aug 9 15:22:58 2007","Thu Aug 9 15:22:58 2007","","","Thu Aug 9 15:22:58 2007","","","Thu Aug 9 15:22:58 2007","Thu Aug 9 15:22:58 2007","","","Thu Aug 9 15:22:58 2007","Thu Aug 9 15:22:58 2007","","","","","yes","","" "ANA_2608","2803308","2804357","1050","5.18","-12.38","37379","GTGGCCATTGCAACCCCGGAGTCCTACGCCGACATGCTTGACCGCGCGAAGGCCGGCAAGTACGCCATCCCCGCGATCAACGTCACCTCGTCCCAGACTCTGTCCGCCGCCCTCAAGGGCTTCGCCGACGCCGAGTCCGACGGCATCGTCCAGATCTCCAACGGTGGTGCCGCCTACTGGTCCGGTTCCTCGCGCCTCGACCGCGTCAAGGGCTCGATCGCCTTCGCCGCTTACGCCCGCGCCGTGGGTGACCTCTACCCCGTCACCATTGGTCTGCACACCGACCACTGCCCCAAGAAGCTCCTGGCCGACTGGATCCACCCGCTCCTGGAGATCGAGGCCGAGCAGGTCAAGAACGGTGAGCTGCCGATGTTCAACTCCCACATGTGGGACGGCTCTGCCGAGGCCCTCGACGACAACATCGAGATCGCCGTCGACATGCTCAAGCGCGCCAAGGCCGCCAACGTCGTCCTCGAGATCGAGATCGGTGCCGTGGGTGGCGAGGAAGACGGCATCAAGGGTGAGGAGAACGCCAACCTCTACACCACCGCCGACGACGCCTGGAAGGCCATCGAGGCCCTCGGTCTGGGTGAGAACGGCCGCTACATCACCGCTCTGACCTTCGGCAACGTGCACGGCTCCTACAAGCCCGGCCACGTCAAGCTCCGCCCGGAGATCCTCGGCGAGATCCAGGAGGACGTGGCCAAGCGCCTCGGCGACCGCCTGTCCTCCAAGGTCGGCGACAAGAGCTCGCCCTTCGACCTGGTCATGCACGGCGGCTCCGGCTCCACCGACGAGGAGATCGCCACCGCGGTGCGCAACGGCGTCATCAAGATGAACGTCGACACCGACACCCAGTACGCCTACACCCGTCCGGTCGCCGGCTGGATGTACACCAACTACGAGGGTGTCCTCAAGATCGACGGCGAGGTCGGCAACAAGAAGCAGTACGACCCGCGCGCCTGGGGCAAGGCCGCCGAGGAGGGCATGGCCGCTCGCGTCGTCGAGGCCTGCGAGCGTCTCGGCTCCGTCGGCTCCGCCCGCAAGTGA","VAIATPESYADMLDRAKAGKYAIPAINVTSSQTLSAALKGFADAESDGIVQISNGGAAYWSGSSRLDRVKGSIAFAAYARAVGDLYPVTIGLHTDHCPKKLLADWIHPLLEIEAEQVKNGELPMFNSHMWDGSAEALDDNIEIAVDMLKRAKAANVVLEIEIGAVGGEEDGIKGEENANLYTTADDAWKAIEALGLGENGRYITALTFGNVHGSYKPGHVKLRPEILGEIQEDVAKRLGDRLSSKVGDKSSPFDLVMHGGSGSTDEEIATAVRNGVIKMNVDTDTQYAYTRPVAGWMYTNYEGVLKIDGEVGNKKQYDPRAWGKAAEEGMAARVVEACERLGSVGSARK$","Fructose-bisphosphate aldolase, class II","Cytoplasm","fructose-bisphosphate aldolase, class II","fructose-bisphosphate aldolase ","fructose-bisphosphate aldolase, class II","","Perham R.N. The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes. Biochem. Soc. Trans. 1990. 18(2):185-187. PMID: 2199259Marsh J.J., Lebherz H.G. Fructose-bisphosphate aldolases: an evolutionary history. Trends Biochem. Sci. 1992. 17(3):110-113. PMID: 1412694Berry A., Marshall K.E. Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett. 1993. 318(1):11-16. PMID: 8436219","","","

InterPro
IPR000771
Family

Ketose-bisphosphate aldolase, class-II
PD002376	$\"[3-339]T$	Q6ADV3_BBBBB_Q6ADV3;
PIRSF001359	$\"[4-347]T$	Fructose-bisphosphate aldolase II
PF01116	$\"[5-347]T$	F_bP_aldolase
TIGR00167	$\"[4-347]T$	cbbA: ketose-bisphosphate aldolases
PS00602	$\"[86-97]T$	ALDOLASE_CLASS_II_1
PS00806	$\"[158-169]T$	ALDOLASE_CLASS_II_2

InterPro
IPR006411
Family

Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype
TIGR01520	$\"[1-347]T$	FruBisAldo_II_A: fructose-bisphosphate aldo

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[3-345]T$	no description

","BeTs to 16 clades of COG0191COG name: Fructose/tagatose bisphosphate aldolaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0191 is ------yqvdrlbcefgh-nuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB000771 (Ketose-bisphosphate aldolase, class-II) with a combined E-value of 7.7e-68. IPB000771A 12-59 IPB000771B 88-99 IPB000771C 122-133 IPB000771D 158-171 IPB000771E 204-216 IPB000771F 257-288 IPB000771G 313-330","","","-54% similar to PDB:1B57 CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE IN COMPLEX WITH PHOSPHOGLYCOLOHYDROXAMATE (E_value = 4.5E_54);-54% similar to PDB:1GYN CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE (E_value = 4.5E_54);-54% similar to PDB:1ZEN CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (E_value = 4.5E_54);-54% similar to PDB:1DOS STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE (E_value = 3.9E_53);-42% similar to PDB:2FJK Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus (E_value = 1.4E_15);","No significant hits to the Pfam 21.0 database.","","aldolase, class II (fbaA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2609","2804758","2806101","1344","5.15","-11.31","48505","ATGCGACTCATCTCCCGCCGCTCCATGCTCGGTGGAACTGCTGCGATCGCCGTCGCCGCGACCCTGGCGGCCTGCTCGAAGGGCTCGTCCGGTTCCGACGGCGCCGGAGGCGTCTACTTCCTCAACTTCAAGCCCGAGTCGGAGCAGGCCTTCAAGGACATCGCGGCCGCCTACACCAAGAAGACCGGTGTGAACGTCAAGGTCGTCACCGCTGCTTCCGGCACCTACGAGCAGACCCTGAAGTCGGAGGTCGCCAAGTCCAACCCGCCCACGTTGTTCAACCTCAACGGCCCCGTGGGCTACGGCAACTGGAAGGACTACGCCTCCGACCTGTCCGACGCCGACTTCACCAAGCAGCTGACGGATGAGTCCATGGCCCTCAAGGGCGACGAGGGCAAGGTCGTGGGCGTCCCGCTGGCCATCGAGGGCTACGGCATCATCTACAACGCCGCCATCCTCAAGAAGTACTTCGGCATGGAGGGCGCCAAGGCCACCTCCGTCGAGGAGATCAAGGGCTTCGACAAGCTCAAGGAGGTCGTCGAGGACATGCAGTCCAAGAAGGCCGACCTCGGTATCGAGGGCGTCTTCGCCGCGACCTCGCTGTCCCCCGGTGAGGACTGGCGCTGGCAGACCCACCTGGCCAACTACCCCGTCTACTACGAGTACCGCGACGCCAAGGTCGACGACCTCGACGAGGTCAAGCTGACCTACTCGGAGAACTACAAGAAGATCTTCGACCTCTACCTCAACAACTCCACCATCAAGCCCACCGAGGCCAGCGCCAAGACGGTCACCGACTCCATGGCCGACTTCGCCCTGGGCAAGGCCGCCATGGTTCAGAACGGCAACTGGGGCTGGTCGCAGATCTCCGAGGTCTCGGGCAACACGGTCAAGGCCGAGGACGTCCACTTCATGCCGATCTACGTCGGCGTCTCCGGCGAGGACAAGTCCAACATCGCCATCGGCACCGAGAACTACCTGACGATCAACTCCCAGGCCGCCGAGGGTGACCAGAAGGCCACCAAGGACTTCCTCACCTGGCTGTTCACCGACGCCGAGGGCTCCAAGATGGCCGCCGAGAAGCTCAGCATCATCGCGCCCTACAAGGCATACGCCGAGCTGGCCCCCTCTGACCCGCTGGGCAAGGAGGTCTCCGCGGCCATCAACAACAAGGACCTCACGCCCGTCAAGTGGGTCTTCCCGACCTTCCCGAGCCAGGACTTCAAGGACCAGCTCGGCCAGCACCTGGCGCAGTACGCCTCCGGCAGCGAGGACTGGGCGAAGGTCAAGGACTTCTTCGTGACCACCTGGGCCTCCGAGAAGAAGGCCTCCAAGGAGGGCTGA","MRLISRRSMLGGTAAIAVAATLAACSKGSSGSDGAGGVYFLNFKPESEQAFKDIAAAYTKKTGVNVKVVTAASGTYEQTLKSEVAKSNPPTLFNLNGPVGYGNWKDYASDLSDADFTKQLTDESMALKGDEGKVVGVPLAIEGYGIIYNAAILKKYFGMEGAKATSVEEIKGFDKLKEVVEDMQSKKADLGIEGVFAATSLSPGEDWRWQTHLANYPVYYEYRDAKVDDLDEVKLTYSENYKKIFDLYLNNSTIKPTEASAKTVTDSMADFALGKAAMVQNGNWGWSQISEVSGNTVKAEDVHFMPIYVGVSGEDKSNIAIGTENYLTINSQAAEGDQKATKDFLTWLFTDAEGSKMAAEKLSIIAPYKAYAELAPSDPLGKEVSAAINNKDLTPVKWVFPTFPSQDFKDQLGQHLAQYASGSEDWAKVKDFFVTTWASEKKASKEG$","ABC-type multiple sugar transport system, periplasmic component","Membrane, Periplasm, Extracellular","ABC-type transporter, periplasmic component","ABC-type sugar transport system; periplasmic component","extracellular solute-binding protein, family 1","","Tam R., Saier Jr M.H. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 1993. 57(2):320-346. PMID: 8336670Sharff A.J., Rodseth L.E., Szmelcman S., Hofnung M., Quiocho F.A. Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. J. Mol. Biol. 1995. 246(1):8-13. PMID: 7853407","","","

InterPro
IPR006059
Family

Bacterial extracellular solute-binding protein, family 1
PF01547	$\"[9-156]T$	SBP_bac_1

InterPro
IPR006061
Domain

Bacterial extracellular solute-binding family 1
PS01037	$\"[138-155]?$	SBP_BACTERIAL_1

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[4-31]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
G3DSA:3.40.190.10	$\"[32-390]T$	no description
PS51257	$\"[1-25]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-19]?$	signal-peptide

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","transporter, periplasmic component","","1","","","","","","","","","","","Tue Aug 14 17:27:13 2007","","Tue Aug 14 17:27:13 2007","","","Tue Aug 14 17:27:13 2007","","","","Tue Aug 14 17:27:13 2007","Tue Aug 14 17:27:13 2007","","","","","yes","","" "ANA_2610","2806152","2807138","987","10.27","16.55","36149","TTGCGACGGCGACTCATCTCCCCATCCCCTCTCCCGCCGGGGCGGCACGTTCGAGCCGTTCGTCTCGCGCGCTGCCGCCCCGGTGGGAGCTCTCTGGTACCCGGCCACTCCGGCGGGTGCCGGTCGCACCTCGAGGCAGATATGACCAAGGCACTGAAAAAGTTCTTCCCAGTTTTTGCAGGGCCAACCCTGTTGGCCTTCATGATCGCGTTCATCGTCCCCTTCTTCATGGGGCTCTATCTCTCCTTCACCAAGTTCAGCACCCTCACCAATGCGCGGTTCGTGGGCACTGACAACTACGCCAGGGCACTGGGGGAGCGCAGCGACTTCCCGCAGGCGCTCGTTTTCACTGCCGTTGTCTCGATCATCTCGATCATCACGGTGAACCTGGGGGCCTTCGCCCTGGCCTACTTCCTGACCCGCAAGCTGCGCGGCACCAACTTCTTCCGTGCCGTGTTCTTCATGCCCAACCTCATCGGCGGCATCGTCCTGGGATACACCTGGCAGGTGATGCTCAACGCGATTCTTCAGCGCTGGGGCCAGACGATCGTCAACGACTGGCGACTGGGGCTGGCCGGACTGGTCATGCTCGTCAACTGGCAGCTCATGGGCTACATGATGGTCATCTACATCGCCGGTCTGCAGAACGTGCCGCCCGAGCTCATCGAGGCCTCGCAGATCGACGGCGCCGGTAGGTGGCAGACGCTGCGCAACGTAACGCTGCCGATGATCATGCCCTCGATCACCATCTGCCTGTTCCTCACTCTGGCCAACACCTTCAAGATGTACGACCAGAACCTCGCCCTGACCAACGGTGCGCCCGCTAAGCAGACTCAGATGGCCGCTCTCAGCATCGTCAACACCATGTACAAGAAGATCGGCCAGGAGGGCGTCGCCCAGGCCGAGGCCGTCATCTTCTTCCTCATCGTCGCCGCCATCGCGCTCATCCAGCTGAGCGCCACTCGTTCCAAGGAGGTCGACGCGTGA","LRRRLISPSPLPPGRHVRAVRLARCRPGGSSLVPGHSGGCRSHLEADMTKALKKFFPVFAGPTLLAFMIAFIVPFFMGLYLSFTKFSTLTNARFVGTDNYARALGERSDFPQALVFTAVVSIISIITVNLGAFALAYFLTRKLRGTNFFRAVFFMPNLIGGIVLGYTWQVMLNAILQRWGQTIVNDWRLGLAGLVMLVNWQLMGYMMVIYIAGLQNVPPELIEASQIDGAGRWQTLRNVTLPMIMPSITICLFLTLANTFKMYDQNLALTNGAPAKQTQMAALSIVNTMYKKIGQEGVAQAEAVIFFLIVAAIALIQLSATRSKEVDA$","ABC-type multiple sugar transport system, permease component","Membrane, Cytoplasm","ABC-type transporter, permease components","K02025 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[110-325]T$	BPD_transp_1
PS50928	$\"[114-317]T$	ABC_TM1

noIPR
unintegrated

unintegrated
tmhmm	$\"[56-76]?$ $\"[113-133]?$ $\"[148-168]?$ $\"[187-209]?$ $\"[239-257]?$ $\"[298-318]?$	transmembrane_regions

","BeTs to 13 clades of COG1175COG name: ABC-type sugar transport systems, permease componentsFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1175 is -o-pkz--vdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","transporter, permease components (permease)","","1","","","","","","","","","","","Tue Aug 14 17:27:49 2007","","Tue Aug 14 17:27:49 2007","","","Tue Aug 14 17:27:49 2007","","","","Tue Aug 14 17:27:49 2007","Tue Aug 14 17:27:49 2007","","","","","yes","","" "ANA_2611","2807135","2808031","897","9.17","5.12","32056","GTGAGCACCGCCGTCAAGACTCAGTCCCCCGCTTCCGCCGCCCCTGCCGGTCAGAAGGTCGCTCCGCAGACGACGGGGCAGAAGACGCTCGTGGGGCTGCTGGCCGTCCTGGCCTTCGTGTGGGTCATTCCGCTGGCCTTCATCGTCATCAACTCCTTCAAGGGCAAGTTCTACATCTCCGACAGCCCCTTCGCCCTGCCGACGGCGAAGACCTTCGCCGGTCTGGACAACTACGCCACCGGCCTGGCCCTGTCGGGCTTCGCCAGCGCCATGGGCTGGTCGCTGTTCATCACCGTGGGCTCCGTCGCCGTCATCGTGTTCCTCACGGCAATGACCGCCTACTACATCACCCGCATCAAGACGTGGTGGACCTCCATGATCTACTACGCCTTCGCCTTCTCCATGATCGCTCCCTTCCAGATGGTCATGTTCCCCACCGTCAAGGTGGCTGACCTGCTCGGCCTGGCCACGCCCTGGGGCATGATCGTTCTCTACCTCGGTTTCGGTGGGGGGCTGTCGGTGTTCCTGTTCGCCGGCTTCATCAAGTCGATCCCCATGGAGATCGAGGAGGCCGCCTACATGGACGGCTGCTCCCCGCTGCAGACCTACTTCAAGGTGGTCATGCCGCTGCTCAAGCCGACAGCGGTCACGGTGGCGATCCTCAACGCCATGTGGGTGTGGAACGACTTCCTCCTGCCCAACCTCGTCATCGGCCAGGACGAGCGCTACAAGACGGTCCCGATCGTCATCCAGTCCCTTGTCGGCTCCAACGGCAACCGAGACATGGGCGCCCAGATGGCCATGCTCGTCTTCGCCATCGTCCCGATCGTCGCCTTCTACCTCTTCGGTCAGAAGCACATCATCGAGGGTGTGGCCGCGGGGGCGGTCAAGGGCTAA","VSTAVKTQSPASAAPAGQKVAPQTTGQKTLVGLLAVLAFVWVIPLAFIVINSFKGKFYISDSPFALPTAKTFAGLDNYATGLALSGFASAMGWSLFITVGSVAVIVFLTAMTAYYITRIKTWWTSMIYYAFAFSMIAPFQMVMFPTVKVADLLGLATPWGMIVLYLGFGGGLSVFLFAGFIKSIPMEIEEAAYMDGCSPLQTYFKVVMPLLKPTAVTVAILNAMWVWNDFLLPNLVIGQDERYKTVPIVIQSLVGSNGNRDMGAQMAMLVFAIVPIVAFYLFGQKHIIEGVAAGAVKG$","ABC-type multiple sugar transport system, permease component","Membrane, Extracellular","ABC-type transporter, permease components","K02026 multiple sugar transport system permease protein","binding-protein-dependent transport systems inner membrane component","","Ames G.F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 1986. 55:397-425. PMID: 3527048Higgins C.F., Hyde S.C., Mimmack M.M., Gileadi U., Gill D.R., Gallagher M.P. Binding protein-dependent transport systems. J. Bioenerg. Biomembr. 1990. 22(4):571-592. PMID: 2229036Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985. 4(9):2287-2293. PMID: 3000770Saurin W., Koster W., Dassa E. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 1994. 12(6):993-1004. PMID: 7934906Pearce S.R., Mimmack M.L., Gallagher M.P., Gileadi U., Hyde S.C., Higgins C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 1992. 6(1):47-57. PMID: 1738314","","","

InterPro
IPR000515
Family

Binding-protein-dependent transport systems inner membrane component
PF00528	$\"[87-293]T$	BPD_transp_1
PS50928	$\"[91-283]T$	ABC_TM1

noIPR
unintegrated

unintegrated
signalp	$\"[1-45]?$	signal-peptide
tmhmm	$\"[30-50]?$ $\"[71-89]?$ $\"[95-117]?$ $\"[127-147]?$ $\"[161-181]?$ $\"[206-226]?$ $\"[263-283]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-46]?$	signal-peptide
tmhmm	$\"[90-110]?$ $\"[129-149]?$ $\"[170-190]?$ $\"[196-216]?$	transmembrane_regions

InterPro
IPR001451
Repeat

Bacterial transferase hexapeptide repeat
PS00101	$\"[14-42]?$	HEXAPEP_TRANSFERASES

noIPR
unintegrated

unintegrated
signalp	$\"[1-23]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[47-69]?$ $\"[74-94]?$	transmembrane_regions

InterPro
IPR001114
Family

Adenylosuccinate synthetase
PD001188	$\"[1-74]T$	Q6ACB0_BBBBB_Q6ACB0;
PTHR11846	$\"[3-427]T$	ADENYLOSUCCINATE SYNTHETASE
PF00709	$\"[3-422]T$	Adenylsucc_synt
SM00788	$\"[3-422]T$	no description
TIGR00184	$\"[5-428]T$	purA: adenylosuccinate synthetase
PS00513	$\"[131-142]T$	ADENYLOSUCCIN_SYN_2
PS01266	$\"[10-17]T$	ADENYLOSUCCIN_SYN_1

noIPR
unintegrated

unintegrated
G3DSA:3.40.440.10	$\"[4-264]T$	no description
G3DSA:3.90.170.10	$\"[265-427]T$	no description

","BeTs to 21 clades of COG0104COG name: Adenylosuccinate synthaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0104 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB001114 (Adenylosuccinate synthetase) with a combined E-value of 1.7e-146. IPB001114A 5-59 IPB001114B 125-150 IPB001114C 217-255 IPB001114D 293-334 IPB001114E 366-413","","","-61% similar to PDB:1ADE STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE PH 7 AT 25 DEGREES CELSIUS (E_value = 2.4E_103);-61% similar to PDB:1ADI STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE AT PH 6.5 AND 25 DEGREES CELSIUS (E_value = 2.4E_103);-61% similar to PDB:1CG0 STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI COMPLEXED WITH HADACIDIN, GDP, 6-PHOSPHORYL-IMP, AND MG2+ (E_value = 2.4E_103);-61% similar to PDB:1CH8 STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI COMPLEXED WITH A STRINGENT EFFECTOR, PPG2':3'P (E_value = 2.4E_103);-61% similar to PDB:1CIB STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI COMPLEXED WITH GDP, IMP, HADACIDIN, AND NO3 (E_value = 2.4E_103);","No significant hits to the Pfam 21.0 database.","","synthetase (purA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2616","2811399","2813306","1908","8.56","7.68","66584","GTGAGTGATAGCGGCTACTCGACGGCACCGCACGCAGGAAGTGGTGTAGAGACCTTCCGAGAGCGTGCCGACCGTGGGCGAGCCGCCCAGGGGTGCCTGGTCAAGGTACTCGGCGCCCTCGTCCTCGTCGGTGGCCTCCTGTGCCTGCGCGGCCCTGAGAAGCCACTGGGCGTCATGCTGGTGGTGGGCAGCCTGAGCCTGGCCCTGTACGGGGCGGGCAGGACAGCCCTGAGCCGTCGGATCGAGCGGTCCGCCGACTACTGGAGCCAAGGGCCCGGATGTGTCCAGTTCGGGCCCTCACGCCCCAGTGGCCTGCAGGAGTATCTGCCTGGAGCGGTGGCGTCTATCGGTGCGCTGACCGCTGTGGGGATGCAGCTCTTCTCCGCCGCGGCCTCTCCCAACGGCGTATGGACAATCGCCTTGGCCGTCGTCGTGCTGCTCGGCTGGCTGGTGGGCTGTGTCACTATTCCTACCGGTGGCAGAGGAGCGCCGGAGATCGTCCTGACGCCGGAGGCGGTATGGATCTGGGCGGGTGGGCACACACGAGTCCGCATCCCCTGGGCGGCGCGGCCGAATCTTGCGGCAAGCATGACTCATCGCATGCGACCGCACGCCGTGATCACCGGTGGTGCGGGAGGGCCGGTGAACTTCCCCATTTTCGTGGTGCCCATTGGGCACGTTCAGCTTCAGTCCGTGCTCGAGCTCTACTCGATTCATGCCGAGCTGCGAGGCGAGCTCAGCACTGGTCAAGGGCTGCAGCGGGTGCGCGCACTCATGACCCCTCCCGTGCAGGAGGGTGAGGGGGCTGCCTCCGGCGTCCCCGTGCAGGCTTCGACGCCGGAAGTGGGCGCATCAGTGTCTCCGACGCCGGTGTATGGGGCGGCACCGGGTTCGGATTCTCCGTATGAGGGTATCCAGTACGGCGGCCCCCAAGGTGGACAGCCACCCCAGGGTGTGGAGTCCTACGGCTCTTCGGGTGCCCAGGCATCGGTGCCTGGATCGGCCGAGCCCCTCCCCGCAGTCCCGTACGGTTCCCCGACTCCGTCTGCTCCCGCAGGGGAGGGTGTCGGGCATGCCTCGCTCGAGGCGGTGCCGCACGTCCCAGCAGACGCGGAGCGTGGCGCAGGGGAGGAGGACCAGGGAGAAAAGTCCTCCCAGCCGAGCACGTGCGAGGAAGCTGACCGACGCGCTCGGCGAGCACCATGGAGGTTCCTGATCTGGGCAGTCGTCGTCCTGATCGGATTCACGTATGCGACGAGCGGGAGACAGACCGCGGGCTTCCTTCTGGGGATGGTCCTCAGCCTGGTGCTCCTCATTCACGCCGTTTCGCTCGCCGCAGCACGCAGGTCTCGAACGGTGGCCCCTCGGCGCTGGATGTGGAGCAGTGAGGGAATCTGCCTGCGGAACACGTGGTTCGTCCAGGTGGTGGTTCACGTGGAGGCGGCGCTCATGGCACTCGGGGGCCTGCTGGCCGTCGGGCTCCTGGCAGTCAGTGACCGCAGTGATCGGGGAGCCGTGGTGGTGCCTTTCCTTCTCGCCATGGTCTTCCTCATCGCCTCCTTCTTCATGGGGTTCGTGAAGCCGCTGCCCGGGCGACGCACGGAGATCGTTCTTGACCCGGAGCGCATCCGCTTCGCCGTAGGGACGAGCCGCGAGTCGCTGTTCTGGTGGGCTGACCGCCCACGGCTCGTGGGCCGCAGCGCCAGTGGGAACCTCGTCATTGAGAACGATCGGGTCGGTCGCATCCGGGCCGAGATGGACACTCTTCCTCTGACCAGTGTGCAGTTGCAGCGGGTGGTGGCGTTCTACTCGCATCATCCTGAGCTGTGCGCCGAGCTCGCGACTGAGCAGGGGCTGGCGCGTGTACAGGGACTGACGGGGCCGGCCTCAGTGGCGCCGTTGCGGTGA","VSDSGYSTAPHAGSGVETFRERADRGRAAQGCLVKVLGALVLVGGLLCLRGPEKPLGVMLVVGSLSLALYGAGRTALSRRIERSADYWSQGPGCVQFGPSRPSGLQEYLPGAVASIGALTAVGMQLFSAAASPNGVWTIALAVVVLLGWLVGCVTIPTGGRGAPEIVLTPEAVWIWAGGHTRVRIPWAARPNLAASMTHRMRPHAVITGGAGGPVNFPIFVVPIGHVQLQSVLELYSIHAELRGELSTGQGLQRVRALMTPPVQEGEGAASGVPVQASTPEVGASVSPTPVYGAAPGSDSPYEGIQYGGPQGGQPPQGVESYGSSGAQASVPGSAEPLPAVPYGSPTPSAPAGEGVGHASLEAVPHVPADAERGAGEEDQGEKSSQPSTCEEADRRARRAPWRFLIWAVVVLIGFTYATSGRQTAGFLLGMVLSLVLLIHAVSLAAARRSRTVAPRRWMWSSEGICLRNTWFVQVVVHVEAALMALGGLLAVGLLAVSDRSDRGAVVVPFLLAMVFLIASFFMGFVKPLPGRRTEIVLDPERIRFAVGTSRESLFWWADRPRLVGRSASGNLVIENDRVGRIRAEMDTLPLTSVQLQRVVAFYSHHPELCAELATEQGLARVQGLTGPASVAPLR$","Membrane protein","Membrane, Cytoplasm, Extracellular","membrane protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-48]?$	signal-peptide
tmhmm	$\"[32-52]?$ $\"[58-78]?$ $\"[108-130]?$ $\"[136-156]?$ $\"[403-421]?$ $\"[427-447]?$ $\"[475-495]?$ $\"[505-525]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-36% similar to PDB:1Q5P S156E/S166D variant of Bacillus lentus subtilisin (E_value = );-34% similar to PDB:1Y0F The structure of collagen type I. Single type I collagen molecule (E_value = );-34% similar to PDB:1YGV The structure of collagen type I. Single type I collagen molecule: rigid refinment (E_value = );-36% similar to PDB:1KB0 Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni (E_value = );-36% similar to PDB:1C9M BACILLUS LENTUS SUBTILSIN (SER 87) N76D/S103A/V104I (E_value = );","No significant hits to the Pfam 21.0 database.","","protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2617","2814566","2813580","987","5.74","-6.19","34171","ATGCGCTACCTCACTCTGAGGCACACCCCAGTCACGAGTCTGATCGGGACGCTCAGTCTCGCTGCCTCGCTGTTCCTGGCGGTGGTGGCAGCCCCCGCCGGCGCCACGCCCCCTGCACAGCTCTCGAGCCAGGAGAAAGTCAACTTTGAGATCGCCATCAAGTCCGACGAAGAGCTGACGACCACTATCACGATCACGTCACCGGCCTCCAGAGAAAAGAACCTGAAGGAGGACTGCGTCCAAGAGACGTTCTCACAGGCCGCTACCCCACCCGACATTACTTTCACCAACGACAACGGGACTCCGACCTGCAAGGCCACGTTCACGACACCCATATCCAGGAACAACTACGTGAGTCACGATGGAGACGAGTACGTCGTCGACACCCACGATGACTCCGCACCTAAGGATGGCAGCGCCGACACGTTCTCTCTCACAGTCATCTTCCCCGGTAAAGTGACGGAATCCGGAGGGGGAAAGATCGAGGGAGATCAACAGAACGAGGTATCGTTCTCCACCTTCTACGGTCACAAGGCCCGCGGCAAGGACACCGCCCAGGCGGCGTCTCAGCCCAGCTCGACACCCTCGCCCAGTTCGACACCCGCATCCAGCTCGGCATCCTCATCCAGTTCGACGCCCGCCCCCAGTTCGACGTCCTCGTCTCAGTCGTCGGATGCGACGACAAGCATGATCGTGATACTCATTGTGATCGCTGTTGCCGGAGCAGTGATCGCCCTTGTCAGCAACACACTCAAGAAGAACCGGGAGCAGAAGTACCTGGATGCGCTGGGGCAGCAGTCGCTTCAGGCAAGCACTCTTATGCCCACTTCCCATCCGGCCGCCTTCCCCTCTCACGCACAGGCAGGTCCGCCCCCCACGCAGCCCGGCTATTCGCCTGTTCCCCAGCAGTACCAGCCCCCGTACCCGCAGGGACCGGCCTCCGCACCGCATCTTCCACCGAACCACAACGGTTACGGCGGCTACTGA","MRYLTLRHTPVTSLIGTLSLAASLFLAVVAAPAGATPPAQLSSQEKVNFEIAIKSDEELTTTITITSPASREKNLKEDCVQETFSQAATPPDITFTNDNGTPTCKATFTTPISRNNYVSHDGDEYVVDTHDDSAPKDGSADTFSLTVIFPGKVTESGGGKIEGDQQNEVSFSTFYGHKARGKDTAQAASQPSSTPSPSSTPASSSASSSSSTPAPSSTSSSQSSDATTSMIVILIVIAVAGAVIALVSNTLKKNREQKYLDALGQQSLQASTLMPTSHPAAFPSHAQAGPPPTQPGYSPVPQQYQPPYPQGPASAPHLPPNHNGYGGY$","Hypothetical protein","Extracellular, Periplasm, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[228-248]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-41% similar to PDB:1FFK CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI AT 2.4 ANGSTROM RESOLUTION (E_value = );-41% similar to PDB:1JJ2 Fully Refined Crystal Structure of the Haloarcula marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution (E_value = );-41% similar to PDB:1K73 Co-crystal Structure of Anisomycin Bound to the 50S Ribosomal Subunit (E_value = );-41% similar to PDB:1K8A Co-crystal structure of Carbomycin A bound to the 50S ribosomal subunit of Haloarcula marismortui (E_value = );-41% similar to PDB:1K9M Co-crystal structure of tylosin bound to the 50S ribosomal subunit of Haloarcula marismortui (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2618","2815528","2814662","867","8.61","3.36","30445","ATGGCCGCCACCACCCCTCGATACCGCCCCCTGGGGGCGCTCGTCCTTCTGTCGCTTCTCTTGACTCTGACGCTCCTGACCCCTCCAAGTCACGCCGTCACCTCCGCCGCGCGCGACGATTCAGAGTCTTCGTTGTCCGTACGGGTCGTCATCAACCAGGACGACACCTACGACATGACCGTCATCGGACAACTCAAGAGCAAGTCCTCCTCCGACAAACGGGGAATGAAGGAGAATTGCAACCCTTCTGACGCCGGAGGGCCGTTTGAAGACCTGAAAGCCTCGTACTCCGAGCGCAACGGCCTTCCCACCTGCACCCTCACCGGCAAGTCGATCGGCCTCTCCGAGGTTGACGGATTCATCAAGCACAAGGGCGACGAGTACACCCTCGACACTCAGAAGGGACAATTTCCCTCCTCTTCCGCATACGGCATTGACTACAAGTTCTCCGTGACATTCCCTGGCGAGGTCACGGATGCAGACGGCGGCAAGGTCAGCGGGAACACGGTGACCTTCACCAAGCCTGGTAGGTATCGCGTCAGCGGCAAGGACGCGCCAGCCTTTCCCTGGATGTGGGTGATCGTGGGGGTCGTGCTGGTCGGAGCAATCGGCGCCGGTCTCTTCTGGTTCCTCAACCGCAAGAAGAAGGCACAGCAGCAGGCCTATGCGGTCAGCACCGCGGGGTATGCACCACAGCAGCCCTACGCCCCTGGGCAGATACCGGCTCCCGGCGCCGTACCTCCGTCCCCCTCTGGCTTCGTCGCCCAGGGCTACAACCAATTCGGACAGAGCAGCGCGATGCCTCAGGGGGCTGTACCGCCTCCTTCCAACTATCCACCGCCTCCCCCCTCCTCCACCTGGGGCTGA","MAATTPRYRPLGALVLLSLLLTLTLLTPPSHAVTSAARDDSESSLSVRVVINQDDTYDMTVIGQLKSKSSSDKRGMKENCNPSDAGGPFEDLKASYSERNGLPTCTLTGKSIGLSEVDGFIKHKGDEYTLDTQKGQFPSSSAYGIDYKFSVTFPGEVTDADGGKVSGNTVTFTKPGRYRVSGKDAPAFPWMWVIVGVVLVGAIGAGLFWFLNRKKKAQQQAYAVSTAGYAPQQPYAPGQIPAPGAVPPSPSGFVAQGYNQFGQSSAMPQGAVPPPSNYPPPPPSSTWG$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[189-211]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-62% similar to PDB:1A3Z REDUCED RUSTICYANIN AT 1.9 ANGSTROMS (E_value = );-62% similar to PDB:1RCY RUSTICYANIN (RC) FROM THIOBACILLUS FERROOXIDANS (E_value = );-62% similar to PDB:1CUR REDUCED RUSTICYANIN, NMR (E_value = );-62% similar to PDB:1E30 CRYSTAL STRUCTURE OF THE MET148GLN MUTANT OF RUSTICYANIN AT 1.5 ANGSTROM RESOLUTION (E_value = );-62% similar to PDB:1GY2 CRYSTAL STRUCTURE OF MET148LEU RUSTICYANIN (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2619","2816520","2815651","870","5.66","-4.15","29832","GTGGGCATGACACCTGCCATCGCCCACCGCATCCCTAGGCCCCTGTCCGTCTTGACGGCTCTTGCGGCGCTCGCCCTGTCCGCACCCCTCGCACTGATCGGTGCCCCGGGACACGCCGCCCCCGCTGAGGACGAGAGCTCCGTCGGCATTGAAGGCTCGTTCGACATCGTGATCAACTCCGATGAGACCTACACCGCCAAGTTCGTGATGACCACCCGCACCGAGTTCCAGCTGAAGAAGTCGTGCACTGAAGAAGCCTTCAAAACTCCTGGCACCAAGGATGTCAAGAACGTGAAGGTGAACTATAAAGAGGACGGCGACACCGCCACCTGCACCGCAGAGGGAAGTCAGAAAATCGCCGACGCCAAGGGACTGGTGAGCCACAAGGATGGCGAGTACACCGTCGAGACCCCTGATTTCGGAACTGACGCCGCTGGTGATGATGTCAAGTTCTCTCAGTCGGTAACTTTCCCCGGCAAGGTCACCAAGGCCGACGGCGGCGAGGTCAAGGGCAATAAGGTCTCCTTCGCCGACGGCTCGTCTCACACGGTGACGGGCAAGGACGGATCCACCCCCATGTGGGTCTGGATCCTCACCGGAGTCGTCGCCCTCGCGGTGATCGGCGCAGCGGCCACGTTCTTCATTCTCCGCAGCAAGAAGAACAAGCCCCAGACGCCCTACGGAACCCCCGCCCAGGGATATGACCCGAGCCAGGCCTTCCCGGCTCAGCCCGGACAGCAGGCGGGTTACGGTGCCCCCCAGGCTCAGCCCGGCTATGGCACGCCCGGCGAGCAGGCGGGCTACGGTGCCCCTCAGGCGCAGCCCGGCCAGCAGCCCGGCTACGGAGCTCCCGGCCAAGGCACCTACTGA","VGMTPAIAHRIPRPLSVLTALAALALSAPLALIGAPGHAAPAEDESSVGIEGSFDIVINSDETYTAKFVMTTRTEFQLKKSCTEEAFKTPGTKDVKNVKVNYKEDGDTATCTAEGSQKIADAKGLVSHKDGEYTVETPDFGTDAAGDDVKFSQSVTFPGKVTKADGGEVKGNKVSFADGSSHTVTGKDGSTPMWVWILTGVVALAVIGAAATFFILRSKKNKPQTPYGTPAQGYDPSQAFPAQPGQQAGYGAPQAQPGYGTPGEQAGYGAPQAQPGQQPGYGAPGQGTY$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[194-216]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-47% similar to PDB:2GTH crystal structure of the wildtype MHV coronavirus non-structural protein nsp15 (E_value = );-47% similar to PDB:2GTI mutation of MHV coronavirus non-structural protein nsp15 (F307L) (E_value = );-53% similar to PDB:1CGT STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE REFINED AT 2.0 ANGSTROMS RESOLUTION (E_value = );-53% similar to PDB:1CGU CATALYTIC CENTER OF CYCLODEXTRIN GLYCOSYLTRANSFERASE DERIVED FROM X-RAY STRUCTURE ANALYSIS COMBINED WITH SITE-DIRECTED MUTAGENESIS (E_value = );-53% similar to PDB:3CGT STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE COMPLEXED WITH ITS MAIN PRODUCT BETA-CYCLODEXTRIN (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2620","2817587","2816586","1002","7.30","1.27","36054","ATGAGCTGTGCCGTTGTAATCAGGAGAGTCCACGCCGTACTGGCTGCGTTGGCCGTTCTCGCTTTCATCGCCGCTATGGCCGTGGCCTCCCCTCCTGCTCACGCGGTGCCGCTCCTTGGAGAGGACAATAAGCTCATCATCACCATCGACATGAAAGTCACCGTCAAGAGCGATGACACCTTTGAGGCGTCCTTCGTCATCACCGATCAGACGAACTACAGCCTGATTCCTCCCATCACTAAGAACAGCTGCACGCTGGACTACTTCCTCGTGGAACCGAACATCTTTTCCCACGCTGAGACGACATTCGTTGACGGGAAGGACAAACGAGTCTGCACCATCACGACGAAGGGGAAGATTTCTGAGACCAACGGGACGATCAGGCACGAGAACGACGAGTACGCCATCGACACCAGCAGCATGGACAGACGCAAGACGCCGTCCCCGGAGCTGCAGCTGTTCTATGCCGCCACGTTCCCCGGAGAGGTGACCCAGAGCCGAGGCGGAAAGGTCGAGGGGGAGGAGAAGAACACCGTCTCCTTCACGGACTTCAAGGGCCGGATCGTCAAGGGCAAGGACCGTCCCGCCTCGGAAACGACGACCAGCAAGGTGTTGCCGTGGATCATCGAAGGCGTCGGCTCGCTCGTGGTCATCGGGCTCATCGCGATGGCGGTCGTTGTGCGACGTCGTCAGCGAAGCGGGCAGGGCGCTCCGGGTGCCGCCATGCAGGCCGTCCCCGTCCCGGATCCTGAACCGCAGTCATCCCACCTCGGTCAGCCGGTTCCTCAGCAGTACCCCGGGCAACCAGTTGCACCTCAACCGAACCACCAGCACCCGGGACAGCTGTCACCGCTCTACTCCCCCTCCAGCACCGCCAACGGCTCCTACCCGCCCTCCCCCACGCAGGCGCCCCAGCAGCACGGCACCTGGCCGCCCCAGCAGCACGGCACCTGGCCGCCCCAGCAGCACGGCACCTGGCCGCCGCCGCAGCAGTTCCAGTAA","MSCAVVIRRVHAVLAALAVLAFIAAMAVASPPAHAVPLLGEDNKLIITIDMKVTVKSDDTFEASFVITDQTNYSLIPPITKNSCTLDYFLVEPNIFSHAETTFVDGKDKRVCTITTKGKISETNGTIRHENDEYAIDTSSMDRRKTPSPELQLFYAATFPGEVTQSRGGKVEGEEKNTVSFTDFKGRIVKGKDRPASETTTSKVLPWIIEGVGSLVVIGLIAMAVVVRRRQRSGQGAPGAAMQAVPVPDPEPQSSHLGQPVPQQYPGQPVAPQPNHQHPGQLSPLYSPSSTANGSYPPSPTQAPQQHGTWPPQQHGTWPPQQHGTWPPPQQFQ$","Hypothetical protein","Periplasm, Membrane, Extracellular","Calcium-binding protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[207-227]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-48% similar to PDB:1BII THE CRYSTAL STRUCTURE OF H-2DD MHC CLASS I IN COMPLEX WITH THE HIV-1 DERIVED PEPTIDE P18-110 (E_value = );-47% similar to PDB:1HHN CALRETICULIN P-DOMAIN (E_value = );-53% similar to PDB:1P32 CRYSTAL STRUCTURE OF HUMAN P32, A DOUGHNUT-SHAPED ACIDIC MITOCHONDRIAL MATRIX PROTEIN (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2621","2818684","2817641","1044","5.06","-11.44","37249","GTGGTCGCGGCGGTACTGACCGGCCTCGCACTGCTGCTGTCCGGATGCGGGGCTCACTACGACTTCGTCATCCACGACAACGAGACCGCCGACCTGACCTACGTCATGTGGGACTCATCGGGGCTGTCACTCATCAGTAGGGAGAGCTGCACCCAGGACAAGCTCGAGAAGTCCACCCCTCTGCCCAAGGAAGTCAAGGCGGTCTACACCTTCACGTCCCACAACGGGCAGCCGGCATGCCAGGTCACAGCCAAGTCGGTTCCGCTCAATAACTTGCAGACCGACATCTGGACGATCAAGCACCAGGACGGGAAGTACGTCTTCGACCTGTCCCCCGAGGCGCTGAGCAAGCTCGGTAAGGACGACTCCCTCCCTTCCTCCCCGGGCGCCTCGGCAGGAATGAAGATCTCGGTAGCCGTGACCTTTCCCGAAGAGGTGACGAAGTCCAACGGGAGGAATGCCGACAACAAAGTCACCTGGGACAACGTGCTGGAGAGCTCTGAGGATCTCCATGCCGAGGGCGGGGACGGCAGGTTCCATCTGCAGTGGTGGATGATCGCGACGGGCGGCGCCGTCGTCCTCCTCATCATTGCCGGGGTCGTGGTGTACCTCCTGAGGACCCGCCGCGCCCGGCAGCTGGCTCCGGCACTGCCGTACGGCGAGGCCCTTCAGGGGGCCGCAGCGACCAGCACCATGCCCCCGGAGGTCTACGTCGGTGACCCGTATCAGTCTCCCCCCGGTCCCCTGCAGCCGGTGCCGGGCTCGACCTACCCCTATCCCGTCACCAACCTTCGCGACGGCTACGCCCCCTACCCCGACCCGGGCCAGGACACCAGCGCCTTCGCGCCACCTCAGGTCTCTGGAAGCGCAGGCGTCTTCAGCACCTACGAGGCCCAGCAGGGGATGTACCAGTCGCCCGGACCGGGCTACACCCAGATGCCCTACCAGGAAGGGCACACTCAGGCCGACTTCCGGCCGCCGCAGGAGCGCACCGGCGGCGGAGGTCAGAACGGGCAGTACTATCCGCCGTATCAGGGTGAGTAG","VVAAVLTGLALLLSGCGAHYDFVIHDNETADLTYVMWDSSGLSLISRESCTQDKLEKSTPLPKEVKAVYTFTSHNGQPACQVTAKSVPLNNLQTDIWTIKHQDGKYVFDLSPEALSKLGKDDSLPSSPGASAGMKISVAVTFPEEVTKSNGRNADNKVTWDNVLESSEDLHAEGGDGRFHLQWWMIATGGAVVLLIIAGVVVYLLRTRRARQLAPALPYGEALQGAAATSTMPPEVYVGDPYQSPPGPLQPVPGSTYPYPVTNLRDGYAPYPDPGQDTSAFAPPQVSGSAGVFSTYEAQQGMYQSPGPGYTQMPYQEGHTQADFRPPQERTGGGGQNGQYYPPYQGE$","Hypothetical protein","Extracellular, Periplasm, Membrane","annexin XIV-like protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-18]?$	signal-peptide
tmhmm	$\"[183-205]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-46% similar to PDB:2FUL Crystal Structure of the C-terminal Domain of S. cerevisiae eIF5 (E_value = );","No significant hits to the Pfam 21.0 database.","","XIV-like protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2622","2819608","2818766","843","9.64","9.54","28315","ATGTCCGTCGCGCCGTCCTCCGCGTCCCGTTCTACGAGCTTCTTGTCGCGCACTCTGTCCCGCCCGCCGGCACTCCGGGCGCTTCGACCGGCCGTCGTGGCGACCGCCGCCTGCCTGGCACTGTCAGCCTGCACCGCTCACATGGACATGACCATCCGCTCCCAGGGCAGCTACGACGTCGCCCTGGAGATGCGCGATACCAGCGGAACCGTCTTCCCGAAGGGAAAGGCCCCCGACTGCTCGACCTACTCCGACCCCACCACCCTGGGCGTGCCTGCCGGCACCACCGTCAAGGCCACCCCGATCACCGGCGACGACGGAATCGGCTGCCAGGTCACCATCAGCGGCGTCAAGGTCCCCCAGGCCTCGCAGGCCGATGCGAACACGATCGTCGTGCGCGACGGCGAGGTCTACAAGGTGACGATCCAGCCCTTCCCCTCCGACCCCTCCCAGGACGCCAACGGGGCCGCAGGTGCGCAGGGCAGCGCATCTCAGGCCCCTGCCGCGCCGTCGGGAGGCCCGGCCGGGGCCCAGCCGACCAGCACGTCCTTCAAGGGCGTCGTCGACACCAAGGTCTCCGTCACCTTTCCCGGCGCGGTGACACAGTCCGGCGGGGGGAAGGTCTCGGGCACCACGGTCACCTGGGACGATCCGGACACGGTGGCCAAGGGCGTGAGCGCCTCGGGCTACGCCCAGGACTCGCGGGGCGTATCGTGGTGGAGTCGTTCCCGTGTCTGGCTGACCGCGGGGCTGGCCCTACTCGGCGGAGCCCTGGCTGCGGCCATCCTCCGACGGCGCAGCAGAGGTCACGCACCCCGCAAGGCAGCGCAGGGGCGGCACTGA","MSVAPSSASRSTSFLSRTLSRPPALRALRPAVVATAACLALSACTAHMDMTIRSQGSYDVALEMRDTSGTVFPKGKAPDCSTYSDPTTLGVPAGTTVKATPITGDDGIGCQVTISGVKVPQASQADANTIVVRDGEVYKVTIQPFPSDPSQDANGAAGAQGSASQAPAAPSGGPAGAQPTSTSFKGVVDTKVSVTFPGAVTQSGGGKVSGTTVTWDDPDTVAKGVSASGYAQDSRGVSWWSRSRVWLTAGLALLGGALAAAILRRRSRGHAPRKAAQGRH$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Sivaraman J., Li Y., Larocque R., Schrag J.D., Cygler M., Matte A. Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate. J. Mol. Biol. 2001. 311(4):761-776. PMID: 11518529","","","

InterPro
IPR001917
Binding_site

Aminotransferase, class-II
PS00599	$\"[220-229]?$	AA_TRANSFER_CLASS_2

noIPR
unintegrated

unintegrated
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[245-263]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-51% similar to PDB:1WCK CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF BCLA, THE MAJOR ANTIGEN OF THE EXOSPORIUM OF THE BACILLUS ANTHRACIS SPORE. (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2623","2819756","2821699","1944","5.19","-22.99","72289","GTGACCTGGGGCGCCCGGTGGGGGAGGATTGCTCTCGACCGAGCGAGTCGGCATCGGCGCGCTCACCGGATCAACATACCCAAGGAAGGGACTCGCATGACTGTGTCTGAGAAGGACGTCCGCGCCGCCGCGCCGGCTAACGCCCCTGAGGATGTCATCGAATTCGTCACGCGCATCGCCGAGCTGGCCAAGCCCGAGAACGTCTACTTCGCGGACGGTTCACAGGAGGAGTGGGACCGCCTCACCACCGAGATGGTGGAGTCCGGCGTGTTCACGCGCCTCAACCCCGACAAGCGCCCCAACTCCTTCCTCGCGCGCTCCCTGCCCAGCGACGTCGCCCGTGTGGAGTCCAGGACCTTCATCTGCTCCGAGAAGGAGGAGGACGCCGGCCCGACCAACAACTGGTACGACCCGGCCGAGATGAAGAAGATCCTCAACGAGAAGTTCGATGGCGCCATGCGCGGCCGGACCCTCTACGTGATCCCCTTCTCCATGGGTCCGCTGGGCGGCCCCATCTCCCAGCTCGGCATCGAGCTGACCGACTCCCCCTACGTGGTGGTCAACATGCGGATCATGACCCGCATGGGTGCGGCCGCCATGGACCTCATCAACGAGGGTCGCCCCTGGGTCCCGGCCGTCCACTCCGTCGGCGCCCCGCTGGCCGAGCACGAGAAGGACACCACCTGGCCCTGTAACGACGAGAAGTACATCACCCACTTCCCGGAGACCAACGAGATCTGGTCCTTCGGCTCCGGCTACGGCGGCAACGCCCTGCTGGGCAAGAAGTGCTACGCGCTGCGCATCGCCTCGACCATGGCCCGCCGTGACGGCTGGATGGCCGAGCACATGCTCATCCTGCGCCTGACCGACGAGAAGAGCGGCAAGCAGTACCACGTCACCGCCGCCTTCCCGAGCGCCTGCGGCAAGACCAACCTCGCCATGCTCCAGCCCACCATCCCGGGCTACAAGGTCGAGACCGTCGGTGACGACATCGCCTGGATGCGCCCCGGCCCTGACGGCCGCCTGCGCGCCATCAACCCCGAGGCCGGCTTCTTCGGCGTCGCCCCCGGCACCTCCTACGACACCAACCCGATGGCCATGGACACCATGAAGGCCAACACCATCTTCACCAACGTCGCCCTGACCGACGACGGTGACGTGTGGTGGGAGGGCATCGACGCCCCGATGCCGGAGCACCTCATCGACTGGCAGGGCAACGACTTCACCCCGGCCGACGCCGCCGAGGGCAAGAAGGCCGCTCACCCCAACAGCCGCTTCACCACCCCGGCCTCGCAGTGCCCGATCATCTGCCCCGACTGGGAGGCCCCCGAGGGCGTGGCCATCGACGCCATCCTCTTCGGCGGTCGCCGCGCCACCAACGTGCCGCTGGTCGCCGAGCAGTACGAGAACGCCCACGGCGTGTTCATCGGCTCCGCCGTGGCCTCTGAGGTCACCGCCGCCGCCCTGGACGCCAAGGTCGGCTCCCTGCGCCACGACCCCATGGCCATGCTGCCCTTCTGCGGCTACCACATGGCCGACTACTGGTCGCACTGGCTGGAGATGCAGGAGAAGCTGGGCGACAAGTTCCCCAAGGTCTACCAGGTCAACTGGTTCCGCAAGGACGAGAACGGCAAGTTCATCTGGCCCGGCTACGGCGACAACTCCCGCGTGCTCGACTGGATCGTGCGCCGCGCCTCCGGCGAGGTCGAGGCCATCGACGGCGTCACCGGCCGCTACCCCAAGTTCGAGGACTTCAACCTCGAGGGCCTCGACCTGGGCGAGGAGGAGTGGGCCAAGATGTACGACATCGACCCCGAGGCCTGGGCCGCCGAGATGGACGACACCGAGGAGTACTACAAGCAGTTCGGTGACAAGCTGCCCGAGGCCATCAAGGAGCAGCTCGCGAAGTTCCGTGCGCGCATTGACGAGGCCAAGAAGGCCTGA","VTWGARWGRIALDRASRHRRAHRINIPKEGTRMTVSEKDVRAAAPANAPEDVIEFVTRIAELAKPENVYFADGSQEEWDRLTTEMVESGVFTRLNPDKRPNSFLARSLPSDVARVESRTFICSEKEEDAGPTNNWYDPAEMKKILNEKFDGAMRGRTLYVIPFSMGPLGGPISQLGIELTDSPYVVVNMRIMTRMGAAAMDLINEGRPWVPAVHSVGAPLAEHEKDTTWPCNDEKYITHFPETNEIWSFGSGYGGNALLGKKCYALRIASTMARRDGWMAEHMLILRLTDEKSGKQYHVTAAFPSACGKTNLAMLQPTIPGYKVETVGDDIAWMRPGPDGRLRAINPEAGFFGVAPGTSYDTNPMAMDTMKANTIFTNVALTDDGDVWWEGIDAPMPEHLIDWQGNDFTPADAAEGKKAAHPNSRFTTPASQCPIICPDWEAPEGVAIDAILFGGRRATNVPLVAEQYENAHGVFIGSAVASEVTAAALDAKVGSLRHDPMAMLPFCGYHMADYWSHWLEMQEKLGDKFPKVYQVNWFRKDENGKFIWPGYGDNSRVLDWIVRRASGEVEAIDGVTGRYPKFEDFNLEGLDLGEEEWAKMYDIDPEAWAAEMDDTEEYYKQFGDKLPEAIKEQLAKFRARIDEAKKA$","Phosphoenolpyruvate carboxykinase (GTP)","Cytoplasm","Phosphoenolpyruvate carboxykinase","phosphoenolpyruvate carboxykinase (GTP) ","Phosphoenolpyruvate carboxykinase (GTP)","","","","","

InterPro
IPR008209
Family

Phosphoenolpyruvate carboxykinase (GTP)
PTHR11561	$\"[7-644]T$	PHOSPHOENOLPYRUVATE CARBOXYKINASE
PF00821	$\"[54-644]T$	PEPCK
PS00505	$\"[303-311]T$	PEPCK_GTP

InterPro
IPR008210
Domain

Phosphoenolpyruvate carboxykinase, N-terminal
PD004738	$\"[89-274]T$	PPCK_RALSO_Q8Y3G3;

noIPR
unintegrated

unintegrated
G3DSA:3.40.449.10	$\"[23-276]T$	no description
G3DSA:3.90.228.20	$\"[277-644]T$	no description

","BeTs to 6 clades of COG1274COG name: Phosphoenolpyruvate carboxykinase (GTP)Functional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1274 is ---pk-----r------------it-Number of proteins in this genome belonging to this COG is 1","***** IPB008209 (Phosphoenolpyruvate carboxykinase (GTP)) with a combined E-value of 6.2e-227. IPB008209A 56-95 IPB008209B 98-131 IPB008209C 155-196 IPB008209D 209-219 IPB008209E 256-308 IPB008209F 320-367 IPB008209G 373-392 IPB008209H 433-487 IPB008209I 532-567","","","-65% similar to PDB:1KHB PEPCK complex with nonhydrolyzable GTP analog, native data (E_value = 1.1E_169);-65% similar to PDB:1KHE PEPCK complex with nonhydrolyzable GTP analog, MAD data (E_value = 1.1E_169);-65% similar to PDB:1KHF PEPCK complex with PEP (E_value = 1.1E_169);-65% similar to PDB:1KHG PEPCK (E_value = 1.1E_169);-65% similar to PDB:1M51 PEPCK complex with a GTP-competitive inhibitor (E_value = 1.1E_169);","Residues 54 to 644 (E_value = 0) place ANA_2623 in the PEPCK family which is described as Phosphoenolpyruvate carboxykinase.","","carboxykinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2624","2824640","2823915","726","5.86","-2.46","25438","ATGAACGCGAGGTCACCATCGAAGATGCACCCCAACGGCTGGGGCACTGACATAGGCCGCTTCACCGCGAACCTGACTTGCTACGCTACAACGGCAGTTCAAGCACCCCCAGAAGACGGACCGATGTCAGCTCCCCAGAATCAGCCCCCGTACCAGCCGCCGTACCAGCCCCAGTATCAGGCCGTGCCTCCTTACGGGCAGCAGCGCCCCCGCCAGAACCACGTCGGAAAGCTGGTCGTGGCGATCATTCTGTTCGTCATCGGCCCATTGATGGGACTGGCCATCTGGGGCATCGGGTCGGTCATCACCGTCGCCAGCATCGCCACCAGTGGTGACGTCGTCACCAACGGACAGCAGGTCACCCTGAGCAGCAATGACGAACGTGCCCTGTACGTATCGAACGCCGCCGCCAACAACTGCACGGTCGTTGACCCTGACGGCAAGGAGGTCCCCACCTCCCCCAACGGCGGGATGACCATCTCCAACAACGACGGCGACTTCAACTCGGTTCTCACCTTCAAAGCCGACAAGTCGGGAGACTACCGGGTCTCATGCGAGGGACTGGATGACACCGACGCGATCCTCGTGGGCCCCACCATCACGTTCGGCAAGTTCGCGGTGCCCCTCGTCGCCGGCCTGGCCGCAGGGGCGATCTGCTGGATCTTTGCCATCATCCTGCTGATCTGGCGCCACCGGGCCCTGGCCGCACAGAATCAAGCGGGCTGA","MNARSPSKMHPNGWGTDIGRFTANLTCYATTAVQAPPEDGPMSAPQNQPPYQPPYQPQYQAVPPYGQQRPRQNHVGKLVVAIILFVIGPLMGLAIWGIGSVITVASIATSGDVVTNGQQVTLSSNDERALYVSNAAANNCTVVDPDGKEVPTSPNGGMTISNNDGDFNSVLTFKADKSGDYRVSCEGLDDTDAILVGPTITFGKFAVPLVAGLAAGAICWIFAIILLIWRHRALAAQNQAG$","Hypothetical protein","Membrane, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[78-98]?$ $\"[209-229]?$	transmembrane_regions

InterPro
IPR001005
Domain

SANT, DNA-binding
PS00037	$\"[138-146]?$	MYB_1

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[188-208]?$ $\"[218-236]?$	transmembrane_regions

InterPro
IPR000005
Domain

Helix-turn-helix, AraC type
PR00032	$\"[104-119]T$ $\"[119-135]T$	HTHARAC
PF00165	$\"[40-86]T$ $\"[92-136]T$	HTH_AraC
SM00342	$\"[52-135]T$	HTH_ARAC
PS01124	$\"[39-137]T$	HTH_ARAC_FAMILY_2
PS00041	$\"[89-131]?$	HTH_ARAC_FAMILY_1

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[26-89]T$	no description

noIPR
unintegrated

unintegrated
PTHR11019	$\"[43-137]T$	THIJ/PFPI
PTHR11019:SF11	$\"[43-137]T$	ARAC FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN

","BeTs to 10 clades of COG2207COG name: AraC-type DNA-binding domain-containing proteinsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2207 is --------v-rlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB003313 (Arac protein, arabinose-binding/dimerisation) with a combined E-value of 8.5e-10. IPB003313E 53-98 IPB003313F 99-139***** IPB000005 (Helix-turn-helix, AraC type) with a combined E-value of 5e-07. IPB000005 104-135 IPB000005 54-85","","","No significant hits to the PDB database (E-value < E-10).","Residues 40 to 86 (E_value = 1.7e-10) place ANA_2626 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, AraC family.Residues 92 to 136 (E_value = 1.8e-07) place ANA_2626 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, AraC family.","","regulator ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2627","2825688","2826470","783","4.40","-22.61","28220","ATGACCGACGCCACCGCCAATGCCCAGACCGCCGAGCGCCTTGTCGGCTTCCCCTGCTGGATCGAGCTGTACACACCCGACATCGACGCCTCGGCGGCCTTCTACCGGGACCTTCTCGGCTGGGAGATCACCCGTGCCGAACCGGGTGAGCCGCTGACCACTGAGGTGTATCACGGCGGTCGGCTCATCGGCTCCTTCGAGCCCTCCAAGGACGTGCCCGGGGCCCCTGGCTGGAGGGTGAGCTTCCTGGTCGACGACGTACGTGCTGCAGCCGGCGCTGCTGAGAGCGCTGGTGGGAGCGTCGTCGTGGAGCCCACCGGCGTCTCGGAGACCATGGCCTACGCCCTCGCCTCCGACCCAGACGGCAACGTTGTCGGGCTCCTGGAGGATGAGGACTGCGAGGGGCCCTACCCCTACCAGGCAGGGATGCCGGTGTGGTTCGACGTCCTGGCCAGTGACCTGGAGCCAGCCGAGCGCTTCTACCGGGAGACCGCCGGGTGGCCCACCCGCCGGCTGACCATGGGCGACCAGGAGCAGGACTTCTACACGAGCGTCGTCGGGGGCAGATCCGTGTGCGGTGTCGGTCGGGCGGGCTACTTCGGGGCTGAAGAGGCCCCCTTGTACTGGCGCATCTACTTCGGGGTGGAGGACGCCGACGCCGCAGCCCGGCGCGTACGTGAGCTCGGGGGAACCGTCATCGTCGAGCCCTTCGACTTCACCTTCGGGCGCATGGTGGAGGTGGCAGACCCGCACGGTGCGCGCTTCCTGCTCACGACTTTCTGA","MTDATANAQTAERLVGFPCWIELYTPDIDASAAFYRDLLGWEITRAEPGEPLTTEVYHGGRLIGSFEPSKDVPGAPGWRVSFLVDDVRAAAGAAESAGGSVVVEPTGVSETMAYALASDPDGNVVGLLEDEDCEGPYPYQAGMPVWFDVLASDLEPAERFYRETAGWPTRRLTMGDQEQDFYTSVVGGRSVCGVGRAGYFGAEEAPLYWRIYFGVEDADAAARRVRELGGTVIVEPFDFTFGRMVEVADPHGARFLLTTF$","Glyoxalase/bleomycin resistance protein/dioxygenase","Cytoplasm","hydroxylase","hypothetical protein","Glyoxalase/bleomycin resistance protein/dioxygenase","","Kim N.S., Umezawa Y., Ohmura S., Kato S. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 1993. 268(15):11217-11221. PMID: 7684374","","","

InterPro
IPR004360
Domain

Glyoxalase/bleomycin resistance protein/dioxygenase
PF00903	$\"[17-127]T$ $\"[143-257]T$	Glyoxalase

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.10	$\"[20-127]T$ $\"[145-257]T$	no description

","No hits to the COGs database.","***** IPB004361 (Glyoxalase I) with a combined E-value of 3.2e-08. IPB004361A 20-53 IPB004361C 206-240***** IPB011588 (Glyoxalase/extradiol ring-cleavage dioxygenase) with a combined E-value of 2.7e-06. IPB011588 20-40 IPB011588 146-166***** IPB004360 (Glyoxalase/Bleomycin resistance protein/dioxygenase domain) with a combined E-value of 8.1e-06. IPB004360 25-40 IPB004360 151-166","","","No significant hits to the PDB database (E-value < E-10).","Residues 17 to 127 (E_value = 3.7e-13) place ANA_2627 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.Residues 143 to 257 (E_value = 2.7e-06) place ANA_2627 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2628","2830503","2828053","2451","6.25","-7.43","88180","ATGAGGCCCGGAATCGCGGGCCCCGCGTGCCCTGGGGCGGGCGTGAGCCGATTCTTAGGAAACCCGGATCGCAGCCGAGTACCCTCAGGTTGTTCCCAAGCACGCAGGCTTCGGACAGCACGGCATCAGGAGGCCCGGGTGGAAGTCGATCAGTCCTCTGCCGGGAGGTGGCTCGCGGTGGGACCCGGTGCGGCAGCCGACCGCACCCCTGAAACCGAGGCAACCGCGGAGCTCAACGCGGTGACGATCCGCCGGCTCGGGGCCGTCTATGTCCTACCCTCCGCCGGCGGACCGGCGCCGTCGCGCTCCGCTTCGCCGCAAGAGGCAGAGCCCACGCCACAGCGGGGCAGTGACGCGGGCGTCGAGACGGCCCTGACCGCGCTGCGCGCCCTGGGCTACCGGCTCTCCGCCCCGGCCCGGGAGGCCCTCATCCACCCCGAGCAGGCGTGGGCACTGGTCAATGCCGTCGCCCGCCTCAGCTCCGGCTCATTGGCCGCCGAGTACCAGCCCTTCTACCCCGACTTCCCTGTCCAGGTGCGCACCGCCTCGGAGGCCACGCTGCTGGTCAACGCCGCCCTGCACTACCTGGGCGACGTCGTCGGGGTCCGGATCCTGCCGGACTACCGGCCCAGCCCCCGCGAGCCCCTGCCGGGAGACGACGGCGCCCTCACCGAGCTGGGCCTGGCCACGACGCAGGACCTGGAGCGGATCGTGGCCCACCTCGCCGCCCAGGCGACTCCCTTCAGCGCCCAGGACCGTGCAGACCTGACGGCCCTGCGCGACTTCGGTCCCAAGGCAGCGCCGCGCGTGGCGGTCAAGGAGAACCTCGCCGTCCTCACCGTCACCTTCCCCGACCTGGACTTCTCCGCCTCCTACCGCACCGTCACCGACGTGCTGCGCCTGGCGGTCGCCCTGGCGGGCGGCGACGTCGCCCTGGCCGAGCCGTGCCGGTTCCCCTCCTTCTCCCGCGCGCAGCGGCGCCGTCTGCTGGGTCTGCTTGACGCCGTCGGGCAGGTCCAGGACAGCCGGGACAGCGCCGAGGAGATGGCTCGGCGCTGCGAGCGATGGAAGCGGCTGGTCCGCCACCTGCGCCCCGGCGACTACGCGCGCCGCTTCCCGCGCGCCACCAAGCTGCTGCACCAGGTCGCCTCCGGGGAGGCCGAAGCGGGTTTCACCTCCCGCCTGGAGGAGGCCCTGGCGCGGCGCGACGTCGATGGCGCTCTTCGTCTGCTTTCCGCCCGCCCGGGGGTCTTCGCCCGCCGACTCAACCACCTGCTGCGGCTGTGCGCCGATGACGCCGCCCGCGAGCGCGTGGTCGCCGAGTTCGCCCGGGTCGCGCCCGAGGTCTCCGTGCCGGTCCTGGTGCGCCTGTGGGAGTACTTCTCCTCCCCCGGGCCAGATGCCCTGCCGTGGCGGGTCGTCGCCATCAAGGCGGCCACGGGCACCAAGACGACGCTCATCCCCTCCACCCGCCGCCCCGGACCCGCCGACACGGCGGTGGTTCGCGCCGTCGAGGAGGCCCTGCGGCAGCGGAAGCGCTTGGGGCGGATCGCCGTCGACCAGGGGCTGTACGAGGGCTACACGGCTCCGGTGGGCCTGCGCTCGGCCTCACCGGGTATGCGCACGGCGGGGCGCGGCACCCGACTGCCGCTGCCCGAGGGTGAGACGATCCGCTTCTTCCTGCACTGGCGCGACCTGCCCGAGAACCCAGCCGAGGCCTCGGGGCCTGCCGGACCTGCTGCCGCCGAGGACAGGGGTACCCGGGTGGATCTGGACCTGTCGGCCTTCTTCGTCTCCGAGGACTTCACACGCACCGAGCAGATCGCCTACTACAACCTGCGCTCGACGGCGGCCGTGCACTCCGGCGACCTCACCTCGGCACCCGATGGGGCGGCCGAGTTCATCGACGTCACCCTGGCCGAGGCGCTGCGGCAGGGATGGCGCTACGTCGTCATGACGGTCCACTCCTTCTCCCACCACCAGCTCAGCGAGGTGCCCGAGTGCTGGGCGGGGGCGATGGCCCGCGGCGCGGACCCGCAGAGCGGCGAGGTCTTCGAGGCCTCCACCGTCATGCAGCGCCTCGACCTGGTCTCCCCCACGTTCAACGCGACGCCCTTCGTCATCGACCTCGCTGAGCGCCGCCTCATCTGGTGGGACCTGCCCGTGGGGGTGGGCGAGCACCAGGTGGCGAACCTGGATCGCAGCAGCAACCGGGTCCTGGCGCACCTGCTCGACCTGCTGGAGGGGCGGCGCATGCCGCTGGCGCACCTACTGGGGCTCCTGGCCGACGATGTCGTCGAGGACCCCGATGAGGCCGAGCTGGTCTTCGGTGAGGGCGGGATCCTGCCGTGGCAGACCGAGCGGATCCTGGCGCTGCTGGGCCCCGCGGAGGTCGCGGCGGAGGAGCTCTCCGACGTGAACGGGGGCGCCGAGGGCCGGCAGTCGGAGTAG","MRPGIAGPACPGAGVSRFLGNPDRSRVPSGCSQARRLRTARHQEARVEVDQSSAGRWLAVGPGAAADRTPETEATAELNAVTIRRLGAVYVLPSAGGPAPSRSASPQEAEPTPQRGSDAGVETALTALRALGYRLSAPAREALIHPEQAWALVNAVARLSSGSLAAEYQPFYPDFPVQVRTASEATLLVNAALHYLGDVVGVRILPDYRPSPREPLPGDDGALTELGLATTQDLERIVAHLAAQATPFSAQDRADLTALRDFGPKAAPRVAVKENLAVLTVTFPDLDFSASYRTVTDVLRLAVALAGGDVALAEPCRFPSFSRAQRRRLLGLLDAVGQVQDSRDSAEEMARRCERWKRLVRHLRPGDYARRFPRATKLLHQVASGEAEAGFTSRLEEALARRDVDGALRLLSARPGVFARRLNHLLRLCADDAARERVVAEFARVAPEVSVPVLVRLWEYFSSPGPDALPWRVVAIKAATGTKTTLIPSTRRPGPADTAVVRAVEEALRQRKRLGRIAVDQGLYEGYTAPVGLRSASPGMRTAGRGTRLPLPEGETIRFFLHWRDLPENPAEASGPAGPAAAEDRGTRVDLDLSAFFVSEDFTRTEQIAYYNLRSTAAVHSGDLTSAPDGAAEFIDVTLAEALRQGWRYVVMTVHSFSHHQLSEVPECWAGAMARGADPQSGEVFEASTVMQRLDLVSPTFNATPFVIDLAERRLIWWDLPVGVGEHQVANLDRSSNRVLAHLLDLLEGRRMPLAHLLGLLADDVVEDPDEAELVFGEGGILPWQTERILALLGPAEVAAEELSDVNGGAEGRQSE$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical cytosolic protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2629","2830531","2831847","1317","4.69","-23.97","44909","GTGAAGATCCTGCTCCTCGGCTCCGGCGCGCGCGAGCACGCCCTGGCCCGTGCCCTCGCCCGTGATCCGCAGACCGCTGAGCTCGTCGTCGCCCCAGGCAACCCCGGCACGGCGGCCATTGCCACGAACCTCAACATTGACCCCAGCGTCCCCGAGGAGGTCGTGGCCCTGGCCACGCAGATGAAGGCGGACCTCGTCGTCGTCGGTCCGGAGGCACCCCTGGTTGCCGGTGTCGCCGACGCCGTGCGCGACGCCGGGATCCCCTGCTTCGGCCCCGGCGCGGAGGCCGCCCGCCTGGAGGGCTCGAAGGCCTTCGCCAAGGAGATCATGACCGCCGCGGGCGTCCCCACCGCCGAGGCCGCCGTGTGCACCACCGAGGCCGAGCTGACCGCCGCCCTGGACCGCTTCGGGGCCCCCTATGTCGTCAAGGAGGACGGCCTGGCCGCCGGCAAGGGCGTCGTCGTCACCGACGAGCGCCCCGTCGCCCTGGCCCACGGACGCGCCTGCCTGACTCGCGGCAGTGGTCGCGTCGTCGTCGAGGACTACCTCGACGGCCCCGAGGCCTCCGTGTTCTGCGTGTGCGACGGCGCCACCGTCCGCCCCCTGGCCCCCGCCCAGGACTTCAAGCGCCTCCTCAATGACGACGCCGGCCCCAACACCGGCGGCATGGGCGCCTACTCGCCCCTGTCCTGGGCCCCGGCGGACCTCACCGAGCAGGTGGTGCGCGAGGTCGCCCAACCCGTCGTCGATGAGATGGCCCGCCGCGGCACCAGCTTCATCGGCCTGCTCTACTGTGGCCTGGCCCTGACCAGCCGCGGCCTGCGCGTCGTCGAGTTCAACGTGCGCTTCGGCGACCCCGAGACCCAGGCCGTCCTGGCCCGCCTGACCTCCTCCCTGCCCGAGCTGCTCCACGCCGCCGCCACCGGTCGCCTCGCCGAGGTCCCCGAGCCCACCTGGTCCGAGCAGTGCGCCGTCGACGTCGTCATCGCCGCCCCCGGCTACCCCGGGACCGTCACCACCGGCGGCACCATCACCGGGATCGAGGCCGCCGAGGAGCTCGACGACGTCCACGTGCTGCACGCCGGCACCGGCAACACCGAGCGCGGGGAGCTGGTCGCCGTCGGCGGGCGGGTCCTGTCCGTCGTCGCCCTGGGGGCGAGCCTCGAGGCGGCGCGGGAACGCGCCTATGAGGCCGTCGAGCGCATCGACCTTGAGGGCGCCCAGTACCGCACCGATATCGCCCAGGCGGCCACTGAAGGCAGCGTTAGCAGCGTTAGCAGCGTCAGCAGTGCTGCCAGCGCCGACCGGACCGAGTAG","VKILLLGSGAREHALARALARDPQTAELVVAPGNPGTAAIATNLNIDPSVPEEVVALATQMKADLVVVGPEAPLVAGVADAVRDAGIPCFGPGAEAARLEGSKAFAKEIMTAAGVPTAEAAVCTTEAELTAALDRFGAPYVVKEDGLAAGKGVVVTDERPVALAHGRACLTRGSGRVVVEDYLDGPEASVFCVCDGATVRPLAPAQDFKRLLNDDAGPNTGGMGAYSPLSWAPADLTEQVVREVAQPVVDEMARRGTSFIGLLYCGLALTSRGLRVVEFNVRFGDPETQAVLARLTSSLPELLHAAATGRLAEVPEPTWSEQCAVDVVIAAPGYPGTVTTGGTITGIEAAEELDDVHVLHAGTGNTERGELVAVGGRVLSVVALGASLEAARERAYEAVERIDLEGAQYRTDIAQAATEGSVSSVSSVSSAASADRTE$","Phosphoribosylamine--glycine ligase","Cytoplasm","phosphoribosylamine--glycine ligase","phosphoribosylamine--glycine ligase ","phosphoribosylamine--glycine ligase","","Galperin M.Y., Koonin E.V. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 1997. 6(12):2639-2643. PMID: 9416615Fan C., Moews P.C., Walsh C.T., Knox J.R. Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. Science 1994. 266(5184):439-443. PMID: 7939684Murzin A.G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 1996. 6(3):386-394. PMID: 8804825Fan C., Moews P.C., Shi Y., Walsh C.T., Knox J.R. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(4):1172-1176. PMID: 7862655","","","

InterPro
IPR000115
Domain

Phosphoribosylglycinamide synthetase
G3DSA:3.90.600.10	$\"[323-423]T$	no description
PF01071	$\"[101-288]T$	GARS_A
PF02843	$\"[323-418]T$	GARS_C
PF02844	$\"[1-100]T$	GARS_N
TIGR00877	$\"[1-419]T$	purD: phosphoribosylamine--glycine ligase
PS00184	$\"[282-289]T$	GARS

InterPro
IPR011761
Domain

ATP-grasp fold
PS50975	$\"[107-308]T$	ATP_GRASP

InterPro
IPR013815
Domain

ATP-grasp fold, subdomain 1
G3DSA:3.30.1490.20	$\"[119-183]T$	no description

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[184-321]T$	no description

InterPro
IPR013817
Domain

Pre-ATP-grasp fold
G3DSA:3.40.50.20	$\"[1-93]T$	no description

noIPR
unintegrated

unintegrated
PTHR10520	$\"[103-417]T$	PHOSPHORIBOSYLAMINE-GLYCINE LIGASE-RELATED
PTHR10520:SF3	$\"[103-417]T$	PHOSPHORIBOSYLAMINE--GLYCINE LIGASE

","BeTs to 21 clades of COG0151COG name: Phosphoribosylamine-glycine ligaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0151 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000115 (Phosphoribosylglycinamide synthetase) with a combined E-value of 1.1e-138. IPB000115A 1-36 IPB000115B 70-120 IPB000115C 139-156 IPB000115D 205-230 IPB000115E 244-273 IPB000115F 274-299 IPB000115G 327-344 IPB000115H 368-414 IPB000115B 359-409","","","-50% similar to PDB:1GSO GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI. (E_value = 2.7E_62);-45% similar to PDB:1VKZ Crystal structure of Phosphoribosylamine--glycine ligase (TM1250) from Thermotoga maritima at 2.30 A resolution (E_value = 3.4E_41);","Residues 1 to 100 (E_value = 3.9e-48) place ANA_2629 in the GARS_N family which is described as Phosphoribosylglycinamide synthetase, N domain.Residues 101 to 288 (E_value = 1.6e-88) place ANA_2629 in the GARS_A family which is described as Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain.Residues 102 to 144 (E_value = 0.00013) place ANA_2629 in the ATP-grasp family which is described as ATP-grasp domain.Residues 104 to 286 (E_value = 0.00076) place ANA_2629 in the ATP-grasp_3 family which is described as ATP-grasp domain.Residues 323 to 418 (E_value = 6.5e-32) place ANA_2629 in the GARS_C family which is described as Phosphoribosylglycinamide synthetase, C domain.","","ligase (purD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2630","2832284","2833234","951","4.74","-18.12","34314","ATGACTCAGTCCGCGAGCTCCGCCTCAGTCGGCCCCACTGCCTCAGCAGCCGACTCCCTGCCCCCCACCGTCCCCGGGTGGGAGCACCGCTCCAGCGGCAAGGTCCGGGACGTCTACGCCCCCACTTCCGACGGCCCATGGGGTGGACAGGATGTGCTCCTCGTGGTCGCCTCGGACCGCATCAGCGCCTACGACCACATCCTGGCCACGCCGATCCCGGACAAGGGCAAGGTCCTCACGGCCCTGAGCGCCTGGTGGTTCGAGCAGCTCGCCGACGTCGTCCCGAACCACCTCGTCTCCCTCGACGTTCCCGCCCAGGTCGCCGGCCGCGCCATGATCTGCCGGCGGCTGGAGATGTACCCGGTGGAGTGCGTGGCCCGCGGCTACCTCACCGGCTCCGGCCTGGTCGAGTACCGCCAGGGCCGCTCCGTGTGCGGCGTCGCCCTGCCCGAGGGACTGACGGAGGCCTCCCGCCTTCCCGAGCCGATCTTCACCCCCGCCGCCAAGGCCGAGCTCGGCGAGCACGATGAGAACGTCACCTTCGAGCGCGTCGTCCAGATGGTGGGGGACAGCGCCGCCACCGCCCTGCGCGAGACCACGCTGGCCCTCTACTCCCGGGCTGCCGAGATCGCTCGGGACCGCGGCATCATCCTGGCCGACACCAAGTTCGAGCTCGGTACCGACGCCGACGGCGAGCTGATCCTGGGTGACGAGGTCCTCACCCCCGACTCCTCCCGCTTCTGGCCCGCCGACGCCTGGGAGCCCGGCCGGGTCACCCCCTCCTTCGACAAGCAGTACGTGCGCGACTGGCTCACCTCCCCGGCCTCCGGCTGGGACCGGGACGGCGACCAGGAGCCTCCTGCCCTGCCTGACGACGTCGTCGAACGGACCCGCGCCCGCTACCTCGAGGCCTACGAGCGGCTGACCGGCTACCCCCTGGAGCTGTCATGA","MTQSASSASVGPTASAADSLPPTVPGWEHRSSGKVRDVYAPTSDGPWGGQDVLLVVASDRISAYDHILATPIPDKGKVLTALSAWWFEQLADVVPNHLVSLDVPAQVAGRAMICRRLEMYPVECVARGYLTGSGLVEYRQGRSVCGVALPEGLTEASRLPEPIFTPAAKAELGEHDENVTFERVVQMVGDSAATALRETTLALYSRAAEIARDRGIILADTKFELGTDADGELILGDEVLTPDSSRFWPADAWEPGRVTPSFDKQYVRDWLTSPASGWDRDGDQEPPALPDDVVERTRARYLEAYERLTGYPLELS$","Phosphoribosylaminoimidazole-succinocarboxamide synthase","Cytoplasm, Membrane","Phosphoribosylaminoimidazole-succinocarboxamidesynthase(SAICAR synthetase)","phosphoribosylaminoimidazole-succinocarboxamide synthase ","phosphoribosylaminoimidazole-succinocarboxamide synthase","","Zalkin H., Dixon J.E. De novo purine nucleotide biosynthesis. Prog. Nucleic Acid Res. Mol. Biol. 1992. 42:259-287. PMID: 1574589","","","

InterPro
IPR001636
Family

SAICAR synthetase
PD003043	$\"[31-120]T$	Q6A6A9_PROAC_Q6A6A9;
PTHR11609	$\"[55-310]T$	PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7
PF01259	$\"[26-293]T$	SAICAR_synt
TIGR00081	$\"[32-310]T$	purC: phosphoribosylaminoimidazole-succinoc
PS01057	$\"[119-133]T$	SAICAR_SYNTHETASE_1

InterPro
IPR013816
Domain

ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20	$\"[118-262]T$	no description

noIPR
unintegrated

unintegrated
PTHR11609:SF1	$\"[55-310]T$	PURINE BIOSYNTHESIS PROTEIN 7, PUR7

","BeTs to 20 clades of COG0152COG name: Phosphoribosylaminoimidazolesuccinocarboxamide (SAICAR) synthaseFunctional Class: FThe phylogenetic pattern of COG0152 is amtkyqvcebrh--------xNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","-59% similar to PDB:1A48 SAICAR SYNTHASE (E_value = 4.7E_60);-59% similar to PDB:1OBD SAICAR-SYNTHASE COMPLEXED WITH ATP (E_value = 4.7E_60);-59% similar to PDB:1OBG SAICAR-SYNTHASE COMPLEXED WITH ATP (E_value = 4.7E_60);-59% similar to PDB:2CNQ ATOMIC RESOLUTION STRUCTURE OF SAICAR-SYNTHASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH ADP, AICAR, SUCCINATE (E_value = 4.7E_60);-59% similar to PDB:2CNU ATOMIC RESOLUTION STRUCTURE OF SAICAR-SYNTHASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH ASPARTIC ACID (E_value = 4.7E_60);","Residues 88 to 355 (E_value = 7.6e-102) place ANA_2630 in the SAICAR_synt family which is described as SAICAR synthetase.","","synthase(SAICAR synthetase) (SAICAR)","","1","","","Thu Aug 9 15:45:51 2007","","Thu Aug 9 15:45:51 2007","","","Thu Aug 9 15:45:51 2007","Thu Aug 9 15:45:51 2007","Thu Aug 9 15:45:51 2007","","","Thu Aug 9 15:45:51 2007","","","Thu Aug 9 15:45:51 2007","Thu Aug 9 15:45:51 2007","","","Thu Aug 9 15:45:51 2007","Thu Aug 9 15:45:51 2007","","","","","yes","","" "ANA_2631","2833231","2833920","690","11.19","9.94","22857","ATGACCACGACCTCATCCACCTCGGACCTCCCCGATACCGGGAGCGCCACCCGCGCCTTCAAACCGGGGCCGGGCTTCTACGTCCTGGTCGGCCTCATCGTCCTGACGATCGTGCTGGCGCTGTCGGCCGCCATCACCTCCGCCCTCGGGGCCACCGAGACCTCCCGCGTCCTGGGTGGTATCGCCCTGGTCCTCGTGGGGCTGGGCATGCTCGCCTCCTTGAGGCTCTCCGCCCGGTCCCTGGTGGTCAACGCCCCCCGCCTGCGTCTGGAGCGCAACCGGGTCCGCGCGGCCCGGGCCCGGCAGGGCGGCGAGTCCTCCGAGAAGGGGGGGAGTGCCAAGGGCGCCCGCGGCAAGGGGGCCAAGGGCTCCCAATCCTCGCAGCGGGGCTCGGCGGCAGACGGCGCAGCCCTGCCCGGCACTGATCTGGCAACGCTCACCGTGCCGGGAACCAAGGTGCTCGTGCCTGAGTCGACAGGTCGGCGCGAGCTGACCACCCTCGACGTGGTCTCCGGCCCCCTCACCACCGCACTGGCCGCGACGTCGCTCGGGCGCGCGGCCGACGAGCGCCTGGCCGGGACCTCCACCGGCGAGACCCTCATCCGTGTCGGCCAGCTCCTGCTCGGCGCCACCGGCTTCGTGCTCGTGGCCCTGGGGCTCGCCTCCATCCTGGGACAGGTGATCTCATGA","MTTTSSTSDLPDTGSATRAFKPGPGFYVLVGLIVLTIVLALSAAITSALGATETSRVLGGIALVLVGLGMLASLRLSARSLVVNAPRLRLERNRVRAARARQGGESSEKGGSAKGARGKGAKGSQSSQRGSAADGAALPGTDLATLTVPGTKVLVPESTGRRELTTLDVVSGPLTTALAATSLGRAADERLAGTSTGETLIRVGQLLLGATGFVLVALGLASILGQVIS$","Hypothetical protein","Membrane, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-50]?$	signal-peptide
tmhmm	$\"[28-48]?$ $\"[54-74]?$ $\"[206-228]?$	transmembrane_regions

InterPro
IPR003850
Family

Phosphoribosylformylglycinamidine synthetase PurS
PD010362	$\"[6-78]T$	Q6ACD5_BBBBB_Q6ACD5;
PIRSF005633	$\"[2-82]T$	Formylglycinamide ribonucleotide amidotransferase, PurS component

noIPR
unintegrated

unintegrated
G3DSA:3.30.1280.10	$\"[1-74]T$	no description

","BeTs to 11 clades of COG1828COG name: Phosphoribosylformylglycinamidine (FGAM) synthase, PurS componentFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG1828 is aompk--qvdrlbc------uj----Number of proteins in this genome belonging to this COG is 1","***** IPB003850 (Protein of unknown function UPF0062) with a combined E-value of 2.7e-20. IPB003850A 6-25 IPB003850B 38-51 IPB003850C 58-75","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","(FGAM) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2634","2836014","2836736","723","5.01","-9.15","25408","GTGAGTGACTCGCTCAGCAGCTCTCCTGCTGCCCGCATCGGCGTTATCACCTTCCCCGGGACGCTCGACGACGTCGACGCCGCCCGCGCCGTGCGCCTGGCCGGCGCTGAGGCAGTGAGCCTCTGGCACAAGGACGCCGACCTGCGCGGGGTCGATGCCGTCGTCGTGCCCGGGGGCTTCTCCTACGGCGACTACCTGCGCTGCGGCGCCATCGCCCGCTTCGCCCCCGTCATGGAGGAGGTCGTGGCCGCCGCCGAGCGCGGCATGCCGGTGCTCGGCATCTGCAACGGCTTCCAGATCCTCGCCGAGGCCCACCTCCTGCCCGGCGCCCTCCTGCGCAACGCGAACCAGCGCTTCTTCTGCGTCGAGCAGCGCCTGCGCGTGGAGACCACGCAGACCGCCTGGACCAACCGGTACGCGGACGGGGAGGAGATCGTCGTTCCCATAAAGAACGGCGAGGGCAACTTCATCGCCTCGCCCGAGGAGCTCGACCGTCTCGAGGGGGAGGGCCTCGTCGTCTTCCGCTACGTGGGCAACCCCAACGGCTCGGCCCGCGACATCGCCGGCGTACGCAATGAACGCGGCAACGTCGTCGGACTCATGCCCCACCCCGAGCACGCCGTGGAGCCCGGTTTCGGTCCCGACTCGCAGGCCGGTCCGCGCACCGGGACCGACGGCCTGGGAGTCTTCCGCTCCGCCATCGACTCGCTGCTGGCCGTCTGA","VSDSLSSSPAARIGVITFPGTLDDVDAARAVRLAGAEAVSLWHKDADLRGVDAVVVPGGFSYGDYLRCGAIARFAPVMEEVVAAAERGMPVLGICNGFQILAEAHLLPGALLRNANQRFFCVEQRLRVETTQTAWTNRYADGEEIVVPIKNGEGNFIASPEELDRLEGEGLVVFRYVGNPNGSARDIAGVRNERGNVVGLMPHPEHAVEPGFGPDSQAGPRTGTDGLGVFRSAIDSLLAV$","Phosphoribosylformylglycinamidine synthase I","Cytoplasm","phosphoribosylformylglycinamidine synthase I","phosphoribosylformylglycinamidine synthase I ","phosphoribosylformylglycinamidine synthase I","","Galperin M.Y., Grishin N.V. The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase. Proteins 2000. 41(2):238-247. PMID: 10966576","","","

InterPro
IPR010075
Family

Phosphoribosylformylglycinamidine synthase I
TIGR01737	$\"[11-237]T$	FGAM_synth_I: phosphoribosylformylglycinami

InterPro
IPR011698
Domain

CobB/CobQ-like glutamine amidotransferase
PF07685	$\"[44-212]T$	GATase_3

InterPro
IPR012998
Active_site

Glutamine amidotransferase, class I, active site
PS00442	$\"[90-101]T$	GATASE_TYPE_I

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.880	$\"[5-209]T$	no description
PTHR10099	$\"[26-213]T$	PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE

","BeTs to 20 clades of COG0047COG name: Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domainFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0047 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 2.5e-10. IPB000991A 90-107 IPB000991B 196-206***** IPB011698 (CobB/CobQ-like glutamine amidotransferase) with a combined E-value of 3.3e-07. IPB011698B 50-66 IPB011698C 88-102***** IPB002818 (Family of unknown function ThiJ/PfpI) with a combined E-value of 9.6e-06. IPB002818A 50-61 IPB002818B 91-101","","","-44% similar to PDB:1T3T Structure of Formylglycinamide synthetase (E_value = 7.5E_12);","Residues 44 to 212 (E_value = 6.2e-05) place ANA_2634 in the GATase_3 family which is described as CobB/CobQ-like glutamine amidotransferase domain.","","synthase I (purQ)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2635","2837692","2837312","381","4.96","-7.91","13811","ATGAGCACTGACAACAAGACCACATCCGACCATGCCTTACGTGTCGCCACCGCCTATCACGAGGCATGGACCAGCGGCGACCTCGACAAGGCGATGAGCTTCATGACCGACGACGTCGTCGTGCATGCACCAGGGAAAGAGATCAACGGCAAGGAGGAGTACCGGGCGTACCTCGGCGGGTTCATGGAGGTCCTGGAAGGGTGCACGCCGCGCGCCGCCTTCGGTGACGACAGCACTGCTGTGCTCTACTACTTCCCCCACACCCCCTCAACCCGCTCCGCCCCAGTTGGAGAGTGCTTTCTCGTTGAGTCAGGGTTGATAAAGGAGAGCCATGTCGTTTTCGATCGACTGTCTTACGCCCCACCCACCGAGTCCCAGTAA","MSTDNKTTSDHALRVATAYHEAWTSGDLDKAMSFMTDDVVVHAPGKEINGKEEYRAYLGGFMEVLEGCTPRAAFGDDSTAVLYYFPHTPSTRSAPVGECFLVESGLIKESHVVFDRLSYAPPTESQ$","SnoaL-like polyketide cyclase","Periplasm, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF1486","","","","","

InterPro
IPR009959
Family

Protein of unknown function DUF1486
PF07366	$\"[13-123]T$	SnoaL

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 123 (E_value = 0.0035) place ANA_2635 in the SnoaL family which is described as SnoaL-like polyketide cyclase.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2636","2838374","2837703","672","7.73","1.64","25300","ATGAGCACCTTCCAAGGACTACCGACAGCCCTTTTCGAGTTCTTCGCCGACCTGGCGCAGGACAACTCGAAGGACTTCTGGAACGCCAACAAGCAGCGTTGGCAGCGGGACGTGAAAGCCCCTATGAGTGCGTTGGTTGACGAGCTTTCCGGAGAGTTCGGTCCTTTGCGCATGTTCCGCCCCAACCGCGACCTGCGTTTCGCCCGCAACAAGGCCCCTTACAAACTCTGGACAGGCGCTACCAGCACCCCTCAGGCCACTGGCGGAATCGGCTACTACCTCAGTGTGTCGACCACCGGTATCACCACCGGCTACGGAGCCATGCGGATGACCGCCGACCAACTTCGCCGCTTCAGGGGCGCCATCGATGCCGACATCAGCGGAATCCGCTTCGAGGAGCTCACCCAAGAGCTCGCCGCACAGGGGCTGCCCGTCTCACCCGGCGCCGACCAGCCATTGAAAAACGCACCGCGAGGCTGGTCGGCCGACCACCCCCGCATCGACTTCCTCAGATGGAAAGGGGCCGCAGTCGTTCAGGACTGGCCCACCGACACTTGGATGCACACTCCCCAGGTGCACGAGAGGATTCGAGATACCTGGGCCGCCGTCGAGCCTCTCAGGGCATGGCTCGACGAGCACGTCATACAGCGACACCATGAACCACCTCATTGA","MSTFQGLPTALFEFFADLAQDNSKDFWNANKQRWQRDVKAPMSALVDELSGEFGPLRMFRPNRDLRFARNKAPYKLWTGATSTPQATGGIGYYLSVSTTGITTGYGAMRMTADQLRRFRGAIDADISGIRFEELTQELAAQGLPVSPGADQPLKNAPRGWSADHPRIDFLRWKGAAVVQDWPTDTWMHTPQVHERIRDTWAAVEPLRAWLDEHVIQRHHEPPH$","Conserved hypothetical protein","Periplasm, Cytoplasm","conserved hypothetical protein","hypothetical protein","conserved hypothetical protein","","","","","

InterPro
IPR012808
Family

Conserved hypothetical protein CHP02453
TIGR02453	$\"[7-215]T$	TIGR02453: conserved hypothetical protein T

InterPro
IPR013538
Family

Activator of Hsp90 ATPase homologue 1-like
PF08327	$\"[11-71]T$	AHSA1

noIPR
unintegrated

unintegrated
G3DSA:3.30.530.40	$\"[1-122]T$	no description

","BeTs to 3 clades of COG3832COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3832 is ----------r-b--------j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 11 to 71 (E_value = 1e-13) place ANA_2638 in the AHSA1 family which is described as Activator of Hsp90 ATPase homolog 1-like protein.","","regulator, ArsR family, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2640","2839496","2839191","306","10.13","4.89","11125","ATGACGCTGCGGGCGTTGGCTGACGGGAACCGTCGGGCGATCCTGCGCGTCATCCGTTCAGAACCGCAGCCCGTCGGCGCCGTCGCACAGGCAGTTGGACTGTCACAGCAGACTGCCTCGCATCATCTCCGGACTCTTCAGAAGGCGGGGCTGGCGACCGTCACCACCGATCACACGCGCCGCCTGTACGCACTCAACACGGACGGGCTCGCGGCGGTGCGCTCCTACCTCGACGACTTCTGGCCCGAGAGGCTGGCAGCCCTCAAGTCCGCCGTCGAGCAGCGAGAGGAGAAACAGCATGGCTGA","MTLRALADGNRRAILRVIRSEPQPVGAVAQAVGLSQQTASHHLRTLQKAGLATVTTDHTRRLYALNTDGLAAVRSYLDDFWPERLAALKSAVEQREEKQHG$","Transcriptional regulator, ArsR family","Cytoplasm","transcription regulator (ArsR family) BH0694","putative transcriptional regulator","regulatory protein, ArsR","","Morby A.P., Turner J.S., Huckle J.W., Robinson N.J. SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 1993. 21(4):921-925. PMID: 8451191Bairoch A. A possible mechanism for metal-ion induced DNA-protein dissociation in a family of prokaryotic transcriptional regulators. Nucleic Acids Res. 1993. 21(10):2515-2515. PMID: 8506147Eicken C., Pennella M.A., Chen X., Koshlap K.M., VanZile M.L., Sacchettini J.C., Giedroc D.P. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins. J. Mol. Biol. 2003. 333(4):683-695. PMID: 14568530Cook W.J., Kar S.R., Taylor K.B., Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J. Mol. Biol. 1998. 275(2):337-346. PMID: 9466913Busenlehner L.S., Pennella M.A., Giedroc D.P. The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 2003. 27(2):131-143. PMID: 12829264Liu T., Nakashima S., Hirose K., Shibasaka M., Katsuhara M., Ezaki B., Giedroc D.P., Kasamo K. A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPx-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II). J. Biol. Chem. 2004. 279(17):17810-17818. PMID: 14960585","","","

InterPro
IPR001845
Domain

Bacterial regulatory protein, ArsR
PF01022	$\"[8-54]T$	HTH_5
SM00418	$\"[1-79]T$	HTH_ARSR
PS50987	$\"[1-99]T$	HTH_ARSR_2

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[2-85]T$	no description

","BeTs to 14 clades of COG0640COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0640 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","***** IPB001845 (Bacterial regulatory protein, ArsR family) with a combined E-value of 2.5e-12. IPB001845 21-65","","","No significant hits to the PDB database (E-value < E-10).","Residues 8 to 54 (E_value = 2.4e-08) place ANA_2640 in the HTH_5 family which is described as Bacterial regulatory protein, arsR family.","","regulator (ArsR family) BH0694","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2641","2841520","2839892","1629","5.50","-19.26","58256","TTGACGAGGGAGTGCGGCCGAGCCAAGCCTACCCACGCCCCACGGCACCTCACACCACGACCCTCGCGGGACCGCGCCCCGCACACCCCGAGCACTTCATGCGAGCCCGATCGGCGCTCTGCGGAATCCGGCCAGAAGAATGCCGAAACGGCAACAAGACGCCACGCCCACACCCAAAGTGCTGCGCCTCACAGGATTTCGGGGGAAGATCGTGTCATGAGAGACATCGACGTCGCCCCGCTGCCCCTGTCGCACTTGGAGAGCCACCTGGACGAGGTGGCCATCAAACGACTGCACACCAGCCTGACGGGGGCCGAGGCCCTGCTGGAGGGGCGCACCGTGTGGACGGTCACGCCGTCGGCAGCCGCCGGCTCGGGGCCCGCGGAGACGGTCGCCCCCCTCGTGGGCTACTCCCTGGGCGCCGGCCTTAACGTGCGCTGGCTGACCCTGGACGCCCCCGAGGAGTTCACCCGGATCGCGGCCCGCCTACACGCCGGCATCCACGGGGACCACGGCGACGGCGGCAAGCTCGGGGACAAGCAGCGCGACATCTACGAGCACGTCCTGGCCTCCAACGCGGAGAACATCGTCGAGGAGGTCCGCCCCGACGACGTCGTCATCCTTCACGACCCACCCACGGCGGGCCTGGCCAAGGCTCTCAAGGCGGCGGGTGCCACGGTCATCTGGCGCTGCCATGCCGGAGCCGAGGGCGCAGGCGAGGCCGCCGACTACGCCTGGGCCTTCCTGGACCGCTACCTGGAGGACGTGGACCTCGTCATCGTCTCCCGCCCCGAGTACCGCCCGCCCTACATCGAGGCCGAGCGCTGCGCGGTCCTGGCCCCCTCCATCGACGCCGACTCCCCCAAGAACCGGGTCCTGGACCTGGATGAGGCCTGGTCGGTGGCGCGCCTGTCCGGGATCTTCGCCGGCGAGCCGCCTTTCGAGGCGGTGCCCTTCATGCGTCACGACGGGCGCGCCGACGCCTTCCGTGGCCTGGCCGACGCCCCGGTCCTGGCCGGTGGTCCGGTGCCGCTGGGTGCCCGGGTCGTCACCCAGGTCAACCGCTGGGACCGCCTCAAGGGCGGCCTGGAGCTGGTGGAGGCCTTCGCCGAGAACATCGCCGTGCTGCCCGAGGACGCCCACCTGCTGCTGGTCGGCCCAACCCCGGACGGTCCCGAGTCGCAGGCCACCCTCACCCAGATCGTGGAGCGCTGCTCAGTGCTGCCGGAATCGGTCGCCTCGCGGATCCACGTGGCCGCGGTGAGCATGGAGGACCGGGAGGTCAACGCCACCGTCGTCAACGCCGTCCAGCGAGTCAGCTCGGTCGTCACCCAGCGCTCCCTCATCGAGGCCTTCGGGCTGACCGTGGCGGAGGCGATGTGGAAGAAGGCCCCAGTGGTCGCCTCCGCAGTGGGCGGCATCCGCGACCAGATCGACGACGGCGTCGACGGCGTCCTGGTCGACCCGACCGACGGCGTCGCTTGGGCCGAGGCCGTGCGCGACCTGCTGCTCTTCCCCGAGCGGGCCCAGGAGATGGGGCTGGCCGCACACGAGTCCGTGCGCCGGGAGTTCCTGTCCAACCGGCACCTGCAGGACCTCCTACAGATCCTGGCCGACCTGGTGGGCTGA","LTRECGRAKPTHAPRHLTPRPSRDRAPHTPSTSCEPDRRSAESGQKNAETATRRHAHTQSAAPHRISGEDRVMRDIDVAPLPLSHLESHLDEVAIKRLHTSLTGAEALLEGRTVWTVTPSAAAGSGPAETVAPLVGYSLGAGLNVRWLTLDAPEEFTRIAARLHAGIHGDHGDGGKLGDKQRDIYEHVLASNAENIVEEVRPDDVVILHDPPTAGLAKALKAAGATVIWRCHAGAEGAGEAADYAWAFLDRYLEDVDLVIVSRPEYRPPYIEAERCAVLAPSIDADSPKNRVLDLDEAWSVARLSGIFAGEPPFEAVPFMRHDGRADAFRGLADAPVLAGGPVPLGARVVTQVNRWDRLKGGLELVEAFAENIAVLPEDAHLLLVGPTPDGPESQATLTQIVERCSVLPESVASRIHVAAVSMEDREVNATVVNAVQRVSSVVTQRSLIEAFGLTVAEAMWKKAPVVASAVGGIRDQIDDGVDGVLVDPTDGVAWAEAVRDLLLFPERAQEMGLAAHESVRREFLSNRHLQDLLQILADLVG$","Glycosyl transferase, group 1","Cytoplasm","glycosyl transferase, group 1 family proteindomain protein","glycosyl transferase; group 1","glycosyl transferase, group 1","","Campbell J.A., Davies G.J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 1997. 326:929-939. PMID: 9334165","","","

InterPro
IPR001296
Domain

Glycosyl transferase, group 1
PF00534	$\"[450-519]T$	Glycos_transf_1

noIPR
unintegrated

unintegrated
PTHR12526	$\"[113-296]T$ $\"[336-540]T$	GLYCOSYLTRANSFERASE

","BeTs to 19 clades of COG0438COG name: Predicted glycosyltransferasesFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0438 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is 20","***** IPB001296 (Glycosyl transferase, group 1) with a combined E-value of 1.7e-08. IPB001296B 446-478***** IPB013534 (Starch synthase catalytic region) with a combined E-value of 3.2e-08. IPB013534B 203-217 IPB013534F 438-478***** IPB000368 (Sucrose synthase) with a combined E-value of 1.7e-06. IPB000368O 420-466 IPB000368P 467-513","","","No significant hits to the PDB database (E-value < E-10).","Residues 334 to 519 (E_value = 1.6e-09) place ANA_2641 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1.","","transferase, group 1 family protein domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2643","2841533","2843893","2361","4.63","-56.87","82487","ATGGCGTCCGAGCCCATGATCCCCGCCGCCCACCCCGACACCGTCGCCGACGCCGCCGCAACACCCGAGCGGGAGATGCCCTGGAAGGAGCTGGGCCTCAAGGCCGACGAGTACGAGTCCATCCGCGAGCTGCTGGGGCGCCGCCCCACCAACGCCGAGCTGGCCATGTACTCGGTCATGTGGTCCGAGCACTGCTCCTACAAGTCCTCCAAGATCCACCTGCGCCAGTTCGGCGCCAAGACCACCCCCGAGATGCGCGAGCACCTCCTGGTCGGCATGGGGGAGAACGCCGGCGTCGTCGACATCGGTGACGGCTGGGCCGTGACCTACAAGGTCGAGTCCCACAACCACCCCAGCTATGTCGAGCCCTACCAGGGTGCCGCCACTGGCGTGGGCGGCATCGTGCGCGACATCATCTCCATGGGGGCGCGGCCCGTGGCCGTCATGGACCAGCTGCGCTTCGGCGCCGTCGACCACCCCGACACCGCGCGCGTCGTCCACGGCGTCGTGGCCGGCGTGGGCACCTACGGCAACTCCCTGGGCCTGCCCAACATCGGCGGCGAGACCGAGTTCGACTCCTCCTACCAGGAGAACCCGCTGGTCAACGCCCTGTGCGTGGGCGTGCTGCGCCACGAGGACATCCATCTGGCCAACGCCACCGGCGCCGGCAACAAGGTGGTGCTCTTCGGGGCCCGCACCGGCGGGGACGGCATCGGCGGGGCCTCCATCCTGGCCTCGGAGTCCTTCGAGGACGGCATGCCCGCCAAGCGCCCCAGCGTCCAGGTGGGCGATCCCTTCATGGAGAAGGTCCTCATCGAGTGCTGCCTGGACCTGTTCGGCGCCGGGCTCGTGCTCGGCATCCAGGACCTGGGCGCCGCCGGCATCTCCTGCGCTACCTCCGAGCTGGCCTCCAACGGCGACGGCGGCATGCACGTGGACCTGGAGAAGGTGCTCCTGCGTGACCCCACCCTGACCGCTGGGGAGATCCTCATGAGCGAGTCCCAGGAGCGCATGATGGCCGTCGTCGCGCCCGACAAGCTCGAGGAGTTCATGACCGTCATCGACAAGTGGGACGTCGAGGCCGCCGTCATCGGGGAGGTCAACGGCTCGGGCCGCCTCACCATCGACCACTTCGGGGAGCGGATCGTCGACGTCGACCCGCGCACCGTGGCCCACGAGGGCCCCACCTACGAGCGCCCCTACGCCCGCCCCGCCTGGCAGGACGCGCTCAACGCCGACACCACTGAGCGCCTGGCCCGCCCCGAGTCGGCCACCGAGCTGGCCGAGCAGGTGCGCGCTGTCGTCACCAGCCCCAACCAGGCCTCCACTGCCTGGGTGACCGACCAGTACGACCGCTTCGTGCGTGGCGACACCGCCCTGTGCCAGCCCGACGACGCCGGCGTCATCCGCGTCGATGAGGCCTCTGGCCGCGGCGTGGCCATCTCCACCGACGCCAACGGCCGCTTCACCAAGCTCGACCCCGCCACCGGCGCCGCCCAGGCCCTGGCCGAGTCCTACCGCAACGTATGCACCGTGGGCGCCCGGCCCCTGGCCGTCACCGACTGCCTCAACTTCGGCTCGCCGGAGGACCCCGACGCCATGTGGCAGCTCGTCGAGGCCATCACCGGCTTGGCCGACGCCTGCGCCGTCATGGGCGTGCCGGTCACCGGCGGCAACGTCTCGCTCTACAACTCCCACGGCAAGGTCAAGGGGCAGATCGACTCCTCGATCAACCCCACGCCCGTCGTCGGCGTCCTGGGCGTCATGGACGACGTGCGCCGTGCCAACCCCTCGGGCTGGCACGAGGAGGGCCTGGCCATCATGGCCCTGGGCACCACCGCCGACGAGCTCGACGGCTCGGCCTGGTCCCGTGTGGTCCACGACCACCTCGGCGGGCTGCCCCCGCGCGTCGACCTCGACGCGGAGATGGCGCTCGGGCGGGTGCTGCTGGCCCTGAGCGAGGCGGAGGGCCCCGGCGGCGAGCCGCTGGTGCGCGCCGCCCACGACTGCTCGACCGGTGGCCTCATCCAGACCCTCGTGGACTCCTGCCTGCGCTGCGGCGTCGGCGCCAGCGTGGACCTGACCGCCATCCAGGAGGAGGGCGTGGACGACTTCACCGCCCTGTTCTCCGAGTCCGGGGCCCGTGCGATCGTCGCCGTGCGCGAGGAGCTCGTACCCGCCGTCACCGCGGCCGCCGAGGCCGAGGACGTCGCCGTGGCACGCCTGGGGACCACCGGCGGTGACCTGCTCGTCGTGGCCGGCAGTGACCTGCTCTCCGACGGCGGCGCCGGGCGCCCCCTCGTCCTGGACCTAGCCGAGCTCGGGGCCGACGTCGAGGGTGTCCTGCCGGAGCTGTTCTGA","MASEPMIPAAHPDTVADAAATPEREMPWKELGLKADEYESIRELLGRRPTNAELAMYSVMWSEHCSYKSSKIHLRQFGAKTTPEMREHLLVGMGENAGVVDIGDGWAVTYKVESHNHPSYVEPYQGAATGVGGIVRDIISMGARPVAVMDQLRFGAVDHPDTARVVHGVVAGVGTYGNSLGLPNIGGETEFDSSYQENPLVNALCVGVLRHEDIHLANATGAGNKVVLFGARTGGDGIGGASILASESFEDGMPAKRPSVQVGDPFMEKVLIECCLDLFGAGLVLGIQDLGAAGISCATSELASNGDGGMHVDLEKVLLRDPTLTAGEILMSESQERMMAVVAPDKLEEFMTVIDKWDVEAAVIGEVNGSGRLTIDHFGERIVDVDPRTVAHEGPTYERPYARPAWQDALNADTTERLARPESATELAEQVRAVVTSPNQASTAWVTDQYDRFVRGDTALCQPDDAGVIRVDEASGRGVAISTDANGRFTKLDPATGAAQALAESYRNVCTVGARPLAVTDCLNFGSPEDPDAMWQLVEAITGLADACAVMGVPVTGGNVSLYNSHGKVKGQIDSSINPTPVVGVLGVMDDVRRANPSGWHEEGLAIMALGTTADELDGSAWSRVVHDHLGGLPPRVDLDAEMALGRVLLALSEAEGPGGEPLVRAAHDCSTGGLIQTLVDSCLRCGVGASVDLTAIQEEGVDDFTALFSESGARAIVAVREELVPAVTAAAEAEDVAVARLGTTGGDLLVVAGSDLLSDGGAGRPLVLDLAELGADVEGVLPELF$","Phosphoribosylformylglycinamidine synthase II","Cytoplasm","phosphoribosylformylglycinamidine synthase II","phosphoribosylformylglycinamidine synthase II ","phosphoribosylformylglycinamidine synthase II","","","","","

InterPro
IPR000728
Domain

AIR synthase related protein
PF00586	$\"[56-210]T$ $\"[426-590]T$	AIRS

InterPro
IPR010074
Family

Phosphoribosylformylglycinamidine synthase II
TIGR01736	$\"[33-786]T$	FGAM_synth_II: phosphoribosylformylglycinam

InterPro
IPR010918
Domain

AIR synthase related protein, C-terminal
PF02769	$\"[221-378]T$ $\"[602-754]T$	AIRS_C

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.10	$\"[59-215]T$	no description
PTHR10099	$\"[55-753]T$	PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE

","BeTs to 20 clades of COG0046COG name: Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domainFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0046 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB010918 (AIR synthase related protein, C-terminal) with a combined E-value of 2.4e-15. IPB010918A 93-119 IPB010918B 137-154***** IPB000728 (AIR synthase related protein) with a combined E-value of 3.1e-09. IPB000728A 111-121 IPB000728B 123-137","","","-53% similar to PDB:1VK3 Crystal structure of Phosphoribosylformylglycinamidine synthase II (TM1246) from Thermotoga maritima at 2.15 A resolution (E_value = 3.1E_86);-53% similar to PDB:2HS0 T. maritima PurL complexed with ATP (E_value = 3.1E_86);-53% similar to PDB:2HS3 T. maritima PurL complexed with FGAR (E_value = 3.1E_86);-53% similar to PDB:2HS4 T. maritima PurL complexed with FGAR and AMPPCP (E_value = 3.1E_86);-53% similar to PDB:2HRU T. maritima PurL complexed with ADP (E_value = 4.5E_85);","Residues 56 to 210 (E_value = 2.5e-51) place ANA_2643 in the AIRS family which is described as AIR synthase related protein, N-terminal domain.Residues 221 to 378 (E_value = 5.3e-38) place ANA_2643 in the AIRS_C family which is described as AIR synthase related protein, C-terminal domain.Residues 426 to 590 (E_value = 1.5e-33) place ANA_2643 in the AIRS family which is described as AIR synthase related protein, N-terminal domain.Residues 602 to 754 (E_value = 1e-18) place ANA_2643 in the AIRS_C family which is described as AIR synthase related protein, C-terminal domain.","","synthase II (purL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2644","2844515","2844688","174","3.83","-12.11","5682","GTGCGTGGAGAGGAGGGTCTGGGGGTGGCTGACTCGTCGGAGGGTGAGGAGGGTCTGGGGATGGCTGACTCGTCGGAGGGTGAGGAGGTTGGGGAGTTCTCGGAGGAGAGGGCCGCGGAGGATGTCATGGCTGGAGCCTGTCAAAGCGGCTGCCGCGTATCAACCAGTGGGTAG","VRGEEGLGVADSSEGEEGLGMADSSEGEEVGEFSEERAAEDVMAGACQSGCRVSTSG$","Hypothetical protein","Periplasm, Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2645","2844698","2845090","393","4.61","-11.41","13179","ATGATCGATCATGCCTCTGTGAGTGTCAGTGATCCGGCGGCCTCGAAGGCCTTCTATGAGGCGGCGCTCGCGCCACTGGGCTACCGCGTCGTCATGGAGTTCGGGCCCGTCACCGGGCTGGGTGGGCCGACGCCCGGCGCGTCGGAGGACTCCCCGGTCCATGCGGACCTGTGGCTGGCCCCGGCGGAGAACCCGACGCCCTGCCATATCGCGCTGGCGGCGTCCTCGACGGCGCAGGTGGACGCCTTCCATGAGGCGGCCCTGGCGGCGGGCGGCACCGACAACGGCGGTCCCGGCGAGCGCCCGCACTACCACCCCGGCTACTACGGGGCCTTCGTCCTCGACCCCGACGGCAACAACCTCGAGGCCGTCTTCCACGGCGCCGGCGACTGA","MIDHASVSVSDPAASKAFYEAALAPLGYRVVMEFGPVTGLGGPTPGASEDSPVHADLWLAPAENPTPCHIALAASSTAQVDAFHEAALAAGGTDNGGPGERPHYHPGYYGAFVLDPDGNNLEAVFHGAGD$","Glyoxalase/bleomycin resistance protein/dioxygenase","Extracellular","glyoxalase family protein","hypothetical protein","Glyoxalase/bleomycin resistance protein/dioxygenase","","Kim N.S., Umezawa Y., Ohmura S., Kato S. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 1993. 268(15):11217-11221. PMID: 7684374","","","

InterPro
IPR004360
Domain

Glyoxalase/bleomycin resistance protein/dioxygenase
PF00903	$\"[1-123]T$	Glyoxalase

noIPR
unintegrated

unintegrated
G3DSA:3.10.180.10	$\"[2-122]T$	no description

","BeTs to 4 clades of COG0346COG name: Lactoylglutathione lyase and related lyasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0346 is aom-kzy--drlbcefghsnuj----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 123 (E_value = 9.1e-11) place ANA_2645 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.","","family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2646","2845759","2849625","3867","4.31","-138.41","133803","GTGGCCTGGAGCCCGGACGGCACGCGGCTCCTGTCCGGATCGCACGACGGCACGGCCCGGGTCTGGGACGCAAGCCGCGGTACCGAGCTGTTCGCGCTGGCCGGCCCCAGCCTGTCCATCAGTGCGGTGGCCTGGAGCCCCGATGGTACGCGGCTACTCACTGCGGCGGAGGACCACAGCGTGCGCGTCTGGGACGCGACCACTGGCGCCGACCTGCTGACCCTGGGGGTCGGCGGCTCCGGCGTGGGCGGGGCGGTGGCCTGGAGCCCCGACTCCACCCGCATCCTCACCAGCTTCGACGACGCCTCGGCCCGCATCTGGGACGCCTCCAGCGGTCAGGTGGTGCGTACTCTGTCAGGGCACACCGAGCACCTCACCGCAGTGTCGTGGAGCCCGGACGGGACCCGAGTGGCCACCGCCTCCGACGACGGCACCGCCCGCGTCTGGGACGTCACCACCGGCACCGAGCTGCTGCGCGTGGGCCCGATGGCCTTCGTGGGGCGCGGCGCCACCATGGGCCCTGACGGCAGGCCGACCCACGTCGGCCCGATCGAGCCGATGACGGGCCTGTCATGGAGCCCGGACTCGCGCCGCATCATCACCGCCTTCGACTCGGCCGAGCCCCGGGTCTGGGACGCCGCCACCGGCGAGGAGGTCCTCAGCCTTCACGGCCGTGAGCGGCGCTGGGTCAGCGTCGTCTCCTGGAGCCCCGACGGCAGCCGCATCATCACCGACGACATCTCCGGCACCACCGCCCACATCTGGGACGCCGCCACCGGCGAGGAACTGCTCAGCCTGCGCGGCCACCACCAGTGGGCCTGCGCCCTGGCATGGAGCCCGGACGGGACCCGAGTGGCCACCGGCTCCCACGATGACACCGTGCGCGTCTGGGACGCCGCCACCGGCCAGACCCAGCTCGTCCTGGGGGCCGGCAACTCCGTGGAGACGGTCTCCTGGAGCCCCGACGGCACCAAGCTCAGCATCGGCGCCAAGATCGGCGGCAACCGTGTCTGGGACGCCACCACTGGCGAGCCGCGCCTCACCGTGGACAACGGCGCCCGAGAGCTGAGCGAGGTCGTCTGGAGCCCAGACGGTACCCGCCTGGCCACCTCCTCCTACCTCTCGCCCCGCGTCCTCATCCTGGATGCCTCCACCGGCGACGTCGTCCAGGCCCTGACCGCCGGGGAGGACGACGTCAACGACATCGCCTGGAGCCCGGACAGCGAGCGCATCCTCACCGGCCTGGGAGACGACCGCGCCGCGATCTGGGACGCCGCCCGCGGCGAGCGCCTCCTGACCCTCGAGGGCCACAGCGACATGATCACCTCGGTCGCCTGGAGCCCCAACGGCCAGCGCGCCCTGACCGGCTCCCAGGACGGGACGGCCCGCATCTGGGATGCCGCCACCGGCGAGGTCATCCACACCTACACCGGCAACTGGGTGCGCGACGTCGTGTGGACTCAAGGGGGCCCGCGCGTCGTCACCGGCAGTGCCGATGGCGCCGCCCACGTCTGGGACGTCATCACCTCCGGCGAGCTCGTGACACTGCGCGACGACGCCGCCATGGTCCGCTCCTACGCCTGGAGCCCCGACGGCGCCAAGGTGCTGGCCGGCTTCGACGACGGCGTCGTGCGCGTGTGGGACGAGGTCTCCGGCAAGATCGTCCTGTCCCTGGCCGGTCACCGCTTCGGCGTCACCGACGCGCAGTGGAGCCCCGACGGCACCCGGATCCTCACCGGCTCCGAGGACGGCACCGTGCGCCTGTGGGACGCCACCACCGGCGAGATGACCGGGCTGTTCCTATGCTTCCTGCCCGACGGCGGGGTCGCCATCCTCGACGCCCCCTCCCTGAGCCTGCGCTCGGGCCCCGCGGAGGTCTGGGACTACCTCGGCCGCCCCGAGATCCTCGCCGGCCAGCTCACCCGCGTGGGCGTGGAACGGCGCCAGTACCTCAACTCCGACCCGCTGCCCACGGTCGTCTCGGAGCCGTCCCCGGCCGAGACCACTGACGAGGACCCGACGACGTCGGAGCCGGTTGAGGAGCCCCAGGTTCCCGAGGCCACTGAGCCCTCTGAGGGGAGGGAAGCATCGGAGGCCGACGTGCTCGGCGATTCTGTCGATACCCCCTCCGTCTTCGCCGTGCCCGCACAGCCGGCGGCCGAGTCCGCTACTGAGGCCGAGCAGCCCGCCGCTTCCCAGTCCCCTGAGGACGCTCCCGCCCAGGCCCCGGAGTCGTCAGCCCCTGCCGGCGAGCCCCTCATCGAGGAGGCCCCCGCCGAGGCTCAGGCCCCGCAGGTCGAGGAGCCCGCCCCGGCCGAGACCGAGAGCTCCGAGACCCCCGAGCCGGTCCCCGCTCCCGAGGAGGAGGACGCCGCCACTGCTCACCAGGCCCGGCACGCGGCGGTGACCGCCCACACGCCGACCGAGGCCGCTCAGGCCCCCGATGCCCTTGGGCAGCCGGTCGCGCCGGCCGAGACCGAACCGGTCGCCGCGCCGACGGGGGAGACCCTCCTCGTCCAGCCCTTCCCCGTGGAGCAGGGCCTTGTGGACGGTGAGGTGAGTGCACCGGCCGTGGCGCCGCCCGCGATGGTTGAGATGCCGCCGGCCCTGGTCGCTCCCGAAGGGGACCGGCAGGAGCAGTCCGAGGCGCAGCCCGTGCTGAGCACCCCAGAGGCCAGCCAGGAGGTCGGCGCCGAGGCCGGCGCCGCCACGCTCACCGTCCCGGCTCCCGAGGCGGAGGCGGCCGATGGCTCGCGCCGGGCTCGGCACGCCGCCGCCACTGCGCAGACCCCGGCTGACGCCCCGGAGCAGGCCGCTGAGGGCGGCACCGAGGCGGCCCAGTCCTCCGAGCCAGGGCTGGCTTCGCCGACCGACGCGGCCCACTCCTCCGGGACGGCCGAGTCCGCCTATGAACCGGTGGCGATCCCCGCCGTTGAGCATGCCGGTGGTGAGCCCGTGGCGGCGCCCACCGGTGAGACCGTTGCCCCCGATCAGCTCGAGCTCCCCCTGGCCCCGGCCGACGCCGTCGCTCACGAGGGTGATGAGGTCACCCTCGACCTCTCCGAGGATGCCTCCGAGGCCCCTGCCCCCGCCGAGGCGACGGCCCCGCCCGTCGCGGACATCGCGGAGACGGCGCGCGCCGCCGGCCCGGTGGATGTCTCCGACGCCGCTGATGCCGCCCCCGCCACCGACTCCGCCGATGCGCCGGCACGTGAGGCGCCGGTGTCCTCCGGTGCTGAGGCCGTCTCCGCGCCGACCGCCTCAACGCCCGAGGGTGAGCCCGAAGACCAGGCGGTGCCGGAGGGCGAGGCCGAGCAGGGCCTGGCCGAGCAGGCCCCCGTCGAGCACCCGCAGGCCCAGGACAACCCGGAGAGGTCGCGTGAGCCTGAGGAGGCCGAGGCCTCGCAGCCCACGGATGCCGAGGCGCCCGCCGAGGACCGACCGGGCGCCGAGCAGGAGCCGACTGAGCCCGCTGAGCCGACCGAGCCGACCCCGGCACCCTGGGGGAGTGCGGACCTGCGTCAGCGGATCTACACCGAGGTCCAGGAGTTCGTCGCCGCCATCGCGCGCCGTGACGTCAACGAGCTGGCGAGCCGCTACGGCATCGCCGGCAACGACCTGGCCGGCCTCGATGAGCAGCTGGCGGGCCTGTCGAGCCCCGCGTCGGATCTGACCCTCTACCCCGTGGAGCAGGCCGACGACTATGTTGACGGCCACCACCGCCTCGACCTCAGTGAGCTGGAGGGCGGCGGCGTCGTCATCAGCAGCGAGCTGTGGGCCCACGATCGGCCCTGCGGTGCGCGCCTCATCGCCCACTGGAACCCCATGGGGATCTACCCCTTCGACTTCCGCAACGTGAGCATGTGA","VAWSPDGTRLLSGSHDGTARVWDASRGTELFALAGPSLSISAVAWSPDGTRLLTAAEDHSVRVWDATTGADLLTLGVGGSGVGGAVAWSPDSTRILTSFDDASARIWDASSGQVVRTLSGHTEHLTAVSWSPDGTRVATASDDGTARVWDVTTGTELLRVGPMAFVGRGATMGPDGRPTHVGPIEPMTGLSWSPDSRRIITAFDSAEPRVWDAATGEEVLSLHGRERRWVSVVSWSPDGSRIITDDISGTTAHIWDAATGEELLSLRGHHQWACALAWSPDGTRVATGSHDDTVRVWDAATGQTQLVLGAGNSVETVSWSPDGTKLSIGAKIGGNRVWDATTGEPRLTVDNGARELSEVVWSPDGTRLATSSYLSPRVLILDASTGDVVQALTAGEDDVNDIAWSPDSERILTGLGDDRAAIWDAARGERLLTLEGHSDMITSVAWSPNGQRALTGSQDGTARIWDAATGEVIHTYTGNWVRDVVWTQGGPRVVTGSADGAAHVWDVITSGELVTLRDDAAMVRSYAWSPDGAKVLAGFDDGVVRVWDEVSGKIVLSLAGHRFGVTDAQWSPDGTRILTGSEDGTVRLWDATTGEMTGLFLCFLPDGGVAILDAPSLSLRSGPAEVWDYLGRPEILAGQLTRVGVERRQYLNSDPLPTVVSEPSPAETTDEDPTTSEPVEEPQVPEATEPSEGREASEADVLGDSVDTPSVFAVPAQPAAESATEAEQPAASQSPEDAPAQAPESSAPAGEPLIEEAPAEAQAPQVEEPAPAETESSETPEPVPAPEEEDAATAHQARHAAVTAHTPTEAAQAPDALGQPVAPAETEPVAAPTGETLLVQPFPVEQGLVDGEVSAPAVAPPAMVEMPPALVAPEGDRQEQSEAQPVLSTPEASQEVGAEAGAATLTVPAPEAEAADGSRRARHAAATAQTPADAPEQAAEGGTEAAQSSEPGLASPTDAAHSSGTAESAYEPVAIPAVEHAGGEPVAAPTGETVAPDQLELPLAPADAVAHEGDEVTLDLSEDASEAPAPAEATAPPVADIAETARAAGPVDVSDAADAAPATDSADAPAREAPVSSGAEAVSAPTASTPEGEPEDQAVPEGEAEQGLAEQAPVEHPQAQDNPERSREPEEAEASQPTDAEAPAEDRPGAEQEPTEPAEPTEPTPAPWGSADLRQRIYTEVQEFVAAIARRDVNELASRYGIAGNDLAGLDEQLAGLSSPASDLTLYPVEQADDYVDGHHRLDLSELEGGGVVISSELWAHDRPCGARLIAHWNPMGIYPFDFRNVSM$","WD-40 repeat protein","Periplasm, Cellwall, Extracellular","beta transducin-like protein HET-E2C*4","WD-40 repeat","WD-40 repeat protein","","Li D., Roberts R. WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. Cell. Mol. Life Sci. 2001. 58(14):2085-2097. PMID: 11814058Smith T.F., Gaitatzes C., Saxena K., Neer E.J. The WD repeat: a common architecture for diverse functions. Trends Biochem. Sci. 1999. 24(5):181-185. PMID: 10322433","","","

InterPro
IPR001680
Repeat

WD-40 repeat
PD000018	$\"[33-65]T$ $\"[117-150]T$ $\"[265-298]T$ $\"[433-466]T$ $\"[557-589]T$	YCW2_YEAST_P25382;
PR00320	$\"[10-24]T$ $\"[285-299]T$ $\"[577-591]T$	GPROTEINBRPT
PF00400	$\"[1-23]T$ $\"[27-65]T$ $\"[70-108]T$ $\"[112-150]T$ $\"[174-212]T$ $\"[260-298]T$ $\"[302-339]T$ $\"[386-424]T$ $\"[428-466]T$ $\"[470-506]T$ $\"[510-548]T$ $\"[552-590]T$	WD40
SM00320	$\"[1-23]T$ $\"[26-65]T$ $\"[68-108]T$ $\"[111-150]T$ $\"[177-212]T$ $\"[215-256]T$ $\"[259-298]T$ $\"[301-339]T$ $\"[342-382]T$ $\"[385-424]T$ $\"[427-466]T$ $\"[469-506]T$ $\"[509-548]T$ $\"[551-590]T$	WD40
PS50082	$\"[1-32]T$ $\"[33-74]T$ $\"[85-117]T$ $\"[118-159]T$ $\"[180-221]T$ $\"[266-307]T$ $\"[307-348]T$ $\"[392-433]T$ $\"[434-475]T$ $\"[481-515]T$ $\"[516-557]T$ $\"[558-599]T$	WD_REPEATS_2
PS50294	$\"[1-599]T$	WD_REPEATS_REGION
PS00678	$\"[10-24]?$ $\"[52-66]?$ $\"[95-109]?$ $\"[137-151]?$ $\"[285-299]T$ $\"[411-425]?$ $\"[453-467]?$ $\"[493-507]?$ $\"[577-591]T$	WD_REPEATS_1

noIPR
unintegrated

unintegrated
G3DSA:2.130.10.10	$\"[1-298]T$ $\"[303-590]T$	no description
PTHR22847	$\"[38-151]T$ $\"[214-477]T$	WD40 REPEAT PROTEIN
PTHR22847:SF50	$\"[38-151]T$ $\"[214-477]T$	G-PROTEIN BETA WD-40 REPEATS CONTAINING PROTEIN

","BeTs to 6 clades of COG2319COG name: WD40 repeat proteinFunctional Class: R [General function prediction only]The phylogenetic pattern of COG2319 is ------y-vd---c--g----j----Number of proteins in this genome belonging to this COG is 1","***** IPB003648 (Splicing factor motif) with a combined E-value of 2.3e-25. IPB003648C 35-62 IPB003648E 106-154 IPB003648G 254-297 IPB003648C 560-587 IPB003648D 106-144***** IPB001680 (G-protein beta WD-40 repeat signature) with a combined E-value of 5.8e-19. IPB001680A 137-151 IPB001680B 285-299 IPB001680C 577-591 IPB001680A 10-24 IPB001680A 577-591 IPB001680A 453-467 IPB001680A 285-299 IPB001680A 493-507 IPB001680A 52-66 IPB001680B 137-151 IPB001680B 453-467 IPB001680B 493-507 IPB001680B 52-66 IPB001680C 285-299 IPB001680C 52-66 IPB001680C 493-507 IPB001680C 453-467 IPB001680C 95-109***** IPB013890 (Transcriptional repressor Tup1, N-terminal) with a combined E-value of 6.3e-19. IPB013890D 274-321 IPB013890G 405-444 IPB013890H 453-465 IPB013890H 411-423 IPB013890H 285-297***** IPB000002 (Cdc20/Fizzy) with a combined E-value of 1.6e-13. IPB000002B 125-150 IPB000002D 269-297 IPB000002B 441-466 IPB000002B 40-65 IPB000002B 481-506 IPB000002D 36-64 IPB000002D 395-423***** IPB007148 (Dip2/Utp12) with a combined E-value of 3.6e-12. IPB007148C 33-83 IPB007148D 95-128 IPB007148H 435-467 IPB007148B 536-547 IPB007148C 434-484 IPB007148C 474-524 IPB007148C 558-608 IPB007148F 556-584 IPB007148H 393-425 IPB007148K 95-126***** IPB001632 (Beta G-protein (transducin) signature) with a combined E-value of 1.4e-09. IPB001632B 10-24 IPB001632D 280-297 IPB001632A 118-134 IPB001632A 434-450 IPB001632A 266-282 IPB001632A 558-574 IPB001632A 33-49 IPB001632B 493-507 IPB001632B 52-66 IPB001632B 411-425 IPB001632D 132-149***** IPB012972 (NLE) with a combined E-value of 4.4e-09. IPB012972C 12-24 IPB012972D 119-140 IPB012972C 54-66 IPB012972C 495-507 IPB012972D 435-456 IPB012972D 267-288***** IPB006692 (Coatomer WD associated region) with a combined E-value of 7.8e-09. IPB006692B 426-476 IPB006692D 549-583 IPB006692A 114-157***** IPB007582 (WD40 associated region in TFIID subunit) with a combined E-value of 8.1e-07. IPB007582I 96-138 IPB007582E 508-549 IPB007582E 258-299 IPB007582F 558-588 IPB007582F 434-464 IPB007582F 118-148 IPB007582F 33-63 IPB007582F 266-296 IPB007582F 516-546 IPB007582G 547-582 IPB007582G 255-290 IPB007582G 107-142 IPB007582H 101-137 IPB007582H 16-52 IPB007582H 541-577 IPB007582H 417-453 IPB007582I 11-53 IPB007582I 536-578 IPB007582I 412-454 IPB007582I 494-536 IPB007582I 578-620 IPB007582I 244-286 IPB007582I 138-180 IPB007582I 286-328***** IPB007190 (Periodic tryptophan protein-associated domain) with a combined E-value of 7.5e-06. IPB007190F 45-74 IPB007190C 551-584 IPB007190C 427-460 IPB007190F 570-599 IPB007190F 130-159 IPB007190F 446-475 IPB007190F 528-557 IPB007190F 278-307 IPB007190F 88-117 IPB007190F 3-32 IPB007190F 486-515 IPB007190F 404-433 IPB007190F 319-348 IPB007190F 192-221 IPB007190G 434-485 IPB007190G 558-609 IPB007190I 398-442 IPB007190I 522-566","","","-50% similar to PDB:2CO0 WDR5 AND UNMODIFIED HISTONE H3 COMPLEX AT 2.25 ANGSTROM (E_value = 1.4E_30);-50% similar to PDB:2G99 Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5 (E_value = 2.4E_30);-50% similar to PDB:2G9A Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5 (E_value = 2.4E_30);-50% similar to PDB:2GNQ Structure of wdr5 (E_value = 2.4E_30);-50% similar to PDB:2H13 Crystal structure of WDR5/histone H3 complex (E_value = 2.4E_30);","Residues 1 to 23 (E_value = 7.5e-08) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 27 to 65 (E_value = 1.6e-09) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 70 to 108 (E_value = 0.0016) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 112 to 150 (E_value = 4e-13) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 174 to 212 (E_value = 212) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 260 to 298 (E_value = 1.3e-11) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 302 to 339 (E_value = 0.0073) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 386 to 424 (E_value = 2.8e-06) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 428 to 466 (E_value = 1.1e-12) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 470 to 506 (E_value = 1.8e-06) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 510 to 548 (E_value = 8e-05) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.Residues 552 to 590 (E_value = 8.8e-13) place ANA_2646 in the WD40 family which is described as WD domain, G-beta repeat.","","transducin-like protein HET-E2C*4","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2647","2849822","2850559","738","9.71","8.06","27227","GTGTCGACGGGGCAGTACCCGGCACGGGCCCGTGTCGCCGCCTGGGCAGTGCACATCTTGACCATGTCGGGACTGGTGTGGGCCAGCCTGGCCATGCTCGCCACGATCCACCCCCGCCGGGAGTTCACGTGGATGTGGGTCTGGCTGCTCGTCGCCCTCGTCGTCGATGGCGTTGACGGCACCCTGGCCCGGCGCGCCCGGGTCTCGGAGATCATCCCCTGGTTCGACGGCGGCATCGTCGACATCGTCGTCGATTACCTCACCTGGACCTTCATCCCGGCGGTCTTCATGTACGTGGCTCTGCCGATGGGCCCCAGGCCGCTGGCGGGACTGCTCATGGCCCTCGTCCTGAGCTCGTCGATGTTCTGCTACGCCAATAAGCAGTGGAAGTCCACCGACTACTACTTCGTGGGCTTCCCGGCCGCCTGGAACATCGTGGCCCTCATGTTCTACGTGCTTCAGACCCCGGCGGTCTTCAACATCATCGTCACCCTCATTTTCGTGGTGCTGACCCTGGTGCCCACGCACTACGCGCACCCGGCCCGCGTCAAGCGCTTCCGCGCCCTCAACATCGGTGCGGTGGCCGTGTGGTTCCTGGCCACCTGCTGGCTGGTGGCGATCTACCCCCACCGGCCGCTCAGCCTGGTCGCCGTCCTCATCGTCTCGGGCGGGTGGTTCCTGCTCGCCGGGGTGCTGCGCTCGATCCGCGGGGAGGAATCGACCGCGGCAGCGGTGTAG","VSTGQYPARARVAAWAVHILTMSGLVWASLAMLATIHPRREFTWMWVWLLVALVVDGVDGTLARRARVSEIIPWFDGGIVDIVVDYLTWTFIPAVFMYVALPMGPRPLAGLLMALVLSSSMFCYANKQWKSTDYYFVGFPAAWNIVALMFYVLQTPAVFNIIVTLIFVVLTLVPTHYAHPARVKRFRALNIGAVAVWFLATCWLVAIYPHRPLSLVAVLIVSGGWFLLAGVLRSIRGEESTAAAV$","CDP-alcohol phosphatidyltransferase","Membrane, Cytoplasm","CDP-alcohol phosphatidyltransferase familyprotein","phosphatidylcholine synthase ","CDP-alcohol phosphatidyltransferase","","Nikawa J., Kodaki T., Yamashita S. Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae. J. Biol. Chem. 1987. 262(10):4876-4881. PMID: 3031032Hjelmstad R.H., Bell R.M. sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products. J. Biol. Chem. 1991. 266(8):5094-5134. PMID: 1848238","","","

InterPro
IPR000462
Family

CDP-alcohol phosphatidyltransferase
PF01066	$\"[47-184]T$	CDP-OH_P_transf

noIPR
unintegrated

unintegrated
signalp	$\"[1-28]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[45-63]?$ $\"[78-98]?$ $\"[104-124]?$ $\"[134-154]?$ $\"[158-178]?$ $\"[188-208]?$ $\"[212-232]?$	transmembrane_regions

","BeTs to 3 clades of COG1183COG name: Phosphatidylserine synthaseFunctional Class: I [Metabolism--Lipid metabolism]The phylogenetic pattern of COG1183 is aom---y---r-b--f--snujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB000462 (CDP-alcohol phosphatidyltransferase) with a combined E-value of 7.4e-07. IPB000462 45-92","","","No significant hits to the PDB database (E-value < E-10).","Residues 47 to 184 (E_value = 0.0098) place ANA_2647 in the CDP-OH_P_transf family which is described as CDP-alcohol phosphatidyltransferase.","","phosphatidyltransferase family protein (AF155772)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2649","2851730","2852743","1014","10.59","7.37","34989","ATGAGTACTCACGCCACCCCCTCAGAGCGGTCCAGCCGGCGCGGCGACCCGGGGCTGCTCGTCGTGGCCGGAGCGGGCCTCATCGGATCCCGCCTGGCGGACATGGCCCGGGACCACGGCTGGAGAATCCGGATCCTCCACCGCAGCGCAGCGGGCCAGGCGCCGCGGGAGAGTATCGAGGTCGATGACTCCGGCAGGGAGCACGCCTGGTGGGCGCCCGCCGAGCGCCTCCTGCCGCCCGGCGCCCTGGAGGGCGCCAGAGCCGTGGTCTGCCTGTCGGGCGCCCCGATCGCGCCGCGCCCCTGGACACCGGCGCGCCGTCGCGAGCTGGCGGCCTCACGCCTGTCCACCACCGCCCTCATCGCCCGGGTCGCCGCGGCCCTGCCCCCGGCCGGGCGACCCGAGGTCCTGCTGAGCGGATCGGCCACTGGCTTCTACGGGGATCGGGGCGAGGAGATCCTCACCGAGGCCAGCGGCCCGGGTGAGGGATTCCTGTCCGAGCTGTGCCGGCGCTGGGAGTCCGTTGCGGGCCCGGCGGCGAGAGCCGGGCTGCGCACGGTCCAGTCCCGCACGGGCCTGGTGGTCAGCTCCTCGGGCGGGCTGGGGAGGATCCTCGGCGCCGCCTACCGGGTCGGGGCGGGGGCCCGGCTGGGCCGCGGCGACCAGTGGCAGCCGTGGATCGGCCTGGAGGATGCCGCCGCCGGGCTCCTGTGGGCCATCGAGCACGACGACGTCCGCGGGCCGGTCAACCTGACCGCGCCCGAGCCGGCGCGCAACCGCGACCTCCACCGTCTGCTGTCGCGCGCCGGCGGCCCGCCCTCGATAGCAGTCGTGCCCCAGTTCCTGCTGGACTGGGCGGGCAGGGTCGGGGCGGCCGGGGGTGCCGGTGGCATCGGCGGGATGCTCGCCGAGCTGCTCGGCGCCTCCCAGCGAGCGGTCCCCCGGGCGCTGCTCGCCTCCGGATTCCGCTTCACCGCGCCGGACGCGGCCTCGATCTGGTCATCGGGCGACTGA","MSTHATPSERSSRRGDPGLLVVAGAGLIGSRLADMARDHGWRIRILHRSAAGQAPRESIEVDDSGREHAWWAPAERLLPPGALEGARAVVCLSGAPIAPRPWTPARRRELAASRLSTTALIARVAAALPPAGRPEVLLSGSATGFYGDRGEEILTEASGPGEGFLSELCRRWESVAGPAARAGLRTVQSRTGLVVSSSGGLGRILGAAYRVGAGARLGRGDQWQPWIGLEDAAAGLLWAIEHDDVRGPVNLTAPEPARNRDLHRLLSRAGGPPSIAVVPQFLLDWAGRVGAAGGAGGIGGMLAELLGASQRAVPRALLASGFRFTAPDAASIWSSGD$","NAD-dependent epimerase/dehydratase","Cytoplasm, Extracellular","conserved hypothetical protein TIGR01777","hypothetical protein","NAD-dependent epimerase/dehydratase","","Stammers D.K., Ren J., Leslie K., Nichols C.E., Lamb H.K., Cocklin S., Dodds A., Hawkins A.R. The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases. EMBO J. 2001. 20(23):6619-6626. PMID: 11726498","","","

InterPro
IPR008030
Family

NmrA-like
PF05368	$\"[19-58]T$	NmrA

InterPro
IPR010099
Family

Conserved hypothetical protein, YfcH
PTHR11092	$\"[21-328]T$	SUGAR NUCLEOTIDE EPIMERASE RELATED
TIGR01777	$\"[20-330]T$	yfcH: conserved hypothetical protein TIGR01

InterPro
IPR013549
Domain

Domain of unknown function DUF1731
PF08338	$\"[278-333]T$	DUF1731

","BeTs to 8 clades of COG1090COG name: Predicted nucleoside-diphosphate sugar epimerases (SulA family)Functional Class: R [General function prediction only]The phylogenetic pattern of COG1090 is ---p------r-bcef-hs-------Number of proteins in this genome belonging to this COG is 1","***** IPB013549 (Domain of unknown function DUF1731) with a combined E-value of 1e-56. IPB013549A 19-43 IPB013549B 87-125 IPB013549C 136-169 IPB013549D 190-240 IPB013549E 245-293 IPB013549A 289-313","","","No significant hits to the PDB database (E-value < E-10).","Residues 19 to 58 (E_value = 0.00034) place ANA_2649 in the NmrA family which is described as NmrA-like family.Residues 20 to 252 (E_value = 6.6e-05) place ANA_2649 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family.Residues 278 to 333 (E_value = 0.00017) place ANA_2649 in the DUF1731 family which is described as Domain of unknown function (DUF1731).","","hypothetical protein TIGR01777","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2650","2853743","2852781","963","7.64","2.30","34206","GTGAGAAGACTTCCACCGAGACGTTCACTGAGACGAAACATCTCGCGATCCGGAGGGAAATTGCCGTTGCGGAGGCCACATTCCGGACGTCCACGCAACACAGATCACATTCCTGGAGGATCTGGAGGCATGAGTAGTGAACAGCTTCCAGACGGTTCCGTCGAGACGGCCCGCTACACCCACGGTCACAGTGCGGCGGTGCTCAGCGCGCACTCGCGGCGCGGCGCGGCGGACTCGGCCGCCTACCTGCTTGCCCACCTGCGTGCGGGAATGGACCTGCTCGACGTCGGCTGCGGGCCGGCGTCCATCACCGCGGATCTCGCTGAGCGCGTCGCCCCGGGGCGGGTCGTCGCCCTCGATGCCGCAGCCGGTGCCCTGGAGGCGGCTCGGGCGACGCTTCGCGAACGGGGGCTGTCCGAGCAGGTGGAGGTGACCAGCGGGGACGTCATGGCCCTGCCCTTCGAGGACGCCTCCTTCGACGTCGTCCACGCCCACCAGGTCCTTCAGCACCTCGCGGACCCGGTGGGTGCCCTGGCCGAGATGCGCCGCGTCACCCGCCCCGGCGGGATCGTGGCCGTGCGCGACGCCGTCTACTCCGCCATGACCTGGTTCCCCGAGCCCGCGGGCATGGAGCAGTGGCGCTCGGTCTACATGGCCACCGCCCGGGCCAACGGAGGCGAGCCCGACGCCGGCAGCAGGCTGCTGTCCTGGGCCCGGGCGGCGGGTTTCGCCGACGCGAGCGCCTCGGCCTCCACCTGGTGCTACGCCACGCCCGCCGACCGGGCCTGGCAGTCGCAGACCTGGGCGCAGCGGTGCCTGACCTCCTTCGGGCCGCGGGCCGTCGAGCTGGGACTGGCGGACAGGGCCGACCTGGAGACGATGGCCCAGGCGTGGCGGCAGTGGGGAGACAGCGAGGACGCCTGGTTCGTCGTCGTGCACGGCGAGGTCCTGGCCCGCGCCTGA","VRRLPPRRSLRRNISRSGGKLPLRRPHSGRPRNTDHIPGGSGGMSSEQLPDGSVETARYTHGHSAAVLSAHSRRGAADSAAYLLAHLRAGMDLLDVGCGPASITADLAERVAPGRVVALDAAAGALEAARATLRERGLSEQVEVTSGDVMALPFEDASFDVVHAHQVLQHLADPVGALAEMRRVTRPGGIVAVRDAVYSAMTWFPEPAGMEQWRSVYMATARANGGEPDAGSRLLSWARAAGFADASASASTWCYATPADRAWQSQTWAQRCLTSFGPRAVELGLADRADLETMAQAWRQWGDSEDAWFVVVHGEVLARA$","SAM-dependent methyltransferase","Cytoplasm, Extracellular","putative methyltransferase-UbiE family","hypothetical protein","Methyltransferase type 11","","","","","

InterPro
IPR013216
Domain

Methyltransferase type 11
PF08241	$\"[94-193]T$	Methyltransf_11

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.150	$\"[84-247]T$	no description
PTHR10108	$\"[87-270]T$	METHYLTRANSFERASE
PTHR10108:SF26	$\"[87-270]T$	METHLYTRANSFERASE, UBIE/COQ5 FAMILY

","BeTs to 17 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism] Functional Class: R [General function prediction only]The phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 6","***** IPB004033 (UbiE/COQ5 methyltransferase) with a combined E-value of 2.4e-09. IPB004033C 152-175 IPB004033D 176-208","","","No significant hits to the PDB database (E-value < E-10).","Residues 51 to 256 (E_value = 2.4e-06) place ANA_2650 in the Ubie_methyltran family which is described as ubiE/COQ5 methyltransferase family.Residues 64 to 194 (E_value = 0.0003) place ANA_2650 in the MTS family which is described as Methyltransferase small domain.Residues 94 to 193 (E_value = 6.2e-34) place ANA_2650 in the Methyltransf_11 family which is described as Methyltransferase domain.Residues 94 to 191 (E_value = 8.4e-23) place ANA_2650 in the Methyltransf_12 family which is described as Methyltransferase domain.","","methyltransferase-UbiE family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2651","2853801","2855138","1338","5.51","-10.70","47218","ATGCAGGACGTTGTCGAAAAGGTCTATGAGCAGGTTGTGGCTCGCAACCGTGGAGAGGTCGAGTTCCATCAGGCCGTCCACGAGGTGCTCGAGTCCCTCGGTCCCGTCATCGCCAAGCACCCCCACTACGCCGATGGCGCCCTCCTGGAGCGCATCGTCGAGCCCGAGCGCCAGATCATGTTCCGGGTCCCGTGGGTCGACGACGCCGGCCAGGTTCACGTCAACCGCGGCTTCCGCATCGAATTCAACTCCGCGCTGGGCCCCTACAAGGGCGGCCTGCGCTTCCACCCCTCGGTCAACGCCGGAATCATCAAGTTCCTCGGCTTCGAGCAGATCTTCAAGAACGCCCTGACCGCCCAGGGCATCGGCGGCGGCAAGGGCGGCTCCGACTTCGACCCGCATGGCCGCTCCGACGCCGAGGTCATGCGCTTCTGCCAGTCCTTCATGACCGAGCTGGCCCGCCACATCGGCCCCTCCACCGACGTGCCCGCCGGCGACATCGGCGTGGGCGGCCGCGAGATCGGTTACATGTTCGGCCAGTACAAGCGCCTGCGGAACTCCTACGACGCCGGTGTCCTCACCGGTAAGGGCCTGGCCTGGGGCGGCTCCCTCGTGCGCACCGAGGCCACCGGCTACGGCACCGTGCTCTTCGCCCAGTCCATGCTCGCCACCAGGGGCGAGTCCCTTGAGGGCAAGAAGGTCCTCGTCTCCGGAGCCGGGAACGTGGCGATCTACGCCATCGAGAAGGCCCAGCAGCTCGGCGCCACCCCCATCACCTTCTCCGACTCCTCCGGCTACGTCGTCGACGAGGCCGGGGTGGACCTCGAGCTGCTCAAGCAGGTCAAGGAGGTCGAGCGCGGCCGCGTGGCCGACTACGTCGAGCGCCGCCCCGGTGCCCGCCTCGTGACCGGCGGCTCCGTGTGGGACGTCCCCGGCGACGTCGCCCTGCCCTGCGCCACCCAGAACGAGCTCGACGGCGACGCCGCGAACACCCTGCTGCGGGGCGGCTGCGGCGTGGTCTCCGAGGGCGCCAACATGCCCTCCACCCCGGAGGCCGTCGAGGCCTTCCAGAAGGCCGGCATCCTCTTCGGCCCCGGTAAGGCCGCCAACGCCGGTGGCGTGGCGACCTCCGCCCTCGAGATGGAGCAGAACGCCGGCCGCACCCGCTGGGACTTCGCCACCGCCGAGGCCAAGCTGACCGGCATCATGGCTGACATCCACGACTCCTGCGTCGCCGCGGCCGAGGAGTACGGCCGCCCCGGCGACTACGTGCTCGGCGCCAACGCGGCCGGTTTCACCCGCGTTGCCGACGTCATGATCGCCCACGGCATCGTCTGA","MQDVVEKVYEQVVARNRGEVEFHQAVHEVLESLGPVIAKHPHYADGALLERIVEPERQIMFRVPWVDDAGQVHVNRGFRIEFNSALGPYKGGLRFHPSVNAGIIKFLGFEQIFKNALTAQGIGGGKGGSDFDPHGRSDAEVMRFCQSFMTELARHIGPSTDVPAGDIGVGGREIGYMFGQYKRLRNSYDAGVLTGKGLAWGGSLVRTEATGYGTVLFAQSMLATRGESLEGKKVLVSGAGNVAIYAIEKAQQLGATPITFSDSSGYVVDEAGVDLELLKQVKEVERGRVADYVERRPGARLVTGGSVWDVPGDVALPCATQNELDGDAANTLLRGGCGVVSEGANMPSTPEAVEAFQKAGILFGPGKAANAGGVATSALEMEQNAGRTRWDFATAEAKLTGIMADIHDSCVAAAEEYGRPGDYVLGANAAGFTRVADVMIAHGIV$","NADP-specific glutamate dehydrogenase","Cytoplasm","NADP-specific glutamate dehydrogenase","glutamate dehydrogenase (NADP+) ","Glutamate dehydrogenase (NADP(+))","","Britton K.L., Baker P.J., Rice D.W., Stillman T.J. Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases. Eur. J. Biochem. 1992. 209(3):851-859. PMID: 1358610Benachenhou-Lahfa N., Forterre P., Labedan B. Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. J. Mol. Evol. 1993. 36(4):335-346. PMID: 8315654Moye W.S., Amuro N., Rao J.K., Zalkin H. Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase. J. Biol. Chem. 1985. 260(14):8502-8508. PMID: 2989290Mavrothalassitis G., Tzimagiorgis G., Mitsialis A., Zannis V., Plaitakis A., Papamatheakis J., Moschonas N. Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc. Natl. Acad. Sci. U.S.A. 1988. 85(10):3494-3498. PMID: 3368458Nagata S., Tanizawa K., Esaki N., Sakamoto Y., Ohshima T., Tanaka H., Soda K. Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases. Biochemistry 1988. 27(25):9056-9062. PMID: 3069133","","","

InterPro
IPR006095
Family

Glu/Leu/Phe/Val dehydrogenase
PR00082	$\"[112-126]T$ $\"[192-214]T$ $\"[234-254]T$ $\"[369-380]T$	GLFDHDRGNASE
PTHR11606:SF2	$\"[18-445]T$	GLUTAMATE DEHYDROGENASE

InterPro
IPR006096
Domain

Glu/Leu/Phe/Val dehydrogenase, C-terminal
PF00208	$\"[201-443]T$	ELFV_dehydrog

InterPro
IPR006097
Domain

Glu/Leu/Phe/Val dehydrogenase, dimerisation region
PF02812	$\"[55-185]T$	ELFV_dehydrog_N

InterPro
IPR014362
Family

Glutamate dehydrogenase
PIRSF000185	$\"[19-445]T$	Glutamate dehydrogenase

noIPR
unintegrated

unintegrated
G3DSA:1.10.285.10	$\"[2-52]T$	no description
G3DSA:3.40.192.10	$\"[57-200]T$	no description
G3DSA:3.40.50.720	$\"[201-443]T$	no description
PTHR11606	$\"[18-445]T$	GLUTAMATE DEHYDROGENASE

","BeTs to 15 clades of COG0334COG name: Glutamate dehydrogenase/leucine dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0334 is ao-pkzy-vd--bcef-h-nuj-i--Number of proteins in this genome belonging to this COG is 2","***** IPB006095 (Glu/Leu/Phe/Val dehydrogenase) with a combined E-value of 9.2e-121. IPB006095A 77-94 IPB006095B 104-152 IPB006095C 156-181 IPB006095D 193-213 IPB006095E 231-272 IPB006095F 336-356 IPB006095G 360-384","","","-65% similar to PDB:1BGV GLUTAMATE DEHYDROGENASE (E_value = 2.5E_119);-65% similar to PDB:1HRD GLUTAMATE DEHYDROGENASE (E_value = 2.5E_119);-65% similar to PDB:2BMA THE CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM GLUTAMATE DEHYDROGENASE, A PUTATIVE TARGET FOR NOVEL ANTIMALARIAL DRUGS (E_value = 3.2E_119);-64% similar to PDB:1K89 K89L MUTANT OF GLUTAMATE DEHYDROGENASE (E_value = 2.7E_118);-64% similar to PDB:1AUP GLUTAMATE DEHYDROGENASE (E_value = 7.9E_118);","Residues 55 to 185 (E_value = 1.3e-75) place ANA_2651 in the ELFV_dehydrog_N family which is described as Glu/Leu/Phe/Val dehydrogenase, dimerisation domain.Residues 201 to 443 (E_value = 1e-127) place ANA_2651 in the ELFV_dehydrog family which is described as Glutamate/Leucine/Phenylalanine/Valine dehydrogenase.","","glutamate dehydrogenase (gdhA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2653","2855415","2857901","2487","4.89","-26.38","83406","ATGTTCCTCTCCTCATCTTCTCCCGGGTCACCATCCCTCCGCCTGATAAGGAACGACATGCGACTGCGCCCCACGCGGGCCGTCAGGGTCAGCGCCGTCCTGTGCGCGCTGACTCTGACAGCCCTCAGTCCCTTCCCGCTCAGCCCTCCCGCCGGTGCTGACGAGCCAGCCGCCCCGGCTGCCCCTCCGGCCGCCGGCGCCACCACCATCGACCTGCTGGGCATCACCGACCTGCACGGCCACATCTCCCGGACCACTCAGACGGACAGCGGTACCGGGCAGACATCCGTCGAGGACCCCGGTGCTGTCACGCTGGCCTGCGAGGTCTCCTCCGCCCGCGCCGCCAACCCCAACACGCTGTTCGTCTCCGCCGGAGACTCCGTGGGTGGATCAGCCTACGTCTCCTCCATCCTCCAGGACCGCCCCACTATGGAGGCGCTCAACGCGATGTCCCTGGATGTCTCCGCCCTGGGCAACCACGAGCTCGACCAGGGCTTGACCGACCTGGAGGCGCGCATCCTGCCCGCCTCGAACTTCCCGATCCTGGCCGCCAATGTCTCCGGCTCGACTCCCTTGAGCGCCGAGGGCGGCGGCAAGGGAGCCTTCATCAAGGAGGTCGGCGGTGTGCGCGTCGGCTTCGTCGGTGTCGTCACCGATGAGCTTCCCACCCTCGTGTCGCCCTCGGCCCTGTCCACTCTCACCCTGAGTCCGGCGGTCGCCGCCGCCAACGCCCGTGCCGCCGAGCTCAAGGACGGCGACCTGGCCAACGGTGAGGCCGACGTCGTCGTCGTGCTCAGCCATGAGGACGCGGCCTCCACGGCCACGAGCTTCTCCAAGAACGTCGACGCCGTCTTCTCCGGGCACACCCACGTGCCCTTCGCCAAGACCGTCACCGGCGCCGAGGGCAACCAGATCGCCGTCGTCCAGGCCGACCACTACGGCTGGGCGCTGGGCCGCATCCGCCTGAGCTACGACCCCGCCAGCCGGAAGACCTCAGTGGTCAGCGCCGACAACAAGGACCTGCGCAGCTCGAGCTGCACCACCGATGCCTACGGCGTCGCCGGAATCGTGTCCCAGGCGGAGAAGGACTCCGCCGCCGAGGGCGGCAAGCCGCTGGCCAAGATCGGCTCGGACTTCCTGCGCGGCTCGGACGGCTCGGGCCCCGGCGCCAACCGCGGCACGGAGTCCACTGCCTCCAACCTCATCGCCGAGTCCTTCCGCAGCTGGCTCGCCACCGACATCCAGCCGACCGGCTCCACCCGCTACGTGGGCATCATGAACCCCGGCGGCGTGCGCGCCGACCTGCTCTACGCCGCCTCCGGCTCGGAGGGCGATGGGGTCCTGACCTCGGGGGAGGCCTACACGGTCCAGCCCTTCGGCAACGAGATGGCCTACACGACCCTCACCGGCGCCGAGCTCAAGGCGCTGCTGTCCCAGCAGTGGCAGCCCGGCTCCAGCCGCCCCGTGCTCACCCTGGGGCTGTCCAGGAACGTCGACGTCCTCACCGAGGCCACCACCGATCCCGCATACGGGGGCGAGGCCGGAGCCGCCCCCGCGATCCGCGAGATCCTCGTCGACGGCAAGCCGCTGGCCGACGGCGACAGCGTCGTCGTCGCCTCCAACTCCTTCCTGCTGACCGGCGGCGACGGCTACACCGTCCTGAAGGACAAGCCCGTGACCAACACCGGCGTCCTCGACCGCGACGTCACCTCCACCTACCTGGCCTCCTTCGGCGACAAGCCCGTCACAGCCGACTACTCCAAGCGGCAGACCGCGATGACCGTGGGGCCCGTATACGTCAGCTCAGGTGGCGCGCGCAGCACCGACACGGTCTCCGTGACCCTGGACTCCCTGGCCTACACCAACCCCACCGAGCAGGCCGCCGGCGCCCGACGCGTGCGCGTCAGCGCGGGGGATAAGGAGATCCTGACCAAGGACCTCGACCTCACCGTCAACCCCACCGGCCCGACCACCGGGCGGGTCGACTTCAACCTCACCTTCCCGACCGACGCCCCCACGCGTGCCTGCCGCACGGTCCAGGCCACCACCTGCCGCTGGGCCTTAGTCGAGACCCTCGACGCCGCAGGTGCGGTTCTCAACCGGTTCTCGGTCGAGATCGAGGATGAGGATGCAGCCGACCCCGGAGCGGGCCCGGGCGACAGCACGGCGACGGGCGCTGACGCTGCGGCGGACGGGGCCGGCGGCAAGGCGGCATCCACCCCGCAGGGCGGCCCTGGTACTGGTGAGACCTCCGCGGGCGGTGGCACCGAGCCGTCTGCGGGTAGCGGCGCGCAGCCCGCAGCCACCGCCGCTCCAGCCGCGTCCGGAGCGCCCGCCCAGGCGGCCGGAGCCGAGCGTCCGAACCAGGCGGCCAGTGATGGTCCTCTGGCCCGCACCGGCGCCTCACTTGGCGCGGGGGTACTCGCCCTCGCCCTGCTCGTCGTCGGCGGCTACCTCATCCTGCGCCGCAGACAGCAGGTCGCCTGA","MFLSSSSPGSPSLRLIRNDMRLRPTRAVRVSAVLCALTLTALSPFPLSPPAGADEPAAPAAPPAAGATTIDLLGITDLHGHISRTTQTDSGTGQTSVEDPGAVTLACEVSSARAANPNTLFVSAGDSVGGSAYVSSILQDRPTMEALNAMSLDVSALGNHELDQGLTDLEARILPASNFPILAANVSGSTPLSAEGGGKGAFIKEVGGVRVGFVGVVTDELPTLVSPSALSTLTLSPAVAAANARAAELKDGDLANGEADVVVVLSHEDAASTATSFSKNVDAVFSGHTHVPFAKTVTGAEGNQIAVVQADHYGWALGRIRLSYDPASRKTSVVSADNKDLRSSSCTTDAYGVAGIVSQAEKDSAAEGGKPLAKIGSDFLRGSDGSGPGANRGTESTASNLIAESFRSWLATDIQPTGSTRYVGIMNPGGVRADLLYAASGSEGDGVLTSGEAYTVQPFGNEMAYTTLTGAELKALLSQQWQPGSSRPVLTLGLSRNVDVLTEATTDPAYGGEAGAAPAIREILVDGKPLADGDSVVVASNSFLLTGGDGYTVLKDKPVTNTGVLDRDVTSTYLASFGDKPVTADYSKRQTAMTVGPVYVSSGGARSTDTVSVTLDSLAYTNPTEQAAGARRVRVSAGDKEILTKDLDLTVNPTGPTTGRVDFNLTFPTDAPTRACRTVQATTCRWALVETLDAAGAVLNRFSVEIEDEDAADPGAGPGDSTATGADAAADGAGGKAASTPQGGPGTGETSAGGGTEPSAGSGAQPAATAAPAASGAPAQAAGAERPNQAASDGPLARTGASLGAGVLALALLVVGGYLILRRRQQVA$","5'-nucleotidase/2',3'-cyclic phosphodiesterase","Extracellular, Cellwall","Ser/Thr protein phosphatase family","5'-nucleotidase ","metallophosphoesterase","","Zimmermann H. 5'-Nucleotidase: molecular structure and functional aspects. Biochem. J. 1992. 285:345-365. PMID: 1637327Champagne D.E., Smartt C.T., Ribeiro J.M., James A.A. The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5'-nucleotidase family. Proc. Natl. Acad. Sci. U.S.A. 1995. 92(3):694-698. PMID: 7846038Airas L., Niemela J., Salmi M., Puurunen T., Smith D.J., Jalkanen S. Differential regulation and function of CD73, a glycosyl-phosphatidylinositol-linked 70-kD adhesion molecule, on lymphocytes and endothelial cells. J. Cell Biol. 1997. 136(2):421-431. PMID: 9015312Thompson L.F., Ruedi J.M., Glass A., Low M.G., Lucas A.H. Antibodies to 5'-nucleotidase (CD73), a glycosyl-phosphatidylinositol-anchored protein, cause human peripheral blood T cells to proliferate. J. Immunol. 1989. 143(6):1815-1821. PMID: 2550543","","","

InterPro
IPR004843
Domain

Metallophosphoesterase
PF00149	$\"[70-292]T$	Metallophos

InterPro
IPR006179
Family

5'-Nucleotidase and apyrase
PR01607	$\"[68-86]T$ $\"[274-297]T$ $\"[305-325]T$ $\"[447-470]T$ $\"[529-548]T$	APYRASEFAMLY
PTHR11575	$\"[47-577]T$	5'-NUCLEOTIDASE-RELATED

InterPro
IPR008334
Domain

5'-Nucleotidase, C-terminal
G3DSA:3.90.780.10	$\"[391-594]T$	no description
PF02872	$\"[374-556]T$	5_nucleotid_C

noIPR
unintegrated

unintegrated
G3DSA:3.60.21.10	$\"[62-339]T$	no description
PTHR11575:SF7	$\"[47-577]T$	5-NUCLEOTIDASE-RELATED
signalp	$\"[1-44]?$	signal-peptide
tmhmm	$\"[801-821]?$	transmembrane_regions

","BeTs to 11 clades of COG0737COG name: 5'-nucleotidase/2',3'-cyclic phosphodiesterase and related esterasesFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0737 is aom---yqvd-lbce-gh--uj--t-Number of proteins in this genome belonging to this COG is 1","***** IPB006179 (Apyrase family signature) with a combined E-value of 1.9e-27. IPB006179A 68-86 IPB006179B 257-274 IPB006179C 274-297 IPB006179D 305-325 IPB006179E 447-470 IPB006179F 529-548***** IPB008334 (-Nucleotdase_C) with a combined E-value of 6.4e-20. IPB008334A 68-85 IPB008334B 118-126 IPB008334C 150-169 IPB008334D 177-186 IPB008334F 547-555","","","No significant hits to the PDB database (E-value < E-10).","Residues 70 to 292 (E_value = 7.5e-13) place ANA_2653 in the Metallophos family which is described as Calcineurin-like phosphoesterase.Residues 374 to 556 (E_value = 1.7e-12) place ANA_2653 in the 5_nucleotid_C family which is described as 5'-nucleotidase, C-terminal domain.","","protein phosphatase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2655","2858418","2859182","765","6.14","-2.82","26671","ATGCGCATTGAGGACAGGCACCGCCAGATCGTGGAGCAGGTGCGCGGTGCAGGGCGGGTTCTCGTCACCGAGCTCGCCGAGCACTTTGATGTCACCCCGGAGACGATCCGCCGCGACCTGACTGCCCTGGACCGCAACGGCGCCCTGCGCAAGGTCCACGGCGGCGCCATCCCCGCCCCCGCCCTGCCGGAGACCGGCGTGACCCAGCGCGAGCAGGTCAACCCCACCGCCAAGCAGGCCATCGCCCGAGCCGCCCTGGCGCGGCTCGCACCGAAGCCCGGCACCACCCTCCTCATCGACGCCGGAACCACCACCGGCTCGCTCGCCCGCCTCCTGCCGGGCGACACCGACCTGACCGTCATCACCAACTCCGTCCTGACCGCCGCCTGGTTGGCCGGCGCCGGACGCACCCGGGTGCGGATCCTGGGCGGCCAGCTGCGCGGACTGACCCAGGCCGCCGTCGGCCCCGAAGCCGTCGAGGCCCTGTCCACCCTGAGGGTCGACGTCGCCGTCCTGGGAGCCAACGGCCTGAGCGCAGCCCACGGACTGTCCACGCCCGACCCCGACGAAGCCACCGTCAAACGCGCCATGGTGCGCAGTGCCCGCCAGGTGGTGGCCCTGGTCGACTCCACCAAGATCGGCCAGGAGCACCTGGTCTCCTTCGCCTCCCTCGACGACATCGACCTCCTGGTCACTGACGTCGAGCTCCCGCCCGCACTCATCGACCAGCTCACCGCCACCGAAACCGAGGTACTTGTCGCATGA","MRIEDRHRQIVEQVRGAGRVLVTELAEHFDVTPETIRRDLTALDRNGALRKVHGGAIPAPALPETGVTQREQVNPTAKQAIARAALARLAPKPGTTLLIDAGTTTGSLARLLPGDTDLTVITNSVLTAAWLAGAGRTRVRILGGQLRGLTQAAVGPEAVEALSTLRVDVAVLGANGLSAAHGLSTPDPDEATVKRAMVRSARQVVALVDSTKIGQEHLVSFASLDDIDLLVTDVELPPALIDQLTATETEVLVA$","Transcriptional regulator, DeoR family","Cytoplasm","Transcriptional regulators of sugar metabolism","K03436 DeoR family transcriptional regulator; fructose operon transcriptional repressor","regulatory protein, DeoR","","Beck von Bodman S., Hayman G.T., Farrand S.K. Opine catabolism and conjugal transfer of the nopaline Ti plasmid pTiC58 are coordinately regulated by a single repressor. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(2):643-647. PMID: 1731335Ray W.K., Larson T.J. Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12. Mol. Microbiol. 2004. 51(3):813-826. PMID: 14731281","","","

InterPro
IPR001034
Domain

Bacterial regulatory protein, DeoR N-terminal
PR00037	$\"[24-38]T$ $\"[38-56]T$	HTHLACR
PF08220	$\"[6-57]T$	HTH_DeoR
SM00420	$\"[6-58]T$	HTH_DEOR
PS51000	$\"[3-58]T$	HTH_DEOR_2
PS00894	$\"[6-40]T$	HTH_DEOR_1

InterPro
IPR014036
Domain

Bacterial regulatory protein, DeoR
PF00455	$\"[75-233]T$	DeoR

","BeTs to 9 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K [Information storage and processing--Transcription] Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is 4","***** IPB001034 (Bacterial regulatory protein, DeoR family) with a combined E-value of 6.6e-59. IPB001034A 18-56 IPB001034B 79-112 IPB001034C 117-125 IPB001034D 139-156 IPB001034E 193-233","","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 57 (E_value = 1.9e-05) place ANA_2655 in the HTH_11 family which is described as HTH domain.Residues 6 to 62 (E_value = 2e-16) place ANA_2655 in the HTH_DeoR family which is described as DeoR-like helix-turn-helix domain.Residues 75 to 233 (E_value = 6.1e-44) place ANA_2655 in the DeoR family which is described as Bacterial regulatory proteins, deoR family.","","regulators of sugar metabolism","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2656","2859179","2860189","1011","4.49","-19.28","33648","ATGATCCTGACCCTCACACCCAACCCGTCCCTCGACCGCACCGTCTCCCTACCCGGACCCCTCCAGCGCGGCGCCGTCCAGCGCCTGACCGGCGTCGTCATGGAACCGGGAGGCAAGGGCGTCAACGTCGCCCGCGTCCTGTCCAACGCCGGGAGCGCCGCCACCGCCGTCCTTCCCGCCGCCGAGAACGACCCCATCCTCACCGCCCTGGGCGCCCTCGAGCTGCCCGGCCTCACCGTGCGATCCGTGCCTGTGGCCGGCCCCGCCCGCATCAACACCGCCGTCACCGAGCCCGACGGCACCACCACCAAGCTCAACGAGCTGGGGGCGGGCTTGAGCGAGGAGGAGATCGACGCCGTCGAGCAGGCCCTCCTGGAGACCCTCACCCTCACGGGGGTGTCGGCCGAAGCCGACACCCACCACTGGGCGGTCCTGTCCGGCTCCCTGCCGCCGGGCGCGCCGGCCAGGTGGTACGCCCGCCTCGTGGGGCTCCTGCGGGAGGCCGCCCCGGGGCTGCGCATCGCTGTCGACACCTCCGACGAACCCCTGGCGGCCCTGGCTGCCGAGCTGCCCGCATCGGCCCCCGACCTCATCAAACCCAACGGTGAGGAGCTCGGTCAGCTCGCCGGCCTGCCCGCCGAGCGCGCCATGGCCCTCGAGGAGGGCGCCGTCCAAGGGGACTACGGCCCCGTCGTCGACGCCGCCCGCCTCCTGGTGGGCCTGGGGCTCGGTGCCGTCATGGTGACCCTCGGCCCCGCCGGCGCCGTCCTGGTGACCGCCGACGGCGCCTGGCACGCCACCGCCCCCGAGGTCCCGGTGGTCTCCACCGTCGGCGCCGGGGACTCCTCGGTGGCCGGCTACATCCTGGCCGACGTCAACGGCGGCGACGAGGCCGAGCGCCTGCGCACCGCCATGGCCTACGGCTCGGCCGCCGCCTCCCTGCCCGGAACCACCCTGCCCACGCCCGCCGACCTGCCCGAGCAGGCGGCCGTCGTCACCCGGCTCTCCTGA","MILTLTPNPSLDRTVSLPGPLQRGAVQRLTGVVMEPGGKGVNVARVLSNAGSAATAVLPAAENDPILTALGALELPGLTVRSVPVAGPARINTAVTEPDGTTTKLNELGAGLSEEEIDAVEQALLETLTLTGVSAEADTHHWAVLSGSLPPGAPARWYARLVGLLREAAPGLRIAVDTSDEPLAALAAELPASAPDLIKPNGEELGQLAGLPAERAMALEEGAVQGDYGPVVDAARLLVGLGLGAVMVTLGPAGAVLVTADGAWHATAPEVPVVSTVGAGDSSVAGYILADVNGGDEAERLRTAMAYGSAAASLPGTTLPTPADLPEQAAVVTRLS$","1-phosphofructokinase","Cytoplasm, Extracellular","1-phosphofructokinase","1-phosphofructokinase ","PfkB domain protein","","Wu L.F., Reizer A., Reizer J., Cai B., Tomich J.M., Saier Jr M.H. Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli. J. Bacteriol. 1991. 173(10):3117-3127. PMID: 1850730Orchard L.M., Kornberg H.L. Sequence similarities between the gene specifying 1-phosphofructokinase (fruK), genes specifying other kinases in Escherichia coli K12, and lacC of Staphylococcus aureus. Proc. R. Soc. Lond., B, Biol. Sci. 1990. 242(1304):87-90. PMID: 1981619Blatch G.L., Scholle R.R., Woods D.R. Nucleotide sequence and analysis of the Vibrio alginolyticus sucrose uptake-encoding region. Gene 1990. 95(1):17-23. PMID: 2174811","","","

InterPro
IPR002173
Family

Carbohydrate kinase, PfkB
PS00584	$\"[275-288]?$	PFKB_KINASES_2

InterPro
IPR011611
Domain

PfkB
PF00294	$\"[144-324]T$	PfkB

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[3-322]T$	no description
PTHR10584	$\"[6-326]T$	SUGAR KINASE RELATED
PTHR10584:SF37	$\"[6-326]T$	PHOSPHOFRUCTOKINASE(PFK1)

","BeTs to 10 clades of COG1105COG name: Fructose-1-phosphate kinase and related fructose-6-phosphate kinase (PfkB)Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1105 is --------vdrlb-efgh------twNumber of proteins in this genome belonging to this COG is 1","***** IPB002173 (Carbohydrate kinase, PfkB) with a combined E-value of 3.3e-10. IPB002173A 36-51 IPB002173B 274-287***** IPB002139 (Ribokinase signature) with a combined E-value of 8.7e-07. IPB002139B 32-51 IPB002139E 246-257","","","-41% similar to PDB:2ABQ Crystal structure of fructose-1-phosphate kinase from Bacillus halodurans (E_value = 3.5E_19);-40% similar to PDB:2AWD Crystal structure of LacC from Enterococcus faecalis (E_value = 4.1E_12);-40% similar to PDB:2F02 Crystal Structure of LacC from Enterococcus Faecalis in complex with ATP (E_value = 4.1E_12);-40% similar to PDB:2JG5 CRYSTAL STRUCTURE OF A PUTATIVE PHOSPHOFRUCTOKINASE FROM STAPHYLOCOCCUS AUREUS (E_value = 4.1E_12);","Residues 5 to 324 (E_value = 2.2e-18) place ANA_2656 in the PfkB family which is described as pfkB family carbohydrate kinase.","","(PfkB) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2657","2860225","2860383","159","11.70","4.84","5526","GTGAGCCCGCGGCCCCTCGCACGCGCCGGCGGCTGCCGGCTGCCGCTACCGACCGCCGAACCGGCTCCGCCACTGACCGCCCACCAACTGTCCGCCACCCGCCCACCGACCCACCGCATGACCACCACCGACCGCATGACCGCCGCCCACCACCCTTGA","VSPRPLARAGGCRLPLPTAEPAPPLTAHQLSATRPPTHRMTTTDRMTAAHHP$","Hypothetical protein","Extracellular, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2658","2860442","2862613","2172","4.94","-22.64","73109","ATGACCGAGAACAAGCCCCTCATCATCCCCGAGCTGGTCGCGCTCGACGCCGACGCCGGCCCGGGCAAGGAAGACGTCATCGAGTTCCTGGCCGCCACCGTGGCCGGCGCCGGCCGGGCCTCCAGCCCCGACGGCCTGGCCGCCGACGCCAAGAAGCGCGAGTCCACCGCCCCCACCGGGATCCCCGGCGGCATCGCCATCCCGCACTGCCGCAGCCCCCACGTCCTGGCCCCCAGCCTCGGCTTCGCCCGCCTGGCGCAGCCGGTCGACTTCGGGGCCGCCGACGGACAGGCCGCCGACCTCATCTTCATGATCGCCGCCCCCGACGGCGCCGACGACTTCCACCTCCAGCTCCTGGCCAAGCTCGCCCGCGGACTCATGCAGACCGAGTTCACCGACGCCCTGCGCCAGGCCGCCGACGCCGAGGAGATCACCCGGATCGTCACGCAGCAGGTCCAGCCCGAGCTGCTCGACGGCGGGGAGGGGGCCGAGGACAGCGCGGCCAGTGAGGCCGGTGAGGCCGGAAGTGCCGCGGACTCGGCCGCAGGGTCCGGTGCCGCGCAGACCAAGGCCGCTGCGGCGTCGTCGGCCCCGGCGGAGGGCGAGACCGTCATCGTAGGGGTCTCCTCCTGCCCCACCGGTATCGCCCACACCTTCATGGCCGCCGAGGCCCTGGAGCAGGCCGGCAAGGACCGCGGCATCACCGTGGCCATCGAGGGCCAGGGCTCGGGCAAGATCGACGCCCTCGACCCCGAGCTCATCAAGCGGGCCAGCGCCGTCATTTTCGCCCACGACCTGCCGGTCAAGGGCCGCGAGCGCTTCGCCGGCAAGCCCGTCATCGACGTCGGCGTTAAGGCCGCCGTCAACGACGCCGGCTCCCTGGTGGACAAGGCTCTGGCCGCCGTTGATGACCCGAGCGCCTCCCGTGTGCCGGCCGGCGGCGAGTCCGCCGAGGAGAGCGAGGAAGGTTCTGAGCACTGGGCCCGGCGCCTCCAGAGGTCCGTCATGACCGGGGTGTCCTACATGATCCCCTTCGTGGCCGCCGGCGGTCTGCTCATTGCGCTGGGCTTCCTCCTGGCCGGGTACGACGTGGCCAACCTCTACGAGAAGATCTCCATCAGCGACTACTCCCTGTGGAACCTGCCCGGCAACGAGTTCGTTCATGAGATCAAGAACTCGGCCGGCGACGTCATCGGCACTGAGACGATCAACGTCTCGCAGTCCGGGCTGCTGCTGTACATCGGGTGGACGCTGTTCCTGCTGGGGCAGGCGGCCATGAGCTTCCTCGTCCCGGCGCTGGCCGGCTACATCTCCTTCGGGCTGGCCGGCAGGCCCGGGATCGCGCCCGGATTCGTCATGGGGGTCGTCGCGGTCGAGGTCGGTGCCGGGTTCATCGGCGGCCTGGTCGGCGGCATCCTCGCGGGCTACTTCGCGGCCTGGCTCGCCGGGCTCAGCGTGCCGGCCTGGCTGCGAGGGCTCATGCCCGTGGTCATCATCCCGTTGGGTACCACGCTCGTGGTCGGCGCCGTCATGTACATGGTCCTCGGGCTGCCGCTGGCCGCCCTCATGACCTCGCTGCAGGACGGGCTGACCTCCATGTCCGGGGGAGGGTCGGCCGTGCTGCTCGGCGTCATCCTCGGGCTCATGATGTGCTTCGACCTGGGCGGGCCGGTCAACAAGGCCGCCTACCTGTTCGGCACCGCGGGACTGTCCGCGGCCAGCGCCAGCAACACTGCTCCCTACGAGATCATGGCCACCGTCATGGCCGCAGGCATGGTGCCGCCGCTGGCGATGTCCGCCGCGACCTTCCTGCGCTCGCGGCTGTTCACCAAGGCCGAGGTCGAGAACGGGCGCAGCGCCTGGCTGCTGGGACTGTCCTTCATCTCCGAGGGCGCCATCCCCTTCGCCGCCGCCGACCCGCTGCGCGTCATCCCGGCCACGATGGCCGGCGGCGCGGTCACCGGCGCGATGACCATGGCGATGCACGTCGGCTCGCGCGCGCCCCACGGTGGCGTGTTCGTCGCCTTCGCCATCACCCACTTCGGTGGCTTCCTCCTGGCGATCCTGGCCGGGACGGTGGTGAGCACCGCGCTGGTCATCGTCCTCAAGGGGCTGGGGCGCAACGCCGACGGCAAGAAGGGTGTTGAGGCGCAGGCCACGGCTGCTGCTTGA","MTENKPLIIPELVALDADAGPGKEDVIEFLAATVAGAGRASSPDGLAADAKKRESTAPTGIPGGIAIPHCRSPHVLAPSLGFARLAQPVDFGAADGQAADLIFMIAAPDGADDFHLQLLAKLARGLMQTEFTDALRQAADAEEITRIVTQQVQPELLDGGEGAEDSAASEAGEAGSAADSAAGSGAAQTKAAAASSAPAEGETVIVGVSSCPTGIAHTFMAAEALEQAGKDRGITVAIEGQGSGKIDALDPELIKRASAVIFAHDLPVKGRERFAGKPVIDVGVKAAVNDAGSLVDKALAAVDDPSASRVPAGGESAEESEEGSEHWARRLQRSVMTGVSYMIPFVAAGGLLIALGFLLAGYDVANLYEKISISDYSLWNLPGNEFVHEIKNSAGDVIGTETINVSQSGLLLYIGWTLFLLGQAAMSFLVPALAGYISFGLAGRPGIAPGFVMGVVAVEVGAGFIGGLVGGILAGYFAAWLAGLSVPAWLRGLMPVVIIPLGTTLVVGAVMYMVLGLPLAALMTSLQDGLTSMSGGGSAVLLGVILGLMMCFDLGGPVNKAAYLFGTAGLSAASASNTAPYEIMATVMAAGMVPPLAMSAATFLRSRLFTKAEVENGRSAWLLGLSFISEGAIPFAAADPLRVIPATMAGGAVTGAMTMAMHVGSRAPHGGVFVAFAITHFGGFLLAILAGTVVSTALVIVLKGLGRNADGKKGVEAQATAAA$","Phosphotransferase system, fructose-specific IIC component","Membrane, Cytoplasm","Phosphotransferase system, fructose-specific IICcomponent","phosphotransferase system; fructose-specific","PTS system, fructose subfamily, IIC subunit","","Saier Jr M.H., Reizer J. Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 1992. 174(5):1433-1438. PMID: 1537788","","","

InterPro
IPR002178
Domain

Phosphotransferase system, phosphoenolpyruvate-dependent sugar EIIA 2
PD001689	$\"[8-142]T$	Q6ABG6_PROAC_Q6ABG6;
G3DSA:3.40.930.10	$\"[7-158]T$	no description
PF00359	$\"[7-151]T$	PTS_EIIA_2
PS51094	$\"[6-151]T$	PTS_EIIA_TYPE_2

InterPro
IPR003352
Domain

Phosphotransferase system, EIIC
PF02378	$\"[336-650]T$	PTS_EIIC

InterPro
IPR003353
Domain

Phosphotransferase system, fructose-specific IIB subunit
PF02379	$\"[204-304]T$	PTS_IIB_fruc
TIGR00829	$\"[206-289]T$	FRU: PTS system, Fru family, IIB component

InterPro
IPR004715
Domain

Phosphotransferase system, IIA component fructose subfamily
TIGR00848	$\"[7-135]T$	fruA: PTS system, fructose subfamily, IIA c

InterPro
IPR006327
Domain

Phosphotransferase system, fructose IIC component
TIGR01427	$\"[317-703]T$	PTS_IIC_fructo: PTS system, Fru family, IIC

InterPro
IPR013011
Domain

Phosphotransferase system, EIIB component, type 2
PS51099	$\"[203-300]T$	PTS_EIIB_TYPE_2

InterPro
IPR013014
Domain

Phosphotransferase system, EIIC component, type 2
PS51104	$\"[331-712]T$	PTS_EIIC_TYPE_2

noIPR
unintegrated

unintegrated
PTHR22931	$\"[3-129]T$	PHOSPHOENOLPYRUVATE DIKINASE-RELATED
PTHR22931:SF10	$\"[3-129]T$	PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE
tmhmm	$\"[341-361]?$ $\"[410-444]?$ $\"[450-484]?$ $\"[496-516]?$ $\"[530-550]?$ $\"[560-580]?$ $\"[586-604]?$ $\"[619-637]?$ $\"[643-663]?$ $\"[673-702]?$	transmembrane_regions

","BeTs to 8 clades of COG1299COG name: Phosphotransferase system, fructose-specific IIC componentFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1299 is ---------d-lb-efgh------twNumber of proteins in this genome belonging to this COG is 1","***** IPB003353 (Phosphotransferase system PTS, fructose-specific IIB subunit) with a combined E-value of 4.2e-20. IPB003353 205-254***** IPB002178 (Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2) with a combined E-value of 4.5e-06. IPB002178 53-70","","","-56% similar to PDB:2A0J Crystal Structure of Nitrogen Regulatory Protein IIA-Ntr from Neisseria meningitidis (E_value = 1.2E_12);","Residues 7 to 151 (E_value = 2.2e-13) place ANA_2658 in the PTS_EIIA_2 family which is described as Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2.Residues 204 to 304 (E_value = 2.3e-34) place ANA_2658 in the PTS_IIB_fruc family which is described as PTS system, Fructose specific IIB subunit.Residues 336 to 650 (E_value = 1.2e-13) place ANA_2658 in the PTS_EIIC family which is described as Phosphotransferase system, EIIC.","","system, fructose-specific IIC component (PTS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2659","2862677","2863567","891","8.89","7.21","30751","GTGTGTGAGGACCTCGGGAGCCGGGTCCGTGAGGCTCGGTGTCCTTCGGCGGGGACGCTTCACGCGGCCGGGGACACACCCCTCCCGCCGGGGACATCCCGCGCGCACGGGGACACTCCGCTCCGACCGGGAACACTCCGCGCGTGCGGGGACAGGATTCCTGTCCCCGGCGGCGTCGAATGCCCCCGGCCGGGACGGCACGCACCCCGCCGCGCAGGATGCCCCCGGCTGCGCGGAACGTCCCTGTGGACTGTGTCGCCCCAGATCGAGGACGTACCTTTCGATCGAGGACTGCGTTCTCCTACAGAAGGTGACGGCCCGGGCGCAGTCGTTTGGGGGAGAAGTACGTCCTGGGCGCAGAACGCAGTCCCCGATGGGCCGGGCCTGGCGCGAGGCGCTGTCGGGCTGGGCTCGCCTGCCAGTTCCGGGCTGCTCCGGCATAGGCTTCGCGCCATGGCTGCAAGACGACGCATCGACCCCGACGCCGGCGCCCAGGCCCTGCGCCAGTGGGCCCAGGAGCAGGGCCCGTCCGACGACGAACCGGCCGGAGCCGGGAGCGGTGCCGACTCCGCCAGTCCCACCGACCGGGCCGCCCGACGTCGGGTGACCGCCACCGCCGTGCGCTACACCCTCGAGGAGCTCGCCGCCTGCGCGCCCGGGCGCTCGGTCGAGGTGCGGGTCCCGCCCTTCGGTGTCACCCAGGCCGTCGCCGGCACTGTCCACCGCCGGGGCACCCCGCCCAGCGTCGTCGAGACCGACGCCGCCACCTGGCTGGCCCTGGCCACCGGCCGGCTCACCTGGCAGGACGCCCTGGCCGACGGCGCCCTGCACGCCTCCGGTGAGCGCTGCGACCTGTCCGCCTACCTGCCTCTGGTCCGGCTCCCCGGGTAG","VCEDLGSRVREARCPSAGTLHAAGDTPLPPGTSRAHGDTPLRPGTLRACGDRIPVPGGVECPRPGRHAPRRAGCPRLRGTSLWTVSPQIEDVPFDRGLRSPTEGDGPGAVVWGRSTSWAQNAVPDGPGLARGAVGLGSPASSGLLRHRLRAMAARRRIDPDAGAQALRQWAQEQGPSDDEPAGAGSGADSASPTDRAARRRVTATAVRYTLEELAACAPGRSVEVRVPPFGVTQAVAGTVHRRGTPPSVVETDAATWLALATGRLTWQDALADGALHASGERCDLSAYLPLVRLPG$","Hypothetical protein","Cytoplasm, Extracellular","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2660","2864032","2865693","1662","5.01","-23.42","58516","ATGAGTCGCACGCGCCTGAGTACCTATACCGCCCCGCCCGCCGAGGTCGCCCGGACCTTGGACGCGTTGCGCGCGCATTACGAGGTGCCTGCCGCTTTCCCGCCCGAGGCCCTCGCCGAGGCGGAGGCCGCTGCCGGCGCCTGGGCCCAGGACGGCCCCGCCCGTCTTCTGGCCGACGGCGCCCGCGACGCCCGCGACCTGGAGCTGGTCACCATTGACCCGCCCGGCTCCATGGACCTCGATCAGGCGGTGCTCCTGGAGCGCCTGCCTACGCAGGCCGGTGTGGGGACCGGGGACGCCCCCGAGCCGTCGGCCGCCTACCGAGTCCACTACGCCATTGCCTCCCTGGCCACCTTCGTCACTCCCGGCGGCGCCCTGGACACCGAGCTGCGCCGCCGCGGCGAGACCATCTACGCCCCCGACGCCGCCACGCCCCTGCACCCGGAGGTCCTCTCCCACGGCGCCGCCTCCCTGCTTCAGGACGCCGAGCGCCCGGCCTGCCTGTGGACCATCGACCTCGACGAGCGCGGTGAGGTCGTCTCCGCCCGCGTCGAGCGGGCCCTCGTGCGCTCGCGGGCGCGCCTTAGCTACGCCCAGGTCCAGGCCGCCATTGACGGGGAGGACGCCCTGCCCCAGGAGGTGCCGGCCGACCTGCCCGAGCTTCTGGCCGAGATCGGCCGTCTGCGTCTGGAGCGGGAGGCCGCCCGCGGCGGTATCAGCATGACCACGCCCGAGCAGGTCGTCGAGGTGACCGAGGCGGCACACGCGGCAGAGGCAACACAGGCGGCGGAGCCGGCGTCGCCGTCGGGTGACGCCGAGTCCGCCGAGCCCGCCAAGAGCGCCAGCCCGGCCGGCTACCGGCTCGCCTACCGCGTGCCCGTGCCCGCCGAGCAGTACAACGCCCAGATCTCCTTGCTCACCGGCATGTGCGCCGCCCGGATCATGGTTGAGTGCGGCATCGGCATCCTGCGGACCCTGCCGCCGGCGCGCCCCGAGGACTACGCCCGCCTGCGGCGCGTCGCCGCGGCCCTGGGCATCGACTGGCCGGCTGCCCAGCCCTACCCCGAGCTCGTGCGCGGCCTGGACCACGCCATCCCCTCCCACGCGGCCTTCATGGAGCAGGCCATGTCCCTCTTCCGTGGATCGGGCTACCTCGCCTTCGGGGTGGGCGGCGTCGGTGTCCCGGCCGACGACGAGGCCGCCGACTCCGAGGAGGCCGTCCACTCCGCGATCGCCGCCCGCTACGCCCACGTCACCGCGCCGCTGCGCCGACTCGTCGACCGCTACGGCGAGGAGGTCTGCATCGCCGCCTGCGCCCAGGCGCCCGTGCCCGAGTGGGTCCTCCAGACGCTGCCCGACCTGCCCGGCGTCATGGAGCAGACCGGCAAGCGCGCCCGCGCCATCGGCCGCGGGGCCCTGACCGCCCTGGAGGCCCTGGTCCTGCGCGGACACGAGGGCGAGGTCTTCGACGGCGTCATCACCTCCGAGCGCGACGGCCGCGGCGAGCTCGTCCTGGCCGAGCCCGCCGTCGTCACCGAGATCCGCGCCGGCAAGAAGGCCTTAGACGGCGGCCTCCCAGTGGGTGAGCGCGTGCGGGTCCGCCTCCTGTCCGCCGACCCCACCTCCGGCATCCGCTTCCAGCTCCTGACGCACCAGCCCTGA","MSRTRLSTYTAPPAEVARTLDALRAHYEVPAAFPPEALAEAEAAAGAWAQDGPARLLADGARDARDLELVTIDPPGSMDLDQAVLLERLPTQAGVGTGDAPEPSAAYRVHYAIASLATFVTPGGALDTELRRRGETIYAPDAATPLHPEVLSHGAASLLQDAERPACLWTIDLDERGEVVSARVERALVRSRARLSYAQVQAAIDGEDALPQEVPADLPELLAEIGRLRLEREAARGGISMTTPEQVVEVTEAAHAAEATQAAEPASPSGDAESAEPAKSASPAGYRLAYRVPVPAEQYNAQISLLTGMCAARIMVECGIGILRTLPPARPEDYARLRRVAAALGIDWPAAQPYPELVRGLDHAIPSHAAFMEQAMSLFRGSGYLAFGVGGVGVPADDEAADSEEAVHSAIAARYAHVTAPLRRLVDRYGEEVCIAACAQAPVPEWVLQTLPDLPGVMEQTGKRARAIGRGALTALEALVLRGHEGEVFDGVITSERDGRGELVLAEPAVVTEIRAGKKALDGGLPVGERVRVRLLSADPTSGIRFQLLTHQP$","Ribonuclease II","Cytoplasm","Exoribonucleases","ribonuclease II","ribonuclease II","","Cheng Z.F., Deutscher M.P. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J. Biol. Chem. 2002. 277(24):21624-21629. PMID: 11948193Kishine M., Takabayashi A., Munekage Y., Shikanai T., Endo T., Sato F. Ribosomal RNA processing and an RNase R family member in chloroplasts of Arabidopsis. Plant Mol. Biol. 2004. 55(4):595-606. PMID: 15604703Dziembowski A., Malewicz M., Minczuk M., Golik P., Dmochowska A., Stepien P.P. The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondrial degradosome in processing and turnover of RNA. Mol. Gen. Genet. 1998. 260(1):108-114. PMID: 9829834Mian I.S. Comparative sequence analysis of ribonucleases HII, III, II PH and D. Nucleic Acids Res. 1997. 25(16):3187-3195. PMID: 9241229","","","

InterPro
IPR001900
Domain

Ribonuclease II and R
PF00773	$\"[61-347]T$	RNB

noIPR
unintegrated

unintegrated
PTHR23355	$\"[62-90]T$ $\"[107-252]T$	RIBONUCLEASE

","BeTs to 18 clades of COG0557COG name: ExoribonucleasesFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG0557 is -o----yqvd-lbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB001900 (Ribonuclease II) with a combined E-value of 2.5e-29. IPB001900A 61-85 IPB001900B 126-179 IPB001900D 407-434***** IPB013668 (Ribonuclease R winged-helix domain) with a combined E-value of 8.4e-10. IPB013668C 60-89 IPB013668D 140-194","","","No significant hits to the PDB database (E-value < E-10).","Residues 61 to 440 (E_value = 1.8e-34) place ANA_2660 in the RNB family which is described as RNB domain.","","(PA4937) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2661","2866225","2865707","519","6.19","-3.42","18426","ATGAGCCAGACAACGGAGGACCGCCTGATCCAGGCAGGGCGGCAGCTGCTCGAAGACGACGGCATCAGCGCGGTGACGGTGCGGGAGGTGGCTCGGCGCTGCGGCGTCTCTCACGGAGCACCGAGACGCCACTTCCCCACCCTCGCGCTGCTACTGGCCGCGATCGCCGAGGTGTGCCTCGGAGAGCTCCGCGAGCGCATCGCCGACGCCGGAGGAAGCCTCAAGGGGACCGCGAGGGCCTACGTCGCCTACGCCGTCGAGCACCCCCACGCCTTCGACCTCATCACCCGTCACGACGTGCTGGCCGGCAGCGGACGGGAGCTTCGGGCCACGTCCCTGCCGCTCCTTCAGCAGTGGCAGACCCGCTTCGCGGAGCAGCACCCGGACGCTCCCAACGCCGCCGCGACCGCCGCCTGGGCGGCCATCCACGGCGTTGCCTCACTCGCCTCACGGGGCGTGCTGGACCTGGTCGGAACCGATGCCCAGGAGCTGCTGGATCAGATTCTCCCGCAGGACTGA","MSQTTEDRLIQAGRQLLEDDGISAVTVREVARRCGVSHGAPRRHFPTLALLLAAIAEVCLGELRERIADAGGSLKGTARAYVAYAVEHPHAFDLITRHDVLAGSGRELRATSLPLLQQWQTRFAEQHPDAPNAAATAAWAAIHGVASLASRGVLDLVGTDAQELLDQILPQD$","TetR-family transcriptional regulator","Cytoplasm","transcriptional regulator","TetR-family transcriptional regulator","regulatory protein, TetR","","Mannervik M. Target genes of homeodomain proteins. Bioessays 1999. 21(4):267-270. PMID: 10377888Hosoda K., Imamura A., Katoh E., Hatta T., Tachiki M., Yamada H., Mizuno T., Yamazaki T. Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators. Plant Cell 2002. 14(9):2015-2029. PMID: 12215502Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 1998. 6(8):1057-1065. PMID: 9739097Kisker C., Hinrichs W., Tovar K., Hillen W., Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. J. Mol. Biol. 1995. 247(2):260-280. PMID: 7707374","","","

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PF00440	$\"[9-55]T$	TetR_N
PS50977	$\"[3-63]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[2-66]T$	no description

InterPro
IPR000620
Domain

Protein of unknown function DUF6, transmembrane
PF00892	$\"[156-282]T$	DUF6

noIPR
unintegrated

unintegrated
signalp	$\"[1-78]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[33-55]?$ $\"[61-81]?$ $\"[91-111]?$ $\"[117-135]?$ $\"[150-170]?$ $\"[176-196]?$ $\"[206-228]?$ $\"[238-258]?$	transmembrane_regions

","BeTs to 5 clades of COG0697COG name: Predicted permeasesFunctional Class: RThe phylogenetic pattern of COG0697 is A-tKYQVCEB-Huj---lINxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 212 to 338 (E_value = 9e-08) place ANA_2662 in the DUF6 family which is described as Integral membrane protein DUF6.","","membrane protein (AL132674)","","1","","","Thu Aug 9 16:01:23 2007","","Thu Aug 9 16:01:23 2007","","","Thu Aug 9 16:01:23 2007","Thu Aug 9 16:01:23 2007","Thu Aug 9 16:01:23 2007","Tue Aug 14 17:30:39 2007","","","","","Thu Aug 9 16:01:23 2007","","","","Thu Aug 9 16:01:23 2007","Thu Aug 9 16:01:23 2007","","","","","yes","","" "ANA_2663","2867199","2869070","1872","5.23","-18.20","65597","GTGCGTGTGCGCACCGGTGAGAACCCCTCGCAGATCACCTCCGACCATCCCGACGGCGCCCGCCTCACACCGCGGGCCGACTCCTCCGAGCCCCTGGGGCGGACCAGCCTTCCGAGCCCGCCCGACCCGGCGGCCCCTGAGGCTCCCGGGGCTCCTGCGGCTCCCGCAGTGCCCGAGGTGCCCGCCGGCGTCCCCGGACTGACCGCCCTGCCTGACGACCACGCCGACGAGCTCGAGCCCTCGCCGCGTGAGGAGTGCGGTGTCTTCGGCGTCTGGGCTCCCGGCGAGGAGGTCTCCCGCCTAACCTACTTCGGCCTGTACGCCCTCCAGCACCGCGGCCAGGAGTCCGCCGGCATCGCCACCTCCAACGGCTCCCAGATCCTCGTCTACAAGGACCTCGGCCTGGTCTCCCAGGTCTTCGACGACCAGGCCCTGTCCAACCTCACCGGCCACATCGCCGTCGGCCACGTCCGCTACGCCACCCAGGGCGCCACCACCTGGGAGAACGCCCAGCCGATGCTCGGCCCGGCGGCCGGCTCCACCCTCGCCCTGGCCCACAACGGCAACCTCACCAACACCCGTGAGCTCATGGACGCCGTGCACGCCACCTCCGGGGAGGACCTCAGCGGCGAGCTCGGCCGCGGCTCCTCCACCGACACCGCCGTCCTGGCCGCCCTGCTCAACCTCGTCTCCGAGCACGGCGCCCTGGAGGGCTGGGACTCGGCCGCCGACATCCTCACCTCCGGCATCACCGACGACGCCGAGCTCGACGCCGCCTACAGTGCACCGGCCCCCCTGAGCGTCCACCAGGCCGCCCGCCGGGTTCTGCCCATGCTGCGCGGCGCCTTCTCCCTGGTCTTCATGGACGAGCGCACCCTCTACGCCGCCCGCGACCCCCACGGGGTGCGCCCCCTGGTGCTGGGGCGCCTGGGCAACGGGTGGGCCGTGGCCTCTGAGACCGCCGCCCTGGACATCGTCGGCGCCACTTTTGTGCGCGAGATCGAGCCCGGCGAGCTCATCGAGATCGACGAGGACGGCGTGCGCTCCACCCGCTTCGCCACCGCCCGCCGGGCCGGCTGCGTCTTCGAGTACGTCTACCTGGCCCGCCCCGACACCCGCATCGCCGGGCGCAGCGTCATCACCTCACGCAACGAGATGGGCGCGGCCCTGGCTCGCGAGCACCCGGTGGAAGCCGACCTCGTCATCGCCACGCCGGAGTCGGGCACCCCGGCCGCCATCGGCTACGCCCAGGCCTCCGGCATCCCCTACGGGCAGGGCCTGGTGAAGAACGCCTACGTGGGGCGCACCTTCATCCAGCCCACCCAGACCCTGCGCCAGCTCGGCATCCGCCTCAAGCTCAACCCCCTGCGCGAGGTCATCGAGGGCAAGCGCCTCGTCGTCGTCGACGACTCCATCGTGCGCGGCAACACCCAGCGGGCCCTGGTGCGGATGCTGCGCGAGGCCGGCGCCGCCGAGGTTCACGTGCGCATCTCCTCCCCGCCGGTCATGTGGCCCTGCTTCTACGGCATCGACTTCGCCACCCGCGCCGAGCTCATCGCCACCGGCATGAGCGTGGAGGAGATCGGTCAGTCCATCGGCGCCGACTCCCTGGGCTTCCTGTCCGTCGAGGGCATGGTGGCCGCCAGCGGCCAGAAGGCCGACGAGCTGTGCCTGGCCTGCTTCACCGGCGACTACCCGATCCCGCCGCCCGTGCGCAGCTTGACGGGCGCCGCCATCCCGGTGCGCCGTGTCCCCACCGCCTACCGCGGTCGGCGCCGCGATCAGGCCGACGACGCCGGCCGCACCGTGCCGCCGGGCAGCATCACCCGGCCGGACCTGGCCTCCGGCAGCCCCCTGGGATCGACGACCTAA","VRVRTGENPSQITSDHPDGARLTPRADSSEPLGRTSLPSPPDPAAPEAPGAPAAPAVPEVPAGVPGLTALPDDHADELEPSPREECGVFGVWAPGEEVSRLTYFGLYALQHRGQESAGIATSNGSQILVYKDLGLVSQVFDDQALSNLTGHIAVGHVRYATQGATTWENAQPMLGPAAGSTLALAHNGNLTNTRELMDAVHATSGEDLSGELGRGSSTDTAVLAALLNLVSEHGALEGWDSAADILTSGITDDAELDAAYSAPAPLSVHQAARRVLPMLRGAFSLVFMDERTLYAARDPHGVRPLVLGRLGNGWAVASETAALDIVGATFVREIEPGELIEIDEDGVRSTRFATARRAGCVFEYVYLARPDTRIAGRSVITSRNEMGAALAREHPVEADLVIATPESGTPAAIGYAQASGIPYGQGLVKNAYVGRTFIQPTQTLRQLGIRLKLNPLREVIEGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHVRISSPPVMWPCFYGIDFATRAELIATGMSVEEIGQSIGADSLGFLSVEGMVAASGQKADELCLACFTGDYPIPPPVRSLTGAAIPVRRVPTAYRGRRRDQADDAGRTVPPGSITRPDLASGSPLGSTT$","Amidophosphoribosyltransferase","Cytoplasm","glutamine phosphoribosylpyrophosphateamidotransferase","amidophosphoribosyltransferase ","amidophosphoribosyltransferase","","Hershey H.V., Taylor M.W. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene 1986. 43(3):287-293. PMID: 3527873","","","

InterPro
IPR000583
Domain

Glutamine amidotransferase, class-II
PF00310	$\"[86-320]T$	GATase_2

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[375-510]T$	Pribosyltran

InterPro
IPR002375
Family

Purine/pyrimidine phosphoribosyl transferase
PS00103	$\"[465-477]T$	PUR_PYR_PR_TRANSFER

InterPro
IPR005854
Family

Amidophosphoribosyl transferase
PTHR11907	$\"[52-246]T$ $\"[270-617]T$	AMIDOPHOSPHORIBOSYLTRANSFERASE
TIGR01134	$\"[86-566]T$	purF: amidophosphoribosyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.60.20.10	$\"[86-429]T$	no description

","BeTs to 20 clades of COG0034COG name: Glutamine phosphoribosylpyrophosphate amidotransferaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0034 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB000583 (Glutamine amidotransferase, class-II) with a combined E-value of 6.8e-08. IPB000583B 106-119 IPB000583C 153-172***** IPB001962 (Asparagine synthase) with a combined E-value of 1.6e-07. IPB001962D 277-306 IPB001962E 311-323","","","-66% similar to PDB:1AO0 GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE FROM B. SUBTILIS COMPLEXED WITH ADP AND GMP (E_value = 7.8E_122);-66% similar to PDB:1GPH STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS (E_value = 1.7E_121);-54% similar to PDB:1ECB ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 GMP, 1 MG PER SUBUNIT (E_value = 8.2E_71);-54% similar to PDB:1ECC ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH MN-CPRPP AND 5-OXO-NORLEUCINE (E_value = 8.2E_71);-54% similar to PDB:1ECF ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE (E_value = 8.2E_71);","Residues 86 to 320 (E_value = 1.8e-30) place ANA_2663 in the GATase_2 family which is described as Glutamine amidotransferases class-II.Residues 375 to 510 (E_value = 2.8e-05) place ANA_2663 in the Pribosyltran family which is described as Phosphoribosyl transferase domain.","","phosphoribosylpyrophosphate amidotransferase (purF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2664","2869232","2870383","1152","4.78","-20.91","39348","ATGACCGAGCAGCCCGAGCAGCCTGAGCAGCCCGCCCCCGCCATCACCTACGCCGACGCCGGCGTGGACACCGCCGCCGGGGACCGGGCCGTCGCGCTCATGAAGGACGCCGTGGCCTCCACCATGACCCCGGCCGTCGTCGGTGGCGTCGGAGGCTTCGCCGGGCTCGTGGACGTCTCCACCCTGCGCGACTACCGCCGCCCCCTGCTGGCCACCTCCACCGACGGGGTGGGCACCAAGGTCGCCATCGCCCAGGCCCTCGACATCCACGACACCATCGGCCAGGACCTGGTGGGGATGGTCGTTGACGACATCGTCGTGGTCGGGGCCCGGCCCCTGCTCATGACCGACTACATCGCCTGCGGGCACGTCGTCCCCGAGCGGATCGCCGACATCGTGCGCGGCATCGCCCAGGCATGCGCCGCCATCGGCACCCCGCTGCTGGGCGGGGAGACCGCCGAGCACCCCGGCCTCATGGCCCCCGACGAGTACGACGTCGCCGGGGCCGCCACCGGCGTCGTCGAGGCCGACCGCATGCTCGGGGCTGAGAAGGTGCGCGCCGGCGACGTCCTGGTCGCTTTGGGTGCCTCCGGGCTGCACTCCAACGGCTACTCCCTGGTGCGCCGCGTCATCGAGCACGCCGGCTGGGGCCTGGAGCGCGAGGTCCCCGAGTTCGGCCGCACCCTGGGCCAGGAGCTGCTCGAGCCCACACGCCTGTACACCCGCGTGTGCCTGGCCATGCTGGAGACCCTCTCCTCGCCGGCCGCCCCGGGGCCGATCCACGCCCTGTCCCACATCACCGGTGGGGGGCTGGCCGCCAACGTCGCCCGGGTCCTGCCGGCCGGGCTCATCGCCGACGTCGCCCGCTCCTCCTGGACGGTGCCGCCGGTGTTCTCCACCGTGCGCGAGCTCGGCTCGGTGCCGTGGGAGGACCTCGAGGGCACCCTCAACCTGGGCGTGGGCATGGTCGCCGTTGTTGAGCCTGGTGTGGTCGACGCCGTCCTGCGGGTCGCCGAGGGCTCCGAGATCCCCGCCTGGGTGCTGGGCGAGGTGCACGACGCCGGGAAGTATGAGGCCCAGGGGCGGGTCGTCTCCGGCACGAAGGGCGTCGACGGGGGAGCGGTCGACATCCACGGCACCTACACCGCCTGA","MTEQPEQPEQPAPAITYADAGVDTAAGDRAVALMKDAVASTMTPAVVGGVGGFAGLVDVSTLRDYRRPLLATSTDGVGTKVAIAQALDIHDTIGQDLVGMVVDDIVVVGARPLLMTDYIACGHVVPERIADIVRGIAQACAAIGTPLLGGETAEHPGLMAPDEYDVAGAATGVVEADRMLGAEKVRAGDVLVALGASGLHSNGYSLVRRVIEHAGWGLEREVPEFGRTLGQELLEPTRLYTRVCLAMLETLSSPAAPGPIHALSHITGGGLAANVARVLPAGLIADVARSSWTVPPVFSTVRELGSVPWEDLEGTLNLGVGMVAVVEPGVVDAVLRVAEGSEIPAWVLGEVHDAGKYEAQGRVVSGTKGVDGGAVDIHGTYTA$","Phosphoribosylformylglycinamidine cyclo-ligase","Cytoplasm","phosphoribosylformylglycinamidine cyclo-ligase","phosphoribosylformylglycinamidine cyclo-ligase ","phosphoribosylformylglycinamidine cyclo-ligase","","","","","

InterPro
IPR000728
Domain

AIR synthase related protein
PF00586	$\"[13-175]T$	AIRS

InterPro
IPR004733
Domain

Phosphoribosylformylglycinamidine cyclo-ligase
TIGR00878	$\"[15-354]T$	purM: phosphoribosylformylglycinamidine cyc

InterPro
IPR010918
Domain

AIR synthase related protein, C-terminal
PF02769	$\"[186-362]T$	AIRS_C

noIPR
unintegrated

unintegrated
G3DSA:3.30.1330.10	$\"[9-180]T$	no description
G3DSA:3.90.650.10	$\"[181-363]T$	no description
PTHR10520	$\"[15-362]T$	PHOSPHORIBOSYLAMINE-GLYCINE LIGASE-RELATED

","BeTs to 20 clades of COG0150COG name: Phosphoribosylaminoimidazol (AIR) synthetaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0150 is aompk-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 1","***** IPB010918 (AIR synthase related protein, C-terminal) with a combined E-value of 7.4e-18. IPB010918A 68-94 IPB010918B 96-113 IPB010918C 198-208","","","-56% similar to PDB:2BTU CRYSTAL STRUCTURE OF PHOSPHORIBOSYLFORMYLGLYCINAMIDINE CYCLO-LIGASE FROM BACILLUS ANTHRACIS AT 2.3A RESOLUTION. (E_value = 8.5E_57);-52% similar to PDB:1CLI X-RAY CRYSTAL STRUCTURE OF AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE (PURM), FROM THE E. COLI PURINE BIOSYNTHETIC PATHWAY, AT 2.5 A RESOLUTION (E_value = 5.2E_54);","Residues 13 to 175 (E_value = 1.8e-54) place ANA_2664 in the AIRS family which is described as AIR synthase related protein, N-terminal domain.Residues 186 to 362 (E_value = 1.2e-35) place ANA_2664 in the AIRS_C family which is described as AIR synthase related protein, C-terminal domain.","","cyclo-ligase (purM)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2666","2870853","2870650","204","4.78","-5.06","7514","ATGGGGCGCGGCCGTCAGAAGGCCAAGGCAACCAAGGTTGCCCGTAAGCTCAAGTACTTCAGCCCGGAGACTGATTACAAGGCTCTGGAGCGGGAGCTCGTCTCAGCGTCCTCGGGATCTGAGCCTGACGACGAGATCGACTACGAGGAGCTGGCCGCCAAGTATGCCGTCGACGACGACGACTGGGACGAGGGCGGCAAGTAG","MGRGRQKAKATKVARKLKYFSPETDYKALERELVSASSGSEPDDEIDYEELAAKYAVDDDDWDEGGK$","Hypothetical protein","Periplasm, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2668","2871690","2872316","627","11.89","14.86","20631","GTGTCAGCGGCGGGCGAGGCGGGTCAGGACGATGCCGGCGGTCACCACGCCTCCGGTGACGGCGGCCGCCTTGGCGAGTTTGGAGGACGCCTCGGAGTCGCCCTGCTTGGCGCGCTCCCAGGTCTCCTCCGCCTGCTCGGCCCAGCGTCGGGCCCCCTCGCGCAGTCGGCCGGCGCCGGCCTCCGCCTGCTCGCGCAAACGGCCGGCCCCGGCCGCGGCCTGCTCTCGCAGGTGGTCGGCCTTGGCGCTCGCCTGCGAGAGCAGGTGCTCCCCGGCCTCCTTGGCCTGTGTGCGCGGGTCGATCCGGGAGGCGAACTCATCCACGCTCGCCGCCAGGGCCTCGCGCTGGGCACGCAGCCGTTCCTCGATCTGCTCGGGGCTCAGCGACCCGGACCCGGCGGCCCCGGCACCCTCAGTGCCGGAGGTGCCGGCCTGCTGTCCGCTGGTCATGCTCGACCCGCCCGGGCGCGGAAGGCCTTGACCGCGGCGACGGTCGCCGTCACGCTCAGGCCCGCCAGGGCGAGACCCGTAACCGTGACGATCCCCAGGGAGGCGGGGTCGCCGTCGCGGGCGTCGTCGAACAAGCGGGAGACACGCTGGCCGAGGGTCCGCGTGCTGGGATCGTAG","VSAAGEAGQDDAGGHHASGDGGRLGEFGGRLGVALLGALPGLLRLLGPASGPLAQSAGAGLRLLAQTAGPGRGLLSQVVGLGARLREQVLPGLLGLCARVDPGGELIHARRQGLALGTQPFLDLLGAQRPGPGGPGTLSAGGAGLLSAGHARPARARKALTAATVAVTLRPARARPVTVTIPREAGSPSRASSNKRETRWPRVRVLGS$","Hypothetical protein","Extracellular, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2669","2873097","2872609","489","10.43","7.16","16508","ATGCCCAACAACCAGCCACCTCCCCCGCCGTCGCAGGCGACGTCGTCGGCCTCCACCACGCCTCCTCGCAGGGCTGCCGGCAGCGCGCAGCCCACGCTCGGGGAGCTCATCGCCCGCATCTCGGAGAACATCTCCGCGCTGGTGCGCGGCGAGATCGACCTGGCCAAGGCCAAGGGCCAGCGCATGGCCAAGGAGATGGGGTTGGGGGCCGGGCTGCTCGCCGCCGCCGGGGTGCTGGCCCTGTTCATCTTCGGGCTGCTGCTGGGGGCCCTGACGACCGGGCTGTCCCACGTCATGCCGCTGTGGGCCGCCTTCCTCGTGGTCGCGCTGATCCTCACCCTCATCGCCGTGACGATGGCCCTCATCGGCATCAAGCGCCTCAAGGCCGCCAAGGCCGACACGCCGACGCCGCAGGAGGGGCTGAAGGAGTCCGTCAACGCCGTCAAGGGGGCCGTGACCTCCGGCCTGCAGAGGGGGAACGCCCAGTGA","MPNNQPPPPPSQATSSASTTPPRRAAGSAQPTLGELIARISENISALVRGEIDLAKAKGQRMAKEMGLGAGLLAAAGVLALFIFGLLLGALTTGLSHVMPLWAAFLVVALILTLIAVTMALIGIKRLKAAKADTPTPQEGLKESVNAVKGAVTSGLQRGNAQ$","Conserved hypothetical protein","Membrane, Periplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","protein of unknown function DUF1469","","","","","

InterPro
IPR009937
Family

Protein of unknown function DUF1469
PF07332	$\"[28-159]T$	DUF1469

noIPR
unintegrated

unintegrated
tmhmm	$\"[68-88]?$ $\"[102-124]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 28 to 159 (E_value = 3.2e-27) place ANA_2669 in the DUF1469 family which is described as Protein of unknown function (DUF1469).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2670","2875163","2873427","1737","5.87","-8.33","62245","ATGGCACTTCCCGTCGCGCCCGGGCCCGTCGCCCTGCGCAAGACCTTCCGCATCATGGCCTCCTACCGGGGGCGCTTCGCCGTCGTCCTGGCCCTCCAGATCACCGCGGTCCTGTCCACGCTCGTGGCCCCCCAGCTGCTGGGGCGGCTGGTCGGGCGGGTCTCGGCCGGGCGGGCCGACGCCGGCTACGTGGACCGGATCGTGCTGACCATCATCGCGGTCACGCTCGTGGGGGCGCTCATCAACCGCTTCGCCCAGAAGCACGCCCGCATCCTGGGCGAGTCGGTTTTCGCCGAGCTGCGCGAACGCATGATGAACCGGGTGGTGCACCTGCCGCTGAGCGCGGTGGAGTCCGCCGGCACCGGCGACCTCGTGGGGCGCACCACCACCGACGTCTCCCGCATCGAGTTCCTGGTGCGGGTGGGGATCCCCCAGATCCTCGTGTGCGTGGTGACGATCGTCTTCACCCTCCTGGCCGCCGCCGTCGCCGACCCCCTCCTGGCGCTCGGGCTGCTCGTCATCGCCCCACCCGTGTGGTCGATGATGCGCTGGTACCTGCCGATCTCCATCCCCGCCTACCGGGCCGAGTCGGCCGCCCAGGCCCGCCTCAACGGGGCGGTCTCCGAGACGGTCGAGCACGCCGAGACCGTGGACGCCCTGGGTATCGGGGCGCGCCGCGAGCGGGCCATCATGACCTCCATCAAGGAGGCCTGGTCCTTGGAGCGCTACACGGCGGCGCTGCGGGTGCGGCTGTTCATGGTGCTCGACATCGCCTGGCGGGCGCCCGTCGTCGCCGTCCTCCTGTGGGGAGGGTTCCTGGCCGGCCGCGGCTACGCGACCCTGGAGGCGATCACCACGGTCGCCCTGTACTCCATGGAGCTGCGCAAGCCGGTGGGCCAGCTCATGTTCTGGGTCGACCAGGTCCAGATCGCCCAGGCCTCCCTGTCCCGCATCCTGGGGGTGGAGGAGGTCCCCGACGACCGCACCCCCACCGGCCAGGAGCCCGAGGGCACGCGGATCGTGCTCGACGACGTGCGCTTCTCCTACCGGGAGGGCGTCGAGGTGCTCCACGGGATCGACCTGGAGCTCGTGCCCGGGGAGCGGCTGGCCGTCGTCGGGCCCTCGGGGTCGGGCAAGTCCACGCTGGGGCGGATGCTGGCGGGCATCAACCCGCCCACCTCCGGGAGCGTCACCGTGGGAGGGGTGTCGCTGACGGACCTGACCGAGGACGAGCTGCGCCGCCACGTGGCCCTGGTGACCCAGGAGCACCACGTGTTCGTCGGCACCGTGGCGGACAACGTGCGCCTGGGGCGGCCGGGCGCCTCCGATGACACGATCCGCGAGGCGATCGAGGCCATCGGGGCCGATGCCTGGGTGGACGGGCTGCCCGAGGGGATGGACACGATGGTCGGCTCGGGGCACCTCGAGCTGAGCCCCGCCCAGGCCCAGGAGGTGGCGCTGGCCCGGCTGGTGCTGCTGGACCCGCACACACTCATCCTGGACGAGGCCACCTCGCTGCTGGACCCGCGCGCCGCCCGCACCCTGGAGCGGACCCTGTCCACGGCGCTGGCCGGGCGCACCGTCATCGAGGTGGCCCACCGCCTCTACACGGCCGCCGACGCCGACCGGGTCGCCGTCGTCATGGACGGGCGGATCGTGGAGCTCGGCACCCACGACGAGCTGGTGGCCCTCGGCGGGGAGTACGCGCGCCTCTGGCAGGCCTGGAACCAGGAGTAG","MALPVAPGPVALRKTFRIMASYRGRFAVVLALQITAVLSTLVAPQLLGRLVGRVSAGRADAGYVDRIVLTIIAVTLVGALINRFAQKHARILGESVFAELRERMMNRVVHLPLSAVESAGTGDLVGRTTTDVSRIEFLVRVGIPQILVCVVTIVFTLLAAAVADPLLALGLLVIAPPVWSMMRWYLPISIPAYRAESAAQARLNGAVSETVEHAETVDALGIGARRERAIMTSIKEAWSLERYTAALRVRLFMVLDIAWRAPVVAVLLWGGFLAGRGYATLEAITTVALYSMELRKPVGQLMFWVDQVQIAQASLSRILGVEEVPDDRTPTGQEPEGTRIVLDDVRFSYREGVEVLHGIDLELVPGERLAVVGPSGSGKSTLGRMLAGINPPTSGSVTVGGVSLTDLTEDELRRHVALVTQEHHVFVGTVADNVRLGRPGASDDTIREAIEAIGADAWVDGLPEGMDTMVGSGHLELSPAQAQEVALARLVLLDPHTLILDEATSLLDPRAARTLERTLSTALAGRTVIEVAHRLYTAADADRVAVVMDGRIVELGTHDELVALGGEYARLWQAWNQE$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","ABC-transporter StrW","K06148 ATP-binding cassette; subfamily C; bacterial","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[26-298]T$	ABC_membrane

InterPro
IPR001412
Family

Aminoacyl-tRNA synthetase, class I
PS00178	$\"[391-402]?$	AA_TRNA_LIGASE_I

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[477-519]T$	O68081_RHOCA_O68081;
PF00005	$\"[366-550]T$	ABC_tran
PS50893	$\"[340-574]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[365-554]T$	AAA

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[27-309]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[303-576]T$	no description
PTHR19242	$\"[4-578]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF59	$\"[4-578]T$	ABC TRANSPORTER (HLYB/MSBA FAMILY)
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[26-48]?$ $\"[62-82]?$ $\"[143-163]?$	transmembrane_regions

","BeTs to 17 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 13","***** IPB005074 (Peptidase family C39, N-terminal leader) with a combined E-value of 5.8e-50. IPB005074A 104-139 IPB005074B 297-327 IPB005074C 355-402 IPB005074D 465-508 IPB005074E 527-547***** IPB013563 (Oligopeptide/dipeptide ABC transporter, C-terminal) with a combined E-value of 3.3e-20. IPB013563A 355-389 IPB013563C 474-501***** IPB010509 (ABC transporter, N-terminal) with a combined E-value of 1.5e-17. IPB010509B 366-391 IPB010509D 472-516***** IPB005116 (TOBE domain) with a combined E-value of 2.3e-11. IPB005116A 373-389 IPB005116C 477-490 IPB005116D 497-516","","","-44% similar to PDB:2HYD Multidrug ABC transporter SAV1866 (E_value = 3.5E_44);-44% similar to PDB:2ONJ Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP (E_value = 3.5E_44);-54% similar to PDB:2GHI Crystal Structure of Plasmodium yoelii Multidrug Resistance Protein 2 (E_value = 1.8E_32);-56% similar to PDB:1MV5 Crystal structure of LmrA ATP-binding domain (E_value = 4.0E_32);-54% similar to PDB:1MT0 ATP-binding domain of haemolysin B from Escherichia coli (E_value = 5.3E_32);","Residues 26 to 298 (E_value = 1.2e-10) place ANA_2670 in the ABC_membrane family which is described as ABC transporter transmembrane region.Residues 366 to 550 (E_value = 8e-50) place ANA_2670 in the ABC_tran family which is described as ABC transporter.","","StrW ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2671","2877100","2875163","1938","6.14","-4.42","67989","ATGCCCGAATCGTCCTCCCGGTCGTTCCCGACCGTCCCGACCGCGCTGTCCGCCCTGACTGCACAGTCAATGACCCCCGACGCCCCGCTGCCCCACCCCCCGTCCTTGGGTGCCGGGGCGCTTCTGCGCTGGCTGCTGCGCCGCGCCGCCGTCCCGGTCACCCTGGCGACCCTGGCGGCCTGCACCTCCAACATCATCCAGGCGATCGTGCCGGCCTTCCTGGGGCAGGCCCTGGACGCCGGCATCGAGAACGGTCTCAACGGCCGTGTCTGGGGCATTGGCGCGCTGCTGCTGGTGCTGTTCGTCGTCTACGCCGTCGGGGACACGATGATGTCCTACTTCGGGGTGACGGCCTGGATGCGCACCGCCTTCGACGTCGACCGGCTCGTGGGCCGGCAGATCTCCGCCACCGGCAAGGACCTGTCCCGGCAGGTCTCCACCGGTGAGGTCGCCACCATCATCGCCTCCGACGCCGACTACCTGGGCAAGTTCATCGAGCACCTGCCGGCCCTGCTGGGGGCGGCGGCCAGCTTCCTCGTCGTGGCCGTCCTCATGCTGCGCACCTCGGTGAGCCTGGGGCTCATCGTCATCCTGGGCATGCCGCTGGTGGCAGCCATCGTCACCCTGGTCATCCGCCCCCTGCAGAAGCGCCAGGCCGTCCAGCGCGAGGCCCAGTCCGCGGTCACCACGGTCACCACGGACACGGTGGCCGGCCTGCGGATCCTGCGGGGCATCGGCGGGGAGGACGTCTTCGCCCGCCGCTACCGGGACGCCTCCCAGGAGCTGCGGCGCCGCGGCGTCGAGGTGGCCTCCTCGCAGGCCACTCTCATGACCCTCCAGGTGCTGCTGCCCGGGCTCTTCGCCGCGATCGTCGTGTGGGTGGCGGCGCGCATGGCCGTGGCCGGCAGCCTCACCCCCGGCGGGCTCATCACCTTCTACGGCTACACCGCCTACCTGTCCTGGCCGCTGTGGGTGTTCACCAGCTGCGTGCAGGACTACACCCGGGCCGTCGTCGGCGCCCGGCGCCTGAGCCGCCTGCTGGAGGTGGCGCCGGCCGCCGGCAGCCTCGTGGAGCGCCTCAACCTGGACCCGGCCGCCGCCCACGCCGTCAGCGGCGACCTGGTGGACACCGGCAGCGGCCTGCGCCTGAAGGAGGGCCGTATGACGGCCCTCGTGTGCCCCGACCCGCAGGTCTCCGCCGACCTGGCCACGCGCCTGGGGCGCTTCACCGACGCCGGCCCCACCGTGACCCTGGCGGGCCGGCCACTGACCACCATGCCCCTGGAGCAGGTGCGCGCCAGCGTCGTCGTCTCCGGCGCCACCGCCCAGCTCTTCACCGGGACCCTGCGTGAGGCCCTCGACGTGCGCAGCGGCCCCGACCCGCAGCCGGCGGGACTGGAGGACCTCCTGCGCGCCGAGACCGAGCGCACCACCGGGGCCGACGTCGACCAGCAGGTCCGCCCCCAGGAGCGCGAAGCCCCCGGCGACGACCGGCTCATCGAGGCCGTCGGGATCGCCGACGCCGGTGATGTCCTGACCTCCCTGAGCGAGGGCCTGGCCGGGATGATTACCGAGAAGGGCCGGTCCCTGTCCGGTGGGCAGCGTCAGCGCGTGGCCCTGGCCCGGGCACTGCTGACCGAGGCACCCACGCTCGTGCTCATCGAACCGACCTCCGCCCTGGACTCCCACACCGAGGCCCGCGTGGCCGCCCAGGTACACCGGGCCCGCGCCGGGCGCACGACCGTCGTCGTCACCGCCTCGCCGCTGGTCCTGGAGGCCTGCGACGAGGTCGTCCTCCTGGACTCCAGCGGGGCCGAGCTGCTGCGCTCCACGCACCGCGAGCTCATGGCGATGGCCCGCGACGGCCACGCGCAGGCAGCCGACTACCGCGCCGTCGTCTCACGGGCCATGGGTGAGGATGAGGAGGCGAGCTGCTGA","MPESSSRSFPTVPTALSALTAQSMTPDAPLPHPPSLGAGALLRWLLRRAAVPVTLATLAACTSNIIQAIVPAFLGQALDAGIENGLNGRVWGIGALLLVLFVVYAVGDTMMSYFGVTAWMRTAFDVDRLVGRQISATGKDLSRQVSTGEVATIIASDADYLGKFIEHLPALLGAAASFLVVAVLMLRTSVSLGLIVILGMPLVAAIVTLVIRPLQKRQAVQREAQSAVTTVTTDTVAGLRILRGIGGEDVFARRYRDASQELRRRGVEVASSQATLMTLQVLLPGLFAAIVVWVAARMAVAGSLTPGGLITFYGYTAYLSWPLWVFTSCVQDYTRAVVGARRLSRLLEVAPAAGSLVERLNLDPAAAHAVSGDLVDTGSGLRLKEGRMTALVCPDPQVSADLATRLGRFTDAGPTVTLAGRPLTTMPLEQVRASVVVSGATAQLFTGTLREALDVRSGPDPQPAGLEDLLRAETERTTGADVDQQVRPQEREAPGDDRLIEAVGIADAGDVLTSLSEGLAGMITEKGRSLSGGQRQRVALARALLTEAPTLVLIEPTSALDSHTEARVAAQVHRARAGRTTVVVTASPLVLEACDEVVLLDSSGAELLRSTHRELMAMARDGHAQAADYRAVVSRAMGEDEEASC$","ABC-type multidrug/protein/lipid transport system, ATPase component","Membrane, Cytoplasm","ABC transporter strV","putative ABC transporter transmembrane protein ","ABC transporter, transmembrane region","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074Holland I.B., Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999. 293(2):381-399. PMID: 10529352","","","

InterPro
IPR001140
Domain

ABC transporter, transmembrane region
PF00664	$\"[53-323]T$	ABC_membrane

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[530-565]T$	Q8CK38_STRCO_Q8CK38;
PF00005	$\"[442-604]T$	ABC_tran
PS50893	$\"[357-628]T$	ABC_TRANSPORTER_2
PS00211	$\"[530-544]T$	ABC_TRANSPORTER_1

InterPro
IPR011527
Domain

ABC transporter, transmembrane region, type 1
PS50929	$\"[55-335]T$	ABC_TM1F

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[496-617]T$	no description
PTHR19242	$\"[42-453]T$ $\"[488-643]T$	ATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF42	$\"[42-453]T$ $\"[488-643]T$	ABC TRANSPORTER TRANSMEMBRANE BACTERIAL
signalp	$\"[1-56]?$	signal-peptide
tmhmm	$\"[49-69]?$ $\"[88-106]?$ $\"[169-187]?$ $\"[193-211]?$ $\"[275-297]?$ $\"[303-325]?$	transmembrane_regions

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[212-389]T$ $\"[681-853]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[265-287]?$ $\"[308-342]?$ $\"[361-381]?$ $\"[403-425]?$ $\"[431-451]?$ $\"[493-513]?$ $\"[735-757]?$ $\"[787-807]?$ $\"[826-846]?$	transmembrane_regions

","BeTs to 15 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 212 to 389 (E_value = 1.9e-36) place ANA_2672 in the FtsX family which is described as Predicted permease.Residues 681 to 853 (E_value = 7.5e-39) place ANA_2672 in the FtsX family which is described as Predicted permease.","","transporter, permease components, putative","","1","","","","","","","","","","","Tue Aug 14 17:31:47 2007","","","","","Tue Aug 14 17:31:47 2007","","","","Tue Aug 14 17:31:47 2007","Tue Aug 14 17:31:47 2007","","","","","yes","","" "ANA_2673","2880730","2879891","840","5.50","-7.39","29811","ATGAGTAGTTCCACCCCCGTCGCCTCATCCTCCGTCCTCACACCTCACCATCCCGTGGATGACCCCGTGGTCTCCGCACGCAACCTCACCAAGGTCTACGGCCGCGGATCGGGCGCCGTCACAGCGCTCGACTCCGTCAACGTCGACATCGCCCGCGCCCGCTTCACCGCCATCATGGGGCCATCCGGCTCCGGCAAGTCCACGCTCATGCACTGCCTGGCCGGCCTGGACTCGATCACCTCCGGGGAGATCATGCTCGACGGCGACATGGTCTCCTCCATGAATCAGCGTCGCCTCACCCGCCTGCGCCGCGAGCGCATCGGCTTCATCTTCCAGTCCTTCAACCTGGTCCCCACTCTCACGGCGGCGGAGAACATCACCCTGCCCCTGGATATCGCCCGCAAGAAGGTCAACCCGCAGCGCTTCGACCAGGTGATCGACGCCGTCGGCCTCAGGGAGCGCCTGTCCCACCGGCCCGCCGAGCTCTCCGGCGGCCAGGTCCAGCGCGTGGCCTGCGCCCGGGCGCTCGTAGGCGAGCCGGCGGTCGTCTTCGCCGACGAGCCCACCGGCAACCTGGACTCCCACTCCACCGATCAGGTCCTGGAGATCCTGCGCCGCAGCGTCGACGACCTGGGGCAGTCGGTGGTCATGGTGACCCACGAGCCGGAGGCGGCCGCCTGGGCCGACACCGTCATCTTCCTGCGCGACGGGCACGTCGTCGCCCAGCTGGACGACCCCGACCGCGACCGGGTCCTGGACGCCCTGCGTGAGCTGAGTGAGACCGAGCCCGCCCCCGCAGCCGCCGCCCCGTTCACCGGCTCGGCCGTCGAGGGGGCCTGA","MSSSTPVASSSVLTPHHPVDDPVVSARNLTKVYGRGSGAVTALDSVNVDIARARFTAIMGPSGSGKSTLMHCLAGLDSITSGEIMLDGDMVSSMNQRRLTRLRRERIGFIFQSFNLVPTLTAAENITLPLDIARKKVNPQRFDQVIDAVGLRERLSHRPAELSGGQVQRVACARALVGEPAVVFADEPTGNLDSHSTDQVLEILRRSVDDLGQSVVMVTHEPEAAAWADTVIFLRDGHVVAQLDDPDRDRVLDALRELSETEPAPAAAAPFTGSAVEGA$","ABC-type transport system involved in lipoprotein release, ATPase component","Membrane, Cytoplasm","ABC-type transporter, ATPase component","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[161-204]T$	Q6NFK2_CORDI_Q6NFK2;
PF00005	$\"[53-237]T$	ABC_tran
PS50893	$\"[24-261]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[52-238]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[18-264]T$	no description
PTHR19222	$\"[24-258]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32	$\"[24-258]T$	ABC TRANSPORTER

InterPro
IPR014983
Domain

GAD-like
PF08887	$\"[1-101]T$	GAD-like

InterPro
IPR015002
Domain

Domain of unknown function DUF1851
PF08906	$\"[115-194]T$	DUF1851

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 101 (E_value = 2e-05) place ANA_2674 in the GAD-like family which is described as GAD-like domain.Residues 115 to 194 (E_value = 2.5e-07) place ANA_2674 in the DUF1851 family which is described as Domain of unknown function (DUF1851).","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2675","2882803","2884200","1398","5.73","-10.19","49815","ATGTCTTCTGAGGGTCGTCTGAATACATCATTGCAGGGTGATCCCTCAGAGTCGGCGCTGATGACGAGGGTCGGGGAGTCGGTTGAGAGTCTTGTTCAGCAGCTTGCCCGCGACCACACATTGGCGAGAGTTCAAGAAGAAGGCTCTCTGTGGAACTACCTCGGAAAATCAATCAGTGACGCCTACATGCAACGTGCGCAGGCTGAAGGGGTGCGTGGCGGCAGGGCTATCGTGATGGCAGGCCCCCCGGGTGCGGGAAAAAGCCGTGGAGTAGAGTCTGTCCATGAAGCGCTAGGGTCGGAGCGAAGTGCTGAGCTGGGGGTCGACGAATCCAACTTCATCACTGTAGATGCCGATGACATCAAACAGCTCCTTCTGGGGTTCCCAGTCGAAGGAATCAACGTGGATCCGGCATTGCTGGCCGGAGCGAAAGAACACTGGGATCACCTCATCGCTGTCGCTGCCCCGGATGTCCTCGAGGATGGGAGGCAGTTGCAGCGGGGTGAGCTATCCACTTTGGTTCATCCGCTGTCCACCGCTCTTGCAGACGGGGTGCGCAGAGACCTGATTGAGACGCAGGTTGACATCAAGGTCGAAGGGACGCTGAGATGGATGGAGAGCCCCACAGTCGGTCAAGGTCCCACGCTGGTTCGTGAACTTGAAGGAGCTGGATACCGGCAGGTTTCCATTGTGGCTGTGGATACCCCATCTGAACTATGCCTCGAGGGTGCTAGAATGCGATGGGAGATTCCTCGTTTCCAGGGTAATGCTGGTGCCCGGTATACTCCACCGGACGCGGTGCTGTCCTGCTTCGAGATAGGGCAGGATGGCGCCGAGATCTCACGATGCGTGAAGAATGCATATTCAACTCACCGGCTTGCTTGTCAGAGCCAGGGCCTTGAGGAAGTCAATCTTTTCGTTGCTCATCGGAACCCCCTGATCCCGACAATCGTCGAGCACATTGATCGCTCGGGGCACTCCGAAATTCTCTCCCAGGGAGCGCCGGAAATGCGGGTGGCGCCTGAAACTACTCCGCCAGACCTTGGGGTCACGCCTCCCGGCAGTTCTGGACTCGAGCGGGTCAACCAGGTCCTCAAAGGGGCGGTAGGTGGGTCTGAGCAGTCACATCCGACTGTCATGGTGCGAGTTTCCGGCGTGGAGGGCAGTATTTCTGTTGAACCCACAGGAGAAGGGGGAGTGCTGACTTCCGAAGATATCACCGGCGCCTTGCGTCGCCTTGGTGTGAGGCCAACTCGAAACTCTCCGGCAAGGGACTCCGCCAGGAAGGTGAGGACTCAAGGGGAAGACGCGCCTCGCACATCGAGAGTGAATCGTCCGAAGGTGAATCCTCATCCCCCTCAGTCTGAGGGAAGAGGTAACCATGGACGTTCGCGCTGA","MSSEGRLNTSLQGDPSESALMTRVGESVESLVQQLARDHTLARVQEEGSLWNYLGKSISDAYMQRAQAEGVRGGRAIVMAGPPGAGKSRGVESVHEALGSERSAELGVDESNFITVDADDIKQLLLGFPVEGINVDPALLAGAKEHWDHLIAVAAPDVLEDGRQLQRGELSTLVHPLSTALADGVRRDLIETQVDIKVEGTLRWMESPTVGQGPTLVRELEGAGYRQVSIVAVDTPSELCLEGARMRWEIPRFQGNAGARYTPPDAVLSCFEIGQDGAEISRCVKNAYSTHRLACQSQGLEEVNLFVAHRNPLIPTIVEHIDRSGHSEILSQGAPEMRVAPETTPPDLGVTPPGSSGLERVNQVLKGAVGGSEQSHPTVMVRVSGVEGSISVEPTGEGGVLTSEDITGALRRLGVRPTRNSPARDSARKVRTQGEDAPRTSRVNRPKVNPHPPQSEGRGNHGRSR$","Hypothetical protein","Cytoplasm, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","BeTs to 3 clades of COG1224COG name: DNA helicase TIP49, TBP-interacting proteinFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1224 is a---kzy-------------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2676","2884352","2886451","2100","4.07","-85.74","71830","ATGGACTCTGTTCAGCTCATGATGGCGGCGCATCAGGCCGATGCGAACGTGGCTGCCCAGACAACTGACCAGGCGCTGCAGGCTGCGATCGCGCAGAGTCGGCCTGACCTGTGGGGTCCACTGTCGACCAACCCCGCAGCCTATGCGGACCTGCTCGGCTGGCTGGCCAGCACCGGGAACGTCGAGGTCCTGGCCAACCTTCGGGCGCGCGGCTACCTGACCGACGACGCGGCGGCTGATGCTGCCGGTGCTGCGGGGTCTGCGGTTGATGAGCCCGCTGTCGAGCCCCATGTCGTGCAGGAGGAGCCGGCGCAGATGGAGTCGGCCGATCCGGCCGAGGACGGCGATGCAGAGTCCGTGGAGCCTGCGGCTGAGGACGCCGTCGACTCCGATGCGGAGGAGACCGCCGATGGAGCCGAGGTGGCTGAGCCGGCTGAGATGCCGGGACCTGACGAGTCGGATGACGAGGAGGCGGGTTCCGTCGCCGGCGGGTCAGCTGATGAGGCCGCGGAGGACGCGGAGGACGCCGCCGACGAGGCTCAGGAGTTGGTGACCGCCGAGCCTGATGATGAGTTCGAGGATGACGTCGAGGACGCCGCGGTCGACGATGACTCTGGCGAGGCCGGTATCGAGCCAGGGACTGAGGAGCCTGCCGAGGATTCCGAGGGTTCCGACGCGGCTGAGACCGCCGTCGATTCCGATACGGAGACCGCAACCGACGAGGCTGCGGACTCCGACAGCAACGCCCCTACCGTCCTCGCCCCCGTATCGCAGTGGCAGGAGGTCGACTCGGCCGACACGACTGACGTCGCGGCTTCAGTCCAGTCCGCGGCCGTGACCTCCGGCTGGACAGCGGGCTCGGCTGCTCCCGCCGCGGGCTCGGCCGAGTCGGTGGCCTTCCCCGTGCCCCCGCCGCCGTCGGCCGAGGACATCGCCGCCTGGGCCGAGACCCCCAGCGGGGCGCCGTCGGGCTTCTCCGCCGCTCAGCCGGCCGTGGAGCTGGACATGTTCGGCCCTCAGATGGTGGCCCAGATGCCGCCACCCCAGCAGAAGCAGCCGTCGAAATCCAGCAGCGGTCGCCTGGTCGCGATCATCGTGGTCCTCCTGCTCGTCCTCGTCGGCGGAGGCGGCCTGTGGGCCGGCACCTACTTCGCCAACAAGGACAAGAGTGGGGATACCTCCCAGGACAGGGCCAACAGCAACGGCGACAAGGACGGCAAGCAGAACGGCCAGGTCGACGCCGCGGCAACGTCCACCGCGGCGGCCCTGCCCTCGGGCGCGGTCAAGGCCTGCTCCAGCATGCCGACCTTCACGATCACCTCCGTTGAGGACGGCCAGGGCGAGCTCAAGGTCCAGGGCACCATGACGACCTCCTGCGCGGAAGGGGACTTCCTGGCCGGGTCGTCCAGCCAGATCCTCGTCTACAGCTCCACCGGCCCCACCGGCGGCGCTGATGTTGACTCCCTTGTCGCCTCGGGAACCTTCGACCTCTCCAGCGAACCGCTCATCATCCCCAACGGCGGGCGGACCGTGACGCTGCGCTTCGGCGAGCAGCACTACTTCCGCACTGCCAAGGACCTCGAGCTCAAGGGCCTGTCGGTCAAGCCCTCCTTCGACCGCGGCTCCTCATCGAGCGTCACCTCGAAGAGCTCGACGAACTCCCCGATGACCGTCGCCTCCTCAACGAGCTCCAACGCCAACCAGGAGGCCCAGGACGAGCAGGCCGCCGGAGACGCCATCGGGTGGCAGGTCAAGCACGACTACCCCATCGTCATGAACAGCATGCGGGGCAAGTGGACCCCGCAGCTGTCCTCCAAACAGGTCGGCCTGGTGGCCGAGGGGCAGACCTGGACCAACCGCTCGATTCTTGCGGAGTTCCTCAAAACTCGGCAGGCCAATCCGAAGGCCGTCATCATCGACACCAGCCAGTGGCCGGTCTACGACGTCGGCGGCTGGTGGGTGACGCTGTCCGGCGAGCTCTACGACGACGCCGACCAGGCCAACGCCTGGTGCGACGCCCAGGGCTACGACTCCGACCACTGCCTGGCCAAGCGCATCGAGTCCAACGGAACATCGCAGGGCACCACCAAGACCCGCTGA","MDSVQLMMAAHQADANVAAQTTDQALQAAIAQSRPDLWGPLSTNPAAYADLLGWLASTGNVEVLANLRARGYLTDDAAADAAGAAGSAVDEPAVEPHVVQEEPAQMESADPAEDGDAESVEPAAEDAVDSDAEETADGAEVAEPAEMPGPDESDDEEAGSVAGGSADEAAEDAEDAADEAQELVTAEPDDEFEDDVEDAAVDDDSGEAGIEPGTEEPAEDSEGSDAAETAVDSDTETATDEAADSDSNAPTVLAPVSQWQEVDSADTTDVAASVQSAAVTSGWTAGSAAPAAGSAESVAFPVPPPPSAEDIAAWAETPSGAPSGFSAAQPAVELDMFGPQMVAQMPPPQQKQPSKSSSGRLVAIIVVLLLVLVGGGGLWAGTYFANKDKSGDTSQDRANSNGDKDGKQNGQVDAAATSTAAALPSGAVKACSSMPTFTITSVEDGQGELKVQGTMTTSCAEGDFLAGSSSQILVYSSTGPTGGADVDSLVASGTFDLSSEPLIIPNGGRTVTLRFGEQHYFRTAKDLELKGLSVKPSFDRGSSSSVTSKSSTNSPMTVASSTSSNANQEAQDEQAAGDAIGWQVKHDYPIVMNSMRGKWTPQLSSKQVGLVAEGQTWTNRSILAEFLKTRQANPKAVIIDTSQWPVYDVGGWWVTLSGELYDDADQANAWCDAQGYDSDHCLAKRIESNGTSQGTTKTR$","Hypothetical protein","Extracellular, Periplasm, Membrane, Cellwall","hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[361-381]?$	transmembrane_regions

InterPro
IPR001764
Domain

Glycoside hydrolase, family 3, N-terminal
PF00933	$\"[133-362]T$	Glyco_hydro_3
PS00775	$\"[318-335]?$	GLYCOSYL_HYDROL_F3

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.300	$\"[75-402]T$	no description
signalp	$\"[1-23]?$	signal-peptide

","BeTs to 13 clades of COG1472COG name: Beta-glucosidase-related glycosidasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG1472 is --------vdrlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB001764 (Glycoside hydrolase, family 3, N-terminal) with a combined E-value of 6.3e-22. IPB001764A 205-253 IPB001764B 300-333","","","-42% similar to PDB:1TR9 Structure of beta-hexosaminidase from Vibrio cholerae (E_value = 6.4E_18);-42% similar to PDB:1Y65 Crystal structure of beta-hexosaminidase from Vibrio cholerae in complex with N-acetyl-D-glucosamine to a resolution of 1.85 (E_value = 6.4E_18);","Residues 133 to 362 (E_value = 1.1e-11) place ANA_2677 in the Glyco_hydro_3 family which is described as Glycosyl hydrolase family 3 N terminal domain.","","hydrolase family 3 N terminal domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2678","2888318","2887944","375","4.10","-25.08","14169","ATGTCGCAGCAGGAGTTCGAGGACGTCGTCGGTGACGCCCTTGACCGGATTCCCGCCGACCTGGCCGAGGTGATGGACAACGTCGTCGTCCTCGTTCAGGACGAGCCCGATCCGGAGATGCTCTCCGAGGAGGACTATGACGAGGCCGGCCTGCCCACGCTCCTGGGGCTGTACGACGGCGTCCCCCTGACCGAGCGCGACGAGGGCTGGTCCATGGTGCTGCCCGACCGCATCCTCATCTTCCGCGGCCCCTTGGAGCGCTGGTGCTCCAGCCGCGAGGAGCTGGAGGAGGAGATCACCGTGACCGTCATCCACGAGGTCGCCCACCACTTCGGCATCCCCGACGAGCGCCTCCACGAGCTGGGCTGGGAGTAG","MSQQEFEDVVGDALDRIPADLAEVMDNVVVLVQDEPDPEMLSEEDYDEAGLPTLLGLYDGVPLTERDEGWSMVLPDRILIFRGPLERWCSSREELEEEITVTVIHEVAHHFGIPDERLHELGWE$","Uncharacterized conserved protein","Cytoplasm","narrowly conserved protein with unknownfunction","hypothetical protein","protein of unknown function DUF1025","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 1989. 242(2):211-214. PMID: 2914602Murphy G.J., Murphy G., Reynolds J.J. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett. 1991. 289(1):4-7. PMID: 1894005","","","

InterPro
IPR006025
Binding_site

Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142	$\"[102-111]?$	ZINC_PROTEASE

InterPro
IPR010428
Family

Protein of unknown function DUF1025
PF06262	$\"[2-123]T$	DUF1025

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 123 (E_value = 1.5e-47) place ANA_2678 in the DUF1025 family which is described as Domain of unknown function (DUF1025).","","conserved protein with unknown function","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2682","2889441","2888926","516","4.58","-9.57","18890","ATGGACACCATCGAGACCTTCCTCGACAACATGTTCGCCCCCTACCCCGCCACACCTCGCCTGATCGAGGCCCGCTCCGAGCTGCGCGCCATGATGGAGGACGCCTACAACGACGCCATCGCCCAGGGCAAGACCCACAATGAGGCGGTCGGGCAGGTCATCACTGACTTCGGCAACCTTCACGAGCTGGCCCCGGTCCTGGGCATCGCTCAGGACATCCAGCCCGGCGGCGCTCCGCAGGTGGCCCCCGCCGGCGCCCCGACGACATTCGCCCCCAATCGTCCCACCACCCCCGCCCCTGTCGGCCAGCCGTCCTCCTGGCAGGGCGAGCAGGACGATGACGATCCCTTCACCAACCTCGTAGCCGGGATCTACTGGCCGGCCGCAGTGGTCATCTACCTGCTGTGGAGCTTCATCTTTGACGCCTGGGACATCTCCTGGATCATCTGGCCGGTGGCCGCCGTCGCCTTCACCATCTTCGCCACCGTGCGCCGCTACCGGCGCGACCGCCAGTGA","MDTIETFLDNMFAPYPATPRLIEARSELRAMMEDAYNDAIAQGKTHNEAVGQVITDFGNLHELAPVLGIAQDIQPGGAPQVAPAGAPTTFAPNRPTTPAPVGQPSSWQGEQDDDDPFTNLVAGIYWPAAVVIYLLWSFIFDAWDISWIIWPVAAVAFTIFATVRRYRRDRQ$","Hypothetical protein","Cytoplasm, Extracellular","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[122-140]?$ $\"[146-164]?$	transmembrane_regions

InterPro
IPR005149
Family

Transcriptional regulator PadR-like
PF03551	$\"[5-90]T$	PadR

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[9-97]T$	no description

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide

","BeTs to 11 clades of COG1695COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1695 is aompkz--vdrlb-e-g----j----Number of proteins in this genome belonging to this COG is 4","***** IPB005149 (Transcriptional regulator PadR-like family) with a combined E-value of 2.5e-06. IPB005149A 25-39 IPB005149B 44-52 IPB005149C 73-82","","","-64% similar to PDB:1XMA Structure of a transcriptional regulator from Clostridium thermocellum Cth-833 (E_value = 4.2E_24);","Residues 5 to 90 (E_value = 4.6e-20) place ANA_2683 in the PadR family which is described as Transcriptional regulator PadR-like family.","","regulator, PadR family (putative)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2684","2889935","2891359","1425","7.64","1.21","50016","ATGCTCGTCGCAGTCACCACCCCTCCCGCGACCCCCAGCGCAGATCCCAGCGCGAGTGCCTCGACCACGCCCACTCCCACGGGTGTGCCCGAAGTCAACGTCGATGAGACCGTCAAGGCGGTGACCAAGACGACCAACGACCTGGTCGCCATCGCCTGGCAGGCCGGCGTGGGAGTCGTCATCGGCCTGGTCATCGCCTTCGTGGTGGTGGCGATCCTGACGTTCATGGGCAGGCGGCGCCTCCTGTACCGCGAGATCGTGGATTTCGGACGCCGGCCGATCGTCGCCGTCGGCGCCATGACCGGGGCCTTCCTGGGTACCCAGCTCGCCCTGACCGCGCTGCGGCACACCAAGAGCGACTCCACGACGATGGTCGTCATCGAGCGCGGGGTCACCATCGCCCTCATCTTCTCGGTGACCTGGCTCGTCGTCGCCTTCGCCAAGGCCATCGAGTCCACCGTCGTCAAAGGGGCGCAGGCCGGCGGGGACCAGGGGCGCGCCAACCGCGTGACCACCCAGAGCCAGATCATCCGGCGTGTGGCCCAGGTGATCATCGTCATCGCCGGGCTCGTCAGCGCCATCATGACCTTCCCCAGCGTCCAGTTCGCCATGGGCTCGCTGCTCGCCTCGGCCGGTCTGGCCTCCGTCATCGCCGGTATGGCCGCCCGCTCCATGCTCGGCAACGTCTTCGCCGGCCTCCAGCTGGCCACCACCGACGCCATCCGCGTGGATGACGTCGTCGTCGTCGATAACGAGCAGGGCACCATCGAGGAGATCACCCTGACCTACGTGGTCATGCGCACCTGGGACGACCGGCGCCTCATCCTGCCCTCGACCCACTTCACCGAGAACCCCTTCGCCAACTGGACGCGCGGAGGCTCCCAGGCCACCGGCTACTTCACCCTTGACCTGGACTGGCGCGTGCCCATCGCCTCGCTGCGTGCCGAGCTGGCCCGCCTCGTGGCCGCCTCGTCGGTCTGGGACGGGCGCCAGGCCTCCCTCGAGGTCTTCGACGCCGTCGGCGGCCACGTCACCGTGCGCATCGTCCTGACCGGGAACGACCCCGGCGACGTCGGCGCCCTCAAGTCCTACGTGCGCGAGGAGCTGGTTACCTGGCTCCAGCGGGAGGCCCCCTACGCCCTGCCGCGCACGCGAGTGGAGGTCGAGCAGGTCGAGGTCACCCAGGACCTCGGCCCCGAGGAGGTGGCCCGCGCCGCCGAGCAGATCGTCGCCAAGCAGAAGGCCGGCCCCGCCGGCGCCACCACGGCCGCTCCAGACAACGGAGGCGATACTGCCGCGACCACGGAGGCCGAGGGGGAGAGCACCGCCCACGGGCTGGGGGCCCGGCGGGCCGTCACCCTGGGGCGGGCCATGGGGCGCTCCCTGCTGCACCGCGCCCGGCGCGGGGGACTGGGACCCAGGTGA","MLVAVTTPPATPSADPSASASTTPTPTGVPEVNVDETVKAVTKTTNDLVAIAWQAGVGVVIGLVIAFVVVAILTFMGRRRLLYREIVDFGRRPIVAVGAMTGAFLGTQLALTALRHTKSDSTTMVVIERGVTIALIFSVTWLVVAFAKAIESTVVKGAQAGGDQGRANRVTTQSQIIRRVAQVIIVIAGLVSAIMTFPSVQFAMGSLLASAGLASVIAGMAARSMLGNVFAGLQLATTDAIRVDDVVVVDNEQGTIEEITLTYVVMRTWDDRRLILPSTHFTENPFANWTRGGSQATGYFTLDLDWRVPIASLRAELARLVAASSVWDGRQASLEVFDAVGGHVTVRIVLTGNDPGDVGALKSYVREELVTWLQREAPYALPRTRVEVEQVEVTQDLGPEEVARAAEQIVAKQKAGPAGATTAAPDNGGDTAATTEAEGESTAHGLGARRAVTLGRAMGRSLLHRARRGGLGPR$","MscS mechanosensitive ion channel","Membrane, Cytoplasm","membrane protein","MscS mechanosensitive ion channel","MscS Mechanosensitive ion channel","","Pivetti C.D., Yen M.R., Miller S., Busch W., Tseng Y.H., Booth I.R., Saier M.H. Two families of mechanosensitive channel proteins. Microbiol. Mol. Biol. Rev. 2003. 67(1):66-85. PMID: 12626684Bass R.B., Strop P., Barclay M., Rees D.C. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science 2002. 298(5598):1582-1587. PMID: 12446901","","","

InterPro
IPR006685
Family

MscS Mechanosensitive ion channel
PF00924	$\"[181-378]T$	MS_channel

noIPR
unintegrated

unintegrated
tmhmm	$\"[51-73]?$ $\"[94-112]?$ $\"[126-146]?$ $\"[176-196]?$ $\"[202-222]?$	transmembrane_regions

","BeTs to 12 clades of COG0668COG name: Small-conductance mechanosensitive channelFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0668 is aompkz-qvdrlbcefg-snujx-t-Number of proteins in this genome belonging to this COG is 1","***** IPB006686 (Mechanosensitive (MS) ion channel subdomain) with a combined E-value of 2e-14. IPB006686A 200-247 IPB006686B 256-288","","","No significant hits to the PDB database (E-value < E-10).","Residues 181 to 378 (E_value = 2e-18) place ANA_2684 in the MS_channel family which is described as Mechanosensitive ion channel.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2685","2891457","2891942","486","4.96","-10.54","17544","ATGAGTACCAATGTCAGCAGCGACCCCTCCGTGACGCCCACCTCCGAGCCCTCTGGCCCGGCCGTCGATGGCCTGGCCCTCGACCTGGAGGCCGCCGCGCGCACCGACGCCCAGTGGCGCGCCGCCCTGAGCCCCATGGAGTACCACGTGCTGCGCGAGGCCGGCACCGAGCGTCCTTTCACCGGCGCCCTGCTCGACGAGCATCGCGAGGGCGTCTACCGCTGCCGCGGCTGCGGCGCCGAACTGTTCCGCTCCACCACCAAGTTCGACTCCCACTGCGGCTGGCCCTCCTTCTACGACCCCTCCGACTCCGAGGCGGTCACCCTGAGCACCGACACCTCCCACGGCATGGTGCGCACCGAGGTCCGCTGCGCCACCTGCCACAGCCACCTGGGACACGTCTTCGACGACGCCCCCCAGACCCCCACCGGCCAGCGCTATTGTATGAACTCCGTGAGCCTGACCTTCGAGGAGGAGCAAGCATGA","MSTNVSSDPSVTPTSEPSGPAVDGLALDLEAAARTDAQWRAALSPMEYHVLREAGTERPFTGALLDEHREGVYRCRGCGAELFRSTTKFDSHCGWPSFYDPSDSEAVTLSTDTSHGMVRTEVRCATCHSHLGHVFDDAPQTPTGQRYCMNSVSLTFEEEQA$","Peptide methionine sulfoxide reductase","Cytoplasm, Periplasm, Extracellular","1.8.4.6","peptide methionine sulfoxide reductase ","methionine-R-sulfoxide reductase","","Lowther W.T., Brot N., Weissbach H., Honek J.F., Matthews B.W. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proc. Natl. Acad. Sci. U.S.A. 2000. 97(12):6463-6468. PMID: 10841552Koonin E.V., Mushegian A.R. Complete genome sequences of cellular life forms: glimpses of theoretical evolutionary genomics. Curr. Opin. Genet. Dev. 1996. 6(6):757-762. PMID: 8994848Mushegian A.R., Koonin E.V. A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(19):10268-10273. PMID: 8816789Lowther W.T., Weissbach H., Etienne F., Brot N., Matthews B.W. The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nat. Struct. Biol. 2002. 9(5):348-352. PMID: 11938352","","","

InterPro
IPR002579
Domain

Methionine sulfoxide reductase B
PD004057	$\"[43-157]T$	Q9X828_STRCO_Q9X828;
PF01641	$\"[36-159]T$	SelR
TIGR00357	$\"[33-161]T$	TIGR00357: methionine-R-sulfoxide reductase

noIPR
unintegrated

unintegrated
PTHR10173	$\"[35-156]T$	METHIONINE SULFOXIDE REDUCTASE

","BeTs to 17 clades of COG0229COG name: Conserved domain frequently associated with peptide methionine sulfoxide reductaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0229 is -om---y--drlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is 1","***** IPB002579 (Protein of unknown function DUF25) with a combined E-value of 1.9e-42. IPB002579A 55-84 IPB002579B 112-152","","","-61% similar to PDB:1XM0 Solution NMR Structure of Methionine Sulfoxide Reductase B Using Minimal Constraint Strategy; Northeast Structural Genomics Target SR10 (E_value = 3.5E_26);-55% similar to PDB:1L1D Crystal structure of the C-terminal methionine sulfoxide reductase domain (MsrB) of N. gonorrhoeae pilB (E_value = 1.7E_20);-48% similar to PDB:2J8X EPSTEIN-BARR VIRUS URACIL-DNA GLYCOSYLASE IN COMPLEX WITH UGI FROM PBS-2 (E_value = 1.7E_20);-42% similar to PDB:1KIT VIBRIO CHOLERAE NEURAMINIDASE (E_value = 1.7E_20);-42% similar to PDB:1W0O VIBRIO CHOLERAE SIALIDASE (E_value = 1.7E_20);","Residues 36 to 159 (E_value = 1.8e-80) place ANA_2685 in the SelR family which is described as SelR domain.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2686","2891939","2892910","972","6.74","-1.13","33411","ATGATCCGGGTCCTGAGCCTCAACCTCCAGCACGGCCTGCCCGGCGCCGGAGCTGGTGACGGCAGCGCCTCCACCGGCTCGCTGGCCGGCGCCGACATCTCCGACCCCGCCACCGCCCGCACCGTCATGCGGGCCACGGCCGAGCAGATCGCCGAGCTGGCCCCCGACATCATCGCCCTCCAGGAGGTGGACCTGGGGCAGGCCCGCTCCGGGCGCCTCCACCAGGCGGCCTTCCTGGCCGAGGAGCTGGGCATGCCGACCTGCCGCTTCTCCGCCAGCTACGCCGGGCCGGTGGTGGGGCTGCGCCGTCGGCCCCTGCGCACCGCGCTGAGCTCGCCGACCGACGACGTCCTGGGGCCGCTGCGCGCCGCCGTCGGGGCCGGGCCGATCGGCTACGGCAACGCCCTCCTGTCGCGCTTCCCGGCCTCGGGCTGGCACGTCAAGCGCCTGGGGCGCGGGGCCTCCAGCGTGGAGAAGCGCGGCGAGCGGGCCTGGGACCCGCGCTCCTACCACGTGTCCACCGCCTCCCAGCGCATCATGGTGGCCGCCACCCTCGAGGTGCCCGAAGGCGCTGGCGGGCCGATCCGCCAGCTGTCAGTCGCCTCCACCCACCTGGCGACCCGCGAGTCCATGGCAGCGCGCCAGCTCGCCGCCGCCTGGGGGGCGCTCGCCGGGCTGCCCGGGCCGCACCTGCTCGTGGGCGACTACAACCTCTCCGCCGAGCAGGTCGACGTCCTGGGGCTGGGACGGACCGTGGGGGAGGGGCTCACCTTCCCGGCAGCCGGCCCCAAGCGCCGCATCGACCACGTGCTGACCGACCTGTGGCCCACCGGCCCCGACGGCCTGCCGCTGACCGATGAGGCCGCCGCGGCCGGCGGGAGCCCGCTCCTGCGCGCCGTGGAGTGGGGCACAAGCTCCTTCATCATCTCCGACCACGTCGGCACCTGGGTGGACCTCGAGCCGGTCGGCTGA","MIRVLSLNLQHGLPGAGAGDGSASTGSLAGADISDPATARTVMRATAEQIAELAPDIIALQEVDLGQARSGRLHQAAFLAEELGMPTCRFSASYAGPVVGLRRRPLRTALSSPTDDVLGPLRAAVGAGPIGYGNALLSRFPASGWHVKRLGRGASSVEKRGERAWDPRSYHVSTASQRIMVAATLEVPEGAGGPIRQLSVASTHLATRESMAARQLAAAWGALAGLPGPHLLVGDYNLSAEQVDVLGLGRTVGEGLTFPAAGPKRRIDHVLTDLWPTGPDGLPLTDEAAAAGGSPLLRAVEWGTSSFIISDHVGTWVDLEPVG$","Endonuclease/exonuclease/phosphatase","Cytoplasm","Endonuclease/Exonuclease/phosphatase familysuperfamily","endonuclease/exonuclease/phosphatase","Endonuclease/exonuclease/phosphatase","","Dlaki M. Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases. Trends Biochem. Sci. 2000. 25(6):272-273. PMID: 10838565","","","

InterPro
IPR005135
Domain

Endonuclease/exonuclease/phosphatase
PF03372	$\"[2-319]T$	Exo_endo_phos

","BeTs to 3 clades of COG3568COG name: Metal-dependent hydrolaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG3568 is --------------ef--s--j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-45% similar to PDB:2B81 Crystal Structure of the Luciferase-like Monooxygenase from Bacillus cereus (E_value = );-50% similar to PDB:1IRU Crystal Structure of the mammalian 20S proteasome at 2.75 A resolution (E_value = );-38% similar to PDB:2OG9 Crystal Structure of mandelate racemase/muconate lactonizing enzyme from Polaromonas sp. JS666 (E_value = );-45% similar to PDB:1JJU Structure of a Quinohemoprotein Amine Dehydrogenase with a Unique Redox Cofactor and Highly Unusual Crosslinking (E_value = );-45% similar to PDB:1PBY Structure of the Phenylhydrazine Adduct of the Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans at 1.7 A Resolution (E_value = );","Residues 2 to 319 (E_value = 7.9e-07) place ANA_2686 in the Exo_endo_phos family which is described as Endonuclease/Exonuclease/phosphatase family.","","family superfamily","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2687","2893105","2894241","1137","9.85","6.86","38728","ATGGCCGATGTGGTGGCGGGACTGGCCGTCTTCGGCGCAGTCATCGCCGTCGGCTGGCTGCTGGTGCGCACCCGCGCCGTGCCCGCTGACGCCGACGGGGTCCTCACCCGCGTCTGCTTCTTCGCCGCCACCCCAGCGCTGCTCGTGACCACGCTGAGCCGCGCCGACCTGACGGCGGTCCTCTCCCGCTCCACCGCGGTGGCCGTGGCCGCCGAGCTCGCGGCCATCGTCTCGGCCTGGTGCCTCCACCGACTCGTGCTGCGCCGCCCCACCGCCGAGGCCACCATCGGCGCGCTCGCCTCCGGCTACGTCAACGCCGCGAACCTGGGAATCCCGGTGGCCGTCCTCGTCCTAGGGGATGCGGCCACGATCGCCCCGATCCTCCTGCTCCAGCTCCTCGTGCTCACCCCGGCCACCTTCACCGTGCTCGACGCCGTCACCCGCCGCGGCAACCCGTCTCGCCTGGCGACCCTGACCGTCCCGCTGCGCAACCCGCTGCTGTGGGGTGTTGTGGCCGGGACTGCGGCGAACCTGGGAGGGGTGGACCTCAAGGAGTGGGGAGGCGGCTATCCGGCCCAGGGCCTGGAGATGCTCGGGCGCGTCGCGGTGCCGCTCATGATGCTGGCCCTGGGGATGAGCCTGGCCGGGGCGCCCCGGCCCCTGCGCAACCTCGTGCCGGAGGAGGCCGCCCCGTCCCTACAAGGCTCGCCGGCCCGGACGGTGCAGTCGCCCCAGTCTGCCCGCCAGAGTCAGGAGCCGCTGGCGGCGGAGGCCGGATCGGAGGCGCACGAGATCAACACCGCGGGAGGCCGACTTCCCCGGGTGGAGGAAGAGCCGGCGCACGGGGCGAGGTCGACGTCCCAGCGCGGCGCGGGTCGGCGCAGGGACTTGTGGCTGGCGGTGGGCTGGAAGCTCGCCGTCATGCCGGGGCTGGCCGTCGTCGTCGGACTGGCGGCGGGACTCAGCGGAGGCCAGCTGCTCGCCCCGGTCGTCACCGCCGCCCTGCCCACGGCGCAGAACGTCTTCATGTACGCCTCGCGCTACGGGGCGGTCAAGGACCTGGCCCGTGACGCCGTCCTGCTGACGACGGCCGGATTCGTGCCCGTGGTCCTGCTGGCCGCCGCCCTCCTGCACTGA","MADVVAGLAVFGAVIAVGWLLVRTRAVPADADGVLTRVCFFAATPALLVTTLSRADLTAVLSRSTAVAVAAELAAIVSAWCLHRLVLRRPTAEATIGALASGYVNAANLGIPVAVLVLGDAATIAPILLLQLLVLTPATFTVLDAVTRRGNPSRLATLTVPLRNPLLWGVVAGTAANLGGVDLKEWGGGYPAQGLEMLGRVAVPLMMLALGMSLAGAPRPLRNLVPEEAAPSLQGSPARTVQSPQSARQSQEPLAAEAGSEAHEINTAGGRLPRVEEEPAHGARSTSQRGAGRRRDLWLAVGWKLAVMPGLAVVVGLAAGLSGGQLLAPVVTAALPTAQNVFMYASRYGAVKDLARDAVLLTTAGFVPVVLLAAALLH$","Permease","Membrane, Cytoplasm","Predicted permeases","predicted permease","Auxin Efflux Carrier","","","","","

InterPro
IPR004776
Family

Auxin efflux carrier
PF03547	$\"[295-374]T$	Mem_trans

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[4-22]?$ $\"[34-54]?$ $\"[60-82]?$ $\"[97-117]?$ $\"[123-143]?$ $\"[164-183]?$ $\"[197-217]?$ $\"[301-319]?$ $\"[325-345]?$ $\"[357-377]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-60% similar to PDB:2C20 CRYSTAL STRUCTURE OF UDP-GLUCOSE 4-EPIMERASE (E_value = );","Residues 9 to 374 (E_value = 4.7e-06) place ANA_2687 in the Mem_trans family which is described as Membrane transport protein.","","permeases ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2688","2895312","2894371","942","4.77","-18.60","32624","ATGTCCGCACCCGGCCGCCCAGGATCCGCCCTCGTCATCGGCGAGGCCCTGGTTGATGTCGTCATCCACCCCGGGCAGGAGCCCGTGGACATCCCCGGCGGCTCGCCTGCCAACGTCGCCCTGGGGCTGGCACGCCTGGGCCGCGACGCCGAACTGCACTGCTGGATCGGCACCGACGAGCGTGGTCAGGCGGTGCGCTCCCACCTGGAGGCCTCCGGGGTTCGTCTGGCTCCGGGTGCCGACGGCGCGGCGCGCACCTCCACGGCGCAGGCCACCATCGGCGAGGACCGCGCCGCCACCTACGTCTTCGACCTGGACTGGAACCCGCCGCGCCCTGCCCTGGACGACAGGCAGGCGCCGCTGCTGGTGCACACCGGCTCGATCGCCGCGATCCTGGCGCCCGGCGCCACCACCGTGGAGCAGGTGCTGCGCGAGACCCGCGCCACCTCCACCATTGCCTACGACCCCAATGCCCGGCCTCAGCTCATGGGTGATCCCGAGGACGCCCGTGAGGTCGTCGAGCGCCTGGTGGGCCTGTCGGACCTGGTCAAGTGCTCGGACGAGGACATCGCCTGGCTCTACGGCGAAGGCGCGGACCTGGAGACGGTGCTGCGCTCCTGGCTGGAGAAGGGGGCGGCCGTCGTGGTGGTCACGCGCGGCAAGCAGGGCGCCCTGGCCCTGTCCGCCTCGGGGGTGCACCTGGAGGTATCCGCCGACCCGAACGTCGTGGTGGCGGACACGGTAGGCGCCGGCGACTCCTTCATGGGCGGCCTGGAGGACGCGCTGTGGAGCGAGGACCTCGTGGGCGCGGACCGACGCGAGGCGCTGCGCGCGGTGGACGCCGCGACCCTGGAGCGGATCGTGCGCCACGCCGCGGCCATCGCCGACATCACGGTCTCGCGGGCGGGGGCCAACCCTCCCACTCGCGACGAACTGCCCTGA","MSAPGRPGSALVIGEALVDVVIHPGQEPVDIPGGSPANVALGLARLGRDAELHCWIGTDERGQAVRSHLEASGVRLAPGADGAARTSTAQATIGEDRAATYVFDLDWNPPRPALDDRQAPLLVHTGSIAAILAPGATTVEQVLRETRATSTIAYDPNARPQLMGDPEDAREVVERLVGLSDLVKCSDEDIAWLYGEGADLETVLRSWLEKGAAVVVVTRGKQGALALSASGVHLEVSADPNVVVADTVGAGDSFMGGLEDALWSEDLVGADRREALRAVDAATLERIVRHAAAIADITVSRAGANPPTRDELP$","PfkB domain protein","Cytoplasm","fructokinase","PfkB domain protein","PfkB domain protein","","Wu L.F., Reizer A., Reizer J., Cai B., Tomich J.M., Saier Jr M.H. Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli. J. Bacteriol. 1991. 173(10):3117-3127. PMID: 1850730Orchard L.M., Kornberg H.L. Sequence similarities between the gene specifying 1-phosphofructokinase (fruK), genes specifying other kinases in Escherichia coli K12, and lacC of Staphylococcus aureus. Proc. R. Soc. Lond., B, Biol. Sci. 1990. 242(1304):87-90. PMID: 1981619Blatch G.L., Scholle R.R., Woods D.R. Nucleotide sequence and analysis of the Vibrio alginolyticus sucrose uptake-encoding region. Gene 1990. 95(1):17-23. PMID: 2174811","","","

InterPro
IPR002173
Family

Carbohydrate kinase, PfkB
PS00583	$\"[33-57]T$	PFKB_KINASES_1

InterPro
IPR011611
Domain

PfkB
PF00294	$\"[7-258]T$	PfkB

noIPR
unintegrated

unintegrated
G3DSA:3.40.1190.20	$\"[9-312]T$	no description
PTHR10584	$\"[11-267]T$ $\"[284-312]T$	SUGAR KINASE RELATED
PTHR10584:SF34	$\"[11-267]T$ $\"[284-312]T$	FRUCTOKINASE

InterPro
IPR003761
Family

Exonuclease VII, small subunit
PD028235	$\"[51-101]T$	Q82IE6_STRAW_Q82IE6;
PF02609	$\"[51-112]T$	Exonuc_VII_S
TIGR01280	$\"[49-112]T$	xseB: exodeoxyribonuclease VII, small subun

","BeTs to 11 clades of COG1722COG name: Exonuclease VII small subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1722 is --------vdrlb-efghsnujx---Number of proteins in this genome belonging to this COG is 1","***** IPB003761 (Exonuclease VII, small subunit) with a combined E-value of 2.4e-17. IPB003761 52-87","","","No significant hits to the PDB database (E-value < E-10).","Residues 51 to 112 (E_value = 4.1e-22) place ANA_2689 in the Exonuc_VII_S family which is described as Exonuclease VII small subunit.","","VII small subunit (AF203881)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2690","2897951","2896560","1392","9.28","6.91","49472","GTGACAGGCCAGAGCCCCTCCCAGCCCAGCCCGCAGCCCAGCCCGCAGCCCTCCCCCGGTGCCGGCCGCGTGTCCGGCCCCCACGCGGGCGGCGGCCCCGGCAACTCCGGCAGCCCCGATGGCCCCCGGGAGCTGGCGCCGCGAGCGAACCTCACCACCGCGGAGAACCCGTGGCCGCTGCGGCTGCTGTCGTCCAAGATCGACCAGTACGTGGCCCGCATGAGCCAGGTGTGGGTGGAGGGGCAGGTCATTCAGCTCAACCGCCGCCCCGGCGCCGGCATGGCCTTCCTCACCCTGCGGGACACGGACGCCGATATCTCCATGTCGGTGTCCATCTACGCCCGGGTCCTCGACGCCGTTCTGGCGCGCACCGGCGCCGAGCTCGGCGAAGGAGCCCGCGTGGTGGTGCGCGCCAAGCCCACCTTCTGGGCCAAGCGGGGCTCGCTCCAGCTGCAGGCCGACGACATCCGGCCCGTCGGCGTCGGCGACCTGCTGGCCCGCATCGAGCAGCTGCGCCGCATCCTGGCCGCCGAGGGCCTGTTCGACGCCGAGCGCAAGCGGCCCCTGCCCTTCCTGCCGCGCAAGGTGGGCCTCGTGTGCGGCCGCCAGGCCAAGGCCAAGGACGACGTGCTCGTCAACGCCCGCCTGCGCTGGCCCGGCCTGCCCTTCGAGGTGCGGGAGGTCGCCGTCCAGGGGGCGCGCGCCGTCGGCGAGGTCACCCGGGCCGTCCAGGAGCTCGACTCCGACGCACTGATCGACGTCATCGTCGTGGCCCGCGGGGGCGGCGCCGTCGAGGACCTGCTGCCCTTCTCCGACGAGGGGCTCGTGCGCGCCGCGGCCGCCTGCCGCACGCCGCTGGTCTCGGCGATCGGCCACGAGACCGACTGCCCCCTACTGGACCTGGTGGCCGACTACCGGGCCTCCACCCCCACCGACGCCGCCCGCCGGATCGTCCCCGACCTCGCCCAGGAGACCGTGGGCCTGGACTCGGCCCGCGAGCGCCTGCGCAGCGTGCTCGCCTCGCGGCTGGACGCCGAGCAGGCGGCCCTGGACCAGCTGCGGGCCCGGCCGGTCATGGCTGACCCCACCTCGATCGTGCGCGACCGGGTGAGCGAGCTGGGGCAGGCCCGCGACAGGATGCGCCGGGCCGTGGAGCATCGCCTGTCGTTGGCGGCCGCGGACCTGCGCGCCGATCGCGCCCGGCTGACGGCCCTGTCGCCGCAGGGGGTCCTGGACCGCGGCTACACGATTCTGCGCACTCCCGGCGGCAAGGTCATCACCAGCGCCGAGGACGTCAAGAAGGGCGACCTCATCGAGGGGGTCCTGGCCCACGGGCGGCTCGTCGCCCAGGTCGTCGGCGCCACCAAGCCCCGGCCCGCCGATATCGACTGA","VTGQSPSQPSPQPSPQPSPGAGRVSGPHAGGGPGNSGSPDGPRELAPRANLTTAENPWPLRLLSSKIDQYVARMSQVWVEGQVIQLNRRPGAGMAFLTLRDTDADISMSVSIYARVLDAVLARTGAELGEGARVVVRAKPTFWAKRGSLQLQADDIRPVGVGDLLARIEQLRRILAAEGLFDAERKRPLPFLPRKVGLVCGRQAKAKDDVLVNARLRWPGLPFEVREVAVQGARAVGEVTRAVQELDSDALIDVIVVARGGGAVEDLLPFSDEGLVRAAAACRTPLVSAIGHETDCPLLDLVADYRASTPTDAARRIVPDLAQETVGLDSARERLRSVLASRLDAEQAALDQLRARPVMADPTSIVRDRVSELGQARDRMRRAVEHRLSLAAADLRADRARLTALSPQGVLDRGYTILRTPGGKVITSAEDVKKGDLIEGVLAHGRLVAQVVGATKPRPADID$","Exodeoxyribonuclease VII, large subunit","Cytoplasm","exodeoxyribonuclease VII, large subunit","exodeoxyribonuclease VII; large subunit ","exodeoxyribonuclease VII, large subunit","","Vales L.D., Rabin B.A., Chase J.W. Subunit structure of Escherichia coli exonuclease VII. J. Biol. Chem. 1982. 257(15):8799-8805. PMID: 6284744","","","

InterPro
IPR003753
Family

Exonuclease VII, large subunit
PF02601	$\"[252-390]T$	Exonuc_VII_L
TIGR00237	$\"[59-451]T$	xseA: exodeoxyribonuclease VII, large subun

InterPro
IPR004365
Domain

Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336	$\"[77-159]T$	tRNA_anti

","BeTs to 14 clades of COG1570COG name: Exonuclease VII, large subunitFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1570 is --------vdrlb-efghsnujxi--Number of proteins in this genome belonging to this COG is 1","***** IPB003753 (Exonuclease VII, large subunit) with a combined E-value of 7.5e-67. IPB003753C 147-198 IPB003753D 204-247 IPB003753E 274-310 IPB003753F 405-417","","","No significant hits to the PDB database (E-value < E-10).","Residues 77 to 159 (E_value = 8.3e-11) place ANA_2690 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.Residues 252 to 390 (E_value = 4e-30) place ANA_2690 in the Exonuc_VII_L family which is described as Exonuclease VII, large subunit.","","VII, large subunit (xseA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2691","2898014","2899072","1059","5.48","-12.98","38054","GTGACGACCAGCGAGCTCGCCAGTGAGCACACCGACGCCGCAGCCCCCTCTACCAAGGGCGGCAAGCGGATCCTCATGGCCGCCCCGCGCGGCTACTGCGCCGGCGTGGACCGCGCCGTCGACGCCGTCGAGCAGGCCCTGGCCCACTACGGGGCGCCGATCTACGTGCGCAAGGAGATCGTCCACAACAAGTACGTCGTGGAGGCCCTCTCCAAGCGCGGCGCCATCTTCGTCTCCGAGACCGACGAGGTGCCGGTGGGCGCCCGCGTCGTCTTCTCCGCCCACGGCGTCTCCCCGGCCGTCCACGCCGAGGCCGCCGAGCGCCGGCTGGACACGATTGACGCGACCTGCCCGCTGGTGACCAAGGTGCACAAGCAGGCGGTGCGCTTCGCGGACAAGGACTACGACATCATCCTCGTGGGCCACACCGGCCACGAGGAGGTCGAGGGCACCCAGGGCGAGGCCCCCGACCACATCCAGGTCGTCAACGGCCCCCACGAGGTGGACCAGGTCGAGGTGCGTGACCCCTCCAAGGTCGTGTGGATCAGCCAGACCACCCTGAGCGTCGATGAGACCATGGAGACGGTGCGCCTGCTGCGCGAGCGCTTCCCGGAGATGATCGATCCGCCCGGCGAGGACATCTGCTACGCCACCCAGAACCGTCAGGCCGCGGTCAAGAAGATCGCCCCGAGGGTGGACCTCATGATCGTGGTCGGCTCCGGCAACTCCTCGAACTCGGTGCGCCTCAAGGAGGTGGCCCTCGAGGCCGGTGCGGGCGCCGCCCACCGGGTGGACTTCGCCAGCGAGATCGACCCGTCCTGGTTCGACGGCGTCGAGACGGTCGGCCTGACCTCGGGTGCCTCGGTGCCGGAGATCCTGGTGCGCGAGGTGGTCGAGCGCCTGGCCGAGTTCGGCTTCGACGACGTGGAGGAGGTGCGCACCACCACGGAGAAGATCTCCTTCTCCCTGCCCAAGAACCTGCGCGCCGACCTCATGGCGGCTCAGGGGGCCGCCTCGGCCCACAAGCGCCGCGAGCCGGCCCCCAACCACACCTGCTGA","VTTSELASEHTDAAAPSTKGGKRILMAAPRGYCAGVDRAVDAVEQALAHYGAPIYVRKEIVHNKYVVEALSKRGAIFVSETDEVPVGARVVFSAHGVSPAVHAEAAERRLDTIDATCPLVTKVHKQAVRFADKDYDIILVGHTGHEEVEGTQGEAPDHIQVVNGPHEVDQVEVRDPSKVVWISQTTLSVDETMETVRLLRERFPEMIDPPGEDICYATQNRQAAVKKIAPRVDLMIVVGSGNSSNSVRLKEVALEAGAGAAHRVDFASEIDPSWFDGVETVGLTSGASVPEILVREVVERLAEFGFDDVEEVRTTTEKISFSLPKNLRADLMAAQGAASAHKRREPAPNHTC$","4-hydroxy-3-methylbut-2-enyl diphosphate reductase","Cytoplasm","4-hydroxy-3-methylbut-2-enyl diphosphatereductase","4-hydroxy-3-methylbut-2-enyl diphosphate reductase ","hydroxymethylbutenyl pyrophosphate reductase","","Cunningham F.X., Lafond T.P., Gantt E. Evidence of a role for LytB in the nonmevalonate pathway of isoprenoid biosynthesis. J. Bacteriol. 2000. 182(20):5841-5848. PMID: 11004185Rohdich F., Hecht S., Gartner K., Adam P., Krieger C., Amslinger S., Arigoni D., Bacher A., Eisenreich W. Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein. Proc. Natl. Acad. Sci. U.S.A. 2002. 99(3):1158-1163. PMID: 11818558Potter S., Yang X., Boulanger M.J., Ishiguro E.E. Occurrence of homologs of the Escherichia coli lytB gene in gram-negative bacterial species. J. Bacteriol. 1998. 180(7):1959-1961. PMID: 9537400","","","

InterPro
IPR003451
Family

LytB protein
PF02401	$\"[24-304]T$	LYTB
TIGR00216	$\"[23-304]T$	ispH_lytB: 4-hydroxy-3-methylbut-2-enyl dip

","BeTs to 16 clades of COG0761COG name: Penicillin tolerance proteinFunctional Class: I [Metabolism--Lipid metabolism] Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0761 is -------qvdr-bcefghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB003451 (LytB protein) with a combined E-value of 1.3e-83. IPB003451A 24-61 IPB003451B 118-153 IPB003451C 212-253 IPB003451D 281-298","","","No significant hits to the PDB database (E-value < E-10).","Residues 24 to 304 (E_value = 2.8e-152) place ANA_2691 in the LYTB family which is described as LytB protein.","","diphosphate reductase (ispH)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2692","2899212","2900834","1623","6.46","-4.00","56492","GTGACACATTCCCATGACGAGTCGGCCCCCAGTGGCCCTGCCCCCGCCGCGTCGGGCGGGTGGCCCGCTGCCGACGGCGCCGGCAGCTCCGACAGTGCTGACCCTGTGACCTCAGCAGACCCAGTGGGCGCGGGGGTCTCCAGCGCCTCCGGGCAGGTCTCCAACGAGGCCCTGGAGGAGGACGGCGGCCTGCACCGGAGCCTGACCAACAGGCACATGCAGATGATCGCCATCGGCGGCGCCATCGGCACGGGGCTGTTCGTCGCCTCAGGCGCCACGGTCTCCACGGCCGGCCCGGGCGGCGCCCTGGTCGCCTACGCGGCCATCGGCCTCATGGTGCTGCTGCTCATGCAGTCCCTGGGTGAGATGACGGCGCACATGCCGGTGGCCGGCTCCTTCCAGACCTACGCCACCCGGTTCGTCAGTCCCTCCTTCGGCTTCGCCATGGGCTGGAACTACTGGTTCAACTGGGCGATCACGGTGGCGGCCGAGCTGGTGGCCGCCGGAATCGTCATGGGCTACTGGCTGCCGGGGGTGCCCTCATGGATCTGGGCGGCACTGTTCCTAGCACTGCTGACAACGCTCAACGCCCTGTCGGCCCGCGCCTTCGGGGAGGGCGAGTTCTGGCTGTCGGCCATCAAGGTGGTCACGGTCATCGTCTTCCTCGTGGCGGGGCTGGCCATGATCGCCGGCATCATCGGCGGGACGTCCCCGGGCTTCAGCAACTGGGTCGTCAAGGACGCGCCCTTCCACGGCGGGATGCTGGCGATCGTGTCGGTGTTCATGGTGGCCGGATTCTCCTTCCAGGGCACCGAGCTGGTGGGCGTGGCGGCCGGTGAGGCCCGCAACCCGCGCCGGGACGTGCCCAAGGCCATCCACACAGTGTTCTGGCGGATCATGATCTTCTACATCGGGGCGATCACGGTCATCGGCTTCCTCATCGCCTTCAACGACAGCCGGCTGCTGCACACCGAGACCGAGGACGTGGCCTACTCTCCCTTCACCCTGGTCTTCGAACGGGCGGGGATCGGGATCGCGGCGGCCCTCATGAACGCCGTCATCCTCACCGCGGTACTCAGCGCCGGAAACTCCGGCCTGTACGCCTCGACCCGCATGCTGCACTCGATGGCCCTGCAGGGGCAGGCGCCGGCCTGGTTCTCCTACGTCAACCGTCACGGGGTCCCGGTGCGTGCCCTGGGGGCGACGGCGCTGGTGGGGGCGGCCGGCTTCCTGACCGCCGTGGTGGGGCAGAACACCGCCTACGCGTGGTTGGTCAACGTCTCGGCCCTGTGCGGGTTCATCGTGTGGCTGGGGATCGCCGCGTGCCACTTCCGCTTCCGGCGCGCCTACGTGCTCCAGGGCAATGACCCGGCCGACCTGCCCTACCAGGCGCCCTGGTTCCCGCTGGGACCGGTCCTGGCCTTCACCCTGTGCGCCCTGGTGATCCTGGGTCAGAACTACGAGGCGGTCTTCAAGGGCCAGCTGGTGGAGGTGCTCTCCTCCTACATCGGCCTACCGGTCTTCGGGGCCATCTGGCTGGGGCACCGCCTGGTGACCGGGTCGCGCATGGTGCGCCTGGAGGAGGCCGACGTCTCCGGCGCCGTCGTTCGCGAGCACAGCTGA","VTHSHDESAPSGPAPAASGGWPAADGAGSSDSADPVTSADPVGAGVSSASGQVSNEALEEDGGLHRSLTNRHMQMIAIGGAIGTGLFVASGATVSTAGPGGALVAYAAIGLMVLLLMQSLGEMTAHMPVAGSFQTYATRFVSPSFGFAMGWNYWFNWAITVAAELVAAGIVMGYWLPGVPSWIWAALFLALLTTLNALSARAFGEGEFWLSAIKVVTVIVFLVAGLAMIAGIIGGTSPGFSNWVVKDAPFHGGMLAIVSVFMVAGFSFQGTELVGVAAGEARNPRRDVPKAIHTVFWRIMIFYIGAITVIGFLIAFNDSRLLHTETEDVAYSPFTLVFERAGIGIAAALMNAVILTAVLSAGNSGLYASTRMLHSMALQGQAPAWFSYVNRHGVPVRALGATALVGAAGFLTAVVGQNTAYAWLVNVSALCGFIVWLGIAACHFRFRRAYVLQGNDPADLPYQAPWFPLGPVLAFTLCALVILGQNYEAVFKGQLVEVLSSYIGLPVFGAIWLGHRLVTGSRMVRLEEADVSGAVVREHS$","Lysine-specific permease","Membrane, Cytoplasm, Extracellular","lysine-specific permease PA4628","K03293 amino acid transporter; AAT family","amino acid permease-associated region","","Weber E., Chevallier M.R., Jund R. Evolutionary relationship and secondary structure predictions in four transport proteins of Saccharomyces cerevisiae. J. Mol. Evol. 1988. 27(4):341-350. PMID: 3146645Vandenbol M., Jauniaux J.C., Grenson M. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases. Gene 1989. 83(1):153-159. PMID: 2687114Reizer J., Finley K., Kakuda D., MacLeod C.L., Reizer A., Saier Jr M.H. Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria. Protein Sci. 1993. 2(1):20-30. PMID: 8382989","","","

InterPro
IPR002293
Family

Amino acid/polyamine transporter I
PTHR11785	$\"[60-539]T$	AMINO ACID TRANSPORTER

InterPro
IPR004840
Family

Amino acid permease
PS00218	$\"[97-128]T$	AMINO_ACID_PERMEASE_1

InterPro
IPR004841
Domain

Amino acid permease-associated region
PF00324	$\"[72-528]T$	AA_permease

noIPR
unintegrated

unintegrated
PIRSF006060	$\"[62-535]T$	High-affinity amino acid transporter
PTHR11785:SF23	$\"[60-539]T$	LYSINE-SPECIFIC PERMEASE
tmhmm	$\"[75-95]?$ $\"[101-121]?$ $\"[154-174]?$ $\"[180-200]?$ $\"[215-235]?$ $\"[254-274]?$ $\"[295-315]?$ $\"[341-361]?$ $\"[393-413]?$ $\"[419-439]?$ $\"[464-484]?$ $\"[498-518]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-17]?$	signal-peptide

InterPro
IPR007627
Domain

RNA polymerase sigma-70 region 2
PF04542	$\"[52-120]T$	Sigma70_r2

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[152-206]T$	no description

InterPro
IPR013249
Domain

RNA polymerase sigma factor 70, region 4 type 2
PF08281	$\"[157-210]T$	Sigma70_r4_2

InterPro
IPR014284
Domain

RNA polymerase sigma-70
TIGR02937	$\"[47-214]T$	sigma70-ECF: RNA polymerase sigma factor, s

noIPR
unintegrated

unintegrated
G3DSA:1.10.1740.10	$\"[36-122]T$	no description

","BeTs to 12 clades of COG1595COG name: DNA-directed RNA polymerase specialized sigma subunits, sigma24 homologsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1595 is --------vdrlbcefghsn-j--t-Number of proteins in this genome belonging to this COG is 3","***** IPB000838 (Sigma factor, ECF subfamily) with a combined E-value of 2.1e-29. IPB000838A 76-112 IPB000838B 164-210***** IPB007630 (Sigma-70 region 4) with a combined E-value of 1.2e-11. IPB007630A 70-103 IPB007630B 184-211","","","-47% similar to PDB:1OR7 Crystal Structure of Escherichia coli sigmaE with the Cytoplasmic Domain of its Anti-sigma RseA (E_value = 2.1E_15);","Residues 52 to 120 (E_value = 1.8e-17) place ANA_2695 in the Sigma70_r2 family which is described as Sigma-70 region 2.Residues 157 to 210 (E_value = 3.1e-12) place ANA_2695 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.Residues 163 to 212 (E_value = 9.6e-05) place ANA_2695 in the Sigma70_r4 family which is described as Sigma-70, region 4.","","polymerase sigma factor (SIGMA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2696","2903173","2902526","648","5.14","-4.66","22160","ATGCGTTCAGTTTCAGGTGTCCTCAACCGGACGGCCCTGGCCGGCTGCGGGCTTCTCATCGCGGCGGCGTCATCCTGGGTCCTGGCCTCCGGCCTTAGTGCCGGTCGGTCCTGGCCCGATGCCGCCCCCTACCTGGCCACGGCGCAGGACCGAGTCGGCAGCCTCATCGCAGCCCAGGCGCACTGGCTCCTGCCGGTGGCCGCGCTGGTCTCCGTGCTCGCCGTCATCGCCGGGTTGGTCCTACTCGCCATGCAGATCCCCCGCAAGGCGGCCGCCTCTCCCCTGAGGCTCAGCGACTCCGAGGGAGTCGTCATGGCCACCGTCGCCCCCGAGGTCCTGTCACAGGCCCTGTCCGAGCGGGCCGAGGACGTCCCCGGGGTGGAGCAGTGCGCCGTGTGGGTCACCGGTTCCCCGAGCAGCCTCTGGGTGCAGGCGGACGCCACCGTGTCCCAGGACTGCGAGGTCGCATGGGCCGTGGCGGAGCTCAGGGGCCGGCTCGAGGATGACGTGACCACGTCCCTGGGCACGCGCCCCCGGCAGGTCGACGTCCTGGTGGGGCTGGAGCGCTCCACGAGCAAGCGCAGCGTCTCACAGACCGTCACAGGTCAGCACTCGCCCGAGATCACCGGGAACGGCGATGGTGCGTGA","MRSVSGVLNRTALAGCGLLIAAASSWVLASGLSAGRSWPDAAPYLATAQDRVGSLIAAQAHWLLPVAALVSVLAVIAGLVLLAMQIPRKAAASPLRLSDSEGVVMATVAPEVLSQALSERAEDVPGVEQCAVWVTGSPSSLWVQADATVSQDCEVAWAVAELRGRLEDDVTTSLGTRPRQVDVLVGLERSTSKRSVSQTVTGQHSPEITGNGDGA$","Hypothetical protein","Membrane, Periplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[63-83]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[60-82]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[5-23]?$ $\"[29-49]?$	transmembrane_regions

InterPro
IPR005531
Family

Protein of unknown function DUF322
PF03780	$\"[57-168]T$	DUF322

noIPR
unintegrated

unintegrated
PD532004	$\"[56-164]T$	Q6AAS7_PROAC_Q6AAS7;

","BeTs to 3 clades of COG1302COG name: Uncharacterized BCRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1302 is --------vd-lb----------i--Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 57 to 168 (E_value = 4.4e-21) place ANA_2700 in the DUF322 family which is described as Protein of unknown function (DUF322).","","shock protein 23","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2701","2905521","2905123","399","9.19","3.82","14199","GTGATGATTGACGCTTCCATGGCGTCTATCAGACAGCGTTGTCTCCCGTCTCATAACTGGCTGACACGCTGCCAGGACGTTCATACGTCCGGCTGGAGAAAGTCTCCACCTCATCAGACCTTCTCGGAGGAAGACATCATGCTGCTGTCATTCATCGGAATGATCATCGCCGGCGCCGTGCTCGGCGCCCTCGCCCGCCTCGTCATGCGCGGCGAGCAGAACATCTCGATCCTGTGGACCATCGTGCTGGGCGCCGTGGGCGCACTCGTCGGGGGTGCGATCGCCAGCGTCTTCGGCGTCGCCCACACCAACGGCTTCGACTGGATCCGCTGGGCCCTGTCCCTCGTCGCCGCCATCGTGGCGATCTCCGTCTACCTGGGCGTCACCGGCCGCAAGTAA","VMIDASMASIRQRCLPSHNWLTRCQDVHTSGWRKSPPHQTFSEEDIMLLSFIGMIIAGAVLGALARLVMRGEQNISILWTIVLGAVGALVGGAIASVFGVAHTNGFDWIRWALSLVAAIVAISVYLGVTGRK$","Membrane protein","Membrane, Cytoplasm","probable membrane protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[46-68]?$ $\"[78-98]?$ $\"[108-128]?$	transmembrane_regions

InterPro
IPR003798
Domain

RmuC
PF02646	$\"[74-401]T$	RmuC

noIPR
unintegrated

unintegrated
signalp	$\"[1-20]?$	signal-peptide
tmhmm	$\"[5-27]?$	transmembrane_regions

","BeTs to 8 clades of COG1322COG name: Uncharacterized BCR, YigN familyFunctional Class: SThe phylogenetic pattern of COG1322 is --------e--h------inxNumber of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 217 to 544 (E_value = 1.9e-53) place ANA_2703 in the RmuC family which is described as RmuC family.","","recombination protein rmuC homolog (YIGN)","","1","","","Thu Aug 9 16:09:36 2007","","Thu Aug 9 16:09:36 2007","","","Thu Aug 9 16:09:36 2007","Thu Aug 9 16:09:36 2007","Thu Aug 9 16:09:36 2007","","","","","","Thu Aug 9 16:09:36 2007","Thu Aug 9 16:09:36 2007","","","Thu Aug 9 16:09:36 2007","Thu Aug 9 16:09:36 2007","","","","","yes","","" "ANA_2704","2907125","2908729","1605","10.05","16.36","55917","GTGAGCCTCTTGCGCAGCATCCCGCTGACCAGCCTGAGAACGATCGCGGTCGTGCTGGTCCTTGCCGTTGTGACTACCGTCGTCGCGGCAGTCCTCCTGCCGCGAACTGTTCCGGCCACCGCGGGCGCCTCCAGCGCAGACGAGCCCACCCGACTCACCCGCCCCGCGCTGCGCACGGTGCTGCGGGGCGTCGGCCGCTATACGGCGCGCATCGTCATGGTGGGCGTGCCGGTACTGCTCGTTGTGGTGCTTGGGGGCCTGCTCATCAACCGGCCCATGCACTACGTGCGCACCGTCGGCGACCTTGCGAAGGCCGCTGCCCCTCGCGCCCAGGCCAACTCGCGCATCGAGTCCCCGCCGAAGTCCTCCGCTTTCGGTACCGCCCCGGCCTCGGCCTGGAAGGCATCCTTCCACGACGTCGGCGACGGCTCGCAGGAGGCCACCTGGACCGGTCCGGTCAGCGGCATCACCCTGCCGGTGCGCGTCGTCCTGCCGGCGGGCTACCGGCCCGATGACGGCCGCACCTACAACGTCCTGGTGGGCCTGCACGGCTGGGTCGGCGACCCGCAGTCCCTGGTGACGGGCATCGCCTCACCCCAGCGGCTCCAGGAGGCGATCGACGCTGGCCGTATCCCGCCGTCGATCCTGGTCTTCCCCTCGCTTAACGCGGACGGCGCCAGCCAGCCCGACTGCGTCAACATCAACGGCCGCCCGCCTGTGGGGACCTGGACCGCGGAGGAGATTCCCCGCATGATCCAGGCGACCTTCCCCAACGTCACCACGCAGCGGGCCGGCTGGATGATCATGGGGATCTCGGCGGGCGCCTACTGCGCGGCACGGACCGCCTACGACGTCCCGCAGCGCTTCGGGGCGGTGGGCGTCATGTCCTCCTACGACCTGCCCGGTGAGGGCTCGCTGGCGCACAGCGGCCGGGAGCTCCAGGCGCAGAACGGGCTGTCCACCATGCTGGGAAAGCGTAAGCCCGACGGCATGCGTTTCTACGTCCTGGGGGCCCAGGACGACCCCTACGGCACGGCGCGAACCGCCTGGAGCATGGATGAGGTGGTGCGCAAACCGGACTCGGTGACGGTTGATACCCCGAGCACGGGCGGGCATTCCTGGACCCTGTGGAGCGGCCATTTCCCGTCACTGCTGACGTGGTGGGGCTCGGACCCGGCCGTGTTCACGGCGGCCGGCCTTCCTGCGCCTCAGGGCGATACGAGGGCCAAGGCCACCACCGATGGTGTGAAGCCCCTGTCGGAGACGTCCAAGGACCAGCGCGCGGCGAAGTCGGTCTCCTCGGTGCGTGCCAAGCCCTTCGAGATCAACGGCCTGGGCACGATGATCGTGGCCGTGGTCGTCTCGCTGGGGGCGCTGGGCGTCGTCTTGTTCTGGTCACCCCGCTGGGGCCGACGGCGCGACGGCGGCAGGCCGTCGGCGGCGCGGCTGGGTGGCGCGATCCTGGGGCGCGCCCTGGTGATCGTGGTGGCGGCGGGCCTGGTTGCGGTGACGGTGGGGATCGGGGCCAATGCCAGTGGGGGCTTCTACACCTCGTGGGGTGATCTGTGGGCATCGGTCCGGACGAGCGAGCTCCCCGGGAAGTGA","VSLLRSIPLTSLRTIAVVLVLAVVTTVVAAVLLPRTVPATAGASSADEPTRLTRPALRTVLRGVGRYTARIVMVGVPVLLVVVLGGLLINRPMHYVRTVGDLAKAAAPRAQANSRIESPPKSSAFGTAPASAWKASFHDVGDGSQEATWTGPVSGITLPVRVVLPAGYRPDDGRTYNVLVGLHGWVGDPQSLVTGIASPQRLQEAIDAGRIPPSILVFPSLNADGASQPDCVNINGRPPVGTWTAEEIPRMIQATFPNVTTQRAGWMIMGISAGAYCAARTAYDVPQRFGAVGVMSSYDLPGEGSLAHSGRELQAQNGLSTMLGKRKPDGMRFYVLGAQDDPYGTARTAWSMDEVVRKPDSVTVDTPSTGGHSWTLWSGHFPSLLTWWGSDPAVFTAAGLPAPQGDTRAKATTDGVKPLSETSKDQRAAKSVSSVRAKPFEINGLGTMIVAVVVSLGALGVVLFWSPRWGRRRDGGRPSAARLGGAILGRALVIVVAAGLVAVTVGIGANASGGFYTSWGDLWASVRTSELPGK$","Esterase","Membrane, Extracellular","Putative esterase family","hypothetical protein","putative esterase","","","","","

InterPro
IPR000801
Family

Putative esterase
PF00756	$\"[143-388]T$	Esterase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[146-388]T$	no description
signalp	$\"[1-30]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[71-89]?$ $\"[446-466]?$ $\"[487-509]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 143 to 388 (E_value = 2.7e-05) place ANA_2704 in the Esterase family which is described as Putative esterase.","","esterase family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2705","2908811","2909896","1086","4.62","-26.79","38922","GTGGCACTTACCATCGGAATCGTCGGACTGCCCAATGTCGGCAAATCCACCCTGTTCAATGCTCTGACCCGCGCGACCGTCTTGGCCGCCAACTACCCGTTCGCGACCATTGAGCCGAACGTGGGGGTTGTGCCCCTGCCGGATGCGCGCCTGGACAAGCTCGCCGAGCTGTTCCACTCCGCGAGGGTGGTGCCGGCGACGGTCTCCTTCGTGGACATCGCCGGGATCGTGCGCGGCGCCAGCGAGGGCGAGGGGCTGGGCAACCAGTTCCTGGCCAACATCCGCGAGGCGGACGCCATCTGCATGGTGACGCGCGCCTTCGAGGACCCGGACGTGGTCCACGTGGATGGGAAGGTGGAGCCGGCCGGGGACATTGAGACGATCAGCACCGAGCTGGTGCTGGCGGACATGCAGACCCTGGAGAAGGCGATCCCGCGCCTGGAGAAGGAGGTGCGGGGCAAGAAGACGGAGCCGGTGGTGCTGGAGACGGCGCAGGCGGCCCTCAAGGTCCTGGAGGAGGGGACGCTGCTGTCCGCCGGGGCCGAGGCTGCCGGGATTGATGCGGAGGTGCTCAAGACCTTCCAGCTCATGACCACCAAGCCGTTCATCTATGTGTTCAACATGGACGACGCCGGGATGAGCGACGAGGCCCGCCAGGCCGAGCTGCGCGAGCTGGTGGCGCCGGCGGAGGCGATCTTCCTGGACGCCCAGTTCGAGGCCGAGCTGGTGGAGCTGGAGCCCGAGGAGGCGGCGGAGATGCTGCACGACAATGGGCAGGAGGAGTCCGGCCTGGACAAGCTGGCCCGGGTTGGGTTTGACACGCTGGGACTGCAGACGTATCTGACGGCGGGGGAGAAGGAGTCTCGCGCATGGACGATCCGCAAGGGCGCGACGGCGCCTCAGGCGGCCGGCGTCATTCACACTGATTTTGAGCGAGGCTTTATCAAGGCCGAGATCGTGAGTTACGATGACCTGGTCCAGTACGGCAGCGTTGCCGAAGCCCGCGCTCACGGCCGAGTGCGCATGGAAGGAAAGGACTACGTCATGGCAGACGGTGATGTCGTGGAGTTTAGGTTTAATGTGTGA","VALTIGIVGLPNVGKSTLFNALTRATVLAANYPFATIEPNVGVVPLPDARLDKLAELFHSARVVPATVSFVDIAGIVRGASEGEGLGNQFLANIREADAICMVTRAFEDPDVVHVDGKVEPAGDIETISTELVLADMQTLEKAIPRLEKEVRGKKTEPVVLETAQAALKVLEEGTLLSAGAEAAGIDAEVLKTFQLMTTKPFIYVFNMDDAGMSDEARQAELRELVAPAEAIFLDAQFEAELVELEPEEAAEMLHDNGQEESGLDKLARVGFDTLGLQTYLTAGEKESRAWTIRKGATAPQAAGVIHTDFERGFIKAEIVSYDDLVQYGSVAEARAHGRVRMEGKDYVMADGDVVEFRFNV$","GTP-binding protein YchF","Cytoplasm","GTP-binding protein YchF","GTP-binding protein YchF","GTP-binding protein YchF","","Vernet C., Ribouchon M.T., Chimini G., Pontarotti P. Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm. Genome 1994. 5(2):100-105. PMID: 8180467","","","

InterPro
IPR002917
Domain

GTP-binding protein, HSR1-related
PF01926	$\"[3-210]T$	MMR_HSR1

InterPro
IPR004396
Family

Conserved hypothetical protein 92
TIGR00092	$\"[3-361]T$	TIGR00092: GTP-binding protein YchF

InterPro
IPR006073
Domain

GTP1/OBG
PR00326	$\"[5-25]T$ $\"[26-44]T$ $\"[70-85]T$ $\"[87-105]T$	GTP1OBG

InterPro
IPR012675
Domain

Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30	$\"[277-361]T$	no description

InterPro
IPR013029
Domain

Protein of unknown function DUF933
PF06071	$\"[277-360]T$	DUF933

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[1-276]T$	no description
PTHR23305	$\"[2-361]T$	GTP-BINDING PROTEIN-RELATED
PTHR23305:SF4	$\"[2-361]T$	GTP-BINDING PROTEIN
signalp	$\"[1-29]?$	signal-peptide

","BeTs to 26 clades of COG0012COG name: Predicted GTPaseFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0012 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB013029 (Protein of unknown function DUF933) with a combined E-value of 1.5e-134. IPB013029A 11-64 IPB013029B 69-121 IPB013029C 282-325 IPB013029D 334-360***** IPB006073 (GTP1/OBG GTP-binding protein family signature) with a combined E-value of 1.4e-38. IPB006073A 5-25 IPB006073B 26-44 IPB006073C 70-85 IPB006073D 87-105***** IPB002917 (GTP-binding protein, HSR1-related) with a combined E-value of 6.6e-18. IPB002917 7-39***** IPB003373 (Ferrous iron transport protein B) with a combined E-value of 6.3e-11. IPB003373A 5-35","","","-67% similar to PDB:1JAL YCHF PROTEIN (HI0393) (E_value = 6.6E_96);-62% similar to PDB:2DBY Crystal structure of the GTP-binding protein YchF in complexed with GDP (E_value = 1.3E_88);-62% similar to PDB:2DWQ Thermus thermophilus YchF GTP-binding protein (E_value = 1.3E_88);-57% similar to PDB:2OHF Crystal structure of human OLA1 in complex with AMPPCP (E_value = 4.0E_69);-55% similar to PDB:1NI3 Structure of the Schizosaccharomyces pombe YchF GTPase (E_value = 4.8E_62);","Residues 3 to 210 (E_value = 1.9e-35) place ANA_2705 in the MMR_HSR1 family which is described as GTPase of unknown function.Residues 277 to 360 (E_value = 1.5e-58) place ANA_2705 in the DUF933 family which is described as Protein of unknown function (DUF933).","","protein YchF (ychF)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2705.1","2910077","2911342","1266","5.73","-9.55","46873","ATGGAATCAAACGTCCTCGATGATGTCTTTGGAATTTCACGAGACATTCCTAAGAACTACGTAGTGAGAGAGTCTGTGGATGGTGCATTAGTTAATGCGCTCGCACGAGACAAGCACATTGTTATATATGGATCGTCTAAGCAAGGGAAGACTTGTCTCCGCAAGTATAATTTGCGGAAGGAAGAGCATCTTGTAGTCACATGTTCTAATAAGATGTCGTTGGCTCAGCTTCACAGCGCGATTCTAAAGACAGCCGGATACGTCATTGAGGCAACCTCGACGGCTAGCATAAGTGGCGAACTCAAAGTGGCGGCTAAACTTGGAGGTGGATTTAACTTATTCGGCAATAAAGCTGAAGCGGGAGTCGGCACCGATGGCTCGATAACGACGTCTAGGGAAAATGAATCTCGGCCTCTCGAGCTGGATCCTAGTGATCCGAACGACATCATAATGGCATTGGATGCCGCGGAAAGTCCCAAGTTCATTACGCTGGAAGACTTTCACTATCTTCCGGAAGAAACACAGAACGATTTTGCCATAGCATTAAAAGCGTTTCATGAATCATCAAGATACTCATTCATCATTGTAGGGGTATGGCGCGACCAGAATCGACTCGTTCTTCAAAATGGCGATCTGACTGGAAGAGTTACGTCTATTGATGCCGATAAATGGGACTCGGATGACCTAATGAAAGTAATTCGAGGGGGAGAGGAATTACTCAATGTGACATTTGAAGACAGCTTCAAGGCCGCATTGGTGAGCAACTGCTTCAACAGTGTCTCTATTCTACAAGAGTGTTGCCGAAATGCGTGCGAAAATTCTGGGGTATTCTATACCCAAGAGCAGGTTCGTTGCATTCGTGGGGACGCTAGAGAACTCATTCAAAACGCGGTCGAAGTGAACTCCGCTAGATATTCCGGGTTTATCACCCATTTTGCTTCAGGATTTCAGCACTCAAGTTTGGCTATGTTCAAATGGCTTCTACACTCTGTGCTGATATCCGAAGTAAGTGATCTTGAAAAAGGGCTGGGCTACTCCTCGTTAAAAAAGAAAATCGATGACCATCATCCTGATGCCCCAATCAATCAAGGGAATATCACACAAGCTTTGAAGTCTGTTGTGTCACTACAGGTGAAAAAGAATGTTAAACCGATTGTTCTTGACTACGACGAAACCAACCGTCGCCTCGATGTGGTGGATAGGGGTTTCATGATTTGGCTTCAACACCAGAATCGAGATGAACTTATAACAATGCTTGAAATTTAG","MESNVLDDVFGISRDIPKNYVVRESVDGALVNALARDKHIVIYGSSKQGKTCLRKYNLRKEEHLVVTCSNKMSLAQLHSAILKTAGYVIEATSTASISGELKVAAKLGGGFNLFGNKAEAGVGTDGSITTSRENESRPLELDPSDPNDIIMALDAAESPKFITLEDFHYLPEETQNDFAIALKAFHESSRYSFIIVGVWRDQNRLVLQNGDLTGRVTSIDADKWDSDDLMKVIRGGEELLNVTFEDSFKAALVSNCFNSVSILQECCRNACENSGVFYTQEQVRCIRGDARELIQNAVEVNSARYSGFITHFASGFQHSSLAMFKWLLHSVLISEVSDLEKGLGYSSLKKKIDDHHPDAPINQGNITQALKSVVSLQVKKNVKPIVLDYDETNRRLDVVDRGFMIWLQHQNRDELITMLEI$","Hypothetical protein","Cytoplasm","","","","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","No significant hits to the Pfam 21.0 database.","","","","1","","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:47:00 2007","Fri Aug 10 14:47:00 2007","Fri Aug 10 14:47:00 2007","Fri Aug 10 14:46:13 2007","","","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","Fri Aug 10 14:46:13 2007","","Fri Aug 10 14:46:13 2007","","Fri Aug 10 14:46:13 2007","yes","","" "ANA_2705.2","2913626","2913898","273","5.41","-2.61","9588","GTGGGTGAACACCTTCTCCGCGGAGGTTGTGTGAGCGACGAGCAGATCCAGGCCTGGGCTGACGAAGCTGAGGCCGGCTACGACCTTCAGCAGCTTCCCCGTCCGATTCCTGGGCGGCCCCCAGTCGGGCGAGGGCCCGGCTCAGTTGTGACTGTCCGACTCGACGAGGAGCTTCTCGCCGCGTTGCTGAAGCGCGCCGCGGATGAGGGCATTACGAACCGGTCGGAGGCCGTGCGAGCTGCTGTCAAGCAATGGGCTCATGTCGCTGCCTGA","VGEHLLRGGCVSDEQIQAWADEAEAGYDLQQLPRPIPGRPPVGRGPGSVVTVRLDEELLAALLKRAADEGITNRSEAVRAAVKQWAHVAA$","Hypothetical protein","Cytoplasm","","","","","","","","

InterPro
IPR002145
Domain

CopG-like DNA-binding
PF01402	$\"[49-86]T$	RHH_1

","No hits to the COGs database.","No significant hits to the Blocks database.","No significant hits to the ProDom database.","","","Residues 49 to 88 (E_value = 3.4e-06) place ANA_2705.2 in the RHH_1 family which is described as Ribbon-helix-helix protein, copG family.","","","","1","","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:57 2007","Fri Aug 10 15:00:57 2007","Fri Aug 10 15:00:57 2007","Fri Aug 10 15:00:45 2007","","","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","Fri Aug 10 15:00:45 2007","","Fri Aug 10 15:00:45 2007","","Fri Aug 10 15:00:45 2007","yes","","" "ANA_2706","2914051","2914443","393","10.98","7.65","14333","TTGCCGGAGACGTTGCCCTCTCGAAGCTCGCTGAACCATACGACCAGCAGCATCGCCACAACTCTCAGTTTGGGCTACTATGGTCGTCATAGTGAACGGGGGAACATGTCAGGCTACAGGATCGACCGTCAGGTGACGGAGTTCGGAGAGCACGTGCGCGGATGGCGCATGGTGCTCGGCCTGACCGCGCAGCAGGTCTCCGAGCGAGCGGGCATCACCCGTGACACCCTGCGCAAGATCGAGTCGGGCAACCCCAGCGTCAGCTTCAACAGCGTCACCCAGGTGCTGCGCGCCCTGGGCATCCTCGACCAGCTTGTCGACGCAGCTGATCCGCTGGCCAGCGACATCGGCCGCCTCCGCGCTGGCCGCCTCACCAGAAAGCGCGCCCGATGA","LPETLPSRSSLNHTTSSIATTLSLGYYGRHSERGNMSGYRIDRQVTEFGEHVRGWRMVLGLTAQQVSERAGITRDTLRKIESGNPSVSFNSVTQVLRALGILDQLVDAADPLASDIGRLRAGRLTRKRAR$","Transcriptional regulator; XRE family","Periplasm, Membrane, Cytoplasm","Helix-turn-helix domain protein","transcriptional regulator; XRE family","helix-turn-helix domain protein","","","","","

InterPro
IPR001387
Domain

Helix-turn-helix type 3
PF01381	$\"[52-106]T$	HTH_3
SM00530	$\"[51-106]T$	HTH_XRE
PS50943	$\"[52-105]T$	HTH_CROC1

noIPR
unintegrated

unintegrated
G3DSA:1.10.260.40	$\"[48-101]T$	no description

","BeTs to 10 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 5","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 52 to 106 (E_value = 6.1e-06) place ANA_2706 in the HTH_3 family which is described as Helix-turn-helix.","","domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2707","2914572","2915684","1113","5.56","-8.28","40649","ATGAACATCGACCCAGCCCTGAGCCTGGTGCCCGGCGCTCAATATCAGTCTGGGCTCATTGGAGCCTTTGCTGACAGCGCGCCTGACCGCTGGGGCCGCAACCTCATCCGCAAGGCCGAACGATCACGAGCCCGCGAAGAGGGACGCGTGCCCCGTCAGCTGGACGACCTCGACTTCCTCCTCGGCGTCAGCGACGACACCCGACAGGGCGCCCTACGCTTCCGGGCCCCCGGGATCGACGAGTTCCTGGGAGAGCCCTCGCGCGTTCCGCGCCTCGTCGCTCTGCCTGAGCTTCTGCACGCCAGCGACGAACTGGCTTCCGATGATGACCCCTCCGGCGCCGTCAAACGACTTCTCGACACAGGCACGACGGGCCTGGGCGGTGCGCGCCCCAAAGCCTCAGTCCGGCTCGATGACGGCGGCCTCGCCATTGCGAAGTTCCCTCACTCCAGCGACTCCTGGGACGTCATGGCCTGGGAGGCCACTGCTCTCGACCTCCTTGAGACCGCGGGCGTTCGCACACCCCAGCACCAGCTCACCCAGGTGGGCAGTCGCAGCATCCTCATCCTGCGGAGATTCGACAGAACCCGTGATGGTGCGCGTATCGGCTATATCAGTGCCATGACGGCCACTGGATCGTCCGACGGAGACCAGAAGGACTACGACGACCTCGCCGAGGCGATTCGCGATCTCTCTCGCTCGCCCGTCCAAGACCTCCATGAGTTCTACGACCGAATCATCGCGAGCATCGCCCTCGGCAACACGGACGACCACCTGCGCAACCACGGGTTCCTCGCCGACCGTGGGCTCTGGAGACTCAGCCCTGTCTTCGACGTCAACCCGAACCCCGACCCCAGTCGGCCCCGAGCGACGTCGATCATGGGAGCAGACGCGATGCCCGACGAGATCGACGGGCTCCTGGCTATCGCAAACGACTACCGGCTCACTCAATCGGAGGCGCGGGAGCGAATCAGACGCATCACTGCGTCCCTGTCAGGATGGCGGGGCCAGGCGCGGGCGAACCGAGTCCCCGAGCGTGAGATCACCATGATGTCCGAGTCCATCGAGCCTCGCCTGGAAGCCCTCACCCGAGCCGCACACGCCAAGGATTGA","MNIDPALSLVPGAQYQSGLIGAFADSAPDRWGRNLIRKAERSRAREEGRVPRQLDDLDFLLGVSDDTRQGALRFRAPGIDEFLGEPSRVPRLVALPELLHASDELASDDDPSGAVKRLLDTGTTGLGGARPKASVRLDDGGLAIAKFPHSSDSWDVMAWEATALDLLETAGVRTPQHQLTQVGSRSILILRRFDRTRDGARIGYISAMTATGSSDGDQKDYDDLAEAIRDLSRSPVQDLHEFYDRIIASIALGNTDDHLRNHGFLADRGLWRLSPVFDVNPNPDPSRPRATSIMGADAMPDEIDGLLAIANDYRLTQSEARERIRRITASLSGWRGQARANRVPEREITMMSESIEPRLEALTRAAHAKD$","HipA domain protein","Cytoplasm, Periplasm","conserved hypothetical protein","hypothetical protein","HipA domain protein","","Black D.S., Kelly A.J., Mardis M.J., Moyed H.S. Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J. Bacteriol. 1991. 173(18):5732-5739. PMID: 1715862Black D.S., Irwin B., Moyed H.S. Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J. Bacteriol. 1994. 176(13):4081-4091. PMID: 8021189","","","

InterPro
IPR012893
Domain

HipA-like, C-terminal
PF07804	$\"[201-278]T$	HipA_C

InterPro
IPR012894
Domain

HipA-like, N-terminal
PF07805	$\"[125-195]T$	HipA_N

","BeTs to 3 clades of COG3550COG name: Uncharacterized protein related to capsule biosynthesis enzymesFunctional Class: R [General function prediction only]The phylogenetic pattern of COG3550 is --------------e--h-n-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 125 to 195 (E_value = 2.8e-17) place ANA_2707 in the HipA_N family which is described as HipA-like N-terminal domain.Residues 201 to 278 (E_value = 1.3e-26) place ANA_2707 in the HipA_C family which is described as HipA-like C-terminal domain.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2708","2915873","2917477","1605","6.81","-0.95","56596","ATGACCATCGAGATGATCGTCGCCCTCATCGGCGCCTCTGTTGTCGCCTACGCGATCGCCAACAGGTTCCGACTCATCGCCCCAGTGCTTCTCATCGTCGCCGGCGTGGGAGTCGCGCTGCTCCCGGTGGGGGAGGAGATGTACCTGCCCAGCACCGTGGTGCTCACGATCTTCCTGCCGATCCTCCTGTACTGGGAGTCCCTGTCCGTCTCCCTCAACCGCATGCGGCGAAGCCTGCGCGGTATCATCCTCAGCGCCACGGTCCTCGTCGCCATCACAGCCGCCCTCATCACCCTCATCGGCGTCCTCATGGGGCTGAGTGTGGGAGCCGCTCTCCTCATCGGAGCCTGCCTCGGCCCCACCGACGCCACCGCCGTCTCCAGCCTAGGACGCGGCATCAACCCCAACAGCCGCACCATCCTCCAAGCCGAGTCACTACTCAACGACGGCACCGCCCTGGTCATCTTCGCCATCGCCCTCCAAGCCGCGCAGGACTCCTCCGGCGTCACCTTTGGCCTCATCACCCATCAGCTCCTCCTGTCCTTCGGGGGAGGAATCGGTGCAGGAGTCCTCGTCGGTGCGGCAGTCACGAAGATCGGCATCCGCATCCGCACCATCACCGACGACCCCATGCTGGCGACGATCACCGCCCTGGCCACCCCGTTCCTCGCCTTCTTCATCGCCGAGGAGATCGGCGGCTCGGGCGTGCTCGCCGTCGTCACCTGCGGAATCGTCATCTCCCGCTTCGCCGCCCCGCACATGTCCCTGGGCTCGCGAGTCCTCGGCATCCCCTTCTGGACGATCCTCACCCACATCCTCAACACCATCCTCTTCGTCATGGTGGGAGTGGCACTCCCCGGCATCGTCGCCGAGCTCCCTCACGCCGACCTCGTGCGCGGCCTCATCCTCATCCCCATCATCTACATCGCCATGGTCGCGGGAAGGTTCGCAGGCCAACACCTCATCATCTACTCCATCCGCGCCCTCGACCGCCGCCCCGAGCAGCGCCTGCGCCGCACCAATTTCCGCGGCCGCATCGTCTCCACGGTCGCAGGCTTCCGCGGCGCGATCTCACTGGCGATGGCACTGTCCATCCCCGTCTCCTTCGACGGCGCCGCCTACACCGAGCGCAACCTCATCATCCTCGTCGTCGCCGGCGCGACCCTCCTGTCGCTCCTCATCCAAGGGATCGCCCTGCCCTACGTGGTCCGCTGGGCCAACGCCAGGCCCTCGGCCGGCACGCAGGCCGCCGAGTGCGTCGAGTCGCAGGAGACCGACGCCCTCGCCGAGATCCTCGCCGACACCATCAGTCAGCTCGATGCCATCGCTAAACGAACGGGCGTTGACGACGACGAAGCCATCGAGGCGGTGCGCCTCGACTATGCACGTCGTCACCAGTCCGTGCTCAACTCGGCCACAGAGAGCGAGGCCGATGTGTACTGCGGCCCGGAAAGCGCCCTGCGGCTCGCCGTCATCGAGCACCTGCGCGAGCGCGTACACGGCCTGCGCTTCTCCGGCCGCATCGACGACTCCACCGCCTCGCGAGTCAACCGACGGTTCGACGTCGAGACCCTCCACATCAACGGCCCCCTCGACGTCGAGTAA","MTIEMIVALIGASVVAYAIANRFRLIAPVLLIVAGVGVALLPVGEEMYLPSTVVLTIFLPILLYWESLSVSLNRMRRSLRGIILSATVLVAITAALITLIGVLMGLSVGAALLIGACLGPTDATAVSSLGRGINPNSRTILQAESLLNDGTALVIFAIALQAAQDSSGVTFGLITHQLLLSFGGGIGAGVLVGAAVTKIGIRIRTITDDPMLATITALATPFLAFFIAEEIGGSGVLAVVTCGIVISRFAAPHMSLGSRVLGIPFWTILTHILNTILFVMVGVALPGIVAELPHADLVRGLILIPIIYIAMVAGRFAGQHLIIYSIRALDRRPEQRLRRTNFRGRIVSTVAGFRGAISLAMALSIPVSFDGAAYTERNLIILVVAGATLLSLLIQGIALPYVVRWANARPSAGTQAAECVESQETDALAEILADTISQLDAIAKRTGVDDDEAIEAVRLDYARRHQSVLNSATESEADVYCGPESALRLAVIEHLRERVHGLRFSGRIDDSTASRVNRRFDVETLHINGPLDVE$","Na+/H+ antiporter","Membrane, Cytoplasm","Putative Na(+)/H(+) exchangerRv2287/MT2345/Mb2309, putative","K03316 monovalent cation:H+ antiporter; CPA1 family","Na+/H+ antiporter","","Orlowski J., Grinstein S. Na+/H+ exchangers of mammalian cells. J. Biol. Chem. 1997. 272(36):22373-22376. PMID: 9278382Numata M., Petrecca K., Lake N., Orlowski J. Identification of a mitochondrial Na+/H+ exchanger. J. Biol. Chem. 1998. 273(12):6951-6959. PMID: 9507001Dibrov P., Fliegel L. Comparative molecular analysis of Na+/H+ exchangers: a unified model for Na+/H+ antiport?. FEBS Lett. 1998. 424(1):1-5. PMID: 9537504","","","

InterPro
IPR004705
Family

Bacterial Na+/H+ antiporter
PTHR10110:SF1	$\"[27-404]T$	SODIUM/HYDROGEN EXCHANGER YJCE
TIGR00831	$\"[5-532]T$	a_cpa1: Na+/H+ antiporter

InterPro
IPR006153
Family

Sodium/hydrogen exchanger
PF00999	$\"[6-405]T$	Na_H_Exchanger

noIPR
unintegrated

unintegrated
PTHR10110	$\"[27-404]T$	SODIUM/HYDROGEN EXCHANGER
signalp	$\"[1-39]?$	signal-peptide
tmhmm	$\"[25-43]?$ $\"[47-67]?$ $\"[82-102]?$ $\"[108-130]?$ $\"[151-171]?$ $\"[177-195]?$ $\"[210-228]?$ $\"[234-252]?$ $\"[272-290]?$ $\"[304-324]?$ $\"[345-365]?$ $\"[379-399]?$	transmembrane_regions

","BeTs to 14 clades of COG0025COG name: NhaP-type Na+/H+ and K+/H+ antiportersFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0025 is aompk-y--drlbcefghs--j----Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 6 to 405 (E_value = 1.1e-44) place ANA_2708 in the Na_H_Exchanger family which is described as Sodium/hydrogen exchanger family.","","Na(+)-H(+) exchanger Rv2287-MT2345-Mb2309, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2709","2920708","2918003","2706","6.17","-10.32","92791","ATGACATCGCACAGTCCTTTTTCCCGGAGGCGCCTGCCGGCCCTCCTGGGCTCCCTGCCTCTGGCCGCCACCGGCCTGATCGCCGCCGCGCCCCCGGCGCTCGCCGTCCCCACCTCTGACGGCCTGGCCGACGTCACCATCACGCAGGTGAACGCGCCTGCGGACGGCCTCTACTCCGTCGGCGATGTCATGACCTTCAACATCACTCTCACCAACACCAGCGGTGAGGCCCACTCCTACGCGCCGGCCTCGACGAACCTGTCCGGGAACGTCTCCAAGTGCCGGTGGCGCAACGTCCCGGCCGGGACGACCAAGACCGACTGCACCGGCCTGGCCACGCACACGGTGACCGCCGAGGACCTCAAGGCCGGCGGCTTCACCCCGCAGATCGCCTACGAGGTCAAGGCCGTGGAGTACGCCGGGAAGGCCCTGAGCACCCCGGAGACGATCAAGGGCGCAACGAGCCCGGTCAAGGCCAACTCGCTGCGGGTCGAGTCGATCACGCCGTCGTCGAGCCAGGAGAACTACAAGCTGGGCGACACCGTCACCTACACGGTGCGCGTGCGCTCGGTGTCGGACAAGACGATCAACGTCGCCGCCACCGAGTCCTCCTTCGACGACCTGGGCCGCCAGTGCCACTGGGGCGGCCTCAAGCCGGGCAAGGGCGCCGTCTACAACTGCAAGCCGCTCACCCACACGATCACGCAAGCCGACGTCGACGCCGGCCGCTGGACGCCGTCGATCACCCTGACGGCCACCGGCACCGACGGCGCCGCCCTCCAGACGCTCACCGCCACCGGCAACCCGATCAACGTCGTCGGCGACCACCCGCAGGCCACGCCCGCGCCGGCGCCCGACGCGAGCACGGAACTGCCGGCCTCGATGAGCCAGGCCCAGCACCTGGCCCCCAACACGGCCACCGACAACTACCGCATCCCGGCGATCACCACCGCCCCCAACGGGGACCTGCTCATCTCCTACGACGAGCGCCCGAAGGACAACGGCAACGGCGGCAGCGACGCCCCCAACCCGAACCACATCGTCCAGCGCCGCTCCACCGACGGCGGCAAGACCTGGTCGGCGCCCACTTACATCCACCAGGGCACGGAGACCGGCAAGAAGGTCGGCTACTCCGACCCGAGCTACGTCGTCGATCACCAGACGGGCACGATCTTCAACTTCCACGTCAAGTCCTACGACCAGGGCTGGGGCGGCTCACAGGCCGGCACCGATCCGGACAACCGGGGCATCATCCAGGCCGAGGTGTCGACCTCCACGGACAACGGCTGGACCTGGACGCACCGCACCATCACCGCGGACATCACGAAGGACAAGCCGTGGACCGCGCGTTTCGCGGCCTCGGGCCAGGGCATCCAGATTCAGCACGGGCCCCACGCCGGGCGCCTCGTGCAGCAGTACACGATCAGGACCGCCGGCGGCGCGGTGCAGGCCGTCTCGGTCTACTCCGACGACCACGGGAAGACGTGGCAGGCCGGCACGCCGATCGGGACCGGCATGGATGAGAACAAGGTCGTTGAGCTCTCCGACGGCTCCCTCATGCTCAACTCGCGCGCCTCGGACGGCTCCGGCTTCCGCAAGGTGGCTCACTCCACCGACGGCGGGCAGACCTGGAGCGAGCCGGTGTCCGACAAGAACCTGCCCGACTCGGTGGACAACGCCCAGATCATTCGGGCCTTCCCGAACGCCGCGCCGGACGACCCGCGCGCCAAGGTGCTGCTGCTGAGCCACTCGCCGAACCCGCGGCCGTGGTCGCGTGACCACGGCACCATCTCGATGTCCTGCGACGACGGCGCCTCCTGGACGACCAGCAAGGTCTTCCACGAGCCCTTCGTCGGCTACACGACGATCGCGGTGCAGTCCGACGGCAGCATCGGGCTGCTCAGCGAGGACGCCCACAACGGCGCCGACTACGGCGGCATCTGGTACCGCAACTTCACGATGAACTGGCTCGGCGAGCAGTGCGGCCAGAAGCCGGCGGAGCCGAGCCCGGCGCCGTCGCCGACGGCGGCACCCTCAGCGGCACCGATGGAGAAGCCGGCCCCGTCGGCCGCGCCGAGCGCCGAGCCCACGCAGGCACCGGCACCATCCTCCGCGTCTGAGCCGAGTGCTGCGCCCGAGCCGAGCAGCGCCCCGGCGCCGGAGCCCACGACCGCTCCGAGCACGGAGCCCACACCGGCTCCTGCGCCCAGCTCCGCACCTGAGCAGACCGATGGGCCGACTGCTGCGCCCGCACCGGAGACGTCCTCTGCACCGGCCGCCGAACCGACGCAGGCCCCGACGGTGGCGCCTTCGGCTGAGCCCACGCAGGCGCCGAGTGCGCAGCCGAGCTCAGCACCCAAGCCGGGGGCGACGGGTCGGGCCCCGTCGGTGGTGAACCCGAAGGCGACCGCGGCGGCGACGGAGCCTGGGAAGCCGTCATCGAGCGCAAGCCCGGCACCGAGCCGGAGCGCGGCGGCGACGCCGAAGCCGGGCATGGAGCCCGATGAGATTGATCGGCCGTCTGACGGCACCATGGCGCAGCCGACCGGTGGCGCCAGCGCGCCGAGCGCCGCGCCGACGCAGGCGGCGAAGGCCGGCAGCAGGCTGTCTCGCACGGGGACCAACGCGCTGCTGGTCCTGGGCCTTGCGGGTGTCGCGGTTGTCGGTGGGTACCTGCTGCTGCGGGCTCGCCGTTCGAAGAACTGA","MTSHSPFSRRRLPALLGSLPLAATGLIAAAPPALAVPTSDGLADVTITQVNAPADGLYSVGDVMTFNITLTNTSGEAHSYAPASTNLSGNVSKCRWRNVPAGTTKTDCTGLATHTVTAEDLKAGGFTPQIAYEVKAVEYAGKALSTPETIKGATSPVKANSLRVESITPSSSQENYKLGDTVTYTVRVRSVSDKTINVAATESSFDDLGRQCHWGGLKPGKGAVYNCKPLTHTITQADVDAGRWTPSITLTATGTDGAALQTLTATGNPINVVGDHPQATPAPAPDASTELPASMSQAQHLAPNTATDNYRIPAITTAPNGDLLISYDERPKDNGNGGSDAPNPNHIVQRRSTDGGKTWSAPTYIHQGTETGKKVGYSDPSYVVDHQTGTIFNFHVKSYDQGWGGSQAGTDPDNRGIIQAEVSTSTDNGWTWTHRTITADITKDKPWTARFAASGQGIQIQHGPHAGRLVQQYTIRTAGGAVQAVSVYSDDHGKTWQAGTPIGTGMDENKVVELSDGSLMLNSRASDGSGFRKVAHSTDGGQTWSEPVSDKNLPDSVDNAQIIRAFPNAAPDDPRAKVLLLSHSPNPRPWSRDHGTISMSCDDGASWTTSKVFHEPFVGYTTIAVQSDGSIGLLSEDAHNGADYGGIWYRNFTMNWLGEQCGQKPAEPSPAPSPTAAPSAAPMEKPAPSAAPSAEPTQAPAPSSASEPSAAPEPSSAPAPEPTTAPSTEPTPAPAPSSAPEQTDGPTAAPAPETSSAPAAEPTQAPTVAPSAEPTQAPSAQPSSAPKPGATGRAPSVVNPKATAAATEPGKPSSSASPAPSRSAAATPKPGMEPDEIDRPSDGTMAQPTGGASAPSAAPTQAAKAGSRLSRTGTNALLVLGLAGVAVVGGYLLLRARRSKN$","Exo-alpha-sialidase","Extracellular, Periplasm","sialidase","exo-alpha-sialidase ","Exo-alpha-sialidase","","Copley R.R., Russell R.B., Ponting C.P. Sialidase-like Asp-boxes: sequence-similar structures within different protein folds. Protein Sci. 2001. 10(2):285-292. PMID: 11266614","","","

InterPro
IPR002860
Repeat

Glycoside hydrolase, BNR repeat
PF02012	$\"[350-361]T$ $\"[423-434]T$ $\"[487-498]T$ $\"[535-546]T$ $\"[598-609]T$	BNR

InterPro
IPR006970
Repeat

PT repeat
PF04886	$\"[673-710]T$ $\"[753-788]T$	PT

noIPR
unintegrated

unintegrated
G3DSA:2.120.10.10	$\"[290-638]T$	no description
PTHR10628	$\"[422-636]T$	SIALIDASE
PTHR10628:SF9	$\"[422-636]T$	SIALIDASE 1
signalp	$\"[1-35]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[876-894]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB004124 (Glycoside hydrolase, family 33, N-terminal) with a combined E-value of 2.4e-12. IPB004124A 308-336 IPB004124E 488-500 IPB004124F 529-558","","","-69% similar to PDB:1EUR SIALIDASE (E_value = 1.4E_111);-69% similar to PDB:1EUS SIALIDASE COMPLEXED WITH 2-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID (E_value = 1.4E_111);-69% similar to PDB:1EUT SIALIDASE, LARGE 68KD FORM, COMPLEXED WITH GALACTOSE (E_value = 1.4E_111);-69% similar to PDB:1EUU SIALIDASE OR NEURAMINIDASE, LARGE 68KD FORM (E_value = 1.4E_111);-69% similar to PDB:1WCQ MUTAGENESIS OF THE NUCLEOPHILIC TYROSINE IN A BACTERIAL SIALIDASE TO PHENYLALANINE. (E_value = 4.2E_111);","Residues 350 to 361 (E_value = 0.01) place ANA_2709 in the BNR family which is described as BNR/Asp-box repeat.Residues 423 to 434 (E_value = 434) place ANA_2709 in the BNR family which is described as BNR/Asp-box repeat.Residues 487 to 498 (E_value = 0.017) place ANA_2709 in the BNR family which is described as BNR/Asp-box repeat.Residues 535 to 546 (E_value = 0.022) place ANA_2709 in the BNR family which is described as BNR/Asp-box repeat.Residues 598 to 609 (E_value = 609) place ANA_2709 in the BNR family which is described as BNR/Asp-box repeat.Residues 673 to 710 (E_value = 0.037) place ANA_2709 in the PT family which is described as PT repeat.Residues 753 to 788 (E_value = 2e-09) place ANA_2709 in the PT family which is described as PT repeat.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2710","2922192","2920972","1221","5.44","-15.19","43221","ATGAGTGCGACCACGTCCTCCTCCTACCCCGTCTCCAGCGGCAGTACCGAGACCGAGCCGGCCGCCTTCGGCGTCGGAACAGCCTCCTCCAAGCTGGTGGACCGCAAGGCCGGCTCCCCCACGGGCGCCTGGCGGCCCGGCGACGAGCCGGGGCACCGCCGGTTCCTGGAGATCGGGGACCTGCCCCTGGAGTCCGGGGAGGTCCTGCCCAACACGGTCCTGGCCTTCGAGACCTGGGGGGAGCTGAGCCCACAGCGCGACAACGCGGTTCTCGTGCTGCATGCCCTGACCGGCGACTCCCACGTCACCGGCGAGGCGGGGCCCGGGCACCCGACGCCGGGCTGGTGGTCGGACCTGGTGGGGCCCGGGCGGGCCATCGACACCGAGCGCTACTTCGTGGTGGCCGCCAACATCCTGGGCGGCTGCCAGGGCTCGACGGGGCCGTCGTCGACGGCGCCGGACGGGCGCCCCTGGGGGTCGCGCTTCCCGTGGCTGACCACGCGCGACGCCGTCGAGGCCGAGGCGCGCCTGGCCGACGCCCTGGGGATCGAGGTCTTCCACCTGGTCATCGGGGCCTCGCTGGGCGGGCACCGAGCCGTCGAGTGGGGGGTCACGCATCCGCAGCGGGTGCGCAACCTGGCGCTGGTAGCCACGGGCGCCTCGACGACCGCCGACCAGCTGGCCTGGTGCCACCTGCAGGAACTGGCGATCGTGGCCGATCCCTTCTTCTTCGACGGCGACTACTACTCCCACTCGGTGGGGCCGGTGCGGGGGCTGGGGCTGGCGCGGGCGCTGGCGCACACGACCTACCGCAGTGCCGCCGAGCTCGATGAGCGCTTCGGGCGGCGCCACCAGGGCGAGGAGGACCCAGCGGTGGGCGGGCGCTACCAGGTGGAGTCCTACCTGGACTACCACGCCGGCAAGCTGCTGGCGCGCTTCGACGCCAACACCTACCTCATCGTCACCCACTCGATGATGGTGCACGACGTCGGCACGGGGCGCGGCGGCATCGAGGCGGCGCTGGCGCGGGTGCAGGCGCGCACGCTCGTGGTGGACGTGGACTCCGACCGGCTCTTCTTGCCCGCCCAGGCCGAGGAGCTGGCCGGCGGCATCCCGGGCGCGAGGCGCGAGACCATCAGCTCCCTGCACGGGCACGACGGCTTTCTCATCGAGGCCGAGCAGATGGACGCGATCCTGCGCGACTTCCTGGCCGGCGCATAG","MSATTSSSYPVSSGSTETEPAAFGVGTASSKLVDRKAGSPTGAWRPGDEPGHRRFLEIGDLPLESGEVLPNTVLAFETWGELSPQRDNAVLVLHALTGDSHVTGEAGPGHPTPGWWSDLVGPGRAIDTERYFVVAANILGGCQGSTGPSSTAPDGRPWGSRFPWLTTRDAVEAEARLADALGIEVFHLVIGASLGGHRAVEWGVTHPQRVRNLALVATGASTTADQLAWCHLQELAIVADPFFFDGDYYSHSVGPVRGLGLARALAHTTYRSAAELDERFGRRHQGEEDPAVGGRYQVESYLDYHAGKLLARFDANTYLIVTHSMMVHDVGTGRGGIEAALARVQARTLVVDVDSDRLFLPAQAEELAGGIPGARRETISSLHGHDGFLIEAEQMDAILRDFLAGA$","Homoserine O-acetyltransferase","Cytoplasm","homoserine O-acetyltransferase","homoserine O-acetyltransferase ","homoserine O-acetyltransferase","","Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992. 5(3):197-211. PMID: 1409539","","","

InterPro
IPR000073
Domain

Alpha/beta hydrolase fold-1
PF00561	$\"[131-401]T$	Abhydrolase_1

InterPro
IPR006296
Family

Homoserine O-acetyltransferase
TIGR01392	$\"[57-404]T$	homoserO_Ac_trn: homoserine O-acetyltransfe

InterPro
IPR008220
Family

Homoserine acetyltransferase
PIRSF000443	$\"[30-406]T$	Homoserine acetyltransferase

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1820	$\"[70-403]T$	no description

","BeTs to 10 clades of COG2021COG name: Homoserine acetyltransferaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2021 is -om---y--dr----f-hsn-j----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-58% similar to PDB:2B61 Crystal Structure of Homoserine Transacetylase (E_value = 1.6E_61);","Residues 131 to 401 (E_value = 3e-08) place ANA_2710 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold.","","O-acetyltransferase (metX)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2711","2923673","2922204","1470","5.17","-17.64","50737","GTGACGCTGACATCGCCGCCGGCCACCGGAAACCACCAAGGAATCCTCATGACCGACCAGCACCCCACCGCCCCCCAGGCCGCCCCCCAGAGCGGGGAGCCGATCCCCTCCCCCACCAGCCCGGCGGGCTGGCGCTTCGAGACCAAGCAGGTCCAGGCCGGGCACGACCCGATGTCCGAGCCCGCCCACGCCCGGGCCATCCCGATCTACCAGACCTCCTCCTACGTCTTCGAGTCGGCCGAGCAGGCGGCCGCCCGCTTCGCCCTGACCGACCTGGGCCCGATCTACACGCGCCTGACCAACCCCACCAATGACATCGTCGAGCAGCGGATCGCGGCCCTGGAGGGCGGCGTCGGGGCGCTGCTGACGTCGTCGGGCCAGGCAGCCACGACCCTGGCCCTGGTGACGCTGGGCGGGGCGGGCGACAACATCGTGGCCTCGCCCTCCCTGTACGGCGGGACCACGAACCTGCTCACCCACACCCTGCCGCGCCTGGGCATCGAGGCGCGCTTCGTGGACGAGCCGGGCGACCCGGCGGCCTGGGCGGCGCTGGCCGATGAGCGCACCGTCGCCTTCTTCGGGGAGTCGATCCCCAACCCGCGCGGCGACATCCTCGACATCGAGGCGATCTCGGCGGCCGCGCACGAGCTGGGCATCCCGCTGATCGTGGACAACACCGTGGCCTCACCCTTCCTGACCCGCCCCTTCGAGTGGGGCGCGGACATCGTGGTGGCCTCGGCGACGAAGTTCCTGGGCGGGCACGGCTCCTCCGTGGCGGGCGTGATCGTGGACTCCGGCAGCTTCGACTTCGCGGCCCAGCCCGAGCGCTTCCCGGGCTTCAACACGCCCGACGAGTCCTACCACGGCCTGGTCTACGCCCGGGACCTGGGGGTGGGCAGCCCGCTGGGCGCGAACCTGGCCTTCATCCTCAAGGCGCGCGCCGAGGGCCAGCGCGACCTCGGCTTCGCGCTGGCGCCGCACTCGGCCTTCCTCATCGCCCAGGGCATCGAGACGCTCTCGCTGCGCATGGAGCGGCACGTGGACAACGCCCTGGCGGTGGCCACCTGGCTGAAGGGGCGCGACGACGTCGCCTCGGTGCGCTACTCGGGGCTGGCCTCCAGCCCCTACTACGAGCGGCACCGCAAGTACTGTCCGCGCGGGGCGGGCTCGATCCTCACCTTCGACCTGGCCGGTGGGCGTGAGGCCGGGGCGGCCTTCATTGACTCCCTGAGTCTGTTCTCCAACCTGGCCAATATCGGGGACGTGCGCTCGCTGGCGATCCACCCGGCCACCACGACGCACTCCCAGCTCGACGACGCCGGCCTGGCCGCGGCCGGGATCAGCGCCGGGACCGTGCGCCTGAGCGTGGGGATCGAGCACATCGACGACATCCTGGCCGACCTCGAGCGCGGCCTGGCGGCGGCCCGGGCCGTCGGGGCGGGCGAGCCGAGCGCGGCGGCCGGGGCCTGA","VTLTSPPATGNHQGILMTDQHPTAPQAAPQSGEPIPSPTSPAGWRFETKQVQAGHDPMSEPAHARAIPIYQTSSYVFESAEQAAARFALTDLGPIYTRLTNPTNDIVEQRIAALEGGVGALLTSSGQAATTLALVTLGGAGDNIVASPSLYGGTTNLLTHTLPRLGIEARFVDEPGDPAAWAALADERTVAFFGESIPNPRGDILDIEAISAAAHELGIPLIVDNTVASPFLTRPFEWGADIVVASATKFLGGHGSSVAGVIVDSGSFDFAAQPERFPGFNTPDESYHGLVYARDLGVGSPLGANLAFILKARAEGQRDLGFALAPHSAFLIAQGIETLSLRMERHVDNALAVATWLKGRDDVASVRYSGLASSPYYERHRKYCPRGAGSILTFDLAGGREAGAAFIDSLSLFSNLANIGDVRSLAIHPATTTHSQLDDAGLAAAGISAGTVRLSVGIEHIDDILADLERGLAAARAVGAGEPSAAAGA$","O-acetylhomoserine/O-acetylserine sulfhydrylase","Cytoplasm, Extracellular","Shy10","O-acetylhomoserine/O-acetylserine sulfhydrylase ","O-acetylhomoserine/O-acetylserine sulfhydrylase","","","","","

InterPro
IPR000277
Family

Cys/Met metabolism pyridoxal-phosphate-dependent enzymes
PTHR11808	$\"[134-268]T$ $\"[311-475]T$	TRANS-SULFURATION ENZYME FAMILY MEMBER
PF01053	$\"[47-473]T$	Cys_Met_Meta_PP
PS00868	$\"[241-255]T$	CYS_MET_METAB_PP

InterPro
IPR006235
Family

O-acetylhomoserine/O-acetylserine sulfhydrylase
PTHR11808:SF12	$\"[134-268]T$ $\"[311-475]T$	O-ACETYLHOMOSERINE (THIOL)-LYASE
TIGR01326	$\"[45-473]T$	OAH_OAS_sulfhy: O-acetylhomoserine aminocar

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[37-339]T$	no description

InterPro
IPR015422
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10	$\"[340-478]T$	no description

noIPR
unintegrated

unintegrated
PIRSF001434	$\"[46-477]T$	Cystathionine gamma-synthase

","BeTs to 9 clades of COG2873COG name: O-acetylhomoserine sulfhydrylaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG2873 is -o----y-vdrlb--f-h--uj----Number of proteins in this genome belonging to this COG is 1","***** IPB000277 (Cys/Met metabolism pyridoxal-phosphate-dependent enzymes) with a combined E-value of 2.3e-90. IPB000277A 93-117 IPB000277B 148-159 IPB000277C 187-220 IPB000277D 224-262 IPB000277E 321-363 IPB000277F 406-427 IPB000277G 451-468","","","-66% similar to PDB:2CTZ Crystal structure of o-acetyl homoserine sulfhydrylase from Thermus thermophilus HB8 (E_value = 5.2E_110);-57% similar to PDB:1Y4I Crystal structure of Citrobacter Freundii L-methionine-lyase (E_value = 5.8E_77);-54% similar to PDB:1GC0 CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA (E_value = 1.4E_70);-54% similar to PDB:1GC2 CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA (E_value = 1.4E_70);-54% similar to PDB:1PG8 Crystal Structure of L-methionine alpha-, gamma-lyase (E_value = 1.4E_70);","Residues 47 to 473 (E_value = 4.3e-178) place ANA_2711 in the Cys_Met_Meta_PP family which is described as Cys/Met metabolism PLP-dependent enzyme.","","(THIOL) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2714","2924271","2925842","1572","4.94","-17.88","54389","ATGGGACCAAAGCGACTAGTGTGGCTTTGTCGCATCCGGGCTGACGCTGCCTGCCGTCTTCGTCCCCTGATCCGCTCCGCGCCCCCTGATTCCGCGGAACGGATCCCGACGGCGGGCCGGCGCCGGTCCCCGGGTGAGGCGTCATCCTCACGTTCAGCCCCATCACGACGGAGAACCCCAGTGAGCCCGATCCCCCCACGACGGCACGGACACGGTGTCGTCGCCACCGCAGTGGTAGCCCTGGCATGCACCCTGGCGCCCTCGGTGCTGGCCGACCCCGTGGACCAGAGCGACATTGATCGTTCCAAGGCCTCCGAGCGCTCGACCTCCACCTCCATCGCTTCCCTCGAGGCCCAGCTCGCCCAGGAGAGCAGCAACCTGGAAGACGCCCAGCTCAAGGCTCAGGTCGCCAATGAGGACTACCTGACCGCCGTTGACGAGCTCAACACGGCCACCAAGGACGCCCAGACCGCCCAGACCAACGCCGACGCCGCCGCCTCCAGCACCGCCGCGGCCCGCTCCGACCTCGGCTCGATCGTCGTCCAGACCTACCAGGAGAGCGGCAACCCGCTCGACCCGCTCACCCCCTACCTGACCAGCGAGTCGCTCGCGGACCTGGCCGACGCCGACGTCGCCCTGACCCGGGCCGGCGAGAAGAACAACGCCAAGGTCCAGAACGTCGAGGCCCTCGAGGCGGTGGCCACGAGCATGCAGACCATCGCCGACCAGAAGGTCACGGCCAAGGAGGCCGCCAAGACCTCCGCCGCCACCGCCAAGTCCGACGCCGAGGCCGCTGCCAACGACGCCCAGAACGCCGTCACCACCACCCGCACCAACCGGCAGAACCTCATCGTCCAGCTGGCGGCGCAGCGCAACACCACCGTCGAGCTGGAGACGAAGTACCAGAACCAGGTCGAGGCCGAGCGCAAGGCCCGTGAGGAGGCGGCCGCCCAGGCCGCCGCCAAGGCTGCCTCGGAGAAGGCCGCTGCCGACCTCGCTCAGAAGCAGGCCGAGCAGGCCGCTGCCCAGCCCCAGGAGTCGGCCCCTGCTCCCCAGGAGCAGTCGAGCCAGCCCAGCCCGAGCCCCCAGTCCTCCGCCCAGGAGCCAGCCACCACCTCCCAGCCGGAGCCCGAGGCGGCCGAAGAGGAGGAGGCCGCACCTGCACCCGCACCGGCCCCGGAGCCTGCGCCCGCGCCGTCGCACTCCGGAAGCGCCGCCTCCACCGCCATCAACGCGGCCATGGGCTACCTCGGCACCCCCTACGTGTGGGCCGGGGAGTCGGCTGCGGGCCTGGACTGCTCCGGGTTGACGATGGTCTCCTATGCCGCCGCCGGCGTGGAGCTCACGCACTCCTCACGCGTGCAGTACGGGGAGGGCTCCCTGGTTCCGCTCGACGCCGCCCAGCCCGGCGACCTCGTCTTCTGGTCCTCCGACGGCAGCCAGTCCGGCATCTACCACGTGGCCATCTACCTGGGTGACGACACGATGATCGAGGCGCCGACCTTCGGCATGACTGTGCGCGTCACCTCCATGCGCTACTCCGGCGTCATGCCCTACGCGGTGCGCCTCTAA","MGPKRLVWLCRIRADAACRLRPLIRSAPPDSAERIPTAGRRRSPGEASSSRSAPSRRRTPVSPIPPRRHGHGVVATAVVALACTLAPSVLADPVDQSDIDRSKASERSTSTSIASLEAQLAQESSNLEDAQLKAQVANEDYLTAVDELNTATKDAQTAQTNADAAASSTAAARSDLGSIVVQTYQESGNPLDPLTPYLTSESLADLADADVALTRAGEKNNAKVQNVEALEAVATSMQTIADQKVTAKEAAKTSAATAKSDAEAAANDAQNAVTTTRTNRQNLIVQLAAQRNTTVELETKYQNQVEAERKAREEAAAQAAAKAASEKAAADLAQKQAEQAAAQPQESAPAPQEQSSQPSPSPQSSAQEPATTSQPEPEAAEEEEAAPAPAPAPEPAPAPSHSGSAASTAINAAMGYLGTPYVWAGESAAGLDCSGLTMVSYAAAGVELTHSSRVQYGEGSLVPLDAAQPGDLVFWSSDGSQSGIYHVAIYLGDDTMIEAPTFGMTVRVTSMRYSGVMPYAVRL$","NLP/P60 protein","Extracellular, Periplasm","NLP/P60 family domain protein","NLP/P60 protein","NLP/P60 protein","","Konig V., Vertesy L., Schneider T.R. Structure of the alpha-amylase inhibitor tendamistat at 0.93 A. Acta Crystallogr. D 2006. Protein of the Month alpha-Amylase.:2003-McDowall J.. PMID: 14501112","","","

InterPro
IPR000064
Domain

NLP/P60
PF00877	$\"[418-522]T$	NLPC_P60

InterPro
IPR000833
Family

Alpha-amylase inhibitor
SM00783	$\"[439-487]T$	no description

noIPR
unintegrated

unintegrated
PTHR21666	$\"[404-513]T$	PEPTIDASE-RELATED
PTHR21666:SF1	$\"[404-513]T$	NLP/P60 FAMILY SECRETED PROTEIN

","BeTs to 13 clades of COG0791COG name: Cell wall-associated hydrolases (invasion-associated proteins)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0791 is ---------drlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 2","***** IPB000064 (NLP/P60) with a combined E-value of 5.1e-14. IPB000064A 424-437 IPB000064B 470-475 IPB000064C 486-503***** IPB008408 (Brain acid soluble protein 1) with a combined E-value of 8.5e-08. IPB008408B 303-351 IPB008408C 361-410 IPB008408B 304-352 IPB008408B 312-360 IPB008408B 327-375 IPB008408C 319-368 IPB008408C 350-399 IPB008408C 308-357","","","No significant hits to the PDB database (E-value < E-10).","Residues 418 to 522 (E_value = 1.5e-31) place ANA_2714 in the NLPC_P60 family which is described as NlpC/P60 family.","","family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2715","2926401","2925901","501","4.84","-14.66","19201","GTGGAGTTCGACGTCACGATTGAGATCCCCAAGGGCAACCGCAACAAGTACGAGATCGATCACGAGACCGGCCGGATTCGCCTGGACCGCATGCTCTTCACCTCGACGCGCTACCCCGACGACTACGGCTACATCGACGGGACCCTCGGCGAGGACGGCGACCCCCTCGACGCACTGGTCCTGCTAGAGGAGCCGACCTTCCCCGGCTGCGTCATCCGCTGCCGCGCGCTGGGCATGTTCCGCATGCGCGATGAGAAGGGCGGCGACGACAAGGTCCTGTGCGTGCCCAGCGCCGACCAGCGCGCCTCCTGGCGTACCGACATCGAGGACGTCTCGGAGTTCCACCGCCTGGAGATCCAGCACTTCTTCGAGGTCTACAAGGACCTCGAGCCCGGCAAGTCCGTCGAGGGCGCCCACTGGGTGGGGCGCGAGGAGGCCGAGGAGGAGATTCGTCAGTCCTTCCAGCGCGAGGCCGACCGCGTCGCCCACGAGGGCCACTGA","VEFDVTIEIPKGNRNKYEIDHETGRIRLDRMLFTSTRYPDDYGYIDGTLGEDGDPLDALVLLEEPTFPGCVIRCRALGMFRMRDEKGGDDKVLCVPSADQRASWRTDIEDVSEFHRLEIQHFFEVYKDLEPGKSVEGAHWVGREEAEEEIRQSFQREADRVAHEGH$","Inorganic pyrophosphatase","Cytoplasm","inorganic pyrophosphatase","inorganic pyrophosphatase ","Inorganic diphosphatase","","Lahti R., Kolakowski Jr L.F., Heinonen J., Vihinen M., Pohjanoksa K., Cooperman B.S. Conservation of functional residues between yeast and E. coli inorganic pyrophosphatases. Biochim. Biophys. Acta 1990. 1038(3):338-345. PMID: 2160278Cooperman B.S., Baykov A.A., Lahti R. Evolutionary conservation of the active site of soluble inorganic pyrophosphatase. Trends Biochem. Sci. 1992. 17(7):262-266. PMID: 1323891","","","

InterPro
IPR008162
Family

Inorganic pyrophosphatase
PD002014	$\"[22-123]T$	IPYR_STRCO_Q9X8I9;
G3DSA:3.90.80.10	$\"[3-160]T$	no description
PTHR10286	$\"[22-156]T$	INORGANIC PYROPHOSPHATASE
PF00719	$\"[4-159]T$	Pyrophosphatase
PS00387	$\"[52-58]?$	PPASE

","BeTs to 22 clades of COG0221COG name: Inorganic pyrophosphataseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0221 is -ompkzyq-dr-bcefghsnujxi-wNumber of proteins in this genome belonging to this COG is 1","***** IPB008162 (Inorganic pyrophosphatase) with a combined E-value of 9.6e-41. IPB008162A 29-82 IPB008162B 119-130","","","-76% similar to PDB:1SXV 1.3A Crystal structure of rv3628, Mycobacterium tuberculosis inorganic pyrophosphatase (PPase) at pH5.0 (E_value = 1.4E_54);-76% similar to PDB:1WCF 1.54 A CRYSTAL STRUCTURE OF RV3628, MYCOBACTERIUM TUBERCULOSIS INORGANIC PYROPHOSPHATASE (PPASE) AT PH7.0 (E_value = 1.4E_54);-62% similar to PDB:2PRD CRYSTAL STRUCTURE OF INORGANIC PYROPHOSPHATASE FROM THERMUS THERMOPHILUS (E_value = 2.0E_35);-65% similar to PDB:1QEZ SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE. (E_value = 1.4E_33);-63% similar to PDB:1UDE Crystal structure of the Inorganic pyrophosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 (E_value = 4.1E_33);","Residues 4 to 159 (E_value = 3.5e-46) place ANA_2715 in the Pyrophosphatase family which is described as Inorganic pyrophosphatase.","","pyrophosphatase (ppa)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2716","2926637","2928028","1392","5.11","-11.62","46267","ATGCGCAAGGTCCAGACCGCTGCCCTGACAGCGGCGAGCCTGCTGGTTTTCGGCGGCTACTACAGCCTGGGCGATGCTCTCGACCTGCTGCCCGGCCCGGTGACGGTCGCCTACGCCGACGTCGCCCCCCGACCCTTCCCGACGCCGGCCGGCCCCAGCGCCAAGACCGCCGCCCCTACCGGCCTGGACCAGGGGGCTCCCACGCCCTCCAAGACGGCTTTGAACGGCTACATCCAGGGCGTGGTTTCCGACGCCGCCCTGACCGGGGGGAACGTGACGGCCTCCGTCGTCGATGTCGCCACCGGCGAGGAGCTGCTGGACCGCTCGGCCGCCAGCGGGGTGACGCCGGCCTCCACCAACAAGGTGCTCACCGCCTGGGCCTCCCTGTCCTCCATGGGGCCGGGGCACACCCTCCAGACCAAGGCCGTCCTGGAGGGGCAGACCCTGACCCTCGTGGGCGGTGGTGACGTGCTGCTGGCCGAGAACGAGGGCGACCCGAACGCCACGGCCGGTCACGCGGGCCTGGGCGATCTCGCCCGAGCCACTGCTGAGAAGCTCAAGTCCCAGGGGACGACGTCGGTCTCCCTGCGCCTGGACGACACCCTGTTCACTGGCCCCCAGTGGAACGATAAGTGGGAGGCCGGCAACGAGCAGTACGTGGCCAAGATTCAGCCGATCATGGTGGATGTCTCGGCCACCCAGAACCAGGGCTACCCGGATGATCCGGCCATGGGGGCCGCCCAGGCCTTCGCCAAGCACCTGAGCGAGGCCGGCATCACGGTCGACGGCGAGCCGACGCGCGCCGCAGCCTCCGGCGGGGCCCGGGAGGTGGCCTCGGTCTCCTCAGCCCCGCTGTCCGACATCCTCGCCCTGTCGCTGAAGACCTCCGATAACACGATGACCGAGGTCGAGGGGCGGCTCGTGGCCGTGCACGCCAAGGAGACCACCGACTTCTCCGGGGCCTCCAAGGCCGTGCTCGCCCAGCTGAGCAAGGACGGCTTCGACACCTCCGGGGTGACGCTCCTGGACTCCTCCGGGCTGGCCAAGGGCAACAAGGTCCCCGCCCGGCTCCTGACCCAGATCATGACCAAGGCCGCCGGAGGCGAGGGCGGCTCGGCCGGGCGCACCCTCATCGCCGACCTGCCCGTCGCCGCCCTGGACGGGACCCTGGGCAACCGCCTGCACGACACCTCCGCGGCCGGGACGGTGCGCGCCAAGACCGGCTCACTGGAGCAGACCGCCTCCCTGGCCGGCGTGGTCACCACCGCCGACGGGCGCCAGCTGGCCTTCGCGGTCATGGCCAACGGCTTCCCCGCCAATGGCGGCGGAGCGGCCGCAGCCGCGATCGACAACCACTTCGTGGCGCCTCTGGCCTCGTGCGGATGCTCGTAA","MRKVQTAALTAASLLVFGGYYSLGDALDLLPGPVTVAYADVAPRPFPTPAGPSAKTAAPTGLDQGAPTPSKTALNGYIQGVVSDAALTGGNVTASVVDVATGEELLDRSAASGVTPASTNKVLTAWASLSSMGPGHTLQTKAVLEGQTLTLVGGGDVLLAENEGDPNATAGHAGLGDLARATAEKLKSQGTTSVSLRLDDTLFTGPQWNDKWEAGNEQYVAKIQPIMVDVSATQNQGYPDDPAMGAAQAFAKHLSEAGITVDGEPTRAAASGGAREVASVSSAPLSDILALSLKTSDNTMTEVEGRLVAVHAKETTDFSGASKAVLAQLSKDGFDTSGVTLLDSSGLAKGNKVPARLLTQIMTKAAGGEGGSAGRTLIADLPVAALDGTLGNRLHDTSAAGTVRAKTGSLEQTASLAGVVTTADGRQLAFAVMANGFPANGGGAAAAAIDNHFVAPLASCGCS$","D-alanyl-D-alanine carboxypeptidase","Extracellular, Periplasm","D-alanyl-D-alanine carboxypeptidase,serine-type, PBP4 family","D-alanyl-D-alanine carboxypeptidase ","D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase","","Rawlings N.D., Barrett A.J. Families of serine peptidases. Meth. Enzymol. 1994. 244:19-61. PMID: 7845208Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. Biochem. J. 1993. 290:205-218. PMID: 8439290Ghuysen J.M. Serine beta-lactamases and penicillin-binding proteins. Annu. Rev. Microbiol. 1991. 45:37-67. PMID: 1741619","","","

InterPro
IPR000667
Family

Peptidase S13, D-Ala-D-Ala carboxypeptidase C
PR00922	$\"[114-133]T$ $\"[276-298]T$ $\"[333-347]T$ $\"[348-362]T$ $\"[413-426]T$	DADACBPTASE3
PF02113	$\"[116-435]T$	Peptidase_S13
TIGR00666	$\"[101-436]T$	PBP4: D-alanyl-D-alanine carboxypeptidase/D

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide
tmhmm	$\"[5-23]?$	transmembrane_regions

","BeTs to 10 clades of COG2027COG name: D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 4)Functional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG2027 is ---------dr-bcefghsn------Number of proteins in this genome belonging to this COG is 1","***** IPB000667 (D-Ala-D-Ala carboxypeptidase 3 (S13) family signature) with a combined E-value of 1.8e-21. IPB000667A 114-133 IPB000667B 276-298 IPB000667C 333-347 IPB000667E 413-426","","","-50% similar to PDB:1W79 CRYSTAL STRUCTURE OF THE DD-TRANSPEPTIDASE-CARBOXYPEPTIDASE FROM ACTINOMADURA R39 (E_value = 2.6E_18);-50% similar to PDB:1W8Q CRYSTAL STRUCTURE OF THE DD-TRANSPEPTIDASE-CARBOXYPEPTIDASE FROM ACTINOMADURA R39 (E_value = 2.6E_18);-50% similar to PDB:1W8Y CRYSTAL STRUCTURE OF THE NITROCEFIN ACYL-DD-PEPTIDASE FROM ACTINOMADURA R39. (E_value = 2.6E_18);-48% similar to PDB:2EX2 Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli (E_value = 1.1E_16);-48% similar to PDB:2EX6 Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with ampicillin (E_value = 1.1E_16);","Residues 116 to 435 (E_value = 1.4e-32) place ANA_2716 in the Peptidase_S13 family which is described as D-Ala-D-Ala carboxypeptidase 3 (S13) family.","","carboxypeptidase, serine-type, PBP4 family (S13)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2717","2928110","2929348","1239","10.65","10.37","42821","GTGACGACCCAGGGCACAGCGGCGGGACTCGTCGACTGGCGGACGGTGGAGCGCCTGACCGCGCTCATCCCGGCGGGCCCCAGCGCCTCACGTTCGGCGCGCGCCAGCTCGGTGGCGGTGCTGCGCCGCTCCGCCCAGGAGGCGCCGGCTTGGGTCGCCAGGATCACCGGCTTGAACCGGGCGGCCCGGCAGGTTGCCGAGACCACCCGCGTGAGCGTTGTCGACCGGGCTGGGCTCGTGCGCGCCTCCAGTCGGGCGCTGCGCGGCCTCATGGAGCAGGTGCCCGCCCCGCAGGCATCGGAGGCGGTCCAGCTCGTCGGGGCCGCCGAGGTCGCCGGGGCGATGAGCCTGCTGGCCACCCGGCTCCTGGGGCAGGTGGTGCCCGCGGCCCCGAGCGGGTCTCACGGTCACGGGGCCGGTAGCGCCGGCCCCGCTCGCCCCGTCGGTGAGAAGGATGGCGAGGGCGACGACGTCGTGACGTCCGCCGCCGGGCCGGCCCGTGACGTGACAACAGGTAGAGGCTGGGATGGGGCGGCGTCGCCGCACCTGCTGCTCGTGGCCCCCAACGTGCTGGCGGTGCGCCGCCAGATGGACCTGGACATGCTCGACCTGCCCGCCTGGGTCTGCCTGCACGAGATGACCCACGCCGTCCAGCTGGCCGCCGCGCCCTGGCTTGGCCCCTACCTGTCGGACTCCATGCGCATGGTGATCGGCGCCGTCGTCGAGGCTGCCTACGGCGGTGCCGACGGTGCCCGAAGCGCCGGCGGCGGGAGCCGGCAGGAACGGGGGAGGCGGCCGCGGCGGGGCCGGGCGGTGCGCCTTGCGGCGCGCGCCGGCCGAGGGCGGGTGCTCGAAGGTCTGATGAACGTCACGGACCGCGCCGAGGTCGCCTCCCTGGCCGCCGCGCTCACCTTCCTGGAGGGACACGCTGAGGTGGTCCTCGATGACGTGCACCCCAACCGGATGCCCTCGGTCCACCGGCTCCGGGCCGTGCTCTCGCGCAGCCGCGCGGCCGACGGCGGCATCGGCCCCGGTCCCGGACTGGGCTCGCTCCTGCTGCACCGGCTCATGGGCCTTGAGGCCAAGGAGGCCCAGTACGCCGACGGCGCCGCCTTCGTGCGCAGCGTCGTGACCCGCATAGGGCACGAGGGGCTCAACGCCGTGTGGGCCGATCCCGAGCTGCTGCCCACGCCGGCTGAGCTCGCCCGACCCGACGTGTGGGTACGTCGCGTCAGCTGA","VTTQGTAAGLVDWRTVERLTALIPAGPSASRSARASSVAVLRRSAQEAPAWVARITGLNRAARQVAETTRVSVVDRAGLVRASSRALRGLMEQVPAPQASEAVQLVGAAEVAGAMSLLATRLLGQVVPAAPSGSHGHGAGSAGPARPVGEKDGEGDDVVTSAAGPARDVTTGRGWDGAASPHLLLVAPNVLAVRRQMDLDMLDLPAWVCLHEMTHAVQLAAAPWLGPYLSDSMRMVIGAVVEAAYGGADGARSAGGGSRQERGRRPRRGRAVRLAARAGRGRVLEGLMNVTDRAEVASLAAALTFLEGHAEVVLDDVHPNRMPSVHRLRAVLSRSRAADGGIGPGPGLGSLLLHRLMGLEAKEAQYADGAAFVRSVVTRIGHEGLNAVWADPELLPTPAELARPDVWVRRVS$","Conserved hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein","conserved hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-51% similar to PDB:2CF2 ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2718","2929477","2930016","540","4.83","-8.56","19524","ATGGGATCGGACCTTCAGCAGGTTCTCATCACCGAGGAGCAGATCGGGCAGCGCCTCGATGAGATGGCCGCGCAGATCGACGCGGACTATGCGGGCCGTGACCCTCTGCTCGTCGGCGTGCTCAAGGGGGCCGTCTACGTCATGGCGGACCTGTCGCGCCGGCTGCACATGAGTGCGCCGATGGACTGGATGGCGGTGTCCTCTTATGGCTCGGGCACCAAGTCCTCCGGCGTGGTGCGCATCCTCAAGGACCTGGACACCGACGTCACCGACCGGCACATCCTCATCGTTGAGGACGTCATCGACTCCGGCCTGACCCTGTCCTGGCTGGTGGGCAACCTGTCCTCGCGCGGCGCGGCCTCGGTGGAGATCGCCACGCTTCTGCGCAAGCCCGACGCCGCCAAGGTTGAGGTGGACGTCAAGTACGTCGGCTTCGATATTCCTACGGAGTTCGTCGTCGGCTACGGGTTGGACTACGCCGAGCGGTACCGCAACCTGCCGTTCATCGGTACGCTGCGCCCTGAGGTCTACGGGGGCTGA","MGSDLQQVLITEEQIGQRLDEMAAQIDADYAGRDPLLVGVLKGAVYVMADLSRRLHMSAPMDWMAVSSYGSGTKSSGVVRILKDLDTDVTDRHILIVEDVIDSGLTLSWLVGNLSSRGAASVEIATLLRKPDAAKVEVDVKYVGFDIPTEFVVGYGLDYAERYRNLPFIGTLRPEVYGG$","Hypoxanthine phosphoribosyltransferase","Cytoplasm","hypoxanthine phosphoribosyltransferase","hypoxanthine phosphoribosyltransferase ","hypoxanthine phosphoribosyltransferase","","Hershey H.V., Taylor M.W. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene 1986. 43(3):287-293. PMID: 3527873","","","

InterPro
IPR000836
Domain

Phosphoribosyltransferase
PF00156	$\"[4-148]T$	Pribosyltran

InterPro
IPR002375
Family

Purine/pyrimidine phosphoribosyl transferase
PS00103	$\"[94-106]T$	PUR_PYR_PR_TRANSFER

InterPro
IPR005904
Family

Hypoxanthine phosphoribosyl transferase
TIGR01203	$\"[8-173]T$	HGPRTase: hypoxanthine phosphoribosyltransf

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2020	$\"[3-177]T$	no description
PTHR22573	$\"[3-179]T$	PHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF9	$\"[3-179]T$	HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE

","BeTs to 12 clades of COG0634COG name: Hypoxanthine-guanine phosphoribosyltransferaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG0634 is -------qvdrlb-efghsn-j---wNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-75% similar to PDB:1R3U Crystal Structure of Hypoxanthine-Guanine Phosphoribosyltransferase from Thermoanaerobacter tengcongensis (E_value = 2.9E_51);-75% similar to PDB:1YFZ Novel IMP Binding in Feedback Inhibition of Hypoxanthine-Guanine Phosphoribosyltransferase from Thermoanaerobacter tengcongensis (E_value = 2.9E_51);-75% similar to PDB:2GEB Crystal structure of the Thermoanaerobacter tengcongensis hypoxanthine-guanine phosphoribosyltransferase L160I mutant: insights into the inhibitor design (E_value = 5.0E_51);-69% similar to PDB:1G9S CRYSTAL STRUCTURE OF A COMPLEX BETWEEN E.COLI HPRT AND IMP (E_value = 3.4E_39);-69% similar to PDB:1G9T CRYSTAL STRUCTURE OF E.COLI HPRT-GMP COMPLEX (E_value = 3.4E_39);","Residues 4 to 148 (E_value = 3.4e-32) place ANA_2718 in the Pribosyltran family which is described as Phosphoribosyl transferase domain.","","phosphoribosyltransferase (hpt)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2720","2930250","2931557","1308","5.20","-6.31","42532","GTGCGTCGACGCGCTCCGAGGCTGGTCGGCCTCGCCGGTGCGGTGGTGCTGTCGTCCTCGCTGAGCATCCCCATGATGGCTCCGGTGTCCGCGGAGCCGACCTCCGGCGACACATTTAATACGGTTGCTGAGATGGCGCAGGTCAGTGGTGCTTCGGGCACCCTGACCACCCTCGGTGACGAGGCGCCCGGCGACGGCGGCGGCCTGACCTACGACGTGCAGAGCACGAGTCCCGAGGGCGCGCTGGGTGCCGTCTCGGTCATGCTGGCCGATGGTCAGTGGGCCGTGCCGCAGGGGCTCCCAGCCGGCCCGGCCGTTGGCGCGGACGGTACCGCCGCCAACGACGTCGTGGCCCGGACCCAGTCCTTCGTCAACGCCGGCGGGTCCCTGGTCTCGGACGCATCACGGCCCACGCCGCTGTCGGGCGCGAATGTGCGTGCCAGCGGCTCCGCCCCGTACGCGATCACCTCCTCAGCGCTGGTGGGCATGGTCCTCTCCGGCTGGGACTACTCGCACACCACGTATGCGGCGGACCAGAACACTCAGGTCGGCTACCGGGCCGACGTCGGCCAGGACCTCTCCGGGGGCTGGAAGCCGGACGACCTGGCCGGCTGGTTCCACTCCCAGGGGCGCCTGTGGCTGAACGCGGACGGCTCGATCAGCCCCGGGGACATTGTCTTCTTCTCCAACCCCTTGCCCGGGGGGCAGGGCGAGTCCGGCTCGGCTCCCGCCCAGTCCACGGTGTTCGCCAACGTCTACGATGTCGGCATCTACGTCGGTAACAACCAGGTGGTGCGGGCCTCGACGGGGACGGCTCAGGCGCAGACCCTGGACGCGCAGACGATGGCCGAGGTGGCTCTGGTGGCGCGCCCGCAGTGGTCCGCCCCTGCTGGTGGCGCGCCCGCCCCGGCGGATCAGCAGCGCGCCGGTGCTGGTGGCGGCGCGGGTGCCGGGAGCACTGCGACGCCGGGCCCGGAGGCTTCGGCGTCGGCCTCGGCTCAGGCGAAGGCTCAGCAGGGCCCGGCCGCGGGGGCCCCGTCCTCCAAAGGTGGCTCGGTGCCGGACGGCTCGAGCGCCGGCTCGATGTCCTCGGGTGGGGCTGGGGGCGGTGACCACAACGAGGTCGTGGTGGGTGCCGCCGGTAGCAGCCAGGGCGCGAAGGGCGTCACGAGTGTCGCTAAGCGGCCCGCCGCCCAGAGTGTTCGGGAGCGGTGGTTGCCGGTGACGGGTGTGGCGATCGGCGTGCTGTCCGTGGCCGCGATCCTGCTGTCTGCCGGCCTCATCGTCCTGCGCCTGCGCCGCGCCTGA","VRRRAPRLVGLAGAVVLSSSLSIPMMAPVSAEPTSGDTFNTVAEMAQVSGASGTLTTLGDEAPGDGGGLTYDVQSTSPEGALGAVSVMLADGQWAVPQGLPAGPAVGADGTAANDVVARTQSFVNAGGSLVSDASRPTPLSGANVRASGSAPYAITSSALVGMVLSGWDYSHTTYAADQNTQVGYRADVGQDLSGGWKPDDLAGWFHSQGRLWLNADGSISPGDIVFFSNPLPGGQGESGSAPAQSTVFANVYDVGIYVGNNQVVRASTGTAQAQTLDAQTMAEVALVARPQWSAPAGGAPAPADQQRAGAGGGAGAGSTATPGPEASASASAQAKAQQGPAAGAPSSKGGSVPDGSSAGSMSSGGAGGGDHNEVVVGAAGSSQGAKGVTSVAKRPAAQSVRERWLPVTGVAIGVLSVAAILLSAGLIVLRLRRA$","Hypothetical protein","Extracellular","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-31]?$	signal-peptide
tmhmm	$\"[410-430]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-57% similar to PDB:1FMT METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI (E_value = );-57% similar to PDB:2FMT METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET (E_value = );-60% similar to PDB:2P5Z Crystal structure of N-terminal domain of Hypothetical protein ORF-c3393 (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2721","2932716","2932988","273","5.79","-2.37","9797","GTGCCCGCCACCGTATTCGTCCGCTTCGATGCGCCCGGCCCGGTCGAGGCCACGCCCCGCCGCCTTCACGCCGCCTGGGGCAGAGTCCTCGACCTCCCCGAAGGAGTCAGCCCCGAGCGCGCCGCCCGCCTGCCCGCCCTCGCTCACCGCCCACCCCACGACCAGCCCGGCCCCAAGCCCTACTGCCTGGGCGACATGACCCAGACCCCGGACGGCCTCGGCGTCGAGCTGCGATTCCTCGACGACCGCCTCCTGGACACGCTCGACGCCTGA","VPATVFVRFDAPGPVEATPRRLHAAWGRVLDLPEGVSPERAARLPALAHRPPHDQPGPKPYCLGDMTQTPDGLGVELRFLDDRLLDTLDA$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-65% similar to PDB:2C7F THE STRUCTURE OF A FAMILY 51 ARABINOFURANOSIDASE, ARAF51, FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH 1,5-ALPHA-L-ARABINOTRIOSE. (E_value = );-65% similar to PDB:2C8N THE STRUCTURE OF A FAMILY 51 ARABINOFURANOSIDASE, ARAF51, FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH 1,3-LINKED ARABINOSIDE OF XYLOBIOSE. (E_value = );-53% similar to PDB:1IYZ Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH (E_value = );-53% similar to PDB:1IZ0 Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH (E_value = );-55% similar to PDB:1PZ2 Crystal structure of a transient covalent reaction intermediate of a family 51 alpha-L-arabinofuranosidase (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2722","2933040","2933525","486","9.92","4.59","17464","ATGCTCGTCGCCGTCGAGGCCCAGGTCCTCGAACATGCCGACTGGGAGGACCTCGCCGCCCAGACCGCCTCCACCGCCTGGGACATCCACCTGCTCACCCCCACTGTCTTCACCTCCCGCGGACACCACGTCCCCGAGGTCACCGCAGCCTCCCTGGCCACCAGCCTCCACGCGCGCTGGCGCCACTGGTGCCGCCCCCTGGCCCCCGAGCTCCCCGAGCGCGAGCGCCTCACCTCCGTCCTCATCACCCAGGACCGCACCCGCCGCACCGTCGTCGGCCTGGGCATGCCGCGTGCCGACCGCCGCGGACGCCTCTCCAGCCGCCGCATCCCCGCCAGCGTCGGCGCCCTGCGCATCAGCGCCCCCGCCGCCGGCTCCATCACCGCCGTCTTCTCCCAGCTCATGGCCCTGGCCCGCTACACGAGCGTCGGCTCCCACAGCGCCTACGGGATGGGCGTCATCGACGTCGTCGCGGACGTGCCATAA","MLVAVEAQVLEHADWEDLAAQTASTAWDIHLLTPTVFTSRGHHVPEVTAASLATSLHARWRHWCRPLAPELPERERLTSVLITQDRTRRTVVGLGMPRADRRGRLSSRRIPASVGALRISAPAAGSITAVFSQLMALARYTSVGSHSAYGMGVIDVVADVP$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2723","2933723","2935798","2076","5.49","-14.51","75142","ATGAAAGATTCTGGGCGCGAGCCCGGCCGCAAGGACTCGGGGAAGCCGGGCAAGGCCGGTAAGAACGACCGCAGCAAGCGCGACCGCAAGCTCCGCGACACCCTGGGCAACCCGTTCCTGTGGTTGGTGCCCTTCCTCCTGGTCGTCATCCTCGGCTGGGCCGTCTTCTCCTCGATGTTCGGCTACCGCACCATCGACACCTCCGACGGCCTGACGCTCCTGCGGGACAAGCCGGACACGATCAAGTCGATCACCGTCGTCGACGGCAACCAGCGCGTCGAGCTGGACCTCACCACCACCTACGTCCAGCCCAAGAAGAAGGGCATCGAGTCGCGCCCGGTGGGCAAGAAGGTCGAGTTCTCCTACACCGACGCCCAGGCCGAGCAGGTCGACCGCCTCGTGCAGGCCGCCGCCCCCAAGGAGGGCTTCAACTCCGTGGTGCCCACCACCAGCTGGTGGTCATCCCTCGTCCAGCTGCTCGTCCCCGCCCTGCTGCTGGGCGGCATCATGTGGTGGCTCATCGGTCGCATGGGCGGCGGGCGCGGCGGCGCCATGGGCTTCGGCCGCTCCAAGGCGAAAGTCGGTTCCAAGGAGATGCCCGACGTCACCTTCGCCGACGTCGCTGGCGAGGACGAGGCCGTCGAGGAGCTCGAGGAGATCCGCGAGTTCCTCTCCGAGCCGGAGAAGTTCCGCGCCGTCGGCGCCAAGATCCCCAAGGGCGTCCTCCTCTACGGCCCGCCCGGAACCGGTAAGACCCTCCTGGCCAAGGCCGTCGCCGGCGAGGCTGGCGTGCCCTTCTTCTCCATGGCCGCCTCCGAGTTCGTCGAGATGTTCGTCGGCGTGGGTGCCTCGCGTGTGCGCGACCTGTTCGACCAGGCCAAGGAGAACGCCCCCGCCATCATCTTCGTCGACGAGATCGACGCCGTCGGCCGCCACCGTGGCTCCGGCACCGGCGGCGGGCACGACGAGCGTGAGCAGACCCTCAACCAGCTCCTCGTCGAGATGGACGGCTTTGACGCCAACACCAACGTCATCCTCATCGCCGCCACCAACCGCCCCGACGTCCTGGACCCGGCCCTCCTGCGCCCGGGCCGCTTCGACCGGCAGGTCAGCGTCGAGGCCCCCGACATGGCCGGTCGCGCCGCCATCCTCAAGGTCCACGCCAAGGGCAAGCCCCTCAACGACGACGTCGACCTCGACCTCGTGGCCAAGCGGACCCCCGGCTTCACCGGCGCGGACCTGGCCAACGTCCTCAACGAGGCCGCCCTGCTCACCGCCCGCTCCAACGCCCACCTCATCGACAACCGGGCCCTGGACGAGGCCATCGACCGCGTCATCGCCGGACCGCAGAAGCGCACCCGCGTCATGCGCGACCACGAGAAGCGCGTCACCGCCTACCACGAGGCCGGCCACGCCCTGTGCGCGGCCGCCGGCGCCTACTCCGACCCGGTCACCAAGGTGACGATCCTGCCGCGCGGGCGCGCCCTGGGCTACACGCAGGTCATGCCTCAGGACGACAAGTACTCCACCACCCGCAACGAGCTGCTCGACCAGCTCGTCTACGCCATGGGTGGGCGGGCCGCCGAGGAGATCATCTTCCGCGACCCCACCACCGGTGCCTCCAACGACATCGAGAAGGCCACCGCCACGGCCCGCAAGATGGTCACCGACTACGGTATGACCAGCGCGGTCGGCGCCGTCAAGCTCGGCACCACCGAGAGCGAGACGGTCCTGGGGCTCAACGCCACCAGCCGTGACTTCTCCGAGCAGGTCGCCGCCACTGTCGACACCGAGGTCCGCGGCCTGCTGGACGCCGCCCACCGGGAGGCCTGGGAAATCCTCACCCGTAACCGCGCCGTGCTCGACAAGCTGGCCGAGGAGCTCCTCAGCCGTGAGACGCTCCTGGAGAAGGACCTGGAGAGGATCTTCGAGGGCGTCATCAAGCAGCCCGAGCGGCCCCTGTGGCGCAGCGACGAGTCGCTGCCCGTCGTCGAGGCCGCCCCCGCCAGTGACGAAGCCGGCGGTGAGTCCGATGACTCCCACAACAACGACGACTTCTGGGGCTACAACCATTGA","MKDSGREPGRKDSGKPGKAGKNDRSKRDRKLRDTLGNPFLWLVPFLLVVILGWAVFSSMFGYRTIDTSDGLTLLRDKPDTIKSITVVDGNQRVELDLTTTYVQPKKKGIESRPVGKKVEFSYTDAQAEQVDRLVQAAAPKEGFNSVVPTTSWWSSLVQLLVPALLLGGIMWWLIGRMGGGRGGAMGFGRSKAKVGSKEMPDVTFADVAGEDEAVEELEEIREFLSEPEKFRAVGAKIPKGVLLYGPPGTGKTLLAKAVAGEAGVPFFSMAASEFVEMFVGVGASRVRDLFDQAKENAPAIIFVDEIDAVGRHRGSGTGGGHDEREQTLNQLLVEMDGFDANTNVILIAATNRPDVLDPALLRPGRFDRQVSVEAPDMAGRAAILKVHAKGKPLNDDVDLDLVAKRTPGFTGADLANVLNEAALLTARSNAHLIDNRALDEAIDRVIAGPQKRTRVMRDHEKRVTAYHEAGHALCAAAGAYSDPVTKVTILPRGRALGYTQVMPQDDKYSTTRNELLDQLVYAMGGRAAEEIIFRDPTTGASNDIEKATATARKMVTDYGMTSAVGAVKLGTTESETVLGLNATSRDFSEQVAATVDTEVRGLLDAAHREAWEILTRNRAVLDKLAEELLSRETLLEKDLERIFEGVIKQPERPLWRSDESLPVVEAAPASDEAGGESDDSHNNDDFWGYNH$","Cell division protein FtsH","Cytoplasm, Membrane, Extracellular","cell division protein FtsH","putative cell division protein FtsH ","ATP-dependent metalloprotease FtsH","","Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth. Enzymol. 1995. 248:183-228. PMID: 7674922","","","

InterPro
IPR000642
Domain

Peptidase M41
PF01434	$\"[434-642]T$	Peptidase_M41

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[237-376]T$	AAA

InterPro
IPR003959
Domain

AAA ATPase, core
PF00004	$\"[240-427]T$	AAA

InterPro
IPR003960
Domain

AAA ATPase, subdomain
PS00674	$\"[344-362]T$	AAA

InterPro
IPR005936
Domain

Peptidase M41, FtsH
TIGR01241	$\"[151-644]T$	FtsH_fam: ATP-dependent metallopeptidase Hf

InterPro
IPR011546
Domain

Peptidase M41, FtsH extracellular
PF06480	$\"[63-214]T$	FtsH_ext

noIPR
unintegrated

unintegrated
G3DSA:1.10.8.60	$\"[375-443]T$	no description
G3DSA:3.40.50.300	$\"[190-372]T$	no description
PTHR23076	$\"[31-633]T$	METALLOPROTEASE M41 FTSH
PTHR23076:SF10	$\"[31-633]T$	CELL DIVISION PROTEIN FTSH HOMOLOG
tmhmm	$\"[40-60]?$ $\"[155-175]?$	transmembrane_regions

","BeTs to 19 clades of COG0465COG name: ATP-dependent Zn proteasesFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG0465 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","***** IPB000642 (Peptidase M41) with a combined E-value of 2.5e-157. IPB000642A 221-270 IPB000642B 272-314 IPB000642C 343-387 IPB000642D 402-427 IPB000642E 461-495 IPB000642F 536-561***** IPB003960 (AAA-protein subdomain) with a combined E-value of 1.9e-85. IPB003960A 204-219 IPB003960B 238-259 IPB003960C 278-313 IPB003960D 330-380 IPB003960E 411-427***** IPB003338 (AAA ATPase VAT, N-terminal) with a combined E-value of 1.7e-73. IPB003338A 224-277 IPB003338B 287-314 IPB003338C 322-376 IPB003338D 392-431***** IPB004201 (Cell division protein 48, CDC48, domain 2) with a combined E-value of 5e-44. IPB004201B 269-321 IPB004201C 342-389 IPB004201D 396-428 IPB004201E 292-329***** IPB007330 (MIT) with a combined E-value of 3.2e-16. IPB007330B 206-259 IPB007330C 266-320***** IPB008543 (Plant protein of unknown function DUF825) with a combined E-value of 1.6e-11. IPB008543D 231-279 IPB008543F 332-383 IPB008543G 400-451***** IPB013725 (DNA replication factor C-terminal) with a combined E-value of 5.2e-06. IPB013725E 233-277","","","-68% similar to PDB:2CE7 EDTA TREATED (E_value = 2.1E_123);-68% similar to PDB:2CEA WILDTYPE (E_value = 2.1E_123);-67% similar to PDB:2DHR Whole cytosolic region of ATP-dependent metalloprotease FtsH (G399L) (E_value = 1.7E_120);-74% similar to PDB:1IY2 Crystal structure of the FtsH ATPase domain from Thermus thermophilus (E_value = 1.9E_79);-74% similar to PDB:1IXZ Crystal structure of the FtsH ATPase domain from Thermus thermophilus (E_value = 2.4E_79);","Residues 63 to 214 (E_value = 6.8e-23) place ANA_2723 in the FtsH_ext family which is described as FtsH Extracellular.Residues 240 to 427 (E_value = 6e-98) place ANA_2723 in the AAA family which is described as ATPase family associated with various cellular activities (AAA).Residues 240 to 374 (E_value = 0.00056) place ANA_2723 in the AAA_5 family which is described as ATPase family associated with various cellular activities (AAA).Residues 434 to 642 (E_value = 2.3e-101) place ANA_2723 in the Peptidase_M41 family which is described as Peptidase family M41.","","division protein FtsH (AJ243808)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2724","2935850","2936422","573","6.88","-0.47","21130","ATGAGCTATGACGCCGAGGGCGTGCGGCGGGCGGTGCGCGACCTGCTCGTCGCCATCGGGGAGGACCCCGAGCGCGACGGGCTGCGTGACACCCCCGAGCGCATGGCGCGCGCCTACGCGGAGATGTTCGCCGGCCTCGACCAGGACCCGGCCGAGCACGTCGAGCGGGTCTTCGACGTCGGGCACGAGGAGATGGTCCTCGTGCGCGACATCCCCATGTGCTCGGTGTGCGAGCACCACCTGCTGCCCTTCCACGGGTTGGCGCACGTGGGCTACATCCCCAGTGAGGACGGGCGCGTCACCGGCCTGTCCAAGGTGGCGCGCCTCGTGGACGGCTACGCCCGGCGCCCCCAGGTCCAGGAGCGGCTCACCCGGCAGATCGCTGACGCCCTCGTCGAGCGCCTCCAGTGCCGTGGCGTGCTCGTGGTGGTTGAGGCCGAGCACCTGTGTATGTCGATGCGGGGCGTGCGCAAGCCCGGTTCCAACACGGTCACCTCCGCCGTGCGCGGCATCATGCGCAACGCCGCCACCCGCTCCGAGGCCATGAGCCTGGTCCTGGGCCGACGGTCCTGA","MSYDAEGVRRAVRDLLVAIGEDPERDGLRDTPERMARAYAEMFAGLDQDPAEHVERVFDVGHEEMVLVRDIPMCSVCEHHLLPFHGLAHVGYIPSEDGRVTGLSKVARLVDGYARRPQVQERLTRQIADALVERLQCRGVLVVVEAEHLCMSMRGVRKPGSNTVTSAVRGIMRNAATRSEAMSLVLGRRS$","GTP cyclohydrolase I","Cytoplasm","GTP cyclohydrolase I","GTP cyclohydrolase I ","GTP cyclohydrolase I","","Maier J., Witter K., Gutlich M., Ziegler I., Werner T., Ninnemann H. Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers. Biochem. Biophys. Res. Commun. 1995. 212(2):705-711. PMID: 7542887","","","

InterPro
IPR001474
Family

GTP cyclohydrolase I
PD003330	$\"[3-166]T$	GCH1_STRAW_Q82EE8;
PF01227	$\"[64-170]T$	GTP_cyclohydroI
TIGR00063	$\"[8-189]T$	folE: GTP cyclohydrolase I
PS00859	$\"[64-80]T$	GTP_CYCLOHYDROL_1_1
PS00860	$\"[114-124]T$	GTP_CYCLOHYDROL_1_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.286.10	$\"[6-53]T$	no description
G3DSA:3.30.1130.10	$\"[53-189]T$	no description
PTHR11109	$\"[13-188]T$	GTP CYCLOHYDROLASE I

","BeTs to 14 clades of COG0302COG name: GTP cyclohydrolase IFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0302 is ------yq-drlbcefghs-ujx---Number of proteins in this genome belonging to this COG is 2","***** IPB001474 (GTP cyclohydrolase I) with a combined E-value of 1.2e-57. IPB001474A 19-39 IPB001474B 63-103 IPB001474C 126-172","","","-66% similar to PDB:1WM9 Structure of GTP cyclohydrolase I from Thermus thermophilus HB8 (E_value = 1.4E_41);-66% similar to PDB:1WUQ Structure of GTP cyclohydrolase I Complexed with 8-oxo-GTP (E_value = 1.4E_41);-66% similar to PDB:1WUR Structure of GTP cyclohydrolase I Complexed with 8-oxo-dGTP (E_value = 1.4E_41);-69% similar to PDB:1IS7 Crystal structure of rat GTPCHI/GFRP stimulatory complex (E_value = 6.9E_41);-69% similar to PDB:1IS8 Crystal structure of rat GTPCHI/GFRP stimulatory complex plus Zn (E_value = 6.9E_41);","Residues 64 to 170 (E_value = 1.2e-48) place ANA_2724 in the GTP_cyclohydroI family which is described as GTP cyclohydrolase I.","","cyclohydrolase I (folE)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2725","2937703","2936483","1221","5.75","-7.82","44974","GTGGACAACATCAACAACCCGTACACACCCAACGCAGGAGCAGCCCCGGAGGTCCTCATTGGTCGCGACGGGCAGACCGAGGCGTTTTCTATCCTACTTCAGAGGCTCAAACGAGGCCGGACAGAGCAATCGATGATCATGACCGGCCTGCGCGGCGTCGGCAAGACCGTCCTGCTTAACAGGTTCGCAGAACTCGCCGAGATGGCAGGATGGGAGTCAATCGAGCTTGAAGCGAGCAAGCACGATGAAACAGCATTCCGTCAGTCCATCTTCTCCAAGTTCCGTGCCGCACTTCTACACATATCGCCTCGTCGCCGCTGGAGCGAACGCGCTCGACACGCCGCAGAAGTACTCAGCTCCTTTGTGCTATCGATCGACCAATCCGGCACTTTTTCCGTCACGTGGGACGTAGACCCGTCCGAGGGCTACGGGGATCACGGCGACCTAGGGCTAGACCTCACGGACGTATTTCTAGCCGTAGGAGAAGTTGCAAAGGAAAAAGGAACCGGGATCGTCCTACTCATCGACGAAGTTCAATTTCTCACCACCGTTCAGCTTGAATCACTCATACAAGCGGTTCACAAGTCCGTTCAGAAGAAGCTCCCCATCACTTTTGTGGGAGCCGGCCTACCACAGATCGCCGAGCTCGCTGGAGACGCCAAGTCTTACGCAGAAAGACTGTTCAAGTTCCCACGCATCGACTCCCTCACCCCCGAGGAAGCCCGACAAGCGCTTGTGGGACCCGCAGAAACCGAGAACGTGTCCTACGACGAAGATGCCGTGGACCTCGCAGTCAGCCTCACTCACGGCTACCCGTACTTCATTCAAGAGTTAGGGTACCAAGCATGGATCGTAGCGAGCGGAAACCACATCACGGCAGAAGACATCAGTACCGCTAAAGACGCATACGAAGCAAAGCTGGACGGGTCGTTCTTCCGCGTACGACTCGACCGTGCAACCCCCCTTCAAACCGCATACATGAGAGCCATGGCGGAACTCGGCTCCGAGCCCCAGAAAGCAGCCGATGTCGCCTCCCTCATGAAACGAGAGTCGTCACAGGTGGCACCCATCAGGTCTCAACTCATTGACATGGGGCTGCTATACACGCCCCAGCACGGCTATGCCGCCTTCACCGTCCCGGACTTCGACAAGTTCATGATGCGAGCCGTGCCCCGTCTCGAGGTCCCAGAGATTCAACATCGCCGCCGACGCGGGAAATAA","VDNINNPYTPNAGAAPEVLIGRDGQTEAFSILLQRLKRGRTEQSMIMTGLRGVGKTVLLNRFAELAEMAGWESIELEASKHDETAFRQSIFSKFRAALLHISPRRRWSERARHAAEVLSSFVLSIDQSGTFSVTWDVDPSEGYGDHGDLGLDLTDVFLAVGEVAKEKGTGIVLLIDEVQFLTTVQLESLIQAVHKSVQKKLPITFVGAGLPQIAELAGDAKSYAERLFKFPRIDSLTPEEARQALVGPAETENVSYDEDAVDLAVSLTHGYPYFIQELGYQAWIVASGNHITAEDISTAKDAYEAKLDGSFFRVRLDRATPLQTAYMRAMAELGSEPQKAADVASLMKRESSQVAPIRSQLIDMGLLYTPQHGYAAFTVPDFDKFMMRAVPRLEVPEIQHRRRRGK$","AAA ATPase","Cytoplasm","conserved hypothetical protein","hypothetical protein","AAA ATPase","","","","","

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[41-234]T$	AAA

","BeTs to 8 clades of COG2812COG name: DNA polymerase III, gamma/tau subunitsFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG2812 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","-45% similar to PDB:1JR3 Crystal Structure of the Processivity Clamp Loader Gamma Complex of E. coli DNA Polymerase III (E_value = );-45% similar to PDB:1NJF Nucleotide bound form of an isolated E. coli clamp loader gamma subunit (E_value = );-45% similar to PDB:1NJG Nucleotide-free form of an Isolated E. coli Clamp Loader Gamma Subunit (E_value = );-45% similar to PDB:1XXH ATPgS Bound E. Coli Clamp Loader Complex (E_value = );-45% similar to PDB:1XXI ADP Bound E. coli Clamp Loader Complex (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2726","2937777","2937932","156","11.61","5.13","5510","GTGTTGGTGGTCGTTGAGGCCGAGCACTTGTGCATGTCGATGCGGGGCGTGCGCAAGCCCGGCTCCAACACGGTCACCTCCGCCGTGCGCGGCATCATGCGCAACGCCGCCACCCGCTCCGAGGCCATGAGCCTGGTCCTGGTCCGGCGGTCCTGA","VLVVVEAEHLCMSMRGVRKPGSNTVTSAVRGIMRNAATRSEAMSLVLVRRS$","GTP cyclohydrolase I","Extracellular, Periplasm","GTP cyclohydrolase I (GTP-CH-I)","GTP cyclohydrolase I ","GTP cyclohydrolase I-like","","Maier J., Witter K., Gutlich M., Ziegler I., Werner T., Ninnemann H. Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers. Biochem. Biophys. Res. Commun. 1995. 212(2):705-711. PMID: 7542887","","","

InterPro
IPR001474
Family

GTP cyclohydrolase I
PD003330	$\"[1-46]T$	Q6NF93_CORDI_Q6NF93;
PF01227	$\"[1-31]T$	GTP_cyclohydroI

noIPR
unintegrated

unintegrated
G3DSA:3.30.1130.10	$\"[1-50]T$	no description
PTHR11109	$\"[1-49]T$	GTP CYCLOHYDROLASE I

","BeTs to 14 clades of COG0302COG name: GTP cyclohydrolase IFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0302 is ------yq-drlbcefghs-ujx---Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 31 (E_value = 1.5e-11) place ANA_2726 in the GTP_cyclohydroI family which is described as GTP cyclohydrolase I.","","cyclohydrolase I (GTP-CH-I) (GTP-CH-I)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2727","2937982","2938392","411","8.01","1.34","15363","ATGAGTCCCACGTACAAGAGGCTGCTGGTGGCCGTCGATGCCGGGCTGCTGCTCTACTGGGCGGCCGTCTTCCTCAATCTCATTCCCGAGCACCTGCGTTTCAAGGACTACTCCAACCAGGTCATCCAGGCCTGGAACTGGTCCTTCTTCCCGCTCGACGTGGCTGCCGCGCTGACCGTCTTCCTCGGCGCCCACCTGACGCGGGTGGGCAGCAGGATCGGGGACCTGGTGCTGACGGTCGGACTCATGCTCACCTTCTGCGCCGGGTTCATGGCGATCTCCTTCTGGTCCTTCTACCGGGACTTCGACCCGCTGTGGTGGGGGCCCAATGCCCTACTCATGATCGTCCCGGCGCTCGCTTTCGGCTCCATGGTCTGCCGGCGGCTCGAGACCGCGGAGAACCGGGCGTGA","MSPTYKRLLVAVDAGLLLYWAAVFLNLIPEHLRFKDYSNQVIQAWNWSFFPLDVAAALTVFLGAHLTRVGSRIGDLVLTVGLMLTFCAGFMAISFWSFYRDFDPLWWGPNALLMIVPALAFGSMVCRRLETAENRA$","Hypothetical protein","Membrane, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
PD082409	$\"[6-124]T$	Q81N65_BACAN_Q81N65;
signalp	$\"[1-25]?$	signal-peptide
tmhmm	$\"[9-29]?$ $\"[48-66]?$ $\"[76-96]?$ $\"[106-126]?$	transmembrane_regions

InterPro
IPR000390
Family

Small multidrug resistance protein
PF00893	$\"[17-108]T$	Multi_Drug_Res

noIPR
unintegrated

unintegrated
signalp	$\"[1-94]?$	signal-peptide
tmhmm	$\"[15-35]?$ $\"[45-63]?$ $\"[73-93]?$ $\"[99-119]?$	transmembrane_regions

InterPro
IPR000390
Family

Small multidrug resistance protein
PF00893	$\"[1-94]T$	Multi_Drug_Res

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide
tmhmm	$\"[2-24]?$ $\"[30-50]?$ $\"[59-79]?$ $\"[83-103]?$	transmembrane_regions

","BeTs to 9 clades of COG2076COG name: Membrane transporters of cations and cationic drugsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2076 is -o-------drlb-efg--nuj----Number of proteins in this genome belonging to this COG is 2","***** IPB000390 (Small multidrug resistance protein) with a combined E-value of 6.5e-25. IPB000390A 3-37 IPB000390B 43-97","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 94 (E_value = 1.2e-20) place ANA_2729 in the Multi_Drug_Res family which is described as Small Multidrug Resistance protein.Residues 69 to 103 (E_value = 6.3e-06) place ANA_2729 in the DUF6 family which is described as Integral membrane protein DUF6.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2730","2940874","2939651","1224","6.74","-1.12","43302","ATGGTGTCCGCTGTTGCGACGAATCTGATGCAGCCCACGCGGTACACGACGTGGCGGCCGACCTGGCGGCTGCACCTGGCGCACGCCTCCCTGGCCGCGCTGATTACTCTGTTCTCGATCGCGACGACCTGGCCAATGTCCTCCATCGCGGTCCTCTCCGAGATCATCGGGGGGCTGGCGCTGGCGCTGAGTAGCCGCTTCCCGTGGCCCGGGGCCCTGCTGGGCAGCGCGTCGGCGTGGACCGCCACCGTGGTGCTGACCGACGTTCCCTTCTCTCCGGGCATCATCCCTTGGCTGTGCACGGCGATCCTCGTGGCCCGCGGCTTCTCGCGTATGCCCGCCTACAGCCTGGTGGTCTTCTCGCTGGTGATCCTCATCGCCGATATCCAGTGGAACGGAGCGAGCCCGGCCTGGTTCACGCTGCTGCAGGTCTCGCTCTTTATCGGGGGCGGGGCCATCACTGTGGCCGAGCTCATCCGCAGCCCGCGCGACCAGGCCGAGCGCTCCTTGCACACCTACCGCGAGAGCATGGAGCGCCAGCGTCTCCTGGTGGTCACTGAACTGCATGACACGGTGGTGCGGGACCTGACCCACGCGGTCATGACGGCCGAGCAGGCCCGACTCGCGCATCCCCAGGACGCGGCGCTGGCACCCGAGCTGGACGCGATGACGGTGGCGGTGCGCGCGGCGGTGGAGCAGATGCGGCACGCGCTGCGCGCCATGAGTGACATCCGCGGGGGCGAGCGGCTGGATATCGAGGCGACCTCCGCGCCGCGCCCCCTGGAGGTGGTCATCTCCGATGCCGCGGCCATCCTGGGACAGCGGGGGGCGCACCTGGAGGTCGAGGGCCTGGAGCTGCTCGGGATCCCCGTGATTCCGCCGGGCGTGCGCCTCCAGCTGCTGCGGGTGCTGGGCGAACTGGTGTCGAACATGTCCAAGTACACGGCTCCGCAGGGGCGGGCGAGGCTGGTCATCGAGTCCGACGGGCGCTCCCTGGAGGCGATGGCAAGTAATGACGTCGGCCTCCCGGGGCAGGTCGGTGGCGTGTGGGCGGGCGCCGGCGCGCCGGGCAGTGGCGTACCGGGCTATGACGCCTTCTCCTCGGGCCTGGGCCTGGAGGGGGCGCGGCGCCGCGTGGAGGCCCTGGGCGGCAGCCTGAGCGTGAGCCAGGGCGAGGGCCGCTGGACCACGGTCTTCAGCGTCCCCTTCCAGGCGGTCTCCTGA","MVSAVATNLMQPTRYTTWRPTWRLHLAHASLAALITLFSIATTWPMSSIAVLSEIIGGLALALSSRFPWPGALLGSASAWTATVVLTDVPFSPGIIPWLCTAILVARGFSRMPAYSLVVFSLVILIADIQWNGASPAWFTLLQVSLFIGGGAITVAELIRSPRDQAERSLHTYRESMERQRLLVVTELHDTVVRDLTHAVMTAEQARLAHPQDAALAPELDAMTVAVRAAVEQMRHALRAMSDIRGGERLDIEATSAPRPLEVVISDAAAILGQRGAHLEVEGLELLGIPVIPPGVRLQLLRVLGELVSNMSKYTAPQGRARLVIESDGRSLEAMASNDVGLPGQVGGVWAGAGAPGSGVPGYDAFSSGLGLEGARRRVEALGGSLSVSQGEGRWTTVFSVPFQAVS$","Two-component system sensor kinase","Membrane, Cytoplasm","ATPase, histidine kinase-, DNA gyrase B-, andHSP90-like domain protein protein","two-component system sensor kinase","ATP-binding region, ATPase domain protein domain protein","","","","","

InterPro
IPR003594
Domain

ATP-binding region, ATPase-like
G3DSA:3.30.565.10	$\"[252-405]T$	no description
PF02518	$\"[295-404]T$	HATPase_c
SM00387	$\"[295-407]T$	HATPase_c

noIPR
unintegrated

unintegrated
signalp	$\"[1-43]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[47-65]?$ $\"[109-129]?$ $\"[135-155]?$	transmembrane_regions

","BeTs to 9 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: T [Cellular processes--Signal transduction mechanisms]The phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 25","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 295 to 404 (E_value = 2.5e-06) place ANA_2730 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.","","histidine kinase-, DNA gyrase B-, and HSP90-like domain protein protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2731","2940916","2941590","675","6.00","-4.38","24255","ATGACGGTTCCCCATGTGACTGATGGTCCGGCTGCTCCCTCGCAGGTCCTGCGCGTCGCCATCGTCGATGACGACCCCTTCGTCCTGCAGGCACTGCGGGCCTACCTCAGCTCCGACGAGCGCATCGAGGTGACCAGCACCTTCTCCCGCGCCGCCGACGCCCTGGCCTTCCTCCACAAGATCCGCGTGGACGTCCTGCTCACCGACGTGCGCATGCCCGAGATGGACGGCCTGGAGCTGCTCACCCGGGTGCGCCGTCAGTGGCCCCGCACGGCCGTCGTCGTGCTGACCTCCTTCGACGACGACGAGGCGATGGTGGCCGCGCTGGCCCAGCACGCCAACGGCTTCCTGCTCAAGGACGCCTCGCCCGAGGAGATCATCCGCGCCGTCATCGCCGCCAGCGCGGGCGGGACCACGATCTCCCCGGCCGCCACCTCCCGGCTCGTTACCCGCCACCTGCGCTCCCCGCAGACGGCCCAGGCCCCCGACGTCACCGAGGCCGAGCAGGCGGTCCTCACCCTCCTGTGCGAGGGCTACTCCAATGCCGAGATCGCCGAGCAACTCGTCGTCGCCGAGTCCACGGTCAAGACCCACGTCTCCCACCTCATGAAGAAGTACGACGTCCCGTCCCGACTCAAGCTCGTCGTCGCCGTTCACAAGACCCAGGGGGCCTGA","MTVPHVTDGPAAPSQVLRVAIVDDDPFVLQALRAYLSSDERIEVTSTFSRAADALAFLHKIRVDVLLTDVRMPEMDGLELLTRVRRQWPRTAVVVLTSFDDDEAMVAALAQHANGFLLKDASPEEIIRAVIAASAGGTTISPAATSRLVTRHLRSPQTAQAPDVTEAEQAVLTLLCEGYSNAEIAEQLVVAESTVKTHVSHLMKKYDVPSRLKLVVAVHKTQGA$","Two-component system regulatory protein","Cytoplasm","Two-component system, response regulatorsconsisting of a CheY-like receiver domain and a HTH","two-component system regulatory protein","response regulator receiver","","Pao G.M., Saier Jr M.H. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. J. Mol. Evol. 1995. 40(2):136-154. PMID: 7699720Blanco A.G., Sola M., Gomis-ruth F.X., Coll M. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 2002. 10(5):701-713. PMID: 12015152Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000. 69:183-215. PMID: 10966457","","","

InterPro
IPR000792
Domain

Bacterial regulatory protein, LuxR
PD000307	$\"[164-216]T$	Q9F2M5_STRCO_Q9F2M5;
PR00038	$\"[164-178]T$ $\"[178-194]T$ $\"[194-206]T$	HTHLUXR
PF00196	$\"[161-218]T$	GerE
SM00421	$\"[161-218]T$	HTH_LUXR
PS50043	$\"[157-222]T$	HTH_LUXR_2
PS00622	$\"[178-205]T$	HTH_LUXR_1

InterPro
IPR001789
Domain

Response regulator receiver
PD000039	$\"[17-130]T$	Q6ABR9_PROAC_Q6ABR9;
PF00072	$\"[17-131]T$	Response_reg
SM00448	$\"[17-130]T$	REC
PS50110	$\"[18-134]T$	RESPONSE_REGULATORY

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[159-224]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.2300	$\"[17-143]T$	no description
PTHR23283	$\"[17-134]T$	SENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF40	$\"[17-134]T$	TWO-COMPONENT SENSOR HISTIDINE KINASE BACTERIA

","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is 17","***** IPB000792 (Bacterial regulatory protein, LuxR family) with a combined E-value of 3.5e-19. IPB000792 164-210***** IPB000673 (CheB methylesterase) with a combined E-value of 2.7e-17. IPB000673A 20-29 IPB000673B 36-89 IPB000673D 129-141***** IPB005143 (Autoinducer binding domain) with a combined E-value of 1.6e-09. IPB005143B 164-207***** IPB001867 (Transcriptional regulatory protein, C terminal) with a combined E-value of 1.8e-08. IPB001867A 64-77 IPB001867B 92-136***** IPB001789 (Response regulator receiver) with a combined E-value of 8.6e-06. IPB001789A 64-77","","","-54% similar to PDB:1A04 THE STRUCTURE OF THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL IN THE MONOCLINIC C2 CRYSTAL FORM (E_value = 9.7E_27);-54% similar to PDB:1RNL THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL (E_value = 9.7E_27);-45% similar to PDB:1YIO Crystallographic structure of response regulator StyR from Pseudomonas fluorescens (E_value = 6.8E_12);-45% similar to PDB:1ZN2 Low Resolution Structure of Response Regulator StyR (E_value = 6.8E_12);-55% similar to PDB:1DZ3 DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A (E_value = 5.7E_11);","Residues 17 to 131 (E_value = 7.1e-36) place ANA_2731 in the Response_reg family which is described as Response regulator receiver domain.Residues 161 to 218 (E_value = 1.2e-13) place ANA_2731 in the GerE family which is described as Bacterial regulatory proteins, luxR family.Residues 165 to 205 (E_value = 6.3e-06) place ANA_2731 in the Sigma70_r4_2 family which is described as Sigma-70, region 4.","","system, response regulators consisting of a CheY-like receiver domain and a HTH DNA-binding domain","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2732","2944115","2941635","2481","8.39","4.60","84704","ATGCCTTCGCTCCTCGACCTGCGGCGAACCATCTCCGCCCTCGTGGCCGTGGCCATGAGCGCCGCCCTCATCGCCTTCGCCTTCATCATCTCCGACTCCTTCCGCACTCAGACGCAGACCAGCGCACGGGTGTCCGTAGGCGACGCCGCTGTCGTCGTCCAGGATGGTCGTGGGGCCAAAAGCACTGAAAAAGCCCTGGACGACTCCCTCCTCAACCGGGTCTCCGCCCTTGACGGCGTCGCCTCGGTCCGCGGCGCCCACTGGGACATGCTGGGGCTCGACCTGCCCAAGCAGCTGAGCCACTCCGTCGGAGCCCAGATCGCCGCGCAGGACGTCCCGGCACTTACCAAGTTCACCACCCTGAGCAGAGGCCGACTCCCCAAGACAACCGGCGAAGTCGCCATCGACTCCATGCTCGCCGAGCAGCAAGGCCTGAGCGTCGGCGACACCATCCGGCTCACGTCCAAGATTGACGACGCCAAGGCCGTCCACTCGGCACCCACAGTGGTCGGCATCATCTCCGCCGGGGCCGACAGCAGGGAGACCGACACCGACACCCTCTACGCCACCACCGAGCAGCTCCAGGCAATGGGCGCTCGTATGGACTACCGCAGCCTGTACGTGAAGGCGAAGCCGGGAACGGACGCAAGCGCACTCCTCACCAAGGTGTCTCAGACCGTTCACTCGGTCCAGCCCGCCGCATCGGTTCAGAGCCGAGACGAGGCCATCGCTCAACGCGCCCAGGCGCAGACGGGCGGCACAACGATTGCGAGCATCATCAATCTCCTGGCCCCGGTCTGTGCGGTCGTCGCCATCATCGTCATCGCCACCACCTTCAGCACCCTGGTGGCGCGTCAGACACGCATGGTCGGACTCATGCGCTGCATCGGCACAACCCGCCGTCAGGTGATGCTCTCCGTCCTGCGCACCGGACTCATGACGGGTCTGGTCGGCTCCGTCCTGGGCGCGGCACTCGGGACCGGCCTCGGCGCCATCGCGGTGTCCTCGGGAACCTTCGCGGACCTCAAGGCGGATCAGCTCACCATCTCCCCAGTGTCGCTCGGGCTCACCGTCGCCCTGGGGACGCTAGTCACCCTCATCGCGGTCCTGCGCCCGGCCCGCAAGGCCACCCGCATCTCACCGCTCGTGGCGCTTACAGGACAGGTCACAAGCACCAAGCAGGCCGGACGCAGAAGGATGTGGGTCGCTGTCGCCGGAGTCATCATCGCTGTCATCGGTGCGGCCATCGTCGCCCTCGGCATTCAGGCCTCCGATATCTACATCACAGCATCTGGAAGCGCCGTCGTCGTCGTTGGGACCGTCCTCAGCCTTCCTCTGCTCGTCACCGCCATCATTGGCTTCATCGGCAAAGTCAGCGGGGACACTCGACTCCCGGTGCTGCAGCTGGCCACACGCAATCTGGCCCGCAACTCCGGACGCTCCGCCGCCACCGCCGCCACACTCTTCGTCTGCGTCCTGGTGGGGTCAGCGCTCTTCGTCGGCCTGTCCTCTCTGAACGCCTCCTTCGACGCCATCCTCGGCCACAGCTCACCCGTGGACGCCAGGATCTTCGGGGTCACGCCGCAGACCGATACCGCGCAGCTAACGAAGCAGGTCAAAGCAGTCGACGGCGTCAAGGACGTCACCTACGTTCCCACCCTCGACCTGACCCAGACCGTCGACGGAGAATCGGAGGACATCAGTGTCGACGTCATTGATACCGGCAGTATCGCGCCTATTGCACGGTCCACCAGCGGCTTGGAGGGCCTCGATGACAAGACCCTCATCGTGAGCGGCATCTATAACATTCCGGACGGCTCCACAGTCACCCTAACCGGGGCAACCGGAAGTGTTGAGCTGACGGCTCGCGTCCAGGAGGGGTGGGGAGCTGTGGTCAGCCCGGCAGTGGCCCAGCGCCTCAACGGCGACACTCCCACCAACGCCACCGTGTGGGTGCGCTCCACCGGCAATTCCATGACATCCGATACCGAGCACGCCCTCATTGCGGCCATCCGCGGTCAAGAAATGATGGTGAGCGGAAGCGCGTCAGCGAGCGAGCAGATGTCATCCCTCATCACGAGGATGGCCCTCATCGTCTGCCTGGTTCTGGGCGCAGCCCTGGTCATCGCCTTGTCCGGGCTGGCCAACACCACGGACGTCTCGGTCCTGGAGCGCATTCGGGAAATCGGGGTTCTACGCGCCACCGGCAGCCCTCGCTCGGAGATCAGGAACCTCATCGTGACCGAGGGGGTCCTCGTGGCGACCGTGGGTGGGGGCCTGGGACTCCTCGTGGGGACGGCGCTGGGCGTTTCCGAAACGCTCGCGATGGCCAAGTCCGCCGAAGGCATGACGGTGCACGTCCCCTACTTCGCACTGATCGGCATGTTCGCCGTGACGCTGGCCGTGGGCCTGGCGGCCTCGCTACGCCCGGCCGGCCGGGCCGCCTCGGTGCCGCCGGTCAGGGCCCTGTCCGAGGAGTGA","MPSLLDLRRTISALVAVAMSAALIAFAFIISDSFRTQTQTSARVSVGDAAVVVQDGRGAKSTEKALDDSLLNRVSALDGVASVRGAHWDMLGLDLPKQLSHSVGAQIAAQDVPALTKFTTLSRGRLPKTTGEVAIDSMLAEQQGLSVGDTIRLTSKIDDAKAVHSAPTVVGIISAGADSRETDTDTLYATTEQLQAMGARMDYRSLYVKAKPGTDASALLTKVSQTVHSVQPAASVQSRDEAIAQRAQAQTGGTTIASIINLLAPVCAVVAIIVIATTFSTLVARQTRMVGLMRCIGTTRRQVMLSVLRTGLMTGLVGSVLGAALGTGLGAIAVSSGTFADLKADQLTISPVSLGLTVALGTLVTLIAVLRPARKATRISPLVALTGQVTSTKQAGRRRMWVAVAGVIIAVIGAAIVALGIQASDIYITASGSAVVVVGTVLSLPLLVTAIIGFIGKVSGDTRLPVLQLATRNLARNSGRSAATAATLFVCVLVGSALFVGLSSLNASFDAILGHSSPVDARIFGVTPQTDTAQLTKQVKAVDGVKDVTYVPTLDLTQTVDGESEDISVDVIDTGSIAPIARSTSGLEGLDDKTLIVSGIYNIPDGSTVTLTGATGSVELTARVQEGWGAVVSPAVAQRLNGDTPTNATVWVRSTGNSMTSDTEHALIAAIRGQEMMVSGSASASEQMSSLITRMALIVCLVLGAALVIALSGLANTTDVSVLERIREIGVLRATGSPRSEIRNLIVTEGVLVATVGGGLGLLVGTALGVSETLAMAKSAEGMTVHVPYFALIGMFAVTLAVGLAASLRPAGRAASVPPVRALSEE$","ABC-type transport system involved in lipoprotein release, permease component","Membrane, Cytoplasm","putative ABC transport system integral membraneprotein","K02004","protein of unknown function DUF214","","","","","

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[203-381]T$ $\"[645-819]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[264-284]?$ $\"[305-339]?$ $\"[349-369]?$ $\"[401-421]?$ $\"[435-455]?$ $\"[482-502]?$ $\"[695-715]?$ $\"[751-771]?$ $\"[785-805]?$	transmembrane_regions

","BeTs to 14 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","","","-43% similar to PDB:1B8F HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA (E_value = );-43% similar to PDB:1EB4 HISTIDINE AMMONIA-LYASE (HAL) MUTANT F329A FROM PSEUDOMONAS PUTIDA (E_value = );-43% similar to PDB:1GK2 HISTIDINE AMMONIA-LYASE (HAL) MUTANT F329G FROM PSEUDOMONAS PUTIDA (E_value = );-43% similar to PDB:1GK3 HISTIDINE AMMONIA-LYASE (HAL) MUTANT D145A FROM PSEUDOMONAS PUTIDA (E_value = );-43% similar to PDB:1GKJ HISTIDINE AMMONIA-LYASE (HAL) MUTANT Y280F FROM PSEUDOMONAS PUTIDA (E_value = );","Residues 203 to 381 (E_value = 5e-28) place ANA_2732 in the FtsX family which is described as Predicted permease.Residues 645 to 819 (E_value = 3.9e-26) place ANA_2732 in the FtsX family which is described as Predicted permease.","","ABC transport system integral membrane protein","","1","","","","","","","","","","","Tue Aug 14 17:34:28 2007","","","","","Tue Aug 14 17:34:28 2007","","","","Tue Aug 14 17:34:28 2007","Tue Aug 14 17:34:28 2007","","","","","yes","","" "ANA_2733","2945164","2944115","1050","9.00","7.01","36575","GTGGACAGGGGCTCGCGCGTCCCGTCCTTCGACGCATTCCGTTGTGATGGCGCCGTTTCTAGGCTTTTTCACGTCAACAGGGCAACCCCCGGACGCGACACGAATCAGACGACCGGCCCTGCCTACCACACGAGTCAGCCACACGAGAAGGGTCCTGAGATGACGACTCAACCCCAGCCCCCGTCCTTCAGCCACGCCGCCAATCCCGCTCCGGTCCCCCAGGGAGGACGGGTGGCCCAGGGAGCACCGGGGGCACCTGCCGCTGCTGCCGCCCCGATGCACGTCGTCGAGGCCCGCGGCCTGACCAAGGTCTACGGCGAGGGCGAGGCCCGGGTCGTCGCCCTGGACTCGGCGAGCCTGGTGGTGGGACGCGGCGAGTTCGTGGCCATCATGGGCCCCTCCGGCTCGGGCAAGTCCACTCTCTTGCACTGCCTGGCGGGCCTGGACACCCCCACCTCCGGCAGCGTCCTCATCGCTGGTCAGGACCTGTCGGGCATGAAGGACAAGCAGCTCACCGCCGTGCGCCGCGACCGCCTCGGCTTCATCTTCCAATCCTTCAACCTGCTGCCTACCTTGAGCGCCGAGGAGAACATCCTCCTGCCTCAGCGCCTGGCCCACCGCAAACCACAGCGGGACTGGTACGACGCCGTCATCTCCACCCTGGGCATCGGTGACCGCCTGTCCCACCGGCCCCACGAGCTCTCCGGCGGCCAGCAGCAGCGAGTGGCCGTGGCCCGCGCCCTCGTGGGCCGCCCCGAGGTTGTCTTCGCCGATGAGCCCACCGGGGCGCTGGACACCGCCTCGGCCGCCGCCCTGCTGGAGACCCTGGCCGGCATGTGCGAGCGCCTGGGGCAGACCGTCGTCATGGTCACCCACGACGAGCAGGCGGCCGCGACCACCAACCGCATCATCCGCCTGCGCGACGGGCACATCACCGGGGTCGAGGCCGTGCGCCGCCCGGCCGGTACCCGCGTGGCCGGGTCCGGCGCCCATCACGCCGCCGTCCCCTCCCCCGCTGCCGGCCCTGCACCCCGGATGGAGGCCCGCTGA","VDRGSRVPSFDAFRCDGAVSRLFHVNRATPGRDTNQTTGPAYHTSQPHEKGPEMTTQPQPPSFSHAANPAPVPQGGRVAQGAPGAPAAAAAPMHVVEARGLTKVYGEGEARVVALDSASLVVGRGEFVAIMGPSGSGKSTLLHCLAGLDTPTSGSVLIAGQDLSGMKDKQLTAVRRDRLGFIFQSFNLLPTLSAEENILLPQRLAHRKPQRDWYDAVISTLGIGDRLSHRPHELSGGQQQRVAVARALVGRPEVVFADEPTGALDTASAAALLETLAGMCERLGQTVVMVTHDEQAAATTNRIIRLRDGHITGVEAVRRPAGTRVAGSGAHHAAVPSPAAGPAPRMEAR$","ABC-type transport system involved in lipoprotein release, ATPase component","Membrane, Cytoplasm, Extracellular","possible ATP binding protein of ABC transporter","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[233-260]T$	Q9K3M8_STRCO_Q9K3M8;
PF00005	$\"[125-309]T$	ABC_tran
PS50893	$\"[96-333]T$	ABC_TRANSPORTER_2
PS00211	$\"[234-248]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[124-310]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[90-319]T$	no description
PTHR19222	$\"[96-312]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32	$\"[96-312]T$	ABC TRANSPORTER

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[240-399]T$ $\"[666-844]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-32]?$	signal-peptide
tmhmm	$\"[29-49]?$ $\"[280-302]?$ $\"[329-349]?$ $\"[368-388]?$ $\"[418-440]?$ $\"[446-466]?$ $\"[504-524]?$ $\"[716-736]?$ $\"[772-794]?$ $\"[813-833]?$	transmembrane_regions

","BeTs to 15 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: R [General function prediction only]The phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 8","No significant hits to the Blocks database.","","","-40% similar to PDB:1ZK7 Crystal Structure of Tn501 MerA (E_value = );-40% similar to PDB:1ZX9 Crystal Structure of Tn501 MerA (E_value = );-38% similar to PDB:1M6N Crystal structure of the SecA translocation ATPase from Bacillus subtilis (E_value = );-38% similar to PDB:1M74 Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis (E_value = );-38% similar to PDB:1TF2 Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis (E_value = );","Residues 240 to 399 (E_value = 2.1e-20) place ANA_2735 in the FtsX family which is described as Predicted permease.Residues 666 to 844 (E_value = 4.1e-28) place ANA_2735 in the FtsX family which is described as Predicted permease.","","ABC transporter, Dbv18","","1","","","","","","","","","","","Tue Aug 14 17:35:42 2007","","","","","Tue Aug 14 17:35:42 2007","","","","Tue Aug 14 17:35:42 2007","Tue Aug 14 17:35:42 2007","","","","","yes","","" "ANA_2736","2948211","2949062","852","5.27","-10.11","29275","GTGCCCCGCGACCGGACGCTCCTCATGGGCGTCCTCAACGTCACCCCCGACTCCTTCTCCGACGGCGGCCGCTGGGCCGACCCCGAGGCGGCCGTCGCCCACGCCCGCGAGCTCATCGCCCAGGGCGCCGACATCATCGACGTCGGCGGGGAGTCCACCCGCCCCGGCGCCCAGAAGGTTGACGTCGACACCGAGATCTCCCGGGTCCTGCCCGTGGTGCGCGCCCTCCTCGCCGACGGGGCAGGCAGTGCCGACGGGGCAGGCGCCTCCGGCAGCGCCATCGTCTCGGTGGACACCATCCACGCCGCCACCGCCGAGGCCGCCATCGACGCCGGCGCCCACATCATCAACGACGTCTCCGGGGGCCTGGCCGACCCAGCCATGCACAGCCTCATCGCCCGCACCGGCGTCGTCTACGTCTGCCAGCACTGGCGAGGCGACCCCGAGACCATGGACCGGCTCACCGACTACCCCGGCGGCGTCGTCGCCGGAGTCGAGGCCGAGCTGCGCGAGCGCCTGGCCGAGCTGGACGCCGCCGGGGTGGACCGCTCCCAGGTGGTCCTGGACCCCGGCCTCGGCTTCGCCAAGACCCACGCCCAGTCCTGGGAGCTGCTGGCGGCCACCTCCCGCCTCATCGCCGACCTGGGCCGGCCCCTCCTGGTCGGCTCCTCCCGCAAGCGCTTCCTCGCCCAGGCCGCTGAGGCCGAGGCCACCCCCGTCCAGCGCGACGCCGTCACCGCCGCCACCACCGCCCTGGCCGCCGCCTCAGGCGCCTGGGCCGTCAGAGTCCACGAGGTCCCGGCCAACCGGGCCGCCGTCCGTACCGCCTCCCTCTGGAAGGAACACCAGTGA","VPRDRTLLMGVLNVTPDSFSDGGRWADPEAAVAHARELIAQGADIIDVGGESTRPGAQKVDVDTEISRVLPVVRALLADGAGSADGAGASGSAIVSVDTIHAATAEAAIDAGAHIINDVSGGLADPAMHSLIARTGVVYVCQHWRGDPETMDRLTDYPGGVVAGVEAELRERLAELDAAGVDRSQVVLDPGLGFAKTHAQSWELLAATSRLIADLGRPLLVGSSRKRFLAQAAEAEATPVQRDAVTAATTALAAASGAWAVRVHEVPANRAAVRTASLWKEHQ$","Dihydropteroate synthase","Cytoplasm","dihydropteroate synthase","dihydropteroate synthase ","dihydropteroate synthase","","Slock J., Stahly D.P., Han C.Y., Six E.W., Crawford I.P. An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene. J. Bacteriol. 1990. 172(12):7211-7226. PMID: 2123867Volpe F., Dyer M., Scaife J.G., Darby G., Stammers D.K., Delves C.J. The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase. Gene 1992. 112(2):213-218. PMID: 1313386","","","

InterPro
IPR000489
Domain

Dihydropteroate synthase, DHPS
G3DSA:3.20.20.20	$\"[1-279]T$	no description
PF00809	$\"[11-233]T$	Pterin_bind
PS50972	$\"[6-274]T$	PTERIN_BINDING
PS00792	$\"[8-23]T$	DHPS_1
PS00793	$\"[42-55]T$	DHPS_2

InterPro
IPR006390
Domain

Dihydropteroate synthase
TIGR01496	$\"[7-279]T$	DHPS: dihydropteroate synthase

noIPR
unintegrated

unintegrated
PTHR20941	$\"[28-278]T$	FOLATE SYNTHESIS PROTEINS
PTHR20941:SF1	$\"[28-278]T$	DIHYDROPTEROATE SYNTHASE

","BeTs to 18 clades of COG0294COG name: Dihydropteroate synthase and related enzymesFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0294 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB000489 (Dihydropteroate synthase, DHPS) with a combined E-value of 7.5e-74. IPB000489A 8-23 IPB000489B 38-73 IPB000489C 95-121 IPB000489E 176-197 IPB000489F 218-230 IPB000489G 257-266","","","-53% similar to PDB:1EYE 1.7 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTEROATE SYNTHASE (DHPS) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH 6-HYDROXYMETHYLPTERIN MONOPHOSPHATE (E_value = 7.7E_38);-48% similar to PDB:2DQW Crystal Structure of Dihydropteroate Synthase (FolP) from Thermus thermophilus HB8 (E_value = 9.7E_33);-48% similar to PDB:2DZA Crystal Structure of Dihydropteroate Synthase from Thermus thermophilus HB8 in Complex with 4-aminobenzoate (E_value = 9.7E_33);-48% similar to PDB:2DZB Crystal Structure of Dihydropteroate Synthase from Thermus thermophilus HB8 in complex with 6HMPPP (E_value = 9.7E_33);-50% similar to PDB:1TWS Dihydropteroate Synthetase From Bacillus anthracis (E_value = 2.2E_29);","Residues 11 to 233 (E_value = 2.5e-81) place ANA_2736 in the Pterin_bind family which is described as Pterin binding enzyme.","","synthase (folP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2737","2949059","2951875","2817","4.07","-91.67","93343","GTGAGCACCACCGTCTCCGCGACCACCGACCGGATCAGCCTCATCGGCCTGTCCGCCCGTGGCCACCACGGCGTCCTGCCCTTCGAACGCGAGGAGGGCCAGCTCTTCACGGTCGATGTCATTCTTGACCTGGGGCAGCGCGGCACCGCCGTGGCCGCCGTCACCGACTCGGTGACCGACGCCGTGGACTACTCCCGCGTGGCCAACGGCATCGTGAGCATCATCGAGGGGGAGCCGGTCAATCTCATCGAGTCCCTGGCGGACCGGATCGCCGAGCGGGTCCTGTCCTTCCCCCGCGTCGTGGCCGCCGAGGTCACCGTGCACAAGCCCGAGGCCCCTCTCGATGTCGCCTTCGAGGACGTCTCAGTGACCATCCACCGAGTGGCCGACGCCGCCGCCGGCCACGGCGGGGCCCCCGCCACCAGCCAGGCCGCCTGGGCCGCGCAGGCCGAGGCGCCGGTGGCCGTCTCCGCCCAGCCCTACGCCTCCCCCTCCTCCTCGGCCTCCCCGGTGGCCGCCGCCTCCCCGGCAGCGCCCGCCTACGAGCCCCCCGCCGCCCCCGCGGCCCCCGTCGTCGCGGAGGTCCCCGACTTCTCGGGAGCCTCCTTCACGGGCGGCGACGCCGCTCCGGCCACCTTGGCCTCCGAGCCCCCCATCACCCCGACGCCCTCGCCGGCCTCGCCGATGGAGGCTCCGGCCCGCTCGCCCTTCGCTGCCGCCGCGCCCTCGGTCCCCACGCCGATGCCGGCCGAGCCCGGCGCCGTCGGTGGGGGCGCCGAGTCGACCCAGCCCTGGGCGCCGGACTGGGCCACCGAGAGCGCGGACTCCTCCGTCGCATCGGCCCCCTCCTGGGCCCCCGAGACCCCGGAGGCCCCCGAGGTCGCCGGCCTGACCTCCGGTGAGTCCACCGGTGAGTCCGCCGATTCCTACGCGGCGTCGAGCGCACTGGACGCCCCCTCGACCAGCGCCCCCACCGCGGCCTCCGCCGGCAGGACCACCGGTGCCGACGGGTTCGTGAGCCTGGCAGCCGACGCCCTGGGCGCGGCGCCCGCCACCAGTGAGCCGGAGGCCAGTGCCCTGAGCTATGCCGAGGAGGTGGCCGCTGACGCCTCCGCAGCAGCCTCGTCCGAGCCGGCTCCCGCCGCCGACGGCCTTGCTGTTCAGCTGCCCCGCGAAGGGCGCCACGTCGCCTCCTCCGAGGAGGGCGAGGGCCAGTCCGCCCCCGCTGTCGAGGGCTCCGCAGACCTTTTGAACGCTCCCGTCGCCTTCGACGAGTCCGGCTCCTACAGCGGAGCCGCCGCCAGCCAGGTCGGTGACGCCGGGGCCGACCCCGAGGCAGCGGTCGCCGATGCTGCCGGCTTCCCCTTCCCCGCGCTGGGTGGGGACGTCTCCGCCTCCGGGACCGCCGCTGACGGTTTCGTTGACTCCTCCTCCGTCCCGGCCTCCCAGTCCCTGGGAGAGCCCGGGCCCAGCCCCTTCGACGTCCCCGGTGAGCTCCCCGGGGCCGTGAGCCAGGACGGCGTGGTACCGGCTTACTCCGAGTCCTCATACTCCGAGCCCTCCTACTCCCAGCCCTCCGTCTCCGAGGACTTCTCCCAGCCCGCTGAGGGCTCGTACGCCGCGCCGTCGGCGCAGCCCGACGTCCTGGGCGCCCCCGGCGCCGCACCGGCTCCCGTTGCGCCTGAGGCCCCGGCGGCTCCCGCAGCTCCGGTGGACCCGCTCTCCGAGCGGCCCGCCCGCCCCGTCGGCGTCGTCTTCGGCCTGGGCGCCAACGTCGGCGGAGTCGTGGACTCCCTGCGCACGGCCGTCCAGAGCCTCAGGGCCACCGAGGGCATCGAGGTCACGCAGGTGGCGCCACTGGCCCGCACGCTCGCCGTCGTCGCCGAGGGCGCCGAGCCCCAGCCCGACTACCTCAACACGGTGGTCACAGCCATGACGACCCTCTCCCCGCGCGAGCTGCTCGAGGTCTGCCAGACCCTGGAGATCGCGGCCGGGCGCGTGCGCACCGAGCCGTGGGGCGTGCGCACCCTGGATGTGGACCTGATCGACGTCGAGGGCATCACCTCCTCCGACCCGGCCCTGTCCCTGCCGCACCCGCGCGCCGCTGAGCGTGCCTTCGTCCTGGTGCCGTGGAGCCAGGCCGACCCCTTCGCCGAGCTGGCCGGGCACTCCGTGTCCGAGCTCGCCGAGAACGCCCCCGACCGGGGTGGCCTGCGCTGGCTGGCCTTCGACTGGCTCGACTCCGAGGCTCTGCCGGACAAGCCCACCGGCCCCTACGTGGAGCCCCCGGTGGCGCAGGACGCCGCAGGCTCCGAGCCCGGGCTGGTCTATGACGCCACCCGAGACGAGTCCTCCGTGGCCGACGCCTCCCTGGCTGCCGACTACGCCGGCAGTATCGCCGAGGCCTCATCGCCCGCCCCGGAGCCCGCCGCCCCCGCGCAGCAGCTCGGTGACCAGGGGCCGTTCGAGTCCTCCCCCTTCGGGCAGTCGCCTTTCGACACCTCCAACGAGGCGGGCTCCTGGGGCGAGCAGGCCCCGCAGATCGACTCGCCCTACCAGGCCGCTTCGGCCCCCGAGGCCGCCGGACCGCAGGGCGCCTACGCCCCCGGTCTCACGGCCGGGTCGGATGGGCTCCCCCACGGCCAGCAGAATGTCGGCAGCTACGCGAACTACGCCTCCAGCCAGCCGGAACAGGCCGATGCCCCGGCCTCGCAGCAGCAGAATGACGCCGCCGGGGACGCCTGGAAGTCCCCGCTCCAGTGGAACGACGTCATCGGTGGTGGCGCCCAGGGGACAGGTCCCCGTCAGGACGTCTGA","VSTTVSATTDRISLIGLSARGHHGVLPFEREEGQLFTVDVILDLGQRGTAVAAVTDSVTDAVDYSRVANGIVSIIEGEPVNLIESLADRIAERVLSFPRVVAAEVTVHKPEAPLDVAFEDVSVTIHRVADAAAGHGGAPATSQAAWAAQAEAPVAVSAQPYASPSSSASPVAAASPAAPAYEPPAAPAAPVVAEVPDFSGASFTGGDAAPATLASEPPITPTPSPASPMEAPARSPFAAAAPSVPTPMPAEPGAVGGGAESTQPWAPDWATESADSSVASAPSWAPETPEAPEVAGLTSGESTGESADSYAASSALDAPSTSAPTAASAGRTTGADGFVSLAADALGAAPATSEPEASALSYAEEVAADASAAASSEPAPAADGLAVQLPREGRHVASSEEGEGQSAPAVEGSADLLNAPVAFDESGSYSGAAASQVGDAGADPEAAVADAAGFPFPALGGDVSASGTAADGFVDSSSVPASQSLGEPGPSPFDVPGELPGAVSQDGVVPAYSESSYSEPSYSQPSVSEDFSQPAEGSYAAPSAQPDVLGAPGAAPAPVAPEAPAAPAAPVDPLSERPARPVGVVFGLGANVGGVVDSLRTAVQSLRATEGIEVTQVAPLARTLAVVAEGAEPQPDYLNTVVTAMTTLSPRELLEVCQTLEIAAGRVRTEPWGVRTLDVDLIDVEGITSSDPALSLPHPRAAERAFVLVPWSQADPFAELAGHSVSELAENAPDRGGLRWLAFDWLDSEALPDKPTGPYVEPPVAQDAAGSEPGLVYDATRDESSVADASLAADYAGSIAEASSPAPEPAAPAQQLGDQGPFESSPFGQSPFDTSNEAGSWGEQAPQIDSPYQAASAPEAAGPQGAYAPGLTAGSDGLPHGQQNVGSYANYASSQPEQADAPASQQQNDAAGDAWKSPLQWNDVIGGGAQGTGPRQDV$","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Extracellular, Periplasm","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, putative","putative hydroxymethyldihydropteridine pyrophosphokinase ","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","","Thomas M.C., Ballantine S.P., Bethell S.S., Bains S., Kellam P., Delves C.J. Single amino acid substitutions disrupt tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carinii. Biochemistry 1998. 37(33):11629-11636. PMID: 9709001","","","

InterPro
IPR000550
Domain

7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK
PF01288	$\"[585-714]T$	HPPK
TIGR01498	$\"[584-716]T$	folK: 2-amino-4-hydroxy-6-hydroxymethyldihy

InterPro
IPR006156
Family

Dihydroneopterin aldolase family
TIGR00525	$\"[10-127]T$	folB: dihydroneopterin aldolase

InterPro
IPR006157
Domain

Dihydroneopterin aldolase
PF02152	$\"[12-127]T$	FolB
TIGR00526	$\"[9-133]T$	folB_dom: FolB domain

noIPR
unintegrated

unintegrated
G3DSA:3.30.1130.10	$\"[8-130]T$	no description
G3DSA:3.30.70.560	$\"[582-741]T$	no description
PTHR20941	$\"[9-128]T$	FOLATE SYNTHESIS PROTEINS
PTHR20941:SF3	$\"[9-128]T$	DIHYDRONEOPTERIN ALDOLASE

","BeTs to 15 clades of COG0801COG name: 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0801 is ------yqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is 1","***** IPB000550 (7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK) with a combined E-value of 1.4e-25. IPB000550A 584-594 IPB000550B 621-654 IPB000550C 665-684 IPB000550D 694-711***** IPB006157 (Dihydroneopterin aldolase) with a combined E-value of 4.5e-23. IPB006157A 10-54 IPB006157B 82-91 IPB006157C 100-127","","","-52% similar to PDB:1NBU 7,8-Dihydroneopterin Aldolase Complexed with Product From Mycobacterium Tuberculosis (E_value = 4.5E_15);-52% similar to PDB:1Z9W Tetrameric structure of apo-7,8-Dihydroneopterin Aldolase from Mycobacterium tuberculosis (E_value = 4.5E_15);-52% similar to PDB:1CBK 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE FROM HAEMOPHILUS INFLUENZAE (E_value = 2.1E_12);-52% similar to PDB:1DY3 TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE. (E_value = 2.1E_12);-52% similar to PDB:1EQ0 SOLUTION STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE COMPLEXED WITH MGAMPPCP (E_value = 2.1E_12);","Residues 12 to 127 (E_value = 2.1e-22) place ANA_2737 in the FolB family which is described as Dihydroneopterin aldolase.Residues 585 to 714 (E_value = 5.3e-40) place ANA_2737 in the HPPK family which is described as 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK).","","pyrophosphokinase, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2738","2951875","2952978","1104","10.59","12.24","38225","ATGCGGCGCACCCGCTGGACCAGTGCCGTCACCTGGTTCATCGCCGCCGCGGTGACCTCCTGGGTGGCCGGTGACCTCCTGCTGCGTCACGTCGGCTGGGTCCCGGTCCTCTCTCCCTGGGGGGCGGTGACGGCGCTGGTCATTGCGGGCATCGTCCTGGTGGCGGGTCTGGCGGTCAGGCGCCTGCGGGCGCGCGAGCGCACCTGGATCACCCCGACCGGCGCCGCCACCACGGCGGCCGCCGCCCAGGCCTCAGCCATCGTGGGGGCGGTGCTCGGCGGCGTCTACGGCGGCGGGATCATCCTGGCGCTGGTGACGCCGCGCTCGCCGGCCATGACCCACCTGGCCTGGACCTCGACCGGCTGCCTGATCGCCTGCCTCCTGTGGTGCGTCGTCGGCTTCGTCGTCGAGCAGTGGTGCTCCATCTCCGGTGACGGCGACGACGACGGCTCGGCCGGCCCCTCCGGGCGGGGCCCCCGAAGGACCGGGAGCCCCCGCATGACCAGTCCCGGAACCGGCCCCGGCGCGATGCCCGGTACCAGCCCGGCCGCACCTGCTGCCCCCGCTGGCCCAGCCCCGGCACCCGTCCGCGCCGGTGAGCCGGCTACGCGGCCACCCGCCGGCGCCGACCCCTTCGCCCCCGACGGCGTCGTCTTCCACCCGGTCTCGCCCCGCCTCATCACCGCCCGCATTCTGGGGGTCGGTCTTTTCTGCGCCGTCGTCATCATCGGCTTCGCCATCCCCGGGGTGCTCGTCTCCTCCGGATACTTCATACCGGCGGGGATCTTCGCAGCGCTGTTCCTCTGGCAGCTCTGGCTCATTCCGCGCCAGGTGCGGGCCATGGGCTACGCCCTGGCCGACAACCACCTCCTGTGGCGACACGGCGTCATGTTCCGCTCCATCACCGTCACCCCATACGGGCGCATGCAGTTCGTGGACACCTCCCAGGGGCCGCTGGCCCGCTGGCTGGGCATCGCCGAGGTCAAGCTCCACACGGCCTCGGCCAGCACCGACGCCACGATCAACGGGCTGCCGGTGGCCGAGGCCGAGCGCCTGCGCCAGGTCCTGTCCCAACGCGGTGAGGAGAGGATGGCCGGGCTGTGA","MRRTRWTSAVTWFIAAAVTSWVAGDLLLRHVGWVPVLSPWGAVTALVIAGIVLVAGLAVRRLRARERTWITPTGAATTAAAAQASAIVGAVLGGVYGGGIILALVTPRSPAMTHLAWTSTGCLIACLLWCVVGFVVEQWCSISGDGDDDGSAGPSGRGPRRTGSPRMTSPGTGPGAMPGTSPAAPAAPAGPAPAPVRAGEPATRPPAGADPFAPDGVVFHPVSPRLITARILGVGLFCAVVIIGFAIPGVLVSSGYFIPAGIFAALFLWQLWLIPRQVRAMGYALADNHLLWRHGVMFRSITVTPYGRMQFVDTSQGPLARWLGIAEVKLHTASASTDATINGLPVAEAERLRQVLSQRGEERMAGL$","Integral membrane protein","Membrane, Cytoplasm, Extracellular","Uncharacterized ACR","hypothetical protein","membrane-flanked domain","","","","","

InterPro
IPR005182
Domain

Protein of unknown function DUF304, prokaryotic transmembrane adjacent region
PF03703	$\"[277-356]T$	DUF304

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide
tmhmm	$\"[9-29]?$ $\"[39-59]?$ $\"[86-106]?$ $\"[116-136]?$ $\"[226-248]?$ $\"[254-274]?$	transmembrane_regions

","BeTs to 3 clades of COG3402COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG3402 is -o--------r-b-------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 277 to 356 (E_value = 3.4e-17) place ANA_2738 in the DUF304 family which is described as Bacterial membrane flanked domain.","","ACR ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2739","2952975","2954735","1761","10.75","20.91","63216","GTGAGCCCCAGCTGGGAGAGCCGGCTGGAGGCCGCCCGGAAGGCCAGGGCGGACGCCGCGGGGGAGAGCGGGCCCGGCGCCTCCCGGGATCTGCCCCTGCCCGAAAATGTCACCTGGCACCGGGTCAGCCTCGTCACGCCGGTGCTGGAGGGCTGGAAGATCGTCACCGGTGTCCTGGCCTTCGTTACGGTCCAGAACCTCGACGAGCTGGTGCGCGCCTACCGCTTCATCTCCGAGCACGGCTTCACCCTGGGCGGGGGGATTGGCTACTACCTGCTCGGCCTGGTCGCGTTCATTGCCCTGTGGGTGGGGCTCGGGCTGCTCAGCTGGTGGCGGCGCGCCTACGCCGTGGACGCCGACGGCGTCTACCTGCGCTCAGGCATCCTCAGCCGCAAGCTGCGCACGGCCCGCCTGCCGCGCATCCAGTCGGTCGACGTCGTCCACCCCCTGCTCGGACGCATCTTCGGTCTGGGGCAGCTGACCGTCGAAGTCGCCGGGGGCCGGGACTCGCGGGTCGTCATCGGATTCCTCACCACCCGCGAGCTTCAGACCCTGCGCGACCGCATCCTCGACCTGGCCGCCGGACAGATCGACCTGCCCGGCCCCACTGTAGCGGGCGGCGCCGTCGGGGCGAGTGCAGTGGGCCGCGACACCGGCGGCATCGATAATGCCACGTCCGCCGTCAGGCCCGAGGGCCTCGCGCCCGAAGGGGTCGCCGGCTCTCAGGCCGCCCCCGAGCAGCGCGCCGTGCCGATGCAGGCCTCCCACTTCCAGGAGCACCCGCTCTACAGCGTCGACGGCTCTGTCCTCCTCGGGTCCCTGCTGCGCAGCGTTTCCCTCTACTTGTCTCTGATCCTGCCGACCGTTGTGATCGTGGTCGGCATCATCGCCTACGTCGTTGACGACCCGCCCAGTGGCGGGGTGTTCGCGCTCGCGACCACCTTCATGAGCACGGTCGCCGGGGCAGTCTCCCTGGTGTGGTCCCGATTCAACAGCGCCTGGAACTTCCAGGCCGCCGCCACCCCCAGCGGCATCCGCATGCGTTACGGGCTCACCTCCGACACCTCCCGCACGCTGCCGCCCGGACGGGTCCACGGCGTCGGGATCGCTCAGCCGATCCTGTGGCGCGGCAAGGACTGGTGGAAGGTGGACGTCACCGTGGCCGGCCGCGAGGACCGATCCCAGGACGGCCAGAACCGGCAGTTCGGCAACCTGCTCCTGCCCGTGGGGGTGCGCGACACCGCCTTGCGTGCGCTGTGGCTCGTGGTCCCCGACCTGGGCGTGCCCGACCCCGACAGGCTGCTCGCCCAGGCCCTCACCGGCCGCGACGATGACGGTGTCGGCGACCCGCAGGCCCCGGCGGGCTCAGCCGAGCGCGGCTTCGTGCGCATCAGCCGCCGCGGACGGCTCTTCCGCCCCCTGACCTGGCGGCGCGCAGCCATCGCCCTCACCGACACCTGCGTCATCATCCGCCACGGCCGCTGGCGGCGGCGAGTGGCCGTCTTCCCCTACGAACGCATCCAGTCCCTGCGTGTGCGCCAGGGGCCGCTGGCGCGCCGGCGGGGCCTGGCCTCCCTCCGACTCGACATGGTCGCCCAGGAGGTCCCCGCCTCGATCACCAACCTCGATGCCGCCGACGCCAAGGCCCTCGCGGCACGGATCAGTCAGCGGGCGCTGCACCGGGCCCGCGCCGAGCAGCTCGACCGGTGGCTCGCGCGCGCCGTCGCCGCCACGCAGCCTGCCGGGCCCTCAGCGCGCTAG","VSPSWESRLEAARKARADAAGESGPGASRDLPLPENVTWHRVSLVTPVLEGWKIVTGVLAFVTVQNLDELVRAYRFISEHGFTLGGGIGYYLLGLVAFIALWVGLGLLSWWRRAYAVDADGVYLRSGILSRKLRTARLPRIQSVDVVHPLLGRIFGLGQLTVEVAGGRDSRVVIGFLTTRELQTLRDRILDLAAGQIDLPGPTVAGGAVGASAVGRDTGGIDNATSAVRPEGLAPEGVAGSQAAPEQRAVPMQASHFQEHPLYSVDGSVLLGSLLRSVSLYLSLILPTVVIVVGIIAYVVDDPPSGGVFALATTFMSTVAGAVSLVWSRFNSAWNFQAAATPSGIRMRYGLTSDTSRTLPPGRVHGVGIAQPILWRGKDWWKVDVTVAGREDRSQDGQNRQFGNLLLPVGVRDTALRALWLVVPDLGVPDPDRLLAQALTGRDDDGVGDPQAPAGSAERGFVRISRRGRLFRPLTWRRAAIALTDTCVIIRHGRWRRRVAVFPYERIQSLRVRQGPLARRRGLASLRLDMVAQEVPASITNLDAADAKALAARISQRALHRARAEQLDRWLARAVAATQPAGPSAR$","Membrane protein","Membrane, Cytoplasm","Bacterial membrane flanked domain family","K08981 putative membrane protein","membrane-flanked domain","","","","","

InterPro
IPR005182
Domain

Protein of unknown function DUF304, prokaryotic transmembrane adjacent region
PF03703	$\"[109-189]T$ $\"[475-554]T$	DUF304

noIPR
unintegrated

unintegrated
tmhmm	$\"[88-108]?$ $\"[278-298]?$ $\"[308-328]?$	transmembrane_regions

","BeTs to 3 clades of COG3428COG name: Predicted membrane proteinFunctional Class: S [Function unknown]The phylogenetic pattern of COG3428 is -o--------r-b-------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-46% similar to PDB:1SIO Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF (E_value = );-46% similar to PDB:1SN7 KUMAMOLISIN-AS, APOENZYME (E_value = );-46% similar to PDB:1ZVJ Structure of Kumamolisin-AS mutant, D164N (E_value = );-46% similar to PDB:1SIU KUMAMOLISIN-AS E78H MUTANT (E_value = );-46% similar to PDB:1ZVK Structure of Double mutant, D164N, E78H of Kumamolisin-As (E_value = );","Residues 109 to 189 (E_value = 2.9e-15) place ANA_2739 in the DUF304 family which is described as Bacterial membrane flanked domain.Residues 475 to 554 (E_value = 1.5e-12) place ANA_2739 in the DUF304 family which is described as Bacterial membrane flanked domain.","","membrane flanked domain family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2740","2955856","2954888","969","5.60","-8.72","32816","ATGAGCGACATCGATGGCAGGGGCCCAGGTACAGGCGGCGAGCACGCGGGCCGGGTCCCGGCCGCCCCTGCCAGCCCGAGCAGGCCGGGCCGGCTGGGCGTTGGCATCATCTCCGCCGGGCGCGTCGGGGCGGTCCTGGGCTGCGCGCTGCGGGCGGTGGAGCACCAGGTCGTCGGCGTCCACGCGGTCTCGGAGGAGTCGCGCGAGCGTGCCGAGATGCTGCTTCCCGGTGTGCCGGTCCTGGAGGTCGAGGAGATCGTCGAGCGTGCCGAGCTGGTCCTGCTGGCCGTCCCTGACGACGCCCTCGGGCCGCTCGTCCAGGGCCTGGCGGACCTGGGACGCTGGCAGCCGGGCCAGCTGGTGGCCCACACCTCGGGGCGCTACGGCGCCACCGTGCTCGCCCCGGCTCAACGCTGCGGGGCGATCCCGTTGGCGATCCACCCGGCGATGACCTTCTCCGGGTTCTCCACGGATGTGGCCCGGCTCGTCGGCTGCCCGATGGCTGTGACTGCGCCCGCGGCGGTGCTGCCAATCGCGGAGGCGCTGGTGGTCGAGCTCGGCGGGGAGCCCTTCGTCCTGGAGGAGTCGGCGCGCCCTGCCTACCACGCAGCCCTCGCGCACGGCGCCAACCACCTGCTGACCGTGGTGACGCAGGCCGTGCGGGTGCTGGCGGCCGCCGGGGTCGAGGACGGTGCGGCCACGCTCGGTCCCCTGCTCACGGCGGCCCTGGACCGGGCGCTGCACGAGGGCGAGGCGGGCCTGACCGGTCCGGTCTCCCGGGGCGACGCCGGAACGGTGGCCGCCCACCTGGAGGCGCTCTCCACGCTGCGCGACAGCCAGGGGCGGGGCCTCGACGACGTGGTCGCCTCCTACCGGCAGCTGGCCGCGGCCACCACTGAGCGCTGCGAGGCCACCGGGCGCCTGACCGCCGAGCAGGCCCTGCGCCTGCGCGACGCCCTGCGCAGCTAG","MSDIDGRGPGTGGEHAGRVPAAPASPSRPGRLGVGIISAGRVGAVLGCALRAVEHQVVGVHAVSEESRERAEMLLPGVPVLEVEEIVERAELVLLAVPDDALGPLVQGLADLGRWQPGQLVAHTSGRYGATVLAPAQRCGAIPLAIHPAMTFSGFSTDVARLVGCPMAVTAPAAVLPIAEALVVELGGEPFVLEESARPAYHAALAHGANHLLTVVTQAVRVLAAAGVEDGAATLGPLLTAALDRALHEGEAGLTGPVSRGDAGTVAAHLEALSTLRDSQGRGLDDVVASYRQLAAATTERCEATGRLTAEQALRLRDALRS$","Uncharacterized conserved protein","Cytoplasm","chalcone/stilbene synthase family protein","hypothetical protein","conserved hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[32-111]T$	no description

InterPro
IPR003721
Family

Pantoate-beta-alanine ligase
PTHR21299:SF1	$\"[40-333]T$	PANTOATE-BETA-ALANINE LIGASE
PF02569	$\"[31-330]T$	Pantoate_ligase
TIGR00018	$\"[20-331]T$	panC: pantoate--beta-alanine ligase

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[7-204]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.1300.10	$\"[205-333]T$	no description
PTHR21299	$\"[40-333]T$	CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE

","BeTs to 14 clades of COG0414COG name: Panthothenate synthetaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0414 is ------yqvdr-bcefg-snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003721 (Pantoate-beta-alanine ligase) with a combined E-value of 2.9e-81. IPB003721A 68-97 IPB003721B 146-185 IPB003721C 191-236 IPB003721D 312-327","","","-46% similar to PDB:1MOP Crystal Structure of a Pantothenate Synthetase from M. tuberculosis (E_value = 2.8E_37);-46% similar to PDB:1N2B Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with AMPCPP and pantoate, higher occupancy of pantoate and lower occupancy of AMPCPP in subunit A (E_value = 2.8E_37);-46% similar to PDB:1N2E Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with AMPCPP and pantoate (E_value = 2.8E_37);-46% similar to PDB:1N2G Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with AMPCPP (E_value = 2.8E_37);-46% similar to PDB:1N2H Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with a reaction intermediate, pantoyl adenylate (E_value = 2.8E_37);","Residues 31 to 330 (E_value = 4.2e-85) place ANA_2741 in the Pantoate_ligase family which is described as Pantoate-beta-alanine ligase.","","ligase (panC)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2742","2957133","2957813","681","8.62","5.95","24185","GTGCCCGGCTCGCCCGGGTGCTTGCGCGGGGCCAACCGCTGTGAACCGGGCCGGCCCCGCGCGAGGACGCACCCTCAAGCGACAGACCCGGCGCCCTATGGCGTGTTCTCGAGAACCGTTGGGCCGGGCCTGGCCTCGCTCAGGTCCGACCGTTCCTGTCAGGTCGCTCACCCTGTGCCGCACCGTACAGTGCTCCGGGCCCGGCGCCGTCTACGCTGTGCGGCGATGAGTTCCCGCACCCGGACGATGATGACGTCCAAGATCCACCGCGCCACCGTGACCCAGGCCGACCTCGACTACGTCGGCTCCATCACGGTGGACATCGACCTGCTCGAGGCCGCCGACCTGCTGCCCGGCGAGCGCGTCGATATCTGCAACTGCACCAACGGCAACCGCCTGTCCACCTACGTCATCCCCGGCGAGCGCGGCGCCGGCGAGATCTGCGTCAACGGCGCTGCCGCCCACCTGGTCAGCCCCGGAGACGTCGTCATCCTCATCGCCTACTCCCAGATGTCCGACGCCGAGGCCCGCACCTACCTGCCCCGGGTCGTCTTCGTCGACGAGGCCAACCGGATCGTGGAGCGGGGCACCGACCCCGGCCAGATCCCGGCCGACTCCGACGTCGCCCGCATTCAGGGCCTGCGGCCCACCGGCATCCCCCTGGCCGAGGCCCGCGCCTGA","VPGSPGCLRGANRCEPGRPRARTHPQATDPAPYGVFSRTVGPGLASLRSDRSCQVAHPVPHRTVLRARRRLRCAAMSSRTRTMMTSKIHRATVTQADLDYVGSITVDIDLLEAADLLPGERVDICNCTNGNRLSTYVIPGERGAGEICVNGAAAHLVSPGDVVILIAYSQMSDAEARTYLPRVVFVDEANRIVERGTDPGQIPADSDVARIQGLRPTGIPLAEARA$","Aspartate 1-decarboxylase","Cytoplasm, Extracellular","Aspartate 1-decarboxylase precursor (Aspartatealpha-decarboxylase)","aspartate 1-decarboxylase ","aspartate 1-decarboxylase","","","","","

InterPro
IPR003190
Family

Aspartate decarboxylase
PD009294	$\"[81-184]T$	PAND_STRCO_P58286;
PTHR21012	$\"[80-215]T$	ASPARTATE 1-DECARBOXYLASE
PF02261	$\"[80-194]T$	Asp_decarbox
TIGR00223	$\"[80-207]T$	panD: aspartate 1-decarboxylase

noIPR
unintegrated

unintegrated
G3DSA:2.40.40.20	$\"[62-204]T$	no description

","BeTs to 12 clades of COG0853COG name: Aspartate 1-decarboxylaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0853 is -------qvdr-bcef--snuj----Number of proteins in this genome belonging to this COG is 1","***** IPB003190 (Aspartate decarboxylase) with a combined E-value of 3.6e-70. IPB003190A 83-120 IPB003190B 121-165 IPB003190C 167-190","","","-78% similar to PDB:2C45 NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE (E_value = 2.0E_40);-77% similar to PDB:1VC3 Crystal Structure of L-Aspartate-alpha-Decarboxylase (E_value = 1.7E_26);-64% similar to PDB:1PPY Native precursor of pyruvoyl dependent Aspartate decarboxylase (E_value = 3.8E_26);-63% similar to PDB:1PQH Serine 25 to Threonine mutation of aspartate decarboxylase (E_value = 4.9E_26);-64% similar to PDB:1PQE S25A mutant of pyruvoyl dependent aspartate decarboxylase (E_value = 8.4E_26);","Residues 80 to 194 (E_value = 5.1e-78) place ANA_2742 in the Asp_decarbox family which is described as Aspartate decarboxylase.","","1-decarboxylase precursor (Aspartate alpha-decarboxylase) (panD)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2743","2958081","2959097","1017","4.95","-15.50","37836","GTGCAGCTCGACTTCGTCGATTACGTCAAGGAGGTCTCCGGCTACCCCGATCTGCCCTACTGCTACCGGCTCACCTGGCCCAAGAGCTGGTTCCGAGGCGGCTCGGCCAGCAAGAGGGCCCTGGCGTCGGCGCAGACCCTCGCCCGCTGGAACGACGGCGTCGTGGCCCTGTTCTTCGAGCACGTGGTACGGCCGCAGGAAGCCCTGTCCGTGCCCGACTTCAATCCCGATGTCTACGAGAAGGAGTGGGAGCGGCTCGACGAGGACGTTCAGGTGGTCAAGATGCGGGCCTATGTGCGCGAGTCCGTCTGCCCCGATCCGGTCAAGGCCTGGATGCACGCCCTCTCCCGGGTGGCCCCGCACTGGAGCCCCACCGAGTACACCGGCCAGGCGCGCATGCTGCCACTGAACGAGGCCACGATTGAGGCCGCCGATGATTGCAGGTATGTCGATGACGTCGGGGTCTTCCTGACCGGGCCAGCGCCGATCAGTACGGCGACGTTCTTTGGCCTCAAGGAGGATCCTCACGGCATGTACATGGTTGAGTGGGTGGCCGAGCTGGCACCCCTCAGCCCCGGCGACCTGGACCTCCTCCACGAGCTGCTGCTCGAGGCCTGCGACGAGCTCGGCGCCGACCTGGCCTGGGCGCAGGTCCTCGATGGATGGAATCACTCCTACGACGGCGACGTCATGCCCGGCTACTTCAGAGCCGAGCAGCCCCAGTCCCTGGCCGCCGACGGCGTCATCCTGAGTGGACTTCCCTCCATCCCGGTCCCGTGGTGCTACCTCGGGCCCGACTACACCAGGCTGCTCTCCGCCTTCCTCTTTCGCACACCACCCCAGTGGGAGCAGCGCCCCACGGCCCGCGGCACCGCCCTGCGCCTGAGCCGGGTTCCGGTCAAGGGCGAGGCCCTGGGCCCCACCTGGTTCCCGGCCGAGTACTGCGTGTCCGTGCACCGCAGCCGGAAGGGAGAGGAAACCGTGACCGGGGCCGCCGTCGTGCCCACCTGGACCTGA","VQLDFVDYVKEVSGYPDLPYCYRLTWPKSWFRGGSASKRALASAQTLARWNDGVVALFFEHVVRPQEALSVPDFNPDVYEKEWERLDEDVQVVKMRAYVRESVCPDPVKAWMHALSRVAPHWSPTEYTGQARMLPLNEATIEAADDCRYVDDVGVFLTGPAPISTATFFGLKEDPHGMYMVEWVAELAPLSPGDLDLLHELLLEACDELGADLAWAQVLDGWNHSYDGDVMPGYFRAEQPQSLAADGVILSGLPSIPVPWCYLGPDYTRLLSAFLFRTPPQWEQRPTARGTALRLSRVPVKGEALGPTWFPAEYCVSVHRSRKGEETVTGAAVVPTWT$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-50% similar to PDB:1U3C Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana (E_value = );-50% similar to PDB:1U3D Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana with AMPPNP bound (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2744","2959201","2960874","1674","4.84","-31.76","61296","GTGACAGACGAGAGCACCCCCAGCCCCGACCCGACCGCCACCGACGCCGCCGGCACTCAGTCGCAGAAGCCGGACCAGCCCAAGCAGCCCAAGGCCGACCCGGGCCCGGGCGAGCAGTTCGAGGTCCGCGCCGGCAAGCGCGAGCGCCTGCGCAGCGAGGGCTGGGACCCCTACCCGGTCTCCGTGCCCGTCACCACCACCATCGCTGCCGTGCGCGAGGGCTACGCCCACCTCGAGGCCGGGCAGGAGACCGACGACGTCGTCGGCGTCGCCGGCCGCGTCGTCTTCCTGCGCAACACCGGCCGCCTGTGCTTCGTCACCCTCCAGGACGGGGCCGGCACCACCCTGCAGGCCATGCTCTCGGCCAAGGCCCTGCCCGCCGAGGGCCACACCGCGCTCGCGGCCTTCAAGGCCGACGTCGACCTGGGTGACCACCTCTTCGTCCACGGCCGCGTCATCTCCTCGCGCCGCGGCGAGCTGTCCGTCATGGCCGAGCCGGTCCTGCGCGAGGGCGTCGAGGCCGCCTCTGCCGGGGATGACGACGTCGAGGTCCCCGCCTGGCGGATCGCCTCCAAGGCGCTGCGTCCCCTGCCCAAGACCTGGACCAACGAGGCTGGCGAGGCGGTGACGCTCTCGGAGGAGCAGCGCGTGCGCCGTCGTGAGCTCGACCTGCTCACCCGGCCCGCCGCCCGCGACATGGTGCGCACCCGCGCCGCCGTCGTGCGCTCCATCCGCGAGAACTTCTTCCGCCGCGACTACCTGGAGCTGGAGACCCCCATGCTGCAGGTCATTCACGGCGGGGCGGCCGCGCGCCCGTTCATCACCCACATGAACGCCTTCGACATGGATCTCTACCTGCGCATCGCCACGGAGATCTACCTCAAGCGCGCTGTGGTCGGCGGTGTGGACCGCGTCTTCGAGATCAACCGCAACTTCCGCAATGAGGGCGCCGACTCCTCCCACTCCCCGGAGTTCACGGCCCTGGAGGCCTACGAGGCCTACTCCGACTACGACGGCATGGCCGAGTTGACCCGCAACCTCGTCCAGCAGGCGGCCCGCGACGCCTTCGACCTGCCTGAGGGCGGGGAGGTCGTCACGCTGGCCGACGGCACCGAGTACGACCTGTCGGGCGAGTGGGACAAGATCGACCTCTACACCTCCGTCTCCGAGGCCCTCGGTGAGGAGATCACCGTGGAGACCCCGCGCGAGCAGCTGGTCGCCCACGCCGAGAAGATCGGCCTGGAGATCGACGACTACGCCGTGGCCGGCAAGGTCGTCGAGGACATCTTCGAGGAGCTCGTGGGCAACAAGCTGTGGGCGCCCACCTTCGTCTACGACTTCCCCGAGGACACCTCGCCGCTGACCCGCTACCACCGCAGCAAGCCGGGCCTGACCGAGAAGTGGGACCTCTACGTGCGCGGCTTCGAGACCGCCACCGCTTACTCCGAGCTCGCCGACCCCGTGGTCCAGCGCGAGCGCTTCGAGGCCCAGGCGCTGGCAGCCGCCAAGGGCGACCCCGAGGCCATGATCCTGGACGAGGACTTCCTGGTGGCCATGGAGCAGGGCTTCCCGCCCAGCGGCGGCATGGGCATGGGCATCGACCGCCTCCTCATGGTGCTCACCGGCCAAGGCATCCGCGAGACCATCACCTTCCCGCTGGTCAAGCGGGGCTGA","VTDESTPSPDPTATDAAGTQSQKPDQPKQPKADPGPGEQFEVRAGKRERLRSEGWDPYPVSVPVTTTIAAVREGYAHLEAGQETDDVVGVAGRVVFLRNTGRLCFVTLQDGAGTTLQAMLSAKALPAEGHTALAAFKADVDLGDHLFVHGRVISSRRGELSVMAEPVLREGVEAASAGDDDVEVPAWRIASKALRPLPKTWTNEAGEAVTLSEEQRVRRRELDLLTRPAARDMVRTRAAVVRSIRENFFRRDYLELETPMLQVIHGGAAARPFITHMNAFDMDLYLRIATEIYLKRAVVGGVDRVFEINRNFRNEGADSSHSPEFTALEAYEAYSDYDGMAELTRNLVQQAARDAFDLPEGGEVVTLADGTEYDLSGEWDKIDLYTSVSEALGEEITVETPREQLVAHAEKIGLEIDDYAVAGKVVEDIFEELVGNKLWAPTFVYDFPEDTSPLTRYHRSKPGLTEKWDLYVRGFETATAYSELADPVVQRERFEAQALAAAKGDPEAMILDEDFLVAMEQGFPPSGGMGMGIDRLLMVLTGQGIRETITFPLVKRG$","Lysyl-tRNA synthetase","Cytoplasm","lysyl-tRNA synthetase","lysyl-tRNA synthetase ","lysyl-tRNA synthetase","","Koonin E.V., Wolf Y.I., Aravind L. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 2000. 54:245-275. PMID: 10829230Keshav K.F., Chen C., Dutta A. Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. Mol. Cell. Biol. 1995. 15(6):3119-3128. PMID: 7760808Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 1997. 385(6612):176-181. PMID: 8990123","","","

InterPro
IPR002313
Family

Lysyl-tRNA synthetase, class-2
PR00982	$\"[249-259]T$ $\"[265-281]T$ $\"[294-307]T$ $\"[312-329]T$ $\"[440-456]T$	TRNASYNTHLYS
PTHR22594:SF4	$\"[177-556]T$	LYSYL-TRNA SYNTHETASE
TIGR00499	$\"[35-557]T$	lysS_bact: lysyl-tRNA synthetase

InterPro
IPR004364
Domain

tRNA synthetase, class II (D, K and N)
PF00152	$\"[212-556]T$	tRNA-synt_2

InterPro
IPR004365
Domain

Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336	$\"[88-170]T$	tRNA_anti

InterPro
IPR006195
Domain

Aminoacyl-transfer RNA synthetase, class II
PS50862	$\"[235-552]T$	AA_TRNA_LIGASE_II

InterPro
IPR012340
Domain

Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140	$\"[23-198]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.930.10	$\"[211-552]T$	no description
PTHR22594	$\"[177-556]T$	ASPARTYL/LYSYL-TRNA SYNTHETASE

","BeTs to 17 clades of COG1190COG name: Lysyl-tRNA synthetase class IIFunctional Class: J [Information storage and processing--Translation, ribosomal structure and biogenesis]The phylogenetic pattern of COG1190 is ------yqvdrlbcefghsnu--i-wNumber of proteins in this genome belonging to this COG is 1","***** IPB002313 (Lysyl-tRNA synthetase signature) with a combined E-value of 3e-36. IPB002313A 249-259 IPB002313B 265-281 IPB002313C 294-307 IPB002313D 312-329 IPB002313E 440-456***** IPB004364 (tRNA synthetase, class II (D, K and N)) with a combined E-value of 5.3e-10. IPB004364 515-553***** IPB002312 (Aspartyl-tRNA synthetase signature) with a combined E-value of 4.1e-07. IPB002312B 303-316 IPB002312D 516-530***** IPB004115 (GAD domain) with a combined E-value of 2.5e-06. IPB004115A 92-117 IPB004115J 510-555","","","-57% similar to PDB:1BBU LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE (E_value = 6.3E_83);-57% similar to PDB:1BBW LYSYL-TRNA SYNTHETASE (LYSS) (E_value = 6.3E_83);-57% similar to PDB:1E1O LYSYL-TRNA SYNTHETASE (LYSU) HEXAGONAL FOR, COMPLEXED WITH L (E_value = 2.0E_81);-57% similar to PDB:1E1T LYSYL-TRNA SYNTHETASE (LYSU) HEXAGONAL FORM COMPLEXED WITH T LYSYL_ADENYLATE INTERMEDIATE (E_value = 2.0E_81);-57% similar to PDB:1E22 LYSYL-TRNA SYNTHETASE (LYSU) HEXAGONAL FORM COMPLEXED WITH LYSINE AND THE NON-HYDROLYSABLE ATP ANALOGUE AMP-PCP (E_value = 2.0E_81);","Residues 84 to 142 (E_value = 0.0031) place ANA_2744 in the TOBE family which is described as TOBE domain.Residues 88 to 170 (E_value = 1.7e-10) place ANA_2744 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain.Residues 212 to 556 (E_value = 1.6e-86) place ANA_2744 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N).","","synthetase (lysS)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2745","2961068","2962369","1302","6.03","-7.96","48317","ATGTTGCTGGACTTCACCGTGGCGAACTACTGCTGCTACGCAGAGGAGGTGACCCTCGATCTCACTCGGAGTTCGCTCAAGACTCTGACGCCGCGCGGCGGCTCCTCCTGGCGGGAGCAGACGTGGCGAGTGGCGGCGATCTTCGGCGCTAACGCTTCAGGCAAGTCGACCCTCCTGGATGCGCTTGACTGCCTCCACCACGCCATCGGGGGGCAGCGGGACATCCTGCACCAGCCCTTCAGTCTCGATCGCAACCACGCGGCACAGCCGTCCCGCTTCACCGTCGGCTTCACTCACGAGGACGAGCGCTACAGCTACAGCGTCGAGGCGCATCGCTGGGGCATTTCGCGCGAGGAGCTCTGGGCGGCGGGGCAGCGCTGGCGCAAGGTCTTCGTGCGCACCCAGGGGCCCGAGGATGACAAGCCTACGATCGAGGCTGGTGCCACCCTCAAGGGCGCCACGACCGAGGTCGGTCGGATTACGACGCCCAAGGACCTCTTTCTCGCCGTGGCTCTGAGGTACGAGCACGCCGCGCTCGCCCCGATCGCGCGCAGCCTGCGATCCATGCGCTTCATCCACCACAGTGATGAGGAGCGCAGTTCGCGTCTGCGGTGGGTGATGAGCCGGCTAGCCGAGTCCCCTGAGCAGTGGACTGGCATTGCGAACTCCATTGCTCAGGCCGCCGACCTGGGCATCGTCGGACTTGAGCTCGAGGAGCAGGAGGTTCCGCAGGAAATGCTTGAGCTCCTGCGTCGCCTTCCCTGGAGCGAGGACGAGGAGGCTGAGGTTCCCGCCGAGGTGCTCAAGGAGCTCCAGCGTCATCTCGTGCTCCAGCACCGTGGGGCGGACGCTAAGGACTACCGGTTAGCGAGCAGCCAGCAGAGTCAGGGCACTCTTACCTGGCTGGCAACGGTCGGTCCCGCCATTGACGCCTTGCGGCTAGGGCAGGTGCTGTGCATTGACGAGCTCGATGCGAGCCTCCATCCGACGCTGACCGCCACGTTGGTGGACATGTTCAAGGACCCGGACCTCAACACCCGGGGCGCCCAGATCGTCTTCACAACCCATGACACGGCACTCCTGGACAATTCTCCCGTCCAGCTCCTGGAGGCGGGCGAGGTGTGGATGACGGAGAAGTCCCCCTTCGGTGCCAGTGAGCTCTTCTCGCTCGCAGACTTCCCCTCCAACCGCAAGGGCACGAACAAGCAGCGCCGCTACCTCGCCGGTGCCTTTGGTGCTATCCCTCGGGTAGACACCTCCAGCCTCCGCCGGTACCTCTCAACGCCGGCGGAGGCGAAGTGA","MLLDFTVANYCCYAEEVTLDLTRSSLKTLTPRGGSSWREQTWRVAAIFGANASGKSTLLDALDCLHHAIGGQRDILHQPFSLDRNHAAQPSRFTVGFTHEDERYSYSVEAHRWGISREELWAAGQRWRKVFVRTQGPEDDKPTIEAGATLKGATTEVGRITTPKDLFLAVALRYEHAALAPIARSLRSMRFIHHSDEERSSRLRWVMSRLAESPEQWTGIANSIAQAADLGIVGLELEEQEVPQEMLELLRRLPWSEDEEAEVPAEVLKELQRHLVLQHRGADAKDYRLASSQQSQGTLTWLATVGPAIDALRLGQVLCIDELDASLHPTLTATLVDMFKDPDLNTRGAQIVFTTHDTALLDNSPVQLLEAGEVWMTEKSPFGASELFSLADFPSNRKGTNKQRRYLAGAFGAIPRVDTSSLRRYLSTPAEAK$","Phage resistance protein","Cytoplasm","RloA, putative","putative phage resistance protein","hypothetical protein","","Biedenkapp H., Borgmeyer U., Sippel A.E., Klempnauer K.H. Viral myb oncogene encodes a sequence-specific DNA-binding activity. Nature 1988. 335(6193):835-837. PMID: 3185713Aasland R., Stewart A.F., Gibson T. The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci. 1996. 21(3):87-88. PMID: 8882580Klempnauer K.H., Sippel A.E. The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain. EMBO J. 1987. 6(9):2719-2725. PMID: 2824190","","","

InterPro
IPR001005
Domain

SANT, DNA-binding
PS00037	$\"[255-263]?$	MYB_1

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-62% similar to PDB:2NQ2 An inward-facing conformation of a putative metal-chelate type ABC transporter. (E_value = );-41% similar to PDB:1MV5 Crystal structure of LmrA ATP-binding domain (E_value = );-59% similar to PDB:1JJ7 Crystal Structure of the C-terminal ATPase domain of human TAP1 (E_value = );-51% similar to PDB:1QK9 THE SOLUTION STRUCTURE OF THE DOMAIN FROM MECP2 THAT BINDS TO METHYLATED DNA (E_value = );-51% similar to PDB:1UB1 Solution structure of the matrix attachment region-binding domain of chicken MeCP2 (E_value = );","No significant hits to the Pfam 21.0 database.","","putative ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2746","2963502","2962960","543","4.67","-11.32","19645","ATGACGATCCTGACGAGCAATGACGTGGACAACGTGAGGTTCACGGCCACCCAGTTCCGAGAGGGCTACGAACAGCACGAGGTTGATAGCTTTCTTGAGAAGATCGCCAGCACGCTGAGGGTTCTCCAGGCAGGAACTAACTCCACTGGGTATGCCTCCAACATCGCCGGCGTCAAGGTGCTCACGGCTGACGACGTGCAGAGCAAGAAGTTCCACGGCACCAGGTTCCGGGAAGGCTACGAGCAGGATGAGGTCGACAGCTTCCTCGACCACGTCGTGGAGACGTTGAGATACCTGGAGGGTGGCGCGCAGGCCTCCGGATATGAAGCACAGTGGGGCGGCAGCTCGTGGGACGGCGGAGTCAACGCGTACGGCAGTGCGTCGTACGCCGCGCCGAGCGGCACCGACGGAACCGGTGATGCCCAGTACGCCGAGGCCATTGCGCAGCGCGACCAGTACATCGCCCAGCTCCAGCAGGAGAACGCCTACCTTCGCGCCGAGCTCGACTCCGCCCAGCGCCGCCTCGGGACGACCGGGTACTAG","MTILTSNDVDNVRFTATQFREGYEQHEVDSFLEKIASTLRVLQAGTNSTGYASNIAGVKVLTADDVQSKKFHGTRFREGYEQDEVDSFLDHVVETLRYLEGGAQASGYEAQWGGSSWDGGVNAYGSASYAAPSGTDGTGDAQYAEAIAQRDQYIAQLQQENAYLRAELDSAQRRLGTTGY$","Hypothetical protein","Extracellular, Cytoplasm","conserved hypothetical protein","hypothetical protein","hypothetical protein","","Cha J.H., Stewart G.C. The divIVA minicell locus of Bacillus subtilis. J. Bacteriol. 1997. 179(5):1671-1683. PMID: 9045828","","","

InterPro
IPR007793
Family

DivIVA
PF05103	$\"[1-32]T$	DivIVA

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-42% similar to PDB:2F3B Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase (E_value = );-42% similar to PDB:2F3D Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase (E_value = );-42% similar to PDB:2F3H Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase (E_value = );","Residues 1 to 32 (E_value = 3.2e-06) place ANA_2746 in the DivIVA family which is described as DivIVA protein.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2747","2962592","2962963","372","7.88","2.49","13808","GTGTGGATCGTCGTCGACCACGATGGCCAGGACCGTCATGACTTTCTGGCCAAATGCCGAAGGCTGAGCAGCAGGCAGACTGTTGTCCATGGCATCGTCTCCGTACCCTGCTTCGAGGTCTGGCTCAACGCCCACTACGCCCCCGTGAAGAACTATCGGAACCAGGCGGACGCTCAGTCGCACTATCTCGAACTGACAGGGCTCAGCAAGAAGAACGCCAAGACGCTCCCTGTTGACTTTCCCTGGGACAAGGTCACGCAGGCCGCGGCCAGGTGCCATCTGCCGATGGACGGCCTCCCCGAGCCCGATACTCAGGGGCCTTGTCCATCGACAACGATGCCCCACCTGCTCCGCAGCCTCGGTCTCCTCTAG","VWIVVDHDGQDRHDFLAKCRRLSSRQTVVHGIVSVPCFEVWLNAHYAPVKNYRNQADAQSHYLELTGLSKKNAKTLPVDFPWDKVTQAAARCHLPMDGLPEPDTQGPCPSTTMPHLLRSLGLL$","Hypothetical protein","Cytoplasm","conserved hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:1GN2 S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS. (E_value = );-43% similar to PDB:1GN3 H145Q MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE. (E_value = );-43% similar to PDB:1GN4 H145E MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE. (E_value = );-43% similar to PDB:1IDS X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS AT 2.0 ANGSTROMS RESOLUTIONS REVEALS NOVEL DIMER-DIMER INTERACTIONS (E_value = );-48% similar to PDB:1LLQ Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide (E_value = );","No significant hits to the Pfam 21.0 database.","","hypothetical protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2748","2964122","2963553","570","4.70","-9.56","20195","ATGACGCTGCTGACAGCTGACGACGTCCTCAACGTGAAGTTCCAGGTCTCCTCATTCAAGGAGGGCTACAACCAGGATGAGGTCGACGAGTTCCTCGACGAAGTGACCACCACGATGCGGGAGTTCGAGGAACGACTCGGCACCTCGCAGGCATCGTCGGGCCCCTCGCACCGGAAGGCCGAGATCCTCCTGACCTCCGAGGGCGTCAGGAACATCCGGTTCTCGACCACCCGGTGGTCGGGGTATCACATCGACCAGGTTGATGCTTTCCTCGCTCAGGTGGTCTCGACGATGGAGGCCCTCGAGGCGCAGGCGCGCACCAGCACATTCGCCGGCCAGCCCGGCGCCGGAGCCGGCGGGGCCTATAGCGGGGCGTACGGTGGCGGAACCTACGGTATGAGCCCGGCTCAGGCGGGGTACGCCCCGGGCGGAGCCGAAGCCGGCGGCTCTCAGTACGCCGAAGCGATCGCCCAGCGCGACCAGTACATCGCCCAGCTCCAGCAGGAGGTCGCCTACCTGCGCGCCGAGCTCGAGGCCGCCCAGCGCCGGCTGGGGACGACAGGGGTCTAG","MTLLTADDVLNVKFQVSSFKEGYNQDEVDEFLDEVTTTMREFEERLGTSQASSGPSHRKAEILLTSEGVRNIRFSTTRWSGYHIDQVDAFLAQVVSTMEALEAQARTSTFAGQPGAGAGGAYSGAYGGGTYGMSPAQAGYAPGGAEAGGSQYAEAIAQRDQYIAQLQQEVAYLRAELEAAQRRLGTTGV$","Cell division protein DivIVA","Cytoplasm","cell division protein DivIVA-like protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","Cha J.H., Stewart G.C. The divIVA minicell locus of Bacillus subtilis. J. Bacteriol. 1997. 179(5):1671-1683. PMID: 9045828","","","

InterPro
IPR007793
Family

DivIVA
PF05103	$\"[1-35]T$	DivIVA

","BeTs to 3 clades of COG3599COG name: Cell division initiation proteinFunctional Class: A, ,DThe phylogenetic pattern of COG3599 is ---------drlb-------------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-63% similar to PDB:1IQC Crystal structure of Di-Heme Peroxidase from Nitrosomonas europaea (E_value = );-64% similar to PDB:1PGN CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM (E_value = );-64% similar to PDB:1PGO CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM (E_value = );-64% similar to PDB:1PGP CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM (E_value = );-64% similar to PDB:1PGQ CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM (E_value = );","Residues 1 to 35 (E_value = 5.7e-08) place ANA_2748 in the DivIVA family which is described as DivIVA protein.","","division protein DivIVA-like protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2749","2964856","2964119","738","5.03","-10.92","26431","ATGACCTCAGGACGGATCGACACGGCCCAGGACGCCTCCCACGTGGCCGCACCGAGGCCGCCGGTCCTCGCGGCACCGGATCTGGGTCGCCTGCGCGACGGCGAGGCCGATGAGCTCACCGCCGGTGAGATGGTCGAGGACCTGGCGCTGGTCGAGGCGGACCTCAGCGGCGGCGACCTGTCTGCGCTCACGCTGCTCAGCTGCCGGTTCTCGGAGGTTTTCGCCAACGACACCGACCTGGCCGCGGCGCGGCTGGTCGACTGCCGCCTGGAACGACTGAGCGCCACCTACCTTCACAGTCCTCGCTCCACCTGGCGCACGGTGGAGATGGTTGACTCCCGTATCGGGGCCTGGGAGCTCTATGACGCTGATGTCGAGTCGCTCCTCATGGAGAACTGCCGCCTGGGCTTCGTCAACCTCGCCGGAACCGCTCTACGCGACGTCCTCATCAGGGCCACCCGGATCGACGAGCTGGACCTGAGCGGAATCGACGCTCAGCGGGTCCGTTTCGAGGACTGCCGGGTGGGCACGCTGCGCCTGCACGGCGGGGGCCTGAGCGACGTCGACCTGCGCGGACTGGAGATGAGAGTGGTCAGCGGGGTCGGCTCCCTGGCCGGGGCGACCATCAACGGCCAGCAGCTCAGTGAGCTCGCGCCGCTCTTGGCGCAGCATCTGGGACTGCGGGTCACGGATCGGGATCACGCACAGAATGCGGCAACAAGGAGTAGAAGAGCATGA","MTSGRIDTAQDASHVAAPRPPVLAAPDLGRLRDGEADELTAGEMVEDLALVEADLSGGDLSALTLLSCRFSEVFANDTDLAAARLVDCRLERLSATYLHSPRSTWRTVEMVDSRIGAWELYDADVESLLMENCRLGFVNLAGTALRDVLIRATRIDELDLSGIDAQRVRFEDCRVGTLRLHGGGLSDVDLRGLEMRVVSGVGSLAGATINGQQLSELAPLLAQHLGLRVTDRDHAQNAATRSRRA$","Hypothetical protein","Cytoplasm","Uncharacterized low-complexity proteins","hypothetical protein","hypothetical protein","","","","","No hits reported.","BeTs to 6 clades of COG1357COG name: Uncharacterized low-complexity proteinsFunctional Class: S [Function unknown]The phylogenetic pattern of COG1357 is -o-------drlbcef-h---jx-t-Number of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","low-complexity proteins","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2750","2967280","2965067","2214","9.31","9.32","76249","ATGAGCCGCATCGCCCTGACCCGGCTGCTCGTCGCCAACGACCGCTCCGCCCGGCGCCGCCTGGCCGGGATCGTCGCCGGAGTCATGGTGGGGGTGGCGTTGTTCCTCATGCTGCTGGCCGCCGCCCAGGCCTTCCCCGAGCGCAGCATGCGCTCCAGCTGGGCGTCCACCGCCCTCATGCCCGGCCTCTCCGAACAGTCGAACCACATCGACCTCCGGCCCGACCACGTCCTCACCGAGGGCGAGCTGGCCGTCGCCAGCAACGTCGACGTCGTCGGCAACCGGCCGATCACCGTCCTGAGGGTGGCCCTGCCGGAGTCGGGCACCACCTCGGTGAAGATCCCGGGCTCCGACATCGTCCCCAAGCGGGGCGAGTACCTGGCCTCGCCGGCCCTGGCCAAGCGCATCGCGTCCCTGCCCGCCGACCAGCTCGGCGACCGCTACGGCAAGCAGGTGGGCGTCCTGTCCCCCGAGGCCGTCGAGGGCCCGGACTCAATGGTGGCCGTCATCGGGACGGACCTGGAGACCGTGGCCGCCTCCGAGTTCTACATCCCGCCCCAGGTAGTCACCTCCTTCCAGGGCATCCCCTTTGAGAACGAGGCGTATCGGATCGCCACGATCGTCGGGGCCATCGCGGTGCTCGTGCCCGCGCTGCTGCTCGTCGGGATCGTCACCGACTTGGGGGCGGCGCAGCGGGCCGAGCGCTTCGCCACGCTGCGCCTCATCGGGGCCACACCGCAGCAGGTGGCCCGCACCGCGACCCTGGAGATCGGGGCCACGACCTTCGTCGGCGCCCTGGCGGGCGTGGCCCTCTACCTGGCCATGATCCCCGTGGCCGCGCAGATCACGCTGAGAACCAGCCGCTTCTACTACGCCGACCTGCTGCGCTCCCCGGTCAACGCGGTCCTCGCCGTCGTCGTGACCACGGCGGGGGCGGCGGCCGTGGCTTGGTGGCGCACGCGACGAGCCGACCTCGGCCCGTTGGGCGGGTCCCGTGAGCGCACCGAGCACCGCCCCCGCCTCATCTCGCTGGCGCCCGTCATCCTGGGGACGGCCGGGCTGGTCAGCGCCCCGACGGTGGCCCATCAGGACTCCAATCTGACCATCTACCTGCTGCCCGCCTCCTTCCTGTGCGCGATGCTGGGTCTGGTGTGGGCCGGGCCGGTCCTGACCTGGTGGGTGGCGCGAGGCGGCAGGGCCGTGGCCCACTCCGCGGCGCAGGTCATCGGTTTCAACCGGATCACTCAGCACCCCCGGGCGGCCTTCCGTGCGGTGGCGGGCGTCGTGATCGCCGTCTACGCCATGACGGTGTTCGCCGTCGCCATCACGGCCGCTGCAGGGACCCATGACGTCACGCGAGGCGGTGGGCACCTGAGCGCCACGACGCTCGCGGCGATGCCTGCGGTCAGCGACGAGGGCGCCCTGAGCGGAGCCATCGACCGGCTCTCCGCCGTGCCCGGGGTGACGACGGTGACCGTAGGAAGGATCGGCGGCGACGGCAAGCAGGACAGTCAGATCATCCTCGAGGCCGACAAGGCCGAGGCCCTCGGGGCCCCGCATGTCGCGGCTCCTGATGGCGCGGTGAGCATCAGTACCCGGTGGCTGTATGAGAACGCGGCCGCCTCGCCGTCGCCGGTCAGTACCGAGGCGCTGGCGAGCGCCCGTGAGAGCGGCGCGCCCGTCATCCTGGTGGGGACGGACCCGGCCAGCCCCGGGGCCATCGAGCGGGCCCGTACCTGCCTGGCCACCTCCGGCCTGACCCTCGGGACCGCCCCGACCTCACCCAGCTCGATCCAGGCCCTTGAGGGCAGTGCCATGGAGAACCAGTTCGCCCAGCTCGGTTACATCGGCATCCTCATCGCCGCGGGCATCTCCGCGGTCTCGCTCGGGGTCTCGACGGTGGCGGCACTGCTGGGGCGTCGGCGGGTCCTCGGTCTGCTGAGGCTGGTCGGCATGCCGGCGGCGACGCTGCGCTCCATGGTCTCCTACGAGGCGGTGCTGCCGGCGGCCACTGCCCTGGTCATGAGCATCGGTCTGGGCTGGCTGACCGCATGGTCGCTGATCGGCGGCGTCTCGGGCCGCCACATCAGCTGGCCGGACGGCGGTTACTGGCTGGTGCTGCTGGCGTGCCTGGCGCTGGTGGTGGTGACGACCCTGGCCAGTGCCCGCTACGGCCGGCGCATGCTGGCGGACTCCACCGTCCGATTCGAGTAG","MSRIALTRLLVANDRSARRRLAGIVAGVMVGVALFLMLLAAAQAFPERSMRSSWASTALMPGLSEQSNHIDLRPDHVLTEGELAVASNVDVVGNRPITVLRVALPESGTTSVKIPGSDIVPKRGEYLASPALAKRIASLPADQLGDRYGKQVGVLSPEAVEGPDSMVAVIGTDLETVAASEFYIPPQVVTSFQGIPFENEAYRIATIVGAIAVLVPALLLVGIVTDLGAAQRAERFATLRLIGATPQQVARTATLEIGATTFVGALAGVALYLAMIPVAAQITLRTSRFYYADLLRSPVNAVLAVVVTTAGAAAVAWWRTRRADLGPLGGSRERTEHRPRLISLAPVILGTAGLVSAPTVAHQDSNLTIYLLPASFLCAMLGLVWAGPVLTWWVARGGRAVAHSAAQVIGFNRITQHPRAAFRAVAGVVIAVYAMTVFAVAITAAAGTHDVTRGGGHLSATTLAAMPAVSDEGALSGAIDRLSAVPGVTTVTVGRIGGDGKQDSQIILEADKAEALGAPHVAAPDGAVSISTRWLYENAAASPSPVSTEALASARESGAPVILVGTDPASPGAIERARTCLATSGLTLGTAPTSPSSIQALEGSAMENQFAQLGYIGILIAAGISAVSLGVSTVAALLGRRRVLGLLRLVGMPAATLRSMVSYEAVLPAATALVMSIGLGWLTAWSLIGGVSGRHISWPDGGYWLVLLACLALVVVTTLASARYGRRMLADSTVRFE$","Uncharacterized conserved protein","Membrane, Cytoplasm","permease, putative domain protein","protein of unknown function DUF214","protein of unknown function DUF214","","Biedenkapp H., Borgmeyer U., Sippel A.E., Klempnauer K.H. Viral myb oncogene encodes a sequence-specific DNA-binding activity. Nature 1988. 335(6193):835-837. PMID: 3185713Aasland R., Stewart A.F., Gibson T. The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci. 1996. 21(3):87-88. PMID: 8882580Klempnauer K.H., Sippel A.E. The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain. EMBO J. 1987. 6(9):2719-2725. PMID: 2824190","","","

InterPro
IPR001005
Domain

SANT, DNA-binding
PS00334	$\"[685-707]?$	MYB_2

InterPro
IPR003838
Domain

Protein of unknown function DUF214, permase predicted
PF02687	$\"[164-325]T$ $\"[561-730]T$	FtsX

noIPR
unintegrated

unintegrated
signalp	$\"[1-44]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[204-224]?$ $\"[262-284]?$ $\"[298-318]?$ $\"[341-361]?$ $\"[367-389]?$ $\"[425-445]?$ $\"[616-638]?$ $\"[666-688]?$ $\"[702-722]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 164 to 325 (E_value = 0.00046) place ANA_2750 in the FtsX family which is described as Predicted permease.Residues 561 to 730 (E_value = 7.3e-05) place ANA_2750 in the FtsX family which is described as Predicted permease.","","putative domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2751","2968113","2967277","837","6.90","-0.34","28690","ATGAGCGCCACCGGCGTCACCACCGCCGTCACGGCCGCCGGAGTCACGCCCGCACCCGGTCAGGGCCAGGCCGGCCTGCCGGGCGGCGTCATCATGAGCGCCCGCGGCCTGGAGATGAGCTTCGGGCAGACCCACGCGCTGCGCGGCGTCGATCTGGATGTCGGGGCCGGAGAGGTGCTGGCCGTCACCGGCCCGTCGGGCTCGGGCAAGTCCACGCTCCTGCACGTCATGGCCGGGGTGCTCGTGCCCGATGCCGGACGCGTCGATTACCACGGAGGCGACGTGTCGCAGGACATCACGGCCCTCGATGAGGCGGCCCGCAGCCGCCTGCGCCTGAAGGAGTTCGGCTTCATCTTCCAGTTCGGCCAGCTCCTGCCGGACCTCTCCGCCCTGGACAACGTCACCATCCCCCTGCTCCTGGCGGGCACTGCGCGCCGGCGGGCGCTGGCCCAGGCCCGCGAGACCCTGGGCGAGCTGGGGCTCAGCGAGCACCTGGACAAGCGCCCCACTCAGCTCTCGGGCGGCCAGGCGCAGCGGACCGCCGTCGCGCGGGCGCTGGTGACCAACCCGCGCCTCCTCTTCGCCGACGAGCCCACCGGCTCCCTGGACTCCCTGGCCGCCGAACGGACCATGGAGGTGCTCCTGAGCTCGGTACGCTCCCGCGGTGCCGGCCTGGTCATCATCACCCATGATGCGCGCGTCGCAGCCTATGCCGACCGGGAGGTCACCGTGCGCGACGGTCGCATCGGCCCCGAGGCCACGCACACCGTGGCCGGACCGAGCCGGCCGGGGCACGCCGAGCCGGGAGACCCGGGAAGTCAGAGGAGCCGGTCATGA","MSATGVTTAVTAAGVTPAPGQGQAGLPGGVIMSARGLEMSFGQTHALRGVDLDVGAGEVLAVTGPSGSGKSTLLHVMAGVLVPDAGRVDYHGGDVSQDITALDEAARSRLRLKEFGFIFQFGQLLPDLSALDNVTIPLLLAGTARRRALAQARETLGELGLSEHLDKRPTQLSGGQAQRTAVARALVTNPRLLFADEPTGSLDSLAAERTMEVLLSSVRSRGAGLVIITHDARVAAYADREVTVRDGRIGPEATHTVAGPSRPGHAEPGDPGSQRSRS$","ABC-type transport system involved in lipoprotein release, ATPase component","Membrane, Extracellular","ATP-binding protein of ABC transporter system","K02003","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[171-214]T$	Q9FBP2_STRCO_Q9FBP2;
PF00005	$\"[57-247]T$	ABC_tran
PS50893	$\"[32-271]T$	ABC_TRANSPORTER_2

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[56-248]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[26-249]T$	no description
PTHR19222	$\"[33-248]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF39	$\"[33-248]T$	ABC TRANSPORTER

InterPro
IPR005149
Family

Transcriptional regulator PadR-like
PF03551	$\"[4-82]T$	PadR

InterPro
IPR011991
Domain

Winged helix repressor DNA-binding
G3DSA:1.10.10.10	$\"[1-89]T$	no description

","BeTs to 11 clades of COG1695COG name: Predicted transcriptional regulatorsFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1695 is aompkz--vdrlb-e-g----j----Number of proteins in this genome belonging to this COG is 4","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 2 to 82 (E_value = 7.4e-11) place ANA_2752 in the PadR family which is described as Transcriptional regulator PadR-like family.","","regulator, PadR family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2754","2968822","2969883","1062","11.13","12.04","35609","ATGCCGATCGGGGTCCTCGGGGACCGTCTTCGCCCCCGTTCTCACAAGGGGACGACGGTGAGTACTCGCGTGATCGCGCGCCGCCCGGCCATCCTCCTGATCGCAGCCGTCCTGCTGGCCCTGTGCCTCCTGGCCTCCCTGTTCGTCGGCTCCTCCAAGATCCCCGCCGGCCAGGTCGCCCACTACCTGCTCCACCCCGACGCCTCTAACGTCAGCTACAACATCCACGTCCTGCGCGTGCAGCGCACCATCCTGGGCGTGCTCGTCGGGACCGCTCTGGGGGTGGCCGGCGCGGTGATGCAGGCCGTCACCCGCAACCCCCTGGCCGAGCCCGGGCTGCTCGGTGTCAACGCCGGCGCCTCGCTGGGCATCGTCTTGGGAACCGCCGTGCTCGGCGTGCTCCCGGTCCCCGGCCAGCTGCTCCTGGCGGCCGGCGGCGCCCTGACTGCCACCGCGCTCGTCCAGGTCATCGGGATGATCGGCGGCTCGACATCCTCACCGGTGCGCCTGGTGCTCATCGGTGTCGCCTTCTCGGCCTTCGCCGGGGCGGTCATCCGGGGTGTCGTGCTGACGATGCCGAACCTGTTCCGCACCTTCATCGACTGGGAGGTCGGCTCCCTGACCCGCACCGACATCCCCTTGCTGCCCGTGGCGGCCCTCGTGGTGGCGGGGACCGGGGCGGCCGTCCTGCTGGCGGGCGCCCTGGACAACATTGCCCTGGGCGACGACGTCGCCGCCGCCCTGGGCACCCGGGTGGGCCTCGTGCGGGGCCTGAGCCTGGCGGTCGTCACGCTCCTGTGCGCCACCGCCACGACGGTGGCCGGCCCCATCGGGTTCGTCGGGCTCATGGCGCCGCTGACGGCCTCCTGGCTCATGGGACCCCACCGGGGCTGGATCGTGGCCCTGTGTGCGCTGGGCGGCCCCGTCGTCGTCCTGGCCGCCGACGTCCTGGGCCGCGTCCTGGCCCGTCCCGGTGAGATGCAGGTCGGTCTGCTGACGGCCTTCGTCGGCTCGCCCGTCCTGCTGCTCATGGTCCTGCGGATGAAGGACCGGGCCTCATGA","MPIGVLGDRLRPRSHKGTTVSTRVIARRPAILLIAAVLLALCLLASLFVGSSKIPAGQVAHYLLHPDASNVSYNIHVLRVQRTILGVLVGTALGVAGAVMQAVTRNPLAEPGLLGVNAGASLGIVLGTAVLGVLPVPGQLLLAAGGALTATALVQVIGMIGGSTSSPVRLVLIGVAFSAFAGAVIRGVVLTMPNLFRTFIDWEVGSLTRTDIPLLPVAALVVAGTGAAVLLAGALDNIALGDDVAAALGTRVGLVRGLSLAVVTLLCATATTVAGPIGFVGLMAPLTASWLMGPHRGWIVALCALGGPVVVLAADVLGRVLARPGEMQVGLLTAFVGSPVLLLMVLRMKDRAS$","ABC-type cobalamin/Fe3+-siderophores transport system, permease component","Membrane, Cytoplasm","ABC-type transporter, permease components","K02015 iron complex transport system permease protein","transport system permease protein","","","","","

InterPro
IPR000522
Family

Bacterial transport system permease protein
PF01032	$\"[38-347]T$	FecCD

noIPR
unintegrated

unintegrated
signalp	$\"[1-44]?$	signal-peptide
tmhmm	$\"[30-50]?$ $\"[83-103]?$ $\"[113-135]?$ $\"[141-161]?$ $\"[170-190]?$ $\"[212-232]?$ $\"[247-267]?$ $\"[273-293]?$ $\"[298-318]?$ $\"[328-346]?$	transmembrane_regions

InterPro
IPR000522
Family

Bacterial transport system permease protein
PF01032	$\"[59-358]T$	FecCD

noIPR
unintegrated

unintegrated
tmhmm	$\"[50-70]?$ $\"[104-124]?$ $\"[134-153]?$ $\"[159-179]?$ $\"[188-208]?$ $\"[231-251]?$ $\"[278-300]?$ $\"[346-366]?$	transmembrane_regions

","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism] Functional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is 7","***** IPB000522 (FecCD transport family) with a combined E-value of 2.1e-36. IPB000522A 100-141 IPB000522C 291-309 IPB000522D 341-364","","","-45% similar to PDB:2NQ2 An inward-facing conformation of a putative metal-chelate type ABC transporter. (E_value = 1.6E_15);-42% similar to PDB:1L7V Bacterial ABC Transporter Involved in B12 Uptake (E_value = 1.3E_14);-57% similar to PDB:1NAS SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN (E_value = 1.3E_14);-57% similar to PDB:1OAA MOUSE SEPIAPTERIN REDUCTASE COMPLEXED WITH NADP AND OXALOACETATE (E_value = 1.3E_14);-57% similar to PDB:1SEP MOUSE SEPIAPTERIN REDUCTASE COMPLEXED WITH NADP AND SEPIAPTERIN (E_value = 1.3E_14);","Residues 59 to 361 (E_value = 1e-61) place ANA_2756 in the FecCD family which is described as FecCD transport family.","","(III) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2757","2970995","2971984","990","6.18","-4.17","34706","GTGACCGACCTGCCCTCCACCGAGTCGAACACCGCCGGGCCGGCCGCCCCCGGGGCTCGCCTGGCCGCCCGGGGCGCGACCATCGCCTACGAGCGCCACGTGGTCTCCCGCAACCTCGACGTCGATATCCCCGCCGGTGTCTTCACCGCCATCGTGGGGCCCAACGCCTGCGGGAAGTCCACGCTGCTGCGCGCCCTGGCCCGGTTGCACCGGCCCGTCCGAGGATCGGTACTCCTCGACGGTGCCGACATCGTTCGCCTGGGCACCAAGGAGGTCGCCCGCCGGGTCGGCCTGCTGCCTCAGAGCGCCACGGTGCCCGGCGGCATGCTGGTGCGTGACCTCGTGGCCCGCGGTCGCTTCCCCCACCAGGGCCTGTTCCGACAGTGGTCGCAGCAGGACAGGCAGGCCGTCGAGGAGGCCATGGAGATGGTGGGGGTCACCGAGCTGGCCGCCCGCCCCGTCGACGAGCTCAGCGGTGGCCAGCGCCAGCGCGTGTGGATCGCCCTGGCCCTGGCTCAGGGCACCGAGACGATCCTGCTCGATGAGCCCACCACCTTCCTCGACCTGGCCCACCAGGTCGACATCCTCCAGCTGTGCCGGCGCCTCAATGCCGACGGTCGCACGGTGGTGGCCGTCCTGCACGACCTCAACCAGGCGGCGCGCTGCGCCGAGCACATGATCGTCATGCACGAGGGCCGCATCCGCACCACCGGCTCCCCGCGCGAGATCCTCACTGAGGACCTCATCGAGGAGGTCTTCGGCCTGGCGGCCGTCATCGCCCCCGACCCGGTGGCCGGCACCCCCATGGTGGTGCCCCGTCACCTGGGCGCGGTCGTGCCGGCCGACCCTGCCCCTGCCGCGACCCCCTCCGCTCCCACCGACTCCACTGGAGGTCCGGCCCCACAGCCCTCTGCCGATCCCGCCTCGGCAGGAACCAGCCCGACTGCTCGTTCCCAGCAGGACGGACAAGAAAGGAACACAGATATATGA","VTDLPSTESNTAGPAAPGARLAARGATIAYERHVVSRNLDVDIPAGVFTAIVGPNACGKSTLLRALARLHRPVRGSVLLDGADIVRLGTKEVARRVGLLPQSATVPGGMLVRDLVARGRFPHQGLFRQWSQQDRQAVEEAMEMVGVTELAARPVDELSGGQRQRVWIALALAQGTETILLDEPTTFLDLAHQVDILQLCRRLNADGRTVVAVLHDLNQAARCAEHMIVMHEGRIRTTGSPREILTEDLIEEVFGLAAVIAPDPVAGTPMVVPRHLGAVVPADPAPAATPSAPTDSTGGPAPQPSADPASAGTSPTARSQQDGQERNTDI$","ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component","Membrane, Cytoplasm","FepC","The iron-vibriobactin/enterobactin uptake porter ","ABC transporter related","","Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999. 48(1):22-41. PMID: 9873074","","","

InterPro
IPR003439
Domain

ABC transporter related
PD000006	$\"[157-198]T$	FHUC_BACSU_P49938;
PF00005	$\"[46-232]T$	ABC_tran
PS50893	$\"[21-256]T$	ABC_TRANSPORTER_2
PS00211	$\"[157-171]T$	ABC_TRANSPORTER_1

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[45-233]T$	AAA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[21-254]T$	no description
PTHR19222	$\"[21-269]T$	ATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31	$\"[21-269]T$	METAL ABC TRANSPORTER

InterPro
IPR002491
Family

Periplasmic binding protein
PF01497	$\"[158-284]T$	Peripla_BP_2
PS50983	$\"[90-367]T$	FE_B12_PBP

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.1980	$\"[87-221]T$	no description
PS51257	$\"[1-30]T$	PROKAR_LIPOPROTEIN
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[15-35]?$	transmembrane_regions

","BeTs to 9 clades of COG0614COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, periplasmic componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0614 is aompkz--vdrlbcefgh-nuj----Number of proteins in this genome belonging to this COG is 4","***** IPB007688 (TrbL/VirB6 plasmid conjugal transfer protein) with a combined E-value of 3.5e-07. IPB007688C 36-62 IPB007688C 39-65 IPB007688C 40-66 IPB007688C 42-68 IPB007688C 38-64 IPB007688C 31-57 IPB007688C 33-59 IPB007688C 35-61 IPB007688C 37-63 IPB007688C 34-60 IPB007688C 44-70 IPB007688C 43-69 IPB007688C 32-58 IPB007688C 28-54 IPB007688C 41-67","","","No significant hits to the PDB database (E-value < E-10).","Residues 88 to 344 (E_value = 5.1e-06) place ANA_2758 in the Peripla_BP_2 family which is described as Periplasmic binding protein.","","periplasmic protein precursor","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2759","2974742","2973210","1533","5.00","-16.60","53702","ATGGCTGACACACGACCCGGCGCGGCAACTGACACAGCGGCGTACACCACCCTCGGAGCCCACCCGGCTCTGGCCGACTACCTGCACAGGATCCGCCCCGAGGAGGGGATGCTCCTGGGCGGGCGGATGACGGCAGCCTCCGACGGCGGAACCTTCGACGTCGTCGACCCCGCCAGCAACGCCGTATTCGCACGCTGCACGGATGCGACTCCGGTGGATGCCGCACGCGCCGTCGACGCGGCCTCCGAGGCGCTGCCTGCCTGGAGCGCCACCCCGCCCCGGCAGCGCGCGGAGCTGCTGCGGACCCTGTTCGACCTCATGGTGGGACAGGTCGAGGAGCTCGCGGTGCTCATCAGCGCCGAGAACGGCAAGTCCCTGGACGACGCTAGGGCGGAGGTCCTCTACGCGGCGGAGTTCTTCCGATGGTTCTCCGAGGAAGCCGTGCGCACCGAGGGCGGTTTCGGCTCCTCCCCGGCAGGCGGGACCCGGACGATCGTCACGCACCGCCCGATCGGGGTGGTTGCCATGATCACCCCCTGGAACTTCCCGGCGGCGATGGGGACCCGCAAGATCGCCCCGGCCCTGGCCGCCGGGTGCACGGTGGTGCTCCGTCCCGCGTCCCTCACGCCCCTGACAGCGGTGGCACTGGGACATCTGATCCAGCAGGCCGGCGTGCCCGCGGGCGTGGTGAACATCGTGCCCTCGAGCCGTTCCGTAGAGGTCTCGACGACGTGGCTCGAGGACTCCCGGGTCCGAGCCGTCTCCTTCACCGGTTCCACCCAGGTCGGTCGTGTGCTCATGAAGCAGGCGGCGGAGAAGGTCCTGGTGTCGTCCATGGAGCTCGGGGGCAACGCACCCTTCGTGGTGGCGGCCGACGCCGATATCGACGCCGCGGTGACGGGTGCCGTTCAGGCCAAGCTCCGAGGCGGGGGCGAAGCCTGCACGGCCGCCAACCGCTTCTACGTCCACCGCGACGTCGCCCAGGAGTTCACCGAGAAGTTCTCCGCCGTCGTCCGCGACCTGAGGGTGGGGCCGGCCCTGGCGGACGAGGCGAACCAGATCGGCCCCCTGGTGACACCGGCTGCCCGCGACAAGATCAACGCCCTGGTGGACGGGGCGGTGGCCGGGGGCGCCGTCGTCCACGCCGAGTCCTCCTGGCCCCAGGAGTCTCCGGGGTCGTTCGTCCCAGTGCGGGTCCTGACGAATGTCGCCCCCGACGCGGAGATCGTGCGCACCGAGATCTTCGGCCCCGTCGCCCCGATCGTCACCTGGGACGACGAGGACGAGCTGCTGACGTGGATCAACGATACGGACTACGGGCTGTCGGGCTACGTCTTCTCCCGCGACCTCGGGTGGGCGCTGCGCCTGGCCGAGCGCATGGAGGTTGGGATGGTCGGTATCAACCGTGGGCTCGTATCCGATCCCGCCGCCCCCTTCGGGGGTGTCAAGCAGTCCGGTATCGGACGTGAGGGCGCGCGTGAAGGGATCCGTGAGTTCCAGGAGACTCAGTACTACTCGGTTGCCTGGGGCTGA","MADTRPGAATDTAAYTTLGAHPALADYLHRIRPEEGMLLGGRMTAASDGGTFDVVDPASNAVFARCTDATPVDAARAVDAASEALPAWSATPPRQRAELLRTLFDLMVGQVEELAVLISAENGKSLDDARAEVLYAAEFFRWFSEEAVRTEGGFGSSPAGGTRTIVTHRPIGVVAMITPWNFPAAMGTRKIAPALAAGCTVVLRPASLTPLTAVALGHLIQQAGVPAGVVNIVPSSRSVEVSTTWLEDSRVRAVSFTGSTQVGRVLMKQAAEKVLVSSMELGGNAPFVVAADADIDAAVTGAVQAKLRGGGEACTAANRFYVHRDVAQEFTEKFSAVVRDLRVGPALADEANQIGPLVTPAARDKINALVDGAVAGGAVVHAESSWPQESPGSFVPVRVLTNVAPDAEIVRTEIFGPVAPIVTWDDEDELLTWINDTDYGLSGYVFSRDLGWALRLAERMEVGMVGINRGLVSDPAAPFGGVKQSGIGREGAREGIREFQETQYYSVAWG$","Succinate-semialdehyde dehydrogenase","Cytoplasm","succinate-semialdehyde dehydrogenase","succinate-semialdehyde dehydrogenase ","aldehyde dehydrogenase","","Hempel J., Harper K., Lindahl R. Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. Biochemistry 1989. 28(3):1160-1167. PMID: 2713359","","","

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PF00171	$\"[43-505]T$	Aldedh
PS00687	$\"[279-286]?$	ALDEHYDE_DEHYDR_GLU

InterPro
IPR012303
Family

NAD-dependent aldehyde dehydrogenase
PIRSF000147	$\"[51-510]T$	NAD-dependent aldehyde dehydrogenase

InterPro
IPR015590
Domain

Aldehyde Dehydrogenase_
PTHR11699	$\"[79-508]T$	ALDEHYDE DEHYDROGENASE-RELATED

noIPR
unintegrated

unintegrated
G3DSA:3.40.605.10	$\"[44-345]T$	no description
PTHR11699:SF49	$\"[79-508]T$	SUCCINATE SEMIALDEHYDE DEHYDROGENASE

InterPro
IPR006095
Family

Glu/Leu/Phe/Val dehydrogenase
PR00082	$\"[92-106]T$ $\"[172-194]T$ $\"[214-234]T$ $\"[341-352]T$	GLFDHDRGNASE
PTHR11606:SF2	$\"[1-415]T$	GLUTAMATE DEHYDROGENASE
PS00074	$\"[100-113]T$	GLFV_DEHYDROGENASE

InterPro
IPR006096
Domain

Glu/Leu/Phe/Val dehydrogenase, C-terminal
PF00208	$\"[181-413]T$	ELFV_dehydrog

InterPro
IPR006097
Domain

Glu/Leu/Phe/Val dehydrogenase, dimerisation region
PF02812	$\"[35-165]T$	ELFV_dehydrog_N

InterPro
IPR014362
Family

Glutamate dehydrogenase
PIRSF000185	$\"[2-416]T$	Glutamate dehydrogenase

noIPR
unintegrated

unintegrated
G3DSA:3.40.192.10	$\"[37-180]T$	no description
G3DSA:3.40.50.720	$\"[181-414]T$	no description
PTHR11606	$\"[1-415]T$	GLUTAMATE DEHYDROGENASE

","BeTs to 16 clades of COG0334COG name: Glutamate dehydrogenase/leucine dehydrogenaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0334 is ao-pkzy-vd--bcef-h-nuj-i--Number of proteins in this genome belonging to this COG is 2","***** IPB006095 (Glu/Leu/Phe/Val dehydrogenase) with a combined E-value of 2e-130. IPB006095A 57-74 IPB006095B 84-132 IPB006095C 136-161 IPB006095D 173-193 IPB006095E 211-252 IPB006095F 308-328 IPB006095G 332-356","","","-62% similar to PDB:1B3B THERMOTOGA MARITIMA GLUTAMATE DEHYDROGENASE MUTANT N97D, G376K (E_value = 7.3E_102);-62% similar to PDB:1B26 GLUTAMATE DEHYDROGENASE (E_value = 1.8E_100);-61% similar to PDB:2TMG THERMOTOGA MARITIMA GLUTAMATE DEHYDROGENASE MUTANT S128R, T158E, N117R, S160E (E_value = 2.6E_99);-59% similar to PDB:1GTM STRUCTURE OF GLUTAMATE DEHYDROGENASE (E_value = 2.1E_85);-57% similar to PDB:1EUZ GLUTAMATE DEHYDROGENASE FROM THERMOCOCCUS PROFUNDUS IN THE UNLIGATED STATE (E_value = 1.4E_84);","Residues 35 to 165 (E_value = 9.5e-68) place ANA_2760 in the ELFV_dehydrog_N family which is described as Glu/Leu/Phe/Val dehydrogenase, dimerisation domain.Residues 181 to 413 (E_value = 9.3e-102) place ANA_2760 in the ELFV_dehydrog family which is described as Glutamate/Leucine/Phenylalanine/Valine dehydrogenase.","","dehydrogenase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2761","2977435","2976113","1323","5.31","-11.25","46027","ATGGCAACGCTGCCCCAGACCATTCATCTCGCCACTCCTCTGCCCGGTCCCGAGGCCCGCGCCCTCGACGAACGCGCAGGTACCGCACTCCCACGCGCCCTGACCGCCGCCATGCCGACATTCGCACGGAGTACGGACCGAGGCGTCCTGGAGGACGTGGACGGCAACCGTCTCATCGACTTCGGATCCGGCATCGCGGTGACAACCGTGGGCGGTGCGGCGGCGCCCGTCGTCGCTGCAATCCAGGAGCAGGCCGAGAACCTGACGCACACCTCCTTCGCCGTCACGAGGTACGCCGGATACGTCGAGGTCGCCGAACGCCTGAACGCCCTGACCCCGGGCAGCTTCCCGAAGAAGACCGCGCTGTTCAACTCCGGGGCGGAGGCCGTCGAGAACGCCATCAAGCTCGCACGCAAGCACACCGGCCGCCAGGCAGTCGTCTGCTTCGACCACGCCTTCCACGGACGCACCTCCCTGACCATGGGACTGACGGCCAAGGTCGCCCCCTACAAGGGCGGCTTCGGCCCCTTCTCCCCTGAGCTCTACCGGGTCCCCGGCTCCTACCCGTACCGCGACGGACTGGACGGCGAGGCCGCCGCCGAGCGCACGATCAGTCAGATCGAGAAGCAGGTGGGGGCATCCTCCGTCGCCGCCGTCATCATCGAGCCCATTCAGGGCGAAGGCGGGTTCATCGTGCCGGCGCCCGGCTTCCTCACCGCGCTCCAGCGCTGGTGCCATGACAACGGCGCGGTCTTCATCGCCGATGAGATCCAGTCGGGAATCGCCCGCACCGGGGCGTGGTTCGCCTGCGACCACGAGGGAGTCGTTCCCGACGTGGTGACGACCGCCAAGGGCCTGGCCGGAGGCACCCCCTTGTCGGCGGTCACCGGTTCGGCCGAGATCATGGACTCCGCCGAACCGGGCGCCCTTGGCGGCACCTACTGCGGTAACCCCCTGGCCTGTGCCGCCGCCCTGGCGACCCTGGACATGATCGAGGAGCACGATCTCCTGGGACGGGCCCGCACGATCGGCGAGACCGGCATCCGCCTGATGGAGCAGTGGAAGGCGAAGGACCCCCGCATCGGCGAGGTCCGGGGCAAGGGCGCCATGATGGCTCTCGAGCTCGTCGACCCCGACTCGCAGAAGCCCGATGCCGCACTGACCGCCGCCGTCGCGCAGGCCGCGCGCTCACGCGGTCTGATCCTGCTCACCTGCGGCACCTACGGCAATGTCATCCGCCTCCTGCCACCGGTGACCATGCCGGACGAGCTGTTCGCCGAAGGCATGGAGATCCTCGAGCAGGCGCTCCGAGACCAGCCCTGA","MATLPQTIHLATPLPGPEARALDERAGTALPRALTAAMPTFARSTDRGVLEDVDGNRLIDFGSGIAVTTVGGAAAPVVAAIQEQAENLTHTSFAVTRYAGYVEVAERLNALTPGSFPKKTALFNSGAEAVENAIKLARKHTGRQAVVCFDHAFHGRTSLTMGLTAKVAPYKGGFGPFSPELYRVPGSYPYRDGLDGEAAAERTISQIEKQVGASSVAAVIIEPIQGEGGFIVPAPGFLTALQRWCHDNGAVFIADEIQSGIARTGAWFACDHEGVVPDVVTTAKGLAGGTPLSAVTGSAEIMDSAEPGALGGTYCGNPLACAAALATLDMIEEHDLLGRARTIGETGIRLMEQWKAKDPRIGEVRGKGAMMALELVDPDSQKPDAALTAAVAQAARSRGLILLTCGTYGNVIRLLPPVTMPDELFAEGMEILEQALRDQP$","4-aminobutyrate aminotransferase","Cytoplasm","4-aminobutyrate aminotransferase","4-aminobutyrate aminotransferase ","4-aminobutyrate aminotransferase","","Yonaha K., Nishie M., Aibara S. The primary structure of omega-amino acid:pyruvate aminotransferase. J. Biol. Chem. 1992. 267(18):12506-12510. PMID: 1618757","","","

InterPro
IPR004632
Family

Bacterial 4-aminobutyrate aminotransferase
TIGR00700	$\"[24-438]T$	GABAtrnsam: 4-aminobutyrate transaminase

InterPro
IPR005814
Family

Aminotransferase class-III
PTHR11986	$\"[35-439]T$	AMINOTRANSFERASE CLASS III
PF00202	$\"[41-377]T$	Aminotran_3
PS00600	$\"[252-289]T$	AA_TRANSFER_CLASS_3

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[74-334]T$	no description

noIPR
unintegrated

unintegrated
PTHR11986:SF17	$\"[35-439]T$	4-AMINOBUTYRATE AMINOTRANSFERASE

","BeTs to 21 clades of COG0160COG name: PLP-dependent aminotransferasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0160 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is 2","***** IPB005814 (Aminotransferase class-III) with a combined E-value of 4e-52. IPB005814A 44-81 IPB005814B 124-138 IPB005814C 237-265 IPB005814D 277-291 IPB005814E 310-328","","","-56% similar to PDB:1SF2 Structure of E. coli gamma-aminobutyrate aminotransferase (E_value = 6.0E_86);-56% similar to PDB:1SFF Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (E_value = 6.0E_86);-56% similar to PDB:1SZS The structure of gamma-aminobutyrate aminotransferase mutant: I50Q (E_value = 6.0E_86);-56% similar to PDB:1SZU The structure of gamma-aminobutyrate aminotransferase mutant: V241A (E_value = 1.8E_85);-56% similar to PDB:1SZK The structure of gamma-aminobutyrate aminotransferase mutant: E211S (E_value = 2.3E_85);","Residues 41 to 377 (E_value = 3.8e-133) place ANA_2761 in the Aminotran_3 family which is described as Aminotransferase class-III.","","aminotransferase (gabT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2763","2977679","2979208","1530","5.08","-14.86","54298","GTGCTTCTGCCCGCACCGCACGCCGCGGTCACCTGGGTCGTCGCGACCGAGCTCCTCCAACCGGCCTCCTACCTCGAGGGTGGCGAGCTCGTTCTCACCACGGGTCTCGTCATGGCCGATGCGGAGGCGGCCACGTGGCGGGAGTACGTGGCATCACTGGTCGAGGCGGGAGTCGCGGCTCTCGGACTGGGGACCGGCATCGCCTTCGACACCGTGCCCGAGGACCTGCGCGAGGCCTGCAGGGCCGGGCGTCTCAATCTCATCGAGGTCCCCCTCGAGGTCTCCTTCGCCTCCATCAGCCGCGAGGTTGGGGCCATGCTTCAGGCCACCGAGCCTGAGATCGGTGCCGAGGGGGCGGGAGACGAGGAGACCCTGGTCCTGCAACAGCTGACGCGTGCAGCCGCCAAGGACAACCAGAGCGCGATCATGCGCGCCTTGGCCTCGATCCTCCGGGGCGAGGTGTCCCTGCGGGATGCCACGGGACGCACCGTGGTCGGTCCCTTCGGGCCGGAGGCGACGGGAATCGACGACGAGGTCGCCGAGTGCATCGACAGGATCCGTCCGGGAGGGATGCGAGGAGCCGGGGCGGTCGGCCTCGGCGACATGCGGCTGGTCGTCCGCCCGGTCGGCATCACCGGCGAGCCCGAGCGCTACCTGGCGACCGTTCAGCGCGAGACGCTCACGCGCGCTCAGACCCTGGGGGTCGATCTCGCCTGGTCGTTTCTGAATCTCATCGCCGAGTCCTCCAAGGCCTTCACCGGATGGCTCCTCCAGCTCGTGGGGGCCTCCACCCGGCATCTCCTGGTGGGTGACATCGCGCAGGGGCTGGCGCTGGCGGACCAGGTTCAGGAGCTCGTCCTCACACGTCTGCCGTCTCCGGAGCGGCGATCGGTGCCCGCTACCGGTGGTGGTCATCAGTGGCGGGTTGTCTGCCTCGAGGGTGGCAGTGCTGACGTTGCTGGGCTCTCCACAGTGCTGGCCCGCCTGCTCGTCGAGAGTCGGGGGGCTCCGGTGGGGGAGCGGCTTCTGTGGCGCACGGACCGGGGCGGGACCCGCCTGATGATCCTCGGTGAGGTCGAGCGCGTTCCCTCCCTTCTTGAGGACGGCAGTGTCACGCCCTGGACGGAGCGGATGCGGATCGGCGTCAGCGGTCCTGTCGGCGTCACTGATCTGCCGCGGGGCGCACAGCAGGCGCTGTCCGCCTGCACCGGAACTCGGCAGCTCGGACAGGCGGTGCGCTGGGAGACCTCGGGACTGCCGTCGGTCACGGACCTCCTGGACGAGGAGCGGGCCCAAGCCTTCGCCCGCGCTCGCCTTGGGGGCGTCGCCGATCAGCCCGAGCTGCTCGAGCTGTTGAGGATCTACCTCAGCGAGGCCGGGGCGGTGCAGCGCATCGCCGAGCGTCTGGGGGTGCATCGAAACTCCGTCCCCGCACGTCTTGCGCGCCTGAGGAGGGCACTCGGCGTCGACATCGAGGATGCCGAGCAGCGGGCGAATTTGTGGTTTGCGTTACATTTTTGGGTGGAGTGA","VLLPAPHAAVTWVVATELLQPASYLEGGELVLTTGLVMADAEAATWREYVASLVEAGVAALGLGTGIAFDTVPEDLREACRAGRLNLIEVPLEVSFASISREVGAMLQATEPEIGAEGAGDEETLVLQQLTRAAAKDNQSAIMRALASILRGEVSLRDATGRTVVGPFGPEATGIDDEVAECIDRIRPGGMRGAGAVGLGDMRLVVRPVGITGEPERYLATVQRETLTRAQTLGVDLAWSFLNLIAESSKAFTGWLLQLVGASTRHLLVGDIAQGLALADQVQELVLTRLPSPERRSVPATGGGHQWRVVCLEGGSADVAGLSTVLARLLVESRGAPVGERLLWRTDRGGTRLMILGEVERVPSLLEDGSVTPWTERMRIGVSGPVGVTDLPRGAQQALSACTGTRQLGQAVRWETSGLPSVTDLLDEERAQAFARARLGGVADQPELLELLRIYLSEAGAVQRIAERLGVHRNSVPARLARLRRALGVDIEDAEQRANLWFALHFWVE$","Regulator of polyketide synthase expression","Cytoplasm","PkwR","regulatory protein","purine catabolism PurC domain protein","","Schultz A.C., Nygaard P., Saxild H.H. Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J. Bacteriol. 2001. 183(11):3293-3302. PMID: 11344136","","","

InterPro
IPR012914
Domain

Purine catabolism PurC-like
PF07905	$\"[1-111]T$	PucR

noIPR
unintegrated

unintegrated
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 3 clades of COG2508COG name: Regulator of polyketide synthase expressionFunctional Class: T [Cellular processes--Signal transduction mechanisms] Functional Class: Q [Metabolism--Secondary metabolites biosynthesis, transport and catabolism]The phylogenetic pattern of COG2508 is ---------drlb--f----------Number of proteins in this genome belonging to this COG is 2","***** IPB008599 (Putative sugar diacid recognition) with a combined E-value of 2.6e-09. IPB008599E 448-502","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 111 (E_value = 2.9e-21) place ANA_2763 in the PucR family which is described as Purine catabolism regulatory protein-like family.",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2764","2979509","2980936","1428","5.06","-18.45","50815","ATGAGCCTTCCTCTCCTCCAGAATTTTATTGACGGACGATTTGTTCCGGCAACCACCGATACCACGTTCGACGTCGTGGATCCTCGAACGGAACAAGTCGTGGCGCAGTGCCCGGTCTCAGGGGCCGCCGATGTCGACGCCGCCTACGACGCCGCCCTCAAGGCATTCGAGAGCTGGCGGCTGACAACGCCGGCGGACCGGCAGCTGCTCCTGCTCCGACTCGCCGACGCCCTGGAGGCCAACGCCGACCGTCTCGTCGAGGCTCAGCGCCGCAACACCGGTCAGCTCGCCGAGATGATCCGGGCGGAGGAAGTCGTGACAGGGGCCTCTCAGCTGCGGTTCTTCGCCGGGGCCGCCCGTCTCCAGTCGGGTGTCGCCTCGGGGGAGTACGCCGAGGGCCTGAACTCGCAGATTCGCCGCGAGCCCATCGGCGTCGTCGGGCAGATCGTCCCGTGGAACTACCCCTTCATGATGCTCATCTGGAAGGTCGGGCCCGCTCTGGCCGCAGGCAACACGGTGGTGCTCAAGCCGAGTGCCAACACGCCCGAGAGCGCCATCGTCTTTGCTGAGATCGCCGGCGAGATCCTCCCGCCCGGGGTCTTCAACCTGGTGCTCGGCACCGGGGAGACCGGGCGCCTCATGAGCGCCCACCCGGTGCCCGGGCTGGTCGCGCTCACCGGTTCGGTGCGCGCGGGCTCGGATCTCGCCGAACAGGCGGCCGGCAACGTGACCCGCGTCCATCTCGAGCTGGGAGGCAAGGCCCCCGCCGTCGTCTTCGCCGATGCCGACATCGAGGCTGCCGCCGAGGGCATCGCCGCGGCAGGGACGTTCAACGCCGGGCAGGACTGCACCGCCGCCACCCGCGTCCTGGTCGAGGCCTCGGTGGCCAAGGAGTTCACCGACGCGTTGGTGCGTCACGTCGAGTCCCTGCGCACCGGTCCGATCCCCGAGGAGGAGGCGTTCTATGGTCCCCTCAACAATGCTCGCCACTTCGACTCCGTGCAGAAGATCGTTGAGGAGCGGCCCGCGCACTCCCACCTGCTGACCGGCGGCCACCGCGTCGGCGAGAGCGGCTACTACTACGCGCCCACCGTCATCTCAGGGCTCAAACAGGACGACGCGCTCGTGCAGCAGGAGATCTTCGGGCCGGTCCTGACCGTTCAGGAGTTCTCCTCCGACGACGACGCCCTGGCCATGGCCAACGGCGTGGACTACGCCCTGTCCTCGTCCATCTGGACGACCGACCACCAGCGTGTCCTGCGATTCAGCAGGGACCTGGACTTCGGCTGCGTCTGGGTGAACTGCCACATCCCCCTCGTCGCGGAGATGCCGCACGGCGGCTTCAAACGGTCCGGCTACGGCAAGGACCTCTCCGTCTACGGCGTGGAGGACTACACACGTATCAAGCACGTCATGAGTGCCCTGTGA","MSLPLLQNFIDGRFVPATTDTTFDVVDPRTEQVVAQCPVSGAADVDAAYDAALKAFESWRLTTPADRQLLLLRLADALEANADRLVEAQRRNTGQLAEMIRAEEVVTGASQLRFFAGAARLQSGVASGEYAEGLNSQIRREPIGVVGQIVPWNYPFMMLIWKVGPALAAGNTVVLKPSANTPESAIVFAEIAGEILPPGVFNLVLGTGETGRLMSAHPVPGLVALTGSVRAGSDLAEQAAGNVTRVHLELGGKAPAVVFADADIEAAAEGIAAAGTFNAGQDCTAATRVLVEASVAKEFTDALVRHVESLRTGPIPEEEAFYGPLNNARHFDSVQKIVEERPAHSHLLTGGHRVGESGYYYAPTVISGLKQDDALVQQEIFGPVLTVQEFSSDDDALAMANGVDYALSSSIWTTDHQRVLRFSRDLDFGCVWVNCHIPLVAEMPHGGFKRSGYGKDLSVYGVEDYTRIKHVMSAL$","Aldehyde dehydrogenase","Cytoplasm","aldehyde dehydrogenase","aldehyde dehydrogenase ","aldehyde dehydrogenase","","Hempel J., Harper K., Lindahl R. Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. Biochemistry 1989. 28(3):1160-1167. PMID: 2713359","","","

InterPro
IPR002086
Domain

Aldehyde dehydrogenase
PF00171	$\"[14-471]T$	Aldedh
PS00687	$\"[248-255]?$	ALDEHYDE_DEHYDR_GLU

InterPro
IPR012303
Family

NAD-dependent aldehyde dehydrogenase
PIRSF000147	$\"[22-475]T$	NAD-dependent aldehyde dehydrogenase

InterPro
IPR015590
Domain

Aldehyde Dehydrogenase_
PTHR11699	$\"[50-475]T$	ALDEHYDE DEHYDROGENASE-RELATED

noIPR
unintegrated

unintegrated
G3DSA:3.40.605.10	$\"[7-291]T$	no description
PTHR11699:SF39	$\"[50-475]T$	ALDEHDYE DEHYDROGENASE

InterPro
IPR006016
Domain

UspA
PF00582	$\"[1-138]T$ $\"[165-276]T$	Usp

InterPro
IPR014729
Domain

Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620	$\"[2-136]T$ $\"[149-282]T$	no description

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-43% similar to PDB:1X08 Crystal structure of D26A mutant UPPs in complex with Mg, IPP and FsPP (E_value = );-43% similar to PDB:1X09 Crystal structure of the D26A mutant UPPs in complex with magnesium and isopentenyl pyrophosphate (E_value = );-43% similar to PDB:1JP3 Structure of E.coli undecaprenyl pyrophosphate synthase (E_value = );-43% similar to PDB:1UEH E. coli undecaprenyl pyrophosphate synthase in complex with Triton X-100, magnesium and sulfate (E_value = );-43% similar to PDB:1V7U Crystal structure of Undecaprenyl Pyrophosphate Synthase with farnesyl pyrophosphate (E_value = );","Residues 1 to 138 (E_value = 1.9e-09) place ANA_2765 in the Usp family which is described as Universal stress protein family.Residues 148 to 276 (E_value = 2.9e-05) place ANA_2765 in the Usp family which is described as Universal stress protein family.","","stress protein family domain protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2766","2981824","2983407","1584","5.13","-5.10","56370","ATGAGCGCCGCGACCACCAGCTCTGGAGGCGGGCTGTCGAAGAAGGGACTGGCTGAGGGCTCTGTCGGCCTGCTCGGCGCCATCATCATCGGCGTGTCCTGCATCGCGCCTCCGTACACCCTCACCGGCGCACTGGGGCCGACCGCCTCAGAGGTGGGCGAGCAGGTACCGGCGATCTTCCTCGTCGGGTTCATCCCGATGCTCCTGGTCGCCTTCGGGTACCGAGAGCTCAATGCGGCGATGCCCGATTCGGGCACCTCCTTCACCTGGGGGACCCGCGCCTTCGGTCCGTGGATCGGGTGGATGAACGGATGGGGGCTGATCGTGGCCACCGTCGTCGTCCTGTCGAACCTCGCGGCCATCGCGGTCGACTTCTTCTACCTGTTGCTCGCACAGGTGACTCGCCGGCCCGCCATTGCGGATCTCTCCGACAACGTATGGGTCAACACCCTCACCTGCCTGGTCTTCATCACGCTGGCGACCTGGATCGCGTATCGCGACATGCAGACCACCCAGAAGCTCCAGTACTGGTTGGTGGGGTTTCAGCTGACGGTGTTCCTCGGCTTCGGCGCGGTGGCGATTTACCGCTACTTCACCGGCACCGCTGTCAATCCGACACCCGTGAAGCTCGAATGGTTCAATCCCTTCGCCGTCGACTCGCTGGGGACCTTTGTGGCGGGCGTGTCCCTGTCCTTGTTCATCTACTGGGGCTGGGACGTGTCGCTGACGGTCAATGAGGAGGCCGACGACGCCAGCTCCACCCCGGGGCGCGCCGCCGTGCTCACCGTCATGACCATCGTCTCGGTGTACATGTTCGTCACGATCGGATCCATGATGTTCGCCGGTCTGGGGAAGGACGGGATAGGGCTGGGCAATCCTGCGATCCAGGACAATGTCTTCTTCGCCTTGGCCAGGCCGGTTCTGGGGCCGTTCGCGATCCTCCTGTCGACGGCGGTGCTGGTCTCGTCGGCGGCGTCCTTGCAGTCCACCTTCGTCTCTCCCGCCCGCACCCTCCTGTCGATGGGGTATTACGGAGCAATGCCGGAGAAGCTCGGTGAGATCTCTCCGCGCTTCCTGACTCCCGGGCGCGCAACAGTCGTCTCGGCGATCGCCGCCTCGACCTTTTACACGCTGCTGCGCTTCGTATCCACCTCCGTCCTGTGGGACACGGTTCAGACCCTGGGGGCGATGATCGCCTTTTACTACGGGCTCACCGCCTTCGCCGCGGTGTGGTACTTCCGAGGACAGTGGTTCCGCTCGGTGAGGAACTTCTTCTTCATGCTGGTCTCACCGGGACTGGGAGGTCTTATCCTCTTCTTGCTGCTCGGCCTGACCCTGAAGGACTCCCTCAACCCCGAGTACGGGTCGGGATCGCAGGTCTTCGGCGTCGGTCTCGTCTTCGTCCTCACCCTCGCCCTCATTCTCCTGGGCGTGGTGCTGATGCTTGTACAGTACGTCCGAGCACCGGCCTTCTTCCGCGGGGAGGTGATCGCACGATCCGACGCTGTCACCGAGGAGTTGAAGGTGGCAACTGTCTTAGAGGAGGACGATGGTGAAGCCTCCCAGCTCCGTGCTGCGTCATAG","MSAATTSSGGGLSKKGLAEGSVGLLGAIIIGVSCIAPPYTLTGALGPTASEVGEQVPAIFLVGFIPMLLVAFGYRELNAAMPDSGTSFTWGTRAFGPWIGWMNGWGLIVATVVVLSNLAAIAVDFFYLLLAQVTRRPAIADLSDNVWVNTLTCLVFITLATWIAYRDMQTTQKLQYWLVGFQLTVFLGFGAVAIYRYFTGTAVNPTPVKLEWFNPFAVDSLGTFVAGVSLSLFIYWGWDVSLTVNEEADDASSTPGRAAVLTVMTIVSVYMFVTIGSMMFAGLGKDGIGLGNPAIQDNVFFALARPVLGPFAILLSTAVLVSSAASLQSTFVSPARTLLSMGYYGAMPEKLGEISPRFLTPGRATVVSAIAASTFYTLLRFVSTSVLWDTVQTLGAMIAFYYGLTAFAAVWYFRGQWFRSVRNFFFMLVSPGLGGLILFLLLGLTLKDSLNPEYGSGSQVFGVGLVFVLTLALILLGVVLMLVQYVRAPAFFRGEVIARSDAVTEELKVATVLEEDDGEASQLRAAS$","Amino acid transporter","Membrane, Cytoplasm","amino acid transporter, putative","amino acid transporter; APC family","amino acid permease-associated region","","Weber E., Chevallier M.R., Jund R. Evolutionary relationship and secondary structure predictions in four transport proteins of Saccharomyces cerevisiae. J. Mol. Evol. 1988. 27(4):341-350. PMID: 3146645Vandenbol M., Jauniaux J.C., Grenson M. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases. Gene 1989. 83(1):153-159. PMID: 2687114Reizer J., Finley K., Kakuda D., MacLeod C.L., Reizer A., Saier Jr M.H. Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria. Protein Sci. 1993. 2(1):20-30. PMID: 8382989","","","

InterPro
IPR002293
Family

Amino acid/polyamine transporter I
PTHR11785	$\"[59-516]T$	AMINO ACID TRANSPORTER

InterPro
IPR004841
Domain

Amino acid permease-associated region
PF00324	$\"[26-490]T$	AA_permease

InterPro
IPR006741
Family

Accessory gene regulator B
SM00793	$\"[336-496]T$	no description

noIPR
unintegrated

unintegrated
PIRSF006060	$\"[16-500]T$	High-affinity amino acid transporter
signalp	$\"[1-34]?$	signal-peptide
tmhmm	$\"[21-41]?$ $\"[55-73]?$ $\"[94-128]?$ $\"[147-165]?$ $\"[177-197]?$ $\"[216-238]?$ $\"[259-281]?$ $\"[307-327]?$ $\"[364-384]?$ $\"[394-414]?$ $\"[424-444]?$ $\"[463-483]?$	transmembrane_regions

","BeTs to 13 clades of COG0531COG name: Amino acid transportersFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0531 is aomp-zy---rlbcefghs--jxi-wNumber of proteins in this genome belonging to this COG is 2","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 490 (E_value = 0.013) place ANA_2766 in the AA_permease family which is described as Amino acid permease.","","acid transporter, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2767","2983581","2984951","1371","5.31","-16.00","50168","ATGAGCATCAACATGGAGCGAGTCGCTGAGCTGACGGAGATCGAGTCCAGGCGCCTCAATGAACGGACCAAGGGGTCCGGCGACATGTACAACCGCGCGAGAAACAGCCTTTCCGGCGGTGTCGCCTCCTCGTACCAGCTGCGCGAGCCCTGGCCCATTTACCTTGAACGGGGGCAGGGGCCGAAGGTCTGGGATGTTGACGGCAACGAGATGTGGGACTTCCACAACGGCTTCGGATCGATGCTTCAGGGGCATGCCCACCCGGTGATCGGAGAAGCCATTCAGGAGCGGTACGGCAAGGGCACCCACTTCGCCGCCCCGACCGAGGACGCCCTGGCGGTGGCGGAGAACCTCTCGAGCAGGTGGGGGCTGCCGAAGTGGCGCTACACGAACTCGGGCTCGGAGTCCACGATGGACGCGATCCGTATTGCACGCGCCTACACCGGTCGCGACACGGTCATGAAGATCTTCGGCTCCTACCACGGGCACCACGACACCGTCATGGTCTCGATCGGCGTCGAGTACGACAAGATCGGTGACCGTGACAACCTGGCCTCGCTGCCCTACGGAGGCGGCATTCCCGACGCCACCGTCCAGATGACGGTGCCGGTTCCCTTCAACGATGCCGAGGCCATGGAGCGCCGCATCATCCGGCTGACCGATGAGGGGCGTAAGCCCGCCTGCGTCATCATGGAGCCGGCCATGATGAACCTGGGCGTCGTGCTGCCGGAACCGGGATATCTGGAGCAGGTCCGCGAGATCACCCGGCGACACGGCGTCGTCCTGATCTTCGATGAGGTCAAGACCGGCCTGTGCATCGGTCCGGGCGGCGCCACCCAGCGCTTCGGAGTGACTCCCGACCTGGTGACCATGGCCAAGGCCCTGGGTGGCGGTCTGCCCTCGGGCGCCATCGGAGGCACCGAGGAAGTCATGTCCGTGGTGGAGGACCACACCGTCTTCCAGGTCGGCACCTACAACGGCAACCCCCTGGTGATGGCCGCAGTGCGGGCCAACCTCGAGAAGGTCCTCAACCCGGAGGCATACGCCCACCTCGACCACCTCAACGATCGCATTCTCGCGGGTTGCACGGAGGTCATTGAGCGCTACAACCTTCCGGGCTACGCGGTGGGCGTCGGCGGCAAGGGGTGCGTCACCTTCTCCCCCAAGAAGGTCGTCGACTACGAGTCCTTCAAGGAGCACCAGAATGCGGAGCTGTCCGAGCTCGCGTGGCTGTTCAACATGAACCGGGGGATCTTCATGACTCCGGGCCGCGAGGAGGAGTGGACCCTGTCAGTGACCCACACGGACGAGGCGATCGACGCCTACGTCAGCTGCTTCGAGGAGCTTGCCGAGGCGATCACTTCCAAGTGA","MSINMERVAELTEIESRRLNERTKGSGDMYNRARNSLSGGVASSYQLREPWPIYLERGQGPKVWDVDGNEMWDFHNGFGSMLQGHAHPVIGEAIQERYGKGTHFAAPTEDALAVAENLSSRWGLPKWRYTNSGSESTMDAIRIARAYTGRDTVMKIFGSYHGHHDTVMVSIGVEYDKIGDRDNLASLPYGGGIPDATVQMTVPVPFNDAEAMERRIIRLTDEGRKPACVIMEPAMMNLGVVLPEPGYLEQVREITRRHGVVLIFDEVKTGLCIGPGGATQRFGVTPDLVTMAKALGGGLPSGAIGGTEEVMSVVEDHTVFQVGTYNGNPLVMAAVRANLEKVLNPEAYAHLDHLNDRILAGCTEVIERYNLPGYAVGVGGKGCVTFSPKKVVDYESFKEHQNAELSELAWLFNMNRGIFMTPGREEEWTLSVTHTDEAIDAYVSCFEELAEAITSK$","Glutamate-1-semialdehyde aminotransferase","Cytoplasm","Glutamate-1-semialdehyde 2,1-aminomutase(GSA)(Glutamate-1-semialdehyde aminotransferase) (GSA-AT)","glutamate-1-semialdehyde aminotransferase ","aminotransferase class-III","","Yonaha K., Nishie M., Aibara S. The primary structure of omega-amino acid:pyruvate aminotransferase. J. Biol. Chem. 1992. 267(18):12506-12510. PMID: 1618757","","","

InterPro
IPR005814
Family

Aminotransferase class-III
PTHR11986	$\"[43-453]T$	AMINOTRANSFERASE CLASS III
PF00202	$\"[54-388]T$	Aminotran_3
PS00600	$\"[262-298]?$	AA_TRANSFER_CLASS_3

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[87-345]T$	no description

noIPR
unintegrated

unintegrated
PTHR11986:SF5	$\"[43-453]T$	GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE

","BeTs to 19 clades of COG0001COG name: Glutamate-1-semialdehyde aminotransferaseFunctional Class: H [Metabolism--Coenzyme metabolism]The phylogenetic pattern of COG0001 is aomp-z-q-dr-bcefghsnuj-i--Number of proteins in this genome belonging to this COG is 2","***** IPB005814 (Aminotransferase class-III) with a combined E-value of 1.9e-51. IPB005814A 57-94 IPB005814B 131-145 IPB005814C 247-275 IPB005814D 286-300 IPB005814E 321-339","","","-50% similar to PDB:2HOY Inter-subunit signaling in GSAM (E_value = 2.3E_59);-50% similar to PDB:2HOZ Inter-subunit signaling in GSAM (E_value = 2.3E_59);-50% similar to PDB:2HP1 Inter-subunit signaling in GSAM (E_value = 2.3E_59);-50% similar to PDB:2HP2 Inter-subunit signaling in GSAM (E_value = 2.3E_59);-50% similar to PDB:2GSA CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE, WILD-TYPE FORM) (E_value = 3.8E_59);","Residues 54 to 388 (E_value = 7.5e-56) place ANA_2767 in the Aminotran_3 family which is described as Aminotransferase class-III.","","2,1-aminomutase (GSA)(Glutamate-1-semialdehyde aminotransferase) (GSA-AT) (hemL)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2768","2985548","2985042","507","6.60","-0.56","19386","GTGAAGGACTACGCCTCCGGTGAGGAGCTCATCGCGGAGATCCGCAAGCGCGCTGAGCTGTTCATCGCCGAGTTCGACGACGTCCCCGCCTCCGAACTCCACACGCTCAAGGACGGGGAGGACCGCACGCCGGCGCAGATGCTCGCCTACCAGCTGGGGTGGATGGACCTGCTGCTGGGCTGGGAGCGCGATGATCGGGCCGGACGCGAGGTGGTCACGCCCGCTCCCGGGTACCGGTGGAACCGACTCGGCGATCTCTACAGCGCCTTCTACGAGCAGTGGCGTGACGCCTCCCTGCCCCGGCTTCAGGAGGCCTTTCGGAACCGGGGCGACGACGTCGTCGCCCTCGTGGCATCGCTGAGCCGGGAGGAGCTCTTCACTTCCGGGCAGCGGGCGTGGGCCTCCTCGACGCCGTCGGCCTGGCCGGTGGCCAAGTGGATCCACATCAACACGGTGGCGCCCTTCACCTCCTTCCGCACGAGGATCCGCGCCTGGAAACGCCGCTGA","VKDYASGEELIAEIRKRAELFIAEFDDVPASELHTLKDGEDRTPAQMLAYQLGWMDLLLGWERDDRAGREVVTPAPGYRWNRLGDLYSAFYEQWRDASLPRLQEAFRNRGDDVVALVASLSREELFTSGQRAWASSTPSAWPVAKWIHINTVAPFTSFRTRIRAWKRR$","Conserved hypothetical protein","Cytoplasm","Unknown","hypothetical protein","protein of unknown function DUF1706","","","","","

InterPro
IPR012550
Family

Protein of unknown function DUF1706
PF08020	$\"[1-168]T$	DUF1706

","No hits to the COGs database.","***** IPB012550 (Protein of unknown function DUF1706) with a combined E-value of 1.9e-51. IPB012550A 1-31 IPB012550B 41-90 IPB012550C 116-126 IPB012550D 141-167","","","-37% similar to PDB:1EV1 ECHOVIRUS 1 (E_value = );-43% similar to PDB:1FOH PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM (E_value = );-43% similar to PDB:1PN0 Phenol hydroxylase from Trichosporon cutaneum (E_value = );-51% similar to PDB:1EJ6 Reovirus core (E_value = );-51% similar to PDB:2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution (E_value = );","Residues 1 to 168 (E_value = 1.2e-56) place ANA_2768 in the DUF1706 family which is described as Protein of unknown function (DUF1706).",""," ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2769","2986169","2985951","219","11.92","8.37","7579","ATGGTGCTGACATCAACCCCGCATCGGCGTTGGGCACCGAGGAAGAACCGCAGGATTCCAACGATCCCCACTGGGCGCACTGGCGCCGGGCTCGTTGATGTCAGCACTGTGGACACCGGGCCGCGCAGGAGCGAGTCCGGAGTTCGTACGGCACGGCCCGGCGCCTCCGTCACAGATCCGCCCCACCGTCCCCTGACCGCCGCCTGCGCAGGGGCCTGA","MVLTSTPHRRWAPRKNRRIPTIPTGRTGAGLVDVSTVDTGPRRSESGVRTARPGASVTDPPHRPLTAACAGA$","Hypothetical protein","Extracellular","breakpoint cluster region protein, putative","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-47% similar to PDB:2BF6 ATOMIC RESOLUTION STRUCTURE OF THE BACTERIAL SIALIDASE NANI FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH ALPHA-SIALIC ACID (NEU5AC). (E_value = );","No significant hits to the Pfam 21.0 database.","","cluster region protein, putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2770","2987938","2986367","1572","9.44","9.36","56391","ATGTCAACGACCCCGACTCCCGTCGAGGACGATCTCGATACTGGTCGGATGATCGCCAGTCGGTGGCGACCCGCCACCCTGCGCACGACGCCGTCGAAGCAGGACCGGGGGCTGTTCGGCCACCCCCGCGGACTGCCCTGGATGCTCAATGTGGAGATGTGGGAGCGCTTCTCCTACTACGGCATGCGCGCCATCCTTCTCTACTTCATCACCGATACCGTGGCCGGCGGTGGCCTGGGCCTGAGCGCCAACTCCGGGCAGGTCATCCTGGCCTCCTACAGTGCGGCCGTCTACCTGCTGGCCATCCCCGGGGGCATCTTCGCCGACCGCATCATCGGACCGTGGCTATCCACCCTCTACGGCGGCGTCGTCATCATGGCGGGCCACATCTGTCTGTCCATCCCCACGCCCGCACTCGCCTGGACGGGGATCGTGCTGGTGGCCGTGGGCACCGGCTTCATCAAGCCGAACCTGTCCACGATCGTCGGGGGTCTCTACGATGACGACGACCCTCGGCGCGACGCCGGATTCCAGCTGTTCTACATGTCGGTCAACCTCGGCTCGCTGGCGTCCCCACTGGTGACCGGCTGGCTGCGTGAGCACTACGGCTACCACGCCGGCTTCTTCTCGGCCGCCGTCGGCATGGGGGTGGCCCTGATCGCCTTCATCTACGGCCGTCACAAGCTCTCCGCCTTCGCCTTCACCGTCCCGAGCCCCATCCGCCCCCAGGAGCGCCGGAGCTTCATACTCGCCTCACTCCTGACCGTGGTGGCCGCGGCCGCACTCGTCACTGTCCTGAGCGCCCTGACCGGGAGCCTGCTCGACGCCATCTCCACGACCATGCTCATCATCCCGGCCGGTGCCGCCCTGGGCTACTTCATCCTCATGTTCCGCTCCCCCAAGGTCACGGCCCGCGAGCGCACCCACCTGCGCGCCTACATCCCCCTGTGGATCGGCGCGGTCCTGTTCTTCATGATCTCCGAGCAGGCGGCTGGCAAGATGGCCACCTTCGCCAAGGACAACACCGATGGCAGTATCCCGTGGCTCGGCTGGGCCATCACCCCGGAGACCTACCAGTCCATCAACCCAGCCACGATCGTCATCCTGGCACCATTCATCGGTTGGCTCTTCACCCGGCGGGCGGGCAGGTTTCCCTCCACCATCATGAAGTTCGCGATCTCGGTGCTCATCATCGGGGGATCGGCCTTCATCCTGGGCTACGGCTTCCAGATCTGGCCGGGCGGCGCAAAGCTGTCCCCCTGGTGGTTCCTGGCGGTGGTCTTCATCATCCAGACCGTCGCCGAGCTCTTCCTGTCCCCGGTAGGACTGTCCACGACGTCGGCGCTGGCACCCAAGAACTTCGCCTCCCAGACGATGAGCCTGTGGCTGCTGACGACGGCCACCGGTCAGGGGCTGGCCGGCTTCATCATCTCCAGGACGGAGAACATCGCGAACTCCACCTACTACTACGGCCTGGGGGCCGTGACGGTCGCCGTGGCCATCATCCTGTTCATCGTCGCCCCGTGGACGGAGCGGAAGATGGCCGACGTCGGGGTCACCTCCCAGGACTAG","MSTTPTPVEDDLDTGRMIASRWRPATLRTTPSKQDRGLFGHPRGLPWMLNVEMWERFSYYGMRAILLYFITDTVAGGGLGLSANSGQVILASYSAAVYLLAIPGGIFADRIIGPWLSTLYGGVVIMAGHICLSIPTPALAWTGIVLVAVGTGFIKPNLSTIVGGLYDDDDPRRDAGFQLFYMSVNLGSLASPLVTGWLREHYGYHAGFFSAAVGMGVALIAFIYGRHKLSAFAFTVPSPIRPQERRSFILASLLTVVAAAALVTVLSALTGSLLDAISTTMLIIPAGAALGYFILMFRSPKVTARERTHLRAYIPLWIGAVLFFMISEQAAGKMATFAKDNTDGSIPWLGWAITPETYQSINPATIVILAPFIGWLFTRRAGRFPSTIMKFAISVLIIGGSAFILGYGFQIWPGGAKLSPWWFLAVVFIIQTVAELFLSPVGLSTTSALAPKNFASQTMSLWLLTTATGQGLAGFIISRTENIANSTYYYGLGAVTVAVAIILFIVAPWTERKMADVGVTSQD$","Dipeptide/tripeptide permease","Membrane, Cytoplasm","di-tripeptide transporter homolog lin0564","K03305 proton-dependent oligopeptide transporter; POT family","amino acid/peptide transporter","","Steiner H.Y., Naider F., Becker J.M. The PTR family: a new group of peptide transporters. Mol. Microbiol. 1995. 16(5):825-834. PMID: 7476181Paulsen I.T., Skurray R.A. The POT family of transport proteins. Trends Biochem. Sci. 1994. 19(10):404-404. PMID: 7817396","","","

InterPro
IPR000109
Family

TGF-beta receptor, type I/II extracellular region
PTHR11654	$\"[32-523]T$	OLIGOPEPTIDE TRANSPORTER-RELATED
PF00854	$\"[115-470]T$	PTR2
PS01023	$\"[177-189]T$	PTR2_2

InterPro
IPR005279
Family

Amino acid/peptide transporter
PTHR11654:SF6	$\"[32-523]T$	DI-TRIPEPTIDE ABC TRANSPORTER
TIGR00924	$\"[37-514]T$	yjdL_sub1_fam: amino acid/peptide transport

InterPro
IPR006311
Domain

Twin-arginine translocation pathway signal
TIGR01409	$\"[243-268]T$	TAT_signal_seq: Tat (twin-arginine transloc

noIPR
unintegrated

unintegrated
tmhmm	$\"[63-83]?$ $\"[89-107]?$ $\"[112-132]?$ $\"[138-158]?$ $\"[179-199]?$ $\"[205-225]?$ $\"[249-269]?$ $\"[275-297]?$ $\"[312-332]?$ $\"[358-376]?$ $\"[391-411]?$ $\"[421-441]?$ $\"[461-479]?$ $\"[485-507]?$	transmembrane_regions

","BeTs to 6 clades of COG3104COG name: Dipeptide/tripeptide permeaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG3104 is ------y----lb-e-g-sn-j----Number of proteins in this genome belonging to this COG is 2","***** IPB000109 (TGF-beta receptor, type I/II extracellular region) with a combined E-value of 5.8e-50. IPB000109A 52-70 IPB000109B 86-131 IPB000109C 143-166 IPB000109D 177-189 IPB000109E 435-470","","","-45% similar to PDB:2O2G Crystal structure of Dienelactone hydrolase (YP_324580.1) from Anabaena variabilis ATCC 29413 at 1.92 A resolution (E_value = );-47% similar to PDB:1XIO Anabaena sensory rhodopsin (E_value = );","Residues 115 to 470 (E_value = 6.4e-36) place ANA_2770 in the PTR2 family which is described as POT family.","","transporter homolog lin0564","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2772","2989783","2988140","1644","8.99","5.62","58785","ATGGCACAGTCCGAGTCCGATTCGACGTCAGGCCCGATGTCAGACTCGACATCCGGCCCGATGTCAGCCCCCACGACGGCGGTCAACGAGCGCGAGGACAGGTTGGCCGAGCCCGGCCGCCTCATCTCCAGCCGGTGGCGGCCCCGCAGCCTGCGCACGACGCCGTCGAGGCAGGACCGGGGACTGTTCGGCCACCCCCGTGGACTGCCATGGATGCTCAACGTGGAGATGTGGGAGCGCTTCTCCTACTACGGCATGCGCGCCATCCTGCTGTACTTCATCACCGACACGGTCGCCCGCGGCGGCCTGGGCCTGAGCGAGACCAGCGGACAGGTCGTCATCGCGCTCTACGGCATGGCCGTCTACTTCCTGGCCATCCCCGGCGGCATCTTCGCCGACCGCATCATCGGGCCCTGGCTGTCCACCCTCTACGGCGGCGTCGTCATCATGGCCGGGCACATCTGCCTGACCATCCCCAGCGCCGTGACCTCCTGGACGGGGATCGTGCTGGTGGCCGTGGGCACCGGCTTCATCAAGCCGAACCTGACGACCATCGTCGGCGGCCTCTACGACGACGATGACATCCGGCGCGACGCCGGATTCCAGCTGTTCTACATGTCCATCAACGTCGGCGCCTTCGCCTCTCCCCTGCTGACCGGCTGGCTGCGCGAGCACTACGGCTACCACGCCGGCTTCTCCTCGGCCGCCGTCGGCATGGCCTTCGCCTTGGGCGCCTTCATCTACGGTCGCCACAAGCTCTCCGCCTTCGCCTTCACCGTCCCGAGCCCCATCCGCCCCCAGGAGCGCCGGCGACTGCTGCTGGGCTCCCTCGGCGTCCTGGTCGCCGTCGGCGCTGTCGTGGCCGCTCTGAAGGCGATCACCGGAAACCTGGTGACCACCGTCGCCACGGCGGGCCTGCTCGTGCCGGTCGGTGCGGCCGTGGCCTACTTCGTGGTCATGTTCCGCTCCCCGAAGGTCACCGCCCCCGAGCGCACGCACCTGCGCGCCTACATCCCCCTGTGGATCGGCGCGGTCCTGTTCTTCATGATTACCGAGCAGGCGGCTGGCAAGATGGCCACCTTCGCCGACTCCAACACGGATCTGCGGCTGCCCCTGTTCGGCTGGTCGATCACCGCGGAGGCCTATCAGTCTGTCAACCCCGCGGCGATCGTGATCCTGGCCCCGCTGATCGGCATGCTTTTCACCCGGCGGGCGGGCCGGTTCCCCTCCACCATCATGAAGTTCGTCATCGCGGTGCTCATCGTGGGGCTCTCGGCGCTCCTGCTGGGCTACGGCTTCCAAATCTGGCCGGGTGGGGAGCACCTGTCCCCCTGGTGGTTCCTGGCACTGGTCTACGTCATCCAGACCGTCGCCGAGCTCTTCCTGTCCCCGGTGGGCCTGGCCACGACGACCGCCCTGGCCCCCAAGAGCTTCGCCTCCCAGGCGATGGGGCTGTGGTGGCTCAGCGTCGCCACCGGGCAGGGCGTGGCCGGCTTCGTCATCGCTCAGACCGAGGACGCCTCCGACGCCACCTACTACTACGGCCTGGGCGCGGCCACGCTGCTCATGGCCCTGGTGCTGTTCGCCGTCGCCCCGTGGACGCAGCGGCAGATGGCCGACGTCGAGGTCGCCGCGCAGGACTAG","MAQSESDSTSGPMSDSTSGPMSAPTTAVNEREDRLAEPGRLISSRWRPRSLRTTPSRQDRGLFGHPRGLPWMLNVEMWERFSYYGMRAILLYFITDTVARGGLGLSETSGQVVIALYGMAVYFLAIPGGIFADRIIGPWLSTLYGGVVIMAGHICLTIPSAVTSWTGIVLVAVGTGFIKPNLTTIVGGLYDDDDIRRDAGFQLFYMSINVGAFASPLLTGWLREHYGYHAGFSSAAVGMAFALGAFIYGRHKLSAFAFTVPSPIRPQERRRLLLGSLGVLVAVGAVVAALKAITGNLVTTVATAGLLVPVGAAVAYFVVMFRSPKVTAPERTHLRAYIPLWIGAVLFFMITEQAAGKMATFADSNTDLRLPLFGWSITAEAYQSVNPAAIVILAPLIGMLFTRRAGRFPSTIMKFVIAVLIVGLSALLLGYGFQIWPGGEHLSPWWFLALVYVIQTVAELFLSPVGLATTTALAPKSFASQAMGLWWLSVATGQGVAGFVIAQTEDASDATYYYGLGAATLLMALVLFAVAPWTQRQMADVEVAAQD$","Dipeptide/tripeptide permease","Membrane, Cytoplasm","di-tripeptide transporter homolog lin0564","K03305 proton-dependent oligopeptide transporter; POT family","amino acid/peptide transporter","","Steiner H.Y., Naider F., Becker J.M. The PTR family: a new group of peptide transporters. Mol. Microbiol. 1995. 16(5):825-834. PMID: 7476181Paulsen I.T., Skurray R.A. The POT family of transport proteins. Trends Biochem. Sci. 1994. 19(10):404-404. PMID: 7817396","","","

InterPro
IPR000109
Family

TGF-beta receptor, type I/II extracellular region
PTHR11654	$\"[56-547]T$	OLIGOPEPTIDE TRANSPORTER-RELATED
PF00854	$\"[139-494]T$	PTR2
PS01023	$\"[201-213]T$	PTR2_2

InterPro
IPR005279
Family

Amino acid/peptide transporter
PTHR11654:SF6	$\"[56-547]T$	DI-TRIPEPTIDE ABC TRANSPORTER
TIGR00924	$\"[61-538]T$	yjdL_sub1_fam: amino acid/peptide transport

noIPR
unintegrated

unintegrated
tmhmm	$\"[88-106]?$ $\"[112-132]?$ $\"[137-157]?$ $\"[163-183]?$ $\"[203-223]?$ $\"[229-249]?$ $\"[272-292]?$ $\"[298-318]?$ $\"[333-351]?$ $\"[382-400]?$ $\"[415-435]?$ $\"[445-467]?$ $\"[482-502]?$ $\"[512-532]?$	transmembrane_regions

","BeTs to 6 clades of COG3104COG name: Dipeptide/tripeptide permeaseFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG3104 is ------y----lb-e-g-sn-j----Number of proteins in this genome belonging to this COG is 2","***** IPB000109 (TGF-beta receptor, type I/II extracellular region) with a combined E-value of 2.5e-49. IPB000109A 76-94 IPB000109B 110-155 IPB000109C 167-190 IPB000109D 201-213 IPB000109E 459-494 IPB000109E 450-485","","","No significant hits to the PDB database (E-value < E-10).","Residues 139 to 494 (E_value = 3.5e-28) place ANA_2772 in the PTR2 family which is described as POT family.","","transporter homolog lin0564","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2773","2991365","2990097","1269","8.55","3.19","46070","ATGGTCAAGCGCCAGCTGCCCAACCCGAGCGAGATCTTCGAGCTGCTCCACTTCAAGACGCCCGAGCTCAACCCCAGGCGTCGCCGCCTCGACGCCGCACTGACCACCTGGGACCTGCGCAAGATCGCTAAGCGCCGCACTCCGGCCGCGGCCTTCGACTACACCGACGGCGCCGCCGAGGGTGAGGTCTCCCTGCGCCGCGCCCGCCAAGCCTTCCGCGACATCGAGTTCCACCCCGACATCCTGCGCCCGGCCATCGACGTCGACACCTCCTGCGAAATCCTGGGCGGACGCTCGGCCATGCCCTTCGGTATCGCGCCCACCGGCTTCACCCGCCTCATGCAGACCGAAGGCGAGGTCGCCGGGGCCGGGGCCGCCGGCGCCGCCGGGATCCCCTTCACCCTGTCCACGCTGGGCACCACCTCCATCGAGGACGTCAAGGCCGCCAACCCCCACGGGCGCAACTGGTTCCAGCTCTACGTCATGCGCCAGCGCGAGATCTCCTACGGGCTGGTCGAGCGTGCCGCGGCCGCCGGCTTCGACACCCTCATGTTCACCGTGGACACCCCAGTGGCCGGGGCCCGCCTGCGCGACAAGCGCAACGGCTTCTCCATCCCGCCCCAGATCACGGCCGGCACCGTCCTCAACGCGATCCCCCGCCCGTGGTGGTGGTTCGACTTCCTGACCACGCCCAAGCTGGAGTTCGCCTCCCTGAAGTCCACCGGCGGCACCGTGGGCGAGCTGCTCGACAACGCCATGGACCCCACCATCAGCGACGAGGACCTCAAGGTCATCCGCTCCATGTGGCCGGGCAAGATCGTCATCAAGGGGGTCCAGACGGTGGAGGACTCCAAGCGCCTCATCGACCTGGGCGTCGACGGCGTCCTGCTGTCCAACCACGGCGGGCGCCAGCTCGACCGCGCCCCCGTCCCCTTCCGCCTCCTGCCCGAGGTGGTCCGTGAGGTCGGCAAGGACGCCACGATCATGGTGGACACCGGCATCATGAACGGCGCCGACGTCGTGGCCGCCGTCGCCCTGGGTGCCAAGTTCGGGCTCGTGGGCCGCGCCTACCTCTACGGCCTCATGGCCGGCGGGCGCGAGGGCGTGGACCGTATGATCGAGATCCTCTCCGACGAGGTCATCCGCACCATGAAGCTCCTGGGCGTCTCCAGCCTGGACGAGCTCGAGCCGCGCCACGTCACCCAGCTGACCCGCCTGACCCCGGTGCGCCCGAACGTCAAGGCCGCAGCCGACGCCCTGGCCCGCTGA","MVKRQLPNPSEIFELLHFKTPELNPRRRRLDAALTTWDLRKIAKRRTPAAAFDYTDGAAEGEVSLRRARQAFRDIEFHPDILRPAIDVDTSCEILGGRSAMPFGIAPTGFTRLMQTEGEVAGAGAAGAAGIPFTLSTLGTTSIEDVKAANPHGRNWFQLYVMRQREISYGLVERAAAAGFDTLMFTVDTPVAGARLRDKRNGFSIPPQITAGTVLNAIPRPWWWFDFLTTPKLEFASLKSTGGTVGELLDNAMDPTISDEDLKVIRSMWPGKIVIKGVQTVEDSKRLIDLGVDGVLLSNHGGRQLDRAPVPFRLLPEVVREVGKDATIMVDTGIMNGADVVAAVALGAKFGLVGRAYLYGLMAGGREGVDRMIEILSDEVIRTMKLLGVSSLDELEPRHVTQLTRLTPVRPNVKAAADALAR$","L-lactate dehydrogenase","Cytoplasm","L-lactate dehydrogenase","L-lactate dehydrogenase ","L-lactate dehydrogenase (cytochrome)","","Minton N.P., Bullman H.M., Scawen M.D., Atkinson T., Gilbert H.J. Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 L-asparaginase gene. Gene 1986. 46(1):25-35. PMID: 3026924Jennings M.P., Beacham I.R. Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins. J. Bacteriol. 1990. 172(3):1491-1498. PMID: 2407723Tanaka S., Robinson E.A., Appella E., Miller M., Ammon H.L., Roberts J., Weber I.T., Wlodawer A. Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi. J. Biol. Chem. 1988. 263(18):8583-8591. PMID: 3379033","","","

InterPro
IPR000262
Domain

FMN-dependent alpha-hydroxy acid dehydrogenase
PF01070	$\"[43-402]T$	FMN_dh

InterPro
IPR006034
Family

Asparaginase/glutaminase
PS00144	$\"[238-246]?$	ASN_GLN_ASE_1

InterPro
IPR008259
Active_site

FMN-dependent alpha-hydroxy acid dehydrogenase, active site
PS00557	$\"[298-304]T$	FMN_HYDROXY_ACID_DH

InterPro
IPR012133
Family

Alpha-hydroxy acid dehydrogenase, FMN-dependent
PIRSF000138	$\"[31-406]T$	Alpha-hydroxy acid dehydrogenase, FMN-dependent

InterPro
IPR013785
Domain

Aldolase-type TIM barrel
G3DSA:3.20.20.70	$\"[29-403]T$	no description

noIPR
unintegrated

unintegrated
PTHR10578	$\"[53-413]T$	(S)-2-HYDROXY-ACID OXIDASE-RELATED
PTHR10578:SF9	$\"[53-413]T$	(S)-2-HYDROXY-ACID OXIDASE

","BeTs to 12 clades of COG1304COG name: L-lactate dehydrogenase (FMN-dependent) and related alpha-hydroxy acid dehydrogenasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1304 is aompkzy--drlbcefgh-n-jx-t-Number of proteins in this genome belonging to this COG is 2","***** IPB000262 (FMN-dependent alpha-hydroxy acid dehydrogenase) with a combined E-value of 2.9e-129. IPB000262A 43-91 IPB000262B 92-143 IPB000262C 156-203 IPB000262D 272-319 IPB000262E 323-376","","","-53% similar to PDB:1HUV CRYSTAL STRUCTURE OF A SOLUBLE MUTANT OF THE MEMBRANE-ASSOCIATED (S)-MANDELATE DEHYDROGENASE FROM PSEUDOMONAS PUTIDA AT 2.15A RESOLUTION (E_value = 7.8E_59);-53% similar to PDB:1P4C High Resolution Structure of Oxidized Active Mutant of (S)-Mandelate Dehydrogenase (E_value = 7.8E_59);-53% similar to PDB:1P5B High Resolution Structure of Reduced Active Mutant of (S)-Mandelate Dehydrogenase (E_value = 7.8E_59);-53% similar to PDB:2A7N Crystal Structure of the G81A mutant of the Active Chimera of (S)-Mandelate Dehydrogenase (E_value = 3.9E_58);-53% similar to PDB:2A7P Crystal Structure of the G81A mutant of the Active Chimera of (S)-Mandelate Dehydrogenase in complex with its substrate 3-indolelactate (E_value = 3.9E_58);","Residues 43 to 402 (E_value = 3.1e-126) place ANA_2773 in the FMN_dh family which is described as FMN-dependent dehydrogenase.","","dehydrogenase (Cereon)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2774","2993352","2991763","1590","5.50","-15.48","57237","GTGGACGCCCACCGGATTTCCAAGGAGGCCGGGTTGACTGAAGGCCACTGGTGGCAGCGCGGAAAGGACCTCTTCTTGACCATCTCACTGACTGAGTCACCCCTGGCCCCCAACTACGACCGCTCCGCCATGACCACCGGGATCGTCCACATCGGCGTGGGCGGCTTCCACCGCGCCCACGAGGCCGCCTACCTCGACCGGCTCATGCGCCGGCGCGCCGGATCCGGCCCCGGCGGCGGAGCAGCCGCCGCAGCGGGCGGATCCTGCCTGGAGTGGGGGATCTGCGGCGTCGGCCTATTGCCCGGGGACGCCCGGATGCGTGACGTGCTGGCGGCTCAGGACCACCTCTACACCCTGGTGCTCAAGCATCCCGGTGGGCTGCGCGATCCAGCGGTCATCGGCTCGATCCACGACTACCTCTTCGCCCCCGACGACCCCGAGGTCGTCCTGGCCCTCCTGAGCGCACCGACCACCCGGATCGTCTCACTGACGGTCACCGAGGGCGGCTACAACGTTGACGACGCCACCGGCATGTTCCGCACTGAGGCACCCGGAGCCGTCCACGACGCCGAGCACCCGGGCGAGCCCACGACCGCCTTCGGCTACATCGTTGAGGCGCTGAGGCGTCGTCGGGAGGCGGGGATCCCGGCGCTGACGGTCATGAGCTGCGACAACCTGCCCGGAAACGGGAAGGTGGCCCGCACGGCGGTGGTCTCCCAGGCCGCGATGAGCGACCCTGAGCTGGCGGACTGGATCGACGGGAACGTCGCCTTCCCCAGCTGCATGGTGGACCGCATCACCCCGCGCACCACGCGGGCTGACGTCGCCGAGCTGCAACGGGCACTCGGTGTGGAGGACGCCTGGCCGGTGGTCTGCGAGCCCTTCACCCAGTGGGTGATCGAGGACGACTTCCCAGCCGGGCGGCCCCCATGGGAGGAGGTCGGGGTGCAGATGGTCGACGACGTCGTCCCCTACGAGCTCATGAAACTGCGTCTGCTCAACGCCTCTCACCAGGGGCTGGCCCACTGGGGGCGGCTGCTGGGGATCGAGTACGCGCACGAGGCCGCGGCCGATGCAGATATCGCCACCTGGGTGAGGGCCTATCTTGAGCGGGAGGCGCGGGCCACCCTGCGCTCGGTGCCGGGGATCGACCTGGACGACTACATCAGCACGCTCTTCAAGCGCTTCACCAACGAGGCGATCGCAGACACGCTCTTCCGCCTGGCGCAGGACGCCTCCAGCCGGATGCCGAAGTTCGTCCTGGGCACGGTGCGCGACAACCTCACCGCTGGCGGGCCAATCCGCCTGGGAACGGCGATGGTGGCGGCCTGGGCGCTGGGCGATGAGGGCGTCGACGAGACCGGCAAGGCGATCGCCATCGACGACCCGCTGGCCGACGAGCTGCTGCTCCTGGCTGCCGCGCAGAGGTCCGGTCACGAGACGGCCTTCATCTCCCACGAGGGGGTCTTCGGGGACCTGGCGACCAACAAGCGCTTCCGACGCACCTTCGTCGAGGAGCTCGAGGCCCTGCGGCGCCAGGGGGCGCGGGAGCGTCTGCGAGCCCTGGCCGGCCGCACTCGAGCGGCCTAG","VDAHRISKEAGLTEGHWWQRGKDLFLTISLTESPLAPNYDRSAMTTGIVHIGVGGFHRAHEAAYLDRLMRRRAGSGPGGGAAAAAGGSCLEWGICGVGLLPGDARMRDVLAAQDHLYTLVLKHPGGLRDPAVIGSIHDYLFAPDDPEVVLALLSAPTTRIVSLTVTEGGYNVDDATGMFRTEAPGAVHDAEHPGEPTTAFGYIVEALRRRREAGIPALTVMSCDNLPGNGKVARTAVVSQAAMSDPELADWIDGNVAFPSCMVDRITPRTTRADVAELQRALGVEDAWPVVCEPFTQWVIEDDFPAGRPPWEEVGVQMVDDVVPYELMKLRLLNASHQGLAHWGRLLGIEYAHEAAADADIATWVRAYLEREARATLRSVPGIDLDDYISTLFKRFTNEAIADTLFRLAQDASSRMPKFVLGTVRDNLTAGGPIRLGTAMVAAWALGDEGVDETGKAIAIDDPLADELLLLAAAQRSGHETAFISHEGVFGDLATNKRFRRTFVEELEALRRQGARERLRALAGRTRAA$","Mannitol dehydrogenase","Cytoplasm","Mannitol-1-phosphate/altronate dehydrogenases","mannitol dehydrogenase-like protein","Mannitol dehydrogenase, C-terminal domain","","Fischer R., von Strandmann R.P., Hengstenberg W. Mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system of Enterococcus faecalis: molecular cloning and nucleotide sequences of the enzyme IIIMtl gene and the mannitol-1-phosphate dehydrogenase gene, expression in Escherichia coli, and comparison of the gene products with similar enzymes. J. Bacteriol. 1991. 173(12):3709-3715. PMID: 1904856Honeyman A.L., Curtiss I.I.I. R. Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system. Infect. Immun. 1992. 60(8):3369-3375. PMID: 1322373Schneider K.H., Giffhorn F., Kaplan S. Cloning, nucleotide sequence and characterization of the mannitol dehydrogenase gene from Rhodobacter sphaeroides. J. Gen. Microbiol. 1993. 139(10):2475-2484. PMID: 8254318","","","

InterPro
IPR000669
Domain

Mannitol dehydrogenase, core
PR00084	$\"[48-58]T$ $\"[256-269]T$ $\"[286-301]T$	MTLDHDRGNASE
PS00974	$\"[256-268]?$	MANNITOL_DHGENASE

InterPro
IPR013118
Domain

Mannitol dehydrogenase, C-terminal
PF08125	$\"[254-499]T$	Mannitol_dh_C

InterPro
IPR013131
Domain

Mannitol dehydrogenase rossman, N-terminal
PF01232	$\"[46-226]T$	Mannitol_dh

InterPro
IPR013328
Domain

Dehydrogenase, multihelical
G3DSA:1.10.1040.10	$\"[320-527]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[20-319]T$	no description

","BeTs to 5 clades of COG0246COG name: Mannitol-1-phosphate/altronate dehydrogenasesFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0246 is ------y-v--lb-efgh---j---wNumber of proteins in this genome belonging to this COG is 1","***** IPB000669 (Mannitol dehydrogenase) with a combined E-value of 3.6e-75. IPB000669A 49-60 IPB000669B 161-170 IPB000669C 217-237 IPB000669D 258-268 IPB000669E 286-301 IPB000669F 315-358 IPB000669G 388-416","","","-59% similar to PDB:1LJ8 Crystal structure of mannitol dehydrogenase in complex with NAD (E_value = 1.1E_105);-59% similar to PDB:1M2W Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and D-mannitol (E_value = 1.1E_105);","Residues 46 to 226 (E_value = 1.9e-60) place ANA_2774 in the Mannitol_dh family which is described as Mannitol dehydrogenase Rossmann domain.Residues 254 to 499 (E_value = 2.9e-89) place ANA_2774 in the Mannitol_dh_C family which is described as Mannitol dehydrogenase C-terminal domain.","","dehydrogenases (mdh)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2775","2994147","2993497","651","5.24","-7.09","23156","ATGGATGCGAAGTCCGCGATCCTGGCCCGCGCCCGCGACGCGATCTCGCGGTCCCAGACCCGACCGGTGGGGCCGATCCCGCGCAACTACATCCGCTCCGGGGAGAATCCCCCCGGCTCCAAGCCCGTCGTTGACGAGATGATCGAGAAGCTTGAGGACTACTCGGCCGAGGTCATCGTCGCCCCTAAGGACGCGGCGATCCTGGATGCCATCGACGAGCTGCTCGGCGAGGCGCGCTCCGTCGTCGTCCCCGCCGGACTGCCCGAGGACTACAAGAAGGCGGCAGCGCGCAACGGCCGCACCGTGGTGGAGGACTCCCGCGAGGAGGCCATCGCCACCCTCGACCTCAATGAGATCGACGCCGTTCTGACCTGCTCGCGGGTGGGCATCTCGATCTCGGGAACGATCGTCCTCGACGGCGAGCCGGACCAGGGCCGCCGGGCCATCTCGCTGGTGCCGGACAAGCACGTCGTGGTCCTGGAGCGCGAGACGATCATGCCGACGGTGCCGCAGGCCGTCGACGTCCTGGGAGAGCACCCCACGCGCCCGATGACGTGGATCGCCGGCGGCTCGGCCACCAGCGACATCGAGCTGGTGCGTGTCAACGGCGTGCACGGCCCGCGCAACCTGCGCGTCGTCATCGCCCACTGA","MDAKSAILARARDAISRSQTRPVGPIPRNYIRSGENPPGSKPVVDEMIEKLEDYSAEVIVAPKDAAILDAIDELLGEARSVVVPAGLPEDYKKAAARNGRTVVEDSREEAIATLDLNEIDAVLTCSRVGISISGTIVLDGEPDQGRRAISLVPDKHVVVLERETIMPTVPQAVDVLGEHPTRPMTWIAGGSATSDIELVRVNGVHGPRNLRVVIAH$","Uncharacterized conserved protein","Cytoplasm","Uncharacterized ACR, YkgG family COG1556 family","K00782 hypothetical protein","protein of unknown function DUF162","","","","","

InterPro
IPR003741
Family

Protein of unknown function DUF162
PF02589	$\"[118-215]T$	DUF162

","BeTs to 8 clades of COG1556COG name: Uncharacterized ACRFunctional Class: S [Function unknown]The phylogenetic pattern of COG1556 is ao-------d-lb-e--h-nu-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-57% similar to PDB:2G40 Crystal structure of hypothetical protein (6459694) from Deinococcus radiodurans at 1.70 A resolution (E_value = 1.1E_32);-49% similar to PDB:1Y8T Crystal Structure of RV0983 from Mycobacterium tuberculosis- Proteolytically active form (E_value = 1.1E_32);-49% similar to PDB:1TO0 X-ray structure of Northeast Structural Genomics target protein sr145 from Bacillus subtilis (E_value = 1.1E_32);-44% similar to PDB:2P4G Crystal structure of hypothetical protein (NP_939744.1) from Corynebacterium diphtheriae at 2.30 A resolution (E_value = 1.1E_32);-52% similar to PDB:1DF7 DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND METHOTREXATE (E_value = 1.1E_32);","Residues 118 to 215 (E_value = 2.3e-33) place ANA_2775 in the DUF162 family which is described as Uncharacterised ACR, YkgG family COG1556.","","ACR, YkgG family COG1556 family","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2777","2995880","2994147","1734","5.72","-13.34","62082","ATGACACAGGTATTTCTCGGCATGCCCCACACGGGCGGGTGGCGCACCGAGGTCGAGCAGCCCGAGGACACGCTGCGCTGGGGACCCACCTTCCCCGAGGGCGCGCACAAGACGCTGGCCAACACCCAGATGCGCCGCAACCTGGGCCACGCCACGCGCACCATCCGCTCCAAGCGCGCCGACCGCGTGTCCGAGATGCCCGACTGGGAGGACCTGCGCAACGCCGCGGAGGCCGTCAAGTTCGAGGTGGCCTCGCGCCTGCCCGAGCTGCTGGAGCAGTTCGAGGCCAACGTGACCGCCCGCGGCGGCATCGTCCACTGGGCACGTGACGCCGCCGAGGCCAACCGGATCATCACCGACATCATCGCCTCCAAGGGCGTCGACGACATCGTCAAGGTCAAGTCGATGGCCACCCAGGAGACGAACCTCAACGAGTACCTGGCCGACCGGGGCATCACCGCCCACGAGACGGACCTGGCCGAGATGATCGTCCAGCTGGCCGACGACATGCCCTCGCACATCGTGGTGCCCGCGATCCACCGCAACCGCTCCGAGGTGCGCGGCATCTTCCTGGACCGTATGGAGGACGCCCCCGCGGACCTCTCCGACGACCCCAAGGAGCTCACGGCCGCGGCCCGCTCGCACCTGCGCAACAAGTTCCTGCACGCCTCGGTGGCCGTCTCCGGAACGAACATGGGTGTGGCCGAGACCGGCACGGTCTCGATCTACGAGTCCGAGGGCAACGGGCGCATGTGCCTGACCCTGCCGGACACGCTCATCACCCTCATGGGCATCGAGAAGCTGGTGCCCCGCTTCCAGGACGTGGAGATCTTCTCCCAGCTCCTGCCGCGCTCGGCCACCGGTGAGCGCATGAACCCCTACACCTCCATGTGGACCGGTGTCACCGAGGGCGACGGCCCCAAGGAGTTCCACCTAGTGCTCATGGACAACGGGCGCACCAAGACCCTGGCCGACCCGGTGGGCCGCCAGGCCCTGGCCTGCATCCGCTGCGGGTCGTGCATGAACATCTGCCCCGTCTACCAGCACACCGGTGGGCACGCCTACGGCTCGGTCTACCCCGGCCCGATCGGCTCGATCATCACACCCCAGCTCACTCAGGGGCTGGCCGACGACGACCCGGTCCACACCCTGCCCTTCGCCTCCTCCCTGTGCGGGGCCTGCGGCGAGGTGTGCCCGGTCAAGATCGACATCCCCACGATCCTCATCCACCTGCGGGCCCGCTCCGTGGACGTCAAGCGCCGCGCGGTGCCGGACGTGTGGGACGTGGCCATGAACGTCTCGGCCCCGGTGATGTCGAAGAGCTCGCTGTGGGCCGCCGCCTCGCAGACGGTCAAGGCCTCGGCGCTGCTGGGCGGCAAGGAGGGCAAGATCGGTGCCCTGCCCTTCCCGGCCTCCCTGTGGACCGGGGCGCGCGACCTGCCGGTGGCCCCCTCGGAGACCTTCCGCCAGTGGTGGAAGCGCACTCACCCCGAGGGTGAGACTCCGCTGAGCCAGGTCGCCGGTACCCAGAGCGGCCGCGGTCACGCGGACGGCTTCCCGGCCGACCCGCCCCCGCCTCCTGGCAAGCCGGTGTCCGGCAGCGCGAGCGCCGACGGCGAGCCCACCCCGGCCGCGCTGGACGCACGCTCGGCCATCAACAACCCTGAGCCGATCGCCCCGGAGGCATCCGCCTCCCAGGCCCCGGCCGGCTCGACCAGCGAGGAGGAGCTGTGA","MTQVFLGMPHTGGWRTEVEQPEDTLRWGPTFPEGAHKTLANTQMRRNLGHATRTIRSKRADRVSEMPDWEDLRNAAEAVKFEVASRLPELLEQFEANVTARGGIVHWARDAAEANRIITDIIASKGVDDIVKVKSMATQETNLNEYLADRGITAHETDLAEMIVQLADDMPSHIVVPAIHRNRSEVRGIFLDRMEDAPADLSDDPKELTAAARSHLRNKFLHASVAVSGTNMGVAETGTVSIYESEGNGRMCLTLPDTLITLMGIEKLVPRFQDVEIFSQLLPRSATGERMNPYTSMWTGVTEGDGPKEFHLVLMDNGRTKTLADPVGRQALACIRCGSCMNICPVYQHTGGHAYGSVYPGPIGSIITPQLTQGLADDDPVHTLPFASSLCGACGEVCPVKIDIPTILIHLRARSVDVKRRAVPDVWDVAMNVSAPVMSKSSLWAAASQTVKASALLGGKEGKIGALPFPASLWTGARDLPVAPSETFRQWWKRTHPEGETPLSQVAGTQSGRGHADGFPADPPPPPGKPVSGSASADGEPTPAALDARSAINNPEPIAPEASASQAPAGSTSEEEL$","Iron-sulfur cluster binding protein","Periplasm, Cytoplasm","iron-sulfur protein","iron-sulfur cluster binding protein","iron-sulfur cluster binding protein","","Lancaster C.R., Kroger A., Auer M., Michel H. Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution. Nature 1999. 402(6760):377-385. PMID: 10586875Dobritzsch D., Ricagno S., Schneider G., Schnackerz K.D., Lindqvist Y. Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer. J. Biol. Chem. 2002. 277(15):13155-13166. PMID: 11796730","","","

InterPro
IPR001450
Domain

4Fe-4S ferredoxin, iron-sulfur binding
PF00037	$\"[327-350]T$	Fer4
PS00198	$\"[334-345]T$	4FE4S_FERREDOXIN

InterPro
IPR003741
Family

Protein of unknown function DUF162
PF02589	$\"[222-315]T$	DUF162

InterPro
IPR004452
Family

Iron-sulfur cluster binding protein
TIGR00273	$\"[39-481]T$	TIGR00273: iron-sulfur cluster binding prot

InterPro
IPR012285
Domain

Fumarate reductase, C-terminal
G3DSA:1.10.1060.10	$\"[330-416]T$	no description

","BeTs to 11 clades of COG1139COG name: Uncharacterized conserved protein containing a ferredoxin-like domainFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1139 is aomp-z---d-lb-e--h-nu-----Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 222 to 315 (E_value = 9.2e-11) place ANA_2777 in the DUF162 family which is described as Uncharacterised ACR, YkgG family COG1556.Residues 327 to 350 (E_value = 0.0062) place ANA_2777 in the Fer4 family which is described as 4Fe-4S binding domain.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2778","2996707","2995877","831","6.51","-3.98","29714","GTGCGAATCGCCCTTTTCGCCACCTGTCTTGCGGACACCATGTTCCCGCAGGCAGCGCAGGCAACCGTCACCATCCTGGAGCGCCTCGGCCACCAGGTCTGCTTCCCCGAGGGACAGGTCTGCTGCGGCCAGATGCACGCCAACACCGGCTACTTCAAGCAGGCCGCCAAGATCACCCGCAACCACGTGGAGACCTTCTCCCCCGTGCTCGACGGCGAGTGGGACGCCATCGTCATCCCCTCGGGCTCGTGCACCGGCGCGGCCCGTCACGAGCAGGGCCTCGTGGCCGAGCACGTGGGTGACACGGCCCTGGCCAAGCGGGTCGAGCAGATCGCCACGCACACCTACGACCTCTCCGAGCTGCTCATCGATGTCCTGGGCACCGAGGACGTGGGCGCCTACTTCCCGCACACGGTCACCTACCACCCCACCTGCCACTCGCTGCGCGTCGCCAAGGTCGCCGACCGCCCCTACCGCCTCCTCAAGGCCGTCGAGGCCCTCACCCTCATCGACCTGCCCGACGCCGAGGTCTGCTGCGGGTTCGGTGGCACCTTCTCCATGAAGAACTCCGAGACCTCCACCGCGATGCTCGCCGACAAGATGAGCAACGTGATGTCCACGCGCGCCGAGGTCCTGTGCGCCGGCGACTACTCCTGCCTCATGCACATCGGTGGCGGCCTGTCCCGCGTCAACTCCGGGGTGCGCATCATGCACCTGGCCGAGATCCTGGCCTCCACCAAGGACGCGCCCTTCGAGGGCAACATCTCCTTCGCCCCCAAGCACGTCCAGCACACCGGTAACTCCCAGCACACACAGGCGGTGGCACGATGA","VRIALFATCLADTMFPQAAQATVTILERLGHQVCFPEGQVCCGQMHANTGYFKQAAKITRNHVETFSPVLDGEWDAIVIPSGSCTGAARHEQGLVAEHVGDTALAKRVEQIATHTYDLSELLIDVLGTEDVGAYFPHTVTYHPTCHSLRVAKVADRPYRLLKAVEALTLIDLPDAEVCCGFGGTFSMKNSETSTAMLADKMSNVMSTRAEVLCAGDYSCLMHIGGGLSRVNSGVRIMHLAEILASTKDAPFEGNISFAPKHVQHTGNSQHTQAVAR$","Fe-S oxidoreductase","Cytoplasm","glycolate oxidase homolog yvfV","hypothetical protein","protein of unknown function DUF224, cysteine-rich region domain protein","","Pellicer M.T., Badia J., Aguilar J., Baldoma L. glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein. J. Bacteriol. 1996. 178(7):2051-2059. PMID: 8606183","","","

InterPro
IPR004017
Domain

Cysteine-rich region, CCG
PF02754	$\"[26-89]T$ $\"[162-224]T$	CCG

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide

","BeTs to 17 clades of COG0247COG name: Fe-S oxidoreductasesFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0247 is aomp-z-q-drlbcefgh-nuj----Number of proteins in this genome belonging to this COG is 2","***** IPB004017 (Protein of unknown function DUF224) with a combined E-value of 2.3e-08. IPB004017A 32-49 IPB004017C 176-186","","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 89 (E_value = 7.4e-10) place ANA_2778 in the CCG family which is described as Cysteine-rich domain.Residues 162 to 224 (E_value = 1.1e-12) place ANA_2778 in the CCG family which is described as Cysteine-rich domain.","","oxidase homolog yvfV","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2779","2998603","2997782","822","7.01","0.05","28140","ATGACTCATGCTCCCCTGGCCGCTGGACGCCGGCACACCGTCCGGTGCCTCACCGACGGGAAGGTGGTCGCCGTCGGAGCGGATGACGCCGGAGAGTGCCGGGTCTCGCAGTGGCGAGGCGTCGTCTCCGTGGCGGCGGGCAGCGTCCACGTGGCCGCCAACACCGGCCGGTCCCACACGCTGGGCCTGCGCAGTGACGGTACGGTGCTGGCCTGCGGCTGGAACGCACAGGGGCAGTGCGACGTCCGGGACTGGCGGGACGTCGTCGCCATCGCCGCAGGATGGAGATTCAGCGCAGGACTGCGCATCGACGGGACGCTGATGACCACCGGCCGCGACGCCGAGGGGCAACGGCAGGTGGGCCACTGGCGCGAGCTCACGGGTATCAGCTGCGGCGACTGGCACACGGTGGCCGTTCGCTCTGACGGGAGCGTCTGCGCGGCCGGTAACAACACCGCCGGCCAGTGCGAGGTGCAGGACTGGCACCGAGTACACGCGGTCTCGGCAGGCTACCTCCATACCCTCGGCCTGCTGGGCAACGGCACTGTTCGCGCGGCCGGGCACCCGGAGTTTTGGTCGGGGGTCGAGAACTGGACCGGTATCACCGCTGTGGCGGCGGGCAGCTGCCACAGCGTCGGGCTCAGAGCCGATGGGACCGTCGTCGCAACGGGGATGTCGGAGGCCGGTCAGTGCGAGGTGAACCGGTGGCACGACATCGTGGCCATTGCGGCGGGCGCGGCCCACACCGTGGGCCTGCGCGCCGACGGCGGCGTCGTCGCCACCGGCTCCAACAGTCACGGCCAGCTCGAAGTCGGGGCCTGA","MTHAPLAAGRRHTVRCLTDGKVVAVGADDAGECRVSQWRGVVSVAAGSVHVAANTGRSHTLGLRSDGTVLACGWNAQGQCDVRDWRDVVAIAAGWRFSAGLRIDGTLMTTGRDAEGQRQVGHWRELTGISCGDWHTVAVRSDGSVCAAGNNTAGQCEVQDWHRVHAVSAGYLHTLGLLGNGTVRAAGHPEFWSGVENWTGITAVAAGSCHSVGLRADGTVVATGMSEAGQCEVNRWHDIVAIAAGAAHTVGLRADGGVVATGSNSHGQLEVGA$","Beta-lactamase inhibitory protein II","Cytoplasm, Extracellular","Beta-lactamase inhibitory protein II","regulator of chromosome condensation; RCC1","Alpha-tubulin suppressor and related RCC1 domain-containing protein-like","","Dasso M. RCC1 in the cell cycle: the regulator of chromosome condensation takes on new roles. Trends Biochem. Sci. 1993. 18(3):96-101. PMID: 8480369Roepman R., van Duijnhoven G., Rosenberg T., Pinckers A.J., Bleeker-Wagemakers L.M., Bergen A.A., Post J., Beck A., Reinhardt R., Ropers H.H., Cremers F.P., Berger W. Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1. Hum. Mol. Genet. 1996. 5(7):1035-1041. PMID: 8817343","","","

InterPro
IPR000408
Repeat

Regulator of chromosome condensation, RCC1
PS00626	$\"[129-139]?$ $\"[167-177]?$ $\"[204-214]?$	RCC1_2

noIPR
unintegrated

unintegrated
G3DSA:2.130.10.30	$\"[6-232]T$	no description
PTHR22870	$\"[6-82]T$ $\"[107-176]T$ $\"[198-272]T$	REGULATOR OF CHROMOSOME CONDENSATION

","No hits to the COGs database.","***** IPB000408 (Regulator of chromosome condensation, RCC1) with a combined E-value of 8.9e-10. IPB000408A 67-81 IPB000408B 129-159","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","inhibitory protein II","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2780","3000575","2998866","1710","9.10","9.01","58358","ATGACGCCAGCCGTCCTGTCAGCACTGCCGATGCATCCGGCACCACTCGCCCCAGCATTGGCGGGACTGCCCACCGCCTTCACGCCGTCGACCACTGCCGTGGGCGGCAACGTCTACCTCACCGCCGCGGTGGGTCTGCTGCCGCTGGTGGTGTTCTTCGTCCTCATGGGCGTGTTCAAGGTGGCCACCCACTGGTGCGCCATCATCTCCCTGGTGATCGCCGCCGTCACCGCGGTCACCCTGTTCCACATGCCGGTGGGCATGACGGTCATGAGCGCCACCCAGGGCATGGCGCTGGGATTCGTCCCGATCATCTACATCATCATCGCGGCCGTGTGGCTCTACAACCTCACTGACGTCTCGGGTCGCTCCAAGGACCTCAAGGCCGTGTTCAACGTGATCGGCAAGGGCGACATGCGCGCCCAGGCCCTTATCGTGGCCTTCTCCTTCTGCGGACTGCTCGAGGGGCTGGCCGGTTTCGGGGCCCCGGTGGCCATCGCCGCCGCCATGGTGGCGACCCTGGGCCTGCCCAAGCTCAAGGCGGCCGTCGTCGTCATGGTCGGTAACGCCATCAACGTGGGCTTCGGCGCCATGGCCATTCCCACCACGACCGCCGGCAAGCTCGGCGGCCAGGAGCCGGTGACGGTTGCGACCGCCATGGGGCACCTGACCTGGGTGTTCTGCGCCTTCATCCCGCTCCTGCTGCTGTTCATCCTCGACGGCGCGCGCGGCGTCAAGCAGCTGTGGCCACTGGCGATCGTGGCGGGGCTGGCCACCGGAGTGGGTCACTTCTTCACCCCCTCGATCTCCTACGAGCTCACCGCCGTGCTGGCCTCCCTGCTGGGCCTGGCCGCCTCCTACGTCTTCCTACTGGTGTGGACCCCCACAACCCCTGAGGAGTACCGCTCCCAGGTAGCTGCCGAGGACGCCCCCGACCGCGAGCGCGTCATCCTGGCCCTGCTGCCCTACGTCCTGGTGGTGGTCATCATCGCCACGACCAAGCTGTGGACCCTGGGCATCAACCTCGACAAGGCATTCAAGGCCACCGACCTGAAGATCAAGTGGCCCGGCGTCTACGGCCAGCTCCTCAACGCCAAGGGCGAGGCCTCCACCGGCGCCATCTACAACCTTCAGACCCTGTCCAACCCGGGCACCTGGATCTTCCTGACCGCCATCATCGTCACCTTCATCTACGCGGCGCGCTCGGTGCCCGGCAAGTTCGAGATGAGCGTGGGCAAGGGCTTCGCCACACTGGCCAAGACCTGCTACACGCTGCGCATGGCGATCCTGACGATCGCCGCCGTCATGGCCCTGGCCTACGTCATGAACTTCTCCGGCCAGACCTCCGCCATCGGTGCGGCCCTGGCCGCCACGGGCGCCGCCTACGCCTTCCTCTCCCCGGCCCTGGGCTGGGTGGGAACCGCCGTGGCCGGCTCGGCGACGAGCGCGGGCGCCCTGTTCGCCAACCTGCAGGCCACCGCCGCCCAGGGTGCCGGGCTCGACCCGAAGATCCTGCTGGCCGCCAACACCATCGGTGGCGGCCTGGGCAAGATCGTCTCCCCGCAGAACCTGGCCATCGCCTCGACCGCGGTGGACGCCCCCGGTACGGACGCCGAGATCCTCAAGAAGGCGGCCCCCTACTCCATCGGGCTGCTGCTGGTGCTGGGCGCTCTCGTGTTCCTGGCCTCCCAGGTGGGGCTGGGGGTCTGA","MTPAVLSALPMHPAPLAPALAGLPTAFTPSTTAVGGNVYLTAAVGLLPLVVFFVLMGVFKVATHWCAIISLVIAAVTAVTLFHMPVGMTVMSATQGMALGFVPIIYIIIAAVWLYNLTDVSGRSKDLKAVFNVIGKGDMRAQALIVAFSFCGLLEGLAGFGAPVAIAAAMVATLGLPKLKAAVVVMVGNAINVGFGAMAIPTTTAGKLGGQEPVTVATAMGHLTWVFCAFIPLLLLFILDGARGVKQLWPLAIVAGLATGVGHFFTPSISYELTAVLASLLGLAASYVFLLVWTPTTPEEYRSQVAAEDAPDRERVILALLPYVLVVVIIATTKLWTLGINLDKAFKATDLKIKWPGVYGQLLNAKGEASTGAIYNLQTLSNPGTWIFLTAIIVTFIYAARSVPGKFEMSVGKGFATLAKTCYTLRMAILTIAAVMALAYVMNFSGQTSAIGAALAATGAAYAFLSPALGWVGTAVAGSATSAGALFANLQATAAQGAGLDPKILLAANTIGGGLGKIVSPQNLAIASTAVDAPGTDAEILKKAAPYSIGLLLVLGALVFLASQVGLGV$","L-lactate permease","Membrane, Cytoplasm","L-lactate permease","L-lactate permease","L-lactate permease","","","","","

InterPro
IPR003804
Family

L-lactate permease
PF02652	$\"[40-562]T$	Lactate_perm

noIPR
unintegrated

unintegrated
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[14-34]?$ $\"[39-59]?$ $\"[65-87]?$ $\"[97-117]?$ $\"[145-167]?$ $\"[182-200]?$ $\"[219-239]?$ $\"[249-267]?$ $\"[273-293]?$ $\"[320-340]?$ $\"[385-403]?$ $\"[424-444]?$ $\"[450-470]?$ $\"[547-567]?$	transmembrane_regions

","BeTs to 12 clades of COG1620COG name: L-lactate permeaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG1620 is ao-------d--b-efgh-nu---t-Number of proteins in this genome belonging to this COG is 1","***** IPB003804 (L-lactate permease) with a combined E-value of 3.5e-45. IPB003804A 145-185 IPB003804B 186-202 IPB003804C 455-491","","","No significant hits to the PDB database (E-value < E-10).","Residues 40 to 562 (E_value = 1.4e-84) place ANA_2780 in the Lactate_perm family which is described as L-lactate permease.","","permease (lctP)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2781","3003071","3000999","2073","5.07","-22.66","71024","ATGACAGCCCGCCCACCCGCTGCCCACGTGTCCCCGCCCACCTCGGCCCCGTCGGCCTCGACGCCGGCGCTGCCCGTCGATGACTCCGACGAGCTCTCCAACACCGCCACCCCCTCAGGTGCCCGCACGGGCGAGCGGATCCTCGAGCGGATCGAGTGGGCCGACGTCGTGCGCATCGCGGTGGTGGGCCTGGCGGCACTGGGTGCCTGGATCGCGGGGGCGGCCGGCACGCCCGGCTGGGCGGTGGGCGCCGTTGGGGCGGTGGTGCTGGCGGTGGGCTGCTGGCCGCTCCTGGTCGAGGCAGCCGAAGACCTGCGCGAGCGCCGCATGAGCATGGAGCTGTCGATGCTCCTGGCCATCGTGGCGGCCGCCATCATCGGCGAGTGGGTGACCGCCCTGGCCGTGACCGTCTTCGCACTGTGCGCCGAGGTCCTCGAGGAGCTGTCCATGGACCGGGGGCGCGACGCCCTGACCGATCTCATGTCCTTCCTGCCGCAGACCGCACGGGTGGTGGGGGCCCCGGAGGCCGCTGAGTCCGCCGAGTCGGCAGAGGCCGCCGAGTCCTCGCAGTCCTCCGGGGTCACTGAGGTCCCCCTGGACGAGGTCCGCCCGGGGCAGGTCATCGCCCTGAGCCCCGGGGGTCGGGTGCCGGTCGACGGCGTCGTGCGCACCGGTAGGGCCGACGTCGATCAGTCCCGGATCACCGGGGAGGCGCTGCCCGTGCAGGTCGGGCCGGGTGACCGGGTGCCGGCCGGCTCCATCACCCGCGGCGCGCTGGAGCTCGAGGTGGAGCGGGTCGGCGAGGAGTCCTCCTACGGGCGGATCGTGGCCGCGGTGCGCCACGCCCAGTCCTCGCGCGCGCCGGTCCAGCGCCTGGCCGACCGGCTGGCGGCCCGCATCGTCTACCTGGCCCTGGCGGCCGCCCTGGTCACCTTCCTGGTCACCCGGGACGTGCGCGCCACGATCTCGGTCATCATCGTGGCCGGGGCCTGCGGGGTGGCCGCGGGCACTCCCCTGGCGGTTTTGGCGGCGATCGCCCGCGCCGCCCGTTGCGGGGCCTTCGTCAAGGACGGCACCCACCTGGAGCAGCTCTCCGCGGTGGACACGGTGGTGATGGACAAGACCGGTACCCTCACCGTCGGCGAGCCCCGGGTCGTGAGCGTCCGCCCCACCGAGGCCGCCGCCGGGGAGGACGAGGTGCTGGCCCTGGCGGCCGCGGCGGAGTGGAACTCCGAGCACCCCATCGGCCGGGCCATCTACAACGAGGCCGCCGTACGCGACCTGACGGTGCCGGTGCCCGGCGACGTCACCTACTCCCCCGGAGCCGGCGTGAGCACCCACATCGAAGGGCGCCGCATCACCGTGGGGCGCTGCCGGGGGCAAGGGCACCAACCGGAGCGGGACACCCCCGGCTGCGAGGATGAGGCCGCCCTGAGTGCCGAGTCCGACCCGGAGGCGCCGTCGGCCACCTCGGTGGTGGAGGTGCGGGCCGACGGACAGCTCCTGGGCACCATCGCCCTGGCCGACCGGCTGCGTCAGGGAGCGGCCACCGCTGTGCGCGACCTGGGTGACATGGGGCTGGAGGTCCTCATGCTCACCGGCGACTCGGCCGCCTCCGCGCACCACGTGGCCGGTCTGCTCGGCCTGACCGAGGAGCAGGTGCGCGCCGACCTGCTGCCCACCGACAAGGAGGAGGTCATCGAGTCGCTGCGCCGGGCGGGCAAGCGGGTGGCCATGGTGGGCGACGGCGTCAACGACGCGCCCGCCCTGGGCGCCGCCGACGTCGGCATCGCCATGGGCACCGGCACGGACGTGGCCCGCGAGGCCGGCGACGTGGTGCTCGTGGGCTCCGCCCCGGCCGACCTGGTCGAGACCGTGCGGGTGGCCCGCCGGGCCAGGCGCATCATCATGGTGAACTTCGTGGGCACAGTGGTGGTCGACGTCGTCGGCATGGTCGCTGCCGGACTGGGACTGCTGGGACCTGTGGCCGCGGCCCTCGTGCACGTCGTCTCCGAATCGGCCTTCATCCTCAACTCGGCCCGACTGGTGCCCCGGCGCCGCCACAGGCGCTGA","MTARPPAAHVSPPTSAPSASTPALPVDDSDELSNTATPSGARTGERILERIEWADVVRIAVVGLAALGAWIAGAAGTPGWAVGAVGAVVLAVGCWPLLVEAAEDLRERRMSMELSMLLAIVAAAIIGEWVTALAVTVFALCAEVLEELSMDRGRDALTDLMSFLPQTARVVGAPEAAESAESAEAAESSQSSGVTEVPLDEVRPGQVIALSPGGRVPVDGVVRTGRADVDQSRITGEALPVQVGPGDRVPAGSITRGALELEVERVGEESSYGRIVAAVRHAQSSRAPVQRLADRLAARIVYLALAAALVTFLVTRDVRATISVIIVAGACGVAAGTPLAVLAAIARAARCGAFVKDGTHLEQLSAVDTVVMDKTGTLTVGEPRVVSVRPTEAAAGEDEVLALAAAAEWNSEHPIGRAIYNEAAVRDLTVPVPGDVTYSPGAGVSTHIEGRRITVGRCRGQGHQPERDTPGCEDEAALSAESDPEAPSATSVVEVRADGQLLGTIALADRLRQGAATAVRDLGDMGLEVLMLTGDSAASAHHVAGLLGLTEEQVRADLLPTDKEEVIESLRRAGKRVAMVGDGVNDAPALGAADVGIAMGTGTDVAREAGDVVLVGSAPADLVETVRVARRARRIIMVNFVGTVVVDVVGMVAAGLGLLGPVAAALVHVVSESAFILNSARLVPRRRHRR$","Heavy metal translocating P-type ATPase","Membrane, Cytoplasm","cation transporting P-type ATPase","heavy metal translocating P-type ATPase","heavy metal translocating P-type ATPase","","Smith D.L., Tao T., Maguire M.E. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 1993. 268(30):22469-22479. PMID: 8226755Fagan M.J., Saier Jr M.H. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 1994. 38(1):57-99. PMID: 8151716","","","

InterPro
IPR000150
Family

Cof protein
PS01229	$\"[580-602]?$	COF_2

InterPro
IPR000695
Family

H+ transporting ATPase, proton pump
PR00120	$\"[580-596]T$ $\"[611-636]T$	HATPASE

InterPro
IPR001757
Family

ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
PR00119	$\"[230-244]T$ $\"[371-385]T$ $\"[503-514]T$ $\"[525-535]T$ $\"[580-599]T$ $\"[603-615]T$	CATATPASE
PTHR11939	$\"[80-175]T$ $\"[194-687]T$	CATION-TRANSPORTING ATPASE
TIGR01494	$\"[500-668]T$	ATPase_P-type: ATPase, P-type (transporting
PS00154	$\"[373-379]?$	ATPASE_E1_E2

InterPro
IPR005834
Domain

Haloacid dehalogenase-like hydrolase
PF00702	$\"[367-603]T$	Hydrolase

InterPro
IPR006416
Family

Heavy metal translocating P-type ATPase
TIGR01525	$\"[112-682]T$	ATPase-IB_hvy: heavy metal translocating P-

InterPro
IPR008250
Domain

E1-E2 ATPase-associated region
PF00122	$\"[134-314]T$ $\"[337-363]T$	E1-E2_ATPase

noIPR
unintegrated

unintegrated
G3DSA:2.70.150.10	$\"[91-248]T$	no description
G3DSA:3.40.50.1000	$\"[498-624]T$	no description
PTHR11939:SF31	$\"[80-175]T$ $\"[194-687]T$	HEAVY METAL CATION TRANSPORT ATPASE (CADMIUM/ZINC TRANSPORTING ATPASE)
tmhmm	$\"[56-74]?$ $\"[80-99]?$ $\"[120-142]?$ $\"[322-342]?$ $\"[635-653]?$ $\"[659-679]?$	transmembrane_regions

","BeTs to 21 clades of COG2217COG name: Cation transport ATPasesFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG2217 is aompkzyqvdrlbcefgh-nuj-itwNumber of proteins in this genome belonging to this COG is 4","***** IPB008250 (E1-E2 ATPase-associated region) with a combined E-value of 2.3e-33. IPB008250A 371-381 IPB008250B 509-549 IPB008250C 577-600***** IPB006068 (Cation transporting ATPase, C-terminal) with a combined E-value of 5.3e-33. IPB006068B 197-237 IPB006068E 350-376 IPB006068H 509-550 IPB006068I 555-587 IPB006068J 597-648***** IPB001757 (ATPase, E1-E2 type) with a combined E-value of 5.2e-20. IPB001757A 371-381 IPB001757B 577-599***** IPB000695 (H+-transporting ATPase (proton pump) signature) with a combined E-value of 9.1e-18. IPB000695B 552-568 IPB000695C 580-596 IPB000695D 611-636***** IPB001756 (Copper-transporting ATPase signature) with a combined E-value of 1.9e-07. IPB001756F 152-170 IPB001756H 354-369 IPB001756I 557-574","","","-53% similar to PDB:2B8E CopA ATP Binding Domain (E_value = 7.2E_31);-47% similar to PDB:1IWO Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+ (E_value = 4.7E_14);-47% similar to PDB:1KJU Ca2+-ATPase in the E2 State (E_value = 4.7E_14);-47% similar to PDB:1SU4 Crystal structure of calcium ATPase with two bound calcium ions (E_value = 4.7E_14);-47% similar to PDB:1T5S Structure of the (SR)Ca2+-ATPase Ca2-E1-AMPPCP form (E_value = 4.7E_14);","Residues 134 to 363 (E_value = 4.5e-43) place ANA_2781 in the E1-E2_ATPase family which is described as E1-E2 ATPase.Residues 367 to 603 (E_value = 7.8e-34) place ANA_2781 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase.","","transporting P-type ATPase (ATP7A)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2782","3004836","3003301","1536","4.81","-25.41","55929","TTGAGCCCCAACAGCACTGAGAAGAAGTACGTCCTGGCCATCGACCAGGGTACGACCTCCTCACGCGCCATCCTGTTCAACCACGACGGCGAGATCGTCGCCGTCGACCAGAAGGAGCACGAGCAGATCTTCCCGCGCGCCGGCTGGGTCGAGCACGACGCGAACGAGATCTGGGACAACATCCGCTTCGTCGTCAGCGGGGTGCTGGCCAAGGCGCAGATCAACCGCCACGAGATCGCCTCGGTGGGCATCACCAACCAGCGCGAGAGCGCCGTCGTGTGGGACAAGAACACCGGCGAGCCCGTCTACAACGTCATCGTCTGGCAGGACACCCGCACCCAGAAGATCTGCGACCGTCTGGCCGGCGAGGACGGCCCGGACAAGTACAAGGACCGCGTGGGCCTGGGGCTGGCGACCTACTTCGCCGGACCCAAGGTGGCCTGGATCCTGGAGAACGTCGAGGGCGCCCGCGAGCGCGCCGAGGCCGGTGACCTCCTCATGGGCACCATGGACACCTGGACGCTGTGGAACCTCACCGGCGGGGTCAACGGTGGTGTGCACGCCACCGACGTCACCAACGCCTCGCGCACGATGCTCATGAATATCGACACCCTGGACTGGAATCCGGAGATCTGCGCGGACATGGGCATCCCCGTCTCCATGCTCCCCGAGATCCGCCCCTCCTCGGGCGTCTTCGGCTACGGCCGCAAGAACGGCCTGCTGGTGGACACCCCCATCAGCGGCATCCTGGGCGACCAGCAGGCGGCCACCTTCGGGCAGGCCTGTTTCGAGAAGGGCCAGGCCAAGAACACCTACGGCACCGGCTGCTTCATGCTCATGAACACGGGCACCACCCCGGTGCGCAGTGAGAACGGGCTGCTGACCACCGTGTGCTACCAGATCGGGGACGAGCCTGCCGTCTACGCCCTGGAGGGCTCGATCGCCGTGGCCGGCTCGCTGGTGCAGTGGCTGCGCGACAACCTGGGCATCATCGCCGACTCCAAGGACATCGAGGCCCTGGCCTCCAGCGTCGAGGACAACGGCGGGGCCTACTTCGTACCGGCCTTCTCCGGACTGTTCGCCCCGCACTGGCGCCCTGACGCCCGCGGCGCCCTGGTGGGTCTGACCCGCTACGTCAACAAGGCGCACATCGCCCGGGCCGTGGAGGAGTCCACCGCTTACCAGACCCGCGAGGTCCTCGAGGCCATGAACGCCGACTCCGGGCAGGCCCTCACCGAGCTCAAGGTCGACGGCGGCATGACCCGCGACGAGCTGCTCATGCAGTTCCAGGCCGACCAGGTGGGCGTGCCCGTGGTGCGCCCGAAGGTCGCCGAGACCACGGCACTGGGTGCCGCCTACGCCTCCGGTATCGCGGTGGGCTTCTGGTCGGGCACCCAGGACGTCATCGACAACTGGGCCGAGGACAAGCGCTGGGAGCCGACCATGGAGGAGGCCGAGCGCGAGCGGCTCTTCCGCAACTGGAACAAGGCCGTCCAGCGCACCCTGGACTGGGTCGACGAGGACGTCGTCGAGTAG","LSPNSTEKKYVLAIDQGTTSSRAILFNHDGEIVAVDQKEHEQIFPRAGWVEHDANEIWDNIRFVVSGVLAKAQINRHEIASVGITNQRESAVVWDKNTGEPVYNVIVWQDTRTQKICDRLAGEDGPDKYKDRVGLGLATYFAGPKVAWILENVEGARERAEAGDLLMGTMDTWTLWNLTGGVNGGVHATDVTNASRTMLMNIDTLDWNPEICADMGIPVSMLPEIRPSSGVFGYGRKNGLLVDTPISGILGDQQAATFGQACFEKGQAKNTYGTGCFMLMNTGTTPVRSENGLLTTVCYQIGDEPAVYALEGSIAVAGSLVQWLRDNLGIIADSKDIEALASSVEDNGGAYFVPAFSGLFAPHWRPDARGALVGLTRYVNKAHIARAVEESTAYQTREVLEAMNADSGQALTELKVDGGMTRDELLMQFQADQVGVPVVRPKVAETTALGAAYASGIAVGFWSGTQDVIDNWAEDKRWEPTMEEAERERLFRNWNKAVQRTLDWVDEDVVE$","Glycerol kinase","Cytoplasm","glycerol kinase","glycerol kinase ","glycerol kinase","","Reizer A., Deutscher J., Saier Jr M.H., Reizer J. Analysis of the gluconate (gnt) operon of Bacillus subtilis. Mol. Microbiol. 1991. 5(5):1081-1089. PMID: 1659648","","","

InterPro
IPR000577
Family

Carbohydrate kinase, FGGY
PTHR10196	$\"[58-511]T$	XYLULOSE KINASE
PF00370	$\"[10-259]T$	FGGY_N
PF02782	$\"[262-488]T$	FGGY_C

InterPro
IPR005999
Family

Glycerol kinase
PTHR10196:SF9	$\"[58-511]T$	GLYCEROL KINASE
TIGR01311	$\"[9-504]T$	glycerol_kin: glycerol kinase

","BeTs to 17 clades of COG0554COG name: Glycerol kinaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0554 is ao-pkzyqvdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB000577 (Carbohydrate kinase, FGGY) with a combined E-value of 3.8e-142. IPB000577A 10-27 IPB000577B 42-58 IPB000577C 83-95 IPB000577D 133-152 IPB000577E 167-179 IPB000577F 187-225 IPB000577G 266-283 IPB000577H 308-326 IPB000577I 349-391 IPB000577J 414-462","","","-85% similar to PDB:2D4W Crystal structure of glycerol kinase from Cellulomonas sp. NT3060 (E_value = );-69% similar to PDB:1BWF ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION (E_value = 8.1E_154);-69% similar to PDB:1GLJ ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION (E_value = 8.1E_154);-69% similar to PDB:1GLL ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION (E_value = 8.1E_154);-69% similar to PDB:1BO5 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE. (E_value = 1.8E_153);","Residues 10 to 259 (E_value = 4.6e-98) place ANA_2782 in the FGGY_N family which is described as FGGY family of carbohydrate kinases, N-terminal domain.Residues 262 to 488 (E_value = 7.7e-78) place ANA_2782 in the FGGY_C family which is described as FGGY family of carbohydrate kinases, C-terminal domain.","","kinase (glpK)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2784","3005692","3004925","768","8.42","2.58","25957","ATGTCTGCGACCCTGACCCAGATCTTCGCCTCGGAGGCTCTGGGGACATTTCTTCTGATTCTTCTGGGCTGCGGCGTCGTCGCCGGTGTCGTGCTGCCCACCTCCAAGGCCAAGGACAGTGGCTGGATCGTCATCACCATGGCCTGGGGTCTGGCGGTCTTCGTGGGTGTCTACGCCGCCTACAAGACCGGCGCGCACCTCAACCCGGCGGTGACCATTGGCAAGGCGGTGGCCGGACAGAACCTCGTGGACATGAATCCCGATGTGCCCGGAACGGTGACCATTCCCGCCACGCCGGTCAACATCCTTGTCTACTGCGCGGCCCAGATGGTGGGCGCCATGGCGGGCGCCGCCACCGTCTGGCTGTCCTACAAGAAGCAGTTCGACCAGGAGGCCGACGCCGCCTCCAAGCTCGCCGTGTTCGCCACCGGCCCGGCGGTGCGCTCCTACGGCTGGAACGTCGTGACCGAGGCGGTGGGCACCTTCGTCCTGCTGGCCTGGATCATCGCCTCGGGCAAGACCCCCTCGGGCCTGGGCCCACTGGCCGTGGCCATGGTCGTCGTCGTCATCGGCATGAGCCTGGGAGGCCCCACCGGCTACGCCATCAACCCGGCCCGTGACCTGGGCCCGCGCATCACCCACGCCCTCCTGCCGATCCCCGGCAAGGGCGGCTCGGACTGGGCCTACTCCTGGGTCCCGATCGTCGGCCCGCTCATCGGCGCCGTCGCCGCCGGACTCATCGTCCCCCACTTCGCCGGGCTGTTCTGA","MSATLTQIFASEALGTFLLILLGCGVVAGVVLPTSKAKDSGWIVITMAWGLAVFVGVYAAYKTGAHLNPAVTIGKAVAGQNLVDMNPDVPGTVTIPATPVNILVYCAAQMVGAMAGAATVWLSYKKQFDQEADAASKLAVFATGPAVRSYGWNVVTEAVGTFVLLAWIIASGKTPSGLGPLAVAMVVVVIGMSLGGPTGYAINPARDLGPRITHALLPIPGKGGSDWAYSWVPIVGPLIGAVAAGLIVPHFAGLF$","Glycerol uptake facilitator protein","Membrane, Cytoplasm, Extracellular","glycerol uptake facilitator protein","K02440 glycerol uptake facilitator protein","major intrinsic protein","","Reizer J., Reizer A., Saier Jr M.H. The MIP family of integral membrane channel proteins: sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins. Crit. Rev. Biochem. Mol. Biol. 1993. 28(3):235-257. PMID: 8325040Pao G.M., Wu L.F., Johnson K.D., Hofte H., Chrispeels M.J., Sweet G., Sandal N.N., Saier Jr M.H. Evolution of the MIP family of integral membrane transport proteins. Mol. Microbiol. 1991. 5(1):33-37. PMID: 2014003Wistow G.J., Pisano M.M., Chepelinsky A.B. Tandem sequence repeats in transmembrane channel proteins. Trends Biochem. Sci. 1991. 16(5):170-171. PMID: 1715617Chrispeels M.J., Agre P. Aquaporins: water channel proteins of plant and animal cells. Trends Biochem. Sci. 1994. 19(10):421-425. PMID: 7529436Reid M.E., Lomas-francis C. Molecular approaches to blood group identification. Curr Opin Hematol 2002. 9(2):152-159. PMID: 11845000","","","

InterPro
IPR000425
Family

Major intrinsic protein
PD000295	$\"[12-246]T$	Q6A5F2_PROAC_Q6A5F2;
PR00783	$\"[7-26]T$ $\"[101-120]T$ $\"[156-174]T$ $\"[184-206]T$ $\"[231-251]T$	MINTRINSICP
G3DSA:1.20.1080.10	$\"[3-251]T$	no description
PTHR19139	$\"[9-233]T$	AQUAPORIN TRANSPORTER
PF00230	$\"[2-248]T$	MIP
PS00221	$\"[66-74]T$	MIP

InterPro
IPR012269
Family

Aquaporin
PIRSF002276	$\"[6-252]T$	Aquaporin

noIPR
unintegrated

unintegrated
PTHR19139:SF10	$\"[9-233]T$	GLYCEROL UPTAKE FACILITATOR
signalp	$\"[1-29]?$	signal-peptide
tmhmm	$\"[14-32]?$ $\"[41-61]?$ $\"[102-122]?$ $\"[150-170]?$ $\"[176-196]?$ $\"[227-247]?$	transmembrane_regions

","BeTs to 13 clades of COG0580COG name: Glycerol uptake facilitator and related permeases (Major Intrinsic Protein Family)Functional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0580 is a-m---y-vd-lbcef-hs--j--twNumber of proteins in this genome belonging to this COG is 1","***** IPB000425 (MIP family) with a combined E-value of 8.7e-06. IPB000425 179-229 IPB000425 44-94","","","-46% similar to PDB:1FX8 CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITH SUBSTRATE GLYCEROL (E_value = 1.0E_14);-46% similar to PDB:1LDA CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITHOUT SUBSTRATE GLYCEROL (E_value = 1.0E_14);-46% similar to PDB:1LDI CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITHOUT SUBSTRATE GLYCEROL (E_value = 1.0E_14);-44% similar to PDB:2EVU Crystal structure of aquaporin AqpM at 2.3A resolution (E_value = 1.9E_13);-44% similar to PDB:2F2B Crystal structure of integral membrane protein Aquaporin AqpM at 1.68A resolution (E_value = 1.9E_13);","Residues 2 to 248 (E_value = 2e-22) place ANA_2784 in the MIP family which is described as Major intrinsic protein.","","uptake facilitator protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2785","3007659","3005860","1800","6.85","-1.41","63787","ATGACCTCCACCCGCAAGCCCTCGTCCAAGAAGACCCCCCGCAGCTCCGGCCCGGCTGGCCCCTCCTACCCCGCCCCCATCCAGGACACCGCGCTCAACGCCGCCCAGCGCGAGCGCGCCCTGGAGGAGATGTCGTCCGCCGAGGGCCTGGACGTGCTGGTCGTCGGCGGAGGTGTCACCGGGGCCGGCATCGCCCTGGACGCCGCGGCCCGCGGCCTGCGCACCGGCATCGTGGAGATGGGCGACTGGGCCTCGGGCACCTCCTCGTGGTCCTCCAAGCTCGTCCACGGCGGCCTGCGCTACCTCTACCAGCTCAACTTCGCCCTCGTGCACGAGGCCCTCACCGAGCGCGGCCGCCTGCTGAGCACCACCGCGCCGCACCTGGTCAAGGCCCAGCCCTTCCTGTGGCCGCTCAAGCACCACTACGAGCGCTCCTACTCCGCGGTCGGCGTGGGCATGTACGACGCCCTGGCCCTGGCCGGCTCCCGCGGCCGCAAGACCGTGCCGATCCAGCGCCACCTGGGCCGCAAGGGCACCTCCGCCCTGGCCCCCTCCCTGGACACCAGCGGCCTGGCCGGCGCCATCCGCTTCTTCGACGCCCGGGTCGACGACGCCCGCCTGGTCATCGACCTGGTGCGCACCGCCGTCGGCCTGGGGGCGCTGGCCGCCAACCGCACGAAGGTCACCGGCTTCCTCACCGACGAGCGCGGCCATGTCCACGGCGCCCGCGTCACCGACCTGGCCACCGGCACCGACCACGAGATCCGGGCCAAGCGGACCATCAACGCCGCCGGCGTGTGGACCGAGGACGTCCAGGACCTGGCCACCGACGCCGGCGGCCTGAAGGTCCTGGCCTCCAAGGGCATCCACATCGTGGTCCCCAAGGAGGCCATCGACGCCGAGACCGGGGTCTTCCTGCGCACCGAGAAGTCCGTCCTGTTCATCATCCCCTGGCCCGAGTACTGGGTCATCGGCACCACCGACACCCCCTGGGACCTGGACGTCTCCAAGCCCGTGGCCACCGCCGCCGACGTCGACTACATCCTCGAGCACGCCAACTCCGTGCTGTCGCGGCCCATCACTCGCGCCGACATCATCGGCGTCTACGCGGGCCTGCGCCCCCTGCTCCAGCCCAAGCTCAAGCCGGGCGCGGAGGCCGCCTCCACGAAGGTCTCCCGCGAGCACACGGTCACCCGGATCGCCCCGGGGCTGACCGCCATCGCCGGCGGCAAGCTGACCACCTACCGGGTCATGGCCGCCGACGCCGTCGACCACGCCCTGGGCGAGGCCCTGTCCCACGCCCACCCCTGCGCCACGCAGGAACTGCCCCTGGTGGGTGCGGCCGGCTACCACGCCCTGGCCAAGCGGGCCGGGCGGATCGCCGGCGAGCGCGGCTGGACCCTGGAGCGGGTCACCCACCTGCTGGACCGCTACGGCGATGAAACCCCGGCACTACTGGAGGCCATCGACGCCGCAGGCCCCGAGGAGCGCCTGGGCGAGCCGCTGGCCGAGGCCCCCACCTACCTGCGCGCCGAGGTCGCCTGGGCCGTCACCCACGAGGGCGCCGAGAGCCTCGACGACGTCCTGCTGCGCCGGGTGCGCCTGGACCTCTCGCGCCGCGACCGGGGCCTGGCCGCCGCCGACGAGATCCTGGCGATCATGGCGCCGCTGCTGAACTGGTCCGAGAAGGACGTCGCCGCCCAGAAGGAGGCCTACGCCCAGCGCGTGGCCCAGATCGCCGCAGCAGAGTCCGAGCTGACCGACGCCGCTGCGGTGGCGCACATCACCGAGCCGATCTAG","MTSTRKPSSKKTPRSSGPAGPSYPAPIQDTALNAAQRERALEEMSSAEGLDVLVVGGGVTGAGIALDAAARGLRTGIVEMGDWASGTSSWSSKLVHGGLRYLYQLNFALVHEALTERGRLLSTTAPHLVKAQPFLWPLKHHYERSYSAVGVGMYDALALAGSRGRKTVPIQRHLGRKGTSALAPSLDTSGLAGAIRFFDARVDDARLVIDLVRTAVGLGALAANRTKVTGFLTDERGHVHGARVTDLATGTDHEIRAKRTINAAGVWTEDVQDLATDAGGLKVLASKGIHIVVPKEAIDAETGVFLRTEKSVLFIIPWPEYWVIGTTDTPWDLDVSKPVATAADVDYILEHANSVLSRPITRADIIGVYAGLRPLLQPKLKPGAEAASTKVSREHTVTRIAPGLTAIAGGKLTTYRVMAADAVDHALGEALSHAHPCATQELPLVGAAGYHALAKRAGRIAGERGWTLERVTHLLDRYGDETPALLEAIDAAGPEERLGEPLAEAPTYLRAEVAWAVTHEGAESLDDVLLRRVRLDLSRRDRGLAAADEILAIMAPLLNWSEKDVAAQKEAYAQRVAQIAAAESELTDAAAVAHITEPI$","Glycerol-3-phosphate dehydrogenase 2","Cytoplasm","Glycerol-3-phosphate dehydrogenase","glycerol-3-phosphate dehydrogenase 2 ","FAD dependent oxidoreductase","","Tu K.Y., Ju H.S., Pettit F., Shive W., Topek N.H., Matthews R., Matthews K. Glycerol-3-phosphate dehydrogenase activity in human lymphocytes: effects of insulin, obesity and weight loss. Biochem. Biophys. Res. Commun. 1995. 207(1):183-190. PMID: 7857262Koike G., Van Vooren P., Shiozawa M., Galli J., Li L.S., Glaser A., Balasubramanyam A., Brown L.J., Luthman H., Szpirer C., MacDonald M.J., Jacob H.J. Genetic mapping and chromosome localization of the rat mitochondrial glycerol-3-phosphate dehydrogenase gene, a candidate for non-insulin-dependent diabetes mellitus. Genomics 1996. 38(1):96-99. PMID: 8954787Austin D., Larson T.J. Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12. J. Bacteriol. 1991. 173(1):101-107. PMID: 1987111Ronnow B., Kielland-Brandt M.C. GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae. Yeast 1993. 9(10):1121-1130. PMID: 8256521Brown L.J., MacDonald M.J., Lehn D.A., Moran S.M. Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence for EF-hand calcium-binding domains. J. Biol. Chem. 1994. 269(20):14363-14366. PMID: 8182039Dummler K., Muller S., Seitz H.J. Regulation of adenine nucleotide translocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues. Biochem. J. 1996. 317:913-918. PMID: 8760382Larsson C., Pahlman I.L., Ansell R., Rigoulet M., Adler L., Gustafsson L. The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae. Yeast 1998. 14(4):347-357. PMID: 9559543MacDonald M.J., Brown L.J. Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied. Arch. Biochem. Biophys. 1996. 326(1):79-84. PMID: 8579375","","","

InterPro
IPR000447
Family

FAD-dependent glycerol-3-phosphate dehydrogenase
PR01001	$\"[50-62]T$ $\"[63-73]T$ $\"[79-91]T$ $\"[125-137]T$ $\"[369-375]T$ $\"[404-416]T$	FADG3PDH
PS00977	$\"[55-72]T$	FAD_G3PDH_1
PS00978	$\"[409-419]T$	FAD_G3PDH_2

InterPro
IPR006076
Family

FAD dependent oxidoreductase
PF01266	$\"[51-416]T$	DAO

noIPR
unintegrated

unintegrated
G3DSA:3.50.50.60	$\"[50-275]T$	no description
PTHR11985	$\"[37-576]T$	GLYCEROL-3-PHOSPHATE DEHYDROGENASE

","BeTs to 12 clades of COG0578COG name: Glycerol-3-phosphate dehydrogenaseFunctional Class: C [Metabolism--Energy production and conversion]The phylogenetic pattern of COG0578 is -o-p--y--drlbcefghs--j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB000447 (FAD-dependent glycerol-3-phosphate dehydrogenase family signature) with a combined E-value of 6.1e-35. IPB000447A 50-62 IPB000447B 63-73 IPB000447C 79-91 IPB000447D 125-137 IPB000447E 369-375 IPB000447F 404-416***** IPB003042 (Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature) with a combined E-value of 9.2e-06. IPB003042A 51-73","","","No significant hits to the PDB database (E-value < E-10).","Residues 51 to 416 (E_value = 6.9e-52) place ANA_2785 in the DAO family which is described as FAD dependent oxidoreductase.","","dehydrogenase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2787","3007739","3009196","1458","9.39","13.38","49888","ATGGGAGGCAGGTCGGGGCCCGGCTTCCGGTGCCCACTGCCTGCCGTCGCGCTCGCACGGCCCTTGTGTGGTGGCGGACACCACTGTCCGTTGTGTGTGGGAGAATGCGCAAGGGGTGTGCACGAATGTGCACGAGACTTTCGAGGTATCCACAAGAATGTCCGCACAACTGTGTGGACGGCTCTCCTGAACAGGACATCCGATGTCGCAGGCGGGAGGATCGTTCCCTCCCGCGGCGGGCAACTGCCGTGTGGAGCCGCCCCGTCGTCGGAGGGCGGAGCCGGATGGAGCAAGGAGGAAGACGTGACTGGCAGAACCGCTGCTGACGCGGCCGGGAGCGCGGCCAGTGCCGCCGACCCTGGCGGCCTCCTGCGCGCCTATGAGGCGGCCTCCATGTACTACGTCCAGGGCGAGACGATGGAGGTGATCGCCCACCACCTGGGGGTGTCGCGCTCGACCGTCTCCCGGCTCCTGGCACGTGCCCGCCAGGAGGGTGTCGTGCGGGTCAGCCTCGTCCAGCCCGGGGGTGCCGGCTCCCTGGAGGGGCGGATGGCGCAGGTCTTCGGGGTCCGCACGCATATCGTCCCGGTGCGTGAGGGCACCACGGAGATCCACCGCCTCCAGCAGGTCGCCTCCGTCGCCGCCGCGCACATGGTCGATCTCATCGAGGCCCTGGCCGAGCCGGGCCGGGGCCGAGGTGTCGGTGCGCCTGAGTCCGGTGGTCCCGAGGGTGACAAGCCCGCCGCGGTCGGCGAGCCCGCCGGGTCGGGTCGGGACGCTGACGCAGGAGGCGTCGTCGTCGGTGTCGCCTGGGGCACCACCATGTCGGAGGTCAGCGCCGCCCTGCCCTCGAGGTCCGTTCCGGGACTGACCGTCGTCCAGCTCAACGGTGCCTCGGATCCTGTGCGTGAGGGGCCCAGCGCCGGTGAGGTGCTCTCCCGGATGCGCCTGTCGCTGGGGGCGCGCACGATCTCCTTCCCGGTGCCGGCCTTCTTCGACCATGTGGCCACGCGCGAGGCCATGTGGTCGGAGCGCTCGGTCAAGCGGGTCCTGTCGGTGGTGCGGCGCGCGAGCCTGGCCGTCTTCGGCGTCGGCGCCCTCGACGCCCTCAACGGGGCCCTGCCCTCCCAGGTCTACGAGGGCGGCCACCTCACGGCCCGGGACCAGGCCGTGCTGCGCCGCCAGAACGTGGTGGGGGACGTGTGCACCGTCCTGCTGCGCGCCGACGGCTCCTGGCGTGACGTCACCCTCAACGCCCGGGCCACCGGCCCGACCCCCGCCCAGCTCGCCCGGATTCCGCGCCGCCTGTGCGTGGCCGCGGGAACCGGCAAGGCCCGCGCCCTGCTGGCCGCGCTGCGCGCCCGGACCGCCACCGATCTCGTCGTCGACGACGCCACTGCCCGCGCCGTCCTGGAACTCGCCGAGGCCCGCGGCCAGAAGGGAGGCGGTTCTCGATGA","MGGRSGPGFRCPLPAVALARPLCGGGHHCPLCVGECARGVHECARDFRGIHKNVRTTVWTALLNRTSDVAGGRIVPSRGGQLPCGAAPSSEGGAGWSKEEDVTGRTAADAAGSAASAADPGGLLRAYEAASMYYVQGETMEVIAHHLGVSRSTVSRLLARARQEGVVRVSLVQPGGAGSLEGRMAQVFGVRTHIVPVREGTTEIHRLQQVASVAAAHMVDLIEALAEPGRGRGVGAPESGGPEGDKPAAVGEPAGSGRDADAGGVVVGVAWGTTMSEVSAALPSRSVPGLTVVQLNGASDPVREGPSAGEVLSRMRLSLGARTISFPVPAFFDHVATREAMWSERSVKRVLSVVRRASLAVFGVGALDALNGALPSQVYEGGHLTARDQAVLRRQNVVGDVCTVLLRADGSWRDVTLNARATGPTPAQLARIPRRLCVAAGTGKARALLAALRARTATDLVVDDATARAVLELAEARGQKGGGSR$","Transcriptional regulator, DeoR family","Cytoplasm, Extracellular","transcription regulator","transcriptional regulator","putative sugar-binding domain protein","","Helmann J.D., Chamberlin M.J. Structure and function of bacterial sigma factors. Annu. Rev. Biochem. 1988. 57:839-872. PMID: 3052291Gribskov M., Burgess R.R. Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins. Nucleic Acids Res. 1986. 14(16):6745-6763. PMID: 3092189Lonetto M., Gribskov M., Gross C.A. The sigma 70 family: sequence conservation and evolutionary relationships. J. Bacteriol. 1992. 174(12):3843-3849. PMID: 1597408Campbell E.A., Muzzin O., Chlenov M., Sun J.L., Olson C.A., Weinman O., Trester-zedlitz M.L., Darst S.A. Structure of the bacterial RNA polymerase promoter specificity sigma subunit. Mol. Cell 2002. 9(3):527-539. PMID: 11931761","","","

InterPro
IPR007324
Domain

Putative sugar-binding region
PF04198	$\"[213-472]T$	Sugar-bind

InterPro
IPR007630
Domain

RNA polymerase sigma-70 region 4
PF04545	$\"[131-163]T$	Sigma70_r4

noIPR
unintegrated

unintegrated
signalp	$\"[1-19]?$	signal-peptide

","BeTs to 4 clades of COG2390COG name: Transcriptional regulator, contains sigma factor-related N-terminal domainFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG2390 is ---------d-lb-e-gh---j----Number of proteins in this genome belonging to this COG is 1","***** IPB007324 (Putative sugar-binding domain) with a combined E-value of 1.2e-16. IPB007324A 151-165 IPB007324B 435-467","","","No significant hits to the PDB database (E-value < E-10).","Residues 131 to 163 (E_value = 5e-06) place ANA_2787 in the Sigma70_r4 family which is described as Sigma-70, region 4.Residues 143 to 167 (E_value = 0.00047) place ANA_2787 in the Crp family which is described as Bacterial regulatory proteins, crp family.Residues 213 to 472 (E_value = 4.2e-38) place ANA_2787 in the Sugar-bind family which is described as Putative sugar-binding domain.","","regulator (AP001509)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2788","3009311","3009955","645","5.63","-5.64","23244","ATGCGGACGACTATGAACAGCACTGCTGTCAGGACAGATGAACACCTGCCCACCGGCCGGGCAGCTCGCCGAGCCGAGGTCTACGGGGTCGACGGCTCCCGACGCGTCCTGCGGCCGGCTCGCCCGGCGGACGTGCGTGCCATCGCCGAGCTGGTGCGGCCCTATGCCGAGCGTCGCGTTCTCATCGCCAAGGACCTCATCTCCTACTTCGAGGACATCCAGGAGTTCATCGTCGCCGAGGAGATCCCCGGCGTCGCCGGGCCCGGTGGAGCAGACGGCGGAGAGGTGTCGGCCGTGCCCAGGATCGTGGGCTGCGGGGCTTTGCACGTCATGTGGGACGACATCGCCGAGGTACGCACCCTGGCCGTTCACCCCGACGCCGTGGGGACCGGGCTCGGTTCAGCCATCCTGCGCGAGCTCATCGCGCAGGCCCGGGAGATGGGGCTCAAGCGGGTGTTCTGCATGACATTCGAGGAGCCCTTCTTCGGTGCCCACGGTTTCGAGCCGATCGAGGGCACCCCAGTGGGTGCGGACGTCTTCTCCGAGATGCTGCGCTCCCACGACGACGGTCTGGCTGAGTTCCTTGACCTGGCCCGCGTCAAGCCCAACACCCTGGGCAACGCCCGCATGCTCCTGCACCTGTGA","MRTTMNSTAVRTDEHLPTGRAARRAEVYGVDGSRRVLRPARPADVRAIAELVRPYAERRVLIAKDLISYFEDIQEFIVAEEIPGVAGPGGADGGEVSAVPRIVGCGALHVMWDDIAEVRTLAVHPDAVGTGLGSAILRELIAQAREMGLKRVFCMTFEEPFFGAHGFEPIEGTPVGADVFSEMLRSHDDGLAEFLDLARVKPNTLGNARMLLHL$","GCN5-related N-acetyltransferase","Cytoplasm","acetyltransferase, GNAT family","hypothetical protein","GCN5-related N-acetyltransferase","","Carrozza M.J., Utley R.T., Workman J.L., Cote J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 2003. 19(6):321-329. PMID: 12801725Neuwald A.F., Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 1997. 22(5):154-155. PMID: 9175471Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 1998. 94(4):427-438. PMID: 9727486Trievel R.C., Rojas J.R., Sterner D.E., Venkataramani R.N., Wang L., Zhou J., Allis C.D., Berger S.L., Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 1999. 96(16):8931-8936. PMID: 10430873","","","

InterPro
IPR000182
Domain

GCN5-related N-acetyltransferase
PF00583	$\"[94-168]T$	Acetyltransf_1
PS51186	$\"[35-188]T$	GNAT

noIPR
unintegrated

unintegrated
G3DSA:3.40.630.30	$\"[36-171]T$	no description

","BeTs to 7 clades of COG1246COG name: N-acetylglutamate synthase and related acetyltransferasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG1246 is -------q-dr---efgh-n------Number of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 94 to 168 (E_value = 1.6e-12) place ANA_2788 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family.","","GNAT family (GNAT)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2790","3010095","3010580","486","10.62","7.16","18065","ATGATCCGCAACGTTCACGAACGCGTCATCAATGCCTCTATCGAGTCCCTGGGCGCCCTGCTTGACGGGCTGGGACAGAAGGACGACCGCCTCTGGCCCTCGCGCTCCTGGCCACCGATGGTCCTGGACCGGCCCCTGGCGGTGGGAGCCGACGGTGGGCACGGCGTCATCCGCTACTACGTGAGCGAGTACAAGCCTGGCCGGCGAGTGCGGTTCACCTTCCGTCCGCGAACAGGGATCATCGGCGCCCATGAACTGAGCCTTGACACCTTGGACGATGAGCGCACTCGCATCCGCCACGTCCTCATCGGCCGTGCCCGCGGCGCCATGCGGCTCATGTTCTCGGCCGTCGTCGAGCCCCTGCACGACGCCGTCGTCGAGGACCTCCTCGACAACGCCGAGCGGGAGGCGACCGGTTCGGTGGCCCGGCCCGCGTCCTGGAGTCCGCGGGTACGCGTGCTGCGCCGCCTCATCGGTGGAAGGTAG","MIRNVHERVINASIESLGALLDGLGQKDDRLWPSRSWPPMVLDRPLAVGADGGHGVIRYYVSEYKPGRRVRFTFRPRTGIIGAHELSLDTLDDERTRIRHVLIGRARGAMRLMFSAVVEPLHDAVVEDLLDNAEREATGSVARPASWSPRVRVLRRLIGGR$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2792","3010807","3011382","576","10.62","6.39","20947","GTGCGCCGAACCGCGTTCACCGGCTCTGGCTGGATCGTGTTCATTTTCTGCGGTATTCCAGGGCTGTACCTGCTGAACATTGCGCGACTCTTCGTGGGGGAATGGGGTGGCGCTTTCTTCACGGCGCTGATAATCGGGCTGTTGCTCCTCCTCCCTGTCGCGGTGGCGACCTCGAGGAGGACGCAGTTCGATGCGGATGGGATCCATGTGCGGGGCCTGTGGAGCGCGCATGATGCCCCGTGGCCCCGCTCCCGCCGCGGGCTGGTCGTCCAGCGGCCGGCTAAGAACCCGGTCCTGGGACTCCTCATCATGGCCTTCGCCGGGCTCTTCATCGTGATTCTGGTGTTCCTGAGTGATGGGAACCTGACCCCGGATGAGTTCCCCGGCATGAGTCTGGCCGCTCGGACCTATGTCCTCGACTCCGAGGGAGAGGCCGTCTGGCTTGCAGGAATGTCGCGCCGAGGATTGTCCAGGTCCGGCACGGAGCGCAGAAGCTCGGCGGAGCTGGATCGGATCTGGGATTGGGCAGTGGCTCGCGGTTATACCCGGGAGACGGGTACGCCTGCGCGATCGTAG","VRRTAFTGSGWIVFIFCGIPGLYLLNIARLFVGEWGGAFFTALIIGLLLLLPVAVATSRRTQFDADGIHVRGLWSAHDAPWPRSRRGLVVQRPAKNPVLGLLIMAFAGLFIVILVFLSDGNLTPDEFPGMSLAARTYVLDSEGEAVWLAGMSRRGLSRSGTERRSSAELDRIWDWAVARGYTRETGTPARS$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-56]?$	signal-peptide
tmhmm	$\"[10-30]?$ $\"[36-56]?$ $\"[98-118]?$	transmembrane_regions

InterPro
IPR001584
Domain

Integrase, catalytic core
PF00665	$\"[140-304]T$	rve
PS50994	$\"[128-307]T$	INTEGRASE

noIPR
unintegrated

unintegrated
G3DSA:3.30.420.10	$\"[143-310]T$	no description

","BeTs to 5 clades of COG1425COG name: Predicted transposaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1425 is a--p-----dr---efgh-n-j----Number of proteins in this genome belonging to this COG is 7","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 140 to 304 (E_value = 6.4e-21) place ANA_2793 in the rve family which is described as Integrase core domain.","","transposase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2794","3012972","3013919","948","7.42","1.26","34000","GTGCCCGACCGCCCCACCCCTGACGACACGCTCACCGCTGCGACCTCGGCGCAGGACGTCATGACCTGGTACGACGCCCATGCCCGCGACCTGCCGTGGCGCCGGCCCGGTACCACGCCGTGGGAGGTCCTCGTCTCGGAGGTCATGAGCCAGCAGACCCCGGTGGCCCGTGTCGTCCCCGCCTGGCAGGAGTGGATGCGGCGCTGGCCCGGCCCCGCCGAGCTCGCCCAGGCCCCCACCGCTGCGGTGCTGCGGGTCTGGGGGCGCCTGGGCTACCCGCGCCGGGCCCTGCGTCTCATCGAGTGCGCCCGCAGCGTCGTCGAGCAGCACGGCGGCGTCCTGCCCGACGATCTGGACGCCCTCCTGGCCCTGCCCGGGGTGGGGGAGTACACGGCCGGCGCGGTCCTGGCCTTCGCCCACGGTCGGCGCGCCCTCGTGCTGGACACGAATGTCAGACGGGTCCTGGCCCGCGCCGTCGCCGGTCAGGCCCTTCCCGCCCCCAGCCTCAACCGGGCCGAGCGCGAGCGGGCACTGGACCTGCTGCCCGACGACGACTCCACTGCCGCCCACTGGTCGGTGGCCGTCATGGAGCTCGGCGCCCTGGTGTGCACCGCCCGCGAGCCGGACTGCGGGGCCTGCCCGTGGCAGACCGGCTGCGCCTGGCTGGCGGCCGGCCGCCCCGCGGACCTCCACGCGGGCCGGCGTCGCACCCAGGCCTGGCACGGCACCGACCGTCAGGCCCGGGGGCTGGTCATGGCCCGCCTGCGCGCGGCCCCCGACGGGCAGCGCGTCGAGGCCGCTGAGCTCAGGGCCTGCGCCGCCAGGGCCGGCACGCGAGCCTCCGGCGGAGCTCGCGACCCCGAGCAGCCGGTGCGCGCCCTGGCCACGCTCCTGGCCGACGGGCTCATCGCCACCGACGACGACGGCGTCACCTACCGGCTTCCCTAA","VPDRPTPDDTLTAATSAQDVMTWYDAHARDLPWRRPGTTPWEVLVSEVMSQQTPVARVVPAWQEWMRRWPGPAELAQAPTAAVLRVWGRLGYPRRALRLIECARSVVEQHGGVLPDDLDALLALPGVGEYTAGAVLAFAHGRRALVLDTNVRRVLARAVAGQALPAPSLNRAERERALDLLPDDDSTAAHWSVAVMELGALVCTAREPDCGACPWQTGCAWLAAGRPADLHAGRRRTQAWHGTDRQARGLVMARLRAAPDGQRVEAAELRACAARAGTRASGGARDPEQPVRALATLLADGLIATDDDGVTYRLP$","A/G-specific adenine glycosylase","Cytoplasm, Extracellular","A/G-specific adenine glycosylase","putative adenine glycosylase ","HhH-GPD family protein","","Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Aravind L., Walker D.R., Koonin E.V. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res. 1999. 27(5):1223-1242. PMID: 9973609Provvedi R., Dubnau D. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol. Microbiol. 1999. 31(1):271-280. PMID: 9987128Doherty A.J., Serpell L.C., Ponting C.P. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 1996. 24(13):2488-2497. PMID: 8692686","","","

InterPro
IPR000445
Domain

Helix-hairpin-helix motif
PF00633	$\"[109-138]T$	HHH

InterPro
IPR003265
Domain

HhH-GPD
PF00730	$\"[45-177]T$	HhH-GPD
SM00478	$\"[49-201]T$	ENDO3c

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[119-138]T$	HhH1

InterPro
IPR003651
Domain

Iron-sulfur cluster loop
SM00525	$\"[202-222]T$	FES

InterPro
IPR004036
Domain

Endonuclease III, HhH
PS01155	$\"[112-139]T$	ENDONUCLEASE_III_2

noIPR
unintegrated

unintegrated
G3DSA:1.10.340.30	$\"[30-141]T$	no description
PTHR10359	$\"[33-238]T$	A/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III
PTHR10359:SF1	$\"[33-238]T$	A/G-SPECIFIC ADENINE GLYCOSYLASE MUTY

","BeTs to 15 clades of COG1194COG name: A/G-specific DNA glycosylaseFunctional Class: L [Information storage and processing--DNA replication, recombination and repair]The phylogenetic pattern of COG1194 is -om--z---drlb-efghsnuj-it-Number of proteins in this genome belonging to this COG is 1","***** IPB004036 (Endonuclease III, HhH) with a combined E-value of 1.2e-42. IPB004036A 41-55 IPB004036B 83-97 IPB004036C 110-141 IPB004036D 147-157 IPB004036E 195-219***** IPB011257 (DNA glycosylase) with a combined E-value of 3.4e-15. IPB011257A 124-133 IPB011257B 147-157 IPB011257C 199-213","","","-52% similar to PDB:1KG6 Crystal structure of the K142R mutant of E.coli MutY (core fragment) (E_value = 3.1E_30);-52% similar to PDB:1KG2 Crystal structure of the core fragment of MutY from E.coli at 1.2A resolution (E_value = 6.8E_30);-52% similar to PDB:1KG3 Crystal structure of the core fragment of MutY from E.coli at 1.55A resolution (E_value = 6.8E_30);-52% similar to PDB:1MUY CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI (E_value = 6.8E_30);-52% similar to PDB:1WEF Catalytic Domain Of Muty From Escherichia Coli K20A Mutant (E_value = 6.8E_30);","Residues 45 to 177 (E_value = 6.5e-16) place ANA_2794 in the HhH-GPD family which is described as HhH-GPD superfamily base excision DNA repair protein.Residues 109 to 138 (E_value = 4.6e-08) place ANA_2794 in the HHH family which is described as Helix-hairpin-helix motif.","","adenine glycosylase","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2796","3014133","3015362","1230","11.66","32.26","40853","ATGGCCAAAGGACGTGGACGCAACCAAGGGGAAAGCGCAGGACGACGAGGCTCGGCCCGTCGCGGCGCAGGCTCCTCGTCGGGGCGCTCCGCCTCGGGCTCCCAGTCCCGGCCCCATCGGCAGGGCGCTTCCGGTGGCGGCCCGCGGACGGGCGCTGGGCAGTCCTCCTCAGCCCGCTCCGGTGGGGCGCCCCGATCCTCCCAGGCCAAGGGACGCGGCGGCCGCGCTTCGGGCGCCAAGTCCACTGGACGCCCCCTGCACTCGGGACAGACGGGTAGGCCCGCCGGCGGGCACTCGGGTCAGGCGGGCCAGGCAGGCAAGAACCGCCGGTCCCCCCAGGGCGGCCAAGGGACCTCGACGTCGCGCTCGCGGCAGGCCGCTCCGGGAACCGCTCGCTCCTCCCGGACGAGCTCGACTCAGGCCGCTGGTTCCGATCGTCGTCGACACGGTTGGGGTGCGGGCCTCCAGTGGGCCCACATCGGCGGTGGACGGTTGTCCGGAGCGCCCGACTCGGTCCCGCAGGGCCCCGACCAGCCTCGCAGCGGGCGCCTGCGCAAGCCGGTCCCGCCCCAGCCCCGCTACGGTCTGCGCCGTGCCTTGGTGCTGGGCGGAGTGCTGCTGGTCCTCCTGCTGTTCGTCGTGGCCATCGTTGTCGGCTACCTCTGGGTCCGCAACACCATCCGCAGCCAGGACGAGGAGCGCGCCGCCGCTCAGGTGCACACCGTCTACCCCACGCCGGGAAAGTGCGACCCCTCGACCTTGAAGAGCACGGTCCAGGGGCCCGAGTCCGTCGGTGTCGGCGCCGGGGCAACCTTCTCCATCTCCCTGGTCAACGGCGGCCAGGCACCCTGCCTGATCGACGTCGGCAGCCAGGCCCTGGGGGTGCGGGTCAGCTCGGGCTCCCAGCAGGTGTGGGACTCTGTCACCTGCCCCGTGGGCCAGACCGAGAAGGCCCTCCTCCTGCCGGCGGGCAAGGGTGCCGATGTCACCGTGACCTGGAACGGCAACGCGGCCACCTCCGACTGCGCAGCAGCGAACGCCGCACCGGCCTCTCCGGCCGGTGCATCGGCCTCCCCGACTCCGAGCGCTACCGCATCCTCCTCTGCGAGCCCCTCAGCGGGTCAGGCGCAGACCGCCCCCGGCAGCACCGCGGGCGCGGGGACCTACCGCTTCCGCTTCGTCATGGGGGACAAGGACCTGTCGGAGGACCGGGTCTTCGTCGTCGGCTGA","MAKGRGRNQGESAGRRGSARRGAGSSSGRSASGSQSRPHRQGASGGGPRTGAGQSSSARSGGAPRSSQAKGRGGRASGAKSTGRPLHSGQTGRPAGGHSGQAGQAGKNRRSPQGGQGTSTSRSRQAAPGTARSSRTSSTQAAGSDRRRHGWGAGLQWAHIGGGRLSGAPDSVPQGPDQPRSGRLRKPVPPQPRYGLRRALVLGGVLLVLLLFVVAIVVGYLWVRNTIRSQDEERAAAQVHTVYPTPGKCDPSTLKSTVQGPESVGVGAGATFSISLVNGGQAPCLIDVGSQALGVRVSSGSQQVWDSVTCPVGQTEKALLLPAGKGADVTVTWNGNAATSDCAAANAAPASPAGASASPTPSATASSSASPSAGQAQTAPGSTAGAGTYRFRFVMGDKDLSEDRVFVVG$","Hypothetical protein","Extracellular, Membrane","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
tmhmm	$\"[200-222]?$	transmembrane_regions

","No hits to the COGs database.","No significant hits to the Blocks database.","","","-59% similar to PDB:2NOB Structure of catalytically inactive H270A human 8-oxoguanine glycosylase crosslinked to 8-oxoguanine DNA (E_value = );-59% similar to PDB:2NOF Structure of Q315F human 8-oxoguanine glycosylase proximal crosslink to 8-oxoguanine DNA (E_value = );-59% similar to PDB:2NOH Structure of catalytically inactive Q315A human 8-oxoguanine glycosylase complexed to 8-oxoguanine DNA (E_value = );-59% similar to PDB:2NOL Structure of catalytically inactive human 8-oxoguanine glycosylase distal crosslink to oxoG DNA (E_value = );-59% similar to PDB:2NOZ Structure of Q315F human 8-oxoguanine glycosylase distal crosslink to 8-oxoguanine DNA (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2797","3016488","3015421","1068","5.24","-9.02","38406","ATGATCGAGGCCGCTGGCCAGCTGCGCGAGACGCTTGCGCTCGTCGCTCCCGGCACCGTTCTTCGCGACGGCCTGGAGCGGATCCTGCGCGGTCGTACCGGGGCGATCATCGTGCTGGGCTTCGACCCGGTGGTCGAGGCCATCTCCTCAGGCGGATTCCACCTGGACGTTGAGCTCTCCGCCGCCCGCCTGCGTGAGCTGGCCAAGATGGACGGCGGCGTCGTCGTCGATATGGACACCGCCCGGATCCGGCGCGCCAACGTCCAGCTGCTGCCCAATGCCTCGATCCAGACCTCGGAGACGGGCATGCGTCACCGCACCGCCGAGCGCGTGGCTCGCCAGACCGGGTACCCGGTCATCTCCGTGAGCCAGTCGATGCGGATCATCTCCCTGTACGTCGACGGCAAGCGCCACGTCCTGGAGCCCAGCGAGTCGATCCTGGCCAGCGCCAACCAGGCCCTGTCCGCCCTGGAGCGCTACAAGGCCCGCCTCGACCAGACCTCCGCCGGCCTGGACTCCCTGGAGATCGAGGACCTCGTCACCGTCCGTGACGTCACCTCGGTCCTCCAGCTCATGGAGATGGTCCGCCGCATCTCCGCCGACATCGACTCCTACGTCCTGGAGCTCGGCACCGACGGGCGCCTCCTGGCGCTCCAGGTCGAGGAGCTCACCCGGGGCCTGCTCGCCGAGCACGGCTTCCTCCTGGAGGACTACCTGCCCGAGGGCCTGGACACGGCCACCGTCGATGCGCGCCTGAAGTGGGTGGGTTCCCCCGCCCTCCTGGACCTGGCGATGGTGGCGCGATCCATGGGACTGGGCGGCATTGACGGACAGGATCTGGACGCTCAGGTCTCCCCGCGCGGCCTGCGGATCCTTTCCAAGATCCCACGCCTGCCCGTGGTGACGGCGCGCGCCGTCGTCGAGCAGTGGGGGTCCCTGCAGGGGGTCCTCGGGGCCACCATCGAGGAACTCGAGGCCGTCGAGGGTGTGGGCGCTCAGCGGGCCCGGACCCTACGCGACGGGCTGTCGCGGCTGGCGGAAATCTCCGTCGTCGAGCGCTACTCCTGA","MIEAAGQLRETLALVAPGTVLRDGLERILRGRTGAIIVLGFDPVVEAISSGGFHLDVELSAARLRELAKMDGGVVVDMDTARIRRANVQLLPNASIQTSETGMRHRTAERVARQTGYPVISVSQSMRIISLYVDGKRHVLEPSESILASANQALSALERYKARLDQTSAGLDSLEIEDLVTVRDVTSVLQLMEMVRRISADIDSYVLELGTDGRLLALQVEELTRGLLAEHGFLLEDYLPEGLDTATVDARLKWVGSPALLDLAMVARSMGLGGIDGQDLDAQVSPRGLRILSKIPRLPVVTARAVVEQWGSLQGVLGATIEELEAVEGVGAQRARTLRDGLSRLAEISVVERYS$","Nucleic-acid-binding protein","Cytoplasm","Predicted nucleic-acid-binding protein (containsthe HHH domain)","protein of unknown function DUF147","protein of unknown function DUF147","","Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995. 14(16):4108-4120. PMID: 7664751Aravind L., Walker D.R., Koonin E.V. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res. 1999. 27(5):1223-1242. PMID: 9973609Provvedi R., Dubnau D. ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol. Microbiol. 1999. 31(1):271-280. PMID: 9987128Doherty A.J., Serpell L.C., Ponting C.P. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 1996. 24(13):2488-2497. PMID: 8692686","","","

InterPro
IPR000445
Domain

Helix-hairpin-helix motif
PF00633	$\"[312-341]T$	HHH

InterPro
IPR003390
Domain

Protein of unknown function DUF147
PF02457	$\"[21-138]T$	DUF147

InterPro
IPR003583
Domain

Helix-hairpin-helix DNA-binding, class 1
SM00278	$\"[322-341]T$	HhH1

noIPR
unintegrated

unintegrated
G3DSA:1.10.150.20	$\"[289-344]T$	no description

","BeTs to 3 clades of COG1623COG name: Predicted nucleic-acid-binding protein (contains the HHH domain)Functional Class: R [General function prediction only]The phylogenetic pattern of COG1623 is --------v-r-b-------------Number of proteins in this genome belonging to this COG is 1","***** IPB003390 (Protein of unknown function DUF147) with a combined E-value of 5.1e-14. IPB003390C 102-131","","","No significant hits to the PDB database (E-value < E-10).","Residues 21 to 138 (E_value = 7.2e-38) place ANA_2797 in the DUF147 family which is described as Domain of unknown function DUF147.Residues 312 to 341 (E_value = 0.0014) place ANA_2797 in the HHH family which is described as Helix-hairpin-helix motif.","","nucleic-acid-binding protein (contains the HHH domain)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2799","3018200","3016779","1422","6.56","-1.75","48205","ATGCCCGCATCGAAGAGTCCCAAGGCCCCCAAGGTCTCCTACTGCTGCACGGAGTGCGGCTGGTCAAGCCCCAAGTGGATGGGCCAGTGCCGGGAGTGCCGCGAGTGGGGAACCCTGGAGGAGACTCAGGTCTCCGACTCCCCGGGTGGGAGCGCCGGCGGGGCCCTGGGCGCTGCCGGCGCCGTGCGGCCCTCGGTGGCCGCCCGCCCCATCGGAGAGGTCAGCGCCACGGAGGCCAGGGCCCGCCCCACCGGGGTGGGTGAGCTGGACCGGGTCCTGGGCGGCGGGATCGTGCCGGGCGCCGTCGTACTGCTGGCCGGCGAGCCCGGCGTCGGCAAGTCCACGCTGCTGCTCGACGTCGCCGCGAAGGCGGCCGCCGTGGCGCGCGAACGCGGGGACGGACCGGTCCTCTACGTCACCGGTGAGGAGTCGGCCTCGCAGGTGCGGCTGCGGGCCGAGCGCATCGACGCCCTGGATCCCGGGCTGCTCCTGGCCGCGGAGACCGAGCTGGGGGCCCTGCTGGGGCACGTGGAGGCGGCCAGTCCCTCCCTGCTGGTGGTGGACTCGGTTCAGACCATCGCCTCGGCTCAGGTCGAGGGCAGTGCCGGGGGCGTCACCCAGGTGCGGGCCGTGGCCGGTGCGCTCATCGCGGTAGCCAAGGAGCGCAATATCCCGGTGCTGCTCGTGGGGCATGTGACCAAGGACGGCGGGATCGCCGGGCCTCGGGTCCTGGAGCACCTGGTCGACGTCGTCACCCAGTTCGAGGGTGACCGTCACGCCCGTCTGCGGCTGCTGCGGGCCGTCAAGAACCGCTACGGCCCCACCGATGAGGTCGGCTGCTTCGACCTGGGCGAGCGGGGCATCGTGGGGCTGGCGGACCCCTCGGGCCTGTTCCTGTCCGCCGCCCGCTCCGAGGTGCCGGGCACCTGTGCCACCGTGACCCTGGAGGGGCGCCGCCCCATGCCTGTGGAGATCCAGGCGCTGGTGGCCCCCACCAACGCCGGCTCCCCGCGGCGCACCACCTCCGGGGTGGACCACTCGCGCACAGCCATGGCGCTGGCCGTCCTCAGCGCCCGGCTGCGGGTGGACACCTCCAGCGCGGACGTCTATGTCTCCACCGTGGGCGGGGCCCGCGCCGTCGAGCCGGCCACGGACCTGGCGGTGGCCATCTCAGTGGTCTCGGCCGCGCGCAACCTGCCCACGCCCGCCGGCCTGGTGGCCTTCGGCGAGGTGGGGCTCACCGGTGAGGTGCGGGCCACCGTCGGCATCCAGCGGCGTCTGGCGGAGGCCTCCCGTCTCGGCTTCGACCGGGCGATCGTGCCGCTGGCGGGCTCGACCGAGCTGCGCGAGGTCGCCGGGATGCAGGTGCTGCCAGTCGCGCACGTGGGTGAGGCCATGGGGGCGGCCCTCCCGCGTGGCTGA","MPASKSPKAPKVSYCCTECGWSSPKWMGQCRECREWGTLEETQVSDSPGGSAGGALGAAGAVRPSVAARPIGEVSATEARARPTGVGELDRVLGGGIVPGAVVLLAGEPGVGKSTLLLDVAAKAAAVARERGDGPVLYVTGEESASQVRLRAERIDALDPGLLLAAETELGALLGHVEAASPSLLVVDSVQTIASAQVEGSAGGVTQVRAVAGALIAVAKERNIPVLLVGHVTKDGGIAGPRVLEHLVDVVTQFEGDRHARLRLLRAVKNRYGPTDEVGCFDLGERGIVGLADPSGLFLSAARSEVPGTCATVTLEGRRPMPVEIQALVAPTNAGSPRRTTSGVDHSRTAMALAVLSARLRVDTSSADVYVSTVGGARAVEPATDLAVAISVVSAARNLPTPAGLVAFGEVGLTGEVRATVGIQRRLAEASRLGFDRAIVPLAGSTELREVAGMQVLPVAHVGEAMGAALPRG$","DNA repair protein RadA","Cytoplasm","DNA repair protein RadA","DNA repair protein RadA","DNA repair protein RadA","","Selbitschka W., Arnold W., Priefer U.B., Rottschafer T., Schmidt M., Simon R., Puhler A. Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobium leguminosarum biovar viciae. Mol. Gen. Genet. 1991. 229(1):86-95. PMID: 1896024Roca A.I., Cox M.M. RecA protein: structure, function, and role in recombinational DNA repair. Prog. Nucleic Acid Res. Mol. Biol. 1997. 56:129-223. PMID: 9187054Karlin S., Weinstock G.M., Brendel V. Bacterial classifications derived from recA protein sequence comparisons. J. Bacteriol. 1995. 177(23):6881-6893. PMID: 7592482Eisen J.A. The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species. J. Mol. Evol. 1995. 41(6):1105-1123. PMID: 8587109Cerutti H., Osman M., Grandoni P., Jagendorf A.T. A homolog of Escherichia coli RecA protein in plastids of higher plants. Proc. Natl. Acad. Sci. U.S.A. 1992. 89(17):8068-8072. PMID: 1518831","","","

InterPro
IPR001553
Family

RecA bacterial DNA recombination
PS50162	$\"[78-203]T$	RECA_2

InterPro
IPR001984
Family

Peptidase S16, Lon protease
PR00830	$\"[107-126]T$ $\"[407-426]T$ $\"[430-448]T$	ENDOLAPTASE

InterPro
IPR003593
Domain

AAA+ ATPase, core
SM00382	$\"[99-258]T$	AAA

InterPro
IPR004504
Family

DNA repair protein RadA
PR01874	$\"[16-40]T$ $\"[91-119]T$ $\"[188-212]T$ $\"[227-255]T$ $\"[262-288]T$ $\"[336-359]T$	DNAREPAIRADA
TIGR00416	$\"[8-466]T$	sms: DNA repair protein RadA

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.300	$\"[62-289]T$	no description

","BeTs to 17 clades of COG1066COG name: Predicted ATP-dependent serine proteaseFunctional Class: O [Cellular processes--Posttranslational modification, protein turnover, chaperones]The phylogenetic pattern of COG1066 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB010624 (KaiC) with a combined E-value of 2.9e-12. IPB010624A 81-125***** IPB013632 (Rad51, C-terminal) with a combined E-value of 1.7e-06. IPB013632B 82-127","","","No significant hits to the PDB database (E-value < E-10).","No significant hits to the Pfam 21.0 database.","","repair protein RadA (radA)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2801","3020450","3018360","2091","4.82","-38.62","73188","ATGAGCGCTGAGCCGCTGCTCACCGACCTCGACCGTCAGACCATCGCGGTGTCCAAGGCCCTGGCCGCCGACGCCGTGGAGAAGGCGGGGTCGGGCCACCCCGGTACGCCGATCTCCCTGGCCGGGGTGGCGTGGCTGCTCTACCAGCGTGAGATGGTCCACGACCCGGCGGATCCGGGGTGGCTGGGACGGGACCGGTTCGTCCTGTCCATCGGGCACGCCTCGCTGGTGCAGTACATCCAGCTGTTCCTGGCCGGGTATGACATCGACCTGGAGGGCTTCACGGCCTTCCGCTCTCCGGCCGGCCTGCCGGGCCACCCCGAGTTCGGAGAGGTTCCCGGGGTGGAGACCACCACGGGCCCGCTGGGGGCGGGCTTCGCCAACGCGGTGGGCCTGGCCATGGCGGCACGCCGCGAGCACGGGCTGCTCGACGCCGGCACCCCGCTGGGCGAGTCGGTCTTCGACCACTTCGTCTACACGGTCCTGGGCGACGGCTGCATGCAGGAGGGCGTGTCCTCGGAGGCCGCCTCCCTGGCCGGCACTCAGCAGCTGGGCAACCTCATCGCCATCTACGACGACAACGACATCTCCATCGAGGGCAACACGGACATCGCCTTCACCGAGGACGTCTCGGCCCGCTTCGAGGCCTACGGCTGGCAGGTGCTCGACGTCGACTGGCGCACCGGCCCCGACGGCTACGCGGAGAACCTCGAGGAGCTGCACGAGGCCATCGTCGCGGCCCGCGCCGAGAGCGCGCGTCCGTCGCTGATCCGTCTGCACACCATCATCGCCTGGCCCTCCCCGACCAAGCAGGGCCAGGAGTCCTCCCACGGCTCCAAGCTCGGGGCCGAGGAGGTCGCCGGGCTCAAGCGGGCCCTGGGCCTGGACCCCGAGCAGAGCTTCATCCTGCCCGAGGACGTCGTCTCCCACGCCCGCAAGCAGGCCGCCGACAACGCCCGGGCCGCCCGAGCGGACTGGGACGCGCGCTTCGCGACCTGGCAGCAGGCCAACCCCGCCGGCGCCGCGCTGCTGGAGCGCCTTGAGGCCTACCGCCTGCCCGAGGGCCTTGAGGAGGCCCTGCCGACCTGGGAGGTGGGTGAGTCCCTGGCCACCCGTGCGGCGTCGGGCAAGGTGCTCTCCGCCCTGGCCGGCGTGGTGCCCGAGCTGTGGGGCGGGTCGGCGGACCTGGCCGGCTCGAACAACACGACCATGGCCGGGGAGCCCTCCTTCCTTCCCGCCGCTCTGGCGCAGTCCGAGGGCGACGGGCCCTTCGGGCGCACCCTCCACTTCGGTGTGCGCGAGCACGCCATGGGCTCGATCCTCAACGGAATCGCCCTGGACGGGCTCACCCGCCCCTACGGGGGCACCTTCATGGTGTTCTCCGACTACATGCGCCCGGCCGTGCGCCTAGCGGCTCTCATGGGGATCGGCCCGGTCTTCGTGTGGTCCCACGACTCCATCGGGGTCGGCGAGGACGGCCCCACGCACCAGCCCGTCGAGCACCTGGCGGCGCTGCGCGCCATCCCCGGCCTGTCCGTGGTGCGCCCCGGGGACGCCAACGAGACCGCCGCGGCCTGGGCGGAGATCCTGCGCCGTCACGACGAGCCGGCCGGCATCGCCCTGTCCCGTCAGAACCTCACCGTGAGCGCCTCCGCCACGGCCGCCGCCGAGGGCGTGCGCCGCGGCGCCTACGTCCTGGCCGAGGCCGCCGACGCCGATGGGCAGCAGGCGGCCCCCGAGGTCGTCCTGATCGCCACCGGCTCCGAGGTCGGCGTGGCCGTGGCCGCCCGGGACATCCTCCAGAAGGAGGGCACCCCCACCCGGGTGGTCTCCGCTCCCTGCCTGGAGTGGTTCGCCCAGCAGGACGCCGCCTACCGGGAGCAGGTGCTGCCGGCCGGCACCGCCAGGGTCGCCATCGAGGCGGGGATCGCCCTGGGCTGGCGCGAGATCGTCGGCGACGCCGGCGAGATCGTCTCCATCGACCACTACGGTTCCTCCGCCCCCGGCACCGCCCTGTTCGAGGAGTACGGCTTCACCGGGGACAACGTCGCCGAGCGGGCCCGCCGGGCGCTGGCCCGCACCCACGGCTGA","MSAEPLLTDLDRQTIAVSKALAADAVEKAGSGHPGTPISLAGVAWLLYQREMVHDPADPGWLGRDRFVLSIGHASLVQYIQLFLAGYDIDLEGFTAFRSPAGLPGHPEFGEVPGVETTTGPLGAGFANAVGLAMAARREHGLLDAGTPLGESVFDHFVYTVLGDGCMQEGVSSEAASLAGTQQLGNLIAIYDDNDISIEGNTDIAFTEDVSARFEAYGWQVLDVDWRTGPDGYAENLEELHEAIVAARAESARPSLIRLHTIIAWPSPTKQGQESSHGSKLGAEEVAGLKRALGLDPEQSFILPEDVVSHARKQAADNARAARADWDARFATWQQANPAGAALLERLEAYRLPEGLEEALPTWEVGESLATRAASGKVLSALAGVVPELWGGSADLAGSNNTTMAGEPSFLPAALAQSEGDGPFGRTLHFGVREHAMGSILNGIALDGLTRPYGGTFMVFSDYMRPAVRLAALMGIGPVFVWSHDSIGVGEDGPTHQPVEHLAALRAIPGLSVVRPGDANETAAAWAEILRRHDEPAGIALSRQNLTVSASATAAAEGVRRGAYVLAEAADADGQQAAPEVVLIATGSEVGVAVAARDILQKEGTPTRVVSAPCLEWFAQQDAAYREQVLPAGTARVAIEAGIALGWREIVGDAGEIVSIDHYGSSAPGTALFEEYGFTGDNVAERARRALARTHG$","Transketolase","Cytoplasm","transketolase","transketolase ","transketolase","","Nikkola M., Lindqvist Y., Schneider G. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. J. Mol. Biol. 1994. 238(3):387-404. PMID: 8176731Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y., Jordan F., Guest J.R., Furey W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry 2002. 41(16):5213-5221. PMID: 11955070Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 1999. 6(8):785-792. PMID: 10426958Chabriere E., Vernede X., Guigliarelli B., Charon M.H., Hatchikian E.C., Fontecilla-Camps J.C. Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase. Science 2001. 294(5551):2559-2563. PMID: 11752578","","","

InterPro
IPR005474
Domain

Transketolase, N-terminal
PF00456	$\"[10-353]T$	Transketolase_N

InterPro
IPR005475
Domain

Transketolase, central region
PF02779	$\"[367-548]T$	Transket_pyr
PS00802	$\"[490-506]T$	TRANSKETOLASE_2

InterPro
IPR005476
Domain

Transketolase, C-terminal
PF02780	$\"[570-683]T$	Transketolase_C

InterPro
IPR005478
Family

Bacterial transketolase
PIRSF000418	$\"[7-693]T$	Transketolase
PTHR11624:SF1	$\"[23-686]T$	TRANSKETOLASE
TIGR00232	$\"[12-692]T$	tktlase_bact: transketolase

InterPro
IPR009014
Domain

Transketolase, C-terminal-like
G3DSA:3.40.50.920	$\"[561-691]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.970	$\"[6-350]T$ $\"[351-559]T$	no description
PTHR11624	$\"[23-686]T$	DEHYDROGENASE RELATED

","BeTs to 22 clades of COG0021COG name: TransketolaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG0021 is --mpkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is 1","***** IPB005476 (Transketolase, C terminal) with a combined E-value of 2.1e-25. IPB005476A 426-451 IPB005476B 490-518***** IPB005475 (Transketolase, central region) with a combined E-value of 2.9e-18. IPB005475A 31-48 IPB005475C 489-518","","","-58% similar to PDB:1ITZ Maize Transketolase in complex with TPP (E_value = 3.2E_140);-56% similar to PDB:1QGD TRANSKETOLASE FROM ESCHERICHIA COLI (E_value = 1.5E_137);-57% similar to PDB:1GPU TRANSKETOLASE COMPLEX WITH REACTION INTERMEDIATE (E_value = 5.9E_134);-57% similar to PDB:1NGS COMPLEX OF TRANSKETOLASE WITH THIAMIN DIPHOSPHATE, CA2+ AND ACCEPTOR SUBSTRATE ERYTHROSE-4-PHOSPHATE (E_value = 5.9E_134);-57% similar to PDB:1TKA SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE (E_value = 5.9E_134);","Residues 10 to 353 (E_value = 2.4e-144) place ANA_2801 in the Transketolase_N family which is described as Transketolase, thiamine diphosphate binding domain.Residues 367 to 548 (E_value = 5.4e-65) place ANA_2801 in the Transket_pyr family which is described as Transketolase, pyrimidine binding domain.Residues 570 to 683 (E_value = 0.00037) place ANA_2801 in the Transketolase_C family which is described as Transketolase, C-terminal domain.","","(tkt) ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2802","3020662","3022044","1383","8.22","3.54","49364","ATGGGTACAGCAAGAGGACGCGCGACGCCGTCGGTGGAGCACGGCAGCGCTTTGGAGCAGATCGACTCCCGGCCCCTGACGGGCCATCAGCGAAGCATCATCGCTCTGGCGATCGTCGCCAACATCTCTGAGTTCTTCGACATGTTCCTCATCGGCTTCGCCGTCGTCCAGCTTCAGAAGGAGTGGAGCCTGGGCGGCTTCGAGACCGGTGTCATCCTGGCCTGCTCCGGGCTGGGCACAGTGCTCGGCTCGGTCCTGTGGGGCCGGGCCGCCGACCGGATGGGCCGACGACGCACCTTCTTCTGGTGCGTCCTGCTCTTCACCGTCTTCACCCTGGCCTCGGTGTTCACCCCCACCGGCTGGTGGATGATGCTGGCCCTGCTGCGGGTGCTGGTCGGAGTGGGCGTCGGGGGCCTCAACATCGTCTCCATCCCCTACGTCCAGGAGTTCGTGCCCACCAGGCAGCGCGGCCTGCTGGCCGGACTGGGCTCGGTGTTCATCCCGCTGGGGCTCTTCCTGGGCTCCCTGGCGCAGCGGCTCCTGCACGACAACTGGCGCGGCCTCATCGCGCTGGGGGTCCTCCCGATCCTCCTGCTGGCGTGGATCCGGATCGTCCCCGAGTCGCCCCGCTTCCTGCTCTCCCACGGGCGCGAGCGCGAGGCCCGCGAGTCCATCGCCTGGGCCCTGGAGCTGAGCCCCAACGACGTCGGAGCCCTGCCGCCGGTGCGGACCGGGCCGCGCATCGCCTACGGCGAGCTGCTGCGCAAGCACCTGCGGCCCCTGCTGATCGTCTCAGTCGGCTCCTTCTGCTTCATCCTGGGCTCCTTTACCGTGCAGTCCTGGGGGCAGACGCTCCTGGAGGTCGGCTTCACCGACATCGGCGCCGACGCCGTGGGGACGCTCTTCATGGGCGTCTCTCTGGTGGATCTGCTCGGGCGCCTGGCCTCGGCTTGGCTCGCCGACCGGATCGGGCGGCGCTGGACGTTGTTCTCCTTCGGGATCCTTGGGGCGCTCGGAGCGGTCATCGTGGCCTTCTCCGCCCACTGGGAGACCTCGTGGATCGTCTTCTTCACCGGCATCTGCCTCACGATGGGCTTCGGCGACGGCGCCTTCGGGATCCTCAACGCCTTCGGCGGCGAGCAGTTCCCCAACGACGCCCGGGGGACCGGCCTGGGCCTGGGCTACGGCATCGGCGCGAGCGCGAAGATCGTCGGGCCGCTGCTCATGGGGGCGATGATCGGCTCAGGCAGTCTTCAGGATCTGGCGCACCCGTTGGCGGCCGTCTTCCCGGCCTTCCTCTTCTTCGCGGCCATGCTGGTCCTGGGGGGCCTGGTCTACCTGCTGGCCCGTGAGACCAAGGGGGAGACCCTCGAGGACATCTGA","MGTARGRATPSVEHGSALEQIDSRPLTGHQRSIIALAIVANISEFFDMFLIGFAVVQLQKEWSLGGFETGVILACSGLGTVLGSVLWGRAADRMGRRRTFFWCVLLFTVFTLASVFTPTGWWMMLALLRVLVGVGVGGLNIVSIPYVQEFVPTRQRGLLAGLGSVFIPLGLFLGSLAQRLLHDNWRGLIALGVLPILLLAWIRIVPESPRFLLSHGREREARESIAWALELSPNDVGALPPVRTGPRIAYGELLRKHLRPLLIVSVGSFCFILGSFTVQSWGQTLLEVGFTDIGADAVGTLFMGVSLVDLLGRLASAWLADRIGRRWTLFSFGILGALGAVIVAFSAHWETSWIVFFTGICLTMGFGDGAFGILNAFGGEQFPNDARGTGLGLGYGIGASAKIVGPLLMGAMIGSGSLQDLAHPLAAVFPAFLFFAAMLVLGGLVYLLARETKGETLEDI$","Sugar transporter, permease protein","Membrane, Extracellular","Transport and binding proteins","sugar transporter; permease protein","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00216	$\"[316-333]?$	SUGAR_TRANSPORT_1
PS00217	$\"[131-156]?$	SUGAR_TRANSPORT_2

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[33-454]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[37-414]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR11600	$\"[18-460]T$	SUGAR TRANSPORTER
tmhmm	$\"[33-55]?$ $\"[69-87]?$ $\"[99-117]?$ $\"[127-147]?$ $\"[157-177]?$ $\"[183-205]?$ $\"[260-278]?$ $\"[292-312]?$ $\"[327-347]?$ $\"[353-375]?$ $\"[390-410]?$ $\"[429-449]?$	transmembrane_regions

InterPro
IPR001107
Family

Band 7 protein
PF01145	$\"[26-211]T$	Band_7
SM00244	$\"[25-202]T$	PHB

InterPro
IPR004851
Domain

Flotillin
PF03149	$\"[236-400]T$	Flotillin

noIPR
unintegrated

unintegrated
PTHR13806	$\"[25-338]T$ $\"[359-456]T$	FLOTILLIN-RELATED
PTHR13806:SF5	$\"[25-338]T$ $\"[359-456]T$	gb def: Putative secreted protein
signalp	$\"[1-21]?$	signal-peptide
tmhmm	$\"[5-25]?$	transmembrane_regions

","No hits to the COGs database.","***** IPB004851 (Flotillin) with a combined E-value of 9.2e-61. IPB004851A 71-103 IPB004851B 134-165 IPB004851C 166-213 IPB004851D 235-289 IPB004851E 359-410***** IPB002499 (Major vault protein, N-terminal) with a combined E-value of 2.8e-06. IPB002499M 320-371 IPB002499M 311-362 IPB002499M 300-351 IPB002499M 322-373 IPB002499M 331-382 IPB002499M 309-360 IPB002499M 302-353 IPB002499M 324-375 IPB002499M 296-347 IPB002499M 307-358","","","No significant hits to the PDB database (E-value < E-10).","Residues 26 to 211 (E_value = 7e-15) place ANA_2803 in the Band_7 family which is described as SPFH domain / Band 7 family.Residues 236 to 400 (E_value = 5.7e-09) place ANA_2803 in the Flotillin family which is described as Flotillin family.","","domain-band 7 family protein","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2804","3024314","3023811","504","5.38","-2.64","17459","GTGGGCGTCTTCGCCTGGTGCGCGATCATCGGCTGCACCGTCCTGGTGGCCGGCATCCTCTTCGACGGGCTGCTGGACGCCCTCCTGCCCGACGGGCTCGTGCCGATCCTCGCTCTGCCGGTGGCCGTGTTCGGCGCCATCGGCATGGGAGTGACGGCGACGACGGGCTCGGCCGCCACACAAGTACCGACGGCGGTGCTGTGGGGCGTTCCCTCCGCGGCGGCCGTTGCGTCCGGGGTGCTCATGCGCTGGCTGTGGAACCGGCTCAGGCGCTCCATGCCGTTGAACACGGCTCCGCCCACTGCCGCAGAGCTGGTCGGTGAGAAGGTCACCGTCCTGTGGTGGAAGGACGGCAGCGGCGAGGTTCGTGCCATCACGCGCGGCCACCAGCTCACCTTGCCGGCGCGCTCCGAGCAGCCGCTGCACTCGGGGCAGAGCGCCTGGGTGCTCGACGCCGTCGACTCCACCCTAGACATCACCCCCTGGGAGCAGATCAGCAGCTGA","VGVFAWCAIIGCTVLVAGILFDGLLDALLPDGLVPILALPVAVFGAIGMGVTATTGSAATQVPTAVLWGVPSAAAVASGVLMRWLWNRLRRSMPLNTAPPTAAELVGEKVTVLWWKDGSGEVRAITRGHQLTLPARSEQPLHSGQSAWVLDAVDSTLDITPWEQISS$","Hypothetical protein","Membrane, Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[4-24]?$ $\"[39-59]?$ $\"[65-85]?$	transmembrane_regions

noIPR
unintegrated

unintegrated
signalp	$\"[1-27]?$	signal-peptide
tmhmm	$\"[5-27]?$	transmembrane_regions

InterPro
IPR004006
Domain

Dak kinase
PF02733	$\"[37-362]T$	Dak1

InterPro
IPR012736
Domain

Dihydroxyacetone kinase DhaK, subunit 1
TIGR02363	$\"[22-358]T$	dhaK1: dihydroxyacetone kinase, DhaK subuni

InterPro
IPR013983
Domain

Aldehyde ferredoxin oxidoreductase, N-terminal
SM00790	$\"[44-181]T$	no description

noIPR
unintegrated

unintegrated
G3DSA:3.30.1180.20	$\"[208-362]T$	no description
G3DSA:3.40.50.10440	$\"[32-206]T$	no description

","BeTs to 4 clades of COG2376COG name: Dihydroxyacetone kinaseFunctional Class: G [Metabolism--Carbohydrate transport and metabolism]The phylogenetic pattern of COG2376 is ------y--d-lb-e--h---j----Number of proteins in this genome belonging to this COG is 3","***** IPB004006 (Dak kinase domain) with a combined E-value of 2.1e-84. IPB004006A 67-114 IPB004006B 120-160 IPB004006C 169-187 IPB004006D 235-245 IPB004006E 323-339","","","-57% similar to PDB:1OI2 X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI (E_value = 6.4E_75);-57% similar to PDB:1OI3 X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI (E_value = 6.4E_75);-57% similar to PDB:1UOD CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM E. COLI IN COMPLEX WITH DIHYDROXYACETONE-PHOSPHATE (E_value = 6.4E_75);-57% similar to PDB:1UOE CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM E. COLI IN COMPLEX WITH GLYCERALDEHYDE (E_value = 1.4E_74);-49% similar to PDB:2IU4 DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ (E_value = 2.6E_31);","Residues 37 to 362 (E_value = 1.5e-128) place ANA_2806 in the Dak1 family which is described as Dak1 domain.","","kinase ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2807","3027728","3028387","660","5.56","-5.59","21670","ATGACCGCAGAGGTGGGAGCCGCCCGCCACTCGCTGAGCGTGGCGGACCTGGCTACCTGGGTGCGCCGCAGCGCCGCACTCATCGCCGAGCACGCCGAGGAGCTCACCGACCTGGACGCCGCCATCGGTGACGCTGACCACGGCACCAACATGAAGCGCGGCCTGGCCGCCGCCGCCGAGGCTGTGGAGGCCGGTAGCTTCGCCAGCGCCGACGTCCTGCTCAAGAAGGTCGGCACCACCCTGGTCTCCACCGTCGGGGGCGCCTCCGGGCCCCTGTACGGCACCTTCTTCCTGCGAGCCGGGGGCGCCGTGGCCGGCCTGGAGGTACTCGACGCCCAGGCGCTCGCGGGCGCCCTGGAGGCCGGGGTCGGCGGCATTGCGGCGCGGGGGCGGGCCACCGCGGGGGAGAAGACCATGCTCGATGCCTGGAGCCCGGCCCTGGAGGCCCTGCGCGCCCATCCCGGCGACCTCGCCGCCGGTGTCGCGGCCGCCGTGCATGCGGCTGCCGAGGGGCGCGAGGCCACCAAGCCCATGGTGGCCACCAAGGGGCGGGCCTCCTACCTGGGAGAGCGCTCCGTGGGGCACATCGACCCCGGTGCCGCCTCCACGGTCCTGCTGCTGACAGCTCTCGACGACGTCGTGGCCGGGAGGGTGTCGTGA","MTAEVGAARHSLSVADLATWVRRSAALIAEHAEELTDLDAAIGDADHGTNMKRGLAAAAEAVEAGSFASADVLLKKVGTTLVSTVGGASGPLYGTFFLRAGGAVAGLEVLDAQALAGALEAGVGGIAARGRATAGEKTMLDAWSPALEALRAHPGDLAAGVAAAVHAAAEGREATKPMVATKGRASYLGERSVGHIDPGAASTVLLLTALDDVVAGRVS$","Dihydroxyacetone kinase, L subunit","Cytoplasm, Extracellular","Dihydroxyacetone kinase","DAK2 domain protein ","dihydroxyacetone kinase, L subunit","","","","","

InterPro
IPR004007
Domain

Dak phosphatase
PF02734	$\"[41-212]T$	Dak2

InterPro
IPR012737
Domain

Dihydroxyacetone kinase, subunit L
TIGR02365	$\"[17-212]T$	dha_L_ycgS: dihydroxyacetone kinase, L subu

noIPR
unintegrated

unintegrated
signalp	$\"[1-26]?$	signal-peptide

InterPro
IPR004701
Domain

Phosphotransferase system, fructose subfamily IIA component
PF03610	$\"[31-149]T$	EIIA-man
PS51096	$\"[30-163]T$	PTS_EIIA_TYPE_4

InterPro
IPR012844
Domain

Dihydroxyacetone kinase, subunit phosphotransferase
TIGR02364	$\"[31-156]T$	dha_pts: dihydroxyacetone kinase, phosphotr

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 31 to 149 (E_value = 1.4e-25) place ANA_2809 in the EIIA-man family which is described as PTS system fructose IIA component.","","ycgC ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2810","3029598","3028930","669","5.62","-4.07","23770","ATGCCTGCCCCGCTCTCGCGCACCGACTCCACGCTCGTCATCGGGCTGGGACGCTTCGGCTCGGCCGTGGCCGCCACCCTGGACCGCCTGGGGCGCGAGGTGCTGGCCGTGGAGGCCAATCCCGCGACCGTGCGGCAGTGGACCGGCCGCATCCCCCTGGTGGAGGCCGATGCCACGGACGTGGAGGCCCTCGAGCAGCTGGGCGCCACCGAGTTCGGCACCGCGGTCGTGGGGGTGGCGACCTCCCTGGAGACCTCCGTCCTCATCACCGGTAACCTCGTGGACCTCGAGACCCCCCAGATCTGGGCCAAGGCCATCTCCCGCGCCCACGGCCGCATCCTGCGCCGCATCGGCGCCCAGCACGTCGTCTACCCCGAGTTCGACGCCGGTCAGCGCGCCGCCCACCTCGTCTCGGGCCGCATGCTCGACTACATCGAGATGGAGAAGGGCGGCTTCACCATCGTCAAGATGCGTCCGCCCACGGAGCTGCACGGCTTCACCATCGGCCAGTCCAAGGTGCGCTCGCGCTACGGGATCACGGTCTTCGGTCTCATGAGCCCGGGCGAGCCGTTTGAGTACGCCACCCCGGACACCCTGGTCTCGGCCGAGGACGTACTCGTCGTCGGCGGGGACGCCGCCCTCCTGGAGCGTTTCGCCAACCGCGCGTGA","MPAPLSRTDSTLVIGLGRFGSAVAATLDRLGREVLAVEANPATVRQWTGRIPLVEADATDVEALEQLGATEFGTAVVGVATSLETSVLITGNLVDLETPQIWAKAISRAHGRILRRIGAQHVVYPEFDAGQRAAHLVSGRMLDYIEMEKGGFTIVKMRPPTELHGFTIGQSKVRSRYGITVFGLMSPGEPFEYATPDTLVSAEDVLVVGGDAALLERFANRA$","K+ transport system, NAD-binding component","Cytoplasm","trk system potassium uptake protein trkA","K03499 trk system potassium uptake protein TrkA","TrkA-N domain protein","","Anantharaman V., Koonin E.V., Aravind L. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J. Mol. Biol. 2001. 307(5):1271-1292. PMID: 11292341","","","

InterPro
IPR003148
Domain

TrkA-N
PF02254	$\"[11-125]T$	TrkA_N
PS51201	$\"[10-131]T$	RCK_N

InterPro
IPR006037
Domain

TrkA-C
PS51202	$\"[142-222]T$	RCK_C

noIPR
unintegrated

unintegrated
G3DSA:3.40.50.720	$\"[9-137]T$	no description
signalp	$\"[1-24]?$	signal-peptide

","BeTs to 10 clades of COG0569COG name: K+ transport systems, NAD-binding componentFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0569 is aom-kz-qvdrlbcefgh-nu---twNumber of proteins in this genome belonging to this COG is 3","No significant hits to the Blocks database.","","","-56% similar to PDB:1LSU KTN Bsu222 Crystal Structure in Complex with NADH (E_value = 3.6E_18);-56% similar to PDB:2HMS Rectangular-shaped octameric ring structure of an RCK domain with NADH bound (E_value = 3.6E_18);-56% similar to PDB:2HMT Diamond-shaped octameric ring structure of an RCK domain with NADH bound (E_value = 3.6E_18);-56% similar to PDB:2HMU Diamond-shaped octameric ring structure of an RCK domain with ATP bound (E_value = 3.6E_18);-56% similar to PDB:2HMV Diamond-shaped octameric ring structure of an RCK domain with ADP bound (E_value = 3.6E_18);","Residues 11 to 125 (E_value = 1.2e-28) place ANA_2810 in the TrkA_N family which is described as TrkA-N domain.","","system potassium uptake protein trkA","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2811","3031234","3029639","1596","9.71","13.24","55845","ATGACGCTCACAGCGACATCCCCCCTCAAGCAGGCCGAACCGGCACAGGAGACACAGGAGGAGACTCCCGCGGCCGTACAGCGGCCCAATCGACGCGCGGTCATGGTCAGCGCCGTCCTCACCCAGCTGATGATCGTCCTGGACCTGACGATCATCGCCATCGCCCTGCCGCACATGCAGGTGGACCTGGGGATGAACGTGTCCCAGAGCCCATGGACGGTCACCGGCTACAGCCTGGCCTTCGGAGGCCTCGTGCTCTTCGGGGGAAGGCTCTGCGCCGTGGTCGGTATCCGACGCTCGTACCAAGTCGGGCTGATCGGATTCGGGATCGCCAGCCTCGCAGCCGGGATGGCGACCTCCTTCTCCGTCCTGCTGGCGGCCCGCGTGGCCCAGGGCTGCTTCGGCGCCCTGCTGGCCCCCACCTCACAGTCACTGCTCAATGTCACCTTCACCGAGCGTGCCGAGCGCGAGCGGGTCTTCGCGATCTTCGGCGCCACTGGCGGCCTGGGAGCGGCTGTCGGACTGCTTGTCGGCGGAGCACTGACCGACTGGTTCAGCTGGCGCTGGGCCCTCTACATCAACATCTTCCTGGCCGCCGCCGCCCTGCTCATCGGGCAGCGCAGCCTTCCGCCGGCCGACCAGCGCGACCGCGGCTCACGCATCACTGATGACCTGAGCGGCCTGGTCCTGGGCTGCGGAGCCTGCTTCAGCGCCGTCTACGGGCTCGACCGGGCCCAGCAGACCTCCTGGACCTCCACGTCGACCGTCAGCTGGCTGGCGCTGGGCGGCATCGCCGCGGCGCTGTTCGTGGTCCGTGAGCGTTTCGCGAATCGACCGGTGCTGCCCCTGTCGATGATGGCGCTGCCGGTGCGGGCGGCCTCCTACGCCACGCAGTTCATCACCGGCGCCGCCCAGATGGGGGCGATCATCTACCTGACCTACTACATGCAGAACCACTTCGGCTACTCGCCCCTCAAGAGCGGGGTCGTCTTCCTCCCGATGGTCCTTGCGTTGATCGCCACCGCGATCCCGGCCGGGCGCATCATCGTGCCCAGGCTCGGGGCGCGCGGCACCCTGCCACTGGGGCTGGCAGTGTTGGCGGGATCCTTCCTCATCTTCTCCCTCATGACCACGGAATCGACTTACGAGCACGTGGCACTGCCCGGCCTCATCGTCTTCGGGATGGGCCTGGGGCTGACGATGCCGGTCACCTTCAACTCAGGAACCCGCGGAGTGGACTCCACGCGTACCGGGCTGGCCTCGGCAATTCTGAGCGCCGCTCAGCAGATCGGTGGCTCCTTCGGGGTGGCTCTCATGACCTCCTACGCCACCCAGCACGCCGAGGACTACGTGACTGACCACGCCGCGGGGGTCAAGGCCACAGCCATGGAGGCGATGATGCGGGCCCACACCCTGCCGCAGTCACCTGCTGGAAAGCAGATCATCGAGGCGCTCAAGGCCCAGCTCATCGACCGGGCGCAGGTCGACGCCTATGCAGGAGGATTCGCGGTGATGGCCTGGATCCTGGCCGGGGCGGCGACGGTCCTGGTGGCCTGCGGGATCGGCCTGAGCCTCCGCCGACGCCGCAGGAGGTAG","MTLTATSPLKQAEPAQETQEETPAAVQRPNRRAVMVSAVLTQLMIVLDLTIIAIALPHMQVDLGMNVSQSPWTVTGYSLAFGGLVLFGGRLCAVVGIRRSYQVGLIGFGIASLAAGMATSFSVLLAARVAQGCFGALLAPTSQSLLNVTFTERAERERVFAIFGATGGLGAAVGLLVGGALTDWFSWRWALYINIFLAAAALLIGQRSLPPADQRDRGSRITDDLSGLVLGCGACFSAVYGLDRAQQTSWTSTSTVSWLALGGIAAALFVVRERFANRPVLPLSMMALPVRAASYATQFITGAAQMGAIIYLTYYMQNHFGYSPLKSGVVFLPMVLALIATAIPAGRIIVPRLGARGTLPLGLAVLAGSFLIFSLMTTESTYEHVALPGLIVFGMGLGLTMPVTFNSGTRGVDSTRTGLASAILSAAQQIGGSFGVALMTSYATQHAEDYVTDHAAGVKATAMEAMMRAHTLPQSPAGKQIIEALKAQLIDRAQVDAYAGGFAVMAWILAGAATVLVACGIGLSLRRRRRR$","Transmembrane efflux protein","Membrane, Cytoplasm","Puromycin resistance protein pur8","transmembrane efflux protein","major facilitator superfamily MFS_1","","Pao S.S., Paulsen I.T., Saier Jr M.H. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 1998. 62(1):1-34. PMID: 9529885Walmsley A.R., Barrett M.P., Bringaud F., Gould G.W. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 1998. 23(12):476-481. PMID: 9868370","","","

InterPro
IPR007114
Family

Major facilitator superfamily
PS50850	$\"[34-529]T$	MFS

InterPro
IPR011701
Family

Major facilitator superfamily MFS_1
PF07690	$\"[38-444]T$	MFS_1

noIPR
unintegrated

unintegrated
PTHR10074	$\"[10-223]T$ $\"[277-446]T$ $\"[501-531]T$	MAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57	$\"[10-223]T$ $\"[277-446]T$ $\"[501-531]T$	DRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
tmhmm	$\"[36-56]?$ $\"[75-95]?$ $\"[97-115]?$ $\"[121-139]?$ $\"[160-180]?$ $\"[184-204]?$ $\"[225-243]?$ $\"[253-271]?$ $\"[292-314]?$ $\"[328-348]?$ $\"[357-375]?$ $\"[385-405]?$ $\"[420-440]?$ $\"[503-525]?$	transmembrane_regions

InterPro
IPR001647
Domain

Bacterial regulatory protein, TetR
PR00455	$\"[13-26]T$ $\"[34-57]T$	HTHTETR
PF00440	$\"[13-60]T$	TetR_N
PS50977	$\"[7-67]T$	HTH_TETR_2

InterPro
IPR012287
Domain

Homeodomain-related
G3DSA:1.10.10.60	$\"[6-60]T$	no description

","BeTs to 14 clades of COG1309COG name: Transcriptional regulatorFunctional Class: K [Information storage and processing--Transcription]The phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is 18","***** IPB001647 (Bacterial regulatory protein TetR, HTH motif) with a combined E-value of 3.4e-12. IPB001647 13-55***** IPB013573 (Tetracycline transcriptional regulator YcdC-like, C-terminal) with a combined E-value of 1.8e-06. IPB013573B 35-76","","","No significant hits to the PDB database (E-value < E-10).","Residues 13 to 60 (E_value = 9.9e-15) place ANA_2812 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family.","","regulator (TetR-AcrR family), putative","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2813","3033737","3032115","1623","9.83","13.04","57451","ATGGCGACCGTGCCCCAGACAGACACCGCTCAGGAGCCGGAGCCCGGCCGCGGATCCCGCGGCGAGACCCCGACCGGGAAGCGCGGCGCCTCCCAGGCCGGCAGGCGCCGTCAGGCCCACTGGCACGCCCCGCTCGTGGGCGTCGTCGGCCATGCGTGGAAGCGCCACAAGAAGCCCCCGAATTCCAAAGAGGGAGCCGGCCTCCTCGAGGAGCCATCGCCTCTCCCCCAGCTGCCGGGTACGGAGCCCACCGGGATTCGCCGACTGCTTCGGCACATCGAGCCACTCAGCCAGATCGCGCGGGCCGCCCGCTTCTACCCGGCCCGGCTGGCCGTGATCGTCTTCGCGGCCATCATCGTGGTGGTGACCGGCCTCCTCAGCCTCCCCATCGCCACGACCAGTGGGGAGCACGCCGACTTCCTCGACGCCTTGTTCACCGCCACCTCGGCCGTGTGCGTCACCGGCCTGAGCACGGTGGACACGGCTGCCTACTGGTCCACCTTCGGGCACGTCGTCATCATCCTGGCCGCGGCCGTGGGCGGTCTGGGAGTCATGACCCTGGCCTCCCTGCTGTCCCTGGCGGTGTCCCGGCACGTGGGACTGACTCAGCGGATGCTGGCGGCCTCGGAGAACCAGTCGCGCCTGGGTGAAGTGGGGCGGCTGCTGCGCGCCGTCATCTACACGGCCGCCGGCTGCGAGCTCCTCCTGACGCTCATGCTGCTGCCACCCTTCCTCAGCCATGGCCTCGATGTGGGCCACGCCCTGTGGTACGCGGTCTTCATGGCACTGTCGATCTTCAACAACGCCGGCTTCGTCATCATGCCCGAGGGCCTGGAGGCCTACTCCACCGACTGGTGGATCGGCCTGCCGATCATCCTGGGGACCTTCATGGGCGCCGTCGGCTTCCCCGTCATCCTGGACATCATGGGCCGACGCCGCCGCCCCCGCACGTGGAGCCTGCACACCAAGCTGACCCTGACGACCTACCTGGCCCTCACTCTCGCCTCGACCATCGCCATCGCCACCTTCGAGTGGAACAACCCGCTCACCTACGGCTCCCTGCCCACGAGCGGAAAGATCATGACCGCGCTCGTCAACGGCGTCAACGCCCGCTCCTCGGGGCTGTCCACGATCCCGCCCGAGCACATGCACGAGGCGACCTGGTTCCTTCAGGACGCCCTTATGTTCGTCGGGGGCGGCTCGGCCTCGACGGCCGGCGGCATCAAGGTGACGACCTTCGCGGTCCTGCTGCTGGCGATTCTCGCCGAGGCCCGGGGCGACCAGGACATCGAGGCCTTCGGGCGGCGCATCACCCCCTCGACCGTGCGCCTGAGCGTGGCGGTGGCCTTCATCGGCTCCAGCATCATCGGTCTGGCCACGCTCCTGCTGCTGCAGATGACCAACCTGTCCCTGGACCGGATCCTCTTCGAGGTCATCAGCGCCTTCGCGACCGTGGGCCTGTCCACGGGCATCACGCCCTCCCTGCCGGACGGGGCCAAGTACGTCATCGTGGCGCTCATGTTCGTCGGCCGTGTGGGCACGATGACGGCGGCCAGCGCCCTGGCGCTGCGCGAGCGGCGCCGCGTTATCCGGATGCCCGAGGCCAGCCCGATGATCGGCTGA","MATVPQTDTAQEPEPGRGSRGETPTGKRGASQAGRRRQAHWHAPLVGVVGHAWKRHKKPPNSKEGAGLLEEPSPLPQLPGTEPTGIRRLLRHIEPLSQIARAARFYPARLAVIVFAAIIVVVTGLLSLPIATTSGEHADFLDALFTATSAVCVTGLSTVDTAAYWSTFGHVVIILAAAVGGLGVMTLASLLSLAVSRHVGLTQRMLAASENQSRLGEVGRLLRAVIYTAAGCELLLTLMLLPPFLSHGLDVGHALWYAVFMALSIFNNAGFVIMPEGLEAYSTDWWIGLPIILGTFMGAVGFPVILDIMGRRRRPRTWSLHTKLTLTTYLALTLASTIAIATFEWNNPLTYGSLPTSGKIMTALVNGVNARSSGLSTIPPEHMHEATWFLQDALMFVGGGSASTAGGIKVTTFAVLLLAILAEARGDQDIEAFGRRITPSTVRLSVAVAFIGSSIIGLATLLLLQMTNLSLDRILFEVISAFATVGLSTGITPSLPDGAKYVIVALMFVGRVGTMTAASALALRERRRVIRMPEASPMIG$","Trk-type K+ transport system, membrane component","Membrane, Cytoplasm, Extracellular","Trk-type K+ transport systems, membranecomponents","cation transporter","H(+)-transporting two-sector ATPase","","Schlosser A., Meldorf M., Stumpe S., Bakker E.P., Epstein W. TrkH and its homolog, TrkG, determine the specificity and kinetics of cation transport by the Trk system of Escherichia coli. J. Bacteriol. 1995. 177(7):1908-1910. PMID: 7896723","","","

InterPro
IPR003445
Family

Cation transporter
PF02386	$\"[209-526]T$	TrkH

noIPR
unintegrated

unintegrated
tmhmm	$\"[110-130]?$ $\"[144-166]?$ $\"[171-191]?$ $\"[224-244]?$ $\"[254-274]?$ $\"[288-308]?$ $\"[323-343]?$ $\"[349-369]?$ $\"[444-464]?$ $\"[501-523]?$	transmembrane_regions

","BeTs to 17 clades of COG0168COG name: Trk-type K+ transport systems, membrane componentsFunctional Class: P [Cellular processes--Inorganic ion transport and metabolism]The phylogenetic pattern of COG0168 is aom-kzyqvd-lbcefgh-nu---twNumber of proteins in this genome belonging to this COG is 1","***** IPB003445 (Cation transporter) with a combined E-value of 5.8e-07. IPB003445B 476-488 IPB003445B 145-157","","","No significant hits to the PDB database (E-value < E-10).","Residues 209 to 526 (E_value = 1.9e-60) place ANA_2813 in the TrkH family which is described as Cation transport protein.","","K+ transport systems, membrane components","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2814","3033920","3034267","348","8.06","1.83","12247","GTGGTAAATGGGGCCCGAGAAACCCTGTGCGAAGGCTGGTGCGGGGATATATTGGCTGTGTTCCTGCCCCGACGGGGCCACCCGCGACGAACGGACCTCAAGCTCATGGCACCGGGCCTTCCCACATCCCCCAGCGCCTCCGGCGCCCCCTCGTTCCTCACCGTGGCTGAGGTGGCGGCGATGCTGCGCGTGTCCAAGATGACCGTCTACCGGATGGTGCACTCCGGCGACCTGCCCGCGATGCAGGTCGGACGCTCCTTCCGCGTCCCCGAGCGCGCCGTTCACGACTACCTGTCCGCCGGGCTGGGTGACTGGGGCCACGACGCGTCAGAGGCATCAGGGTCCTAG","VVNGARETLCEGWCGDILAVFLPRRGHPRRTDLKLMAPGLPTSPSASGAPSFLTVAEVAAMLRVSKMTVYRMVHSGDLPAMQVGRSFRVPERAVHDYLSAGLGDWGHDASEASGS$","Excisionase/Xis, DNA-binding","Cytoplasm, Extracellular","DNA binding domain, excisionase family protein","hypothetical protein","DNA binding domain, excisionase family","","","","","

InterPro
IPR010093
Domain

Excisionase/Xis, DNA-binding
TIGR01764	$\"[52-100]T$	excise: DNA binding domain, excisionase fam

noIPR
unintegrated

unintegrated
PD053214	$\"[50-98]T$	Q82H37_STRAW_Q82H37;

InterPro
IPR013177
Domain

Protein of unknown function DUF1713, mitochondria
PF08213	$\"[1-32]T$	DUF1713

","No hits to the COGs database.","No significant hits to the Blocks database.","","","No significant hits to the PDB database (E-value < E-10).","Residues 1 to 32 (E_value = 0.0028) place ANA_2815 in the DUF1713 family which is described as Mitochondrial domain of unknown function (DUF1713).","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2816","3034544","3035920","1377","4.98","-15.59","47403","GTGCACACTACTGGTGTGAGCGGGGCCCTGCTTGTCTCACGAGGAACCGATCAGGAAGAGCGGAGACCTCCGTTGACCACTACCCCAGATGACCGCACTCCTGCTGCCCCCGCTGAGGGATCGACGGTGCCGGCTGCGCCGTCGGCCGAGCCGCAGCTGGTGGCAGGCGACTGCACCGTTCCGCTGAGCGTCGACGTCGACCCGTCCGCCTGGCCCGCACCTGTCCAGGCCCTGGCGCACACGCCCGGCTCCGGCGCCCGGCCGACCAGCCTGGCCGAGCTGACGACGCTTCGCGTGGGCGGCCCGGTGGGCAGCTACGTCGAGGCCACCACGCAGAGCGAGCTGACCGAGGCGATCCGCGAGGCCGACGCCGCCGGTACGCCCGTCCTCGTCATCGGCGGCGGCTCCAACATCCTGGCCTCCGATGCCGGCTTCGACGGGCTCGTCATCCGGGATGCCCGCGCCGAGGTCTCACTCGTCTCGGACTCGGTGTGCGGCGGCGTCGAGGTCACTGCCACCGCCGGAACCACCTGGGACGACCTGGTGCGCGAGGCCATCGCCAGCCAGTGGGCCGGGTTCGCGCCCCTGTCCGGGATCCCCGGCACGGTGGGCGCCGCCCCCGTGCAGAACATCGGGGCCTACGGCGCCGAGGTCGCCGAGCTCATTGCCAGCGTGCGTGCCTGGGACCGACTGCGCAACCGGGTGGTCTGGCTGGCCCTGGGCGAGCTGGGGCTGGCCTACCGGGACTCGCGTCTCAAGCAGTCCCTCACCGACACCGAGGTGGGTGGCGGGCGCCTGTGGGGGCCGACCGGGCGCTGGGTGGTCCTCGACGCCACCTTCGCCGTGCGGCAGGGCTCCCTGTCCTCCCGGATCGCCTACTCCCAGCTGGCCGGGGCGCTCGGCGTCGAGCTGGGTGAGCGCGTGCCCGAGCGCGAGCTGCGTGAGGCGGTTCTTGAGCTGCGCCGCTCCAAGGGGATGGTGCTGGACGGCGCCGACCACGACACCTGGTCGGCCGGCTCCTTCTTCACCAACCCGATCCTGACCACGGAGCAGGCCGAGCAGCTGCCCGAGGACGCGCCGCGCTTCCCGGTCACCGACCACTCGCAGGTGGTGCTCGGCACCAAGGCCGCCCCTGTCATCGAGGGGTTGGTCAAGACCAGTGCCGCCTGGCTCATCGACCACGCCGGCTTCAGCAAGGGCTTCGCCGTGGAGGCCGGCGCACCGGCCGGGTTGTCCACCAAGCACGTGCTGGCACTGACCAACCGGGGCGGCGCGACCGGGGCGGACCTGGCGCGCCTGCGTGACGCGGTGGTGGCCGGAGTGCGTGAGCGCTACGGCGTCACTCTCGTACCCGAGCCCGTTCAGGTCGGTTTCTAG","VHTTGVSGALLVSRGTDQEERRPPLTTTPDDRTPAAPAEGSTVPAAPSAEPQLVAGDCTVPLSVDVDPSAWPAPVQALAHTPGSGARPTSLAELTTLRVGGPVGSYVEATTQSELTEAIREADAAGTPVLVIGGGSNILASDAGFDGLVIRDARAEVSLVSDSVCGGVEVTATAGTTWDDLVREAIASQWAGFAPLSGIPGTVGAAPVQNIGAYGAEVAELIASVRAWDRLRNRVVWLALGELGLAYRDSRLKQSLTDTEVGGGRLWGPTGRWVVLDATFAVRQGSLSSRIAYSQLAGALGVELGERVPERELREAVLELRRSKGMVLDGADHDTWSAGSFFTNPILTTEQAEQLPEDAPRFPVTDHSQVVLGTKAAPVIEGLVKTSAAWLIDHAGFSKGFAVEAGAPAGLSTKHVLALTNRGGATGADLARLRDAVVAGVRERYGVTLVPEPVQVGF$","UDP-N-acetylmuramate dehydrogenase","Membrane, Cytoplasm","UDP-N-acetylenolpyruvoylglucosamine reductase(UDP-N-acetylmuramate dehydrogenase)","UDP-N-acetylmuramate dehydrogenase ","UDP-N-acetylmuramate dehydrogenase","","Fraaije M.W., Van den heuvel R.H., van Berkel W.J., Mattevi A. Structural analysis of flavinylation in vanillyl-alcohol oxidase. J. Biol. Chem. 2000. 275(49):38654-38658. PMID: 10984479","","","

InterPro
IPR003170
Family

UDP-N-acetylenolpyruvoylglucosamine reductase
PTHR21071	$\"[63-252]T$	UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE

InterPro
IPR006094
Domain

FAD linked oxidase, N-terminal
PF01565	$\"[103-239]T$	FAD_binding_4

InterPro
IPR011601
Domain

UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal
PF02873	$\"[310-457]T$	MurB_C

noIPR
unintegrated

unintegrated
G3DSA:3.30.43.10	$\"[90-156]T$	no description
G3DSA:3.30.465.10	$\"[158-325]T$	no description
G3DSA:3.90.78.10	$\"[330-457]T$	no description

","BeTs to 16 clades of COG0812COG name: UDP-N-acetylmuramate dehydrogenaseFunctional Class: M [Cellular processes--Cell envelope biogenesis, outer membrane]The phylogenetic pattern of COG0812 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 1","***** IPB003170 (UDP-N-acetylenolpyruvoylglucosamine reductase) with a combined E-value of 9.4e-53. IPB003170A 131-140 IPB003170B 170-220 IPB003170C 233-253 IPB003170D 336-345 IPB003170E 402-453","","","-44% similar to PDB:1MBB OXIDOREDUCTASE (E_value = 6.1E_12);-44% similar to PDB:1MBT OXIDOREDUCTASE (E_value = 6.1E_12);-44% similar to PDB:1UXY MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE (E_value = 6.1E_12);-44% similar to PDB:2MBR MURB WILD TYPE, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE (E_value = 6.1E_12);-40% similar to PDB:1HSK CRYSTAL STRUCTURE OF S. AUREUS MURB (E_value = 7.4E_10);","Residues 103 to 239 (E_value = 9.7e-19) place ANA_2816 in the FAD_binding_4 family which is described as FAD binding domain.Residues 310 to 457 (E_value = 1.5e-20) place ANA_2816 in the MurB_C family which is described as UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain.","","reductase (UDP-N-acetylmuramate dehydrogenase) (murB)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2817","3037313","3036195","1119","5.48","-9.91","39713","ATGCGAGACCTCGCCACCCTCCCCAAGGCGCACCTGCACCTGCACTTCACGGGGTCGATGCGCCTGGAGACCCTCATCGAGTTGGCCTCCAGCGCGCGCACGCGCCTGCCCTCGAACTTCCTGGACGGCGACCCCCTGCGTGTCCCCGCCGATCGACGCGGCTGGTTCCGCTTCCAGCGCGCCTATGACACGGCCCGGGCCCTGGTGCGCACGGAGGAGGTCATGCGCCGCATTGTCCTGGAAGCTGCCCTGGATGACGCCGCCGAGGGCTCGCGCCGCCTGGAGATCCAGGTCGACCCGACCAGCTACGCCCCCTTCGTCGGCGGGATCACCCCCGCCTTGGAGATCATCCTCGATGCCGCCAAGCAGGCCACGACCCTGAGCGGGGTGGAGGTGGCGGTCATCGTGGCGGCCTCCCGGATGCGTCACCCGTTGGACGCCCGCACGCTCGCGCGCCTGGCGGTGCGCTACGCCGGAGACCAGCCGGGCGAGGTGATCGGCTTCGGCCTGTCCAACGATGAGCGCGCCGGGCAGACCTCCTCCTGGGAGCGGGCCTTCGCCATCGCCCGCCGGGGTGGCCTGGCCTCCATGCCTCACGGAGGGGAGCTCTTAGGGCCCGACCACCTGCGCGAGGTCGTCTCCTCCCTCGGCCCCACACGCCTGGGCCACGGGGTTCGCGCCGGTGAGGACCCCGCCCTGCTGGACGCGATCGTCGCTTCCGGCATCAGCCTCGAGGTCTGCCCCGCCTCCAACGTGAGCCTGGGGGTCTATCACAGCCCCGACGACGTCCCCCTGCGTACGCTCATGAGCCACGGAGCCCAAATCGCCCTGAGCGCCGACGACCCCCTGCTCTTCCAGTCCCGGCTCGTCGACCAGTACGAGATCGCCCGGGCCCTGGGCTGCGACGACGCCGAGCTGGCCGAGCTGGCCCGCGGCTCGATCCGCGCCTGCCTGGCCTCCCCGACGGCGAAGCAGACCTGGTTGGCCGAGGTGGACGCCTGGCTGGCGGCGCCCGACCAGGCTCCAGGAGTGCAGTCCGACAGCCCGGAGGCCGGCGACCTCGAGTCTCGCGCGGTTGCGCGCTATGGGCTAGAACCGGCAGCGAGCACGCCCGGATAA","MRDLATLPKAHLHLHFTGSMRLETLIELASSARTRLPSNFLDGDPLRVPADRRGWFRFQRAYDTARALVRTEEVMRRIVLEAALDDAAEGSRRLEIQVDPTSYAPFVGGITPALEIILDAAKQATTLSGVEVAVIVAASRMRHPLDARTLARLAVRYAGDQPGEVIGFGLSNDERAGQTSSWERAFAIARRGGLASMPHGGELLGPDHLREVVSSLGPTRLGHGVRAGEDPALLDAIVASGISLEVCPASNVSLGVYHSPDDVPLRTLMSHGAQIALSADDPLLFQSRLVDQYEIARALGCDDAELAELARGSIRACLASPTAKQTWLAEVDAWLAAPDQAPGVQSDSPEAGDLESRAVARYGLEPAASTPG$","Adenosine deaminase","Cytoplasm","adenosine deaminase","adenosine deaminase ","adenosine deaminase","","Skarstad K., Boye E. The initiator protein DnaA: evolution, properties and function. Biochim. Biophys. Acta 1994. 1217(2):111-130. PMID: 8110826Yoshikawa H., Ogasawara N. Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial replication origins. Mol. Microbiol. 1991. 5(11):2589-2597. PMID: 1779750Georgopoulos C. The E. coli dnaA initiation protein: a protein for all seasons. Trends Genet. 1989. 5(10):319-321. PMID: 2558436Skovgaard O. Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli. Gene 1990. 93(1):27-34. PMID: 2172087","","","

InterPro
IPR001365
Domain

Adenosine/AMP deaminase
PTHR11409	$\"[114-334]T$	ADENOSINE DEAMINASE
PF00962	$\"[6-330]T$	A_deaminase

InterPro
IPR006330
Family

Adenosine deaminase
TIGR01430	$\"[7-331]T$	aden_deam: adenosine deaminase

InterPro
IPR006650
Active_site

Adenosine/AMP deaminase active site
PS00485	$\"[276-282]?$	A_DEAMINASE

InterPro
IPR013159
Domain

Chromosomal replication initiator, DnaA C-terminal
SM00760	$\"[113-176]T$	no description

InterPro
IPR013838
Binding_site

Beta tubulin, autoregulation binding site
PS00228	$\"[1-4]?$	TUBULIN_B_AUTOREG

noIPR
unintegrated

unintegrated
G3DSA:3.20.20.140	$\"[4-336]T$	no description
PTHR11409:SF21	$\"[114-334]T$	ADENOSINE DEAMINASE

","BeTs to 6 clades of COG1816COG name: Adenosine deaminaseFunctional Class: F [Metabolism--Nucleotide transport and metabolism]The phylogenetic pattern of COG1816 is ------y---rl--efg----j--t-Number of proteins in this genome belonging to this COG is 1","***** IPB006650 (Adenosine/AMP deaminase active site) with a combined E-value of 2.8e-22. IPB006650A 8-18 IPB006650C 196-209 IPB006650D 216-251 IPB006650E 275-285","","","-43% similar to PDB:1A4L ADA STRUCTURE COMPLEXED WITH DEOXYCOFORMYCIN AT PH 7.0 (E_value = 1.5E_18);-43% similar to PDB:1A4M ADA STRUCTURE COMPLEXED WITH PURINE RIBOSIDE AT PH 7.0 (E_value = 1.5E_18);-43% similar to PDB:1ADD A PRE-TRANSITION STATE MIMIC OF AN ENZYME: X-RAY STRUCTURE OF ADENOSINE DEAMINASE WITH BOUND 1-DEAZA-ADENOSINE AND ZINC-ACTIVATED WATER (E_value = 1.5E_18);-43% similar to PDB:2ADA ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS (E_value = 1.5E_18);-43% similar to PDB:1FKW MURINE ADENOSINE DEAMINASE (D295E) (E_value = 4.4E_18);","Residues 6 to 330 (E_value = 1e-72) place ANA_2817 in the A_deaminase family which is described as Adenosine/AMP deaminase.","","deaminase (add)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2819","3038232","3037492","741","9.59","9.23","26557","GTGAGCTGTGGACACGCGATGAAGCACTACGGCATCCCGCTGAGGACATCACCCGGTGTTCTCCATGTCGCCATCCCAGCGCAGCGAAGCCGCGTTCCCAATGCAATCGGCCGCACGGTTGTCCACCGCGTCAGGGGACTGGCCCTGCCCGAGGACACTCAGCCACCAGTGGCGCAGGTCGAGCAGGCTCTCATCTGCTTCATGCGCTGCGCCGACGAGCTCGACGCCCTCATCGCACTCGACGCGGCCCTGCGCCTGGGATACACAACCCGCAGTCAGCTGGAATCCGCGTTGCCGGGCCCGCGCAACGCACCGCTGCGCTCCCTACTCTCCCAGGCCCGCCCGGGGGCGCGCTCCCTGCTGGAGACGATCGCCCGCTACGACCTGAAGCGGGCCGGCTACCGCCCCGTCGCGGCGGTCATGGTGGACGGGGTCGGCGAGGTGGATCTGGTGCTCAGCCGAAGGCCTCAGGCGATCGTTCCCGGGCCGGCGAACGGCACTCATGTCCTCACCGCAGCGGCCTGCCCGGCCCTGCTCATCGAGACGGACGGCTACACCTACCACTCCTCCCGCCCGGACTGGCACAGCGACCACCTGCGCGATCAGGCCGCTCTCGCGCGCGGCCACACTCCGCTACGCCTCACCAGCAACCAGGTAGTGGATCGGGAGACGGTGCGGATCGTCTCTTCGGTGGCGCGCCGTCTCGGAATCCACCCGAATGTCACTCCTGGCGACTTTTAG","VSCGHAMKHYGIPLRTSPGVLHVAIPAQRSRVPNAIGRTVVHRVRGLALPEDTQPPVAQVEQALICFMRCADELDALIALDAALRLGYTTRSQLESALPGPRNAPLRSLLSQARPGARSLLETIARYDLKRAGYRPVAAVMVDGVGEVDLVLSRRPQAIVPGPANGTHVLTAAACPALLIETDGYTYHSSRPDWHSDHLRDQAALARGHTPLRLTSNQVVDRETVRIVSSVARRLGIHPNVTPGDF$","Hypothetical protein","Cytoplasm","hypothetical protein","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-44% similar to PDB:1O94 TERNARY COMPLEX BETWEEN TRIMETHYLAMINE DEHYDROGENASE AND ELECTRON TRANSFERRING FLAVOPROTEIN (E_value = );-44% similar to PDB:1O95 TERNARY COMPLEX BETWEEN TRIMETHYLAMINE DEHYDROGENASE AND ELECTRON TRANSFERRING FLAVOPROTEIN (E_value = );-44% similar to PDB:1O96 STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FOR METHYLOPHILUS METHYLOTROPHUS. (E_value = );-44% similar to PDB:1O97 STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FROM METHYLOPHILUS METHYLOTROPHUS, RECOGNITION LOOP REMOVED BY LIMITED PROTEOLYSIS (E_value = );-43% similar to PDB:2GOU Structure of wild type, oxidized SYE1, an OYE homologue from S. oneidensis (E_value = );","No significant hits to the Pfam 21.0 database.","","protein ","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2820","3041466","3040165","1302","5.48","-9.90","46073","GTGTACCGGAGGCTCCCCGGCGTCGTCACTGGCGGATCCGACGTGTTTCAGACGCACGGATGTCGCTGGTCGTGGGACCATGGTCGGGTGACACCTGCACCCACGCACCGCGTTTCCGCCCGACTGTCCGCCATCGCCCCCTCCGCCACCCTGGCCGTCGACGCCAAGGCCAAGGCCCTCAAGGCCGCCGGCCGCCCCGTCATCGGCTTCGGCGCCGGAGAGCCCGACTTCCCCACCCCCGACTACATCGTTGAAGCCGCCGTCGCCGCCGCGAAGGACCCGGCCAACCACAAGTACTCCCCCGCCAAGGGCCTGCCGGTCCTGCGCGAGGCCATCGCCGCCAAGACGCTGCGCGACTCCGGCTACGAGGTCTCCCCCGACGACATCCTGGTCACCAACGGCGGCAAGCAGGCCGTCTTCCAGGCCTTCGCCGCACTCGTCGACCCCGGCGACGAGGTCCTCCTGCCCGCGCCCTACTGGACCACCTACCCCGAAGCCGTCGCCCTGGCCGGGGGGACCACGGTCGAGGTCTTCGCCGGGGCCGACCAGGACTACAAGGTCAGCGTCGACCAGCTCGAGGCCGCCCGCACCGAGCGCACCAAGGTGCTACTGCTGTGCTCGCCGTCGAACCCGACCGGCTCGGTCTACACGCCCGAGGAGCTCACCGCCATCGGCCAGTGGGCCCTGGAGCACGGGATCTGGGTCATCACCGACGAGATCTACGAGCACCTCCTCTACGACGGCGCCCAGACCGCGCACGTCGTCAAGCTGGTTCCCGAGCTGGCCGACCAGACGATCGTCCTCAACGGCGTGGCCAAGACCTACGCCATGACCGGATGGCGCGTGGGCTGGATGATCGCTCCCAGCGACGTCATCAAGGCGGCCACGAACTTCCAGTCGCACCTGACCTCCAACGTCGCCAACGTCTCACAGCGCGCGGCACTGGCGGCCGTCAGCGGCGACCTGACCGCCGTCGAGCAGATGCGCACCGCCTTCGACCGGCGCCGGCGCACGATGGTGGAGATGCTCTCGCAGATCGAGGGGCTGACCGTGCCCGTGCCCCGCGGCGCCTTCTACGCCTACCCCAGCATCGAGGGGCTCGTGGGACGCACGCTGCGCGGCACCACGATCGACAGCTCAGCCACGCTGGCTGCGCTCATCCTCGAGCACGCCGAGGTCGCCGTCGTTCCCGGTGAGGCCTTCGGTCCCTCGGGCTTCGTGCGGCTGTCCTACGCGCTGGGCGACGACGACCTGGTCGAGGGCGTGGGCCGCGTCCAGAAGCTGCTGGCCGAGGTCGAGTAG","VYRRLPGVVTGGSDVFQTHGCRWSWDHGRVTPAPTHRVSARLSAIAPSATLAVDAKAKALKAAGRPVIGFGAGEPDFPTPDYIVEAAVAAAKDPANHKYSPAKGLPVLREAIAAKTLRDSGYEVSPDDILVTNGGKQAVFQAFAALVDPGDEVLLPAPYWTTYPEAVALAGGTTVEVFAGADQDYKVSVDQLEAARTERTKVLLLCSPSNPTGSVYTPEELTAIGQWALEHGIWVITDEIYEHLLYDGAQTAHVVKLVPELADQTIVLNGVAKTYAMTGWRVGWMIAPSDVIKAATNFQSHLTSNVANVSQRAALAAVSGDLTAVEQMRTAFDRRRRTMVEMLSQIEGLTVPVPRGAFYAYPSIEGLVGRTLRGTTIDSSATLAALILEHAEVAVVPGEAFGPSGFVRLSYALGDDDLVEGVGRVQKLLAEVE$","Aminotransferase, class I and II","Cytoplasm, Membrane","aspartate aminotransferase","aspartate aminotransferase ","aminotransferase, class I and II","","Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K., Okamoto A., Higuchi T., Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 1991. 266(4):2567-2572. PMID: 1990006","","","

InterPro
IPR001176
Family

1-aminocyclopropane-1-carboxylate synthase
PR00753	$\"[150-171]T$ $\"[197-221]T$ $\"[233-256]T$ $\"[264-288]T$	ACCSYNTHASE

InterPro
IPR004838
Binding_site

Aminotransferases class-I pyridoxal-phosphate-binding site
PS00105	$\"[270-283]T$	AA_TRANSFER_CLASS_1

InterPro
IPR004839
Domain

Aminotransferase, class I and II
PF00155	$\"[65-425]T$	Aminotran_1_2

InterPro
IPR005829
Family

Sugar transporter superfamily
PS00217	$\"[67-92]?$	SUGAR_TRANSPORT_2

InterPro
IPR015421
Domain

Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10	$\"[81-326]T$	no description

noIPR
unintegrated

unintegrated
PTHR11751	$\"[82-433]T$	SUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF35	$\"[82-433]T$	ASPARTATE AMINOTRANSFERASE

","BeTs to 25 clades of COG0436COG name: PLP-dependent aminotransferasesFunctional Class: E [Metabolism--Amino acid transport and metabolism]The phylogenetic pattern of COG0436 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is 3","***** IPB001176 (1-aminocyclopropane-1-carboxylate synthase signature) with a combined E-value of 2.3e-66. IPB001176A 40-66 IPB001176B 93-109 IPB001176C 128-148 IPB001176D 150-171 IPB001176E 197-221 IPB001176F 233-256 IPB001176G 264-288 IPB001176H 297-320***** IPB011715 (Tyrosine aminotransferase ubiquitination region) with a combined E-value of 5.6e-15. IPB011715C 130-173 IPB011715E 204-241 IPB011715H 388-428***** IPB004839 (Aminotransferase, class I and II) with a combined E-value of 1.8e-13. IPB004839A 194-214 IPB004839C 272-283***** IPB004838 (Aminotransferase, class-I) with a combined E-value of 2e-13. IPB004838B 140-150 IPB004838C 203-215 IPB004838D 270-283","","","-61% similar to PDB:1J32 Aspartate Aminotransferase from Phormidium lapideum (E_value = 2.6E_89);-57% similar to PDB:1BJW ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS (E_value = 1.7E_69);-57% similar to PDB:1BKG ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS WITH MALEATE (E_value = 1.7E_69);-57% similar to PDB:1B5O THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1 (E_value = 6.5E_69);-56% similar to PDB:1B5P THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 (E_value = 2.5E_68);","Residues 65 to 425 (E_value = 5.4e-86) place ANA_2820 in the Aminotran_1_2 family which is described as Aminotransferase class I and II.Residues 76 to 338 (E_value = 0.0011) place ANA_2820 in the Beta_elim_lyase family which is described as Beta-eliminating lyase.","","aminotransferase (aspat)","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","","" "ANA_2821","3039698","3040237","540","12.16","25.94","19857","ATGTCCTCATGGAGGGCGAGTCCGTCACCAGCCTGCTCGACGTGGACTCCCTGGGGCCCGGTTACCGGGTTGATGACCTGGCCTGCCTGCTGGGGCACGTCAGTGTGCTGGACCACCTGGCGCCCGCCTCCTACCCGAAGCTGCGCCCCATCCTGGAGACCTGGACCCGCATGGCTGAGCAGCAGGTGGATCCGGTCTCCCTGCGTGCCCGCTGTGCCGGCGTGGTCCTGTCTCTGGTGGCCGGCGCCCGCCGCGAGGACGGTGGCCCGTGGCGCCCCGACGCCGAGGGCCGCCTGGCCCGCGCCGAGACCTGGCTGGCGCAGGGCCGCGAGATCCAGGCGCGGCGCGGCGCCCACTGAAGCCCGCTGGTCTCACGCCGAGCCGGGCAGGTTTCGCGGTGCCCGACAGACTCTCTGTCGGCTTGCGCGAAACCTGCCCGGCTCGGTGAGGAAGCGGAGCCTCAGGCGCTACTCGACCTCGGCCAGCAGCTTCTGGACGCGGCCCACGCCCTCGACCAGGTCGTCGTCGCCCAGCGCGTAG","MSSWRASPSPACSTWTPWGPVTGLMTWPACWGTSVCWTTWRPPPTRSCAPSWRPGPAWLSSRWIRSPCVPAVPAWSCLWWPAPAARTVARGAPTPRAAWPAPRPGWRRAARSRRGAAPTEARWSHAEPGRFRGARQTLCRLARNLPGSVRKRSLRRYSTSASSFWTRPTPSTRSSSPSA$","Hypothetical protein","Extracellular, Cytoplasm","low-specificity D-threonine aldolase","hypothetical protein predicted by Glimmer/Critica","hypothetical protein","","","","","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","","","-60% similar to PDB:1W0R SOLUTION STRUCTURE OF DIMERIC FORM OF PROPERDIN BY X-RAY SOLUTION SCATTERING AND ANALYTICAL ULTRACENTRIFUGATION (E_value = );-60% similar to PDB:1W0S SOLUTION STRUCTURE OF TRIMERIC FORM OF PROPERDIN BY X-RAY SOLUTION SCATTERING AND ANALYTICAL ULTRACENTRIFUGATION (E_value = );","No significant hits to the Pfam 21.0 database.","","D-threonine aldolase","","1","","","","","","","","","","","","","","","","Wed Aug 15 20:34:16 2007","","","","Wed Aug 15 20:34:16 2007","Wed Aug 15 20:34:16 2007","","","","","yes","","" "ANA_2823","3041757","3041993","237","10.40","3.92","8909","ATGAGCGAGAGCGCACGCGCTGCGACAGGCAAGTCGGCCACCAAGCGCGGCTTCTTCGGGCGCATCGCCCTGTTCATCCGCCAGGTCATTGACGAGCTGCGCAAAGTCGTCTGGCCCACCATGAACGAGCTGTGGACCTACTTCACGGTAGTGGTCGTCTTCATCATTGCCATCATGGCCTTCACCGGGGTACTGGACTTCGCCTTCAACCGGGCCGTCATGTGGCTCTTCGCCTGA","MSESARAATGKSATKRGFFGRIALFIRQVIDELRKVVWPTMNELWTYFTVVVVFIIAIMAFTGVLDFAFNRAVMWLFA$","Preprotein translocase subunit SecE","Membrane, Cytoplasm","","hypothetical protein predicted by Glimmer/Critica","preprotein translocase, SecE subunit","","Bieker K.L., Phillips G.J., Silhavy T.J. The sec and prl genes of Escherichia coli. J. Bioenerg. Biomembr. 1990. 22(3):291-310. PMID: 2202721Driessen A.J. SecB, a molecular chaperone with two faces. Trends Microbiol. 2001. 9(5):193-196. PMID: 11336818Muller J.P. Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. FEMS Microbiol. Lett. 1999. 176(1):219-227. PMID: 10418149Hartmann E., Sommer T., Prehn S., Gorlich D., Jentsch S., Rapoport T.A. Evolutionary conservation of components of the protein translocation complex. Nature 1994. 367(6464):654-657. PMID: 8107851Pohlschroder M., Prinz W.A., Hartmann E., Beckwith J. Protein translocation in the three domains of life: variations on a theme. Cell 1997. 91(5):563-566. PMID: 9393849","","","

InterPro
IPR001901
Family

Protein secE/sec61-gamma protein
PF00584	$\"[21-77]T$	SecE
PS01067	$\"[25-53]T$	SECE_SEC61G

InterPro
IPR005807
Family

SecE subunit of protein translocation complex
TIGR00964	$\"[22-78]T$	secE_bact: preprotein translocase, SecE sub

noIPR
unintegrated

unintegrated
tmhmm	$\"[44-64]?$	transmembrane_regions

","BeTs to 7 clades of COG0690COG name: Preprotein translocase subunit SecEFunctional Class: N [Cellular processes--Cell motility and secretion]The phylogenetic pattern of COG0690 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","No significant hits to the Blocks database.","","","-68% similar to PDB:2AKH Normal mode-based flexible fitted coordinates of a non-translocating SecYEG protein-conducting channel into the cryo-EM map of a SecYEG-nascent chain-70S ribosome complex from E. coli (E_value = );-68% similar to PDB:2AKI Normal mode-based flexible fitted coordinates of a translocating SecYEG protein-conducting channel into the cryo-EM map of a SecYEG-nascent chain-70S ribosome complex from E. coli (E_value = );","","","translocase secE subunit","","1","","","","","","","","","","","","","","","","","","","","","","","","","","yes","",""